EP1002061A1 - FAMILY 6 ENDO-1,4-$g(b)-GLUCANASE VARIANTS AND CLEANING COMPOSIT IONS CONTAINING THEM - Google Patents

FAMILY 6 ENDO-1,4-$g(b)-GLUCANASE VARIANTS AND CLEANING COMPOSIT IONS CONTAINING THEM

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Publication number
EP1002061A1
EP1002061A1 EP98929249A EP98929249A EP1002061A1 EP 1002061 A1 EP1002061 A1 EP 1002061A1 EP 98929249 A EP98929249 A EP 98929249A EP 98929249 A EP98929249 A EP 98929249A EP 1002061 A1 EP1002061 A1 EP 1002061A1
Authority
EP
European Patent Office
Prior art keywords
atom
humicola
endo
glucanase
cellulase
Prior art date
Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
Withdrawn
Application number
EP98929249A
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German (de)
French (fr)
Inventor
Henrik Lund
Jack Bech Nielsen
Martin Schulein
Bo Damgaard
Kim Vilbour Andersen
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Novozymes AS
Original Assignee
Novo Nordisk AS
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Filing date
Publication date
Application filed by Novo Nordisk AS filed Critical Novo Nordisk AS
Publication of EP1002061A1 publication Critical patent/EP1002061A1/en
Withdrawn legal-status Critical Current

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Classifications

    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/14—Hydrolases (3)
    • C12N9/24—Hydrolases (3) acting on glycosyl compounds (3.2)
    • C12N9/2402—Hydrolases (3) acting on glycosyl compounds (3.2) hydrolysing O- and S- glycosyl compounds (3.2.1)
    • C12N9/2405—Glucanases
    • C12N9/2434—Glucanases acting on beta-1,4-glucosidic bonds
    • C12N9/2437—Cellulases (3.2.1.4; 3.2.1.74; 3.2.1.91; 3.2.1.150)
    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
    • C11D3/16—Organic compounds
    • C11D3/38—Products with no well-defined composition, e.g. natural products
    • C11D3/386—Preparations containing enzymes, e.g. protease or amylase
    • C11D3/38645—Preparations containing enzymes, e.g. protease or amylase containing cellulase
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12Y—ENZYMES
    • C12Y302/00—Hydrolases acting on glycosyl compounds, i.e. glycosylases (3.2)
    • C12Y302/01—Glycosidases, i.e. enzymes hydrolysing O- and S-glycosyl compounds (3.2.1)
    • C12Y302/01004—Cellulase (3.2.1.4), i.e. endo-1,4-beta-glucanase

Definitions

  • the present invention relates to cleaning compositions, including laundry detergent compositions and fabric softener or fabric conditioning compositions, containing an endo-l,4- ⁇ - glucanase of the glycosyl hydrolase family 6, preferably an improved variant of a parent Humicola endoglucanase or Humicola- li e cellulase; the improved variants; and a method of con- structing the variants.
  • Performance of a cleaning composition for use in a washing or cleaning method, such as a laundry, dishwashing or sur- face cleaning method, is judged by a number of factors, including the ability to remove soils, the ability to prevent the re- deposition of the soils, or, in case of laundry, the ability to maintain the original colours of the washed garment and the ability to maintain fabric or garment durability.
  • the anti- harshening or softening effect of cellulase on fabrics and the fabric care (colour care/colour clarification) effect is known, e.g. from GB 1 368 599 and EP 269 168, along with other very beneficial cellulolytic effects such as particulate soil removal and de-pilling.
  • Fabric conditioning or fabric softener compositions in particular compositions to be used in the rinse cycle of laundry washing processes, are also well known.
  • such compositions contain a water-insoluble quaternary-ammonium fabric softening agent, the most commonly used having been di-long alkyl chain ammonium chloride.
  • Fabric conditioning compositions comprising cellulase have also been suggested, e.g. in US 5,445,747, in particular compositions using a specific ⁇ 43kD cellulase obtained from the fungus Humicola insolens .
  • CBD cellulose-binding domain
  • CAD catalytically active domain
  • Agaricus bisporus exoglucanase 3 (cel3) , Cellulomonas fimi endoglucanase A (cenA) , Cellulomonas fimi exoglucanase A (cbhA) , Microspora bispora endoglucanase A (celA) , Streptomyces halste- dii endoglucanase A (celA) , Streptomyces strain KSM-9 endoglucanase 1 (casA) , Thermomonospora fusca endoglucanase E-2 (celB) , Trichoderma reesei exoglucanase II (cbh2) , and probably Neocal- limastix patriciarum exoglucanase (celA) (Denman et al., 1996) and Orpinomyces ⁇ p.
  • the inverting mechanism involves protonation of the glycosidic oxygen of the scissile bond by an acidic amino acid residue (general acid catalyst) with concerted attack of a water ole- cule at the anomeric carbon.
  • the nucleophilicity of this water molecule is greatly increased through deprotonation by a basic amino acid residue (general basic catalyst) .
  • the partial positive charge formed at the anomeric carbon in the transition state is stabilised through resonance with the ring oxygen. This gives the transition state significant oxocarbonium ion character which is stabilised by electrostatic interactions with the nearby carboxylate side chains and by specific binding interactions with the sugar in its half-chair conformation.
  • glutamate and aspartate residues act directly as general acid or base catalysts in glycosidases (Damude et. al. 1996) .
  • the present invention re- lates to cleaning compositions comprising one or more enzymes having cellulolytic activity wherein at least 25% of the total weight of cellulolytic active enzyme protein derives from the presence of a Humicola endo-1, 4- ⁇ -glucanase or Humi cola-like cellulase (endo-type (Cel6B) or exo-type (Cel6A))of the glycosyl hydrolase family 6, the Humicola-like cellulase being an enzyme comprising a catalytically core domain having an amino acid sequence being at least 35% homologous to the appended SEQ ID NO: 4.
  • the invention provides a method of constructing a variant of a parent Humicola family 6 en- do-beta-l,4-glucanase or a Humicola-like family 6 cellulase which variant has endo-beta-l,4-glucanase activity and improved deter- gent compability as compared to the parent endo-beta-l,4-glucanase or cellulase; and variants provided by the method.
  • Fig. 3 shows the nucleotide sequence of pC6H from BamHI- Xbal disturb the translational initiation codon is underlined (see e- xample 3) .
  • Figure 4 Secondary structure elements (strand and helix only) of catalytic core domain of Humicola insolens Cel6B as determined by DSSP for the two independent molecules in the asymmetric unit. (H) ⁇ -helix, (3) 3-10-helix, (S) ⁇ -strand.
  • Figure 5 The loop regions encompassing the binding cleft in the catalytic core region of Humicola insolens Cel6B. (L) indicate the defined loop regions encompassing the binding cleft,
  • FIG. 6 shows the loop regions encompassing the binding cleft in Humicola insolens Cel6A as determined from sequence alignment to Humicola insolens EGIV (Cel6B) . The numbering refers to the mature full length protein.
  • Fig. 7 shows the loop regions encompassing the binding cleft in Humicola insolens Cel6A as determined from analysis of X-ray structure.
  • Fig. 8 Residues on the surface of Humicola insolens Cel6B catalytic core domain and Neocallimastix patriciarum catalytic core domain (Q12646) are shown in bold and underline (see example 6) .
  • FIG. 9 Residues on the surface of Humicola insolens Cel6B catalytic core domain and Orpinomyces sp .
  • CelA catalytic core domain (P78720) are shown in bold and underline (see example 6) .
  • FIG. 10 Residues on the surface of Humicola insolens Cel6B catalytic core domain and Orpinomyces sp .
  • CelC catalytic core domain (P78721) are shown in bold and underline (see exam- pie 6) .
  • Appendix 1 shows the structural coordinates of Humicola insolens EG VI (Cel6B) endo-beta-1, 4-glucanase.
  • Appendix 2 shows the structural coordinates of Humicola insolens Cel6A cellulase.
  • figure 1 a number of selected amino acid sequences of cellulases of different microbial origin are aligned.
  • P49* Deletion of a proline (P) at position 49 in the amino acid sequence of the cellulase from Humicola insolens is indicated as P49*.
  • Multiple mutations are separated by slash marks ("/") , e.g. Q119H/Q146R, representing mutations in positions 119 and 146 substituting glutamine (Q) with histidine (H) , and glutamine (Q) acid with arginine (R) , respectively.
  • a substitution is made by mutation in e.g. a cellulase derived from a strain of Humicola insolens , the product is designated e.g. "Humicola insolens/*49P" .
  • the term "endoglucanase” is intended to denote enzymes with cellulolytic activity, espe- cially endo-1, 4- ⁇ -glucanase activity, which are classified in EC 3.2.1.4 according to the Enzyme Nomenclature (1992) and are capable of catalysing (endo) hydrolysis of 1, 4- ⁇ -D-glucosidic link- ages in cellulose, lichenin and cereal ⁇ -D-glucans including
  • inverting type endoglucanase means an endo- ⁇ -l,4-glucanase which hydrolyses the gly- cosidic bond with net inversion of anomeric configuration, i.e. which operate via a direct displacement of the leaving group by water: one residue acts as a general acid and the other as a general base.
  • retaining type endoglu- canase means an endo- ⁇ -1, 4-glucanase" which hydrolyses the gly- cosidic bond with net retention of anomeric configuration, i.e. which utilizes a double-displacement mechanism involving a gly- cosyl-enzyme intermediate: one residue functions as general acid and general base while the other acts as a nucleophile and leav- ing group (McCarter et al., 1994).
  • the cleaning composition comprises a Humicola endo-1, 4- ⁇ -glucanase or Humicola-like cellulase of the glycosyl hydrolase family 6 in an amount corresponding to at least 25%, preferably at least 30%, more preferably at least 40%, even more preferably at least 90%, especially at least 98%, of the total weight of enzyme protein having cellulolytic activity.
  • the term "Humicola-like cellulase” denotes an endoglucanase or an exoglucanase (cellobiohydrolase) comprising a catalytically core domain which has an amino acid sequence being at least 35% homologous to SEQ ID NO: 4. This is explained in further detail below.
  • family 6 endoglucanase will usually be present in a mixture of other enzymes having cellulolytic activity. This mixture may either be a conventional fermentation product, possibly isolated and purified, from a single species of a microorganism.
  • examples of other cellulolytic enzymes usually present in a fungal cellulolytic mixture, i.e.
  • a cellulase complex produced by a fungal species are endo-l,4- ⁇ - glucanases of the glycosyl hydrolase families 5, 7, 12, or 45; and examples of other cellulolytic enzymes usually present in a bacterial cellulolytic mixture, i.e. a cellulase complex produced by a bacterial species, are endo-1, 4- ⁇ -glucanases of the glycosyl hydrolase families 5, 8, 9, 12, 41, 45 or 48.
  • the mixture may also be a mixture of monocomponent enzymes, preferably enzymes derived from bacterial or fungal species by using conventional recombinant techniques, which enzymes have been fermented and possibly isolated and purified separately and which may originate from different species, preferably fungal or bacterial species.
  • essentially all cellulolytic activity present in the composition of the invention re- suits from one single enzyme component, i.e. a monocomponent endo-l,4- ⁇ -glucanase of the glycosyl hydrolase family 6.
  • a monocomponent endo-l,4- ⁇ -glucanase of the glycosyl hydrolase family 6 are those derived from the species Humicola insolens (eg EG VI also denoted Cel6B) , Neocallimastix patriciarum, Orpinomyces sp .
  • Trichoderma reesei and Fusarium oxy ⁇ porum produces enzymes which are suitable as starting material for the protein engineering method by which well-performing family 6 endoglucanase variants can be constructed.
  • the family 6 endo-1, 4- ⁇ -glucanase comprises one or two cellulose-binding domains (CBD) operably linked to the catalytic domain.
  • a cellulose binding domain (CBD) is a polypeptide which has high affinity for or binds to water-insoluble forms of cellulose and chitin, including crystalline forms.
  • CBDs are found as integral parts of large protein complexes consisting of two or more different polypeptides, for example in hydrolytic enzymes (hydrolases) which typically are composed of a catalytic domain containing the active site for substrate hydrolysis, and a carbohydrate-binding domain or cellulose-binding domain (CBD) for binding to the insoluble matrix.
  • hydrolytic enzymes hydrolytic enzymes
  • Such enzymes can comprise more than one catalytic domain and one, two or three CBDs and optionally one or more polypeptide regions linking the CBD(s) with the catalytic domain (s) , the latter regions usually being denoted a "linker".
  • hydrolytic enzymes comprising a CBD are cellulases, xylanases, mannanases, arabinofuranosidases, acetyl esterases and chitinases.
  • CBDs have also been found in algae, e.g. the red alga Porphyra purpurea as a non-hydrolytic polysaccharide- binding protein, see Peter Tomme et al. "Cellulose-Binding Domains: Classification and Properties" in "Enzymatic Degradation of Insoluble Carbohydrates", John N. Saddler and Michael H. Penner (Eds.), ACS Symposium Series, No. 618, 1996.
  • most of the known CBDs are from cellulases and xylanases.
  • cellulose-binding domain is intended to be understood as defined by Tomme et al., op . cit . This definition classifies more than 120 cellulose-binding domains into 10 families (I-X) which may have different functions or roles in connection with the mechanism of substrate binding. However, it is anticipated that new family representatives and additional CBD families will appear in the future.
  • CBDs may be useful as a single domain polypeptide or as a dimer, a trimer, or a polymer; or as a part of a protein hybrid.
  • Chimeric protein hybrids are known in the art, see e.g. WO 90/00609, WO 94/24158 and WO 95/16782, and comprise a cellulose binding domain (CBD) from another origin, preferably from another microbial origin, than the chimeric protein as such, which CBD exists as an integral part of the protein.
  • CBD cellulose binding domain
  • the chimeric protein hybrids are enzyme hybrids, i.e. contain a catalytic domain together with the binding domain.
  • Chimaric protein hybrids and enzyme hybrids can be prepared by transforming into a host cell a DNA construct comprising at least a fragment of DNA encoding the cellulose- binding domain (CBD) ligated, with or without a linker, to a DNA sequence encoding the protein or enzyme and growing the host cell to express the fused gene.
  • CBD cellulose- binding domain
  • the recombinant fusion protein or enzyme hybrids may be described by the following formula:
  • recombinant fusion protein or enzyme hybrids having an internal CBD are also contemplated.
  • the structural part to be modified is the binding cleft, the loop region encompassing the binding cleft, or the side chain of the catalytic acid Aspl39.
  • the invention provides a method of constructing a variant of a parent Humicola-like family 6 cellulase, which variant has endo-beta-l,4-glucanase activity and improved detergent compatibility as compared to the parent cellulase, which method comprises i) comparing the three- dimensional structure of the Humicola endo-beta-l,4-glucanase with the structure of a Humicola-like cellulase, ii) identifying a part- of the Humicola-like cellulase structure which is different from the Humicola endo-beta-l,4-glucanase structure and which from structural or functional considerations is contemplated to be responsible for differences in the detergent compatibility of the Humicola endo-beta-1, 4-glucanase and Humicola-like cellulase, iii) modifying the part of the Humicola-like cellulase identified in ii) whereby a
  • the part of the Humicola-like cellulase is modified so as to resemble the corresponding part of the Humicola family 6 endo-beta-l,4-glucanase.
  • the modification is, in step iii) of the method, accomplished by deleting one or more amino acid residues of the part of the Humicola-like cellulase to be modified; or the modification is accomplished by replacing one or more amino acid residues of the part of the Humi ⁇ ola-like cellulase to be modified with the amino acid residues occupying corresponding positions in the Humicola endo-beta-l,4-glucanase; or the modification is accomplished by insertion of one or more amino acid residues present in the Humicola endo-beta-1, 4-glucanase into a corresponding position in the Humicola-like cellulase.
  • the parent Humicola endo-beta- 1,4-glucanase is derived from a strain of Humicola in ⁇ olen ⁇ , more preferably from the strain Humicola in ⁇ olens, DSM 1800.
  • improved detergent compability improved properties of the enzyme with respect to enzymatic activity and stability in commercial detergent compositions. More specifically, these improved properties are improved enzymatic performance or enzymatic activity at a high pH, preferably at a pH above 8, more preferably above 9, especially at a pH about or above 10; improved stability towards conventional commercial detergent composition ingredients such as anionic or non-ionic surfactants, cf. examples 4-7; improved thermal stability; and improved resistance to oxidation (ie improved compatibility towards conventional detergent composition ingredients such as bleaching agents) .
  • the three-dimensional structure of Humicola insolens Cel6B (EG VI) catalytic core domain The three-dimensional structure of the catalytic core domain of the Humicola insolens Cel6B fungal cellulase was solved by X-ray crystallographic methods. The extent of the catalytic core domain used for the experiment was the 347 amino acid resi- 5 dues starting from position 27 of SEQ ID NO: 4 (and including position 373 of SEQ ID NO:4).
  • the obtained three-dimensional structure is believed to be representative for the structure of the any fungal endoglucanase catalytic core domain belonging to family 6 of glycosyl hydrola-
  • PDB Protein Data Bank
  • E. E. Abola, F. C. Bernstein, S. H. Bryant, T. F. Koetzle, and J. Weng Protein Data Bank, in Crystallographic Databases-Information Content, Software Systems, Scientific Applications, F. H. Allen, G. Berger- hoff, and R. Sievers, eds., Data Commission of the International
  • the catalytic Br ⁇ n- sted acid (D139) and the catalytic base (D316) are located on e- ach side of a cleft at a distance of 9.12A and 9.64A for the two independent molecules respectively consistent with the catalytic mechanism occurring with inversion of the anomeric configurati- on.
  • a third acidic residue (D180) is located close to the Br ⁇ n- sted acid having the effect of stabilizing the protonated form of the D139 thereby making the enzyme active even at alkaline conditions.
  • the secondary structure of the core domain of the Humicola insolens Cel6B fungal cellulase as determined by the DSSP program (W.Kabsch & C.Sander, Dictionary of protein secondary structure : pattern recognition of hydrogen bond and geometrical features . Biopoly ers 22, 2577-2637 (1983)) is shown in figure 4.
  • the three-dimensional structure of the catalytic core domain of the Humicola insolens Cel6A cellulase was solved by X- ray crystallographic methods as described above and is shown in Appendix 2.
  • a binding cleft is defined as consisting of the largest cave (pocket) on the surface of an enzyme and can extend beyond this pocket.
  • WHAT IF G.Vriend, WHAT IF: a molecular modelling and drug design program . J.Mol. Graph. 8, 52-56, (1990) version 19980317-1938
  • the binding cleft in contact with the substrate can consist of more residues than those in the concave cleft detected above. Those can be detected by visual inspection of the three- dimensional structure e.g.
  • the complete binding cleft is defined as comprising of the following residues: N14, D16, K20, Y51, W52, S54 , L58, Y86, R91, D92, P138, D139, D180,
  • the loop regions encompassing the binding cleft Given the binding cleft as described above, the loop regions encompassing the binding cleft is defined as the regions of contiguous sequence not belonging to a ⁇ -helical region or a ⁇ - strand region in any of the determined structures. In this definition the 3-10 helices are included in the loop definition as they are not seen as an integral part of the inner core structure.
  • the binding cleft encompassing loops are defined as: L12, V13 , N14, S54 , N55, 156, F57, L58, L59, Y86, N87, L88, P89, D90, R91, D92, C93, S94, A95, G96, E97, S98, S99, G100, E101, L102, K103, L104, S105, Q106, N107, E137, P138, D139, V181, A182, N183, G188, W189, A190, D191, K192, N219, V220, S221, N222, Y223, N224, P225, Y226, S227, T228, S229, N230, P231, P232, P233, Y234, T235, S236, G237, S238, P239, S240, P241, D242, A271, L272, S273, G274, A275, R276, S
  • the Sub ⁇ et zone command of the Insightll program is applied.
  • the command detects residues or individual atoms within a defined distance from a predefined subset, groups of residues or groups of atoms.
  • the Sub ⁇ et li ⁇ t command can be used to investigate the result.
  • mutations/deletions of surface exposed residues are performed.
  • the mutation is towards a more negatively charged residue, and preferably from a potentially positively charged residue (His, Lys or Arg, more preferably Arg) .
  • His, Lys or Arg, more preferably Arg a potentially positively charged residue
  • a hydrogen bond involving the back bone amide proton is defined as those with an energy determined by DSSP smaller than or equal to -1.4 kcal/mole.
  • Unsatisfied hydrogen bond donors and/or acceptors as well as unpaired buried charged groups from potentially charged residues can destabilize an enzyme structure. Removing the unsatisfied partner by mutagenesis to a residue without these properties or mutation of neighboring residues to fulfill the unsatisfied hydrogen bond or salt bridge can most often stabilize the enzyme structure.
  • These unsatisfied hydrogen bond/salt bridge partners can be found using the WHAT CHECK routine which is an integral part of the WHAT IF program.
  • residues having their side chains exposed to the cavity in a favorable position for mutagenesis as judged visually using In ⁇ ightll V13, N14 , Y17, S18, L21, V40,
  • the mutations should preferably be made to surface exposed residues and preferably not more than 15A from the catalytic proton donor, more preferably not more than loA from the cataly- tic proton donor and most preferably nor more than ⁇ A from the catalytic proton donor.
  • Insertions/deletions should only be made in loop/turn regions and preferably not more than l ⁇ A from the catalytic proton donor .
  • Another method to alter the pH profile of an enzyme is to mutate the residues in or close to the binding cleft. This will create a variant enzyme where the electrostatics of the active site will be changed either directly due to altered charges or partial charges in the binding cleft, or due to altered geometry around the active site changing the degree of burial of the active site residues. These changes should be made not more than 5A from a residue in the binding cleft, and preferably not more than 2.5A from a residue in the binding cleft most preferably mutating residues in the binding cleft.
  • the present invention includes variants of sequences having at least 35% identity to the catalytic core domain of Humicola insolens Cel6B. Percent sequence identity is determined by conventional methods, by means of computer programs known in the art such as GAP provided in the GCG program package (Program Ma- nual for the Wisconsin Package, Version 8, August 1994, Genetics Computer Group, 575 Science Drive, Madison, Wisconsin, USA 53711) as disclosed in Needleman, S.B.
  • the catalytic core domain of Humicola in ⁇ olen ⁇ Cel6B is defined as the 347 residues used for the X-ray structure determination (positions 27-374 of SEQ ID NO: 4).
  • the Profile /Structure alignment option of ClustalW is applied. Only the part of the sequence extending from the start of the GAP alignment to the catalytic core domain of Humicola in ⁇ olens Cel6B to the last residue aligning with to the catalytic core domain of Humicola in ⁇ olen ⁇ Cel6B are included.
  • the alignment in Fig. 4 is read as 1 st profile and the new sequence is read as 2 profile .
  • the option Align ⁇ equence ⁇ to 1 st profile is used to align a new sequence to the sequence alignment in Fig. 4. No alterations is made to the default parameters. From such an alignment residues in a new sequence at positions equivalent to positions in the catalytic core domain of Humicola in ⁇ olen ⁇ Cel6B can be identified.
  • An more preferred way of identifying equivalent residues between a "new" sequence ant the catalytic core domain of Humicola in ⁇ olen ⁇ Cel6B is to determine the three-dimensional X-ray structure fold of the "new" sequence and apply a structure based sequence alignment as implemented in the Modeler 97.0 program included in the Homology 97.0 package from MSI INC. using the MALIGN3D command with the GAP_PENALTIES_3D parameters set to 0.0 and 1.75 and the FIT_ATOMS set to CA. This alignment will find residues at structurally equivalent positions, i.e. having their CA atoms not more than 3.5A apart in a structural superposition. From this alignment equivalent residues in a "new" sequence can be identified. Increased color care activity by trimming of binding cleft loops.
  • the origin of this is thought to be a more open binding cleft caused by one or more of the binding cleft encompassing loops being shorter that in the other fungal family 6 cellulases, preferably one of the four longer loops: Y86-N107, N219-D242, L272-P287 or W308-F331 (Humicola in ⁇ olens Cel6B numbering) or equivalent regions as determined by the multiple sequence alignment, more preferably the regions N219-D242 or W308-F331 which are seen in the multiple sequence alignment to be different in length.
  • the extent of the loop regions can be trimmed (ie made shorter) by deletion of individual residues which together with mutation of neighboring residues can optimize the color care effect.
  • the loop manipulations can be performed using site directed mutagenesis, region specific random mutagenesis using spiked oligonucleotides, protein family shuffling or by other methods.
  • Cloning of cellulase-encoding DNA sequences and methods for generating mutations at specific sites within the cellulase-encoding sequence are mentioned in the following. Cloning a DNA sequence encoding a cellulase The DNA sequence encoding a parent cellulase may be isolated from any cell or microorganism producing the cellulase in question, using various methods well known in the art. First, a genomic DNA and/or cDNA library should be constructed using chromosomal DNA or messenger RNA from the organism that produces the cellulase to be studied.
  • homologous, labelled oligonucleotide probes may be synthesized and used to identify cellulase-encoding clones from a genomic library prepared from the organism in question.
  • a labelled oligonucleotide probe containing sequences homologous to a known cellulase gene could be used as a probe to identify cellulase-encoding clones, using hybridization and washing conditions of lower stringency.
  • a method for identifying cellulase-encoding clones involves inserting cDNA into an expression vector, such as a plasmid, transforming cellulase-negative fungi with the resulting cDNA library, and then plating the transformed fungi onto agar containing a substrate for cellulase, thereby allowing clones expressing the cellulase to be identified.
  • an expression vector such as a plasmid, transforming cellulase-negative fungi with the resulting cDNA library
  • plating the transformed fungi onto agar containing a substrate for cellulase thereby allowing clones expressing the cellulase to be identified.
  • the DNA sequence encoding the enzyme may be prepared synthetically by established standard methods, e.g. the phosphoroamidite method. In the phosphoroamidite method, oligonucleotides are synthesized, e.g.
  • the DNA sequence may be of mixed genomic and synthetic origin, mixed synthetic and cDNA origin or mixed genomic and cDNA origin, prepared by ligating fragments of synthetic, genomic or cDNA origin (as appropriate, the fragments corresponding to various parts of the entire DNA sequence) , in accordance with standard techniques.
  • the DNA sequence may also be prepared by polymerase chain reaction (PCR) using specific primers. Site-directed mutagenesis
  • the random mutagenesis of a DNA sequence encoding a parent cellulase may conveniently be performed by use of any method known in the art.
  • the random mutagenesis may be performed by use of a suitable physical or chemical mutagenizing agent, by use of a suitable oligonucleotide, or by subjecting the DNA sequence to PCR generated mutagenesis.
  • the random mutagenesis may be performed by use of any combination of these mutagenizing agents.
  • the mutagenizing agent may, e.g., be one which induces transitions, transversions, inversions, scrambling, deletions, and/or insertions .
  • Examples of a physical or chemical mutagenizing agent suitable for the present purpose include ultraviolet (UV) irradiation, hydrox lamine, N-methyl-N ' -nitro-N-nitrosoguanidine (MNNG) , O- methyl hydroxylamine, nitrous acid, ethyl methane sulphonate (EMS) , sodium bisulphite, formic acid, and nucleotide analogues.
  • UV ultraviolet
  • MNNG N-methyl-N ' -nitro-N-nitrosoguanidine
  • EMS ethyl methane sulphonate
  • sodium bisulphite formic acid
  • nucleotide analogues examples include ultraviolet (UV) irradiation, hydrox lamine, N-methyl-N ' -nitro-N-nitrosoguanidine (MNNG) , O- methyl hydroxylamine, nitrous acid, ethyl methane sulphonate (EMS) , sodium bis
  • the oligonucleotide may be doped or spiked with the three non-parent nucleotides during the synthesis of the oligonucleotide at the positions which are to be changed.
  • the doping or spiking may be done so that codons for unwanted amino acids are avoided.
  • the doped or spiked oligonucleotide can be incorporated into the DNA encoding the cellulase enzyme by any published technique, using e.g. PCR, LCR or any DNA polymerase and ligase.
  • PCR-generated mutagenesis When PCR-generated mutagenesis is used, either a chemically treated or non-treated gene encoding a parent cellulase enzyme is subjected to PCR under conditions that increase the mis- incorporation of nucleotides (Deshler 1992; Leung et al., Technique, Vol.l, 1989, pp. 11-15).
  • the DNA sequence to be mutagenized may conveniently be present in a genomic or cDNA library prepared from an organism expressing the parent cellulase enzyme.
  • the DNA sequence may be present on a suitable vector such as a plasmid or a bacteriophage, which as such may be incubated with or otherwise exposed to the mutagenizing agent.
  • the DNA to be mutagenized may also be present in a host cell either by being integrated in the genome of said cell or by being present on a vector harboured in the cell.
  • the DNA to be mutagenized may be in isolated form. It will be understood that the DNA sequence to be subjected to random mutagenesis is preferably a cDNA or a genomic DNA sequence.
  • the mutated DNA sequence may be amplify prior to the expression step or the screening step being performed. Such amplification may be performed in accordance with methods known in the art, the presently preferred method being PCR-generated amplification using oligonucleotide primers prepared on the basis of the DNA or amino acid sequence of the parent enzyme.
  • the mutated DNA is expressed by culturing a suitable host cell carrying the DNA sequence under conditions allowing expression to take place.
  • the host cell used for this purpose may be one which has been transformed with the mutated DNA sequence, optionally present on a vector, or one which was carried the DNA sequence encoding the parent enzyme during the mutagenesis treatment.
  • Suitable host cells are fungal hosts such as A ⁇ pergillus niger or Aspergillus oryzae.
  • the mutated DNA sequence may further comprise a DNA sequence encoding functions permitting expression of the mutated DNA sequence. Localized random mutagenesis
  • the random mutagenesis may advantageously be localized to a part of the parent cellulase in question. This may, e.g., be advantageous when certain regions of the enzyme have been identified to be of particular importance for a given property of the enzyme, and when modified are expected to result in a variant having improved properties. Such regions may normally be identified when the tertiary structure of the parent enzyme has been elucidated and related to the function of the enzyme.
  • a microorganism capable of expressing the mutated cellulase enzyme of interest is incubated on a suitable medium and under suitable conditions for the enzyme to be secreted, the medium being provided with a double filter comprising a first protein- binding filter and on top of that a second filter exhibiting a low protein binding capability.
  • the microorganism is located on the second filter.
  • the first filter comprising enzymes secreted from the microorganisms is separated from the second filter comprising the microorganisms.
  • the first filter is subjected to screening for the desired enzymatic activity and the corresponding microbial colonies present on the second filter are identified.
  • the filter used for binding the enzymatic activity may be any protein binding filter e.g.
  • the detecting compound may be immobilized by any immobilizing agent, e.g., agarose, agar, gelatine, polyacrylamide, starch, filter paper, cloth; or any combination of immobilizing agents.
  • immobilizing agent e.g., agarose, agar, gelatine, polyacrylamide, starch, filter paper, cloth; or any combination of immobilizing agents.
  • a DNA sequence encoding the variant produced by methods described above, or by any alternative methods known in the art can be expressed, in enzyme form, using an expression vector which typically includes control sequences encoding a promoter, operator, ribosome binding site, translation initiation signal, and, optionally, a repressor gene or various activator genes.
  • the recombinant expression vector carrying the DNA sequence encoding a cellulase variant of the invention may be any vector which may conveniently be subjected to recombinant DNA procedures, and the choice of vector will often depend on the host cell into which it is to be introduced.
  • the vector may be an autonomously replicating vector, i.e. a vector which exists as an extrachromosomal entity, the replication of which is independent of chromosomal replication, e.g. a plasmid, a bacteriophage or an extrachromosomal element, minichromosome or an artificial chromosome.
  • Rhizomucor miehei aspartic proteinase A. niger neutral ⁇ -amylase, A. niger acid stable ⁇ -amylase, A. niger glucoamylase, Rhizomucor miehei lipase, A. oryzae alkaline protease, A. oryzae triose phosphate isomerase or A. nidulan ⁇ acetamidase.
  • suitable promoters for use in bacterial host cells include the promoter of the Bacillu ⁇ ⁇ tearothermophilu ⁇ maltogenic amylase gene, the Bacillu ⁇ licheniformis alpha- amylase gene, the Bacillus amyloliquefaciens alpha-amylase gene, the Bacillus subtili ⁇ alkaline protease gen, or the Bacillu ⁇ pumilu ⁇ xylosidase gene, or the phage Lambda P R or P promoters or the E. coli lac, trp or tac promoters.
  • the expression vector of the invention may also comprise a suitable transcription terminator and, in eukaryotes, poly- adenylation sequences operably connected to the DNA sequence encoding the cellulase variant of the invention. Termination and polyadenylation sequences may suitably be derived from the same sources as the promoter.
  • the vector may further comprise a DNA sequence enabling the vector to replicate in the host cell in question.
  • a DNA sequence enabling the vector to replicate in the host cell in question. Examples of such sequences are the origins of replication of plasmids pUC19, pACYC177, pUBHO, pE194, pAMBl and pIJ702.
  • the vector may also comprise a selectable marker, e.g. a gene, the product of which complements a defect in the host cell, such as one which confers antibiotic resistance such as ampicillin, kanamycin, chloramphenicol or tetracyclin resistance.
  • the vector may comprise A ⁇ pergillu ⁇ selection markers such as amdS, argB, niaD and sC, a marker giving rise to hygromycin resistance, or the selection may be accomplished by co-transformation, e.g. as described in WO 91/17243.
  • the procedures used to ligate the DNA construct of the invention encoding a cellulase variant, the promoter, terminator and other elements, respectively, and to insert them into suitable vectors containing the information necessary for replication, are well known to persons skilled in the art (cf., for instance, Sambrook et al. (1989)).
  • the cell of the invention either comprising a DNA construct or an expression vector of the invention as defined above, is advantageously used as a host cell in the recombinant production of a cellulase variant of the invention.
  • the cell may be transformed with the DNA construct of the invention encoding the variant, conveniently by integrating the DNA construct (in one or more copies) in the host chromosome.
  • This integration is generally considered to be an advantage as the DNA sequence is more likely to be stably maintained in the cell.
  • Integration of the DNA con- structs into the host chromosome may be performed according to conventional methods, e.g. by homologous or heterologous recombination.
  • the cell may be transformed with an expression vector as described above in connection with the different types of host cells.
  • the cell of the invention may be a cell of a higher organism such as a mammal or an insect, but is preferably a microbial cell, e.g. a bacterial or fungal cell.
  • Examples of bacterial host cells which on cultivation are capable of producing the enzyme of the invention may be a gram-positive bacteria such as a strain of Bacillu ⁇ , in particular Bacillu ⁇ alkalophilu ⁇ , Bacillu ⁇ amyloliquefacien ⁇ , Bacillu ⁇ brevi ⁇ , Bacillu ⁇ lautu ⁇ , Bacillu ⁇ lentu ⁇ , Bacillu ⁇ licheniformi ⁇ , Bacillu ⁇ circulan ⁇ , Bacillus coagulans , Bacillu ⁇ megatherium, Bacillu ⁇ ⁇ tearothermophilu ⁇ , Bacillu ⁇ ⁇ ubtili ⁇ and Bacillu ⁇ thuringien ⁇ is , a strain of Lactobacillus , a strain of Streptococcus , a strain of Streptomyces , in particular Streptomyces lividans and Streptomyces murinus , or the host cell may be a gram-negative bacteria such as a strain of E ⁇ cherichia
  • the enzyme When expressing the enzyme in a bacteria such as E ⁇ cherichia coli , the enzyme may be retained in the cytoplasm, typically as insoluble granules (known as inclusion bodies) , or may be directed to the periplasmic space by a bacterial secretion sequence. In the former case, the cells are lysed and the granules are recovered and denatured after which the enzyme is refolded by diluting the denaturing agent. In the latter case, the enzyme may be recovered from the periplasmic space by disrupting the cells, e.g. by sonication or osmotic shock, to release the contents of the periplasmic space and recovering the enzyme.
  • a ⁇ pergillu ⁇ or Fu ⁇ arium in particular A ⁇ pergillu ⁇ aw amor i , A ⁇ pergillu ⁇ nidulan ⁇ , A ⁇ pergillu ⁇ niger, A ⁇ pergillu ⁇ oryzae , and Fu ⁇ arium oxysporum, and a strain of Trichoderma , preferably Trichoderma harzianum , Trichoderma ree ⁇ ei and Trichoderma viride .
  • Fungal cells may be transformed by a process involving protoplast formation and transformation of the protoplasts followed by regeneration of the cell wall in a manner known per ⁇ e .
  • the use of a strain of A ⁇ pergillu ⁇ as a host cell is described in EP 238 023 (Novo Nordisk A/S) , the contents of which are hereby incorporated by reference.
  • Schizosaccharomyces pombe and a strain of Yarrowia ⁇ p . , in particular Yarrowia lipolytica .
  • the medium used to cultivate the cells may be any conventional medium suitable for growing the host cell in question and obtaining expression of the cellulase variant of the invention. Suitable media are available from commercial suppliers or may be prepared according to published recipes (e.g. as described in catalogues of the American Type Culture Collection) .
  • the cellulase variant secreted from the host cells may con- veniently be recovered from the culture medium by well-known procedures, including separating the cells from the medium by centrifugation or filtration, and precipitating proteinaceous components of the medium by means of a salt such as ammonium sulphate, followed by the use of chromatographic procedures such as ion exchange chromatography, affinity chromatography, or the like.
  • colour clarification is meant the partly restoration of the initial colours of fabric or garment throughout multiple washing cycles.
  • de-pilling denotes removing of pills from the fabric surface.
  • soaking liquor denotes an aqueous liquor in which laundry may be immersed prior to being subjected to a conventional washing process.
  • the soaking liquor may contain one or more ingredients conventionally used in a washing or laundering process.
  • washing liquor denotes an aqueous liquor in which laundry is subjected to a washing process, i.e. usually a combined chemical and mechanical action either manually or in a washing machine.
  • the washing liquor is an aqueous solution of a powder or liquid detergent composition.
  • washing liquor denotes an aqueous liquor in which laundry is immersed and treated, conventionally immediately after being subjected to a washing process, in order to rinse the laundry, i.e. essentially remove the detergent solution from the laundry.
  • the rinsing liquor may contain a fabric conditioning or softening composition.
  • the present invention also relates to a process for machine treatment of fabrics which process comprises treating fabric during a rinse cycle of a machine washing process with a rinse solution containing the composition according to the invention.
  • the laundry subjected to the composition or the method of the present invention may be conventional washable laundry.
  • the major part of the laundry is sewn or unsewn fabrics, including knits, wovens, denims, yarns, and toweling, made from cotton, cotton blends or natural or manmade cellulosics (e.g. originating from xylan-containing cellulose fibers such as from wood pulp) or blends thereof.
  • blends are blends of cotton or rayon/viscose with one or more companion material such as wool, synthetic fibers (e.g.
  • polyamide fibers acrylic fibers, polyester fibers, polyvinyl alcohol fibers, polyvinyl chloride fibers, polyvinylidene chloride fibers, polyurethane fibers, polyurea fibers, aramid fibers) , and cellulose-containing fibers (e.g. rayon/viscose, ramie, flax/linen, jute, cellulose acetate fibers, lyocell) .
  • Cleaning composition according to claim 1 wherein the composi- tion is a fabric softener or fabric conditioning composition for the treatment of fabrics.
  • the cleaning compositions according to the present invention comprise a surfactant system, wherein the surfactant can be selected from nonionic and/or anionic and/or cationic 5 and/or ampholytic and/or zwitterionic and/or semi-polar surfactants.
  • the surfactant is typically present at a level from 0.1% to 60% by weight.
  • the surfactant is preferably formulated to be compatible
  • the surfactant is most preferably formulated in such a way that it promotes, or at least does not degrade, the stability of any enzyme in these compositions.
  • glucose, galactose and galactosyl moieties can be substituted for the glucosyl moieties (optionally the hydrophobic group is attached at the 2-, 3-, 4-, etc. positions thus giving a glucose or galactose as opposed to a glucoside or galactoside) .
  • the intersaccharide bonds can be, e.g. , between the one position of the additional saccharide units and the 2-, 3-, 4-, and/or 6- positions on the preceding saccharide units.
  • the preferred alkylpolyglycosides have the formula
  • compositions of the present invention typically include
  • Semi-polar nonionic surfactants are a special category of nonionic surfactants which include water-soluble amine oxides containing one alkyl moiety of from about 10 to about 18 carbon atoms and 2 moieties selected from the group consisting of alkyl groups and hydroxyalkyl groups containing from about 1 to about 3 carbon atoms; watersoluble phosphine oxides containing one alkyl moiety of from about 10 to about 18 carbon atoms and 2 moieties selected from the group consisting of alkyl groups and hydroxyalkyl groups containing from about 1 to about 3 carbon atoms; and water-soluble sulfoxides containing one alkyl moiety from about 10 to about 18 carbon atoms and a moiety selected from the group consisting of alkyl and hydroxyalkyl moieties of from about 1 to about 3 carbon atoms.
  • Semi-polar nonionic detergent surfactants include the amine oxide surfactants having the formula:
  • R is an alkyl, hydroxyalkyl, or alkyl phenyl group or mixtures thereof containing from about 8 to about 22 carbon atoms;
  • R is an alkylene or hydroxyalkylene group containing from about 2 to about 3 carbon atoms or mixtures thereof;
  • x is from 0 to about 3 : and each R 5 is an alkyl or hydroxyalkyl group containing from about 1 to about 3 carbon atoms or a polyethylene oxide group containing from about 1 to about 3 ethylene oxide groups.
  • the R 5 groups can be attached to each other, e.g., through an oxygen or nitrogen atom, to form a ring structure .
  • These amine oxide surfactants in particular include C ⁇ o _ Ci 8 alkyl dimethyl amine oxides and C 8 -C 12 alkoxy ethyl dihydroxy ethyl amine oxides.
  • the cleaning compositions of the present invention typically comprise from 0.2% to about 15%, preferably from about 1% to about 10% by weight of such semi- polar nonionic surfactants.
  • compositions according to the present invention may further comprise a builder system.
  • a builder system Any conventional builder system is suitable for use herein including aluminosilicate materials, silicates, polycarboxylates and fatty acids, materials such as ethylenediamine tetraacetate, metal ion
  • sequestrants such as aminopolyphosphonates, particularly ethylenediamine tetramethylene phosphonic acid and diethylene triamine pentamethylenephosphonic acid.
  • aminopolyphosphonates particularly ethylenediamine tetramethylene phosphonic acid and diethylene triamine pentamethylenephosphonic acid.
  • phosphate builders can also be used herein.
  • Suitable builders can be an inorganic ion exchange material, commonly an inorganic hydrated aluminosilicate material, more particularly a hydrated synthetic zeolite such as hydrated zeolite A, X, B, HS or MAP.
  • inorganic ion exchange material commonly an inorganic hydrated aluminosilicate material, more particularly a hydrated synthetic zeolite such as hydrated zeolite A, X, B, HS or MAP.
  • Another suitable inorganic builder material is layered
  • silicate e.g. SKS-6 (Hoechst) .
  • SKS-6 is a crystalline layered silicate consisting of sodium silicate (Na 2 Si 2 0 5 ) .
  • Suitable polycarboxylates containing one carboxy group include lactic acid, glycolic acid and ether derivatives thereof as disclosed in Belgian Patent Nos. 831,368, 821,369 and
  • Polycarboxylates containing two carboxy groups include the water-soluble salts of succinic acid, malonic acid, (ethylenedioxy) diacetic acid, aleic acid, diglycollic acid, tartaric acid, tartronic acid and fumaric acid, as well as the ether carboxylates described in German Offenle-enschrift
  • Polycarboxylates containing three carboxy groups include, in particular, water-soluble citrates, aconitrates and citraconates as well as succinate derivatives such as the
  • Alicyclic and heterocyclic polycarboxylates include cyclopentane-cis , cis-cis-tetracarboxylates , cyclopentadienide pentacarboxylates, 2, 3 , 4, 5-tetrahydro-furan - cis, cis, cis- tetracarboxylates , 2 , 5-tetrahydro-furan-cis, discarboxylates, 2 , 2 , 5 , 5 , -tetrahydrof ran - tetracarboxylates, 1, 2 , 3 , 4 , 5 , 6-hexane - hexacarboxylates and carboxymethyl derivatives of polyhydric alcohols such as sorbitol, mannitol and xylitol.
  • polyhydric alcohols such as sorbitol, mannitol and xylitol.
  • Aromatic polycarboxylates include mellitic acid, pyromellitic acid and the phthalic acid derivatives disclosed in British Patent No. 1,425,343. Of the above, the preferred polycarboxylates are hydroxy- carboxylates containing up to three carboxy groups per molecule, more particularly citrates.
  • Preferred builder systems for use in the present compositions include a mixture of a water-insoluble aluminosilicate builder such as zeolite A or of a layered silicate (SKS-6) , and a water-soluble carboxylate chelating agent such as citric acid.
  • a water-insoluble aluminosilicate builder such as zeolite A or of a layered silicate (SKS-6)
  • a water-soluble carboxylate chelating agent such as citric acid.
  • a suitable chelant for inclusion in the cleaning compositions in accordance with the invention is ethylenediamine-N,N' - disuccinic acid (EDDS) or the alkali metal, alkaline earth metal, ammonium, or substituted ammonium salts thereof, or mixtures thereof.
  • EDDS compounds are the free acid form and the sodium or magnesium salt thereof. Examples of such preferred sodium salts of EDDS include Na 2 EDDS and Na 4 EDDS. Examples of such preferred magnesium salts of EDDS include
  • MgEDDS and Mg 2 EDDS are the most preferred for inclusion in compositions in accordance with the invention.
  • Preferred builder systems include a mixture of a water- insoluble aluminosilicate builder such as zeolite A, and a water soluble carboxylate chelating agent such as citric acid.
  • builder materials that can form part of the builder system for use in granular compositions include inorganic materials such as alkali metal carbonates, bicarbonates, silicates, and organic materials such as the organic phosphonates , amino polyalkylene phosphonates and amino polycarboxylates .
  • inorganic materials such as alkali metal carbonates, bicarbonates, silicates
  • organic materials such as the organic phosphonates , amino polyalkylene phosphonates and amino polycarboxylates .
  • suitable water-soluble organic salts are the homo- or co-polymeric acids or their salts, in which the polycarboxylic acid comprises at least two carboxyl radicals separated form each other by not more than two carbon atoms.
  • Polymers of this type are disclosed in GB-A-1, 596, 756.
  • Examples of such salts are polyacrylates of MW 2000-5000 and their copolymers with maleic anhydride, such copolymers having a molecular weight of from 20,000 to 70,000, especially about 40,000.
  • Detergency builder salts are normally included in amounts of from 5% to 80% by weight of the composition. Preferred levels of builder for liquid detergents are from 5% to 30%.
  • Preferred cleaning compositions in addition to the family 6 endo- ⁇ -l,4-glucanase, comprise other enzyme(s) which provides cleaning performance and/or fabric care benefits.
  • proteases include proteases, lipases, cutinases, amylases, other cellulases, peroxidases, oxidases (e.g. laccases) .
  • proteases Any protease suitable for use in alkaline solutions can be used. Suitable proteases include those of animal, vegetable or microbial origin. Microbial origin is preferred. Chemically or genetically modified mutants are included.
  • the protease may be a serine protease, preferably an alkaline microbial protease or a trypsin-like protease.
  • alkaline proteases are subtilisins, especially those derived from Bacillus, e.g., subtilisin Novo, subtilisin Carlsberg, subtilisin 309, subtilisin 147 and subtilisin 168 (described in WO 89/06279) .
  • trypsin-like proteases are trypsin (e.g. of porcine or bovine origin) and the Fusarium protease described in WO 89/06270.
  • Preferred commercially available protease enzymes include those sold under the trade names Alcalase, Savinase, Primase, Durazym, and Esperase by Novo Nordisk A/S (Denmark) , those sold under the tradename Maxatase, Maxacal, Maxapem, Properase, Purafect and Purafect OXP by Genencor International, and those sold under the tradename Opticlean and Optimase by Solvay Enzymes.
  • Protease enzymes may be incorporated into the compositions in accordance with the invention at a level of from 0.00001% to 2% of enzyme protein by weight of the composition, preferably at a level of from 0.0001% to 1% of enzyme protein by weight of the composition, more preferably at a level of from 0.001% to 0.5% of enzyme protein by weight of the composition, even more preferably at a level of from 0.01% to 0.2% of enzyme protein by weight of the composition.
  • Lipases Any lipase suitable for use in alkaline solutions can be used. Suitable lipases include those of bacterial or fungal origin. Chemically or genetically modified mutants are included.
  • useful lipases include a Humicola lanuqinosa lipase, e.g., as described in EP 258 068 and EP 305 216, a Rhizomucor miehei lipase, e.g., as described in EP 238 023, a Candida lipase, such as a C. antarctica lipase, e.g., the C. antarctica lipase A or B described in EP 214 761, a Pseudomonas lipase such as a P. alcaligenes and P. pseudoalcaligenes lipase, e.g., as described in EP 218 272, a P.
  • a Humicola lanuqinosa lipase e.g., as described in EP 258 068 and EP 305 216
  • a Rhizomucor miehei lipase e.g., as described in EP 238 023
  • cepacia lipase e.g., as described in EP 331 376, a P. stutzeri lipase, e.g., as disclosed in GB 1,372,034, a P. fluorescens lipase, a Bacillus lipase , e.g., a B. subtilis lipase (Dartois et al., (1993), Biochemica et Biophysica acta 1131, 253-260) , a B. stearo- thermophilus lipase (JP 64/744992) and a B. pu ilus lipase (WO 91/16422) .
  • cloned lipases may be useful, including the Penicillium camembertii lipase described by Yamaguchi et al., (1991), Gene 103, 61-67), the Geotricum candidum lipase (Schimada, Y. et al., (1989), J. Biochem., 106, 383-388) , and various Rhizopus lipases such as a R. delemar lipase (Hass, M.J et al. , (1991), Gene 109, 117-113), a R. niveus lipase (Kugimiya et al., (1992), Biosci. Biotech. Biochem. 56, 716-719) and a R. oryzae lipase.
  • R. delemar lipase Hass, M.J et al. , (1991), Gene 109, 117-113
  • R. niveus lipase Kugi
  • cutinases may also be useful, e.g., a cutinase derived from Pseudomonas mendocina as described in WO 88/09367, or a cutinase derived from Fusarium solani pisi (e.g. described in WO 90/09446) .
  • lipases such as Ml LipaseTM, Luma fastTM and LipomaxTM (Genencor) , LipolaseTM and Lipolase UltraTM (Novo Nordisk A/S) , and Lipase P "Amano” (Amano Pharmaceutical Co. Ltd.).
  • the lipases are normally incorporated in the detergent composition at a level of from 0.00001% to 2% of enzyme protein by weight of the composition, preferably at a level of from 0.0001% to 1% of enzyme protein by weight of the composition, more preferably at a level of from 0.001% to 0.5% of enzyme protein by weight of the composition, even more preferably at a level of from 0.01% to 0.2% of enzyme protein by weight of the composition.
  • Amylases Any amylase (a and/or b) suitable for use in alkaline solutions can be used. Suitable amylases include those of bacterial or fungal origin. Chemically or genetically modified mutants are included. Amylases include, for example, a- amylases obtained from a special strain of B. licheniformis.
  • amylases are Duramyl TM, TermamylTM, FungamylTM and BANTM (available from Novo Nordisk A/S) and RapidaseTM and Maxamyl PTM (available from Genencor) .
  • amylases are normally incorporated in the detergent composition at a level of from 0.00001% to 2% of enzyme protein by weight of the composition, preferably at a level of from 0.0001% to 1% of enzyme protein by weight of the composition, more preferably at a level of from 0.001% to 0.5% of enzyme protein by weight of the composition, even more preferably at a level of from 0.01% to 0.2% of enzyme protein by weight of the composition.
  • Cellulases Any cellulase suitable for use in alkaline solutions can be used. Suitable cellulases include those of bacterial or fungal origin. Chemically or genetically modified mutants are included. Suitable cellulases are disclosed in US 4,435,307 which discloses fungal cellulases produced from Humicola insolens , in WO 96/34108 and WO 96/34092 which disclose bacterial alkalophilic cellulases (BCE 103) from Bacillus , and 5 in WO 94/21801, US 5,475,101 and US 5,419,778 which disclose EG III cellulases from Trichoderma . Especially suitable cellulases are the cellulases having colour care benefits. Examples of such cellulases are cellulases described in European patent application No. 0 495 257 and the endoglucanase of the present
  • CommerciIally avaiIlable cellulases i.nclude CelluzymeTM and CarezymeTM produced by a strain of Humicola insolen ⁇ (Novo Nordisk A/S), KAC-500(B)TM (Kao Corporation), and PuradaxTM (Genencor International) .
  • Peroxidases/Oxidases Peroxidases/Oxidases : Peroxidase enzymes are used in combination with hydrogen peroxide or a source thereof (e.g. a percarbonate, perborate or persulfate) . Oxidase enzymes are used
  • Peroxidase and/or oxidase enzymes are normally incorporated in the detergent composition at a level of from
  • Mixtures of the above mentioned enzymes are encompassed herein, in particular a mixture of a protease, an amylase, a lipase and/or a cellulase.
  • the hydrogen peroxide releasing agents can be used in combination with bleach activators such as tetra- acetylethylenediamine (TAED) , nonanoyloxybenzenesulfonate (NOBS, described in US 4,412,934), 3 , 5-trimethyl- hexsanoloxybenzenesulfonate (ISONOBS, described in EP 120 591) or pentaacetylglucose (PAG) , which are perhydrolyzed to form a peracid as the active bleaching species, leading to improved bleaching effect.
  • bleach activators such as tetra- acetylethylenediamine (TAED) , nonanoyloxybenzenesulfonate (NOBS, described in US 4,412,934), 3 , 5-trimethyl- hexsanoloxybenzenesulfonate (ISONOBS, described in EP 120 591) or pentaacetylglucose (PAG
  • bleach activators C8 (6-octanamido-caproyl) oxybenzene-sulfonate, C9(6- nonanamido caproyl) oxybenzenesulfonate and CIO (6-decanamido caproyl) oxybenzenesulfonate or mixtures thereof.
  • acylated citrate esters such as disclosed in European Patent Application No. 91870207.7.
  • bleaching agents including peroxyacids and bleaching systems comprising bleach activators and peroxygen bleaching compounds for use in cleaning compositions according to the invention are described in application USSN 08/136,626.
  • the hydrogen peroxide may also be present by adding an enzymatic system (i.e. an enzyme and a substrate therefore) which is capable of generation of hydrogen peroxide at the beginning or during the washing and/or rinsing process.
  • an enzymatic system i.e. an enzyme and a substrate therefore
  • Such enzymatic systems are disclosed in European Patent Application EP 0 537 381.
  • Bleaching agents other than oxygen bleaching agents are also known in the art and can be utilized herein.
  • One type of non-oxygen bleaching agent of particular interest includes photoactivated bleaching agents such as the sulfonated zinc and- /or aluminium phthalocyanines. These materials can be deposited upon the substrate during the washing process. Upon irradiation with light, in the presence of oxygen, such as by hanging clothes out to dry in the daylight, the sulfonated zinc phthalocyanine is activated and, consequently, the substrate is bleached.
  • Preferred zinc phthalocyanine and a photoactivated bleaching process are described in US 4,033,718.
  • detergent composition will contain about 0.025% to about 1.25%, by weight, of sulfonated zinc phthalocyanine.
  • Bleaching agents may also comprise a manganese catalyst.
  • the manganese catalyst may, e.g., be one of the compounds described in "Efficient manganese catalysts for low-temperature bleaching", Nature 369, 1994, pp. 637-639.
  • a suds suppressor exemplified by silicones, and silica-silicone mixtures.
  • Silicones can generally be represented by alkylated polysiloxane materials, while silica is normally used in finely divided forms exemplified by silica aerogels and xerogels and hydrophobic silicas of various types. Theses materials can be incorporated as particulates, in which the suds suppressor is advantageously releasably incorporated in a water-soluble or waterdispersible, substantially non surface-active detergent impermeable carrier.
  • the suds suppressor can be dissolved or dispersed in a liquid carrier and applied by spraying on to one or more of the other components.
  • a preferred silicone suds controlling agent is disclosed in US 3,933,672.
  • Other particularly useful suds suppressors are the self-emulsifying silicone suds suppressors, described in German Patent Application DTOS 2,646,126.
  • An example of such a compound is DC-544, commercially available form Dow Corning, which is a siloxane-glycol copolymer.
  • Especially preferred suds controlling agent are the suds suppressor system comprising a mixture of silicone oils and 2-alkyl-alkanols. Suitable 2-alkyl- alkanols are 2-butyl-octanol which are commercially available under the trade name Isofol 12 R.
  • Such suds suppressor system are described in European Patent Application EP 0 593 841.
  • compositions can comprise a silicone/ silica mixture in combination with fumed nonporous silica such as Aerosil R .
  • the suds suppressors described above are normally employed at levels of from 0.001% to 2% by weight of the composition, preferably from 0.01% to 1% by weight.
  • compositions may be employed such as soil-suspending agents, soil-releasing agents, optical brighteners, abrasives, bactericides, tarnish inhibitors, coloring agents, and/or encapsulated or nonencapsulated perfumes.
  • encapsulating materials are water soluble capsules which consist of a matrix of polysaccharide and polyhydroxy compounds such as described in GB 1,464,616.
  • Suitable water soluble encapsulating materials comprise dextrins derived from ungelatinized starch acid esters of substituted dicarboxylic acids such as described in US 3,455,838. These acid-ester dextrins are, preferably, prepared from such starches as waxy maize, waxy sorghum, sago, tapioca and potato. Suitable examples of said encapsulation materials include N-Lok manufactured by National Starch. The N-Lok encapsulating material consists of a modified maize starch and glucose. The starch is modified by adding monofunctional substituted groups such as octenyl succinic acid anhydride.
  • Antiredeposition and soil suspension agents suitable herein include cellulose derivatives such as methylcellulose, carboxymethylcellulose and hydroxyethylcellulose, and homo- or co-polymeric polycarboxylic acids or their salts.
  • Polymers of this type include the polyacrylates and maleic anhydride-acrylic acid copolymers previously mentioned as builders, as well as copolymers of maleic anhydride with ethylene, methylvinyl ether or methacrylic acid, the maleic anhydride constituting at least 20 mole percent of the copolymer. These materials are normally used at levels of from 0.5% to 10% by weight, more preferably form 0.75% to 8%, most preferably from 1% to 6% by weight of the composition.
  • Preferred optical brighteners are anionic in character, examples of which are disodium 4 , 4 ' -bis-(2-diethanolamino-4- anilino -s- triazin-6-ylamino) stilbene-2: 2 • disulphonate, disodium 4, - 4 '-bis- (2-morpholino-4-anilino-s-triazin-6- ylamino-stilbene-2:2 ' - disulphonate, disodium 4,4' - bis- (2,4- dianilino-s-triazin-6-ylamino) stilbene-2:2 * - disulphonate, monosodium 4 ',4'' - bis- (2, 4-dianilino-s-tri-azin-6 ylamino) stilbene-2-sulphonate, disodium 4,4' -bis-(2-anilino-4- (N-methyl-N-2-hydroxyethylamino) -s-triazin-6-yla
  • polyethylene glycols particularly those of molecular weight 1000-10000, more particularly 2000 to 8000 and most preferably about 4000. These are used at levels of from 0.20% to 5% more preferably from 0.25% to 2.5% by weight.
  • Soil release agents useful in compositions of the present invention are conventionally copolymers or terpolymers of terephthalic acid with ethylene glycol and/or propylene glycol units in various arrangements. Examples of such polymers are disclosed in US 4,116,885 and 4,711,730 and EP 0 272 033.
  • a particular preferred polymer in accordance with EP 0 272 033 has the formula:
  • polyesters as random copolymers of dimethyl terephthalate, dimethyl sulfoisophthalate, ethylene glycol and 1, 2-propanediol, the end groups consisting primarily of sulphobenzoate and secondarily of mono esters of ethylene glycol and/or 1, 2-propanediol.
  • the target is to obtain a polymer capped at both end by sulphobenzoate groups, "primarily", in the present context most of said copolymers herein will be endcapped by sulphobenzoate groups.
  • some copolymers will be less than fully capped, 5 and therefore their end groups may consist of monoester of ethylene glycol and/or 1, 2-propanediol, thereof consist “secondarily” of such species.
  • the selected polyesters herein contain about 46% by weight of dimethyl terephthalic acid, about 16% by weight of 1,2- 10 propanediol, about 10% by weight ethylene glycol, about 13% by weight of dimethyl sulfobenzoic acid and about 15% by weight of sulfoisophthalic acid, and have a molecular weight of about 3.000.
  • the polyesters and their method of preparation are described in detail in EP 311 342.
  • Fabric softening agents can also be incorporated into cleaning compositions in accordance with the present invention. These agents may be inorganic or organic in type. Inorganic
  • Organic fabric softening agents include the water insoluble tertiary amines as disclosed in GB-A1 514 276 and EP 0 011 340 and their combination with mono Ci 2 ⁇ Ci 4 quaternary ammonium salts are disclosed in EP-B-0
  • the high molecular weight polyethylene oxide materials and the water soluble cationic materials are added at levels of from 0.1% to 2%, normally from 0.15% to 1.5% by weight. These materials are normally added to the spray dried portion of the composition, although in some instances it may be more convenient to add them as a dry mixed particulate, or spray them as molten liquid on to other solid components of the composition.
  • Especially suitable polymeric dye-transfer inhibiting agents are polyamine N-oxide polymers, copolymers of N-vinyl- pyrrolidone and N-vinylimidazole, polyvinylpyrrolidone polymers, polyvinyloxazolidones and polyvinylimidazoles or mixtures thereof.
  • the cleaning composition according to the invention can be in liquid, paste, gels, bars or granular forms.
  • Non-dusting granulates may be produced, e.g., as disclosed in US 4,106,991 and 4,661,452 (both to Novo Industri A/S) and may optionally be coated by methods known in the art.
  • waxy coating materials are poly(ethylene oxide) products (polyethyleneglycol, PEG) with mean molecular weights of 1000 to 20000; ethoxylated nonylphenols having from 16 to 50 ethylene oxide units; ethoxylated fatty alcohols in which the alcohol contains from 12 to 20 carbon atoms and in which there are 15 to 80 ethylene oxide units; fatty alcohols; fatty acids; and mono- and di- and triglycerides of fatty acids.
  • film- forming coating materials suitable for application by fluid bed techniques are given in GB 1483591.
  • the liquid detergent compositions according to the present invention will contain a lower amount of water, compared to conventional liquid detergents.
  • the water content of the concentrated liquid detergent is less than 30%, more preferably less than
  • the cleaning composition is a granular detergent composition containing no more than 40%, preferably no more than 15%, by weight of inorganic filler salt.
  • compositions of the invention may for example, be formulated as hand and machine laundry detergent compositions including laundry additive compositions and compositions suitable for use in the pretreatment of stained fabrics, rinse added fabric softener compositions, and compositions for use in
  • compositions for the present invention are not necessarily meant to limit or otherwise define the scope of the invention.
  • LAS Sodium linear C 12 alkyl benzene sulphonate
  • TAS Sodium tallow alkyl sulphate
  • XYAS Sodium C lx - C l ⁇ alkyl sulfate
  • XYEZS C lx - Ciy sodium alkyl sulfate condensed with an average of Z moles of ethylene oxide per mole
  • Nonionic C ⁇ 3 - C 15 mixed ethoxylated/propoxylated fatty alcohol with an average degree of ethoxylation of 3.8 and an average degree of propoxylation of 4.5 sold under the tradename
  • Polyacrylate Polyacrylate homopolymer with an average molecular weight of 8,000 sold under the tradename PA30 by BASF
  • Gmbh Zeolite A Hydrated Sodium Aluminosilicate of formula
  • Percarbonate Anhydrous sodium percarbonate bleach of empirical formula 2Na 2 C0 3 .3H 2 0 2 TAED: Tetraacetyl ethylene diamine
  • DETPMP Diethylene triamine penta (methylene phosphonic acid) , marketed by Monsanto under the Tradename Dequest 2060
  • PVP Polyvinylpyrrolidone polymer
  • EDDS Ethylenediamine-N, N' -disuccinic acid, [S,S] isomer in the form of the sodium salt
  • Enzyme of the invention 0.1
  • Example III Granular fabric cleaning compositions in accordance with the invention which are especially useful in the laundering of coloured fabrics were prepared as follows:
  • Granular fabric cleaning compositions in accordance with the invention which provide "Softening through the wash” capability may be prepared as follows: 45AS - 10.0
  • Enzyme of the invention 0.10 0.05
  • the cellulolytic activity may be measured in endo-cellulase units (ECU), determined at pH 7.5, with carboxymethyl cellulose (CMC) as substrate.
  • ECU endo-cellulase units
  • CMC carboxymethyl cellulose
  • the ECU assay quantifies the amount of catalytic activity present in the sample by measuring the ability of the sample to 0 reduce the viscosity of a solution of carboxy-methylcellulose (CMC).
  • CMC carboxy-methylcellulose
  • the assay is carried out at 40°C; pH 7.5; 0.1M phosphate buffer; time 30 min; using a relative enzyme standard for reducing the viscosity of the CMC Hercules 7 LFD substrate; enzyme concentration approx. 0.15 ECU/ l.
  • the arch standard is defined 5 to 8200 ECU/g.
  • the relative tensile strength loss (%TSL) is quantified 5 versus "enzyme blank", i.e. an experiment where the fabric is incubated in buffer without any enzyme present and the cellulase is then classified into one of the following 4 groups:
  • inverting endoglucanases were 15 tested: a. " 43 kD EGV from the fungal species Humicola in ⁇ olen ⁇ , DSM 1800, belonging to family 45 of glycosyl hydrolases and described in detail in WO 91/17243. b. EGVI from the fungal species Humicola in ⁇ olen ⁇ , DSM 20 1800, belonging to the cellulase family 6 and having the amino acid sequence listed in SEQ ID NO: 4. The DNA sequence encoding for this enzyme is listed in SEQ ID NO: 3 (the coding region corresponding to positions 16-1356) .
  • Swatches of 7x7 cm swatches of black, woven cotton cloth were stapled to one common piece of cloth, and 7x7 cm swatches of blue knitted cotton cloth was stapled to another piece of cloth. This together with a standardised household load of laundry cloth was entered into a household washing machine.
  • TAKA-R 5' CCCCATCCTTTAACTATAGCGAAATGG
  • Humicola in ⁇ olen ⁇ Cel6A In order to alter Humicola in ⁇ olen ⁇ Cel6A to a Humicola endoglucanase type in order to create an enzyme having improved performance in colour clarification, mutations which reduce the length of one or more of the binding cleft encompassing loops was performed.
  • the extent of the binding cleft encompassing loops can be determined either from the multiple sequence alignment or by solving the three dimensional X-ray structure of Humicola in ⁇ olen ⁇ Cel6A and perform the same analysis as described for Humicola in ⁇ olen ⁇ EGIV (Cel6B) .
  • the four longer loops encompassing the binding cleft are in the numbering scheme of Humicola in ⁇ olen ⁇ Cel6A V173-N195, N307-D330, K360-G376 and W397-F435 (using Humicola in ⁇ olen ⁇ Cel6A numbering) when the multiple sequence alignment method is used and it is Y174-N195, N307-D330, K360-Y391 and W397-F435 F435 (using Humicola in ⁇ olen ⁇ Cel6A numbering) when the X-ray structure method is used. Constructions of loop trimming:
  • cel6A-type cellulases from the species Fusarium oxysporum, Trichoderma ree ⁇ ei, Agaricu ⁇ bi ⁇ - pora, Acremonium cellulyticu ⁇ , Phanerochaete chry ⁇ o ⁇ porium, Penicillium purpurogenum which are aligned in fig. 1A/B can be altered to a Humicola endoglucanase type enzyme (Cel6B-type) .
  • Variants of the present invention may show improved performance with respect to an altered sensitivity towards anionic surfactants (tensides) .
  • Anionic tensides are products frequently incorporated into detergent compositions. Unfolding of cellulases tested so far, is accompanied by a decay in the intrinsic fluorescence of the proteins. The intrinsic fluorescence derives from Trp side chains (and to a smaller extent Tyr side chains) and is sensitive to the hydrophobicity of the side chain environment. Unfolding leads to a more hydrophilic environment as the side-chains become more exposed to solvent, and this quenches fluorescence.
  • Fluorescence is followed on a Perkin/ElmerTM LS50 luminescence spectrometer.
  • the greatest change in fluore- scence on unfolding is obtained by excitation at 280 nm and emission at 340 nm.
  • Slit widths (which regulate the magnitude of the signal) are usually 5 nm for both emission and excitation at a protein concentration of 5 ⁇ g/ml. Fluorescence is measured in 2-ml quartz cuvettes thermostatted with a circulating water bath and stirred with a small magnet. The magnet-stirrer is built into the spectrometer.
  • Positions already containing one of these residues are the primary target for mutagenesis
  • secondary targets are positions which has one of these residues on an equivalent position in another cellulase
  • third target are any surface exposed re- sidue.
  • wild type Humicola in ⁇ olen ⁇ Cel6B cellulase are being compared to Humicola in ⁇ olen ⁇ Cel6B cellulase variants belonging to all three of the above groups, comparing the stability towards LAS in detergent.
  • the reaction medium contained 5.0 g/1 of a commercial regular powder detergent from the detergent manufacturer NOPA Den- mark.
  • the detergent was formulated without surfactants for this experiment and pH adjusted to pH 7.0.
  • the reaction medium included 0.5 g/1 PASC and was with or without 1 g/1 LAS (linear alkylbenzenesulphonate) , which is an anionic surfactant, and the reaction proceeded at the temperature 30°C for 30 minu- tes.
  • Cellulase was dosed at 0.20 S-CEVU/1. After the 30 minutes of incubation the reaction was stopped with 2 N NaOH and the amount of reducing sugar ends determined through reduction of p- hydroxybenzoic acid hydrazide. The decrease in absorption of re- prised p-hydroxybenzoic acid hydrazide relates to the cellulase activity.
  • Neocallima ⁇ tix patriciarum Taking the Neocallimastix patriciarum SPTREMBL entry ql2646 as an example figure 8 shows the residues considered as being on the surface of the Neocallimastix patriciarum catalytic core domain.
  • Preferably potentially positively charged residues should be mutagenized to neutral or negatively charged residues.
  • Orpinomyce ⁇ ⁇ p. CelC this results to (using the numbering scheme of Humicola in ⁇ olen ⁇ Cel6B) : K16, R27, K42, K43, R64, K72, R91, R131, H156, H159, K160, K169, K173, R176, H183, R195, R205, K212, R214, H247, R252, R257, R260, K262, R272, K286, R293, K310, R320 or H332.
  • the pH activity profile of a cellulase is governed by the pH dependent behavior of specific titratable groups, typically the acidic residues in the active site.
  • the pH profile can be altered by changing the electrostatic environment of these residues, either by substitution of residues involving charged or potentially charged groups such as Arg (R) , Lys (K) , Tyr (Y) , His (H) , Glu (E) , Asp (D) or Cys (C) if not involved in a disulphide bridge or by changes in the surface accessibility of these specific titratable groups by mutation of these specific residues on the surface of the enzyme close to the proton donor as described above or by mutation of residues in the vicinity of the binding cleft as described herein, preferably by mutation (s) in the binding cleft within 5h, more preferably 2.5A, of the substrate, or preferably by mutations within l ⁇ A, more preferably ⁇ A, from the active site (D139) .
  • the relative alkaline activity can be increased by creating variants involving potentially charged residues which are mutated towards a more negatively charged residue and/or by altering residues not more than ⁇ A from the residues in the binding cleft.
  • Neocallimastix patriciarum cellulase cDNA (celA) homologous to 10 Trichoderma reesei cellobiohydrolase II. Appl. Environ. Micro- biol., 62 (6) :1889-1896.

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Abstract

Cleaning compositions comprising one or more enzymes having cellulolytic activity wherein at least 25 % of the total weight of cellulolytic active protein derives from the presence of a Humicola endo-1,4-β-glucanase or Humicola-like cellulase of the glycolsyl hydrolase family 6, the Humicola-like cellulase being an enzyme comprising a catalytically core domain having an amino acid sequence being at least 35 % homologous to the appended SEQ ID NO:4; a method of constructing a variant of a parent Humicola family 6 (Cel6B) endo-beta-1,4-glucanase or a Humicola-like family 6 cellulase which variant has endo-beta-1,4-glucanase activity and improved detergent compatibility as compared to the parent endo-beta-1,4-glucanase or cellulase; and variants mutated eg. in positions 20, 56, 94, 95, 103, 182, 183 and 318 (Cel6B numbering).

Description

FAMILY 6 ENDO-l,4-β-GLUCANASE VARIANTS AND CLEANING COMPOSITIONS CONTAINING THEM
The present invention relates to cleaning compositions, including laundry detergent compositions and fabric softener or fabric conditioning compositions, containing an endo-l,4-β- glucanase of the glycosyl hydrolase family 6, preferably an improved variant of a parent Humicola endoglucanase or Humicola- li e cellulase; the improved variants; and a method of con- structing the variants.
BACKGROUND OF THE INVENTION
Performance of a cleaning composition, for use in a washing or cleaning method, such as a laundry, dishwashing or sur- face cleaning method, is judged by a number of factors, including the ability to remove soils, the ability to prevent the re- deposition of the soils, or, in case of laundry, the ability to maintain the original colours of the washed garment and the ability to maintain fabric or garment durability. The anti- harshening or softening effect of cellulase on fabrics and the fabric care (colour care/colour clarification) effect is known, e.g. from GB 1 368 599 and EP 269 168, along with other very beneficial cellulolytic effects such as particulate soil removal and de-pilling. Fabric conditioning or fabric softener compositions, in particular compositions to be used in the rinse cycle of laundry washing processes, are also well known. Typically, such compositions contain a water-insoluble quaternary-ammonium fabric softening agent, the most commonly used having been di-long alkyl chain ammonium chloride. Fabric conditioning compositions comprising cellulase have also been suggested, e.g. in US 5,445,747, in particular compositions using a specific ~43kD cellulase obtained from the fungus Humicola insolens .
Cellulose is a polymer of glucose linked by β-1,4- glucosidic bonds. Cellulose chains form numerous intra- and in- termolecular hydrogen bonds, which result in the formation of insoluble cellulose microfibrils. Microbial hydrolysis of cellulose to glucose involves the following three major classes of cellulases: endo-l,4-β-glucanases (EC 3.2.1.4), which cleave β- 1,4-glucosidic links randomly throughout cellulose molecules; cellobiohydrolases (EC 3.2.1.91) (exoglucanases) , which digest cellulose from the nonreducing end; and β-glucosidases (EC 3.2.1.21), which hydrolyse cellobiose and low-molecular-mass cellodextrins to release glucose. Most cellulases consist of a cellulose-binding domain (CBD) and a catalytic core or catalytic domain (CAD = catalytically active domain) separated by a linker rich in proline and hydroxy amino acid residues. All cellulases hydrolyse by either a "retaining" or "inverting" mechanism.
Cellulases are produced by many microorganisms and are often present in multiple forms. Recognition of the economic significance of the enzymatic degradation of cellulose has promoted an extensive search for industrially useful microbial cellu- lases. As a result, the enzymatic properties and the primary structures of a large number of cellulases have been investigated. On the basis of the results of a hydrophobic cluster analysis of the amino acid sequence of the catalytically active domain (CAD) , these cellulases have been placed into 11 differ- ent families of glycosyl hydrolases (Henrissat, 1991; Henrissat et al., 1993). One of these families is known as the cellulase family B or as the glycosyl hydrolase family 6. Up till now, the following enzymes have been identified as belonging to this family: Agaricus bisporus exoglucanase 3 (cel3) , Cellulomonas fimi endoglucanase A (cenA) , Cellulomonas fimi exoglucanase A (cbhA) , Microspora bispora endoglucanase A (celA) , Streptomyces halste- dii endoglucanase A (celA) , Streptomyces strain KSM-9 endoglucanase 1 (casA) , Thermomonospora fusca endoglucanase E-2 (celB) , Trichoderma reesei exoglucanase II (cbh2) , and probably Neocal- limastix patriciarum exoglucanase (celA) (Denman et al., 1996) and Orpinomyces εp. (celA) . The following two conserved regions have been used as signature patterns (PROSITE: PDOC00563. February 1997): V-x-Y-x(2)-P-x-R-D-C-[GSAF]-x(2)-[GSA] (2)-x-G; and [LIVMYA]-[LIVA]-[LIVT]-[LIV]-E-P-D-[SAL]-[LI]-[PSAG] . The first conserved region contains a conserved aspartic acid residue which is potentially involved in the catalytic mechanism; the aspartate is followed by a cysteine which is involved in a di- sulfide bond. The second conserved region contains an aspartate which seems to be the proton donor in the catalytic mechanism. WO 97/20025 and WO 97/20026 discloses detergent compositions comprising an endoglucanase from Thermomonospora fuεca . An interesting feature of family 6 is that it contains both endoglucanases and exoglucanases which show definite differences in amino acid sequence, the exoglucanases having extra amino acid insertions. Without being bound to this theory it is presently believed that cellulolytic enzymes belonging to family 6 are inverting type enzymes, i.e. hydrolyse the β-1,4- glucosidic bond with inversion of anomeric configuration. The inverting mechanism involves protonation of the glycosidic oxygen of the scissile bond by an acidic amino acid residue (general acid catalyst) with concerted attack of a water ole- cule at the anomeric carbon. The nucleophilicity of this water molecule is greatly increased through deprotonation by a basic amino acid residue (general basic catalyst) . The partial positive charge formed at the anomeric carbon in the transition state is stabilised through resonance with the ring oxygen. This gives the transition state significant oxocarbonium ion character which is stabilised by electrostatic interactions with the nearby carboxylate side chains and by specific binding interactions with the sugar in its half-chair conformation. In general, only glutamate and aspartate residues act directly as general acid or base catalysts in glycosidases (Damude et. al. 1996) .
Detergent compositions with cellulases, either monocompo- nent endoglucanases or cellulase enzyme systems, i.e. a mixture of cellulases, have successfully been used commercially for some years. However, these compositions are neither recommendable for use in a presoaking bath nor for use in case of prolonged storage of the washed and rinsed wet laundry, e.g. in the washing machine prior to line or tumbler drying, since such prolonged enzymatic impact may result in a weakening of the fabric or garment presumably due to the actual (but unknown) mechanisms by which the cellulase types hitherto used in cleaning compositions have acted on the cellulose-containing or cellulosic fabric.
Thus, it is an object of the present invention to provide cleaning compositions containing enzymes with cellulolytic ac- tivity which enzymes provides colour clarification (colour care benefits) and possibly also soil removal of the laundry without any substantial weakening thereof when the laundry is subjected to pre-soaking or wet storage.
SUMMARY OF THE INVENTION
We have now found that endo-l,4-β-glucanases of the glycosyl hydrolase family 6 may valuably be incorporated into cleaning compositions at such a level that at least about 25% of the total weight of cellulolytic active enzyme protein present in the composition derives from the family 6 endoglucanase. The inclusion of such enzymes provides colour care benefits, i.e. colour clarification of laundry containing cotton or other cellu- losic fabrics. It is known that such colour care benefit is also provided by endo-1, 4-β-glucanases of the glycosyl hydrolase families 5, 7, 45, and 12. However, we now have surprisingly found that, in contrast to endoglucanases belonging to other families, application of family 6 endoglucanases in cleaning compositions delivers an important improvement in the degree of fabric durability, i.e. a considerable reduction in fabric weakening due to subjecting the laundry to a pre-soaking bath or prolonged wet storage of the washed or rinsed laundry within the washing machine.
Accordingly, in a first aspect the present invention re- lates to cleaning compositions comprising one or more enzymes having cellulolytic activity wherein at least 25% of the total weight of cellulolytic active enzyme protein derives from the presence of a Humicola endo-1, 4-β-glucanase or Humi cola-like cellulase (endo-type (Cel6B) or exo-type (Cel6A))of the glycosyl hydrolase family 6, the Humicola-like cellulase being an enzyme comprising a catalytically core domain having an amino acid sequence being at least 35% homologous to the appended SEQ ID NO: 4.
By using the present invention, it is now possible to use , high performance cleaning compositions in any cleaning or laundering method without a substantial, negative impact on fabric durability. In second and third aspects, the invention provides a method of constructing a variant of a parent Humicola family 6 en- do-beta-l,4-glucanase or a Humicola-like family 6 cellulase which variant has endo-beta-l,4-glucanase activity and improved deter- gent compability as compared to the parent endo-beta-l,4-glucanase or cellulase; and variants provided by the method.
By using the protein engineering method of the invention it is now possible to provide well-performing endoglucanases from enzymatic starting material originally having different activities and/or different properties, eg can a cellobiohydrolase enzyme with poor detergent compability be engineered into a well- performing endoglucanase enzyme based on the findings disclosed herein.
THE DRAWINGS
In the accompanying drawings.
Fig. 1 shows ClustalW multiple sequence alignment of Family 6 cellulases. The ! SS_HI_CEL6B row shows the definition of α- helical (H) and β-strand (S) regions. Fig. 2 shows the nucleotide sequence of pCA6H from BamHI- Xbal; the translational initiation codon is underlined (see e- xa ple 3) .
Fig. 3 shows the nucleotide sequence of pC6H from BamHI- Xbal „ the translational initiation codon is underlined (see e- xample 3) .
Figure 4: Secondary structure elements (strand and helix only) of catalytic core domain of Humicola insolens Cel6B as determined by DSSP for the two independent molecules in the asymmetric unit. (H) α-helix, (3) 3-10-helix, (S) β-strand. Figure 5: The loop regions encompassing the binding cleft in the catalytic core region of Humicola insolens Cel6B. (L) indicate the defined loop regions encompassing the binding cleft,
(H) α-helical structure in both molecules, (S) β-strand regions in both molecules. Fig. 6 shows the loop regions encompassing the binding cleft in Humicola insolens Cel6A as determined from sequence alignment to Humicola insolens EGIV (Cel6B) . The numbering refers to the mature full length protein. Fig. 7 shows the loop regions encompassing the binding cleft in Humicola insolens Cel6A as determined from analysis of X-ray structure.
Fig. 8: Residues on the surface of Humicola insolens Cel6B catalytic core domain and Neocallimastix patriciarum catalytic core domain (Q12646) are shown in bold and underline (see example 6) .
Figure 9: Residues on the surface of Humicola insolens Cel6B catalytic core domain and Orpinomyces sp . CelA catalytic core domain (P78720) are shown in bold and underline (see example 6) .
Figure 10: Residues on the surface of Humicola insolens Cel6B catalytic core domain and Orpinomyces sp . CelC catalytic core domain (P78721) are shown in bold and underline (see exam- pie 6) .
In addition to the drawings, the present specification contains two appendices:
Appendix 1 shows the structural coordinates of Humicola insolens EG VI (Cel6B) endo-beta-1, 4-glucanase. Appendix 2 shows the structural coordinates of Humicola insolens Cel6A cellulase.
DETAILED DESCRIPTION OF THE INVENTION Cellulase Numbering In the context of this invention a specific numbering of amino acid residue positions in cellulolytic enzymes is employed. By aligning the amino acid sequences of known cellulases, as in figure 1 below, it is possible to unambiguously allot an amino acid position number to any amino acid residue in any cellulolytic enzyme, if its amino acid sequence is known.
In figure 1 a number of selected amino acid sequences of cellulases of different microbial origin are aligned.
Using the numbering system originating from the amino acid sequence of the cellulase (endo-β-1, 4-glucanase EG VI) obtained from the strain of Humicola insolens, DSM 1800, disclosed in e.g. Fig.l, aligned with the amino acid sequence of a number of other cellulases, it is possible to indicate the position of an amino acid residue in a cellulolytic enzyme unambiguously.
In describing the various cellulase variants produced or contemplated according to the invention, the following nomen- clatures are adapted for ease of reference:
[Original amino acid; Position; Substituted amino acid] Accordingly, the substitution of glutamine with histidine in position 119 is designated as Q119H.
Amino acid residues which represent insertions in relation to the amino acid sequence of the cellulase from Humicola insolens , are numbered by the addition of letters in alphabetical order to the preceding cellulase number, such as e.g. position *21aV for the "inserted" valine (V) , where no amino acid residue is present, between lysine at position 21 and alanine at position 22 of the amino acid sequence of the cellulase from Humicola insolens , cf. Table 1.
Deletion of a proline (P) at position 49 in the amino acid sequence of the cellulase from Humicola insolens is indicated as P49*. Multiple mutations are separated by slash marks ("/") , e.g. Q119H/Q146R, representing mutations in positions 119 and 146 substituting glutamine (Q) with histidine (H) , and glutamine (Q) acid with arginine (R) , respectively.
If a substitution is made by mutation in e.g. a cellulase derived from a strain of Humicola insolens , the product is designated e.g. "Humicola insolens/*49P" .
All positions referred to in this application by cellulase numbering refer, unless otherwise stated, to the cellulase numbers described above, and are determined relative to the amino acid sequence of the cellulase derived from Humicola insolens Cel6B. Definitions
In the specification and claims, the term "endoglucanase" is intended to denote enzymes with cellulolytic activity, espe- cially endo-1, 4-β-glucanase activity, which are classified in EC 3.2.1.4 according to the Enzyme Nomenclature (1992) and are capable of catalysing (endo) hydrolysis of 1, 4-β-D-glucosidic link- ages in cellulose, lichenin and cereal β-D-glucans including
1,4-linkages in β-D-glucans also containing 1, 3-linkages.
In the present context, the term "inverting type endoglucanase" means an endo-β-l,4-glucanase which hydrolyses the gly- cosidic bond with net inversion of anomeric configuration, i.e. which operate via a direct displacement of the leaving group by water: one residue acts as a general acid and the other as a general base.
In the present context, the term "retaining type endoglu- canase" means an endo-β-1, 4-glucanase" which hydrolyses the gly- cosidic bond with net retention of anomeric configuration, i.e. which utilizes a double-displacement mechanism involving a gly- cosyl-enzyme intermediate: one residue functions as general acid and general base while the other acts as a nucleophile and leav- ing group (McCarter et al., 1994).
The enzyme
In a preferred embodiment of the present invention, the cleaning composition comprises a Humicola endo-1, 4-β-glucanase or Humicola-like cellulase of the glycosyl hydrolase family 6 in an amount corresponding to at least 25%, preferably at least 30%, more preferably at least 40%, even more preferably at least 90%, especially at least 98%, of the total weight of enzyme protein having cellulolytic activity. In the present context, the term "Humicola-like cellulase" denotes an endoglucanase or an exoglucanase (cellobiohydrolase) comprising a catalytically core domain which has an amino acid sequence being at least 35% homologous to SEQ ID NO: 4. This is explained in further detail below. It is believed that no naturally occurring microorganism is capable of producing a cellulase complex comprising a family 6 endoglucanase in an amount of at least 25% by weight of the total amount of enzyme protein having cellulolytic activity. Accordingly, family 6 endoglucanase will usually be present in a mixture of other enzymes having cellulolytic activity. This mixture may either be a conventional fermentation product, possibly isolated and purified, from a single species of a microorganism. Besides family 6 endoglucanase, examples of other cellulolytic enzymes usually present in a fungal cellulolytic mixture, i.e. a cellulase complex produced by a fungal species, are endo-l,4-β- glucanases of the glycosyl hydrolase families 5, 7, 12, or 45; and examples of other cellulolytic enzymes usually present in a bacterial cellulolytic mixture, i.e. a cellulase complex produced by a bacterial species, are endo-1, 4-β-glucanases of the glycosyl hydrolase families 5, 8, 9, 12, 41, 45 or 48. The mixture may also be a mixture of monocomponent enzymes, preferably enzymes derived from bacterial or fungal species by using conventional recombinant techniques, which enzymes have been fermented and possibly isolated and purified separately and which may originate from different species, preferably fungal or bacterial species. The mixture may also be the fermentation product of a microorganism which acts as a host cell for expression of a recombinant endoglucanase, e.g. a family 6 endoglucanase, but which microorganism simultaneously produces other cellulases being naturally occurring fermentation products of the microorganism, i.e. the cellulase complex conventionally produced by the corresponding naturally occurring microorganism. Examples of useful recombinantly producible endo-1, 4-β-glucanases of the glycosyl hydrolase family 45 are disclosed e.g. in W091/17243, WO94/07998, and W096/29397 which are hereby incorporated by reference. Examples of other useful endo-l,4-β-glucanases of the glycosyl hydrolase families 5, 7, 8, 9, 12, 41 and 48 are disclosed e.g. in Henrissat, 1991, and in Henrissat et al, 1993, which are hereby incorporated by reference.
In another preferred embodiment, essentially all cellulolytic activity present in the composition of the invention re- suits from one single enzyme component, i.e. a monocomponent endo-l,4-β-glucanase of the glycosyl hydrolase family 6. Examples of endo-1, 4-β-glucanases of the glycosyl hydrolase family 6 are those derived from the species Humicola insolens (eg EG VI also denoted Cel6B) , Neocallimastix patriciarum, Orpinomyces sp . Further, it is comtemplated that the species Trichoderma reesei and Fusarium oxyεporum produces enzymes which are suitable as starting material for the protein engineering method by which well-performing family 6 endoglucanase variants can be constructed.
In general, the family 6 endo-l,4-β-glucanase may be present in the cleaning composition of the present invention in an amount corresponding to from about 1 ECU to about 100000 ECU per liter washing or rinsing solution.
Preferably, the family 6 endo-1, 4-β-glucanase, either native or variant, comprises one or two cellulose-binding domains (CBD) operably linked to the catalytic domain. A cellulose binding domain (CBD) is a polypeptide which has high affinity for or binds to water-insoluble forms of cellulose and chitin, including crystalline forms.
CBDs are found as integral parts of large protein complexes consisting of two or more different polypeptides, for example in hydrolytic enzymes (hydrolases) which typically are composed of a catalytic domain containing the active site for substrate hydrolysis, and a carbohydrate-binding domain or cellulose-binding domain (CBD) for binding to the insoluble matrix. Such enzymes can comprise more than one catalytic domain and one, two or three CBDs and optionally one or more polypeptide regions linking the CBD(s) with the catalytic domain (s) , the latter regions usually being denoted a "linker". Examples of hydrolytic enzymes comprising a CBD are cellulases, xylanases, mannanases, arabinofuranosidases, acetyl esterases and chitinases. CBDs have also been found in algae, e.g. the red alga Porphyra purpurea as a non-hydrolytic polysaccharide- binding protein, see Peter Tomme et al. "Cellulose-Binding Domains: Classification and Properties" in "Enzymatic Degradation of Insoluble Carbohydrates", John N. Saddler and Michael H. Penner (Eds.), ACS Symposium Series, No. 618, 1996. However, most of the known CBDs are from cellulases and xylanases.
In this context, the term "cellulose-binding domain" is intended to be understood as defined by Tomme et al., op . cit . This definition classifies more than 120 cellulose-binding domains into 10 families (I-X) which may have different functions or roles in connection with the mechanism of substrate binding. However, it is anticipated that new family representatives and additional CBD families will appear in the future.
In the protein complex, typically a hydrolytic enzyme, a CBD is located at the N or C termini or is internal. A monomeric CBD typically consists of more than about 30 and less than about 250 amino acid residues. For example, a CBD classified in Family I consists of 33-37 amino acid residues; a CBD classified in Family Ila consists of 95-108 amino acid residues; and a CBD classified in Family VI consists of 85-92 amino acid residues. Accordingly, the molecular weight of a monomeric CBD will typically be in the range of from about 4kD to about 40kD, and usually below about 35kD.
CBDs may be useful as a single domain polypeptide or as a dimer, a trimer, or a polymer; or as a part of a protein hybrid. Chimeric protein hybrids are known in the art, see e.g. WO 90/00609, WO 94/24158 and WO 95/16782, and comprise a cellulose binding domain (CBD) from another origin, preferably from another microbial origin, than the chimeric protein as such, which CBD exists as an integral part of the protein. Typically, the chimeric protein hybrids are enzyme hybrids, i.e. contain a catalytic domain together with the binding domain.
Chimaric protein hybrids and enzyme hybrids can be prepared by transforming into a host cell a DNA construct comprising at least a fragment of DNA encoding the cellulose- binding domain (CBD) ligated, with or without a linker, to a DNA sequence encoding the protein or enzyme and growing the host cell to express the fused gene. The recombinant fusion protein or enzyme hybrids may be described by the following formula:
CBD - MR - X
wherein CBD is the N-terminal or the C-terminal region of an amino acid sequence corresponding to at least the cellulose- binding domain; MR is the middle region (the linker) , and may be a bond, or a short linking group preferably of from about 2 to about 100 carbon atoms, more preferably of from 2 to 40 carbon atoms; or is preferably from about 2 to to about 100 amino acids, more preferably of from 2 to 40 amino acids; and X is an N-terminal or C-terminal region of a polypeptide encoded by the DNA sequence encoding the protein or enzyme.
However, recombinant fusion protein or enzyme hybrids having an internal CBD are also contemplated.
The method of constructing enzyme variants and the variants
In a preferred embodiment, the invention provides a method of constructing a variant of a parent Humicola family 6 endo-beta- 1,4-glucanase, which variant has endo-beta-l,4-glucanase activity and improved detergent compability as compared to the parent endo- beta-l,4-glucanase, which method comprises i) analysing the structure of the parent Humicola family 6 endo-beta-l,4-glucanase to identify at least one amino acid residue or at least one structural part of the Humicola family 6 endo-beta-l,4-glucanase catalytically core domain structure, which amino acid residue or structural part is believed to be of relevance for altering the detergent compatibility of the parent Humicola family 6 endo-beta- 1,4-glucanase as evaluated on the basis of structural or functional considerations, ii) constructing a Humicola family 6 endo-beta-l,4-glucanase variant, which as compared to the parent Humicola family 6 endo-beta-l,4-glucanase has been modified in the amino acid residue or structural part identified in i) so as to alter the detergent compatibility, and, optionally, iii) testing the resulting Humicola family 6 endo-beta-l,4-glucanase variant with respect to detergent compatibility.
Preferably, the structural part to be modified is the binding cleft, the loop region encompassing the binding cleft, or the side chain of the catalytic acid Aspl39.
In another preferred embodiment, the invention provides a method of constructing a variant of a parent Humicola-like family 6 cellulase, which variant has endo-beta-l,4-glucanase activity and improved detergent compatibility as compared to the parent cellulase, which method comprises i) comparing the three- dimensional structure of the Humicola endo-beta-l,4-glucanase with the structure of a Humicola-like cellulase, ii) identifying a part- of the Humicola-like cellulase structure which is different from the Humicola endo-beta-l,4-glucanase structure and which from structural or functional considerations is contemplated to be responsible for differences in the detergent compatibility of the Humicola endo-beta-1, 4-glucanase and Humicola-like cellulase, iii) modifying the part of the Humicola-like cellulase identified in ii) whereby a Humicola-like endo-beta-l,4-glucanase variant is obtained, which has an improved detergent compatibility compared to the parent Humicola-like cellulase, and optionally, iv) testing the resulting Humicola-like endo-beta-l,4-glucanase variant with respect to detergent compatibility.
Preferably, the part of the Humicola-like cellulase is modified so as to resemble the corresponding part of the Humicola family 6 endo-beta-l,4-glucanase.
The modification is, in step iii) of the method, accomplished by deleting one or more amino acid residues of the part of the Humicola-like cellulase to be modified; or the modification is accomplished by replacing one or more amino acid residues of the part of the Humiσola-like cellulase to be modified with the amino acid residues occupying corresponding positions in the Humicola endo-beta-l,4-glucanase; or the modification is accomplished by insertion of one or more amino acid residues present in the Humicola endo-beta-1, 4-glucanase into a corresponding position in the Humicola-like cellulase.
In a preferred embodiment, the parent Humicola endo-beta- 1,4-glucanase is derived from a strain of Humicola inεolenε , more preferably from the strain Humicola inεolens, DSM 1800.
By the term "improved detergent compability" as used herein is meant improved properties of the enzyme with respect to enzymatic activity and stability in commercial detergent compositions. More specifically, these improved properties are improved enzymatic performance or enzymatic activity at a high pH, preferably at a pH above 8, more preferably above 9, especially at a pH about or above 10; improved stability towards conventional commercial detergent composition ingredients such as anionic or non-ionic surfactants, cf. examples 4-7; improved thermal stability; and improved resistance to oxidation (ie improved compatibility towards conventional detergent composition ingredients such as bleaching agents) .
The three-dimensional structure of Humicola insolens Cel6B (EG VI) catalytic core domain The three-dimensional structure of the catalytic core domain of the Humicola insolens Cel6B fungal cellulase was solved by X-ray crystallographic methods. The extent of the catalytic core domain used for the experiment was the 347 amino acid resi- 5 dues starting from position 27 of SEQ ID NO: 4 (and including position 373 of SEQ ID NO:4).
The obtained three-dimensional structure is believed to be representative for the structure of the any fungal endoglucanase catalytic core domain belonging to family 6 of glycosyl hydrola-
10 ses (Henrissat B. "A classification of glycosyl hydrolases based on amino-acid sequence similarities." Biochem. J. 280 309-316 (1991). Henrissat B., Bairoch A. "New families in the classification of glycosyl hydrolases based on amino-acid sequence similarities. Biochem. J. 293 781-788 (1993). Henrissat B. , Bairoch
15 A. "Updating the sequence-based classification of glycosyl hydrolases." Biochem. J. 316 695-696 (1996) .Davies G. , Henrissat B. "Structures and mechanisms of glycosyl hydrolases." Structure 3 853-859 (1995) ) .
The structure was solved in accordance with the principles
20 for X-ray crystallographic methods given in "X-Ray Structure Determination", Stout, G.K. and Jensen, L.H. , John Wiley and Sons, Inc. N.Y. 1989. The structural coordinates of the catalytic core domain of the Humicola insolens Cel6B fungal cellulase solved at 1.6A resolution are given in Appendix 1 in a conventional Brook-
25 haven Protein Data Bank (PDB) format (E. E. Abola, F. C. Bernstein, S. H. Bryant, T. F. Koetzle, and J. Weng, Protein Data Bank, in Crystallographic Databases-Information Content, Software Systems, Scientific Applications, F. H. Allen, G. Berger- hoff, and R. Sievers, eds., Data Commission of the International
30 Union of Crystallography, Bonn/Cambridge/Chester (1987) pp. 107- 132. ; F. C. Bernstein, T. F. Koetzle, G. J. B. Williams, E. F. Meyer, Jr., M. D. Brice, J. R. Rodgers, 0. Kennard, T. Shimanou- chi, and M. Tasu i, The Protein Data Bank: a Computer-based Archival File for Macromolecular Structures, J. Mol. Biol. 112,
35 535-542 (1977); http://www.pdb.bnl.gov/).
The structure contains two independent molecules in the asymmetric unit identified by the letters A and B respectively. Only the part from residue G3 to A347 are detectable in the X- ray structure. It is thought that the remaining residues are disordered under these crystallization and data collection conditions and therefore not detectable in the X-ray structure. It is to be understood that Appendix 1 forms part of the present application. The structure of the catalytic core domain of the Humicola insolens Cel6B fungal cellulase exhibits the distorted barrel topology first described for a family 6 glycoside hydrolase by the Trichoderma reesei CBHII structure (J.Rouvinen et . al . "Three-dimensional structure of cellobiohydrolase from Thricho- derma reesei" Science 249, p380-386 (1990)). The catalytic Brøn- sted acid (D139) and the catalytic base (D316) are located on e- ach side of a cleft at a distance of 9.12A and 9.64A for the two independent molecules respectively consistent with the catalytic mechanism occurring with inversion of the anomeric configurati- on. A third acidic residue (D180) is located close to the Brøn- sted acid having the effect of stabilizing the protonated form of the D139 thereby making the enzyme active even at alkaline conditions.
The secondary structure of the core domain of the Humicola insolens Cel6B fungal cellulase as determined by the DSSP program (W.Kabsch & C.Sander, Dictionary of protein secondary structure : pattern recognition of hydrogen bond and geometrical features . Biopoly ers 22, 2577-2637 (1983)) is shown in figure 4. The three-dimensional structure of the catalytic core domain of the Humicola insolens Cel6A cellulase was solved by X- ray crystallographic methods as described above and is shown in Appendix 2.
Definition of the binding cleft of a three-dimensional structure of an enzyme belonging to Family 6 of glycosyl hydrolases:
A binding cleft is defined as consisting of the largest cave (pocket) on the surface of an enzyme and can extend beyond this pocket. Using WHAT IF (G.Vriend, WHAT IF: a molecular modelling and drug design program . J.Mol. Graph. 8, 52-56, (1990) version 19980317-1938) applying the AACAVI command of the MAP menu with a PROBE RADIUS of 1.4 A the residues on the surface of the largest cave (pocket) can be detected. The binding cleft in contact with the substrate can consist of more residues than those in the concave cleft detected above. Those can be detected by visual inspection of the three- dimensional structure e.g. using the program Insightll (© 1996, Molecular Simulations Incorporated) finding surface exposed residues extending from the concave cleft defined above. Surface exposure are detected either by the DSSP program (se below) or by the Surface Molecule command of Insightll.
Definition of the binding cleft of the catalytic core domain of
Humicola insolens Cel6B.
Applying the method to the three-dimensional structure of the catalytic core domain of Humicola insolens Cel6B the concave part of the binding cleft as detected by WHAT IF is defined as comprising of the following residues: W52, S54, Y86, D92, P138,
D139, D180, A182, N183, W186, N219, V220, S221, N222, W282,
K310, P311, E314, S315, D316, A327 and G328.
By visual inspection using Insightll the complete binding cleft is defined as comprising of the following residues: N14, D16, K20, Y51, W52, S54 , L58, Y86, R91, D92, P138, D139, D180,
A182, N183, G185, W186, W189, N219, V220, S221, N222, W279,
W282, K310, P311, E314, D316, A327 and G328.
The loop regions encompassing the binding cleft: Given the binding cleft as described above, the loop regions encompassing the binding cleft is defined as the regions of contiguous sequence not belonging to a α-helical region or a β- strand region in any of the determined structures. In this definition the 3-10 helices are included in the loop definition as they are not seen as an integral part of the inner core structure. Using this definition together with the secondary structure information in figure 4 the binding cleft encompassing loops are defined as: L12, V13 , N14, S54 , N55, 156, F57, L58, L59, Y86, N87, L88, P89, D90, R91, D92, C93, S94, A95, G96, E97, S98, S99, G100, E101, L102, K103, L104, S105, Q106, N107, E137, P138, D139, V181, A182, N183, G188, W189, A190, D191, K192, N219, V220, S221, N222, Y223, N224, P225, Y226, S227, T228, S229, N230, P231, P232, P233, Y234, T235, S236, G237, S238, P239, S240, P241, D242, A271, L272, S273, G274, A275, R276, S277,
E278, W279, G280, Q281, W282, C283, N284, V285, N286, P287,
W308, V309, K310, P311, G312, G313, E314, S315, D316, G317,
Q318, C319, G320, M321, G322, G323, A324, P325, A326, A327, G328, M329, W330, F331.
This can be seen graphically in figure 5.
Residues in proximity:
To detect residues in proximity of each other the Subεet zone command of the Insightll program is applied. The command detects residues or individual atoms within a defined distance from a predefined subset, groups of residues or groups of atoms. The Subεet liεt command can be used to investigate the result.
Residues within 5 A of residues in the binding cleft:
Based on the above definition of the binding cleft the following residues are within 5 A of the residues in the binding cleft (including the residues in the binding cleft): L12, V13,
N14, S15, D16, Y17, S18, S19 K20, L21, D22, Q23, T24, V47, G48, T49, F50, Y51, W52, 153, S54 N55, 156, F57, L58, L59, R60, D61,
162, V64, A65, N68, V81, G82 L83, V84, L85, Y86, N87, L88, P89,
D90, R91, D92, C93, S94, A95 G96, E97, S98, S99, G100, L102,
Y116, 1135, L136, E137, P138 D139, A140, 1141, G142, N143,
T146, Q159, Y178, L179, D180 V181, A182, N183, G184, G185, W186, L187, G188, W189, A190 D191, K192, L193, S217, S218,
N219, V220, S221, N222, Y223 N224, Y234, T235, S236, G237,
S238, P239, S240, P241, E243 Y246, 1265, D266, Q267, S268,
R269, R276, S277, E278, W279 G280, Q281, W282, C283, N284,
V285, W308, V309, K310, P311 G312, G313, E314, S315, D316, G317, Q318, C319, A324, P325 A326, A327, G328, M329, W330,
F331, D332.
Residues within 2.5 A of residues in the binding cleft:
Based on the above definition of the binding cleft the following residues are within 2.5 A of the residues in the binding cleft (including the residues in the binding cleft): V13, N14, S15, D16, Y17 , S19, K20, L21, F50, Y51, W52, 153, S54, N55, F57, L58, L59, L85, Y86, N87, D90, R91, D92, C93, E137, P138, D139, A140, L179, D180, V181, A182, N183, G184, G185, W186, L187, G188, W189, A190, S218, N219, V220, S221, N222, Y223, E278, W279, G280, Q281, W282 , C283, V309, K310, P311, G312, G313, E314, S315, D316, A326, A327, G328, M329.
Residues within 15.0 A of D139 side chain in the three- dimensional structure of Humicola inεolens Cel6B catalytic core domain:
The following residues are found to be within 15.0 A of an atom in the side chain of the catalytic acid (D139) defined as any of the atoms CB, CG, ODl or 0D2 in one of the two independent structures in the three-dimensional structure of Humicola inεolenε Cel6B catalytic core domain: F50, W52, 153, S54 , L83, V84, L85, Y86, N87, L88, P89, D90, R91, D92, C93 , S94, A95, G96, E97, S98, S99, G100, E101, L102, Y112, Y116, V134, 1135, L136, E137, P138, D139, A140, 1141, G142, N143, M144, V145, T146, G147, T148, S149, F151, C152, R153, A155, R156, P158, Q159, Q160, A162, 1163, Y178, L179, D180, V181, A182, N183, G184, G185, W186, L187, G188, W189, K192, L193, P195, T196, A197 , E199, V200, 1203, G215, F216, S217, S218, N219, V220, S221, N222, Y223, N224, P225, Y234, S240, D242, E243, Y246, A247, 1250, M254, Q262, F263, 1264, 1265, D266, Q267, S268, R269, R276, E278, W279, G280, Q281, W282, C283, N284, V285, V307, W308, V309, K310, P311, G312, E314, S315, D316, G317, Q318, C319, A327, G328, Y334.
Residues within 10.0 A of D139 side chain in the three- dimensional structure of Humicola inεolens Cel6B catalytic core domain:
The following residues are found to be within 10.0 A of an atom in the side chain of the catalytic acid (D139) defined as any of the atoms CB, CG, ODl or OD2 in one of the two independent structures in the three-dimensional structure of Humicola insolens Cel6B catalytic core domain: W52, V84, L85, Y86, L88, D90, R91, D92, C93, S94, A95, S99, 1135, L136, E137, P138, D139, A140, 1141, G142, N143, M144, V145, T146, C152, Q159, 1163, L179, D180, V181, A182, N183, G184, G185, W186, L187, S217, S218, N219, V220, S221, N222, Y223, N224, E243, Y246, D266, R269, G280, Q281, W282, C283, K310, D316. Residues within 5.0 A of D139 side chain in the three- dimensional structure of Humicola inεolenε Cel6B catalytic core domain: The following residues are found to be within 5.0 A of an atom in the side chain of the catalytic acid (D139) defined as any of the atoms CB, CG, ODl or OD2 in one of the two independent structures in the three-dimensional structure of Humicola inεolenε Cel6B catalytic core domain: D92, P138, D139, A140, N143, D180, A182, W186.
Residues on the surface of the molecule:
Residues on the surface of the three-dimensional structure of a molecule is defined as those having any part of their sur- face exposed to the solvent as calculated by the DSSP program (W.Kabsch & C.Sander, Dictionary of protein εecondary structure : pattern recognition of hydrogen bond and geometrical featureε . Biopolymers 22, 2577-2637 (1983)).
For three-dimensional structure of the catalytic core do- main of the Humicola inεolenε Cel6B fungal cellulase the application of the DSSP program to both of the molecules reveiled that the following residues were defined as being on the surface of the molecule: G3, N4, P5, S7, G8 , R9 , T10, Lll, L12 , V13, N14 , S15, D16, Y17, S18, S19, K20, D22, Q23, R25, Q26, A27, L29, S30, R31, G32, D33, Q34, T35, N36, A37, A38, K39, K41, Y42, V43, Q44, E45, K46, V47, G48, T49, Y51, W52, S54, N55, 156, F57 , L58, L59, R60, D61, D63, V64, 166, Q67, N68, A69, R70, A71, A72, K73, A74, R75, G76, E77, N78, P79, Y86, L88, D90, R91, D92, C93, S94, A95, G96, E97, S98, S99, GlOO, ElOl, L102, K103, L104, S105, Q106, N107, G108, L109, N110, Rill, Y112, K113 , N114, E115, V117, N118, P119, F120, A121, Q122, K123, K125, A126, A127, S128, D129, V130, Q131, L136, E137, P138, D139, A140, 1141, N143, M144, V145, T146, G147, T148, S149, A150, F151, C152, R153 , N154, R156, G157, P158, Q159, Q160, E161, 1163, G164, Y165, A166, S168, Q169, L170, Q171, A172, S173, H174, 1175, H176, L177, L179, D180, A182, N183, G185, W186, W189, A190, D191, K192, L193, E194, P195, Q198, E199, A201, T202, L204, Q205, K206, A207, G208, N209, N210, A211, K212, 1213, R214, S217, N219, V220, S221, N222, N224, P225, Y226, S227, T228, S229, N230, P231, P232,
P233, Y234, T235, S236, G237, S238, P239, P241, D242, S244,
R245, T248, N249, N252 , A253, R255, Q256, R257, G258, L259,
P260, T261, Q262, 1264, D266, Q267, S268, V270, A271, L272,
5 S273, G274, A275, R276, S277, E278, W279, G280, Q281, W282,
C283, V285, N286, P287, G289, F290, G291, Q292, P293, F294,
T295, T296, N297, T298, N299, N300, P301, N302, V303, D304,
1306, V309, K310, P311, E314, D316, G317, Q318, C319, G320,
M321, G322, G323, A324, P325, A326, A327, G328, M329, W330,
10 F331, D332, A333, Y334, Q336, M337, Q340, N341, A342, H343,
D344, E345, 1346.
Residues within 15.0 A of D139 side chain in the three- dimensional structure of Humicola inεolenε Cel6B catalytic core
15 domain and defined as being on the surface:
The following residues are found to be within 15.0 A of an atom in the side chain of the catalytic acid (D139) defined as any of the atoms CB, CG, ODl or OD2 in one of the two independent structures in the three-dimensional structure of Humicola
20 insolens Cel6B catalytic core domain and are defined as being on the surface of the molecule: W52, S54, Y86, L88, D90, R91, D92, C93, S94, A95, G96, E97, S98, S99, G100, ElOl, L102, Y112, L136, E137, P138, D139, A140, 1141, N143, M144, V145, T146, G147, T148, S149, F151, C152, R153, A155, R156, P158, Q159, Q160,
25 1163, L179, D180, A182, N183, G185, W186, W189, K192, L193, P195, E199, S217, N219, V220, S221, N222, N224, P225, Y234, D242, Q262, 1264, D266, Q267, S268, R276, E278, W279, G280, Q281, W282, C283, V285, V309, K310, P311, E314, D316, G317, Q318, C319, A327, G328, Y334.
30
Residues within 10.0 A of D139 side chain in the three- dimensional structure of Humicola inεolenε Cel6B catalytic core domain and defined as being on the surface:
The following residues are found to be within 10.0 A of an 35 atom in the side chain of the catalytic acid (D139) defined as any of the atoms CB, CG, ODl or 0D2 in one of the two independent structures in the three-dimensional structure of Humicola insolens Cel6B catalytic core domain and are defined as being on the surface of the molecule: W52, Y86, L88, D90, R91, D92, C93, S94, A95, S99, L136, E137, P138, D139, A140, 1141, N143, M144, V145, T146, C152, Q159, 1163, L179, D180, A182, N183, G185, W186, S217, N219, V220, S221, N222, N224, D266, G280, Q281, W282, C283, K310, D316.
Residues within 5.0 A of D139 side chain in the three- dimensional structure of Humicola inεolenε Cel6B catalytic core domain and defined as being on the surface:
The following residues are found to be within 5.0 A of an atom in the side chain of the catalytic acid (D139) defined as any of the atoms CB, CG, ODl or 0D2 in one of the two independent structures in the three-dimensional structure of Humicola insolens Cel6B catalytic core domain and are defined as being on the surface of the molecule: D92, P138, D139, A140, N143, D180, A182, W186.
Improved Stability Towards Anionic Surfactants
In order so stabilize an enzyme against denaturation by anionic tensides mutations/deletions of surface exposed residues are performed. The mutation is towards a more negatively charged residue, and preferably from a potentially positively charged residue (His, Lys or Arg, more preferably Arg) . These points are thought to be anchor points for the anionic tensides especially the potentially positively charged residues and more preferably the Argini- ne residues.
The mutations from neutrally charged surface residues towards potentially negatively charged residues (Asp or Glu) should preferably be performed at points where the sequence holds the e- quivalent amide (Asn or Gin) . Mutating surface exposed residues towards more negatively charged residues for the core domain of Humicola inεolenε Cel6B comprises of the following mutations:
Neutral residues to be mutated to Asp or Glu (excluding His) : G3, N4, P5, S7 , G8 , T10, Lll, L12 , V13, N14 , S15, Y17, S18, S19,- Q23, Q26, A27, L29, S30, G32, Q34, T35, N36, A37, A38, Y42, V43, Q44, V47, G48, T49, Y51, W52 , S54, N55, 156, F57, L58, L59, V64, 166, Q67, N68, A69, A71, A72, A74, G76, N78, P79, Y86, L88, C93, S94, A95, G96, S98, S99, GlOO, L102, L104, S105, Q106, N107 , A121, 1141, C152, S168, N183, L204, V220, P231, S244, Q262, S277, F290, N300, G320, W330,
Preferably at the points where the sequence already contains Asn or Gin, which in the core domain of Humicola inεolenε Cel6B comprises residues: N4 , N14, Q23, Q26, Q34, N36, Q44, N55, Q67, N68, N78, Q106, N107, NllO, N114, N118, Q122, Q131, N143, N154, Q159, Q160, Q169, Q171, N183, Q198, Q205, N209, N210, N219, N222, N224, N230, N249, N252, Q256, Q262, Q267, Q281, N286, Q292, N297, N299, N300, N302, Q318, Q336, Q340, N341.
Preferably mutations should be performed at surface exposed positions containing a potentially positively charged residue (His, Lys or Arg) mutating to a residue not belonging to this group. In the core domain of Humicola inεolenε Cel6B this comprises residues: R9, K20, R25, R31, K39, K41, K46, R60, R70, K73, R75, R91, K103, Rill, K113, K123, K125, R153, R156, H174, H176, K192, K206, K212, R214, R245, R255, R257, R276, K310, H343, most preferably: R9, R25, R31, R60, R70, R75, R91, Rill, R153, R156, R214, R245, R255, R257, R276.
Improved thermal stability A enzyme can be stabilized towards thermal denaturation can by substitution of a naturally occurring amino acid residue other than proline with a proline residue at positions in the structure where the backbone dihedral angle φ (phi) are in the interval [-90° < φ < -40°] and where the back bone amide proton of the residue to be substituted does not participate as donor in a hydrogen bond. Preferably the residue should be outside - helical regions as well as β-strand regions. More preferably the back bone ψ (psi) dihedral angle should be in the intervals: [-
180° < ψ < -150°] or [-80° < ψ < 10°] or [100° < ψ < 180°]. The dihedral angles as well as the potential hydrogen bonds involving the back bone amide proton can be investigated using the program DSSP. A hydrogen bond involving the back bone amide proton is defined as those with an energy determined by DSSP smaller than or equal to -1.4 kcal/mole.
Applying this method to the three-dimensional structure of the catalyic core domain of Humicola inεolenε Cel6B rsults in the following positions as targets for Xxx -> Pro mutations: N4 , S7, Lll, V13, N14 , S15, D16, Y17, D22, Q23, T24, T35, N36, G48, S54, 156, F57, L58, R60, D63, A74, L88, R91, C93, S94, S98, S99, ElOl, L104, S105, L109, NllO, S128, D129, 1141, G142, G147, S149, A150, F151, C152, R156, G157, S173, G184, G185, W189, A190, D191, L193, E194, N209, N210, A211, V220, N224, Y226, Y234, R245, Q256, Q262, S268, S273, S277, W279, G280, C283, V285, Q292, F294, N297, N302, K310, G312, D316, Q318, G322, A324, A326, A327, D332, A333, Y334, W330, D344, E345, preferably N4, S7, V13, N14, G48, S54, 156, F57, L58, L88, R91, C93, S94, S98, S99, ElOl, L104, S105, S128, D129, G147, S149, S173, W189, A190, D191, N209, N210, A211, V220, N224, Y226, Y234, S268, S273, S277, W279, G280, C283, V285, Q292, F294, N297, N302, K310, G312, D316, Q318, G322, A324, A326, A327, W330, D344, E345, more preferably N4 , S7, V13 , N14 , G48, S54 , 156, F57, L58, L88, R91, C93, S94, S98, S99, E101, L104 , S105, AER128, D129, S149, S173, W189, A190, D191, N209, N210, A211, V220, N224, Y226, Y234, S268, S273, S277, W279, G280, C283, V285, Q292, F294, N302, K310, G312, D316, G322, A324, A326, A327, W330, D344, E345.
Capping of alpha-helices
Due to the helix dipole created due to alignment of the many polar atoms in the backbone an alpha-helix exhibits a dipo- le with a partial positive charge at the N-terminus and a partial negative charge at the C-terminus. This dipole can be further stabilized by introduction of opposite charges or partial charges at the ends or removal of equal charges or partial char- ges. The most well know example is the N-capping of the N- terminal of the alpha Helix with a Asn residue which can satisfy a hydrogen bond donor in the back bone which would else be unpaired. Alternatively an Asp residue located at the N-terminal can counteract the partial positive charge and stabilize the en- zyme structure. From a structural analysis other substitutions can be found which will place a residue close to a helix terminal with a stabilizing charge or partial charge.
Examination of the tree-dimensional structure of Humicola inεolenε Cel6B catalytic core domain results in the following potentially stabilizing mutations in the N-terminal regions of the alpha helices: N14D ; N55D ; S149N,D ; N183D ; K192Q ; F331N,D.
And the following potentially stabilizing mutations in the C-terminal regions of the alpha-helices: V13K,R ; E77Q ; S128N,Q,K,R ; T148N,Q,K,R ; S168N,Q,K,R ; L193Q ; D344N,Q,K,R.
Satisfaction of internal hydrogen bonds and salt bridges
"Unsatisfied" hydrogen bond donors and/or acceptors as well as unpaired buried charged groups from potentially charged residues can destabilize an enzyme structure. Removing the unsatisfied partner by mutagenesis to a residue without these properties or mutation of neighboring residues to fulfill the unsatisfied hydrogen bond or salt bridge can most often stabilize the enzyme structure. These unsatisfied hydrogen bond/salt bridge partners can be found using the WHAT CHECK routine which is an integral part of the WHAT IF program.
Applying the WHAT CHECK routine on the complete three dimensional structure of Humicola inεolenε Cel6B catalytic core domain followed by subsequent visual analysis using Inεightll results in the following mutations to satisfy unsatisfied hydrogen bonds/salt bridges: L11Y ; T49A,S,N,Q,V,M,G ; N55G,A,S,T ; N87Q,E,D ; A95S,T,N,D,Q,E ; I175T,G,A,V ; A182G ; L187G,A,S,T,N,Q,H ; K192Q, E,N,D, S,T ; S268G,A,V,L, I ,F ; F249N,Q,S,T,D,E ; M337Q, Y,N, D, T, E. Residues on the surface of internal cavities
This defines residues which are found to be on the surface of internal cavities in the enzyme structure. To detect these 5 the options CAVITY and AACAVI in the WHAT IF program is used. A probe radius of 1.4 A is typically used to detect internal cavities where mutations could be performed. The mutations are preferentially mutating to a residue with a larger side chain, thereby decreasing the volume of the cavity, or mutating to a resi- ιo due with a smaller side chain, thereby increasing the volume of the cavity making it possible for a water molecule to be accommodated in the cavity. Both methods can increase the thermal stability of the enzyme structure. Residues having their side chain exposed to the cavity as determined by the AACAVI command
15 in WHAT IF or by visual inspection using e.g. the Insightll program are prefered targets for mutagenesis.
In Humicola inεolenε Cel6B this results to: V13, N14, Y17, S18, L21, K39, V40, V43, V47, N87, L88, R91, D92, C93, K103 , Rill, V117, F120, L136, E137, P138, A140, 1141, N143, Q159,
20 1163, A166, L170, L179, D180, S217, V220, N222, 1264, D266, Q267, R269, N284, F290, V309, G313, E314, S315, F331, Y334.
Preferably the following residues having their side chains exposed to the cavity in a favorable position for mutagenesis as judged visually using Inεightll : V13, N14 , Y17, S18, L21, V40,
25 V43, L88, V117, F120, L136, E137, A140, 1141, Q159, 1163, A166, L170, L179, S217, V220, N284, F290, V309, S315, F331, Y334.
Preferably the following mutations to decrease the volume of said cavities (in one letter code): V13L, I,F, Y,W; N14,Q,Y,V,L,I,F,W; Y17W; S18T,N,Q, V,L, I, F, Y,W; L21F,Y,W,I ;
30 V40I,L,F,Y,W ; V43I,L,F,Y,W ; L88F,Y,W,I ; V117L, I , F, Y, W ;
F120Y,W ; L136I,F,Y,W ; E137Q, I, L, F, Y,W A140S,T,V,L, I , F, Y,W ; I141L,F,Y,W ; Q159I, F, Y,W,L ; I163L,F,Y,W ; L170I,F,Y,W ; L179I,F,Y,W ; S217T,N,Q,V,L, I , F, Y, W ; V220L, I , F, Y,W ; N284Q ; F290Y,W ; V309L, I, F, Y,W ; S315T ; F331Y,W ; Y334W.
35 The following mutations are preferred in order to increase the volume of said cavities: V13G,A,S,T ; N14G,A,S,T ; Y17G,A,S,T,F,V,L,I ; S18G,A ; L21V,G,A,S,T ; V40G,A,S,T ; V43G,A,S,T ; L88V,G,A,S,T ; V117G,A,S,T ; F120V, I , L, G, A, S, T ; L136V,G,A,S,T ; E137G,A, S,T, D,N,V ; A140G ; I141V,G,A, S,T ; Q159N,G,A,S,T,V ; I163V, G,A, S , T ; A166G ; L170V, G,A, S, T ; L179V,G,A,S,T ; S217G,A ; V220G,A,S,T ; N284G,A,S,T ; F290I,V,L ; V309G,A,S,T ; F331V,L, I,G,A, S,T ; Y334F,V,L, I ,G,A, S,T.
Improved Stability Towards Oxidation
Some amino acid residues are sensitive towards oxidation by oxidative detergents and will in their oxidized form have altered properties e.g. catalytic properties, stability, pH optimum. Surface exposed residues of the type Met are most labile towards oxidation. Tyr or Trp are also known to be labile towards oxidation. Mutation of surface exposed residues of the above mentioned type will remove the sensitivity towards oxidation. This comprises the residues: Y17, Y42, Y51, W52, Y86, Y112, M144, Y165, W186, W189, Y226, Y234, W279, W282, M321, M329, W330, Y334, M337, more preferably those which are also present in the binding cleft: Y51, W52, Y86, W186, W189, W279, W282.
Altered pH profile The pH profile of an enzyme can be altered by changing the electrostatic environment of the active site. Especially the electrostatic field at the position of the catalytic proton donor is a determinant of the alkalinisity of the enzyme. A change in the electrostatic field at the point of the catalytic proton donor towards a more negative electrostatic field can increase the apparent pKa of the catalytic proton donor, and thereby increase the activity at more alkaline conditions. This change in the electrostatic field can be obtained by mutations/deletions or insertions of residues in the vicinity of the catalytic pro- ton donor as follows:
1) Deletion of potentially positively charged residues.
2) Mutation of potentially positively charged residues to neutral or potentially negatively charged residues.
3) Mutation of neutral residues to potentially negatively char- ged residues.
4) Insertion of potentially negatively charged residues.
The mutations should preferably be made to surface exposed residues and preferably not more than 15A from the catalytic proton donor, more preferably not more than loA from the cataly- tic proton donor and most preferably nor more than δA from the catalytic proton donor.
Insertions/deletions should only be made in loop/turn regions and preferably not more than lδA from the catalytic proton donor .
This results in the following positions: 1) R9del, R31del, R75del, R91del, K103del, H174del, K192del, K212del, R214del, R257del, R269del, R276del, K310del, H343del.
2) R9, K20, R25, R31, K39, K41, K46, R60, R70, K73, R75, R91, K103, Rill, K113, K123, K125, R153, R156, H174, H176, K192, K206, K212, R214, R245, R255, R257, R276, K310, H343 to neutral or potentially negatively charged residues (i.e. All 20 except R,K,H) , preferably on the surface within loA of the catalytic proton donor (D139) : R91, K310
3) G3, N4, P5, S7, G8 , T10, Lll, L12, V13 , N14, S15, Y17, S18
S19, Q23, Q26, A27, L29 , S30, G32, Q34, T35, N36, A37, A38, Y42,
V43, Q44, V47, G48, T49 , Y51, W52, S54, N55, 156, F57, L58, L59, V64, 166, Q67, N68, A69 , A71, A72, A74, G76, N78, P79, Y86, L88,
C93, S94, A95, G96, S98 , S99, G100, L102, L104, S105, Q106,
N107, G108, L109, NllO, Y112, N114, V117, N118, P119, F120,
A121, Q122, A126, A127, S128, V130, Q131, L136, P138, A140,
1141, N143 M144, V145, T146 G147 T148 S149 A150, F151, C152, N154 G157, P158, Q159 Q160 1163 G164 Y165( A166,
S168, Q169, L170, Q171, A172 S173 1175 L177 L179, A182,
N183, G185 W186, W189, A190 L193 P195, Q198 A201, T202,
L204 Q205 A207 G208, N209 N210 A211 1213 S217 N219,
V220 S221 , N222 N224, P225 , Y226 , S227 T228 S229 N230, P231 P232 P233 Y234, T235 , S236 G237 S238 P239 P241,
S244 T248 , N249 N252, A253 , Q256 G258 L259 P260 T261,
Q262 , 1264 , Q267 , S268, V270 , A271 , L272 , S273 , G274 , A275,
S277 , W279 , G280 , Q281, W282 , C283 , V285 , N286 , P287 , G289,
F290 , G291 , Q292 , P293, F294 , T295 , T296 , N297 , T298 , N299, N300 , P301 , N302 , V303, 1306 , V309 , P311 , G317 , Q318 r C319,
G320 , M321 , G322 , G323, A324 , P325 , A326 , A327 , G328 , M329,
W330 , F331 , A333 , Y334, Q336 , M337 , Q340 , N341 , A342 , 1346.
Prefe rably < DΠ the surfa< ze witlin lOi K of tlιe cat*alytic pro- ton donor (D139) : W52, Y86, ] L88, C< .3, S9< 1, A95 , S99, L136, P138, A140, 1141, nl43, M144 , V145, T146, C152, Q159, 1163, L179, A182, N183, G185, W186, S217, N219, V220, S221, N222, N224, G280, Q281, W282, C283, more preferably on the surface within δA of the catalytic proton donor (D139) : P138, A140, N143, A182, W186.
Altering the pH profile of an enzyme ( 2 )
Another method to alter the pH profile of an enzyme is to mutate the residues in or close to the binding cleft. This will create a variant enzyme where the electrostatics of the active site will be changed either directly due to altered charges or partial charges in the binding cleft, or due to altered geometry around the active site changing the degree of burial of the active site residues. These changes should be made not more than 5A from a residue in the binding cleft, and preferably not more than 2.5A from a residue in the binding cleft most preferably mutating residues in the binding cleft.
Definition of Humicola-like cellulases and their sequences The present invention includes variants of sequences having at least 35% identity to the catalytic core domain of Humicola insolens Cel6B. Percent sequence identity is determined by conventional methods, by means of computer programs known in the art such as GAP provided in the GCG program package (Program Ma- nual for the Wisconsin Package, Version 8, August 1994, Genetics Computer Group, 575 Science Drive, Madison, Wisconsin, USA 53711) as disclosed in Needleman, S.B. and Wunsch, CD., (1970), Journal of Molecular Biology, 48, 443-453, which is hereby incorporated by reference in its entirety, ie using the GAP algo- rithm of the GCG package version 8 using a gap creation penalty of 3.00 and a gap extension penalty of 0.10 and all other parameters are kept at their default value. The catalytic core domain of Humicola inεolenε Cel6B is defined as the 347 residues used for the X-ray structure determination (positions 27-374 of SEQ ID NO: 4). Only the part of the sequence extending from the start of the alignment to the catalytic core domain of Humicola inεolenε Cel6B to the last residue aligning with to the catalytic core domain of Humicola inεolens Cel6B are included (as seen in Figure 1 (1A+1B)). Following known sequences are within the definition: Orpinomyceε sp. SPTREMBL entry p78720 [residues 128-
459], Orpinomyces sp. SPTREMBL entry p78721 [residues 127-449], Humicola inεolenε Cel6B (endocellulase CMC 38K in patent W09311249-A) [residues 27-379], Trichoderma reeεei (Trichoderma longibrachiatum) SwissProt entry p07987 [residues 112-471], Fuεarium oxyεporum SwissProt entry p46236 [residues 103-462], Humicola inεolenε Cel6A and patent number JP 1996126492-A/1) [residues 112-473], Acremonium cellulolyticuε (patent number
W09733982-A1) [residues 86-437], Penicillium purpurogenum (Presented at The Annual Meeting of Japan Society for Bi- oscience, Biotechnology, and Agrochemistry, April 1-2, 1998, Na- goya, Japan. The sequence was recorded on videotape) [residues 96-457], Agaricuε biεporus SwissProt entry p49075 [residues 87- 438], Phanerochaete chrysoεporium SPTREMBL entry q02321 [residues 103-460], Neocallimaεtix patriciarum SPTREMBL entry ql2646 [residues 98-428], Humicola inεolenε EMBL entry E11341
[residues 115-476].
Multiple alignment of sequences of the invention Sequences having more than 35.0% identity to the catalytic core domain of Humicola inεolenε Cel6B as defined above can be aligned using the multiple alignment program Clustal W ver. 1.7 (Thompson et . al . Nucleic Acids Research Vol. 22 , No. 22 pp. 4673-4680 (1994)) which is able to include secondary structure information in the alignment. The secondary structure of the catalytic core domain of Humicola inεolenε Cel6B as defined previously in fig. 4 for the α-helix and β-strand regions can be included in the input for a prof He /structure alignment . Only positions belonging to α-helical region or a β-strand region in both og the independant molecules are considered as being in a to α-helical region or a β-strand region respectively (see also fig. 1A/B) . Using this information as the 1st profile and using the remaining sequences as the 2nd profile . The option Align εe- quenceε to 1st profile is used to align sequences to the sequen- ce of the catalytic core domain of Humicola inεolenε Cel6B taking the structural elements into account. No alterations is made to the default parameters. The result of the alignment are seen in figure 1A/B. This alignment is used to identify the positions equivalent to positions in the catalytic core domain of Humicola inεolenε Cel6B.
Alignment of new seguence to known alignment
To align a new sequence with more than 35.0% sequence identity as determined by the GAP program to the known alignment in Fig. 4 the Profile /Structure alignment option of ClustalW is applied. Only the part of the sequence extending from the start of the GAP alignment to the catalytic core domain of Humicola inεolens Cel6B to the last residue aligning with to the catalytic core domain of Humicola inεolenε Cel6B are included. The alignment in Fig. 4 is read as 1st profile and the new sequence is read as 2 profile . The option Align εequenceε to 1st profile is used to align a new sequence to the sequence alignment in Fig. 4. No alterations is made to the default parameters. From such an alignment residues in a new sequence at positions equivalent to positions in the catalytic core domain of Humicola inεolenε Cel6B can be identified.
Structure based seguence alignment
An more preferred way of identifying equivalent residues between a "new" sequence ant the catalytic core domain of Humicola inεolenε Cel6B is to determine the three-dimensional X-ray structure fold of the "new" sequence and apply a structure based sequence alignment as implemented in the Modeler 97.0 program included in the Homology 97.0 package from MSI INC. using the MALIGN3D command with the GAP_PENALTIES_3D parameters set to 0.0 and 1.75 and the FIT_ATOMS set to CA. This alignment will find residues at structurally equivalent positions, i.e. having their CA atoms not more than 3.5A apart in a structural superposition. From this alignment equivalent residues in a "new" sequence can be identified. Increased color care activity by trimming of binding cleft loops.
The Humicola inεolenε Cel6B is able to perform color clarification as seen in examples 1 and 2 and has activity towards CMC. Neocallimaεtix patriciarum SPTREMBL entry ql2646 have been shown to have activity towards CMC, the same is believed to be the case for Orpinomyceε εp. SPTREMBL entry p78720 and Orpi- nomyceε εp. SPTREMBL entry p78721. The origin of this is thought to be a more open binding cleft caused by one or more of the binding cleft encompassing loops being shorter that in the other fungal family 6 cellulases, preferably one of the four longer loops: Y86-N107, N219-D242, L272-P287 or W308-F331 (Humicola inεolens Cel6B numbering) or equivalent regions as determined by the multiple sequence alignment, more preferably the regions N219-D242 or W308-F331 which are seen in the multiple sequence alignment to be different in length. The extent of the loop regions can be trimmed (ie made shorter) by deletion of individual residues which together with mutation of neighboring residues can optimize the color care effect. The loop manipulations can be performed using site directed mutagenesis, region specific random mutagenesis using spiked oligonucleotides, protein family shuffling or by other methods.
Methods of preparing endoglucanase variants Several methods for introducing mutations into genes are known in the art. Cloning of cellulase-encoding DNA sequences and methods for generating mutations at specific sites within the cellulase-encoding sequence are mentioned in the following. Cloning a DNA sequence encoding a cellulase The DNA sequence encoding a parent cellulase may be isolated from any cell or microorganism producing the cellulase in question, using various methods well known in the art. First, a genomic DNA and/or cDNA library should be constructed using chromosomal DNA or messenger RNA from the organism that produces the cellulase to be studied. Then, if the amino acid sequence of the cellulase is known, homologous, labelled oligonucleotide probes may be synthesized and used to identify cellulase-encoding clones from a genomic library prepared from the organism in question. Alternatively, a labelled oligonucleotide probe containing sequences homologous to a known cellulase gene could be used as a probe to identify cellulase-encoding clones, using hybridization and washing conditions of lower stringency.
A method for identifying cellulase-encoding clones involves inserting cDNA into an expression vector, such as a plasmid, transforming cellulase-negative fungi with the resulting cDNA library, and then plating the transformed fungi onto agar containing a substrate for cellulase, thereby allowing clones expressing the cellulase to be identified. Alternatively, the DNA sequence encoding the enzyme may be prepared synthetically by established standard methods, e.g. the phosphoroamidite method. In the phosphoroamidite method, oligonucleotides are synthesized, e.g. in an automatic DNA synthesizer, purified, annealed, ligated and cloned in appropriate vectors. Finally, the DNA sequence may be of mixed genomic and synthetic origin, mixed synthetic and cDNA origin or mixed genomic and cDNA origin, prepared by ligating fragments of synthetic, genomic or cDNA origin (as appropriate, the fragments corresponding to various parts of the entire DNA sequence) , in accordance with standard techniques. The DNA sequence may also be prepared by polymerase chain reaction (PCR) using specific primers. Site-directed mutagenesis
Once a cellulase-encoding DNA sequence has been isolated, and desirable sites for mutation identified, mutations may be intro- duced using synthetic oligonucleotides. These oligonucleotides contain nucleotide sequences flanking the desired mutation sites; mutant nucleotides are inserted during oligonucleotide synthesis. In a specific method, a single-stranded gap of DNA, bridging the cellulase-encoding sequence, is created in a vector carrying the cellulase gene. Then the synthetic nucleotide, bearing the desired mutation, is annealed to a homologous portion of the single- stranded DNA. The remaining gap is then filled in with T7 DNA polymerase and the construct is ligated using T4 ligase. A specific example of this method is described in Morinaga et al. (1984). US 4,760,025 discloses the introduction of oligonucleotides encoding multiple mutations by performing minor alterations of the cassette. However, an even greater variety of mutations can be introduced at any one time by the Morinaga method, because a multitude of oligonucleotides, of various lengths, can be introduced.
Another method of introducing mutations into cellulase-encoding DNA sequences is described in Nelson and Long (1989) . It involves the 3-step generation of a PCR fragment containing the desired mutation introduced by using a chemically synthesized DNA strand as one of the primers in the PCR reactions. From the PCR-generated fragment, a DNA fragment carrying the mutation may be isolated by cleavage with restriction endonucleases and reinserted into an expression plasmid. Random mutagenesis
The random mutagenesis of a DNA sequence encoding a parent cellulase may conveniently be performed by use of any method known in the art. For instance, the random mutagenesis may be performed by use of a suitable physical or chemical mutagenizing agent, by use of a suitable oligonucleotide, or by subjecting the DNA sequence to PCR generated mutagenesis. Furthermore, the random mutagenesis may be performed by use of any combination of these mutagenizing agents. The mutagenizing agent may, e.g., be one which induces transitions, transversions, inversions, scrambling, deletions, and/or insertions .
Examples of a physical or chemical mutagenizing agent suitable for the present purpose include ultraviolet (UV) irradiation, hydrox lamine, N-methyl-N ' -nitro-N-nitrosoguanidine (MNNG) , O- methyl hydroxylamine, nitrous acid, ethyl methane sulphonate (EMS) , sodium bisulphite, formic acid, and nucleotide analogues. When such agents are used, the mutagenesis is typically performed by incubating the DNA sequence encoding the parent enzyme to be utagenized in the presence of the mutagenizing agent of choice under suitable conditions for the mutagenesis to take place, and selecting for mutated DNA having the desired properties.
When the mutagenesis is performed by the use of an oligonucleo- tide, the oligonucleotide may be doped or spiked with the three non-parent nucleotides during the synthesis of the oligonucleotide at the positions which are to be changed. The doping or spiking may be done so that codons for unwanted amino acids are avoided. The doped or spiked oligonucleotide can be incorporated into the DNA encoding the cellulase enzyme by any published technique, using e.g. PCR, LCR or any DNA polymerase and ligase.
When PCR-generated mutagenesis is used, either a chemically treated or non-treated gene encoding a parent cellulase enzyme is subjected to PCR under conditions that increase the mis- incorporation of nucleotides (Deshler 1992; Leung et al., Technique, Vol.l, 1989, pp. 11-15).
A mutator strain of E. coli (Fowler et al., Molec. Gen. Genet., 133, 1974, pp. 179-191), S . cereviεeae or any other microbial organism may be used for the random mutagenesis of the DNA encoding the cellulase enzyme by e.g. transforming a plasmid containing the parent enzyme into the mutator strain, growing the mutator strain with the plasmid and isolating the mutated plasmid from the mutator strain. The mutated plasmid may subsequently be transformed into the expression organism.
The DNA sequence to be mutagenized may conveniently be present in a genomic or cDNA library prepared from an organism expressing the parent cellulase enzyme. Alternatively, the DNA sequence may be present on a suitable vector such as a plasmid or a bacteriophage, which as such may be incubated with or otherwise exposed to the mutagenizing agent. The DNA to be mutagenized may also be present in a host cell either by being integrated in the genome of said cell or by being present on a vector harboured in the cell. Finally, the DNA to be mutagenized may be in isolated form. It will be understood that the DNA sequence to be subjected to random mutagenesis is preferably a cDNA or a genomic DNA sequence.
In some cases it may be convenient to amplify the mutated DNA sequence prior to the expression step or the screening step being performed. Such amplification may be performed in accordance with methods known in the art, the presently preferred method being PCR-generated amplification using oligonucleotide primers prepared on the basis of the DNA or amino acid sequence of the parent enzyme. Subsequent to the incubation with or exposure to the mutagenizing agent, the mutated DNA is expressed by culturing a suitable host cell carrying the DNA sequence under conditions allowing expression to take place. The host cell used for this purpose may be one which has been transformed with the mutated DNA sequence, optionally present on a vector, or one which was carried the DNA sequence encoding the parent enzyme during the mutagenesis treatment. Examples of suitable host cells are fungal hosts such as Aεpergillus niger or Aspergillus oryzae. The mutated DNA sequence may further comprise a DNA sequence encoding functions permitting expression of the mutated DNA sequence. Localized random mutagenesis
The random mutagenesis may advantageously be localized to a part of the parent cellulase in question. This may, e.g., be advantageous when certain regions of the enzyme have been identified to be of particular importance for a given property of the enzyme, and when modified are expected to result in a variant having improved properties. Such regions may normally be identified when the tertiary structure of the parent enzyme has been elucidated and related to the function of the enzyme.
The localized random mutagenesis is conveniently performed by use of PCR-generated mutagenesis techniques as described above or any other suitable technique known in the art. Alternatively, the DNA sequence encoding the part of the DNA sequence to be modified may be isolated, e.g. by being inserted into a suitable vector, and said part may subsequently be subjected to mutagenesis by use of any of the mutagenesis methods discussed above. With respect to the screening step in the above-mentioned method of the invention, this may conveniently be performed by use of aa filter assay based on the following principle:
A microorganism capable of expressing the mutated cellulase enzyme of interest is incubated on a suitable medium and under suitable conditions for the enzyme to be secreted, the medium being provided with a double filter comprising a first protein- binding filter and on top of that a second filter exhibiting a low protein binding capability. The microorganism is located on the second filter. Subsequent to the incubation, the first filter comprising enzymes secreted from the microorganisms is separated from the second filter comprising the microorganisms. The first filter is subjected to screening for the desired enzymatic activity and the corresponding microbial colonies present on the second filter are identified. The filter used for binding the enzymatic activity may be any protein binding filter e.g. nylon or nitrocellulose. The top filter carrying the colonies of the expression organism may be any filter that has no or low affinity for binding proteins e.g. cellulose acetate or Durapore™. The filter may be pretreated with any of the conditions to be used for screening or may be treated during the detection of enzymatic activity.
The enzymatic activity may be detected by a dye, fluorescence, precipitation, pH indicator, IR-absorbance or any other known technique for detection of enzymatic activity.
The detecting compound may be immobilized by any immobilizing agent, e.g., agarose, agar, gelatine, polyacrylamide, starch, filter paper, cloth; or any combination of immobilizing agents. Expression of cellulase variants According to the invention, a DNA sequence encoding the variant produced by methods described above, or by any alternative methods known in the art, can be expressed, in enzyme form, using an expression vector which typically includes control sequences encoding a promoter, operator, ribosome binding site, translation initiation signal, and, optionally, a repressor gene or various activator genes.
The recombinant expression vector carrying the DNA sequence encoding a cellulase variant of the invention may be any vector which may conveniently be subjected to recombinant DNA procedures, and the choice of vector will often depend on the host cell into which it is to be introduced. Thus, the vector may be an autonomously replicating vector, i.e. a vector which exists as an extrachromosomal entity, the replication of which is independent of chromosomal replication, e.g. a plasmid, a bacteriophage or an extrachromosomal element, minichromosome or an artificial chromosome. Alternatively, the vector may be one which, when introduced into a host cell, is integrated into the host cell genome and replicated together with the chromosome (s) into which it has been integrated. In the vector, the DNA sequence should be operably connected to ' a suitable promoter sequence. The promoter may be any DNA sequence which shows transcriptional activity in the host cell of choice and may be derived from genes encoding proteins either homologous or heterologous to the host cell. Examples of suitable promoters for directing the transcription of the DNA sequence encoding a cellulase variant of the invention, especially in a fungal host, are those derived from the gene encoding A. oryzae TAKA amylase,
Rhizomucor miehei aspartic proteinase, A. niger neutral α-amylase, A. niger acid stable α-amylase, A. niger glucoamylase, Rhizomucor miehei lipase, A. oryzae alkaline protease, A. oryzae triose phosphate isomerase or A. nidulanε acetamidase.
Examples of suitable promoters for use in bacterial host cells include the promoter of the Bacilluε εtearothermophiluε maltogenic amylase gene, the Bacilluε licheniformis alpha- amylase gene, the Bacillus amyloliquefaciens alpha-amylase gene, the Bacillus subtiliε alkaline protease gen, or the Bacilluε pumiluε xylosidase gene, or the phage Lambda PR or P promoters or the E. coli lac, trp or tac promoters. The expression vector of the invention may also comprise a suitable transcription terminator and, in eukaryotes, poly- adenylation sequences operably connected to the DNA sequence encoding the cellulase variant of the invention. Termination and polyadenylation sequences may suitably be derived from the same sources as the promoter.
The vector may further comprise a DNA sequence enabling the vector to replicate in the host cell in question. Examples of such sequences are the origins of replication of plasmids pUC19, pACYC177, pUBHO, pE194, pAMBl and pIJ702. The vector may also comprise a selectable marker, e.g. a gene, the product of which complements a defect in the host cell, such as one which confers antibiotic resistance such as ampicillin, kanamycin, chloramphenicol or tetracyclin resistance. Furthermore, the vector may comprise Aεpergilluε selection markers such as amdS, argB, niaD and sC, a marker giving rise to hygromycin resistance, or the selection may be accomplished by co-transformation, e.g. as described in WO 91/17243.
The procedures used to ligate the DNA construct of the invention encoding a cellulase variant, the promoter, terminator and other elements, respectively, and to insert them into suitable vectors containing the information necessary for replication, are well known to persons skilled in the art (cf., for instance, Sambrook et al. (1989)). The cell of the invention, either comprising a DNA construct or an expression vector of the invention as defined above, is advantageously used as a host cell in the recombinant production of a cellulase variant of the invention. The cell may be transformed with the DNA construct of the invention encoding the variant, conveniently by integrating the DNA construct (in one or more copies) in the host chromosome. This integration is generally considered to be an advantage as the DNA sequence is more likely to be stably maintained in the cell. Integration of the DNA con- structs into the host chromosome may be performed according to conventional methods, e.g. by homologous or heterologous recombination. Alternatively, the cell may be transformed with an expression vector as described above in connection with the different types of host cells. The cell of the invention may be a cell of a higher organism such as a mammal or an insect, but is preferably a microbial cell, e.g. a bacterial or fungal cell.
Examples of bacterial host cells which on cultivation are capable of producing the enzyme of the invention may be a gram-positive bacteria such as a strain of Bacilluε , in particular Bacilluε alkalophiluε , Bacilluε amyloliquefacienε, Bacilluε breviε , Bacilluε lautuε , Bacilluε lentuε, Bacilluε licheniformiε , Bacilluε circulanε , Bacillus coagulans , Bacilluε megatherium, Bacilluε εtearothermophiluε , Bacilluε εubtiliε and Bacilluε thuringienεis , a strain of Lactobacillus , a strain of Streptococcus , a strain of Streptomyces , in particular Streptomyces lividans and Streptomyces murinus , or the host cell may be a gram-negative bacteria such as a strain of Eεcherichia coli . The transformation of the bacteria may be effected by protoplast transformation, electroporation, conjugation, or by using competent cells in a manner known per se (cf. e.g. Sambrook et al., εupra) .
When expressing the enzyme in a bacteria such as Eεcherichia coli , the enzyme may be retained in the cytoplasm, typically as insoluble granules (known as inclusion bodies) , or may be directed to the periplasmic space by a bacterial secretion sequence. In the former case, the cells are lysed and the granules are recovered and denatured after which the enzyme is refolded by diluting the denaturing agent. In the latter case, the enzyme may be recovered from the periplasmic space by disrupting the cells, e.g. by sonication or osmotic shock, to release the contents of the periplasmic space and recovering the enzyme.
When expressing the enzyme in a gram-positive bacteria such as a strain of Bacilluε or a strain of Streptomyceε , the enzyme may be retained in the cytoplasm, or may be directed to the extracellular medium by a bacterial secretion sequence. Examples of a fungal host cell which on cultivation are capable of producing the enzyme of the invention is e.g. a strain of Aεpergilluε or Fuεarium , in particular Aεpergilluε aw amor i , Aεpergilluε nidulanε , Aεpergilluε niger, Aεpergilluε oryzae , and Fuεarium oxysporum, and a strain of Trichoderma , preferably Trichoderma harzianum , Trichoderma reeεei and Trichoderma viride .
Fungal cells may be transformed by a process involving protoplast formation and transformation of the protoplasts followed by regeneration of the cell wall in a manner known per εe . The use of a strain of Aεpergilluε as a host cell is described in EP 238 023 (Novo Nordisk A/S) , the contents of which are hereby incorporated by reference.
Examples of a host cell of yeast origin which on cultivation are capable of producing the enzyme of the invention is e.g. a strain of Hanεenula sp., a strain of Kluyveromyceε sp . , in particular Kluyveromyceε lactiε and Kluyveromyceε marcianuε , a strain of Pichia εp. , a strain of Saccharomyces , in particular Saccharomyces carlεbergenεiε , Saccharomyceε cerevisae, Saccharomyceε kluyveri and Saccharomyceε uvarum , a strain of Schizoεaccharomyceε εp . , in particular
Schizosaccharomyces pombe , and a strain of Yarrowia εp . , in particular Yarrowia lipolytica .
Examples of a host cell of plant origin which on cultivation are capable of producing the enzyme of the invention is e.g. a plant cell of Solanum tuberoεum or Nicotiana tabacum . In a yet further aspect, the present invention relates to a method of producing a cellulase variant of the invention, which method comprises cultivating a host cell as described above under conditions conducive to the production of the variant and recovering the variant from the cells and/or culture medium.
The medium used to cultivate the cells may be any conventional medium suitable for growing the host cell in question and obtaining expression of the cellulase variant of the invention. Suitable media are available from commercial suppliers or may be prepared according to published recipes (e.g. as described in catalogues of the American Type Culture Collection) .
The cellulase variant secreted from the host cells may con- veniently be recovered from the culture medium by well-known procedures, including separating the cells from the medium by centrifugation or filtration, and precipitating proteinaceous components of the medium by means of a salt such as ammonium sulphate, followed by the use of chromatographic procedures such as ion exchange chromatography, affinity chromatography, or the like.
The cleaning or detergent or fabric conditioning compositions
During washing and wearing, dyestuff from dyed fabrics or garment will conventionally bleed from the fabric which then looks faded and worn. Removal of surface fibers from the fabric will partly restore the original colours and looks of the fabric. By the term "colour clarification", as used herein, is meant the partly restoration of the initial colours of fabric or garment throughout multiple washing cycles.
The term "de-pilling" denotes removing of pills from the fabric surface.
The term "soaking liquor" denotes an aqueous liquor in which laundry may be immersed prior to being subjected to a conventional washing process. The soaking liquor may contain one or more ingredients conventionally used in a washing or laundering process.
The term "washing liquor" denotes an aqueous liquor in which laundry is subjected to a washing process, i.e. usually a combined chemical and mechanical action either manually or in a washing machine. Conventionally, the washing liquor is an aqueous solution of a powder or liquid detergent composition.
The term "rinsing liquor" denotes an aqueous liquor in which laundry is immersed and treated, conventionally immediately after being subjected to a washing process, in order to rinse the laundry, i.e. essentially remove the detergent solution from the laundry. The rinsing liquor may contain a fabric conditioning or softening composition. In another aspect, the present invention also relates to a process for machine treatment of fabrics which process comprises treating fabric during a rinse cycle of a machine washing process with a rinse solution containing the composition according to the invention. The laundry subjected to the composition or the method of the present invention may be conventional washable laundry. Preferably, the major part of the laundry is sewn or unsewn fabrics, including knits, wovens, denims, yarns, and toweling, made from cotton, cotton blends or natural or manmade cellulosics (e.g. originating from xylan-containing cellulose fibers such as from wood pulp) or blends thereof. Examples of blends are blends of cotton or rayon/viscose with one or more companion material such as wool, synthetic fibers (e.g. polyamide fibers, acrylic fibers, polyester fibers, polyvinyl alcohol fibers, polyvinyl chloride fibers, polyvinylidene chloride fibers, polyurethane fibers, polyurea fibers, aramid fibers) , and cellulose-containing fibers (e.g. rayon/viscose, ramie, flax/linen, jute, cellulose acetate fibers, lyocell) . Cleaning composition according to claim 1 wherein the composi- tion is a fabric softener or fabric conditioning composition for the treatment of fabrics.
The cleaning composition of the invention may be in the form of a fabric softener composition comprising from about 1% to about 90%, preferably from about 2% to about 50%, by weight of one or more cationic fabric softening agents, nonionic fabric softening agents, or mixtures thereof. In case of cationic fabric softening agents, such agents may advantageously comprise quaternary ammonium softening agents or a ine precursors thereof. A Specific example of a useful quaternary ammonium sof- tening agent is N,N-di (2-tallowoyl-oxy-ethyl) -N,N-dimethyl ammonium chloride.
DETERGENT AND FABRIC SOFTENER DISCLOSURE AND EXAMPLES surfactant system
The cleaning compositions according to the present invention comprise a surfactant system, wherein the surfactant can be selected from nonionic and/or anionic and/or cationic 5 and/or ampholytic and/or zwitterionic and/or semi-polar surfactants.
The surfactant is typically present at a level from 0.1% to 60% by weight.
The surfactant is preferably formulated to be compatible
10 with enzyme components present in the composition. In liquid or gel compositions the surfactant is most preferably formulated in such a way that it promotes, or at least does not degrade, the stability of any enzyme in these compositions.
Preferred systems to be used according to the present
15 invention comprise as a surfactant one or more of the nonionic and/or anionic surfactants described herein.
Polyethylene, polypropylene, and polybutylene oxide condensates of alkyl phenols are suitable for use as the nonionic surfactant of the surfactant systems of the present
20 invention, with the polyethylene oxide condensates being preferred. These compounds include the condensation products of alkyl phenols having an alkyl group containing from about 6 to about 14 carbon atoms, preferably from about 8 to about 14 carbon atoms, in either a straight chain or branched-chain con-
25 figuration with the alkylene oxide. In a preferred embodiment, the ethylene oxide is present in an amount equal to from about 2 to about 25 moles, more preferably from about 3 to about 15 moles, of ethylene oxide per mole of alkyl phenol. Commercially available nonionic surfactants of this type include Igepal CO-
30 630, marketed by the GAF Corporation; and Triton™ X-45, X-114, X-100 and X-102, all marketed by the Rohm & Haas Company. These surfactants are commonly referred to as alkylphenol alkoxylates (e.g., alkyl phenol ethoxylates) .
The condensation products of primary and secondary
35 aliphatic alcohols with about 1 to about 25 moles of ethylene oxide are suitable for use as the nonionic surfactant of the nonionic surfactant systems of the present invention. The alkyl chain of the aliphatic alcohol can either be straight or branched, primary or secondary, and generally contains from about 8 to about 22 carbon atoms. Preferred are the condensation products of alcohols having an alkyl group containing from about 8 to about 20 carbon atoms, more preferably from about 10 to about 18 carbon atoms, with from about 2 to about 10 moles of ethylene oxide per mole of alcohol. About 2 to about 7 moles of ethylene oxide and most preferably from 2 to 5 moles of ethylene oxide per mole of alcohol are present in said condensation products. Examples of commercially available nonionic surfactants of this type include Tergitol™ 15-S-9 (The condensation product of Cji-Cis linear alcohol with 9 moles ethylene oxide) , Tergitol™ 24-L-6 NMW (the condensation product of C12-C14 primary alcohol with 6 moles ethylene oxide with a narrow molecular weight distribution) , both marketed by Union Carbide
Corporati •on; NeodolTM 45-9 (the condensation product of C1 -C15 linear alcohol with 9 moles of ethylene oxide) , Neodol™ 23-3 (the condensation product of C12-C13 linear alcohol with 3.0 moles of ethylene oxide) , Neodol™ 45-7 (the condensation product of C1 -Ci5 linear alcohol with 7 moles of ethylene oxide) , Neodol™ 45-5 (the condensation product of Ci4-C15 linear alcohol with 5 moles of ethylene oxide) marketed by Shell
Chemical Company, Kyro™ EOB (the condensation product of C13-C15 alcohol with 9 moles ethylene oxide) , marketed by The Procter & Gamble Company, and Genapol LA 050 (the condensation product of Ci2~Ci4 alcohol with 5 moles of ethylene oxide) marketed by Hoechst. Preferred range of HLB in these products is from 8-11 and most preferred from 8-10.
Also useful as the nonionic surfactant of the surfactant systems of the present invention are alkylpolysaccharides disclosed in US 4,565,647, having a hydrophobic group containing from about 6 to about 30 carbon atoms, preferably from about 10 to about 16 carbon atoms and a polysaccharide, e.g. a polyglycoside, hydrophilic group containing from about 1.3 to about 10, preferably from about 1.3 to about 3, most preferably from about 1.3 to about 2.7 saccharide units. Any reducing saccharide containing 5 or 6 carbon atoms can be used, e.g. , glucose, galactose and galactosyl moieties can be substituted for the glucosyl moieties (optionally the hydrophobic group is attached at the 2-, 3-, 4-, etc. positions thus giving a glucose or galactose as opposed to a glucoside or galactoside) . The intersaccharide bonds can be, e.g. , between the one position of the additional saccharide units and the 2-, 3-, 4-, and/or 6- positions on the preceding saccharide units.
The preferred alkylpolyglycosides have the formula
R2o (cnH2n0) t (glycosyl) x
wherein R2 is selected from the group consisting of alkyl, alkylphenyl, hydroxyalkyl, hydroxyalkylphenyl, and mixtures thereof in which the alkyl groups contain from about 10 to about 18, preferably from about 12 to about 14, carbon atoms; n is 2 or 3, preferably 2; t is from 0 to about 10, pre-ferably 0; and x is from about 1.3 to about 10, preferably from about 1.3 to about 3 , most preferably from about 1.3 to about 2.7. The glycosyl is preferably derived from glucose. To prepare these compounds, the alcohol or alkylpolyethoxy alcohol is formed first and then reacted with glucose, or a source of glucose, to form the glucoside (attachment at the 1-position) . The additional glycosyl units can then be attached between their 1- position and the preceding glycosyl units 2-, 3-, 4-, and/or 6- position, preferably predominantly the 2-position.
The condensation products of ethylene oxide with a hydrophobic base formed by the condensation of propylene oxide with propylene glycol are also suitable for use as the additional nonionic surfactant systems of the present invention. The hydrophobic portion of these compounds will preferably have a molecular weight from about 1500 to about 1800 and will exhibit water insolubility. The addition of polyoxyethylene moieties to this hydrophobic portion tends to increase the water solubility of the molecule as a whole, and the liquid character of the product is retained up to the point where the polyoxyethylene content is about 50% of the total weight of the condensation product, which corresponds to condensation with up to about 40 moles of ethylene oxide. Examples of compounds of this type include certain of the commercially available Pluronic™ surfactants, marketed by BASF.
Also suitable for use as the nonionic surfactant of the nonionic surfactant system of the present invention, are the condensation products of ethylene oxide with the product resulting from the reaction of propylene oxide and ethylenediamine. The hydrophobic moiety of these products consists of the reaction product of ethylenediamine and excess propylene oxide, and generally has a molecular weight of from about 2500 to about 3000. This hydrophobic moiety is condensed with ethylene oxide to the extent that the condensation product contains from about 40% to about 80% by weight of polyoxyethylene and has a molecular weight of from about 5,000 to about 11,000. Examples of this type of nonionic surfactant i •nclude certai•n of the commerci.ally avai.lable Tetroni■cTM compounds, marketed by BASF.
Preferred for use as the nonionic surfactant of the surfactant systems of the present invention are polyethylene oxide condensates of alkyl phenols, condensation products of primary and secondary aliphatic alcohols with from about 1 to about 25 moles of ethyleneoxide, alkylpolysaccharides, and mixtures hereof. Most preferred are C8-C14 alkyl phenol ethoxylates having from 3 to 15 ethoxy groups and Cs-Cis alcohol ethoxylates (preferably C10 avg.) having from 2 to 10 ethoxy groups, and mixtures thereof.
Highly preferred nonionic surfactants are polyhydroxy fatty acid amide surfactants of the formula
R2 - C - N - Z,
II II 0 R1 wherein R is H, or R is C!_4 hydrocarbyl, 2-hydroxyethyl, 2- hydroxypropyl or a mixture thereof, R2 is C5_31 hydrocarbyl, and Z is a polyhydroxyhydrocarbyl having a linear hydrocarbyl chain with at least 3 hydroxyIs directly connected to the chain, or an alkoxylated derivative thereof. Preferably, R1 is methyl, R2 is straight Cιι_ι5 alkyl or C16_18 alkyl or alkenyl chain such as coconut alkyl or mixtures thereof, and Z is derived from a reducing sugar such as glucose, fructose, maltose or lactose, in a reductive amination reaction. Highly preferred anionic surfactants include alkyl alkoxylated sulfate surfactants. Examples hereof are water soluble salts or acids of the formula R0(A)mS03M wherein R is an unsubstituted C10-C-24 alkyl or hydroxyalkyl group having a C^o- C24 alkyl component, preferably a C12-C2o alkyl or hydro-xyalkyl. more preferably Cι2~Ci8 alkyl or hydroxyalkyl, A is an ethoxy or propoxy unit, m is greater than zero, typically between about 0.5 and about 6 , more preferably between about 0.5 and about 3 , and M is H or a cation which can be, for example, a metal cation (e.g., sodium, potassium, lithium, calcium, magnesium, etc.), ammonium or substituted-ammonium cation. Alkyl ethoxylated sulfates as well as alkyl propoxylated sulfates are contemplated herein. Specific examples of substituted ammonium cations include methyl-, dimethyl, trimethyl-ammonium cations and quaternary ammonium cations such as tetramethyl-ammonium and dimethyl piperdinium cations and those derived from alkylamines such as ethylamine, diethylamine, triethylamine, mixtures thereof, and the like. Exemplary surfactants are Ci2-C18 alkyl polyethoxylate (1.0) sulfate (C12-C18E(1.0)M) , C12-C18 alkyl polyethoxylate (2.25) sulfate (C12-C18 (2.25)M, and C12-C18 alkyl polyethoxylate (3.0) sulfate (C12-C18E(3.0)M) , and C12-C18 alkyl polyethoxylate (4.0) sulfate (C12-C18E(4.0)M) , wherein M is conveniently selected from sodium and potassium. Suitable anionic surfactants to be used are alkyl ester sulfonate surfactants including linear esters of C8-C2o carboxylic acids (i.e., fatty acids) which are sulfonated with gaseous S03 according to "The Journal of the American Oil Chemists Society", 52 (1975), pp. 323-329. Suitable starting materials would include natural fatty substances as derived from tallow, palm oil, etc.
The preferred alkyl ester sulfonate surfactant, especially for laundry applications, comprise alkyl ester sulfonate surfactants of the structural formula:
0 I I
R3 - CH - C - OR4
S03M
wherein R3 is a C8-C2o hydrocarbyl, preferably an alkyl, or combination thereof, R4 is a Ci-Cβ hydrocarbyl, preferably an alkyl, or combination thereof, and M is a cation which forms a water soluble salt with the alkyl ester sulfonate. Suitable salt-forming cations include metals such as sodium, potassium, and lithium, and substituted or unsubstituted ammonium cations, such as monoethanolamine, diethonolamine, and triethanolamine. Preferably, R3 is C10-C16 alkyl, and R4 is methyl, ethyl or isopropyl. Especially preferred are the methyl ester sulfonates wherein R3 is Cio-C^ alkyl.
Other suitable anionic surfactants include the alkyl sulfate surfactants which are water soluble salts or acids of the formula ROSO3M wherein R preferably is a C10-C24 hydrocarbyl, preferably an alkyl or hydroxyalkyl having a C10-C2o alkyl com- ponent, more preferably a Ci2~C18 alkyl or hydroxyalkyl, and M is H or a cation, e.g., an alkali metal cation (e.g. sodium, potassium, lithium) , or ammonium or substituted ammonium (e.g. methyl-, dimethyl-, and trimethyl ammonium cations and quaternary ammonium cations such as tetramethyl-ammonium and dimethyl piperdinium cations and quaternary ammonium cations derived from alkylamines such as ethylamine, diethylamine, triethylamine, and mixtures thereof, and the like) . Typically, alkyl chains of Ci2~C_6 are preferred for lower wash temperatures (e.g. below about 50°C) and C^-C s alkyl chains are preferred for higher wash temperatures (e.g. above about 50 °C) .
Other anionic surfactants useful for detersive purposes can also be included in the cleaning, especially laundry detergent, compositions of the present invention. Theses can include salts (including, for example, sodium, potassium, ammonium, and substituted ammonium salts such as mono- di- and triethanolamine salts) of soap, C8-C22 primary or secondary alkanesulfonates, C8-C24 olefinsulfonates, sulfonated polycarboxylic acids prepared by sulfonation of the pyrolyzed product of alkaline earth metal citrates, e.g., as described in British patent specification No. 1,082,179, C8-C24 alkylpo- lyglycolethersulfates (containing up to 10 moles of ethylene oxide) ; alkyl glycerol sulfonates, fatty acyl glycerol sulfonates, fatty oleyl glycerol sulfates, alkyl phenol ethylene oxide ether sulfates, paraffin sulfonates, alkyl phosphates, isethionates such as the acyl isethionates, N-acyl taurates, alkyl succinamates and sulfosuccinates, monoesters of sulfosuccinates (especially saturated and unsaturated Ci2~Cι8 monoesters) and diesters of sulfosuccinates (especially saturated and unsaturated C6-C12 diesters) , acyl sarcosinates, sulfates of alkylpolysaccharides such as the sulfates of alkylpolyglucoside (the nonionic nonsulfated compounds being described below) , branched primary alkyl sulfates, and alkyl polyethoxy carboxylates such as those of the formula RO(CH2CH2O) -CH2C00-M+ wherein R is a C8-C22 alkyl, k is an integer from 1 to 10, and M is a soluble salt forming cation. Resin acids and hydrogenated resin acids are also suitable, such as rosin, hydrogenated rosin, and resin acids and hydrogenated resin acids present in or derived from tall oil. Alkylbenzene sulfonates are highly preferred. Especially preferred are linear (straight-chain) alkyl benzene sulfonates (LAS) wherein the alkyl group preferably contains from 10 to 18 carbon atoms.
Further examples are described in "Surface Active Agents and Detergents" (Vol. I and II by Schwartz, Perrry and Berch) . A variety of such surfactants are also generally disclosed in US 3,929,678, (Column 23, line 58 through Column 29, line 23, herein incorporated by reference) .
When included therein, the cleaning, especially laundry detergent, compositions of the present invention typically comprise from about 1% to about 40%, preferably from about 3% to about 20% by weight of such anionic surfactants.
The cleaning compositions of the present invention may also contain cationic, ampholytic, zwitterionic, and semi-polar surfactants, as well as the nonionic and/or anionic surfactants other than those already described herein.
Cationic detersive surfactants suitable for use in the laundry detergent compositions of the present invention are those having one long-chain hydrocarbyl group. Examples of such cationic surfactants include the ammonium surfactants such as alkyltrimethylammonium halogenides, and those surfactants having the formula:
[R2(OR3)y] [R4(OR3)y]2R5N+X- wherein R2 is an alkyl or alkyl benzyl group having from about 8 to about 18 carbon atoms in the alkyl chain, each R3 is selected form the group consisting of -CH2CH2-, -CH2CH(CH3) -, - CH2CH(CH2OH)-, -CH2CH2CH2-, and mixtures thereof; each R4 is selected from the group consisting of C!-C4 alkyl, Cι~C hydroxyalkyl, benzyl ring structures formed by joining the two R4 groups, -CH2CHOHCHOHCOR6CHOHCH2OH, wherein R6 is any hexose or hexose polymer having a molecular weight less than about 1000, and hydrogen when y is not 0; R5 is the same as R or is an alkyl chain,wherein the total number of carbon atoms or R plus R5 is not more than about 18; each y is from 0 to about 10, and the sum of the y values is from 0 to about 15; and X is any compatible anion.
Highly preferred cationic surfactants are the water soluble quaternary ammonium compounds useful in the present composition having the formula:
R1R2R3R4N+X" (i)
wherein Ri is C8-C16 alkyl, each of R2, R3 and R4 is independently C!-C4 alkyl, C!-C4 hydroxy alkyl, benzyl, and - (c 2 H 4θ)xH where x has a value from 2 to 5, and X is an anion. Not more than one of R2, R3 or R4 should be benzyl.
The preferred alkyl chain length for Ri is C12-C15, particularly where the alkyl group is a mixture of chain lengths derived from coconut or palm kernel fat or is derived synthetically by olefin build up or 0X0 alcohols synthesis.
Preferred groups for R2R3 and R4 are methyl and hydroxyethyl groups and the anion X may be selected from halide, methosulphate, acetate and phosphate ions.
Examples of suitable quaternary ammonium compounds of formulae (i) for use herein are: coconut trimethyl ammonium chloride or bromide; coconut methyl dihydroxyethyl ammonium chloride or bromide; decyl triethyl ammonium chloride; decyl dimethyl hydroxyethyl ammonium chloride or bromide; C 12-15 dimethyl hydroxyethyl ammonium chloride or bromide; coconut dimethyl hydroxyethyl ammonium chloride or bromide; myristyl trimethyl ammonium methyl sulphate; lauryl dimethyl benzyl ammonium chloride or bromide; lauryl dimethyl (ethenoxy)4 ammonium chloride or bromide; choline esters (compounds of formula (i) wherein Ri is
CH2-CH2-0-C-C12-ι4 alkyl and R2R3R4 are methyl) .
10 di-alkyl imidazolines [compounds of formula (i)].
Other cationic surfactants useful herein are also described in US 4,228,044 and in EP 000 224.
When included therein, the laundry detergent compositions of the present invention typically comprise from 0.2% to about
15 25%, preferably from about 1% to about 8% by weight of such cationic surfactants.
Ampholytic surfactants are also suitable for use in the laundry detergent compositions of the present invention. These surfactants can be broadly described as aliphatic derivatives of
20 secondary or tertiary amines, or aliphatic derivatives of heterocyclic secondary and tertiary amines in which the aliphatic radical can be straight- or branched-chain. One of the aliphatic substituents contains at least about 8 carbon atoms, typically from about 8 to about 18 carbon atoms, and at least
25 one contains an anionic water-solubilizing group, e.g. carboxy, sulfonate, sulfate. See US 3,929,678 (column 19, lines 18-35) for examples of ampholytic surfactants.
When included therein, the cleaning, e.g. laundry detergent, compositions of the present invention typically
30 comprise from 0.2% to about 15%, preferably from about 1% to about 10% by weight of such ampholytic surfactants.
Zwitterionic surfactants are also suitable for use in cleaning compositions. These surfactants can be broadly described as derivatives of secondary and tertiary amines,
35 derivatives of heterocyclic secondary and tertiary amines, or derivatives of quaternary ammonium, quaternary phosphonium or tertiary sulfonium compounds. See US 3,929,678 (column 19, line 38 through column 22, line 48) for examples of zwitterionic surfactants. When included therein, the cleaning compositions of the present invention typically comprise from 0.2% to about 15%, preferably from about 1% to about 10% by weight of such zwitterionic surfactants. Semi-polar nonionic surfactants are a special category of nonionic surfactants which include water-soluble amine oxides containing one alkyl moiety of from about 10 to about 18 carbon atoms and 2 moieties selected from the group consisting of alkyl groups and hydroxyalkyl groups containing from about 1 to about 3 carbon atoms; watersoluble phosphine oxides containing one alkyl moiety of from about 10 to about 18 carbon atoms and 2 moieties selected from the group consisting of alkyl groups and hydroxyalkyl groups containing from about 1 to about 3 carbon atoms; and water-soluble sulfoxides containing one alkyl moiety from about 10 to about 18 carbon atoms and a moiety selected from the group consisting of alkyl and hydroxyalkyl moieties of from about 1 to about 3 carbon atoms.
Semi-polar nonionic detergent surfactants include the amine oxide surfactants having the formula:
O
R3(OR4)xN(R5)2
wherein R is an alkyl, hydroxyalkyl, or alkyl phenyl group or mixtures thereof containing from about 8 to about 22 carbon atoms; R is an alkylene or hydroxyalkylene group containing from about 2 to about 3 carbon atoms or mixtures thereof; x is from 0 to about 3 : and each R5 is an alkyl or hydroxyalkyl group containing from about 1 to about 3 carbon atoms or a polyethylene oxide group containing from about 1 to about 3 ethylene oxide groups. The R5 groups can be attached to each other, e.g., through an oxygen or nitrogen atom, to form a ring structure . These amine oxide surfactants in particular include Cιo_Ci8 alkyl dimethyl amine oxides and C8-C12 alkoxy ethyl dihydroxy ethyl amine oxides.
When included therein, the cleaning compositions of the present invention typically comprise from 0.2% to about 15%, preferably from about 1% to about 10% by weight of such semi- polar nonionic surfactants.
Builder system
5 The compositions according to the present invention may further comprise a builder system. Any conventional builder system is suitable for use herein including aluminosilicate materials, silicates, polycarboxylates and fatty acids, materials such as ethylenediamine tetraacetate, metal ion
10 sequestrants such as aminopolyphosphonates, particularly ethylenediamine tetramethylene phosphonic acid and diethylene triamine pentamethylenephosphonic acid. Though less preferred for obvious environmental reasons, phosphate builders can also be used herein.
15 Suitable builders can be an inorganic ion exchange material, commonly an inorganic hydrated aluminosilicate material, more particularly a hydrated synthetic zeolite such as hydrated zeolite A, X, B, HS or MAP.
Another suitable inorganic builder material is layered
20 silicate, e.g. SKS-6 (Hoechst) . SKS-6 is a crystalline layered silicate consisting of sodium silicate (Na2Si205) .
Suitable polycarboxylates containing one carboxy group include lactic acid, glycolic acid and ether derivatives thereof as disclosed in Belgian Patent Nos. 831,368, 821,369 and
25 821,370. Polycarboxylates containing two carboxy groups include the water-soluble salts of succinic acid, malonic acid, (ethylenedioxy) diacetic acid, aleic acid, diglycollic acid, tartaric acid, tartronic acid and fumaric acid, as well as the ether carboxylates described in German Offenle-enschrift
30 2,446,686, and 2,446,487, US 3,935,257 and the sulfinyl carboxylates described in Belgian Patent No. 840,623. Polycarboxylates containing three carboxy groups include, in particular, water-soluble citrates, aconitrates and citraconates as well as succinate derivatives such as the
35 carboxy ethyloxysuccinates described in British Patent No. 1,379,241, lactoxysuccinates described in Netherlands Application 7205873, and the oxypolycarboxylate materials such as 2-oxa-l, 1, 3-propane tricarboxylates described in British Patent No. 1,387,447. Polycarboxylates containing four carboxy groups include oxydisuccinates disclosed in British Patent No. 1,261,829, 1,1,2,2, -ethane tetracarboxylates , 1,1,3,3-propane tetrac7arboxylates containing sulfo substituents include the sulfosuccinate derivatives disclosed in British Patent Nos.
1,398,421 and 1,398,422 and in US 3,936,448, and the sulfonated pyrolysed citrates described in British Patent No. 1,082,179, while polycarboxylates containing phosphone substituents are disclosed in British Patent No. 1,439,000. Alicyclic and heterocyclic polycarboxylates include cyclopentane-cis , cis-cis-tetracarboxylates , cyclopentadienide pentacarboxylates, 2, 3 , 4, 5-tetrahydro-furan - cis, cis, cis- tetracarboxylates , 2 , 5-tetrahydro-furan-cis, discarboxylates, 2 , 2 , 5 , 5 , -tetrahydrof ran - tetracarboxylates, 1, 2 , 3 , 4 , 5 , 6-hexane - hexacarboxylates and carboxymethyl derivatives of polyhydric alcohols such as sorbitol, mannitol and xylitol. Aromatic polycarboxylates include mellitic acid, pyromellitic acid and the phthalic acid derivatives disclosed in British Patent No. 1,425,343. Of the above, the preferred polycarboxylates are hydroxy- carboxylates containing up to three carboxy groups per molecule, more particularly citrates.
Preferred builder systems for use in the present compositions include a mixture of a water-insoluble aluminosilicate builder such as zeolite A or of a layered silicate (SKS-6) , and a water-soluble carboxylate chelating agent such as citric acid.
A suitable chelant for inclusion in the cleaning compositions in accordance with the invention is ethylenediamine-N,N' - disuccinic acid (EDDS) or the alkali metal, alkaline earth metal, ammonium, or substituted ammonium salts thereof, or mixtures thereof. Preferred EDDS compounds are the free acid form and the sodium or magnesium salt thereof. Examples of such preferred sodium salts of EDDS include Na2EDDS and Na4EDDS. Examples of such preferred magnesium salts of EDDS include
MgEDDS and Mg2EDDS. The magnesium salts are the most preferred for inclusion in compositions in accordance with the invention. Preferred builder systems include a mixture of a water- insoluble aluminosilicate builder such as zeolite A, and a water soluble carboxylate chelating agent such as citric acid.
Other builder materials that can form part of the builder system for use in granular compositions include inorganic materials such as alkali metal carbonates, bicarbonates, silicates, and organic materials such as the organic phosphonates , amino polyalkylene phosphonates and amino polycarboxylates . Other suitable water-soluble organic salts are the homo- or co-polymeric acids or their salts, in which the polycarboxylic acid comprises at least two carboxyl radicals separated form each other by not more than two carbon atoms.
Polymers of this type are disclosed in GB-A-1, 596, 756. Examples of such salts are polyacrylates of MW 2000-5000 and their copolymers with maleic anhydride, such copolymers having a molecular weight of from 20,000 to 70,000, especially about 40,000.
Detergency builder salts are normally included in amounts of from 5% to 80% by weight of the composition. Preferred levels of builder for liquid detergents are from 5% to 30%.
Enzymes
Preferred cleaning compositions, in addition to the family 6 endo-β-l,4-glucanase, comprise other enzyme(s) which provides cleaning performance and/or fabric care benefits.
Such enzymes include proteases, lipases, cutinases, amylases, other cellulases, peroxidases, oxidases (e.g. laccases) . Proteases: Any protease suitable for use in alkaline solutions can be used. Suitable proteases include those of animal, vegetable or microbial origin. Microbial origin is preferred. Chemically or genetically modified mutants are included. The protease may be a serine protease, preferably an alkaline microbial protease or a trypsin-like protease. Examples of alkaline proteases are subtilisins, especially those derived from Bacillus, e.g., subtilisin Novo, subtilisin Carlsberg, subtilisin 309, subtilisin 147 and subtilisin 168 (described in WO 89/06279) . Examples of trypsin-like proteases are trypsin (e.g. of porcine or bovine origin) and the Fusarium protease described in WO 89/06270.
Preferred commercially available protease enzymes include those sold under the trade names Alcalase, Savinase, Primase, Durazym, and Esperase by Novo Nordisk A/S (Denmark) , those sold under the tradename Maxatase, Maxacal, Maxapem, Properase, Purafect and Purafect OXP by Genencor International, and those sold under the tradename Opticlean and Optimase by Solvay Enzymes. Protease enzymes may be incorporated into the compositions in accordance with the invention at a level of from 0.00001% to 2% of enzyme protein by weight of the composition, preferably at a level of from 0.0001% to 1% of enzyme protein by weight of the composition, more preferably at a level of from 0.001% to 0.5% of enzyme protein by weight of the composition, even more preferably at a level of from 0.01% to 0.2% of enzyme protein by weight of the composition.
Lipases: Any lipase suitable for use in alkaline solutions can be used. Suitable lipases include those of bacterial or fungal origin. Chemically or genetically modified mutants are included.
Examples of useful lipases include a Humicola lanuqinosa lipase, e.g., as described in EP 258 068 and EP 305 216, a Rhizomucor miehei lipase, e.g., as described in EP 238 023, a Candida lipase, such as a C. antarctica lipase, e.g., the C. antarctica lipase A or B described in EP 214 761, a Pseudomonas lipase such as a P. alcaligenes and P. pseudoalcaligenes lipase, e.g., as described in EP 218 272, a P. cepacia lipase, e.g., as described in EP 331 376, a P. stutzeri lipase, e.g., as disclosed in GB 1,372,034, a P. fluorescens lipase, a Bacillus lipase , e.g., a B. subtilis lipase (Dartois et al., (1993), Biochemica et Biophysica acta 1131, 253-260) , a B. stearo- thermophilus lipase (JP 64/744992) and a B. pu ilus lipase (WO 91/16422) . Furthermore, a number of cloned lipases may be useful, including the Penicillium camembertii lipase described by Yamaguchi et al., (1991), Gene 103, 61-67), the Geotricum candidum lipase (Schimada, Y. et al., (1989), J. Biochem., 106, 383-388) , and various Rhizopus lipases such as a R. delemar lipase (Hass, M.J et al. , (1991), Gene 109, 117-113), a R. niveus lipase (Kugimiya et al., (1992), Biosci. Biotech. Biochem. 56, 716-719) and a R. oryzae lipase.
Other types of lipolytic enzymes such as cutinases may also be useful, e.g., a cutinase derived from Pseudomonas mendocina as described in WO 88/09367, or a cutinase derived from Fusarium solani pisi (e.g. described in WO 90/09446) .
Especially suitable lipases are lipases such as Ml Lipase™, Luma fast™ and Lipomax™ (Genencor) , Lipolase™ and Lipolase Ultra™ (Novo Nordisk A/S) , and Lipase P "Amano" (Amano Pharmaceutical Co. Ltd.).
The lipases are normally incorporated in the detergent composition at a level of from 0.00001% to 2% of enzyme protein by weight of the composition, preferably at a level of from 0.0001% to 1% of enzyme protein by weight of the composition, more preferably at a level of from 0.001% to 0.5% of enzyme protein by weight of the composition, even more preferably at a level of from 0.01% to 0.2% of enzyme protein by weight of the composition. Amylases: Any amylase (a and/or b) suitable for use in alkaline solutions can be used. Suitable amylases include those of bacterial or fungal origin. Chemically or genetically modified mutants are included. Amylases include, for example, a- amylases obtained from a special strain of B. licheniformis. described in more detail in GB 1,296,839. Commercially available amylases are Duramyl TM, TermamylTM, FungamylTM and BANTM (available from Novo Nordisk A/S) and Rapidase™ and Maxamyl P™ (available from Genencor) .
The amylases are normally incorporated in the detergent composition at a level of from 0.00001% to 2% of enzyme protein by weight of the composition, preferably at a level of from 0.0001% to 1% of enzyme protein by weight of the composition, more preferably at a level of from 0.001% to 0.5% of enzyme protein by weight of the composition, even more preferably at a level of from 0.01% to 0.2% of enzyme protein by weight of the composition.
Cellulases: Any cellulase suitable for use in alkaline solutions can be used. Suitable cellulases include those of bacterial or fungal origin. Chemically or genetically modified mutants are included. Suitable cellulases are disclosed in US 4,435,307 which discloses fungal cellulases produced from Humicola insolens , in WO 96/34108 and WO 96/34092 which disclose bacterial alkalophilic cellulases (BCE 103) from Bacillus , and 5 in WO 94/21801, US 5,475,101 and US 5,419,778 which disclose EG III cellulases from Trichoderma . Especially suitable cellulases are the cellulases having colour care benefits. Examples of such cellulases are cellulases described in European patent application No. 0 495 257 and the endoglucanase of the present
10 i InventiIon. CommerciIally avaiIlable cellulases i.nclude CelluzymeTM and Carezyme™ produced by a strain of Humicola insolenε (Novo Nordisk A/S), KAC-500(B)™ (Kao Corporation), and Puradax™ (Genencor International) .
Cellulases are normally incorporated in the detergent
15 composition at a level of from 0.00001% to 2% of enzyme protein by weight of the composition, preferably at a level of from 0.0001% to 1% of enzyme protein by weight of the composition, more preferably at a level of from 0.001% to 0.5% of enzyme protein by weight of the composition, even more preferably at a
20 level of from 0.01% to 0.2% of enzyme protein by weight of the composition.
Peroxidases/Oxidases :Peroxidase enzymes are used in combination with hydrogen peroxide or a source thereof (e.g. a percarbonate, perborate or persulfate) . Oxidase enzymes are used
25 in combination with oxygen. Both types of enzymes are used for "solution bleaching", i.e. to prevent transfer of a textile dye from a dyed fabric to another fabric when said fabrics are washed together in a wash liquor, preferably together with an enhancing agent as described in e.g. WO 94/12621 and WO
30 95/01426. Suitable peroxidases/oxidases include those of plant, bacterial or fungal origin. Chemically or genetically modified mutants are included.
Peroxidase and/or oxidase enzymes are normally incorporated in the detergent composition at a level of from
35 0.00001% to 2% of enzyme protein by weight of the composition, preferably at a level of from 0.0001% to 1% of enzyme protein by weight of the composition, more preferably at a level of from 0.001% to 0.5% of enzyme protein by weight of the composition, even more preferably at a level of from 0.01% to 0.2% of enzyme protein by weight of the composition.
Mixtures of the above mentioned enzymes are encompassed herein, in particular a mixture of a protease, an amylase, a lipase and/or a cellulase.
The enzyme of the invention, or any other enzyme incorporated in the detergent composition, is normally incorporated in the detergent composition at a level from 0.00001% to 2% of enzyme protein by weight of the composition, preferably at a level from 0.0001% to 1% of enzyme protein by weight of the composition, more preferably at a level from 0.001% to 0.5% of enzyme protein by weight of the composition, even more preferably at a level from 0.01% to 0.2% of enzyme protein by weight of the composition.
Bleaching agents
Additional optional detergent ingredients that can be included in the cleaning or detergent compositions of the present invention include bleaching agents such as PB1, PB4 and percarbonate with a particle size of 400-800 microns. These bleaching agent components can include one or more oxygen bleaching agents and, depending upon the bleaching agent chosen, one or more bleach activators. When present oxygen bleaching compounds will typically be present at levels of from about 1% to about 25%. In general, bleaching compounds are optional added components in non-liquid formulations, e.g. granular detergents.
The bleaching agent component for use herein can be any of the bleaching agents useful for detergent compositions including oxygen bleaches as well as others known in the art. The bleaching agent suitable for the present invention can be an activated or non-activated bleaching agent.
One category of oxygen bleaching agent that can be used encompasses percarboxylic acid bleaching agents and salts thereof. Suitable examples of this class of agents include magnesium monoperoxyphthalate hexahydrate, the magnesium salt of meta-chloro perbenzoic acid, 4-nonylamino-4-oxoperoxybutyric acid and diperoxydodecanedioic acid. Such bleaching agents are disclosed in US 4,483,781, US 740,446, EP 0 133 354 and US 4,412,934. Highly preferred bleaching agents also include 6- nonylamino-6-oxoperoxycaproic acid as described in US 4,634,551.
Another category of bleaching agents that can be used encompasses the halogen bleaching agents. Examples of hypohalite bleaching agents, for example, include trichloro isocyanuric acid and the sodium and potassium dichloroisocyanurates and N- chloro and N-bromo alkane sulphonamides. Such materials are normally added at 0.5-10% by weight of the finished product, preferably 1-5% by weight. The hydrogen peroxide releasing agents can be used in combination with bleach activators such as tetra- acetylethylenediamine (TAED) , nonanoyloxybenzenesulfonate (NOBS, described in US 4,412,934), 3 , 5-trimethyl- hexsanoloxybenzenesulfonate (ISONOBS, described in EP 120 591) or pentaacetylglucose (PAG) , which are perhydrolyzed to form a peracid as the active bleaching species, leading to improved bleaching effect. In addition, very suitable are the bleach activators C8 (6-octanamido-caproyl) oxybenzene-sulfonate, C9(6- nonanamido caproyl) oxybenzenesulfonate and CIO (6-decanamido caproyl) oxybenzenesulfonate or mixtures thereof. Also suitable activators are acylated citrate esters such as disclosed in European Patent Application No. 91870207.7.
Useful bleaching agents, including peroxyacids and bleaching systems comprising bleach activators and peroxygen bleaching compounds for use in cleaning compositions according to the invention are described in application USSN 08/136,626.
The hydrogen peroxide may also be present by adding an enzymatic system (i.e. an enzyme and a substrate therefore) which is capable of generation of hydrogen peroxide at the beginning or during the washing and/or rinsing process. Such enzymatic systems are disclosed in European Patent Application EP 0 537 381.
Bleaching agents other than oxygen bleaching agents are also known in the art and can be utilized herein. One type of non-oxygen bleaching agent of particular interest includes photoactivated bleaching agents such as the sulfonated zinc and- /or aluminium phthalocyanines. These materials can be deposited upon the substrate during the washing process. Upon irradiation with light, in the presence of oxygen, such as by hanging clothes out to dry in the daylight, the sulfonated zinc phthalocyanine is activated and, consequently, the substrate is bleached. Preferred zinc phthalocyanine and a photoactivated bleaching process are described in US 4,033,718. Typically, detergent composition will contain about 0.025% to about 1.25%, by weight, of sulfonated zinc phthalocyanine.
Bleaching agents may also comprise a manganese catalyst. The manganese catalyst may, e.g., be one of the compounds described in "Efficient manganese catalysts for low-temperature bleaching", Nature 369, 1994, pp. 637-639.
Suds suppressors
Another optional ingredient is a suds suppressor, exemplified by silicones, and silica-silicone mixtures. Silicones can generally be represented by alkylated polysiloxane materials, while silica is normally used in finely divided forms exemplified by silica aerogels and xerogels and hydrophobic silicas of various types. Theses materials can be incorporated as particulates, in which the suds suppressor is advantageously releasably incorporated in a water-soluble or waterdispersible, substantially non surface-active detergent impermeable carrier. Alternatively the suds suppressor can be dissolved or dispersed in a liquid carrier and applied by spraying on to one or more of the other components. A preferred silicone suds controlling agent is disclosed in US 3,933,672. Other particularly useful suds suppressors are the self-emulsifying silicone suds suppressors, described in German Patent Application DTOS 2,646,126. An example of such a compound is DC-544, commercially available form Dow Corning, which is a siloxane-glycol copolymer. Especially preferred suds controlling agent are the suds suppressor system comprising a mixture of silicone oils and 2-alkyl-alkanols. Suitable 2-alkyl- alkanols are 2-butyl-octanol which are commercially available under the trade name Isofol 12 R. Such suds suppressor system are described in European Patent Application EP 0 593 841.
Especially preferred silicone suds controlling agents are described in European Patent Application No. 92201649.8. Said compositions can comprise a silicone/ silica mixture in combination with fumed nonporous silica such as AerosilR.
The suds suppressors described above are normally employed at levels of from 0.001% to 2% by weight of the composition, preferably from 0.01% to 1% by weight.
Other components
Other components conventionally used in cleaning or detergent compositions may be employed such as soil-suspending agents, soil-releasing agents, optical brighteners, abrasives, bactericides, tarnish inhibitors, coloring agents, and/or encapsulated or nonencapsulated perfumes.
Especially suitable encapsulating materials are water soluble capsules which consist of a matrix of polysaccharide and polyhydroxy compounds such as described in GB 1,464,616.
Other suitable water soluble encapsulating materials comprise dextrins derived from ungelatinized starch acid esters of substituted dicarboxylic acids such as described in US 3,455,838. These acid-ester dextrins are, preferably, prepared from such starches as waxy maize, waxy sorghum, sago, tapioca and potato. Suitable examples of said encapsulation materials include N-Lok manufactured by National Starch. The N-Lok encapsulating material consists of a modified maize starch and glucose. The starch is modified by adding monofunctional substituted groups such as octenyl succinic acid anhydride. Antiredeposition and soil suspension agents suitable herein include cellulose derivatives such as methylcellulose, carboxymethylcellulose and hydroxyethylcellulose, and homo- or co-polymeric polycarboxylic acids or their salts. Polymers of this type include the polyacrylates and maleic anhydride-acrylic acid copolymers previously mentioned as builders, as well as copolymers of maleic anhydride with ethylene, methylvinyl ether or methacrylic acid, the maleic anhydride constituting at least 20 mole percent of the copolymer. These materials are normally used at levels of from 0.5% to 10% by weight, more preferably form 0.75% to 8%, most preferably from 1% to 6% by weight of the composition.
Preferred optical brighteners are anionic in character, examples of which are disodium 4 , 4 ' -bis-(2-diethanolamino-4- anilino -s- triazin-6-ylamino) stilbene-2: 2 • disulphonate, disodium 4, - 4 '-bis- (2-morpholino-4-anilino-s-triazin-6- ylamino-stilbene-2:2 ' - disulphonate, disodium 4,4' - bis- (2,4- dianilino-s-triazin-6-ylamino) stilbene-2:2 * - disulphonate, monosodium 4 ',4'' - bis- (2, 4-dianilino-s-tri-azin-6 ylamino) stilbene-2-sulphonate, disodium 4,4' -bis-(2-anilino-4- (N-methyl-N-2-hydroxyethylamino) -s-triazin-6-ylamino) stilbene- 2,2' - disulphonate, di-sodium 4,4' -bis- (4-phenyl-2 , 1, 3- triazol-2-yl) -stilbene-2 ,2 ' disulphonate, di-so-dium 4, 4* bis (2- anilino-4-(l-methyl-2-hydroxyethylamino) -s-triazin-6-ylami- no) stilbene-2, 2 'disulphonate, sodium 2 (stilbyl-4 ' ' -(naphtho- 1' ,2 ' :4,5) -1,2,3, - triazole-2 ' ' -sulphonate and 4,4 '-bis (2- sulphostyry1) bipheny1.
Other useful polymeric materials are the polyethylene glycols, particularly those of molecular weight 1000-10000, more particularly 2000 to 8000 and most preferably about 4000. These are used at levels of from 0.20% to 5% more preferably from 0.25% to 2.5% by weight. These polymers and the previously mentioned homo- or co-polymeric poly-carboxylate salts are valuable for improving whiteness maintenance, fabric ash deposition, and cleaning performance on clay, proteinaceous and oxidizable soils in the presence of transition metal impurities. Soil release agents useful in compositions of the present invention are conventionally copolymers or terpolymers of terephthalic acid with ethylene glycol and/or propylene glycol units in various arrangements. Examples of such polymers are disclosed in US 4,116,885 and 4,711,730 and EP 0 272 033. A particular preferred polymer in accordance with EP 0 272 033 has the formula:
(CH3 (PEG) 43) 0.75 (POH) 0.25 [T-PO) 2.8(T- PEG)o.4]T(POH) o.25 ( (PEG) 43CH3) o.75
where PEG is -(OC2H4)0-, PO is (OC3H60) and T is (pOOC6H4CO) . Also very useful are modified polyesters as random copolymers of dimethyl terephthalate, dimethyl sulfoisophthalate, ethylene glycol and 1, 2-propanediol, the end groups consisting primarily of sulphobenzoate and secondarily of mono esters of ethylene glycol and/or 1, 2-propanediol. The target is to obtain a polymer capped at both end by sulphobenzoate groups, "primarily", in the present context most of said copolymers herein will be endcapped by sulphobenzoate groups. However, some copolymers will be less than fully capped, 5 and therefore their end groups may consist of monoester of ethylene glycol and/or 1, 2-propanediol, thereof consist "secondarily" of such species.
The selected polyesters herein contain about 46% by weight of dimethyl terephthalic acid, about 16% by weight of 1,2- 10 propanediol, about 10% by weight ethylene glycol, about 13% by weight of dimethyl sulfobenzoic acid and about 15% by weight of sulfoisophthalic acid, and have a molecular weight of about 3.000. The polyesters and their method of preparation are described in detail in EP 311 342.
15
Softening agents
Fabric softening agents can also be incorporated into cleaning compositions in accordance with the present invention. These agents may be inorganic or organic in type. Inorganic
20 softening agents are exemplified by the smectite clays disclosed in GB-A-1 400898 and in US 5,019,292. Organic fabric softening agents include the water insoluble tertiary amines as disclosed in GB-A1 514 276 and EP 0 011 340 and their combination with mono Ci2~Ci4 quaternary ammonium salts are disclosed in EP-B-0
25 026 528 and di-long-chain amides as disclosed in EP 0 242 919. Other useful organic ingredients of fabric softening systems include high molecular weight polyethylene oxide materials as disclosed in EP 0 299 575 and 0 313 146.
Levels of smectite clay are normally in the range from 5%
30 to 15%, more preferably from 8% to 12% by weight, with the material being added as a dry mixed component to the remainder of the formulation. Organic fabric softening agents such as the water-insoluble tertiary amines or dilong chain amide materials are incorporated at levels of from 0.5% to 5% by weight,
35 normally from 1% to 3% by weight whilst the high molecular weight polyethylene oxide materials and the water soluble cationic materials are added at levels of from 0.1% to 2%, normally from 0.15% to 1.5% by weight. These materials are normally added to the spray dried portion of the composition, although in some instances it may be more convenient to add them as a dry mixed particulate, or spray them as molten liquid on to other solid components of the composition.
Polymeric dye-transfer inhibiting agents
The cleaning, especially laundry detergent, compositions according to the present invention may also comprise from 0.001% to 10%, preferably from 0.01% to 2%, more preferably form 0.05% to 1% by weight of polymeric dye- transfer inhibiting agents. Said polymeric dye-transfer inhibiting agents are normally incorporated into detergent compositions in order to inhibit the transfer of dyes from colored fabrics onto fabrics washed therewith. These polymers have the ability of complexing or adsorbing the fugitive dyes washed out of dyed fabrics before the dyes have the opportunity to become attached to other articles in the wash.
Especially suitable polymeric dye-transfer inhibiting agents are polyamine N-oxide polymers, copolymers of N-vinyl- pyrrolidone and N-vinylimidazole, polyvinylpyrrolidone polymers, polyvinyloxazolidones and polyvinylimidazoles or mixtures thereof.
Addition of such polymers also enhances the performance of the enzymes according the invention.
The cleaning composition according to the invention can be in liquid, paste, gels, bars or granular forms.
Non-dusting granulates may be produced, e.g., as disclosed in US 4,106,991 and 4,661,452 (both to Novo Industri A/S) and may optionally be coated by methods known in the art. Examples of waxy coating materials are poly(ethylene oxide) products (polyethyleneglycol, PEG) with mean molecular weights of 1000 to 20000; ethoxylated nonylphenols having from 16 to 50 ethylene oxide units; ethoxylated fatty alcohols in which the alcohol contains from 12 to 20 carbon atoms and in which there are 15 to 80 ethylene oxide units; fatty alcohols; fatty acids; and mono- and di- and triglycerides of fatty acids. Examples of film- forming coating materials suitable for application by fluid bed techniques are given in GB 1483591.
Granular compositions according to the present invention can also be in "compact form", i.e. they may have a relatively higher density than conventional granular detergents or cleaning compositions, i.e. form 550 to 950 g/1; in such case, the granular detergent compositions according to the present invention will contain a lower amount of "Inorganic filler 5 salt", compared to conventional granular detergents; typical filler salts are alkaline earth metal salts of sulphates and chlorides, typically sodium sulphate; "Compact" detergent typically comprise not more than 10% filler salt. The liquid compositions according to the present invention can also be in
10 "concentrated form", in such case, the liquid detergent compositions according to the present invention will contain a lower amount of water, compared to conventional liquid detergents. Typically, the water content of the concentrated liquid detergent is less than 30%, more preferably less than
15 20%, most preferably less than 10% by weight of the detergent compositions.
In another preferred embodiment, the cleaning composition is a granular detergent composition containing no more than 40%, preferably no more than 15%, by weight of inorganic filler salt.
20 The compositions of the invention may for example, be formulated as hand and machine laundry detergent compositions including laundry additive compositions and compositions suitable for use in the pretreatment of stained fabrics, rinse added fabric softener compositions, and compositions for use in
25 general household hard surface cleaning operations and dishwashing operations.
The following examples are meant to exemplify compositions for the present invention, but are not necessarily meant to limit or otherwise define the scope of the invention.
30 In the detergent compositions, the abbreviated component identifications have the following meanings:
LAS: Sodium linear C12 alkyl benzene sulphonate TAS: Sodium tallow alkyl sulphate 35 XYAS: Sodium Clx - Clγ alkyl sulfate
SS: Secondary soap surfactant of formula 2-butyl octanoic acid
25EY: A C12 - C15 predominantly linear primary alcohol condensed with an average of Y moles of ethylene oxide 45EY: A C14 - C15 predominantly linear primary alcohol condensed with an average of Y moles of ethylene oxide
XYEZS: Clx - Ciy sodium alkyl sulfate condensed with an average of Z moles of ethylene oxide per mole Nonionic: Cχ3 - C15 mixed ethoxylated/propoxylated fatty alcohol with an average degree of ethoxylation of 3.8 and an average degree of propoxylation of 4.5 sold under the tradename
Plurafax LF404 by BASF Gmbh
CFAA: C12 _ C_4 alkyl N-methyl glucamide TFAA: C16 - C18 alkyl N-methyl glucamide
Silicate: Amorphous Sodium Silicate (Si02 Na2θ ratio = 2.0)
NaSKS-6: Crystalline layered silicate of formula d-Na2Si20s
Carbonate: Anhydrous sodium carbonate
Phosphate: Sodium tripolyphosphate MA/AA: Copolymer of 1:4 maleic/acrylic acid, average molecular weight about 80,000
Polyacrylate: Polyacrylate homopolymer with an average molecular weight of 8,000 sold under the tradename PA30 by BASF
Gmbh Zeolite A: Hydrated Sodium Aluminosilicate of formula
Nai2 (Alθ2Si02) i2« 27H2O having a primary particle size in the range from 1 to 10 micrometers
Citrate: Tri-sodium citrate dihydrate
Citric: Citric Acid Perborate: Anhydrous sodium perborate monohydrate bleach, empirical formula NaB02.H2θ2
PB4 : Anhydrous sodium perborate tetrahydrate
Percarbonate: Anhydrous sodium percarbonate bleach of empirical formula 2Na2C03.3H202 TAED: Tetraacetyl ethylene diamine
CMC: Sodium carboxymethyl cellulose
DETPMP: Diethylene triamine penta (methylene phosphonic acid) , marketed by Monsanto under the Tradename Dequest 2060
PVP: Polyvinylpyrrolidone polymer EDDS: Ethylenediamine-N, N' -disuccinic acid, [S,S] isomer in the form of the sodium salt
Suds Suppressor: 25% paraffin wax Mpt 50°C, 17% hydrophobic silica, 58% paraffin oil Granular Suds suppressor: 12% Silicone/silica, 18% stearyl alcohol, 70% starch in granular form Sulphate: Anhydrous sodium sulphate HMWPEO: High molecular weight polyethylene oxide TAE 25: Tallow alcohol ethoxylate (25)
Detergent Example I
A granular fabric cleaning composition in accordance with the invention may be prepared as follows:
Sodium linear C12 alkyl 6.5 benzene sulfonate
Sodium sulfate 15.0
Zeolite A 26.0
Sodium nitrilotriacetate 5.0
Enzyme of the invention 0.1
PVP 0.5
TAED 3.0
Boric acid 4.0
Perborate 18.0
Phenol sulphonate 0.1
Minors Up to 100
Detergent Example II
A compact granular fabric cleaning composition (density 800 g/1) in accord with the invention may be prepared as follows:
45AS 8.0
25E3S 2.0 25E5 3.0
25E3 3.0
TFAA 2.5
Zeolite A 17.0
NaSKS-6 12.0 Citric acid 3.0
Carbonate 7.0
MA/AA 5.0
CMC 0.4 Enzyme of the invention 0. 1 TAED 6 . 0
Percarbonate 22 . 0 EDDS 0 . 3 Granular suds suppressor 3 . 5 water/minors Up to 100%
Detergent Example III Granular fabric cleaning compositions in accordance with the invention which are especially useful in the laundering of coloured fabrics were prepared as follows:
LAS 10.7 —
TAS 2.4 -
TFAA - 4.0
45AS 3.1 10.0
45E7 4.0 -
25E3S - 3.0
68E11 1.8 -
25E5 - 8.0
Citrate 15.0 7.0
Carbonate - 10
Citric acid 2.5 3.0
Zeolite A 32.1 25.0
Na-SKS-6 - 9.0
MA/AA 5.0 5.0
DETPMP 0.2 0.8
Enzyme of the invention 0.10 0.05
Silicate 2.5 -
Sulphate 5.2 3.0
PVP 0.5 -
Poly (4-vinylpyridine) -N- - 0.2
Oxide/copolymer of vinyl- imidazole and vinyl- pyrrolidone
Perborate 1.0 -
Phenol sulfonate 0.2 -
Water/Minors Up to 100% Detergent Example IV
Granular fabric cleaning compositions in accordance with the invention which provide "Softening through the wash" capability may be prepared as follows: 45AS - 10.0
LAS 7.6
68AS 1.3
45E7 4.0
25E3 — 5.0
10 Coco-alkyl-dimethyl hydroxy1.4 1.0 ethyl ammoniurcι chloride
Citrate 5.0 3.0
Na-SKS-6 - 11.0
Zeolite A 15.0 15.0
15 MA/AA 4.0 4.0
DETPMP 0.4 0.4
Perborate 15.0 -
Percarbonate - 15.0
TAED 5.0 5.0
20 Smectite clay 10.0 10.0
HMWPEO - 0.1
Enzyme of the invention 0.10 0.05
Silicate 3.0 5.0
Carbonate 10.0 10.0
25 Granular suds suppressor 1.0 4.0
CMC 0.2 0.1
Water/Minors Up to 100%
Detergent Example V
30 Heavy duty liquid fabric cleaning compositions in accordance with the invention may be prepared as follows:
I II
LAS acid form - 25.0
Citric acid 5.0 2.0
35 25AS acid form 8.0
25AE2S acid form 3.0
25AE7 8.0
CFAA 5 DETPMP 1.0 1.0
Fatty acid 8 -
Oleic acid - 1.0
Ethanol 4.0 6.0
5 Propanediol 2.0 6.0
Enzyme of the invention 0.10 0.05
Coco-alkyl dimethyl - 3.0 hydroxy ethyl ammonium chloride o Smectite clay - 5.0
PVP 2.0 -
Water / Minors Up to 100%
Cellulolytic Activity 5 The cellulolytic activity may be measured in endo-cellulase units (ECU), determined at pH 7.5, with carboxymethyl cellulose (CMC) as substrate.
The ECU assay quantifies the amount of catalytic activity present in the sample by measuring the ability of the sample to 0 reduce the viscosity of a solution of carboxy-methylcellulose (CMC). The assay is carried out at 40°C; pH 7.5; 0.1M phosphate buffer; time 30 min; using a relative enzyme standard for reducing the viscosity of the CMC Hercules 7 LFD substrate; enzyme concentration approx. 0.15 ECU/ l. The arch standard is defined 5 to 8200 ECU/g.
EXAMPLE 1
A. Wet storage test for cellulases
The following example is intended to describe the inven- 0 tion that different inverting endoglucanases may differ significantly in respect to their ability to cause fabric weakening upon wet storage.
To illustrate that major differences can be observed between inverting endoglucanases from different cellulase families 5 the following experiment can be made:
A new bleached wowen cotton (app. 350 g/m2) swatch (25cmx25cm) is incubated at elevated dosage (100 kECU/1) for 7 days in Tris buffer pH 7 at 25°C and after this prolonged incubation the fabric is rinsed in MilliQ-water (25°C) for 10 min- utes, line-dried and equilibrated in a constant climate room (60%RH, 20°C) for 48 hours. Finally the loss in tensile strength is measured on an Instron.
The relative tensile strength loss (%TSL) is quantified 5 versus "enzyme blank", i.e. an experiment where the fabric is incubated in buffer without any enzyme present and the cellulase is then classified into one of the following 4 groups:
Class A (%TSL is in the range of [0%-25%])
10 Class B (%TSL is in the range of [25%-50%])
Class C (%TSL is in the range of [50%-75%])
Class D (%TSL is in the range of [75%-100%])
In the following example two inverting endoglucanases were 15 tested: a. "43 kD EGV from the fungal species Humicola inεolenε , DSM 1800, belonging to family 45 of glycosyl hydrolases and described in detail in WO 91/17243. b. EGVI from the fungal species Humicola inεolenε , DSM 20 1800, belonging to the cellulase family 6 and having the amino acid sequence listed in SEQ ID NO: 4. The DNA sequence encoding for this enzyme is listed in SEQ ID NO: 3 (the coding region corresponding to positions 16-1356) .
25 The following results were obtained from the evaluation: Enzyme Tensile strength class
EG V C
EG VI A
It is thus found that the cellulase belonging to family 6 is much less prone to cause tensile strength loss upon prolonged wet storage.
30 B. Colour Clarification in Terg-O-Meter
In this example the capability of family 6 endoglucanases to rejuvenate the colour of cotton textile is demonstrated using an assay for determining colour care benefits, i.e. "Color Clarification", of cotton cloth in a miniaturised washing a- 35 chine, the 100 ml Terg-O-Meter. 250 ml beakers with 100 ml buffer (or detergent) eas positioned in a Terg-O-Meter and equilibrated to 35°C. Then two 7x7 cm swatches of black, woven cotton cloth was added to each beaker, the stirrers were put in motion, and finally enzyme was added: A) A blank, B) Three different dosages of a standard
(e.g. the commercial available enzyme preparation Celluzyme™) , and C) Two different dosages of the family 6 endoglucanase. Incubation then proceeded for 30 minutes at 35 °C
After the 30 minutes of incubation the swatches were rinsed in cold tap water for 10 minutes and dried in a tumble dryer. The cycle of incubation and rinsing/drying was repeated once - or until the swatches clearly differed in respect to colour and/or fuzz in the swatches surface.
Finally the swatches were graded against the blank (no en- zyme) and the standard (e.g. Celluzyme) swatches. Visual grading was performed by a panel of trained graders, and colour was measured with a remission spectrometer. Results are expressed in the table below as "Colour Clarification" (CC) of the swatches obtained per activity unit of enzyme.
EXAMPLE 2
"Colour Clarification" in Household Laundering The capability of a family 6 endoglucanase to rejuvenate the colour of cotton textile was demonstrated using an assay for determining "Colour Clarification" of cotton cloth in a normal household washing machine.
Swatches of 7x7 cm swatches of black, woven cotton cloth were stapled to one common piece of cloth, and 7x7 cm swatches of blue knitted cotton cloth was stapled to another piece of cloth. This together with a standardised household load of laundry cloth was entered into a household washing machine.
Such loads were laundered in pH 7 buffer, and at the relevant step in the washing cycle enzyme was added: A) A blank, B) Three different dosages of a standard (e.g. the commercially available cellulase preparation Celluzyme™) , and C) Two different dosages of the family 6 endoglucanase.
After laundering the loads were dried in a tumble dryer, and the cycle of incubation and rinsing/drying were repeated for a total of 14 times.
Finally the swatches were graded against the blank (no enzyme) and the standard (e.g. Celluzyme™) swatches. Visual grading was performed by a panel of trained graders, and colour was measured with a remission spectrometer. Results are expressed in the table below as "Colour Clarification" (CC) of the swatches obtained per activity unit of enzyme.
EXAMPLE 3
Cloning of Humicola insolenε Cel6A and EG VI (CelβB)
Cel6A and B cDNA clones were identified in a Humicola inεolenε cDNA expression library (disclosed in WO 91/17244 (Cel6A) and W093/11249(Cel6B) ) . The expression plasmids for cel6A and B (pCA6H and pC6H) were constructed by PCR addition of adequate restrictions sites (BamHI-Xbal) to the individual CDS's, and introduction into Xbal- BamHI cut pCaHj418 vector. The resulting DNA sequences from BamHI- Xbal are given in Figures 2 and 3, respectively (the translational initiation codon is underlined in each sequence) . Cel6B (& cel6A) variants with the exeption of larger deletions/inserts (>9bp) were constructed by application of the Chameleon™ Double-stranded, site-directed Mutagenesis kit, from Stratagene. The following synthetic oligo-nucleotide were used as selection primer:
S/M GAATGACTTGGTTGACGCGTCACCAGTCAC, or M/S GAATGACTTGGTTGAGTACTCACCAGTCAC .
S/M replaces the Seal site in the beta-lactamase gene of the plasmid with a Mlul site and M/S does the reverse. The later is used to introduce secondary mutations in variants generated by the first selection primer. CA6H4 and 5 were made by SOE PCR utilizing the following primers: CA6H4-F: 5' GGTGAGTGCGACGGCTGCGGTCTGGAGGCTGGCCAGTTT
AATGAATATTTCATTCAGTTGCTGCG CA6H4-R: 5' CGCAGCAACTGAATGAAATATTCATTAAACTGGCCAGCCTC CAGACCGCAGCCGTCGCACTCACC
CA6H5-F: 5' GGTGAGTGCGACGGCTGCATCGCCGGCGCTGGCCAGTTTA
ATGAATATTTCATTCAGTTGCTGCG CA6H5-R: 5' CGCAGCAACTGAATGAAATATTCATTAAACTGGCCAGCGCC GGCGATGCAGCCGTCGCACTCACC TAKA-F: 5' CGACAACATCACATCAAGCTCTCC
TAKA-R: 5' CCCCATCCTTTAACTATAGCGAAATGG
With pCA6H as template (10 ng/100 ml) , Pwo (Boehringer) based PCR reactions were performed, under standard conditions, as recommended by the manufactor, with the following primer pairs:
1: TAKA-F/CA6H4-R 2: TAKA-R/CA6H4-F
3: TAKA-F/CA6H5-R 4: TAKA-R/CA6H5-F
96°C, 2' - 4X( 94 °C,30''- 50°C, 30''- 72°C, 45'') - 25x( 94 °C,30''- 57°C, 30"- 72°C, 45'') -72°C, 7'- 4°C, hold
The resulting products, 1&3 1398 bp, 2&4 153 bp were purified via agarose gel electrophoresis and applied in two new PCR's with templates as listed about 0.1 pmol/100 ml each: 5: PCRlprod.-l- PCR2prod 6: PCR3prod.+ PCR4prod and TAKA-F/R as primers: 96°C, 2' - 4x( 94 °C, 30''-72°C, 30' •- 72°C, 45' •) - 20x( 94 °C, 30''-57°C, 30''- 72°C, 45'') -72°C, 7'- 4°C, hold.
The resulting products of 1477 bp were purified via agaro- se gel elctrophoresis, subjected to BamHl-Xbal restriction nu- clease digestions and the resulting 1365 bp bands isolated as above and cloned into pCaHj418 Xbal - BamHI vector.
EXAMPLE 4
Trimming of binding cleft loops to increase activity
In order to alter Humicola inεolenε Cel6A to a Humicola endoglucanase type in order to create an enzyme having improved performance in colour clarification, mutations which reduce the length of one or more of the binding cleft encompassing loops was performed. The extent of the binding cleft encompassing loops can be determined either from the multiple sequence alignment or by solving the three dimensional X-ray structure of Humicola inεolenε Cel6A and perform the same analysis as described for Humicola inεolenε EGIV (Cel6B) .
From the sequence alignment in fig. 1A/B the binding cleft loop regions of Humicola inεolenε Cel6A can be found as shown in Fig. 6.
The same analysis could be performed by solving the X-ray structure of Humicola insolens Cel6A catalytic core domain and performing the same analysis as described for the X-ray structure of Humicola insolenε EG VI (Cel6B) catalytic core domain. In this case the result is a little different as shown in Fig. 7. The four longer loops encompassing the binding cleft (residues Y86-N107, N219-D242, L272-P287 or W308-F331 using Humicola inεolenε Cel6B numbering) are in the numbering scheme of Humicola inεolenε Cel6A V173-N195, N307-D330, K360-G376 and W397-F435 (using Humicola inεolenε Cel6A numbering) when the multiple sequence alignment method is used and it is Y174-N195, N307-D330, K360-Y391 and W397-F435 F435 (using Humicola inεolenε Cel6A numbering) when the X-ray structure method is used. Constructions of loop trimming:
In one example (A) the loop W397-F435 (using Humicola inεolenε Cel6A numbering) which is equivalent to the W308-F331 in Humicola inεolenε Cel6B is mutagenized altering the sequence from
WVKPGGECDGTSDTTAARYDYHCGLEDALKPAPEAGOWF to WVKPGGECDGCGLEAGQF
(the underlined residues have been deleted) thereby making the binding cleft more accessible and generating color care activity for the variant.
In another example (B) the same loop is shortened as in (A) and three extra mutations is introduced to alter the loop geometry (G420I+L421A+E422G in Humicola inεolenε Cel6A numbering) :
WVKPGGECDGTSDTTAARYDYHCGLEDALKPAPEAGOWF to WVKPGGECDGCIAGAGQF
(A) and (B) were made by SOE PCR as described in example 3.
In a similar manner, the cel6A-type cellulases from the species Fusarium oxysporum, Trichoderma reeεei, Agaricuε biε- pora, Acremonium cellulyticuε , Phanerochaete chryεoεporium, Penicillium purpurogenum which are aligned in fig. 1A/B can be altered to a Humicola endoglucanase type enzyme (Cel6B-type) .
EXAMPLE 5
Resistance to anionic surfactants in detergent. As described it is possible to stabilize an enzyme against denaturation by anionic tensides by mutation/deletion of surface exposed residue (s) towards more negatively charged residue (s) i.e. removal of positively charged residue(s) and/or the introduction of negatively charged residue (s) . Resistance to anionic surfactants in detergent (A)
Variants of the present invention may show improved performance with respect to an altered sensitivity towards anionic surfactants (tensides) . Anionic tensides are products frequently incorporated into detergent compositions. Unfolding of cellulases tested so far, is accompanied by a decay in the intrinsic fluorescence of the proteins. The intrinsic fluorescence derives from Trp side chains (and to a smaller extent Tyr side chains) and is sensitive to the hydrophobicity of the side chain environment. Unfolding leads to a more hydrophilic environment as the side-chains become more exposed to solvent, and this quenches fluorescence.
Fluorescence is followed on a Perkin/Elmer™ LS50 luminescence spectrometer. In practice, the greatest change in fluore- scence on unfolding is obtained by excitation at 280 nm and emission at 340 nm. Slit widths (which regulate the magnitude of the signal) are usually 5 nm for both emission and excitation at a protein concentration of 5 μg/ml. Fluorescence is measured in 2-ml quartz cuvettes thermostatted with a circulating water bath and stirred with a small magnet. The magnet-stirrer is built into the spectrometer.
Unfolding can be followed in real time using the available software. Rapid unfolding (going to completion within less than 5-10 minutes) is monitored in the TimeDrive option, in which the fluorescence is measured every few (2-5) seconds. For slower unfolding, four cuvettes can be measured at a time in the cuvette-holder using the Wavelength Program option, in which the fluorescence of each cuvette is measured every 30 seconds. In all cases, unfolding is initiated by adding a small volume (typically 50 μl) of concentrated enzyme solution to the thermostatted cuvette solution where mixing is complete within a few seconds due to the rapid rotation of the magnet.
Data are measured in the software program GraphPad Prism. Unfolding fits in all cases to a single-exponential function from which a single half-time of unfolding (or unfolding rate constant) can be obtained. Typical unfolding conditions are 50 mM HEPES pH 7, 0-500 ppm LAS/250 ppm LAS, 25°C. In both cases, the protein concentration is 5-10 μg/ml (the protein concentration is not crucial, as LAS is in excess) .
Enzyme t%relative
Humicola insolens Ceϊέϊ. Ϊ00%
Humicola insolens Cel6B/K20E 170%
Humicola insolens Cel6B/K103E 156%
Humicola insolens Cel6B/Q318E 436%
From this table it is seen that mutation of residues resulting in the removal of positively charged residue (s) and/or the introduction of negatively charged residue (s) increase the resistance towards LAS. Resistance to anionic surfactants in detergent (B)
The alteration of the surface electrostatics of an enzyme will influence the sensibility towards anionic tensides such as LAS (linear alkylbenzenesulfonate) . Especially variants where positive charged residues have been removed and/or negatively charged residues have been introduced will increase the resistance towards LAS, whereas the opposite, i.e. the introduction of positively charged residues and/or the removal of negatively charged residues will lower the resistance towards LAS. The residues Arg (R) , Lys (K) and His (H) are viewed as positively or potentially positively charged residue and the residues Asp (D) , Glu (E) and Cys (C) if not included in a disulphide bridge are viewed as negatively or potentially negatively charged residues. Positions already containing one of these residues are the primary target for mutagenesis, secondary targets are positions which has one of these residues on an equivalent position in another cellulase, and third target are any surface exposed re- sidue. In this experiment wild type Humicola inεolenε Cel6B cellulase are being compared to Humicola inεolenε Cel6B cellulase variants belonging to all three of the above groups, comparing the stability towards LAS in detergent.
Cellulase resistance to anionic surfactants was measured as activity on PASC (phosphoric acid swollen cellulose) in the presence of anionic surfactant vs. activity on PASC in the absence of anionic surfactant.
The reaction medium contained 5.0 g/1 of a commercial regular powder detergent from the detergent manufacturer NOPA Den- mark. The detergent was formulated without surfactants for this experiment and pH adjusted to pH 7.0. Further the reaction medium included 0.5 g/1 PASC and was with or without 1 g/1 LAS (linear alkylbenzenesulphonate) , which is an anionic surfactant, and the reaction proceeded at the temperature 30°C for 30 minu- tes. Cellulase was dosed at 0.20 S-CEVU/1. After the 30 minutes of incubation the reaction was stopped with 2 N NaOH and the amount of reducing sugar ends determined through reduction of p- hydroxybenzoic acid hydrazide. The decrease in absorption of re- duced p-hydroxybenzoic acid hydrazide relates to the cellulase activity.
The type of mutation and the resistance towards LAS for variants with increased LAS resistance is summarized in the fol- lowing table:
Variant Relative LAS resistance
[%] Humicola insolens CeΪ6B ΪOO
Humicola insolens Cel6B/S56D 122
Humicola insolens Cel6B/K103E 123
Humicola insolens Cel6B/Q138E 113
From this table it is seen that mutation of residues resulting in the removal of positively charged residue (s) and/or the introduction of negatively charged residue (s) increase the resistance towards LAS.
EXAMPLE 6
Improving stability towards anionic surfactants of any Humicola- like family 6 cellulase In order to stabilize any Humicola-like family 6 cellulase towards anionic surfactants, residues on the surface of the molecule should be mutated towards a more negatively charged surface as described in the text resulting in the removal of positively charged residue (s) and/or introduction of negatively charged residue (s) . The residues on the surface of the molecule can be detected from the multiple sequence alignment in the following way: Residues at a position in the sequence equivalent to residues on the surface of the Humicola inεolenε Cel6A X-ray structure are thought to most likely be on the surface of a gi- ven family 6 cellulase. In the case of an insertion the inserted residue (s) are considered as being on the surface of the molecule if one of the flanking residues of the insertion is considered as being on the surface.
To achieve improved performance of the enzyme in color clarification a linker and a CBD have to bee attached to the catalytic core domain. In the cases where the wild type enzyme does not include the linker region and/or the CBD these segments can be included from another enzyme e.g. Humicola inεolenε Cel6B by standard techniques to achive a hybrid enzyme with the desired improved properties.
(A) Neocallimaεtix patriciarum Taking the Neocallimastix patriciarum SPTREMBL entry ql2646 as an example figure 8 shows the residues considered as being on the surface of the Neocallimastix patriciarum catalytic core domain.
Preferably potentially positively charged residues should be mutagenized to neutral or negatively charged residues. In the case of Neocallimaεtix patriciarum this results to (using the numbering scheme of Humicola inεolenε Cel6B) : K4 , K16, R27, K43, K45, K67, K72, R91, K113, R122, R125, K131, R156, H159, K160, H183, K195, K201, K212, R214, K249, H262, R293, R295, K310, R318e, R323C, H332, R340, R343.
More preferably the positions which hold an Arg: R27, R91, R122, R125, R156, R214, R293, R295, R318e, R323c, R340 or R343.
Or preferably positions which in other Humi col a-like family 6 cellulases have been shown to improve stability towards anionic tensides.
(B) Orpinomγceε εp . CelA
Taking the Orpinomyceε εp . CelA SPTREMBL entry p78720 (residues 128-459) as an example figure 9 shows the residues considered as being on the surface of the Orpinomyceε εp . CelA catalytic core domain.
Preferably potentially positively charged residues should be mutagenized to neutral or negatively charged residues. In the case of Orpinomyceε εp . CelA this results to (using the numbering scheme of Humicola inεolenε Cel6B) : K16, K26, K27, K38, K40, K43, K45, K72, Kill, K113, K128, K131, R153, R156, H159, K160, K169, H174, K176, H183, K201, K212, R214, K245, H247, R252, K257, R260, K262, R269, K286, R293, K295, K310, R318e, R321 or H332.
More preferably the positions which hold an Arg: R153, R156, R214, R252, R260, R269, R293, R318e or R321.
Or preferably positions which in other Humicola-like family 6 cellulases have been shown to improve stability towards anionic tensides (surfactants) . (C) Orpinomyceε εp. CelC
Taking the Orpinomyceε εp . CelC SPTREMBL entry p78721 (residues 127-449) as an example figure 10 shows the residues considered as being on the surface of the Orpinomyceε εp. CelA catalytic core domain.
Preferably potentially positively charged residues should be mutagenized to neutral or negatively charged residues. In the case of Orpinomyceε εp. CelC this results to (using the numbering scheme of Humicola inεolenε Cel6B) : K16, R27, K42, K43, R64, K72, R91, R131, H156, H159, K160, K169, K173, R176, H183, R195, R205, K212, R214, H247, R252, R257, R260, K262, R272, K286, R293, K310, R320 or H332.
More preferably the positions which hold an Arg: R27, R64, R91, R131, R176, R195, R205, R214, R252, R257, R260, R272, R293 or R320.
Or preferably positions which in other Humicola-like family 6 cellulases have been shown to improve stability towards anionic tensides (surfactants) .
EXAMPLE 7
Alteration of pH activity profile
The pH activity profile of a cellulase is governed by the pH dependent behavior of specific titratable groups, typically the acidic residues in the active site. The pH profile can be altered by changing the electrostatic environment of these residues, either by substitution of residues involving charged or potentially charged groups such as Arg (R) , Lys (K) , Tyr (Y) , His (H) , Glu (E) , Asp (D) or Cys (C) if not involved in a disulphide bridge or by changes in the surface accessibility of these specific titratable groups by mutation of these specific residues on the surface of the enzyme close to the proton donor as described above or by mutation of residues in the vicinity of the binding cleft as described herein, preferably by mutation (s) in the binding cleft within 5h, more preferably 2.5A, of the substrate, or preferably by mutations within lθA, more preferably δA, from the active site (D139) .
In this example Humicola inεolenε Cel6B cellulase and variants of Humicola inεolenε Cel6B cellulase involving substi- tution of charged or potentially charged residues have been tested for activity towards PASC at pH 7 and pH 10, respectively.
In order to determine the pH optimum for cellulases we have selected organic buffers because it is common known that e.g. borate forms covalent complexes with mono- and oligo-saccharides and phosphate can precipitate with Ca-ions. In DATA FOR BIOCHEMICAL RESEARCH Third Edition OXFORD SCIENCE PUBLICATIONS page 223 to 241, suitable organic buffers has been found. In respect of their pKa values we decided to use Na-acetate in the range 4 - 5.5, MES at 6.0, MOPS in the range 6.5 - 7.5, Na- barbiturate 8.0 - 8.5 and glycine in the range 9.0 - 10.5. Method:
The method is enzymatic degradation of carboxy-methylcellulose, at different pH's. Buffers are prepared in the range 4.0 to 10.5 with intervals of 0.5 pH unit. The analyze is based on formation of new reducing ends in carboxy-methyl-cellulose, these are visualized by reaction with PHBAH in strong alkaline environment, were they forms a yellow compound with absorption maximum at 410 nm. Experimental Protocol:
Buffer preparation: 0.2 mol of each buffer substance is weighed out and dissolved in 1 liter of Milli Q water. 250 ml 0.2M buffer solution and 200 ml Milli Q water is mixed. The pH are measured using Radiometer PHM92 labmeter calibrated using standard buffer solutions from Radiometer. The pH of the buffers are adjusted to actual pH using 4M NaOH or 4M HCl and adjusted to total 500 ml with water. When adjusting Na-barbiturate to pH 8.0 there might be some precipitation, this can be re-dissolved by heating to 50°C. Acetic acid 100% 0.2 mol = 12.01 g. MES 0.2 mol = 39.04 g. MOPS 0.2 mol = 41.86 g. Na-barbiturate 0.2 mol = 41.24 g. Glycine 0.2mol = 15.01 g. Buffers: as disclosed in WO 98/12307, page 89.
The actual pH is measured in a series treated as the main values, but without stop reagent, pH is measured after 20 min. incubation at 40 °C. Substrate Preparation:
2.0 g CMC , in 250 ml conic glass flask with a magnet rod, is moistened with 2.5 ml. 96% ethanol, 100 ml. Milli Q water is added and then boiled to transparency on a heating magnetic stirrer. Approximately 2 min. boiling. Cooled to room temperature on magnetic stirrer. Stop Reagent:
1.5 g PHBAH and 5 g K-Na-tartrate dissolved in 2% NaOH. Procedure: There are made 3 main values and 2 blank value using 5 ml glass test tubes. (1 main value for pH determination )
Mixing on a Heidolph REAX 2000 mixer with permanent mix and maximum speed (9) . No stirring during incubation on water bath with temperature control. Immediately after adding PHBAH-reagent and mixing the samples are boiled 10 min. Cooled in cold tap water for 5 min. Absorbance read at 410 nm.
Determination of Activity The absorbance at 410 nm from the 2 Main values are added and divided by 2 and the 2 Blank values are added and divided by
2, the 2 mean values are subtracted. The percentages are calculated by using the highest value as 100%.
The measured pH is plotted against the relative activity. Buffer reagents as disclosed in W098/12307, page 90. Cellulase resistance to anionic surfactants was measured as activity on PASC (phosphoric acid swollen cellulose) at neutral pH (pH 7.0) vs. activity on PASC at alkaline pH (pH 10.0). The reaction medium contained 5.0 g/1 of a commercial regular powder detergent from the detergent manufacturer NOPA Denmark. The pH was adjusted to pH 7.0 and pH 10.0, respectively. Further the reaction medium included 0.5 g/1 PASC, and the reaction proceeded at the temperature 30°C for 30 minutes. Cellulase was dosed at 0.20 S-CEVU/1. After the 30 minutes of incubation the re- action was stopped with 2 N NaOH and the amount of reducing sugar ends determined through reduction of p-hydroxybenzoic acid hydrazide. The decrease in absorption of reduced p- hydroxybenzoic acid hydrazide relates to the cellulase activity. The results are presented below, the activity at pH 10 re- lative to pH 7 is compared to that of wild type Humicola inεolenε Cel6B cellulase.
Variant PASC activity pH10/pH7 relative to wild type
[%] Humicola insolens Ϊ00
Humicola insolens/N183H 400
Humicola insolens/A182G,N183H 250
Humicola insolens/A182G 140
From the above table it is seen that the relative alkaline activity can be increased by creating variants involving potentially charged residues which are mutated towards a more negatively charged residue and/or by altering residues not more than δA from the residues in the binding cleft.
EXAMPLE 8
Variants with improved catalytic properties
The following site directed variants of Humicola inεolenε Cel6B (EG VI) endoglucanase were prepared as described above: K20E, K103Q, K103E, S94D, A95G. The specific activity on CMC of the variants and the wild- type H . inεolenε endoglucanase were measured in the ECU (endo- cellulase unit) assay (cf. above under "Cellulolytic Activity") with the following results:
Wild-type 100%
K20E 109%
K103Q 120%
K103E 115%
S94D 180%
A95G 116% All the tested variants have improved specific activity.
LITERATURE
Da ude, H.G., V. Ferro, S.G. Withers, and R.A.J. Warren. 1996. Substrate specificity of endoglucanase A from Cellulomonas fimi: 5 fundamental differences between endoglucanases and exoglucanases from family 6. Biochem. J., 315:467-472.
Denman, S., G-P. Xue, and B. Patel. 1996. Characterization of a Neocallimastix patriciarum cellulase cDNA (celA) homologous to 10 Trichoderma reesei cellobiohydrolase II. Appl. Environ. Micro- biol., 62 (6) :1889-1896.
Henrissat, B. 1991. A classification of glycosyl hydrolases based on amino acid sequence similaritites. Biochem. J. , 15 280:309-316.
Henrissat, B., and A. Bairoch. 1993. New families in the classification of glycosyl hydrolases based on amino acid sequence similaritites. Biochem. J. , 293:781-788. 20
McCarter, J.D., and S.G. Withers. 1994. Mechanisms of enzymatic glycoside hydrolysis. Current Opinion in Structural Biology, 4:885-892.
25 Irwin, D.C., Spezio, M. , and Wilson, D.B. Activity studies of 8 purified cellulases - specificity, synergism, and binding domain effects. Biotechnology and Bioengineering. 42:1002-1013, 1993.
Shen, H. , Meinke, A., Tomme, P. Damude, E. K. , Kilburn, D. G., 30 Miller, R. C. Warren, R. A. J. and Gilkes, N. R. Cellulomonas fimi Cellobiohydrolases. In Enzymatic Degradation of insoluble Carbohydrates, ed. J. N. Sadler and M. H. Penner ACS Symposium sreies 618, Washington 1995. Chapter 12, p. 174-196.
35 Sambrook et al. (1989) Molecular cloning: A laboratory manual, Cold Spring Harbor lab., Cold Spring Harbor, NY.
Schulein, M. , Tikhomirov, D. F. and Schou, C. Humicola insolens Alkaline Cellulases. In Proceedings of the second TRICEL sympo- sium on Trichoderma reesei cellulases and other hydrolases, Espoo 1993. Ed. by P. Souminen and T. Reinikainen. Foundation for Biotechnical and Industrial Fermentation Research 8, 1993, p. 109-116.
APPENDIX 1
The structural coordinated of the three-dimensional structure of the Humicola inεolenε Cel6B catalytic core domain.
The structural coordinates of the Humicola inεolenε Cel6B catalytic core domain as determined by X-ray crystallography. The format of the coordinates is the conventional Brookhaven Protein Data Bank (PDB) format:
ATOM 1 N GLY A 3 -1.219 43.542 30.269 1.00 38.26 N
ATOM 2 CA GLY A 3 -2.014 43.426 29.045 1.00 37.85 c
ATOM 3 c GLY A 3 -1.696 42.106 28.320 1.00 30.25 c
ATOM 4 O GLY A 3 -0.625 41.520 28.474 1.00 29.98 O
ATOM 5 N ASN A 4 -2.694 41.653 27.583 1.00 26.24 N
ATOM 6 CA ASN A 4 -2.522 40.422 26.779 1.00 20.56 C
ATOM 7 C ASN A 4 -1.763 40.898 25.563 1.00 18.81 C
ATOM 8 O ASN A 4 -2.111 41.817 24.819 1.00 18.03 O
ATOM 9 CB ASN A 4 -3.894 39.853 26.486 1.00 25.75 C
ATOM 10 CG ASN A 4 -3.998 38.898 25.313 1.00 25.58 C
ATOM 11 ODl ASN A 4 -2.969 38.503 24.764 1.00 18.12 o
ATOM 12 ND2 ASN A 4 -5.222 38.545 24.933 1.00 25.83 N
ATOM 13 N PRO A 5 -0.620 40.287 25.287 1.00 18.82 N
ATOM 14 CA PRO A 5 0.217 40.707 24.170 1.00 21.77 c
ATOM 15 C PRO A 5 -0.379 40.490 22.795 1.00 19.14 c
ATOM 16 O PRO A 5 0.116 41.014 21.786 1.00 20.12 0
ATOM 17 CB PRO A 5 1.551 39.962 24.330 1.00 22.32 c
ATOM 18 CG PRO A 5 1.247 38.911 25.348 1.00 27.04 c
ATOM 19 CD PRO A 5 -0.027 39.231 26.096 1.00 23.52 c
ATOM 20 N PHE A 6 -1.420 39.660 22.675 1.00 20.14 N
ATOM 21 CA PHE A 6 -2.025 39.349 21.392 1.00 18.69 c
ATOM 22 c PHE A 6 -3.168 40.333 21.066 1.00 21.14 c
ATOM 23 O PHE A 6 -3.659 40.333 19.958 1.00 19.59 O
ATOM 24 CB PHE A 6 -2.571 37.924 21.376 1.00 17.61 c
ATOM 25 CG PHE A 6 -1.492 36.869 21.367 1.00 12.55 c
ATOM 26 CD1 PHE A 6 -0.937 36.390 22.554 1.00 17.74 c
ATOM 27 CD2 PHE A 6 -1.033 36.378 20.163 1.00 19.19 c
ATOM 28 CE1 PHE A 6 0.045 35.415 22.547 1.00 19.08 c
ATOM 29 CE2 PHE A 6 -0.017 35.442 20.127 1.00 13.64 c
ATOM 30 cz PHE A 6 0.496 34.966 21.322 1.00 17.40 c
ATOM 31 N SER A 7 -3.625 41.041 22.085 1.00 24.32 N
ATOM 32 CA SER A 7 -4.696 42.029 21.934 1.00 25.88 c
ATOM 33 c SER A 7 -4.451 42.995 20.789 1.00 20.85 c
ATOM 34 O SER A 7 -3.459 43.730 20.688 1.00 24.54 0
ATOM 35 CB SER A 7 -4.820 42.841 23.237 1.00 26.78 c
ATOM 36 OG SER A 7 -6.172 43.198 23.483 1.00 41.47 O
ATOM 37 N GLY A 8 -5.371 42.997 19.824 1.00 26.40 N
ATOM 38 CA GLY A 8 -5.340 43.814 18.652 1.00 24.54 c
ATOM 39 c GLY A 8 -4.269 43.464 17.635 1.00 26.47 C
ATOM 40 O GLY A 8 -4.064 44.173 16.658 1.00 27.08 0
ATOM 41 N ARG A 9 -3.612 42.315 17.808 1.00 21.06 N
ATOM 42 CA ARG A 9 -2.572 41.872 16.890 1.00 22.18 c
ATOM 43 c ARG A 9 -3.019 40.660 16.083 1.00 18.93 c
ATOM 44 O ARG A 9 -4.011 40.028 16.400 1.00 19.47 O
ATOM 45 CB ARG A 9 -1.284 41.600 17.687 1.00 23.74 c ATOM 46 CG ARG A 9 -0.655 42.881 18.192 1.00 23.86 c
ATOM 47 CD ARG A 9 0.697 42.725 18.882 1.00 27.92 c
ATOM 48 NE ARG A 9 1.213 44.064 19.199 1.00 27.01 N
ATOM 49 cz ARG A 9 1.488 44.533 20.404 1.00 37.53 c
ATOM 50 NH1 ARG A 9 1.321 43.763 21.468 1.00 36.85 N
ATOM 51 NH2 ARG A 9 1.946 45.781 20.503 1.00 32.23 N
ATOM 52 N THR A 10 -2.288 40.327 15.027 1.00 24.28 N
ATOM 53 CA THR A 10 -2.564 39.132 14.227 1.00 19.42 c
ATOM 54 c THR A 10 -1.354 38.193 14.346 1.00 24.81 c
ATOM 55 O THR A 10 -0.251 38.690 14.163 1.00 20.25 O
ATOM 56 CB THR A 10 -2.737 39.467 12.744 1.00 26.72 c
ATOM 57 OG1 THR A 10 -1.768 40.459 12.367 1.00 25.66 O
ATOM 58 CG2 THR A 10 -4.140 40.042 12.529 1.00 28.94 c
ATOM 59 N LEU A 11 -1.572 36.927 14.675 1.00 19.06 N
ATOM 60 CA LEU A 11 -0.435 35.982 14.697 1.00 19.38 c
ATOM 61 c LEU A 11 0.111 35.848 13.287 1.00 14.73 c
ATOM 62 O LEU A 11 -0.555 35.657 12.279 1.00 15.07 O
ATOM 63 CB LEU A 11 -0.920 34.622 15.217 1.00 16.36 c
ATOM 64 CG LEU A 11 0.196 33.575 15.358 1.00 17.32 c
ATOM 65 CD1 LEU A 11 1.351 33.982 16.269 1.00 18.77 c
ATOM 66 CD2 LEU A 11 -0.436 32.245 15.788 1.00 16.40 c
ATOM 67 N LEU A 12 1.444 36.024 13.141 1.00 16.75 N
ATOM 68 CA LEU A 12 2.060 36.058 11.830 1.00 13.59 c
ATOM 69 c LEU A 12 2.020 34.739 11.061 1.00 18.27 c
ATOM 70 O LEU A 12 2.255 33.691 11.661 1.00 16.05 O
ATOM 71 CB LEU A 12 3.505 36.577 11.950 1.00 14.84 c
ATOM 72 CG LEU A 12 4.283 36.764 10.640 1.00 19.82 c
ATOM 73 CD1 LEU A 12 3.878 38.020 9.888 1.00 16.23 c
ATOM 74 CD2 LEU A 12 5.779 36.782 10.927 1.00 21.50 c
ATOM 75 N VAL A 13 1.740 34.836 9.760 1.00 18.01 N
ATOM 76 CA VAL A 13 1.775 33.596 8.958 1.00 15.29 c
ATOM 77 c VAL A 13 3.197 33.038 8.957 1.00 17.10 c
ATOM 78 O VAL A 13 4.189 33.771 8.935 1.00 20.59 O
ATOM 79 CB VAL A 13 1.307 33.883 7.521 1.00 16.36 c
ATOM 80 CGI VAL A 13 1.842 32.878 6.516 1.00 25.91 c
ATOM 81 CG2 VAL A 13 -0.229 33.978 7.423 1.00 20.83 c
ATOM 82 N ASN A 14 3.330 31.716 8.968 1.00 15.04 N
ATOM 83 CA ASN A 14 4.621 31.037 8.860 1.00 17.17 c
ATOM 84 c ASN A 14 4.809 30.806 7.358 1.00 19.93 c
ATOM 85 O ASN A 14 4.099 30.022 6.721 1.00 15.61 O
ATOM 86 CB ASN A 14 4.611 29.761 9.683 1.00 14.05 c
ATOM 87 CG ASN A 14 5.850 28.897 9.544 1.00 15.07 c
ATOM 88 ODl ASN A 14 6.505 28.972 8.533 1.00 18.33 O
ATOM 89 ND2 ASN A 14 6.119 28.082 10.587 1.00 19.81 N
ATOM 90 N SER A 15 5.772 31.480 6.722 1.00 16.93 N
ATOM 91 CA SER A 15 5.972 31.375 5.291 1.00 19.54 c
ATOM 92 c SER A 15 6.450 30.003 4.841 1.00 19.95 c
ATOM 93 O SER A 15 6.081 29.590 3.731 1.00 19.84 O
ATOM 94 CB SER A 15 6.925 32.465 4.794 1.00 23.25 c
ATOM 95 OG SER A 15 8.109 32.414 5.573 1.00 23.52 O
ATOM 96 N ASP A 16 7.229 29.316 5.679 1.00 20.02 N
ATOM 97 CA ASP A 16 7.678 27.986 5.233 1.00 18.50 c
ATOM 98 c ASP A 16 6.490 27.032 5.160 1.00 19.89 v.
ATOM 99 O ASP A 16 6.297 26.266 4.196 1.00 20.29 O
ATOM 100 CB ASP A 16 8.749 27.479 6.183 1.00 21.86 c
ATOM 101 CG ASP A 16 9.262 26.115 5.708 1.00 36.14 c
ATOM 102 ODl ASP A 16 9.486 25.883 4.491 1.00 38.17 O
ATOM 103 OD2 ASP A 16 9.383 25.267 6.609 1.00 36.83 O
ATOM 104 N TYR A 17 5.686 27.053 6.241 1.00 18.14 N ATOM 105 CA TYR A 17 4.487 26.234 6.264 1.00 16.72 C
ATOM 106 C TYR A 17 3.546 26.568 5.133 1.00 15.19 C
ATOM 107 O TYR A 17 2.949 25.740 4.432 1.00 16.05 O
ATOM 108 CB TYR A 17 3.789 26.452 7.608 1.00 17.07 C
ATOM 109 CG TYR A 17 2.526 25.697 7.890 1.00 13.43 C
ATOM 110 CD1 TYR A 17 2.341 24.363 7.550 1.00 13.11 C
ATOM 111 CD2 TYR A 17 1.474 26.357 8.535 1.00 16.87 C
ATOM 112 CE1 TYR A 17 1.155 23.717 7.871 1.00 13.74 C
ATOM 113 CE2 TYR A 17 0.283 25.717 8.850 1.00 16.10 C
ATOM 114 CZ TYR A 17 0.148 24.400 8.508 1.00 13.11 C
ATOM 115 OH TYR A 17 1.005 23.712 8.810 1.00 14.15 O
ATOM 116 N SER A 18 3.263 27.851 4.904 1.00 15.39 N
ATOM 117 CA SER A 18 2.428 28.267 3.776 1.00 18.04 C
ATOM 118 C SER A 18 2.941 27.767 2.434 1.00 17.83 C
ATOM 119 O SER A 18 2.158 27.327 1.586 1.00 19.59 O
ATOM 120 CB SER A 18 2.354 29.805 3.817 1.00 21.27 C
ATOM 121 OG ; &.SER A 18 1.253 30.217 4.608 0.50 27.39 O
ATOM 122 OG ] BSER A 18 1.514 30.236 2.772 0.50 17.06 O
ATOM 123 N SER A 19 4.260 27.733 2.243 1.00 17.26 N
ATOM 124 CA SER A 19 4.815 27.191 1.004 1.00 17.67 C
ATOM 125 C SER A 19 4.528 25.702 0.844 1.00 17.75 C
ATOM 126 O SER A 19 4.127 25.224 -0.225 1.00 18.25 o
ATOM 127 CB SER A 19 6.327 27.476 0.932 1.00 20.98 C
ATOM 128 OG ; A.SER A 19 6.550 28.864 0.860 0.60 16.86 o
ATOM 129 OG 1 BSER A 19 6.775 27.266 -0.395 0.40 20.68 o
ATOM 130 N LYS A 20 4.695 24.963 1.949 1.00 17.13 N
ATOM 131 CA LYS A 20 4.459 23.529 1.922 1.00 13.44 C
ATOM 132 C LYS A 20 2.999 23.195 1.626 1.00 17.29 C
ATOM 133 O LYS A 20 2.697 22.239 0.907 1.00 16.89 O
ATOM 134 CB LYS A 20 4.869 22.910 3.261 1.00 17.94 C
ATOM 135 CG LYS A 20 6.366 23.122 3.543 1.00 24.75 C
ATOM 136 CD LYS A 20 6.660 22.371 4.825 1.00 22.80 C
ATOM 137 CE LYS A 20 7.852 22.839 5.589 1.00 28.68 C
ATOM 138 NZ LYS A 20 8.141 21.933 6.735 1.00 22.43 N
ATOM 139 N LEU A 21 2.077 24.008 2.094 1.00 17.11 N
ATOM 140 CA LEU A 21 0.653 23.842 1.855 1.00 13.52 C
ATOM 141 C LEU A 21 0.270 24.012 0.389 1.00 17.88 C
ATOM 142 O LEU A 21 •0.817 23.570 0.016 1.00 16.70 O
ATOM 143 CB LEU A 21 ■0.161 24.861 2.673 1.00 15.72 C
ATOM 144 CG LEU A 21 •0.303 24.401 4.117 1.00 17.14 C
ATOM 145 CD1 LEU A 21 •0.813 25.536 5.018 1.00 19.64 C
ATOM 146 CD2 LEU A 21 •1.222 23.189 4.269 1.00 16.96 C
ATOM 147 N ASP A 22 1.128 24.695 -0.366 1.00 18.31 N
ATOM 148 CA ASP A 22 0.822 24.788 -1.808 1.00 17.60 C
ATOM 149 C ASP A 22 0.638 23.406 -2.411 1.00 20.83 C
ATOM 150 O ASP A 22 ■0.254 23.185 -3.245 1.00 20.39 o
ATOM 151 CB ASP A 22 1.881 25.579 -2.571 1.00 17.76 C
ATOM 152 CG ASP A 22 1.220 26.464 -3.611 1.00 28.60 c
ATOM 153 ODl ASP A 22 0.380 27.281 -3.181 1.00 23.59 O
ATOM 154 OD2 ASP A 22 1.538 26.321 -4.821 1.00 24.61 o
ATOM 155 N GLN A 23 1.421 22.406 -1.967 1.00 18.04 N
ATOM 156 CA GLN A 23 1.235 21.045 -2.460 1.00 19.08 C
ATOM 157 C GLN A 23 •0.185 20.580 -2.188 1.00 21.56 c
ATOM 158 O GLN A 23 ■0.830 19.948 -3.036 1.00 22.98 O
ATOM 159 CB GLN A 23 2.218 20.086 -1.768 1.00 19.16 c
ATOM 160 CG GLN A 23 2.036 18.643 -2.223 1.00 25.29 C
ATOM 161 CD GLN A 23 3.155 17.731 -1.760 1.00 30.48 C
ATOM 162 OE1 GLN A 23 3.144 16.538 -2.090 1.00 28.64 o
ATOM 163 NE2 GLN A 23 4.122 18.234 -1.013 1.00 17.97 N ATOM 164 N THR A 24 0.712 20.919 -0.992 1.00 17.27 N
ATOM 165 CA THR A 24 2.063 20.490 -0.634 1.00 17.10 C
ATOM 166 C THR A 24 3.098 21.160 -1.512 1.00 20.53 C
ATOM 167 O THR A 24 4.054 20.548 -1.974 1.00 20.84 O
ATOM 168 CB THR A 24 2.364 20.775 0.866 1.00 12.75 C
ATOM 169 OG1 THR A 24 1.188 20.411 1.618 1.00 18.44 O
ATOM 170 CG2 THR A 24 3.525 19.954 1.375 1.00 16.82 C
ATOM 171 N ARG A 25 2.957 22.462 -1.681 1.00 21.00 N
ATOM 172 CA ARG A 25 3.821 23.238 -2.549 1.00 17.91 C
ATOM 173 C ARG A 25 3.739 22.679 -3.965 1.00 19.93 C
ATOM 174 O ARG A 25 4.831 22.459 -4.486 1.00 24.01 O
ATOM 175 CB ARG A 25 3.388 24.704 -2.613 1.00 21.80 C
ATOM 176 CG ARG A 25 4.578 25.612 -2.940 1.00 27.75 C
ATOM 177 CD ARG A 25 3.977 27.048 -3.098 1.00 31.43 C
ATOM 178 NE ARG A 25 3.193 26.903 -4.331 1.00 36.58 N
ATOM 179 CZ ARG A 25 3.849 26.988 -5.499 1.00 38.46 c
ATOM 180 NH1 ARG A 25 5.138 27.272 -5.631 1.00 41.76 N
ATOM 181 NH2 ARG A 25 3.095 26.750 -6.543 1.00 22.34 N
ATOM 182 N GLN A 26 2.539 22.412 -4.480 1.00 18.69 N
ATOM 183 CA GLN A 26 2.482 21.757 -5.798 1.00 22.07 C
ATOM 184 C GLN A 26 3.191 20.412 -5.836 1.00 26.43 C
ATOM 185 O GLN A 26 3.894 20.096 -6.817 1.00 24.10 O
ATOM 186 CB GLN A 26 0.997 21.539 -6.162 1.00 22.74 C
ATOM 187 CG GLN A 26 0.280 22.867 -6.444 1.00 21.81 C
ATOM 188 CD GLN A 26 1.223 22.710 -6.460 1.00 26.15 C
ATOM 189 OE1 GLN A 26 2.014 23.650 -6.360 1.00 29.54 O
ATOM 190 NE2 GLN A 26 1.731 21.487 -6.570 1.00 28.77 N
ATOM 191 N ALA A 27 3.069 19.553 -4.823 1.00 22.76 N
ATOM 192 CA ALA A 27 3.702 18.238 -4.801 1.00 22.86 C
ATOM 193 C ALA A 27 5.214 18.331 -4.878 1.00 26.56 C
ATOM 194 O ALA A 27 5.876 17.654 -5.683 1.00 29.72 O
ATOM 195 CB ALA A 27 3.266 17.435 -3.575 1.00 21.10 C
ATOM 196 N PHE A 28 5.822 19.221 -4.098 1.00 24.85 N
ATOM 197 CA PHE A 28 7.262 19.417 -4.131 1.00 23.17 C
ATOM 198 C PHE A 28 7.673 19.939 -5.510 1.00 24.62 C
ATOM 199 O PHE A 28 8.581 19.365 -6.109 1.00 31.47 O
ATOM 200 CB PHE A 28 7.720 20.401 -3.055 1.00 17.75 C
ATOM 201 CG PHE A 28 7.884 19.772 -1.700 1.00 20.87 C
ATOM 202 CD1 PHE A 28 8.654 18.639 -1.493 1.00 18.88 C
ATOM 203 CD2 PHE A 28 7.183 20.333 -0.634 1.00 17.62 C
ATOM 204 CE1 PHE A 28 8.766 18.080 -0.228 1.00 23.06 C
ATOM 205 CE2 PHE A 28 7.315 19.775 0.637 1.00 17.25 C
ATOM 206 CZ PHE A 28 8.091 18.678 0.843 1.00 19.95 C
ATOM 207 N LEU A 29 6.970 20.945 -6.032 1.00 23.80 N
ATOM 208 CA LEU A 29 7.312 21.458 -7.359 1.00 32.14 C
ATOM 209 C LEU A 29 7.335 20.339 -8.402 1.00 35.33 C
ATOM 210 O LEU A 29 8.298 20.213 -9.177 1.00 35.15 O
ATOM 211 CB LEU A 29 ■6.325 22.512 -7.803 1.00 29.77 c
ATOM 212 CG LEU A 29 6.540 23.986 -7.615 1.00 35.01 C
ATOM 213 CD1 LEU A 29 ■5.522 24.766 -8.416 1.00 34.32 C
ATOM 214 CD2 LEU A 29 •7.957 24.417 -7.890 1.00 39.08 C
ATOM 215 N SER A 30 ■6.344 19.464 -8.396 1.00 34.71 N
ATOM 216 CA SER A 30 ■6.204 18.354 -9.322 1.00 37.80 C
ATOM 217 C SER A 30 ■7.277 17.288 -9.316 1.00 38.86 C
ATOM 218 O SER A 30 ■7.306 16.359 -10.139 1.00 38.27 O
ATOM 219 CB SER A 30 ■4.825 17.723 -9.056 1.00 38.75 C
ATOM 220 OG ASER A 30 -3.831 18.716 -9.316 0.50 38.25 O
ATOM 221 OG BSER A 30 -4.948 16.650 -8.135 0.50 44.07 O
ATOM 222 N ARG A 31 -8.204 17.328 -8.380 1.00 35.46 N ATOM 223 CA ARG A 31 -9.349 16.448 -8.287 1.00 32.92 C
ATOM 224 C ARG A 31 -10.619 17.277 -8.477 1.00 34.41 C
ATOM 225 O ARG A 31 -11.715 16.814 -8.172 1.00 36.73 O
ATOM 226 CB ARG A 31 -9.378 15.675 -6.979 1.00 37.41 C
ATOM 227 CG ARG A 31 -8.085 14.880 -6.791 1.00 30.23 C
ATOM 228 CD ARG A 31 -8.224 13.944 -5.620 1.00 38.62 C
ATOM 229 NE ARG A 31 -8.688 14.611 -4.394 1.00 36.87 N
ATOM 230 CZ ARG A 31 -7.839 14.794 -3.375 1.00 38.36 C
ATOM 231 NH1 ARG A 31 -6.572 14.397 -3.497 1.00 24.37 N
ATOM 232 NH2 ARG A 31 -8.280 15.378 -2.275 1.00 39.97 N
ATOM 233 N GLY A 32 -10.453 18.524 -8.901 1.00 30.79 N
ATOM 234 CA GLY A 32 -11.568 19.435 -9.124 1.00 32.88 C
ATOM 235 C GLY A 32 -12.219 19.961 -7.851 1.00 34.01 C
ATOM 236 O GLY A 32 -13.269 20.611 -7.881 1.00 29.91 O
ATOM 237 N ASP A 33 -11.555 19.733 -6.717 1.00 28.54 N
ATOM 238 CA ASP A 33 -12.087 20.173 -5.436 1.00 21.21 C
ATOM 239 C ASP A 33 -11.644 21.598 -5.118 1.00 28.79 C
ATOM 240 O ASP A 33 -10.639 21.863 -4.449 1.00 27.97 O
ATOM 241 CB ASP A 33 -11.705 19.175 -4.360 1.00 21.50 C
ATOM 242 CG ASP A 33 -12.294 19.460 -3.007 1.00 20.79 C
ATOM 243 ODl ASP A 33 -13.016 20.472 -2.838 1.00 23.24 o
ATOM 244 OD2 ASP A 33 -12.052 18.642 -2.085 1.00 23.15 O
ATOM 245 N GLN A 34 -12.472 22.543 -5.591 1.00 25.22 N
ATOM 246 CA GLN A 34 -12.204 23.959 -5.402 1.00 22.75 C
ATOM 247 C GLN A 34 -12.474 24.393 -3.962 1.00 22.82 C
ATOM 248 O GLN A 34 -11.800 25.313 -3.483 1.00 26.92 O
ATOM 249 CB GLN A 34 -13.126 24.830 -6.265 1.00 31.62 C
ATOM 250 CG GLN A 34 -12.464 25.374 -7.505 1.00 39.47 C
ATOM 251 CD GLN A 34 -11.961 24.251 -8.392 1.00 45.04 C
ATOM 252 OE1 GLN A 34 -10.834 24.245 -8.874 1.00 50.64 O
ATOM 253 NE2 GLN A 34 -12.826 23.258 -8.600 1.00 52.85 N
ATOM 254 N THR A 35 -13.484 23.784 -3.368 1.00 20.80 N
ATOM 255 CA THR A 35 -13.900 24.112 -2.012 1.00 21.60 C
ATOM 256 C THR A 35 -12.757 23.884 -1.026 1.00 18.34 C
ATOM 257 O THR A 35 -12.439 24.766 -0.221 1.00 20.03 O
ATOM 258 CB THR A 35 -15.137 23.325 -1.574 1.00 27.01 C
ATOM 259 OG1 THR A 35 -16.266 23.811 -2.338 1.00 28.82 O
ATOM 260 CG2 THR A 35 -15.442 23.548 -0.100 1.00 27.13 C
ATOM 261 N ASN A 36 -12.139 22.715 -1.098 1.00 20.66 N
ATOM 262 CA ASN A 36 -10.988 22.500 -0.189 1.00 15.84 C
ATOM 263 C ASN A 36 -9.741 23.202 -0.662 1.00 21.68 C
ATOM 264 O ASN A 36 -8.901 23.559 0.199 1.00 20.93 O
ATOM 265 CB ASN A 36 -10.797 21.004 0.050 1.00 20.04 C
ATOM 266 CG ASN A 36 -11.785 20.400 0.999 1.00 21.52 C
ATOM 267 ODl ASN A 36 -11.967 20.808 2.153 1.00 20.71 O
ATOM 268 ND2 ASN A 36 -12.466 19.303 0.606 1.00 21.89 N
ATOM 269 N ALA A 37 -9.535 23.468 -1.947 1.00 19.31 N
ATOM 270 CA ALA A 37 -8.366 24.216 -2.399 1.00 16.22 C
ATOM 271 C ALA A 37 -8.414 25.628 -1.806 1.00 22.25 C
ATOM 272 O ALA A 37 -7.410 26.175 -1.365 1.00 20.26 O
ATOM 273 CB ALA A 37 -8.347 24.311 -3.926 1.00 22.22 C
ATOM 274 N ALA A 38 -9.617 26.185 -1.751 1.00 19.54 N
ATOM 275 CA ALA A 38 -9.855 27.521 -1.216 1.00 16.76
ATOM 276 C ALA A 38 -9.602 27.541 0.295 1.00 21.41 C
ATOM 277 O ALA A 38 -9.085 28.533 0.810 1.00 20.71 O
ATOM 278 CB ALA A 38 -11.300 27.921 -1.500 1.00 18.76 C
ATOM 279 N LYS A 39 -9.984 26.451 0.954 1.00 18.20 N
ATOM 280 CA LYS A 39 -9.697 26.347 2.402 1.00 16.71 C
ATOM 281 C LYS A 39 -8.176 26.312 2.607 1.00 18.03 C ATOM 282 O LYS A 39 -7.736 26.952 3.590 1.00 16.49 O
ATOM 283 CB LYS A 39 10.373 25.055 2.871 1.00 15.79 C
ATOM 284 CG LYS A 39 11.841 25.247 3.160 1.00 15.84 C
ATOM 285 CD LYS A 39 12.685 23.997 3.177 1.00 24.79 C
ATOM 286 CE LYS A 39 12.603 23.222 4.473 1.00 23.47 C
ATOM 287 NZ LYS A 39 13.371 21.928 4.356 1.00 25.57 N
ATOM 288 N VAL A 40 -7.425 25.584 1.796 1.00 18.40 N
ATOM 289 CA VAL A 40 -5.964 25.612 1.920 1.00 16.71 C
ATOM 290 C VAL A 40 -5.436 27.032 1.739 1.00 18.50 C
ATOM 291 O VAL A 40 -4.613 27.534 2.522 1.00 17.77 O
ATOM 292 CB VAL A 40 -5.271 24.618 0.962 1.00 13.77 C
ATOM 293 CGI VAL A 40 -3.753 24.733 1.145 1.00 18.12 C
ATOM 294 CG2 VAL A 40 -5.711 23.177 1.245 1.00 17.94 C
ATOM 295 N LYS A 41 -5.896 27.745 0.679 1.00 18.92 N
ATOM 296 CA LYS A 41 -5.418 29.127 0.476 1.00 22.78 C
ATOM 297 C LYS A 41 -5.760 30.039 1.647 1.00 21.74 C
ATOM 298 O LYS A 41 -4.993 30.940 1.994 1.00 18.77 O
ATOM 299 CB LYS A 41 -5.956 29.684 -0.855 1.00 23.98 C
ATOM 300 CG LYS A 41 -5.119 30.858 -1.369 1.00 21.98 C
ATOM 301 CD LYS A 41 -5.158 30.897 -2.897 1.00 32.46 C
ATOM 302 CE LYS A 41 -5.617 32.247 -3.405 1.00 40.42 C
ATOM 303 NZ LYS A 41 -4.582 33.307 -3.303 1.00 45.05 N
ATOM 304 N TYR A 42 -6.859 29.813 2.333 1.00 17.12 N
ATOM 305 CA TYR A 42 -7.288 30.552 3.516 1.00 17.44 C
ATOM 306 C TYR A 42 -6.200 30.342 4.583 1.00 17.60 C
ATOM 307 O TYR A 42 -5.664 31.327 5.062 1.00 18.30 O
ATOM 308 CB TYR A 42 -8.641 30.140 4.083 1.00 18.45 C
ATOM 309 CG TYR A 42 -9.121 30.848 5.331 1.00 19.03 C
ATOM 310 CD1 TYR A 42 -8.662 30.530 6.587 1.00 17.73 C
ATOM 311 CD2 TYR A 42 ■10.071 31.867 5.243 1.00 21.04 C
ATOM 312 CE1 TYR A 42 -9.098 31.175 7.732 1.00 18.75 C
ATOM 313 CE2 TYR A 42 •10.531 32.515 6.385 1.00 28.47 C
ATOM 314 CZ TYR A 42 ■10.044 32.170 7.623 1.00 28.03 C
ATOM 315 OH TYR A 42 ■10.504 32.830 8.743 1.00 25.85 O
ATOM 316 N VAL A 43 -5.877 29.067 4.811 1.00 16.45 N
ATOM 317 CA VAL A 43 -4.792 28.828 5.785 1.00 13.47 C
ATOM 318 C VAL A 43 -3.503 29.471 5.327 1.00 18.93 C
ATOM 319 O VAL A 43 -2.730 30.002 6.145 1.00 17.25 O
ATOM 320 CB VAL A 43 -4.610 27.311 6.026 1.00 17.47 C
ATOM 321 CGI VAL A 43 -3.458 27.002 6.989 1.00 15.90 C
ATOM 322 CG2 VAL A 43 -5.918 26.733 6.532 1.00 14.49 C
ATOM 323 N GLN A 44 -3.153 29.403 4.028 1.00 14.80 N
ATOM 324 CA GLN A 44 -1.897 29.944 3.546 1.00 16.17 C
ATOM 325 C GLN A 44 -1.682 31.442 3.770 1.00 15.63 C
ATOM 326 O GLN A 44 -0.556 31.878 4.029 1.00 16.96 O
ATOM 327 CB GLN A 44 -1.734 29.716 2.015 1.00 16.42 C
ATOM 328 CG GLN A 44 -1.411 28.265 1.679 1.00 19.44 C
ATOM 329 CD GLN A 44 -1.289 28.090 0.171 1.00 23.66 C
ATOM 330 OE1 GLN A 44 -2.276 28.257 -0.536 1.00 20.63 O
ATOM 331 NE2 GLN A 44 -0.100 27.763 -0.334 1.00 21.61 N
ATOM 332 N GLU A 45 -2.761 32.201 3.656 1.00 17.72 N
ATOM 333 CA GLU A 45 -2.657 33.649 3.741 1.00 20.01 C
ATOM 334 C GLU A 45 -3.167 34.238 5.026 1.00 18.93 c
ATOM 335 O GLU A 45 -2.740 35.356 5.356 1.00 23.99 O
ATOM 336 CB GLU A 45 -3.494 34.245 2.606 1.00 18.32 C
ATOM 337 CG GLU A 45 -3.188 33.674 1.244 1.00 23.77 C
ATOM 338 CD GLU A 45 -3.500 34.633 0.120 1.00 33.30 C
ATOM 339 OE1 GLU A 45 -4.472 35.405 0.247 1.00 45.19 O
ATOM 340 OE2 GLU A 45 -2.787 34.615 -0.904 1.00 35.39 o ATOM 341 N LYS A 46 -4.104 33.593 5.696 1.00 18.31 N
ATOM 342 CA LYS A 46 -4.722 34.224 6.846 1.00 18.40 C
ATOM 343 C LYS A 46 -4.564 33.547 8.178 1.00 23.82 C
ATOM 344 O LYS A 46 -5.174 34.044 9.143 1.00 24.60 O
ATOM 345 CB LYS A 46 -6.240 34.381 6.571 1.00 18.01 C
ATOM 346 CG LYS A 46 -6.516 35.375 5.452 1.00 23.69 C
ATOM 347 CD LYS A 46 -7.584 34.839 4.507 1.00 30.76 C
ATOM 348 CE LYS A 46 -7.954 35.887 3.473 1.00 45.46 c
ATOM 349 NZ LYS A 46 -6.969 36.044 2.357 1.00 43.16 N
ATOM 350 N VAL A 47 -3.852 32.412 8.262 1.00 17.29 N
ATOM 351 CA VAL A 47 -3.835 31.749 9.578 1.00 15.28 c
ATOM 352 C VAL A 47 -2.404 31.717 10.121 1.00 13.52 c
ATOM 353 O VAL A 47 -1.586 31.140 9.413 1.00 16.31 O
ATOM 354 CB VAL A 47 -4.379 30.325 9.435 1.00 14.62 c
ATOM 355 CGI VAL A 47 -4.238 29.497 10.692 1.00 13.84 c
ATOM 356 CG2 VAL A 47 -5.895 30.343 9.099 1.00 17.49 c
ATOM 357 N GLY A 48 -2.167 32.430 11.230 1.00 15.51 N
ATOM 358 CA GLY A 48 -0.768 32.459 11.709 1.00 16.24 c
ATOM 359 C GLY A 48 -0.370 31.116 12.317 1.00 15.45 c
ATOM 360 O GLY A 48 -1.210 30.436 12.875 1.00 15.17 O
ATOM 361 N THR A 49 0.919 30.785 12.177 1.00 16.03 N
ATOM 362 CA THR A 49 1.435 29.557 12.783 1.00 16.13 c
ATOM 363 C THR A 49 2.805 29.901 13.377 1.00 17.15 c
ATOM 364 O THR A 49 3.492 30.741 12.790 1.00 15.90 O
ATOM 365 CB THR A 49 1.526 28.452 11.739 1.00 16.91 c
ATOM 366 OG1 THR A 49 0.181 28.169 11.289 1.00 14.21 0
ATOM 367 CG2 THR A 49 1.936 27.132 12.400 1.00 16.21 c
ATOM 368 N PHE A 50 3.164 29.322 14.530 1.00 16.48 N
ATOM 369 CA PHE A 50 4.518 29.587 15.003 1.00 13.84 c
ATOM 370 C PHE A 50 5.592 28.969 14.111 1.00 14.81 c
ATOM 371 O PHE A 50 5.376 28.019 13.352 1.00 15.09 0
ATOM 372 CB PHE A 50 4.656 28.868 16.371 1.00 13.55 c
ATOM 373 CG PHE A 50 4.098 29.651 17.514 1.00 13.29 c
ATOM 374 CD1 PHE A 50 2.810 30.140 17.494 1.00 16.48 c
ATOM 375 CD2 PHE A 50 4.892 29.919 18.620 1.00 15.87 c
ATOM 376 CE1 PHE A 50 2.321 30.870 18.548 1.00 15.15 c
ATOM 377 CE2 PHE A 50 4.421 30.680 19.684 1.00 16.11 c
ATOM 378 CZ PHE A 50 3.105 31.159 19.662 1.00 15.82 c
ATOM 379 N TYR A 51 6.778 29.576 14.225 1.00 11.65 N
ATOM 380 CA TYR A 51 8.011 29.069 13.590 1.00 12.70 c
ATOM 381 C TYR A 51 8.790 28.246 14.609 1.00 11.84 c
ATOM 382 O TYR A 51 9.086 28.745 15.718 1.00 15.79 O
ATOM 383 CB TYR A 51 8.865 30.294 13.217 1.00 13.11 c
ATOM 384 CG TYR A 51 8.379 31.139 12.051 1.00 13.50 c
ATOM 385 CD1 TYR A 51 7.326 32.026 12.276 1.00 13.00 c
ATOM 386 CD2 TYR A 51 8.951 31.115 10.801 1.00 15.21 c
ATOM 387 CE1 TYR A 51 6.833 32.845 11.286 1.00 15.73 c
ATOM 388 CE2 TYR A 51 8.473 31.940 9.786 1.00 16.71 c
ATOM 389 CZ TYR A 51 7.410 32.788 10.036 1.00 19.01 c
ATOM 390 OH TYR A 51 6.947 33.585 9.011 1.00 16.58 O
ATOM 391 N TRP A 52 9.153 27.012 14.272 1.00 13.83 N
ATOM 392 CA TRP A 52 9.890 26.152 15.154 1.00 12.86 c
ATOM 393 C TRP A 52 11.404 26.265 14.965 1.00 13.06 c
ATOM 394 O TRP A 52 11.934 25.983 13.899 1.00 15.63 O
ATOM 395 CB TRP A 52 9.489 24.692 14.949 1.00 13.88 c
ATOM 396 CG TRP A 52 8.104 24.398 15.475 1.00 11.93 c
ATOM 397 CD1 TRP A 52 6.914 24.897 15.023 1.00 14.24 c
ATOM 398 CD2 TRP A 52 7.786 23.552 16.602 1.00 12.10 c
ATOM 399 NE1 TRP A 52 5.866 24.374 15.731 1.00 10.67 N ATOM 400 CE2 TRP A 52 6.392 23..553 16..715 1.00 12..07 C
ATOM 401 CE3 TRP A 52 8.562 22. .791 17. ,485 1.00 12. .55 C
ATOM 402 CZ2 TRP A 52 5.737 22. .798 17. ,706 1.00 12. ,99 C
ATOM 403 CZ3 TRP A 52 7.912 22. .053 18. ,466 1.00 13. .86 C ATOM 404 CH2 TRP A 52 6.502 22. .056 18. ,557 1.00 13. .59 C
ATOM 405 N ILE A 53 12.019 26. .684 16. ,082 1.00 11. ,99 N
ATOM 406 CA ILE A 53 13.490 26. .888 16. ,037 1.00 13. .95 C
ATOM 407 C ILE A 53 14.119 25. .692 16. ,735 1.00 15. .56 C
ATOM 408 O ILE A 53 14.563 25. ,776 17. ,907 1.00 13. .88 O ATOM 409 CB ILE A 53 13.887 28. .213 16. ,688 1.00 11. ,83 C
ATOM 410 CGI ILE A 53 13.108 29. .433 16. ,197 1.00 13. .23 C
ATOM 411 CG2 ILE A 53 15.388 28. ,449 16. ,348 1.00 15. .04 C
ATOM 412 CD1 ILE A 53 12.866 29. ,590 14. ,723 1.00 14. .75 C
ATOM 413 N SER A 54 13.986 24. .549 16. .079 1.00 15. .20 N ATOM 414 CA SER A 54 14.235 23. ,237 16. .686 1.00 10. .25 C
ATOM 415 C SER A 54 15.685 22. .814 16. .750 1.00 14. .35 C
ATOM 416 O SER A 54 15.968 21. .697 17. ,179 1.00 15. .04 O
ATOM 417 CB SER A 54 13.378 22. ,178 15. ,982 1.00 13. .89 C
ATOM 418 OG SER A 54 11.993 22. .583 15. ,969 1.00 17. .22 O ATOM 419 N ASN A 55 16.595 23. .631 16. .271 1.00 15. .12 N
ATOM 420 CA ASN A 55 18.028 23. ,347 16. ,337 1.00 14. .74 C
ATOM 421 C ASN A 55 18.794 24. .601 15. ,916 1.00 15. .53 C
ATOM 422 O ASN A 55 18.212 25. ,630 15. ,547 1.00 15. ,28 O
ATOM 423 CB ASN A 55 18.434 22. .138 15. ,511 1.00 14. .25 C ATOM 424 CG ASN A 55 17.949 22. .297 14. ,094 1.00 15. .84 C
ATOM 425 ODl ASN A 55 18.306 23. .220 13. ,368 1.00 15. .76 O
ATOM 426 ND2 ASN A 55 17.034 21. .393 13. ,725 1.00 20. .84 N
ATOM 427 N ILE A 56 20.115 24. .557 16. ,063 1.00 13, .68 N
ATOM 428 CA ILE A 56 20.993 25, .713 15. ,847 1.00 16, .07 C ATOM 429 C ILE A 56 20.940 26. .138 14. .395 1.00 15. .12 C
ATOM 430 O ILE A 56 20.891 27. .354 14. .124 1.00 14. .39 O
ATOM 431 CB ILE A 56 22.429 25. .397 16. .309 1.00 14. .99 C
ATOM 432 CGI ILE A 56 22.495 25. .468 17. .849 1.00 15. .05 C
ATOM 433 CG2 ILE A 56 23.449 26. .373 15. .726 1.00 15, .64 c ATOM 434 CD1 ILE A 56 23.657 24. .585 18. .367 1.00 15, .09 C
ATOM 435 N PHE A 57 20.901 25. .200 13. .464 1.00 15. .86 N
ATOM 436 CA PHE A 57 20.747 25. .523 12. ,048 1.00 11, .80 C
ATOM 437 C PHE A 57 19.503 26. .421 11. ,832 1.00 15, .24 C
ATOM 438 O PHE A 57 19.550 27. .342 11. .017 1.00 14, .57 O ATOM 439 CB PHE A 57 20.610 24. .230 11. .256 1.00 15, .25 C
ATOM 440 CG PHE A 57 20.373 24, .376 9. .783 1.00 14, .23 C
ATOM 441 CD1 PHE A 57 21.438 24, .566 8, .932 1.00 15, .89 C
ATOM 442 CD2 PHE A 57 19.093 24, .374 9, .256 1.00 15, .74 C
ATOM 443 CE1 PHE A 57 21.242 24. .700 7. .568 1.00 16, .76 C ATOM 444 CE2 PHE A 57 18.873 24. .474 7, .900 1.00 21, .90 C
ATOM 445 CZ PHE A 57 19.959 24. .679 7, .063 1.00 19. .88 C
ATOM 446 N LEU A 58 18.390 26. .082 12. .443 1.00 13, .64 N
ATOM 447 CA LEU A 58 17.153 26. .810 12, .307 1.00 13, .38 C
ATOM 448 C LEU A 58 17.143 28. .147 13, .024 1.00 13, .46 C ATOM 449 O LEU A 58 16.116 28, .830 12. .829 1.00 14, .86 O
ATOM 450 CB LEU A 58 15.905 25. .998 12. .647 1.00 18, .35 C
ATOM 451 CG LEU A 58 15.736 24. .741 11, .797 1.00 16, .27 c
ATOM 452 CD1 LEU A 58 14.647 23, .822 12, .365 1.00 14, .80 C
ATOM 453 CD2 LEU A 58 15.377 25. .128 10, .359 1.00 19, .12 C ATOM 454 N LEU A 59 18.172 28 .584 13, .736 1.00 13, .01 N
ATOM 455 CA LEU A 59 18.157 29 .994 14, .198 1.00 11, .72 C
ATOM 456 C LEU A 59 17.950 30, .951 13. .038 1.00 14, .70 C
ATOM 457 O LEU A 59 17.368 32 .026 13, .261 1.00 16, .53 O
ATOM 458 CB LEU A 59 19.516 30 .336 14, .855 1.00 14, .46 C ATOM 459 CG LEU A 59 19.716 29.678 16.239 1.00 18.29 C
ATOM 460 CD1 LEU A 59 21.206 29.708 16.577 1.00 18.73 C
ATOM 461 CD2 LEU A 59 18.916 30.460 17.273 1.00 17.83 C
ATOM 462 N ARG A 60 18.333 30.604 11.813 1.00 15.56 N ATOM 463 CA ARG A 60 18.133 31.405 10.610 1.00 16.80 C
ATOM 464 C ARG A 60 16.664 31.649 10.348 1.00 15.95 C
ATOM 465 O ARG A 60 16.319 32.692 9.806 1.00 17.25 O
ATOM 466 CB ARG A 60 18.783 30.774 9.370 1.00 20.89 C
ATOM 467 CG ARG A 60 18.104 29.517 8.845 1.00 24.06 C ATOM 468 CD ARG A 60 18.985 28.721 7.869 1.00 31.87 C
ATOM 469 NE ARG A 60 20.262 28.394 8.447 1.00 33.83 N
ATOM 470 CZ ARG A 60 21.518 28.222 8.089 1.00 35.90 C
ATOM 471 NH1 ARG A 60 21.967 28.348 6.842 1.00 29.08 N
ATOM 472 NH2 ARG A 60 22.384 27.921 9.063 1.00 33.10 N ATOM 473 N ASP A 61 15.755 30.730 10.778 1.00 19.09 N
ATOM 474 CA ASP A 61 14.329 30.969 10.622 1.00 15.63 C
ATOM 475 C ASP A 61 13.852 32.144 11.476 1.00 15.44 C
ATOM 476 O ASP A 61 12.804 32.711 11.159 1.00 18.75 O
ATOM 477 CB ASP A 61 13.487 29.720 10.897 1.00 14.39 C ATOM 478 CG ASP A 61 13.363 28.861 9.648 1.00 18.12 c
ATOM 479 ODl ASP A 61 13.802 29.295 8.564 1.00 23.64 O
ATOM 480 OD2 ASP A 61 12.828 27.718 9.718 1.00 18.24 O
ATOM 481 N ILE A 62 14.596 32.541 12.545 1.00 13.50 N
ATOM 482 CA ILE A 62 14.158 33.734 13.271 1.00 16.23 c ATOM 483 C ILE A 62 14.319 34.970 12.382 1.00 20.75 c
ATOM 484 O ILE A 62 13.452 35.865 12.334 1.00 16.45 O
ATOM 485 CB ILE A 62 14.966 33.902 14.572 1.00 18.28 c
ATOM 486 CGI ILE A 62 14.729 32.710 15.498 1.00 18.12 c
ATOM 487 CG2 ILE A 62 14.544 35.150 15.339 1.00 16.41 c ATOM 488 CD1 ILE A 62 15.606 32.777 16.745 1.00 19.28 c
ATOM 489 N ASP A 63 15.422 35.030 11.631 1.00 17.23 N
ATOM 490 CA ASP A 63 15.624 36.137 10.689 1.00 19.20 c
ATOM 491 C ASP A 63 14.500 36.146 9.653 1.00 19.34 c
ATOM 492 O ASP A 63 13.958 37.217 9.321 1.00 22.74 O ATOM 493 CB ASP A 63 17.019 36.085 10.059 1.00 21.12 c
ATOM 494 CG ASP A 63 18.111 36.118 11.113 1.00 21.39 c
ATOM 495 ODl ASP A 63 18.085 36.935 12.055 1.00 25.66 O
ATOM 496 OD2 ASP A 63 19.068 35.309 11.065 1.00 30.68 O
ATOM 497 N VAL A 64 14.140 34.951 9.165 1.00 17.14 N ATOM 498 CA VAL A 64 13.036 34.834 8.226 1.00 15.53 c
ATOM 499 C VAL A 64 11.744 35.398 8.835 1.00 14.91 c
ATOM 500 O VAL A 64 11.044 36.197 8.188 1.00 16.37 O
ATOM 501 CB VAL A 64 12.781 33.392 7.750 1.00 17.08 c
ATOM 502 CGI VAL A 64 11.594 33.375 6.782 1.00 18.67 c ATOM 503 CG2 VAL A 64 14.023 32.836 7.077 1.00 20.31 c
ATOM 504 N ALA A 65 11.417 34.975 10.063 1.00 15.69 N
ATOM 505 CA ALA A 65 10.189 35.446 10.713 1.00 15.10 c
ATOM 506 C ALA A 65 10.193 36.967 10.892 1.00 17.42 c
ATOM 507 O ALA A 65 9.203 37.683 10.672 1.00 15.84 O ATOM 508 CB ALA A 65 9.954 34.724 12.052 1.00 17.84 c
ATOM 509 N ILE A 66 11.336 37.499 11.317 1.00 14.55 N
ATOM 510 CA ILE A 66 11.454 38.954 11.529 1.00 23.15 C
ATOM 511 C ILE A 66 11.294 39.695 10.214 1.00 18.04 V'
ATOM 512 O ILE A 66 10.668 40.758 10.198 1.00 20.04 O ATOM 513 CB ILE A 66 12.812 39.258 12.179 1.00 19.03 c
ATOM 514 CGI ILE A 66 12.785 38.863 13.645 1.00 19.68 c
ATOM 515 CG2 ILE A 66 13.210 40.743 12.075 1.00 18.72 c
ATOM 516 CD1 ILE A 66 14.150 38.787 14.282 1.00 18.42 c
ATOM 517 N GLN A 67 11.856 39.221 9.122 1.00 18.61 N ATOM 518 CA GLN A 67 11.702 39.831 7.802 1.00 16.62 C
ATOM 519 C GLN A 67 10.233 39.906 7.451 1.00 21.78 C
ATOM 520 O GLN A 67 9.628 40.914 7.073 1.00 19.15 O
ATOM 521 CB GLN A 67 12.487 39.068 6.726 1.00 21.47 C
ATOM 522 CG GLN A 67 12.027 39.497 5.328 1.00 35.22 C
ATOM 523 CD GLN A 67 12.918 38.994 4.211 1.00 37.11 C
ATOM 524 OE1 GLN A 67 14.114 38.779 4.391 1.00 33.68 O
ATOM 525 NE2 GLN A 67 12.348 38.809 3.028 1.00 41.81 N
ATOM 526 N ASN A 68 9.551 38.748 7.606 1.00 18.06 N
ATOM 527 CA ASN A 68 8.127 38.671 7.361 1.00 18.35 C
ATOM 528 C ASN A 68 7.322 39.597 8.261 1.00 19.58 C
ATOM 529 O ASN A 68 6.359 40.200 7.802 1.00 23.36 O
ATOM 530 CB ASN A 68 7.647 37.217 7.516 1.00 14.91 C
ATOM 531 CG ASN A 68 8.226 36.286 6.479 1.00 22.58 c
ATOM 532 ODl ASN A 68 8.639 36.711 5.397 1.00 24.04 o
ATOM 533 ND2 ASN A 68 8.200 34.978 6.758 1.00 18.67 N
ATOM 534 N ALA A 69 7.682 39.721 9.539 1.00 19.23 N
ATOM 535 CA ALA A 69 6.991 40.578 10.476 1.00 15.96 c
ATOM 536 C ALA A 69 7.135 42.046 10.004 1.00 22.11 C
ATOM 537 O ALA A 69 6.139 42.743 9.941 1.00 21.63 O
ATOM 538 CB ALA A 69 7.453 40.465 11.917 1.00 18.59 C
ATOM 539 N ARG A 70 8.343 42.432 9.609 1.00 22.18 N
ATOM 540 CA ARG A 70 8.567 43.803 9.148 1.00 22.08 c
ATOM 541 C ARG A 70 7.864 44.100 7.832 1.00 27.11 c
ATOM 542 O ARG A 70 7.398 45.233 7.637 1.00 30.23 o
ATOM 543 CB ARG A 70 10.067 44.076 9.026 1.00 19.06 C
ATOM 544 CG ARG A 70 10.775 44.009 10.370 1.00 22.53 c
ATOM 545 CD ARG A 70 12.270 44.320 10.277 1.00 23.54 C
ATOM 546 NE ARG A 70 12.742 44.598 11.647 1.00 21.57 N
ATOM 547 CZ ARG A 70 13.950 44.268 12.072 1.00 16.33 c
ATOM 548 NH1 ARG A 70 14.809 43.724 11.227 1.00 23.70 N
ATOM 549 NH2 ARG A 70 14.256 44.540 13.351 1.00 20.71 N
ATOM 550 N ALA A 71 7.694 43.123 6.946 1.00 24.69 N
ATOM 551 CA ALA A 71 6.964 43.311 5.701 1.00 27.59 C
ATOM 552 C ALA A 71 5.463 43.444 5.954 1.00 33.23 C
ATOM 553 O ALA A 71 4.738 44.190 5.279 1.00 34.34 O
ATOM 554 CB ALA A 71 7.209 42.148 4.740 1.00 32.45 C
ATOM 555 N ALA A 72 4.962 42.719 6.947 1.00 25.47 N
ATOM 556 CA ALA A 72 3.554 42.744 7.303 1.00 25.49 C
ATOM 557 C ALA A 72 3.206 44.121 7.858 1.00 30.33 C
ATOM 558 O ALA A 72 2.244 44.778 7.498 1.00 28.16 O
ATOM 559 CB ALA A 72 3.216 41.648 8.308 1.00 21.10 C
ATOM 560 N LYS A 73 4.103 44.596 8.714 1.00 30.08 N
ATOM 561 CA LYS A 73 3.891 45.888 9.381 1.00 34.22 c
ATOM 562 C LYS A 73 4.012 47.017 8.373 1.00 32.67 C
ATOM 563 O LYS A 73 3.334 48.039 8.511 1.00 28.18 o
ATOM 564 CB LYS A 73 4.812 45.861 10.576 1.00 41.50 C
ATOM 565 CG LYS A 73 5.848 46.941 10.667 1.00 48.31 c
ATOM 566 CD LYS A 73 5.362 48.086 11.538 1.00 50.90 c
ATOM 567 CE LYS A 73 5.118 47.686 12.983 1.00 59.96 C
ATOM 568 NZ LYS A 73 6.022 46.596 13.449 1.00 60.78 N
ATOM 569 N ALA A 74 4.766 46.799 7.290 1.00 30.13 N
ATOM 570 CA ALA A 74 4.858 47.776 6.212 1.00 35.21 C
ATOM 571 C ALA A 74 3.594 47.834 5.365 1.00 42.35 C
ATOM 572 O ALA A 74 3.390 48.892 4.743 1.00 45.03 O
ATOM 573 CB ALA A 74 6.059 47.523 5.311 1.00 29.40 C
ATOM 574 N ARG A 75 2.718 46.830 5.332 1.00 40.77 N
ATOM 575 CA ARG A 75 1.478 46.989 4.565 1.00 36.94 C
ATOM 576 C ARG A 75 0.316 47.321 5.496 1.00 36.22 C ATOM 577 O ARG A 75 -0.855 47.166 5.152 1.00 37.82 O
ATOM 578 CB ARG A 75 1.151 45.795 3.681 1.00 43.25 c
ATOM 579 CG ARG A 75 1.341 44.478 4.378 1.00 44.99 c
ATOM 580 CD ARG A 75 1.163 43.280 3.447 1.00 49.43 c
ATOM 581 NE ARG A 75 0.818 42.142 4.312 1.00 43.11 N
ATOM 582 CZ ARG A 75 1.679 41.201 4.679 1.00 44.77 c
ATOM 583 NH1 ARG A 75 2.931 41.211 4.256 1.00 39.44 N
ATOM 584 NH2 ARG A 75 1.266 40.222 5.473 1.00 46.52 N
ATOM 585 N GLY A 76 0.648 47.799 6.695 1.00 33.79 N
ATOM 586 CA GLY A 76 -0.308 48.248 7.663 1.00 34.23 c
ATOM 587 C GLY A 76 -0.776 47.269 8.710 1.00 38.37 c
ATOM 588 O GLY A 76 -1.611 47.609 9.558 1.00 35.19 o
ATOM 589 N GLU A 77 -0.234 46.057 8.695 1.00 32.72 N
ATOM 590 CA GLU A 77 -0.648 45.064 9.690 1.00 27.88 c
ATOM 591 C GLU A 77 0.040 45.289 11.024 1.00 25.54 c
ATOM 592 O GLU A 77 0.981 46.072 11.184 1.00 23.07 o
ATOM 593 CB GLU A 77 -0.336 43.672 9.139 1.00 29.69 c
ATOM 594 CG GLU A 77 -0.915 43.442 7.742 1.00 29.74 c
ATOM 595 CD GLU A 77 -0.701 42.023 7.258 1.00 34.45 c
ATOM 596 OE1 GLU A 77 -0.172 41.186 8.014 1.00 35.54 o
ATOM 597 OE2 GLU A 77 -1.068 41.769 6.096 1.00 37.17 o
ATOM 598 N ASN A 78 -0.416 44.560 12.030 1.00 25.11 N
ATOM 599 CA ASN A 78 0.075 44.595 13.395 1.00 29.31 c
ATOM 600 C ASN A 78 0.282 43.157 13.914 1.00 21.55 c
ATOM 601 O ASN A 78 -0.569 42.589 14.611 1.00 20.53 o
ATOM 602 CB ASN A 78 -0.954 45.253 14.320 1.00 32.70 c
ATOM 603 CG ASN A 78 -0.321 46.480 14.944 1.00 48.63 c
ATOM 604 ODl ASN A 78 -0.413 47.540 14.329 1.00 43.28 o
ATOM 605 ND2 ASN A 78 0.326 46.303 16.087 1.00 47.85 N
ATOM 606 N PRO A 79 1.411 42.633 13.518 1.00 26.64 N
ATOM 607 CA PRO A 79 1.735 41.238 13.758 1.00 22.72 c
ATOM 608 C PRO A 79 2.301 40.962 15.126 1.00 21.56 c
ATOM 609 O PRO A 79 2.821 41.834 15.829 1.00 20.72 0
ATOM 610 CB PRO A 79 2.779 40.863 12.672 1.00 19.05 c
ATOM 611 CG PRO A 79 3.404 42.190 12.343 1.00 27.23 c
ATOM 612 CD PRO A 79 2.420 43.275 12.683 1.00 25.70 C
ATOM 613 N ILE A 80 2.171 39.680 15.477 1.00 15.61 N
ATOM 614 CA ILE A 80 2.938 39.180 16.628 1.00 19.10 C
ATOM 615 C ILE A 80 3.537 37.877 16.092 1.00 19.54 C
ATOM 616 O ILE A 80 2.820 37.100 15.472 1.00 16.60 o
ATOM 617 CB ILE A 80 2.178 39.061 17.925 1.00 15.55 C
ATOM 618 CGI ILE A 80 3.108 38.513 19.022 1.00 17.32 C
ATOM 619 CG2 ILE A 80 0.910 38.217 17.736 1.00 16.24 C
ATOM 620 CD1 ILE A 80 2.543 38.603 20.427 1.00 17.37 C
ATOM 621 N VAL A 81 4.850 37.747 16.231 1.00 15.36 N
ATOM 622 CA VAL A 81 5.518 36.539 15.724 1.00 15.23 c
ATOM 623 C VAL A 81 5.580 35.411 16.750 1.00 18.65 c
ATOM 624 O VAL A 81 6.040 35.685 17.849 1.00 14.58 0
ATOM 625 CB VAL A 81 6.984 36.937 15.403 1.00 19.78 c
ATOM 626 CGI VAL A 81 7.811 35.721 14.984 1.00 16.80 c
ATOM 627 CG2 VAL A 81 6.991 38.009 14.325 1.00 18.73 c
ATOM 628 N GLY A 82 5.128 34.206 16.412 1.00 13.32 N
ATOM 629 CA GLY A 82 5.241 33.099 17.379 1.00 14.02 c
ATOM 630 C GLY A 82 6.521 32.327 17.019 1.00 12.83 c
ATOM 631 O GLY A 82 6.688 31.929 15.865 1.00 11.47 0
ATOM 632 N LEU A 83 7.336 32.090 18.064 1.00 11.68 N
ATOM 633 CA LEU A 83 8.565 31.294 17.886 1.00 12.33 c
ATOM 634 C LEU A 83 8.548 30.159 18.919 1.00 13.16 c
ATOM 635 O LEU A 83 8.168 30.411 20.064 1.00 13.82 o ATOM 636 CB LEU A 83 9.847 32.102 18.122 1.00 11.71 C
ATOM 637 CG LEU A 83 10.062 33.262 17.139 1.00 14.81 C
ATOM 638 CD1 LEU A 83 11.339 34.012 17.563 1.00 14.82 C
ATOM 639 CD2 LEU A 83 10.147 32.759 15.722 1.00 13.22 C ATOM 640 N VAL A 84 9.038 28.983 18.533 1.00 11.69 N
ATOM 641 CA VAL A 84 9.103 27.865 19.496 1.00 9.75 C
ATOM 642 C VAL A 84 10.601 27.669 19.809 1.00 11.01 C
ATOM 643 O VAL A 84 11.359 27.478 18.879 1.00 14.07 O
ATOM 644 CB VAL A 84 8.547 26.553 18.921 1.00 12.58 C ATOM 645 CGI VAL A 84 8.466 25.532 20.063 1.00 15.29 C
ATOM 646 CG2 VAL A 84 7.133 26.763 18.360 1.00 11.72 C
ATOM 647 N LEU A 85 10.971 27.880 21.063 1.00 12.20 N
ATOM 648 CA LEU A 85 12.380 27.722 21.480 1.00 11.40 C
ATOM 649 C LEU A 85 12.426 26.283 21.969 1.00 12.29 C ATOM 650 O LEU A 85 11.824 25.945 23.006 1.00 13.55 O
ATOM 651 CB LEU A 85 12.649 28.760 22.580 1.00 13.55 C
ATOM 652 CG LEU A 85 14.109 28.879 23.015 1.00 12.40 C
ATOM 653 CD1 LEU A 85 14.379 30.308 23.458 1.00 15.19 C
ATOM 654 CD2 LEU A 85 14.415 27.880 24.115 1.00 17.10 C ATOM 655 N TYR A 86 13.095 25.437 21.178 1.00 13.64 N
ATOM 656 CA TYR A 86 13.032 23.997 21.430 1.00 10.83 C
ATOM 657 C TYR A 86 14.341 23.293 21.099 1.00 15.34 C
ATOM 658 O TYR A 86 14.442 22.719 20.022 1.00 14.86 o
ATOM 659 CB TYR A 86 11.871 23.417 20.596 1.00 12.42 C ATOM 660 CG TYR A 86 11.571 21.960 20.640 1.00 12.60 C
ATOM 661 CD1 TYR A 86 11.395 21.258 21.829 1.00 9.94 C
ATOM 662 CD2 TYR A 86 11.444 21.206 19.462 1.00 13.74 C
ATOM 663 CE1 TYR A 86 11.067 19.904 21.879 1.00 12.13 C
ATOM 664 CE2 TYR A 86 11.148 19.865 19.480 1.00 16.78 C ATOM 665 CZ TYR A 86 10.962 19.209 20.687 1.00 15.36 C
ATOM 666 OH TYR A 86 10.661 17.861 20.674 1.00 14.76 O
ATOM 667 N ASN A 87 15.301 23.394 22.011 1.00 15.39 N
ATOM 668 CA ASN A 87 16.574 22.656 21.769 1.00 10.89 C
ATOM 669 C ASN A 87 17.212 22.231 23.068 1.00 12.51 C ATOM 670 O ASN A 87 18.464 22.143 23.192 1.00 14.17 O
ATOM 671 CB ASN A 87 17.480 23.536 20.917 1.00 12.53 C
ATOM 672 CG ASN A 87 18.561 22.708 20.211 1.00 15.12 C
ATOM 673 ODl ASN A 87 18.454 21.490 20.075 1.00 13.51 O
ATOM 674 ND2 ASN A 87 19.600 23.388 19.764 1.00 14.63 N ATOM 675 N LEU A 88 16.400 21.886 24.068 1.00 12.48 N
ATOM 676 CA LEU A 88 16.959 21.489 25.367 1.00 13.76 c
ATOM 677 C LEU A 88 17.902 20.318 25.277 1.00 13.37 c
ATOM 678 O LEU A 88 17.751 19.344 24.520 1.00 14.66 O
ATOM 679 CB LEU A 88 15.748 21.029 26.236 1.00 16.32 C ATOM 680 CG LEU A 88 15.926 21.035 27.755 1.00 16.68 C
ATOM 681 CD1 LEU A 88 16.144 22.457 28.258 1.00 16.55 C
ATOM 682 CD2 LEU A 88 14.696 20.405 28.411 1.00 16.00 C
ATOM 683 N PRO A 89 18.969 20.370 26.058 1.00 15.44 N
ATOM 684 CA PRO A 89 19.862 19.217 26.120 1.00 15.41 C ATOM 685 C PRO A 89 19.082 18.051 26.703 1.00 15.17 C
ATOM 686 O PRO A 89 18.248 18.176 27.631 1.00 14.69 O
ATOM 687 CB PRO A 89 21.036 19.606 27.042 1.00 15.65 C
ATOM 688 CG PRO A 89 20.869 21.083 27.115 1.00 15.43 e
ATOM 689 CD PRO A 89 19.403 21.455 26.923 1.00 12.94 c ATOM 690 N ASP A 90 19.234 16.866 26.126 1.00 12.82 N
ATOM 691 CA ASP A 90 18.521 15.656 26.505 1.00 16.10 C
ATOM 692 C ASP A 90 17.005 15.834 26.379 1.00 19.34 C
ATOM 693 O ASP A 90 16.188 15.366 27.198 1.00 17.20 O
ATOM 694 CB ASP A 90 18.860 15.221 27.942 1.00 13.45 C ATOM 695 CG ASP A 90 20.270 14.653 28.032 1.00 24.51 C
ATOM 696 ODl ASP A 90 20.987 14.711 27.006 1.00 19.04 O
ATOM 697 OD2 ASP A 90 20.643 14.173 29.132 1.00 18.33 o
ATOM 698 N ARG A 91 16.643 16.574 25.345 1.00 13.43 N
ATOM 699 CA ARG A 91 15.274 16.893 24.957 1.00 14.50 C
ATOM 700 C ARG A 91 14.362 15.679 24.953 1.00 14.98 C
ATOM 701 O ARG A 91 14.786 14.585 24.580 1.00 15.76 o
ATOM 702 CB ARG A 91 15.330 17.432 23.511 1.00 13.98 C
ATOM 703 CG ARG A 91 14.190 18.399 23.179 1.00 13.34 C
ATOM 704 CD ARG A 91 14.482 19.165 21.896 1.00 13.92 C
ATOM 705 NE ARG A 91 14.392 18.287 20.703 1.00 13.23 N
ATOM 706 CZ ARG A 91 14.566 18.799 19.485 1.00 12.35 C
ATOM 707 NH1 ARG A 91 14.823 20.077 19.201 1.00 13.29 N
ATOM 708 NH2 ARG A 91 14.487 17.914 18.456 1.00 14.70 N
ATOM 709 N ASP A 92 13.125 15.846 25.494 1.00 11.96 N
ATOM 710 CA ASP A 92 12.175 14.744 25.570 1.00 17.95 C
ATOM 711 C ASP A 92 12.803 13.526 26.251 1.00 15.83 C
ATOM 712 O ASP A 92 12.795 12.409 25.748 1.00 13.78 o
ATOM 713 CB ASP A 92 11.670 14.338 24.184 1.00 14.41 C
ATOM 714 CG ASP A 92 10.927 15.477 23.512 1.00 16.54 C
ATOM 715 ODl ASP A 92 9.841 15.800 24.048 1.00 18.60 o
ATOM 716 OD2 ASP A 92 11.358 16.080 22.499 1.00 16.72 o
ATOM 717 N CYS A 93 13.231 13.758 27.514 1.00 14.74 N
ATOM 718 CA CYS A 93 14.057 12.726 28.159 1.00 18.87 C
ATOM 719 C CYS A 93 13.371 11.401 28.341 1.00 16.21 C
ATOM 720 O CYS A 93 13.982 10.318 28.447 1.00 21.36 0
ATOM 721 CB CYS A 93 14.638 13.268 29.478 1.00 17.56 C
ATOM 722 SG CYS A 93 13.408 13.566 30.760 1.00 17.27 S
ATOM 723 N SER A 94 12.030 11.356 28.441 1.00 17.34 N
ATOM 724 CA SER A 94 11.314 10.116 28.685 1.00 19.63 C
ATOM 725 C SER A 94 11.521 9.075 27.608 1.00 22.85 C
ATOM 726 o SER A 94 11.374 7.890 27.948 1.00 23.92 o
ATOM 727 CB SER A 94 9.826 10.341 28.937 1.00 18.36 C
ATOM 728 OG ASER A 94 9.631 10.981 30.198 0.50 18.80 o
ATOM 729 OG BSER A 94 9.246 11.173 27.951 0.50 20.11 0
ATOM 730 N ALA A 95 11.995 9.428 26.413 1.00 18.96 N
ATOM 731 CA ALA A 95 12.274 8.454 25.376 1.00 23.37 C
ATOM 732 C ALA A 95 13.675 7.868 25.545 1.00 20.16 C
ATOM 733 O ALA A 95 13.983 6.871 24.895 1.00 21.70 o
ATOM 734 CB ALA A 95 12.079 9.129 24.033 1.00 22.92 C
ATOM 735 N GLY A 96 14.482 8.417 26.464 1.00 17.34 N
ATOM 736 CA GLY A 96 15.756 7.783 26.787 1.00 16.87 C
ATOM 737 C GLY A 96 17.013 8.322 26.168 1.00 17.95 C
ATOM 738 O GLY A 96 18.124 7.930 26.541 1.00 19.74 0
ATOM 739 N GLU A 97 16.863 9.329 25.305 1.00 15.22 N
ATOM 740 CA GLU A 97 18.012 9.956 24.639 1.00 14.61 C
ATOM 741 C GLU A 97 17.522 11.306 24.118 1.00 14.63 C
ATOM 742 O GLU A 97 16.351 11.361 23.733 1.00 16.47 o
ATOM 743 CB GLU A 97 18.464 9.075 23.457 1.00 13.39 C
ATOM 744 CG GLU A 97 19.491 9.749 22.553 1.00 15.47 C
ATOM 745 CD GLU A 97 19.803 8.954 21.307 1.00 18.25 C
ATOM 746 OE1 GLU A 97 18.951 8.168 20.843 1.00 16.69 o
ATOM 747 OE2 GLU A 97 20.919 9.159 20.768 1.00 24.69 -
ATOM 748 N SER A 98 18.328 12.363 24.076 1.00 16.83 N
ATOM 749 CA SER A 98 17.811 13.612 23.483 1.00 15.37 C
ATOM 750 C SER A 98 17.165 13.351 22.115 1.00 13.72 C
ATOM 751 O SER A 98 17.722 12.667 21.288 1.00 18.18 o
ATOM 752 CB SER A 98 18.961 14.591 23.250 1.00 13.25 C
ATOM 753 OG SER A 98 18.475 15.843 22.800 1.00 14.77 o ATOM 754 N SER A 99 16.031 14.,033 21..889 1.00 13.,48 N
ATOM 755 CA SER A 99 15. 397 14. ,000 20. ,581 1.00 12. .53 C
ATOM 756 C SER A 99 16. 013 15. ,107 19. ,702 1.00 13. ,29 C
ATOM 757 O SER A 99 15. 610 15. ,164 18. ,536 1.00 15. .74 O
ATOM 758 CB SER A 99 13. 894 14. 283 20. ,703 1.00 14. ,05 C
ATOM 759 OG SER A 99 13. 664 15. ,522 21. 322 1.00 13. ,06 O
ATOM 760 N GLY A 100 16. 896 15. ,925 20. ,256 1.00 14. ,54 N
ATOM 761 CA GLY A 100 17. 558 17. ,017 19. ,521 1.00 11. .74 C
ATOM 762 C GLY A 100 19. ,068 16. .771 19. .471 1.00 15. ,29 C
ATOM 763 O GLY A 100 19. ,642 15. ,757 19. ,892 1.00 15. ,03 O
ATOM 764 N GLU A 101 19. .770 17. ,796 18. ,993 1.00 12. ,15 N
ATOM 765 CA GLU A 101 21. ,205 17. ,711 18. ,778 1.00 13. ,21 C
ATOM 766 C GLU A 101 22. .048 17. ,876 20. ,030 1.00 14. .91 c
ATOM 767 O GLU A 101 23. ,240 17. ,482 19. .964 1.00 15. ,83 O
ATOM 768 CB GLU A 101 21. ,613 18. ,752 17. ,710 1.00 14. ,60 c
ATOM 769 CG GLU A 101 21. ,471 20. ,171 18. .302 1.00 14. ,60 c
ATOM 770 CD GLU A 101 21. ,410 21. .197 17. .188 1.00 16. .09 c
ATOM 771 OE1 GLU A 101 21. ,582 20. ,878 15. .990 1.00 14. .91 O
ATOM 772 OE2 GLU A 101 21. ,171 22. ,369 17. .547 1.00 14. .19 o
ATOM 773 N LEU A 102 21. ,483 18. ,344 21. .140 1.00 14. .14 N
ATOM 774 CA LEU A 102 22. ,247 18. ,594 22. .362 1.00 15. ,84 C
ATOM 775 C LEU A 102 22. ,010 17. ,503 23. .401 1.00 13. ,78 C
ATOM 776 O LEU A 102 20. .907 17. ,058 23. .637 1.00 13. .84 O
ATOM 777 CB LEU A 102 21. ,902 19. ,952 22. .983 1.00 14. ,72 c
ATOM 778 CG LEU A 102 22. ,083 21. .148 22. .052 1.00 13. .44 c
ATOM 779 CD1 LEU A 102 21. ,767 22. ,432 22. ,815 1.00 15. .55 c
ATOM 780 CD2 LEU A 102 23. ,493 21. ,236 21. ,498 1.00 15. .65 c
ATOM 781 N LYS A 103 23. ,123 17. ,055 23. .946 1.00 15. .05 N
ATOM 782 CA LYS A 103 23. ,126 16. ,009 24. ,981 1.00 18. .34 c
ATOM 783 C LYS A 103 23. .906 16, .514 26. .181 1.00 17. .23 c
ATOM 784 O LYS A 103 24. .975 17, .124 26. .013 1.00 16, .83 O
ATOM 785 CB LYS A 103 23, .780 14. .739 24. .415 1.00 15. .93 c
ATOM 786 CG LYS A 103 23, .064 14, .205 23. .170 1.00 14, .26 c
ATOM 787 CD LYS A 103 23, .580 12. .857 22. .734 1.00 20. .35 c
ATOM 788 CE LYS A 103 22. .554 12, .151 21. .828 1.00 18. .89 c
ATOM 789 NZ LYS A 103 23, .106 10, .796 21. .493 1.00 20. .43 N
ATOM 790 N LEU A 104 23, .408 16. .241 27. .385 1.00 17, .62 N
ATOM 791 CA LEU A 104 24. .102 16, .750 28, .573 1.00 19, .92 c
ATOM 792 C LEU A 104 25, .507 16. .188 28, .674 1.00 19, .44 c
ATOM 793 O LEU A 104 26, .416 16, .961 28, .996 1.00 18, .23 O
ATOM 794 CB LEU A 104 23, .292 16, .527 29. .844 1.00 14, .04 c
ATOM 795 CG LEU A 104 22. .010 17, .371 29. .962 1.00 17, .18 c
ATOM 796 CD1 LEU A 104 21. .202 16, .833 31. .126 1.00 18, .42 c
ATOM 797 CD2 LEU A 104 22. .366 18, .840 30. .141 1.00 17. .13 c
ATOM 798 N SER A 105 25. .691 14. .929 28. .284 1.00 18. .96 N
ATOM 799 CA SER A 105 27. .001 14, .293 28. .324 1.00 20. .51 c
ATOM 800 C SER A 105 27. .940 14. .733 27. .209 1.00 23. .29 c
ATOM 801 O SER A 105 29, .071 14. .218 27. .138 1.00 23, .43 O
ATOM 802 CB SER A 105 26, .769 12, .775 28. .282 1.00 21. .63 c
ATOM 803 OG SER A 105 26, .052 12, .401 27, .118 1.00 18 .93 o
ATOM 804 N GLN A 106 27, .535 15, .630 26, .320 1.00 21. .97 N
ATOM 805 CA GLN A 106 28, .345 16, .194 25, .269 1.00 16, .00 C
ATOM 806 C GLN A 106 28, .348 17, .712 25, .417 1.00 18 .59 C
ATOM 807 O GLN A 106 28, .097 18, .485 24, .485 1.00 18, .41 O
ATOM 808 CB GLN A 106 27, .885 15, .789 23, .863 1.00 16, .42 c
ATOM 809 CG GLN A 106 27, .863 14, .274 23, .614 1.00 19, .64 c
ATOM 810 CD GLN A 106 27, .231 13, .951 22, .265 1.00 30, .90 c
ATOM 811 OE1 GLN A 106 26 .602 14, .783 21, .593 1.00 24, .11 O
ATOM 812 NE2 GLN A 106 27 .373 12, .676 21, .882 1.00 24, .20 N ATOM 813 N ASN A 107 28.,624 18.,165 26.,651 1.00 17.,89 N
ATOM 814 CA ASN A 107 28. .697 19. ,566 27. .024 1.00 16. ,26 C
ATOM 815 C ASN A 107 27. ,422 20. .303 26. ,625 1.00 18. .05 C
ATOM 816 O ASN A 107 27. ,448 21. .473 26. ,294 1.00 20. ,14 O
ATOM 817 CB ASN A 107 29. ,928 20. ,225 26. ,384 1.00 19. ,79 C
ATOM 818 CG ASN A 107 30. ,297 21. ,606 26. ,886 1.00 17. ,57 C
ATOM 819 ODl ASN A 107 30. ,798 22. ,410 26. ,077 1.00 26. ,88 O
ATOM 820 ND2 ASN A 107 30. ,122 21. ,937 28. ,157 1.00 15. ,24 N
ATOM 821 N GLY A 108 26. .284 19. ,631 26. .678 1.00 18. ,99 N
ATOM 822 CA GLY A 108 25. ,043 20. ,199 26. .134 1.00 13. ,67 C
ATOM 823 C GLY A 108 24. .518 21. .427 26. .811 1.00 16. ,60 C
ATOM 824 O GLY A 108 23. ,943 22. ,317 26. .149 1.00 16. ,83 O
ATOM 825 N LEU A 109 24. ,644 21. ,522 28. ,134 1.00 15. ,55 N
ATOM 826 CA LEU A 109 24. .209 22. ,706 28. ,828 1.00 17. .89 C
ATOM 827 C LEU A 109 24. ,961 23. ,942 28. ,372 1.00 15. ,95 c
ATOM 828 O LEU A 109 24. ,352 24. ,949 28. ,010 1.00 15. ,07 O
ATOM 829 CB LEU A 109 24. ,335 22. ,490 30. ,355 1.00 21. ,55 c
ATOM 830 CG LEU A 109 23. ,899 23. ,758 31. ,092 1.00 16. ,19 c
ATOM 831 CD1 LEU A 109 22. ,397 23. .997 30. .832 1.00 23. ,18 c
ATOM 832 CD2 LEU A 109 24. .129 23. .642 32. ,589 1.00 19. ,38 c
ATOM 833 N ASN A 110 26. .304 23. ,883 28. ,269 1.00 17. .29 N
ATOM 834 CA ASN A 110 27. ,036 25. ,042 27. ,788 1.00 20. ,46 C
ATOM 835 C ASN A 110 26, .684 25, ,408 26. .347 1.00 18. ,61 C
ATOM 836 O ASN A 110 26. .533 26. .598 26. .066 1.00 19. .34 O
ATOM 837 CB ASN A 110 28. .560 24. .824 27. .887 1.00 23. .88 c
ATOM 838 CG ASN A 110 29. .020 25. ,013 29. .319 1.00 27. ,93 c
ATOM 839 ODl ASN A 110 29. .893 24. .295 29. ,839 1.00 30. ,25 O
ATOM 840 ND2 ASN A 110 28. .426 25, .997 29. .984 1.00 32. .83 N
ATOM 841 N ARG A 111 26. .536 24, .438 25. .456 1.00 20. .77 N
ATOM 842 CA ARG A 111 26, .220 24, .652 24. .042 1.00 17. .52 c
ATOM 843 C ARG A 111 24. .806 25. .273 23. .901 1.00 12. .78 c
ATOM 844 O ARG A 111 24, .605 26. .179 23, .096 1.00 16. .87 O
ATOM 845 CB ARG A 111 26, .333 23. .376 23. .231 1.00 19. .76 c
ATOM 846 CG ARG A 111 27, .693 22. .673 23, .233 1.00 20, .68 c
ATOM 847 CD ARG A 111 27, .628 21. .341 22, .482 1.00 19. .60 c
ATOM 848 NE ARG A 111 29. .014 20, .871 22, .251 1.00 24, .33 N
ATOM 849 CZ ARG A 111 29, .280 19, .666 21, .733 1.00 25, .75 c
ATOM 850 NH1 ARG A 111 28, .329 18. .817 21, .355 1.00 23, .72 N
ATOM 851 NH2 ARG A 111 30, .563 19. .339 21, .577 1.00 28, .92 N
ATOM 852 N TYR A 112 23, .886 24. .784 24. .736 1.00 16, .65 N
ATOM 853 CA TYR A 112 22, .542 25, .373 24, .766 1.00 17, .96 C
ATOM 854 C TYR A 112 22, .594 26, .844 25, .170 1.00 15, .90 c
ATOM 855 O TYR A 112 21. .966 27, .683 24, .518 1.00 16, .47 o
ATOM 856 CB TYR A 112 21. .660 24. .671 25, .767 1.00 17, .04 c
ATOM 857 CG TYR A 112 20, .209 25. .072 25, .859 1.00 13, .37 c
ATOM 858 CD1 TYR A 112 19, .281 24, .698 24, .901 1.00 16. .21 c
ATOM 859 CD2 TYR A 112 19, .783 25, .793 26. .956 1.00 15. .93 c
ATOM 860 CE1 TYR A 112 17, .941 25. .064 25. .062 1.00 15. .95 c
ATOM 861 CE2 TYR A 112 18, .444 26, .143 27. .118 1.00 18. .62 c
ATOM 862 CZ TYR A 112 17, .529 25, .757 26. .153 1.00 17, .89 c
ATOM 863 OH TYR A 112 16, .211 26, .118 26, .334 1.00 14, .52 O
ATOM 864 N LYS A 113 23, .349 27, .159 26, .241 1.00 16, .36 N
ATOM 865 CA LYS A 113 23, .430 28, .607 26, .528 1.00 17, .52 c
ATOM 866 C LYS A 113 24, .110 29, .426 25, .443 1.00 18. .91 c
ATOM 867 O LYS A 113 23 .591 30 .478 25, .023 1.00 17, .56 o
ATOM 868 CB LYS A 113 24 .226 28. .828 27, .825 1.00 18, .04 c
ATOM 869 CG LYS A 113 23 .621 28, .083 28, .988 1.00 16, .40 c
ATOM 870 CD LYS A 113 24 .470 28, .340 30, .255 1.00 23. .83 c
ATOM 871 CE LYS A 113 23 .682 27 .860 31. .470 1.00 24, .00 c ATOM 872 NZ LYS A 113 24.,572 27.,690 32.,648 1.00 30.,37 N
ATOM 873 N ASN A 114 25. ,331 29. ,043 25. ,055 1.00 17. ,28 N
ATOM 874 CA ASN A 114 26. .162 29. .880 24. ,208 1.00 19. ,38 C
ATOM 875 c ASN A 114 25. .897 29. ,777 22. .727 1.00 19. ,48 C
ATOM 876 O ASN A 114 26. ,052 30. ,807 22. .048 1.00 17. 22 O
ATOM 877 CB ASN A 114 27. ,650 29. ,525 24. .511 1.00 24. ,81 C
ATOM 878 CG ASN A 114 27. ,899 29. ,742 26. ,006 1.00 24. ,65 C
ATOM 879 ODl ASN A 114 27. ,481 30. ,742 26. .575 1.00 31. ,58 O
ATOM 880 ND2 ASN A 114 28. .549 28. ,810 26. ,686 1.00 36. .52 N
ATOM 881 N GLU A 115 25. ,496 28. ,635 22. .218 1.00 16. ,28 N
ATOM 882 CA GLU A 115 25. .288 28. ,484 20. ,787 1.00 14. ,50 C
ATOM 883 C GLU A 115 23. ,802 28. .539 20. ,394 1.00 15. ,88 C
ATOM 884 O GLU A 115 23. ,602 28. ,663 19. ,175 1.00 16. ,27 O
ATOM 885 CB GLU A 115 25. ,885 27. ,144 20. ,316 1.00 19. ,55 C
ATOM 886 CG GLU A 115 27. ,406 27. ,095 20. ,373 1.00 22. ,17 C
ATOM 887 CD GLU A 115 27. ,970 25. ,805 19. ,793 1.00 22. ,87 C
ATOM 888 OE1 GLU A 115 27. ,790 25. ,506 18. .589 1.00 27. ,70 O
ATOM 889 OE2 GLU A 115 28. ,558 25. ,016 20. ,552 1.00 23. .83 O
ATOM 890 N TYR A 116 22. ,906 28. .446 21. .387 1.00 15. ,52 N
ATOM 891 CA TYR A 116 21. ,481 28. ,462 21. ,014 1.00 17. ,64 C
ATOM 892 C TYR A 116 20. ,716 29. ,588 21. ,719 1.00 16. ,03 C
ATOM 893 O TYR A 116 20. ,259 30. ,450 20. ,953 1.00 15. ,92 O
ATOM 894 CB TYR A 116 20. .872 27. .073 21. .205 1.00 13. ,83 C
ATOM 895 CG TYR A 116 19. .393 27. .030 20. .870 1.00 13. ,56 C
ATOM 896 CD1 TYR A 116 18, .953 26. .958 19. .553 1.00 13. ,73 C
ATOM 897 CD2 TYR A 116 18. .451 27. .119 21. ,875 1.00 13. ,86 C
ATOM 898 CE1 TYR A 116 17. .593 26. .953 19. .239 1.00 13. .57 C
ATOM 899 CE2 TYR A 116 17, .074 27. .119 21, .576 1.00 14. .58 c
ATOM 900 CZ TYR A 116 16, .674 27, .016 20, .267 1.00 15. .69 c
ATOM 901 OH TYR A 116 15. .326 27, .015 19. .946 1.00 13. .22 O
ATOM 902 N VAL A 117 20, .689 29, .631 23, .048 1.00 17. .46 N
ATOM 903 CA VAL A 117 19, .957 30. .735 23. .679 1.00 13. .96 c
ATOM 904 C VAL A 117 20, .588 32, .097 23, .387 1.00 14. .91 c
ATOM 905 O VAL A 117 19, .864 33, .020 22, .982 1.00 15. .45 o
ATOM 906 CB VAL A 117 19, .824 30, .480 25, .193 1.00 14. .52 c
ATOM 907 CGI VAL A 117 19, .161 31, .623 25, .904 1.00 16, .06 c
ATOM 908 CG2 VAL A 117 18. .994 29, .189 25, .400 1.00 13, .31 c
ATOM 909 N ASN A 118 21. .917 32, .244 23. .509 1.00 18, .31 N
ATOM 910 CA ASN A 118 22. .459 33, .596 23. .271 1.00 14. .39 c
ATOM 911 C ASN A 118 22, .109 34. .178 21. .939 1.00 13. .82 c
ATOM 912 O ASN A 118 21, .577 35. .308 21. .869 1.00 18, .34 O
ATOM 913 CB ASN A 118 23, .952 33. .624 23. .584 1.00 14, .65 c
ATOM 914 CG ASN A 118 24, .168 33, .447 25. .071 1.00 15, .75 c
ATOM 915 ODl ASN A 118 23, .329 33. .421 25, .965 1.00 19, .36 O
ATOM 916 ND2 ASN A 118 25, .470 33, .291 25, .396 1.00 17, .69 N
ATOM 917 N PRO A 119 22, .313 33, .482 20, .856 1.00 13, .44 N
ATOM 918 CA PRO A 119 22 .025 33, .949 19, .513 1.00 12, .82 C
ATOM 919 C PRO A 119 20. .532 34, .203 19, .352 1.00 19. .27 C
ATOM 920 O PRO A 119 20 .144 35, .160 18, .669 1.00 15. .57 O
ATOM 921 CB PRO A 119 22 .616 33, .003 18, .473 1.00 19. .42 C
ATOM 922 CG PRO A 119 23 .256 31. .959 19, .330 1.00 25. .27 C
ATOM 923 CD PRO A 119 23 .073 32, .222 20, .803 1.00 18, .21 c
ATOM 924 N PHE A 120 19 .712 33 .365 19. .971 1.00 16, .00 '
ATOM 925 CA PHE A 120 18 .271 33 .558 19 .941 1.00 17, .20 c
ATOM 926 C PHE A 120 17 .931 34 .921 20 .561 1.00 15, .58 c
ATOM 927 O PHE A 120 17 .244 35 .731 19 .920 1.00 16, .71 O
ATOM 928 CB PHE A 120 17 .575 32 .443 20 .722 1.00 14. .76 c
ATOM 929 CG PHE A 120 16 .127 32 .181 20 .415 1.00 14, .80 c
ATOM 930 CD1 PHE A 120 15 .135 33 .137 20 .606 1.00 13 .11 c ATOM 931 CD2 PHE A 120 15.811 30.899 19.974 1.00 16.69 C
ATOM 932 CE1 PHE A 120 13.826 32.780 20.356 1.00 15.61 C
ATOM 933 CE2 PHE A 120 14.501 30.528 19.727 1.00 14.01 C
ATOM 934 CZ PHE A 120 13.525 31.502 19.905 1.00 15.53 C ATOM 935 N ALA A 121 18.517 35.154 21.734 1.00 14.93 N
ATOM 936 CA ALA A 121 18.220 36.414 22.434 1.00 15.88 c
ATOM 937 C ALA A 121 18.742 37.624 21.686 1.00 17.20 c
ATOM 938 O ALA A 121 18.061 38.658 21.692 1.00 18.44 O
ATOM 939 CB ALA A 121 18.765 36.348 23.837 1.00 16.02 c ATOM 940 N GLN A 122 19.903 37.496 21.070 1.00 19.30 N
ATOM 941 CA GLN A 122 20.493 38.612 20.326 1.00 15.89 c
ATOM 942 C GLN A 122 19.552 39.054 19.218 1.00 19.44 c
ATOM 943 O GLN A 122 19.306 40.256 19.035 1.00 17.37 O
ATOM 944 CB GLN A 122 21.839 38.182 19.716 1.00 17.87 c ATOM 945 CG GLN A 122 22.486 39.243 18.821 1.00 28.60 c
ATOM 946 CD GLN A 122 23.758 38.701 18.187 1.00 38.44 c
ATOM 947 OE1 GLN A 122 24.263 37.620 18.507 1.00 38.79 O
ATOM 948 NE2 GLN A 122 24.324 39.459 17.253 1.00 33.90 N
ATOM 949 N LYS A 123 19.049 38.076 18.443 1.00 17.09 N ATOM 950 CA LYS A 123 18.160 38.404 17.337 1.00 16.59 c
ATOM 951 C LYS A 123 16.855 39.041 17.785 1.00 14.92 c
ATOM 952 O LYS A 123 16.394 40.013 17.186 1.00 16.41 O
ATOM 953 CB LYS A 123 17.793 37.060 16.645 1.00 16.25 c
ATOM 954 CG LYS A 123 18.976 36.600 15.780 1.00 17.30 c ATOM 955 CD LYS A 123 18.545 35.275 15.127 1.00 20.49 c
ATOM 956 CE LYS A 123 19.754 34.575 14.492 1.00 18.08 c
ATOM 957 NZ LYS A 123 20.333 35.361 13.386 1.00 22.16 N
ATOM 958 N LEU A 124 16.276 38.563 18.893 1.00 15.41 N
ATOM 959 CA LEU A 124 15.018 39.180 19.341 1.00 13.86 c ATOM 960 C LEU A 124 15.260 40.546 19.983 1.00 17.17 c
ATOM 961 O LEU A 124 14.435 41.432 19.748 1.00 19.88 O
ATOM 962 CB LEU A 124 14.280 38.258 20.315 1.00 15.51 c
ATOM 963 CG LEU A 124 13.315 37.246 19.683 1.00 15.13 c
ATOM 964 CD1 LEU A 124 14.037 36.293 18.737 1.00 17.75 c ATOM 965 CD2 LEU A 124 12.708 36.415 20.806 1.00 15.78 c
ATOM 966 N LYS A 125 16.333 40.712 20.751 1.00 15.59 N
ATOM 967 CA LYS A 125 16.557 42.023 21.399 1.00 16.00 c
ATOM 968 C LYS A 125 16.931 43.048 20.348 1.00 21.55 c
ATOM 969 O LYS A 125 16.623 44.235 20.538 1.00 21.82 O ATOM 970 CB LYS A 125 17.618 41.910 22.503 1.00 18.83 c
ATOM 971 CG LYS A 125 17.099 41.184 23.743 1.00 20.04 c
ATOM 972 CD LYS A 125 18.175 41.020 24.821 1.00 18.92 c
ATOM 973 CE LYS A 125 17.525 40.401 26.050 1.00 21.03 c
ATOM 974 NZ LYS A 125 18.489 40.092 27.118 1.00 22.21 N ATOM 975 N ALA A 126 17.534 42.650 19.231 1.00 17.28 N
ATOM 976 CA ALA A 126 17.842 43.631 18.166 1.00 13.39 c
ATOM 977 C ALA A 126 16.568 44.077 17.483 1.00 19.73 c
ATOM 978 O ALA A 126 16.429 45.242 17.085 1.00 22.21 o
ATOM 979 CB ALA A 126 18.817 43.020 17.172 1.00 21.36 c ATOM 980 N ALA A 127 15.578 43.182 17.380 1.00 20.52 N
ATOM 981 CA ALA A 127 14.338 43.538 16.686 1.00 21.72 c
ATOM 982 C ALA A 127 13.312 44.074 17.657 1.00 19.05 c
ATOM 983 O ALA A 127 12.205 43.547 17.850 1.00 17.22 'v.
ATOM 984 CB ALA A 127 13.813 42.301 15.934 1.00 15.16 c ATOM 985 N SER A 128 13.624 45.197 18.304 1.00 18.37 N
ATOM 986 CA SER A 128 12.805 45.859 19.306 1.00 22.55 c
ATOM 987 C SER A 128 11.468 46.408 18.805 1.00 20.88 c
ATOM 988 O SER A 128 10.576 46.703 19.612 1.00 19.69 O
ATOM 989 CB SER A 128 13.606 47.005 19.943 1.00 18.62 c ATOM 990 OG ASER A 128 14.055 46.604 21.223 0.30 23.23 O
ATOM 991 OG 1 3SER A 128 14.073 47.950 19.019 0.70 16.43 O
ATOM 992 N ASP A 129 11.327 46.525 17.506 1.00 19.68 N
ATOM 993 CA ASP A 129 10.194 46.960 16.749 1.00 20.35 C ATOM 994 C ASP A 129 9.193 45.823 16.508 1.00 24.26 C
ATOM 995 O ASP A 129 8.088 46.035 16.017 1.00 24.84 O
ATOM 996 CB ASP A 129 10.637 47.474 15.372 1.00 18.77 C
ATOM 997 CG ASP A 129 11.386 46.503 14.498 1.00 24.11 C
ATOM 998 ODl ASP A 129 12.305 45.798 14.988 1.00 22.58 O ATOM 999 OD2 ASP A 129 11.170 46.385 13.273 1.00 23.69 O
ATOM 1000 N VAL A 130 9.631 44.595 16.790 1.00 19.32 N
ATOM 1001 CA VAL A 130 8.732 43.454 16.572 1.00 19.81 C
ATOM 1002 C VAL A 130 8.239 42.838 17.866 1.00 16.92 C
ATOM 1003 O VAL A 130 8.997 42.653 18.818 1.00 17.20 O ATOM 1004 CB VAL A 130 9.533 42.417 15.749 1.00 14.96 C
ATOM 1005 CGI VAL A 130 8.736 41.144 15.490 1.00 22.58 C
ATOM 1006 CG2 VAL A 130 9.963 43.040 14.417 1.00 16.89 C
ATOM 1007 N GLN A 131 6.940 42.453 17.883 1.00 16.00 N
ATOM 1008 CA GLN A 131 6.467 41.776 19.092 1.00 17.10 C ATOM 1009 C GLN A 131 6.631 40.255 18.958 1.00 15.89 C
ATOM 1010 O GLN A 131 6.252 39.764 17.885 1.00 18.07 O
ATOM 1011 CB GLN A 131 4.966 42.099 19.344 1.00 15.42 C
ATOM 1012 CG GLN A 131 4.836 43.607 19.652 1.00 19.47 C
ATOM 1013 CD GLN A 131 5.269 43.973 21.054 1.00 18.68 C ATOM 1014 OE1 GLN A 131 5.002 43.270 22.033 1.00 21.52 O
ATOM 1015 NE2 GLN A 131 5.997 45.089 21.171 1.00 23.09 N
ATOM 1016 N PHE A 132 7.089 39.584 20.007 1.00 14.56 N
ATOM 1017 CA PHE A 132 7.284 38.147 19.930 1.00 15.44 C
ATOM 1018 C PHE A 132 6.559 37.406 21.041 1.00 19.18 C ATOM 1019 O PHE A 132 6.544 37.825 22.201 1.00 16.83 O
ATOM 1020 CB PHE A 132 8.787 37.804 20.110 1.00 13.70 C
ATOM 1021 CG PHE A 132 9.705 38.310 19.036 1.00 12.58 C
ATOM 1022 CD1 PHE A 132 9.937 37.640 17.844 1.00 14.61 C
ATOM 1023 CD2 PHE A 132 10.297 39.565 19.184 1.00 14.89 C ATOM 1024 CE1 PHE A 132 10.763 38.155 16.888 1.00 16.67 C
ATOM 1025 CE2 PHE A 132 11.098 40.101 18.195 1.00 14.44 C
ATOM 1026 CZ PHE A 132 11.377 39.390 17.039 1.00 24.08 C
ATOM 1027 N ALA A 133 5.966 36.272 20.665 1.00 13.43 N
ATOM 1028 CA ALA A 133 5.450 35.323 21.629 1.00 12.38 C ATOM 1029 C ALA A 133 6.337 34.058 21.520 1.00 16.52 c
ATOM 1030 O ALA A 133 6.392 33.482 20.436 1.00 14.68 O
ATOM 1031 CB ALA A 133 4.033 34.835 21.390 1.00 13.99 c
ATOM 1032 N VAL A 134 7.053 33.780 22.595 1.00 13.32 N
ATOM 1033 CA VAL A 134 7.990 32.652 22.516 1.00 14.91 c ATOM 1034 C VAL A 134 7.502 31.562 23.433 1.00 15.83 c
ATOM 1035 O VAL A 134 7.346 31.694 24.636 1.00 14.31 O
ATOM 1036 CB VAL A 134 9.423 33.077 22.932 1.00 14.14 c
ATOM 1037 CGI VAL A 134 10.355 31.869 22.932 1.00 12.93 c
ATOM 1038 CG2 VAL A 134 9.927 34.185 22.031 1.00 15.66 c ATOM 1039 N ILE A 135 7.293 30.362 22.869 1.00 11.12 N
ATOM 1040 CA ILE A 135 6.941 29.189 23.589 1.00 11.50 c
ATOM 1041 C ILE A 135 8.257 28.518 23.987 1.00 12.31 C
ATOM 1042 O ILE A 135 9.110 28.250 23.147 1.00 14.89 G
ATOM 1043 CB ILE A 135 6.038 28.247 22.790 1.00 12.69 C ATOM 1044 CGI ILE A 135 4.654 28.910 22.741 1.00 11.65 C
ATOM 1045 CG2 ILE A 135 6.039 26.855 23.412 1.00 13.80 C
ATOM 1046 CD1 ILE A 135 3.609 28.073 21.999 1.00 13.61 C
ATOM 1047 N LEU A 136 8.344 28.301 25.297 1.00 13.71 N
ATOM 1048 CA LEU A 136 9.575 27.726 25.781 1.00 12.72 C ATOM 1049 c LEU A 136 9.461 26.231 26.045 1.00 10.83 C
ATOM 1050 o LEU A 136 8.802 25.712 26.924 1.00 13.13 O
ATOM 1051 CB LEU A 136 10.030 28.354 27.100 1.00 12.51 C
ATOM 1052 CG LEU A 136 10.209 29.869 27.074 1.00 16.39 C
ATOM 1053 CD1 LEU A 136 10.168 30.365 28.507 1.00 15.36 C
ATOM 1054 CD2 LEU A 136 11.501 30.220 26.353 1.00 18.35 C
ATOM 1055 N GLU A 137 10.284 25.506 25.301 1.00 12.51 N
ATOM 1056 CA GLU A 137 10.564 24.096 25.410 1.00 14.89 C
ATOM 1057 C GLU A 137 9.404 23.159 25.670 1.00 11.61 c
ATOM 1058 O GLU A 137 9.116 22.614 26.758 1.00 13.87 O
ATOM 1059 CB GLU A 137 11.622 23.904 26.533 1.00 12.34 c
ATOM 1060 CG GLU A 137 12.972 24.554 26.230 1.00 13.28 c
ATOM 1061 CD GLU A 137 13.743 23.890 25.071 1.00 12.17 c
ATOM 1062 OE1 GLU A 137 13.360 22.784 24.653 1.00 11.92 O
ATOM 1063 OE2 GLU A 137 14.762 24.465 24.687 1.00 13.65 O
ATOM 1064 N PRO A 138 8.640 22.899 24.631 1.00 12.86 N
ATOM 1065 CA PRO A 138 7.510 21.986 24.623 1.00 8.34 C
ATOM 1066 C PRO A 138 7.864 20.672 25.317 1.00 14.11 c
ATOM 1067 O PRO A 138 8.894 20.035 25.171 1.00 12.67 O
ATOM 1068 CB PRO A 138 7.175 21.749 23.148 1.00 13.80 c
ATOM 1069 CG PRO A 138 7.626 23.075 22.551 1.00 14.20 c
ATOM 1070 CD PRO A 138 8.896 23.480 23.286 1.00 14.92 c
ATOM 1071 N ASP A 139 6.963 20.237 26.190 1.00 13.22 N
ATOM 1072 CA ASP A 139 6.937 19.052 26.998 1.00 14.09 C
ATOM 1073 C ASP A 139 8.046 18.965 28.040 1.00 15.12 C
ATOM 1074 O ASP A 139 8.124 17.912 28.658 1.00 15.93 O
ATOM 1075 CB ASP A 139 6.914 17.744 26.167 1.00 13.10 c
ATOM 1076 CG ASP A 139 5.615 17.654 25.399 1.00 15.49 c
ATOM 1077 ODl ASP A 139 4.615 18.248 25.910 1.00 14.68 O
ATOM 1078 OD2 ASP A 139 5.546 16.987 24.341 1.00 18.06 O
ATOM 1079 N ALA A 140 8.932 19.959 28.186 1.00 14.06 N
ATOM 1080 CA ALA A 140 10.039 19.789 29.147 1.00 13.79 c
ATOM 1081 C ALA A 140 9.464 19.621 30.554 1.00 15.47 c
ATOM 1082 O ALA A 140 9.906 18.741 31.254 1.00 17.78 O
ATOM 1083 CB ALA A 140 11.006 20.969 29.099 1.00 12.43 c
ATOM 1084 N ILE A 141 8.568 20.517 30.944 1.00 15.62 N
ATOM 1085 CA ILE A 141 7.991 20.357 32.313 1.00 14.08 c
ATOM 1086 C ILE A 141 7.253 19.069 32.503 1.00 19.31 c
ATOM 1087 O ILE A 141 7.331 18.423 33.567 1.00 20.35 o
ATOM 1088 CB ILE A 141 7.160 21.607 32.590 1.00 16.62 c
ATOM 1089 CGI ILE A 141 8.134 22.779 32.763 1.00 22.60 c
ATOM 1090 CG2 ILE A 141 6.308 21.455 33.857 1.00 20.87 c
ATOM 1091 CD1 ILE A 141 7.414 24.098 32.915 1.00 22.62 c
ATOM 1092 N GLY A 142 6.559 18.556 31.485 1.00 16.46 N
ATOM 1093 CA GLY A 142 5.894 17.256 31.563 1.00 17.32 c
ATOM 1094 C GLY A 142 6.924 16.182 31.917 1.00 19.41 c
ATOM 1095 O GLY A 142 6.728 15.401 32.840 1.00 18.39 O
ATOM 1096 N ASN A 143 8.024 16.143 31.179 1.00 18.77 N
ATOM 1097 CA ASN A 143 9.090 15.165 31.396 1.00 18.65 C
ATOM 1098 C ASN A 143 9.720 15.333 32.774 1.00 25.02 C
ATOM 1099 O ASN A 143 10.147 14.331 33.374 1.00 24.01 O
ATOM 1100 CB ASN A 143 10.076 15.318 30.241 1.00 16.63 c
ATOM 1101 CG ASN A 143 9.715 14.612 28.954 1.00 15.12 c'
ATOM 1102 ODl ASN A 143 9.886 13.401 28.887 1.00 25.88 O
ATOM 1103 ND2 ASN A 143 9.252 15.382 27.980 1.00 17.49 N
ATOM 1104 N MET A 144 9.786 16.550 33.303 1.00 18.94 N
ATOM 1105 CA MET A 144 10.307 16.798 34.636 1.00 26.82 C
ATOM 1106 C MET A 144 9.372 16.318 35.746 1.00 32.01 C
ATOM 1107 O MET A 144 9.881 15.713 36.711 1.00 35.38 O ATOM 1108 CB MET A 144 10.542 18.287 34.,866 1.00 27.38 c
ATOM 1109 CG MET A 144 11.979 18.760 34. ,828 1.00 37.46 c
ATOM 1110 SD MET A 144 11.961 20.522 34. ,459 1.00 41.27 s
ATOM 1111 CE MET A 144 12.279 20.503 32. .697 1.00 16.91 c
ATOM 1112 N VAL A 145 8.072 16.516 35. ,629 1.00 28.09 N
ATOM 1113 CA VAL A 145 7.098 16.068 36. .618 1.00 27.59 C
ATOM 1114 C VAL A 145 6.868 14.570 36. .679 1.00 34.48 c
ATOM 1115 O VAL A 145 6.650 13.976 37. .744 1.00 34.53 O
ATOM 1116 CB VAL A 145 5.704 16.703 36. ,353 1.00 28.57 c
ATOM 1117 CGI VAL A 145 4.575 16.007 37. ,108 1.00 36.94 c
ATOM 1118 CG2 VAL A 145 5.701 18.182 36. ,679 1.00 30.18 c
ATOM 1119 N THR A 146 6.732 13.920 35. .538 1.00 25.46 N
ATOM 1120 CA THR A 146 6.393 12.500 35. .516 1.00 27.86 C
ATOM 1121 C THR A 146 7.560 11.630 35. .097 1.00 27.16 C
ATOM 1122 O THR A 146 7.452 10.404 35. .049 1.00 31.17 O
ATOM 1123 CB THR A 146 5.176 12.309 34. .591 1.00 31.04 C
ATOM 1124 OG1 THR A 146 5.574 12.739 33. ,275 1.00 24.62 O
ATOM 1125 CG2 THR A 146 3.993 13.150 35, .046 1.00 38.27 C
ATOM 1126 N GLY A 147 8.703 12.234 34. ,779 1.00 22.60 N
ATOM 1127 CA GLY A 147 9.856 11.498 34. ,294 1.00 22.02 C
ATOM 1128 C GLY A 147 10.643 10.820 35. ,411 1.00 22.12 C
ATOM 1129 O GLY A 147 11.517 11.476 35. .968 1.00 25.38 O
ATOM 1130 N THR A 148 10.389 9.547 35. .668 1.00 22.71 N
ATOM 1131 CA THR A 148 11.132 8.866 36. .740 1.00 22.82 C
ATOM 1132 C THR A 148 12.224 7.909 36. .295 1.00 27.70 C
ATOM 1133 O THR A 148 12.851 7.257 37. .145 1.00 24.98 O
ATOM 1134 CB THR A 148 10.158 8.034 37. .602 1.00 26.91 C
ATOM 1135 OG1 THR A 148 9.501 7.109 36. .735 1.00 32.28 O
ATOM 1136 CG2 THR A 148 9.145 8.931 38. .302 1.00 25.46 C
ATOM 1137 N SER A 149 12.449 7.803 34. .991 1.00 24.08 N
ATOM 1138 CA SER A 149 13.513 6.934 34, .489 1.00 21.87 C
ATOM 1139 C SER A 149 14.846 7.513 34, .922 1.00 21.61 C
ATOM 1140 O SER A 149 15.002 8.706 35. .238 1.00 22.03 O
ATOM 1141 CB SER A 149 13.419 6.882 32. .948 1.00 20.36 C
ATOM 1142 OG SER A 149 13.890 8.171 32. .486 1.00 23.85 O
ATOM 1143 N ALA A 150 15.871 6.669 34. .978 1.00 22.79 N
ATOM 1144 CA ALA A 150 17.213 7.091 35, .329 1.00 23.93 C
ATOM 1145 C ALA A 150 17.705 8.217 34, .438 1.00 22.88 C
ATOM 1146 O ALA A 150 18.224 9.216 34, .903 1.00 21.44 O
ATOM 1147 CB ALA A 150 18.141 5.880 35, .220 1.00 27.97 C
ATOM 1148 N PHE A 151 17.467 8.078 33, .129 1.00 23.42 N
ATOM 1149 CA PHE A 151 17.883 9.112 32. .198 1.00 16.87 C
ATOM 1150 C PHE A 151 17.269 10.473 32. .486 1.00 10.90 C
ATOM 1151 O PHE A 151 17.979 11.482 32. .471 1.00 20.09 O
ATOM 1152 CB PHE A 151 17.583 8.620 30. .780 1.00 18.22 C
ATOM 1153 CG PHE A 151 18.153 9.589 29. .751 1.00 18.83 C
ATOM 1154 CD1 PHE A 151 19.497 9.662 29. .502 1.00 18.91 C
ATOM 1155 CD2 PHE A 151 17.293 10.422 29, .056 1.00 21.05 C
ATOM 1156 CE1 PHE A 151 20.013 10.525 28, .570 1.00 19.18 C
ATOM 1157 CE2 PHE A 151 17.784 11.288 28, .099 1.00 20.98 C
ATOM 1158 CZ PHE A 151 19.148 11.362 27, .870 1.00 18.15 C
ATOM 1159 N CYS A 152 15.965 10.573 32, .683 1.00 16.28 N
ATOM 1160 CA CYS A 152 15.344 11.860 33, .014 1.00 15.15 c
ATOM 1161 C CYS A 152 15.785 12.443 34, .358 1.00 18.37 c
ATOM 1162 O CYS A 152 16.001 13.661 34. .510 1.00 20.83 o
ATOM 1163 CB CYS A 152 13.816 11.744 33, .144 1.00 21.04 c
ATOM 1164 SG CYS A 152 12.996 11.728 31, .528 1.00 18.91 s
ATOM 1165 N ARG A 153 15.898 11.539 35, .327 1.00 22.50 N
ATOM 1166 CA ARG A 153 16.290 11.972 36, .679 1.00 18.82 C ATOM 1167 C ARG A 153 17.682 12.565 36.676 1.00 19.45 C
ATOM 1168 O ARG A 153 18.000 13.552 37.359 1.00 22.29 O
ATOM 1169 CB ARG A 153 16.170 10.769 37.639 1.00 22.11 C
ATOM 1170 CG ARG A 153 14.729 10.397 37.953 1.00 23.68 C ATOM 1171 CD ARG A 153 14.613 9.459 39.159 1.00 24.90 C
ATOM 1172 NE ARG A 153 15.024 8.085 38.873 1.00 22.17 N
ATOM 1173 CZ ARG A 153 16.145 7.558 39.389 1.00 19.83 C
ATOM 1174 NH1 ARG A 153 16.919 8.263 40.199 1.00 20.95 N
ATOM 1175 NH2 ARG A 153 16.417 6.317 39.040 1.00 23.59 N ATOM 1176 N ASN A 154 18.555 12.017 35.832 1.00 17.62 N
ATOM 1177 CA ASN A 154 19.891 12.505 35.625 1.00 22.93 C
ATOM 1178 C ASN A 154 19.944 13.851 34.912 1.00 23.27 C
ATOM 1179 O ASN A 154 20.981 14.497 34.968 1.00 27.40 O
ATOM 1180 CB ASN A 154 20.693 11.525 34.745 1.00 31.91 C ATOM 1181 CG ASN A 154 21.708 10.799 35.600 1.00 40.14 C
ATOM 1182 ODl ASN A 154 22.689 11.414 36.026 1.00 39.02 O
ATOM 1183 ND2 ASN A 154 21.455 9.522 35.834 1.00 45.43 N
ATOM 1184 N ALA A 155 18.926 14.179 34.145 1.00 18.21 N
ATOM 1185 CA ALA A 155 18.859 15.400 33.361 1.00 20.94 C ATOM 1186 C ALA A 155 18.123 16.554 34.032 1.00 21.85 C
ATOM 1187 O ALA A 155 18.222 17.717 33.652 1.00 17.04 O
ATOM 1188 CB ALA A 155 18.080 15.044 32.076 1.00 24.09 C
ATOM 1189 N ARG A 156 17.357 16.210 35.068 1.00 20.11 N
ATOM 1190 CA ARG A 156 16.464 17.138 35.759 1.00 26.10 C ATOM 1191 C ARG A 156 17.140 18.440 36.145 1.00 23.61 C
ATOM 1192 O ARG A 156 16.738 19.539 35.711 1.00 19.66 O
ATOM 1193 CB ARG A 156 15.851 16.443 36.986 1.00 22.71 C
ATOM 1194 CG ARG A 156 14.935 17.330 37.849 1.00 22.00 C
ATOM 1195 CD ARG A 156 14.180 16.552 38.884 1.00 33.46 C ATOM 1196 NE ARG A 156 12.937 16.977 39.460 1.00 37.06 N
ATOM 1197 CZ ARG A 156 11.980 17.789 39.076 1.00 36.95 C
ATOM 1198 NH1 ARG A 156 12.104 18.423 37.923 1.00 42.13 N
ATOM 1199 NH2 ARG A 156 10.914 18.011 39.839 1.00 35.77 N
ATOM 1200 N GLY A 157 18.179 18.376 36.968 1.00 23.96 N ATOM 1201 CA GLY A 157 18.945 19.511 37.459 1.00 23.34 C
ATOM 1202 C GLY A 157 19.376 20.503 36.404 1.00 26.04 C
ATOM 1203 O GLY A 157 19.006 21.685 36.305 1.00 18.02 O
ATOM 1204 N PRO A 158 20.199 20.029 35.458 1.00 21.24 N
ATOM 1205 CA PRO A 158 20.703 20.821 34.357 1.00 15.71 C ATOM 1206 C PRO A 158 19.562 21.320 33.473 1.00 16.28 C
ATOM 1207 O PRO A 158 19.615 22.448 32.934 1.00 18.27 O
ATOM 1208 CB PRO A 158 21.654 19.887 33.571 1.00 19.23 C
ATOM 1209 CG PRO A 158 22.064 18.906 34.666 1.00 20.64 C
ATOM 1210 CD PRO A 158 20.797 18.692 35.492 1.00 22.65 C ATOM 1211 N GLN A 159 18.499 20.542 33.322 1.00 17.51 N
ATOM 1212 CA GLN A 159 17.421 21.043 32.433 1.00 20.20 C
ATOM 1213 C GLN A 159 16.707 22.221 33.072 1.00 20.95 C
ATOM 1214 O GLN A 159 16.347 23.201 32.396 1.00 19.79 O
ATOM 1215 CB GLN A 159 16.470 19.942 31.991 1.00 16.22 C ATOM 1216 CG GLN A 159 17.047 18.970 30.976 1.00 15.45 C
ATOM 1217 CD GLN A 159 16.000 17.932 30.596 1.00 17.65 C
ATOM 1218 OE1 GLN A 159 15.070 17.662 31.333 1.00 19.74 O
ATOM 1219 NE2 GLN A 159 16.150 17.353 29.418 1.00 16.86 ri
ATOM 1220 N GLN A 160 16.549 22.207 34.393 1.00 19.49 N ATOM 1221 CA GLN A 160 15.933 23.343 35.084 1.00 20.57 C
ATOM 1222 C GLN A 160 16.804 24.574 34.939 1.00 18.11 C
ATOM 1223 O GLN A 160 16.350 25.689 34.671 1.00 17.46 O
ATOM 1224 CB GLN A 160 15.666 23.065 36.554 1.00 22.41 C
ATOM 1225 CG GLN A 160 14.623 21.977 36.821 1.00 27.14 C ATOM 1226 CD GLN A 160 14.497 21.713 38.312 1.00 33.51 C
ATOM 1227 OE1 GLN A 160 15. 338 22. 146 39. 102 1.00 44. 68 O
ATOM 1228 NE2 GLN A 160 13. 483 20. 991 38. 760 1.00 33. 51 N
ATOM 1229 N GLU A 161 18. 131 24. 381 35. .068 1.00 17. 66 N
ATOM 1230 CA GLU A 161 19. 072 25. 468 34. 873 1.00 18. 15 C
ATOM 1231 C GLU A 161 19. 028 25. ,979 33. ,429 1.00 20. 38 C
ATOM 1232 O GLU A 161 19. 076 27. ,188 33. .196 1.00 20. 25 O
ATOM 1233 CB GLU A 161 20. 503 25. ,022 35. ,222 1.00 20. .40 C
ATOM 1234 CG GLU A 161 21. 530 26. ,108 34. ,926 1.00 26. .49 C
ATOM 1235 CD GLU A 161 22. ,926 25. ,765 35. ,413 1.00 32. ,47 C
ATOM 1236 OE1 GLU A 161 23. ,055 24. .829 36. .231 1.00 29. ,68 o
ATOM 1237 OE2 GLU A 161 23. ,896 26. ,436 34. ,997 1.00 33. ,32 O
ATOM 1238 N ALA A 162 18. ,891 25. ,063 32. ,456 1.00 21. ,33 N
ATOM 1239 CA ALA A 162 18. 805 25. ,494 31. .068 1.00 18. ,84 C
ATOM 1240 C ALA A 162 17. ,588 26. ,379 30. .799 1.00 16. ,13 C
ATOM 1241 O ALA A 162 17. ,703 27. ,406 30. .123 1.00 16. ,11 o
ATOM 1242 CB ALA A 162 18. ,721 24. .318 30. .095 1.00 17. ,53 C
ATOM 1243 N ILE A 163 16. ,436 25. .946 31. .297 1.00 17. ,98 N
ATOM 1244 CA ILE A 163 15. ,206 26. ,713 31. .030 1.00 14. ,97 C
ATOM 1245 C ILE A 163 15. ,241 28. ,062 31. ,757 1.00 18. .57 C
ATOM 1246 O ILE A 163 14. ,916 29. ,148 31. ,234 1.00 16. ,69 o
ATOM 1247 CB ILE A 163 13. ,981 25. .889 31. ,412 1.00 17. ,85 C
ATOM 1248 CGI ILE A 163 13. ,861 24. .602 30. .579 1.00 19. .40 C
ATOM 1249 CG2 ILE A 163 12. .753 26. ,776 31. .167 1.00 22. ,22 c
ATOM 1250 CD1 ILE A 163 12. ,644 23. .748 30. .917 1.00 18. ,79 c
ATOM 1251 N GLY A 164 15. ,741 28. .003 33. .013 1.00 20. .77 N
ATOM 1252 CA GLY A 164 15. ,870 29, .267 33. .766 1.00 17. .85 C
ATOM 1253 C GLY A 164 16. .780 30. .222 33. .012 1.00 15. ,29 C
ATOM 1254 O GLY A 164 16. .565 31. .430 33. .021 1.00 20. ,23 o
ATOM 1255 N TYR A 165 17. ,854 29. .674 32. .412 1.00 17. .68 N
ATOM 1256 CA TYR A 165 18. .766 30. .488 31. .651 1.00 14. .10 C
ATOM 1257 C TYR A 165 18. .089 31. .131 30, .436 1.00 17. .53 C
ATOM 1258 O TYR A 165 18. .269 32. .328 30, .188 1.00 19. .89 o
ATOM 1259 CB TYR A 165 20, .018 29, .700 31. .213 1.00 12. .38 c
ATOM 1260 CG TYR A 165 20, .983 30, .576 30. .444 1.00 17. .60 c
ATOM 1261 CD1 TYR A 165 21. .894 31, .360 31. .178 1.00 19, .80 C
ATOM 1262 CD2 TYR A 165 21. .050 30, .678 29. .074 1.00 18. .96 C
ATOM 1263 CE1 TYR A 165 22, .771 32. .196 30. .527 1.00 20, .15 C
ATOM 1264 CE2 TYR A 165 21, .922 31. .525 28. .423 1.00 20, .01 c
ATOM 1265 CZ TYR A 165 22. .809 32, .288 29, .158 1.00 17, .49 C
ATOM 1266 OH TYR A 165 23. .706 33. .124 28, .549 1.00 21, .23 o
ATOM 1267 N ALA A 166 17. .258 30. .328 29, .773 1.00 16. .23 N
ATOM 1268 CA ALA A 166 16, .539 30. .882 28, .616 1.00 16. .91 C
ATOM 1269 C ALA A 166 15, .573 31, .997 29, .042 1.00 15. .92 C
ATOM 1270 O ALA A 166 15, .608 33, .036 28. .368 1.00 16. .18 O
ATOM 1271 CB ALA A 166 15, .810 29, .697 27. .993 1.00 15, .30 C
ATOM 1272 N ILE A 167 14, .870 31, .833 30, .160 1.00 16, .04 N
ATOM 1273 CA ILE A 167 13, .983 32, .893 30, .634 1.00 16, .03 C
ATOM 1274 C ILE A 167 14, .836 34, .112 30, .968 1.00 17, .37 C
ATOM 1275 O ILE A 167 14. .478 35 .231 30. .619 1.00 16, .76 O
ATOM 1276 CB ILE A 167 13 .211 32 .456 31, .886 1.00 14, .55 C
ATOM 1277 CGI ILE A 167 12 .262 31 .286 31 .540 1.00 20, .02 C
ATOM 1278 CG2 ILE A 167 12 .380 33 .571 32 .515 1.00 16, .28 C
ATOM 1279 CD1 ILE A 167 11 .683 30 .536 32 .720 1.00 18, .04 C
ATOM 1280 N SER A 168 15. .938 33 .863 31. .701 1.00 19, .53 N
ATOM 1281 CA SER A 168 16 .787 34 .999 32 .105 1.00 21, .13 C
ATOM 1282 C SER A 168 17 .281 35 .813 30 .932 1.00 19, .30 C
ATOM 1283 O SER A 168 17 .511 37 .031 31 .058 1.00 19, .82 O
ATOM 1284 CB SER A 168 17 .975 34 .532 32 .958 1.00 21. .41 C ATOM 1285 OG SER A 168 19.078 33.943 32.267 1.00 20.79 O
ATOM 1286 N GLN A 169 17.566 35.192 29.786 1.00 15.41 N
ATOM 1287 CA GLN A 169 18.084 35.921 28.646 1.00 14.97 C
ATOM 1288 C GLN A 169 17.052 36.594 27.745 1.00 15.50 C ATOM 1289 O GLN A 169 17.444 37.311 26.826 1.00 17.12 O
ATOM 1290 CB GLN A 169 18.887 34.976 27.726 1.00 16.43 C
ATOM 1291 CG GLN A 169 20.239 34.598 28.343 1.00 18.51 C
ATOM 1292 CD GLN A 169 21.179 35.766 28.084 1.00 17.43 C
ATOM 1293 OE1 GLN A 169 21.376 36.223 26.946 1.00 21.30 O ATOM 1294 NE2 GLN A 169 21.702 36.323 29.165 1.00 18.42 N
ATOM 1295 N LEU A 170 15.767 36.358 27.972 1.00 16.44 N
ATOM 1296 CA LEU A 170 14.716 36.849 27.106 1.00 18.88 C
ATOM 1297 C LEU A 170 13.745 37.780 27.801 1.00 19.41 C
ATOM 1298 O LEU A 170 12.524 37.701 27.642 1.00 18.95 O ATOM 1299 CB LEU A 170 13.946 35.619 26.545 1.00 16.72 c
ATOM 1300 CG LEU A 170 14.844 34.795 25.607 1.00 12.75 c
ATOM 1301 CD1 LEU A 170 14.174 33.440 25.307 1.00 12.96 c
ATOM 1302 CD2 LEU A 170 15.157 35.480 24.300 1.00 15.61 c
ATOM 1303 N GLN A 171 14.283 38.632 28.694 1.00 18.55 N ATOM 1304 CA GLN A 171 13.418 39.609 29.362 1.00 18.48 c
ATOM 1305 C GLN A 171 13.442 40.916 28.568 1.00 20.27 c
ATOM 1306 O GLN A 171 14.508 41.531 28.466 1.00 22.91 O
ATOM 1307 CB GLN A 171 13.958 39.868 30.763 1.00 18.70 c
ATOM 1308 CG GLN A 171 13.960 38.733 31.738 1.00 20.71 c ATOM 1309 CD GLN A 171 12.579 38.204 32.086 1.00 28.28 c
ATOM 1310 OE1 GLN A 171 11.751 38.921 32.646 1.00 26.82 O
ATOM 1311 NE2 GLN A 171 12.355 36.945 31.756 1.00 18.32 N
ATOM 1312 N ALA A 172 12.326 41.329 27.990 1.00 22.62 N
ATOM 1313 CA ALA A 172 12.253 42.585 27.236 1.00 18.98 c ATOM 1314 C ALA A 172 10.780 42.954 27.087 1.00 23.47 c
ATOM 1315 O ALA A 172 9.943 42.041 27.155 1.00 22.25 O
ATOM 1316 CB ALA A 172 12.896 42.466 25.877 1.00 19.85 c
ATOM 1317 N SER A 173 10.416 44.223 26.924 1.00 21.36 N
ATOM 1318 CA SER A 173 8.994 44.537 26.823 1.00 25.83 c ATOM 1319 C SER A 173 8.326 44.033 25.553 1.00 24.83 c
ATOM 1320 O SER A 173 7.092 43.994 25.534 1.00 22.13 O
ATOM 1321 CB SER A 173 8.821 46.056 26.951 1.00 23.74 c
ATOM 1322 OG SER A 173 9.243 46.705 25.773 1.00 29.00 O
ATOM 1323 N HIS A 174 9.065 43.646 24.512 1.00 17.75 N ATOM 1324 CA HIS A 174 8.492 43.188 23.265 1.00 17.50 C
ATOM 1325 C HIS A 174 8.600 41.658 23.132 1.00 16.39 C
ATOM 1326 O HIS A 174 8.197 41.102 22.124 1.00 17.58 O
ATOM 1327 CB HIS A 174 9.116 43.875 22.050 1.00 17.07 C
ATOM 1328 CG HIS A 174 10.579 43.533 21.916 1.00 20.56 C ATOM 1329 ND1 HIS A 174 11.527 43.924 22.837 1.00 21.16 N
ATOM 1330 CD2 HIS A 174 11.226 42.822 20.967 1.00 20.15 C
ATOM 1331 CE1 HIS A 174 12.711 43.476 22.448 1.00 13.95 C
ATOM 1332 NE2 HIS A 174 12.559 42.762 21.333 1.00 18.66 N
ATOM 1333 N ILE A 175 9.091 41.040 24.204 1.00 19.18 N ATOM 1334 CA ILE A 175 9.207 39.573 24.216 1.00 15.87 C
ATOM 1335 C ILE A 175 8.289 39.008 25.292 1.00 17.27 C
ATOM 1336 O ILE A 175 8.399 39.307 26.485 1.00 18.00 O
ATOM 1337 CB ILE A 175 10.648 39.123 24.522 1.00 23.04 d
ATOM 1338 CGI ILE A 175 11.644 39.643 23.490 1.00 19.39 C ATOM 1339 CG2 ILE A 175 10.705 37.589 24.597 1.00 17.36 C
ATOM 1340 CD1 ILE A 175 13.104 39.351 23.876 1.00 16.58 C
ATOM 1341 N HIS A 176 7.338 38.143 24.885 1.00 15.25 N
ATOM 1342 CA HIS A 176 6.341 37.569 25.775 1.00 18.06 C
ATOM 1343 C HIS A 176 6.522 36.060 25.891 1.00 17.50 C ATOM 1344 O HIS A 176 6.411 35.373 24.891 1.00 19.93 O
ATOM 1345 CB HIS A 176 4.948 37.913 25.227 1.00 20.20 C
ATOM 1346 CG HIS A 176 4.893 39.398 24.933 1.00 17.31 C
ATOM 1347 ND1 HIS A 176 4.705 40.329 25.945 1.00 23.89 N ATOM 1348 CD2 HIS A 176 5.080 40.067 23.785 1.00 16.22 C
ATOM 1349 CE1 HIS A 176 4.746 41.528 25.369 1.00 19.91 C
ATOM 1350 NE2 HIS A 176 4.966 41.415 24.080 1.00 17.72 N
ATOM 1351 N LEU A 177 6.930 35.639 27.079 1.00 16.15 N
ATOM 1352 CA LEU A 177 7.302 34.237 27.266 1.00 20.26 C ATOM 1353 C LEU A 177 6.172 33.394 27.776 1.00 18.87 C
ATOM 1354 O LEU A 177 5.507 33.721 28.751 1.00 17.54 O
ATOM 1355 CB LEU A 177 8.505 34.179 28.213 1.00 16.68 C
ATOM 1356 CG LEU A 177 9.750 34.949 27.759 1.00 20.48 C
ATOM 1357 CD1 LEU A 177 10.829 34.890 28.838 1.00 23.84 C ATOM 1358 CD2 LEU A 177 10.287 34.407 26.443 1.00 19.91 C
ATOM 1359 N TYR A 178 5.971 32.234 27.121 1.00 15.13 N
ATOM 1360 CA TYR A 178 4.968 31.268 27.522 1.00 16.57 C
ATOM 1361 C TYR A 178 5.682 29.949 27.741 1.00 13.83 C
ATOM 1362 O TYR A 178 6.202 29.325 26.803 1.00 16.26 0 ATOM 1363 CB TYR A 178 3.884 31.164 26.436 1.00 13.81 C
ATOM 1364 CG TYR A 178 3.010 32.412 26.288 1.00 14.31 C
ATOM 1365 CD1 TYR A 178 1.871 32.534 27.089 1.00 13.04 C
ATOM 1366 CD2 TYR A 178 3.321 33.410 25.402 1.00 14.39 C
ATOM 1367 CE1 TYR A 178 1.042 33.643 26.958 1.00 13.10 C ATOM 1368 CE2 TYR A 178 2.528 34.539 25.279 1.00 14.79 C
ATOM 1369 CZ TYR A 178 1.403 34.639 26.063 1.00 16.55 C
ATOM 1370 OH TYR A 178 0.641 35.766 25.884 1.00 17.40 0
ATOM 1371 N LEU A 179 5.784 29.489 28.974 1.00 13.35 N
ATOM 1372 CA LEU A 179 6.462 28.249 29.352 1.00 17.07 C ATOM 1373 C LEU A 179 5.542 27.065 29.143 1.00 19.44 C
ATOM 1374 O LEU A 179 4.405 27.017 29.634 1.00 16.44 o
ATOM 1375 CB LEU A 179 6.963 28.405 30.803 1.00 16.46 C
ATOM 1376 CG LEU A 179 7.666 27.233 31.449 1.00 19.83 C
ATOM 1377 CD1 LEU A 179 8.937 26.875 30.675 1.00 15.49 C ATOM 1378 CD2 LEU A 179 8.015 27.580 32.907 1.00 23.07 C
ATOM 1379 N ASP A 180 6.029 26.088 28.354 1.00 14.36 N
ATOM 1380 CA ASP A 180 5.125 25.000 27.961 1.00 15.05 C
ATOM 1381 C ASP A 180 4.761 24.105 29.111 1.00 13.43 C
ATOM 1382 O ASP A 180 5.631 23.795 29.919 1.00 14.07 0 ATOM 1383 CB ASP A 180 5.781 24.192 26.800 1.00 12.47 C
ATOM 1384 CG ASP A 180 4.684 23.234 26.354 1.00 13.76 c
ATOM 1385 ODl ASP A 180 3.794 23.702 25.682 1.00 13.82 0
ATOM 1386 OD2 ASP A 180 4.713 22.059 26.727 1.00 13.22 0
ATOM 1387 N VAL A 181 3.467 23.779 29.265 1.00 13.82 N ATOM 1388 CA VAL A 181 3.027 22.841 30.278 1.00 16.72 C
ATOM 1389 C VAL A 181 2.236 21.692 29.648 1.00 15.67 C
ATOM 1390 O VAL A 181 1.300 21.117 30.214 1.00 16.61 o
ATOM 1391 CB VAL A 181 2.254 23.512 31.436 1.00 15.74 c
ATOM 1392 CGI VAL A 181 3.113 24.562 32.107 1.00 16.55 C ATOM 1393 CG2 VAL A 181 1.043 24.270 30.879 1.00 14.73 C
ATOM 1394 N ALA A 182 2.766 21.112 28.559 1.00 15.84 N
ATOM 1395 CA ALA A 182 2.257 19.878 27.954 1.00 11.85 C
ATOM 1396 C ALA A 182 0.796 19.975 27.567 1.00 17.64 d
ATOM 1397 O ALA A 182 0.425 20.845 26.796 1.00 16.55 0 ATOM 1398 CB ALA A 182 2.536 18.728 28.928 1.00 13.37 C
ATOM 1399 N ASN A 183 -0.074 19.076 28.056 1.00 15.15 N
ATOM 1400 CA ASN A 183 -1.496 19.177 27.691 1.00 16.26 C
ATOM 1401 C ASN A 183 -2.265 18.644 28.894 1.00 17.26 C
ATOM 1402 O ASN A 183 -1.684 17.994 29.777 1.00 18.17 o ATOM 1403 CB ASN A 183 1.835 18.454 26.401 1.00 16.35 C
ATOM 1404 CG ASN A 183 1.767 16.965 26. 559 1.00 17. 94 c
ATOM 1405 ODl ASN A 183 2.792 16.319 26. 797 1.00 16. 51 o
ATOM 1406 ND2 ASN A 183 0.582 16.382 26. 436 1.00 18. 25 N
ATOM 1407 N GLY A 184 3.592 18.844 28. 847 1.00 16. 86 N
ATOM 1408 CA GLY A 184 4.388 18.416 30. 015 1.00 19. 04 C
ATOM 1409 C GLY A 184 4.359 16.935 30. 329 1.00 21. 08 c
ATOM 1410 O GLY A 184 4.483 16.535 31. 490 1.00 19. 31 o
ATOM 1411 N GLY A 185 4.123 16.070 29. 349 1.00 15. 52 N
ATOM 1412 CA GLY A 185 4.026 14.643 29. 525 1.00 18. 46 c
ATOM 1413 C GLY A 185 2.809 14.180 30. 305 1.00 17. 75 c
ATOM 1414 O GLY A 185 2.746 13.069 30. 846 1.00 22. 14 o
ATOM 1415 N TRP A 186 1.764 14.986 30. 239 1.00 15 80 N
ATOM 1416 CA TRP A 186 0.519 14.664 30. 916 1.00 18 17 c
ATOM 1417 C TRP A 186 0.515 15.232 32. 333 1.00 24. 27 c
ATOM 1418 O TRP A 186 0.289 14.510 33. 294 1.00 23. 57 o
ATOM 1419 CB TRP A 186 0.639 15.315 30. 122 1.00 17. 51 c
ATOM 1420 CG TRP A 186 2.016 14.820 30. 460 1.00 18. 20 c
ATOM 1421 CD1 TRP A 186 2.509 14.350 31. 646 1.00 20 95 c
ATOM 1422 CD2 TRP A 186 3.143 14.779 29 546 1.00 15 73 c
ATOM 1423 NE1 TRP A 186 3.840 13.989 31 533 1.00 21 92 N
ATOM 1424 CE2 TRP A 186 4.236 14.248 30 235 1.00 19 99 c
ATOM 1425 CE3 TRP A 186 3.305 15.112 28 191 1.00 20 33 c
ATOM 1426 CZ2 TRP A 186 5.493 14.056 29 657 1.00 22 00 c
ATOM 1427 CZ3 TRP A 186 4.558 14.913 27 629 1.00 20 80 c
ATOM 1428 CH2 TRP A 186 5.640 14.413 28 347 1.00 17 58 c
ATOM 1429 N LEU A 187 0.720 16.532 32 461 1.00 19 08 N
ATOM 1430 CA LEU A 187 0.550 17.251 33 706 1.00 17 71 c
ATOM 1431 C LEU A 187 1.826 17.878 34 279 1.00 24 49 c
ATOM 1432 O LEU A 187 1.705 18.631 35 261 1.00 21 87 o
ATOM 1433 CB LEU A 187 0.449 18.392 33 475 1.00 17 69 c
ATOM 1434 CG LEU A 187 1.845 17.972 32 991 1.00 19 27 c
ATOM 1435 CD1 LEU A 187 2.755 19.184 32 845 1.00 18 62 c
ATOM 1436 CD2 LEU A 187 2.406 16.956 33 963 1.00 17 99 c
ATOM 1437 N GLY A 188 2.936 17.551 33 659 1.00 18 10 N
ATOM 1438 CA GLY A 188 4.232 18.107 34 068 1.00 21 .65 c
ATOM 1439 C GLY A 188 ■4.939 17.303 35 143 1.00 21 .97 c
ATOM 1440 O GLY A 188 ■5.921 17.793 35 701 1.00 24 .01 o
ATOM 1441 N TRP A 189 ■4.503 16.086 35 398 1.00 22 .20 N
ATOM 1442 CA TRP A 189 ■5.096 15.289 36 469 1.00 22 .87 c
ATOM 1443 C TRP A 189 4.970 16.007 37 799 1.00 25 .04 c
ATOM 1444 O TRP A 189 ■4.080 16.805 38 040 1.00 27 .88 o
ATOM 1445 CB TRP A 189 ■4.314 13.975 36 627 1.00 27 .16 c
ATOM 1446 CG TRP A 189 ■4.390 13.238 35 .316 1.00 22 .25 c
ATOM 1447 CD1 TRP A 189 ■3.421 13.194 34 .350 1.00 25 .61 c
ATOM 1448 CD2 TRP A 189 ■5.499 12.487 34 .827 1.00 29 .01 c
ATOM 1449 NE1 TRP A 189 ■3.871 12.429 33 .293 1.00 23 .98 N
ATOM 1450 CE2 TRP A 189 ■5.137 11.991 33 .560 1.00 28 .33 c
ATOM 1451 CE3 TRP A 189 ■6.778 12.198 35 .343 1.00 27 .34 c
ATOM 1452 CZ2 TRP A 189 ■5.994 11.197 32 .797 1.00 25 .20 c
ATOM 1453 CZ3 TRP A 189 ■7.609 11.402 34 .572 1.00 36 .57 c
ATOM 1454 CH2 TRP A 189 -7.230 10.916 33 .313 1.00 33 .11 c
ATOM 1455 N ALA A 190 -5.857 15.619 38 .712 1.00 29 .58 ' J
ATOM 1456 CA ALA A 190 -5.823 16.164 40 .069 1.00 23 .81 c
ATOM 1457 C ALA A 190 -4.469 16.087 40 .736 1.00 21 .28 c
ATOM 1458 O ALA A 190 •3.950 17.088 41 .228 1.00 31 .06 o
ATOM 1459 CB ALA A 190 -6.849 15.334 40 .862 1.00 29 .66 c
ATOM 1460 N ASP A 191 -3.855 14.912 40 .801 1.00 23 .12 N
ATOM 1461 CA ASP A 191 -2.557 14.712 41 .428 1.00 27 .43 c ATOM 1462 C ASP A 191 1.385 15.277 40.,632 1.00 25.,12 C
ATOM 1463 O ASP A 191 0.266 15.091 41. .114 1.00 27. ,19 o
ATOM 1464 CB ASP A 191 2.325 13.225 41. ,691 1.00 32. .82 c
ATOM 1465 CG ASP A 191 1.922 12.405 40. ,483 1.00 39. ,62 C
ATOM 1466 ODl ASP A 191 2.175 12.787 39. ,317 1.00 36. ,24 O
ATOM 1467 OD2 ASP A 191 1.324 11.319 40. ,701 1.00 38. .36 O
ATOM 1468 N LYS A 192 1.604 15.905 39. ,475 1.00 26. .92 N
ATOM 1469 CA LYS A 192 0.546 16.487 38. ,698 1.00 24. .87 C
ATOM 1470 C LYS A 192 0.518 18.003 38. ,637 1.00 24. ,18 C
ATOM 1471 O LYS A 192 0.548 18.530 38. .317 1.00 23. ,32 O
ATOM 1472 CB LYS A 192 0.617 16.067 37. .212 1.00 25. ,77 C
ATOM 1473 CG LYS A 192 0.373 14.587 36. .992 1.00 29. ,05 C
ATOM 1474 CD LYS A 192 1.095 14.275 37. .240 1.00 27. ,96 C
ATOM 1475 CE LYS A 192 1.222 13.128 38. ,227 1.00 45. .28 c
ATOM 1476 NZ LYS A 192 0.408 11.964 37. ,780 1.00 39. ,91 N
ATOM 1477 N LEU A 193 1.596 18.697 38. ,966 1.00 25. ,73 N
ATOM 1478 CA LEU A 193 1.610 20.157 38. ,900 1.00 21. ,89 C
ATOM 1479 C LEU A 193 0.630 20.856 39. ,818 1.00 25. ,66 C
ATOM 1480 O LEU A 193 0.012 21.880 39. ,460 1.00 21. ,93 O
ATOM 1481 CB LEU A 193 3.027 20.671 39. .198 1.00 28. ,06 C
ATOM 1482 CG LEU A 193 4.184 20.155 38. ,357 1.00 30. ,24 c
ATOM 1483 CD1 LEU A 193 5.493 20.353 39. .123 1.00 29. .65 c
ATOM 1484 CD2 LEU A 193 •4.248 20.844 37. .006 1.00 29. ,18 C
ATOM 1485 N GLU A 194 ■0.506 20.349 41. .057 1.00 25. .45 N
ATOM 1486 CA GLU A 194 0.444 21.002 41, .980 1.00 28. .77 C
ATOM 1487 C GLU A 194 1.888 20.693 41, .663 1.00 23. .06 C
ATOM 1488 O GLU A 194 2.726 21.586 41, .561 1.00 24. .93 O
ATOM 1489 CB GLU A 194 0.116 20.784 43. .452 1.00 29. .05 C
ATOM 1490 CG GLU A 194 1.144 21.554 43. .846 1.00 30. .23 C
ATOM 1491 CD GLU A 194 •0.983 23.063 43. .816 1.00 25. .96 C
ATOM 1492 OE1 GLU A 194 0.158 23.580 43, .710 1.00 28. .60 O
ATOM 1493 OE2 GLU A 194 ■2.043 23.728 43. .906 1.00 25. .23 o
ATOM 1494 N PRO A 195 2.227 19.456 41, ,360 1.00 23. .57 N
ATOM 1495 CA PRO A 195 3.575 19.085 40. .953 1.00 22. .27 C
ATOM 1496 C PRO A 195 3.960 19.921 39, .737 1.00 24. ,12 C
ATOM 1497 O PRO A 195 5.112 20.339 39. .663 1.00 26. .09 o
ATOM 1498 CB PRO A 195 3.555 17.581 40. .620 1.00 26, .84 C
ATOM 1499 CG PRO A 195 2.402 17.142 41. .492 1.00 27. .05 C
ATOM 1500 CD PRO A 195 1.377 18.276 41. .509 1.00 23. .97 C
ATOM 1501 N THR A 196 3.011 20.243 38. .851 1.00 24, .28 N
ATOM 1502 CA THR A 196 3.316 21.124 37, .717 1.00 25. .48 C
ATOM 1503 C THR A 196 3.610 22.543 38, .149 1.00 23. .30 C
ATOM 1504 O THR A 196 4.576 23.199 37. .736 1.00 25, .84 o
ATOM 1505 CB THR A 196 2.137 21.128 36. .715 1.00 20. .97 C
ATOM 1506 OG1 THR A 196 1.985 19.758 36. .314 1.00 28, .42 o
ATOM 1507 CG2 THR A 196 2.446 21.981 35. .505 1.00 24. .74 C
ATOM 1508 N ALA A 197 2.802 23.097 39. .073 1.00 22, .38 N
ATOM 1509 CA ALA A 197 3.073 24.439 39. .568 1.00 18, .61 C
ATOM 1510 C ALA A 197 4.376 24.556 40. .331 1.00 17, .24 C
ATOM 1511 O ALA A 197 5.035 25.590 40, .273 1.00 21, .98 o
ATOM 1512 CB ALA A 197 1.914 24.910 40, .464 1.00 22, .57 C
ATOM 1513 N GLN A 198 4.751 23.492 41, .045 1.00 25, .96 N
ATOM 1514 CA GLN A 198 5.985 23.455 41, .814 1.00 24. .97 C
ATOM 1515 C GLN A 198 7.186 23.526 40, .870 1.00 24. .11 C
ATOM 1516 O GLN A 198 8.171 24.217 41. .114 1.00 25, .56 o
ATOM 1517 CB GLN A 198 6.050 22.185 42. .683 1.00 28, .98 C
ATOM 1518 CG GLN A 198 7.336 22.134 43. .531 1.00 24, .27 C
ATOM 1519 CD GLN A 198 7.314 23.356 44, .454 1.00 34. .76 C
ATOM 1520 OE1 GLN A 198 6.362 23.450 45, .232 1.00 36, .44 o ATOM 1521 NE2 GLN A 198 8.272 24..266 44.,352 1.00 38.,30 N
ATOM 1522 N GLU A 199 7.066 22. .768 39. ,768 1.00 25. .95 N
ATOM 1523 CA GLU A 199 8.129 22. .788 38. ,753 1.00 25. .16 C
ATOM 1524 C GLU A 199 8.329 24. .172 38. ,183 1.00 21. .81 C
ATOM 1525 O GLU A 199 9.475 24. .628 38. ,023 1.00 26. .10 O
ATOM 1526 CB GLU A 199 7.821 21. ,778 37. ,656 1.00 27. .77 C
ATOM 1527 CG GLU A 199 9.018 21. .058 37. ,068 1.00 32. .81 C
ATOM 1528 CD GLU A 199 10.146 20. ,739 38. ,020 1.00 36. .59 c
ATOM 1529 OE1 GLU A 199 9.946 20. ,366 39. .186 1.00 33. .97 O
ATOM 1530 OE2 GLU A 199 11.309 20. ,869 37. .542 1.00 37. ,28 O
ATOM 1531 N VAL A 200 7.248 24. ,875 37. .829 1.00 21. ,28 N
ATOM 1532 CA VAL A 200 7.337 26. ,244 37. ,348 1.00 17. ,50 C
ATOM 1533 C VAL A 200 7.929 27. ,150 38. ,425 1.00 18. .55 c
ATOM 1534 O VAL A 200 8.756 27. .994 38. .109 1.00 22. .64 o
ATOM 1535 CB VAL A 200 5.925 26. ,698 36. ,913 1.00 20. .34 c
ATOM 1536 CGI VAL A 200 5.890 28. ,166 36. ,596 1.00 18. .70 c
ATOM 1537 CG2 VAL A 200 5.443 25. .853 35. ,727 1.00 20. .27 c
ATOM 1538 N ALA A 201 7.481 26. .973 39. ,688 1.00 22. ,75 N
ATOM 1539 CA ALA A 201 8.056 27. .851 40. .711 1.00 23. ,99 C
ATOM 1540 C ALA A 201 9.574 27. .628 40. .801 1.00 21. ,12 C
ATOM 1541 O ALA A 201 10.304 28. .619 40. .901 1.00 25. ,72 O
ATOM 1542 CB ALA A 201 7.402 27. ,722 42. ,071 1.00 31. ,11 c
ATOM 1543 N THR A 202 10.037 26. .397 40. .827 1.00 21. ,45 N
ATOM 1544 CA THR A 202 11.468 26. ,099 40. .906 1.00 26. ,32 C
ATOM 1545 C THR A 202 12.229 26. ,681 39. .733 1.00 26. .11 C
ATOM 1546 O THR A 202 13.303 27. .249 39. .932 1.00 27. ,66 o
ATOM 1547 CB THR A 202 11.678 24. ,581 40. .980 1.00 26. ,18 c
ATOM 1548 OG1 THR A 202 11.067 24. ,107 42. .183 1.00 30. ,40 o
ATOM 1549 CG2 THR A 202 13.147 24. .200 40. .939 1.00 27. ,67 c
ATOM 1550 N ILE A 203 11.723 26, .511 38. .504 1.00 24. .82 N
ATOM 1551 CA ILE A 203 12.363 27. .083 37. .334 1.00 21. .56 C
ATOM 1552 C ILE A 203 12.438 28. ,596 37, .366 1.00 24. .19 C
ATOM 1553 O ILE A 203 13.453 29. .168 36. .940 1.00 25. ,72 O
ATOM 1554 CB ILE A 203 11.645 26. .649 36. .030 1.00 21. ,53 c
ATOM 1555 CGI ILE A 203 12.036 25. .183 35. .809 1.00 27. ,33 c
ATOM 1556 CG2 ILE A 203 11.963 27. .516 34. .829 1.00 21. .78 c
ATOM 1557 CD1 ILE A 203 11.091 24. .441 34. .901 1.00 23. .73 c
ATOM 1558 N LEU A 204 11.384 29. .267 37. .808 1.00 26. .14 N
ATOM 1559 CA LEU A 204 11.387 30. .726 37. .873 1.00 24. .06 C
ATOM 1560 C LEU A 204 12.383 31. .235 38. .912 1.00 24. .89 C
ATOM 1561 O LEU A 204 13.069 32. .248 38, .691 1.00 28. .09 O
ATOM 1562 CB LEU A 204 9.969 31, .235 38. .164 1.00 26. .98 C
ATOM 1563 CG LEU A 204 9.041 31. .157 36. .934 1.00 24. .81 C
ATOM 1564 CD1 LEU A 204 7.638 31. .604 37, .285 1.00 22. .92 c
ATOM 1565 CD2 LEU A 204 9.587 32. .042 35. .826 1.00 30. .35 c
ATOM 1566 N GLN A 205 12.512 30, .521 40. .037 1.00 28. .00 N
ATOM 1567 CA GLN A 205 13.533 30, .926 41, .015 1.00 29. .64 C
ATOM 1568 C GLN A 205 14.920 30. .924 40, .374 1.00 33. ,03 C
ATOM 1569 O GLN A 205 15.684 31, .869 40, .569 1.00 33. .55 o
ATOM 1570 CB GLN A 205 13.567 30. .012 42, .225 1.00 31, .06 c
ATOM 1571 CG GLN A 205 12.277 29. .942 43, .023 1.00 40. .96 c
ATOM 1572 CD GLN A 205 12.403 28. .925 44, .147 1.00 53, .67 c
ATOM 1573 OE1 GLN A 205 11.542 28. .067 44, .360 1.00 58, .84 o
ATOM 1574 NE2 GLN A 205 13.509 29. .019 44, .879 1.00 57. .55 N
ATOM 1575 N LYS A 206 15.250 29. .884 39, .608 1.00 31, .53 N
ATOM 1576 CA LYS A 206 16.521 29. .777 38, .912 1.00 30, .90 c
ATOM 1577 C LYS A 206 16.725 30. .823 37, .838 1.00 28. .64 c
ATOM 1578 O LYS A 206 17.869 31. .293 37, .679 1.00 35. .87 o
ATOM 1579 CB LYS A 206 16.679 28. .369 38, .307 1.00 30. ,49 c ATOM 1580 CG LYS A 206 16.409 27.316 39.361 1.00 32.33 C
ATOM 1581 CD LYS A 206 17.005 25.969 39.023 1.00 31.07 C
ATOM 1582 CE LYS A 206 16.472 24.899 39.969 1.00 41.01 C
ATOM 1583 NZ LYS A 206 16.780 25.229 41.395 1.00 49.48 N ATOM 1584 N ALA A 207 15.684 31.325 37.196 1.00 25.35 N
ATOM 1585 CA ALA A 207 15.793 32.401 36.215 1.00 25.49 C
ATOM 1586 C ALA A 207 16.070 33.719 36.952 1.00 28.60 C
ATOM 1587 O ALA A 207 16.637 34.636 36.375 1.00 33.48 o
ATOM 1588 CB ALA A 207 14.551 32.572 35.347 1.00 21.82 c ATOM 1589 N GLY A 208 15.672 33.737 38.228 1.00 24.19 N
ATOM 1590 CA GLY A 208 16.054 34.891 39.047 1.00 29.70 c
ATOM 1591 C GLY A 208 14.854 35.556 39.680 1.00 34.18 c
ATOM 1592 O GLY A 208 13.713 35.180 39.440 1.00 34.37 o
ATOM 1593 N ASN A 209 15.136 36.575 40.487 1.00 36.06 N ATOM 1594 CA ASN A 209 14.093 37.337 41.139 1.00 42.26 c
ATOM 1595 C ASN A 209 13.351 38.247 40.168 1.00 37.42 c
ATOM 1596 O ASN A 209 12.116 38.192 40.188 1.00 44.08 0
ATOM 1597 CB ASN A 209 14.620 38.188 42.294 1.00 48.61 c
ATOM 1598 CG ASN A 209 15.196 37.459 43.479 1.00 54.89 c ATOM 1599 ODl ASN A 209 15.546 38.114 44.474 1.00 61.55 o
ATOM 1600 ND2 ASN A 209 15.339 36.141 43.424 1.00 57.53 N
ATOM 1601 N ASN A 210 13.994 39.030 39.320 1.00 38.97 N
ATOM 1602 CA ASN A 210 13.295 39.964 38.445 1.00 39.96 c
ATOM 1603 C ASN A 210 12.741 39.332 37.170 1.00 38.36 c ATOM 1604 O ASN A 210 12.022 39.980 36.417 1.00 42.09 o
ATOM 1605 CB ASN A 210 14.158 41.176 38.091 1.00 39.67 c
ATOM 1606 CG ASN A 210 14.897 41.131 36.777 1.00 51.11 c
ATOM 1607 ODl ASN A 210 15.937 40.479 36.659 1.00 54.23 0
ATOM 1608 ND2 ASN A 210 14.400 41.823 35.755 1.00 48.58 N ATOM 1609 N ALA A 211 13.091 38.082 36.921 1.00 40.09 N
ATOM 1610 CA ALA A 211 12.648 37.337 35.764 1.00 33.43 c
ATOM 1611 C ALA A 211 11.135 37.146 35.739 1.00 31.19 c
ATOM 1612 O ALA A 211 10.524 36.870 36.773 1.00 34.58 0
ATOM 1613 CB ALA A 211 13.297 35.955 35.811 1.00 28.11 c ATOM 1614 N LYS A 212 10.554 37.288 34.545 1.00 25.79 N
ATOM 1615 CA LYS A 212 9.120 36.999 34.492 1.00 24.00 c
ATOM 1616 C LYS A 212 8.812 36.212 33.208 1.00 24.95 c
ATOM 1617 O LYS A 212 9.542 36.287 32.230 1.00 22.45 o
ATOM 1618 CB LYS A 212 8.174 38.183 34.496 1.00 32.81 c ATOM 1619 CG LYS A 212 8.614 39.486 33.883 1.00 43.81 c
ATOM 1620 CD LYS A 212 9.337 40.299 34.942 1.00 53.00 c
ATOM 1621 CE LYS A 212 8.469 41.362 35.589 1.00 60.57 c
ATOM 1622 NZ LYS A 212 9.336 42.506 36.020 1.00 61.75 N
ATOM 1623 N ILE A 213 7.648 35.577 33.278 1.00 20.62 N ATOM 1624 CA ILE A 213 7.049 34.967 32.109 1.00 19.54 c
ATOM 1625 C ILE A 213 5.610 35.517 32.058 1.00 22.44 c
ATOM 1626 O ILE A 213 5.102 35.955 33.109 1.00 19.92 0
ATOM 1627 CB ILE A 213 7.008 33.436 32.102 1.00 20.33 c
ATOM 1628 CGI ILE A 213 6.183 32.871 33.255 1.00 17.85 c ATOM 1629 CG2 ILE A 213 8.462 32.924 32.079 1.00 19.41 c
ATOM 1630 CD1 ILE A 213 6.300 31.354 33.414 1.00 17.47 c
ATOM 1631 N ARG A 214 5.010 35.503 30.868 1.00 17.88 N
ATOM 1632 CA ARG A 214 3.607 35.940 30.819 1.00 18.46 c
ATOM 1633 C ARG A 214 2.685 34.838 31.295 1.00 21.26 c ATOM 1634 O ARG A 214 1.614 35.037 31.864 1.00 17.92 o
ATOM 1635 CB ARG A 214 3.248 36.367 29.389 1.00 19.56 c
ATOM 1636 CG ARG A 214 1.749 36.458 29.110 1.00 23.23 c
ATOM 1637 CD ARG A 214 1.110 37.594 29.907 1.00 18.30 c
ATOM 1638 NE ARG A 214 -0.304 37.719 29.494 1.00 17.36 N ATOM 1639 CZ ARG A 214 -1.084 38.648 30.077 1.00 29.29 C
ATOM 1640 NH1 ARG A 214 -0.615 39.444 31.035 1.00 30.58 N
ATOM 1641 NH2 ARG A 214 -2.352 38.736 29.692 1.00 27.97 N
ATOM 1642 N GLY A 215 3.090 33.592 31.036 1.00 18.68 N
ATOM 1643 CA GLY A 215 2.303 32.450 31.353 1.00 17.92 C
ATOM 1644 C GLY A 215 2.783 31.206 30.594 1.00 17.40 C
ATOM 1645 O GLY A 215 3.971 30.919 30.664 1.00 16.91 O
ATOM 1646 N PHE A 216 1.819 30.432 30.117 1.00 15.76 N
ATOM 1647 CA PHE A 216 2.091 29.062 29.685 1.00 15.22 C
ATOM 1648 C PHE A 216 1.536 28.700 28.315 1.00 21.72 C
ATOM 1649 O PHE A 216 0.615 29.393 27.889 1.00 16.93 o
ATOM 1650 CB PHE A 216 1.454 28.052 30.706 1.00 17.19 C
ATOM 1651 CG PHE A 216 1.805 28.479 32.128 1.00 18.17 C
ATOM 1652 CD1 PHE A 216 3.078 28.261 32.605 1.00 18.71 C
ATOM 1653 CD2 PHE A 216 0.880 29.187 32.900 1.00 15.71 C
ATOM 1654 CE1 PHE A 216 3.463 28.695 33.864 1.00 22.37 c
ATOM 1655 CE2 PHE A 216 1.266 29.606 34.157 1.00 19.25 c
ATOM 1656 CZ PHE A 216 2.536 29.379 34.638 1.00 19.49 c
ATOM 1657 N SER A 217 2.008 27.589 27.734 1.00 15.56 N
ATOM 1658 CA SER A 217 1.369 27.131 26.496 1.00 17.02 c
ATOM 1659 C SER A 217 0.904 25.698 26.741 1.00 14.93 c
ATOM 1660 O SER A 217 1.472 25.017 27.598 1.00 15.08 o
ATOM 1661 CB SER A 217 2.312 27.206 25.291 1.00 21.00 c
ATOM 1662 OG SER A 217 3.536 26.478 25.506 1.00 14.08 o
ATOM 1663 N SER A 218 -0.111 25.257 25.994 1.00 12.72 N
ATOM 1664 CA SER A 218 -0.578 23.873 26.150 1.00 13.00 c
ATOM 1665 C SER A 218 -1.173 23.379 24.842 1.00 13.14 c
ATOM 1666 O SER A 218 -1.507 24.158 23.945 1.00 13.35 0
ATOM 1667 CB SER A 218 -1.578 23.773 27.295 1.00 20.14 c
ATOM 1668 OG i P.SER A 218 -2.810 24.361 26.895 0.50 14.84 o
ATOM 1669 OG ] BSER A 218 -2.018 22.467 27.590 0.50 17.53 o
ATOM 1670 N ASN A 219 -1.256 22.045 24.761 1.00 13.03 N
ATOM 1671 CA ASN A 219 -1.784 21.338 23.606 1.00 11.66 c
ATOM 1672 C ASN A 219 -0.866 21.452 22.392 1.00 14.11 C
ATOM 1673 O ASN A 219 -1.353 21.126 21.273 1.00 14.12 o
ATOM 1674 CB ASN A 219 -3.201 21.817 23.223 1.00 14.10 C
ATOM 1675 CG ASN A 219 -4.080 20.725 22.613 1.00 17.99 C
ATOM 1676 ODl ASN A 219 -4.037 19.626 23.166 1.00 15.33 o
ATOM 1677 ND2 ASN A 219 -4.815 21.094 21.565 1.00 17.07 N
ATOM 1678 N VAL A 220 0.368 21.934 22.552 1.00 13.71 N
ATOM 1679 CA VAL A 220 1.247 22.075 21.386 1.00 11.95 C
ATOM 1680 C VAL A 220 1.538 20.682 20.846 1.00 13.76 C
ATOM 1681 O VAL A 220 1.934 19.740 21.510 1.00 13.52 0
ATOM 1682 CB VAL A 220 2.556 22.805 21.735 1.00 10.00 C
ATOM 1683 CGI VAL A 220 3.448 22.783 20.485 1.00 13.46 C
ATOM 1684 CG2 VAL A 220 2.220 24.204 22.233 1.00 14.70 c
ATOM 1685 N SER A 221 1.255 20.499 19.559 1.00 11.96 N
ATOM 1686 CA SER A 221 1.341 19.261 18.833 1.00 14.66 c
ATOM 1687 C SER A 221 0.313 18.231 19.263 1.00 12.51 c
ATOM 1688 O SER A 221 0.439 17.128 18.744 1.00 16.81 o
ATOM 1689 CB SER A 221 2.723 18.593 18.901 1.00 14.72 c
ATOM 1690 OG SER A 221 3.724 19.605 18.684 1.00 12.62 o
ATOM 1691 N ASN A 222 -0.631 18.601 20.110 1.00 13.47 VI
ATOM 1692 CA ASN A 222 -1.625 17.642 20.572 1.00 14.48 c
ATOM 1693 C ASN A 222 -2.925 17.979 19.829 1.00 12.73 c
ATOM 1694 O ASN A 222 -2.928 18.650 18.818 1.00 13.89 o
ATOM 1695 CB ASN A 222 -1.770 17.526 22.086 1.00 13.91 c
ATOM 1696 CG ASN A 222 -2.016 16.103 22.503 1.00 19.90 c
ATOM 1697 ODl ASN A 222 -3.127 15.605 22.333 1.00 19.28 o ATOM 1698 ND2 ASN A 222 -1.003 15.406 23.038 1.00 18.83 N
ATOM 1699 N TYR A 223 -3.966 17.275 20.257 1.00 13.32 N
ATOM 1700 CA TYR A 223 -5.237 17.270 19.551 1.00 11.77 C
ATOM 1701 c TYR A 223 -6.437 17.515 20.460 1.00 15.77 C ATOM 1702 O TYR A 223 -7.578 17.316 19.988 1.00 16.62 O
ATOM 1703 CB TYR A 223 -5.372 15.864 18.943 1.00 15.06 C
ATOM 1704 CG TYR A 223 -4.199 15.350 18.137 1.00 15.92 C
ATOM 1705 CD1 TYR A 223 -3.132 14.677 18.750 1.00 15.93 C
ATOM 1706 CD2 TYR A 223 -4.146 15.572 16.762 1.00 16.14 C ATOM 1707 CE1 TYR A 223 -2.060 14.243 17.988 1.00 15.58 C
ATOM 1708 CE2 TYR A 223 -3.077 15.117 15.999 1.00 17.85 C
ATOM 1709 CZ TYR A 223 -2.047 14.465 16.639 1.00 16.41 C
ATOM 1710 OH TYR A 223 -0.997 13.959 15.898 1.00 19.26 O
ATOM 1711 N ASN A 224 -6.198 17.896 21.713 1.00 13.31 N ATOM 1712 CA ASN A 224 -7.316 18.118 22.631 1.00 14.52 C
ATOM 1713 C ASN A 224 -8.139 19.326 22.186 1.00 16.01 C
ATOM 1714 O ASN A 224 -7.654 20.246 21.549 1.00 16.80 O
ATOM 1715 CB ASN A 224 -6.786 18.372 24.027 1.00 13.57 C
ATOM 1716 CG ASN A 224 -5.958 17.284 24.658 1.00 12.50 C ATOM 1717 ODl ASN A 224 -6.099 16.139 24.245 1.00 19.32 O
ATOM 1718 ND2 ASN A 224 -5.140 17.615 25.660 1.00 16.34 N
ATOM 1719 N PRO A 225 -9.451 19.241 22.399 1.00 17.76 N
ATOM 1720 CA PRO A 225 -10.332 20.344 22.059 1.00 14.38 C
ATOM 1721 C PRO A 225 -10.173 21.441 23.092 1.00 18.93 C ATOM 1722 O PRO A 225 -9.865 21.169 24.250 1.00 16.45 O
ATOM 1723 CB PRO A 225 -11.751 19.727 22.146 1.00 17.67 C
ATOM 1724 CG PRO A 225 -11.529 18.670 23.188 1.00 20.92 C
ATOM 1725 CD PRO A 225 -10.084 18.178 23.153 1.00 17.10 C
ATOM 1726 N TYR A 226 -10.328 22.677 22.638 1.00 21.84 N ATOM 1727 CA TYR A 226 -10.285 23.838 23.506 1.00 18.19 C
ATOM 1728 C TYR A 226 -11.472 23.772 24.472 1.00 19.97 C
ATOM 1729 O TYR A 226 -11.307 23.726 25.676 1.00 21.67 0
ATOM 1730 CB TYR A 226 -10.317 25.144 22.709 1.00 14.39 C
ATOM 1731 CG TYR A 226 -10.388 26.355 23.619 1.00 17.51 C ATOM 1732 CD1 TYR A 226 -9.335 26.691 24.448 1.00 21.80 C
ATOM 1733 CD2 TYR A 226 -11.509 27.164 23.645 1.00 22.13 C
ATOM 1734 CE1 TYR A 226 -9.367 27.780 25.297 1.00 25.82 c
ATOM 1735 CE2 TYR A 226 -11.561 28.263 24.486 1.00 24.30 c
ATOM 1736 CZ TYR A 226 -10.503 28.573 25.303 1.00 23.10 c ATOM 1737 OH TYR A 226 -10.543 29.646 26.149 1.00 26.30 o
ATOM 1738 N SER A 227 -12.699 23.702 23.944 1.00 23.66 N
ATOM 1739 CA SER A 227 -13.857 23.741 24.842 1.00 24.42 c
ATOM 1740 C SER A 227 -14.978 22.828 24.340 1.00 23.09 c
ATOM 1741 O SER A 227 -15.376 23.033 23.193 1.00 29.17 0 ATOM 1742 CB SER A 227 -14.383 25.186 24.890 1.00 25.47 c
ATOM 1743 OG SER A 227 -15.470 25.316 25.798 1.00 37.46 0
ATOM 1744 N THR A 228 -15.357 21.875 25.167 1.00 27.13 N
ATOM 1745 CA THR A 228 -16.464 21.001 24.769 1.00 28.02 c
ATOM 1746 C THR A 228 -17.186 20.456 25.988 1.00 23.08 c ATOM 1747 O THR A 228 -16.696 20.174 27.071 1.00 27.84 o
ATOM 1748 CB THR A 228 -16.068 19.880 23.804 1.00 33.27 c
ATOM 1749 OG1 THR A 228 -17.198 18.986 23.652 1.00 35.88 0
ATOM 1750 CG2 THR A 228 -14.932 19.033 24.316 1.00 25.38 c
ATOM 1751 N SER A 229 -18.506 20.266 25.777 1.00 29.62 N ATOM 1752 CA SER A 229 -19.376 19.714 26.794 1.00 24.79 c
ATOM 1753 C SER A 229 -19.466 18.198 26.648 1.00 30.28 c
ATOM 1754 O SER A 229 -20.122 17.514 27.430 1.00 31.44 0
ATOM 1755 CB SER A 229 -20.804 20.261 26.747 1.00 29.37 c
ATOM 1756 OG SER A 229 -21.203 20.465 25.408 1.00 39.50 o ATOM 1757 N ASN A 230 -18.810 17.654 25.621 1.00 25.35 N
ATOM 1758 CA ASN A 230 -18.765 16.231 25.359 1.00 32.28 C
ATOM 1759 c ASN A 230 -17.358 15.680 25.188 1.00 30.97 C
ATOM 1760 O ASN A 230 -16.998 15.188 24.113 1.00 30.41 o ATOM 1761 CB ASN A 230 -19.544 15.958 24.037 1.00 32.54 C
ATOM 1762 CG ASN A 230 -20.620 16.961 23.684 1.00 43.39 c
ATOM 1763 ODl ASN A 230 -21.700 16.950 24.292 1.00 34.12 o
ATOM 1764 ND2 ASN A 230 -20.364 17.870 22.742 1.00 41.60 N
ATOM 1765 N PRO A 231 -16.512 15.734 26.199 1.00 25.90 N ATOM 1766 CA PRO A 231 -15.149 15.229 26.098 1.00 27.71 c
ATOM 1767 C PRO A 231 -15.155 13.714 26.028 1.00 30.87 c
ATOM 1768 O PRO A 231 -16.009 12.988 26.547 1.00 30.76 o
ATOM 1769 CB PRO A 231 -14.382 15.655 27.361 1.00 24.52 c
ATOM 1770 CG PRO A 231 -15.543 15.819 28.321 1.00 30.64 c ATOM 1771 CD PRO A 231 -16.762 16.264 27.541 1.00 27.64 c
ATOM 1772 N PRO A 232 -14.125 13.202 25.384 1.00 30.58 N
ATOM 1773 CA PRO A 232 -13.915 11.771 25.232 1.00 29.59 C
ATOM 1774 C PRO A 232 -13.958 11.072 26.562 1.00 24.88 C
ATOM 1775 O PRO A 232 -13.516 11.585 27.600 1.00 26.56 o ATOM 1776 CB PRO A 232 -12.484 11.657 24.628 1.00 30.65 C
ATOM 1777 CG PRO A 232 -12.437 12.951 23.845 1.00 27.71 C
ATOM 1778 CD PRO A 232 -13.073 14.007 24.739 1.00 33.43 C
ATOM 1779 N PRO A 233 -14.455 9.840 26.595 1.00 31.50 N
ATOM 1780 CA PRO A 233 -14.537 8.982 27.755 1.00 30.02 C ATOM 1781 C PRO A 233 -13.271 8.784 28.549 1.00 31.77 c
ATOM 1782 O PRO A 233 -13.309 8.664 29.766 1.00 36.82 o
ATOM 1783 CB PRO A 233 -14.946 7.570 27.272 1.00 33.21 c
ATOM 1784 CG PRO A 233 -15.369 7.806 25.859 1.00 35.54 c
ATOM 1785 CD PRO A 233 -14.998 9.195 25.395 1.00 31.97 c ATOM 1786 N TYR A 234 -12.109 8.784 27.890 1.00 31.90 N
ATOM 1787 CA TYR A 234 -10.829 8.611 28.542 1.00 29.83 C
ATOM 1788 C TYR A 234 -10.450 9.783 29.436 1.00 25.38 C
ATOM 1789 O TYR A 234 -9.515 9.662 30.251 1.00 31.82 o
ATOM 1790 CB TYR A 234 -9.798 8.250 27.477 1.00 30.08 c ATOM 1791 CG TYR A 234 -9.519 9.265 26.400 1.00 28.08 c
ATOM 1792 CD1 TYR A 234 -9.099 10.543 26.733 1.00 26.39 c
ATOM 1793 CD2 TYR A 234 -9.635 8.948 25.056 1.00 25.60 c
ATOM 1794 CE1 TYR A 234 -8.811 11.452 25.745 1.00 20.54 c
ATOM 1795 CE2 TYR A 234 -9.363 9.872 24.060 1.00 27.19 c ATOM 1796 CZ TYR A 234 -8.934 11.124 24.427 1.00 21.27 c
ATOM 1797 OH TYR A 234 -8.645 12.095 23.490 1.00 26.71 o
ATOM 1798 N THR A 235 -11.182 10.888 29.339 1.00 22.74 N
ATOM 1799 CA THR A 235 -10.999 12.048 30.204 1.00 25.50 c
ATOM 1800 C THR A 235 -11.837 11.912 31.486 1.00 26.78 c ATOM 1801 O THR A 235 -11.832 12.804 32.346 1.00 32.19 0
ATOM 1802 CB THR A 235 -11.370 13.374 29.533 1.00 28.11 c
ATOM 1803 OG1 THR A 235 -12.800 13.416 29.380 1.00 24.65 0
ATOM 1804 CG2 THR A 235 -10.745 13.554 28.158 1.00 28.48 c
ATOM 1805 N SER A 236 -12.535 10.793 31.673 1.00 31.61 N ATOM 1806 CA SER A 236 -13.313 10.558 32.886 1.00 31.99 c
ATOM 1807 C SER A 236 -12.412 10.540 34.115 1.00 32.80 c
ATOM 1808 O SER A 236 -11.325 9.955 34.100 1.00 36.29 o
ATOM 1809 CB SER A 236 -14.079 9.222 32.787 1.00 35.41 V C
ATOM 1810 OG SER A 236 -15.443 9.535 32.572 1.00 42.20 o ATOM 1811 N GLY A 237 -12.805 11.299 35.139 1.00 34.05 N
ATOM 1812 CA GLY A 237 -12.009 11.406 36.358 1.00 38.66 c
ATOM 1813 C GLY A 237 -11.021 12.566 36.291 1.00 32.49 C
ATOM 1814 O GLY A 237 -10.372 12.866 37.294 1.00 36.66 0
ATOM 1815 N SER A 238 -10.896 13.223 35.135 1.00 29.05 N ATOM 1816 CA SER A 238 -9.947 14..337 35..082 1.00 24.29 C
ATOM 1817 C SER A 238 10.699 15. .634 35. .256 1.00 20.53 c
ATOM 1818 O SER A 238 11.716 15. .841 34. .600 1.00 24.25 O
ATOM 1819 CB SER A 238 -9.226 14. ,413 33. ,733 1.00 32.02 c
ATOM 1820 OG SER A 238 -8.667 15. .717 33. .584 1.00 28.04 O
ATOM 1821 N PRO A 239 10.147 16. ,536 36. .060 1.00 21.54 N
ATOM 1822 CA PRO A 239 10.693 17. .874 36. .238 1.00 18.57 c
ATOM 1823 C PRO A 239 10.376 18. ,806 35. .075 1.00 22.82 c
ATOM 1824 O PRO A 239 10.899 19. .905 34. .875 1.00 23.72 o
ATOM 1825 CB PRO A 239 -9.979 18. .447 37. .486 1.00 24.85 c
ATOM 1826 CG PRO A 239 -8.670 17. .715 37. ,418 1.00 23.95 c
ATOM 1827 CD PRO A 239 -8.920 16. .341 36. .812 1.00 25.04 c
ATOM 1828 N SER A 240 -9.561 18. .346 34. .115 1.00 22.32 N
ATOM 1829 CA SER A 240 -9.129 19. ,075 32. ,956 1.00 25.70 c
ATOM 1830 C SER A 240 -9.406 18. ,372 31. ,642 1.00 22.46 c
ATOM 1831 O SER A 240 -8.481 18. ,072 30. ,889 1.00 24.11 o
ATOM 1832 CB SER A 240 -7.579 19. ,154 33. ,074 1.00 19.12 c
ATOM 1833 OG SER A 240 -7.242 19. .930 34. .207 1.00 22.92 o
ATOM 1834 N PRO A 241 10.652 18. .085 31. ,336 1.00 21.89 N
ATOM 1835 CA PRO A 241 11.085 17. .366 30. .160 1.00 20.08 c
ATOM 1836 C PRO A 241 11.108 18. .113 28. .853 1.00 23.99 c
ATOM 1837 O PRO A 241 11.345 17. .491 27. .815 1.00 23.82 o
ATOM 1838 CB PRO A 241 12.477 16, .775 30. .512 1.00 26.26 c
ATOM 1839 CG PRO A 241 12.979 17. .963 31, .310 1.00 21.14 c
ATOM 1840 CD PRO A 241 11.825 18, .433 32. .163 1.00 21.90 c
ATOM 1841 N ASP A 242 •10.811 19. .404 28. .878 1.00 22.81 N
ATOM 1842 CA ASP A 242 10.580 20. .180 27. .666 1.00 17.96 C
ATOM 1843 C ASP A 242 -9.522 21. .207 28. .055 1.00 19.55 C
ATOM 1844 O ASP A 242 -9.178 21. .283 29. .260 1.00 16.73 o
ATOM 1845 CB ASP A 242 11.824 20. .722 27. .010 1.00 25.88 C
ATOM 1846 CG ASP A 242 12.649 21, .633 27. .872 1.00 24.73 C
ATOM 1847 ODl ASP A 242 12.110 22. .106 28, .890 1.00 20.38 o
ATOM 1848 OD2 ASP A 242 •13.832 21. .863 27, .532 1.00 26.06 o
ATOM 1849 N GLU A 243 -8.916 21. .840 27. .055 1.00 20.71 N
ATOM 1850 CA GLU A 243 -7.813 22, .756 27. .320 1.00 19.80 C
ATOM 1851 C GLU A 243 -8.245 24, .021 28. .020 1.00 19.53 C
ATOM 1852 O GLU A 243 -7.470 24, .598 28. .787 1.00 17.45 O
ATOM 1853 CB GLU A 243 -7.031 22. .968 26. .025 1.00 15.20 C
ATOM 1854 CG GLU A 243 -6.412 21. .632 25. .576 1.00 17.65 c
ATOM 1855 CD GLU A 243 -5.270 21. .219 26. .502 1.00 14.78 C
ATOM 1856 OE1 GLU A 243 -4.317 22, .022 26. .567 1.00 20.61 o
ATOM 1857 OE2 GLU A 243 -5.348 20, .190 27. .177 1.00 18.25 o
ATOM 1858 N SER A 244 -9.484 24. .464 27. .770 1.00 20.35 N
ATOM 1859 CA SER A 244 -9.996 25, .633 28, .480 1.00 19.44 C
ATOM 1860 C SER A 244 ■10.046 25, .291 29. .966 1.00 16.46 C
ATOM 1861 O SER A 244 -9.606 26, .134 30. .752 1.00 22.95 o
ATOM 1862 CB SER A 244 ■11.385 26. .024 27. .985 1.00 20.18 C
ATOM 1863 OG SER A 244 11.832 27. .143 28. .763 1.00 25.46 o
ATOM 1864 N ARG A 245 ■10.522 24, .105 30. .367 1.00 20.70 N
ATOM 1865 CA ARG A 245 ■10.553 23, .804 31. .798 1.00 22.33 C
ATOM 1866 C ARG A 245 -9.157 23, .507 32. .329 1.00 21.53 C
ATOM 1867 O ARG A 245 -8.808 23, .825 33. .464 1.00 21.46 o
ATOM 1868 CB ARG A 245 ■11.549 22, .720 32, .174 1.00 23.77 c
ATOM 1869 CG ARG A 245 ■12.974 23, .320 32, .084 1.00 19.77 C
ATOM 1870 CD ARG A 245 ■13.958 22. .164 32, .185 1.00 27.37 C
ATOM 1871 NE ARG A 245 ■14.218 21. .591 30, .852 1.00 25.15 N
ATOM 1872 CZ ARG A 245 ■15.082 20, .586 30, .707 1.00 28.20 C
ATOM 1873 NH1 ARG A 245 ■15.666 20, .094 31. .806 1.00 31.28 N
ATOM 1874 NH2 ARG A 245 ■15.348 20, .084 29. .516 1.00 21.61 N 12C1
ATOM 1875 N TYR A 246 -8.275 22.976 31.464 1.00 23.79 N
ATOM 1876 CA TYR A 246 -6.892 22.755 31.942 1.00 19.09 C
ATOM 1877 C TYR A 246 -6.250 24.092 32.303 1.00 21.17 C
ATOM 1878 O TYR A 246 -5.656 24.186 33.382 1.00 22.27 O ATOM 1879 CB TYR A 246 -6.082 22.025 30.869 1.00 16.61 C
ATOM 1880 CG TYR A 246 -4.621 21.807 31.233 1.00 19.40 c
ATOM 1881 CD1 TYR A 246 -4.232 21.257 32.435 1.00 19.75 c
ATOM 1882 CD2 TYR A 246 -3.624 22.129 30.323 1.00 22.69 c
ATOM 1883 CE1 TYR A 246 -2.898 21.061 32.772 1.00 21.82 c ATOM 1884 CE2 TYR A 246 -2.289 21.944 30.627 1.00 25.37 c
ATOM 1885 CZ TYR A 246 -1.934 21.391 31.846 1.00 21.41 c
ATOM 1886 OH TYR A 246 -0.611 21.235 32.182 1.00 17.17 o
ATOM 1887 N ALA A 247 -6.413 25.097 31.433 1.00 18.27 N
ATOM 1888 CA ALA A 247 -5.867 26.435 31.638 1.00 21.58 C ATOM 1889 C ALA A 247 -6.361 27.056 32.938 1.00 19.91 C
ATOM 1890 O ALA A 247 -5.583 27.602 33.725 1.00 21.76 o
ATOM 1891 CB ALA A 247 -6.144 27.352 30.452 1.00 17.25 C
ATOM 1892 N THR A 248 -7.674 26.975 33.196 1.00 22.30 N
ATOM 1893 CA THR A 248 -8.206 27.498 34.468 1.00 24.66 C ATOM 1894 C THR A 248 -7.660 26.776 35.686 1.00 22.02 C
ATOM 1895 O THR A 248 -7.340 27.412 36.700 1.00 29.44 o
ATOM 1896 CB THR A 248 -9.756 27.436 34.447 1.00 27.51 C
ATOM 1897 OG1 THR A 248 -10.192 28.341 33.436 1.00 27.39 o
ATOM 1898 CG2 THR A 248 -10.344 27.815 35.808 1.00 29.59 C ATOM 1899 N ASN A 249 -7.441 25.465 35.641 1.00 19.27 N
ATOM 1900 CA ASN A 249 -6.982 24.661 36.752 1.00 17.79 c
ATOM 1901 C ASN A 249 -5.527 25.000 37.068 1.00 22.81 c
ATOM 1902 O ASN A 249 -5.180 25.165 38.229 1.00 22.30 o
ATOM 1903 CB ASN A 249 -7.149 23.183 36.454 1.00 22.00 c ATOM 1904 CG ASN A 249 -8.610 22.748 36.490 1.00 25.24 c
ATOM 1905 ODl ASN A 249 -9.465 23.408 37.106 1.00 28.91 o
ATOM 1906 ND2 ASN A 249 -8.881 21.640 35.820 1.00 23.15 N
ATOM 1907 N ILE A 250 -4.716 25.086 35.998 1.00 20.27 N
ATOM 1908 CA ILE A 250 -3.330 25.480 36.216 1.00 23.25 c ATOM 1909 C ILE A 250 -3.315 26.925 36.706 1.00 22.66 c
ATOM 1910 O ILE A 250 -2.639 27.222 37.696 1.00 27.25 o
ATOM 1911 CB ILE A 250 -2.420 25.320 34.977 1.00 17.89 c
ATOM 1912 CGI ILE A 250 -2.194 23.851 34.643 1.00 21.31 c
ATOM 1913 CG2 ILE A 250 -1.090 26.048 35.232 1.00 20.72 c ATOM 1914 CD1 ILE A 250 -1.316 23.045 35.577 1.00 25.73 c
ATOM 1915 N ALA A 251 -4.088 27.817 36.066 1.00 20.78 N
ATOM 1916 CA ALA A 251 -4.077 29.231 36.474 1.00 21.60 c
ATOM 1917 C ALA A 251 -4.486 29.407 37.933 1.00 19.92 c
ATOM 1918 O ALA A 251 -3.871 30.204 38.636 1.00 23.77 o ATOM 1919 CB ALA A 251 -4.989 30.018 35.540 1.00 24.91 c
ATOM 1920 N ASN A 252 -5.412 28.586 38.413 1.00 21.91 N
ATOM 1921 CA ASN A 252 -5.826 28.633 39.826 1.00 27.37 C
ATOM 1922 C ASN A 252 -4.738 28.168 40.782 1.00 26.91 C
ATOM 1923 O ASN A 252 -4.485 28.787 41.835 1.00 30.43 o ATOM 1924 CB ASN A 252 -7.124 27.817 39.959 1.00 29.77 c
ATOM 1925 CG ASN A 252 -8.329 28.501 39.340 1.00 34.19 c
ATOM 1926 ODl ASN A 252 -8.275 29.635 38.845 1.00 41.35 o
ATOM 1927 ND2 ASN A 252 -9.494 27.860 39.294 1.00 33.75 -.
ATOM 1928 N ALA A 253 -3.983 27.119 40.433 1.00 22.42 N ATOM 1929 CA ALA A 253 -2.875 26.607 41.200 1.00 23.09 c
ATOM 1930 C ALA A 253 -1.754 27.646 41.233 1.00 23.39 c
ATOM 1931 O ALA A 253 -1.161 27.852 42.291 1.00 29.01 o
ATOM 1932 CB ALA A 253 -2.317 25.300 40.661 1.00 30.28 c
ATOM 1933 N MET A 254 -1.457 28.282 40.105 1.00 22.12 N ATOM 1934 CA MET A 254 -0.429 29.305 40.049 1.00 23.50 C
ATOM 1935 C MET A 254 -0.745 30.535 40.880 1.00 26.16 C
ATOM 1936 O MET A 254 0.113 31.148 41.503 1.00 26.18 O
ATOM 1937 CB MET A 254 -0.216 29.745 38.587 1.00 23.03 C ATOM 1938 CG MET A 254 0.259 28.577 37.730 1.00 18.94 C
ATOM 1939 SD MET A 254 1.967 28.036 38.050 1.00 21.24 S
ATOM 1940 CE MET A 254 1.983 26.637 36.907 1.00 25.64 C
ATOM 1941 N ARG A 255 -1.996 30.967 40.779 1.00 22.68 N
ATOM 1942 CA ARG A 255 -2.490 32.151 41.472 1.00 26.36 C ATOM 1943 C ARG A 255 -2.288 32.106 42.969 1.00 21.34 C
ATOM 1944 O ARG A 255 -1.853 33.058 43.616 1.00 32.51 0
ATOM 1945 CB ARG A 255 -3.986 32.236 41.116 1.00 27.08 C
ATOM 1946 CG ARG A 255 -4.696 33.315 41.916 1.00 35.35 c
ATOM 1947 CD ARG A 255 -6.087 33.527 41.365 1.00 29.58 c ATOM 1948 NE ARG A 255 -6.065 33.882 39.948 1.00 28.85 N
ATOM 1949 CZ ARG A 255 -6.582 33.147 38.982 1.00 21.00 c
ATOM 1950 NH1 ARG A 255 -7.137 31.971 39.273 1.00 32.44 N
ATOM 1951 NH2 ARG A 255 -6.545 33.507 37.716 1.00 24.26 N
ATOM 1952 N GLN A 256 -2.543 30.948 43.577 1.00 27.23 N ATOM 1953 CA GLN A 256 -2.399 30.658 44.976 1.00 27.13 c
ATOM 1954 C GLN A 256 -0.947 30.638 45.438 1.00 29.65 c
ATOM 1955 O GLN A 256 -0.659 30.653 46.641 1.00 31.23 O
ATOM 1956 CB GLN A 256 -2.983 29.281 45.317 1.00 30.48 c
ATOM 1957 CG GLN A 256 -4.478 29.257 45.517 1.00 30.07 c ATOM 1958 CD GLN A 256 -4.987 30.523 46.192 1.00 40.42 c
ATOM 1959 OE1 GLN A 256 -5.818 31.222 45.622 1.00 34.76 O
ATOM 1960 NE2 GLN A 256 -4.437 30.833 47.356 1.00 41.99 N
ATOM 1961 N ARG A 257 -0.022 30.525 44.486 1.00 24.01 N
ATOM 1962 CA ARG A 257 1.399 30.535 44.797 1.00 21.55 c ATOM 1963 C ARG A 257 1.976 31.875 44.337 1.00 24.24 c
ATOM 1964 O ARG A 257 3.175 32.158 44.345 1.00 31.12 0
ATOM 1965 CB ARG A 257 2.156 29.371 44.178 1.00 29.04 c
ATOM 1966 CG ARG A 257 1.677 27.967 44.546 1.00 27.64 c
ATOM 1967 CD ARG A 257 2.263 26.993 43.527 1.00 23.53 c ATOM 1968 NE ARG A 257 2.195 25.596 43.873 1.00 30.09 N
ATOM 1969 CZ ARG A 257 3.188 24.804 44.274 1.00 22.17 c
ATOM 1970 NH1 ARG A 257 4.418 25.245 44.470 1.00 27.53 N
ATOM 1971 NH2 ARG A 257 2.890 23.529 44.500 1.00 28.30 N
ATOM 1972 N GLY A 258 1.088 32.724 43.827 1.00 24.82 N ATOM 1973 CA GLY A 258 1.376 34.040 43.296 1.00 20.44 c
ATOM 1974 C GLY A 258 2.242 34.116 42.049 1.00 30.44 c
ATOM 1975 O GLY A 258 3.100 34.974 41.844 1.00 26.62 O
ATOM 1976 N LEU A 259 2.070 33.157 41.158 1.00 25.18 N
ATOM 1977 CA LEU A 259 2.848 33.060 39.909 1.00 25.26 c ATOM 1978 C LEU A 259 1.925 33.380 38.754 1.00 25.85 c
ATOM 1979 O LEU A 259 0.705 33.474 38.968 1.00 26.59 O
ATOM 1980 CB LEU A 259 3.303 31.605 39.791 1.00 24.85 C
ATOM 1981 CG LEU A 259 4.215 31.028 40.875 1.00 30.31 C
ATOM 1982 CD1 LEU A 259 4.334 29.521 40.738 1.00 28.83 C ATOM 1983 CD2 LEU A 259 5.599 31.661 40.841 1.00 30.15 C
ATOM 1984 N PRO A 260 2.446 33.585 37.561 1.00 27.65 N
ATOM 1985 CA PRO A 260 1.709 33.887 36.355 1.00 25.68 C
ATOM 1986 C PRO A 260 0.651 32.844 36.038 1.00 20.39 c
ATOM 1987 O PRO A 260 0.699 31.709 36.479 1.00 23.63 0 ATOM 1988 CB PRO A 260 2.689 34.067 35.185 1.00 23.29 c
ATOM 1989 CG PRO A 260 3.982 33.631 35.795 1.00 26.45 c
ATOM 1990 CD PRO A 260 3.893 33.520 37.292 1.00 24.34 c
ATOM 1991 N THR A 261 -0.376 33.287 35.321 1.00 19.28 N
ATOM 1992 CA THR A 261 -1.538 32.450 35.042 1.00 19.40 c ATOM 1993 c THR A 261 -1.965 32.285 33.592 1.00 23.58 C
ATOM 1994 o THR A 261 -2.832 31.429 33.354 1.00 24.45 O
ATOM 1995 CB THR A 261 -2.753 33.182 35.712 1.00 26.00 C
ATOM 1996 OG1 THR A 261 -2.798 34.536 35.252 1.00 25.75 O ATOM 1997 CG2 THR A 261 -2.633 33.186 37.226 1.00 27.44 C
ATOM 1998 N GLN A 262 -1.499 33.063 32.650 1.00 19.65 N
ATOM 1999 CA GLN A 262 -2.055 33.188 31.321 1.00 22.46 C
ATOM 2000 C GLN A 262 -1.636 32.146 30.292 1.00 24.66 C
ATOM 2001 O GLN A 262 -0.461 31.868 30.203 1.00 26.22 o ATOM 2002 CB GLN A 262 -1.812 34.585 30.741 1.00 22.70 C
ATOM 2003 CG GLN A 262 -2.375 35.682 31.656 1.00 25.82 C
ATOM 2004 CD GLN A 262 -3.876 35.523 31.891 1.00 23.40 C
ATOM 2005 OE1 GLN A 262 -4.287 35.179 32.987 1.00 23.21 0
ATOM 2006 NE2 GLN A 262 -4.698 35.735 30.875 1.00 23.57 N ATOM 2007 N PHE A 263 -2.601 31.624 29.528 1.00 21.18 N
ATOM 2008 CA PHE A 263 -2.275 30.568 28.570 1.00 19.80 C
ATOM 2009 C PHE A 263 -2.409 30.984 27.113 1.00 18.97 C
ATOM 2010 O PHE A 263 -3.201 31.833 26.749 1.00 17.16 o
ATOM 2011 CB PHE A 263 -3.277 29.394 28.705 1.00 15.84 C ATOM 2012 CG PHE A 263 -2.886 28.393 29.744 1.00 15.38 C
ATOM 2013 CD1 PHE A 263 -2.905 28.746 31.087 1.00 18.32 c
ATOM 2014 CD2 PHE A 263 -2.380 27.139 29.437 1.00 16.13 C
ATOM 2015 CE1 PHE A 263 -2.509 27.879 32.064 1.00 12.79 C
ATOM 2016 CE2 PHE A 263 -2.012 26.250 30.410 1.00 20.12 C ATOM 2017 CZ PHE A 263 -2.051 26.597 31.761 1.00 16.90 C
ATOM 2018 N ILE A 264 -1.691 30.285 26.236 1.00 14.08 N
ATOM 2019 CA ILE A 264 -1.919 30.314 24.797 1.00 14.26 C
ATOM 2020 C ILE A 264 -2.127 28.826 24.458 1.00 19.29 C
ATOM 2021 O ILE A 264 -1.458 28.031 25.082 1.00 17.00 o ATOM 2022 CB ILE A 264 -0.969 30.953 23.805 1.00 13.88 C
ATOM 2023 CGI ILE A 264 0.462 30.428 24.019 1.00 12.80 C
ATOM 2024 CG2 ILE A 264 -1.024 32.472 24.010 1.00 15.27 C
ATOM 2025 CD1 ILE A 264 1.529 31.126 23.211 1.00 17.13 C
ATOM 2026 N ILE A 265 -3.163 28.483 23.687 1.00 15.04 N ATOM 2027 CA ILE A 265 -3.506 27.060 23.525 1.00 15.32 C
ATOM 2028 C ILE A 265 -3.537 26.706 22.048 1.00 13.65 C
ATOM 2029 O ILE A 265 -4.166 27.350 21.230 1.00 16.17 o
ATOM 2030 CB ILE A 265 -4.918 26.746 24.070 1.00 15.48 c
ATOM 2031 CGI ILE A 265 -4.898 26.920 25.592 1.00 18.66 c ATOM 2032 CG2 ILE A 265 -5.334 25.302 23.764 1.00 14.76 c
ATOM 2033 CD1 ILE A 265 -6.107 26.488 26.355 1.00 24.38 c
ATOM 2034 N ASP A 266 -2.776 25.669 21.674 1.00 12.09 N
ATOM 2035 CA ASP A 266 -2.667 25.279 20.269 1.00 10.33 c
ATOM 2036 C ASP A 266 -3.993 24.615 19.867 1.00 15.37 c ATOM 2037 O ASP A 266 -4.476 23.766 20.627 1.00 13.38 0
ATOM 2038 CB ASP A 266 -1.580 24.192 20.143 1.00 13.35 c
ATOM 2039 CG ASP A 266 -1.068 23.980 18.726 1.00 11.89 c
ATOM 2040 ODl ASP A 266 -1.529 24.571 17.727 1.00 12.25 o
ATOM 2041 OD2 ASP A 266 -0.121 23.140 18.575 1.00 14.61 0 ATOM 2042 N GLN A 267 -4.526 25.013 18.716 1.00 13.05 N
ATOM 2043 CA GLN A 267 -5.660 24.305 18.129 1.00 10.30 c
ATOM 2044 C GLN A 267 -5.314 24.023 16.675 1.00 15.72 c
ATOM 2045 O GLN A 267 -6.183 23.837 15.842 1.00 15.22 v.
ATOM 2046 CB GLN A 267 -7.003 25.069 18.183 1.00 16.05 c ATOM 2047 CG GLN A 267 -7.580 25.206 19.587 1.00 13.66 c
ATOM 2048 CD GLN A 267 -8.125 23.881 20.110 1.00 14.01 c
ATOM 2049 OE1 GLN A 267 -9.284 23.536 19.860 1.00 15.83 o
ATOM 2050 NE2 GLN A 267 -7.288 23.160 20.808 1.00 14.73 N
ATOM 2051 N SER A 268 -3.998 23.871 16.360 1.00 15.92 N ATOM 2052 CA SER A 268 -3.594 23.553 14..991 1.00 13.57 C
ATOM 2053 c SER A 268 -4.227 22.267 14. .502 1.00 13.43 c
ATOM 2054 O SER A 268 -4.570 22.147 13, .318 1.00 12.19 O
ATOM 2055 CB SER A 268 -2.061 23.394 14. .919 1.00 12.06 c
ATOM 2056 OG SER A 268 -1.657 22.381 15. .866 1.00 15.19 o
ATOM 2057 N ARG A 269 -4.408 21.285 15. .362 1.00 16.05 N
ATOM 2058 CA ARG A 269 -5.049 20.016 14, .997 1.00 10.93 c
ATOM 2059 C ARG A 269 -5.955 19.613 16. .157 1.00 14.16 c
ATOM 2060 O ARG A 269 -5.548 19.739 17. .306 1.00 13.60 o
ATOM 2061 CB ARG A 269 -4.000 18.897 14. .846 1.00 13.90 c
ATOM 2062 CG ARG A 269 -2.988 19.181 13. .742 1.00 13.59 c
ATOM 2063 CD ARG A 269 -1.989 18.057 13. .516 1.00 16.30 c
ATOM 2064 NE ARG A 269 -1.138 17.891 14. .719 1.00 14.26 N
ATOM 2065 CZ ARG A 269 -0.194 16.958 14, .761 1.00 12.94 c
ATOM 2066 NH1 ARG A 269 0.001 16.127 13. .759 1.00 13.40 N
ATOM 2067 NH2 ARG A 269 0.565 16.830 15. .870 1.00 16.04 N
ATOM 2068 N VAL A 270 -7.193 19.217 15, .883 1.00 14.90 N
ATOM 2069 CA VAL A 270 -8.126 18.765 16, .899 1.00 13.01 C
ATOM 2070 C VAL A 270 -8.668 17.386 16. .490 1.00 15.91 c
ATOM 2071 O VAL A 270 -9.160 17.241 15, .379 1.00 15.04 o
ATOM 2072 CB VAL A 270 -9.293 19.767 17. .054 1.00 17.38 c
ATOM 2073 CGI VAL A 270 ■10.238 19.254 18. .148 1.00 21.04 c
ATOM 2074 CG2 VAL A 270 -8.827 21.151 17. .476 1.00 15.46 c
ATOM 2075 N ALA A 271 -8.546 16.440 17, .412 1.00 14.81 N
ATOM 2076 CA ALA A 271 -9.073 15.103 17, .158 1.00 15.02 c
ATOM 2077 C ALA A 271 10.594 15.173 17. ,103 1.00 16.45 c
ATOM 2078 O ALA A 271 11.260 15.904 17, .849 1.00 21.19 o
ATOM 2079 CB ALA A 271 -8.642 14.204 18, .318 1.00 16.61 c
ATOM 2080 N LEU A 272 •11.140 14.389 16. .187 1.00 16.83 N
ATOM 2081 CA LEU A 272 12.567 14.231 16. .006 1.00 23.67 C
ATOM 2082 C LEU A 272 •12.964 12.969 16, .771 1.00 24.17 C
ATOM 2083 O LEU A 272 ■12.119 12.262 17, .350 1.00 23.04 o
ATOM 2084 CB LEU A 272 12.963 14.088 14, .531 1.00 23.17 c
ATOM 2085 CG LEU A 272 12.250 15.054 13, .566 1.00 29.20 c
ATOM 2086 CD1 LEU A 272 •12.578 14.774 12, .103 1.00 29.62 c
ATOM 2087 CD2 LEU A 272 12.608 16.500 13. .880 1.00 30.09 c
ATOM 2088 N SER A 273 •14.280 12.749 16. .779 1.00 31.07 N
ATOM 2089 CA SER A 273 •14.843 11.633 17. .524 1.00 27.11 C
ATOM 2090 C SER A 273 •14.149 10.312 17. .247 1.00 23.70 C
ATOM 2091 O SER A 273 •14.052 9.898 16, .063 1.00 27.36 O
ATOM 2092 CB SER A 273 •16.309 11.408 17. .153 1.00 35.15 c
ATOM 2093 OG SER A 273 •16.962 12.527 16. .600 1.00 32.10 o
ATOM 2094 N GLY A 274 ■13.713 9.646 18, .301 1.00 27.43 N
ATOM 2095 CA GLY A 274 ■13.117 8.330 18. .179 1.00 28.98 c
ATOM 2096 C GLY A 274 ■11.731 8.210 17. .631 1.00 27.96 c
ATOM 2097 O GLY A 274 ■11.218 7.109 17. .341 1.00 28.77 o
ATOM 2098 N ALA A 275 •11.040 9.343 17, .518 1.00 20.25 N
ATOM 2099 CA ALA A 275 -9.692 9.284 16, .938 1.00 21.95 c
ATOM 2100 C ALA A 275 -8.718 8.598 17, .867 1.00 24.84 c
ATOM 2101 O ALA A 275 -7.725 8.035 17. .391 1.00 25.22 o
ATOM 2102 CB ALA A 275 -9.210 10.672 16, .549 1.00 20.57 c
ATOM 2103 N ARG A 276 -8.910 8.700 19, .177 1.00 24.15 N
ATOM 2104 CA ARG A 276 -7.957 8.063 20, .084 1.00 23.88 c
ATOM 2105 C ARG A 276 -8.693 7.172 21. .078 1.00 22.10 c
ATOM 2106 O ARG A 276 -9.749 7.584 21. .514 1.00 24.86 o
ATOM 2107 CB ARG A 276 -7.294 9.184 20, .902 1.00 20.86 c
ATOM 2108 CG ARG A 276 -6.299 9.993 20, .078 1.00 21.98 c
ATOM 2109 CD ARG A 276 -5.456 10.831 21, .016 1.00 23.38 c
ATOM 2110 NE ARG A 276 -6.148 12.055 21, .395 1.00 20.58 N ATOM 2111 CZ ARG A 276 -5.491 13.084 21.949 1.00 27.48 C
ATOM 2112 NH1 ARG A 276 -4.191 12.993 22.186 1.00 20.08 N
ATOM 2113 NH2 ARG A 276 -6.192 14.161 22.275 1.00 22.71 N
ATOM 2114 N SER A 277 -8.138 6.018 21.450 1.00 24.83 N ATOM 2115 CA SER A 277 -8.749 5.195 22.483 1.00 22.06 C
ATOM 2116 C SER A 277 -8.060 5.412 23.812 1.00 28.83 C
ATOM 2117 O SER A 277 -8.535 5.063 24.899 1.00 29.56 O
ATOM 2118 CB SER A 277 -8.679 3.712 22.061 1.00 30.69 C
ATOM 2119 OG SER A 277 -7.356 3.402 21.654 1.00 35.22 O ATOM 2120 N GLU A 278 -6.873 6.031 23.760 1.00 21.99 N
ATOM 2121 CA GLU A 278 -6.072 6.339 24.932 1.00 26.09 C
ATOM 2122 C GLU A 278 -5.646 7.803 24.818 1.00 21.55 C
ATOM 2123 O GLU A 278 -5.249 8.222 23.723 1.00 24.01 O
ATOM 2124 CB GLU A 278 -4.850 5.438 25.021 1.00 23.82 C ATOM 2125 CG GLU A 278 -5.051 3.956 24.784 1.00 40.17 C
ATOM 2126 CD GLU A 278 -4.851 3.092 26.010 1.00 52.25 C
ATOM 2127 OE1 GLU A 278 -3.918 3.383 26.788 1.00 56.27 O
ATOM 2128 OE2 GLU A 278 -5.618 2.118 26.202 1.00 64.20 O
ATOM 2129 N TRP A 279 -5.678 8.557 25.916 1.00 21.94 N ATOM 2130 CA TRP A 279 -5.350 9.979 25.821 1.00 16.41 C
ATOM 2131 C TRP A 279 -3.899 10.240 25.453 1.00 20.94 C
ATOM 2132 O TRP A 279 -3.578 11.239 24.820 1.00 21.93 O
ATOM 2133 CB TRP A 279 -5.636 10.659 27.154 1.00 20.36 c
ATOM 2134 CG TRP A 279 -5.958 12.125 27.086 1.00 20.26 C ATOM 2135 CD1 TRP A 279 -5.807 13.006 26.054 1.00 23.25 C
ATOM 2136 CD2 TRP A 279 -6.556 12.851 28.164 1.00 23.44 C
ATOM 2137 NE1 TRP A 279 -6.270 14.240 26.432 1.00 22.30 N
ATOM 2138 CE2 TRP A 279 -6.735 14.173 27.717 1.00 14.66 C
ATOM 2139 CE3 TRP A 279 -6.953 12.507 29.466 1.00 21.31 C ATOM 2140 CZ2 TRP A 279 -7.270 15.151 28.559 1.00 22.16 C
ATOM 2141 CZ3 TRP A 279 -7.484 13.466 30.298 1.00 20.85 C
ATOM 2142 CH2 TRP A 279 -7.641 14.780 29.828 1.00 22.45 C
ATOM 2143 N GLY A 280 -3.012 9.305 25.757 1.00 20.36 N
ATOM 2144 CA GLY A 280 -1.585 9.496 25.487 1.00 22.05 C ATOM 2145 C GLY A 280 -1.204 9.252 24.041 1.00 24.17 C
ATOM 2146 O GLY A 280 -0.033 9.486 23.712 1.00 20.78 O
ATOM 2147 N GLN A 281 -2.101 8.821 23.175 1.00 22.02 N
ATOM 2148 CA GLN A 281 -1.792 8.665 21.746 1.00 17.94 C
ATOM 2149 C GLN A 281 -1.425 10.024 21.156 1.00 16.82 C ATOM 2150 O GLN A 281 -2.077 11.031 21.445 1.00 23.09 O
ATOM 2151 CB GLN A 281 -2.938 8.032 20.965 1.00 22.30 C
ATOM 2152 CG GLN A 281 -3.128 6.535 21.211 1.00 29.03 C
ATOM 2153 CD GLN A 281 -4.426 6.108 20.538 1.00 38.84 C
ATOM 2154 OE1 GLN A 281 -5.495 6.224 21.137 1.00 36.72 O ATOM 2155 NE2 GLN A 281 -4.350 5.656 19.294 1.00 41.84 N
ATOM 2156 N TRP A 282 -0.324 10.090 20.396 1.00 19.27 N
ATOM 2157 CA TRP A 282 0.161 11.374 19.890 1.00 19.52 C
ATOM 2158 C TRP A 282 0.607 11.442 18.441 1.00 19.99 c
ATOM 2159 O TRP A 282 0.853 12.568 17.964 1.00 18.26 O ATOM 2160 CB TRP A 282 1.421 11.768 20.726 1.00 24.77 c
ATOM 2161 CG TRP A 282 2.451 10.677 20.637 1.00 23.68 c
ATOM 2162 CD1 TRP A 282 2.525 9.543 21.411 1.00 22.06 c
ATOM 2163 CD2 TRP A 282 3.533 10.578 19.695 1.00 25.36 c
ATOM 2164 NE1 TRP A 282 3.562 8.748 20.988 1.00 30.20 N ATOM 2165 CE2 TRP A 282 4.205 9.373 19.944 1.00 29.10 c
ATOM 2166 CE3 TRP A 282 4.012 11.422 18.690 1.00 24.71 c
ATOM 2167 CZ2 TRP A 282 5.322 8.960 19.211 1.00 25.73 c
ATOM 2168 CZ3 TRP A 282 5.102 11.005 17.950 1.00 23.84 c
ATOM 2169 CH2 TRP A 282 5.760 9.789 18.208 1.00 27.45 c auuoocoaooooooaaoooϋouaooooooaaoϋooυυauoooaϋooaϋoooooϋoϋoaυ
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ATOM 2229 O GLY A 291 -8.734 25.731 13.322 1.00 16.86 O
ATOM 2230 N GLN A 292 -9.714 25.814 15.329 1.00 16.03 N
ATOM 2231 CA GLN A 292 -9.998 27.240 15.283 1.00 18.15 C
ATOM 2232 c GLN A 292 -8.728 28.041 15.042 1.00 16.47 C ATOM 2233 O GLN A 292 -7.733 27.885 15.754 1.00 20.75 O
ATOM 2234 CB GLN A 292 -10.569 27.625 16.671 1.00 25.11 C
ATOM 2235 CG GLN A 292 -10.367 29.061 17.091 1.00 36.07 C
ATOM 2236 CD GLN A 292 -11.444 29.979 16.538 1.00 39.06 c
ATOM 2237 OE1 GLN A 292 -12.607 29.754 16.883 1.00 42.29 0 ATOM 2238 NE2 GLN A 292 -11.079 30.982 15.746 1.00 33.92 N
ATOM 2239 N PRO A 293 -8.759 28.904 14.063 1.00 19.51 N
ATOM 2240 CA PRO A 293 -7.624 29.791 13.787 1.00 16.62 c
ATOM 2241 C PRO A 293 -7.430 30.766 14.931 1.00 17.64 c
ATOM 2242 O PRO A 293 -8.296 31.000 15.764 1.00 19.12 0 ATOM 2243 CB PRO A 293 -7.937 30.514 12.468 1.00 21.39 c
ATOM 2244 CG PRO A 293 -8.969 29.551 11.868 1.00 21.89 c
ATOM 2245 CD PRO A 293 -9.802 29.074 13.063 1.00 20.59 c
ATOM 2246 N PHE A 294 -6.244 31.406 14.941 1.00 15.74 N
ATOM 2247 CA PHE A 294 -5.933 32.344 15.986 1.00 18.02 c ATOM 2248 C PHE A 294 -7.076 33.330 16.288 1.00 19.91 C
ATOM 2249 O PHE A 294 -7.647 33.926 15.394 1.00 19.02 O
ATOM 2250 CB PHE A 294 -4.656 33.121 15.620 1.00 18.48 C
ATOM 2251 CG PHE A 294 -4.543 34.434 16.357 1.00 18.57 C
ATOM 2252 CD1 PHE A 294 -4.124 34.446 17.665 1.00 17.71 C ATOM 2253 CD2 PHE A 294 -4.873 35.640 15.760 1.00 20.19 C
ATOM 2254 CE1 PHE A 294 -4.048 35.634 18.374 1.00 22.25 C
ATOM 2255 CE2 PHE A 294 -4.789 36.832 16.450 1.00 17.34 C
ATOM 2256 CZ PHE A 294 -4.381 36.844 17.773 1.00 17.52 C
ATOM 2257 N THR A 295 -7.275 33.509 17.600 1.00 18.12 N ATOM 2258 CA THR A 295 -8.237 34.492 18.090 1.00 19.71 C
ATOM 2259 C THR A 295 -7.955 34.819 19.546 1.00 18.88 C
ATOM 2260 O THR A 295 -7.459 33.959 20.293 1.00 20.71 0
ATOM 2261 CB THR A 295 -9.702 34.025 17.895 1.00 16.83 C
ATOM 2262 OG1 THR A 295 -10.540 35.131 18.350 1.00 22.18 O ATOM 2263 CG2 THR A 295 -10.020 32.817 18.737 1.00 26.18 C
ATOM 2264 N THR A 296 -8.328 36.047 19.971 1.00 18.59 N
ATOM 2265 CA THR A 296 -8.221 36.396 21.376 1.00 19.93 C
ATOM 2266 C THR A 296 -9.611 36.301 22.028 1.00 22.13 C
ATOM 2267 O THR A 296 -9.744 36.454 23.241 1.00 20.87 o ATOM 2268 CB THR A 296 -7.661 37.802 21.631 1.00 26.99 C
ATOM 2269 OG1 THR A 296 -8.369 38.746 20.796 1.00 23.44 0
ATOM 2270 CG2 THR A 296 -6.195 37.975 21.282 1.00 23.00 C
ATOM 2271 N ASN A 297 -10.607 35.947 21.225 1.00 24.08 N
ATOM 2272 CA ASN A 297 -11.993 35.733 21.725 1.00 23.19 C ATOM 2273 C ASN A 297 -12.052 34.316 22.287 1.00 21.04 C
ATOM 2274 O ASN A 297 -12.578 33.371 21.686 1.00 25.87 o
ATOM 2275 CB ASN A 297 -12.934 35.862 20.537 1.00 28.03 C
ATOM 2276 CG ASN A 297 -13.122 37.223 19.915 1.00 44.66 c
ATOM 2277 ODl ASN A 297 -12.951 38.288 20.520 1.00 51.46 o ATOM 2278 ND2 ASN A 297 -13.519 37.244 18.635 1.00 44.39 N
ATOM 2279 N THR A 298 -11.458 34.105 23.451 1.00 22.06 N
ATOM 2280 CA THR A 298 -11.312 32.803 24.064 1.00 21.60 C
ATOM 2281 C THR A 298 -12.372 32.416 25.064 1.00 21.86 ' C
ATOM 2282 O THR A 298 -12.474 31.269 25.519 1.00 28.44 o ATOM 2283 CB THR A 298 -9.923 32.741 24.772 1.00 20.07 C
ATOM 2284 OG1 THR A 298 -9.972 33.643 25.882 1.00 20.59 0
ATOM 2285 CG2 THR A 298 -8.848 33.157 23.786 1.00 17.68 C
ATOM 2286 N ASN A 299 -13.136 33.422 25.519 1.00 26.27 N
ATOM 2287 CA ASN A 299 -14.174 33.192 26.525 1.00 27.86 C ATOM 2288 C ASN A 299 13.626 32.575 27.790 1.00 27.60 c
ATOM 2289 O ASN A 299 14.276 31.744 28. 437 1.00 33.49 o
ATOM 2290 CB ASN A 299 15.260 32.299 25. 906 1.00 29.99 c
ATOM 2291 CG ASN A 299 16.009 33.012 24. 804 1.00 41.81 c
ATOM 2292 ODl ASN A 299 16.247 32.460 23 728 1.00 53.74 o
ATOM 2293 ND2 ASN A 299 16.390 34.253 25 099 1.00 51.24 N
ATOM 2294 N ASN A 300 12.389 32.913 28 161 1.00 25.75 N
ATOM 2295 CA ASN A 300 11.731 32.425 29 348 1.00 27.94 c
ATOM 2296 C ASN A 300 10.626 33.425 29 680 1.00 24.49 c
ATOM 2297 O ASN A 300 -9.723 33.658 28 908 1.00 23.71 o
ATOM 2298 CB ASN A 300 11.167 31.012 29 147 1.00 27.27 c
ATOM 2299 CG ASN A 300 10.493 30.462 30 369 1.00 21.67 c
ATOM 2300 ODl ASN A 300 -9.985 31.174 31 217 1.00 23.30 o
ATOM 2301 ND2 ASN A 300 10.463 29.121 30 514 1.00 22.06 N
ATOM 2302 N PRO A 301 10.743 34.051 30. 831 1.00 29.89 N
ATOM 2303 CA PRO A 301 -9.859 35.064 31. 350 1.00 30.80 c
ATOM 2304 C PRO A 301 -8.405 34.617 31. 461 1.00 30.75 c
ATOM 2305 O PRO A 301 -7.486 35.423 31. 353 1.00 25.94 o
ATOM 2306 CB PRO A 301 10.317 35.436 32. 785 1.00 25.23 c
ATOM 2307 CG PRO A 301 11.418 34.448 33 052 1.00 30.76 c
ATOM 2308 CD PRO A 301 11.839 33.763 31 782 1.00 33.01 c
ATOM 2309 N ASN A 302 -8.222 33.326 31 719 1.00 23.27 N
ATOM 2310 CA ASN A 302 -6.910 32.735 31 869 1.00 20.97 c
ATOM 2311 C ASN A 302 -6.277 32.405 30 530 1.00 24.01 c
ATOM 2312 O ASN A 302 -5.148 31.916 30 552 1.00 20.89 o
ATOM 2313 CB ASN A 302 -7.082 31.403 32 631 1.00 25.19 c
ATOM 2314 CG ASN A 302 -7.806 31.646 33 957 1.00 27.19 c
ATOM 2315 ODl ASN A 302 -8.855 31.068 34 242 1.00 25.05 o
ATOM 2316 ND2 ASN A 302 -7.182 32.493 34 750 1.00 24.65 N
ATOM 2317 N VAL A 303 -6.990 32.602 29 442 1.00 18.61 N
ATOM 2318 CA VAL A 303 -6.442 32.199 28 134 1.00 20.42 c
ATOM 2319 C VAL A 303 -6.288 33.441 27 263 1.00 24.90 c
ATOM 2320 O VAL A 303 -7.251 34.018 26 765 1.00 21.13 o
ATOM 2321 CB VAL A 303 -7.316 31.130 27 461 1.00 18.54 c
ATOM 2322 CGI VAL A 303 -6.696 30.695 26 124 1.00 18.31 c
ATOM 2323 CG2 VAL A 303 -7.460 29.870 28 315 1.00 19.58 c
ATOM 2324 N ASP A 304 -5.048 33.910 27 097 1.00 19.18 N
ATOM 2325 CA ASP A 304 -4.734 35.011 26 238 1.00 15.86 C
ATOM 2326 C ASP A 304 -5.156 34.814 24 769 1.00 17.85 c
ATOM 2327 O ASP A 304 -5.612 35.718 24 070 1.00 20.58 o
ATOM 2328 CB ASP A 304 -3.230 35.343 26 184 1.00 19.27 c
ATOM 2329 CG ASP A 304 -2.708 36.094 27 388 1.00 22.98 c
ATOM 2330 ODl ASP A 304 -3.493 36.707 28 138 1.00 22.43 o
ATOM 2331 OD2 ASP A 304 -1.472 36.094 27 606 1.00 18.86 o
ATOM 2332 N ALA A 305 -4.924 33.623 24 221 1.00 17.98 N
ATOM 2333 CA ALA A 305 -5.254 33.428 22 814 1.00 17.71 C
ATOM 2334 C ALA A 305 -5.275 31.957 22 .431 1.00 19.11 c
ATOM 2335 O ALA A 305 -4.637 31.115 23 .076 1.00 17.63 o
ATOM 2336 CB ALA A 305 -4.242 34.158 21 .922 1.00 18.77 c
ATOM 2337 N ILE A 306 -6.068 31.675 21 .413 1.00 18.04 N
ATOM 2338 CA ILE A 306 -5.999 30.372 20 .744 1.00 15.41 C
ATOM 2339 C ILE A 306 -5.022 30.628 19 .604 1.00 13.99 C
ATOM 2340 O ILE A 306 -5.103 31.676 18 .961 1.00 17.21 'ϋ
ATOM 2341 CB ILE A 306 -7.353 29.841 20 .204 1.00 17.17 C
ATOM 2342 CGI ILE A 306 -8.169 29.421 21 427 1.00 18.89 C
ATOM 2343 CG2 ILE A 306 -7.116 28.702 19 .206 1.00 15.71 C
ATOM 2344 CD1 ILE A 306 -9.660 29.264 21 .276 1.00 24.44 C
ATOM 2345 N VAL A 307 -3.976 29.811 19 .464 1.00 14.07 N
ATOM 2346 CA VAL A 307 -2.988 29.942 18 .410 1.00 16.02 C ATOM 2347 C VAL A 307 2.806 28.614 17.675 1.00 14.25 c
ATOM 2348 O VAL A 307 3.426 27.581 18.026 1.00 12.07 O
ATOM 2349 CB VAL A 307 1.602 30.385 18.993 1.00 10.04 c
ATOM 2350 CGI VAL A 307 1.709 31.787 19.590 1.00 18.88 c
ATOM 2351 CG2 VAL A 307 1.171 29.347 20.032 1.00 15.95 c
ATOM 2352 N TRP A 308 2.073 28.598 16.567 1.00 14.38 N
ATOM 2353 CA TRP A 308 1.582 27.370 15.937 1.00 13.45 C
ATOM 2354 C TRP A 308 0.048 27.348 16.136 1.00 12.10 c
ATOM 2355 O TRP A 308 0.666 28.300 15.767 1.00 15.65 o
ATOM 2356 CB TRP A 308 1.868 27.212 14.458 1.00 13.60 c
ATOM 2357 CG TRP A 308 3.279 26.991 14.043 1.00 13.39 c
ATOM 2358 CD1 TRP A 308 4.388 27.092 14.809 1.00 15.59 c
ATOM 2359 CD2 TRP A 308 3.696 26.593 12.734 1.00 10.36 c
ATOM 2360 NE1 TRP A 308 5.515 26.770 14.054 1.00 15.23 N
ATOM 2361 CE2 TRP A 308 5.107 26.479 12.789 1.00 12.08 c
ATOM 2362 CE3 TRP A 308 3.021 26.329 11.530 1.00 12.71 c
ATOM 2363 CZ2 TRP A 308 5.823 26.135 11.633 1.00 14.21 c
ATOM 2364 CZ3 TRP A 308 3.738 25.990 10.407 1.00 14.85 c
ATOM 2365 CH2 TRP A 308 5.135 25.870 10.483 1.00 16.00 c
ATOM 2366 N VAL A 309 0.413 26.249 16.757 1.00 13.08 N
ATOM 2367 CA VAL A 309 1.864 26.155 17.006 1.00 11.26 c
ATOM 2368 C VAL A 309 2.422 25.027 16.146 1.00 10.78 c
ATOM 2369 O VAL A 309 3.254 25.284 15.308 1.00 13.32 o
ATOM 2370 CB VAL A 309 2.080 25.918 18.507 1.00 8.84 c
ATOM 2371 CGI VAL A 309 3.579 25.973 18.800 1.00 10.12 c
ATOM 2372 CG2 VAL A 309 1.338 26.928 19.376 1.00 15.13 c
ATOM 2373 N LYS A 310 1.965 23.761 16.347 1.00 12.84 N
ATOM 2374 CA LYS A 310 2.445 22.719 15.437 1.00 14.13 c
ATOM 2375 C LYS A 310 1.918 22.993 14.044 1.00 13.15 c
ATOM 2376 O LYS A 310 0.720 23.277 13.871 1.00 13.30 o
ATOM 2377 CB LYS A 310 1.808 21.402 15.905 1.00 13.66 c
ATOM 2378 CG LYS A 310 1.851 20.224 14.964 1.00 12.89 c
ATOM 2379 CD LYS A 310 3.249 19.629 14.825 1.00 15.43 c
ATOM 2380 CE LYS A 310 3.193 18.660 13.641 1.00 13.14 c
ATOM 2381 NZ LYS A 310 4.483 17.865 13.599 1.00 18.31 N
ATOM 2382 N PRO A 311 2.722 22.855 13.039 1.00 12.10 N
ATOM 2383 CA PRO A 311 2.281 23.027 11.635 1.00 12.11 c
ATOM 2384 C PRO A 311 1.569 21.776 11.145 1.00 14.07 c
ATOM 2385 O PRO A 311 2.270 20.812 10.803 1.00 13.76 o
ATOM 2386 CB PRO A 311 3.531 23.309 10.796 1.00 14.97 c
ATOM 2387 CG PRO A 311 4.536 23.666 11.894 1.00 16.80 c
ATOM 2388 CD PRO A 311 4.177 22.732 13.048 1.00 13.71 c
ATOM 2389 N GLY A 312 0.245 21.712 11.140 1.00 12.88 N
ATOM 2390 CA GLY A 312 0.478 20.520 10.763 1.00 15.35 C
ATOM 2391 C GLY A 312 0.218 20.217 9.284 1.00 15.66 C
ATOM 2392 O GLY A 312 ■0.432 21.081 8.432 1.00 14.37 o
ATOM 2393 N GLY A 313 0.242 18.983 9.091 1.00 12.66 N
ATOM 2394 CA GLY A 313 0.651 18.507 7.772 1.00 12.24 C
ATOM 2395 C GLY A 313 2.121 18.063 7.876 1.00 14.01 C
ATOM 2396 O GLY A 313 2.548 17.178 7.132 1.00 15.98 o
ATOM 2397 N GLU A 314 2.858 18.604 8.844 1.00 15.55 N
ATOM 2398 CA GLU A 314 4.220 18.088 9.099 1.00 16.28 C
ATOM 2399 C GLU A 314 4.099 16.836 9.963 1.00 17.65 v;
ATOM 2400 O GLU A 314 3.464 16.906 10.997 1.00 14.94 o
ATOM 2401 CB GLU A 314 5.002 19.155 9.912 1.00 15.42 c
ATOM 2402 CG GLU A 314 5.448 20.292 9.018 1.00 14.51 c
ATOM 2403 CD GLU A 314 6.343 21.356 9.600 1.00 21.84 c
ATOM 2404 OE1 GLU A 314 6.761 21.212 10.767 1.00 22.23 o
ATOM 2405 OE2 GLU A 314 6.631 22.367 8.915 1.00 22.72 o ATOM 2406 N SER A 315 4.636 15.699 9.550 1.00 14.50 N
ATOM 2407 CA SER A 315 4.468 14.474 10.303 1.00 14.77 C
ATOM 2408 C SER A 315 5.050 14.546 11.706 1.00 15.80 C
ATOM 2409 O SER A 315 6.062 15.191 11.967 1.00 17.95 O
ATOM 2410 CB SER A 315 5.106 13.334 9.520 1.00 13.06 C
ATOM 2411 OG SER A 315 4.970 12.075 10.141 1.00 17.54 O
ATOM 2412 N ASP A 316 4.397 13.801 12.585 1.00 12.32 N
ATOM 2413 CA ASP A 316 4.886 13.609 13.931 1.00 16.00 C
ATOM 2414 C ASP A 316 5.972 12.506 13.986 1.00 14.01 C
ATOM 2415 O ASP A 316 6.657 12.408 14.998 1.00 15.96 O
ATOM 2416 CB ASP A 316 3.755 13.207 14.871 1.00 13.64 C
ATOM 2417 CG ASP A 316 2.728 14.328 15.016 1.00 16.05 C
ATOM 2418 ODl ASP A 316 3.170 15.484 15.121 1.00 17.74 O
ATOM 2419 OD2 ASP A 316 1.536 13.946 15.002 1.00 21.87 O
ATOM 2420 N GLY A 317 5.965 11.649 12.958 1.00 15.50 N
ATOM 2421 CA GLY A 317 6.890 10.494 12.924 1.00 12.47 C
ATOM 2422 C GLY A 317 6.293 9.453 11.979 1.00 14.64 C
ATOM 2423 O GLY A 317 5.155 9.623 11.523 1.00 16.59 O
ATOM 2424 N GLN A 318 6.977 8.340 11.737 1.00 14.21 N
ATOM 2425 CA GLN A 318 6.502 7.304 10.831 1.00 14.75 C
ATOM 2426 C GLN A 318 5.593 6.349 11.600 1.00 22.28 C
ATOM 2427 o GLN A 318 5.967 5.234 11.947 1.00 22.93 O
ATOM 2428 CB GLN A 318 7.679 6.551 10.217 1.00 16.11 C
ATOM 2429 CG GLN A 318 8.723 7.423 9.590 1.00 24.55 C
ATOM 2430 CD GLN A 318 9.902 6.636 9.018 1.00 31.53 C
ATOM 2431 OE1 GLN A 318 10.937 6.714 9.660 1.00 27.30 o
ATOM 2432 NE2 GLN A 318 9.546 5.995 7.915 1.00 29.42 N
ATOM 2433 N CYS A 319 4.391 6.858 11.897 1.00 19.08 N
ATOM 2434 CA CYS A 319 3.477 6.164 12.770 1.00 16.55 C
ATOM 2435 C CYS A 319 2.093 6.788 12.606 1.00 22.67 C
ATOM 2436 O CYS A 319 1.943 7.782 11.891 1.00 16.92 O
ATOM 2437 CB CYS A 319 3.965 6.301 14.213 1.00 21.55 C
ATOM 2438 SG CYS A 319 4.718 7.796 14.848 1.00 17.95 s
ATOM 2439 N GLY A 320 1.130 6.124 13.233 1.00 22.31 N
ATOM 2440 CA GLY A 320 -0.208 6.629 13.343 1.00 22.24 C
ATOM 2441 C GLY A 320 -1.176 6.558 12.208 1.00 27.16 C
ATOM 2442 O GLY A 320 -2.371 6.257 12.400 1.00 29.10 O
ATOM 2443 N MET A 321 -0.736 6.903 11.019 1.00 29.52 N
ATOM 2444 CA MET A 321 -1.576 6.966 9.836 1.00 31.67 C
ATOM 2445 C MET A 321 -0.722 6.420 8.705 1.00 27.43 C
ATOM 2446 O MET A 321 0.483 6.663 8.652 1.00 30.77 o
ATOM 2447 CB MET A 321 -2.121 8.365 9.601 1.00 28.11 C
ATOM 2448 CG MET A 321 -3.156 8.405 8.480 1.00 31.81 C
ATOM 2449 SD MET A 321 -3.906 10.023 8.248 1.00 31.22 s
ATOM 2450 CE MET A 321 -3.513 10.340 6.526 1.00 26.93 C
ATOM 2451 N GLY A 322 -1.329 5.533 7.926 1.00 32.97 N
ATOM 2452 CA GLY A 322 -0.603 4.883 6.831 1.00 31.12 C
ATOM 2453 C GLY A 322 0.025 5.915 5.908 1.00 25.96 C
ATOM 2454 O GLY A 322 -0.624 6.902 5.547 1.00 34.14 o
ATOM 2455 N GLY A 323 1.288 5.724 5.539 1.00 34.72 N
ATOM 2456 CA GLY A 323 1.967 6.646 4.640 1.00 33.66 C
ATOM 2457 C GLY A 323 2.742 7.742 5.334 1.00 30.88 C
ATOM 2458 O GLY A 323 3.421 8.547 4.684 1.00 29.21 o
ATOM 2459 N ALA A 324 2.726 7.769 6.667 1.00 24.89 N
ATOM 2460 CA ALA A 324 3.457 8.775 7.412 1.00 21.70 C
ATOM 2461 C ALA A 324 4.966 8.740 7.280 1.00 25.53 C
ATOM 2462 O ALA A 324 5.655 7.743 7.577 1.00 22.74 O
ATOM 2463 CB ALA A 324 3.092 8.591 8.892 1.00 17.64 C
ATOM 2464 N PRO A 325 5.539 9.881 6.893 1.00 25.63 N ATOM 2465 CA PRO A 325 6.970 10.103 6.811 1.00 26.66 C
ATOM 2466 C PRO A 325 7.646 10.398 8.125 1.00 29.25 c
ATOM 2467 O PRO A 325 6.894 10.457 9.109 1.00 21.69 O
ATOM 2468 CB PRO A 325 7.111 11.313 5.850 1.00 22.47 c
ATOM 2469 CG PRO A 325 5.802 12.037 6.045 1.00 21.32 c
ATOM 2470 CD PRO A 325 4.739 11.079 6.525 1.00 17.88 c
ATOM 2471 N ALA A 326 8.954 10.544 8.317 1.00 19.09 N
ATOM 2472 CA ALA A 326 9.615 10.890 9.561 1.00 23.89 c
ATOM 2473 C ALA A 326 9.216 12.216 10.173 1.00 23.29 c
ATOM 2474 O ALA A 326 8.714 13.059 9.401 1.00 25.62 O
ATOM 2475 CB ALA A 326 11.139 10.907 9.252 1.00 27.19 c
ATOM 2476 N ALA A 327 9.426 12.504 11.455 1.00 19.22 N
ATOM 2477 CA ALA A 327 9.023 13.727 12.100 1.00 26.18 C
ATOM 2478 C ALA A 327 9.522 14.940 11.333 1.00 26.83 C
ATOM 2479 O ALA A 327 10.684 15.067 10.954 1.00 27.01 O
ATOM 2480 CB ALA A 327 9.482 13.838 13.551 1.00 27.41 C
ATOM 2481 N GLY A 328 8.623 15.877 11.114 1.00 23.90 N
ATOM 2482 CA GLY A 328 8.851 17.114 10.424 1.00 21.79 C
ATOM 2483 C GLY A 328 8.712 17.019 8.906 1.00 18.01 C
ATOM 2484 O GLY A 328 8.705 18.086 8.313 1.00 20.46 O
ATOM 2485 N MET A 329 8.605 15.830 8.317 1.00 20.58 N
ATOM 2486 CA MET A 329 8.483 15.690 6.867 1.00 19.38 C
ATOM 2487 C MET A 329 7.020 15.942 6.473 1.00 15.08 C
ATOM 2488 O MET A 329 6.132 15.611 7.248 1.00 15.65 O
ATOM 2489 CB MET A 329 8.920 14.272 6.515 1.00 25.54 c
ATOM 2490 CG MET A 329 10.030 13.990 5.558 1.00 38.71 c
ATOM 2491 SD MET A 329 11.606 14.772 5.863 1.00 34.88 s
ATOM 2492 CE MET A 329 12.668 13.369 6.212 1.00 26.53 c
ATOM 2493 N TRP A 330 6.793 16.575 5.336 1.00 15.69 N
ATOM 2494 CA TRP A 330 5.437 16.883 4.904 1.00 16.18 C
ATOM 2495 C TRP A 330 4.669 15.610 4.585 1.00 14.06 C
ATOM 2496 O TRP A 330 5.159 14.658 3.978 1.00 18.94 O
ATOM 2497 CB TRP A 330 5.527 17.777 3.670 1.00 17.74 C
ATOM 2498 CG TRP A 330 4.163 18.313 3.348 1.00 15.93 C
ATOM 2499 CD1 TRP A 330 3.367 18.005 2.307 1.00 16.88 C
ATOM 2500 CD2 TRP A 330 3.478 19.317 4.118 1.00 17.09 C
ATOM 2501 NE1 TRP A 330 2.180 18.738 2.345 1.00 15.83 N
ATOM 2502 CE2 TRP A 330 2.266 19.558 3.461 1.00 15.02 C
ATOM 2503 CE3 TRP A 330 3.756 20.024 5.288 1.00 16.31 C
ATOM 2504 CZ2 TRP A 330 1.309 20.466 3.919 1.00 14.94 C
ATOM 2505 CZ3 TRP A 330 2.836 20.949 5.753 1.00 17.53 C
ATOM 2506 CH2 TRP A 330 1.606 21.153 5.078 1.00 16.24 C
ATOM 2507 N PHE A 331 3.433 15.559 5.065 1.00 16.09 N
ATOM 2508 CA PHE A 331 2.550 14.406 4.961 1.00 14.41 C
ATOM 2509 C PHE A 331 1.262 14.921 4.313 1.00 16.69 C
ATOM 2510 O PHE A 331 0.322 15.273 5.035 1.00 15.30 O
ATOM 2511 CB PHE A 331 2.322 13.836 6.367 1.00 16.27 C
ATOM 2512 CG PHE A 331 1.521 12.564 6.476 1.00 17.29 C
ATOM 2513 CD1 PHE A 331 1.080 11.879 5.353 1.00 18.71 C
ATOM 2514 CD2 PHE A 331 1.246 12.028 7.726 1.00 15.36 C
ATOM 2515 CE1 PHE A 331 0.357 10.699 5.463 1.00 18.22 C
ATOM 2516 CE2 PHE A 331 0.517 10.859 7.857 1.00 16.90 C
ATOM 2517 CZ PHE A 331 0.080 10.205 6.721 1.00 19.20 C '
ATOM 2518 N ASP A 332 1.326 15.006 2.969 1.00 17.34 N
ATOM 2519 CA ASP A 332 0.227 15.702 2.292 1.00 19.24 C
ATOM 2520 C ASP A 332 -1.131 15.069 2.432 1.00 16.36 C
ATOM 2521 O ASP A 332 -2.111 15.825 2.522 1.00 16.52 O
ATOM 2522 CB ASP A 332 0.641 15.973 0.839 1.00 15.59 c
ATOM 2523 CG ASP A 332 -0.222 17.075 0.249 1.00 18.84 c ATOM 2524 ODl ASP A 332 -0.019 18.223 0.689 1.00 18.37 O
ATOM 2525 OD2 ASP A 332 -1.055 16.776 -0.643 1.00 21.30 O
ATOM 2526 N ALA A 333 -1.266 13.736 2.534 1.00 16.52 N
ATOM 2527 CA ALA A 333 -2.595 13.180 2.750 1.00 16.87 C
ATOM 2528 C ALA A 333 -3.173 13.621 4.115 1.00 13.54 C
ATOM 2529 O ALA A 333 -4.387 13.716 4.262 1.00 16.52 O
ATOM 2530 CB ALA A 333 -2.514 11.657 2.691 1.00 20.56 C
ATOM 2531 N TYR A 334 -2.261 13.791 5.066 1.00 15.39 N
ATOM 2532 CA TYR A 334 -2.709 14.255 6.379 1.00 14.46 C
ATOM 2533 C TYR A 334 -3.178 15.708 6.293 1.00 15.06 C
ATOM 2534 O TYR A 334 -4.201 16.014 6.922 1.00 16.95 o
ATOM 2535 CB TYR A 334 -1.604 14.026 7.397 1.00 14.33 C
ATOM 2536 CG TYR A 334 -2.063 14.109 8.826 1.00 16.96 C
ATOM 2537 CD1 TYR A 334 -2.223 15.362 9.413 1.00 12.69 C
ATOM 2538 CD2 TYR A 334 -2.320 13.005 9.604 1.00 17.31 C
ATOM 2539 CE1 TYR A 334 -2.633 15.496 10.733 1.00 14.54 c
ATOM 2540 CE2 TYR A 334 -2.720 13.099 10.917 1.00 16.18 C
ATOM 2541 CZ TYR A 334 -2.873 14.362 11.474 1.00 14.97 C
ATOM 2542 OH TYR A 334 -3.293 14.462 12.773 1.00 16.04 o
ATOM 2543 N ALA A 335 -2.419 16.527 5.566 1.00 17.05 N
ATOM 2544 CA ALA A 335 -2.806 17.906 5.335 1.00 18.69 C
ATOM 2545 C ALA A 335 -4.152 17.990 4.599 1.00 18.05 C
ATOM 2546 O ALA A 335 -5.010 18.776 5.025 1.00 16.39 o
ATOM 2547 CB ALA A 335 -1.763 18.653 4.526 1.00 16.72 C
ATOM 2548 N GLN A 336 -4.406 17.124 3.644 1.00 17.93 N
ATOM 2549 CA GLN A 336 -5.726 17.086 2.988 1.00 16.33 C
ATOM 2550 C GLN A 336 -6.789 16.721 4.000 1.00 14.31 C
ATOM 2551 O GLN A 336 -7.854 17.362 4.089 1.00 18.81 o
ATOM 2552 CB GLN A 336 -5.681 16.104 1.788 1.00 16.97 C
ATOM 2553 CG GLN A 336 -4.786 16.614 0.669 1.00 21.18 C
ATOM 2554 CD GLN A 336 -4.707 15.562 -0.429 1.00 22.27 C
ATOM 2555 OE1 GLN A 336 -5.782 15.113 -0.864 1.00 26.15 o
ATOM 2556 NE2 GLN A 336 -3.511 15.175 -0.828 1.00 19.55 N
ATOM 2557 N MET A 337 -6.575 15.748 4.886 1.00 16.42 N
ATOM 2558 CA MET A 337 -7.510 15.368 5.919 1.00 15.57 C
ATOM 2559 C MET A 337 -7.844 16.517 6.861 1.00 19.15 C
ATOM 2560 O MET A 337 -8.997 16.828 7.214 1.00 17.09 o
ATOM 2561 CB MET A 337 -7.029 14.130 6.691 1.00 12.96 C
ATOM 2562 CG MET A 337 -7.841 13.856 7.949 1.00 13.77 C
ATOM 2563 SD MET A 337 -7.030 12.851 9.216 1.00 17.79 S
ATOM 2564 CE MET A 337 -5.797 14.064 9.728 1.00 15.11 C
ATOM 2565 N LEU A 338 -6.791 17.252 7.292 1.00 17.12 N
ATOM 2566 CA LEU A 338 -7.037 18.360 8.215 1.00 13.22 C
ATOM 2567 C LEU A 338 -7.920 19.420 7.512 1.00 12.62 c
ATOM 2568 O LEU A 338 -8.692 20.078 8.208 1.00 16.09 o
ATOM 2569 CB LEU A 338 -5.750 19.033 8.672 1.00 12.72 c
ATOM 2570 CG LEU A 338 -4.854 18.184 9.613 1.00 12.16 c
ATOM 2571 CD1 LEU A 338 -3.504 18.883 9.684 1.00 14.66 c
ATOM 2572 CD2 LEU A 338 -5.481 17.933 10.963 1.00 14.99 c
ATOM 2573 N THR A 339 -7.762 19.530 6.207 1.00 15.20 N
ATOM 2574 CA THR A 339 -8.517 20.549 5.466 1.00 14.07 c
ATOM 2575 C THR A 339 -9.973 20.127 5.340 1.00 17.40 c
ATOM 2576 O THR A 339 ■10.853 20.895 5.693 1.00 16.52 o'
ATOM 2577 CB THR A 339 -7.925 20.705 4.064 1.00 14.09 c
ATOM 2578 OG1 THR A 339 -6.543 21.106 4.095 1.00 17.23 o
ATOM 2579 CG2 THR A 339 -8.676 21.807 3.307 1.00 15.79 c
ATOM 2580 N GLN A 340 ■10.209 18.932 4.816 1.00 17.13 N
ATOM 2581 CA GLN A 340 •11.600 18.444 4.763 1.00 18.38 c
ATOM 2582 C GLN A 340 ■12.301 18.472 6.108 1.00 21.25 c ATOM 2583 O GLN A 340 13.537 18.629 6.155 1.00 21.95 O
ATOM 2584 CB GLN A 340 11.617 16.996 4.243 1.00 19.29 C
ATOM 2585 CG GLN A 340 10.990 16.788 2.898 1.00 20.15 c
ATOM 2586 CD GLN A 340 10.844 15.347 2.464 1.00 39.34 c
ATOM 2587 OE1 GLN A 340 11.666 14.856 1.695 1.00 48.75 O
ATOM 2588 NE2 GLN A 340 -9.811 14.662 2.941 1.00 41.51 N
ATOM 2589 N ASN A 341 11.648 18.269 7.254 1.00 16.74 N
ATOM 2590 CA ASN A 341 12.266 18.284 8.571 1.00 17.02 C
ATOM 2591 C ASN A 341 12.058 19.597 9.323 1.00 14.87 C
ATOM 2592 O ASN A 341 12.344 19.646 10.530 1.00 16.75 O
ATOM 2593 CB ASN A 341 11.733 17.147 9.439 1.00 20.22 C
ATOM 2594 CG ASN A 341 12.196 15.814 8.876 1.00 29.67 C
ATOM 2595 ODl ASN A 341 13.358 15.425 9.026 1.00 27.00 O
ATOM 2596 ND2 ASN A 341 11.285 15.111 8.228 1.00 27.87 N
ATOM 2597 N ALA A 342 11.655 20.620 8.570 1.00 15.69 N
ATOM 2598 CA ALA A 342 11.376 21.899 9.250 1.00 16.57 C
ATOM 2599 C ALA A 342 12.564 22.549 9.947 1.00 15.33 C
ATOM 2600 O ALA A 342 13.726 22.421 9.579 1.00 17.77 o
ATOM 2601 CB ALA A 342 10.770 22.898 8.286 1.00 16.11 C
ATOM 2602 N HIS A 343 12.166 23.352 10.924 1.00 15.51 N
ATOM 2603 CA HIS A 343 13.073 24.222 11.681 1.00 17.62 C
ATOM 2604 C HIS A 343 13.823 25.077 10.667 1.00 15.64 C
ATOM 2605 O HIS A 343 13.259 25.492 9.663 1.00 17.37 O
ATOM 2606 CB HIS A 343 12.241 25.177 12.540 1.00 20.31 C
ATOM 2607 CG HIS A 343 13.053 25.933 13.534 1.00 19.46 C
ATOM 2608 ND1 HIS A 343 13.707 27.108 13.227 1.00 19.05 N
ATOM 2609 CD2 HIS A 343 13.310 25.671 14.840 1.00 20.32 C
ATOM 2610 CE1 HIS A 343 14.338 27.522 14.319 1.00 19.65 C
ATOM 2611 NE2 HIS A 343 14.098 26.687 15.323 1.00 18.29 N
ATOM 2612 N ASP A 344 15.103 25.337 11.008 1.00 18.61 N
ATOM 2613 CA ASP A 344 15.950 26.127 10.114 1.00 20.83 C
ATOM 2614 C ASP A 344 15.454 27.497 9.712 1.00 18.50 C
ATOM 2615 O ASP A 344 15.776 28.009 8.617 1.00 19.65 O
ATOM 2616 CB ASP A 344 17.319 26.381 10.775 1.00 25.00 C
ATOM 2617 CG ASP A 344 18.236 25.186 10.782 1.00 34.89 C
ATOM 2618 ODl ASP A 344 17.973 24.200 10.064 1.00 34.92 O
ATOM 2619 OD2 ASP A 344 19.239 25.245 11.525 1.00 39.34 O
ATOM 2620 N GLU A 345 14.615 28.169 10.499 1.00 19.67 N
ATOM 2621 CA GLU A 345 14.047 29.439 10.063 1.00 22.09 C
ATOM 2622 C GLU A 345 ■13.243 29.344 8.768 1.00 16.48 C
ATOM 2623 O GLU A 345 13.207 30.294 7.988 1.00 20.11 O
ATOM 2624 CB GLU A 345 13.182 30.059 11.183 1.00 21.92 C
ATOM 2625 CG GLU A 345 14.086 30.236 12.402 1.00 35.84 c
ATOM 2626 CD GLU A 345 ■13.699 31.384 13.305 1.00 41.79 c
ATOM 2627 OE1 GLU A 345 ■12.517 31.778 13.290 1.00 36.10 O
ATOM 2628 OE2 GLU A 345 ■14.612 31.865 14.006 1.00 48.99 O
ATOM 2629 N ILE A 346 ■12.591 28.208 8.483 1.00 15.60 N
ATOM 2630 CA ILE A 346 ■11.750 28.048 7.307 1.00 15.20 C
ATOM 2631 C ILE A 346 ■12.598 27.728 6.083 1.00 16.62 C
ATOM 2632 O ILE A 346 ■13.272 26.691 6.039 1.00 17.87 O
ATOM 2633 CB ILE A 346 ■10.755 26.878 7.551 1.00 17.64 c
ATOM 2634 CGI ILE A 346 -9.853 27.349 8.700 1.00 18.77 c
ATOM 2635 CG2 ILE A 346 -9.930 26.542 6.323 1.00 16.36
ATOM 2636 CD1 ILE A 346 -9.204 26.204 9.476 1.00 17.77 c
ATOM 2637 N ALA A 347 ■12.535 28.650 5.137 1.00 18.51 N
ATOM 2638 CA ALA A 347 -13.315 28.522 3.902 1.00 19.06 C
ATOM 2639 C ALA A 347 ■12.714 29.367 2.772 1.00 22.31 C
ATOM 2640 O ALA A 347 ■12.227 30.448 3.199 1.00 20.04 O
ATOM 2641 CB ALA A 347 ■14.730 29.018 4.179 1.00 23.68 c ATOM 2642 N GLY B 3 103.122 49.891 57.804 1.00 33.72 N
ATOM 2643 CA GLY B 3 102.929 51.013 56.900 1.00 37.30 C
ATOM 2644 C GLY B 3 101.701 50.803 56.016 1.00 27.78 C
ATOM 2645 O GLY B 3 101.105 49.740 55.924 1.00 26.94 0 ATOM 2646 N ASN B 4 101.361 51.854 55.290 1.00 25.02 N
ATOM 2647 CA ASN B 4 100.206 51.840 54.362 1.00 24.16 c
ATOM 2648 C ASN B 4 100.539 51.062 53.114 1.00 24.20 c
ATOM 2649 O ASN B 4 101.457 51.312 52.321 1.00 23.81 o
ATOM 2650 CB ASN B 4 99.927 53.330 54.110 1.00 21.34 c ATOM 2651 CG ASN B 4 98.845 53.603 53.108 1.00 18.32 c
ATOM 2652 ODl ASN B 4 98.145 52.680 52.633 1.00 21.01 o
ATOM 2653 ND2 ASN B 4 98.670 54.870 52.732 1.00 23.62 N
ATOM 2654 N PRO B 5 99.752 50.008 52.818 1.00 23.45 N
ATOM 2655 CA PRO B 5 99.932 49.151 51.683 1.00 24.15 c ATOM 2656 C PRO B 5 99.726 49.772 50.330 1.00 19.72 c
ATOM 2657 O PRO B 5 100.062 49.190 49.307 1.00 22.93 o
ATOM 2658 CB PRO B 5 98.966 47.952 51.875 1.00 23.21 c
ATOM 2659 CG PRO B 5 97.901 48.595 52.725 1.00 27.26 c
ATOM 2660 CD PRO B 5 98.585 49.633 53.628 1.00 23.90 c ATOM 2661 N PHE B 6 99.082 50.954 50.275 1.00 22.55 N
ATOM 2662 CA PHE B 6 98.818 51.618 49.018 1.00 22.78 c
ATOM 2663 C PHE B 6 99.917 52.630 48.660 1.00 21.92 c
ATOM 2664 O PHE B 6 100.009 53.070 47.530 1.00 22.74 o
ATOM 2665 CB PHE B 6 97.491 52.382 49.197 1.00 22.52 c ATOM 2666 CG PHE B 6 96.277 51.475 49.205 1.00 18.54 c
ATOM 2667 CD1 PHE B 6 95.697 51.154 47.985 1.00 18.88 c
ATOM 2668 CD2 PHE B 6 95.782 50.982 50.380 1.00 18.39 c
ATOM 2669 CE1 PHE B 6 94.573 50.328 47.949 1.00 19.90 c
ATOM 2670 CE2 PHE B 6 94.657 50.143 50.361 1.00 18.61 c ATOM 2671 CZ PHE B 6 94.093 49.845 49.141 1.00 16.10 c
ATOM 2672 N SER B 7 100.716 52.943 49.665 1.00 24.78 N
ATOM 2673 CA SER B 7 101.800 53.926 49.472 1.00 27.38 c
ATOM 2674 C SER B 7 102.702 53.477 48.327 1.00 25.04 c
ATOM 2675 O SER B 7 103.250 52.365 48.263 1.00 29.27 o ATOM 2676 CB SER B 7 102.550 54.137 50.776 1.00 30.87 c
ATOM 2677 OG SER B 7 103.739 54.880 50.521 1.00 37.92 0
ATOM 2678 N GLY B 8 102.794 54.334 47.312 1.00 28.72 N
ATOM 2679 CA GLY B 8 103.560 54.109 46.121 1.00 26.32 C
ATOM 2680 C GLY B 8 103.077 53.121 45.096 1.00 28.15 C ATOM 2681 O GLY B 8 103.742 52.785 44.120 1.00 26.94 0
ATOM 2682 N ARG B 9 101.841 52.650 45.259 1.00 26.95 N
ATOM 2683 CA ARG B 9 101.181 51.735 44.362 1.00 28.04 C
ATOM 2684 C ARG B 9 99.972 52.375 43.668 1.00 22.76 C
ATOM 2685 O ARG B 9 99.538 53.452 44.037 1.00 21.72 O ATOM 2686 CB ARG B 9 100.738 50.492 45.161 1.00 24.98 C
ATOM 2687 CG ARG B 9 101.954 49.691 45.639 1.00 31.04 C
ATOM 2688 CD ARG B 9 101.592 48.439 46.392 1.00 26.45 C
ATOM 2689 NE ARG B 9 102.739 47.573 46.687 1.00 34.70 N
ATOM 2690 CZ ARG B 9 103.129 47.266 47.922 1.00 39.40 C ATOM 2691 NH1 ARG B 9 102.497 47.728 48.993 1.00 40.64 N
ATOM 2692 NH2 ARG B 9 104.182 46.475 48.156 1.00 38.19 N
ATOM 2693 N THR B 10 99.545 51.709 42.607 1.00 29.44 N
ATOM 2694 CA THR B 10 98.378 52.151 41.854 1.00 23.64 C
ATOM 2695 C THR B 10 97.303 51.088 42.118 1.00 27.59 C ATOM 2696 O THR B 10 97.648 49.914 42.291 1.00 23.93 O
ATOM 2697 CB THR B 10 98.632 52.288 40.348 1.00 25.71 C
ATOM 2698 OG1 THR B 10 99.474 51.229 39.879 1.00 31.15 0
ATOM 2699 CG2 THR B 10 99.297 53.629 40.037 1.00 33.46 C
ATOM 2700 N LEU B 11 96.082 51.548 42.339 1.00 23.03 N ATOM 2701 CA LEU B 11 94.945 50.621 42.,493 1.00 18.,79 C
ATOM 2702 C LEU B 11 94.659 50.101 41. .095 1.00 14. ,75 c
ATOM 2703 O LEU B 11 94.434 50.820 40. .105 1.00 19. ,53 o
ATOM 2704 CB LEU B 11 93.703 51.317 42. .992 1.00 19. ,12 c
ATOM 2705 CG LEU B 11 92.446 50.438 43. ,132 1.00 22. ,71 c
ATOM 2706 CD1 LEU B 11 92.684 49.287 44. ,090 1.00 22. ,76 c
ATOM 2707 CD2 LEU B 11 91.334 51.306 43. ,695 1.00 23. ,60 c
ATOM 2708 N LEU B 12 94.670 48.775 40. ,941 1.00 20. ,03 N
ATOM 2709 CA LEU B 12 94.482 48.192 39. ,636 1.00 14. ,43 c
ATOM 2710 C LEU B 12 93.109 48.404 39. ,022 1.00 16. ,53 c
ATOM 2711 O LEU B 12 92.075 48.340 39. ,716 1.00 17. ,06 o
ATOM 2712 CB LEU B 12 94.730 46.652 39. ,765 1.00 18. ,12 c
ATOM 2713 CG LEU B 12 94.712 45.939 38. ,405 1.00 23. ,15 c
ATOM 2714 CD1 LEU B 12 95.987 46.244 37. ,614 1.00 24. .69 c
ATOM 2715 CD2 LEU B 12 94.566 44.423 38. .575 1.00 22. .51 c
ATOM 2716 N VAL B 13 93.076 48.695 37. .729 1.00 19. ,62 N
ATOM 2717 CA VAL B 13 91.835 48.843 36. ,974 1.00 19. .10 c
ATOM 2718 C VAL B 13 91.086 47.512 36. .956 1.00 19. .52 c
ATOM 2719 O VAL B 13 91.709 46.440 36. .878 1.00 18. .73 o
ATOM 2720 CB VAL B 13 92.151 49.237 35. .528 1.00 23. ,99 c
ATOM 2721 CGI VAL B 13 91.012 49.042 34. .543 1.00 23. .48 c
ATOM 2722 CG2 VAL B 13 92.603 50.694 35. .559 1.00 22. .45 c
ATOM 2723 N ASN B 14 89.792 47.641 37, .161 1.00 16. .64 N
ATOM 2724 CA ASN B 14 88.902 46.462 37. .078 1.00 15. .44 c
ATOM 2725 C ASN B 14 88.490 46.297 35. .627 1.00 18. .11 c
ATOM 2726 O ASN B 14 87.770 47.107 35. .020 1.00 14. .84 o
ATOM 2727 CB ASN B 14 87.715 46.703 38, .013 1.00 14. .45 c
ATOM 2728 CG ASN B 14 86.631 45.653 37, .899 1.00 19. .96 c
ATOM 2729 ODl ASN B 14 86.414 45.004 36, .897 1.00 15. .36 o
ATOM 2730 ND2 ASN B 14 85.848 45.438 38. .973 1.00 18. .43 N
ATOM 2731 N SER B 15 89.019 45.241 34. .979 1.00 17. .61 N
ATOM 2732 CA SER B 15 88.778 45.057 33, .557 1.00 16. .10 C
ATOM 2733 C SER B 15 87.346 44.735 33. .185 1.00 20. .23 C
ATOM 2734 O SER B 15 86.885 45.045 32. .065 1.00 18. .77 O
ATOM 2735 CB SER B 15 89.701 43.954 33. .019 1.00 16. .38 C
ATOM 2736 OG SER B 15 89.481 42.715 33. .689 1.00 20, .77 O
ATOM 2737 N ASP B 16 86.592 44.137 34. .073 1.00 19. .24 N
ATOM 2738 CA ASP B 16 85.190 43.844 33. .821 1.00 16. .45 C
ATOM 2739 C ASP B 16 84.450 45.189 33. .744 1.00 17. .33 C
ATOM 2740 O ASP B 16 83.692 45.492 32. .828 1.00 17, .87 O
ATOM 2741 CB ASP B 16 84.590 42.974 34. .935 1.00 20, .42 C
ATOM 2742 CG ASP B 16 83.077 42.890 34. .869 1.00 22, .12 C
ATOM 2743 ODl ASP B 16 82.524 42.626 33. .772 1.00 26, .25 O
ATOM 2744 OD2 ASP B 16 82.412 43.124 35, .897 1.00 23, .78 O
ATOM 2745 N TYR B 17 84.652 45.986 34, .804 1.00 16. .40 N
ATOM 2746 CA TYR B 17 84.039 47.311 34, .862 1.00 15. .09 C
ATOM 2747 C TYR B 17 84.426 48.129 33, .628 1.00 16, .41 C
ATOM 2748 O TYR B 17 83.594 48.788 33, .016 1.00 15. .14 O
ATOM 2749 CB TYR B 17 84.533 48.014 36, .119 1.00 12, .96 C
ATOM 2750 CG TYR B 17 83.977 49.372 36, .442 1.00 11, .69 C
ATOM 2751 CD1 TYR B 17 82.630 49.681 36, .177 1.00 12, .39 C
ATOM 2752 CD2 TYR B 17 84.772 50.340 37, .005 1.00 13, .55 C
ATOM 2753 CE1 TYR B 17 82.134 50.932 36, .528 1.00 11, .19 c
ATOM 2754 CE2 TYR B 17 84.272 51.581 37, .387 1.00 16, .44 C
ATOM 2755 CZ TYR B 17 82.951 51.882 37, .093 1.00 13, .70 C
ATOM 2756 OH TYR B 17 82.480 53.119 37, .473 1.00 15, .10 O
ATOM 2757 N SER B 18 85.731 48.186 33, .337 1.00 13, .96 N
ATOM 2758 CA SER B 18 86.225 48.933 32, .189 1.00 21, .06 C
ATOM 2759 C SER B 18 85.520 48.551 30, .898 1.00 17, .15 C ATOM 2760 O SER B 18 85.025 49.407 30.156 1.00 17.69 O
ATOM 2761 CB SER B 18 87.759 48.802 32.115 1.00 18.47 C
ATOM 2762 OG SER B 18 88.274 49.530 31.018 1.00 22.46 O
ATOM 2763 N SER B 19 85.393 47.235 30.611 1.00 16.95 N
ATOM 2764 CA SER B 19 84.689 46.797 29.425 1.00 14.73 C
ATOM 2765 C SER B 19 83.208 47.203 29.374 1.00 15.35 C
ATOM 2766 O SER B 19 82.698 47.600 28.333 1.00 17.71 O
ATOM 2767 CB SER B 19 84.740 45.281 29.224 1.00 17.05 C
ATOM 2768 OG i USER B 19 84.336 44.578 30.374 0.50 25.68 O
ATOM 2769 OG ] BSER B 19 86.059 44.756 29.207 0.50 13.93 O
ATOM 2770 N LYS B 20 82.539 47.130 30.541 1.00 17.29 N
ATOM 2771 CA LYS B 20 81.145 47.563 30.583 1.00 15.79 C
ATOM 2772 C LYS B 20 80.977 49.058 30.370 1.00 20.37 C
ATOM 2773 O LYS B 20 79.998 49.449 29.734 1.00 16.23 O
ATOM 2774 CB LYS B 20 80.437 47.108 31.865 1.00 18.21 C
ATOM 2775 CG LYS B 20 80.500 45.588 31.941 1.00 17.99 C
ATOM 2776 CD LYS B 20 79.701 44.984 33.082 1.00 20.47 C
ATOM 2777 CE LYS B 20 80.240 45.293 34.450 1.00 25.73 C
ATOM 2778 NZ LYS B 20 79.681 44.396 35.515 1.00 15.48 N
ATOM 2779 N LEU B 21 81.945 49.848 30.786 1.00 17.84 N
ATOM 2780 CA LEU B 21 81.958 51.284 30.570 1.00 14.20 C
ATOM 2781 C LEU B 21 82.143 51.611 29.088 1.00 16.72 C
ATOM 2782 O LEU B 21 81.834 52.739 28.712 1.00 16.34 O
ATOM 2783 CB LEU B 21 83.073 51.995 31.345 1.00 14.43 C
ATOM 2784 CG LEU B 21 82.776 52.173 32.845 1.00 18.41 C
ATOM 2785 CD1 LEU B 21 84.055 52.438 33.615 1.00 17.41 C
ATOM 2786 CD2 LEU B 21 81.749 53.281 33.062 1.00 21.73 C
ATOM 2787 N ASP B 22 82.479 50.650 28.231 1.00 18.10 N
ATOM 2788 CA ASP B 22 82.612 50.917 26.803 1.00 16.43 C
ATOM 2789 C ASP B 22 81.260 51.283 26.221 1.00 18.02 C
ATOM 2790 O ASP B 22 81.183 52.150 25.337 1.00 17.76 O
ATOM 2791 CB ASP B 22 83.216 49.735 26.032 1.00 14.85 C
ATOM 2792 CG ASP B 22 84.007 50.276 24.848 1.00 21.61 C
ATOM 2793 ODl ASP B 22 84.856 51.157 25.068 1.00 21.20 O
ATOM 2794 OD2 ASP B 22 83.709 49.787 23.734 1.00 20.22 O
ATOM 2795 N GLN B 23 80.180 50.681 26.744 1.00 15.67 N
ATOM 2796 CA GLN B 23 78.834 51.047 26.331 1.00 14.85 C
ATOM 2797 C GLN B 23 78.552 52.514 26.610 1.00 17.57 C
ATOM 2798 O GLN B 23 77.967 53.225 25.786 1.00 20.19 O
ATOM 2799 CB GLN B 23 77.838 50.153 27.129 1.00 17.93 C
ATOM 2800 CG GLN B 23 76.388 50.488 26.741 1.00 16.53 C
ATOM 2801 CD GLN B 23 75.372 49.548 27.329 1.00 19.21 C
ATOM 2802 OE1 GLN B 23 74.175 49.729 27.059 1.00 21.84 O
ATOM 2803 NE2 GLN B 23 75.795 48.555 28.100 1.00 16.64 N
ATOM 2804 N THR B 24 79.024 53.034 27.761 1.00 15.10 N
ATOM 2805 CA THR B 24 78.793 54.423 28.128 1.00 17.67 C
ATOM 2806 C THR B 24 79.559 55.381 27.210 1.00 16.82 C
ATOM 2807 O THR B 24 79.033 56.425 26.808 1.00 19.08 O
ATOM 2808 CB THR B 24 79.235 54.676 29.587 1.00 18.56 C
ATOM 2809 OG1 THR B 24 78.812 53.527 30.352 1.00 17.18 O
ATOM 2810 CG2 THR B 24 78.646 55.918 30.192 1.00 16.79 C
ATOM 2811 N ARG B 25 80.790 54.974 26.923 1.00 17.68 N
ATOM 2812 CA ARG B 25 81.654 55.784 26.046 1.00 16.68 C
ATOM 2813 C ARG B 25 80.930 55.912 24.694 1.00 17.50 C
ATOM 2814 O ARG B 25 80.788 57.022 24.168 1.00 17.95 O
ATOM 2815 CB ARG B 25 82.984 55.049 25.833 1.00 15.96 C
ATOM 2816 CG ARG B 25 83.958 55.832 24.919 1.00 16.61 C
ATOM 2817 CD ARG B 25 85.292 55.070 24.781 1.00 20.12 C
ATOM 2818 NE ARG B 25 85.047 53.796 24.103 1.00 19.63 N ATOM 2819 CZ ARG B 25 84.,876 53,,624 22.,799 1.00 21..31 C
ATOM 2820 NH1 ARG B 25 85. ,025 54. ,639 21. ,955 1.00 23. .29 N
ATOM 2821 NH2 ARG B 25 84. ,594 52. ,426 22. ,306 1.00 18. .01 N
ATOM 2822 N GLN B 26 80. ,472 54. ,773 24. ,177 1.00 15. .24 N
ATOM 2823 CA GLN B 26 79. ,753 54. ,727 22. ,912 1.00 20. .13 C
ATOM 2824 C GLN B 26 78. ,454 55. ,526 22. ,953 1.00 21. .90 C
ATOM 2825 O GLN B 26 78. ,079 56. ,177 21. ,976 1.00 19. .59 O
ATOM 2826 CB GLN B 26 79. ,452 53. ,293 22. ,449 1.00 16. .49 C
ATOM 2827 CG GLN B 26 80. ,730 52. ,536 22. ,062 1.00 19. .82 C
ATOM 2828 CD GLN B 26 80. ,487 51. ,135 21. ,548 1.00 21. ,12 C
ATOM 2829 OE1 GLN B 26 79. ,563 50. ,862 20. ,790 1.00 23. ,63 o
ATOM 2830 NE2 GLN B 26 81. ,333 50. .181 21. ,990 1.00 20. ,52 N
ATOM 2831 N ALA B 27 77. .719 55. .483 24. ,078 1.00 19. ,85 N
ATOM 2832 CA ALA B 27 76. ,475 56. .261 24. ,107 1.00 17. ,20 C
ATOM 2833 C ALA B 27 76. ,798 57. ,746 24. ,065 1.00 17. .74 C
ATOM 2834 O ALA B 27 76. ,034 58. .491 23. ,405 1.00 21. .26 O
ATOM 2835 CB ALA B 27 75. ,751 55. .913 25. .397 1.00 17. ,02 C
ATOM 2836 N PHE B 28 77. ,814 58. .219 24. .767 1.00 18. ,68 N
ATOM 2837 CA PHE B 28 78. ,171 59. ,648 24. .658 1.00 17. ,61 C
ATOM 2838 C PHE B 28 78. ,571 59. ,970 23. .210 1.00 19. ,64 c
ATOM 2839 O PHE B 28 78. ,146 61. ,039 22. .729 1.00 20. ,51 o
ATOM 2840 CB PHE B 28 79. .324 60. ,001 25. .599 1.00 17. ,36 c
ATOM 2841 CG PHE B 28 78. .806 60. ,206 27. ,009 1.00 15. ,23 c
ATOM 2842 CD1 PHE B 28 77. .849 61. ,155 27. ,289 1.00 17. ,88 c
ATOM 2843 CD2 PHE B 28 79. .338 59. .462 28. ,049 1.00 20. .22 c
ATOM 2844 CE1 PHE B 28 77. .379 61. .358 28. ,578 1.00 16. .98 c
ATOM 2845 CE2 PHE B 28 78. .897 59. .678 29. .345 1.00 15. .66 c
ATOM 2846 CZ PHE B 28 77. .912 60. ,615 29. .620 1.00 22. .38 c
ATOM 2847 N LEU B 29 79. .315 59. .075 22. .582 1.00 19. ,38 N
ATOM 2848 CA LEU B 29 79. .724 59. ,297 21. .189 1.00 22. ,95 c
ATOM 2849 C LEU B 29 78. .522 59. .369 20. ,260 1.00 25. .65 c
ATOM 2850 O LEU B 29 78, .529 60. .163 19. .315 1.00 24. .09 o
ATOM 2851 CB LEU B 29 80. .729 58, .239 20. ,713 1.00 22. .39 c
ATOM 2852 CG LEU B 29 82, .107 58, .293 21. .394 1.00 23. .42 c
ATOM 2853 CD1 LEU B 29 82. .984 57, .090 21. .110 1.00 20. .32 c
ATOM 2854 CD2 LEU B 29 82, .811 59. .580 20. .990 1.00 22. .99 c
ATOM 2855 N SER B 30 77, .447 58. .605 20. .504 1.00 21, .76 N
ATOM 2856 CA SER B 30 76, .290 58. .676 19. .603 1.00 23, .84 c
ATOM 2857 C SER B 30 75, .561 60. .000 19. .630 1.00 30, .86 c
ATOM 2858 O SER B 30 74. .799 60. .289 18. .694 1.00 27, .94 o
ATOM 2859 CB SER B 30 75. .340 57. .511 19. .882 1.00 28, .32 c
ATOM 2860 OG SER B 30 74. .727 57. .678 21. .156 1.00 24. .32 o
ATOM 2861 N ARG B 31 75. .740 60. .809 20, .663 1.00 25. .20 N
ATOM 2862 CA ARG B 31 75. .111 62. .122 20, .762 1.00 25, .58 C
ATOM 2863 C ARG B 31 76, .077 63, .255 20, .458 1.00 24, .05 C
ATOM 2864 O ARG B 31 75, .808 64, .405 20, .746 1.00 24, .27 O
ATOM 2865 CB ARG B 31 74, .550 62, .247 22, .193 1.00 23, .48 c
ATOM 2866 CG ARG B 31 73, .450 61, .195 22, .340 1.00 23, .60 c
ATOM 2867 CD ARG B 31 72, .572 61, .452 23, .533 1.00 26. .31 c
ATOM 2868 NE ARG B 31 73, .241 61, .792 24, .778 1.00 30. .79 N
ATOM 2869 CZ ARG B 31 73 .602 60, .915 25. .704 1.00 34, .02 c
ATOM 2870 NH1 ARG B 31 73 .374 59, .634 25. .507 1.00 21, .49 N
ATOM 2871 NH2 ARG B 31 74 .193 61, .322 26, .822 1.00 35, .78 N\
ATOM 2872 N GLY B 32 77, .267 62, .900 19, .959 1.00 27, .50 N
ATOM 2873 CA GLY B 32 78, .297 63. .906 19, .677 1.00 27, .73 C
ATOM 2874 C GLY B 32 78, .864 64. .523 20, .950 1.00 26, .07 C
ATOM 2875 O GLY B 32 79, .424 65, .625 20, .952 1.00 24, .79 O
ATOM 2876 N ASP B 33 78, .739 63, .780 22. .072 1.00 21, .51 N
ATOM 2877 CA ASP B 33 79, .272 64, .322 23. .326 1.00 17. .26 C ATOM 2878 c ASP B 33 80.671 63.782 23.531 1.00 23.38 C
ATOM 2879 O ASP B 33 80.962 62.783 24.197 1.00 20.23 O
ATOM 2880 CB ASP B 33 78.371 63.893 24.506 1.00 18.03 C
ATOM 2881 CG ASP B 33 78.755 64.589 25.799 1.00 23.16 C ATOM 2882 ODl ASP B 33 79.847 65.168 25.886 1.00 17.12 O
ATOM 2883 OD2 ASP B 33 77.919 64.566 26.743 1.00 21.92 O
ATOM 2884 N GLN B 34 81.642 64.453 22.890 1.00 18.68 N
ATOM 2885 CA GLN B 34 83.032 64.085 22.980 1.00 17.11 C
ATOM 2886 C GLN B 34 83.617 64.292 24.378 1.00 16.67 C ATOM 2887 O GLN B 34 84.465 63.483 24.770 1.00 18.63 o
ATOM 2888 CB GLN B 34 83.892 64.916 22.005 1.00 21.52 C
ATOM 2889 CG GLN B 34 83.495 64.774 20.561 1.00 25.49 C
ATOM 2890 CD GLN B 34 83.557 63.381 19.996 1.00 32.14 C
ATOM 2891 OE1 GLN B 34 84.375 62.547 20.371 1.00 25.68 0 ATOM 2892 NE2 GLN B 34 82.683 63.054 19.052 1.00 34.50 N
ATOM 2893 N THR B 35 83.262 65.383 25.040 1.00 16.15 N
ATOM 2894 CA THR B 35 83.786 65.638 26.390 1.00 18.33 C
ATOM 2895 C THR B 35 83.466 64.467 27.333 1.00 17.28 C
ATOM 2896 O THR B 35 84.391 63.927 27.942 1.00 18.52 o ATOM 2897 CB THR B 35 83.192 66.937 26.953 1.00 20.49 C
ATOM 2898 OG1 THR B 35 83.582 68.016 26.080 1.00 18.80 0
ATOM 2899 CG2 THR B 35 83.729 67.268 28.329 1.00 22.79 C
ATOM 2900 N ASN B 36 82.220 64.022 27.361 1.00 18.47 N
ATOM 2901 CA ASN B 36 81.889 62.914 28.274 1.00 16.82 C ATOM 2902 C ASN B 36 82.424 61.593 27.770 1.00 18.94 C
ATOM 2903 O ASN B 36 82.865 60.768 28.585 1.00 18.04 o
ATOM 2904 CB ASN B 36 80.404 62.893 28.637 1.00 15.49 c
ATOM 2905 CG ASN B 36 80.105 63.991 29.652 1.00 18.24 c
ATOM 2906 ODl ASN B 36 80.760 64.136 30.689 1.00 21.37 0 ATOM 2907 ND2 ASN B 36 79.061 64.787 29.393 1.00 17.27 N
ATOM 2908 N ALA B 37 82.450 61.357 26.455 1.00 16.55 N
ATOM 2909 CA ALA B 37 83.035 60.129 25.929 1.00 12.94 c
ATOM 2910 C ALA B 37 84.479 60.003 26.404 1.00 19.48 c
ATOM 2911 O ALA B 37 84.887 58.931 26.854 1.00 16.36 O ATOM 2912 CB ALA B 37 83.006 60.113 24.395 1.00 17.12 c
ATOM 2913 N ALA B 38 85.254 61.082 26.287 1.00 19.45 N
ATOM 2914 CA ALA B 38 86.647 61.049 26.736 1.00 17.62 c
ATOM 2915 C ALA B 38 86.763 60.821 28.234 1.00 16.35 C
ATOM 2916 O ALA B 38 87.642 60.068 28.688 1.00 19.97 O ATOM 2917 CB ALA B 38 87.338 62.347 26.340 1.00 15.26 C
ATOM 2918 N LYS B 39 85.895 61.385 29.084 1.00 14.88 N
ATOM 2919 CA LYS B 39 85.901 61.135 30.520 1.00 15.65 C
ATOM 2920 C LYS B 39 85.664 59.647 30.810 1.00 15.04 C
ATOM 2921 O LYS B 39 86.327 59.029 31.670 1.00 17.25 O ATOM 2922 CB LYS B 39 84.797 61.963 31.195 1.00 13.01 C
ATOM 2923 CG LYS B 39 85.152 63.436 31.336 1.00 16.07 C
ATOM 2924 CD LYS B 39 83.981 64.250 31.914 1.00 17.28 C
ATOM 2925 CE LYS B 39 84.457 65.717 31.963 1.00 23.58 c
ATOM 2926 NZ LYS B 39 83.694 66.512 32.953 1.00 22.14 N ATOM 2927 N VAL B 40 84.767 59.013 30.031 1.00 16.86 N
ATOM 2928 CA VAL B 40 84.549 57.570 30.256 1.00 15.40 c
ATOM 2929 C VAL B 40 85.834 56.788 29.935 1.00 19.13 c
ATOM 2930 O VAL B 40 86.232 55.883 30.659 1.00 17.59 0
ATOM 2931 CB VAL B 40 83.418 56.974 29.421 1.00 14.63 c ATOM 2932 CGI VAL B 40 83.327 55.444 29.573 1.00 18.22 c
ATOM 2933 CG2 VAL B 40 82.066 57.551 29.814 1.00 16.24 c
ATOM 2934 N LYS B 41 86.465 57.134 28.806 1.00 17.77 N
ATOM 2935 CA LYS B 41 87.713 56.435 28.415 1.00 17.35 c
ATOM 2936 C LYS B 41 88.782 56.611 29.461 1.00 17.10 c ATOM 2937 O LYS B 41 89.,558 55.,679 29.,761 1.00 16.37 O
ATOM 2938 CB LYS B 41 88. ,091 56. ,942 27. ,004 1.00 15.63 C
ATOM 2939 CG LYS B 41 89. ,337 56. ,336 26. ,374 1.00 16.16 C
ATOM 2940 CD LYS B 41 89. .330 56. ,705 24. ,910 1.00 20.47 C
ATOM 2941 CE LYS B 41 90. ,499 56. ,198 24. ,097 1.00 32.61 C
ATOM 2942 NZ LYS B 41 91. ,783 56. ,437 24. ,797 1.00 25.93 N
ATOM 2943 N TYR B 42 88. ,895 57. ,790 30. ,084 1.00 15.00 N
ATOM 2944 CA TYR B 42 89. ,826 57. ,980 31. .171 1.00 19.39 C
ATOM 2945 C TYR B 42 89. ,511 56. ,996 32. .293 1.00 18.06 C
ATOM 2946 O TYR B 42 90. ,402 56. ,343 32. ,806 1.00 15.47 O
ATOM 2947 CB TYR B 42 89. ,780 59. ,402 31. ,721 1.00 19.03 C
ATOM 2948 CG TYR B 42 90. ,687 59. .655 32. ,903 1.00 21.12 C
ATOM 2949 CD1 TYR B 42 92. ,000 60. .061 32. ,704 1.00 20.08 C
ATOM 2950 CD2 TYR B 42 90. ,259 59. .467 34. ,208 1.00 18.89 C
ATOM 2951 CE1 TYR B 42 92. ,845 60. ,265 33. ,780 1.00 21.84 C
ATOM 2952 CE2 TYR B 42 91. ,083 59. .685 35. ,292 1.00 21.59 C
ATOM 2953 CZ TYR B 42 92. ,386 60. .079 35. ,060 1.00 25.44 C
ATOM 2954 OH TYR B 42 93. .258 60. ,300 36. .103 1.00 28.09 O
ATOM 2955 N VAL B 43 88. ,222 56. .872 32. .660 1.00 16.57 N
ATOM 2956 CA VAL B 43 87. .924 55. ,927 33. .751 1.00 17.22 C
ATOM 2957 C VAL B 43 88. .268 54. ,492 33. .369 1.00 18.41 C
ATOM 2958 O VAL B 43 88. ,787 53. .694 34. .173 1.00 19.16 O
ATOM 2959 CB VAL B 43 86. .443 56, .066 34. ,123 1.00 15.91 C
ATOM 2960 CGI VAL B 43 86. ,060 55. .029 35. ,183 1.00 15.52 C
ATOM 2961 CG2 VAL B 43 86. .229 57. .462 34. ,671 1.00 15.11 C
ATOM 2962 N GLN B 44 88. ,045 54. .148 32. ,127 1.00 16.42 N
ATOM 2963 CA GLN B 44 88. ,324 52. .852 31. .572 1.00 14.39 C
ATOM 2964 C GLN B 44 89. ,799 52. .482 31. .679 1.00 16.33 C
ATOM 2965 O GLN B 44 90. .153 51. .337 31. .946 1.00 18.86 O
ATOM 2966 CB GLN B 44 87, .958 52. .831 30. .087 1.00 14.26 C
ATOM 2967 CG GLN B 44 86, .486 52. .590 29. .827 1.00 17.37 C
ATOM 2968 CD GLN B 44 86. .197 52. .495 28. .344 1.00 17.65 C
ATOM 2969 OE1 GLN B 44 86. .357 53, .467 27. .614 1.00 17.67 O
ATOM 2970 NE2 GLN B 44 85. .749 51. .319 27. .909 1.00 18.10 N
ATOM 2971 N GLU B 45 90. .666 53. .451 31. .406 1.00 18.18 N
ATOM 2972 CA GLU B 45 92. .090 53. .186 31. .389 1.00 18.82 C
ATOM 2973 C GLU B 45 92. .866 53. .515 32. .636 1.00 20.67 C
ATOM 2974 O GLU B 45 93. .924 52. .875 32, .827 1.00 19.61 O
ATOM 2975 CB GLU B 45 92. .673 54. .042 30, .215 1.00 17.98 C
ATOM 2976 CG GLU B 45 92. .159 53, .564 28, .877 1.00 18.26 C
ATOM 2977 CD GLU B 45 92. .554 54, .418 27, .674 1.00 24.06 c
ATOM 2978 OE1 GLU B 45 93, .130 55, .502 27, .863 1.00 30.46 O
ATOM 2979 OE2 GLU B 45 92, .205 53, .983 26, .560 1.00 29.87 o
ATOM 2980 N LYS B 46 92, .454 54, .525 33, .414 1.00 15.25 N
ATOM 2981 CA LYS B 46 93. .260 55, .020 34, .515 1.00 18.10 C
ATOM 2982 C LYS B 46 92. .736 54. .996 35, .926 1.00 20.90 C
ATOM 2983 O LYS B 46 93. .491 55. .354 36, .841 1.00 23.35 o
ATOM 2984 CB LYS B 46 93. .611 56. .497 34, .178 1.00 22.72 C
ATOM 2985 CG LYS B 46 94. .615 56, .617 33, .044 1.00 30.17 c
ATOM 2986 CD LYS B 46 94, .268 57, .636 31, .994 1.00 38.77 c
ATOM 2987 CE LYS B 46 95, .380 57, .862 30, .984 1.00 43.17 c
ATOM 2988 NZ LYS B 46 94, .911 58, .643 29. .800 1.00 37.54 N
ATOM 2989 N VAL B 47 91, .489 54, .630 36. .166 1.00 17.52 N
ATOM 2990 CA VAL B 47 90, .884 54, .655 37. .490 1.00 16.01 c
ATOM 2991 C VAL B 47 90 .772 53, .239 38, .066 1.00 14.36 c
ATOM 2992 O VAL B 47 90 .044 52, .459 37, .492 1.00 18.15 o
ATOM 2993 CB VAL B 47 89 .506 55 .334 37, .430 1.00 15.12 c
ATOM 2994 CGI VAL B 47 88 .909 55 .406 38, .832 1.00 16.31 c
ATOM 2995 CG2 VAL B 47 89 .727 56 .780 36, .937 1.00 19.69 c 13S1
ATOM 2996 N GLY B 48 91.503 52.943 39.131 1.00 16.55 N
ATOM 2997 CA GLY B 48 91.387 51.585 39.695 1.00 19.29 C
ATOM 2998 C GLY B 48 90.043 51.399 40.401 1.00 18.66 C
ATOM 2999 O GLY B 48 89.530 52.341 40.986 1.00 14.72 0 ATOM 3000 N THR B 49 89.494 50.198 40.339 1.00 16.12 N
ATOM 3001 CA THR B 49 88.237 49.855 41.041 1.00 14.90 C
ATOM 3002 C THR B 49 88.393 48.415 41.533 1.00 17.66 C
ATOM 3003 O THR B 49 89.005 47.580 40.846 1.00 15.77 0
ATOM 3004 CB THR B 49 87.037 49.926 40.087 1.00 17.65 C ATOM 3005 OG1 THR B 49 86.992 51.266 39.546 1.00 15.90 O
ATOM 3006 CG2 THR B 49 85.672 49.699 40.741 1.00 16.18 C
ATOM 3007 N PHE B 50 87.760 48.147 42.674 1.00 12.91 N
ATOM 3008 CA PHE B 50 87.783 46.809 43.232 1.00 12.56 C
ATOM 3009 C PHE B 50 86.928 45.873 42.388 1.00 14.04 C ATOM 3010 O PHE B 50 85.972 46.212 41.701 1.00 14.93 O
ATOM 3011 CB PHE B 50 87.171 46.812 44.639 1.00 16.20 C
ATOM 3012 CG PHE B 50 88.114 47.169 45.740 1.00 14.17 c
ATOM 3013 CD1 PHE B 50 88.834 48.355 45.750 1.00 17.64 c
ATOM 3014 CD2 PHE B 50 88.291 46.322 46.824 1.00 17.20 c ATOM 3015 CE1 PHE B 50 89.697 48.670 46.788 1.00 17.52 c
ATOM 3016 CE2 PHE B 50 89.168 46.599 47.857 1.00 20.19 c
ATOM 3017 CZ PHE B 50 89.882 47.785 47.844 1.00 17.21 c
ATOM 3018 N TYR B 51 87.373 44.606 42.445 1.00 14.41 N
ATOM 3019 CA TYR B 51 86.674 43.510 41.828 1.00 13.73 c ATOM 3020 C TYR B 51 85.790 42.829 42.877 1.00 14.03 c
ATOM 3021 O TYR B 51 86.288 42.466 43.930 1.00 15.34 O
ATOM 3022 CB TYR B 51 87.646 42.442 41.381 1.00 12.64 c
ATOM 3023 CG TYR B 51 88.506 42.798 40.204 1.00 13.85 c
ATOM 3024 CD1 TYR B 51 89.572 43.690 40.443 1.00 15.01 c ATOM 3025 CD2 TYR B 51 88.330 42.263 38.939 1.00 15.30 c
ATOM 3026 CE1 TYR B 51 90.434 44.011 39.409 1.00 17.70 c
ATOM 3027 CE2 TYR B 51 89.183 42.587 37.887 1.00 18.70 c
ATOM 3028 CZ TYR B 51 90.209 43.475 38.170 1.00 15.33 c
ATOM 3029 OH TYR B 51 91.095 43.819 37.155 1.00 16.64 o ATOM 3030 N TRP B 52 84.484 42.728 42.594 1.00 11.83 N
ATOM 3031 CA TRP B 52 83.585 42.122 43.579 1.00 12.69 c
ATOM 3032 C TRP B 52 83.409 40.620 43.379 1.00 14.01 c
ATOM 3033 O TRP B 52 83.018 40.188 42.279 1.00 14.38 o
ATOM 3034 CB TRP B 52 82.193 42.751 43.450 1.00 14.32 c ATOM 3035 CG TRP B 52 82.162 44.154 43.985 1.00 14.78 c
ATOM 3036 CD1 TRP B 52 82.825 45.261 43.503 1.00 17.01 c
ATOM 3037 CD2 TRP B 52 81.431 44.580 45.136 1.00 10.23 c
ATOM 3038 NE1 TRP B 52 82.527 46.344 44.300 1.00 12.92 N
ATOM 3039 CE2 TRP B 52 81.691 45.947 45.313 1.00 11.33 c ATOM 3040 CE3 TRP B 52 80.575 43.916 46.032 1.00 13.21 c
ATOM 3041 CZ2 TRP B 52 81.101 46.657 46.346 1.00 14.79 c
ATOM 3042 CZ3 TRP B 52 79.982 44.607 47.073 1.00 11.88 c
ATOM 3043 CH2 TRP B 52 80.254 45.988 47.191 1.00 14.19 c
ATOM 3044 N ILE B 53 83.794 39.876 44.423 1.00 11.74 N ATOM 3045 CA ILE B 53 83.692 38.397 44.302 1.00 14.76 c
ATOM 3046 C ILE B 53 82.428 38.000 45.018 1.00 11.18 c
ATOM 3047 O ILE B 53 82.357 37.517 46.150 1.00 13.16 o
ATOM 3048 CB ILE B 53 84.928 37.720 44.892 1.00 16.03 c
ATOM 3049 CGI ILE B 53 86.217 38.340 44.377 1.00. 11.84 c ATOM 3050 CG2 ILE B 53 84.912 36.226 44.483 1.00 15.36 c
ATOM 3051 CD1 ILE B 53 86.356 38.462 42.856 1.00 14.62 c
ATOM 3052 N SER B 54 81.294 38.352 44.344 1.00 15.26 N
ATOM 3053 CA SER B 54 79.995 38.297 45.007 1.00 17.10 c
ATOM 3054 C SER B 54 79.253 36.975 45.018 1.00 12.48 c ATOM 3055 O SER B 54 78.137 36.937 45.535 1.00 14.16 o
ATOM 3056 CB SER B 54 79. 088 39. ,388 44. 431 1.00 17. 50 C
ATOM 3057 OG ASER B 54 79. 760 40. 633 44. ,392 0.50 14. 39 o
ATOM 3058 OG BSER B 54 78. 982 39. ,340 43. ,029 0.50 11. ,72 o
ATOM 3059 N ASN B 55 79. 855 35. 944 44. ,435 1.00 12. 63 N
ATOM 3060 CA ASN B 55 79. 276 34. ,607 44. 451 1.00 13. 77 C
ATOM 3061 C ASN B 55 80. ,417 33. ,640 44. ,177 1.00 18. 96 C
ATOM 3062 O ASN B 55 81. ,551 34. ,064 43. ,897 1.00 15. ,24 o
ATOM 3063 CB ASN B 55 78. ,063 34. ,514 43. ,523 1.00 10. ,44 c
ATOM 3064 CG ASN B 55 78. ,380 34. ,867 42. ,080 1.00 15. ,09 c
ATOM 3065 ODl ASN B 55 79. ,345 34. ,340 41. ,549 1.00 15. ,91 o
ATOM 3066 ND2 ASN B 55 77. ,637 35. ,804 41. ,488 1.00 17. ,05 N
ATOM 3067 N ILE B 56 80. ,140 32. ,340 44. ,256 1.00 14. ,37 N
ATOM 3068 CA ILE B 56 81. ,168 31. ,330 44. ,010 1.00 12. ,05 C
ATOM 3069 C ILE B 56 81. ,582 31. ,291 42. ,553 1.00 15. ,02 C
ATOM 3070 O ILE B 56 82. ,787 31. ,241 42. ,259 1.00 16. ,51 O
ATOM 3071 CB ILE B 56 80. ,609 29. ,989 44. ,520 1.00 13. ,92 C
ATOM 3072 CGI ILE B 56 80. .647 29. ,953 46. ,060 1.00 14. .27 C
ATOM 3073 CG2 ILE B 56 81. .303 28. ,780 43. ,946 1.00 13. .39 C
ATOM 3074 CD1 ILE B 56 79. ,734 28. ,896 46. ,661 1.00 18. .34 C
ATOM 3075 N PHE B 57 80. ,670 31. ,496 41. ,607 1.00 12. .96 N
ATOM 3076 CA PHE B 57 81. .087 31. .527 40. ,187 1.00 11. .15 C
ATOM 3077 C PHE B 57 82. .144 32. .597 39. ,972 1.00 18. .24 C
ATOM 3078 O PHE B 57 83. .073 32. .351 39. ,185 1.00 14. ,89 o
ATOM 3079 CB PHE B 57 79. .825 31. .815 39. .333 1.00 17. .42 C
ATOM 3080 CG PHE B 57 80, .111 32. .010 37. .873 1.00 18. .10 C
ATOM 3081 CD1 PHE B 57 80. .429 33. .246 37. .355 1.00 16. .97 c
ATOM 3082 CD2 PHE B 57 80. .052 30. .934 36. ,994 1.00 14. .67 c
ATOM 3083 CE1 PHE B 57 80, .738 33. .428 36. .019 1.00 19. .79 c
ATOM 3084 CE2 PHE B 57 80. .309 31. .126 35, ,654 1.00 17. .22 c
ATOM 3085 CZ PHE B 57 80. .668 32. .365 35, .150 1.00 15. .53 c
ATOM 3086 N LEU B 58 82. .051 33, .749 40, .663 1.00 12. .88 N
ATOM 3087 CA LEU B 58 82. .941 34. .882 40. .453 1.00 15. .64 c
ATOM 3088 C LEU B 58 84. .292 34. .713 41, .117 1.00 16. .65 c
ATOM 3089 O LEU B 58 85, .169 35. .545 40, .902 1.00 13. .78 o
ATOM 3090 CB LEU B 58 82. .288 36. .211 40, .863 1.00 14, .15 c
ATOM 3091 CG LEU B 58 81. .170 36. .613 39. .900 1.00 15, .42 c
ATOM 3092 CD1 LEU B 58 80. .372 37. .740 40. .500 1.00 15. .14 c
ATOM 3093 CD2 LEU B 58 81. .753 36. .966 38. .533 1.00 16. .23 c
ATOM 3094 N LEU B 59 84, .493 33, .550 41. .768 1.00 14. .14 N
ATOM 3095 CA LEU B 59 85, .882 33, .264 42. .190 1.00 14. .17 c
ATOM 3096 C LEU B 59 86, .811 33, .291 40. .991 1.00 15. .97 c
ATOM 3097 O LEU B 59 87, .976 33, .685 41. .212 1.00 17, .98 o
ATOM 3098 CB LEU B 59 85, .985 31, .894 42. .870 1.00 12, .98 c
ATOM 3099 CG LEU B 59 85, .333 31. .756 44, .252 1.00 16, .55 c
ATOM 3100 CD1 LEU B 59 85, .121 30, .298 44, .621 1.00 19. .47 c
ATOM 3101 CD2 LEU B 59 86, .193 32, .475 45, .310 1.00 17. .68 c
ATOM 3102 N ARG B 60 86 .369 33, .070 39, .762 1.00 16, .56 N
ATOM 3103 CA ARG B 60 87 .252 33, .082 38, .583 1.00 18, .08 c
ATOM 3104 C ARG B 60 87 .752 34, .471 38, .264 1.00 20, .54 c
ATOM 3105 O ARG B 60 88 .803 34, .657 37, .644 1.00 20, .75 o
ATOM 3106 CB ARG B 60 86 .466 32, .516 37, .411 1.00 21, .86 c
ATOM 3107 CG ARG B 60 85 .219 33, .309 37, .020 1.00 21, .71 c
ATOM 3108 CD ARG B 60 84 .396 32, .497 36, .023 1.00 28, .01 c
ATOM 3109 NE ARG B 60 83 .808 31 .296 36 .593 1.00 21 .97 N
ATOM 3110 CZ ARG B 60 83 .596 30 .115 36 .046 1.00 27 .05 c
ATOM 3111 NH1 ARG B 60 83 .941 29 .850 34 .800 1.00 22 .97 N
ATOM 3112 NH2 ARG B 60 83 .017 29 .129 36 .742 1.00 32 .90 N
ATOM 3113 N ASP B 61 87 .031 35 .497 38 .730 1.00 13 .93 N ATOM 3114 CA ASP B 61 87.471 36.,869 38.,545 1.00 17.,59 c
ATOM 3115 C ASP B 61 88.704 37. ,179 39. ,381 1.00 22. ,52 c
ATOM 3116 O ASP B 61 89.421 38. ,145 39. ,094 1.00 17. ,88 o
ATOM 3117 CB ASP B 61 86.353 37. 862 38. ,885 1.00 16. ,90 c ATOM 3118 CG ASP B 61 85.552 38. 222 37. ,655 1.00 24. ,41 c
ATOM 3119 ODl ASP B 61 85.883 37. ,820 36. ,516 1.00 26. 33 o
ATOM 3120 OD2 ASP B 61 84.560 38. ,958 37. ,845 1.00 20. ,11 o
ATOM 3121 N ILE B 62 88.965 36. ,384 40. ,410 1.00 15. ,89 N
ATOM 3122 CA ILE B 62 90.211 36. ,540 41. ,174 1.00 22. ,74 c ATOM 3123 C ILE B 62 91.347 36. ,208 40. ,208 1.00 24. ,25 c
ATOM 3124 O ILE B 62 92.316 37. ,001 40. ,151 1.00 20. ,29 o
ATOM 3125 CB ILE B 62 90.245 35. ,700 42. ,458 1.00 17. ,44 c
ATOM 3126 CGI ILE B 62 89.279 36. ,139 43. .559 1.00 15. ,61 c
ATOM 3127 CG2 ILE B 62 91.691 35. .767 43. .043 1.00 16. ,55 c ATOM 3128 CD1 ILE B 62 88.989 35. ,140 44. .653 1.00 21. .53 c
ATOM 3129 N ASP B 63 91.263 35. ,153 39. ,375 1.00 20. .12 N
ATOM 3130 CA ASP B 63 92.325 34. ,842 38. ,422 1.00 22. .02 C
ATOM 3131 C ASP B 63 92.476 35. ,889 37. .338 1.00 28. ,10 c
ATOM 3132 O ASP B 63 93.570 36. .181 36. ,843 1.00 26. ,70 o ATOM 3133 CB ASP B 63 92.099 33. ,458 37. .787 1.00 26. ,51 c
ATOM 3134 CG ASP B 63 92.012 32. ,385 38. .855 1.00 25. ,59 c
ATOM 3135 ODl ASP B 63 92.913 32. .296 39. ,718 1.00 32. ,65 o
ATOM 3136 OD2 ASP B 63 91.021 31. .610 38. .867 1.00 26. .76 o
ATOM 3137 N VAL B 64 91.387 36. ,560 36. ,943 1.00 19. .62 N ATOM 3138 CA VAL B 64 91.463 37. ,621 35. ,960 1.00 18. ,25 c
ATOM 3139 C VAL B 64 92.214 38. .797 36. ,588 1.00 21. ,72 c
ATOM 3140 O VAL B 64 93.012 39. .409 35. ,887 1.00 25. .35 o
ATOM 3141 CB VAL B 64 90.051 38. .101 35. .562 1.00 25. .41 c
ATOM 3142 CGI VAL B 64 90.120 39. .394 34. .752 1.00 22. .56 c ATOM 3143 CG2 VAL B 64 89.294 37. .027 34. .798 1.00 22. .99 c
ATOM 3144 N ALA B 65 91.924 39. .139 37. .848 1.00 18. .19 N
ATOM 3145 CA ALA B 65 92.546 40. .304 38. .485 1.00 17. .64 C
ATOM 3146 C ALA B 65 94.052 40. .091 38. .656 1.00 22. .70 C
ATOM 3147 O ALA B 65 94.871 40. .970 38. .477 1.00 23. .51 o ATOM 3148 CB ALA B 65 91.934 40. .531 39. .859 1.00 15. .79 C
ATOM 3149 N ILE B 66 94.375 38. .839 38. .975 1.00 21. .84 N
ATOM 3150 CA ILE B 66 95.781 38. .440 39. .170 1.00 28. .23 C
ATOM 3151 C ILE B 66 96.564 38. .586 37. .880 1.00 27. .27 C
ATOM 3152 O ILE B 66 97.681 39. .142 37. .852 1.00 25. .81 O ATOM 3153 CB ILE B 66 95.791 36, .984 39, .710 1.00 18. .66 C
ATOM 3154 CGI ILE B 66 95.610 36, .997 41, .200 1.00 19. .19 C
ATOM 3155 CG2 ILE B 66 97.156 36, .353 39, .354 1.00 30. .76 C
ATOM 3156 CD1 ILE B 66 95.212 35, .770 41, .980 1.00 22. ■ 60 c
ATOM 3157 N GLN B 67 96.014 38, .095 36, .786 1.00 23. .96 N ATOM 3158 CA GLN B 67 96.538 38, .148 35. .446 1.00 26. .59 c
ATOM 3159 C GLN B 67 96.741 39, .613 35. .061 1.00 31. .49 c
ATOM 3160 O GLN B 67 97.813 39, .964 34. .573 1.00 30. .87 o
ATOM 3161 CB GLN B 67 95.599 37, .486 34, .453 1.00 30. .04 c
ATOM 3162 CG GLN B 67 95.974 37, .661 32, .987 1.00 38. .09 c ATOM 3163 CD GLN B 67 95.313 36, .596 32, .124 1.00 38, .32 c
ATOM 3164 OE1 GLN B 67 94.872 35, .587 32, .686 1.00 44. .84 o
ATOM 3165 NE2 GLN B 67 95.272 36, .846 30, .822 1.00 43, .52 N
ATOM 3166 N ASN B 68 95.729 40, .435 35 .384 1.00 26 .37 N
ATOM 3167 CA ASN B 68 95.856 41, .857 35 .070 1.00 26, .18 C ATOM 3168 C ASN B 68 96.902 42 .518 35 .948 1.00 24, .99 C
ATOM 3169 O ASN B 68 97.641 43 .373 35 .419 1.00 27 .97 o
ATOM 3170 CB ASN B 68 94.489 42 .548 35 .204 1.00 22 .86 c
ATOM 3171 CG ASN B 68 93.435 42 .064 34 .261 1.00 23 .04 c
ATOM 3172 ODl ASN B 68 93.593 41 .520 33 .154 1.00 24 .93 o ATOM 3173 ND2 ASN B 68 92.163 42.255 34.667 1.00 19.91 N
ATOM 3174 N ALA B 69 97.081 42.130 37.202 1.00 24.84 N
ATOM 3175 CA ALA B 69 98.108 42.702 38.062 1.00 17.02 C
ATOM 3176 c ALA B 69 99.505 42.250 37.579 1.00 28.34 C ATOM 3177 O ALA B 69 100.468 42.988 37.819 1.00 29.63 0
ATOM 3178 CB ALA B 69 97.941 42.370 39.523 1.00 21.95 C
ATOM 3179 N ARG B 70 99.608 41.108 36.908 1.00 28.89 N
ATOM 3180 CA ARG B 70 100.912 40.675 36.369 1.00 27.69 C
ATOM 3181 c ARG B 70 101.172 41.393 35.055 1.00 34.67 C ATOM 3182 O ARG B 70 102.314 41.815 34.788 1.00 38.31 o
ATOM 3183 CB ARG B 70 100.962 39.139 36.232 1.00 28.12 C
ATOM 3184 CG ARG B 70 101.205 38.453 37.562 1.00 20.96 C
ATOM 3185 CD ARG B 70 101.046 36.944 37.597 1.00 25.41 C
ATOM 3186 NE ARG B 70 101.052 36.271 38.872 1.00 22.35 N ATOM 3187 CZ ARG B 70 100.582 35.084 39.331 1.00 17.36 C
ATOM 3188 NH1 ARG B 70 99.918 34.222 38.627 1.00 29.75 N
ATOM 3189 NH2 ARG B 70 100.766 34.790 40.617 1.00 26.53 N
ATOM 3190 N ALA B 71 100.161 41.596 34.219 1.00 30.93 N
ATOM 3191 CA ALA B 71 100.294 42.318 32.968 1.00 30.96 C ATOM 3192 C ALA B 71 100.677 43.782 33.204 1.00 37.18 C
ATOM 3193 O ALA B 71 101.481 44.352 32.459 1.00 39.92 o
ATOM 3194 CB ALA B 71 99.018 42.308 32.147 1.00 29.82 C
ATOM 3195 N ALA B 72 100.094 44.395 34.233 1.00 32.39 N
ATOM 3196 CA ALA B 72 100.363 45.798 34.516 1.00 33.17 C ATOM 3197 C ALA B 72 101.778 45.996 35.037 1.00 37.85 C
ATOM 3198 O ALA B 72 102.537 46.828 34.537 1.00 31.27 0
ATOM 3199 CB ALA B 72 99.402 46.323 35.586 1.00 31.02 c
ATOM 3200 N LYS B 73 102.150 45.181 36.027 1.00 36.44 N
ATOM 3201 CA LYS B 73 103.486 45.309 36.615 1.00 41.38 c ATOM 3202 C LYS B 73 104.577 44.894 35.642 1.00 38.65 c
ATOM 3203 O LYS B 73 105.734 45.315 35.790 1.00 41.24 0
ATOM 3204 CB LYS B 73 103.547 44.645 37.973 1.00 46.45 c
ATOM 3205 CG LYS B 73 104.074 43.240 38.070 1.00 44.37 c
ATOM 3206 CD LYS B 73 105.446 43.196 38.718 1.00 51.56 c ATOM 3207 CE LYS B 73 105.404 43.638 40.174 1.00 55.82 c
ATOM 3208 NZ LYS B 73 104.882 42.582 41.083 1.00 57.90 N
ATOM 3209 N ALA B 74 104.258 44.186 34.569 1.00 40.93 N
ATOM 3210 CA ALA B 74 105.166 43.862 33.486 1.00 44.54 c
ATOM 3211 C ALA B 74 105.270 45.016 32.486 1.00 46.62 c ATOM 3212 O ALA B 74 106.250 45.084 31.734 1.00 46.58 0
ATOM 3213 CB ALA B 74 104.759 42.604 32.742 1.00 40.60 c
ATOM 3214 N ARG B 75 104.321 45.956 32.501 1.00 44.45 N
ATOM 3215 CA ARG B 75 104.414 47.111 31.609 1.00 43.68 c
ATOM 3216 C ARG B 75 105.075 48.270 32.358 1.00 40.42 c ATOM 3217 O ARG B 75 105.136 49.398 31.869 1.00 44.75 0
ATOM 3218 CB ARG B 75 103.095 47.509 30.995 1.00 47.64 c
ATOM 3219 CG ARG B 75 102.059 48.208 31.837 1.00 50.87 c
ATOM 3220 CD ARG B 75 100.792 48.450 31.029 1.00 55.65 c
ATOM 3221 NE ARG B 75 100.644 47.576 29.868 1.00 51.77 N ATOM 3222 CZ ARG B 75 99.612 46.760 29.660 1.00 54.53 c
ATOM 3223 NH1 ARG B 75 98.626 46.716 30.555 1.00 45.97 N
ATOM 3224 NH2 ARG B 75 99.570 46.002 28.568 1.00 49.67 N
ATOM 3225 N GLY B 76 105.608 47.960 33.530 1.00 37.48 ' N
ATOM 3226 CA GLY B 76 106.335 48.878 34.357 1.00 38.17 C ATOM 3227 C GLY B 76 105.619 49.433 35.566 1.00 40.99 c
ATOM 3228 O GLY B 76 106.260 50.163 36.330 1.00 40.23 0
ATOM 3229 N GLU B 77 104.338 49.116 35.769 1.00 39.57 N
ATOM 3230 CA GLU B 77 103.619 49.694 36.910 1.00 35.86 c
ATOM 3231 C GLU B 77 103.784 48.907 38.201 1.00 31.34 c 1421
ATOM 3232 O GLU B 77 104.348 47.812 38.247 1.00 34.21 O
ATOM 3233 CB GLU B 77 102.148 49.842 36.527 1.00 36.57 C
ATOM 3234 CG GLU B 77 101.910 50.384 35.118 1.00 32.98 C
ATOM 3235 CD GLU B 77 100.472 50.184 34.691 1.00 35.04 C ATOM 3236 OE1 GLU B 77 99.679 49.697 35.529 1.00 39.41 O
ATOM 3237 OE2 GLU B 77 100.175 50.525 33.532 1.00 39.68 O
ATOM 3238 N ASN B 78 103.270 49.434 39.300 1.00 29.74 N
ATOM 3239 CA ASN B 78 103.318 48.849 40.626 1.00 33.87 C
ATOM 3240 C ASN B 78 101.927 48.815 41.259 1.00 29.45 C ATOM 3241 O ASN B 78 101.564 49.642 42.088 1.00 29.17 O
ATOM 3242 CB ASN B 78 104.207 49.732 41.502 1.00 40.90 C
ATOM 3243 CG ASN B 78 104.759 48.982 42.691 1.00 53.71 c
ATOM 3244 ODl ASN B 78 104.943 49.534 43.779 1.00 56.49 O
ATOM 3245 ND2 ASN B 78 105.032 47.692 42.515 1.00 57.03 N ATOM 3246 N PRO B 79 101.166 47.796 40.934 1.00 30.67 N
ATOM 3247 CA PRO B 79 99.756 47.717 41.296 1.00 24.65 c
ATOM 3248 C PRO B 79 99.415 47.064 42.601 1.00 24.32 c
ATOM 3249 O PRO B 79 100.176 46.309 43.201 1.00 25.61 0
ATOM 3250 CB PRO B 79 99.142 46.816 40.199 1.00 25.81 c ATOM 3251 CG PRO B 79 100.299 45.838 40.064 1.00 27.62 c
ATOM 3252 CD PRO B 79 101.529 46.745 39.972 1.00 31.59 c
ATOM 3253 N ILE B 80 98.196 47.424 43.059 1.00 20.77 N
ATOM 3254 CA ILE B 80 97.637 46.743 44.226 1.00 19.20 c
ATOM 3255 C ILE B 80 96.211 46.367 43.762 1.00 23.06 c ATOM 3256 O ILE B 80 95.556 47.217 43.192 1.00 20.46 0
ATOM 3257 CB ILE B 80 97.649 47.484 45.527 1.00 19.08 c
ATOM 3258 CGI ILE B 80 96.951 46.679 46.638 1.00 18.64 c
ATOM 3259 CG2 ILE B 80 96.981 48.851 45.340 1.00 23.47 c
ATOM 3260 CD1 ILE B 80 97.181 47.154 48.044 1.00 17.98 c ATOM 3261 N VAL B 81 95.838 45.122 43.976 1.00 18.21 N
ATOM 3262 CA VAL B 81 94.534 44.615 43.513 1.00 18.86 c
ATOM 3263 C VAL B 81 93.512 44.736 44.620 1.00 21.20 c
ATOM 3264 O VAL B 81 93.661 44.252 45.748 1.00 18.06 0
ATOM 3265 CB VAL B 81 94.658 43.113 43.125 1.00 23.72 c ATOM 3266 CGI VAL B 81 93.311 42.502 42.727 1.00 16.06 c
ATOM 3267 CG2 VAL B 81 95.608 42.840 41.968 1.00 23.95 c
ATOM 3268 N GLY B 82 92.378 45.440 44.324 1.00 18.45 N
ATOM 3269 CA GLY B 82 91.308 45.487 45.330 1.00 15.70 c
ATOM 3270 C GLY B 82 90.294 44.370 45.026 1.00 13.73 c ATOM 3271 O GLY B 82 89.804 44.235 43.929 1.00 17.77 o
ATOM 3272 N LEU B 83 89.963 43.631 46.085 1.00 14.05 N
ATOM 3273 CA LEU B 83 88.964 42.558 45.968 1.00 17.56 c
ATOM 3274 C LEU B 83 87.924 42.737 47.057 1.00 15.62 c
ATOM 3275 O LEU B 83 88.271 43.147 48.177 1.00 16.11 o ATOM 3276 CB LEU B 83 89.571 41.157 46.130 1.00 16.40 c
ATOM 3277 CG LEU B 83 90.630 40.728 45.112 1.00 14.56 c
ATOM 3278 CD1 LEU B 83 91.176 39.351 45.502 1.00 18.19 c
ATOM 3279 CD2 LEU B 83 90.104 40.735 43.678 1.00 14.73 c
ATOM 3280 N VAL B 84 86.627 42.452 46.736 1.00 12.40 N ATOM 3281 CA VAL B 84 85.581 42.466 47.717 1.00 9.97 c
ATOM 3282 C VAL B 84 85.119 41.030 48.067 1.00 12.63 c
ATOM 3283 O VAL B 84 84.737 40.324 47.149 1.00 14.90 o
ATOM 3284 CB VAL B 84 84.314 43.259 47.363 1.00 11.26 'v.
ATOM 3285 CGI VAL B 84 83.414 43.471 48.557 1.00 15.71 c ATOM 3286 CG2 VAL B 84 84.746 44.684 46.936 1.00 12.74 c
ATOM 3287 N LEU B 85 85.335 40.635 49.312 1.00 12.20 N
ATOM 3288 CA LEU B 85 84.902 39.271 49.736 1.00 16.61 c
ATOM 3289 C LEU B 85 83.483 39.484 50.236 1.00 16.55 c
ATOM 3290 0 LEU B 85 83.281 40.195 51.230 1.00 14.38 0 ATOM 3291 CB LEU B 85 85.889 38.,744 50.,751 1.00 16.,92 c
ATOM 3292 CG LEU B 85 85.764 37. ,272 51. ,235 1.00 11. ,24 c
ATOM 3293 CD1 LEU B 85 87.185 36. ,884 51. ,677 1.00 15. ,64 c
ATOM 3294 CD2 LEU B 85 84.716 37. ,100 52. ,277 1.00 18. ,62 c
ATOM 3295 N TYR B 86 82.498 38. ,954 49. ,465 1.00 13. ,72 N
ATOM 3296 CA TYR B 86 81.104 39. ,294 49. .795 1.00 12. ,98 c
ATOM 3297 C TYR B 86 80.179 38. ,128 49. .427 1.00 12. .07 c
ATOM 3298 O TYR B 86 79.588 38. ,120 48. .336 1.00 14. .09 o
ATOM 3299 CB TYR B 86 80.739 40. ,507 48. ,922 1.00 16. .67 c
ATOM 3300 CG TYR B 86 79.377 41. ,112 49. ,048 1.00 12. .71 c
ATOM 3301 CD1 TYR B 86 78.819 41. ,467 50. ,254 1.00 9. .83 c
ATOM 3302 CD2 TYR B 86 78.617 41. .371 47. ,901 1.00 14. .46 c
ATOM 3303 CE1 TYR B 86 77.563 42. ,063 50. ,364 1.00 11. .41 c
ATOM 3304 CE2 TYR B 86 77.386 41. ,979 47. .992 1.00 12. .89 c
ATOM 3305 CZ TYR B 86 76.843 42. .320 49. .195 1.00 15. .90 c
ATOM 3306 OH TYR B 86 75.609 42. ,945 49. .266 1.00 15. .27 o
ATOM 3307 N ASN B 87 80.096 37. ,198 50. .341 1.00 15. .20 N
ATOM 3308 CA ASN B 87 79.150 36. .062 50. .062 1.00 11. .63 c
ATOM 3309 C ASN B 87 78.629 35. .510 51. .379 1.00 12. .79 c
ATOM 3310 O ASN B 87 78.400 34. .272 51. .428 1.00 13. .83 o
ATOM 3311 CB ASN B 87 79.811 35. .016 49. .174 1.00 12. .57 c
ATOM 3312 CG ASN B 87 78.746 34. .160 48. .458 1.00 10. .94 c
ATOM 3313 ODl ASN B 87 77.582 34. .519 48. .394 1.00 13. .75 o
ATOM 3314 ND2 ASN B 87 79.185 33. .053 47. .881 1.00 16. .09 N
ATOM 3315 N LEU B 88 78.462 36. .316 52. .424 1.00 14. .04 N
ATOM 3316 CA LEU B 88 78.049 35. .760 53. .714 1.00 15. .61 C
ATOM 3317 C LEU B 88 76.730 35. .027 53. .630 1.00 17. .12 C
ATOM 3318 O LEU B 88 75.794 35. .390 52. .907 1.00 14. .00 o
ATOM 3319 CB LEU B 88 77.884 36. .944 54. .667 1.00 17. .52 c
ATOM 3320 CG LEU B 88 78.240 36. .818 56. .140 1.00 27. .36 c
ATOM 3321 CD1 LEU B 88 79.664 36. .360 56. .359 1.00 18. .97 c
ATOM 3322 CD2 LEU B 88 77.936 38. .171 56. .773 1.00 25. .99 c
ATOM 3323 N PRO B 89 76.595 33. .928 54. .345 1.00 14. .93 N
ATOM 3324 CA PRO B 89 75.300 33. .272 54. .481 1.00 15. .30 C
ATOM 3325 C PRO B 89 74.319 34. .269 55. .084 1.00 18. .82 C
ATOM 3326 O PRO B 89 74.671 35. .073 55. .971 1.00 17. .39 o
ATOM 3327 CB PRO B 89 75.454 32. .089 55. .441 1.00 18. .75 c
ATOM 3328 CG PRO B 89 76.911 32. .127 55. .775 1.00 22. .27 c
ATOM 3329 CD PRO B 89 77.598 33. .384 55. .270 1.00 17. .79 c
ATOM 3330 N ASP B 90 73.075 34. .337 54. .620 1.00 14. .45 N
ATOM 3331 CA ASP B 90 72.078 35. .307 55. .049 1.00 13. .10 c
ATOM 3332 C ASP B 90 72.598 36. .756 54. .898 1.00 17, .12 c
ATOM 3333 O ASP B 90 72.337 37. .603 55, .727 1.00 14, .68 o
ATOM 3334 CB ASP B 90 71.627 35. .011 56, .490 1.00 15, .34 c
ATOM 3335 CG ASP B 90 70.821 33. .718 56, .516 1.00 16, .30 c
ATOM 3336 ODl ASP B 90 70.637 33. .052 55, .464 1.00 17, .37 o
ATOM 3337 OD2 ASP B 90 70.315 33, .377 57, .608 1.00 16, .22 o
ATOM 3338 N ARG B 91 73.262 36. .976 53, .766 1.00 15, .09 N
ATOM 3339 CA ARG B 91 73.846 38. .280 53, .397 1.00 14, .08 C
ATOM 3340 C ARG B 91 72.850 39. .393 53, .402 1.00 13, .92 c
ATOM 3341 O ARG B 91 71.705 39. .187 52, .965 1.00 14, .74 o
ATOM 3342 CB ARG B 91 74.452 38. .102 51, .977 1.00 11. .17
ATOM 3343 CG ARG B 91 75.513 39. .121 51, .618 1.00 13. .54
ATOM 3344 CD ARG B 91 76.207 38. .741 50, .329 1.00 16, .43 c
ATOM 3345 NE ARG B 91 75.305 39 .005 49 .180 1.00 11 .52 N
ATOM 3346 CZ ARG B 91 75.678 38 .748 47 .931 1.00 12, .08 c
ATOM 3347 NH1 ARG B 91 76.862 38 .249 47 .617 1.00 12 .65 N
ATOM 3348 NH2 ARG B 91 74.802 39 .025 46 .956 1.00 13 .47 N
ATOM 3349 N ASP B 92 73.193 40 .557 53 .927 1.00 15 .59 N ATOM 3350 CA ASP B 92 72.285 41.,720 54.,001 1.00 13..61 c
ATOM 3351 C ASP B 92 70.999 41. ,306 54. .686 1.00 17. ,53 c
ATOM 3352 O ASP B 92 69.886 41. ,474 54. .202 1.00 14. ,63 o
ATOM 3353 CB ASP B 92 71.990 42. ,294 52. .604 1.00 13. 48 c
ATOM 3354 CG ASP B 92 73.246 42. ,882 51. ,985 1.00 16. ,12 c
ATOM 3355 ODl ASP B 92 73.757 43. ,901 52. ,521 1.00 15. ,18 o
ATOM 3356 OD2 ASP B 92 73.727 42. ,331 50. ,969 1.00 15. ,75 o
ATOM 3357 N CYS B 93 71.155 40. .868 55. ,957 1.00 17. ,61 N
ATOM 3358 CA CYS B 93 70.009 40. .272 56. ,632 1.00 20. ,60 c
ATOM 3359 C CYS B 93 68.842 41. .222 56. ,804 1.00 16. ,80 c
ATOM 3360 O CYS B 93 67.718 40. .751 57. ,022 1.00 20. 22 o
ATOM 3361 CB CYS B 93 70.440 39. .580 57. ,940 1.00 15. ,36 c
ATOM 3362 SG CYS B 93 71.096 40. ,824 59. ,138 1.00 15. ,95 S
ATOM 3363 N SER B 94 69.052 42. .527 56. .734 1.00 19. ,34 N
ATOM 3364 CA SER B 94 68.034 43. .538 56. .905 1.00 24. ,34 c
ATOM 3365 C SER B 94 66.845 43. .260 55. .976 1.00 25. ,94 c
ATOM 3366 O SER B 94 65.712 43. ,477 56. .391 1.00 31. ,09 o
ATOM 3367 CB SER B 94 68.601 44. .929 56. .610 1.00 25. ,66 c
ATOM 3368 OG SER B 94 69.396 44. .897 55. .419 1.00 28. ,46 o
ATOM 3369 N ALA B 95 67.134 42. .748 54. ,757 1.00 23. ,27 N
ATOM 3370 CA ALA B 95 66.043 42. ,455 53. ,839 1.00 23. ,45 c
ATOM 3371 C ALA B 95 65.176 41. ,268 54. .217 1.00 25. ,46 c
ATOM 3372 O ALA B 95 64.118 41. .102 53. .585 1.00 29. ,31 o
ATOM 3373 CB ALA B 95 66.601 42. .230 52. .433 1.00 28. ,35 c
ATOM 3374 N GLY B 96 65.558 40. ,404 55. .153 1.00 18. ,90 N
ATOM 3375 CA GLY B 96 64.738 39. .292 55. .575 1.00 16. ,51 c
ATOM 3376 C GLY B 96 65.130 37. ,951 54. .950 1.00 21. ,15 c
ATOM 3377 O GLY B 96 64.644 36. .899 55. .360 1.00 20. .60 o
ATOM 3378 N GLU B 97 66.086 37. .958 54. .003 1.00 16. .87 N
ATOM 3379 CA GLU B 97 66.480 36. .715 53, .347 1.00 16. .60 C
ATOM 3380 C GLU B 97 67.843 36. .965 52. .702 1.00 15. .32 C
ATOM 3381 O GLU B 97 68.070 38. .157 52. .454 1.00 13. .74 O
ATOM 3382 CB GLU B 97 65.475 36. .336 52. .237 1.00 19. .41 C
ATOM 3383 CG GLU B 97 65.767 35. .072 51. .479 1.00 20. .53 C
ATOM 3384 CD GLU B 97 64.839 34. .821 50. .290 1.00 21. .51 c
ATOM 3385 OE1 GLU B 97 63.895 35. .597 50. .119 1.00 20. .50 o
ATOM 3386 OE2 GLU B 97 65.046 33. .804 49. .589 1.00 26. .57 o
ATOM 3387 N SER B 98 68.710 35. .979 52. .574 1.00 16. .47 N
ATOM 3388 CA SER B 98 70.010 36. .336 52. .010 1.00 16. .57 c
ATOM 3389 C SER B 98 69.889 37. .053 50. .670 1.00 15. .71 c
ATOM 3390 O SER B 98 69.141 36. .612 49. .797 1.00 19. .00 o
ATOM 3391 CB SER B 98 70.801 35, .041 51. .768 1.00 14. .64 c
ATOM 3392 OG SER B 98 72.123 35, .331 51. .379 1.00 13. .12 o
ATOM 3393 N SER B 99 70.707 38. .063 50. .493 1.00 16. .31 N
ATOM 3394 CA SER B 99 70.822 38, .773 49. .214 1.00 15. .12 c
ATOM 3395 C SER B 99 71.707 37, .998 48. .234 1.00 15. .31 c
ATOM 3396 O SER B 99 71.769 38, .379 47. .076 1.00 16. .33 o
ATOM 3397 CB SER B 99 71.417 40, .163 49. .396 1.00 16. .49 c
ATOM 3398 OG SER B 99 72.754 40, .162 49. .876 1.00 15. .92 o
ATOM 3399 N GLY B 100 72.381 36. .966 48. .679 1.00 15. .73 N
ATOM 3400 CA GLY B 100 73.262 36. .129 47. .906 1.00 13. .03 C
ATOM 3401 C GLY B 100 72.799 34. .671 47. .892 1.00 13. .87 c
ATOM 3402 O GLY B 100 71.698 34. .327 48. .386 1.00 15. .71 o
ATOM 3403 N GLU B 101 73.652 33. .811 47. .359 1.00 11. .69 N
ATOM 3404 CA GLU B 101 73.278 32, .415 47, .187 1.00 15. .02 c
ATOM 3405 C GLU B 101 73.360 31, .535 48, .421 1.00 18. .59 c
ATOM 3406 O GLU B 101 72.787 30, .421 48, .383 1.00 16. .26 o
ATOM 3407 CB GLU B 101 74.214 31, .817 46, .127 1.00 13. .93 c
ATOM 3408 CG GLU B 101 75.670 31, .717 46, .493 1.00 13. .37 c ATOM 3409 CD GLU B 101 76.649 31.,626 45.,365 1.00 16.,54 C
ATOM 3410 OE1 GLU B 101 76.271 31. .479 44. ,184 1.00 17. ,14 O
ATOM 3411 OE2 GLU B 101 77.854 31. ,744 45. ,716 1.00 15. .54 o
ATOM 3412 N LEU B 102 74.055 31. ,928 49. ,470 1.00 16. .38 N
ATOM 3413 CA LEU B 102 74.171 31. ,114 50. ,681 1.00 15. ,29 c
ATOM 3414 C LEU B 102 73.216 31. .505 51. ,785 1.00 14. .96 c
ATOM 3415 O LEU B 102 72.915 32. ,670 52. ,036 1.00 14. ,26 o
ATOM 3416 CB LEU B 102 75.611 31. .184 51. ,209 1.00 14. ,48 c
ATOM 3417 CG LEU B 102 76.703 30. .761 50. ,220 1.00 17. ,33 c
ATOM 3418 CD1 LEU B 102 78.042 30. .799 50. .932 1.00 15. .63 c
ATOM 3419 CD2 LEU B 102 76.414 29. ,358 49. ,699 1.00 16. .22 c
ATOM 3420 N LYS B 103 72.627 30. ,482 52. ,427 1.00 16. ,41 N
ATOM 3421 CA LYS B 103 71.656 30. .716 53. ,489 1.00 16. ,99 C
ATOM 3422 C LYS B 103 72.058 29. ,882 54. .711 1.00 15. .52 C
ATOM 3423 O LYS B 103 72.422 28. ,704 54. .548 1.00 17. .11 o
ATOM 3424 CB LYS B 103 70.220 30. ,301 53. .103 1.00 18. .12 C
ATOM 3425 CG LYS B 103 69.770 30. ,941 51. .788 1.00 13. .55 c
ATOM 3426 CD LYS B 103 68.263 30. ,726 51. .558 1.00 20. .50 c
ATOM 3427 CE LYS B 103 67.928 31. ,352 50. .210 1.00 20. .50 c
ATOM 3428 NZ LYS B 103 66.456 31. .179 49. .879 1.00 20. .97 N
ATOM 3429 N LEU B 104 71.895 30. ,436 55. .912 1.00 15. .54 N
ATOM 3430 CA LEU B 104 72.323 29. ,640 57. .085 1.00 18. .37 C
ATOM 3431 C LEU B 104 71.534 28. .333 57. .226 1.00 17. .70 C
ATOM 3432 O LEU B 104 72.153 27. .292 57. .539 1.00 21. .48 O
ATOM 3433 CB LEU B 104 72.237 30. .470 58. .361 1.00 19. .22 C
ATOM 3434 CG LEU B 104 73.351 31. .511 58. .460 1.00 18. ,43 C
ATOM 3435 CD1 LEU B 104 73.039 32. .540 59. .546 1.00 16. .79 c
ATOM 3436 CD2 LEU B 104 74.707 30. .896 58. .759 1.00 20. .30 c
ATOM 3437 N SER B 105 70.262 28. ,420 56. .853 1.00 15. .63 N
ATOM 3438 CA SER B 105 69.424 27. .197 56. .887 1.00 22. .72 C
ATOM 3439 C SER B 105 69.716 26. .184 55. .801 1.00 25. ,35 C
ATOM 3440 O SER B 105 69.107 25. .090 55. .816 1.00 25. .55 O
ATOM 3441 CB SER B 105 67.940 27. .580 56. .798 1.00 25. .19 c
ATOM 3442 OG SER B 105 67.655 28. .248 55, .590 1.00 22. .90 O
ATOM 3443 N GLN B 106 70.579 26. .437 54. .838 1.00 24. .54 N
ATOM 3444 CA GLN B 106 71.020 25. .557 53. .787 1.00 19. .81 c
ATOM 3445 C GLN B 106 72.513 25. .283 53. .898 1.00 17, .26 c
ATOM 3446 O GLN B 106 73.328 25. .300 52. .971 1.00 19, .40 O
ATOM 3447 CB GLN B 106 70.674 26. .095 52. .384 1.00 24. .04 c
ATOM 3448 CG GLN B 106 69.197 26. .406 52. .243 1.00 27. .32 c
ATOM 3449 CD GLN B 106 68.780 26, .862 50. .863 1.00 25. .24 c
ATOM 3450 OE1 GLN B 106 69.575 27. .265 50. .002 1.00 27. .75 O
ATOM 3451 NE2 GLN B 106 67.474 26. .821 50. .626 1.00 32. .87 N
ATOM 3452 N ASN B 107 72.935 24. .976 55. .142 1.00 17, .62 N
ATOM 3453 CA ASN B 107 74.327 24. .653 55. .431 1.00 16, .37 C
ATOM 3454 C ASN B 107 75.287 25. .772 54. .989 1.00 17, .04 C
ATOM 3455 O ASN B 107 76.401 25. .529 54. .569 1.00 18, .76 O
ATOM 3456 CB ASN B 107 74.759 23. .358 54. .721 1.00 18. .52 c
ATOM 3457 CG ASN B 107 76.035 22. .716 55. .196 1.00 14. .62 c
ATOM 3458 ODl ASN B 107 76.850 22. .091 54, .472 1.00 23. .47 O
ATOM 3459 ND2 ASN B 107 76.342 22. .805 56, .481 1.00 16. .64 N
ATOM 3460 N GLY B 108 74.789 27. .008 55. .135 1.00 20. .03 N
ATOM 3461 CA GLY B 108 75.529 28. .138 54, .573 1.00 15. .91 C
ATOM 3462 C GLY B 108 76.853 28. .453 55. .201 1.00 15. .34 C
ATOM 3463 O GLY B 108 77.800 28. .841 54, .531 1.00 14. .99 O
ATOM 3464 N LEU B 109 76.918 28. .350 56. .548 1.00 17. .11 N
ATOM 3465 CA LEU B 109 78.238 28. .582 57, .170 1.00 16. .63 C
ATOM 3466 C LEU B 109 79.308 27, .666 56, .601 1.00 16. .78 C
ATOM 3467 O LEU B 109 80.394 28, .102 56, .264 1.00 17, .74 o ATOM 3468 CB LEU B 109 78.,045 28..403 58..674 1.00 16.,02 C
ATOM 3469 CG LEU B 109 79. ,285 28. ,695 59. .550 1.00 18. .11 C
ATOM 3470 CD1 LEU B 109 79. ,918 30. ,037 59. .214 1.00 21. .27 c
ATOM 3471 CD2 LEU B 109 78. ,825 28. ,695 61. .011 1.00 21. ,87 c
ATOM 3472 N ASN B 110 79. ,082 26. ,340 56. ,525 1.00 18. ,97 N
ATOM 3473 CA ASN B 110 80. ,055 25. ,430 55. .940 1.00 19. ,83 C
ATOM 3474 C ASN B 110 80. ,390 25. ,650 54. .475 1.00 13. ,49 c
ATOM 3475 O ASN B 110 81. ,532 25. .583 54. .036 1.00 17. .00 o
ATOM 3476 CB ASN B 110 79. ,560 23. ,960 56. .072 1.00 26. ,50 c
ATOM 3477 CG ASN B 110 79. ,843 23. ,395 57. .451 1.00 25. ,67 c
ATOM 3478 ODl ASN B 110 79. ,055 22. ,559 57. .915 1.00 31. ,15 o
ATOM 3479 ND2 ASN B 110 80. ,911 23. .824 58. ,102 1.00 22. .53 N
ATOM 3480 N ARG B 111 79. .372 25. .929 53. .639 1.00 15. .53 N
ATOM 3481 CA ARG B 111 79. .602 26. .241 52. .240 1.00 18. ,42 C
ATOM 3482 C ARG B 111 80. ,426 27. .536 52. .103 1.00 12. ,97 C
ATOM 3483 O ARG B 111 81. ,265 27. .589 51. .220 1.00 16. ,22 O
ATOM 3484 CB ARG B 111 78. ,251 26. .371 51. .550 1.00 19. ,94 c
ATOM 3485 CG ARG B 111 77. ,526 25. ,045 51. .335 1.00 23. ,93 c
ATOM 3486 CD ARG B 111 76. ,123 25. ,319 50. .813 1.00 27. ,24 c
ATOM 3487 NE ARG B 111 75. ,432 24. ,095 50. .438 1.00 29. ,18 N
ATOM 3488 CZ ARG B 111 74. ,175 23. ,977 50. ,018 1.00 32. .12 C
ATOM 3489 NH1 ARG B 111 73. ,334 24. ,981 49. ,893 1.00 27. .86 N
ATOM 3490 NH2 ARG B 111 73. ,780 22. ,735 49. .720 1.00 33. .98 N
ATOM 3491 N TYR B 112 80. ,153 28. ,503 52. .975 1.00 15. .72 N
ATOM 3492 CA TYR B 112 80. ,949 29. .738 52. .898 1.00 16. ,36 C
ATOM 3493 C TYR B 112 82. .409 29. .452 53. .196 1.00 16. .66 C
ATOM 3494 O TYR B 112 83. .279 29. .873 52. .454 1.00 18. .17 o
ATOM 3495 CB TYR B 112 80. .415 30. .736 53, ,894 1.00 16. .37 C
ATOM 3496 CG TYR B 112 81. .101 32. .070 54. .017 1.00 16. .65 C
ATOM 3497 CD1 TYR B 112 80. .811 33. .066 53. .073 1.00 17. .33 c
ATOM 3498 CD2 TYR B 112 81, .969 32. .347 55, .060 1.00 16. .53 c
ATOM 3499 CE1 TYR B 112 81. .437 34. .303 53. .196 1.00 16. ,50 c
ATOM 3500 CE2 TYR B 112 82. .545 33. .611 55. .203 1.00 18. .00 c
ATOM 3501 CZ TYR B 112 82. .271 34. .561 54. .254 1.00 18. .48 c
ATOM 3502 OH TYR B 112 82. .827 35. .831 54. .359 1.00 13. .95 o
ATOM 3503 N LYS B 113 82. .660 28, .682 54, .275 1.00 16. .58 N
ATOM 3504 CA LYS B 113 84. .061 28. .386 54, .579 1.00 18. .32 c
ATOM 3505 C LYS B 113 84. .761 27. .596 53, .510 1.00 15. .29 c
ATOM 3506 O LYS B 113 85. .855 27, .869 53. .070 1.00 18. .38 o
ATOM 3507 CB LYS B 113 84. .087 27, .503 55. .841 1.00 17. .98 c
ATOM 3508 CG LYS B 113 83. .505 28, .228 57. .029 1.00 18. .74 c
ATOM 3509 CD LYS B 113 84. .011 27, .468 58. .263 1.00 24. .57 c
ATOM 3510 CE LYS B 113 83. .412 28, .071 59. .510 1.00 24. .59 c
ATOM 3511 NZ LYS B 113 83. .538 27, .158 60. .701 1.00 24. .23 N
ATOM 3512 N ASN B 114 84. .093 26, .469 53. .123 1.00 21. .04 N
ATOM 3513 CA ASN B 114 84. .713 25, .516 52, .225 1.00 18. .95 C
ATOM 3514 C ASN B 114 84, .566 25. .712 50, .741 1.00 17. .06 C
ATOM 3515 O ASN B 114 85, .498 25, .342 50, .030 1.00 21. .17 o
ATOM 3516 CB ASN B 114 84, .244 24, .088 52, .611 1.00 21, .37 c
ATOM 3517 CG ASN B 114 84, .538 23, .806 54, .073 1.00 21. .77 c
ATOM 3518 ODl ASN B 114 85, .591 24, .130 54, .628 1.00 28. .59 o
ATOM 3519 ND2 ASN B 114 83, .629 23, .146 54, .778 1.00 22. .63 N
ATOM 3520 N GLU B 115 83, .477 26, .315 50, .275 1.00 17. .20 N
ATOM 3521 CA GLU B 115 83, .314 26, .474 48, .828 1.00 15, .43 C
ATOM 3522 C GLU B 115 83, .543 27, .947 48, .422 1.00 17, .69 c
ATOM 3523 O GLU B 115 83, .680 28, .188 47. .207 1.00 17, .94 o
ATOM 3524 CB GLU B 115 81, .894 26, .107 48. .362 1.00 20, .26 c
ATOM 3525 CG GLU B 115 81, .545 24, .640 48. .624 1.00 27, .90 c
ATOM 3526 CD GLU B 115 80, .211 24. .311 47. .945 1.00 29, .81 c ATOM 3527 OE1 GLU B 115 79.,997 24.,659 46.,763 1.00 35.,00 O
ATOM 3528 OE2 GLU B 115 79. ,370 23. .736 48. ,635 1.00 29. .84 O
ATOM 3529 N TYR B 116 83. ,681 28. ,819 49. ,414 1.00 19. ,55 N
ATOM 3530 CA TYR B 116 83. .927 30. .230 49. .082 1.00 15. .79 c
ATOM 3531 C TYR B 116 85. ,250 30. ,766 49. ,639 1.00 13. ,17 c
ATOM 3532 O TYR B 116 86. ,134 31. ,063 48. .848 1.00 17. ,40 o
ATOM 3533 CB TYR B 116 82. .688 31. ,068 49. .466 1.00 16. .80 c
ATOM 3534 CG TYR B 116 82. .895 32. ,545 49. ,114 1.00 16. .19 c
ATOM 3535 CD1 TYR B 116 82. .924 32. .938 47. ,783 1.00 15. ,08 c
ATOM 3536 CD2 TYR B 116 83. .175 33. .478 50. .093 1.00 16. .80 c
ATOM 3537 CE1 TYR B 116 83. .132 34. .267 47. .441 1.00 14. .73 c
ATOM 3538 CE2 TYR B 116 83. .425 34. .808 49. .764 1.00 18. ,20 c
ATOM 3539 CZ TYR B 116 83. ,400 35. ,174 48. .437 1.00 17. ,15 c
ATOM 3540 OH TYR B 116 83. ,675 36. ,484 48. ,037 1.00 16. ,59 o
ATOM 3541 N VAL B 117 85. ,406 30. .857 50. .938 1.00 16. ,29 N
ATOM 3542 CA VAL B 117 86. ,616 31. .394 51. .565 1.00 14. ,14 c
ATOM 3543 C VAL B 117 87. ,840 30. .546 51. .232 1.00 15. ,15 c
ATOM 3544 O VAL B 117 88. ,869 31. ,118 50. ,868 1.00 16. ,72 o
ATOM 3545 CB VAL B 117 86. ,448 31. ,519 53. ,090 1.00 16. ,96 c
ATOM 3546 CGI VAL B 117 87. ,758 31. ,948 53. .772 1.00 18. ,85 c
ATOM 3547 CG2 VAL B 117 85. ,366 32. ,462 53. .592 1.00 17. ,76 c
ATOM 3548 N ASN B 118 87. ,766 29. ,212 51. .346 1.00 18. ,58 N
ATOM 3549 CA ASN B 118 88. .986 28. ,435 51. .072 1.00 18. ,85 c
ATOM 3550 C ASN B 118 89. .617 28. ,655 49. ,741 1.00 18. ,78 c
ATOM 3551 O ASN B 118 90. .782 28. .997 49. ,557 1.00 20. ,41 o
ATOM 3552 CB ASN B 118 88. .753 26. .969 51. .441 1.00 19. ,32 c
ATOM 3553 CG ASN B 118 88. .628 26. .758 52. .933 1.00 24. ,69 c
ATOM 3554 ODl ASN B 118 88. .870 27. .594 53. .815 1.00 22. ,08 o
ATOM 3555 ND2 ASN B 118 88. .207 25. .539 53. .310 1.00 31. .80 N
ATOM 3556 N PRO B 119 88. .865 28. .536 48. .630 1.00 16. .00 N
ATOM 3557 CA PRO B 119 89. .376 28. .772 47. .297 1.00 18. .36 C
ATOM 3558 C PRO B 119 89. .812 30. .217 47. ,102 1.00 18. .46 C
ATOM 3559 O PRO B 119 90. .734 30. .476 46. .322 1.00 18. .94 O
ATOM 3560 CB PRO B 119 88. .274 28. .372 46. .302 1.00 23. ,95 C
ATOM 3561 CG PRO B 119 87. .122 28. .036 47. .199 1.00 23. .80 c
ATOM 3562 CD PRO B 119 87. .514 27, .982 48. .655 1.00 21. .92 c
ATOM 3563 N PHE B 120 89. .090 31, .142 47. .763 1.00 17. .52 N
ATOM 3564 CA PHE B 120 89. .500 32, .560 47. .596 1.00 19. .31 C
ATOM 3565 C PHE B 120 90, .922 32, .719 48. .172 1.00 14. .13 c
ATOM 3566 O PHE B 120 91, .774 33. .239 47. .481 1.00 17. .68 o
ATOM 3567 CB PHE B 120 88. .489 33, .405 48. .344 1.00 16. .45 c
ATOM 3568 CG PHE B 120 88, .475 34. .899 48. .228 1.00 18. .75 c
ATOM 3569 CD1 PHE B 120 89, .595 35. .656 48. .551 1.00 18. .72 c
ATOM 3570 CD2 PHE B 120 87, .313 35. .550 47. .837 1.00 18. .58 c
ATOM 3571 CE1 PHE B 120 89, .557 37, .045 48, .449 1.00 16, .89 c
ATOM 3572 CE2 PHE B 120 87 .239 36, .921 47, .758 1.00 15, .08 c
ATOM 3573 CZ PHE B 120 88 .373 37, .668 48, .061 1.00 15, .36 c
ATOM 3574 N ALA B 121 91 .044 32, .220 49, .402 1.00 20. .28 N
ATOM 3575 CA ALA B 121 92 .355 32, .303 50, .080 1.00 19. .92 c
ATOM 3576 C ALA B 121 93 .427 31 .557 49, .323 1.00 22, .39 c
ATOM 3577 O ALA B 121 94 .543 32 .096 49, .181 1.00 26, .17 o
ATOM 3578 CB ALA B 121 92 .204 31 .902 51, .546 1.00 22 .68 c
ATOM 3579 N GLN B 122 93 .173 30 .403 48 .696 1.00 24, .30 N
ATOM 3580 CA GLN B 122 94 .147 29 .651 47 .925 1.00 24, .97 c
ATOM 3581 C GLN B 122 94 .710 30, .392 46, .725 1.00 29, .12 c
ATOM 3582 O GLN B 122 95 .905 30. .396 46, .404 1.00 23. .53 o
ATOM 3583 CB GLN B 122 93 .567 28, .295 47, .507 1.00 28. .16 c
ATOM 3584 CG GLN B 122 93 .999 27, .719 46, .174 1.00 38. .86 c
ATOM 3585 CD GLN B 122 93 .454 26 .315 45, .965 1.00 49. .47 c ATOM 3586 OE1 GLN B 122 92.636 25.826 46.757 1.00 48.11 O
ATOM 3587 NE2 GLN B 122 93.897 25.646 44.905 1.00 54.45 N
ATOM 3588 N LYS B 123 93.835 31.057 45.965 1.00 20.97 N
ATOM 3589 CA LYS B 123 94.256 31.820 44.798 1.00 21.89 C ATOM 3590 C LYS B 123 95.123 32.995 45.256 1.00 21.71 C
ATOM 3591 O LYS B 123 96.093 33.238 44.551 1.00 27.66 O
ATOM 3592 CB LYS B 123 92.980 32.282 44.105 1.00 20.46 C
ATOM 3593 CG LYS B 123 92.157 31.220 43.405 1.00 24.83 C
ATOM 3594 CD LYS B 123 90.883 31.875 42.836 1.00 20.09 C ATOM 3595 CE LYS B 123 89.917 30.771 42.393 1.00 22.82 C
ATOM 3596 NZ LYS B 123 90.440 30.048 41.189 1.00 24.93 N
ATOM 3597 N LEU B 124 94.801 33.647 46.357 1.00 24.17 N
ATOM 3598 CA LEU B 124 95.595 34.801 46.816 1.00 21.76 C
ATOM 3599 C LEU B 124 96.966 34.322 47.296 1.00 23.77 c ATOM 3600 O LEU B 124 97.984 34.931 46.910 1.00 28.41 O
ATOM 3601 CB LEU B 124 94.865 35.593 47.906 1.00 24.20 c
ATOM 3602 CG LEU B 124 94.030 36.776 47.367 1.00 24.16 c
ATOM 3603 CD1 LEU B 124 92.891 36.270 46.469 1.00 19.80 c
ATOM 3604 CD2 LEU B 124 93.476 37.582 48.531 1.00 23.53 c ATOM 3605 N LYS B 125 97.011 33.151 47.910 1.00 25.42 N
ATOM 3606 CA LYS B 125 98.294 32.590 48.376 1.00 26.58 c
ATOM 3607 C LYS B 125 99.199 32.158 47.259 1.00 30.33 c
ATOM 3608 O LYS B 125 100.412 32.491 47.235 1.00 33.95 O
ATOM 3609 CB LYS B 125 97.976 31.495 49.407 1.00 31.01 c ATOM 3610 CG LYS B 125 97.495 32.128 50.703 1.00 21.58 c
ATOM 3611 CD LYS B 125 96.749 31.229 51.629 1.00 31.88 c
ATOM 3612 CE LYS B 125 96.490 31.809 53.011 1.00 20.97 c
ATOM 3613 NZ LYS B 125 95.641 30.823 53.749 1.00 29.14 N
ATOM 3614 N ALA B 126 98.709 31.551 46.182 1.00 27.52 N ATOM 3615 CA ALA B 126 99.534 31.183 45.026 1.00 23.70 c
ATOM 3616 C ALA B 126 100.120 32.404 44.329 1.00 28.30 c
ATOM 3617 O ALA B 126 101.157 32.390 43.659 1.00 28.11 O
ATOM 3618 CB ALA B 126 98.757 30.328 44.041 1.00 31.19 c
ATOM 3619 N ALA B 127 99.450 33.540 44.486 1.00 29.13 N ATOM 3620 CA ALA B 127 99.802 34.835 43.955 1.00 31.16 c
ATOM 3621 C ALA B 127 100.578 35.654 44.977 1.00 34.21 c
ATOM 3622 O ALA B 127 100.174 36.709 45.476 1.00 29.41 O
ATOM 3623 CB ALA B 127 98.495 35.543 43.595 1.00 28.04 c
ATOM 3624 N SER B 128 101.786 35.180 45.298 1.00 32.43 N ATOM 3625 CA SER B 128 102.660 35.800 46.271 1.00 32.25 c
ATOM 3626 C SER B 128 103.319 37.073 45.750 1.00 24.54 c
ATOM 3627 O SER B 128 103.683 37.927 46.552 1.00 33.73 O
ATOM 3628 CB SER B 128 103.762 34.818 46.706 1.00 37.87 c
ATOM 3629 OG SER B 128 104.163 33.963 45.661 1.00 39.24 O ATOM 3630 N ASP B 129 103.460 37.197 44.455 1.00 31.97 N
ATOM 3631 CA ASP B 129 104.009 38.308 43.721 1.00 29.79 c
ATOM 3632 C ASP B 129 103.026 39.481 43.644 1.00 32.25 c
ATOM 3633 O ASP B 129 103.376 40.560 43.141 1.00 34.17 O
ATOM 3634 CB ASP B 129 104.320 37.840 42.292 1.00 33.19 c ATOM 3635 CG ASP B 129 103.185 37.218 41.511 1.00 25.83 c
ATOM 3636 ODl ASP B 129 102.435 36.421 42.110 1.00 36.80 O
ATOM 3637 OD2 ASP B 129 103.035 37.497 40.296 1.00 37.23 o
ATOM 3638 N VAL B 130 101.776 39.231 44.051 1.00 29.46 < N
ATOM 3639 CA VAL B 130 100.738 40.263 43.980 1.00 27.44 c ATOM 3640 C VAL B 130 100.293 40.772 45.328 1.00 24.03 c
ATOM 3641 O VAL B 130 100.064 40.117 46.353 1.00 25.62 o
ATOM 3642 CB VAL B 130 99.506 39.748 43.191 1.00 26.99 c
ATOM 3643 CGI VAL B 130 98.401 40.809 43.180 1.00 26.96 c
ATOM 3644 CG2 VAL B 130 99.835 39.387 41.758 1.00 22.05 c ATOM 3645 N GLN B 131 100.121 42.129 45.350 1.00 22.96 N
ATOM 3646 CA GLN B 131 99.636 42.783 46.551 1.00 19.81 C
ATOM 3647 c GLN B 131 98.094 42.915 46.465 1.00 20.68 C
ATOM 3648 O GLN B 131 97.674 43.446 45.445 1.00 21.77 O ATOM 3649 CB GLN B 131 100.117 44.242 46.677 1.00 22.81 C
ATOM 3650 CG GLN B 131 101.640 44.255 46.912 1.00 29.87 C
ATOM 3651 CD GLN B 131 102.033 43.500 48.158 1.00 24.86 C
ATOM 3652 OE1 GLN B 131 101.618 43.807 49.273 1.00 29.69 O
ATOM 3653 NE2 GLN B 131 102.876 42.482 47.939 1.00 32.63 N ATOM 3654 N PHE B 132 97.470 42.488 47.537 1.00 22.94 N
ATOM 3655 CA PHE B 132 96.000 42.517 47.546 1.00 26.91 C
ATOM 3656 c PHE B 132 95.452 43.357 48.671 1.00 21.14 C
ATOM 3657 O PHE B 132 95.838 43.264 49.848 1.00 20.79 o
ATOM 3658 CB PHE B 132 95.431 41.088 47.798 1.00 20.65 c ATOM 3659 CG PHE B 132 95.700 40.115 46.695 1.00 22.40 c
ATOM 3660 CD1 PHE B 132 94.934 40.079 45.556 1.00 19.64 c
ATOM 3661 CD2 PHE B 132 96.746 39.195 46.807 1.00 17.32 c
ATOM 3662 CE1 PHE B 132 95.143 39.205 44.510 1.00 24.57 c
ATOM 3663 CE2 PHE B 132 96.985 38.348 45.750 1.00 20.68 c ATOM 3664 CZ PHE B 132 96.213 38.312 44.619 1.00 26.31 c
ATOM 3665 N ALA B 133 94.401 44.159 48.370 1.00 16.96 N
ATOM 3666 CA ALA B 133 93.639 44.809 49.395 1.00 16.49 c
ATOM 3667 C ALA B 133 92.235 44.136 49.389 1.00 18.38 c
ATOM 3668 O ALA B 133 91.665 44.209 48.323 1.00 17.13 o ATOM 3669 CB ALA B 133 93.387 46.292 49.193 1.00 14.60 c
ATOM 3670 N VAL B 134 91.895 43.491 50.475 1.00 18.42 N
ATOM 3671 CA VAL B 134 90.606 42.760 50.517 1.00 15.66 c
ATOM 3672 C VAL B 134 89.659 43.423 51.467 1.00 14.54 c
ATOM 3673 O VAL B 134 89.874 43.572 52.675 1.00 14.16 0 ATOM 3674 CB VAL B 134 90.900 41.306 50.918 1.00 13.72 c
ATOM 3675 CGI VAL B 134 89.589 40.495 50.974 1.00 17.54 c
ATOM 3676 CG2 VAL B 134 91.842 40.596 49.957 1.00 19.02 c
ATOM 3677 N ILE B 135 88.502 43.872 50.951 1.00 13.30 N
ATOM 3678 CA ILE B 135 87.422 44.400 51.774 1.00 14.75 c ATOM 3679 C ILE B 135 86.485 43.235 52.160 1.00 14.96 c
ATOM 3680 O ILE B 135 86.101 42.470 51.285 1.00 15.76 o
ATOM 3681 CB ILE B 135 86.667 45.528 51.047 1.00 11.61 c
ATOM 3682 CGI ILE B 135 87.543 46.792 51.091 1.00 14.70 c
ATOM 3683 CG2 ILE B 135 85.287 45.746 51.620 1.00 13.63 c ATOM 3684 CD1 ILE B 135 86.940 47.902 50.221 1.00 16.11 c
ATOM 3685 N LEU B 136 86.357 43.089 53.449 1.00 13.52 N
ATOM 3686 CA LEU B 136 85.589 41.989 54.021 1.00 15.53 c
ATOM 3687 C LEU B 136 84.171 42.363 54.349 1.00 13.72 c
ATOM 3688 O LEU B 136 83.800 43.154 55.212 1.00 15.39 0 ATOM 3689 CB LEU B 136 86.291 41.489 55.298 1.00 13.79 c
ATOM 3690 CG LEU B 136 87.737 41.035 55.172 1.00 18.13 c
ATOM 3691 CD1 LEU B 136 88.333 40.902 56.570 1.00 23.01 c
ATOM 3692 CD2 LEU B 136 87.832 39.733 54.380 1.00 19.02 c
ATOM 3693 N GLU B 137 83.252 41.681 53.633 1.00 13.75 N ATOM 3694 CA GLU B 137 81.840 41.685 53.812 1.00 13.00 C
ATOM 3695 C GLU B 137 81.161 43.006 54.106 1.00 11.93 c
ATOM 3696 O GLU B 137 80.680 43.291 55.204 1.00 13.48 0
ATOM 3697 CB GLU B 137 81.481 40.595 54.861 1.00 16.46 , c
ATOM 3698 CG GLU B 137 81.909 39.210 54.399 1.00 17.10 c ATOM 3699 CD GLU B 137 81.006 38.627 53.309 1.00 12.29 c
ATOM 3700 OE1 GLU B 137 79.988 39.251 52.933 1.00 11.47 0
ATOM 3701 OE2 GLU B 137 81.388 37.542 52.856 1.00 13.64 o
ATOM 3702 N PRO B 138 80.949 43.765 53.021 1.00 9.65 N
ATOM 3703 CA PRO B 138 80.283 45.064 53.165 1.00 11.66 c ATOM 3704 c PRO B 138 78..950 44..922 53..848 1.00 16..41 c
ATOM 3705 O PRO B 138 78. .139 43. .988 53. .674 1.00 14. ,38 o
ATOM 3706 CB PRO B 138 80. ,041 45. .531 51. .710 1.00 14. .17 c
ATOM 3707 CG PRO B 138 81. .226 44. .915 51. .017 1.00 14. .54 c
ATOM 3708 CD PRO B 138 81. ,479 43. .552 51. .696 1.00 15. .40 c
ATOM 3709 N ASP B 139 78. .715 45. .822 54. .776 1.00 12. .09 N
ATOM 3710 CA ASP B 139 77. .649 46. .085 55. .646 1.00 11. .26 c
ATOM 3711 C ASP B 139 77. .235 44. .998 56. .635 1.00 13. .19 c
ATOM 3712 O ASP B 139 76. ,240 45. .146 57. .330 1.00 13. .01 o
ATOM 3713 CB ASP B 139 76. ,407 46. .427 54. .798 1.00 17. .62 c
ATOM 3714 CG ASP B 139 76. ,503 47. .802 54. .204 1.00 14. .56 c
ATOM 3715 ODl ASP B 139 77. ,318 48. .629 54. ,675 1.00 15. ,57 o
ATOM 3716 OD2 ASP B 139 75. ,746 48. .063 53. .230 1.00 15. .76 o
ATOM 3717 N ALA B 140 78. ,031 43. .911 56. .724 1.00 12. ,47 N
ATOM 3718 CA ALA B 140 77. ,659 42. .855 57. .667 1.00 10. ,82 c
ATOM 3719 C ALA B 140 77. ,712 43. .418 59. .088 1.00 14. ,07 c
ATOM 3720 O ALA B 140 76. ,781 43. .169 59. .838 1.00 16. .04 o
ATOM 3721 CB ALA B 140 78. ,585 41. .661 57. .526 1.00 11. .51 c
ATOM 3722 N ILE B 141 78. ,782 44. .156 59. .401 1.00 14. .29 N
ATOM 3723 CA ILE B 141 78. ,873 44. .726 60. .760 1.00 15. .41 C
ATOM 3724 C ILE B 141 77. ,744 45. .675 61. .073 1.00 17. .38 c
ATOM 3725 O ILE B 141 77. ,192 45. .707 62. ,164 1.00 17. .24 o
ATOM 3726 CB ILE B 141 80. ,265 45. .340 61. ,014 1.00 15. .52 c
ATOM 3727 CGI ILE B 141 81. .238 44. .163 61. .224 1.00 16. .65 c
ATOM 3728 CG2 ILE B 141 80. .260 46. .205 62. .265 1.00 13. .33 c
ATOM 3729 CD1 ILE B 141 82. .712 44. .518 61. .367 1.00 17. .73 c
ATOM 3730 N GLY B 142 77. .318 46. .494 60. .115 1.00 15. .85 N
ATOM 3731 CA GLY B 142 76. .202 47. .426 60. .341 1.00 17. .76 c
ATOM 3732 C GLY B 142 74. .947 46. .627 60. .715 1.00 18. .26 c
ATOM 3733 O GLY B 142 74. .254 47. .011 61. .640 1.00 17. .59 o
ATOM 3734 N ASN B 143 74. .662 45. .572 59. .958 1.00 15. .58 N
ATOM 3735 CA ASN B 143 73. .447 44. .801 60. .289 1.00 18. ,17 c
ATOM 3736 C ASN B 143 73. .555 44. .149 61. .676 1.00 20. .16 c
ATOM 3737 O ASN B 143 72. .572 43, .925 62. .379 1.00 17. .81 o
ATOM 3738 CB ASN B 143 73. .251 43. .732 59. .230 1.00 18. .60 c
ATOM 3739 CG ASN B 143 72. .637 44. .316 57. .969 1.00 20. .06 c
ATOM 3740 ODl ASN B 143 71. .501 44. .746 58. .042 1.00 21. ,17 o
ATOM 3741 ND2 ASN B 143 73. .368 44. .350 56. ,859 1.00 14. .95 N
ATOM 3742 N MET B 144 74. .774 43. .774 62. .040 1.00 15. .40 N
ATOM 3743 CA MET B 144 74. .950 43. .151 63. .357 1.00 21. .47 c
ATOM 3744 C MET B 144 74. .707 44. .124 64. ,496 1.00 27. .91 c
ATOM 3745 O MET B 144 74. .087 43. .756 65. .488 1.00 20. .91 o
ATOM 3746 CB MET B 144 76. .366 42. .653 63. .517 1.00 19. .67 c
ATOM 3747 CG MET B 144 76. .579 41. .381 62. .717 1.00 23. .41 c
ATOM 3748 SD MET B 144 78. .362 40. .995 62. .834 1.00 25. .38 s
ATOM 3749 CE MET B 144 78. .546 40. .493 61. .116 1.00 20. .83 c
ATOM 3750 N VAL B 145 75, .271 45. .322 64. .360 1.00 25. .22 N
ATOM 3751 CA VAL B 145 75, .142 46, .311 65. .417 1.00 25. .15 C
ATOM 3752 C VAL B 145 73, .738 46, .835 65. .618 1.00 30. .65 C
ATOM 3753 O VAL B 145 73, .289 47, .026 66. .762 1.00 27. .78 O
ATOM 3754 CB VAL B 145 76, .128 47. .460 65. .094 1.00 22. .43 c
ATOM 3755 CGI VAL B 145 75. .864 48. .678 65. .958 1.00 22. .21 c
ATOM 3756 CG2 VAL B 145 77. .553 46. .962 65. .248 1.00 28. .65 Ό
ATOM 3757 N THR B 146 73. .028 47. .150 64. .530 1.00 26. .11 N
ATOM 3758 CA THR B 146 71. .720 47. .744 64. .633 1.00 24. .62 c
ATOM 3759 C THR B 146 70. .561 46. .853 64. .238 1.00 21. .06 c
ATOM 3760 0 THR B 146 69. .448 47. .260 64. .540 1.00 25. .27 o
ATOM 3761 CB THR B 146 71. .631 49. .013 63. .729 1.00 31. .66 c
ATOM 3762 OG1 THR B 146 71. .703 48. .607 62. ,352 1.00 23. .88 o ATOM 3763 CG2 THR B 146 72.758 49.978 64.,049 1.00 28.37 C
ATOM 3764 N GLY B 147 70.768 45. 718 63. 583 1.00 20. 50 N
ATOM 3765 CA GLY B 147 69.651 44. 916 63. ,122 1.00 20. 46 C
ATOM 3766 C GLY B 147 68.875 44. 278 64. ,273 1.00 18. 32 C
ATOM 3767 O GLY B 147 69.468 43. 540 65. ,037 1.00 20. 95 O
ATOM 3768 N THR B 148 67.568 44. 479 64. ,311 1.00 24. 13 N
ATOM 3769 CA THR B 148 66.775 43. ,925 65. ,408 1.00 24. 05 C
ATOM 3770 C THR B 148 65.763 42. ,876 64. ,960 1.00 25. 46 C
ATOM 3771 O THR B 148 65.031 42. 311 65. ,767 1.00 25. 50 O
ATOM 3772 CB THR B 148 66.057 45. 010 66. ,231 1.00 25. 43 C
ATOM 3773 OG1 THR B 148 65.214 45. ,829 65. ,414 1.00 27. 55 O
ATOM 3774 CG2 THR B 148 67.034 45. ,917 66. ,974 1.00 28. 06 c
ATOM 3775 N SER B 149 65.689 42. ,559 63. ,663 1.00 27. 18 N
ATOM 3776 CA SER B 149 64.722 41. ,545 63. .240 1.00 24. 73 c
ATOM 3777 C SER B 149 65.216 40. ,177 63. ,668 1.00 21. 36 c
ATOM 3778 O SER B 149 66.397 39. ,964 63. ,907 1.00 22. ,14 O
ATOM 3779 CB SER B 149 64.514 41. ,576 61. ,723 1.00 27. ,41 c
ATOM 3780 OG SER B 149 65.677 41. ,056 61. .080 1.00 24. ,60 O
ATOM 3781 N ALA B 150 64.301 39. ,197 63. ,771 1.00 24. ,58 N
ATOM 3782 CA ALA B 150 64.688 37. ,849 64. ,162 1.00 26. ,91 c
ATOM 3783 C ALA B 150 65.694 37. ,235 63. ,203 1.00 22. ,48 c
ATOM 3784 O ALA B 150 66.622 36. ,553 63. ,595 1.00 22. ,71 O
ATOM 3785 CB ALA B 150 63.428 36. ,972 64. .220 1.00 33. ,42 c
ATOM 3786 N PHE B 151 65.458 37. ,491 61. .898 1.00 23. ,13 N
ATOM 3787 CA PHE B 151 66.368 36. .988 60. .867 1.00 20. ,01 c
ATOM 3788 C PHE B 151 67.793 37. .464 61. .091 1.00 14. ,60 c
ATOM 3789 O PHE B 151 68.722 36. .671 61. .044 1.00 16. .97 O
ATOM 3790 CB PHE B 151 65.816 37. .414 59. .493 1.00 19. .44 c
ATOM 3791 CG PHE B 151 66.510 36. .652 58. .401 1.00 20. .06 c
ATOM 3792 CD1 PHE B 151 66.301 35. .300 58. .182 1.00 19. ,19 c
ATOM 3793 CD2 PHE B 151 67.463 37. .327 57. .641 1.00 16. ,93 c
ATOM 3794 CE1 PHE B 151 67.009 34. .647 57. .181 1.00 20. .25 c
ATOM 3795 CE2 PHE B 151 68.138 36. .687 56. .617 1.00 16. .16 c
ATOM 3796 CZ PHE B 151 67.927 35. .336 56. .396 1.00 20. .13 c
ATOM 3797 N CYS B 152 67.954 38. .782 61. .329 1.00 16. .81 N
ATOM 3798 CA CYS B 152 69.288 39. .304 61. .614 1.00 15. .93 c
ATOM 3799 C CYS B 152 69.806 38. .800 62, .967 1.00 18. .99 c
ATOM 3800 O CYS B 152 71.012 38. .520 63, .019 1.00 18, .93 O
ATOM 3801 CB CYS B 152 69.314 40, .852 61, .640 1.00 19, .71 c
ATOM 3802 SG CYS B 152 69.415 41. .586 59, .968 1.00 18. .74 S
ATOM 3803 N ARG B 153 68.916 38. .725 63, .955 1.00 23. .55 N
ATOM 3804 CA ARG B 153 69.333 38. .282 65, .296 1.00 22. .77 C
ATOM 3805 C ARG B 153 69.814 36. .842 65, .255 1.00 23. .76 C
ATOM 3806 O ARG B 153 70.875 36, .517 65, .805 1.00 23. .55 O
ATOM 3807 CB ARG B 153 68.252 38, .489 66, .361 1.00 20. .42 C
ATOM 3808 CG ARG B 153 67.967 39, .949 66 .637 1.00 23. .45 c
ATOM 3809 CD ARG B 153 67.009 40, .140 67 .796 1.00 27, .75 c
ATOM 3810 NE ARG B 153 65.610 40 .114 67 .348 1.00 24, .45 N
ATOM 3811 CZ ARG B 153 64.716 39 .303 67 .928 1.00 31, .22 c
ATOM 3812 NH1 ARG B 153 65.090 38, .508 68, .917 1.00 26, .50 N
ATOM 3813 NH2 ARG B 153 63.469 39, .317 67 .506 1.00 34, ■ 12 N
ATOM 3814 N ASN B 154 69.141 35, .998 64 .466 1.00 23, .30 N
ATOM 3815 CA ASN B 154 69.616 34 .627 64 .260 1.00 23, .76 C
ATOM 3816 C ASN B 154 70.882 34 .451 63 .467 1.00 29, .27 C
ATOM 3817 O ASN B 154 71.704 33 .528 63 .676 1.00 28 .91 O
ATOM 3818 CB ASN B 154 68.417 33 .836 63 .680 1.00 28, .21 C
ATOM 3819 CG ASN B 154 67.595 33 .415 64 .907 1.00 39, .80 c
ATOM 3820 ODl ASN B 154 66.569 33 .992 65 .266 1.00 42 .56 O
ATOM 3821 ND2 ASN B 154 68.119 32 .409 65 .605 1.00 41 .92 N ATOM 3822 N ALA B 155 71.229 35.349 62.,536 1.00 19.,55 N
ATOM 3823 CA ALA B 155 72. ,407 35. 276 61. ,729 1.00 21. ,10 C
ATOM 3824 C ALA B 155 73. .666 35. ,848 62. ,390 1.00 19. ,96 C
ATOM 3825 O ALA B 155 74. ,765 35. 498 61. .967 1.00 19. ,05 O ATOM 3826 CB ALA B 155 72. .207 36. ,110 60. ,446 1.00 24. .59 c
ATOM 3827 N ARG B 156 73. .440 36. ,658 63. ,427 1.00 19. ,26 N
ATOM 3828 CA ARG B 156 74. .601 37. ,336 64. ,006 1.00 26. ,41 c
ATOM 3829 C ARG B 156 75. .771 36. ,457 64. ,418 1.00 18. ,67 c
ATOM 3830 O ARG B 156 76. .914 36. ,682 64. .000 1.00 19. .84 o ATOM 3831 CB ARG B 156 74. .141 38. .185 65. ,207 1.00 21. ,59 c
ATOM 3832 CG ARG B 156 75. .359 38. .989 65. .714 1.00 20. ,92 c
ATOM 3833 CD ARG B 156 74. .928 40. ,415 65. .920 1.00 23. .67 c
ATOM 3834 NE ARG B 156 75. .912 41. ,117 66. ,780 1.00 21. .37 N
ATOM 3835 CZ ARG B 156 75. .490 41. ,785 67. .855 1.00 28. .37 c ATOM 3836 NH1 ARG B 156 74. .198 41. ,794 68. .117 1.00 28. .16 N
ATOM 3837 NH2 ARG B 156 76. .368 42. ,438 68. .609 1.00 34. .74 N
ATOM 3838 N GLY B 157 75. .520 35. ,424 65. .217 1.00 20. .28 N
ATOM 3839 CA GLY B 157 76. ,588 34. ,546 65. ,705 1.00 24. .46 C
ATOM 3840 C GLY B 157 77. .394 33. ,874 64. .627 1.00 18. .18 c ATOM 3841 O GLY B 157 78. .598 33. ,833 64. .470 1.00 17. .26 o
ATOM 3842 N PRO B 158 76. .641 33. ,170 63. ,734 1.00 21. .55 N
ATOM 3843 CA PRO B 158 77. .199 32. .455 62. ,603 1.00 18. .68 C
ATOM 3844 C PRO B 158 77. .948 33. .430 61. .706 1.00 15. .85 C
ATOM 3845 O PRO B 158 78. .981 33. .067 61. ,152 1.00 17. .84 O ATOM 3846 CB PRO B 158 76. .024 31. .762 61. .910 1.00 20. .46 C
ATOM 3847 CG PRO B 158 75. .007 31. .699 63. .043 1.00 20. .08 C
ATOM 3848 CD PRO B 158 75. .200 32. .970 63. .847 1.00 21. .53 C
ATOM 3849 N GLN B 159 77. .459 34. .652 61. .491 1.00 20. .97 N
ATOM 3850 CA GLN B 159 78. .154 35. .643 60. .669 1.00 24. .31 C ATOM 3851 C GLN B 159 79. .452 36. .120 61. .316 1.00 16. .22 c
ATOM 3852 O GLN B 159 80. .465 36. .222 60. .622 1.00 17. .79 o
ATOM 3853 CB GLN B 159 77. .224 36. .821 60. .334 1.00 20. .42 c
ATOM 3854 CG GLN B 159 76. .138 36. ,406 59. .331 1.00 15. .14 c
ATOM 3855 CD GLN B 159 75. .227 37. .553 58. .938 1.00 22. .68 c ATOM 3856 OE1 GLN B 159 75. .105 38. .528 59. .677 1.00 21. .04 o
ATOM 3857 NE2 GLN B 159 74. .576 37. .389 57. .768 1.00 19. .53 N
ATOM 3858 N GLN B 160 79. .471 36. .244 62. .622 1.00 22. .08 N
ATOM 3859 CA GLN B 160 80. .740 36. .575 63. .308 1.00 23. .01 c
ATOM 3860 C GLN B 160 81. .735 35. .435 63. .139 1.00 20. .22 c ATOM 3861 O GLN B 160 82. .915 35. .648 62. .850 1.00 18. .55 o
ATOM 3862 CB GLN B 160 80. .541 36. .850 64. .779 1.00 21. .58 c
ATOM 3863 CG GLN B 160 79. .630 38. .029 65. .115 1.00 29. .04 c
ATOM 3864 CD GLN B 160 79. .304 38. .031 66. .599 1.00 30, .14 c
ATOM 3865 OE1 GLN B 160 79. .323 36. .968 67, .230 1.00 33, .19 o ATOM 3866 NE2 GLN B 160 78. .976 39. .169 67, .174 1.00 26. .06 N
ATOM 3867 N GLU B 161 81, .253 34. .177 63, .293 1.00 20. .88 N
ATOM 3868 CA GLU B 161 82, .152 33. .059 63, .057 1.00 19. .00 c
ATOM 3869 C GLU B 161 82. .647 33. .067 61. .610 1.00 15. .67 c
ATOM 3870 O GLU B 161 83, .811 32. .804 61. .387 1.00 16. .94 o ATOM 3871 CB GLU B 161 81, .484 31. .713 63, .351 1.00 19. .88 c
ATOM 3872 CG GLU B 161 82, .362 30. .484 63. .169 1.00 26. .32 c
ATOM 3873 CD GLU B 161 81, .686 29. .167 63, .519 1.00 31. .91 c
ATOM 3874 OE1 GLU B 161 80, .710 29. .144 64, .301 1.00 28, .71 o
ATOM 3875 OE2 GLU B 161 82, .134 28. .110 63, .009 1.00 28, .21 o ATOM 3876 N ALA B 162 81, .746 33. .316 60, .652 1.00 16, .26 N
ATOM 3877 CA ALA B 162 82, .176 33. .282 59. .262 1.00 16, .15 c
ATOM 3878 C ALA B 162 83, .222 34. .367 58, .954 1.00 14, .47 c
ATOM 3879 O ALA B 162 84 .159 34, .044 58, .223 1.00 17, .52 o
ATOM 3880 CB ALA B 162 80, .982 33, .487 58, .322 1.00 17, .33 c ATOM 3881 N ILE B 163 82.968 35.,572 59.486 1.00 15.,58 N
ATOM 3882 CA ILE B 163 83. ,957 36. ,628 59. ,133 1.00 14. .22 C
ATOM 3883 C ILE B 163 85. 293 36. .372 59. ,844 1.00 17. ,29 C
ATOM 3884 O ILE B 163 86. ,339 36. ,439 59. ,202 1.00 18. ,10 O ATOM 3885 CB ILE B 163 83. ,382 38. .015 59. ,471 1.00 18. ,52 C
ATOM 3886 CGI ILE B 163 82. ,140 38. ,248 58. ,603 1.00 18. ,71 C
ATOM 3887 CG2 ILE B 163 84. ,425 39. ,094 59. ,237 1.00 16. ,28 c
ATOM 3888 CD1 ILE B 163 81. ,358 39. ,499 58. ,982 1.00 19. .48 c
ATOM 3889 N GLY B 164 85. ,219 35. ,958 61. ,110 1.00 20. ,76 N ATOM 3890 CA GLY B 164 86. ,449 35. ,554 61. ,813 1.00 19. ,29 C
ATOM 3891 C GLY B 164 87. ,190 34. ,462 61. ,061 1.00 16. ,00 C
ATOM 3892 O GLY B 164 88. .385 34. .511 60. ,721 1.00 21. .59 O
ATOM 3893 N TYR B 165 86. .441 33. .459 60. ,539 1.00 21. ,55 N
ATOM 3894 CA TYR B 165 87. ,076 32. .430 59. ,709 1.00 19. ,82 C ATOM 3895 C TYR B 165 87. ,811 33. .022 58. ,525 1.00 22. ,07 C
ATOM 3896 O TYR B 165 88. ,962 32. .742 58. ,212 1.00 19. .77 O
ATOM 3897 CB TYR B 165 86. ,058 31. .346 59. ,295 1.00 19. .85 C
ATOM 3898 CG TYR B 165 86. ,698 30. .256 58. ,488 1.00 19. .36 c
ATOM 3899 CD1 TYR B 165 87. .436 29. .240 59. ,125 1.00 18. .97 c ATOM 3900 CD2 TYR B 165 86. ,671 30. .208 57. ,100 1.00 15. .34 c
ATOM 3901 CE1 TYR B 165 88. .053 28. .270 58. ,376 1.00 20. .37 c
ATOM 3902 CE2 TYR B 165 87. .284 29. .236 56. ,350 1.00 20. ,09 c
ATOM 3903 CZ TYR B 165 87. .974 28. .229 57. .005 1.00 21. .43 c
ATOM 3904 OH TYR B 165 88. .595 27. .252 56. .252 1.00 22. .80 O ATOM 3905 N ALA B 166 87. .155 33. .915 57. .749 1.00 17. .04 N
ATOM 3906 CA ALA B 166 87. .725 34. .565 56. .613 1.00 18. .38 C
ATOM 3907 C ALA B 166 89. .059 35. .250 56. .956 1.00 14. .16 C
ATOM 3908 O ALA B 166 90. .040 34, .989 56. .274 1.00 19. .46 o
ATOM 3909 CB ALA B 166 86. .662 35. .520 56. .061 1.00 19. .60 C ATOM 3910 N ILE B 167 89. .027 36. .047 58. .033 1.00 18. .27 N
ATOM 3911 CA ILE B 167 90. .266 36. .704 58. .446 1.00 18. .66 C
ATOM 3912 C ILE B 167 91. .386 35. .684 58. .772 1.00 17. .26 c
ATOM 3913 O ILE B 167 92. .496 35. .827 58. .326 1.00 18. .08 o
ATOM 3914 CB ILE B 167 90. .000 37. .589 59. .654 1.00 14. .42 c ATOM 3915 CGI ILE B 167 89. .059 38. .761 59. .275 1.00 18. .50 c
ATOM 3916 CG2 ILE B 167 91. .311 38. .167 60. .174 1.00 16. .55 c
ATOM 3917 CD1 ILE B 167 88. .377 39. .388 60. .481 1.00 24. .38 c
ATOM 3918 N SER B 168 90. .966 34, .656 59. .532 1.00 22. .19 N
ATOM 3919 CA SER B 168 91. .957 33, .617 59. .886 1.00 19. .64 C ATOM 3920 C SER B 168 92. .588 32. .977 58. .677 1.00 21. .84 C
ATOM 3921 O SER B 168 93. .758 32. .547 58. .729 1.00 21. .47 o
ATOM 3922 CB SER B 168 91. .301 32. .584 60. .815 1.00 19. .90 c
ATOM 3923 OG SER B 168 90, .604 31. .576 60. .094 1.00 22. .30 o
ATOM 3924 N GLN B 169 91. .930 32, .830 57. .528 1.00 17. .10 N ATOM 3925 CA GLN B 169 92, .461 32, .225 56, .332 1.00 19, .22 c
ATOM 3926 C GLN B 169 93, .170 33, .155 55, .375 1.00 16, .88 c
ATOM 3927 O GLN B 169 93, .714 32, .693 54. .354 1.00 17, .87 o
ATOM 3928 CB GLN B 169 91. .354 31, .448 55. .573 1.00 20, .00 c
ATOM 3929 CG GLN B 169 90, .545 30, .491 56. .437 1.00 19, .27 c ATOM 3930 CD GLN B 169 91, .447 29, .334 56, .948 1.00 15, .65 c
ATOM 3931 OE1 GLN B 169 92 .035 28 .669 56, .116 1.00 21 .59 o
ATOM 3932 NE2 GLN B 169 91, .500 29, .311 58, .271 1.00 20 .57 N
ATOM 3933 N LEU B 170 93 .261 34 .470 55, .692 1.00 17, .99 N
ATOM 3934 CA LEU B 170 93 .877 35 .454 54 .837 1.00 21 .91 C ATOM 3935 C LEU B 170 95 .005 36 .226 55, .501 1.00 22 .99 C
ATOM 3936 O LEU B 170 95 .210 37 .430 55 .365 1.00 22 .45 o
ATOM 3937 CB LEU B 170 92 .771 36 .441 54 .362 1.00 19 .03 c
ATOM 3938 CG LEU B 170 91 .787 35 .709 53 .389 1.00 11 .90 c
ATOM 3939 CD1 LEU B 170 90 .504 36 .553 53 .408 1.00 20 .05 c ATOM 3940 CD2 LEU B 170 92.333 35.528 52.010 1.00 16.63 C
ATOM 3941 N GLN B 171 95.834 35.461 56.212 1.00 22.80 N
ATOM 3942 CA GLN B 171 96.962 36.026 56.963 1.00 19.78 C
ATOM 3943 C GLN B 171 98.268 35.782 56.247 1.00 24.71 c ATOM 3944 O GLN B 171 98.874 34.698 56.310 1.00 25.88 o
ATOM 3945 CB GLN B 171 96.965 35.418 58.367 1.00 20.61 c
ATOM 3946 CG GLN B 171 95.775 35.673 59.248 1.00 24.02 c
ATOM 3947 CD GLN B 171 95.650 37.161 59.536 1.00 28.19 c
ATOM 3948 OE1 GLN B 171 96.632 37.693 60.055 1.00 24.58 o ATOM 3949 NE2 GLN B 171 94.512 37.768 59.202 1.00 21.14 N
ATOM 3950 N ALA B 172 98.685 36.743 55.428 1.00 21.73 N
ATOM 3951 CA ALA B 172 99.921 36.699 54.683 1.00 18.05 C
ATOM 3952 C ALA B 172 100.420 38.147 54.555 1.00 27.99 C
ATOM 3953 O ALA B 172 99.603 39.072 54.673 1.00 25.60 o ATOM 3954 CB ALA B 172 99.768 36.013 53.353 1.00 19.69 C
ATOM 3955 N SER B 173 101.690 38.324 54.224 1.00 30.83 N
ATOM 3956 CA SER B 173 102.318 39.617 54.015 1.00 31.75 C
ATOM 3957 C SER B 173 101.873 40.447 52.825 1.00 30.88 C
ATOM 3958 O SER B 173 102.192 41.639 52.676 1.00 32.10 o ATOM 3959 CB SER B 173 103.847 39.346 53.804 1.00 22.83 C
ATOM 3960 OG SER B 173 104.156 39.184 52.435 1.00 45.16 o
ATOM 3961 N HIS B 174 101.240 39.848 51.822 1.00 22.71 N
ATOM 3962 CA HIS B 174 100.821 40.532 50.613 1.00 24.45 C
ATOM 3963 C HIS B 174 99.304 40.744 50.591 1.00 19.78 C ATOM 3964 O HIS B 174 98.803 41.254 49.599 1.00 26.27 o
ATOM 3965 CB HIS B 174 101.204 39.783 49.362 1.00 22.82 C
ATOM 3966 CG HIS B 174 100.641 38.397 49.255 1.00 28.16 C
ATOM 3967 ND1 HIS B 174 100.753 37.458 50.253 1.00 35.93 N
ATOM 3968 CD2 HIS B 174 99.977 37.810 48.229 1.00 27.74 C ATOM 3969 CE1 HIS B 174 100.171 36.342 49.850 1.00 28.43 C
ATOM 3970 NE2 HIS B 174 99.721 36.506 48.620 1.00 25.95 N
ATOM 3971 N ILE B 175 98.683 40.341 51.682 1.00 21.04 N
ATOM 3972 CA ILE B 175 97.208 40.486 51.755 1.00 22.53 C
ATOM 3973 C ILE B 175 96.883 41.436 52.878 1.00 23.42 C ATOM 3974 O ILE B 175 97.264 41.229 54.036 1.00 21.16 0
ATOM 3975 CB ILE B 175 96.602 39.086 51.998 1.00 24.23 C
ATOM 3976 CGI ILE B 175 97.093 38.037 51.010 1.00 19.57 c
ATOM 3977 CG2 ILE B 175 95.075 39.209 51.938 1.00 23.51 c
ATOM 3978 CD1 ILE B 175 96.634 36.620 51.311 1.00 21.61 c ATOM 3979 N HIS B 176 96.217 42.567 52.570 1.00 17.50 N
ATOM 3980 CA HIS B 176 95.889 43.636 53.469 1.00 20.14 c
ATOM 3981 C HIS B 176 94.360 43.710 53.601 1.00 21.15 c
ATOM 3982 O HIS B 176 93.697 43.974 52.598 1.00 21.58 o
ATOM 3983 CB HIS B 176 96.463 44.968 52.938 1.00 21.60 c ATOM 3984 CG HIS B 176 97.862 44.760 52.425 1.00 26.55 c
ATOM 3985 ND1 HIS B 176 98.891 44.778 53.345 1.00 28.92 N
ATOM 3986 CD2 HIS B 176 98.398 44.491 51.223 1.00 21.41 c
ATOM 3987 CE1 HIS B 176 100.000 44.545 52.699 1.00 16.22 C
ATOM 3988 NE2 HIS B 176 99.771 44.351 51.420 1.00 24.82 N ATOM 3989 N LEU B 177 93.930 43.374 54.787 1.00 19.28 N
ATOM 3990 CA LEU B 177 92.523 43.207 55.083 1.00 20.75 C
ATOM 3991 C LEU B 177 91.935 44.466 55.688 1.00 21.35 C
ATOM 3992 O LEU B 177 92.383 45.057 56.659 1.00 19.15 ' 0
ATOM 3993 CB LEU B 177 92.288 42.047 56.057 1.00 22.63 c ATOM 3994 CG LEU B 177 92.910 40.694 55.691 1.00 19.00 c
ATOM 3995 CD1 LEU B 177 92.545 39.675 56.773 1.00 19.67 c
ATOM 3996 CD2 LEU B 177 92.457 40.201 54.318 1.00 19.27 c
ATOM 3997 N TYR B 178 90.787 44.840 55.114 1.00 14.82 N
ATOM 3998 CA TYR B 178 89.982 45.956 55.543 1.00 15.89 c ATOM 3999 C TYR B 178 88.565 45.492 55.865 1.00 14.99 C
ATOM 4000 O TYR B 178 87.795 45.103 54.968 1.00 17.46 O
ATOM 4001 CB TYR B 178 90.003 47.028 54.452 1.00 13.76 C
ATOM 4002 CG TYR B 178 91.363 47.691 54.257 1.00 18.56 C ATOM 4003 CD1 TYR B 178 92.255 47.228 53.310 1.00 16.23 C
ATOM 4004 CD2 TYR B 178 91.664 48.817 55.003 1.00 14.49 C
ATOM 4005 CE1 TYR B 178 93.490 47.848 53.135 1.00 19.41 c
ATOM 4006 CE2 TYR B 178 92.889 49.453 54.813 1.00 13.99 c
ATOM 4007 CZ TYR B 178 93.779 48.971 53.891 1.00 18.09 c ATOM 4008 OH TYR B 178 94.996 49.588 53.671 1.00 19.67 O
ATOM 4009 N LEU B 179 88.252 45.433 57.155 1.00 14.15 N
ATOM 4010 CA LEU B 179 86.945 44.949 57.574 1.00 15.09 c
ATOM 4011 C LEU B 179 85.908 46.031 57.335 1.00 18.64 c
ATOM 4012 O LEU B 179 86.125 47.170 57.773 1.00 15.59 O ATOM 4013 CB LEU B 179 87.029 44.576 59.053 1.00 17.68 c
ATOM 4014 CG LEU B 179 85.858 43.984 59.803 1.00 19.25 c
ATOM 4015 CD1 LEU B 179 85.208 42.837 59.020 1.00 17.72 c
ATOM 4016 CD2 LEU B 179 86.352 43.412 61.146 1.00 19.10 c
ATOM 4017 N ASP B 180 84.827 45.736 56.611 1.00 13.88 N ATOM 4018 CA ASP B 180 83.869 46.850 56.364 1.00 11.40 C
ATOM 4019 C ASP B 180 83.148 47.333 57.600 1.00 16.37 C
ATOM 4020 O ASP B 180 82.611 46.570 58.398 1.00 16.08 O
ATOM 4021 CB ASP B 180 82.804 46.411 55.332 1.00 16.37 C
ATOM 4022 CG ASP B 180 81.995 47.642 54.897 1.00 11.61 C ATOM 4023 ODl ASP B 180 82.599 48.428 54.135 1.00 16.82 o
ATOM 4024 OD2 ASP B 180 80.862 47.773 55.344 1.00 14.55 o
ATOM 4025 N VAL B 181 82.956 48.678 57.708 1.00 12.65 N
ATOM 4026 CA VAL B 181 82.199 49.268 58.767 1.00 14.80 c
ATOM 4027 C VAL B 181 81.137 50.252 58.253 1.00 14.21 c ATOM 4028 O VAL B 181 80.827 51.259 58.862 1.00 15.92 0
ATOM 4029 CB VAL B 181 83.023 49.951 59.867 1.00 17.14 c
ATOM 4030 CGI VAL B 181 83.817 48.896 60.638 1.00 16.17 c
ATOM 4031 CG2 VAL B 181 84.003 50.983 59.295 1.00 13.24 c
ATOM 4032 N ALA B 182 80.488 49.882 57.152 1.00 14.94 N ATOM 4033 CA ALA B 182 79.336 50.623 56.613 1.00 13.26 c
ATOM 4034 C ALA B 182 79.668 52.072 56.259 1.00 15.95 c
ATOM 4035 O ALA B 182 80.574 52.224 55.459 1.00 13.82 o
ATOM 4036 CB ALA B 182 78.077 50.580 57.479 1.00 15.06 c
ATOM 4037 N ASN B 183 78.947 53.053 56.828 1.00 16.04 N ATOM 4038 CA ASN B 183 79.265 54.430 56.463 1.00 14.57 c
ATOM 4039 C ASN B 183 78.919 55.295 57.658 1.00 16.62 c
ATOM 4040 O ASN B 183 78.236 54.846 58.588 1.00 15.71 0
ATOM 4041 CB ASN B 183 78.480 54.927 55.237 1.00 14.63 c
ATOM 4042 CG ASN B 183 77.001 55.065 55.438 1.00 14.62 c ATOM 4043 ODl ASN B 183 76.475 56.190 55.606 1.00 13.42 o
ATOM 4044 ND2 ASN B 183 76.214 53.977 55.388 1.00 16.69 N
ATOM 4045 N GLY B 184 79.367 56.553 57.578 1.00 14.55 N
ATOM 4046 CA GLY B 184 79.138 57.420 58.712 1.00 16.22 C
ATOM 4047 C GLY B 184 77.674 57.597 59.071 1.00 16.07 C ATOM 4048 O GLY B 184 77.376 57.813 60.275 1.00 19.13 0
ATOM 4049 N GLY B 185 76.722 57.531 58.158 1.00 15.30 N
ATOM 4050 CA GLY B 185 75.316 57.665 58.412 1.00 18.26 C
ATOM 4051 C GLY B 185 74.647 56.500 59.133 1.00 20.22 • C
ATOM 4052 O GLY B 185 73.528 56.625 59.641 1.00 20.18 0 ATOM 4053 N TRP B 186 75.328 55.354 59.138 1.00 16.86 N
ATOM 4054 CA TRP B 186 74.807 54.152 59.763 1.00 18.31 C
ATOM 4055 C TRP B 186 75.444 53.953 61.148 1.00 19.08 c
ATOM 4056 O TRP B 186 74.728 53.882 62.153 1.00 19.51 0
ATOM 4057 CB TRP B 186 75.154 52.921 58.882 1.00 15.77 c ATOM 4058 CG TRP B 186 74.,468 51.,641 59.,240 1.00 18.,73 c
ATOM 4059 CD1 TRP B 186 74. ,001 51. ,208 60. ,459 1.00 22. ,80 c
ATOM 4060 CD2 TRP B 186 74. .174 50. ,566 58. ,333 1.00 14. ,01 c
ATOM 4061 NE1 TRP B 186 73. .426 49. .957 60. ,363 1.00 19, ,33 N
ATOM 4062 CE2 TRP B 186 73. .513 49. ,549 59. ,061 1.00 18, ,76 c
ATOM 4063 CE3 TRP B 186 74. .372 50. .359 56. ,967 1.00 16, ,51 c
ATOM 4064 CZ2 TRP B 186 73. ,074 48. .368 58. ,453 1.00 16. ,28 c
ATOM 4065 CZ3 TRP B 186 73. .948 49. .190 56. .367 1.00 17. ,55 c
ATOM 4066 CH2 TRP B 186 73. ,296 48. ,210 57. .115 1.00 18. ,14 c
ATOM 4067 N LEU B 187 76. ,769 53. ,926 61. ,187 1.00 18. ,02 N
ATOM 4068 CA LEU B 187 77. ,494 53. ,658 62. .420 1.00 17. ,51 C
ATOM 4069 C LEU B 187 78. .296 54. .812 62. ,993 1.00 22. .64 C
ATOM 4070 O LEU B 187 79. ,034 54. ,668 63. .989 1.00 19. ,42 o
ATOM 4071 CB LEU B 187 78. ,456 52. .469 62. .187 1.00 12. ,33 c
ATOM 4072 CG LEU B 187 77. .746 51. .144 61. .813 1.00 13. .44 c
ATOM 4073 CD1 LEU B 187 78. ,720 50. .036 61. ,481 1.00 16. ,68 c
ATOM 4074 CD2 LEU B 187 76. .737 50. .778 62. .907 1.00 16. ,94 c
ATOM 4075 N GLY B 188 78. .154 56. .008 62. .417 1.00 17. .49 N
ATOM 4076 CA GLY B 188 79. .042 57. .102 62. ,879 1.00 18. ,99 C
ATOM 4077 C GLY B 188 78. .385 58. .011 63. ,904 1.00 21. ,19 C
ATOM 4078 O GLY B 188 78. .987 59. .012 64. .334 1.00 22. .58 O
ATOM 4079 N TRP B 189 77. .171 57. .698 64. .335 1.00 19. .19 N
ATOM 4080 CA TRP B 189 76. .481 58. .462 65. ,351 1.00 18. .56 C
ATOM 4081 C TRP B 189 77. .189 58. .251 66. .686 1.00 17. .15 C
ATOM 4082 O TRP B 189 77. .791 57. .202 66. .914 1.00 21. .16 o
ATOM 4083 CB TRP B 189 75. .038 58. .019 65. .527 1.00 24. ,63 C
ATOM 4084 CG TRP B 189 74. .290 58. .220 64. .240 1.00 21. .45 c
ATOM 4085 CD1 TRP B 189 74. .115 57. .301 63. .254 1.00 20. .66 c
ATOM 4086 CD2 TRP B 189 73. .654 59. .425 63. .814 1.00 20, .71 c
ATOM 4087 NE1 TRP B 189 73. .387 57. .843 62. .228 1.00 23. .07 N
ATOM 4088 CE2 TRP B 189 73. .081 59. .145 62. .543 1.00 20. .52 c
ATOM 4089 CE3 TRP B 189 73. .489 60. .689 64. .367 1.00 22. .01 c
ATOM 4090 CZ2 TRP B 189 72. .370 60. .107 61. .830 1.00 30. .12 c
ATOM 4091 CZ3 TRP B 189 72. .785 61. .648 63. .657 1.00 31. .63 c
ATOM 4092 CH2 TRP B 189 72. .227 61. .336 62. .411 1.00 25, .50 c
ATOM 4093 N ALA B 190 77. .038 59. .277 67. .527 1.00 22. .55 N
ATOM 4094 CA ALA B 190 77. .668 59. .162 68. .838 1.00 20. .98 c
ATOM 4095 C ALA B 190 77. .286 57. .850 69. .521 1.00 20. .20 c
ATOM 4096 O ALA B 190 78. .187 57. .320 70. .172 1.00 22. .91 o
ATOM 4097 CB ALA B 190 77. .260 60. .333 69. .720 1.00 20, .91 c
ATOM 4098 N ASP B 191 76. .053 57. .388 69. .485 1.00 21. .69 N
ATOM 4099 CA ASP B 191 75. .726 56, .149 70. .196 1.00 21. .21 c
ATOM 4100 C ASP B 191 76, .133 54. .889 69. .452 1.00 25, .03 c
ATOM 4101 o ASP B 191 75. .835 53, .780 69, .936 1.00 27. .43 o
ATOM 4102 CB ASP B 191 74, .242 56, .161 70, .528 1.00 23. .50 c
ATOM 4103 CG ASP B 191 73, .313 56, .167 69, .337 1.00 34, .66 c
ATOM 4104 ODl ASP B 191 73, .715 56, .403 68, .185 1.00 28. .87 o
ATOM 4105 OD2 ASP B 191 72, .102 55, .925 69, .521 1.00 39. .36 o
ATOM 4106 N LYS B 192 76, .708 54. .961 68, .244 1.00 22. .39 N
ATOM 4107 CA LYS B 192 77. .035 53. .753 67, .497 1.00 21. .64 c
ATOM 4108 C LYS B 192 78, .505 53. .458 67. .315 1.00 18. .45 c
ATOM 4109 o LYS B 192 78, .925 52, .341 66, .985 1.00 19. .82 o
ATOM 4110 CB LYS B 192 76, .397 53, .858 66, .095 1.00 18. .64 c
ATOM 4111 CG LYS B 192 74, .909 54, .087 66, .080 1.00 27. .26 c
ATOM 4112 CD LYS B 192 74 .112 52, .803 65, .949 1.00 32, .40 c
ATOM 4113 CE LYS B 192 73 .210 52, .595 67, .147 1.00 45, .02 c
ATOM 4114 NZ LYS B 192 71. .956 53, .403 67, .110 1.00 39, .32 N
ATOM 4115 N LEU B 193 79 .362 54, .470 67, .635 1.00 18, .85 N
ATOM 4116 CA LEU B 193 80 .785 54, .260 67, .463 1.00 16, .44 C ATOM 4117 C LEU B 193 81.,337 53..159 68..374 1.00 17..74 c
ATOM 4118 o LEU B 193 82. ,117 52. .317 67. .925 1.00 17. .73 o
ATOM 4119 CB LEU B 193 81. ,543 55. ,578 67. .670 1.00 22. .25 c
ATOM 4120 CG LEU B 193 81. ,264 56. .699 66. .645 1.00 20. .40 c
ATOM 4121 CD1 LEU B 193 81. ,824 57. .997 67. .255 1.00 23. .94 c
ATOM 4122 CD2 LEU B 193 81. ,909 56. ,441 65. .302 1.00 20, .89 c
ATOM 4123 N GLU B 194 80. ,957 53. .189 69. ,666 1.00 21. .89 N
ATOM 4124 CA GLU B 194 81. ,459 52. .212 70. ,634 1.00 23. .64 c
ATOM 4125 C GLU B 194 80, ,961 50. .799 70. .321 1.00 16. .92 c
ATOM 4126 O GLU B 194 81. ,784 49. .916 70. .239 1.00 20. .19 o
ATOM 4127 CB GLU B 194 81. ,192 52. .617 72. .090 1.00 22. .40 c
ATOM 4128 CG GLU B 194 82, ,108 53. .730 72. .607 1.00 21. .77 c
ATOM 4129 CD GLU B 194 83. .523 53. .298 72. .932 1.00 22. .30 c
ATOM 4130 OE1 GLU B 194 83. ,765 52. .158 73. .360 1.00 24. .06 o
ATOM 4131 OE2 GLU B 194 84. ,489 54. .101 72. .809 1.00 21. .90 o
ATOM 4132 N PRO B 195 79. ,693 50. .673 70. .037 1.00 17. .89 N
ATOM 4133 CA PRO B 195 79. ,115 49. .382 69. .643 1.00 20. .40 c
ATOM 4134 C PRO B 195 79. ,814 48. .784 68. ,438 1.00 22. ,63 c
ATOM 4135 O PRO B 195 80. .025 47. .563 68. .298 1.00 22. .72 o
ATOM 4136 CB PRO B 195 77. ,645 49. ,719 69. ,321 1.00 23. .25 c
ATOM 4137 CG PRO B 195 77. .372 50. .862 70. .264 1.00 22. .51 c
ATOM 4138 CD PRO B 195 78. .666 51. .682 70. .278 1.00 19. .04 c
ATOM 4139 N THR B 196 80. .172 49. .638 67, .447 1.00 20. .58 N
ATOM 4140 CA THR B 196 80. .898 49. .206 66. .266 1.00 19. .89 c
ATOM 4141 C THR B 196 82. .272 48. .665 66. .635 1.00 24. .24 c
ATOM 4142 O THR B 196 82. .738 47. .623 66. .194 1.00 22. .29 o
ATOM 4143 CB THR B 196 81. .134 50. .350 65. .244 1.00 17. .63 c
ATOM 4144 OG1 THR B 196 79. .848 50. .839 64. .879 1.00 19. .07 o
ATOM 4145 CG2 THR B 196 81, .931 49. .843 64. .041 1.00 17. .48 c
ATOM 4146 N ALA B 197 82. .973 49. .394 67. .506 1.00 20. .28 N
ATOM 4147 CA ALA B 197 84. .267 48. .931 67. .971 1.00 17. .40 c
ATOM 4148 C ALA B 197 84, .169 47. .590 68. .726 1.00 17. .96 c
ATOM 4149 O ALA B 197 85. .070 46. ,783 68. .539 1.00 19. .17 o
ATOM 4150 CB ALA B 197 84. .848 50. .007 68. .893 1.00 18. .28 c
ATOM 4151 N GLN B 198 83. .109 47. .400 69. .483 1.00 24. .07 N
ATOM 4152 CA GLN B 198 82. .891 46. .175 70. .250 1.00 20. .46 c
ATOM 4153 C GLN B 198 82. .731 44. .999 69. .282 1.00 24. .02 c
ATOM 4154 O GLN B 198 83. .379 43. .965 69. .426 1.00 20. .77 o
ATOM 4155 CB GLN B 198 81. .635 46. .302 71. .091 1.00 24, .08 c
ATOM 4156 CG GLN B 198 81. .336 45. .090 72. .005 1.00 24, .24 c
ATOM 4157 CD GLN B 198 81. .023 45. .766 73. .348 1.00 46, .63 c
ATOM 4158 OE1 GLN B 198 81. .914 46, .254 74. .057 1.00 49, .94 o
ATOM 4159 NE2 GLN B 198 79, .738 45, .868 73. .646 1.00 32, .33 N
ATOM 4160 N GLU B 199 81, .964 45, .263 68. .206 1.00 21, .26 N
ATOM 4161 CA GLU B 199 81, .710 44, .210 67. .219 1.00 17, .59 c
ATOM 4162 C GLU B 199 82, .962 43, .750 66. .546 1.00 18, .76 c
ATOM 4163 O GLU B 199 83, .259 42. .572 66. .319 1.00 20, .01 o
ATOM 4164 CB GLU B 199 80, .661 44. .680 66. .175 1.00 14, .84 c
ATOM 4165 CG GLU B 199 80, .115 43. .422 65. .480 1.00 21, .74 c
ATOM 4166 CD GLU B 199 79, .175 42. .675 66. .415 1.00 22, .93 c
ATOM 4167 OE1 GLU B 199 78, .933 43. .099 67. .563 1.00 25, .14 o
ATOM 4168 OE2 GLU B 199 78, .683 41. ,609 66. .000 1.00 25, .57 o
ATOM 4169 N VAL B 200 83, .858 44. .700 66, .188 1.00 18, .66 N
ATOM 4170 CA VAL B 200 85, .154 44, .447 65, .642 1.00 15, .67 c
ATOM 4171 C VAL B 200 85, .989 43, .606 66. .611 1.00 20, .44 c
ATOM 4172 O VAL B 200 86, .705 42. .706 66. .180 1.00 19, .49 o
ATOM 4173 CB VAL B 200 85, .847 45, .774 65, .268 1.00 15, .78 c
ATOM 4174 CGI VAL B 200 87. .303 45. .574 64, .934 1.00 15, .44 c
ATOM 4175 CG2 VAL B 200 85, .140 46. .395 64. .055 1.00 20, .64 c ATOM 4176 N ALA B 201 85..954 43.,931 67.,904 1.00 21.,57 N
ATOM 4177 CA ALA B 201 86. ,771 43. .176 68. ,863 1.00 21. ,21 C
ATOM 4178 C ALA B 201 86, ,249 41. .746 68. ,914 1.00 23. ,43 C
ATOM 4179 O ALA B 201 87. ,070 40. ,840 68. ,864 1.00 23. ,67 o
ATOM 4180 CB ALA B 201 86. ,701 43. ,889 70. ,203 1.00 24. ,56 c
ATOM 4181 N THR B 202 84. ,935 41. ,591 69. ,002 1.00 17. ,97 N
ATOM 4182 CA THR B 202 84. ,363 40. ,229 69. ,026 1.00 21. ,03 c
ATOM 4183 C THR B 202 84. ,776 39. ,414 67. ,816 1.00 23. ,31 c
ATOM 4184 O THR B 202 85. .291 38. ,288 67. ,880 1.00 22. ,39 o
ATOM 4185 CB THR B 202 82. .846 40. ,408 69. ,146 1.00 21. ,23 c
ATOM 4186 OG1 THR B 202 82. ,532 40. ,984 70. ,419 1.00 26. .10 o
ATOM 4187 CG2 THR B 202 82. ,103 39. ,075 69. ,021 1.00 19. ,41 c
ATOM 4188 N ILE B 203 84. ,649 39. ,961 66. .604 1.00 20. ,55 N
ATOM 4189 CA ILE B 203 85. ,060 39. .248 65. ,383 1.00 17. ,22 c
ATOM 4190 C ILE B 203 86. ,537 38. ,940 65. ,344 1.00 21. ,69 c
ATOM 4191 O ILE B 203 86. ,960 37. ,849 64. .925 1.00 24. ,70 o
ATOM 4192 CB ILE B 203 84. ,671 40. ,097 64. ,146 1.00 23. ,56 c
ATOM 4193 CGI ILE B 203 83. ,156 40. ,158 64. .079 1.00 20. ,76 c
ATOM 4194 CG2 ILE B 203 85. .266 39. ,551 62. ,854 1.00 22. ,65 c
ATOM 4195 CD1 ILE B 203 82. ,542 41. ,185 63. ,182 1.00 16. ,15 c
ATOM 4196 N LEU B 204 87. .374 39. ,870 65. ,815 1.00 21. ,97 N
ATOM 4197 CA LEU B 204 88. ,808 39. ,629 65. ,818 1.00 21. ,00 C
ATOM 4198 C LEU B 204 89. ,142 38. .558 66. ,871 1.00 19. ,40 C
ATOM 4199 O LEU B 204 90. .024 37. .761 66. .581 1.00 22. ,15 O
ATOM 4200 CB LEU B 204 89. .636 40. .903 66. ,041 1.00 22. .16 c
ATOM 4201 CG LEU B 204 89. .683 41. .872 64. .860 1.00 26. .66 c
ATOM 4202 CD1 LEU B 204 90. .227 43. .248 65. .256 1.00 20. .14 c
ATOM 4203 CD2 LEU B 204 90. .510 41. .268 63. .734 1.00 19. .60 c
ATOM 4204 N GLN B 205 88. .431 38. .536 67. .984 1.00 25. .29 N
ATOM 4205 CA GLN B 205 88. .689 37. .441 68. .953 1.00 29. .23 C
ATOM 4206 C GLN B 205 88. .481 36. .104 68. .240 1.00 29. .46 C
ATOM 4207 O GLN B 205 89. .308 35. .183 68. .275 1.00 31. .76 O
ATOM 4208 CB GLN B 205 87. .778 37. .588 70. .156 1.00 31. .93 c
ATOM 4209 CG GLN B 205 87. .873 38. .892 70. .913 1.00 36. .03 c
ATOM 4210 CD GLN B 205 86. .973 39. .045 72. .115 1.00 53. .54 c
ATOM 4211 OE1 GLN B 205 85. .754 39. .207 72. .055 1.00 58. .56 o
ATOM 4212 NE2 GLN B 205 87. .591 39. .016 73. .298 1.00 59. .02 N
ATOM 4213 N LYS B 206 87. .366 35. .960 67. .515 1.00 27. .02 N
ATOM 4214 CA LYS B 206 87. .055 34. .738 66. .782 1.00 29, .14 C
ATOM 4215 C LYS B 206 88. .019 34. .360 65. .687 1.00 30, .36 c
ATOM 4216 O LYS B 206 88. .238 33. .180 65. .372 1.00 34, .85 o
ATOM 4217 CB LYS B 206 85. .620 34. .848 66. .211 1.00 27, .96 c
ATOM 4218 CG LYS B 206 84. .561 34. .708 67. .291 1.00 26, .91 c
ATOM 4219 CD LYS B 206 83. .195 35. .168 66. .822 1.00 36, .28 c
ATOM 4220 CE LYS B 206 82, .131 35, .001 67. .890 1.00 37. .81 c
ATOM 4221 NZ LYS B 206 82, .314 33, .718 68. .638 1.00 46. .57 N
ATOM 4222 N ALA B 207 88, .716 35, .284 65. .050 1.00 18, .42 N
ATOM 4223 CA ALA B 207 89, .696 35, .096 64, .023 1.00 19, .99 c
ATOM 4224 C ALA B 207 90, .984 34, .424 64, .499 1.00 22, .55 c
ATOM 4225 O ALA B 207 91, .703 33, .827 63, .706 1.00 29, .59 o
ATOM 4226 CB ALA B 207 90, .061 36, .463 63, .428 1.00 24, .95 c
ATOM 4227 N GLY B 208 91, .259 34, .556 65, .796 1.00 24, .32 N
ATOM 4228 CA GLY B 208 92 .446 33, .948 66, .388 1.00 29, .50 ■ c
ATOM 4229 C GLY B 208 93 .367 34, .971 67, .047 1.00 33, .60 c
ATOM 4230 O GLY B 208 93, .393 36, .160 66. .727 1.00 29, .02 o
ATOM 4231 N ASN B 209 94, .179 34, .483 67. .985 1.00 32. .42 N
ATOM 4232 CA ASN B 209 95, .127 35, .288 68. .723 1.00 36, .56 c
ATOM 4233 C ASN B 209 96 .022 36, .241 67, .969 1.00 35, .01 c
ATOM 4234 O ASN B 209 96 .286 37, .375 68, .368 1.00 39, .29 o ATOM 4235 CB ASN B 209 96.102 34.307 69.434 1.00 40.51 C
ATOM 4236 CG ASN B 209 95.501 34.026 70.802 1.00 45.73 C
ATOM 4237 ODl ASN B 209 95.316 34.992 71.541 1.00 45.04 O
ATOM 4238 ND2 ASN B 209 95.202 32.771 71.083 1.00 46.97 N ATOM 4239 N ASN B 210 96.639 35.699 66.922 1.00 32.93 N
ATOM 4240 CA ASN B 210 97.585 36.441 66.113 1.00 32.79 C
ATOM 4241 C ASN B 210 96.962 36.953 64.824 1.00 31.82 C
ATOM 4242 O ASN B 210 97.687 37.414 63.951 1.00 34.76 o
ATOM 4243 CB ASN B 210 98.782 35.527 65.819 1.00 26.91 c ATOM 4244 CG ASN B 210 99.657 35.408 67.060 1.00 41.97 c
ATOM 4245 ODl ASN B 210 99.999 36.425 67.659 1.00 41.64 o
ATOM 4246 ND2 ASN B 210 99.982 34.182 67.442 1.00 31.49 N
ATOM 4247 N ALA B 211 95.653 36.837 64.699 1.00 29.07 N
ATOM 4248 CA ALA B 211 94.971 37.289 63.492 1.00 29.41 C ATOM 4249 C ALA B 211 94.990 38.820 63.433 1.00 32.04 C
ATOM 4250 O ALA B 211 94.552 39.426 64.425 1.00 32.62 o
ATOM 4251 CB ALA B 211 93.495 36.901 63.543 1.00 23.68 C
ATOM 4252 N LYS B 212 95.416 39.361 62.302 1.00 24.74 N
ATOM 4253 CA LYS B 212 95.385 40.829 62.245 1.00 27.27 C ATOM 4254 C LYS B 212 94.603 41.298 61.021 1.00 28.66 C
ATOM 4255 O LYS B 212 94.354 40.534 60.092 1.00 22.48 O
ATOM 4256 CB LYS B 212 96.786 41.411 62.167 1.00 35.37 C
ATOM 4257 CG LYS B 212 97.730 40.830 61.148 1.00 46.38 c
ATOM 4258 CD LYS B 212 98.806 39.954 61.744 1.00 53.65 c ATOM 4259 CE LYS B 212 99.834 40.670 62.600 1.00 58.55 c
ATOM 4260 NZ LYS B 212 100.782 39.680 63.206 1.00 62.28 N
ATOM 4261 N ILE B 213 94.250 42.574 61.052 1.00 22.99 N
ATOM 4262 CA ILE B 213 93.661 43.263 59.894 1.00 21.04 C
ATOM 4263 C ILE B 213 94.415 44.604 59.825 1.00 21.00 C ATOM 4264 o ILE B 213 94.865 45.032 60.893 1.00 21.34 O
ATOM 4265 CB ILE B 213 92.158 43.552 59.955 1.00 18.61 c
ATOM 4266 CGI ILE B 213 91.757 44.315 61.205 1.00 19.97 c
ATOM 4267 CG2 ILE B 213 91.387 42.210 59.857 1.00 20.94 c
ATOM 4268 CD1 ILE B 213 90.298 44.682 61.343 1.00 17.36 c ATOM 4269 N ARG B 214 94.462 45.214 58.666 1.00 24.30 N
ATOM 4270 CA ARG B 214 95.078 46.533 58.504 1.00 21.11 c
ATOM 4271 C ARG B 214 94.124 47.591 59.043 1.00 24.53 c
ATOM 4272 O ARG B 214 94.507 48.605 59.661 1.00 20.28 o
ATOM 4273 CB ARG B 214 95.425 46.813 57.035 1.00 19.86 c ATOM 4274 CG ARG B 214 95.725 48.301 56.765 1.00 19.19 c
ATOM 4275 CD ARG B 214 97.012 48.673 57.511 1.00 22.59 c
ATOM 4276 NE ARG B 214 97.350 50.091 57.324 1.00 20.91 N
ATOM 4277 CZ ARG B 214 98.432 50.691 57.812 1.00 24.12 C
ATOM 4278 NHl ARG B 214 99.297 50.011 58.549 1.00 24.52 N ATOM 4279 NH2 ARG B 214 98.666 51.992 57.600 1.00 21.57 N
ATOM 4280 N GLY B 215 92.820 47.388 58.826 1.00 18.54 N
ATOM 4281 CA GLY B 215 91.857 48.396 59.259 1.00 19.25 C
ATOM 4282 C GLY B 215 90.498 48.108 58.625 1.00 19.04 c
ATOM 4283 O GLY B 215 89.978 47.011 58.746 1.00 19.44 o ATOM 4284 N PHE B 216 89.815 49.203 58.277 1.00 19.68 N
ATOM 4285 CA PHE B 216 88.409 49.183 57.895 1.00 14.50 c
ATOM 4286 C PHE B 216 88.107 49.853 56.552 1.00 19.42 c
ATOM 4287 O PHE B 216 88.901 50.617 56.024 1.00 15.19 o
ATOM 4288 CB PHE B 216 87.642 49.917 59.012 1.00 17.06 c ATOM 4289 CG PHE B 216 88.044 49.412 60.390 1.00 17.34 c
ATOM 4290 CD1 PHE B 216 87.646 48.179 60.831 1.00 19.49 c
ATOM 4291 CD2 PHE B 216 88.926 50.166 61.174 1.00 21.89 c
ATOM 4292 CE1 PHE B 216 88.037 47.706 62.075 1.00 23.76 c
ATOM 4293 CE2 PHE B 216 89.334 49.684 62.406 1.00 19.58 c ATOM 4294 CZ PHE B 216 88.,890 48.,452 62.,870 1.00 21.,70 c
ATOM 4295 N SER B 217 86. .922 49. ,497 56. .006 1.00 16. .32 N
ATOM 4296 CA SER B 217 86. ,474 50. ,183 54. .788 1.00 16. ,98 C
ATOM 4297 C SER B 217 85. ,180 50. .925 55. .147 1.00 15. .15 c
ATOM 4298 O SER B 217 84. .440 50. ,462 56. .015 1.00 14. .34 O
ATOM 4299 CB SER B 217 86. .227 49. ,279 53. .606 1.00 13. .74 c
ATOM 4300 OG SER B 217 85. .326 48. ,193, 53. .828 1.00 12. ,93 O
ATOM 4301 N SER B 218 84. ,951 52. ,061 54. ,487 1.00 12. ,49 N
ATOM 4302 CA SER B 218 83. .675 52. ,747 54. ,704 1.00 12. ,51 c
ATOM 4303 C SER B 218 83. ,210 53. ,404 53. .398 1.00 12. .40 c
ATOM 4304 O SER B 218 83. ,985 53. ,623 52. .462 1.00 13. ,94 O
ATOM 4305 CB SER B 218 83. ,751 53. .770 55. .827 1.00 17. ,22 c
ATOM 4306 OG ; F_SER B 218 84. ,532 54. .868 55. .397 0.50 14. ,96 O
ATOM 4307 OG ] BSER B 218 82. .502 54. .368 56. .122 0.50 16. .14 O
ATOM 4308 N ASN B 219 81. .929 53. .702 53. .337 1.00 14. .12 N
ATOM 4309 CA ASN B 219 81. ,208 54. .299 52. ,231 1.00 12. .90 C
ATOM 4310 C ASN B 219 81. .113 53. .462 50. .987 1.00 16. .12 C
ATOM 4311 O ASN B 219 80. .782 53. ,927 49. .875 1.00 12. .91 O
ATOM 4312 CB ASN B 219 81. ,867 55. .662 51. .876 1.00 10. .77 C
ATOM 4313 CG ASN B 219 80. ,897 56. .685 51. .330 1.00 16. .28 C
ATOM 4314 ODl ASN B 219 79. ,799 56. .902 51. .815 1.00 17. .19 O
ATOM 4315 ND2 ASN B 219 81. ,306 57. .374 50. ,250 1.00 13. .28 N
ATOM 4316 N VAL B 220 81. ,400 52. .147 51. ,127 1.00 13. .21 N
ATOM 4317 CA VAL B 220 81. ,315 51. ,260 49. ,996 1.00 13. ,06 C
ATOM 4318 C VAL B 220 79. .860 51. .199 49. .547 1.00 13. .26 C
ATOM 4319 0 VAL B 220 78. .910 50. .985 50. .281 1.00 13. .48 O
ATOM 4320 CB VAL B 220 81. .753 49. .830 50. .385 1.00 13. .78 C
ATOM 4321 CGI VAL B 220 81. .547 48. .868 49. .222 1.00 13. .64 C
ATOM 4322 CG2 VAL B 220 83. .199 49. .850 50. .862 1.00 14. .47 C
ATOM 4323 N SER B 221 79. .680 51. .466 48. .244 1.00 9. .67 N
ATOM 4324 CA SER B 221 78. .378 51. .572 47. .610 1.00 11. .45 C
ATOM 4325 C SER B 221 77, .516 52. .699 48. .132 1.00 13. .47 C
ATOM 4326 O SER B 221 76. .336 52. ,762 47. .785 1.00 14. .77 O
ATOM 4327 CB SER B 221 77. .505 50. .294 47. .594 1.00 12. .65 C
ATOM 4328 OG ,f\SER B 221 76. .769 50. .171 48. .791 0.30 18. .63 O
ATOM 4329 OG : BSER B 221 78. .324 49. .126 47. .513 0.70 9. .29 O
ATOM 4330 N ASN B 222 78. .085 53. .611 48. .902 1.00 12. .82 N
ATOM 4331 CA ASN B 222 77. .345 54. .753 49. .412 1.00 11. .81 C
ATOM 4332 C ASN B 222 77. .835 56. .003 48. .709 1.00 13. .32 C
ATOM 4333 O ASN B 222 78. .395 55. .957 47. .618 1.00 14. .21 O
ATOM 4334 CB ASN B 222 77. .416 54. .905 50. .931 1.00 10. .47 C
ATOM 4335 CG ASN B 222 76. .177 55. .500 51. .553 1.00 21, .50 c
ATOM 4336 ODl ASN B 222 75. .953 56, .728 51, .558 1.00 18, .33 O
ATOM 4337 ND2 ASN B 222 75. .378 54, .578 52. .121 1.00 21. .35 N
ATOM 4338 N TYR B 223 77. .387 57, .152 49. .273 1.00 12. .91 N
ATOM 4339 CA TYR B 223 77. .534 58, .381 48. .477 1.00 14. .69 C
ATOM 4340 C TYR B 223 78. .008 59, .592 49. .271 1.00 15. .82 c
ATOM 4341 O TYR B 223 77. .906 60, .753 48. .824 1.00 13. .70 O
ATOM 4342 CB TYR B 223 76. .133 58, .730 47. .923 1.00 14, .43 c
ATOM 4343 CG TYR B 223 75, .378 57, .629 47. .190 1.00 12, .12 c
ATOM 4344 CD1 TYR B 223 74, .615 56, .724 47, .912 1.00 17, .11 c
ATOM 4345 CD2 TYR B 223 75. .462 57, .507 45. .796 1.00 15, .17 c
ATOM 4346 CE1 TYR B 223 73, .946 55, .694 47, .297 1.00 13. .38 c
ATOM 4347 CE2 TYR B 223 74, .769 56, .495 45. .184 1.00 14. .55 c
ATOM 4348 CZ TYR B 223 74, .022 55, .597 45, .921 1.00 12, .53 c
ATOM 4349 OH TYR B 223 73, .321 54. .625 45, .270 1.00 14, .37 O
ATOM 4350 N ASN B 224 78, .454 59, .323 50, .508 1.00 13, .79 N
ATOM 4351 CA ASN B 224 78, .842 60. .453 51, .363 1.00 12. .59 c
ATOM 4352 C ASN B 224 80 .120 61, .070 50, .847 1.00 14, .44 c ATOM 4353 O ASN B 224 80.968 60.,387 50.275 1.00 12.99 O
ATOM 4354 CB ASN B 224 79. 167 59. ,917 52. ,781 1.00 16. 69 c
ATOM 4355 CG ASN B 224 77. ,938 59. ,330 53. ,427 1.00 14. 29 c
ATOM 4356 ODl ASN B 224 76. 808 59. ,567 53. ,104 1.00 16. 54 o ATOM 4357 ND2 ASN B 224 78. 142 58. ,414 54. ,402 1.00 14. ,31 N
ATOM 4358 N PRO B 225 80. ,259 62. ,388 51. .020 1.00 16. ,23 N
ATOM 4359 CA PRO B 225 81. 490 63. ,065 50. ,712 1.00 17. ,76 C
ATOM 4360 C PRO B 225 82. ,639 62. ,611 51. ,615 1.00 16. 04 C
ATOM 4361 O PRO B 225 82. .396 62. ,280 52. ,786 1.00 17. ,79 o ATOM 4362 CB PRO B 225 81. ,199 64. .571 50. ,986 1.00 17. ,09 c
ATOM 4363 CG PRO B 225 80. ,087 64. .480 51. ,991 1.00 16. ,17 c
ATOM 4364 CD PRO B 225 79. ,300 63. .187 51. ,788 1.00 16. .78 c
ATOM 4365 N TYR B 226 83. ,849 62. .647 51. ,095 1.00 18. 45 N
ATOM 4366 CA TYR B 226 85. .011 62. ,365 51. ,936 1.00 14. .80 c ATOM 4367 C TYR B 226 85. ,263 63. .539 52. .885 1.00 20. ,68 c
ATOM 4368 O TYR B 226 85. ,364 63. .344 54. ,097 1.00 20. ,55 o
ATOM 4369 CB TYR B 226 86. ,262 62. .121 51. ,102 1.00 15. .96 c
ATOM 4370 CG TYR B 226 87. ,496 62. .006 51. ,962 1.00 18. ,14 c
ATOM 4371 CD1 TYR B 226 87. .686 60. .837 52. ,703 1.00 19. .66 c ATOM 4372 CD2 TYR B 226 88. .486 62. .969 52. ,041 1.00 19. .41 c
ATOM 4373 CE1 TYR B 226 88. .794 60. ,644 53. ,497 1.00 19. .27 c
ATOM 4374 CE2 TYR B 226 89. .600 62. .778 52. ,823 1.00 20. .75 c
ATOM 4375 CZ TYR B 226 89. .754 61. .611 53. .557 1.00 20. ,23 c
ATOM 4376 OH TYR B 226 90. .889 61. .455 54. .340 1.00 24. .36 o ATOM 4377 N SER B 227 85. .340 64. .760 52. .342 1.00 21. .66 N
ATOM 4378 CA SER B 227 85. .624 65. .894 53. .235 1.00 21. .29 c
ATOM 4379 C SER B 227 84. .835 67. .105 52. .729 1.00 23. .86 c
ATOM 4380 O SER B 227 85. .046 67. .459 51. .573 1.00 24. .44 o
ATOM 4381 CB SER B 227 87. .109 66. .229 53. .249 1.00 24. .88 c ATOM 4382 OG SER B 227 87. .427 67. .292 54. .137 1.00 28. .51 o
ATOM 4383 N THR B 228 84. .001 67. .611 53. .596 1.00 19. .81 N
ATOM 4384 CA THR B 228 83. .268 68. .825 53. .158 1.00 21. .93 c
ATOM 4385 C THR B 228 83. .020 69. .704 54. .372 1.00 19. .87 c
ATOM 4386 O THR B 228 82, .687 69. .251 55. .472 1.00 23. .64 o ATOM 4387 CB THR B 228 81. .950 68. .501 52. .450 1.00 22. .85 c
ATOM 4388 OG1 THR B 228 81. .263 69. .728 52. .152 1.00 25. .99 o
ATOM 4389 CG2 THR B 228 81. .049 67. .657 53. .327 1.00 25. .62 c
ATOM 4390 N SER B 229 83. .016 71. .024 54, .068 1.00 26. .47 N
ATOM 4391 CA SER B 229 82. .660 72. .003 55. .078 1.00 23. .55 C ATOM 4392 C SER B 229 81. .166 72. .317 54. .991 1.00 27. .25 C
ATOM 4393 O SER B 229 80. .593 73, .105 55. .752 1.00 27. .41 o
ATOM 4394 CB SER B 229 83. .451 73, .328 54. .991 1.00 19. .89 C
ATOM 4395 OG SER B 229 83. .457 73, .796 53. .656 1.00 30. .00 o
ATOM 4396 N ASN B 230 80. .424 71, .620 54. .124 1.00 21. .18 N ATOM 4397 CA ASN B 230 78. .979 71. .814 54. .004 1.00 24. .17 c
ATOM 4398 C ASN B 230 78. .234 70, .508 53. .842 1.00 22. .40 c
ATOM 4399 O ASN B 230 77, .512 70, .266 52. .879 1.00 24. .08 o
ATOM 4400 CB ASN B 230 78, .682 72, .769 52. .838 1.00 32. .64 c
ATOM 4401 CG ASN B 230 77, .230 73, .165 52, .652 1.00 38. .99 c ATOM 4402 ODl ASN B 230 76, .521 73 .432 53, .622 1.00 36, .44 o
ATOM 4403 ND2 ASN B 230 76, .748 73, .186 51, .407 1.00 38, .74 N
ATOM 4404 N PRO B 231 78, .252 69 .665 54, .873 1.00 20. .53 N
ATOM 4405 CA PRO B 231 77, .533 68 .396 54, .895 1.00 22, .58 C
ATOM 4406 C PRO B 231 76, .045 68 .653 54, .907 1.00 24, .40 C ATOM 4407 O PRO B 231 75, .617 69 .735 55, .320 1.00 24, .70 O
ATOM 4408 CB PRO B 231 77, .988 67, .687 56. .190 1.00 25, .34 C
ATOM 4409 CG PRO B 231 78 .412 68 .850 57, .050 1.00 26, .80 C
ATOM 4410 CD PRO B 231 78 .998 69 .904 56 .124 1.00 25, .68 c
ATOM 4411 N PRO B 232 75. .205 67 .751 54, .415 1.00 23, .71 N ATOM 4412 CA PRO B 232 73..774 67..879 54,.388 1.00 23..71 C
ATOM 4413 C PRO B 232 73. .179 68. .075 55. .765 1.00 24. .02 c
ATOM 4414 O PRO B 232 73. .680 67. .567 56. .765 1.00 23. .48 O
ATOM 4415 CB PRO B 232 73. .219 66. .522 53. .894 1.00 23. .88 c
ATOM 4416 CG PRO B 232 74. ,408 65. .936 53. .217 1.00 23. .07 c
ATOM 4417 CD PRO B 232 75. ,674 66. ,457 53. .871 1.00 30. .70 c
ATOM 4418 N PRO B 233 72. ,056 68. .760 55, .886 1.00 24. .16 N
ATOM 4419 CA PRO B 233 71. ,321 68. .972 57. .108 1.00 24. .88 c
ATOM 4420 C PRO B 233 70. ,961 67. ,707 57. .878 1.00 27. .28 c
ATOM 4421 O PRO B 233 70. .979 67. .711 59. .117 1.00 28. .43 o
ATOM 4422 CB PRO B 233 69. .984 69. .661 56. .725 1.00 30. .23 c
ATOM 4423 CG PRO B 233 70. .404 70. .326 55. .438 1.00 32. ,57 c
ATOM 4424 CD PRO B 233 71. .387 69. .395 54. .737 1.00 30. ,54 c
ATOM 4425 N TYR B 234 70. .697 66. .594 57. .179 1.00 23. ,72 N
ATOM 4426 CA TYR B 234 70. .395 65. ,334 57. .851 1.00 27. ,99 c
ATOM 4427 C TYR B 234 71. .568 64. ,812 58. .678 1.00 25. ,78 c
ATOM 4428 O TYR B 234 71. .374 63. ,870 59. .463 1.00 27. ,46 o
ATOM 4429 CB TYR B 234 69. .874 64. .270 56. .897 1.00 25. ,83 c
ATOM 4430 CG TYR B 234 70. .776 63. .812 55. .785 1.00 25. ,15 c
ATOM 4431 CD1 TYR B 234 72. .057 63. ,297 56. .036 1.00 22. .25 c
ATOM 4432 CD2 TYR B 234 70. .371 63. ,873 54. .468 1.00 23. .87 c
ATOM 4433 CE1 TYR B 234 72. .889 62. .901 55. .007 1.00 20. ,62 c
ATOM 4434 CE2 TYR B 234 71. .199 63. .467 53. .433 1.00 21. ,14 c
ATOM 4435 CZ TYR B 234 72. .452 62. .975 53. .711 1.00 20. ,43 c
ATOM 4436 OH TYR B 234 73. .262 62. .582 52. .670 1.00 23. ,64 o
ATOM 4437 N THR B 235 72. .775 65. .352 58. .557 1.00 21. .65 N
ATOM 4438 CA THR B 235 73. .920 64. .952 59. .351 1.00 21. .99 c
ATOM 4439 C THR B 235 74. .004 65. .716 60. .676 1.00 22. .96 c
ATOM 4440 O THR B 235 74. .986 65. .634 61. .416 1.00 22. .87 o
ATOM 4441 CB THR B 235 75. .263 65. .175 58. .626 1.00 21. .87 c
ATOM 4442 OG1 THR B 235 75. .544 66. .580 58. .504 1.00 20. .86 o
ATOM 4443 CG2 THR B 235 75. .228 64. .555 57. .228 1.00 19. .21 c
ATOM 4444 N SER B 236 73. .049 66. .606 60. .865 1.00 27. .15 N
ATOM 4445 CA SER B 236 72. .966 67. .439 62. .047 1.00 31. .54 c
ATOM 4446 C SER B 236 72. .893 66. .519 63. .264 1.00 29. .28 c
ATOM 4447 O SER B 236 72. .138 65. .550 63. .292 1.00 33. .89 o
ATOM 4448 CB SER B 236 71. .772 68. .383 61. .977 1.00 38. .83 c
ATOM 4449 OG SER B 236 71. .692 69. .151 63. .159 1.00 38. .58 o
ATOM 4450 N GLY B 237 73. .763 66. .820 64. .220 1.00 30. .14 N
ATOM 4451 CA GLY B 237 73. .809 66. .005 65, .433 1.00 32. .92 c
ATOM 4452 C GLY B 237 74. .818 64. .872 65. .317 1.00 34. .16 c
ATOM 4453 O GLY B 237 75, .027 64. .190 66. .327 1.00 34. .16 o
ATOM 4454 N SER B 238 75. .426 64. .651 64. .143 1.00 24. .81 N
ATOM 4455 CA SER B 238 76. .369 63. .523 64. .099 1.00 20. .48 c
ATOM 4456 C SER B 238 77. .777 64. .047 64. .173 1.00 20. .06 c
ATOM 4457 O SER B 238 78. .173 64. .990 63. .476 1.00 24. .23 o
ATOM 4458 CB SER B 238 76. .187 62. .748 62. .775 1.00 28. .36 c
ATOM 4459 OG SER B 238 77, .364 61. .974 62. .545 1.00 24. .23 o
ATOM 4460 N PRO B 239 78. .666 63. .363 64, .886 1.00 20. .04 N
ATOM 4461 CA PRO B 239 80, .078 63. .684 64, .921 1.00 23. .84 C
ATOM 4462 C PRO B 239 80, .830 63. .214 63, .691 1.00 23. .75 C
ATOM 4463 O PRO B 239 81, .982 63. .560 63, .409 1.00 23. .78 O
ATOM 4464 CB PRO B 239 80, .626 62. .959 66, .178 1.00 24. .80
ATOM 4465 CG PRO B 239 79, .732 61. .744 66, .157 1.00 17. .59 C
ATOM 4466 CD PRO B 239 78. .345 62. .201 65, .711 1.00 24. .29 c
ATOM 4467 N SER B 240 80. .168 62. .455 62. .816 1.00 20. .96 N
ATOM 4468 CA SER B 240 80. .710 61. .906 61. .586 1.00 23. .28 C
ATOM 4469 C SER B 240 79. .992 62, .332 60. .325 1.00 22. .01 C
ATOM 4470 O SER B 240 79. .560 61. .499 59. .498 1.00 17. .70 O ATOM 4471 CB SER B 240 80.544 60.356 61.687 1.00 19.75 c
ATOM 4472 OG SER B 240 81. 166 59. 827 62. 845 1.00 18. 91 o
ATOM 4473 N PRO B 241 79. 895 63. 621 60. 066 1.00 19. ,53 N
ATOM 4474 CA PRO B 241 79. 162 64. 146 58. 921 1.00 20. ,71 C ATOM 4475 C PRO B 241 79. 806 64. ,007 57. 558 1.00 20. 64 C
ATOM 4476 O PRO B 241 79. 147 64. ,301 56. 551 1.00 22. .07 O
ATOM 4477 CB PRO B 241 78. 831 65. ,606 59. ,294 1.00 19. .91 C
ATOM 4478 CG PRO B 241 80. ,113 65. ,964 60. ,019 1.00 19. ,53 c
ATOM 4479 CD PRO B 241 80. 376 64. 736 60. 887 1.00 19. ,55 c ATOM 4480 N ASP B 242 81. 048 63. ,584 57. 490 1.00 18. ,48 N
ATOM 4481 CA ASP B 242 81. 722 63. ,229 56. ,263 1.00 17. ,92 c
ATOM 4482 C ASP B 242 82. ,564 61. ,990 56. ,594 1.00 18. ,21 c
ATOM 4483 O ASP B 242 82. ,681 61. .686 57. ,792 1.00 17. .57 o
ATOM 4484 CB ASP B 242 82. ,558 64. .303 55. ,593 1.00 20. ,52 c ATOM 4485 CG ASP B 242 83. ,556 65. .012 56. ,472 1.00 27. ,92 c
ATOM 4486 ODl ASP B 242 84. ,037 64. ,411 57. ,455 1.00 20. ,00 o
ATOM 4487 OD2 ASP B 242 83. .877 66. ,193 56. ,178 1.00 22. ,02 o
ATOM 4488 N GLU B 243 83. ,020 61. ,312 55. .564 1.00 18. ,13 N
ATOM 4489 CA GLU B 243 83. ,793 60. ,089 55. ,816 1.00 13. .20 c ATOM 4490 C GLU B 243 85. ,141 60. .306 56. .431 1.00 21. ,87 c
ATOM 4491 O GLU B 243 85. ,600 59. .439 57. ,192 1.00 18. ,81 o
ATOM 4492 CB GLU B 243 83. ,824 59. .242 54. .533 1.00 17. ,00 c
ATOM 4493 CG GLU B 243 82. ,417 58. ,789 54. ,159 1.00 16. .21 c
ATOM 4494 CD GLU B 243 81. ,840 57. ,737 55. ,108 1.00 19. .62 c ATOM 4495 OE1 GLU B 243 82. ,484 56. .677 55. ,223 1.00 18. .36 o
ATOM 4496 OE2 GLU B 243 80. .797 57. .993 55. ,701 1.00 15. .08 o
ATOM 4497 N SER B 244 85, .841 61. .433 56. ,247 1.00 16. .18 N
ATOM 4498 CA SER B 244 87, ,140 61. .627 56. .880 1.00 20. .14 c
ATOM 4499 C SER B 244 86, .919 61. .676 58, .392 1.00 21. .14 c ATOM 4500 O SER B 244 87. .711 61. .092 59. .135 1.00 18. .74 o
ATOM 4501 CB SER B 244 87. .780 62. .927 56. .410 1.00 21. .94 c
ATOM 4502 OG SER B 244 88. .857 63. .321 57. .246 1.00 22. .91 o
ATOM 4503 N ARG B 245 85. .857 62. .334 58. .815 1.00 21. .95 N
ATOM 4504 CA ARG B 245 85. .576 62, .480 60. .229 1.00 24. .46 c ATOM 4505 C ARG B 245 85. .093 61. .160 60. .826 1.00 25. .03 c
ATOM 4506 O ARG B 245 85. .457 60. .863 61. .970 1.00 22, .74 o
ATOM 4507 CB ARG B 245 84. .607 63. .628 60. .522 1.00 22, .43 c
ATOM 4508 CG ARG B 245 85. .326 65. .003 60. .416 1.00 20, .04 c
ATOM 4509 CD ARG B 245 84. .286 66. .080 60. .770 1.00 23, .38 c ATOM 4510 NE ARG B 245 83. .742 66. .531 59. .487 1.00 25, .92 N
ATOM 4511 CZ ARG B 245 83. .046 67. .651 59, .310 1.00 31, .16 C
ATOM 4512 NHl ARG B 245 82, .755 68. .449 60, .324 1.00 27, .40 N
ATOM 4513 NH2 ARG B 245 82, .611 67, .940 58, .082 1.00 20, .28 N
ATOM 4514 N TYR B 246 84, .326 60, .401 60, .034 1.00 21, .70 N ATOM 4515 CA TYR B 246 83, .846 59, .101 60, .505 1.00 21, .93 C
ATOM 4516 C TYR B 246 85, .045 58, .214 60, .834 1.00 22 .04 C
ATOM 4517 O TYR B 246 85 .134 57 .627 61, .913 1.00 17 .94 O
ATOM 4518 CB TYR B 246 82 .952 58 .421 59, .464 1.00 20 .67 C
ATOM 4519 CG TYR B 246 82 .500 57 .013 59, .837 1.00 17 .47 C ATOM 4520 CD1 TYR B 246 82 .012 56, .711 61, .087 1.00 16, .32 C
ATOM 4521 CD2 TYR B 246 82 .590 56 .036 58, .862 1.00 13 .90 C
ATOM 4522 CE1 TYR B 246 81 .592 55 .408 61, .386 1.00 16 .81 C
ATOM 4523 CE2 TYR B 246 82 .191 54 .734 59 .143 1.00 16 .56 C
ATOM 4524 CZ TYR B 246 81 .735 54 .446 60 .413 1.00 20 .55 C ATOM 4525 OH TYR B 246 81 .362 53 .141 60 .701 1.00 15 .95 O
ATOM 4526 N ALA B 247 85 .995 58 .146 59 .929 1.00 18 .03 N
ATOM 4527 CA ALA B 247 87 .244 57 .423 60 .003 1.00 20 .86 C
ATOM 4528 C ALA B 247 87 .991 57 .842 61 .276 1.00 20 .26 C
ATOM 4529 O ALA B 247 88 .391 57 .011 62 .071 1.00 21 .88 O ATOM 4530 CB ALA B 247 88.,147 57.,635 58.,805 1.00 19..65 c
ATOM 4531 N THR B 248 88. 113 59. .154 61. .499 1.00 21. ,15 N
ATOM 4532 CA THR B 248 88. ,812 59. ,566 62. ,735 1.00 21. ,86 C
ATOM 4533 C THR B 248 88. ,071 59. ,138 63. ,978 1.00 18. ,72 c
ATOM 4534 O THR B 248 88. 707 58. ,749 64. .973 1.00 22. .28 o
ATOM 4535 CB THR B 248 88. ,987 61. ,098 62. .679 1.00 16. .96 c
ATOM 4536 OG1 THR B 248 89. ,909 61. ,383 61. .646 1.00 20. .38 o
ATOM 4537 CG2 THR B 248 89. ,525 61. ,609 64. ,019 1.00 21. .61 c
ATOM 4538 N ASN B 249 86. .757 59. ,205 64. ,008 1.00 16. .99 N
ATOM 4539 CA ASN B 249 85. ,951 58. ,832 65. .160 1.00 18. .48 C
ATOM 4540 C ASN B 249 86. ,076 57. ,327 65. ,390 1.00 22. .24 C
ATOM 4541 O ASN B 249 86. ,310 56. ,931 66. .529 1.00 18. .80 o
ATOM 4542 CB ASN B 249 84. ,503 59. ,259 64. .948 1.00 24. .07 c
ATOM 4543 CG ASN B 249 84. ,429 60. .787 64. ,892 1.00 23. .08 c
ATOM 4544 ODl ASN B 249 85. ,320 61. .484 65. .353 1.00 23. .66 o
ATOM 4545 ND2 ASN B 249 83. ,297 61. ,244 64. .379 1.00 19. .45 N
ATOM 4546 N ILE B 250 85. ,997 56. ,509 64. ,341 1.00 20. ,93 N
ATOM 4547 CA ILE B 250 86. ,164 55. ,064 64. .633 1.00 17. .50 C
ATOM 4548 C ILE B 250 87. ,566 54. ,751 65. .123 1.00 18. .42 C
ATOM 4549 O ILE B 250 87. ,767 53. .941 66. .061 1.00 23. .75 O
ATOM 4550 CB ILE B 250 85. ,780 54. .209 63. .421 1.00 15. .48 C
ATOM 4551 CGI ILE B 250 84. ,274 54. .216 63. .241 1.00 17. .22 c
ATOM 4552 CG2 ILE B 250 86. .322 52. .783 63. .614 1.00 13. .80 c
ATOM 4553 CD1 ILE B 250 83. ,405 53. .287 64. .039 1.00 18. .66 c
ATOM 4554 N ALA B 251 88. ,598 55. .345 64. .535 1.00 17. .26 N
ATOM 4555 CA ALA B 251 89. .988 55. .092 64. .920 1.00 18. .33 c
ATOM 4556 C ALA B 251 90. ,157 55. .460 66. .394 1.00 19. .88 c
ATOM 4557 O ALA B 251 90. ,787 54. .730 67. .157 1.00 18. .65 o
ATOM 4558 CB ALA B 251 90. .939 55. .868 64. .042 1.00 17. .72 c
ATOM 4559 N ASN B 252 89. ,572 56. .591 66. .785 1.00 18. .07 N
ATOM 4560 CA ASN B 252 89. .623 56. .975 68. .203 1.00 17. .37 c
ATOM 4561 C ASN B 252 89. .035 55. .876 69. .094 1.00 23. .95 c
ATOM 4562 O ASN B 252 89. .667 55. .562 70. .105 1.00 21. .93 o
ATOM 4563 CB ASN B 252 88. .926 58. .310 68. .433 1.00 21. .38 c
ATOM 4564 CG ASN B 252 89. .731 59. .490 67. .902 1.00 24. .79 c
ATOM 4565 ODl ASN B 252 90. .894 59. .386 67. .516 1.00 23. ,42 o
ATOM 4566 ND2 ASN B 252 89. .081 60. .663 67. .888 1.00 23. .22 N
ATOM 4567 N ALA B 253 87. .873 55. .317 68. .780 1.00 18. .25 N
ATOM 4568 CA ALA B 253 87. .318 54. .232 69. .622 1.00 20. .03 c
ATOM 4569 C ALA B 253 88. .192 52. .998 69. .551 1.00 22. .96 c
ATOM 4570 O ALA B 253 88. .501 52. .365 70. .570 1.00 22. .86 o
ATOM 4571 CB ALA B 253 85. .934 53. .901 69. .054 1.00 20. .69 c
ATOM 4572 N MET B 254 88. .698 52, .639 68. .358 1.00 15. .53 N
ATOM 4573 CA MET B 254 89. .563 51. .497 68. .183 1.00 18. .63 C
ATOM 4574 C MET B 254 90. .884 51. .601 68, .934 1.00 25. .70 c
ATOM 4575 O MET B 254 91. .377 50, .658 69, .568 1.00 18. .30 o
ATOM 4576 CB MET B 254 89. .891 51, .236 66, .688 1.00 17. .39 c
ATOM 4577 CG MET B 254 88, .669 51. .001 65, .833 1.00 18, .39 c
ATOM 4578 SD MET B 254 87, .924 49. .373 66, .273 1.00 17, .66 s
ATOM 4579 CE MET B 254 86, .459 49. .553 65, .268 1.00 20, .05 c
ATOM 4580 N ARG B 255 91, .460 52, .806 68 .953 1.00 17, .46 N
ATOM 4581 CA ARG B 255 92, .758 52, .993 69, .624 1.00 17, .68 c
ATOM 4582 C ARG B 255 92, .716 52, .734 71, .115 1.00 16, .19 c
ATOM 4583 O ARG B 255 93, .642 52, .099 71 .652 1.00 20, .59 o
ATOM 4584 CB ARG B 255 93, .236 54, .416 69, .294 1.00 20, .26 c
ATOM 4585 CG ARG B 255 94, .571 54, .756 69 .920 1.00 22, .42 c
ATOM 4586 CD ARG B 255 95 .046 56 .177 69 .563 1.00 18 .77 c
ATOM 4587 NE ARG B 255 94, .961 56, .385 68 .122 1.00 22 .61 N
ATOM 4588 CZ ARG B 255 94 .034 57 .163 67 .563 1.00 19 .19 C ATOM 4589 NHl ARG B 255 93.,114 57.,776 68..290 1.00 24..62 N
ATOM 4590 NH2 ARG B 255 94. .000 57. ,265 66. .235 1.00 22. .17 N
ATOM 4591 N GLN B 256 91. ,609 53. ,085 71. ,747 1.00 19. .29 N
ATOM 4592 CA GLN B 256 91. ,386 52. .922 73. .171 1.00 20. .77 C
ATOM 4593 C GLN B 256 91. ,249 51. ,452 73. .561 1.00 27. ,72 C
ATOM 4594 O GLN B 256 91. ,450 51. ,090 74. .721 1.00 28. ,03 O
ATOM 4595 CB GLN B 256 90. ,108 53. .645 73. .572 1.00 23. .65 C
ATOM 4596 CG GLN B 256 90. ,199 55. ,157 73. .583 1.00 25. .96 C
ATOM 4597 CD GLN B 256 88. .817 55. .719 73. .918 1.00 29. .96 C
ATOM 4598 OE1 GLN B 256 88. .445 55. .660 75. .100 1.00 28. .44 O
ATOM 4599 NE2 GLN B 256 88. .148 56. ,199 72. .894 1.00 33. .23 N
ATOM 4600 N ARG B 257 90. .881 50. ,620 72. .582 1.00 22. .52 N
ATOM 4601 CA ARG B 257 90. .759 49. .192 72. .787 1.00 18. .53 C
ATOM 4602 C ARG B 257 91. ,938 48. ,414 72. .222 1.00 25. .19 C
ATOM 4603 O ARG B 257 91. ,978 47. .169 72. .260 1.00 25. .60 o
ATOM 4604 CB ARG B 257 89. .434 48. .704 72. .155 1.00 15. .54 c
ATOM 4605 CG ARG B 257 88. ,158 49. ,344 72. .603 1.00 21. .95 c
ATOM 4606 CD ARG B 257 86. .940 48. .932 71. .771 1.00 21. .22 c
ATOM 4607 NE ARG B 257 85. .701 49. .434 72. .374 1.00 21. .40 N
ATOM 4608 CZ ARG B 257 84. ,770 48. ,681 72. .962 1.00 17. ,04 c
ATOM 4609 NHl ARG B 257 84. ,937 47. .355 73. .034 1.00 18. .04 N
ATOM 4610 NH2 ARG B 257 83. .688 49. .216 73. .464 1.00 20. .59 N
ATOM 4611 N GLY B 258 92. .970 49. .052 71. .671 1.00 18. .10 N
ATOM 4612 CA GLY B 258 94. .132 48. .442 71. .124 1.00 18. .57 C
ATOM 4613 C GLY B 258 93. .982 47. .778 69. .767 1.00 25. .57 C
ATOM 4614 O GLY B 258 94. .725 46. .876 69. .383 1.00 23. .23 o
ATOM 4615 N LEU B 259 92. .983 48. .247 69. .022 1.00 21. .02 N
ATOM 4616 CA LEU B 259 92. .663 47. .659 67. .714 1.00 20. .21 c
ATOM 4617 C LEU B 259 93. .165 48. .547 66. .601 1.00 23. .47 c
ATOM 4618 O LEU B 259 93. .520 49. .710 66. .835 1.00 22. .18 o
ATOM 4619 CB LEU B 259 91. .131 47. .552 67. .707 1.00 17. .78 c
ATOM 4620 CG LEU B 259 90. .521 46. .633 68. .776 1.00 24. .62 c
ATOM 4621 CD1 LEU B 259 89. .009 46. .719 68. .792 1.00 23. .42 c
ATOM 4622 CD2 LEU B 259 90. .994 45. .203 68. .523 1.00 29. .45 c
ATOM 4623 N PRO B 260 93. .130 48. .065 65. .382 1.00 20. .15 N
ATOM 4624 CA PRO B 260 93. .529 48. .786 64. .187 1.00 20. .61 c
ATOM 4625 C PRO B 260 92. .744 50. .082 64. .006 1.00 18. .29 c
ATOM 4626 O PRO B 260 91. .636 50. .251 64. .507 1.00 20. .65 o
ATOM 4627 CB PRO B 260 93. .341 47. .801 63. .018 1.00 20. .96 c
ATOM 4628 CG PRO B 260 93. .530 46. .497 63. .777 1.00 20. .35 c
ATOM 4629 CD PRO B 260 92. .747 46. .669 65, .064 1.00 18. .86 c
ATOM 4630 N THR B 261 93. .364 51. .040 63. .322 1.00 20. .56 N
ATOM 4631 CA THR B 261 92. .777 52. .370 63. .164 1.00 22. .31 C
ATOM 4632 C THR B 261 92. .637 52. .857 61. .724 1.00 29. .16 c
ATOM 4633 O THR B 261 92. .116 53. .964 61. .491 1.00 26. .56 o
ATOM 4634 CB THR B 261 93. .773 53. .376 63. .826 1.00 22. .09 c
ATOM 4635 OG1 THR B 261 95. .056 53. .131 63. .247 1.00 22. .50 o
ATOM 4636 CG2 THR B 261 93. .768 53. .250 65. .336 1.00 21. .07 c
ATOM 4637 N GLN B 262 93. .150 52. .131 60. .751 1.00 17. .49 N
ATOM 4638 CA GLN B 262 93. .230 52. .631 59. .381 1.00 22. .49 c
ATOM 4639 C GLN B 262 92. .056 52. .337 58. .467 1.00 26. .06 c
ATOM 4640 O GLN B 262 91. .470 51. .253 58. .480 1.00 23. .98 o
ATOM 4641 CB GLN B 262 94. .514 52. .097 58. .745 1.00 17. .85 c
ATOM 4642 CG GLN B 262 95. .809 52. .399 59. .496 1.00 23. .30 c
ATOM 4643 CD GLN B 262 95. .927 53. .919 59. .725 1.00 18. .41 c
ATOM 4644 OE1 GLN B 262 95. .747 54. .378 60. .837 1.00 21. .83 o
ATOM 4645 NE2 GLN B 262 96. .207 54. .610 58. .633 1.00 24. .59 N
ATOM 4646 N PHE B 263 91. .705 53. .324 57. .616 1.00 19, .57 N
ATOM 4647 CA PHE B 263 90. .609 53. .162 56. .688 1.00 20, .56 C ATOM 4648 C PHE B 263 91.,016 53..271 55..222 1.00 19..01 c
ATOM 4649 O PHE B 263 91. ,971 53. ,925 54. .796 1.00 17. .87 o
ATOM 4650 CB PHE B 263 89. ,606 54. .332 56. .900 1.00 13. .96 c
ATOM 4651 CG PHE B 263 88. ,624 54. ,096 57. .976 1.00 13. .70 c
ATOM 4652 CD1 PHE B 263 89. ,001 54. ,066 59. .317 1.00 18. .13 c
ATOM 4653 CD2 PHE B 263 87. ,278 53. .888 57. .681 1.00 16. ,32 c
ATOM 4654 CE1 PHE B 263 88. ,063 53. ,857 60. .308 1.00 15. .53 c
ATOM 4655 CE2 PHE B 263 86. ,339 53. ,631 58. .665 1.00 22. .27 c
ATOM 4656 CZ PHE B 263 86. ,738 53. .620 60. .009 1.00 17. .15 c
ATOM 4657 N ILE B 264 90. ,154 52. .689 54. .389 1.00 16. .44 N
ATOM 4658 CA ILE B 264 90. ,078 52. .972 52. .963 1.00 14. .67 c
ATOM 4659 C ILE B 264 88. ,632 53. .444 52. .759 1.00 18. .83 c
ATOM 4660 O ILE B 264 87. ,694 52. .963 53. .392 1.00 15. .16 o
ATOM 4661 CB ILE B 264 90. ,502 51. .924 51. .960 1.00 17. .36 c
ATOM 4662 CGI ILE B 264 89. ,801 50. .578 52, .219 1.00 12. .42 c
ATOM 4663 CG2 ILE B 264 92. ,023 51. .758 51. .922 1.00 16. .92 c
ATOM 4664 CD1 ILE B 264 90. ,167 49. .471 51. .282 1.00 21. .20 c
ATOM 4665 N ILE B 265 88. ,431 54. .530 52. .024 1.00 13. .66 N
ATOM 4666 CA ILE B 265 87. ,103 55. .132 51. .874 1.00 14. .44 C
ATOM 4667 C ILE B 265 86. .702 55. .132 50. .415 1.00 16. .12 C
ATOM 4668 O ILE B 265 87. .430 55. .579 49. .531 1.00 14. .22 o
ATOM 4669 CB ILE B 265 87. ,030 56. .546 52. .499 1.00 16. .36 c
ATOM 4670 CGI ILE B 265 87. .156 56. .412 54. .028 1.00 17. .93 c
ATOM 4671 CG2 ILE B 265 85. .671 57. .178 52. .177 1.00 11. .34 c
ATOM 4672 CD1 ILE B 265 87. .527 57. .706 54. .719 1.00 32. .91 c
ATOM 4673 N ASP B 266 85. .496 54. .580 50. .125 1.00 14. .62 N
ATOM 4674 CA ASP B 266 85. .067 54. .528 48. .738 1.00 12. .31 c
ATOM 4675 C ASP B 266 84. .567 55. .926 48. .329 1.00 15. .66 c
ATOM 4676 O ASP B 266 83. .870 56. .550 49. .118 1.00 14. .39 o
ATOM 4677 CB ASP B 266 83. .853 53. .587 48. .624 1.00 13. .98 c
ATOM 4678 CG ASP B 266 83. .447 53. .191 47. .228 1.00 12. .35 c
ATOM 4679 ODl ASP B 266 84. .072 53. .622 46. .233 1.00 12. .31 o
ATOM 4680 OD2 ASP B 266 82. .482 52. .385 47, .141 1.00 12. .07 o
ATOM 4681 N GLN B 267 84. .963 56. .354 47. .130 1.00 13. .29 N
ATOM 4682 CA GLN B 267 84. .397 57. .580 46. .562 1.00 12. .36 C
ATOM 4683 C GLN B 267 83. .959 57. .320 45. .136 1.00 16. .31 C
ATOM 4684 O GLN B 267 83. .874 58. .239 44. .299 1.00 13. .76 o
ATOM 4685 CB GLN B 267 85. .318 58. .792 46. .591 1.00 11. .72 c
ATOM 4686 CG GLN B 267 85. .624 59. .350 47. .970 1.00 16. .66 c
ATOM 4687 CD GLN B 267 84. .495 60. .168 48. .541 1.00 17. .67 c
ATOM 4688 OE1 GLN B 267 84. .362 61. .389 48. .308 1.00 18. .52 o
ATOM 4689 NE2 GLN B 267 83. .667 59. .527 49, .367 1.00 16. .26 N
ATOM 4690 N SER B 268 83, .606 56. .064 44, .794 1.00 12. .12 N
ATOM 4691 CA SER B 268 83, .135 55. .714 43, .472 1.00 13. .53 C
ATOM 4692 C SER B 268 81. .933 56. .564 43. .051 1.00 13. .38 C
ATOM 4693 O SER B 268 81. .773 56. .916 41. .897 1.00 12. .66 o
ATOM 4694 CB SER B 268 82. .677 54. .246 43. .416 1.00 12. .82 C
ATOM 4695 OG SER B 268 81. .788 54. .024 44. .520 1.00 13. .85 o
ATOM 4696 N ARG B 269 81, .035 56. .843 43. .976 1.00 14. .34 N
ATOM 4697 CA ARG B 269 79. .865 57. .678 43. .732 1.00 12. .27 C
ATOM 4698 C ARG B 269 79. .701 58. .680 44. .863 1.00 13. .37 C
ATOM 4699 O ARG B 269 79. .838 58. .316 46. .041 1.00 15, .59 o
ATOM 4700 CB ARG B 269 78, .577 56. .826 43. .677 1.00 12. .81 c
ATOM 4701 CG ARG B 269 78. .638 55. .757 42. .577 1.00 13. .14 c
ATOM 4702 CD ARG B 269 77. .348 54. .948 42. .459 1.00 14. .78 c
ATOM 4703 NE ARG B 269 77, .138 54. .162 43, .692 1.00 13. .58 N
ATOM 4704 CZ ARG B 269 76, .098 53, .362 43, .885 1.00 15. .13 c
ATOM 4705 NHl ARG B 269 75, .239 53, .220 42, .872 1.00 13. .64 N
ATOM 4706 NH2 ARG B 269 75, .941 52, .716 45, .055 1.00 14. .12 N ATOM 4707 N VAL B 270 79.450 59.,965 44.,572 1.00 11.,08 N
ATOM 4708 CA VAL B 270 79. ,220 60. ,960 45. ,622 1.00 15. ,78 C
ATOM 4709 C VAL B 270 77. 922 61. .683 45. ,289 1.00 14. ,22 C
ATOM 4710 O VAL B 270 77. ,683 62. ,069 44. ,123 1.00 14. .63 o
ATOM 4711 CB VAL B 270 80. ,396 61. .948 45. .739 1.00 15. ,78 c
ATOM 4712 CGI VAL B 270 80. ,112 63. .059 46. ,732 1.00 17. ,62 c
ATOM 4713 CG2 VAL B 270 81. ,698 61. ,216 46. ,150 1.00 16. ,79 c
ATOM 4714 N ALA B 271 76. ,995 61. .815 46. .225 1.00 13. .05 N
ATOM 4715 CA ALA B 271 75. ,731 62. ,478 45. .926 1.00 12. ,38 c
ATOM 4716 C ALA B 271 75. ,874 63. ,987 45. .850 1.00 17. ,18 c
ATOM 4717 O ALA B 271 76. ,680 64. ,586 46. .587 1.00 20. ,63 o
ATOM 4718 CB ALA B 271 74. ,769 62. ,156 47. .096 1.00 13. ,94 c
ATOM 4719 N LEU B 272 75. ,065 64. ,598 44. .958 1.00 16. .98 N
ATOM 4720 CA LEU B 272 75. ,024 66. ,072 44. ,969 1.00 24. ,18 C
ATOM 4721 C LEU B 272 74. ,209 66. .579 46. .151 1.00 23. ,47 C
ATOM 4722 O LEU B 272 73. ,377 65. .881 46. ,759 1.00 24. ,74 o
ATOM 4723 CB LEU B 272 74. ,379 66. ,603 43. .680 1.00 21. ,83 C
ATOM 4724 CG LEU B 272 74. ,884 66. ,139 42. .328 1.00 31. ,92 c
ATOM 4725 CD1 LEU B 272 74. .547 67. ,178 41. ,245 1.00 24. ,20 c
ATOM 4726 CD2 LEU B 272 76. .376 65. ,868 42. .313 1.00 30. ,13 c
ATOM 4727 N SER B 273 74. .464 67. ,830 46. .586 1.00 29. ,62 N
ATOM 4728 CA SER B 273 73. .681 68. .382 47. .696 1.00 32. ,76 C
ATOM 4729 C SER B 273 72. .195 68. .333 47. .341 1.00 27. ,46 C
ATOM 4730 O SER B 273 71. .805 68. .780 46. ,260 1.00 27. .26 O
ATOM 4731 CB SER B 273 74. .033 69. .813 48. .083 1.00 36. .21 C
ATOM 4732 OG SER B 273 75. .439 69. .961 48. .150 1.00 40. .72 o
ATOM 4733 N GLY B 274 71. .409 67. .858 48. .288 1.00 26. .91 N
ATOM 4734 CA GLY B 274 69. .990 67. .671 48. .146 1.00 25. .28 C
ATOM 4735 C GLY B 274 69. .530 66. .376 47. .545 1.00 25. .72 c
ATOM 4736 O GLY B 274 68. .312 66. .199 47. .480 1.00 31. .28 o
ATOM 4737 N ALA B 275 70. .374 65, .443 47. .085 1.00 19. .25 N
ATOM 4738 CA ALA B 275 69. .891 64. .234 46. .418 1.00 20. .46 c
ATOM 4739 C ALA B 275 69. .075 63. .304 47. .297 1.00 22. .81 c
ATOM 4740 O ALA B 275 68. .142 62. .608 46. .889 1.00 23. .98 o
ATOM 4741 CB ALA B 275 71. .080 63. .488 45. .811 1.00 22. .82 c
ATOM 4742 N ARG B 276 69. .503 63. .229 48. .572 1.00 24. .55 N
ATOM 4743 CA ARG B 276 68. .787 62. .401 49. .533 1.00 21. .37 c
ATOM 4744 C ARG B 276 68. .081 63. .258 50. .581 1.00 16. .59 c
ATOM 4745 O ARG B 276 68. .673 64. .155 51. .190 1.00 21. .69 o
ATOM 4746 CB ARG B 276 69. .768 61. .504 50. .338 1.00 17. .11 c
ATOM 4747 CG ARG B 276 70. .402 60. .465 49. .439 1.00 17. .37 c
ATOM 4748 CD ARG B 276 71. .283 59. .517 50. .245 1.00 18. .12 c
ATOM 4749 NE ARG B 276 72. .595 60. .136 50. .504 1.00 22. .72 N
ATOM 4750 CZ ARG B 276 73. .613 59. .419 51. .016 1.00 22. .19 C
ATOM 4751 NHl ARG B 276 73. .350 58. .151 51. .305 1.00 20. .30 N
ATOM 4752 NH2 ARG B 276 74. .781 59. .988 51. .209 1.00 20. .97 N
ATOM 4753 N SER B 277 66, .841 62, .835 50. .883 1.00 18, .66 N
ATOM 4754 CA SER B 277 66. .154 63, .554 51. .962 1.00 22, .06 C
ATOM 4755 C SER B 277 66. .502 62, .870 53. .289 1.00 28, .16 C
ATOM 4756 O SER B 277 66, .397 63, .504 54. .335 1.00 31, .85 O
ATOM 4757 CB SER B 277 64, .643 63, .547 51. .741 1.00 34, .95 c
ATOM 4758 OG SER B 277 64, .206 62, .271 51. .329 1.00 36, .51 O
ATOM 4759 N GLU B 278 66, .827 61, .575 53, .217 1.00 21, .65 ' M
ATOM 4760 CA GLU B 278 67, .207 60. .828 54. .415 1.00 25, .67 c
ATOM 4761 C GLU B 278 68, .593 60, .195 54, .195 1.00 20, .70 c
ATOM 4762 O GLU B 278 68 .900 59, .690 53, .109 1.00 20, .38 O
ATOM 4763 CB GLU B 278 66 .175 59, .758 54, .763 1.00 24, .88 c
ATOM 4764 CG GLU B 278 64 .889 60, .288 55, .393 1.00 39, .32 c
ATOM 4765 CD GLU B 278 63 .837 59, .185 55, .355 1.00 49, .61 c ATOM 4766 OE1 GLU B 278 63.547 58.,733 54.,226 1.00 52.,41 O
ATOM 4767 OE2 GLU B 278 63.335 58. ,777 56. ,419 1.00 60. ,57 O
ATOM 4768 N TRP B 279 69.376 60. ,134 55. ,266 1.00 18. ,34 N
ATOM 4769 CA TRP B 279 70.739 59. ,628 55. .170 1.00 17. .14 C
ATOM 4770 C TRP B 279 70.786 58. ,146 54. .779 1.00 18. ,27 C
ATOM 4771 O TRP B 279 71.724 57. ,717 54. ,116 1.00 21. ,89 O
ATOM 4772 CB TRP B 279 71.519 59. ,831 56. ,465 1.00 20. ,35 C
ATOM 4773 CG TRP B 279 73.009 59. ,958 56. ,306 1.00 22. ,96 C
ATOM 4774 CD1 TRP B 279 73.797 59. ,680 55. ,225 1.00 17. ,88 c
ATOM 4775 CD2 TRP B 279 73.894 60. ,447 57. ,314 1.00 17. ,12 c
ATOM 4776 NE1 TRP B 279 75.100 59. ,932 55. .515 1.00 17. ,15 N
ATOM 4777 CE2 TRP B 279 75.208 60. ,429 56. ,797 1.00 19. ,55 C
ATOM 4778 CE3 TRP B 279 73.713 60. ,838 58. ,654 1.00 15. ,78 C
ATOM 4779 CZ2 TRP B 279 76.330 60. ,794 57. ,534 1.00 16. .75 C
ATOM 4780 CZ3 TRP B 279 74.810 61. .250 59. ,361 1.00 20. .70 c
ATOM 4781 CH2 TRP B 279 76.099 61. .231 58. .827 1.00 14. .86 c
ATOM 4782 N GLY B 280 69.777 57. .387 55. .211 1.00 21. .03 N
ATOM 4783 CA GLY B 280 69.756 55. .964 54. .906 1.00 20. .84 c
ATOM 4784 C GLY B 280 69.462 55. .576 53. .469 1.00 25. .19 c
ATOM 4785 O GLY B 280 69.573 54. .374 53. .175 1.00 21. .44 o
ATOM 4786 N GLN B 281 69.059 56. .510 52. .617 1.00 22. .17 N
ATOM 4787 CA GLN B 281 68.731 56. ,154 51. ,229 1.00 18. .91 c
ATOM 4788 C GLN B 281 70.001 55. ,609 50. ,570 1.00 19. .28 c
ATOM 4789 O GLN B 281 71.078 56. ,147 50. ,744 1.00 17. .79 o
ATOM 4790 CB GLN B 281 68.184 57. ,375 50. .504 1.00 23. .41 c
ATOM 4791 CG GLN B 281 66.691 57. ,638 50. .745 1.00 29. .18 c
ATOM 4792 CD GLN B 281 66.288 58. .876 49. .952 1.00 43. .17 c
ATOM 4793 OE1 GLN B 281 66.607 58. .938 48. .756 1.00 46. .46 o
ATOM 4794 NE2 GLN B 281 65.625 59. .831 50. .578 1.00 48. .62 N
ATOM 4795 N TRP B 282 69.846 54. .485 49. .872 1.00 17. .84 N
ATOM 4796 CA TRP B 282 71.024 53. .830 49. .288 1.00 15. .47 c
ATOM 4797 C TRP B 282 70.895 53. .356 47. .865 1.00 13. .97 c
ATOM 4798 O TRP B 282 71.961 53. .156 47. .234 1.00 14. .89 o
ATOM 4799 CB TRP B 282 71.378 52. .597 50. .171 1.00 15. .87 c
ATOM 4800 CG TRP B 282 70.260 51, .623 50. .330 1.00 17. .68 c
ATOM 4801 CD1 TRP B 282 69.266 51. .681 51, .270 1.00 19. .19 c
ATOM 4802 CD2 TRP B 282 69.985 50. .470 49. .520 1.00 16. .68 c
ATOM 4803 NE1 TRP B 282 68.410 50. .595 51. .107 1.00 21. .00 N
ATOM 4804 CE2 TRP B 282 68.828 49. .858 50. .032 1.00 23. .86 C
ATOM 4805 CE3 TRP B 282 70.612 49. .905 48. .404 1.00 16. .62 c
ATOM 4806 CZ2 TRP B 282 68.266 48. .700 49. .482 1.00 18. .80 c
ATOM 4807 CZ3 TRP B 282 70.060 48. .758 47. .860 1.00 19. .39 c
ATOM 4808 CH2 TRP B 282 68.921 48. .166 48. .400 1.00 20. .13 c
ATOM 4809 N CYS B 283 69.692 53. .076 47. .347 1.00 12. .68 N
ATOM 4810 CA CYS B 283 69.582 52, .471 46. .026 1.00 14. .66 C
ATOM 4811 C CYS B 283 69.553 53, .452 44. .864 1.00 12. .13 C
ATOM 4812 O CYS B 283 68.673 54, .255 44. .725 1.00 13. .82 O
ATOM 4813 CB CYS B 283 68.244 51, .668 46. .012 1.00 17. .06 C
ATOM 4814 SG CYS B 283 68.140 50, .674 44. .507 1.00 14. .06 s
ATOM 4815 N ASN B 284 70.620 53, .380 44. .070 1.00 13. .37 N
ATOM 4816 CA ASN B 284 70.767 54, .190 42. .855 1.00 14. .56 C
ATOM 4817 C ASN B 284 70.366 55, .640 43. .073 1.00 14. .31 c
ATOM 4818 O ASN B 284 69.482 56, .192 42. .403 1.00 15, .21 \ 0
ATOM 4819 CB ASN B 284 69.940 53. .566 41. .726 1.00 12. .20 c
ATOM 4820 CG ASN B 284 70.316 52. .135 41. .425 1.00 16. .26 c
ATOM 4821 ODl ASN B 284 71.465 51. .700 41, .358 1.00 15, .41 O
ATOM 4822 ND2 ASN B 284 69.314 51, .298 41, .223 1.00 18, .26 N
ATOM 4823 N VAL B 285 71.078 56. .226 44, .027 1.00 13, .81 N
ATOM 4824 CA VAL B 285 70.833 57. .605 44. .418 1.00 14, .84 c ATOM 4825 C VAL B 285 71.176 58.,547 43.,281 1.00 17..91 C
ATOM 4826 O VAL B 285 72. ,205 58, ,439 42. ,610 1.00 16. .75 o
ATOM 4827 CB VAL B 285 71. ,569 58. ,000 45. ,709 1.00 11. ,45 c
ATOM 4828 CGI VAL B 285 71. ,336 59. ,495 45. ,973 1.00 13. ,91 c
ATOM 4829 CG2 VAL B 285 70. ,959 57. ,145 46. .827 1.00 16. ,29 c
ATOM 4830 N ASN B 286 70. ,250 59. ,504 43. .071 1.00 16. ,29 N
ATOM 4831 CA ASN B 286 70. ,476 60. ,470 41. .979 1.00 16. ,54 c
ATOM 4832 C ASN B 286 69. ,860 61. ,799 42. .348 1.00 15. ,52 c
ATOM 4833 O ASN B 286 68. ,892 61. ,807 43. ,106 1.00 15. .21 o
ATOM 4834 CB ASN B 286 69. ,912 59. ,916 40. ,678 1.00 18. ,51 c
ATOM 4835 CG ASN B 286 68. ,438 59. ,597 40. ,666 1.00 23. ,49 c
ATOM 4836 ODl ASN B 286 67. ,883 58. ,810 41. ,424 1.00 24. ,91 o
ATOM 4837 ND2 ASN B 286 67. ,727 60. ,222 39. ,732 1.00 26. ,12 N
ATOM 4838 N PRO B 287 70. .520 62. .886 41. .991 1.00 16. ,84 N
ATOM 4839 CA PRO B 287 71. ,731 62. .923 41. .204 1.00 15. ,33 c
ATOM 4840 C PRO B 287 73. ,023 62. .608 41. .969 1.00 20. ,76 c
ATOM 4841 O PRO B 287 73. ,191 62. ,979 43. .119 1.00 18. ,29 o
ATOM 4842 CB PRO B 287 71. ,862 64. ,412 40. .768 1.00 17. ,77 c
ATOM 4843 CG PRO B 287 71. ,057 65. ,157 41. .796 1.00 24. ,90 c
ATOM 4844 CD PRO B 287 69. ,996 64. ,231 42. .347 1.00 20. ,11 c
ATOM 4845 N ALA B 288 73. ,980 62. ,004 41. .291 1.00 16. ,07 N
ATOM 4846 CA ALA B 288 75. ,293 61. ,699 41. .890 1.00 12. .92 C
ATOM 4847 C ALA B 288 76. ,345 61. .834 40. .776 1.00 12. .89 c
ATOM 4848 O ALA B 288 75. .981 61. .765 39. .585 1.00 13. .94 o
ATOM 4849 CB ALA B 288 75. ,199 60. .257 42, .410 1.00 16. .57 c
ATOM 4850 N GLY B 289 77. .608 61. .805 41. .206 1.00 14. .38 N
ATOM 4851 CA GLY B 289 78. ,717 61. .872 40. .264 1.00 14. .79 C
ATOM 4852 C GLY B 289 79. .871 60. .943 40. .685 1.00 16. .05 C
ATOM 4853 O GLY B 289 79. .944 60. .554 41. .862 1.00 16. .87 O
ATOM 4854 N PHE B 290 80. .701 60. .568 39. .715 1.00 12. .12 N
ATOM 4855 CA PHE B 290 81. .926 59. .862 40. .087 1.00 14. .57 C
ATOM 4856 C PHE B 290 82. .690 60. .736 41. .070 1.00 14. .55 C
ATOM 4857 O PHE B 290 82. .795 61. .976 40. .885 1.00 15. .82 o
ATOM 4858 CB PHE B 290 82. .840 59. .632 38, .887 1.00 14. .56 C
ATOM 4859 CG PHE B 290 82. .401 58. .646 37, .873 1.00 12. .24 c
ATOM 4860 CD1 PHE B 290 81. .898 57. .403 38, .281 1.00 17. .69 c
ATOM 4861 CD2 PHE B 290 82. .526 58. .900 36, .526 1.00 14. .49 c
ATOM 4862 CE1 PHE B 290 81. .516 56. .477 37, .329 1.00 15. .94 c
ATOM 4863 CE2 PHE B 290 82. .125 57. .966 35, .579 1.00 14. .72 c
ATOM 4864 CZ PHE B 290 81. .604 56. .744 35, .971 1.00 13. .26 c
ATOM 4865 N GLY B 291 83. .254 60. .153 42, .134 1.00 14. .32 N
ATOM 4866 CA GLY B 291 84. .080 60. .878 43, .097 1.00 13. .56 c
ATOM 4867 C GLY B 291 85. .575 60. .795 42, .756 1.00 14. .72 c
ATOM 4868 O GLY B 291 86. .021 60. .309 41, .725 1.00 16. .84 o
ATOM 4869 N GLN B 292 86. .344 61, .367 43. .673 1.00 16. .20 N
ATOM 4870 CA GLN B 292 87. ,785 61, .417 43. .454 1.00 19. .01 c
ATOM 4871 C GLN B 292 88. .333 60, .028 43, .217 1.00 18. .50 c
ATOM 4872 O GLN B 292 88. .113 59, .157 44, .037 1.00 20. .58 o
ATOM 4873 CB GLN B 292 88. .381 61, .895 44, .786 1.00 16. .55 c
ATOM 4874 CG GLN B 292 89. .820 61, .601 45, .118 1.00 30. .27 c
ATOM 4875 CD GLN B 292 90, .769 62. .538 44, .403 1.00 36. .94 c
ATOM 4876 OE1 GLN B 292 90, .717 63. .747 44, .626 1.00 34. .55 o
ATOM 4877 NE2 GLN B 292 91, .611 61. .962 43, .560 1.00 29. .92 N
ATOM 4878 N PRO B 293 89. .086 59. .843 42, .167 1.00 17. .71 N
ATOM 4879 CA PRO B 293 89, .803 58. .622 41, .871 1.00 19. .36 c
ATOM 4880 C PRO B 293 90, .854 58, .335 42. .942 1.00 18, .36 c
ATOM 4881 O PRO B 293 91, .326 59, .167 43 .712 1.00 18, .12 o
ATOM 4882 CB PRO B 293 90, .531 58, .845 40 .536 1.00 21, .73 c
ATOM 4883 CG PRO B 293 89, .645 59, .932 39 .937 1.00 24, .28 c ATOM 4884 CD PRO B 293 89.,302 60..841 41..102 1.00 20.,17 c
ATOM 4885 N PHE B 294 91. ,261 57. .059 43. ,006 1.00 16. ,57 N
ATOM 4886 CA PHE B 294 92. ,215 56. ,553 43. ,924 1.00 16. ,15 C
ATOM 4887 C PHE B 294 93. ,376 57. ,526 44. .216 1.00 16. ,82 c
ATOM 4888 O PHE B 294 93. ,996 57. .979 43. .250 1.00 20. ,81 o
ATOM 4889 CB PHE B 294 92. ,804 55. ,227 43. .384 1.00 16. ,83 c
ATOM 4890 CG PHE B 294 94. ,109 54. ,894 44. ,060 1.00 23. ,44 c
ATOM 4891 CDl PHE B 294 94. ,122 54. ,537 45. ,393 1.00 21. ,32 c
ATOM 4892 CD2 PHE B 294 95. .305 55. ,006 43. ,364 1.00 18. .05 c
ATOM 4893 CE1 PHE B 294 95. ,325 54. ,251 46. ,024 1.00 25. ,41 c
ATOM 4894 CE2 PHE B 294 96. ,510 54. ,726 43. .995 1.00 18. ,84 c
ATOM 4895 CZ PHE B 294 96. ,515 54. ,361 45. .327 1.00 18. ,69 c
ATOM 4896 N THR B 295 93. ,628 57. ,702 45. .484 1.00 15. .75 N
ATOM 4897 CA THR B 295 94. ,797 58. ,491 45. .902 1.00 19. .31 C
ATOM 4898 C THR B 295 95. ,174 58. ,162 47. ,341 1.00 23. ,18 c
ATOM 4899 O THR B 295 94. .333 57. ,930 48. ,215 1.00 22. ,10 o
ATOM 4900 CB THR B 295 94. .546 59. ,993 45. ,778 1.00 16. ,87 c
ATOM 4901 OGl THR B 295 95. .759 60. ,706 46. ,216 1.00 20. ,58 o
ATOM 4902 CG2 THR B 295 93. .476 60. ,529 46. ,701 1.00 23. ,09 c
ATOM 4903 N THR B 296 96. .462 58. ,245 47. ,649 1.00 19. ,25 N
ATOM 4904 CA THR B 296 97. ,022 58. ,148 48. ,983 1.00 19. ,89 c
ATOM 4905 C THR B 296 97. ,117 59. .554 49. ,589 1.00 23. ,47 c
ATOM 4906 O THR B 296 97. .290 59. ,735 50. ,797 1.00 26. ,59 o
ATOM 4907 CB THR B 296 98. .393 57. .455 48. .999 1.00 30. ,30 c
ATOM 4908 OGl THR B 296 99. .329 58. .080 48. .102 1.00 27. .34 o
ATOM 4909 CG2 THR B 296 98. .262 56. .010 48. ,525 1.00 21. .53 c
ATOM 4910 N ASN B 297 96. .818 60. .592 48. .797 1.00 24. .34 N
ATOM 4911 CA ASN B 297 96. .844 61. .963 49. .359 1.00 27. .55 c
ATOM 4912 C ASN B 297 95. .489 62. .289 49. .977 1.00 26. .04 c
ATOM 4913 O ASN B 297 94. .632 62, .886 49. .330 1.00 25. .16 o
ATOM 4914 CB ASN B 297 97. .273 62. .887 48. .234 1.00 29. .73 c
ATOM 4915 CG ASN B 297 97. .614 64. .306 48. .636 1.00 39. .58 c
ATOM 4916 ODl ASN B 297 97. .568 64. .672 49. .805 1.00 35. .86 o
ATOM 4917 ND2 ASN B 297 97. .949 65. .109 47. .628 1.00 41. .91 N
ATOM 4918 N THR B 298 95. .267 61. .850 51. .220 1.00 24. .28 N
ATOM 4919 CA THR B 298 94. .005 61. .925 51. .918 1.00 24. .81 c
ATOM 4920 C THR B 298 93. .823 62. .981 52. .978 1.00 19. .80 c
ATOM 4921 O THR B 298 92. .743 63, .235 53. .507 1.00 22. .95 o
ATOM 4922 CB THR B 298 93. .701 60, .556 52. .594 1.00 23. .11 c
ATOM 4923 OGl THR B 298 94. .702 60, .282 53. .589 1.00 23. .00 o
ATOM 4924 CG2 THR B 298 93. .698 59, .411 51, .578 1.00 19. .46 c
ATOM 4925 N ASN B 299 94. .955 63, .577 53, .443 1.00 24. .08 N
ATOM 4926 CA ASN B 299 94. .877 64, .613 54. .472 1.00 27, .10 C
ATOM 4927 C ASN B 299 94. .219 64, .126 55. .754 1.00 25. .38 c
ATOM 4928 O ASN B 299 93, .474 64, .767 56. .495 1.00 28, .22 o
ATOM 4929 CB ASN B 299 94. .178 65, .816 53. .842 1.00 34. .95 c
ATOM 4930 CG ASN B 299 94. .840 66. .388 52. .606 1.00 50. .61 c
ATOM 4931 ODl ASN B 299 94. .167 66, .712 51. .622 1.00 51. .90 o
ATOM 4932 ND2 ASN B 299 96, .164 66, .522 52. .624 1.00 52. .62 N
ATOM 4933 N ASN B 300 94, .496 62, .853 56, .080 1.00 29. .32 N
ATOM 4934 CA ASN B 300 93, .978 62, .180 57. .274 1.00 29. .91 c
ATOM 4935 C ASN B 300 94, .899 60, .976 57. .453 1.00 26. .89 c
ATOM 4936 O ASN B 300 94, .995 60, .090 56. .612 1.00 24. .38 o
ATOM 4937 CB ASN B 300 92, .526 61, .740 57. .117 1.00 26. .98 c
ATOM 4938 CG ASN B 300 91. .862 61, .285 58, .389 1.00 22. .71 c
ATOM 4939 ODl ASN B 300 92, .503 60, .721 59, .312 1.00 23. .84 o
ATOM 4940 ND2 ASN B 300 90, .568 61, .539 58, .546 1.00 24, .04 N
ATOM 4941 N PRO B 301 95 .630 60, .969 58, .564 1.00 28, .29 N
ATOM 4942 CA PRO B 301 96 .603 59, .944 58, .877 1.00 28, .45 C ATOM 4943 C PRO B 301 95.,950 58..579 59.,090 1.00 26.,03 C
ATOM 4944 O PRO B 301 96. ,644 57. ,584 58. ,891 1.00 27. ,20 o
ATOM 4945 CB PRO B 301 97. ,325 60. .385 60. ,172 1.00 31. ,40 c
ATOM 4946 CG PRO B 301 96. ,271 61. ,258 60. ,787 1.00 29. ,13 c ATOM 4947 CD PRO B 301 95. 522 61. ,951 59. ,647 1.00 27. ,45 c
ATOM 4948 N ASN B 302 94. ,670 58. ,582 59. ,456 1.00 24. ,31 N
ATOM 4949 CA ASN B 302 94. ,010 57. ,270 59. ,623 1.00 17. ,94 c
ATOM 4950 C ASN B 302 93. ,250 56. ,833 58. ,383 1.00 23. ,46 c
ATOM 4951 O ASN B 302 92. .516 55. ,829 58. ,492 1.00 21. ,92 o ATOM 4952 CB ASN B 302 93. .052 57. ,339 60. ,800 1.00 23. .72 c
ATOM 4953 CG ASN B 302 93. ,859 57. ,544 62. ,081 1.00 32. .32 c
ATOM 4954 ODl ASN B 302 93. ,402 58. .344 62. ,876 1.00 28. .78 o
ATOM 4955 ND2 ASN B 302 94. ,995 56. .875 62. ,208 1.00 28. .32 N
ATOM 4956 N VAL B 303 93. ,428 57. .528 57. .282 1.00 18. .31 N ATOM 4957 CA VAL B 303 92. ,845 57. .140 55. .988 1.00 19. .53 C
ATOM 4958 C VAL B 303 93. .990 56. ,793 55. .056 1.00 22. .04 C
ATOM 4959 O VAL B 303 94. ,810 57. .576 54. .515 1.00 20. .79 o
ATOM 4960 CB VAL B 303 91. .877 58. .194 55. .407 1.00 15. .05 c
ATOM 4961 CGI VAL B 303 91. .381 57. .717 54. .039 1.00 16. .25 c ATOM 4962 CG2 VAL B 303 90. .718 58. ,492 56. .338 1.00 20. .06 c
ATOM 4963 N ASP B 304 94. .201 55. ,479 54. .860 1.00 20. .31 N
ATOM 4964 CA ASP B 304 95. .268 54. ,971 54. .029 1.00 17. .92 c
ATOM 4965 C ASP B 304 95. • 111 55. .406 52. .568 1.00 20. .89 c
ATOM 4966 O ASP B 304 96. .065 55. .783 51. .886 1.00 22. .23 o ATOM 4967 CB ASP B 304 95. .362 53. .453 54. .046 1.00 20. .18 c
ATOM 4968 CG ASP B 304 96. .019 52. .851 55. .258 1.00 21. .75 c
ATOM 4969 ODl ASP B 304 96. .823 53. .498 55. .975 1.00 20. ,68 o
ATOM 4970 OD2 ASP B 304 95. .724 51. .650 55. .489 1.00 20. .32 o
ATOM 4971 N ALA B 305 93. .860 55. .351 52. .098 1.00 19. .29 N ATOM 4972 CA ALA B 305 93. .601 55. .759 50. .747 1.00 18. .86 C
ATOM 4973 C ALA B 305 92. .112 55. .997 50. .462 1.00 20. .52 c
ATOM 4974 O ALA B 305 91. .253 55. .458 51. .134 1.00 16. .38 o
ATOM 4975 CB ALA B 305 94. .093 54. .699 49. .773 1.00 24. .87 c
ATOM 4976 N ILE B 306 91. .901 56. .849 49. .470 1.00 21, .75 N ATOM 4977 CA ILE B 306 90. .554 57. .011 48. .884 1.00 16. .22 c
ATOM 4978 C ILE B 306 90. .603 56, ,061 47. .700 1.00 16. .41 c
ATOM 4979 O ILE B 306 91. .590 55. .973 46. .952 1.00 17. .02 o
ATOM 4980 CB ILE B 306 90. .323 58. .462 48. .419 1.00 17. .23 c
ATOM 4981 CGI ILE B 306 89. .975 59. .367 49. .594 1.00 22. .93 c ATOM 4982 CG2 ILE B 306 89. .188 58. .496 47. .400 1.00 17. .43 c
ATOM 4983 CDl ILE B 306 90, .105 60. .852 49. .248 1.00 21. .04 c
ATOM 4984 N VAL B 307 89. .572 55. .192 47. .559 1.00 14. .89 N
ATOM 4985 CA VAL B 307 89. .531 54. .185 46. .538 1.00 17, .89 c
ATOM 4986 C VAL B 307 88. .172 54. .196 45. .825 1.00 13, .24 c ATOM 4987 O VAL B 307 87. .311 54. .920 46. .282 1.00 13, .69 o
ATOM 4988 CB VAL B 307 89, .684 52. .752 47. .152 1.00 11, .95 c
ATOM 4989 CGI VAL B 307 91, .149 52. .568 47. .634 1.00 16, .72 c
ATOM 4990 CG2 VAL B 307 88, .759 52. .486 48. .299 1.00 15, .70 c
ATOM 4991 N TRP B 308 88, .021 53. .379 44. .795 1.00 14, .95 N ATOM 4992 CA TRP B 308 86, .686 53. .165 44, .207 1.00 11, .27 c
ATOM 4993 C TRP B 308 86, .400 51. .692 44. .521 1.00 14, .29 c
ATOM 4994 O TRP B 308 87, .217 50. .868 44, .096 1.00 14, .70 o
ATOM 4995 CB TRP B 308 86, .540 53. .367 42, .708 1.00 12, .68 c
ATOM 4996 CG TRP B 308 86, .445 54. .809 42. .281 1.00 14, .81 c ATOM 4997 CDl TRP B 308 86, .775 55. .892 43, .036 1.00 15, .98 c
ATOM 4998 CD2 TRP B 308 85, .992 55. .283 41 .021 1.00 13, .63 c
ATOM 4999 NE1 TRP B 308 86, .511 57, .060 42 .315 1.00 14, .41 N
ATOM 5000 CE2 TRP B 308 86, .039 56, .696 41 .094 1.00 12, .63 C
ATOM 5001 CE3 TRP B 308 85, .553 54, .666 39 .850 1.00 11, .90 c ATOM 5002 CZ2 TRP B 308 85..667 57..480 39..984 1.00 12..59 c
ATOM 5003 CZ3 TRP B 308 85. .141 55. .441 38. .773 1.00 14. .38 c
ATOM 5004 CH2 TRP B 308 85. .265 56. ,827 38. .868 1.00 15. .58 c
ATOM 5005 N VAL B 309 85. ,299 51. ,443 45. .230 1.00 13. .29 N
ATOM 5006 CA VAL B 309 84. ,972 50. .037 45. .507 1.00 14. .73 C
ATOM 5007 C VAL B 309 83. .750 49. .608 44. .706 1.00 13. .65 C
ATOM 5008 O VAL B 309 83. ,879 48. .722 43. .867 1.00 13. .80 o
ATOM 5009 CB VAL B 309 84. ,734 49. .821 46. .980 1.00 12. .40 C
ATOM 5010 CGI VAL B 309 84. .566 48. .313 47. .282 1.00 13. .46 C
ATOM 5011 CG2 VAL B 309 85. ,948 50. .337 47. .749 1.00 10. .65 C
ATOM 5012 N LYS B 310 82. ,619 50. .234 44. .912 1.00 12. .78 N
ATOM 5013 CA LYS B 310 81. .449 49. .907 44. .078 1.00 11. .36 C
ATOM 5014 C LYS B 310 81. .740 50. .360 42. .667 1.00 13. .36 c
ATOM 5015 O LYS B 310 82. ,224 51. .488 42. .520 1.00 14. .33 o
ATOM 5016 CB LYS B 310 80. .261 50. .704 44. .648 1.00 14. .63 c
ATOM 5017 CG LYS B 310 79. .036 50. .837 43. .769 1.00 10. .97 c
ATOM 5018 CD LYS B 310 78. .204 49. .575 43. .718 1.00 12. .43 c
ATOM 5019 CE LYS B 310 77. .103 49. .754 42. .675 1.00 11. .20 c
ATOM 5020 NZ LYS B 310 76. .158 48. .578 42. .821 1.00 12. .70 N
ATOM 5021 N PRO B 311 81. .409 49. .601 41. .642 1.00 12. .47 N
ATOM 5022 CA PRO B 311 81. .669 49. .978 40. .249 1.00 14. ,66 C
ATOM 5023 C PRO B 311 80. .498 50. .829 39. .775 1.00 14. .22 C
ATOM 5024 O PRO B 311 79. .444 50. ,257 39. .427 1.00 15. .04 O
ATOM 5025 CB PRO B 311 81. .788 48. .682 39. .433 1.00 15. .63 c
ATOM 5026 CG PRO B 311 82. .043 47. .691 40. .573 1.00 14. .70 c
ATOM 5027 CD PRO B 311 81, .088 48. .165 41. .700 1.00 12. .82 c
ATOM 5028 N GLY B 312 80. .608 52. ,139 39, .907 1.00 13, .21 N
ATOM 5029 CA GLY B 312 79. .469 53. .012 39. .589 1.00 11. .15 c
ATOM 5030 C GLY B 312 78. .962 52. .784 38. .170 1.00 12. .40 c
ATOM 5031 O GLY B 312 79. .705 52. .893 37. .222 1.00 14, .28 o
ATOM 5032 N GLY B 313 77. .656 52. .548 38. .046 1.00 12. .20 N
ATOM 5033 CA GLY B 313 77. .094 52. .123 36. .763 1.00 11. .67 c
ATOM 5034 C GLY B 313 76. .479 50. .737 36. .964 1.00 10. .84 c
ATOM 5035 O GLY B 313 75. .506 50, .481 36. .273 1.00 15. .55 o
ATOM 5036 N GLU B 314 76. .998 49, .902 37. .884 1.00 14, .09 N
ATOM 5037 CA GLU B 314 76. .294 48, .640 38. .241 1.00 11. .26 C
ATOM 5038 C GLU B 314 75. .156 48. .979 39, .210 1.00 15, .02 c
ATOM 5039 O GLU B 314 75, .322 49. .622 40. .235 1.00 14, .85 o
ATOM 5040 CB GLU B 314 77, .227 47. .638 38. .916 1.00 12, .56 c
ATOM 5041 CG GLU B 314 78. .345 47. .197 37. .989 1.00 13. .65 c
ATOM 5042 CD GLU B 314 79, .269 46. .157 38, .596 1.00 20, .26 c
ATOM 5043 OE1 GLU B 314 79. .220 45, .790 39. .779 1.00 18, .56 o
ATOM 5044 OE2 GLU B 314 80. .126 45, .667 37. .826 1.00 19, .69 o
ATOM 5045 N SER B 315 73. .944 48, .583 38. .816 1.00 14. .99 N
ATOM 5046 CA SER B 315 72. .771 48. .879 39. .634 1.00 14. .73 C
ATOM 5047 C SER B 315 72. .870 48. .300 41. .037 1.00 13. .26 c
ATOM 5048 O SER B 315 73, .336 47. .195 41. .262 1.00 15. .35 o
ATOM 5049 CB SER B 315 71, .539 48. .241 38, .950 1.00 15. .36 c
ATOM 5050 OG SER B 315 70, .384 48. .695 39, .680 1.00 14, .07 o
ATOM 5051 N ASP B 316 72, .193 49. .015 41, .949 1.00 13, .79 N
ATOM 5052 CA ASP B 316 72, .043 48. .515 43, .320 1.00 11, .24 c
ATOM 5053 C ASP B 316 70, .763 47. .686 43, .457 1.00 15, .64 c
ATOM 5054 O ASP B 316 70, .565 47. .094 44, .534 1.00 16, .84 o
ATOM 5055 CB ASP B 316 71, .918 49. .667 44, .335 1.00 11, .91 c
ATOM 5056 CG ASP B 316 73, .175 50. .524 44, .351 1.00 17, .95 c
ATOM 5057 ODl ASP B 316 74. .263 49. .936 44. .427 1.00 15, .26 o
ATOM 5058 OD2 ASP B 316 73. .013 51. .757 44. .339 1.00 13. .75 o
ATOM 5059 N GLY B 317 69, .974 47, .626 42. .383 1.00 14, .29 N
ATOM 5060 CA GLY B 317 68. .667 46, .962 42. .484 1.00 17, .43 C ATOM 5061 c GLY B 317 67.,632 47.,787 41.,733 1.00 15.,37 C
ATOM 5062 O GLY B 317 67. ,876 48. ,859 41. ,215 1.00 16. .97 o
ATOM 5063 N GLN B 318 66. ,437 47. .195 41. ,540 1.00 17. ,59 N
ATOM 5064 CA GLN B 318 65. ,406 47. ,926 40. ,758 1.00 15. ,47 C ATOM 5065 C GLN B 318 64. ,751 48. .890 41. ,740 1.00 22. ,68 C
ATOM 5066 O GLN B 318 63. ,691 48. ,608 42. ,320 1.00 23. ,51 O
ATOM 5067 CB GLN B 318 64. .360 46. ,888 40. ,293 1.00 14. ,02 C
ATOM 5068 CG GLN B 318 64. ,917 45. ,887 39. ,325 1.00 15. ,43 c
ATOM 5069 CD GLN B 318 64. ,300 44. .495 39. ,327 1.00 23. .03 c ATOM 5070 OE1 GLN B 318 64. .058 43. .792 40. ,291 1.00 23. ,47 o
ATOM 5071 NE2 GLN B 318 64. ,130 43. .985 38. ,123 1.00 18. ,29 N
ATOM 5072 N CYS B 319 65. ,378 50. ,029 41. ,963 1.00 21. ,27 N
ATOM 5073 CA CYS B 319 64. .938 51. ,000 42. ,955 1.00 19. ,17 c
ATOM 5074 C CYS B 319 65. .762 52. .263 42. .667 1.00 21. ,68 c ATOM 5075 O CYS B 319 66. .610 52. .187 41. .753 1.00 17. ,30 o
ATOM 5076 CB CYS B 319 65. .119 50. .517 44. .387 1.00 14. ,69 c
ATOM 5077 SG CYS B 319 66. .550 49. .505 44. .821 1.00 14. ,68 s
ATOM 5078 N GLY B 320 65. .449 53. .332 43. .373 1.00 20. ,58 N
ATOM 5079 CA GLY B 320 66. .123 54. .596 43. .086 1.00 14. .87 c ATOM 5080 C GLY B 320 65. .812 55. .025 41. .651 1.00 22. ,75 c
ATOM 5081 O GLY B 320 64. .696 54. .914 41. .173 1.00 20. ,22 o
ATOM 5082 N MET B 321 66. .820 55. .475 40. .924 1.00 24. ,95 N
ATOM 5083 CA MET B 321 66. .659 55. .983 39. .581 1.00 24. ,67 c
ATOM 5084 C MET B 321 65. .847 55. .079 38. .673 1.00 26. .28 c ATOM 5085 O MET B 321 66. .088 53. .883 38. .560 1.00 22. .52 o
ATOM 5086 CB MET B 321 68. .053 56. .249 38. .981 1.00 24. .83 c
ATOM 5087 CG MET B 321 67. .907 56. .968 37. .630 1.00 19. .87 c
ATOM 5088 SD MET B 321 69. .561 57. .484 37, .139 1.00 20. .71 s
ATOM 5089 CE MET B 321 69. .517 57. .154 35. .383 1.00 19. .55 c ATOM 5090 N GLY B 322 64. .850 55. .664 38, .014 1.00 22. .65 N
ATOM 5091 CA GLY B 322 63. .975 54. .949 37. .116 1.00 27. .77 c
ATOM 5092 C GLY B 322 64. .732 54. .273 35. .974 1.00 20. .77 c
ATOM 5093 O GLY B 322 65. .711 54. .760 35, .455 1.00 24. .66 o
ATOM 5094 N GLY B 323 64, .224 53. .080 35. .645 1.00 24. .85 N ATOM 5095 CA GLY B 323 64. .777 52. .208 34. .640 1.00 24. .99 C
ATOM 5096 C GLY B 323 65. .819 51. .273 35. .238 1.00 24. .75 c
ATOM 5097 O GLY B 323 66, .540 50. .623 34. .483 1.00 23. .18 o
ATOM 5098 N ALA B 324 65, .983 51, .299 36. .563 1.00 21, .11 N
ATOM 5099 CA ALA B 324 67. .046 50, .519 37. .173 1.00 21, .32 c ATOM 5100 C ALA B 324 66. .774 49. .023 37, .079 1.00 21. .16 c
ATOM 5101 O ALA B 324 65. .717 48. .521 37, .460 1.00 20, .17 o
ATOM 5102 CB ALA B 324 67. .205 50. .888 38, .648 1.00 18. .27 c
ATOM 5103 N PRO B 325 67, .795 48. .303 36, .676 1.00 17, .93 N
ATOM 5104 CA PRO B 325 67, .767 46. .867 36. .532 1.00 17. .77 C ATOM 5105 C PRO B 325 68, .166 46. .232 37. .865 1.00 18. .95 C
ATOM 5106 O PRO B 325 68, .424 46. .937 38. .844 1.00 18. .68 O
ATOM 5107 CB PRO B 325 68, .785 46. .541 35. .423 1.00 18. .76 C
ATOM 5108 CG PRO B 325 69, .832 47. .590 35. .757 1.00 20. .96 C
ATOM 5109 CD PRO B 325 69, .067 48, .848 36. .132 1.00 17. .27 C ATOM 5110 N ALA B 326 68, .113 44. .923 37. .906 1.00 15. .89 N
ATOM 5111 CA ALA B 326 68, .385 44, .174 39. .129 1.00 20. .27 C
ATOM 5112 C ALA B 326 69. .802 44, .411 39. .595 1.00 21. .35 C
ATOM 5113 O ALA B 326 70. .709 44. .866 38. .872 1.00 19, .75 o
ATOM 5114 CB ALA B 326 68. .000 42. .721 38. .869 1.00 22, .21 c ATOM 5115 N ALA B 327 70 .080 44, .150 40 .863 1.00 15, .97 N
ATOM 5116 CA ALA B 327 71 .392 44, .371 41 .448 1.00 15, .02 c
ATOM 5117 C ALA B 327 72 .533 43, .748 40 .640 1.00 20, .42 c
ATOM 5118 O ALA B 327 72 .504 42, .591 40 .232 1.00 21, .94 o
ATOM 5119 CB ALA B 327 71 .452 43, .803 42 .869 1.00 18, .25 c ATOM 5120 N GLY B 328 73.556 44.570 40.432 1.00 17.,85 N
ATOM 5121 CA GLY B 328 74. 734 44. 200 39. 671 1.00 15. ,80 C
ATOM 5122 C GLY B 328 74. 522 44. 308 38. ,146 1.00 13. ,02 C
ATOM 5123 O GLY B 328 75. 563 44. ,150 37. 488 1.00 17. ,91 O
ATOM 5124 N MET B 329 73. 339 44. ,536 37. ,648 1.00 14. ,05 N
ATOM 5125 CA MET B 329 73. ,187 44. ,626 36. ,178 1.00 16. ,72 C
ATOM 5126 C MET B 329 73. ,655 46. ,016 35. ,783 1.00 16. ,72 C
ATOM 5127 O MET B 329 73. ,507 46. ,968 36. ,558 1.00 18. ,00 O
ATOM 5128 CB MET B 329 71. ,703 44. ,478 35. ,815 1.00 17. ,62 C
ATOM 5129 CG MET B 329 71. ,148 43. ,088 36. ,101 1.00 21. .62 C
ATOM 5130 SD MET B 329 71. .711 41. ,853 34. ,921 1.00 21. .71 s
ATOM 5131 CE MET B 329 70. ,731 42. ,298 33. ,467 1.00 18. .50 c
ATOM 5132 N TRP B 330 74. ,158 46. ,132 34. ,566 1.00 14. .64 N
ATOM 5133 CA TRP B 330 74. ,611 47. 412 34. ,062 1.00 16. ,09 c
ATOM 5134 C TRP B 330 73. ,444 48. ,353 33. ,806 1.00 14. ,70 c
ATOM 5135 O TRP B 330 72. ,396 48. ,025 33. .253 1.00 17. ,39 O
ATOM 5136 CB TRP B 330 75. .413 47. ,152 32. .769 1.00 16. ,88 c
ATOM 5137 CG TRP B 330 76. ,152 48. ,413 32. ,382 1.00 15. ,32 c
ATOM 5138 CDl TRP B 330 75. .913 49. ,194 31. ,287 1.00 16. .38 c
ATOM 5139 CD2 TRP B 330 77. .213 49. ,007 33. ,105 1.00 14. .28 c
ATOM 5140 NE1 TRP B 330 76. ,780 50. ,270 31. ,291 1.00 13. .72 N
ATOM 5141 CE2 TRP B 330 77. ,605 50. .169 32. ,389 1.00 14. .27 C
ATOM 5142 CE3 TRP B 330 77. .889 48. .672 34. ,282 1.00 15. .92 C
ATOM 5143 CZ2 TRP B 330 78. .637 50. .995 32. ,842 1.00 15. .79 C
ATOM 5144 CZ3 TRP B 330 78. .921 49. .494 34. ,714 1.00 20. .19 C
ATOM 5145 CH2 TRP B 330 79. .280 50. .647 33. .992 1.00 16. .72 c
ATOM 5146 N PHE B 331 73. .603 49. .579 34. .262 1.00 14. .26 N
ATOM 5147 CA PHE B 331 72. .631 50. ,645 34. .198 1.00 12. .56 C
ATOM 5148 C PHE B 331 73. .277 51. .818 33. .482 1.00 16. .00 C
ATOM 5149 O PHE B 331 73. .748 52. .750 34. .100 1.00 16. .17 O
ATOM 5150 CB PHE B 331 72, .171 50. .926 35. .632 1.00 14. .49 c
ATOM 5151 CG PHE B 331 71. .002 51. .856 35. .770 1.00 13. .84 c
ATOM 5152 CDl PHE B 331 70. .246 52. .354 34. .721 1.00 14. .56 c
ATOM 5153 CD2 PHE B 331 70. .653 52. .210 37. .068 1.00 12. .45 c
ATOM 5154 CE1 PHE B 331 69. .204 53. .213 34. .937 1.00 17. .22 c
ATOM 5155 CE2 PHE B 331 69. .579 53. .083 37. .268 1.00 16. .15 c
ATOM 5156 CZ PHE B 331 68. .844 53. .568 36. .226 1.00 14. .96 c
ATOM 5157 N ASP B 332 73. .307 51. .684 32. .136 1.00 15. .82 N
ATOM 5158 CA ASP B 332 74. .068 52. .692 31. .372 1.00 14. .89 C
ATOM 5159 C ASP B 332 73, .656 54. .120 31. .616 1.00 16. .28 C
ATOM 5160 O ASP B 332 74, .516 55. .013 31. .778 1.00 15. .63 O
ATOM 5161 CB ASP B 332 74, .023 52. .384 29. .845 1.00 12. .37 C
ATOM 5162 CG ASP B 332 75, .290 52. .999 29. .236 1.00 15. .09 c
ATOM 5163 ODl ASP B 332 76, .376 52. .553 29. .641 1.00 16. .23 o
ATOM 5164 OD2 ASP B 332 75. .029 53. .878 28. .395 1.00 17. .26 o
ATOM 5165 N ALA B 333 72, .375 54. .477 31. .685 1.00 17. .37 N
ATOM 5166 CA ALA B 333 72, .005 55. .867 31. .958 1.00 14. .48 C
ATOM 5167 C ALA B 333 72, .529 56. .367 33, .293 1.00 13, .03 c
ATOM 5168 O ALA B 333 72, .765 57, .580 33, .459 1.00 16, .00 o
ATOM 5169 CB ALA B 333 70 .478 55, .995 31, .914 1.00 18, .93 c
ATOM 5170 N TYR B 334 72 .653 55, .489 34, .287 1.00 14, .79 N
ATOM 5171 CA TYR B 334 73 .238 55, .916 35, .567 1.00 15, .54 C
ATOM 5172 C TYR B 334 74 .744 56, .190 35 .447 1.00 14 .76 c
ATOM 5173 O TYR B 334 75 .270 57 .152 35 .997 1.00 14 .60 o
ATOM 5174 CB TYR B 334 72 .924 54, .852 36, .607 1.00 14, .79 c
ATOM 5175 CG TYR B 334 73 .200 55, .311 38, .009 1.00 14, .39 c
ATOM 5176 CDl TYR B 334 74 .472 55, .268 38, .535 1.00 13, .24 c
ATOM 5177 CD2 TYR B 334 72 .190 55 .795 38, .826 1.00 19, .92 c
ATOM 5178 CE1 TYR B 334 74 .758 55 .708 39 .833 1.00 10, .89 c ATOM 5179 CE2 TYR B 334 72.423 56.215 40.113 1.00 14.81 c
ATOM 5180 CZ TYR B 334 73. 718 56. 145 40. ,618 1.00 17. ,00 c
ATOM 5181 OH TYR B 334 73. 941 56. ,617 41. ,885 1.00 15. .30 o
ATOM 5182 N ALA B 335 75. 440 55. .376 34. .648 1.00 14. ,75 N
ATOM 5183 CA ALA B 335 76. 858 55. ,517 34. .354 1.00 14. ,21 c
ATOM 5184 C ALA B 335 77. 037 56. ,846 33. ,582 1.00 15. ,83 c
ATOM 5185 O ALA B 335 77. ,933 57. .607 33. ,921 1.00 16. .22 o
ATOM 5186 CB ALA B 335 77. 427 54. ,363 33. ,559 1.00 17. 01 c
ATOM 5187 N GLN B 336 76. ,050 57. ,169 32. .733 1.00 13. ,70 N
ATOM 5188 CA GLN B 336 76. ,150 58. .467 32. .034 1.00 17. ,57 C
ATOM 5189 C GLN B 336 76. ,036 59. ,643 32. ,987 1.00 15. 83 C
ATOM 5190 O GLN B 336 76. ,803 60. ,644 32. ,981 1.00 14. ,80 o
ATOM 5191 CB GLN B 336 75. ,149 58. ,505 30. ,890 1.00 16. ,21 c
ATOM 5192 CG GLN B 336 75. 471 57. ,638 29. ,680 1.00 19. ,45 c
ATOM 5193 CD GLN B 336 74. ,324 57. ,610 28. ,662 1.00 19. ,15 c
ATOM 5194 OE1 GLN B 336 73. ,880 58. ,705 28. ,298 1.00 21. ,21 o
ATOM 5195 NE2 GLN B 336 73. ,927 56. ,404 28. .315 1.00 17. ,62 N
ATOM 5196 N MET B 337 75. ,076 59. ,580 33. .925 1.00 15. .24 N
ATOM 5197 CA MET B 337 74. .903 60. ,627 34. ,933 1.00 15. .88 C
ATOM 5198 C MET B 337 76. .142 60. .819 35. ,785 1.00 15. ,62 C
ATOM 5199 O MET B 337 76. .679 61. ,905 36. ,045 1.00 15. ,22 O
ATOM 5200 CB MET B 337 73. .688 60. ,289 35. .834 1.00 15. ,13 C
ATOM 5201 CG MET B 337 73. .743 61. .191 37. .099 1.00 15. .31 c
ATOM 5202 SD MET B 337 72. .582 60. ,588 38. .364 1.00 15. .31 s
ATOM 5203 CE MET B 337 73. .524 59. .199 39. .035 1.00 20. .45 c
ATOM 5204 N LEU B 338 76. .770 59. .694 36. .202 1.00 13. .63 N
ATOM 5205 CA LEU B 338 77. .969 59. ,774 37. .028 1.00 12. .19 C
ATOM 5206 C LEU B 338 79. .113 60. .449 36. .260 1.00 15. .16 C
ATOM 5207 O LEU B 338 79. .891 61. .162 36, .874 1.00 17. .16 o
ATOM 5208 CB LEU B 338 78. .503 58. .357 37. .382 1.00 14. .20 c
ATOM 5209 CG LEU B 338 77. .608 57. .594 38. .380 1.00 12. .41 c
ATOM 5210 CDl LEU B 338 78. .170 56. .196 38. .662 1.00 12. .02 c
ATOM 5211 CD2 LEU B 338 77. .571 58. .216 39. .753 1.00 13. .59 c
ATOM 5212 N THR B 339 79. ,172 60. .253 34, .960 1.00 13. .77 N
ATOM 5213 CA THR B 339 80, .194 60. .822 34, .103 1.00 13. .86 c
ATOM 5214 C THR B 339 79. .947 62. .333 33, .957 1.00 16. .24 c
ATOM 5215 O THR B 339 80, .838 63. .158 34, .147 1.00 17. .72 o
ATOM 5216 CB THR B 339 80, .156 60. .183 32, .705 1.00 15. .98 c
ATOM 5217 OGl THR B 339 80. .425 58. .760 32, .823 1.00 15. .82 o
ATOM 5218 CG2 THR B 339 81. .296 60. .734 31, .820 1.00 15. .86 c
ATOM 5219 N GLN B 340 78, .694 62. .706 33. .675 1.00 15, .53 N
ATOM 5220 CA GLN B 340 78, .327 64. .124 33. .556 1.00 17, .42 C
ATOM 5221 C GLN B 340 78. .686 64. .878 34. .817 1.00 20, .77 c
ATOM 5222 O GLN B 340 79. .222 65. .994 34, .793 1.00 21, .75 o
ATOM 5223 CB GLN B 340 76, .808 64, .216 33, .278 1.00 19, .47 c
ATOM 5224 CG GLN B 340 76, .514 63. .658 31, .893 1.00 28, .91 c
ATOM 5225 CD GLN B 340 75, .119 63, .924 31, .363 1.00 41, .77 c
ATOM 5226 OE1 GLN B 340 74, .986 64, .138 30 .149 1.00 31, .47 o
ATOM 5227 NE2 GLN B 340 74, .118 63, .889 32, .234 1.00 37, .28 N
ATOM 5228 N ASN B 341 78, .441 64, .309 36, .005 1.00 18, .07 N
ATOM 5229 CA ASN B 341 78, .740 64, .989 37 .256 1.00 19, .06 C
ATOM 5230 C ASN B 341 80, .075 64, .597 37, .881 1.00 15, .53 c
ATOM 5231 O ASN B 341 80, .233 64, .710 39 .115 1.00 19, .04 0
ATOM 5232 CB ASN B 341 77, .641 64 .656 38 .283 1.00 25 .21 c
ATOM 5233 CG ASN B 341 76, .273 65, .115 37 .815 1.00 30, .07 c
ATOM 5234 ODl ASN B 341 76, .166 66, .220 37 .289 1.00 29 .59 o
ATOM 5235 ND2 ASN B 341 75 .284 64 .263 38 .024 1.00 27 .05 N
ATOM 5236 N ALA B 342 80, .998 64, .063 37 .109 1.00 16, .08 N
ATOM 5237 CA ALA B 342 82 .250 63 .523 37 .561 1.00 14, .20 C ATOM 5238 c ALA B 342 83.199 64.,529 38.,175 1.00 16..06 c
ATOM 5239 O ALA B 342 83.217 65. ,686 37. ,753 1.00 18. ,87 o
ATOM 5240 CB ALA B 342 83.019 62. ,766 36. ,475 1.00 16. .71 c
ATOM 5241 N HIS B 343 83.931 64. ,067 39. ,175 1.00 17. .34 N
ATOM 5242 CA HIS B 343 85.008 64. ,836 39. ,809 1.00 18. ,17 C
ATOM 5243 C HIS B 343 85.915 65. ,431 38. ,730 1.00 18. .50 c
ATOM 5244 O HIS B 343 86.200 64. ,789 37. ,710 1.00 17. .20 o
ATOM 5245 CB HIS B 343 85.784 63. ,852 40. ,691 1.00 19. ,94 c
ATOM 5246 CG HIS B 343 86.774 64. ,465 41. .621 1.00 22. ,89 c
ATOM 5247 ND1 HIS B 343 88.000 64. ,909 41. .162 1.00 23. ,62 N
ATOM 5248 CD2 HIS B 343 86.703 64. ,773 42. .934 1.00 19. ,84 C
ATOM 5249 CE1 HIS B 343 88.658 65. ,422 42. .190 1.00 27. ,92 c
ATOM 5250 NE2 HIS B 343 87.906 65. ,362 43. .275 1.00 27. ,70 N
ATOM 5251 N ASP B 344 86.403 66. ,641 38. ,974 1.00 25. .16 N
ATOM 5252 CA ASP B 344 87.307 67. ,338 38. ,068 1.00 21. ,59 C
ATOM 5253 C ASP B 344 88.558 66. .591 37. ,673 1.00 26. .29 C
ATOM 5254 O ASP B 344 89.141 66. ,903 36. ,628 1.00 22. .86 o
ATOM 5255 CB ASP B 344 87.746 68. ,637 38. ,790 1.00 28. .98 c
ATOM 5256 CG ASP B 344 86.684 69. .662 39. ,075 1.00 41. .99 c
ATOM 5257 ODl ASP B 344 85.782 69. .858 38. ,231 1.00 41. ,42 o
ATOM 5258 OD2 ASP B 344 86.722 70. .322 40. ,145 1.00 50. ,37 o
ATOM 5259 N GLU B 345 89.059 65. ,567 38. ,364 1.00 18. ,73 N
ATOM 5260 CA GLU B 345 90.241 64. ,832 37. ,985 1.00 18. ,17 c
ATOM 5261 C GLU B 345 90.008 64. ,038 36. ,691 1.00 21. .30 c
ATOM 5262 O GLU B 345 90.930 63. ,660 35. ,964 1.00 21. .94 o
ATOM 5263 CB GLU B 345 90.628 63. ,874 39. .110 1.00 20. .24 c
ATOM 5264 CG GLU B 345 91.837 63. .010 38. .757 1.00 25. .76 c
ATOM 5265 CD GLU B 345 92.587 62. .562 40. .004 1.00 36. .30 c
ATOM 5266 OE1 GLU B 345 92.592 63. .298 41. .018 1.00 33. .65 o
ATOM 5267 OE2 GLU B 345 93.185 61. .458 39. .968 1.00 34. .93 o
ATOM 5268 N ILE B 346 88.745 63. .635 36. .496 1.00 17. .40 N
ATOM 5269 CA ILE B 346 88.371 62. .847 35, .329 1.00 16. .88 c
ATOM 5270 C ILE B 346 88.219 63. .690 34. .074 1.00 17. .04 c
ATOM 5271 O ILE B 346 87.359 64. .583 34. .071 1.00 20. .05 o
ATOM 5272 CB ILE B 346 87.041 62. .130 35. .697 1.00 15. .39 c
ATOM 5273 CGI ILE B 346 87.409 61. .190 36. .850 1.00 18. .55 c
ATOM 5274 CG2 ILE B 346 86.493 61. .353 34. .507 1.00 18. .29 c
ATOM 5275 CDl ILE B 346 86.198 60. .561 37. .539 1.00 14. .82 c
ATOM 5276 N ALA B 347 88.960 63. .398 33. .021 1.00 18. .37 N
ATOM 5277 CA ALA B 347 88.861 64. .168 31. .760 1.00 17. .33 c
ATOM 5278 C ALA B 347 89.318 63. .412 30, .497 1.00 20. .08 c
ATOM 5279 O ALA B 347 90.250 62. .608 30, .770 1.00 20, .39 o
ATOM 5280 CB ALA B 347 89.727 65. .428 31, .837 1.00 20, .16 c
ATOM 5281 OWO WAT W 1 79.112 54. .022 45, .738 1.00 12, .17 o
ATOM 5282 OWO WAT W 2 4.055 20. .110 23, .781 1.00 12, .73 o
ATOM 5283 OWO WAT W 3 2.034 21. .964 24, .841 1.00 12. .38 o
ATOM 5284 OWO WAT W 4 81.210 50. .505 53, .418 1.00 12. .48 o
ATOM 5285 OWO WAT W 5 18.092 19, .751 17. .952 1.00 13, .16 o
ATOM 5286 OWO WAT W 6 78.129 41, .012 53. .890 1.00 13, .41 o
ATOM 5287 OWO WAT W 7 81.306 56, .076 47, .142 1.00 13, .32 o
ATOM 5288 OWO WAT W 8 11.893 20, .570 25, .469 1.00 14, .06 o
ATOM 5289 OWO WAT W 9 -2.426 22, .881 11, .531 1.00 14, .23 o
ATOM 5290 OWO WAT W 10 -1.267 19, .759 16, .839 1.00 13, .86 o
ATOM 5291 OWO WAT W 11 18.608 19, .198 21, .819 1.00 13, .78 o
ATOM 5292 OWO WAT W 12 88.547 50, .226 37, .081 1.00 14, .21 o
ATOM 5293 OWO WAT W 13 75.880 52, .351 40, .140 1.00 14, .75 o
ATOM 5294 OWO WAT W 14 -3.729 30, .367 14, .059 1.00 14 .40 o
ATOM 5295 OWO WAT W 15 91.589 46, .538 41 .796 1.00 15 .04 o
ATOM 5296 OWO WAT W 16 -3.671 21. .503 18 .469 1.00 15 .32 o ATOM 5297 OWO WAT W 17 79.062 48.715 52.517 1.00 15.04 o
ATOM 5298 OWO WAT W 18 2.175 17.093 25.581 1.00 15.54 o
ATOM 5299 OWO WAT W 19 73.198 52.473 39.528 1.00 15.46 o
ATOM 5300 OWO WAT W 20 78.461 47.746 49.834 1.00 15.58 o
ATOM 5301 OWO WAT W 21 82.073 54.693 40.194 1.00 15.32 o
ATOM 5302 OWO WAT W 22 76.464 49.833 51.285 1.00 15.48 o
ATOM 5303 OWO WAT W 23 0.721 17.028 11.027 1.00 15.78 o
ATOM 5304 OWO WAT W 24 75.548 43.374 54.531 1.00 16.49 o
ATOM 5305 OWO WAT W 25 75.361 34.637 50.038 1.00 15.38 o
ATOM 5306 OWO WAT W 26 87.493 51.275 34.699 1.00 16.09 o
ATOM 5307 OWO WAT W 27 76.610 51.276 54.441 1.00 15.92 o
ATOM 5308 OWO WAT W 28 78.105 47.615 29.014 1.00 16.54 o
ATOM 5309 OWO WAT W 29 4.161 33.336 13.790 1.00 16.72 o
ATOM 5310 OWO WAT W 30 0.715 18.929 24.143 1.00 16.01 o
ATOM 5311 OWO WAT W 31 75.699 40.905 55.224 1.00 15.75 o
ATOM 5312 OWO WAT W 32 72.285 45.414 54.390 1.00 16.94 o
ATOM 5313 OWO WAT W 33 8.177 22.864 29.335 1.00 16.44 o
ATOM 5314 OWO WAT w 34 75.943 34.973 46.108 1.00 16.92 o
ATOM 5315 OWO WAT w 35 12.402 18.231 26.887 1.00 17.33 o
ATOM 5316 OWO WAT w 36 0.823 30.118 8.990 1.00 16.04 o
ATOM 5317 OWO WAT w 37 81.149 44.222 57.670 1.00 17.82 o
ATOM 5318 OWO WAT w 38 89.733 54.803 42.176 1.00 16.98 o
ATOM 5319 OWO WAT w 39 26.067 19.553 29.823 1.00 17.33 o
ATOM 5320 OWO WAT w 40 67.030 53.636 48.885 1.00 16.30 o
ATOM 5321 OWO WAT w 41 76.393 45.904 49.422 1.00 17.54 o
ATOM 5322 OWO WAT w 42 85.206 62.816 45.996 1.00 17.54 o
ATOM 5323 OWO WAT w 43 76.471 47.028 47.000 1.00 17.44 o
ATOM 5324 OWO WAT w 44 0.832 14.465 10.111 1.00 17.68 o
ATOM 5325 OWO WAT w 45 17.126 39.270 29.347 1.00 17.51 o
ATOM 5326 OWO WAT w 46 73.780 40.503 57.255 1.00 17.25 o
ATOM 5327 OWO WAT w 47 21.723 18.784 14.274 1.00 17.45 o
ATOM 5328 OWO WAT w 48 77.775 46.337 41.963 1.00 17.43 o
ATOM 5329 OWO WAT w 49 74.042 51.423 47.868 1.00 17.43 o
ATOM 5330 OWO WAT w 50 5.173 19.793 21.019 1.00 16.93 o
ATOM 5331 OWO WAT w 51 23.296 13.219 28.911 1.00 17.88 o
ATOM 5332 OWO WAT w 52 68.576 33.406 53.686 1.00 17.34 o
ATOM 5333 OWO WAT w 53 79.676 60.534 56.642 1.00 17.94 o
ATOM 5334 OWO WAT w 54 20.966 12.588 25.236 1.00 17.68 o
ATOM 5335 OWO WAT w 55 79.455 46.852 58.012 1.00 18.46 o
ATOM 5336 OWO WAT w 56 21.961 22.672 13.906 1.00 18.30 o
ATOM 5337 OWO WAT w 57 23.164 37.315 22.948 1.00 18.83 o
ATOM 5338 OWO WAT w 58 27.796 21.790 29.543 1.00 19.01 o
ATOM 5339 OWO WAT w 59 21.970 7.754 18.732 1.00 17.60 o
ATOM 5340 OWO WAT w 60 86.215 67.889 25.424 1.00 18.90 o
ATOM 5341 OWO WAT w 61 74.166 48.563 46.894 1.00 17.91 o
ATOM 5342 OWO WAT w 62 78.589 52.339 52.824 1.00 18.37 o
ATOM 5343 OWO WAT w 63 82.800 44.837 37.893 1.00 18.85 o
ATOM 5344 OWO WAT w 64 92.766 63.033 31.253 1.00 19.30 o
ATOM 5345 OWO WAT w 65 76.648 25.143 57.923 1.00 18.49 o
ATOM 5346 OWO WAT w 66 13.779 11.916 23.075 1.00 18.38 o
ATOM 5347 OWO WAT w 67 83.618 43.219 39.903 1.00 18.64 o
ATOM 5348 OWO WAT w 68 10.042 17.714 26.131 1.00 18.79 o
ATOM 5349 OWO WAT w 69 8.435 26.201 11.599 1.00 18.52 o
ATOM 5350 OWO WAT w 70 77.564 31.577 41.883 1.00 18.71 o
ATOM 5351 OWO WAT w 71 5.877 20.685 29.317 1.00 18.50 o
ATOM 5352 OWO WAT w 72 86.752 52.258 72.789 1.00 18.85 o
ATOM 5353 OWO WAT w 73 20.904 8.069 26.108 1.00 18.78 o
ATOM 5354 OWO WAT w 74 22.378 10.212 25.677 1.00 19.26 o
ATOM 5355 OWO WAT w 75 77.680 35.889 38.422 1.00 18.55 o ATOM 5356 OWO WAT W 76 88.452 62.,598 22.,788 1.00 19.24 o
ATOM 5357 OWO WAT W 77 21.318 39. 505 23. ,558 1.00 19.73 o
ATOM 5358 OWO WAT W 78 14.011 32. ,525 2. ,931 1.00 18.99 o
ATOM 5359 OWO WAT W 79 78.129 62. ,243 54. ,938 1.00 18.80 o
ATOM 5360 OWO WAT W 80 0.014 29. ,221 6. ,595 1.00 20.44 o
ATOM 5361 OWO WAT W 81 23.996 15. .750 17. ,833 1.00 20.07 o
ATOM 5362 OWO WAT W 82 76.322 59. ,580 62. .028 1.00 18.85 o
ATOM 5363 OWO WAT W 83 72.629 47. ,922 53. ,167 1.00 19.93 o
ATOM 5364 OWO WAT W 84 79.463 28. ,268 40. ,776 1.00 19.66 o
ATOM 5365 OWO WAT W 85 74.825 46. ,354 29. ,274 1.00 19.67 o
ATOM 5366 OWO WAT W 86 70.232 52. ,683 31. ,008 1.00 19.14 o
ATOM 5367 OWO WAT W 87 5.443 16. ,610 15. ,882 1.00 20.49 o
ATOM 5368 OWO WAT W 88 74.886 27. ,202 58. .421 1.00 20.34 o
ATOM 5369 OWO WAT W 89 10.776 24. ,484 17. ,845 1.00 20.49 o
ATOM 5370 OWO WAT W 90 20.491 12. ,405 31. .298 1.00 19.76 o
ATOM 5371 OWO WAT W 91 17.200 40. ,737 14. .546 1.00 20.80 o
ATOM 5372 OWO WAT w 92 13.133 16. ,256 28. ,864 1.00 20.36 o
ATOM 5373 OWO WAT w 93 77.384 45. .372 30. .597 1.00 20.53 o
ATOM 5374 OWO WAT w 94 1.984 14. .905 18. .988 1.00 20.94 o
ATOM 5375 OWO WAT w 95 •14.038 26. .920 0. .625 1.00 20.67 o
ATOM 5376 OWO WAT w 96 -7.581 18. .636 28. ,025 1.00 20.23 o
ATOM 5377 OWO WAT w 97 67.099 43. .329 35. ,735 1.00 20.97 o
ATOM 5378 OWO WAT w 98 63.796 52. .216 39. ,947 1.00 21.26 o
ATOM 5379 OWO WAT w 99 16.979 6. ,692 21. ,514 1.00 20.30 o
ATOM 5380 OWO WAT w 100 88.035 52. .621 25. .577 1.00 20.12 o
ATOM 5381 OWO WAT w 101 6.531 19. .613 12. .905 1.00 21.09 o
ATOM 5382 OWO WAT w 102 74.606 41. .058 59. .683 1.00 20.58 o
ATOM 5383 OWO WAT w 103 86.280 57. .327 75. .910 1.00 20.45 o
ATOM 5384 OWO WAT w 104 85.786 61. .915 22. .821 1.00 20.13 o
ATOM 5385 OWO WAT w 105 20.695 42. .402 20. .167 1.00 21.81 o
ATOM 5386 OWO WAT w 106 87.016 65. .242 28. .514 1.00 21.68 o
ATOM 5387 OWO WAT w 107 5.790 14. .131 24. .305 1.00 20.94 o
ATOM 5388 OWO WAT w 108 73.679 27. .845 51. .659 1.00 20.35 o
ATOM 5389 OWO WAT w 109 71.431 41. .848 64. .176 1.00 20.97 o
ATOM 5390 OWO WAT w 110 76.779 46. .335 44. .417 1.00 20.12 o
ATOM 5391 OWO WAT w 111 82.550 47. .394 23. .709 1.00 21.31 o
ATOM 5392 OWO WAT w 112 ■14.734 32. .395 7. .536 1.00 22.16 o
ATOM 5393 OWO WAT w 113 24.029 10. .879 27. .547 1.00 21.29 o
ATOM 5394 OWO WAT w 114 76.023 62. .807 53. .231 1.00 21.31 o
ATOM 5395 OWO WAT w 115 8.897 11. .264 16. .028 1.00 22.17 o
ATOM 5396 OWO WAT w 116 66.003 32. .311 54. .132 1.00 20.55 o
ATOM 5397 OWO WAT w 117 69.194 33. .931 59. .941 1.00 21.61 o
ATOM 5398 OWO WAT w 118 83.824 28. .975 40. .950 1.00 21.84 o
ATOM 5399 OWO WAT w 119 72.876 46. .300 46. .114 1.00 21.25 o
ATOM 5400 OWO WAT w 120 86.864 59. .383 23, .726 1.00 21.02 o
ATOM 5401 OWO WAT w 121 ■15.572 25. .586 4, .811 1.00 21.90 o
ATOM 5402 OWO WAT w 122 8.301 14, .073 25, .474 1.00 21.23 o
ATOM 5403 OWO WAT w 123 87.698 51. .566 21, .397 1.00 21.20 o
ATOM 5404 OWO WAT w 124 -1.348 12. .529 23, .820 1.00 21.80 o
ATOM 5405 OWO WAT w 125 68.941 31. .017 57, .321 1.00 21.59 o
ATOM 5406 OWO WAT w 126 80.433 41. .114 34, .021 1.00 22.68 o
ATOM 5407 OWO WAT w 127 11.397 26, .193 11, .415 1.00 22.37 o
ATOM 5408 OWO WAT w 128 68.643 45, .302 45, .632 1.00 21.64 o
ATOM 5409 OWO WAT w 129 80.143 43, .408 40, .169 1.00 21.83 o
ATOM 5410 OWO WAT w 130 3.654 17, .397 22, .289 1.00 21.64 o
ATOM 5411 OWO WAT w 131 27.369 33, .046 23, .038 1.00 23.05 o
ATOM 5412 OWO WAT w 132 86.626 48, .296 26, .583 1.00 22.72 o
ATOM 5413 OWO WAT w 133 83.480 64, .481 44, .955 1.00 23.16 o
ATOM 5414 OWO WAT w 134 -8.973 16, .987 26, .256 1.00 23.30 o ATOM 5415 OWO WAT W 135 0.809 11.,826 1.,518 1.00 21..80 O
ATOM 5416 OWO WAT W 136 92.390 58. .996 64. ,959 1.00 23. .18 o
ATOM 5417 OWO WAT W 137 4.534 35. .854 7. ,060 1.00 22. .30 o
ATOM 5418 OWO WAT W 138 79.163 46. ,278 26. ,907 1.00 23. .33 o
ATOM 5419 OWO WAT W 139 0.694 7. ,404 19. ,192 1.00 22. .66 o
ATOM 5420 OWO WAT W 140 18.809 13. ,132 18. ,869 1.00 23. ,05 o
ATOM 5421 OWO WAT W 141 72.220 27. ,994 49. ,426 1.00 23. ,25 o
ATOM 5422 OWO WAT W 142 4.841 20. ,502 0. ,208 1.00 22. ,22 o
ATOM 5423 OWO WAT W 143 71.919 49. .722 30. ,760 1.00 22. ,99 o
ATOM 5424 OWO WAT W 144 12.098 11. .046 21. ,210 1.00 23. ,01 o
ATOM 5425 OWO WAT W 145 79.245 64. ,449 43. ,320 1.00 23. ,00 o
ATOM 5426 OWO WAT W 146 93.063 61. .183 67. ,355 1.00 22. .64 o
ATOM 5427 OWO WAT W 147 11.553 46. .298 24. .111 1.00 22. .04 o
ATOM 5428 OWO WAT W 148 82.911 39. .487 35. .756 1.00 22. .87 o
ATOM 5429 OWO WAT W 149 74.637 48. .588 49. .552 1.00 22. ,99 o
ATOM 5430 OWO WAT W 150 0.578 37. .358 8. .807 1.00 24. .31 o
ATOM 5431 OWO WAT w 151 82.019 64. ,007 42. .624 1.00 23. ,21 o
ATOM 5432 OWO WAT w 152 85.036 65. .669 35. .200 1.00 22. ,76 o
ATOM 5433 OWO WAT w 153 3.475 14. ,190 1. .312 1.00 24. ,09 o
ATOM 5434 OWO WAT w 154 83.528 40. ,660 39. .595 1.00 22. ,95 o
ATOM 5435 OWO WAT w 155 73.419 54. .004 55. .803 1.00 23. .90 o
ATOM 5436 OWO WAT w 156 20.863 38. .812 26. .443 1.00 22. .34 o
ATOM 5437 OWO WAT w 157 16.827 38. .006 33. ,689 1.00 22. ,92 o
ATOM 5438 OWO WAT w 158 74.104 31. .412 42. ,612 1.00 23. ,56 o
ATOM 5439 OWO WAT w 159 12.323 8. .383 20. ,449 1.00 23. ,19 o
ATOM 5440 OWO WAT w 160 21.369 35. .472 32. .065 1.00 24. .40 o
ATOM 5441 OWO WAT w 161 71.705 40. .995 66. .703 1.00 24. .45 o
ATOM 5442 OWO WAT w 162 -5.979 37. .842 28. .612 1.00 24. .65 o
ATOM 5443 OWO WAT w 163 72.046 44. .098 47. .546 1.00 23. .63 o
ATOM 5444 OWO WAT w 164 5.984 18. .873 17. .140 1.00 23. .83 o
ATOM 5445 OWO WAT w 165 70.903 29. .794 46. .355 1.00 23. .57 o
ATOM 5446 OWO WAT w 166 10.226 38. .929 28. .299 1.00 23. .19 o
ATOM 5447 OWO WAT w 167 81.774 28. .127 39. .317 1.00 23. .01 o
ATOM 5448 OWO WAT w 168 95.769 49, .468 36. .463 1.00 24. .35 o
ATOM 5449 OWO WAT w 169 ■14.213 24, .342 7. .233 1.00 23. .09 o
ATOM 5450 OWO WAT w 170 25.309 29. .408 17, .242 1.00 24. .67 o
ATOM 5451 OWO WAT w 171 7.199 37, .272 29. .329 1.00 23. .58 o
ATOM 5452 OWO WAT w 172 93.606 45, .696 34. .708 1.00 23, .69 o
ATOM 5453 OWO WAT w 173 7.433 18, .620 20. .711 1.00 24. .48 o
ATOM 5454 OWO WAT w 174 74.074 46, .632 51. .295 1.00 22. .55 o
ATOM 5455 OWO WAT w 175 91.787 49, .455 30. .732 1.00 23. .38 o
ATOM 5456 OWO WAT w 176 79.639 67, .570 27. .300 1.00 24. .62 o
ATOM 5457 OWO WAT w 177 7.342 19, .972 1. .553 1.00 23. .88 o
ATOM 5458 OWO WAT w 178 22.202 7, .130 28. .005 1.00 24. .13 o
ATOM 5459 OWO WAT w 179 83.838 26. .307 45. .281 1.00 23. .96 o
ATOM 5460 OWO WAT w 180 -6.270 12. .318 2, .985 1.00 24. .29 o
ATOM 5461 OWO WAT w 181 72.112 45. .217 50. .025 1.00 23. .42 o
ATOM 5462 OWO WAT w 182 -6.885 34, .340 12. .754 1.00 24, .84 o
ATOM 5463 OWO WAT w 183 14.139 6, .716 21. .899 1.00 24, .03 o
ATOM 5464 OWO WAT w 184 87.813 50, .090 24. .798 1.00 24, .38 o
ATOM 5465 OWO WAT w 185 81.933 66, .920 35. .565 1.00 24. .82 o
ATOM 5466 OWO WAT w 186 25.620 17, .202 21. .196 1.00 24. .48 o
ATOM 5467 OWO WAT w 187 86.075 49, .356 22, .479 1.00 24. .44 o
ATOM 5468 OWO WAT w 188 72.702 63, .321 49, .994 1.00 24. .35 o
ATOM 5469 OWO WAT w 189 81.920 57, .675 17, .338 1.00 24. .05 o
ATOM 5470 OWO WAT w 190 ■17.260 27, .155 6, .346 1.00 23. .60 o
ATOM 5471 OWO WAT w 191 -1.447 26, .525 44, .543 1.00 25. .86 o
ATOM 5472 OWO WAT w 192 87.376 41, .125 32, .826 1.00 25. .44 o
ATOM 5473 OWO WAT w 193 4.539 15, .379 17, .997 1.00 25. .59 o ATOM 5474 OWO WAT W 194 5.371 43.111 15.411 1.00 24.20 O
ATOM 5475 OWO WAT W 195 25.699 18.596 23.262 1.00 25.28 O
ATOM 5476 OWO WAT W 196 -8.314 37.998 17.944 1.00 24.46 O
ATOM 5477 OWO WAT W 197 73.193 40.020 62.202 1.00 24.69 O ATOM 5478 OWO WAT W 198 18.395 5.676 28.085 1.00 24.78 O
ATOM 5479 OWO WAT W 199 90.064 63.465 67.583 1.00 25.09 O
ATOM 5480 OWO WAT W 200 88.914 45.770 29.800 1.00 25.04 O
ATOM 5481 OWO WAT W 201 63.582 49.954 38.656 1.00 24.94 0
ATOM 5482 OWO WAT W 202 76.428 68.398 60.395 1.00 24.83 o ATOM 5483 OWO WAT W 203 91.288 61.774 28.305 1.00 24.77 o
ATOM 5484 OWO WAT W 204 -0.050 13.513 27.019 1.00 26.50 o
ATOM 5485 OWO WAT W 205 64.652 31.023 52.052 1.00 25.92 o
ATOM 5486 OWO WAT W 206 76.022 52.460 23.809 1.00 25.11 0
ATOM 5487 OWO WAT W 207 78.488 54.816 19.424 1.00 23.62 o ATOM 5488 OWO WAT W 208 81.501 43.128 29.272 1.00 25.00 o
ATOM 5489 OWO WAT W 209 16.543 48.590 19.406 1.00 25.78 o
ATOM 5490 OWO WAT W 210 -3.946 34.269 12.357 1.00 26.09 o
ATOM 5491 OWO WAT w 211 0.274 36.004 34.072 1.00 25.48 o
ATOM 5492 OWO WAT w 212 -2.700 42.880 11.941 1.00 25.30 o ATOM 5493 OWO WAT w 213 22.253 10.326 31.624 1.00 25.92 o
ATOM 5494 OWO WAT w 214 84.603 26.874 42.606 1.00 26.89 o
ATOM 5495 OWO WAT w 215 64.317 34.102 55.024 1.00 25.23 0
ATOM 5496 OWO WAT w 216 100.011 55.967 44.835 1.00 24.71 0
ATOM 5497 OWO WAT w 217 19.449 8.432 37.301 1.00 27.30 o ATOM 5498 OWO WAT w 218 23.712 9.203 23.629 1.00 25.71 o
ATOM 5499 OWO WAT w 219 16.643 5.516 31.940 1.00 26.43 o
ATOM 5500 OWO WAT w 220 26.369 14.624 18.707 1.00 26.31 0
ATOM 5501 OWO WAT w 221 94.635 61.074 30.648 1.00 27.32 o
ATOM 5502 OWO WAT w 222 66.778 30.489 55.915 1.00 25.29 o ATOM 5503 OWO WAT w 223 8.164 19.413 5.946 1.00 26.20 0
ATOM 5504 OWO WAT w 224 68.319 61.045 57.703 1.00 26.16 o
ATOM 5505 OWO WAT w 225 77.614 67.608 62.700 1.00 27.09 0
ATOM 5506 OWO WAT w 226 -13.213 23.887 21.011 1.00 25.97 o
ATOM 5507 OWO WAT w 227 81.456 70.408 58.740 1.00 26.11 0 ATOM 5508 OWO WAT w 228 -7.666 13.454 38.533 1.00 25.22 o
ATOM 5509 OWO WAT w 229 -12.884 34.121 8.799 1.00 26.58 o
ATOM 5510 OWO WAT w 230 -6.303 15.066 32.884 1.00 26.62 o
ATOM 5511 OWO WAT w 231 24.817 36.357 21.147 1.00 27.41 0
ATOM 5512 OWO WAT w 232 68.975 40.819 51.555 1.00 26.80 o ATOM 5513 OWO WAT w 233 62.632 37.812 50.828 1.00 25.32 o
ATOM 5514 OWO WAT w 234 95.525 42.626 57.196 1.00 26.53 o
ATOM 5515 OWO WAT w 235 8.338 47.544 8.902 1.00 27.70 o
ATOM 5516 OWO WAT w 236 -12.390 22.508 16.772 1.00 25.11 o
ATOM 5517 OWO WAT w 237 25.216 19.415 32.498 1.00 26.28 o ATOM 5518 OWO WAT w 238 92.994 63.579 33.943 1.00 26.27 0
ATOM 5519 OWO WAT w 239 -9.096 14.877 24.581 1.00 26.39 o
ATOM 5520 OWO WAT w 240 2.134 44.607 16.924 1.00 27.42 0
ATOM 5521 OWO WAT w 241 -14.304 21.455 6.854 1.00 28.45 o
ATOM 5522 OWO WAT w 242 -14.778 17.616 2.235 1.00 27.58 o ATOM 5523 OWO WAT w 243 66.731 32.731 60.491 1.00 26.64 o
ATOM 5524 OWO WAT w 244 90.919 46.924 31.342 1.00 27.52 0
ATOM 5525 OWO WAT w 245 92.157 28.892 53.486 1.00 25.99 0
ATOM 5526 OWO WAT w 246 71.890 56.261 26.053 1.00 26.43 • 0
ATOM 5527 OWO WAT w 247 83.746 35.879 35.372 1.00 27.14 o ATOM 5528 OWO WAT w 248 76.418 38.214 42.342 1.00 27.43 o
ATOM 5529 OWO WAT w 249 98.151 58.311 45.251 1.00 26.58 o
ATOM 5530 OWO WAT w 250 27.142 35.285 21.962 1.00 27.17 0
ATOM 5531 OWO WAT w 251 93.551 54.559 39.859 1.00 26.49 0
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ATOM 5710 OWO WAT W 430 96.611 39.539 56.194 1.00 32.67 O
ATOM 5711 OWO WAT W 431 83.825 71.440 51.248 1.00 34.89 O
ATOM 5712 OWO WAT W 432 63.076 53.522 44.892 1.00 32.71 O
ATOM 5713 OWO WAT W 433 1.793 39.751 32.248 1.00 31.74 0 ATOM 5714 OWO WAT W 434 7.509 15.071 20.571 1.00 32.45 0
ATOM 5715 OWO WAT W 435 87.907 67.566 34.260 1.00 32.31 0
ATOM 5716 OWO WAT W 436 73.062 34.735 66.838 1.00 33.20 o
ATOM 5717 OWO WAT W 437 9.377 24.058 1.441 1.00 31.00 o
ATOM 5718 OWO WAT W 438 71.507 59.603 32.113 1.00 33.60 o ATOM 5719 OWO WAT W 439 2.503 4.737 9.893 1.00 33.38 o
ATOM 5720 OWO WAT W 440 18.348 15.377 16.447 1.00 32.53 o
ATOM 5721 OWO WAT W 441 23.326 22.289 35.972 1.00 33.15 o
ATOM 5722 OWO WAT W 442 96.229 51.515 70.636 1.00 34.46 o
ATOM 5723 OWO WAT W 443 87.126 64.081 47.478 1.00 33.24 o ATOM 5724 OWO WAT W 444 2.034 19.051 -6.435 1.00 32.01 o
ATOM 5725 OWO WAT W 445 5.619 39.208 30.464 1.00 32.83 0
ATOM 5726 OWO WAT w 446 62.240 51.450 36.949 1.00 33.03 o
ATOM 5727 OWO WAT w 447 -6.360 35.580 35.084 1.00 32.64 o
ATOM 5728 OWO WAT w 448 -16.362 24.399 13.206 1.00 32.67 o ATOM 5729 OWO WAT w 449 -4.304 43.530 13.748 1.00 34.24 o
ATOM 5730 OWO WAT w 450 73.798 51.681 25.011 1.00 30.52 o
ATOM 5731 OWO WAT w 451 -14.918 12.722 35.144 1.00 32.68 o
ATOM 5732 OWO WAT w 452 85.074 65.041 49.650 1.00 34.07 o
ATOM 5733 OWO WAT w 453 -11.926 28.889 39.111 1.00 34.00 o ATOM 5734 OWO WAT w 454 96.844 56.355 64.597 1.00 31.66 o
ATOM 5735 OWO WAT w 455 96.000 55.934 36.767 1.00 34.06 o
ATOM 5736 OWO WAT w 456 71.256 69.262 41.963 1.00 31.80 o
ATOM 5737 OWO WAT w 457 3.783 33.221 3.346 1.00 34.65 0
ATOM 5738 OWO WAT w 458 84.579 31.320 65.966 1.00 33.69 0 ATOM 5739 OWO WAT w 459 101.511 33.113 49.526 1.00 32.83 o
ATOM 5740 OWO WAT w 460 95.878 33.666 64.881 1.00 33.85 o
ATOM 5741 OWO WAT w 461 67.042 56.019 46.154 1.00 31.64 o
ATOM 5742 OWO WAT w 462 22.413 30.668 10.728 1.00 33.39 o
ATOM 5743 OWO WAT w 463 -9.497 10.447 8.753 1.00 35.70 0 ATOM 5744 OWO WAT w 464 14.729 20.358 11.887 1.00 33.61 o
ATOM 5745 OWO WAT w 465 92.689 63.328 63.676 1.00 31.71 o
ATOM 5746 OWO WAT w 466 15.981 43.467 27.839 1.00 30.27 o
ATOM 5747 OWO WAT w 467 16.882 39.161 12.466 1.00 33.44 o
ATOM 5748 OWO WAT w 468 28.031 22.957 32.264 1.00 32.89 o ATOM 5749 OWO WAT w 469 -6.646 34.418 -1.404 1.00 36.83 o
ATOM 5750 OWO WAT w 470 -13.840 28.684 27.438 1.00 34.43 0
ATOM 5751 OWO WAT w 471 -2.396 37.137 36.497 1.00 34.74 o
ATOM 5752 OWO WAT w 472 6.953 49.811 9.092 1.00 34.54 o
ATOM 5753 OWO WAT w 473 75.076 54.086 21.905 1.00 32.21 o ATOM 5754 OWO WAT w 474 20.045 28.872 34.962 1.00 34.48 o
ATOM 5755 OWO WAT w 475 100.497 60.231 49.583 1.00 33.76 o
ATOM 5756 OWO WAT w 476 66.281 28.570 48.683 1.00 33.64 o
ATOM 5757 OWO WAT w 477 68.813 29.894 59.688 1.00 31.09 0
ATOM 5758 OWO WAT w 478 10.065 47.685 22.178 1.00 33.96 o ATOM 5759 OWO WAT w 479 12.553 46.154 27.739 1.00 33.98 o
ATOM 5760 OWO WAT w 480 81.162 41.327 38.156 1.00 33.89 0
ATOM 5761 OWO WAT w 481 29.486 16.634 20.506 1.00 35.11 0
ATOM 5762 OWO WAT w 482 7.059 20.591 15.062 1.00 33.39 • 0
ATOM 5763 OWO WAT w 483 94.321 48.607 31.411 1.00 32.81 0 ATOM 5764 OWO WAT w 484 78.394 45.611 69.111 1.00 32.11 0
ATOM 5765 OWO WAT w 485 103.001 46.778 44.265 1.00 37.49 0
ATOM 5766 OWO WAT w 486 98.032 44.220 57.538 1.00 34.11 o
ATOM 5767 OWO WAT w 487 6.769 35.856 36.005 1.00 34.21 o
ATOM 5768 OWO WAT w 488 13.875 5.362 28.985 1.00 32.93 o O O O O O O O O O O O O O O O O O O O O O O O O d d d d d d d d d d d d O O O O O O O O d O d d d O O O O O d d O O
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ATOM 5887 OWO WAT W 607 87.521 28.175 42.171 1.00 37.58 0
ATOM 5888 OWO WAT W 608 71.639 50.540 23.811 1.00 38.19 0
ATOM 5889 OWO WAT W 609 103.850 43.189 44.252 1.00 39.03 0
ATOM 5890 OWO WAT W 610 79.919 66.791 18.426 1.00 41.53 O ATOM 5891 OWO WAT W 611 22.945 32.780 14.876 1.00 34.39 o
ATOM 5892 OWO WAT W 612 -6.425 36.916 12.432 1.00 35.27 o
ATOM 5893 OWO WAT W 613 103.393 36.820 51.468 1.00 38.09 o
ATOM 5894 OWO WAT W 614 84.674 36.411 69.979 1.00 36.89 o
ATOM 5895 OWO WAT W 615 71.088 52.342 54.383 1.00 43.94 o ATOM 5896 OWO WAT W 616 81.351 67.541 24.003 1.00 35.74 o
ATOM 5897 OWO WAT W 617 93.560 55.832 22.511 1.00 50.17 o
ATOM 5898 OWO WAT W 618 84.136 69.091 49.838 1.00 41.33 o
ATOM 5899 OWO WAT W 619 64.940 49.108 48.394 1.00 37.74 0
ATOM 5900 OWO WAT W 620 2.665 46.841 14.692 1.00 39.07 o ATOM 5901 OWO WAT W 621 99.738 60.325 45.893 1.00 36.08 o
ATOM 5902 OWO WAT W 622 86.148 29.099 38.975 1.00 34.64 o
ATOM 5903 OWO WAT w 623 -2.502 13.269 26.328 1.00 36.55 o
ATOM 5904 OWO WAT w 624 88.662 27.282 61.964 1.00 41.22 o
ATOM 5905 OWO WAT w 625 14.262 15.472 7.561 1.00 37.33 o ATOM 5906 OWO WAT w 626 65.127 51.794 48.053 1.00 40.14 0
ATOM 5907 OWO WAT w 627 93.290 67.912 55.616 1.00 39.49 o
ATOM 5908 OWO WAT w 628 -3.988 9.437 35.385 1.00 40.11 0
ATOM 5909 OWO WAT w 629 92.772 43.143 30.995 1.00 40.79 o
ATOM 5910 OWO WAT w 630 73.931 63.142 17.034 1.00 34.53 o ATOM 5911 OWO WAT w 631 20.339 39.005 11.660 1.00 42.20 0
ATOM 5912 OWO WAT w 632 4.096 21.094 45.525 1.00 31.66 0
ATOM 5913 OWO WAT w 633 -1.502 7.283 16.652 1.00 41.72 o
ATOM 5914 OWO WAT w 634 23.127 12.995 37.830 1.00 35.93 0
ATOM 5915 OWO WAT w 635 20.482 6.101 32.242 1.00 38.43 o ATOM 5916 OWO WAT w 636 105.998 50.158 46.365 1.00 43.98 o
ATOM 5917 OWO WAT w 637 97.647 61.168 54.360 1.00 41.64 o
ATOM 5918 OWO WAT w 638 31.773 17.209 19.642 1.00 43.04 o
ATOM 5919 OWO WAT w 639 95.597 47.557 33.970 1.00 39.95 0
ATOM 5920 OWO WAT w 640 86.892 46.712 76.072 1.00 40.36 o ATOM 5921 OWO WAT w 641 15.550 35.912 6.020 1.00 36.75 0
ATOM 5922 OWO WAT w 642 -15.301 21.138 -4.031 1.00 38.85 o
ATOM 5923 OWO WAT w 643 -9.762 25.136 39.215 1.00 41.44 0
ATOM 5924 OWO WAT w 644 90.558 58.656 75.134 1.00 46.13 0
ATOM 5925 OWO WAT w 645 66.247 46.236 62.249 1.00 39.42 o ATOM 5926 OWO WAT w 646 71.142 40.474 40.944 1.00 36.49 o
ATOM 5927 OWO WAT w 647 77.446 48.504 23.425 1.00 38.60 o
ATOM 5928 OWO WAT w 648 104.114 48.119 59.318 1.00 37.83 0
ATOM 5929 OWO WAT w 649 101.742 43.229 56.344 1.00 38.57 o
ATOM 5930 OWO WAT w 650 -15.216 26.550 18.282 1.00 41.02 o ATOM 5931 OWO WAT w 651 81.533 73.256 58.329 1.00 43.24 0
ATOM 5932 OWO WAT w 652 95.421 27.742 50.189 1.00 36.56 0
ATOM 5933 OWO WAT w 653 66.407 63.471 57.158 1.00 40.06 0
ATOM 5934 OWO WAT w 654 95.111 62.749 63.048 1.00 44.41 o
ATOM 5935 OWO WAT w 655 74.563 73.382 48.784 1.00 38.15 0 ATOM 5936 OWO WAT w 656 100.257 49.012 62.406 1.00 38.80 0
ATOM 5937 OWO WAT w 657 70.436 27.659 60.745 1.00 40.98 0
ATOM 5938 OWO WAT w 658 61.433 39.445 63.329 1.00 37.65 o
ATOM 5939 OWO WAT w 659 70.260 64.484 61.726 1.00 36.07 ' 0
ATOM 5940 OWO WAT w 660 -2.658 11.192 37.261 1.00 41.10 o ATOM 5941 OWO WAT w 661 20.907 40.221 15.814 1.00 42.41 o
ATOM 5942 OWO WAT w 662 70.216 52.007 62.455 1.00 42.64 o
ATOM 5943 OWO WAT w 663 95.740 46.358 66.747 1.00 40.91 0
ATOM 5944 OWO WAT w 664 10.857 34.594 38.679 1.00 36.48 0
ATOM 5945 OWO WAT w 665 -6.107 5.304 14.570 1.00 39.62 0 ooooooooooodoooooooooooooooooooooooooooooooodooooddooooooo
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ON
Ov o
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19C1
ATOM 6005 OWO WAT W 725 -12.304 5.241 21.205 1.00 42.82 o
ATOM 6006 OWO WAT W 726 31.924 25.055 26.803 1.00 43.20 0
ATOM 6007 OWO WAT W 727 18.724 23.829 42.625 1.00 38.81 o
ATOM 6008 OWO WAT W 728 -15.918 22.825 4.228 1.00 42.40 o ATOM 6009 OWO WAT W 729 29.725 32.703 23.905 1.00 41.71 o
ATOM 6010 OWO WAT W 730 70.143 50.223 57.006 1.00 40.87 o
ATOM 6011 OWO WAT W 731 20.042 34.462 8.889 1.00 42.39 o
ATOM 6012 OWO WAT W 732 101.912 41.183 29.473 1.00 44.98 o
ATOM 6013 OWO WAT W 733 70.685 57.140 59.173 1.00 45.13 o ATOM 6014 OWO WAT W 734 31.199 27.580 14.855 1.00 42.48 o
ATOM 6015 OWO WAT W 735 -8.718 8.222 9.842 1.00 38.68 o
ATOM 6016 OWO WAT W 736 20.384 26.278 40.423 1.00 47.84 o
ATOM 6017 OWO WAT W 737 78.929 66.905 45.969 1.00 40.33 0
ATOM 6018 OWO WAT W 738 72.878 40.783 38.029 1.00 37.88 0 ATOM 6019 OWO WAT W 739 -17.127 11.555 34.870 1.00 45.57 0
ATOM 6020 OWO WAT W 740 72.198 61.923 33.145 1.00 38.23 0
ATOM 6021 OWO WAT w 741 74.361 48.471 69.557 1.00 46.46 0
ATOM 6022 OWO WAT w 742 70.838 21.961 53.843 1.00 38.46 0
ATOM 6023 OWO WAT w 743 71.920 73.260 47.796 1.00 34.51 0 ATOM 6024 OWO WAT w 744 -6.649 30.436 43.185 1.00 41.17 o
ATOM 6025 OWO WAT w 745 12.073 41.176 33.835 1.00 37.25 o
ATOM 6026 OWO WAT w 746 3.772 39.827 28.311 1.00 37.06 o
ATOM 6027 OWO WAT w 747 83.695 22.688 57.551 1.00 44.64 o
ATOM 6028 OWO WAT w 748 78.868 70.209 60.269 1.00 41.47 0 ATOM 6029 OWO WAT w 749 2.681 11.135 29.107 1.00 45.78 o
ATOM 6030 OWO WAT w 750 -3.851 36.672 12.548 1.00 37.71 o
ATOM 6031 OWO WAT w 751 -5.580 38.158 34.749 1.00 41.72 o
ATOM 6032 OWO WAT w 752 -12.061 14.443 -4.143 1.00 44.23 o
ATOM 6033 OWO WAT w 753 74.848 71.019 57.494 1.00 39.65 o ATOM 6034 OWO WAT w 754 30.226 11.993 24.909 1.00 39.53 0
ATOM 6035 OWO WAT w 755 93.979 60.877 42.464 1.00 42.70 0
ATOM 6036 OWO WAT w 756 100.237 56.962 53.576 1.00 47.39 0
ATOM 6037 OWO WAT w 757 -13.131 14.248 -6.671 1.00 46.71 0
ATOM 6038 OWO WAT w 758 108.902 46.661 31.726 1.00 39.82 o ATOM 6039 OWO WAT w 759 12.306 29.385 6.036 1.00 39.68 o
ATOM 6040 OWO WAT w 760 -4.770 13.938 -5.501 1.00 42.83 o
ATOM 6041 OWO WAT w 761 71.964 54.065 57.950 1.00 55.02 0
ATOM 6042 OWO WAT w 762 69.804 56.288 28.236 1.00 51.12 0
ATOM 6043 OWO WAT w 763 72.043 64.834 22.297 1.00 38.68 o ATOM 6044 OWO WAT w 764 69.376 47.883 61.076 1.00 40.50 0
ATOM 6045 OWO WAT w 765 -10.414 39.373 22.827 1.00 49.80 o
ATOM 6046 OWO WAT w 766 71.511 56.324 65.919 1.00 48.05 o
ATOM 6047 OWO WAT w 767 76.124 53.448 72.761 1.00 37.85 0
ATOM 6048 OWO WAT w 768 10.346 15.094 16.176 1.00 45.99 0 ATOM 6049 OWO WAT w 769 15.803 34.194 3.861 1.00 49.50 0
ATOM 6050 OWO WAT w 770 -17.712 26.632 -2.259 1.00 45.78 o
ATOM 6051 OWO WAT w 771 -2.116 9.781 29.937 1.00 45.05 o
ATOM 6052 OWO WAT w 772 6.585 5.057 17.549 1.00 50.86 0
ATOM 6053 OWO WAT w 773 0.254 30.093 -3.787 1.00 50.11 0 ATOM 6054 OWO WAT w 774 4.530 14.340 42.939 1.00 51.12 0
ATOM 6055 OWO WAT w 775 86.938 69.887 53.752 1.00 49.90 o
ATOM 6056 OWO WAT w 776 67.819 39.098 38.776 1.00 44.79 o
ATOM 6057 OWO WAT w 777 92.894 39.175 30.950 1.00 47.99 'ϋ
ATOM 6058 OWO WAT w 778 -11.615 37.194 25.543 1.00 45.92 o ATOM 6059 OWO WAT w 779 13.548 43.187 32.985 1.00 48.99 o
ATOM 6060 OWO WAT w 780 -9.029 36.912 6.899 1.00 45.44 0
ATOM 6061 OWO WAT w 781 8.228 34.312 40.323 1.00 49.13 o
ATOM 6062 OWO WAT w 782 -7.639 39.531 26.233 1.00 42.83 0
ATOM 6063 OWO WAT w 783 103.282 53.320 41.696 1.00 39.23 o ATOM 6064 OWO WAT W 784 79.849 68.198 63.615 1.00 49.76 0
ATOM 6065 OWO WAT W 785 10.806 46.703 30.027 1.00 48.50 O
ATOM 6066 OWO WAT W 786 10.278 28.104 2.256 1.00 45.08 0
ATOM 6067 OWO WAT W 787 -12.731 22.003 19.395 1.00 50.84 0 ATOM 6068 OWO WAT W 788 11.556 51.442 15.949 1.00 55.13 O
ATOM 6069 OWO WAT W 789 18.137 17.684 15.574 1.00 54.06 O
ATOM 6070 OWO WAT W 790 16.007 38.138 37.419 1.00 37.69 O
ATOM 6071 OWO WAT W 791 107.269 39.366 40.596 1.00 42.10 O
ATOM 6072 OWO WAT W 792 92.138 28.005 42.151 1.00 47.51 O ATOM 6073 OWO WAT W 793 -15.958 20.134 34.862 1.00 50.35 O
ATOM 6074 OWO WAT W 794 105.554 44.211 46.382 1.00 43.27 O
ATOM 6075 OWO WAT W 795 70.984 24.764 48.554 1.00 45.16 O
ATOM 6076 OWO WAT W 796 -0.589 11.408 28.727 1.00 55.93 o
ATOM 6077 OWO WAT W 797 -8.325 13.863 0.933 1.00 37.99 o ATOM 6078 OWO WAT W 798 -13.851 31.784 20.354 1.00 39.81 o
ATOM 6079 OWO WAT W 799 77.983 26.725 66.736 1.00 42.60 0
ATOM 6080 OWO WAT w 800 -12.394 7.735 25.189 1.00 50.65 o
ATOM 6081 OWO WAT w 801 86.791 30.618 34.057 1.00 41.19 o
ATOM 6082 OWO WAT w 802 10.740 12.887 19.762 1.00 34.20 o ATOM 6083 OWO WAT w 803 4.597 12.434 38.677 1.00 44.86 0
ATOM 6084 OWO WAT w 804 65.489 50.372 52.067 1.00 45.48 o
ATOM 6085 OWO WAT w 805 75.557 75.724 47.677 1.00 44.91 0
ATOM 6086 OWO WAT w 806 99.252 56.498 61.878 1.00 45.48 0
ATOM 6087 OWO WAT w 807 22.230 33.247 12.252 1.00 45.16 o ATOM 6088 OWO WAT w 808 4.275 5.280 18.625 1.00 50.93 o
ATOM 6089 OWO WAT w 809 -2.790 38.549 3.137 1.00 48.40 0
ATOM 6090 OWO WAT w 810 82.611 31.253 67.441 1.00 55.10 0
ATOM 6091 OWO WAT w 811 60.665 49.734 46.321 1.00 40.99 o
ATOM 6092 OWO WAT w 812 3.154 9.852 31.212 1.00 51.47 0 ATOM 6093 OWO WAT w 813 2.709 29.749 -1.904 1.00 43.68 o
ATOM 6094 OWO WAT w 814 -1.134 36.876 4.079 1.00 42.69 o
ATOM 6095 OWO WAT w 815 67.768 52.395 54.902 1.00 47.66 o
ATOM 6096 OWO WAT w 816 64.711 32.171 65.883 1.00 37.49 o
ATOM 6097 OWO WAT w 817 75.140 18.625 52.961 1.00 43.29 o ATOM 6098 OWO WAT w 818 13.727 35.581 3.827 1.00 35.43 o
ATOM 6099 OWO WAT w 819 107.138 47.462 48.743 1.00 47.50 o
ATOM 6100 OWO WAT w 820 0.890 13.799 43.411 1.00 70.20 o
ATOM 6101 OWO WAT w 821 -17.909 22.541 28.674 1.00 45.25 o
ATOM 6102 OWO WAT w 822 62.987 48.439 32.191 1.00 49.64 o ATOM 6103 OWO WAT w 823 19.134 36.015 6.954 1.00 47.91 0
ATOM 6104 OWO WAT w 824 95.386 52.724 38.315 1.00 39.06 0
ATOM 6105 OWO WAT w 825 -4.894 43.275 26.604 1.00 38.70 o
ATOM 6106 OWO WAT w 826 70.867 34.003 44.766 1.00 37.40 o
ATOM 6107 OWO WAT w 827 73.436 69.331 51.280 1.00 49.45 0 ATOM 6108 OWO WAT w 828 86.534 44.038 26.647 1.00 35.57 o
ATOM 6109 OWO WAT w 829 70.185 51.742 58.933 1.00 48.32 o
ATOM 6110 OWO WAT w 830 80.291 69.174 49.279 1.00 52.56 0
ATOM 6111 OWO WAT w 831 70.714 71.457 45.425 1.00 37.69 0
ATOM 6112 OWO WAT w 832 71.705 69.101 39.220 1.00 49.67 o ATOM 6113 OWO WAT w 833 3.992 22.633 -2.782 1.00 51.36 0
ATOM 6114 OWO WAT w 834 67.983 57.801 57.503 1.00 40.80 o
ATOM 6115 OWO WAT w 835 80.669 39.481 72.617 1.00 48.51 0
ATOM 6116 OWO WAT w 836 68.686 48.728 55.013 1.00 55.84 ' o
ATOM 6117 OWO WAT w 837 12.458 16.480 15.148 1.00 40.89 o ATOM 6118 OWO WAT w 838 90.722 65.542 49.220 1.00 50.70 o
ATOM 6119 OWO WAT w 839 75.060 21.496 58.444 1.00 56.11 o
ATOM 6120 OWO WAT w 840 103.112 46.836 52.279 1.00 37.29 o
ATOM 6121 OWO WAT w 841 5.629 13.125 21.912 1.00 48.36 o
ATOM 6122 OWO WAT w 842 3.750 2.529 14.238 1.00 35.83 0 ATOM 6123 OWO WAT W 843 96.158 41.458 31.534 1.00 48.18 0
ATOM 6124 OWO WAT W 844 86.258 43.077 73.686 1.00 42.52 O
ATOM 6125 OWO WAT W 845 84.232 44.670 73.912 1.00 45.77 o
ATOM 6126 OWO WAT W 846 8.098 41.074 31.261 1.00 48.80 0 ATOM 6127 OWO WAT W 847 20.738 14.720 16.149 1.00 39.73 o
ATOM 6128 OWO WAT W 848 -2.346 44.407 25.480 1.00 49.90 o
ATOM 6129 OWO WAT W 849 -15.526 22.362 -6.197 1.00 44.31 o
ATOM 6130 OWO WAT W 850 89.590 64.098 46.869 1.00 56.09 0
ATOM 6131 OWO WAT W 851 -3.449 43.486 5.353 1.00 41.49 o ATOM 6132 OWO WAT W 852 68.901 52.226 68.217 1.00 44.27 o
ATOM 6133 OWO WAT W 853 98.320 50.981 30.117 1.00 46.85 0
ATOM 6134 OWO WAT W 854 70.073 58.300 64.610 1.00 44.99 0
ATOM 6135 OWO WAT W 855 4.624 47.036 1.440 1.00 42.81 o
ATOM 6136 OWO WAT W 856 87.815 67.533 49.547 1.00 48.12 o ATOM 6137 OWO WAT W 857 6.013 5.658 20.716 1.00 45.71 o
ATOM 6138 OWO WAT W 858 83.044 64.897 47.940 1.00 44.88 o
ATOM 6139 OWO WAT w 859 -4.280 42.843 9.627 1.00 47.04 o
ATOM 6140 OWO WAT w 860 97.665 48.641 62.942 1.00 47.67 o
ATOM 6141 OWO WAT w 861 85.390 70.389 57.138 1.00 39.39 o ATOM 6142 OWO WAT w 862 -24.321 19.975 24.770 1.00 55.66 o
ATOM 6143 OWO WAT w 863 106.910 40.893 42.688 1.00 46.05 o
ATOM 6144 OWO WAT w 864 23.971 35.886 30.562 1.00 50.30 0
ATOM 6145 OWO WAT w 865 88.613 34.316 71.466 1.00 52.11 o
ATOM 6146 OWO WAT w 866 78.329 44.285 72.155 1.00 47.56 0 ATOM 6147 OWO WAT w 867 5.442 10.717 28.127 1.00 57.69 o
ATOM 6148 OWO WAT w 868 4.909 23.695 -5.622 1.00 40.14 o
ATOM 6149 OWO WAT w 869 61.766 54.883 42.345 1.00 56.27 o
ATOM 6150 OWO WAT w 870 -15.697 18.900 -6.609 1.00 48.58 o
ATOM 6151 OWO WAT w 871 -1.994 38.190 34.240 1.00 40.58 o ATOM 6152 OWO WAT w 872 17.593 39.195 7.785 1.00 47.30 o
ATOM 6153 OWO WAT w 873 -6.929 8.637 30.485 1.00 48.70 o
ATOM 6154 OWO WAT w 874 -13.762 10.759 20.840 1.00 45.69 0
ATOM 6155 OWO WAT w 875 106.016 45.679 51.075 1.00 52.89 0
ATOM 6156 OWO WAT w 876 98.597 47.854 32.956 1.00 47.28 o ATOM 6157 OWO WAT w 877 -19.570 20.500 21.619 1.00 59.90 o
ATOM 6158 OWO WAT w 878 4.953 51.376 4.522 1.00 49.58 o
ATOM 6159 OWO WAT w 879 65.082 30.981 58.030 1.00 52.58 o
ATOM 6160 OWO WAT w 880 -4.570 45.999 8.945 1.00 47.97 o
ATOM 6161 OWO WAT w 881 71.448 72.042 52.347 1.00 48.22 o ATOM 6162 OWO WAT w 882 -5.192 37.121 9.739 1.00 52.84 o
ATOM 6163 OWO WAT w 883 22.418 42.988 17.741 1.00 51.35 o
ATOM 6164 OWO WAT w 884 1.325 32.956 0.433 1.00 51.82 o
ATOM 6165 OWO WAT w 885 26.545 39.446 15.718 1.00 58.29 o
ATOM 6166 OWO WAT w 886 20.591 28.184 37.538 1.00 44.12 0 ATOM 6167 OWO WAT w 887 61.327 62.516 49.641 1.00 53.61 0
ATOM 6168 OWO WAT w 888 18.556 37.697 46.622 1.00 40.96 o
ATOM 6169 OWO WAT w 889 67.601 59.213 44.343 1.00 55.82 o
ATOM 6170 OWO WAT w 890 6.062 6.589 3.745 1.00 49.33 o
ATOM 6171 OWO WAT w 891 30.616 25.513 17.869 1.00 41.76 o ATOM 6172 OWO WAT w 892 30.863 14.820 21.717 1.00 43.84 o
ATOM 6173 OWO WAT w 893 92.619 60.972 62.041 1.00 39.33 o
ATOM 6174 OWO WAT w 894 106.528 35.567 45.737 1.00 45.09 o
ATOM 6175 OWO WAT w 895 14.117 13.422 8.846 1.00 50.37 ' 0
ATOM 6176 OWO WAT w 896 -10.147 38.227 29.237 1.00 58.96 o ATOM 6177 OWO WAT w 897 97.900 38.773 30.904 1.00 50.37 o
ATOM 6178 OWO WAT w 898 -8.204 21.942 -12.704 1.00 59.84 0
ATOM 6179 OWO WAT w 899 -10.215 8.200 32.625 1.00 53.18 o
ATOM 6180 OWO WAT w 900 69.667 48.886 31.602 1.00 47.81 o
ATOM 6181 OWO WAT w 901 -7.032 38.633 30.903 1.00 55.74 0 APPENDIX 2
The structural coordinated of the three-dimensional structure of the Humicola inεolenε CelβA catalytic core domain The structural coordinates of the Humicola inεolenε Cel6A catalytic core domain as determined by X-ray crystallography. The format of the coordinates is the conventional Brookhaven Protein Data Bank (PDB) format. The residue numbering follows the sequence shown in appendix 2. Only the residues from G91 to F450 are detected in the X-ray structure.
ATOM 1 N GLY A 91 .828 21.757 9.329 1.00 27.61 N
ATOM 2 CA GLY A 91 .961 20.868 8.549 1.00 26.62 C
ATOM 3 C GLY A 91 .950 19.476 9.174 1.00 23. .16 C
ATOM 4 O GLY A 91 .477 18.537 8.545 1.00 27..18 O
ATOM 5 N ASN A 92 .449 19.342 10.398 1.00 20.23 N
ATOM 6 CA ASN A 92 .426 18.015 11.044 1.00 18.66 C
ATOM 7 C ASN A 92 .990 17.624 11.337 1.00 16.69 C
ATOM 8 O ASN A 92 7.352 18.239 12.192 1 .00 13.84 0
ATOM 9 CB ASN A 92 10.249 18.108 12.329 1, .00 16.13 C
ATOM 10 CG ASN A 92 10.331 16.807 13.101 1, 00 16.07 C
ATOM 11 ODl ASN A 92 9.705 15.808 12.762 1, 00 13.45 O
ATOM 12 ND2 ASN A 92 11.109 16.810 14.174 1, 00 13.31 N
ATOM 13 N PRO A 93 7.470 16.551 10.744 1, 00 15.88 N
ATOM 14 CA PRO A 93 .110 16.099 10.975 1, 00 14.91 C
ATOM 15 C PRO A 93 .783 15.665 12.389 1 00 13.63 C
ATOM 16 O PRO A 93 .608 15.589 12.779 1 00 11.92 O
ATOM 17 CB PRO A 93 .925 14.918 10.014 1 00 15.68 C
ATOM 18 CG PRO A 93 .299 14.505 ,624 1 00 16.21 C
ATOM 19 CD PRO A 93 .179 15.720 .735 1 00 14.29 C
ATOM 20 N PHE A 94 .803 15.345 13.194 1 00 9.81 N
ATOM 21 CA PHE A 94 .566 14.988 14.582 1 00 11.25 C
ATOM 22 C PHE A 94 .440 16.220 15.475 1 00 13.53 C
ATOM 23 O PHE A 94 .079 16.085 16.650 1 00 16.11 O
ATOM 24 CB PHE A 94 .728 14.116 15.085 1 00 8.75 c
ATOM 25 CG PHE A 94 .681 12.739 14.468 1 00 10.16 c
ATOM 26 CDl PHE A 94 8.194 12.506 13.205 1 00 9.57 c
ATOM 27 CD2 PHE A 94 7.103 11.697 15.167 1.00 9.98 c
ATOM 28 CE1 PHE A 94 8.132 11.225 12.652 1.00 9.81 c
ATOM 29 CE2 PHE A 94 7.042 10.427 14.625 1.00 11.75 c
ATOM 30 CZ PHE A 94 7.559 10.193 13.361 1.00 12.26 c
ATOM 31 N GLU A 95 6.817 17.388 15.001 1.00 15.32 N
ATOM 32 CA GLU A 95 6.781 18.611 15.804 1.00 16.74 C
ATOM 33 C GLU A 95 5..392 19.219 15.808 1.00 16.65 C
ATOM 34 O GLU A 95 4..738 19.314 14.770 .00 13. .35 o
ATOM 35 CB GLU A 95 7..823 19.604 15.275 .00 24. .87 c
ATOM 36 CG GLU A 95 7..847 20.963 15.949 .00 34. .84 c
ATOM 37 CD GLU A 95 9..003 21.854 15.527 .00 40. .67 c
ATOM 38 OE1 GLU A 95 9..824 21.487 14.651 .00 42. .82 o
ATOM 39 OE2 GLU A 95 9..122 22.978 16.072 .00 43. .58 0
ATOM 40 N GLY A 96 4..934 19.612 17.002 .00 17. .62 N
ATOM 41 CA GLY A 96 3..664 20.312 17.128 .00 17. .15 C
ATOM 42 C GLY A 96 2, .464 19.392 17.235 .00 17. .80 C
ATOM 43 O GLY A 96 1, .321 19.849 17.105 .00 17. .14 O
ATOM 44 N VAL A 97 2..699 18.090 17.418 .00 15. .31 N
ATOM 45 CA VAL A 97 1..610 17.136 17.562 .00 12, .55 C
ATOM 46 C VAL A 97 1..989 16.133 18.660 .00 14. .12 C
ATOM 47 0 VAL A 97 3.169 15.913 18.939 .00 14. .61 O
ATOM 48 CB VAL A 97 1.317 16.325 16.282 .0 000 14. .51 C
ATOM 49 CGI VAL A 97 0.777 17.184 15.144 .0000 11, .76 C
ATOM 50 CG2 VAL A 97 2.565 15.577 15.794 .00 13. .66 C
ATOM 51 N GLN A 98 0.972 15.501 19.217 .00 11. .88 N
ATOM 52 CA GLN A 98 1.109 14.391 20.127 .00 16, .04 C
ATOM 53 C GLN A 98 0.991 13.118 19.263 .00 15, .13 c ATOM 54 0 GLN A 98 0.281 13.150 18.250 1.00 14.70 o
ATOM 55 CB GLN A 98 -0. 026 14. 324 21. 147 1. 00 17. 18 C
ATOM 56 CG GLN A 98 -0. 175 15. 582 21. 987 1. 00 21. 23 C
ATOM 57 CD GLN A 98 -1. 140 15. 329 23. 137 1. 00 21. 79 c
ATOM 58 OE1 GLN A 98 -0. 836 14. 528 24. 018 1. 00 23. 39 o
ATOM 59 NE2 GLN A 98 -2. 269 16. 008 23. 088 1. 00 19. 82 N
ATOM 60 N LEU A 99 1. 685 12. 064 19. 647 1. 00 13. 40 N
ATOM 61 CA LEU A 99 1. 574 10. 809 18. 906 1. 00 12. 87 C
ATOM 62 C LEU A 99 0. 480 9. 966 19. 545 1. 00 12. 55 C
ATOM 63 0 LEU A 99 0. 562 9. 745 20. 743 1. 00 10. 08 0
ATOM 64 CB LEU A 99 2. 929 10. 095 18. 888 1. 00 10. 90 C
ATOM 65 CG LEU A 99 4. 041 10. 857 18. 146 1. 00 11. 33 C
ATOM 66 CDl LEU A 99 5. 370 10. 125 18. 219 1. ,00 10. 04 C
ATOM 67 CD2 LEU A 99 3. 650 11. 070 16. 683 1. 00 8. 20 C
ATOM 68 N TRP A 100 -0. 481 9. 486 18. 775 1. 00 9. 83 N
ATOM 69 CA TRP A 100 -1. 568 8. 666 19. 269 1. ,00 13. 08 C
ATOM 70 C TRP A 100 -1. 104 7. 307 19. 781 1. 00 11. 95 C
ATOM 71 0 TRP A 100 -0. 470 6. 523 19. 060 1. 00 11. 49 O
ATOM 72 CB TRP A 100 -2. 567 8. 424 18. 127 1. 00 12. 95 C
ATOM 73 CG TRP A 100 -3. 757 7. 579 18. 460 1. 00 12. 82 C
ATOM 74 CDl TRP A 100 -4. 004 6. 299 18. 079 1. 00 12. 80 C
ATOM 75 CD2 TRP A 100 -4. 887 7. 984 19. 253 1. 00 14. 62 C
ATOM 76 NE1 TRP A 100 -5. ,219 5. 878 18. 575 1. ,00 12. 79 N
ATOM 77 CE2 TRP A 100 -5. ,775 6. 896 19. 302 1. ,00 13. 02 C
ATOM 78 CE3 TRP A 100 -5. ,214 9. 169 19. 918 1. ,00 13. 29 C
ATOM 79 CZ2 TRP A 100 -6. ,986 6. .954 19. 999 1. ,00 15. .91 C
ATOM 80 CZ3 TRP A 100 -6. ,419 9. ,229 20. 607 1. .00 17. 23 C
ATOM 81 CH2 TRP A 100 -7. ,282 8. ,122 20. ,645 1. ,00 15. .85 C
ATOM 82 N ALA A 101 -1. .436 7. ,030 21. ,034 1. .00 12. ,27 N
ATOM 83 CA ALA A 101 -1. .158 5. ,728 21. .649 1. .00 12. ,90 C
ATOM 84 C ALA A 101 -2. .456 4. ,940 21. ,451 1. .00 12. ,69 C
ATOM 85 O ALA A 101 -3. .483 5. .283 22. .046 1. .00 12. ,00 O
ATOM 86 CB ALA A 101 -0. .806 5. .883 23. .117 1. .00 13. ,01 C
ATOM 87 N ASN A 102 -2. .445 3. ,939 20. .574 1. .00 12. ,63 N
ATOM 88 CA ASN A 102 -3. .655 3. ,221 20. .224 1. .00 13. .57 C
ATOM 89 C ASN A 102 -4. .229 2. .289 21. .272 1. .00 16. .03 C
ATOM 90 O ASN A 102 -3. .592 1. .764 22. .182 1. .00 13. .63 O
ATOM 91 CB ASN A 102 -3. .418 2. .495 18. .886 1. .00 14. .58 C
ATOM 92 CG ASN A 102 -2, .484 1. .298 19. .075 1. .00 14. .01 C
ATOM 93 ODl ASN A 102 -2, .947 0. .252 19. .508 1. .00 12. .96 O
ATOM 94 ND2 ASN A 102 -1, .211 1. .454 18. .763 1, .00 13. .58 N
ATOM 95 N ASN A 103 -5, .523 2. .011 21. .085 1, .00 16. .33 N
ATOM 96 CA ASN A 103 -6, .301 1, .175 21, .976 1. .00 17. .82 C
ATOM 97 C ASN A 103 -6 .027 -0, .306 21, .875 1, .00 17. .45 C
ATOM 98 O ASN A 103 -6 .278 -1, .017 22, .847 1. .00 13. .94 O
ATOM 99 CB ASN A 103 -7 .803 1, .460 21, .751 1 .00 24, .29 C
ATOM 100 CG ASN A 103 -8 .157 2, .779 22, .423 1 .00 31, .47 C
ATOM 101 ODl ASN A 103 -7 .659 3, .038 23 .526 1. .00 33, .49 O
ATOM 102 ND2 ASN A 103 -8 .974 3. .601 21. .771 1 .00 33, .07 N
ATOM 103 N TYR A 104 -5 .505 -0 .778 20 .744 1 .00 17, .87 N
ATOM 104 CA TYR A 104 -5 .194 -2 .202 20 .629 1 .00 18 .15 C
ATOM 105 C TYR A 104 -4 .025 -2 .552 21. .544 1 .00 15 .79 C
ATOM 106 0 TYR A 104 -4 .103 -3 .454 22 .386 1 .00 16 .76 0
ATOM 107 CB TYR A 104 -4 .931 -2 .573 19 .167 1 .00 19 .04 C
ATOM 108 CG TYR A 104 -4 .677 -4 .053 18 .973 1 .00 20 .66 C
ATOM 109 CDl TYR A 104 -5 .726 -4 .945 18 .794 1 .00 22 .58 C
ATOM 110 CD2 TYR A 104 -3 .388 -4 .549 18 .963 1 .00 21 .13 C
ATOM 111 CE1 TYR A 104 -5 .493 -6 .298 18 .619 1 .00 23 .34 C
ATOM 112 CE2 TYR A 104 -3 .139 -5 .900 18 .785 1 .00 21 .04 C
ATOM 113 CZ TYR A 104 -4 .193 -6 .764 18 .626 1 .00 21 .38 C
ATOM 114 OH TYR A 104 -3 .940 -8 .104 18 .442 1 .00 20 .27 0
ATOM 115 N TYR A 105 -2 .930 -1 .798 21 .435 1 .00 15 .57 N
ATOM 116 CA TYR A 105 -1 .762 -2 .036 22 .287 1 .00 14 .64 C
ATOM 117 C TYR A 105 -2 .128 -1 .770 23 .746 1 .00 13 .79 C
ATOM 118 0 TYR A 105 -1 .781 -2 .574 24 .612 1 .00 13 .07 0
ATOM 119 CB TYR A 105 -0 .574 -1 .185 21 .846 1 .00 12 .73 C
ATOM 120 CG TYR A 105 0 .710 -1 .527 22 .574 1 .00 14 .55 C
ATOM 121 CDl TYR A 105 1 .532 -2 .556 22 .138 1 .00 13 .48 C
ATOM 122 CD2 TYR A 105 1 .072 -0 .827 23 .720 1 .00 15 .08 C
ATOM 123 CE1 TYR A 105 2 .711 -2 .873 22 .816 1 .00 10 .63 C
ATOM 124 CE2 TYR A 105 2 .246 -1 .125 24 .390 1 .00 15 .04 C
ATOM 125 CZ TYR A 105 3 .054 -2 .142 23 .930 1 .00 14 .14 C ATOM 126 OH TYR A 105 4.207 -2.457 24.634 1.00 13.84 o
ATOM 127 N ARG A 106 2. 866 -0. 700 24. 025 1. 00 12. 63 N
ATOM 128 CA ARG A 106 3. 316 -0. 425 25. 390 1. 00 16. 09 C
ATOM 129 C ARG A 106 4. 035 -1. 622 26. 003 1. 00 17. 52 C
ATOM 130 0 ARG A 106 3. 702 -2. 067 27. 110 1. 00 16. 80 0
ATOM 131 CB ARG A 106 4. 249 0 797 25. 424 1. 00 14. 23 c
ATOM 132 CG ARG A 106 4. 567 1 195 26 865 1. 00 19 17 c
ATOM 133 CD ARG A 106 5. 415 2. 445 27. 013 1. 00 18. 85 c
ATOM 134 NE ARG A 106 4. 720 3. 667 26. 672 1. 00 18. 87 N
ATOM 135 CZ ARG A 106 4. 661 4. 258 25. 485 1. 00 23. 19 C
ATOM 136 NHl ARG A 106 5. 322 3 770 24. 449 1. 00 26. 18 N
ATOM 137 NH2 ARG A 106 3. 929 5. 358 25. 327 1. 00 25. 10 N
ATOM 138 N SER A 107 5. 012 -2 174 25. 288 1. 00 17. 36 N
ATOM 139 CA SER A 107 5. 770 -3 351 25 686 1 00 19 45 C
ATOM 140 C SER A 107 4. 936 -4 610 25 883 1 00 19 71 C
ATOM 141 0 SER A 107 5 137 -5 364 26 861 1 00 16 83 O
ATOM 142 CB SER A 107 6 855 -3 647 24 633 1 00 24 20 C
ATOM 143 OG SER A 107 7. 479 -4 899 24 916 1. 00 30. 43 O
ATOM 144 N GLU A 108 3. 953 -4 830 24 999 1 00 17 17 N
ATOM 145 CA GLU A 108 3. 051 -5 962 25 193 1 00 17 05 C
ATOM 146 C GLU A 108 2 347 -5 819 26 541 1 00 16 74 C
ATOM 147 0 GLU A 108 2 312 -6 777 27 306 1 00 20 10 0
ATOM 148 CB GLU A 108 1 994 -6 053 24 081 1 00 15 60 C
ATOM 149 CG GLU A 108 2 539 -6 470 22 728 1 00 15 75 C
ATOM 150 CD GLU A 108 1 473 -6 462 21 652 1 00 17 15 C
ATOM 151 OE1 GLU A 108 0 860 -5 401 21 385 1 00 16 01 O
ATOM 152 OE2 GLU A 108 1 262 -7 542 21 070 1 00 16 95 O
ATOM 153 N VAL A 109 1 800 -4 653 26 881 1 00 17 55 N
ATOM 154 CA VAL A 109 1 122 -4 525 28 167 1 00 17 37 C
ATOM 155 C VAL A 109 2 106 -4 680 29 328 1 00 18 11 C
ATOM 156 0 VAL A 109 1 852 -5 452 30 262 1 00 19 67 O
ATOM 157 CB VAL A 109 0 377 -3 185 28 317 1 00 17 76 C
ATOM 158 CGI VAL A 109 0 285 -3 119 29 683 1 00 17 70 C
ATOM 159 CG2 VAL A 109 0 660 -3 015 27 210 1 00 17 80 C
ATOM 160 N HIS A 110 3 209 -3 932 29 316 1 00 19 28 N
ATOM 161 CA HIS A 110 4 154 -4 021 30 427 1 00 22 54 C
ATOM 162 C HIS A 110 4 804 -5 379 30 605 1 00 24 72 C
ATOM 163 0 HIS A 110 4 922 -5 839 31 750 1 00 27 30 O
ATOM 164 CB HIS A 110 5 219 -2 911 30 361 1 00 21 81 C
ATOM 165 CG HIS A 110 4 646 -1 600 30 826 1 00 25 02 C
ATOM 166 ND1 HIS A 110 4 517 -1 286 32 161 1 00 25 96 N
ATOM 167 CD2 HIS A 110 4 116 -0 565 30 139 1 00 23 36 C
ATOM 168 CE1 HIS A 110 3 952 -0 097 32 277 1 00 27 07 C
ATOM 169 NE2 HIS A 110 3 707 0 362 31 063 1 00 25 46 N
ATOM 170 N THR A 111 5 230 -6 044 29 547 1 00 27 02 N
ATOM 171 CA THR A 111 5 941 -7 306 29 635 1 00 28 01 C
ATOM 172 C THR A 111 5 064 -8 547 29 590 1 00 29 56 C
ATOM 173 0 THR A 111 5 390 -9 550 30 237 1 00 27 25 O
ATOM 174 CB THR A 111 6 979 -7 396 28 490 1 00 28 98 C
ATOM 175 OGl THR A 111 7 849 -6 255 28 515 1 00 32 65 0
ATOM 176 CG2 THR A 111 7 817 -8 654 28 631 1 00 30 57 C
ATOM 177 N LEU A 112 3 959 -8 518 28 832 1 00 27 67 N
ATOM 178 CA LEU A 112 3 .106 -9 .700 28 766 1 00 26 67 C
ATOM 179 C LEU A 112 1 .926 -9 .674 29 718 1 00 26 00 C
ATOM 180 0 LEU A 112 1 .683 -10 .667 30 .417 1 00 27 .00 O
ATOM 181 CB LEU A 112 2 .640 -9 .915 27 .316 1 .00 26 .49 C
ATOM 182 CG LEU A 112 3 744 -9 881 26 262 1 00 26 08 C
ATOM 183 CDl LEU A 112 3 .188 -10 032 24 850 1 00 23 69 C
ATOM 184 CD2 LEU A 112 4 .775 -10 .977 26 .535 1 00 26 41 C
ATOM 185 N ALA A 113 1 .220 -8 .559 29 836 1 00 25 .53 N
ATOM 186 CA ALA A 113 0 .018 -8 .486 30 .657 1 .00 24 .31 C
ATOM 187 C ALA A 113 -0 .191 -8 .212 32 .139 1 .00 23 .97 C
ATOM 188 0 ALA A 113 0 .260 -8 .970 33 .009 1 .00 22 .26 O
ATOM 189 CB ALA A 113 0 .899 -7 .392 30 .084 1 .00 23 .61 C
ATOM 190 N ILE A 114 -0 .831 -7 .080 32 .461 1 .00 22 .40 N
ATOM 191 CA ILE A 114 -0 .940 -6 .637 33 .839 1 .00 23 .74 C
ATOM 192 C ILE A 114 ■1 .503 -7 .677 34 .785 1 .00 26 .57 C
ATOM 193 0 ILE A 114 -0 .851 -7 .946 35 .798 1 .00 25 .46 O
ATOM 194 CB ILE A 114 -1 .633 -5 .278 33 .976 1 .00 21 .40 C
ATOM 195 CGI ILE A 114 -0 .711 -4 .203 33 .390 1 .00 16 .26 C
ATOM 196 CG2 ILE A 114 -1 .961 -4 .951 35 .430 1 .00 19 .78 c
ATOM 197 CDl ILE A 114 -1 .313 -2 .817 33 .321 1 .00 21 .39 c ATOM 198 N PRO A 115 2.603 -8.340 34.475 1.00 30.09 N
ATOM 199 CA PRO A 115 3. 163 -9. 372 35. 330 1. 00 34. 92 C
ATOM 200 C PRO A 115 2. 175 -10. 418 35. 811 1. 00 40. 86 C
ATOM 201 0 PRO A 115 2. 276 -10. 899 36. 945 1. 00 41. 94 O
ATOM 202 CB PRO A 115 4. 255 -9. 993 34. 464 1. 00 34. 42 C
ATOM 203 CG PRO A 115 4. 684 -8. 899 33. 548 1. 00 32. 96 C
ATOM 204 CD PRO A 115 3. 440 -8. 094 33. 276 1. 00 30. 71 C
ATOM 205 N GLN A 116 1. 190 -10. 794 35. 004 1. 00 45. 84 N TOM 206 CA GLN A 116 0. 168 -11. 761 35. 330 1. 00 49. 55 C
ATOM 207 C GLN A 116 1. 065 -11. 195 36. 022 1. 00 50. 64 C
ATOM 208 0 GLN A 116 1. 982 -11. 971 36. 327 1. 00 52. 61 O
ATOM 209 CB GLN A 116 0. 321 -12. 436 34. 038 1. 00 53. .69 C
ATOM 210 CG GLN A 116 0. .768 -12. 787 33. 044 1. 00 56. .00 C
ATOM 211 CD GLN A 116 •1. .650 -13. 931 33. 495 1. 00 59. .17 C
ATOM 212 OE1 GLN A 116 2. ,844 -13. 948 33. 177 1. 00 60. ,02 O
ATOM 213 NE2 GLN A 116 1. .079 -14. .893 34. .218 1. 00 58. .44 N
ATOM 214 N ILE A 117 1. 153 -9. 895 36. 263 1. 00 49. 79 N
ATOM 215 CA ILE A 117 2. 359 -9. 340 36. 897 1. 00 48. 90 C
ATOM 216 C ILE A 117 2. 173 -9. 200 38. 403 1. 00 48. 85 C
ATOM 217 0 ILE A 117 1. .240 -8. 546 38. 878 1. 00 47. .80 O
ATOM 218 CB ILE A 117 2. .707 -7. .969 36. 257 1. 00 48. .99 C
ATOM 219 CGI ILE A 117 3. .093 -8. .201 34. .774 1. 00 49. ,40 C
ATOM 220 CG2 ILE A 117 3. ,925 -7. ,366 36. ,972 1. 00 49. ,20 C
ATOM 221 CDl ILE A 117 3. ,081 -6. ,933 33. .936 1. 00 49. ,29 C
ATOM 222 N THR A 118 3. ,081 -9. ,830 39. .155 1. 00 46. ,94 N
ATOM 223 CA THR A 118 2. .965 -9. ,779 40. ,610 1. 00 45. ,80 C
ATOM 224 C THR A 118 3. .655 -8. .550 41. ,170 1. 00 45. ,43 C
ATOM 225 O THR A 118 3. .100 -7. .895 42. ,047 1. .00 46. .96 O
ATOM 226 CB THR A 118 3. .428 -11. .069 41. .317 1. ,00 46. .82 C
ATOM 227 OGl THR A 118 4. .776 -11. .411 41. .099 1. ,00 46. .50 O
ATOM 228 CG2 THR A 118 2. .577 -12. .229 40. .772 1. ,00 44. .46 C
ATOM 229 N ASP A 119 4. .845 -8. .222 40. .697 1. .00 44. .01 N
ATOM 230 CA ASP A 119 5. .550 -7. .055 41. .219 1. ,00 43. .17 C
ATOM 231 C ASP A 119 4. .710 -5. .802 41. .052 1. .00 41. .01 C
ATOM 232 O ASP A 119 4. .392 -5. .416 39. .925 1. ,00 39. .94 O
ATOM 233 CB ASP A 119 6. .870 -6. .900 40. .457 1. ,00 46. .99 C
ATOM 234 CG ASP A 119 7, .907 -6. .098 41. .205 1. .00 49. .42 C
ATOM 235 ODl ASP A 119 7, .579 -5. .155 41. .952 1. .00 52. .21 O
ATOM 236 OD2 ASP A 119 9, .104 -6. .434 41. .035 1. .00 51. .58 O
ATOM 237 N PRO A 120 4, .452 -5, .090 42. .142 1. .00 39. .04 N
ATOM 238 CA PRO A 120 3, .724 -3, .834 42. .086 1. .00 36. .91 C
ATOM 239 C PRO A 120 4. .446 -2, .802 41. .227 1. .00 35. .45 C
ATOM 240 0 PRO A 120 3, .810 -2, .032 40. .508 1. .00 33. .13 O
ATOM 241 CB PRO A 120 3. .592 -3, .389 43, .528 1. .00 37, .45 C
ATOM 242 CG PRO A 120 4 .443 -4, .278 44. .352 1. .00 37, .57 C
ATOM 243 CD PRO A 120 .841 -5, .463 43. .521 1, .00 38, .90 C
ATOM 244 N ALA A 121 5 .770 -2, .776 41, .298 1, .00 34, .03 N
ATOM 245 CA ALA A 121 6 .612 -1 .876 40, .528 1, .00 32. .17 C
ATOM 246 C ALA A 121 6 .511 -2. .197 39, .042 1, .00 29 .70 C
ATOM 247 0 ALA A 121 6 .338 -1 .288 38. .233 1, .00 31 .94 O
ATOM 248 CB ALA A 121 8 .068 -1 .972 40 .969 1, .00 34 .01 C
ATOM 249 N LEU A 122 6 .548 -3 .480 38 .683 1. .00 26 .92 N
ATOM 250 CA LEU A 122 6 .351 -3 .864 37 .296 1. .00 26 .18 C
ATOM 251 C LEU A 122 4 .944 -3 .511 36 .812 1. .00 25 .84 C
ATOM 252 0 LEU A 122 4 .805 -3 .163 35 .634 1 .00 21 .96 O
ATOM 253 CB LEU A 122 6 .640 -5 .336 37 .038 1 .00 26 .91 C
ATOM 254 CG LEU A 122 8 .108 -5 .769 37 .001 1 .00 27 .40 C
ATOM 255 CDl LEU A 122 8 .189 -7 .241 36 .625 1 .00 29 .77 C
ATOM 256 CD2 LEU A 122 8 .910 -4 .923 36 .020 1 .00 28 .91 C
ATOM 257 N ARG A 123 3 .923 -3 .611 37 .671 1 .00 23 .27 N
ATOM 258 CA ARG A 123 2 .574 -3 .278 37 .254 1 .00 23 .17 C
ATOM 259 C ARG A 123 2 .428 -1 .802 36 .911 1 .00 22 .59 C
ATOM 260 0 ARG A 123 1 .844 -1 .448 35 .887 1 .00 21 .89 O
ATOM 261 CB ARG A 123 1 .522 -3 .583 38 .319 1 .00 22 .73 C
ATOM 262 CG ARG A 123 1 .114 -5 .044 38 .379 1 .00 24 .61 C
ATOM 263 CD ARG A 123 -0 .281 -5 .084 39 .056 1 .00 21 .93 C
ATOM 264 NE ARG A 123 -0 .674 -6 .472 39 .087 1 .00 22 .49 N
ATOM 265 CZ ARG A 123 -1 .896 -6 .959 38 .970 1 .00 21 .33 C
ATOM 266 NHl ARG A 123 -2 .921 -6 .135 38 .827 1 .00 17 .12 N
ATOM 267 NH2 ARG A 123 -1 .990 -8 .282 39 .016 1 .00 23 .60 N
ATOM 268 N ALA A 124 2 .932 -0 .947 37 .801 1 .00 22 .35 N
ATOM 269 CA ALA A 124 2 .879 0 .486 37 .574 1 .00 22 .62 C ATOM 270 C ALA A 124 3.631 0..867 36.,293 1..00 22.,96 c
ATOM 271 O ALA A 124 3. .219 1. .765 35. ,557 1. ,00 22. ,62 o
ATOM 272 CB ALA A 124 3. .479 1. ,237 38. .766 1. ,00 25. .24 c
ATOM 273 N ALA A 125 4. .744 0. .194 36. .020 1. .00 21. .29 N
ATOM 274 CA ALA A 125 5. ,526 0. .460 34. .821 1. .00 22. .37 C
ATOM 275 C ALA A 125 4. ,780 -0. ,052 33. .594 1. .00 21. .22 c
ATOM 276 O ALA A 125 4. ,739 0. ,642 32. .568 1. .00 20. .55 0
ATOM 277 CB ALA A 125 6. 917 -0. .142 34. ,974 1. .00 21. ,61 c
ATOM 278 N ALA A 126 4. ,072 -1. ,174 33. ,716 1. .00 16. ,70 N
ATOM 279 CA ALA A 126 3. ,285 -1. ,695 32. .600 1. .00 16. .03 C
ATOM 280 C ALA A 126 2. ,168 -0. ,718 32. .228 1. ,00 16. .88 C
ATOM 281 0 ALA A 126 1. ,894 -0. ,493 31. ,048 1. .00 14. ,78 O
ATOM 282 CB ALA A 126 2. ,685 -3. ,048 32. .933 1. ,00 13. .36 C
ATOM 283 N SER A 127 1. .521 -0. .113 33. .226 1. ,00 16. .69 N
ATOM 284 CA SER A 127 0. .485 0. .884 32. ,968 1. ,00 18. ,32 C
ATOM 285 C SER A 127 1. ,084 2. ,042 32. ,171 1. ,00 16. ,53 C
ATOM 286 O SER A 127 0. .373 2. ,585 31. .322 1. .00 18. ,15 O
ATOM 287 CB SER A 127 0. .188 1. .369 34. .261 1. .00 22. .44 C
ATOM 288 OG . ASER A 127 0. ,899 0. ,330 34. ,893 0. ,50 29. ,80 O
ATOM 2830 OG BSER A 127 ■1. .331 2. ,154 33. ,971 0. ,50 21. ,53 O
ATOM 289 N ALA A 128 2. .294 2. .473 32. .496 1. .00 13. .16 N
ATOM 290 CA ALA A 128 2. ,912 3. ,582 31. ,783 1. .00 12. ,91 C
ATOM 291 C ALA A 128 3. .262 3. ,233 30. ,340 1. .00 13. ,03 c
ATOM 292 O ALA A 128 3. .021 4. .030 29. .407 1. ,00 12, .54 0
ATOM 293 CB ALA A 128 4. .130 4. .062 32. .554 1. .00 13, .61 c
ATOM 294 N VAL A 129 3. .801 2. ,045 30. .104 1. ,00 12. ,24 N
ATOM 295 CA VAL A 129 4. ,162 1. .543 28. .787 1. ,00 13, .46 C
ATOM 296 C VAL A 129 2. .926 1. .449 27. .888 1. ,00 15. .33 C
ATOM 297 O VAL A 129 3. .004 1. .619 26. .673 1. .00 13. .42 O
ATOM 298 CB VAL A 129 4. .800 0. .134 28. .822 1. .00 15. ,74 C
ATOM 299 CGI VAL A 129 5. .053 -0. .415 27. .423 1. .00 21. .31 C
ATOM 300 CG2 VAL A 129 6. .116 0. .115 29. .582 1. .00 20. .61 C
ATOM 301 N ALA A 130 1. .756 1. .188 28. .469 1. ,00 16. .19 N
ATOM 302 CA ALA A 130 0. .500 1. .091 27. .750 1. .00 17. .34 C
ATOM 303 C ALA A 130 0. .140 2. .374 27. .011 1. .00 16. .78 C
ATOM 304 O ALA A 130 •0. .623 2. .364 26. .036 1. .00 19. .11 O
ATOM 305 CB ALA A 130 0. .620 0. .704 28. .713 1. .00 14. .76 C
ATOM 306 N GLU A 131 0. .616 3. .509 27. .490 1. .00 13. .17 N
ATOM 307 CA GLU A 131 0. .387 4. .814 26. .930 1. .00 14. .63 C
ATOM 308 C GLU A 131 1. .484 5. .274 25. .975 1. .00 13. .20 C
ATOM 309 O GLU A 131 1. .331 6. .391 25. .480 1. .00 14. .75 O
ATOM 310 CB GLU A 131 0. .214 5. .864 28. .047 1. .00 14. .20 C
ATOM 311 CG GLU A 131 0. .804 5. .390 29. .101 1. .00 16. .67 C
ATOM 312 CD GLU A 131 2. .191 5. .251 28. .492 1. .00 17. .68 C
ATOM 313 OE1 GLU A 131 ■2. .549 6. .169 27. .715 1. .00 16. .62 O
ATOM 314 OE2 GLU A 131 ■2. .890 4. .265 28. .795 1. .00 18. .66 O
ATOM 315 N VAL A 132 2. .538 4. .512 25. ,741 1. ,00 11. ,88 N
ATOM 316 CA VAL A 132 3. .603 4. .952 24. .822 1. .00 11. .08 C
ATOM 317 C VAL A 132 3, .135 4. .692 23. .394 1. .00 11. .44 C
ATOM 318 O VAL A 132 2, .668 3. .588 23. .097 1. .00 13. .60 O
ATOM 319 CB VAL A 132 4. .907 4. .193 25. .123 1. .00 11. .89 C
ATOM 320 CGI VAL A 132 6, .018 4. .587 24. .167 1. .00 8. .60 C
ATOM 321 CG2 VAL A 132 5, .390 4, .506 26. .543 1. .00 10. .07 C
ATOM 322 N PRO A 133 3, .122 5, .711 22, .555 1. .00 11, .44 N
ATOM 323 CA PRO A 133 2, .549 5. .627 21. .221 1. .00 10. .93 C
ATOM 324 C PRO A 133 3. .425 4, .887 20. .236 1. .00 11. .01 C
ATOM 325 O PRO A 133 4. .486 5, .413 19, .901 1, .00 13. .15 O
ATOM 326 CB PRO A 133 2, .382 7. .091 20. .847 1. .00 11. .30 C
ATOM 327 CG PRO A 133 3, .475 7. .826 21. .566 1. .00 14. .33 C
ATOM 328 CD PRO A 133 3. .628 7, .078 22. .871 1. .00 13. .04 C
ATOM 329 N SER A 134 3 .040 3. .701 19, .796 1, .00 9, .43 N
ATOM 330 CA SER A 134 3, .825 2, .928 18. .845 1. .00 9. .61 c
ATOM 331 C SER A 134 3. .095 2, .858 17. .506 1. .00 9, .08 c
ATOM 332 O SER A 134 1 .886 3, .119 17, .451 1. .00 7. .95 0
ATOM 333 CB SER A 134 4, .090 1, .508 19, .364 1. .00 11, .46 c
ATOM 334 OG SER A 134 2, .893 0, .905 19, .850 1. .00 9. .22 0
ATOM 335 N PHE A 135 3 .804 2. .513 16, .435 1. .00 7, .57 N
ATOM 336 CA PHE A 135 3 .157 2. .391 15, .122 1. .00 6. .79 C
ATOM 337 C PHE A 135 2 .172 1, .234 15, .076 1. .00 7. .10 C
ATOM 338 O PHE A 135 2. .370 0, .257 15, .810 1. .00 6, .61 O
ATOM 339 CB PHE A 135 4 .240 2 .198 14, .047 1, .00 6. .80 C
ATOM 340 CG PHE A 135 4 .901 3, .451 13, .541 1. .00 8, .54 C ATOM 341 CDl PHE A 135 5.742 4..230 14..318 1..00 7..25 C
ATOM 342 CD2 PHE A 135 4. 669 3. 849 12. ,227 1. .00 8. .57 c
ATOM 343 CE1 PHE A 135 6. 329 5. 368 13. 811 1. 00 6. 65 c
ATOM 344 CE2 PHE A 135 5. 247 4. 983 11. 706 1. 00 7. 30 c
ATOM 345 CZ PHE A 135 6. 079 5. 765 12. .505 1. ,00 8. 25 c
ATOM 346 N GLN A 136 1. 200 1. 181 14. .163 1. 00 8. 59 N
ATOM 347 CA GLN A 136 0. 314 0. .072 13. ,882 1. .00 7. 41 C
ATOM 348 C GLN A 136 0. 533 -0. .390 12. ,449 1. ,00 8. 09 C
ATOM 349 0 GLN A 136 0. 975 0. ,452 11. ,680 1. ,00 9. .99 0
ATOM 350 CB GLN A 136 1. 133 0. 533 14. 041 1. 00 8. 77 C
ATOM 351 CG GLN A 136 1. 414 0. 850 15. .526 1. .00 8. 45 c
ATOM 352 CD GLN A 136 2. 881 1. .260 15. .641 1. ,00 9. 06 c
ATOM 353 OE1 GLN A 136 3. 276 2. .356 15. .230 1. ,00 13. 11 o
ATOM 354 NE2 GLN A 136 3. 625 0. ,336 16. ,178 1. ,00 10. ,30 N
ATOM 355 N TRP A 137 0. 466 -1. ,677 12. ,180 1. .00 8. ,68 N
ATOM 356 CA TRP A 137 0. 915 -2. ,150 10. .884 1. .00 8. ,62 C
ATOM 357 C TRP A 137 0. 191 -2. ,564 9. .948 1. .00 7. 64 C
ATOM 358 O TRP A 137 1. 013 -3. ,398 10. .316 1. .00 8. .36 O
ATOM 359 CB TRP A 137 1. 824 -3. ,349 11. .237 1. ,00 7. .40 C
ATOM 360 CG TRP A 137 3. 105 -2. .973 11. ,930 1. ,00 9. ,26 C
ATOM 361 CDl TRP A 137 3. .286 -2. .305 13. .106 1. ,00 9. .31 C
ATOM 362 CD2 TRP A 137 4. ,420 -3. .292 11. .476 1. .00 6. .21 C
ATOM 363 NE1 TRP A 137 4. ,621 -2. .162 13. .414 1. .00 8. .45 N
ATOM 364 CE2 TRP A 137 5. 335 -2. .772 12. ,426 1. ,00 8. ,77 C
ATOM 365 CE3 TRP A 137 4. 916 -3. ,979 10. ,357 1. ,00 10. ,04 C
ATOM 366 CZ2 TRP A 137 6. ,720 -2. .902 12. ,307 1. ,00 8. ,70 C
ATOM 367 CZ3 TRP A 137 6. .302 -4. .097 10. .235 1. .00 8. .51 C
ATOM 368 CH2 TRP A 137 7. .161 -3. .571 11. .205 1. .00 7. .62 C
ATOM 369 N LEU A 138 ■0. ,086 -2. .138 8. .689 1. .00 6. .71 N
ATOM 370 CA LEU A 138 •1. .011 -2. .672 7. .669 1. .00 7. .17 C
ATOM 371 C LEU A 138 ■0. .235 -3. .793 6. .979 1. .00 6. .99 C
ATOM 372 O LEU A 138 0. .173 -3. .705 5. .828 1. .00 6. .77 0
ATOM 373 CB LEU A 138 ■1. .459 -1. .602 6. .685 1. .00 8. .93 C
ATOM 374 CG LEU A 138 ■1. .894 -0. .268 7. .300 1. .00 6. .21 C
ATOM 375 CDl LEU A 138 ■2. .279 0. .680 6. .146 1. .00 6. .42 C
ATOM 376 CD2 LEU A 138 ■3. .057 -0. .459 8. .260 1. .00 8. .15 C
ATOM 377 N ASP A 139 •0. .070 -4, .895 7, .720 1. .00 7. .95 N
ATOM 378 CA ASP A 139 0. .735 -6, .017 7. .251 1. .00 8. .19 C
ATOM 379 C ASP A 139 ■0. .084 -7. .090 6. .568 1. .00 8. .76 C
ATOM 380 O ASP A 139 0. .469 -8. .089 6. .083 1. .00 7. .32 O
ATOM 381 CB ASP A 139 1. .524 -6, .582 8. .447 1. .00 12. .08 C
ATOM 382 CG ASP A 139 0. .609 -7. .212 9. .478 1. .00 14. .55 C
ATOM 383 ODl ASP A 139 ■0. .510 -6, .736 9. .703 1. .00 14. .60 O
ATOM 384 OD2 ASP A 139 1. .032 -8, .226 10, .067 1, .00 22. .92 O
ATOM 385 N ARG A 140 ■1, .393 -6, .858 6, .496 1, .00 6, .66 N
ATOM 386 CA ARG A 140 ■2. .339 -7, .713 5, .806 1. .00 8. .02 C
ATOM 387 C ARG A 140 ■3. .390 -6, .789 5, .177 1. .00 8. .44 C
ATOM 388 0 ARG A 140 •3. .736 -5, .759 5, .755 1. .00 10. .03 O
ATOM 389 CB ARG A 140 ■3, .085 -8, .676 6, .727 1. .00 14. .54 C
ATOM 390 CG ARG A 140 ■2. .369 -9, .962 7, .108 1. .00 21. .01 C
ATOM 391 CD ARG A 140 ■2, .810 -10 .380 8 .518 1. .00 26. .38 C
ATOM 392 NE ARG A 140 ■2. .423 -9 .344 9 .477 1 .00 25, .95 N
ATOM 393 CZ ARG A 140 ■3, .224 -8. .786 10, .378 1, .00 27, .50 C
ATOM 394 NHl ARG A 140 •4, .503 -9 .156 10, .464 1. .00 24, .37 N
ATOM 395 NH2 ARG A 140 -2, .714 -7 .848 11 .169 1. .00 26, .06 N
ATOM 396 N ASN A 141 ■3, .891 -7 .143 4 .011 1. .00 7, .01 N
ATOM 397 CA ASN A 141 ■4 .890 -6 .359 3. .301 1. .00 7. .11 C
ATOM 398 C ASN A 141 -6 .119 -6 .052 4 .142 1 .00 7 .69 C
ATOM 399 O ASN A 141 -6 .718 -4 .960 4 .039 1. .00 5 .66 O
ATOM 400 CB ASN A 141 ■5 .253 -7. .072 1 .984 1. .00 8, .96 C
ATOM 401 CG ASN A 141 ■6 .154 -6 .226 1 .085 1 .00 10. .45 C
ATOM 402 ODl ASN A 141 -5 .846 -5 .034 0 .880 1 .00 7 .27 O
ATOM 403 ND2 ASN A 141 ■7 .223 -6 .834 0 .569 1. .00 8. .87 N
ATOM 404 N VAL A 142 -6 .547 -6 .985 4 .989 1. .00 7 .41 N
ATOM 405 CA VAL A 142 -7 .727 -6 .810 5 .832 1 .00 9 .96 C
ATOM 406 C VAL A 142 -7 .616 -5 .666 6 .818 1 .00 8 .09 C
ATOM 407 0 VAL A 142 -8 .642 -5 .128 7 .251 1 .00 9 .90 O
ATOM 408 CB VAL A 142 -8 .057 -8 .122 6 .577 1. .00 12 .41 C
ATOM 409 CGI VAL A 142 -7 .037 -8 .366 7 .688 1 .00 14 .72 C
ATOM 410 CG2 VAL A 142 -9 .473 -8 .091 7 .129 1 .00 15 .00 C
ATOM 411 N THR A 143 -6 .408 -5 .206 7 .181 1 .00 8 .26 N
ATOM 412 CA THR A 143 -6 .245 -4 .077 8 .090 1 .00 7 .37 C ATOM 413 C THR A 143 -6.655 -2.742 7.471 1.00 8.31 c
ATOM 414 0 THR A 143 -6. 899 -1. 791 8. 214 1. 00 8. 19 o
ATOM 415 CB THR A 143 -4. 765 -3. 917 8. 541 1. 00 7. 79 c
ATOM 416 OGl THR A 143 -3. 960 -3. 639 7. 385 1. 00 8. 04 0
ATOM 417 CG2 THR A 143 -4. 277 -5. 213 9. 187 1. 00 7. 60 c
ATOM 418 N VAL A 144 -6. 684 -2. 611 6. 143 1. 00 8. 65 N
ATOM 419 CA VAL A 144 -6. 965 -1. 313 5. 511 1. 00 7. 32 C
ATOM 420 C VAL A 144 -8. 367 -0. 798 5. 834 1. 00 8. 88 C
ATOM 421 0 VAL A 144 -8. 533 0. 335 6. 267 1. 00 8. 24 0
ATOM 422 CB VAL A 144 -6. 764 -1. 432 3. 995 1. 00 5. 69 C
ATOM 423 CGI VAL A 144 -7. 176 -0. 172 3. 234 1. 00 6. 76 c
ATOM 424 CG2 VAL A 144 -5. 299 -1. 737 3. 659 1. 00 6. 96 c
ATOM 425 N ASP A 145 -9. 415 -1. 614 5. 663 1. 00 7. 58 N
ATOM 426 CA ASP A 145 10. 790 -1. 172 5. 925 1. 00 8. 56 C
ATOM 427 C ASP A 145 11. 217 -1. 428 7. 358 1. 00 8. 48 C
ATOM 428 O ASP A 145 12. 375 -1. .268 7. 765 1. 00 8. 12 O
ATOM 429 CB ASP A 145 11. 768 -1. .844 4. .961 1. 00 10. 52 C
ATOM 430 CG ASP A 145 11. 807 -1. ,217 3. ,589 1. 00 12. 26 C
ATOM 431 ODl ASP A 145 11. .524 -0. ,004 3. .452 1. 00 11. 52 O
ATOM 432 OD2 ASP A 145 12. 185 -1. .921 2. ,626 1. 00 13. 96 0
ATOM 433 N THR A 146 10. ,255 -1. ,842 8. .199 1. .00 9. 54 N
ATOM 434 CA THR A 146 10. .525 -2. ,084 9. ,611 1. .00 7. .82 C
ATOM 435 C THR A 146 -9. ,638 -1. ,204 10. .486 1. .00 8. 67 C
ATOM 436 O THR A 146 -9. .993 -0. ,061 10. ,796 1. .00 8. ,39 O
ATOM 437 CB THR A 146 ■10. .395 -3. .571 9. .973 1. ,00 9. .97 C
ATOM 438 OGl THR A 146 -9. ,098 -4. ,103 9. ,642 1. .00 8. ,75 O
ATOM 439 CG2 THR A 146 11. ,420 -4. .412 9. ,206 1. ,00 8. ,34 C
ATOM 440 N LEU A 147 -8. ,471 -1. .689 10. .890 1. .00 8. ,40 N
ATOM 441 CA LEU A 147 -7. ,542 -0. .952 11. .737 1. .00 10. ,01 C
ATOM 442 C LEU A 147 -7. .281 0. .470 11. .267 1. .00 10. .27 C
ATOM 443 O LEU A 147 -7. ,281 1. .392 12. .076 1. .00 8. .52 O
ATOM 444 CB LEU A 147 -6. .213 -1. .720 11. .744 1. .00 13. .76 C
ATOM 445 CG LEU A 147 -5. .066 -1. .285 12. .639 1. .00 16. .03 C
ATOM 446 CDl LEU A 147 -3. .972 -2. .369 12. .648 1. .00 18. .03 C
ATOM 447 CD2 LEU A 147 -4. .415 0. .014 12. .171 1. .00 18. .36 C
ATOM 448 N LEU A 148 -6. .956 0. .639 9. .973 1. .00 10. .54 N
ATOM 449 CA LEU A 148 -6. .619 1. .984 9. .504 1. .00 9. .28 C
ATOM 450 C LEU A 148 -7. .794 2. .923 9. .769 1. .00 7. .49 C
ATOM 451 O LEU A 148 -7. .589 3, .995 10. .327 1. .00 8. .53 o
ATOM 452 CB LEU A 148 -6. .228 1, .992 8. .026 1. .00 8. .01 c
ATOM 453 CG LEU A 148 -5. .819 3, .358 7. .451 1. .00 7. .92 c
ATOM 454 CDl LEU A 148 -4. .615 3, .958 8. .156 1. .00 7. .68 c
ATOM 455 CD2 LEU A 148 -5. .536 3, .247 5, .956 1. .00 7. .20 c
ATOM 456 N VAL A 149 -8. .988 2, .562 9, .318 1. .00 5. .78 N
ATOM 457 CA VAL A 149 •10. .167 3, .430 9, .467 1, .00 7. .27 C
ATOM 458 C VAL A 149 ■10, .478 3. .688 10, .936 1, .00 8. .10 C
ATOM 459 0 VAL A 149 •10, .764 4, .808 11, .362 1. .00 10. .37 O
ATOM 460 CB VAL A 149 ■11, .381 2. .848 8, .730 1, .00 4, .23 C
ATOM 461 CGI VAL A 149 ■12, .663 3. .648 8, .960 1, .00 7. .29 c
ATOM 462 CG2 VAL A 149 -11, .103 2 .833 7, .218 1, .00 5, .93 c
ATOM 463 N GLN A 150 ■10, .410 2 .628 11. .739 1, .00 8, .03 N
ATOM 464 CA GLN A 150 -10, .681 2 .741 13 .164 1, .00 9, .11 C
ATOM 465 C GLN A 150 -9 .678 3 .677 13 .823 1. .00 8, .39 C
ATOM 466 0 GLN A 150 -10 .097 4 .550 14 .580 1 .00 9, .35 0
ATOM 467 CB GLN A 150 -10 .642 1 .352 13 .817 1 .00 14 .96 c
ATOM 468 CG GLN A 150 -11 .105 1 .462 15 .267 1 .00 22 .14 c
ATOM 469 CD GLN A 150 -11 .602 0 .156 15 .841 1 .00 25 .50 c
ATOM 470 0E1 GLN A 150 -11 .083 -0 .910 15 .519 1 .00 28 .18 0
ATOM 471 NE2 GLN A 150 -12 .615 0 .244 16 .702 1 .00 29 .84 N
ATOM 472 N THR A 151 -8 .378 3 .521 13 .556 1 .00 8 .05 N
ATOM 473 CA THR A 151 -7 .400 4 .440 14 .162 1 .00 7 .96 C
ATOM 474 C THR A 151 -7 .647 5 .894 13 .798 1 .00 8 .35 C
ATOM 475 0 THR A 151 -7 .720 6 .772 14 .661 1 .00 8 .22 0
ATOM 476 CB THR A 151 -5 .968 4 .021 13 .785 1 .00 11 .32 C
ATOM 477 OGl THR A 151 -5 .756 2 .735 14 .387 1 .00 11 .96 0
ATOM 478 CG2 THR A 151 -4 .924 5 .009 14 .282 1 .00 9 .34 C
ATOM 479 N LEU A 152 -7 .832 6 .168 12 .504 1 .00 8 .14 N
ATOM 480 CA LEU A 152 -8 .041 7 .551 12 .051 1 .00 7 .29 C
ATOM 481 C LEU A 152 -9 .347 8 .115 12 .612 1 .00 9 .17 c
ATOM 482 0 LEU A 152 -9 .432 9 .297 12 .977 1 .00 8 .29 o
ATOM 483 CB LEU A 152 -7 .959 7 .571 10 .528 1 .00 6 .78 c
ATOM 484 CG LEU A 152 -6 .569 7 .205 9 .945 1 .00 6 .61 c ATOM 485 CDl LEU A 152 -6.681 7 078 8 430 1 00 5 51 c
ATOM 486 CD2 LEU A 152 -5 516 8 245 10 319 1 00 7 04 c
ATOM 487 N SER A 153 10. 373 7 285 12 706 1 00 7 28 N
ATOM 488 CA SER A 153 11. 652 7 727 13 278 1 00 11 14 C
ATOM 489 C SER A 153 11. 444 8 099 14 745 1 00 10 95 C
ATOM 490 O SER A 153 11 930 9 127 15 225 1 00 11 85 O
ATOM 491 CB SER A 153 12 692 6 604 13 137 1 00 7 29 C
ATOM 492 OG ASER A 153 12 965 6 370 11 762 0 50 6 72 o
ATOM 493 OG BSER A 153 13 872 6 992 13 815 0 50 12 37 0
ATOM 494 N GLU A 154 10 730 7 252 15 499 1 00 12 45 N
ATOM 495 CA GLU A 154 10 492 7 518 16 924 1 00 13 47 C
ATOM 496 C GLU A 154 -9 680 8 783 17 155 1 00 12 90 C
ATOM 497 0 GLU A 154 -9 967 9 552 18 076 1 00 12 37 O
ATOM 498 CB GLU A 154 -9 833 6 309 17 615 1 00 12 58 C
ATOM 499 CG GLU A 154 10 822 5 161 17 779 1 00 14 64 C
ATOM 500 CD GLU A 154 10 314 3 936 18 499 1 00 20 19 C
ATOM 501 OE1 GLU A 154 -9 272 3 982 19 194 1 00 21 91 0
ATOM 502 OE2 GLU A 154 10 963 2 868 18 411 1 00 19 21 0
ATOM 503 N ILE A 155 -8 666 9 039 16 336 1 00 10 49 N
ATOM 504 CA ILE A 155 -7 852 10 237 16 439 1 00 9 77 C
ATOM 505 C ILE A 155 -8 686 11 472 16 092 1 00 10 81 C
ATOM 506 O ILE A 155 -8 660 12 463 16 812 1 00 10 95 O
ATOM 507 CB ILE A 155 -6 633 10 141 15 490 1 00 11 73 C
ATOM 508 CGI ILE A 155 -5 740 9 000 15 991 1 00 10 67 C
ATOM 509 CG2 ILE A 155 -5 898 11 473 15 427 1 00 9 54 C
ATOM 510 CDl ILE A 155 -4 548 8 672 15 106 1 00 7 45 c
ATOM 511 N ARG A 156 -9 513 11 399 15 052 1 00 10 62 N
ATOM 512 CA ARG A 156 10 364 12 547 14 726 1 00 12 10 C
ATOM 513 C ARG A 156 11 260 12 931 15 905 1 00 12 02 C
ATOM 514 O ARG A 156 11 376 14 120 16 227 1 00 11 35 0
ATOM 515 CB ARG A 156 11 216 12 236 13 497 1 00 11 23 C
ATOM 516 CG ARG A 156 12 289 13 283 13 233 1 00 12 89 C
ATOM 517 CD ARG A 156 13 139 12 927 12 031 1 00 12 14 C
ATOM 518 NE ARG A 156 12 449 13 190 10 767 1 00 11 44 N
ATOM 519 CZ ARG A 156 12 838 12 636 9 622 1 00 12 60 C
ATOM 520 NHl ARG A 156 13 835 11 754 9 531 1 00 10 76 N
ATOM 521 NH2 ARG A 156 12 175 12 940 8 522 1 00 11 99 N
ATOM 522 N GLU A 157 11 881 11 936 16 518 1 00 12 42 N
ATOM 523 CA GLU A 157 12 768 12 146 17 675 1 00 16 51 C
ATOM 524 C GLU A 157 12 006 12 784 18 822 1 00 16 44 C
ATOM 525 O GLU A 157 12 458 13 761 19 418 1 00 12 67 O
ATOM 526 CB GLU A 157 13 386 10 799 18 005 1 00 21 63 C
ATOM 527 CG GLU A 157 13 788 10 427 19 406 1 00 30 85 C
ATOM 528 CD GLU A 157 14 376 9 033 19 538 1 00 35 79 C
ATOM 529 OE1 GLU A 157 13 654 8 015 19 378 1 00 36 29 O
ATOM 530 OE2 GLU A 157 15 602 8 937 19 804 1 00 39 48 O
ATOM 531 N ALA A 158 10 788 12 307 19 108 1 00 16 94 N
ATOM 532 CA ALA A 158 -9 981 12 868 20 193 1 00 15 78 C
ATOM 533 C ALA A 158 -9 602 14 304 19 878 1 00 16 51 C
ATOM 534 O ALA A 158 -9 706 15 195 20 729 1 00 17 18 0
ATOM 535 CB ALA A 158 -8 743 12 008 20 432 1 00 16 24 C
ATOM 536 N ASN A 159 -9 223 14 574 18 624 1 00 14 61 N
ATOM 537 CA ASN A 159 -8 868 15 913 18 191 1 00 15 00 C
ATOM 538 C ASN A 159 10 037 16 888 18 204 1 00 16 92 C
ATOM 539 O ASN A 159 -9 907 18 044 18 647 1 00 16 12 0
ATOM 540 CB ASN A 159 -8 281 15 876 16 764 1 00 15 00 C
ATOM 541 CG ASN A 159 -6 866 15 331 16 789 1 00 14 91 C
ATOM 542 ODl ASN A 159 -6 .283 15 148 17 875 1 00 14 98 0
ATOM 543 ND2 ASN A 159 -6 .305 15 067 15 614 1 00 8 87 N
ATOM 544 N GLN A 160 11 198 16 415 17 763 1 00 16 89 N
ATOM 545 CA GLN A 160 12 .403 17 252 17 753 1 00 20 76 C
ATOM 546 C GLN A 160 12 877 17 .542 19 172 1 00 21 81 C
ATOM 547 O GLN A 160 13 481 18 590 19 413 1 00 22 79 0
ATOM 548 CB GLN A 160 13 .517 16 .631 16 906 1 00 21 05 C
ATOM 549 CG GLN A 160 13 .248 16 .762 15 412 1 00 21 .93 C
ATOM 550 CD GLN A 160 14 .287 16 .101 14 534 1 .00 26 .67 c
ATOM 551 OE1 GLN A 160 15 086 15 265 14 957 1 00 28 67 o
ATOM 552 NE2 GLN A 160 14 277 16 430 13 245 1 00 26 21 N
ATOM 553 N ALA A 161 12 542 16 686 20 128 1 00 22 26 N
ATOM 554 CA ALA A 161 12 847 16 897 21 526 1 00 24 95 C
ATOM 555 C ALA A 161 11 860 17 842 22 199 1 00 26 81 C
ATOM 556 O ALA A 161 12 048 18 124 23 387 1 00 29 25 0 ATOM 557 CB ALA A 161 12.910 15..578 22.,289 1.00 25.,97 C
ATOM 558 N GLY A 162 10. 830 18. .339 21. ,523 1. 00 24. ,43 N
ATOM 559 CA GLY A 162 -9. 914 19. .293 22. ,107 1. 00 24. ,73 C
ATOM 560 C GLY A 162 -8. 499 18. ,847 22. ,403 1. 00 24. ,28 C
ATOM 561 0 GLY A 162 -7. 802 19. 578 23. ,135 1. 00 21. ,95 O
ATOM 562 N ALA A 163 -8. 037 17. ,706 21. ,885 1. .00 19. ,55 N
ATOM 563 CA ALA A 163 -6. 654 17. .315 22. ,188 1. 00 22. ,03 C
ATOM 564 C ALA A 163 -5. 755 18. .510 21. ,891 1. 00 22. ,46 C
ATOM 565 0 ALA A 163 -5. 933 19. ,174 20. ,870 1. 00 21. ,19 O
ATOM 566 CB ALA A 163 -6. 215 16. ,110 21. ,375 1. 00 23. ,50 C
ATOM 567 N ASN A 164 -4. 763 18. .764 22. ,735 1. .00 22. ,29 N
ATOM 568 CA ASN A 164 -3. 832 19. ,860 22. ,459 1. .00 23. ,47 C
ATOM 569 C ASN A 164 -2. 460 19. .539 23. ,016 1. 00 21. ,73 C
ATOM 570 0 ASN A 164 -2. ,333 19. ,448 24. ,239 1. .00 22. ,31 O
ATOM 571 CB ASN A 164 -4. .314 21. ,173 23. ,100 1. .00 28. .72 C
ATOM 572 CG ASN A 164 -3. ,286 22. ,273 22. ,897 1. 00 32. .01 C
ATOM 573 ODl ASN A 164 -2. .696 22. .368 21. .821 1. .00 34. .27 O
ATOM 574 ND2 ASN A 164 -3. .054 23. .080 23. .922 1. .00 34. .56 N
ATOM 575 N PRO A 165 -1. .465 19. .415 22. .149 1. .00 20. .86 N
ATOM 576 CA PRO A 165 -1. .606 19. .526 20. .713 1. .00 19. .44 C
ATOM 577 C PRO A 165 -2. .423 18. .398 20. .090 1. .00 17. .35 C
ATOM 578 O PRO A 165 -2. .698 17. .420 20. .779 1. .00 14. .86 O
ATOM 579 CB PRO A 165 -0. .181 19. .385 20. .174 1. .00 20. .03 C
ATOM 580 CG PRO A 165 0. .738 19. .450 21. .333 1. .00 21. .24 C
ATOM 581 CD PRO A 165 -0. .070 19. .110 22. .558 1. .00 22. .04 C
ATOM 582 N GLN A 166 -2. .809 18. .527 18. .822 1. .00 14. .41 N
ATOM 583 CA GLN A 166 -3. .583 17. .498 18. .150 1. .00 14. .75 C
ATOM 584 C GLN A 166 -2. .780 16. .200 18. .022 1. .00 12. .60 C
ATOM 585 0 GLN A 166 -1. .551 16. .271 17. .991 1. .00 12. .39 O
ATOM 586 CB GLN A 166 -3. .992 17. .942 16. .725 1. .00 18. .33 C
ATOM 587 CG GLN A 166 -2. .869 17. .964 15. .707 1. .00 24. .17 C
ATOM 588 CD GLN A 166 -3. .253 18. .266 14. .273 1. .00 26. .89 C
ATOM 589 OE1 GLN A 166 -4. .407 18. .104 13. .845 1. .00 34. .04 O
ATOM 590 NE2 GLN A 166 -2. .281 18. .693 13. .472 1. .00 24. .83 N
ATOM 591 N TYR A 167 -3. .466 15. .080 17. .893 1. .00 10. .69 N
ATOM 592 CA TYR A 167 -2. .810 13. .784 17. .726 1. .00 10. .57 C
ATOM 593 C TYR A 167 -2. .529 13. .452 16. .260 1. .00 10. .87 C
ATOM 594 0 TYR A 167 -3. .375 13, .762 15. .404 1. .00 9. .79 O
ATOM 595 CB TYR A 167 -3. .726 12. .671 18. .254 1. .00 12. .05 C
ATOM 596 CG TYR A 167 -3. .790 12. .556 19, .766 1. .00 15. .59 C
ATOM 597 CDl TYR A 167 -2. .765 11. .974 20, .497 1. .00 19. .75 C
ATOM 598 CD2 TYR A 167 -4. .916 12. .998 20, .445 1. .00 17. .73 C
ATOM 599 CE1 TYR A 167 -2. .839 11. .856 21, .879 1. .00 22, .74 C
ATOM 600 CE2 TYR A 167 -5. .005 12. .886 21, .826 1. .00 20. .59 C
ATOM 601 CZ TYR A 167 -3. .965 12. .324 22, .531 1. .00 24. .04 c
ATOM 602 OH TYR A 167 -4. .074 12, .243 23, .899 1. .00 27. .41 0
ATOM 603 N ALA A 168 -1. .451 12, .721 16, .020 1. .00 9. .52 N
ATOM 604 CA ALA A 168 -1. .092 12. .256 14, .689 1. .00 11, .13 C
ATOM 605 C ALA A 168 -0. .963 10. .725 14, .700 1. .00 11, .90 C
ATOM 606 0 ALA A 168 -0. .722 10, .128 15, .751 1. .00 11, .35 O
ATOM 607 CB ALA A 168 0. .221 12, .842 14, .200 1. .00 12, .45 C
ATOM 608 N ALA A 169 -1. .218 10, .122 13, .552 1. .00 9, .29 N
ATOM 609 CA ALA A 169 -1. .212 8, .683 13, .390 1. .00 8, .97 C
ATOM 610 C ALA A 169 0, .163 8, .226 12, .887 1. .00 8, .20 C
ATOM 611 0 ALA A 169 0, .842 8, .962 12, .163 1. .00 8, .12 O
ATOM 612 CB ALA A 169 -2, .248 8, .244 12, .351 1. .00 9, .83 C
ATOM 613 N GLN A 170 0, .529 7, .022 13, .300 1, .00 6, .87 N
ATOM 614 CA GLN A 170 1, .795 6, .399 12, .914 1. .00 7, .82 C
ATOM 615 C GLN A 170 1, .418 5, .032 12, .340 1. .00 7, .61 C
ATOM 616 0 GLN A 170 0, .853 4, .194 13 .040 1, .00 8, .51 O
ATOM 617 CB GLN A 170 2, .725 6, .237 14, .111 1, .00 8, .74 C
ATOM 618 CG GLN A 170 3, .190 7, .555 14, .746 1, .00 9, .33 C
ATOM 619 CD GLN A 170 3, .961 7, .214 16. .017 1, .00 12. .58 C
ATOM 620 OE1 GLN A 170 5, .185 7, .326 16. .054 1. .00 10, .59 O
ATOM 621 NE2 GLN A 170 3 .199 6, .777 17. .011 1, .00 9. .26 N
ATOM 622 N ILE A 171 1, .645 4 .834 11 .048 1, .00 7, .15 N
ATOM 623 CA ILE A 171 1 .226 3 .620 10 .354 1 .00 7 .05 C
ATOM 624 C ILE A 171 2 .338 3 .035 9 .484 1 .00 6 .89 C
ATOM 625 O ILE A 171 3 .093 3 .776 8 .848 1 .00 8 .42 O
ATOM 626 CB ILE A 171 0 .038 3 .999 9 .427 1 .00 5 .53 C
ATOM 627 CGI ILE A 171 -1 .228 4 .417 10 .189 1 .00 5 .97 C
ATOM 628 CG2 ILE A 171 -0 .294 2 .858 8 .468 1 .00 8 .49 C ATOM 629 CDl ILE A 171 -1.839 3.285 11.007 1.00 8.37 c
ATOM 630 N VAL A 172 2.444 1.724 9.418 1.00 6.22 N
ATOM 631 CA VAL A 172 3.425 1.038 8.580 1.00 6.50 C
ATOM 632 C VAL A 172 2.716 0.401 7.390 1.00 6.35 C
ATOM 633 0 VAL A 172 1.708 -0.268 7.599 1.00 5.88 O
ATOM 634 CB VAL A 172 4.207 -0.059 9.340 1.00 6.33 c
ATOM 635 CGI VAL A 172 5.357 -0.606 8.507 1.00 6.37 c
ATOM 636 CG2 VAL A 172 4.753 0.482 10.667 1.00 6.87 c
ATOM 637 N VAL A 173 3.180 0.647 6.171 1.00 6.59 N
ATOM 638 CA VAL A 173 2.676 0.020 4.957 1.00 5.00 C
ATOM 639 C VAL A 173 3.564 -1.211 4.727 1.00 5.91 C
ATOM 640 0 VAL A 173 4.768 -1.025 4.523 1.00 5.01 O
ATOM 641 CB VAL A 173 2.726 0.999 3.774 1.00 4.06 c
ATOM 642 CGI VAL A 173 2.177 0.400 2.487 1.00 6.54 c
ATOM 643 CG2 VAL A 173 1.871 2.218 4.174 1.00 4.80 c
ATOM 644 N TYR A 174 3.009 -2.416 4.842 1.00 4.19 N
ATOM 645 CA TYR A 174 3.867 -3.614 4.739 1.00 5.44 C
ATOM 646 C TYR A 174 3.151 -4.781 4.065 1.00 7.78 C
ATOM 647 0 TYR A 174 2.787 -5.753 4.744 1.00 7.53 O
ATOM 648 CB TYR A 174 4.329 -3.976 6.152 1.00 7.25 C
ATOM 649 CG TYR A 174 5.310 -5.116 6.345 1.00 6.83 C
ATOM 650 CDl TYR A 174 6.397 -5.292 5.515 1.00 5.84 C
ATOM 651 CD2 TYR A 174 5.140 -6.023 7.387 1.00 9.12 C
ATOM 652 CE1 TYR A 174 7.298 -6.342 5.684 1.00 7.16 c
ATOM 653 CE2 TYR A 174 6.029 -7.078 7.570 1.00 8.99 c
ATOM 654 CZ TYR A 174 7.098 -7.227 6.726 1.00 9.40 c
ATOM 655 OH TYR A 174 8.002 -8.265 6.909 1.00 9.56 o
ATOM 656 N ASP A 175 2.979 -4.716 2.736 1.00 7.78 N
ATOM 657 CA ASP A 175 2.342 -5.832 2.032 1.00 8.15 C
ATOM 658 C ASP A 175 2.855 -6.052 0.621 1.00 7.45 C
ATOM 659 O ASP A 175 2.092 -6.538 -0.233 1.00 5.39 O
ATOM 660 CB ASP A 175 0.817 -5.703 2.009 1.00 8.19 C
ATOM 661 CG ASP A 175 0.075 -7.027 2.027 1.00 10.97 C
ATOM 662 ODl ASP A 175 0.706 -8.107 2.080 1.00 7.42 o
ATOM 663 OD2 ASP A 175 -1.180 -7.003 2.036 1.00 8.40 o
ATOM 664 N LEU A 176 4.113 -5.716 0.305 1.00 6.84 N
ATOM 665 CA LEU A 176 4.585 -5.961 -1.066 1.00 5.89 c
ATOM 666 C LEU A 176 4.435 -7.443 -1.408 1.00 6.90 c
ATOM 667 0 LEU A 176 4.642 -8.303 -0.543 1.00 5.82 o
ATOM 668 CB LEU A 176 6.058 -5.572 -1.209 1.00 5.16 c
ATOM 669 CG LEU A 176 6.371 -4.071 -1.318 1.00 8.40 c
ATOM 670 CDl LEU A 176 7.863 -3.845 -1.163 1.00 7.00 c
ATOM 671 CD2 LEU A 176 5.876 -3.554 -2.669 1.00 7.87 c
ATOM 672 N PRO A 177 4.162 -7.741 -2.668 1.00 6.19 N
ATOM 673 CA PRO A 177 4.102 -9.103 -3.168 1.00 7.49 C
ATOM 674 C PRO A 177 5.488 -9.712 -3.184 1.00 8.85 C
ATOM 675 O PRO A 177 6.476 -8.983 -3.364 1.00 7.84 O
ATOM 676 CB PRO A 177 3.535 -8.953 -4.579 1.00 6.43 C
ATOM 677 CG PRO A 177 4.086 -7.627 -5.027 1.00 5.53 c
ATOM 678 CD PRO A 177 4.018 -6.763 -3.780 1.00 5.57 c
ATOM 679 N ASP A 178 5.605 -11.022 -2.954 1.00 7.91 N
ATOM 680 CA ASP A 178 6.923 -11.654 -2.815 1.00 7.32 C
ATOM 681 C ASP A 178 7.691 -10.927 -1.693 1.00 9.26 C
ATOM 682 O ASP A 178 8.886 -10.638 -1.786 1.00 8.12 O
ATOM 683 CB ASP A 178 7.785 -11.636 -4.080 1.00 7.96 C
ATOM 684 CG ASP A 178 7.401 -12.747 -5.057 1.00 9.44 c
ATOM 685 ODl ASP A 178 6.251 -13.216 -5.066 1.00 8.40 o
ATOM 686 OD2 ASP A 178 8.275 -13.156 -5.851 1.00 7.75 o
ATOM 687 N ARG A 179 7.008 -10.677 -0.581 1.00 8.32 N
ATOM 688 CA ARG A 179 7.517 -9.895 0.528 1.00 6.43 C
ATOM 689 C ARG A 179 8.684 -10.629 1.171 1.00 8.91 C
ATOM 690 O ARG A 179 8.739 -11.867 1.142 1.00 7.98 O
ATOM 691 CB ARG A 179 6.421 -9.671 1.585 1.00 6.59 C
ATOM 692 CG ARG A 179 6.548 -8.377 2.388 1.00 6.39 c
ATOM 693 CD ARG A 179 5.390 -8.181 3.371 1.00 5.74 c
ATOM 694 NE ARG A 179 5.439 -9.112 4.496 1.00 7.74 N
ATOM 695 CZ ARG A 179 4.466 -9.286 5.388 1.00 9.10 C
ATOM 696 NHl ARG A 179 3.330 -8.584 5.305 1.00 7.63 N
ATOM 697 NH2 ARG A 179 4.658 -10.174 6.357 1.00 9.35 N
ATOM 698 N ASP A 180 9.538 -9.839 1.800 1.00 5.91 N
ATOM 699 CA ASP A 180 10.674 -10.407 2.538 1.00 8.70 C
ATOM 700 C ASP A 180 11.403 -11.412 1.678 1.00 8.46 C ATOM 701 0 ASP A 180 11.639 -12.554 2.082 1.00 8.16 o
ATOM 702 CB ASP A 180 10. 138 -11. 100 3. 804 1. 00 10. 53 c
ATOM 703 CG ASP A 180 9. 162 -10. 249 4. 584 1. 00 11. 25 c
ATOM 704 ODl ASP A 180 9. 586 -9. 194 5. 098 1. 00 10. 71 0
ATOM 705 OD2 ASP A 180 7. 975 -10. 647 4. 660 1. 00 11. 09 0
ATOM 706 N CYS A 181 11. 866 -11. 005 0. 501 1. 00 5. 59 N
ATOM 707 CA CYS A 181 12. 461 -11. 902 0. 473 1. 00 9. 32 C
ATOM 708 C CYS A 181 13. 595 -12. 764 0. 064 1. 00 11. 57 C
ATOM 709 o CYS A 181 13. 790 -13. 878 0. 451 1. 00 9. 99 O
ATOM 710 CB CYS A 181 12. 849 -11. 108 1. 739 1. 00 10. 48 C
ATOM 711 SG CYS A 181 14. 106 -9. 825 483 1. 00 10. 63 s
ATOM 712 N ALA A 182 14. 452 -12. 284 0. 955 1. 00 11. 66 N
ATOM 713 CA ALA A 182 15. 609 -13. 089 1. 370 1. 00 12. 75 C
ATOM 714 C ALA A 182 15. 377 -13. 877 2. 645 1. 00 13. 68 C
ATOM 715 0 ALA A 182 16. .312 -14. 523 3. .150 1. .00 15. 78 O
ATOM 716 CB ALA A 182 16. ,798 -12. 153 1. .601 1. .00 13. ,81 C
ATOM 717 N ALA A 183 14. 190 -13. 781 3. 223 1. 00 12. 52 N
ATOM 718 CA ALA A 183 13. 925 -14. 428 4. .501 1. .00 15. 56 C
ATOM 719 C ALA A 183 13. 746 -15. 932 4. .321 1. ,00 16. 39 C
ATOM 720 0 ALA A 183 13. ,307 -16. 398 3. .278 1. ,00 14. ,02 O
ATOM 721 CB ALA A 183 12. ,721 -13. 814 5. ,186 1. .00 15. .25 C
ATOM 722 N ALA A 184 13. ,975 -16. .656 5. .411 1. .00 16. .34 N
ATOM 723 CA ALA A 184 13. .732 -18. 103 5. .392 1. ,00 18. .14 C
ATOM 724 C ALA A 184 12. ,235 -18. 367 5. ,334 1. ,00 18. ,59 c
ATOM 725 O ALA A 184 11. ,798 -19. .336 4. ,716 1. ,00 18. ,36 0
ATOM 726 CB ALA A 184 14. .347 -18. .746 6. .629 1. .00 18. ,88 c
ATOM 727 N ALA A 185 11. ,437 -17. ,518 5. .972 1. .00 18. ,11 N
ATOM 728 CA ALA A 185 9. ,987 -17. 645 5. ,958 1. .00 18. .85 C
ATOM 729 C ALA A 185 9. ,374 -16. .253 5. ,803 1. .00 19. .79 C
ATOM 730 0 ALA A 185 10. .044 -15. ,282 6. .165 1. .00 21. .64 O
ATOM 731 CB ALA A 185 9. .519 -18. ,312 7. .244 1. .00 18. .74 C
ATOM 732 N SER A 186 8. .174 -16. .131 5. .257 1. .00 16. .50 N
ATOM 733 CA SER A 186 7. .534 -14. .824 5. .138 1. .00 14. .74 C
ATOM 734 C SER A 186 6. .037 -14. .928 5. .406 1. .00 11. .68 C
ATOM 735 0 SER A 186 5. .400 -15. .854 4. .927 1. .00 15. .58 O
ATOM 736 CB SER A 186 7. .669 -14. .191 3. .738 1. .00 12. .02 C
ATOM 737 OG SER A 186 6. .873 -12. .991 3. .674 1. .00 7. .18 O
ATOM 738 N ASN A 187 5, .474 -13. .916 6, .073 1, .00 12. .93 N
ATOM 739 CA ASN A 187 4. .019 -13. .951 6. .288 1. .00 14. .15 C
ATOM 740 C ASN A 187 3. .294 -13. .102 5. .253 1. .00 14. .18 C
ATOM 741 0 ASN A 187 2, .092 -12. .870 5. .422 1, .00 13. .19 O
ATOM 742 CB ASN A 187 3, .676 -13. .526 7, .709 1, .00 16. .10 C
ATOM 743 CG ASN A 187 4, .233 -14. .531 8, .710 1. .00 19, .21 C
ATOM 744 ODl ASN A 187 4 .132 -15. .734 8 .460 1 .00 19, .15 O
ATOM 745 ND2 ASN A 187 4. .824 -14. .016 9, .784 1, .00 19, .14 N
ATOM 746 N GLY A 188 4, .005 -12. .650 4, .213 1. .00 10, .41 N
ATOM 747 CA GLY A 188 3. .325 -11, .847 3, .180 1 .00 11. .38 C
ATOM 748 C GLY A 188 2. .240 -12, .689 2. .509 1. .00 12 .88 C
ATOM 749 0 GLY A 188 2 .471 -13, .886 2 .263 1 .00 13 .06 O
ATOM 750 N GLU A 189 1 .122 -12, .085 2. .113 1 .00 8. .31 N
ATOM 751 CA GLU A 189 0. .035 -12, .869 1 .510 1 .00 8 .27 C
ATOM 752 C GLU A 189 0 .009 -12. .907 0 .001 1 .00 9 .32 C
ATOM 753 0 GLU A 189 -0 .786 -13 .650 -0 .600 1 .00 9 .95 O
ATOM 754 CB GLU A 189 -1 .306 -12 .307 2 .026 1 .00 13 .12 C
ATOM 755 CG GLU A 189 -1 .596 -10 .879 1 .619 1 .00 12 .11 C
ATOM 756 CD GLU A 189 -2 .654 -10 .205 2 .484 1 .00 17 .28 C
ATOM 757 OE1 GLU A 189 -3 .502 -10 .846 3 .146 1 .00 14 .92 O
ATOM 758 OE2 GLU A 189 -2 .641 -8 .957 2 .510 1 .00 10 .34 O
ATOM 759 N TRP A 190 0 .735 -12 .007 -0 .681 1 .00 6 .80 N
ATOM 760 CA TRP A 190 0 .667 -11 .938 -2 .126 1 .00 6 .48 C
ATOM 761 C TRP A 190 1 .961 -12 .320 -2 .816 1 .00 6 .91 C
ATOM 762 O TRP A 190 3 .045 -12 .169 -2 .267 1 .00 7 .46 O
ATOM 763 CB TRP A 190 0 .271 -10 .501 -2 .546 1 .00 6 .49 C
ATOM 764 CG TRP A 190 -1 .127 -10 .157 -2 .118 1 .00 7 .61 C
ATOM 765 CDl TRP A 190 -2 .204 -11 .011 -2 .031 1 .00 7 .87 C
ATOM 766 CD2 TRP A 190 -1 .608 -8 .862 -1 .737 1 .00 8 .08 c
ATOM 767 NE1 TRP A 190 -3 .321 -10 .324 -1 .599 1 .00 8 .98 N
ATOM 768 CE2 TRP A 190 -2 .985 -9 .004 -1 .429 1 .00 10 .21 C
ATOM 769 CE3 TRP A 190 -1 .016 -7 .605 -1 .624 1 .00 6 .64 C
ATOM 770 CZ2 TRP A 190 -3 .762 -7 .929 -0 .994 1 .00 8 .76 C
ATOM 771 CZ3 TRP A 190 -1 .785 -6 .535 -1 .202 1 .00 7 .39 C
ATOM 772 CH2 TRP A 190 -3 .157 -6 .706 -0 .910 1 .00 8 .88 C ATOM 773 N ALA A 191 1.,815 -12.,812 -4.,045 1..00 7..08 N
ATOM 774 CA ALA A 191 2. ,962 -13. .223 -4. ,841 1. .00 7. .97 C
ATOM 775 C ALA A 191 2. .912 -12. ,539 -6. .197 1. .00 6. .92 C
ATOM 776 0 ALA A 191 1. .857 -12. .425 -6. .839 1. .00 8. .51 0
ATOM 777 CB ALA A 191 2. ,960 -14. ,745 -5. ,066 1. .00 8. .04 C
ATOM 778 N ILE A 192 4. ,096 -12. ,148 -6. ,674 1. .00 6. .38 N
ATOM 779 CA ILE A 192 4. .187 -11. ,531 -7. .990 1. .00 7. .15 C
ATOM 780 C ILE A 192 3. .598 -12. .423 -9. ,067 1. .00 9. .47 C
ATOM 781 0 ILE A 192 2. .875 -11. .970 -9. .960 1. .00 8. .26 O
ATOM 782 CB ILE A 192 5. ,670 -11. .171 -8. .242 1. ,00 9. ,08 C
ATOM 783 CGI ILE A 192 6. .110 -10. ,095 -7. ,237 1. ,00 7. ,02 C
ATOM 784 CG2 ILE A 192 5. .867 -10. .697 -9. .671 1. ,00 10. .47 C
ATOM 785 CDl ILE A 192 7. ,612 -9, .782 -7. ,333 1. .00 8. .31 C
ATOM 786 N ALA A 193 3. ,830 -13. .744 -9. .006 1. .00 8. .91 N
ATOM 787 CA ALA A 193 3. ,331 -14. .652 -10. .052 1. .00 8. .35 C
ATOM 788 C ALA A 193 1. ,840 -14. ,919 -9. ,952 1. .00 9. .08 C
ATOM 789 0 ALA A 193 1. .250 -15. .499 -10. ,890 1. .00 9. .70 0
ATOM 790 CB ALA A 193 4. .122 -15. .944 -9. .990 1. .00 5. .81 C
ATOM 791 N ASN A 194 1. .179 -14. .440 -8. .894 1. .00 7. .87 N
ATOM 792 CA ASN A 194 0. .260 -14. ,629 -8. .743 1. ,00 9. ,39 C
ATOM 793 C ASN A 194 1. .023 -13. .329 -8. ,518 1. .00 9. ,01 C
ATOM 794 O ASN A 194 1. .675 -13. .106 -7. .493 1. .00 7. ,99 O
ATOM 795 CB ASN A 194 0. .489 -15. .590 -7. .568 1. .00 8. .00 C
ATOM 796 CG ASN A 194 1. .917 -16. .126 -7. .515 1. .00 8. .97 C
ATOM 797 ODl ASN A 194 2. .644 -16. .088 -8. .495 1. .00 9. .02 O
ATOM 798 ND2 ASN A 194 2. .306 -16. .592 -6. .336 1. .00 8. .31 N
ATOM 799 N ASN A 195 0. .891 -12. .397 -9. .451 1. .00 8. .58 N
ATOM 800 CA ASN A 195 1. .520 -11. .088 -9. .442 1. .00 9. .85 C
ATOM 801 C ASN A 195 1. .061 -10. .154 -8. .338 1. .00 8. .67 C
ATOM 802 O ASN A 195 1. .754 -9. .165 -8. .033 1. .00 8. .91 O
ATOM 803 CB ASN A 195 3. .057 -11. .250 -9. .381 1. .00 12. .56 c
ATOM 804 CG ASN A 195 3. .782 -10. .203 -10. .209 1. .00 19. .10 c
ATOM 805 ODl ASN A 195 3. .299 -9. .703 -11. .231 1. .00 21. .35 0
ATOM 806 ND2 ASN A 195 4. .977 -9. .821 -9. .778 1. .00 22. .07 N
ATOM 807 N GLY A 196 0. .135 -10. .327 -7. .790 1. .00 8. .59 N
ATOM 808 CA GLY A 196 0. .601 -9. .515 -6. .670 1. .00 9. .21 C
ATOM 809 C GLY A 196 0. .707 -8. .029 -6. .987 1. .00 8. .96 C
ATOM 810 O GLY A 196 0. .419 -7. .218 -6. .108 1. .00 7. .60 0
ATOM 811 N VAL A 197 1. .115 -7. .657 -8. .194 1. .00 8. .08 N
ATOM 812 CA VAL A 197 1. .235 -6. .222 -8. .519 1. .00 10. .31 C
ATOM 813 C VAL A 197 0. .120 -5. .546 -8. .524 1. .00 10. .94 c
ATOM 814 0 VAL A 197 ■0, .286 -4. .489 -7. .904 1. .00 9. .21 0
ATOM 815 CB VAL A 197 1. .957 -6. .067 -9. .864 1. .00 11. .44 c
ATOM 816 CGI VAL A 197 1, .779 -4. .680 -10. .467 1. .00 14. .20 c
ATOM 817 CG2 VAL A 197 3. .446 -6. .345 -9. .654 1. .00 10. .24 c
ATOM 818 N ASN A 198 ■1, .098 -6. .124 -9. .230 1. .00 8. .07 N
ATOM 819 CA ASN A 198 2, .440 -5. .558 -9. .228 1. .00 9. .21 C
ATOM 820 C ASN A 198 ■3, .019 -5. .589 -7. .809 1. .00 8. .59 C
ATOM 821 O ASN A 198 •3 .643 -4, .598 -7, .430 1. .00 6. .84 O
ATOM 822 CB ASN A 198 3, .380 -6. .276 -10. .188 1. .00 12. .07 C
ATOM 823 CG ASN A 198 •3, .021 -5, .967 -11. .636 1. .00 15. .65 c
ATOM 824 ODl ASN A 198 2, .439 -4, .920 -11, .921 1, .00 18, .16 0
ATOM 825 ND2 ASN A 198 ■3 .343 -6, .918 -12, .491 1. .00 19, .39 N
ATOM 826 N ASN A 199 ■2 .781 -6, .648 -7, .045 1. .00 8. .80 N
ATOM 827 CA ASN A 199 ■3, .261 -6, .673 -5. .669 1. .00 8, .85 C
ATOM 828 C ASN A 199 •2. .649 -5, .532 -4, .869 1, .00 8, .69 C
ATOM 829 0 ASN A 199 ■3 .354 -4, .844 -4, .095 1. .00 6, .34 0
ATOM 830 CB ASN A 199 ■2 .926 -8 .008 -4, .977 1. .00 9. .54 C
ATOM 831 CG ASN A 199 •3 .773 -9 .134 -5, .551 1 .00 10 .26 C
ATOM 832 ODl ASN A 199 ■4 .717 -8, .930 -6. .282 1. .00 6, .60 O
ATOM 833 ND2 ASN A 199 ■3 .358 -10, .343 -5, .169 1. .00 12, .35 N
ATOM 834 N TYR A 200 ■1 .355 -5. .282 -4, .968 1. .00 8. .36 N
ATOM 835 CA TYR A 200 0 .721 -4 .227 -4, .190 1 .00 7 .73 C
ATOM 836 C TYR A 200 ■1 .138 -2 .842 -4. .636 1 .00 7 .43 C
ATOM 837 O TYR A 200 1 .330 -1. .912 -3. .846 1, .00 6, .72 0
ATOM 838 CB TYR A 200 0 .797 -4. .402 -4, .311 1. .00 7. .60 C
ATOM 839 CG TYR A 200 1 .557 -3 .495 -3, .363 1. .00 7, .71 C
ATOM 840 CDl TYR A 200 1 .701 -3 .853 -2. .034 1 .00 7 .33 C
ATOM 841 CD2 TYR A 200 2 .119 -2 .300 -3 .797 1 .00 5 .65 C
ATOM 842 CE1 TYR A 200 2 .375 -3. .028 -1, .151 1. .00 6, .11 C
ATOM 843 CE2 TYR A 200 2 .816 -1 .480 -2, .932 1. .00 6 .72 C
ATOM 844 CZ TYR A 200 2 .934 -1 .846 -1. .609 1 .00 6 .44 C ATOM 845 OH TYR A 200 3.630 -1.,063 -0..706 1.00 4.84 o
ATOM 846 N LYS A 201 -1. 249 -2. ,654 -5. ,967 1. .00 6. 14 N
ATOM 847 CA LYS A 201 -1. 711 -1. .332 -6. ,421 1. .00 8. .44 C
ATOM 848 C LYS A 201 -3. .084 -0. ,987 -5. ,888 1. .00 8. .09 C
ATOM 849 0 LYS A 201 -3. 358 0. ,162 -5. .537 1. ,00 7. .64 O
ATOM 850 CB LYS A 201 -1. .722 -1. ,275 -7. ,958 1. ,00 8. ,28 C
ATOM 851 CG LYS A 201 -0. ,263 -1. ,194 -8. .455 1. ,00 11. ,36 C
ATOM 852 CD LYS A 201 -0. ,270 -1. .168 -9. .985 1. ,00 17. ,13 C
ATOM 853 CE LYS A 201 1. ,119 -0. ,858 -10. .519 1. ,00 24. .94 C
ATOM 854 NZ LYS A 201 1. ,127 -0. ,609 -11. .994 1. ,00 28. ,50 N
ATOM 855 N ALA A 202 -3. ,996 -1. ,970 -5. .845 1. ,00 5. ,77 N
ATOM 856 CA ALA A 202 -5. ,339 -1. .699 -5. .334 1. ,00 4. ,88 C
ATOM 857 C ALA A 202 -5. ,303 -1. .387 -3. .846 1. ,00 7. ,44 C
ATOM 858 0 ALA A 202 -6. .086 -0. .566 -3. .327 1. .00 7. ,04 0
ATOM 859 CB ALA A 202 -6. .274 -2. .864 -5. .654 1. ,00 6. ,18 C
ATOM 860 N TYR A 203 -4. .447 -2. .079 -3. .096 1. ,00 6. ,09 N
ATOM 861 CA TYR A 203 -4. ,255 -1. ,839 -1. ,660 1. .00 6. 29 C
ATOM 862 C TYR A 203 -3. .753 -0. ,412 -1. ,434 1. ,00 7. 79 C
ATOM 863 0 TYR A 203 -4. ,301 0. ,324 -0. ,608 1. .00 8. ,11 O
ATOM 864 CB TYR A 203 -3. .305 -2. ,875 -1. ,132 1. .00 8. .66 C
ATOM 865 CG TYR A 203 -2. ,451 -2. ,706 0. .101 1. .00 7. .91 C
ATOM 866 CDl TYR A 203 -1. ,162 -2. ,207 -0. ,008 1. .00 8. .34 C
ATOM 867 CD2 TYR A 203 -2. ,886 -3. ,130 1. ,346 1. ,00 6. ,58 C
ATOM 868 CE1 TYR A 203 -0. ,339 -2. .076 1. ,106 1. ,00 7. .67 C
ATOM 869 CE2 TYR A 203 -2. ,071 -3. ,013 2. ,464 1. ,00 6. ,79 C
ATOM 870 CZ TYR A 203 -0. ,805 -2. .506 2. .334 1. ,00 6. ,29 C
ATOM 871 OH TYR A 203 0. ,025 -2. .399 3. .437 1. ,00 7. .31 O
ATOM 872 N ILE A 204 -2. ,737 0. .009 -2. .173 1. .00 6. ,92 N
ATOM 873 CA ILE A 204 -2. .239 1. .390 -2. .051 1. .00 7. ,79 C
ATOM 874 C ILE A 204 -3. .362 2. .374 -2. .397 1. ,00 9. .37 C
ATOM 875 0 ILE A 204 -3. .577 3. .389 -1. .721 1. .00 6. .39 0
ATOM 876 CB ILE A 204 -1. .038 1. .581 -2. .999 1. .00 7. .73 C
ATOM 877 CGI ILE A 204 0. .193 0. .800 -2. .523 1. .00 6. .07 C
ATOM 878 CG2 ILE A 204 -0. .725 3. .066 -3. .180 1. .00 7. .51 C
ATOM 879 CDl ILE A 204 0. .716 1. .160 -1. .132 1. .00 6. .22 C
ATOM 880 N ASN A 205 -4. .148 2. .106 -3. .436 1. .00 7. .38 N
ATOM 881 CA ASN A 205 -5. .225 2. .975 -3. .886 1. .00 7. .98 C
ATOM 882 C ASN A 205 -6. .309 3. .135 -2. .825 1. .00 8. .46 C
ATOM 883 O ASN A 205 -6. .838 4. .226 -2. .623 1. .00 7. .81 O
ATOM 884 CB ASN A 205 -5. .875 2, .429 -5. .171 1. .00 10. .52 C
ATOM 885 CG ASN A 205 -4. .998 2, .549 -6. .397 1. .00 13. .03 C
ATOM 886 ODl ASN A 205 -4. .030 3. .305 -6, .346 1. .00 11. .52 0
ATOM 887 ND2 ASN A 205 -5. .294 1, .837 -7. .478 1. .00 13. .75 N
ATOM 888 N ARG A 206 -6, .674 2, .048 -2, .147 1. .00 7. .82 N
ATOM 889 CA ARG A 206 -7, .691 2, .110 -1. .098 1. .00 5. .94 C
ATOM 890 C ARG A 206 -7, .129 2, .869 0, .098 1. .00 6. .34 C
ATOM 891 0 ARG A 206 -7, .811 3, .702 0, .689 1. .00 6. .50 O
ATOM 892 CB ARG A 206 -8, .131 0, .704 -0, .678 1, .00 7. .36 C
ATOM 893 CG ARG A 206 -9. .162 0. .698 0, .434 1. .00 9. .57 C
ATOM 894 CD ARG A 206 10. .424 1. .492 0, .047 1, .00 11. .46 C
ATOM 895 NE ARG A 206 -11. .310 1. .549 1. .207 1. .00 9, .53 N
ATOM 896 CZ ARG A 206 -12 .180 2, .501 1. .508 1, .00 13, .46 C
ATOM 897 NHl ARG A 206 •12. .351 3 .567 0, .730 1, .00 10, .85 N
ATOM 898 NH2 ARG A 206 ■12 .883 2 .371 2 .629 1, .00 15, .76 N
ATOM 899 N ILE A 207 -5 .869 2 .603 0 .470 1. .00 5, .91 N
ATOM 900 CA ILE A 207 -5 .243 3 .399 1 .535 1 .00 6 .69 C
ATOM 901 C ILE A 207 -5 .280 .901 1 .186 1. .00 6. .65 C
ATOM 902 O ILE A 207 -5 .635 5 .728 2 .039 1 .00 5. .55 0
ATOM 903 CB ILE A 207 -3 .772 2 .974 1 .749 1 .00 4 .84 C
ATOM 904 CGI ILE A 207 -3 .769 1 .547 2 .340 1 .00 6 .07 C
ATOM 905 CG2 ILE A 207 -3 .072 3 .984 2 .664 1 .00 5 .33 C
ATOM 906 CDl ILE A 207 -2 .368 0 .923 2 .318 1 .00 6 .90 C
ATOM 907 N ARG A 208 -4 .945 5 .229 -0 .056 1 .00 5 .80 N
ATOM 908 CA ARG A 208 -4 .962 6 .626 -0 .500 1 .00 7 .25 C
ATOM 909 C ARG A 208 -6 .349 7 .205 -0 .305 1 .00 8 .00 C
ATOM 910 0 ARG A 208 -6 .494 8 .305 0 .255 1 .00 7 .26 0
ATOM 911 CB ARG A 208 -4 .500 6 .734 -1 .967 1. .00 7, .91 C
ATOM 912 CG ARG A 208 -4 .591 8 .134 -2 .560 1. .00 8. .82 C
ATOM 913 CD ARG A 208 -4 .430 8 .105 -4 .089 1 .00 12 .48 C
ATOM 914 NE ARG A 208 -4 .761 9 .411 - .660 1 .00 17. .58 N
ATOM 915 CZ ARG A 208 -4 .008 10 .500 -4 .595 1 .00 18 .05 C
ATOM 916 NHl ARG A 208 -2 .813 10 .447 -4 .042 1 .00 18 .69 N ATOM 917 NH2 ARG A 208 -4.390 11.662 -5.107 1.00 18.85 N
ATOM 918 N GLU A 209 -7.387 6. 464 -0. 697 1. 00 8. 98 N
ATOM 919 CA GLU A 209 -8.762 6. 936 -0. 549 1. 00 9. 20 C
ATOM 920 C GLU A 209 -9.100 7. 252 0. 907 1. 00 9. 37 C
ATOM 921 0 GLU A 209 -9.811 8. 213 1. 198 1. 00 5. 42 O
ATOM 922 CB GLU A 209 -9.801 5. 898 -1. 011 1. 00 14. 19 C
ATOM 923 CG GLU A 209 -9.775 5. 577 -2. 482 1. 00 19. 51 C
ATOM 924 CD GLU A 209 10.953 4. 737 -2. 955 1. 00 27. 56 C
ATOM 925 OE1 GLU A 209 11.688 4. 142 -2. 142 1. 00 23. 86 O
ATOM 926 OE2 GLU A 209 11.168 4. 699 -4. 190 1. 00 31. 35 O
ATOM 927 N ILE A 210 -8.689 6. 342 1. 796 1. 00 8. 27 N
ATOM 928 CA ILE A 210 -8.939 6. 537 3. 227 1. 00 8. 19 C
ATOM 929 C ILE A 210 -8.127 7. 721 3. 754 1. 00 7. 27 C
ATOM 930 0 ILE A 210 -8.739 8. 567 4. 436 1. 00 8. 19 O
ATOM 931 CB ILE A 210 -8.574 5. 249 3. 992 1. 00 9. 16 C
ATOM 932 CGI ILE A 210 -9.549 4. 163 3. 491 1. 00 8. 59 C
ATOM 933 CG2 ILE A 210 -8.663 5. 453 5. .503 1. 00 7. 84 C
ATOM 934 CDl ILE A 210 -9.135 2. 750 3. 850 1. 00 10. 60 C
ATOM 935 N LEU A 211 -6.863 7. 839 3. .375 1. .00 5. 07 N
ATOM 936 CA LEU A 211 -6.078 8. 999 3. ,850 1. .00 6. 69 C
ATOM 937 C LEU A 211 -6.699 10. .305 3. .366 1. ,00 6. .81 C
ATOM 938 0 LEU A 211 -6.818 11. .271 4. ,153 1. ,00 8. .01 O
ATOM 939 CB LEU A 211 -4.601 8. .904 3. ,452 1. .00 4. .38 C
ATOM 940 CG LEU A 211 -3.888 7. 624 3. .952 1. .00 7. 45 C
ATOM 941 CDl LEU A 211 -2.414 7. .656 3. ,560 1. .00 8. 00 C
ATOM 942 CD2 LEU A 211 -4.015 7. .430 5. ,452 1. .00 5. .27 C
ATOM 943 N ILE A 212 -7.118 10. .390 2. ,120 1. ,00 7. 40 N
ATOM 944 CA ILE A 212 -7.801 11. ,589 1. ,608 1. ,00 6. ,87 C
ATOM 945 C ILE A 212 -9.026 11. .931 2. ,435 1. ,00 9. ,74 C
ATOM 946 0 ILE A 212 -9.303 13. .118 2. .669 1. ,00 8. ,71 O
ATOM 947 CB ILE A 212 -8.200 11. .389 0. .129 1. .00 11. ,16 C
ATOM 948 CGI ILE A 212 -6.928 11. .407 -0, .743 1. .00 13. ,44 C
ATOM 949 CG2 ILE A 212 -9.192 12. .447 -0. .350 1. .00 10. .28 c
ATOM 950 CDl ILE A 212 -7.159 11. .067 -2. .205 1. .00 14. .96 c
ATOM 951 N SER A 213 -9.794 10. .940 2. .885 1. .00 9. .55 N
ATOM 952 CA SER A 213 ■10.992 11. .131 3. .688 1, .00 9. .05 C
ATOM 953 C SER A 213 -10.670 11. .535 5. .124 1. .00 10. .31 C
ATOM 954 0 SER A 213 ■11.534 12. .085 5. .825 1. .00 10. .55 O
ATOM 955 CB SER A 213 •11.906 9. .887 3. .682 1. .00 10. .81 C
ATOM 956 OG SER A 213 -11.416 8. .921 4. .600 1. .00 14. .21 O
ATOM 957 N PHE A 214 -9.423 11. .361 5. .552 1. .00 7. .72 N
ATOM 958 CA PHE A 214 -8.973 11, .784 6, .869 1. .00 6. .91 C
ATOM 959 C PHE A 214 -7.857 12, .811 6, .726 1, .00 6. .54 C
ATOM 960 0 PHE A 214 -6.825 12, .751 7, .397 1, .00 5. .46 O
ATOM 961 CB PHE A 214 -8.517 10, .572 7. .718 1, .00 7. .89 C
ATOM 962 CG PHE A 214 -9.681 9, .776 8. .269 1, .00 7. .67 C
ATOM 963 CDl PHE A 214 -10.359 10, .203 9 .394 1. .00 6, .38 C
ATOM 964 CD2 PHE A 214 -10.100 8, .616 7 .637 1 .00 8, .19 C
ATOM 965 CE1 PHE A 214 -11.432 9, .478 9, .884 1, .00 10, .20 C
ATOM 966 CE2 PHE A 214 -11.173 7, .884 8, .124 1. .00 10, .30 c
ATOM 967 CZ PHE A 214 -11.842 8. .314 9, .262 1. .00 9, .78 c
ATOM 968 N SER A 215 -8.016 13. .782 5, .808 1. .00 4, .80 N
ATOM 969 CA SER A 215 -6.997 14. .821 5 .612 1 .00 6, .15 C
ATOM 970 C SER A 215 -6.789 15 .757 6 .800 1 .00 7, .31 C
ATOM 971 0 SER A 215 -5.872 16 .593 6 .816 1 .00 7 .37 0
ATOM 972 CB SER A 215 -7.343 15 .653 4 .369 1 .00 7 .97 c
ATOM 973 OG SER A 215 -8.585 16 .325 4 .547 1 .00 11 .45 0
ATOM 974 N ASP A 216 -7.645 15 .679 7 .812 1 .00 6 .24 N
ATOM 975 CA ASP A 216 -7.578 16 .404 9 .055 1 .00 8 .27 C
ATOM 976 C ASP A 216 -6.767 15 .636 10 .105 1 .00 9 .81 C
ATOM 977 0 ASP A 216 -6.671 16 .088 11 .245 1 .00 9 .16 O
ATOM 978 CB ASP A 216 -8.980 16 .663 9 .637 1 .00 9 .81 C
ATOM 979 CG ASP A 216 -9.831 15 .421 9 .784 1 .00 12 .85 C
ATOM 980 ODl ASP A 216 -9.695 14 .429 9 .033 1 .00 10 .45 O
ATOM 981 OD2 ASP A 216 -10.692 15 .391 10 .687 1 .00 15 .34 O
ATOM 982 N VAL A 217 -6.190 14 .487 9 .749 1 .00 5 .95 N
ATOM 983 CA VAL A 217 -5.360 13 .723 10 .683 1 .00 5 .79 C
ATOM 984 C VAL A 217 -3.938 13 .613 10 .124 1 .00 7 .70 C
ATOM 985 0 VAL A 217 -3.735 12 .902 9 .151 1 .00 5 .95 O
ATOM 986 CB VAL A 217 -5.911 12 .334 10 .993 1 .00 9 .08 C
ATOM 987 CGI VAL A 217 -4.996 11 .613 11 .995 1 .00 8 .10 C
ATOM 988 CG2 VAL A 217 -7.317 12 .378 11 .593 1 .00 8 .01 C ATOM 989 N ARG A 218 -2.984 14.287 10.773 1.00 7.72 N
ATOM 990 CA ARG A 218 -1.606 14. 206 10. 279 1. 00 8.05 C
ATOM 991 C ARG A 218 -1.222 12. 723 10. 372 1. 00 9.55 C
ATOM 992 0 ARG A 218 -1.431 12. 118 11. 429 1. 00 8.04 O
ATOM 993 CB ARG A 218 -0.644 15. 065 11. 087 1. 00 9.92 C
ATOM 994 CG ARG A 218 0.727 15. 180 10. 422 1. 00 12.76 C
ATOM 995 CD ARG A 218 1.728 15. 977 11. 253 1. 00 10.15 C
ATOM 996 NE ARG A 218 1.237 17. .334 11. 507 1. 00 11.99 N
ATOM 997 CZ ARG A 218 1.944 18. .259 12. 160 1. 00 13.54 C
ATOM 998 NHl ARG A 218 3.164 17. .975 12. .601 1. 00 12.59 N
ATOM 999 NH2 ARG A 218 1.452 19. .476 12. ,384 1. 00 10.56 N
ATOM 1000 N THR A 219 -0.697 12. ,195 9. ,276 1. ,00 7.51 N
ATOM 1001 CA THR A 219 -0.395 10. ,762 9. ,218 1. .00 8.29 C
ATOM 1002 C THR A 219 1.046 10. ,497 8. ,809 1. 00 8.47 C
ATOM 1003 0 THR A 219 1.514 10. ,933 7. .766 1. 00 6.27 O
ATOM 1004 CB THR A 219 -1.359 10. .093 8. ,215 1. ,00 8.28 C
ATOM 1005 OGl THR A 219 -2.725 10. .291 8. 627 1. 00 7.46 O
ATOM 1006 CG2 THR A 219 -1.118 8. .588 8. 121 1. 00 8.07 C
ATOM 1007 N ILE A 220 1.781 9. .799 9. 677 1. 00 7.04 N
ATOM 1008 CA ILE A 220 3.192 9. 486 9. 398 1. 00 7.74 C
ATOM 1009 C ILE A 220 3.272 8. .026 8. 982 1. 00 6.46 C
ATOM 1010 0 ILE A 220 2.739 7. ,170 9. 692 1. 00 5.26 O
ATOM 1011 CB ILE A 220 4.044 9. ,834 10. ,625 1. 00 7.97 C
ATOM 1012 CGI ILE A 220 3.943 11. ,354 10. .891 1. 00 9.58 C
ATOM 1013 CG2 ILE A 220 5.493 9. .406 10. .446 1. 00 8.88 C
ATOM 1014 CDl ILE A 220 4.225 11. ,767 12. ,324 1. ,00 11.24 C
ATOM 1015 N LEU A 221 3.910 7. ,730 7. .846 1. 00 4.42 N
ATOM 1016 CA LEU A 221 4.010 6. ,376 7. ,365 1. ,00 6.25 C
ATOM 1017 C LEU A 221 5.442 5. .863 7. ,213 1. .00 8.14 C
ATOM 1018 O LEU A 221 6.346 6. .579 6. ,779 1. ,00 7.11 0
ATOM 1019 CB LEU A 221 3.407 6. .243 5. ,931 1. ,00 6.11 c
ATOM 1020 CG LEU A 221 1.985 6. .793 5. .768 1. ,00 8.34 c
ATOM 1021 CDl LEU A 221 1.566 6. .788 4. .300 1. ,00 8.35 c
ATOM 1022 CD2 LEU A 221 0.973 5. .975 6. .577 1. ,00 4.68 c
ATOM 1023 N VAL A 222 5.592 4. .582 7. .549 1. ,00 5.20 N
ATOM 1024 CA VAL A 222 6.867 3. .906 7. .304 1. ,00 5.61 C
ATOM 1025 C VAL A 222 6.541 3. .014 6. .099 1. .00 5.98 C
ATOM 1026 O VAL A 222 5.570 2. .247 6. .152 1. .00 6.56 O
ATOM 1027 CB VAL A 222 7.393 3. .085 8. .477 1. .00 8.41 C
ATOM 1028 CGI VAL A 222 8.539 2. .173 8. .068 1. .00 6.12 C
ATOM 1029 CG2 VAL A 222 7.894 4, .027 9. .576 1. .00 6.69 c
ATOM 1030 N ILE A 223 7.297 3, .159 5. .014 1. .00 6.12 N
ATOM 1031 CA ILE A 223 7.018 2, .373 3. .826 1. .00 5.11 C
ATOM 1032 C ILE A 223 7.865 1. .110 3. .763 1. .00 6.29 C
ATOM 1033 O ILE A 223 9.086 1. .170 3. .619 1. .00 5.79 O
ATOM 1034 CB ILE A 223 7.239 3. .173 2. .517 1. .00 5.92 C
ATOM 1035 CGI ILE A 223 6.440 4, .490 2. .557 1. .00 5.92 c
ATOM 1036 CG2 ILE A 223 6.843 2. .332 1, .305 1. .00 9.29 c
ATOM 1037 CDl ILE A 223 4.940 4 .302 2, .735 1. .00 3.99 c
ATOM 1038 N GLU A 224 7.174 -0 .023 3, .783 1, .00 7.38 N
ATOM 1039 CA GLU A 224 7.718 -1 .348 3, .561 1. .00 5.45 C
ATOM 1040 C GLU A 224 9.063 -1 .750 4, .140 1, .00 6.90 C
ATOM 1041 0 GLU A 224 10.090 -1 .913 3, .466 1, .00 5.04 O
ATOM 1042 CB GLU A 224 7.752 -1. .568 2. .032 1, .00 6.41 C
ATOM 1043 CG GLU A 224 6.387 -1 .497 1 .317 1, .00 4.81 C
ATOM 1044 CD GLU A 224 5.466 -2 .652 1 .652 1 .00 6.84 c
ATOM 1045 OE1 GLU A 224 5.958 -3 .707 2 .120 1 .00 6.22 0
ATOM 1046 OE2 GLU A 224 4.237 -2 .557 1 .460 1 .00 5.52 0
ATOM 1047 N PRO A 225 9.084 -2 .095 5. .423 1. .00 6.71 N
ATOM 1048 CA PRO A 225 10.274 -2 .656 6 .051 1 .00 8.09 C
ATOM 1049 C PRO A 225 10.767 -3 .901 5. .313 1 .00 10.00 C
ATOM 1050 O PRO A 225 10.009 -4 .657 4 .678 1 .00 7.14 O
ATOM 1051 CB PRO A 225 9.770 -3 .045 7 .438 1 .00 9.09 C
ATOM 1052 CG PRO A 225 8.619 -2 .126 7 .711 1 .00 7.49 C
ATOM 1053 CD PRO A 225 7.926 -1 .993 6 .363 1 .00 6.45 c
ATOM 1054 N ASP A 226 12.084 -4 .153 5 .348 1 .00 10.93 N
ATOM 1055 CA ASP A 226 12.639 -5 .358 4 .718 1 .00 10.38 C
ATOM 1056 C ASP A 226 12.259 -5 .464 3. .249 1. .00 10.37 C
ATOM 1057 O ASP A 226 11.984 -6 .559 2 .750 1 .00 10.02 O
ATOM 1058 CB ASP A 226 12.172 -6 .595 5 .489 1. .00 13.13 C
ATOM 1059 CG . AASP A 226 12.883 -7 .895 5 .169 0. .50 11.23 C
ATOM 1060 CG BASP A 226 12.838 -6 .714 6 .844 0. .50 16.23 C ATOM 1061 OD2AASP A 226 12.269 -8.989 5.193 0.50 7.45 0
ATOM 1062 OD2BASP A 226 13. 364 -5. 720 7. 384 0. 50 17. 41 0
ATOM 1063 ODIAASP A 226 14. 097 -7. 854 4. 880 0. 50 10. 95 0
ATOM 1064 ODIBASP A 226 12. 859 -7. 821 7. .414 0. 50 18. 21 0
ATOM 1065 N SER A 227 12. 377 -4. 362 2. 506 1. 00 7. 14 N
ATOM 1066 CA SER A 227 12. 089 -4. 405 1. 069 1. 00 8. 07 C
ATOM 1067 C SER A 227 13. 321 -3. 964 0. 290 1. 00 8. 60 C
ATOM 1068 0 SER A 227 14. 169 -4. 804 -0. 011 1. 00 7. 25 O
ATOM 1069 CB SER A 227 10. 844 -3. 643 0. 674 1. 00 8. 53 C
ATOM 1070 OG SER A 227 10. 899 -2. 242 0. 929 1. 00 6. 19 O
ATOM 1071 N LEU A 228 13. 467 -2. 671 0. 005 1. 00 9. 78 N
ATOM 1072 CA LEU A 228 14. 606 -2. 190 -0. 765 1. 00 10. 16 C
ATOM 1073 C LEU A 228 15. 971 -2. 396 -0. 150 1. 00 11. 89 C
ATOM 1074 0 LEU A 228 16. 936 -2. 500 -0. 923 1. 00 9. 90 O
ATOM 1075 CB LEU A 228 14. 415 -0. 717 -1. .154 1. 00 12. 52 c
ATOM 1076 CG LEU A 228 13. 187 -0. 457 -2. .044 1. 00 10. 94 c
ATOM 1077 CDl LEU A 228 13. 015 1. 032 -2. .258 1. 00 10. 51 c
ATOM 1078 CD2 LEU A 228 13. 333 -1. 187 -3. ,379 1. 00 12. .27 c
ATOM 1079 N ALA A 229 16. 106 -2. 590 1. .158 1. 00 10. .91 N
ATOM 1080 CA ALA A 229 17. 402 -2. 905 1. ,755 1. .00 10. ,73 C
ATOM 1081 C ALA A 229 17. 939 -4. .214 1. ,165 1. .00 9. ,94 C
ATOM 1082 o ALA A 229 19. ,151 -4. ,412 1. ,091 1. .00 8. ,43 O
ATOM 1083 CB ALA A 229 17. .331 -3. ,029 3. .270 1. .00 10. ,39 C
ATOM 1084 N ASN A 230 17. ,043 -5. ,134 0. .796 1. .00 10. ,02 N
ATOM 1085 CA ASN A 230 17. ,402 -6. ,383 0. .154 1. ,00 9. ,78 C
ATOM 1086 C ASN A 230 18. .080 -6. ,167 -1. .190 1. ,00 11. ,01 C
ATOM 1087 0 ASN A 230 18. ,924 -6. .985 -1. .607 1. .00 8. .16 O
ATOM 1088 CB ASN A 230 16. ,180 -7. .289 -0. .076 1. .00 10. .90 C
ATOM 1089 CG ASN A 230 15. ,665 -7. .868 1. .232 1. .00 13. .68 C
ATOM 1090 ODl ASN A 230 16. ,356 -8. ,610 1. .937 1. ,00 11. ,06 O
ATOM 1091 ND2 ASN A 230 14. ,437 -7. ,511 1. .589 1. ,00 15. ,05 N
ATOM 1092 N MET A 231 17. .715 -5. ,091 -1. .899 1. ,00 9. .45 N
ATOM 1093 CA MET A 231 18. .340 -4. ,808 -3. .192 1. .00 10. .59 C
ATOM 1094 C MET A 231 19. .808 -4. .410 -3. .053 1. .00 10. .84 C
ATOM 1095 0 MET A 231 20. .564 -4. .461 -4. .022 1. .00 12. .21 O
ATOM 1096 CB MET A 231 17. .608 -3. .666 -3. .919 1. .00 12. .34 C
ATOM 1097 CG MET A 231 16. .450 -4. .121 -4. .794 1. .00 15. .64 C
ATOM 1098 SD MET A 231 15. .058 -4. .853 -3. .927 1. .00 11. .65 S
ATOM 1099 CE MET A 231 15. .413 -6. .601 -3. .854 1. .00 13. .16 C
ATOM 1100 N VAL A 232 20. .200 -3. .884 -1. .900 1. .00 11. .74 N
ATOM 1101 CA VAL A 232 21. .588 -3. .474 -1, .680 1. .00 11. .04 C
ATOM 1102 C VAL A 232 22. .452 -4. .703 -1, .472 1, .00 11, .67 C
ATOM 1103 0 VAL A 232 23. .484 -4. .871 -2, .124 1, .00 13. .75 O
ATOM 1104 CB VAL A 232 21. .697 -2. .530 -0. .458 1, .00 10. .10 C
ATOM 1105 CGI VAL A 232 23. .134 -2, .096 -0, .176 1, .00 12, .45 C
ATOM 1106 CG2 VAL A 232 20, .817 -1, .303 -0 .703 1, .00 10, .12 C
ATOM 1107 N THR A 233 22, .042 -5, .620 -0 .579 1. .00 11, .16 N
ATOM 1108 CA THR A 233 22, .885 -6, .754 -0 .252 1 .00 11. .44 C
ATOM 1109 C THR A 233 22, .409 -8. .159 -0 .569 1 .00 12. .43 C
ATOM 1110 0 THR A 233 23, .254 -9. .071 -0 .499 1 .00 13. .82 O
ATOM 1111 CB THR A 233 23 .152 -6. .773 1. .286 1 .00 12 .21 C
ATOM 1112 OGl THR A 233 21 .935 -7 .075 1 .982 1 .00 11 .48 O
ATOM 1113 CG2 THR A 233 23 .726 -5 .458 1 .773 1 .00 12 .53 C
ATOM 1114 N ASN A 234 21 .127 -8 .356 -0 .818 1 .00 11 .88 N
ATOM 1115 CA ASN A 234 20. .616 -9, .717 -0 .990 1. .00 13, .01 C
ATOM 1116 C ASN A 234 20, .192 -10, .087 -2 .389 1 .00 13. .03 C
ATOM 1117 0 ASN A 234 19. .417 -11. .045 -2 .547 1 .00 12 .32 O
ATOM 1118 CB ASN A 234 19 .422 -9 .917 -0 .011 1 .00 11 .09 C
ATOM 1119 CG ASN A 234 19 .900 -9 .933 1 .425 1 .00 12 .72 C
ATOM 1120 ODl ASN A 234 21 .021 -10 .376 1 .709 1 .00 15 .41 O
ATOM 1121 ND2 ASN A 234 19 .083 -9 .488 2 .364 1 .00 11 .44 N
ATOM 1122 N MET A 235 20 .732 -9 .438 -3 .422 1 .00 13 .27 N
ATOM 1123 CA MET A 235 20 .423 -9 .806 -4 .801 1 .00 15 .84 C
ATOM 1124 C MET A 235 20 .991 -11 .142 -5 .243 1 .00 16 .75 C
ATOM 1125 0 MET A 235 20 .510 -11 .707 -6 .236 1 .00 16 .47 O
ATOM 1126 CB MET A 235 20 .954 -8 .728 -5 .757 1 .00 16 .88 C
ATOM 1127 CG MET A 235 20 .264 -7 .389 -5 .527 1 .00 19 .25 C
ATOM 1128 SD MET A 235 18 .530 -7 .530 -6 .067 1 .00 18 .42 S
ATOM 1129 CE MET A 235 18 .808 -7 .014 -7 .770 1 .00 13 .39 C
ATOM 1130 N ASN A 236 21 .905 -11 .734 -4 .466 1 .00 16 .70 N
ATOM 1131 CA ASN A 236 22 .385 -13 .080 -4 .752 1 .00 18 .69 C
ATOM 1132 C ASN A 236 21 .281 -14 .103 -4 .516 1 .00 17 .60 c ATOM 1133 O ASN A 236 21.370 -15.234 -5.014 1.00 19.39 o
ATOM 1134 CB ASN A 236 23. 592 -13. 434 -3. 878 1. 00 24. 86 c
ATOM 1135 CG ASN A 236 23. 375 -13. 190 -2. 401 1. 00 29. 76 c
ATOM 1136 ODl ASN A 236 23. 012 -12. 095 -1. 965 1. 00 30. 79 o
ATOM 1137 ND2 ASN A 236 23. 608 -14. 195 -1. 564 1. 00 32. 96 N
ATOM 1138 N VAL A 237 20. 265 -13. 744 -3. 720 1. 00 12. 86 N
ATOM 1139 CA VAL A 237 19. 159 -14. 656 -3. 440 1. 00 10. 84 C
ATOM 1140 C VAL A 237 18. 199 -14. 566 -4. 601 1. .00 10. 77 C
ATOM 1141 O VAL A 237 17. 678 -13. 470 -4. 874 1. 00 8. 02 O
ATOM 1142 CB VAL A 237 18. 450 -14. 269 -2. 128 1. .00 12. .65 C
ATOM 1143 CGI VAL A 237 17. 229 -15. 166 -1. 897 1. .00 9. .59 C
ATOM 1144 CG2 VAL A 237 19. 411 -14. 335 -0. 951 1. ,00 12. ,38 C
ATOM 1145 N PRO A 238 17. 933 -15. 670 -5. .290 1. ,00 11. .53 N
ATOM 1146 CA PRO A 238 17. ,135 -15. 606 -6. .508 1. ,00 13. ,54 C
ATOM 1147 C PRO A 238 15. .788 -14. 927 -6. ,356 1. ,00 13. ,33 C
ATOM 1148 O PRO A 238 15. ,396 -14. .168 -7. ,260 1. ,00 11. .57 O
ATOM 1149 CB PRO A 238 17. 065 -17. 067 -6. 975 1. ,00 14. 34 C
ATOM 1150 CG PRO A 238 18. 402 -17. 598 -6. 532 1. .00 13. 36 C
ATOM 1151 CD PRO A 238 18. 597 -16. 987 -5. 147 1. .00 12. 77 C
ATOM 1152 N LYS A 239 15. 057 -15. 133 -5. 272 1. ,00 9. .72 N
ATOM 1153 CA LYS A 239 13. ,747 -14. 485 -5. 107 1. ,00 11. ,18 C
ATOM 1154 C LYS A 239 13. .898 -12. 963 -5. .032 1. ,00 11. .25 C
ATOM 1155 O LYS A 239 13. .080 -12. .221 -5. ,597 1. ,00 10. ,72 O
ATOM 1156 CB LYS A 239 13. .000 -15. .028 -3. ,895 1. .00 11. ,60 C
ATOM 1157 CG LYS A 239 11. ,556 -14. .534 -3. ,816 1. .00 9. .45 C
ATOM 1158 CD LYS A 239 10. ,745 -15. .325 -2. ,815 1. .00 12. .82 c
ATOM 1159 CE LYS A 239 9. .280 -14. ,874 -2. ,783 1. .00 11. .28 c
ATOM 1160 NZ LYS A 239 8. .531 -15. ,664 -1. ,755 1. .00 13. .11 N
ATOM 1161 N CYS A 240 14. .998 -12. .503 -4. .454 1. .00 9. .32 N
ATOM 1162 CA CYS A 240 15. .282 -11. .070 -4. .374 1. .00 11. .03 C
ATOM 1163 C CYS A 240 15. .647 -10. .495 -5. .727 1. .00 11. .24 C
ATOM 1164 O CYS A 240 15. .131 -9. .438 -6. .097 1. .00 11. .81 O
ATOM 1165 CB CYS A 240 16. .353 -10. .776 -3. .337 1. .00 11. .15 C
ATOM 1166 SG CYS A 240 15. .880 -10. .935 -1. ,606 1. .00 10. .16 S
ATOM 1167 N SER A 241 16. .485 -11. .187 -6. ,535 1. .00 11. .59 N
ATOM 1168 CA SER A 241 16. .794 -10. .609 -7. .842 1. .00 10. .98 C
ATOM 1169 C SER A 241 15. .546 -10. .620 -8. .721 1. .00 12. .23 C
ATOM 1170 O SER A 241 15. .364 -9. .712 -9. .539 1. .00 10. .81 0
ATOM 1171 CB SER A 241 17. .975 -11. .312 -8. .522 1, .00 14. .36 C
ATOM 1172 OG SER A 241 17. .623 -12. .670 -8. .727 1, .00 17. .92 O
ATOM 1173 N GLY A 242 14, .682 -11. .620 -8. .525 1. .00 9. .61 N
ATOM 1174 CA GLY A 242 13, .437 -11. .713 -9. .280 1, .00 11, .36 C
ATOM 1175 C GLY A 242 12, .417 -10. .676 -8, .821 1, .00 9, .27 C
ATOM 1176 O GLY A 242 11, .547 -10. .289 -9, .600 1. .00 9. .69 0
ATOM 1177 N ALA A 243 12, .504 -10. .218 -7, .577 1 .00 8, .27 N
ATOM 1178 CA ALA A 243 11. .534 -9. .251 -7, .064 1. .00 9, .72 C
ATOM 1179 C ALA A 243 11. .966 -7, .798 -7, .195 1. .00 9, .87 C
ATOM 1180 O ALA A 243 11. .124 -6, .889 -7, .101 1. .00 7. .13 O
ATOM 1181 CB ALA A 243 11 .322 -9, .519 -5. .570 1. .00 9, .32 C
ATOM 1182 N ALA A 244 13 .264 -7. .577 -7. .399 1. .00 9. .86 N
ATOM 1183 CA ALA A 244 13, .819 -6. .236 -7, .422 1. .00 9, .88 C
ATOM 1184 C ALA A 244 13, .058 -5, .229 -8, .259 1, .00 9. .98 C
ATOM 1185 O ALA A 244 12, .794 -4, .128 -7, .758 1. .00 8, .52 0
ATOM 1186 CB ALA A 244 15. .293 -6, .280 -7, .855 1. .00 8, .30 C
ATOM 1187 N SER A 245 12 .827 -5, .478 -9. .557 1. .00 9, .52 N
ATOM 1188 CA SER A 245 12 .158 -4, .461 -10, .365 1 .00 10. .82 C
ATOM 1189 C SER A 245 10 .756 -4, .175 -9 .832 1. .00 11, .56 C
ATOM 1190 O SER A 245 10 .316 -3, .022 -9. .846 1 .00 11 .54 0
ATOM 1191 CB SER A 245 12 .087 -4 .828 -11 .856 1 .00 11 .02 C
ATOM 1192 OG ASER A 245 11 .406 -6 .064 -12. .001 0 .50 13 .46 O
ATOM 1193 OG BSER A 245 13 .372 -4 .621 -12. .429 0 .50 11 .05 O
ATOM 1194 N THR A 246 10 .041 -5 .209 -9. .369 1 .00 10 .04 N
ATOM 1195 CA THR A 246 8 .708 -5 .019 -8. .815 1 .00 10 .31 C
ATOM 1196 C THR A 246 8 .746 -4 .210 -7 .530 1 .00 8 .77 C
ATOM 1197 O THR A 246 7 .950 -3 .275 -7 .371 1 .00 9 .85 0
ATOM 1198 CB THR A 246 8 .040 -6 .387 -8 .524 1 .00 11 .56 C
ATOM 1199 OGl THR A 246 7 .898 -7 .080 -9. .757 1 .00 9. .95 O
ATOM 1200 CG2 THR A 246 6 .675 -6 .177 -7 .889 1 .00 13. .88 C
ATOM 1201 N TYR A 247 9 .687 - .501 -6 .633 1 .00 7 .35 N
ATOM 1202 CA TYR A 247 9 .820 -3. .680 -5 .425 1 .00 5 .31 C TOM 1203 C TYR A 247 10 .095 -2 .223 -5 .818 1 .00 8 .45 C
ATOM 1204 O TYR A 247 9 .554 -1 .322 -5 .174 1 .00 8 .15 O ATOM 1205 CB TYR A 247 10.964 -4.149 -4.543 1..00 7..25 c
ATOM 1206 CG TYR A 247 10. 812 -5. 356 -3. 654 1. .00 5. .93 c
ATOM 1207 CDl TYR A 247 9. 760 -6. 251 -3. 782 1. .00 7. ,84 c
ATOM 1208 CD2 TYR A 247 11. 782 -5. .599 -2. 687 1. .00 5. ,89 c
ATOM 1209 CE1 TYR A 247 9. 683 -7. .359 -2. 943 1. ,00 8. ,77 c
ATOM 1210 CE2 TYR A 247 11. 738 -6. ,708 -1. 864 1. ,00 7. .30 c
ATOM 1211 CZ TYR A 247 10. 670 -7. 583 -2. 005 1. 00 8. 15 c
ATOM 1212 OH TYR A 247 10. 621 -8. 706 -1. 200 1. 00 9. 79 0
ATOM 1213 N ARG A 248 10. 955 -1. 993 -6. 806 1. 00 9. 34 N
ATOM 1214 CA ARG A 248 11. 263 -0. .611 -7. 196 1. .00 10. ,80 c
ATOM 1215 C ARG A 248 10. 000 0. .067 -7. 725 1. .00 10. ,45 c
ATOM 1216 O ARG A 248 9. 688 1. .163 -7. 285 1. .00 8. .94 o
ATOM 1217 CB ARG A 248 12. 402 -0. .503 -8. 214 1. ,00 12. ,72 c
ATOM 1218 CG AARG A 248 12. 641 0. ,928 -8. 699 0. ,50 12. ,38 c
ATOM 1219 CG ] BARG A 248 12. 270 0. ,660 -9. .186 0. .50 17. ,76 c
ATOM 1220 CD AARG A 248 13. 730 1. ,057 -9. ,756 0. ,50 15. ,55 c
ATOM 1221 CD BARG A 248 13. 565 0. 956 -9. 942 0. .50 22. .28 c
ATOM 1222 NE AARG A 248 13. 710 2. .362 -10. 429 0. .50 12. .89 N
ATOM 1223 NE ] BARG A 248 13. 843 2. .384 -9. 730 0. .50 25. ,14 N
ATOM 1224 CZ AARG A 248 12. 903 2. ,720 -11. 413 0. ,50 14. .27 C
ATOM 1225 CZ ] BARG A 248 15. 026 2. ,886 -9. 411 0. ,50 24. .43 C
ATOM 1226 NH1AARG A 248 12. ,018 1. ,864 -11. ,921 0. .50 15. .68 N
ATOM 1227 NH1BARG A 248 16. .065 2. .069 -9. .294 0. .50 27. .65 N
ATOM 1228 NH2AARG A 248 12. ,932 3. ,945 -11. ,929 0. .50 12. .72 N
ATOM 1229 NH2BARG A 248 15. .171 4. .186 -9. ,194 0. .50 20. .27 N
ATOM 1230 N GLU A 249 9. ,334 -0. .560 -8. ,699 1. .00 9. .14 N
ATOM 1231 CA GLU A 249 8. 155 0. ,007 -9. 324 1. ,00 11. .86 C
ATOM 1232 C GLU A 249 7. .014 0. ,270 -8. 342 1. .00 11. .04 C
ATOM 1233 O GLU A 249 6. ,338 1. .299 -8. .404 1. .00 9. .44 O
ATOM 1234 CB GLU A 249 7. ,639 -0. ,907 -10. .447 1. .00 15. .60 C
ATOM 1235 CG GLU A 249 6. ,258 -0. .557 -10. ,968 1. .00 26. .28 C
ATOM 1236 CD GLU A 249 5. .399 -1. .675 -11. ,504 1. .00 34. .08 C
ATOM 1237 OE1 GLU A 249 5. .717 -2. .882 -11. ,348 1. .00 36. .44 O
ATOM 1238 OE2 GLU A 249 4. .334 -1. .373 -12. .103 1. .00 37. .85 0
ATOM 1239 N LEU A 250 6. .764 -0. .682 -7. .457 1. .00 8. .69 N
ATOM 1240 CA LEU A 250 5. .690 -0. .555 -6. .480 1. .00 8. .28 C
ATOM 1241 C LEU A 250 6. .018 0. .439 -5. .377 1. .00 10. .64 C
ATOM 1242 O LEU A 250 5. .113 1. .137 -4. .916 1. .00 10. .39 0
ATOM 1243 CB LEU A 250 5. .318 -1. .931 -5. .922 1. .00 11. .06 C
ATOM 1244 CG LEU A 250 4. .659 -2. .872 -6. .942 1. .00 9. .15 C
ATOM 1245 CDl LEU A 250 4. .275 -4. .171 -6. .250 1. .00 6. .98 C
ATOM 1246 CD2 LEU A 250 3. .457 -2, .211 -7. .617 1. .00 6. .07 c
ATOM 1247 N THR A 251 7. .293 0, .585 -5, .017 1, .00 8, .51 N
ATOM 1248 CA THR A 251 7. .668 1, .608 -4. .035 1, .00 7, .50 C
ATOM 1249 C THR A 251 7, .401 2. .978 -4. .660 1 .00 7, .68 C
ATOM 1250 O THR A 251 6. .779 3. .872 -4, .055 1 .00 8, .26 O
ATOM 1251 CB THR A 251 9. .146 1, .452 -3. .629 1, .00 8, .52 C
ATOM 1252 OGl THR A 251 9, .332 0, .179 -2. .992 1, .00 10, .75 O
ATOM 1253 CG2 THR A 251 9, .555 2, .553 -2. .655 1. .00 4, .33 c
ATOM 1254 N ILE A 252 7, .818 3. .173 -5. .907 1. .00 7, .33 N
ATOM 1255 CA ILE A 252 7. .574 4 .449 -6, .601 1 .00 8, .12 C
ATOM 1256 C ILE A 252 6, .080 4 .720 -6, .667 1 .00 9. .23 C
ATOM 1257 O ILE A 252 5 .616 5 .821 -6, .332 1 .00 9 .66 0
ATOM 1258 CB ILE A 252 8 .260 .512 -7. .979 1 .00 8 .41 C
ATOM 1259 CGI ILE A 252 9 .776 4 .518 -7, .776 1 .00 5 .97 C
ATOM 1260 CG2 ILE A 252 7 .819 5 .776 -8 .726 1 .00 6 .79 C
ATOM 1261 CDl ILE A 252 10. .655 4. .280 -8, .990 1. .00 6. .68 C
ATOM 1262 N TYR A 253 5. .291 3 .723 -7, .045 1. .00 10 .43 N
ATOM 1263 CA TYR A 253 3 .842 3 .829 -7, .063 1 .00 10 .43 C
ATOM 1264 C TYR A 253 3 .309 .297 -5, .716 1 .00 10 .13 c
ATOM 1265 0 TYR A 253 2 .536 5 .241 -5. .660 1 .00 9 .33 0
ATOM 1266 CB TYR A 253 3 .209 2 .467 -7 .421 1 .00 9 .73 c
ATOM 1267 CG TYR A 253 1 .724 2 .557 -7 .706 1 .00 11 .41 c
ATOM 1268 CDl TYR A 253 1 .269 3 .034 -8 .937 1 .00 12 .68 c
ATOM 1269 CD2 TYR A 253 0 .792 2 .164 -6 .755 1 .00 8 .44 c
ATOM 1270 CE1 TYR A 253 -0 .094 3 .112 -9 .195 1 .00 11 .16 c
ATOM 1271 CE2 TYR A 253 -0 .571 2 .232 -7 .008 1 .00 8 .64 c
ATOM 1272 CZ TYR A 253 -0 .994 2 .699 -8 .245 1 .00 11 .35 c
ATOM 1273 OH TYR A 253 -2 .341 2 .787 -8 .502 1 .00 11 .75 0
ATOM 1274 N ALA A 254 3 .717 3 .682 - .614 1 .00 8 .28 N
ATOM 1275 CA ALA A 254 3 .283 4 .028 -3 .275 1 .00 7 .14 c
ATOM 1276 C ALA A 254 3 .718 5 .439 -2 .900 1 .00 8 .13 c ATOM 1277 O ALA A 254 2.916 6.216 -2.381 1.00 7.26 o TOM 1278 CB ALA A 254 3. 864 3. 041 -2. 265 1. 00 11. 06 c
ATOM 1279 N LEU A 255 4. 971 5. 802 -3. 195 1. 00 7. 07 N
ATOM 1280 CA LEU A 255 5. 439 7. 156 -2. 874 1. 00 6. 68 C
ATOM 1281 C LEU A 255 4. 602 8. 225 -3. 576 1. 00 9. .25 C
ATOM 1282 0 LEU A 255 4. 363 9. 299 -3. 015 1. 00 8. .62 0
ATOM 1283 CB LEU A 255 6. 916 7. 283 -3. 245 1. 00 8. ,51 C
ATOM 1284 CG LEU A 255 7. 906 6. 351 -2. .519 1. 00 6. .84 C
ATOM 1285 CDl LEU A 255 9. 335 6. 656 -2. .942 1. 00 9. .42 c
ATOM 1286 CD2 LEU A 255 7. 832 6. .506 -1. .008 1. .00 5. ,35 c
ATOM 1287 N LYS A 256 4. 247 8. .010 -4. ,847 1. .00 6. .95 N
ATOM 1288 CA LYS A 256 3. .397 9. .002 -5. ,523 1. ,00 9. ,07 C
ATOM 1289 C LYS A 256 1. .946 8. .953 -5. ,105 1. .00 9. ,44 C
ATOM 1290 0 LYS A 256 1. ,285 10. .005 -4. ,937 1. ,00 7. .99 0
ATOM 1291 CB LYS A 256 3. ,519 8. .828 -7. ,051 1. .00 9. .73 C
ATOM 1292 CG LYS A 256 4. ,942 9. ,110 -7. ,521 1. .00 11. .89 C
ATOM 1293 CD LYS A 256 5. .192 8. 569 -8. 919 1. 00 20. ,28 C
ATOM 1294 CE LYS A 256 4. .745 9. 547 -9. 986 1. 00 24. ,47 c
ATOM 1295 NZ LYS A 256 5. 634 9. ,467 -11. .186 1. 00 26. ,97 N
ATOM 1296 N GLN A 257 1. .329 7. .775 -4. .920 1. .00 10. ,04 N
ATOM 1297 CA GLN A 257 0. .096 7. .720 -4. .550 1. .00 10. ,34 C
ATOM 1298 C GLN A 257 0. .391 8. .176 -3. .129 1. 00 11. ,61 C
ATOM 1299 O GLN A 257 1. .497 8. .611 -2. ,839 1. ,00 9. ,42 O
ATOM 1300 CB GLN A 257 0. ,566 6. ,279 -4. ,767 1. .00 12. .04 C
ATOM 1301 CG GLN A 257 0. ,662 5. .908 -6. ,251 1. .00 14. .99 C
ATOM 1302 CD GLN A 257 ■1. ,847 6. ,614 -6. .908 1. ,00 18. .94 C
ATOM 1303 OE1 GLN A 257 ■3. .002 6. ,344 -6. .559 1. ,00 24. .20 O
ATOM 1304 NE2 GLN A 257 ■1. ,532 7. .503 -7. .813 1. ,00 21. .56 N
ATOM 1305 N LEU A 258 0. ,652 8. .046 -2. .285 1. .00 8. .27 N
ATOM 1306 CA LEU A 258 0. .472 8. .455 -0. .883 1. .00 9. .74 C
ATOM 1307 C LEU A 258 1. .091 9. .816 -0. .603 1. .00 7. .64 c TOM 1308 O LEU A 258 1. .143 10. .255 0. .547 1. .00 7. .79 o
ATOM 1309 CB LEU A 258 0. .984 7. .399 0. .098 1. .00 7. .61 c
ATOM 1310 CG LEU A 258 0. .386 5. .990 -0. .168 1. .00 7. .82 c
ATOM 1311 CDl LEU A 258 0. .997 5. .000 0. .800 1. .00 8. .98 c
ATOM 1312 CD2 LEU A 258 ■1. .135 6. .032 -0. .040 1. .00 6. .93 c
ATOM 1313 N ASP A 259 1. .437 10. .543 -1. .660 1. .00 9. .21 N
ATOM 1314 CA ASP A 259 1. .980 11. .894 -1. .564 1. .00 9. .04 C
ATOM 1315 C ASP A 259 0. .809 12. .868 -1. .385 1. .00 9. .52 C
ATOM 1316 O ASP A 259 0. .303 13. .450 -2. .340 1. .00 8. .58 O
ATOM 1317 CB ASP A 259 2. .768 12. .227 -2. .832 1. .00 8. .93 C
ATOM 1318 CG ASP A 259 3. .337 13. .635 -2. .841 1. .00 11. .25 C
ATOM 1319 ODl ASP A 259 3, .548 14. .222 -1, .757 1. .00 8, .51 0
ATOM 1320 OD2 ASP A 259 3, .597 14. .170 -3. .940 1. .00 6, .70 o
ATOM 1321 N LEU A 260 0, .351 12, .990 -0, .147 1, .00 8, .63 N
ATOM 1322 CA LEU A 260 -0, .790 13, .836 0, .201 1. .00 8, .38 C
ATOM 1323 C LEU A 260 -0, .343 14, .900 1, .191 1, .00 6, .27 C
ATOM 1324 O LEU A 260 0. .561 14, .654 1, .982 1, .00 7. .26 O
ATOM 1325 CB LEU A 260 -1 .854 12. .950 0. .855 1, .00 6. .89 C
ATOM 1326 CG LEU A 260 -2. .359 11. .781 -0, .005 1, .00 4, .65 C
ATOM 1327 CDl LEU A 260 ■3, .267 10. .858 0, .805 1, .00 7, .42 c
ATOM 1328 CD2 LEU A 260 •3, .133 12, .333 -1, .200 1, .00 9, .69 c
ATOM 1329 N PRO A 261 -0. .949 16, .078 1, .156 1, .00 8, .32 N
ATOM 1330 CA PRO A 261 -0. .548 17, .206 1. .974 1. .00 8. .79 C
ATOM 1331 C PRO A 261 -0 .417 16. .955 3. .463 1, .00 7. .80 C
ATOM 1332 O PRO A 261 0 .421 17, .587 4. .112 1. .00 7 .02 O
ATOM 1333 CB PRO A 261 -1 .664 18. .235 1 .687 1, .00 8 .92 C
ATOM 1334 CG PRO A 261 -1 .893 17. .995 0 .216 1, .00 11 .25 C
ATOM 1335 CD PRO A 261 -1. .933 16 .474 0 .102 1. .00 7. .59 C
ATOM 1336 N HIS A 262 -1 .221 16 .080 4 .059 1 .00 6 .58 N
ATOM 1337 CA HIS A 262 -1 .175 15 .789 5 .475 1 .00 7 .08 C
ATOM 1338 C HIS A 262 -0 .362 14 .555 5 .842 1 .00 8 .37 C
ATOM 1339 O HIS A 262 -0 .404 14 .132 7 .007 1 .00 8 .87 0
ATOM 1340 CB HIS A 262 -2 .606 15 .587 6 .014 1 .00 6 .94 C
ATOM 1341 CG HIS A 262 -3 .300 14 .397 5 .408 1 .00 7 .70 C
ATOM 1342 ND1 HIS A 262 -3 .671 14 .326 4 .078 1 .00 9 .51 N
ATOM 1343 CD2 HIS A 262 -3 .715 13 .238 5 .983 1 .00 8. .94 C
ATOM 1344 CE1 HIS A 262 -4 .272 13 .170 3 .862 1 .00 7 .83 C
ATOM 1345 NE2 HIS A 262 -4 .350 12 .500 5 .011 1 .00 7 .29 N
ATOM 1346 N VAL A 263 0 .373 13 .988 4 .901 1 .00 8 .17 N
ATOM 1347 CA VAL A 263 1 .167 12 .796 5 .115 1. .00 7 .47 C
ATOM 1348 C VAL A 263 2 .671 13 .092 5 .100 1 .00 10 .21 C ATOM 1349 O VAL A 263 3.141 13.969 4..381 1.00 7.,85 o
ATOM 1350 CB VAL A 263 0. 883 11. 756 4. ,004 1. 00 7. ,89 c
ATOM 1351 CGI VAL A 263 1. 834 10. 579 4. ,025 1. 00 7. ,91 c
ATOM 1352 CG2 VAL A 263 -0. 548 11. .206 4. ,113 1. 00 6. ,51 c
ATOM 1353 N ALA A 264 3. 434 12. 300 5. ,848 1. 00 6. ,28 N
ATOM 1354 CA ALA A 264 4. 872 12. .311 5. ,829 1. 00 6. .81 C
ATOM 1355 C ALA A 264 5. 278 10. ,833 5. ,635 1. 00 7. ,80 C
ATOM 1356 O ALA A 264 4. 767 9. ,998 6. .380 1. 00 10. .65 O TOM 1357 CB ALA A 264 5. .544 12. ,819 7. .089 1. .00 6. ,72 C
ATOM 1358 N MET A 265 6. .148 10. ,541 4. .691 1. .00 5. ,71 N
ATOM 1359 CA MET A 265 6. .595 9. ,167 4. .502 1. ,00 7. ,12 C
ATOM 1360 C MET A 265 8. .090 8. ,992 4. .768 1. .00 8. ,32 C
ATOM 1361 O MET A 265 8. ,894 9. ,841 4. .397 1. ,00 9. ,40 O
ATOM 1362 CB MET A 265 6. ,352 8. ,707 3. .058 1. ,00 7. .47 C
ATOM 1363 CG MET A 265 4. ,936 8. .211 2. .771 1. .00 7. .41 C
ATOM 1364 SD MET A 265 4. ,708 7. .866 1. .001 1. .00 5. .91 S
ATOM 1365 CE MET A 265 4. .504 9. ,530 0. ,382 1. 00 6. ,40 C
ATOM 1366 N TYR A 266 8. .448 7. ,873 5. .397 1. 00 5. ,61 N
ATOM 1367 CA TYR A 266 9. ,823 7. .463 5. ,616 1. 00 6. ,24 C
ATOM 1368 C TYR A 266 10. ,029 6. ,067 5. ,014 1. .00 5. ,80 C
ATOM 1369 O TYR A 266 9. ,327 5. .139 5. ,424 1. .00 5. .17 O
ATOM 1370 CB TYR A 266 10. ,158 7. ,399 7. ,111 1. ,00 7. .31 C
ATOM 1371 CG TYR A 266 10. ,084 8. ,745 7. .806 1. .00 6. .53 C
ATOM 1372 CDl TYR A 266 8. ,850 9. ,207 8. .285 1. ,00 5. .70 C
ATOM 1373 CD2 TYR A 266 11. .194 9. .556 7. .963 1. ,00 6. .84 C
ATOM 1374 CE1 TYR A 266 8. .770 10. ,426 8. .920 1. ,00 9. .26 c
ATOM 1375 CE2 TYR A 266 11. .090 10. .785 8. .587 1. ,00 6. .80 c
ATOM 1376 CZ TYR A 266 9. .879 11. .226 9. .065 1. ,00 8. .64 c
ATOM 1377 OH TYR A 266 9. .765 12. .463 9. .705 1. ,00 5. .96 o
ATOM 1378 N MET A 267 10. .904 5. .915 4. .037 1. .00 4. .22 N
ATOM 1379 CA MET A 267 11. .160 4. .616 3. .435 1. .00 6. .69 C
ATOM 1380 C MET A 267 12. .027 3. .777 4. .380 1. .00 6. .85 C
ATOM 1381 O MET A 267 12. .956 4. .352 4. .958 1. .00 4. .90 O
ATOM 1382 CB MET A 267 11. .906 4. .723 2. .104 1. .00 5. .80 C
ATOM 1383 CG MET A 267 10. .954 5. .071 0. .954 1. ,00 7. .99 C
ATOM 1384 SD MET A 267 11. .836 5. .079 -0. .611 1. .00 7. .34 s
ATOM 1385 CE MET A 267 12. .686 6. .662 -0. .482 1. .00 8. .84 c
ATOM 1386 N ASP A 268 11. .734 2. .482 4. .507 1. .00 6. .17 N
ATOM 1387 CA ASP A 268 12. .610 1. .695 5. .385 1. .00 7. .93 C
ATOM 1388 C ASP A 268 14. .036 1. .684 4. .838 1. .00 7. .64 C
ATOM 1389 0 ASP A 268 14. .190 1. .558 3, .614 1. .00 5. .93 O
ATOM 1390 CB ASP A 268 12. .083 0. .264 5, .496 1. .00 5. .54 C
ATOM 1391 CG ASP A 268 12. .981 -0, .619 6, .339 1. .00 7, .42 C
ATOM 1392 ODl ASP A 268 12, .758 -0, .686 7, .564 1. .00 9, .31 0
ATOM 1393 OD2 ASP A 268 13, .881 -1, .266 5, .750 1. .00 7, .67 0
ATOM 1394 N ALA A 269 15. .032 1. .753 5. .719 1. .00 7, .13 N
ATOM 1395 CA ALA A 269 16. .425 1, .690 5 .259 1. .00 8, .60 C
ATOM 1396 C ALA A 269 17. .255 0. .747 6, .135 1. .00 7, .36 C
ATOM 1397 O ALA A 269 18, .388 1. .083 6. .518 1, .00 7. .20 0
ATOM 1398 CB ALA A 269 17. .057 3 .077 5 .267 1. .00 10, .76 C
ATOM 1399 N GLY A 270 16, .717 -0, .438 6, .431 1. .00 7, .15 N
ATOM 1400 CA GLY A 270 17, .431 -1, .438 7, .225 1. .00 6, .15 C
ATOM 1401 C GLY A 270 17, .936 -0, .885 8, .555 1. .00 8, .83 C
ATOM 1402 O GLY A 270 17, .253 -0, .126 9, .235 1. .00 7, .05 O
ATOM 1403 N HIS A 271 19. .154 -1. .275 8, .945 1. .00 8, .31 N
ATOM 1404 CA HIS A 271 19, .752 -0. .807 10. .197 1. .00 8, .40 C
ATOM 1405 C HIS A 271 21, .274 -0, .845 10 .079 1. .00 8, .58 C
ATOM 1406 O HIS A 271 21, .839 -1, .232 9 .040 1, .00 10, .19 O
ATOM 1407 CB HIS A 271 19. .265 -1. .626 11 .398 1, .00 5, .83 C
ATOM 1408 CG HIS A 271 19 .612 -3 .088 11 .325 1. .00 7 .27 C
ATOM 1409 ND1 HIS A 271 20 .778 -3, .599 11 .881 1. .00 7 .14 N
ATOM 1410 CD2 HIS A 271 18 .970 -4 .128 10 .742 1. .00 8 .91 C
ATOM 1411 CE1 HIS A 271 20 .810 -4 .900 11 .669 1, .00 8 .80 C
ATOM 1412 NE2 HIS A 271 19 .745 -5 .248 10 .957 1, .00 9. .04 N
ATOM 1413 N ALA A 272 21 .972 -0 .383 11 .116 1. .00 7 .51 N
ATOM 1414 CA ALA A 272 23 .421 -0 .288 11 .084 1 .00 8 .94 C
ATOM 1415 C ALA A 272 24 .116 -1. .596 10 .753 1, .00 10. .29 C
ATOM 1416 O ALA A 272 25 .148 -1. .579 10 .067 1, .00 11. .43 0
ATOM 1417 CB ALA A 272 23 .957 0 .267 12 .411 1, .00 8. .86 C
ATOM 1418 N GLY A 273 23 .604 -2. .730 11 .211 1, .00 9 .19 N
ATOM 1419 CA GLY A 273 24 .165 -4. .035 10 .965 1. .00 8 .84 C
ATOM 1420 C GLY A 273 23 .765 -4 .618 9 .629 1. .00 8 .39 C ATOM 1421 O GLY A 273 24.143 -5.758 9..351 1..00 12.18 o
ATOM 1422 N TRP A 274 23. 008 -3. 903 8. .803 1. .00 8. 78 N
ATOM 1423 CA TRP A 274 22. 622 -4. 344 7. .476 1. .00 11. 33 C
ATOM 1424 C TRP A 274 23. 290 -3. 410 6. ,459 1. ,00 11. 41 C
ATOM 1425 0 TRP A 274 24. 263 -3. 765 5. 787 1. 00 12. 00 0
ATOM 1426 CB TRP A 274 21. 105 -4. 321 7. .248 1. 00 12. 55 C
ATOM 1427 CG TRP A 274 20. 574 -4. 994 6. 020 1. 00 12. 97 C
ATOM 1428 CDl TRP A 274 21. 282 -5. 388 4. .906 1. 00 13. 66 C
ATOM 1429 CD2 TRP A 274 19. 209 -5. 365 5. 757 1. 00 11. 08 C
ATOM 1430 NE1 TRP A 274 20. 456 -5. 975 3. .999 1. .00 10. 98 N
ATOM 1431 CE2 TRP A 274 19. .169 -5. 962 4. .488 1. .00 11. 39 C
ATOM 1432 CE3 TRP A 274 18. 013 -5. 213 6. .473 1. ,00 11. 56 C
ATOM 1433 CZ2 TRP A 274 17. ,983 -6. .443 3. .923 1. ,00 12. 85 C
ATOM 1434 CZ3 TRP A 274 16. ,831 -5. .679 5. .906 1. ,00 11. 52 C
ATOM 1435 CH2 TRP A 274 16. ,813 -6. .293 4. .643 1. ,00 12. 41 C
ATOM 1436 N LEU A 275 22. .777 -2. ,187 6. .356 1. ,00 10. 15 N
ATOM 1437 CA LEU A 275 23. ,304 -1. ,220 5. ,404 1. ,00 9. ,63 C
ATOM 1438 C LEU A 275 24. ,376 -0. ,308 5. ,960 1. .00 7. .62 C
ATOM 1439 O LEU A 275 24. .967 0. ,453 5. .187 1. ,00 11. ,04 0
ATOM 1440 CB LEU A 275 22. .155 -0. ,353 4. .845 1. ,00 9. .26 C
ATOM 1441 CG LEU A 275 20. .957 -1. .094 4. .247 1. .00 11. ,24 C
ATOM 1442 CDl LEU A 275 19. .944 -0. ,099 3. .689 1. .00 8. .62 C
ATOM 1443 CD2 LEU A 275 21. .391 -2. .079 3. .162 1. ,00 13. .03 C
ATOM 1444 N GLY A 276 24. .670 -0. .361 7. .248 1. .00 9. ,05 N
ATOM 1445 CA GLY A 276 25. .651 0. ,545 7. .870 1. .00 8. ,53 C
ATOM 1446 C GLY A 276 27. .096 0. .102 7. .676 1. .00 9. ,78 C
ATOM 1447 O GLY A 276 28. .020 0. .909 7. .878 1. .00 10. .26 O
ATOM 1448 N TRP A 277 27. .311 -1. .153 7. .287 1. .00 10. .13 N
ATOM 1449 CA TRP A 277 28. .700 -1. .589 7. .017 1. .00 11. .51 C
ATOM 1450 C TRP A 277 29. .252 -0. ,645 5. .956 1. .00 12. ,13 C
ATOM 1451 O TRP A 277 28. .585 -0. .383 4. .946 1. .00 12. ,84 O
ATOM 1452 CB TRP A 277 28. .705 -3. .020 6. .482 1. .00 10. .92 C
ATOM 1453 CG TRP A 277 28. .246 -4. .049 7. .479 1. .00 12. .31 C
ATOM 1454 CDl TRP A 277 26. .962 -4. .446 7. .745 1. .00 11. .68 C
ATOM 1455 CD2 TRP A 277 29. .093 -4. .760 8. .388 1. .00 12. .51 C
ATOM 1456 NE1 TRP A 277 26. .973 -5. .383 8. .762 1. .00 11. .14 N
ATOM 1457 CE2 TRP A 277 28. .263 -5. .600 9. .163 1. .00 11. .67 C
ATOM 1458 CE3 TRP A 277 30. .477 -4. .765 8. .611 1, .00 11. .80 C
ATOM 1459 CZ2 TRP A 277 28. .780 -6. .428 10. .157 1, .00 12. .92 C
ATOM 1460 CZ3 TRP A 277 30. .991 -5. .622 9, .581 1, .00 14. .44 C
ATOM 1461 CH2 TRP A 277 30, .134 -6. .445 10, .340 1, .00 15. .36 C
ATOM 1462 N PRO A 278 30, .510 -0. .238 6, .068 1. .00 12. .38 N
ATOM 1463 CA PRO A 278 31, .102 0, .724 5, .160 1. .00 12. .46 C
ATOM 1464 C PRO A 278 30. .950 0, .422 3, .688 1. .00 13. .57 C
ATOM 1465 0 PRO A 278 30. .584 1, .328 2. .922 1 .00 14. .10 O
ATOM 1466 CB PRO A 278 32 .561 0, .774 5 .610 1 .00 11. .83 C
ATOM 1467 CG PRO A 278 32 .432 0, .638 7. .102 1 .00 12. .89 C
ATOM 1468 CD PRO A 278 31 .331 -0. .386 7 .304 1. .00 13. .10 C
ATOM 1469 N ALA A 279 31 .030 -0 .844 3 .277 1. .00 12. .89 N
ATOM 1470 CA ALA A 279 30 .878 -1, .223 1 .884 1 .00 13, .58 C
ATOM 1471 C ALA A 279 29 .441 -1, .111 1 .381 1 .00 13, .99 C
ATOM 1472 O ALA A 279 29 .250 -1 .084 0. .165 1 .00 12, .43 O
ATOM 1473 CB ALA A 279 31 .365 -2 .663 1. .692 1 .00 13. .49 C
ATOM 1474 N ASN A 280 28 .449 -1 .061 2 .280 1 .00 11. .55 N
ATOM 1475 CA ASN A 280 27 .058 -0, .991 1, .842 1 .00 11. .36 C
ATOM 1476 C ASN A 280 26 .497 0, .425 1 .836 1. .00 12. .48 C
ATOM 1477 O ASN A 280 25 .510 0. .659 1 .122 1. .00 10, .23 O
ATOM 1478 CB ASN A 280 26 .155 -1, .851 2. .742 1. .00 10, .12 C
ATOM 1479 CG ASN A 280 26 .557 -3. .316 2 .710 1 .00 15. .79 C
ATOM 1480 ODl ASN A 280 27 .172 -3. .773 1 .742 1 .00 12, .50 0
ATOM 1481 ND2 ASN A 280 26 .213 -4 .055 3. .761 1 .00 12 .07 N
ATOM 1482 N ILE A 281 27 .174 1 .370 2 .459 1 .00 14. .04 N
ATOM 1483 CA ILE A 281 26 .693 2 .735 2 .572 1 .00 16 .09 C
ATOM 1484 C ILE A 281 26 .393 3. .442 1 .264 1 .00 14 .58 C
ATOM 1485 O ILE A 281 25 .332 4 .030 1 .060 1 .00 12 .07 O
ATOM 1486 CB ILE A 281 27 .661 3 .651 3 .367 1 .00 21 .92 C
ATOM 1487 CGI ILE A 281 27 .963 3 .086 4 .745 1 .00 23 .78 C
ATOM 1488 CG2 ILE A 281 27 .013 5 .041 3 .496 1 .00 22 .45 C
ATOM 1489 CDl ILE A 281 27 .021 3 .472 5 .859 1 .00 23 .17 C
ATOM 1490 N GLN A 282 27 .345 3 .471 0 .345 1 .00 15 .72 N
ATOM 1491 CA GLN A 282 27 .147 4 .169 -0 .922 1 .00 13 .98 C
ATOM 1492 C GLN A 282 26 .202 3 .541 -1 .919 1 .00 11 .05 C ATOM 1493 0 GLN A 282 25.394 4.239 -2.534 1.00 12.05 o
ATOM 1494 CB GLN A 282 28. 550 4. 314 -1. 539 1. 00 19. 90 c
ATOM 1495 CG GLN A 282 28. 436 4. 984 -2. 913 1. 00 28. 16 c
ATOM 1496 CD GLN A 282 29. 824 5. 146 -3. 498 1. 00 37. 02 c
ATOM 1497 OE1 GLN A 282 30. 768 5. 539 -2. 800 1. 00 37. 94 0
ATOM 1498 NE2 GLN A 282 29. 968 4. 834 -4. 783 1. 00 37. 58 N
ATOM 1499 N PRO A 283 26. 259 2. 224 -2. 056 1. 00 10. 83 N
ATOM 1500 CA PRO A 283 25. 269 1. 531 -2. 877 1. 00 12. 76 C
ATOM 1501 C PRO A 283 23. 874 1. 810 -2. 333 1. 00 11. 45 C
ATOM 1502 0 PRO A 283 22. 927 1. 999 -3. .106 1. 00 8. 19 O
ATOM 1503 CB PRO A 283 25. 608 0. ,051 -2. .775 1. .00 14. 50 C
ATOM 1504 CG PRO A 283 26. 904 -0. ,036 -2. .068 1. .00 13. 85 C
ATOM 1505 CD PRO A 283 27. 298 1. .316 -1. .551 1. .00 11. 96 C
ATOM 1506 N ALA A 284 23. 702 1. .803 -1. ,007 1. .00 10. 70 N
ATOM 1507 CA ALA A 284 22. 397 2. ,118 -0. ,416 1. .00 11. 63 C
ATOM 1508 C ALA A 284 21. 986 3. ,550 -0. ,728 1. .00 10. 83 C
ATOM 1509 O ALA A 284 20. 843 3. 894 -1. 028 1. 00 8. 26 O
ATOM 1510 CB ALA A 284 22. 489 1. 945 1. 107 1. 00 7. 27 C
ATOM 1511 N ALA A 285 22. 968 4. 461 -0. 610 1. 00 11. 82 N
ATOM 1512 CA ALA A 285 22. 704 5. .880 -0. 882 1. 00 11. 59 C
ATOM 1513 C ALA A 285 22. 330 6. 073 -2. .341 1. 00 11. 08 C
ATOM 1514 O ALA A 285 21. 407 6. .822 -2. 662 1. 00 7. 85 0
ATOM 1515 CB ALA A 285 23. 912 6. .727 -0. ,496 1. 00 9. 98 C
ATOM 1516 N GLU A 286 23. 026 5. .375 -3. .240 1. 00 11. 14 N
ATOM 1517 CA GLU A 286 22. .665 5. .446 -4. .662 1. 00 12. 08 C
ATOM 1518 C GLU A 286 21. .250 4. ,935 -4. ,903 1. .00 13. 20 C
ATOM 1519 O GLU A 286 20. .436 5. ,589 -5. ,573 1. .00 10. 15 O
ATOM 1520 CB GLU A 286 23. ,676 4. ,661 -5. ,491 1. .00 16. 73 C
ATOM 1521 CG GLU A 286 25. ,013 5. ,366 -5. ,630 1. ,00 24. 97 C
ATOM 1522 CD GLU A 286 26. ,147 4. ,424 -5. .977 1. ,00 30. ,68 C
ATOM 1523 OE1 GLU A 286 26. ,008 3. .197 -5. .761 1. ,00 35. .88 O
ATOM 1524 OE2 GLU A 286 27. .184 4. .909 -6. .458 1. .00 29. .85 O
ATOM 1525 N LEU A 287 20. .923 3. .784 -4. .325 1. .00 11. ,82 N
ATOM 1526 CA LEU A 287 19. .576 3. .241 -4. .501 1. .00 11. ,32 C
ATOM 1527 C LEU A 287 18. .470 4. .140 -3. .981 1. .00 10. .45 C
ATOM 1528 O LEU A 287 17. .530 4. .425 -4. .745 1. .00 10. .62 O
ATOM 1529 CB LEU A 287 19. .493 1. .861 -3. .836 1. .00 14. .87 C
ATOM 1530 CG LEU A 287 18. .094 1. .222 -3. .820 1. .00 17. .45 C
ATOM 1531 CDl LEU A 287 17. .700 0. .818 -5. .235 1. .00 22. .29 C
ATOM 1532 CD2 LEU A 287 18. .098 0. .011 -2. .897 1. .00 18. .87 C
ATOM 1533 N PHE A 288 18, .537 4, .602 -2. .730 1. .00 7. .31 N
ATOM 1534 CA PHE A 288 17, .460 5, .404 -2, .172 1, .00 7. .68 C
ATOM 1535 C PHE A 288 17. .338 6. .775 -2. .818 1, .00 9. .78 C
ATOM 1536 O PHE A 288 16, .219 7. .265 -3, .024 1. .00 7. .80 O
ATOM 1537 CB PHE A 288 17. .533 5. .508 -0. .641 1, .00 6. .27 C
ATOM 1538 CG PHE A 288 17. .152 4 .214 0, .034 1, .00 8. .96 C
ATOM 1539 CDl PHE A 288 15. .825 3. .831 0 .127 1. .00 9. .32 C
ATOM 1540 CD2 PHE A 288 18. .136 3. .384 0 .551 1, .00 8. .51 C
ATOM 1541 CE1 PHE A 288 15 .464 2. .628 0. .706 1 .00 10, .48 C
ATOM 1542 CE2 PHE A 288 17 .782 2 .176 1. .146 1 .00 10, .59 C
ATOM 1543 CZ PHE A 288 16 .445 1. .800 1. .229 1 .00 9, .25 c
ATOM 1544 N ALA A 289 18 .475 7 .408 -3 .144 1 .00 10, .79 N
ATOM 1545 CA ALA A 289 18 .396 8 .721 -3 .771 1 .00 11, .58 C
ATOM 1546 C ALA A 289 17 .815 8 .612 -5 .180 1. .00 11, .29 C
ATOM 1547 O ALA A 289 17 .094 9 .523 -5 .595 1 .00 10 .16 O
ATOM 1548 CB ALA A 289 19 .740 9 .434 -3 .836 1. .00 9 .82 C
ATOM 1549 N LYS A 290 18 .100 7 .518 -5 .886 1 .00 10 .82 N
ATOM 1550 CA LYS A 290 17 .570 7 .400 -7 .248 1 .00 14 .48 C
ATOM 1551 C LYS A 290 16 .070 7 .118 -7 .243 1 .00 12 .08 C
ATOM 1552 O LYS A 290 15 .310 7 .642 -8 .055 1 .00 10 .89 0
ATOM 1553 CB LYS A 290 18 .353 6 .355 -8 .041 1 .00 15 .13 c
ATOM 1554 CG LYS A 290 17 .902 6 .210 -9 .483 1 .00 22 .86 c
ATOM 1555 CD LYS A 290 17 .873 7 .530 -10 .229 1 .00 28 .98 c
ATOM 1556 CE LYS A 290 19 .178 7 .771 -10 .978 1 .00 35 .23 c
ATOM 1557 NZ LYS A 290 19 .255 6 .883 -12 .180 1 .00 38 .20 N
ATOM 1558 N ILE A 291 15 .603 6 .316 -6 .299 1 .00 11 .63 N
ATOM 1559 CA ILE A 291 14 .168 6 .055 -6 .145 1 .00 10 .44 C
ATOM 1560 C ILE A 291 13 .491 7 .404 -5 .897 1 .00 10 .20 C
ATOM 1561 O ILE A 291 12 .464 7 .731 -6 .479 1 .00 11 .65 O
ATOM 1562 CB ILE A 291 13 .914 5 .148 -4 .917 1 .00 13 .66 C
ATOM 1563 CGI ILE A 291 14 .364 3 .716 -5 .209 1 .00 16 .69 C
ATOM 1564 CG2 ILE A 291 12 .462 5 .192 -4 .433 1 .00 13 .26 C ATOM 1565 CDl ILE A 291 13.457 2.919 -6.109 .00 19.35 C
ATOM 1566 N TYR A 292 14.019 8.162 -4.933 00 .98 N
ATOM 1567 CA TYR A 292 13.464 9.478 -4.595 00 .51 C
ATOM 1568 C TYR A 292 13.333 10.357 -5.838 00 .92 C
ATOM 1569 0 TYR A 292 12.310 11.002 -6.091 00 .77 O
ATOM 1570 CB TYR A 292 14.367 10.154 -3.562 00 .38 C
ATOM 1571 CG TYR A 292 13.950 11.518 -3.064 00 10.61 C
ATOM 1572 CDl TYR A 292 12.766 11.693 -2.364 00 12.16 C
ATOM 1573 CD2 TYR A 292 14.750 12.633 -3.283 00 10.96 C
ATOM 1574 CE1 TYR A 292 12.378 12.940 -1 .896 00 12.18 C
ATOM 1575 CE2 TYR A 292 14.378 13.887 -2.821 00 11.86 C
ATOM 1576 CZ TYR A 292 13.198 14.032 -2.132 00 13.20 C
ATOM 1577 OH TYR A 292 12.811 15.270 -1.664 00 14.21 O
ATOM 1578 N GLU A 293 14.403 10.437 -6.624 00 9. ,98 N
ATOM 1579 CA GLU A 293 14.409 11.220 -7.846 00 11.16 C
ATOM 1580 C GLU A 293 13.405 10.676 -8.852 00 12.04 C
ATOM 1581 O GLU A 293 12.650 11.440 -9.456 00 11.19 O
ATOM 1582 CB GLU A 293 15.788 11.173 -8.526 00 14.97 C
ATOM 1583 CG GLU A 293 16.736 12.189 -7.935 00 30.37 C
ATOM 1584 CD GLU A 293 18.049 12.319 -8.680 00 36.86 C
ATOM 1585 OE1 GLU A 293 18.304 11.559 -9.640 00 37.27 0
ATOM 1586 OE2 GLU A 293 18.814 13.216 -8.257 00 42.21 O
ATOM 1587 N ASP A 294 13.438 9.358 -9.058 00 9. .56 N
ATOM 1588 CA ASP A 294 12.526 733 -10.008 00 11.87 C
ATOM 1589 C ASP A 294 11.066 888 -9.617 1.00 13.02 C
ATOM 1590 O ASP A 294 10.217 .854 10.513 1.00 12.14 O
ATOM 1591 CB ASP A 294 12.871 .246 10.191 .00 12.24 C
ATOM 1592 CG ASP A 294 14.145 .070 -11.000 .00 17.67 C
ATOM 1593 ODl ASP A 294 14.688 .063 -11.519 .00 16.93 O
ATOM 1594 OD2 ASP A 294 14.642 .938 -11.142 .00 15.94 0
ATOM 1595 N ALA A 295 10.717 .051 -8.345 .00 10.18 N
ATOM 1596 CA ALA A 295 9.347 .285 -7.937 1. . 0000 8. ,76 C
ATOM 1597 C ALA A 295 8.963 10.770 -8.046 1. .0000 10. .32 C
ATOM 1598 O ALA A 295 7..851 11.106 668 1. .0000 9. .41 O
ATOM 1599 CB ALA A 295 9..076 8.870 486 1, .0000 8. .68 C
ATOM 1600 N GLY A 296 9..836 11.646 520 1, .00 11. .57 N
ATOM 1601 CA GLY A 296 9.560 13.062 635 1. .00 14. .12 C
ATOM 1602 C GLY A 296 9.834 13.856 366 1. .00 12. .59 C
ATOM 1603 O GLY A 296 9.264 14.933 181 1, .00 11. .99 0
ATOM 1604 N LYS A 297 10.600 13.324 -6.420 1. .00 10. .82 N
ATOM 1605 CA LYS A 297 10.841 13.965 -5.127 1. .00 11. .02 C
ATOM 1606 C LYS A 297 526 14.469 -4.539 1 .00 12. .69 C
ATOM 1607 O LYS A 297 265 15.657 -4.383 1 .00 12. .46 O
ATOM 1608 CB LYS A 297 11.841 15.117 -5.341 1 .00 14. .05 C
ATOM 1609 CG LYS A 297 13.137 14.611 -5.968 1 .00 13. .27 C
ATOM 1610 CD LYS A 297 14.250 15.649 -5.839 1 .00 17. .64 C
ATOM 1611 CE LYS A 297 15.526 15.116 -6.478 1 .00 19. .52 C
ATOM 1612 NZ LYS A 297 16.686 15.962 -6.079 1 .00 24. .20 N
ATOM 1613 N PRO A 298 8.610 13.543 -4.246 1 .00 10. .53 N
ATOM 1614 CA PRO A 298 309 13.872 -3..716 00 8.33 C
ATOM 1615 C PRO A 298 437 14.688 -2..437 00 8.91 C
ATOM 1616 O PRO A 298 278 14.375 -1..593 00 7.49 0
ATOM 1617 CB PRO A 298 638 12.524 -3.473 00 9.86 C
ATOM 1618 CG PRO A 298 441 11.519 -4.231 00 8.01 C
ATOM 1619 CD PRO A 298 839 12.070 .376 00 8.83 C
ATOM 1620 N ARG A 299 596 15.702 .263 00 8.72 N
ATOM 1621 CA ARG A 299 714 16.557 -1.064 00 9.08 C
ATOM 1622 C ARG A 299 626 15.776 0.235 00 8.93 C
ATOM 1623 O ARG A 299 398 15.987 1.168 00 7.66 0
ATOM 1624 CB ARG A 299 608 17.621 -1.085 00 8.46 C
ATOM 1625 CG ARG A 299 631 18.563 0.113 00 10.62 C
ATOM 1626 CD ARG A 299 202 18.995 0.464 00 13.20 C
ATOM 1627 NE ARG A 299 458 17.838 0.979 00 10.71 N
ATOM 1628 CZ ARG A 299 692 17.217 2.136 00 11.86 C
ATOM 1629 NHl ARG A 299 634 17.638 2.980 00 .47 N
ATOM 1630 NH2 ARG A 299 939 16.156 2.399 00 .13 N
ATOM 1631 N ALA A 300 736 14.781 0.285 1.00 .86 N
ATOM 1632 CA ALA A 300 493 13.978 1.469 1.00 .80 C
ATOM 1633 C ALA A 300 624 13.039 1.855 1.00 8.97 C
ATOM 1634 0 ALA A 300 635 12.577 3.019 1.00 9.64 O
ATOM 1635 CB ALA A 300 221 13.133 1.229 1.00 6.82 C
ATOM 1636 N VAL A 301 549 12.776 0.934 1.00 5.06 N ATOM 1637 CA VAL A 301 8.688 11.902 1..247 1.00 9.62 c
ATOM 1638 C VAL A 301 9. 691 12. 699 2. .086 1. 00 11. ,03 c
ATOM 1639 0 VAL A 301 10. 416 13. 568 1. .583 1. 00 11. 13 0
ATOM 1640 CB VAL A 301 9. 361 11. 291 0. ,018 1. 00 9. .77 c
ATOM 1641 CGI VAL A 301 10. 522 10. 378 0. .420 1. 00 11. .10 c
ATOM 1642 CG2 VAL A 301 8. 333 10. 444 -0. .751 1. 00 8. ,91 c
ATOM 1643 N ARG A 302 9. 680 12. 393 3. .376 1. 00 8. ,40 N
ATOM 1644 CA ARG A 302 10. 495 13. 108 4. ,350 1. 00 10. ,39 C
ATOM 1645 C ARG A 302 11. 868 12. 486 4. ,530 1. 00 9. ,44 C
ATOM 1646 0 ARG A 302 12. 856 13. ,182 4. .763 1. 00 6. ,90 O
ATOM 1647 CB ARG A 302 9. 706 13. .168 5. ,659 1. 00 12. .00 c
ATOM 1648 CG ARG A 302 10. 384 13. 914 6. ,786 1. 00 13. ,82 c
ATOM 1649 CD ARG A 302 10. 666 15. .391 6. ,484 1. 00 13. ,53 c
ATOM 1650 NE ARG A 302 11. 305 16. .005 7. ,659 1. ,00 11. ,16 N
ATOM 1651 CZ ARG A 302 11. ,618 17. .286 7. ,764 1. 00 14. .08 C
ATOM 1652 NHl ARG A 302 11. .400 18. ,142 6. ,771 1. .00 12. ,81 N
ATOM 1653 NH2 ARG A 302 12. 171 17. 743 8. .888 1. 00 11. 84 N
ATOM 1654 N GLY A 303 11. 992 11. 171 4. .283 1. 00 8. .63 N
ATOM 1655 CA GLY A 303 13. 325 10. 562 4. ,407 1. 00 8. ,56 C
ATOM 1656 C GLY A 303 13. 220 9. 072 4. ,674 1. 00 6. .34 C
ATOM 1657 O GLY A 303 12. 510 8. 373 3. .944 1. 00 5. .44 O
ATOM 1658 N LEU A 304 13. 973 8. 573 5. ,641 1. 00 8. ,57 N
ATOM 1659 CA LEU A 304 14. 121 7. 127 5. ,836 1. 00 5. ,76 C
ATOM 1660 C LEU A 304 13. 901 6. .720 7. ,283 1. .00 6. .88 C
ATOM 1661 O LEU A 304 14. .114 7. .560 8. ,154 1. 00 6. ,28 O
ATOM 1662 CB LEU A 304 15. .557 6. ,752 5. .431 1. 00 9. ,81 C
ATOM 1663 CG LEU A 304 15. ,996 7. ,063 3. ,989 1. 00 7. ,82 C
ATOM 1664 CDl LEU A 304 17. ,465 6. ,694 3. .808 1. .00 11. .27 C
ATOM 1665 CD2 LEU A 304 15. ,109 6. ,295 3. .008 1. ,00 6. ,00 c
ATOM 1666 N ALA A 305 13. .551 5. ,451 7. .512 1. .00 6. .26 N
ATOM 1667 CA ALA A 305 13. .395 4. .934 8. .864 1. .00 7. .52 c
ATOM 1668 C ALA A 305 14. .415 3. .815 9. .084 1. .00 8. .92 c
ATOM 1669 0 ALA A 305 14. .677 3. .045 8. .155 1. ,00 8. .95 0
ATOM 1670 CB ALA A 305 12. .015 4. .342 9. .091 1. .00 5. .11 c
ATOM 1671 N THR A 306 15. .050 3. .768 10. .252 1. ,00 7. .71 N
ATOM 1672 CA THR A 306 16. .025 2. .728 10. .517 1. .00 6. .41 C
ATOM 1673 C THR A 306 15. .738 1. .990 11. .826 1. ,00 6. .71 C
ATOM 1674 O THR A 306 15. .011 2. .441 12. .714 1. .00 5. .64 O
ATOM 1675 CB THR A 306 17. .491 3. .219 10. .550 1. .00 8. .52 C
ATOM 1676 OGl THR A 306 17. .728 3. .932 11, .767 1. .00 8. .64 O
ATOM 1677 CG2 THR A 306 17. .824 4. .120 9, .367 1. .00 7. .21 C
ATOM 1678 N ASN A 307 16. .347 0, .807 11, .914 1. .00 6, .96 N
ATOM 1679 CA ASN A 307 16. .252 -0. • 111 13. .042 1. .00 7. .89 C
ATOM 1680 C ASN A 307 14, .853 -0, .649 13. .282 1. .00 9. .11 C
ATOM 1681 O ASN A 307 14, .592 -1, .152 14. .374 1. .00 7, .66 o
ATOM 1682 CB ASN A 307 16, .773 0, .571 14. .342 1. .00 7, .51 c
ATOM 1683 CG ASN A 307 17, .210 -0, .456 15. .379 1, .00 11. .22 c
ATOM 1684 ODl ASN A 307 17, .893 -1, .433 15 .062 1. .00 8, .51 o
ATOM 1685 ND2 ASN A 307 16, .797 -0. .293 16 .640 1, .00 12, .34 N
ATOM 1686 N VAL A 308 13. .944 -0. .583 12 .302 1, .00 8. .35 N
ATOM 1687 CA VAL A 308 12. .579 -1. .061 12 .459 1. .00 8. .75 C
ATOM 1688 C VAL A 308 12. .584 -2. .533 12 .855 1, .00 8. .64 C
ATOM 1689 O VAL A 308 13 .242 -3 .359 12 .216 1, .00 8 .42 O
ATOM 1690 CB VAL A 308 11 .740 -0 .895 11 .170 1, .00 6 .29 C
ATOM 1691 CGI VAL A 308 10 .350 -1 .495 11 .336 1. .00 7 .20 C
ATOM 1692 CG2 VAL A 308 11 .605 0 .588 10 .831 1. .00 5 .27 C
ATOM 1693 N ALA A 309 11 .961 -2 .861 13 .976 1. .00 8 .32 N
ATOM 1694 CA ALA A 309 11 .870 -4 .210 14 .496 1. .00 9 .02 C
ATOM 1695 C ALA A 309 13 .226 -4 .796 14 .872 1 .00 10 .25 C
ATOM 1696 O ALA A 309 13 .294 -5 .994 15 .155 1 .00 12 .32 O
ATOM 1697 CB ALA A 309 11 .168 -5 .146 13 .504 1 .00 9 .76 C
ATOM 1698 N ASN A 310 14 .249 -3 .970 15 .008 1 .00 9 .63 N
ATOM 1699 CA ASN A 310 15 .553 -4 .462 15 .435 1 .00 10 .80 C
ATOM 1700 C ASN A 310 15 .855 -3 .886 16 .803 1. .00 10 .72 C
ATOM 1701 0 ASN A 310 15 .000 -3 .215 17 .384 1. .00 11 .68 0
ATOM 1702 CB ASN A 310 16 .612 -4 .161 14 .362 1 .00 11 .11 c
ATOM 1703 CG ASN A 310 16 .726 -5 .384 13 .459 1 .00 16 .07 c
ATOM 1704 ODl ASN A 310 17 .473 -6 .305 13 .786 1 .00 13 .72 0
ATOM 1705 ND2 ASN A 310 15 .920 -5 .457 12 .399 1 .00 16 .01 N
ATOM 1706 N TYR A 311 17 .046 -4 .168 17 .342 1 .00 10 .84 N
ATOM 1707 CA TYR A 311 17 .364 -3 .801 18 .713 1 .00 11 .23 C
ATOM 1708 C TYR A 311 18 .564 -2 .896 18 .884 1 .00 12 .18 C ATOM 1709 0 TYR A 311 19.034 -2.,763 20..028 1.00 12.23 0
ATOM 1710 CB TYR A 311 17. 672 -5. .122 19. ,491 1. 00 11. .01 c
ATOM 1711 CG TYR A 311 16. .663 -6. ,219 19. ,229 1. 00 11. ,75 c
ATOM 1712 CDl TYR A 311 15. .492 -6. ,315 19. ,983 1. .00 11. ,64 c
ATOM 1713 CD2 TYR A 311 16. .876 -7. ,136 18. ,194 1. 00 11. ,12 c
ATOM 1714 CE1 TYR A 311 14. .574 -7. ,318 19. ,724 1. ,00 11. ,23 c
ATOM 1715 CE2 TYR A 311 15. ,943 -8. ,136 17. .939 1. ,00 11. .43 c
ATOM 1716 CZ TYR A 311 14. ,813 -8. .219 18. ,711 1. .00 11. ,12 c
ATOM 1717 OH TYR A 311 13. ,890 -9. .224 18. .468 1. .00 12. ,16 0
ATOM 1718 N ASN A 312 19. .092 -2. .337 17. .791 1. .00 12. ,04 N
ATOM 1719 CA ASN A 312 20. ,292 -1. .527 17. .882 1. .00 13. ,38 c
ATOM 1720 C ASN A 312 20. .155 -0. .300 18. .764 1. ,00 12. ,71 c
ATOM 1721 0 ASN A 312 19. .105 0. .324 18. .940 1. .00 10. ,84 0
ATOM 1722 CB ASN A 312 20. .755 -1. .051 16. .493 1. .00 11. .78 c
ATOM 1723 CG ASN A 312 21. .006 -2. .203 15. .545 1. .00 12. .16 c
ATOM 1724 ODl ASN A 312 20. .933 -3. .367 15. .926 1. ,00 12. .39 o
ATOM 1725 ND2 ASN A 312 21. .275 -1. ,906 14. .280 1. .00 11. .61 N TOM 1726 N ALA A 313 21. ,308 0. .102 19. .310 1. .00 11. ,20 N
ATOM 1727 CA ALA A 313 21. ,350 1. .317 20. ,119 1. .00 11. ,45 C
ATOM 1728 C ALA A 313 21. ,286 2. .516 19. ,167 1. .00 12. ,29 C
ATOM 1729 0 ALA A 313 21. ,675 2. .380 18. ,003 1. ,00 10. .46 O
ATOM 1730 CB ALA A 313 22. .702 1. .392 20. .835 1. ,00 10. ,42 C
ATOM 1731 N TRP A 314 20. .850 3. ,644 19. .684 1. ,00 11. ,45 N
ATOM 1732 CA TRP A 314 20. .937 4. .902 18. .966 1. .00 14. ,41 C
ATOM 1733 C TRP A 314 22. .418 5. .307 19. .086 1. ,00 14. ,21 C
ATOM 1734 0 TRP A 314 23. .128 5. .516 18. .113 1. ,00 10. .80 O
ATOM 1735 CB TRP A 314 20. .037 5. .990 19. .573 1. .00 14. .64 C
ATOM 1736 CG TRP A 314 20. .510 7. .386 19. .280 1. .00 13. .52 C
ATOM 1737 CDl TRP A 314 20. .929 8. .314 20. .203 1. .00 15. .05 C
ATOM 1738 CD2 TRP A 314 20. .688 7. .989 18. .004 1. .00 12. .63 C TOM 1739 NE1 TRP A 314 21. .329 9. .462 19. .568 1. .00 13. .76 N
ATOM 1740 CE2 TRP A 314 21. .210 9. .280 18. .216 1. .00 14. .52 C TOM 1741 CE3 TRP A 314 20. .456 7. .572 16. .688 1. .00 9. .95 C
ATOM 1742 CZ2 TRP A 314 21. .474 10. .168 17. .169 1. .00 12. ,11 C
ATOM 1743 CZ3 TRP A 314 20. .733 8. .442 15. .650 1. .00 8. .98 C
ATOM 1744 CH2 TRP A 314 21. .237 9. .737 15. .898 1. .00 11. .19 C
ATOM 1745 N SER A 315 22. .912 5. .318 20. .334 1. .00 15. .23 N
ATOM 1746 CA SER A 315 24. .287 5. .751 20. .548 1. .00 18. .72 C
ATOM 1747 C SER A 315 24. .833 5. .213 21. .867 1. .00 21. .49 C
ATOM 1748 0 SER A 315 24. .350 5. .586 22. .934 1. .00 21. .81 0
ATOM 1749 CB SER A 315 24. .377 7. .278 20. .558 1. .00 21. .30 C
ATOM 1750 OG SER A 315 25. .704 7. .736 20. .802 1. .00 21. .21 O
ATOM 1751 N VAL A 316 25, .825 4, .351 21. .762 1. .00 21. .34 N
ATOM 1752 CA VAL A 316 26, .497 3, .791 22. .932 1. .00 22. .22 C
ATOM 1753 C VAL A 316 28, .002 3, .983 22, .739 1. .00 23. .86 C
ATOM 1754 0 VAL A 316 28, .511 3, .976 21, .622 1. .00 19. .29 O
ATOM 1755 CB VAL A 316 26. .173 2. .323 23, .197 1. .00 21. .02 C
ATOM 1756 CGI VAL A 316 24. .794 2, .201 23, .842 1, .00 24, .42 C
ATOM 1757 CG2 VAL A 316 26. .265 1. .504 21. .923 1. .00 22. .66 C
ATOM 1758 N SER A 317 28 .698 4. .173 23. .854 1. .00 25, .44 N
ATOM 1759 CA SER A 317 30, .119 4, .470 23. .854 1. .00 28. .10 C
ATOM 1760 C SER A 317 30, .995 3, .307 23, .433 1. .00 28. .90 C
ATOM 1761 0 SER A 317 32, .074 3, .513 22, .866 1. .00 31. .11 0
ATOM 1762 CB SER A 317 30, .491 4, .924 25, .284 1. .00 29. .64 C
ATOM 1763 OG SER A 317 30. .252 3, .803 26. .135 1. .00 31. .24 0
ATOM 1764 N SER A 318 30. .568 2, .083 23, .699 1. .00 26. .74 N
ATOM 1765 CA SER A 318 31 .332 0. .908 23, .319 1. .00 28. .86 C
ATOM 1766 C SER A 318 30 .525 -0. .007 22, .400 1, .00 26. .66 C
ATOM 1767 0 SER A 318 29 .340 -0 .241 22. .642 1. .00 25, .50 0
ATOM 1768 CB SER A 318 31 .740 0 .147 24, .590 1, .00 32, .29 C
ATOM 1769 OG SER A 318 32 .564 -0 .953 24, .249 1. .00 37, .63 0
ATOM 1770 N PRO A 319 31 .159 -0 .537 21 .363 1. .00 23, .88 N
ATOM 1771 CA PRO A 319 30 .511 -1 .437 20 .435 1, .00 22. .82 C
ATOM 1772 C PRO A 319 30 .168 -2 .788 21 .027 1. .00 22, .89 C
ATOM 1773 0 PRO A 319 31 .012 -3 .521 21 .559 1. .00 21. .86 O
ATOM 1774 CB PRO A 319 31 .514 -1. .623 19 .300 1, .00 24. .00 C
ATOM 1775 CG PRO A 319 32 .806 -1 .049 19. .750 1, .00 23. .83 C
ATOM 1776 CD PRO A 319 32 .578 -0, .276 21, .014 1, .00 24. .62 C
ATOM 1777 N PRO A 320 28 .901 -3 .176 20, .921 1, .00 21, .38 N
ATOM 1778 CA PRO A 320 28 .458 -4 .495 21, .378 1, .00 20, .94 C
ATOM 1779 C PRO A 320 29 .264 -5. .524 20 .607 1. .00 21. .78 C
ATOM 1780 0 PRO A 320 29 .468 -5 .395 19 .391 1 .00 20, .52 O ATOM 1781 CB PRO A 320 26.978 -4.539 21.056 1.00 17.82 c
ATOM 1782 CG PRO A 320 26. 572 -3. 113 20. 877 1. 00 19. .44 c
ATOM 1783 CD PRO A 320 27. 787 -2. 408 20. 312 1. 00 21. .26 c
ATOM 1784 N PRO A 321 29. 711 -6. 577 21. 275 1. 00 23. ,19 N
ATOM 1785 CA PRO A 321 30. 559 -7. 598 20. .681 1. 00 21. .99 C
ATOM 1786 C PRO A 321 30. 047 -8. 219 19. 403 1. 00 20. ,97 C
ATOM 1787 0 PRO A 321 30. 853 -8. 472 18. .487 1. 00 18. .77 0
ATOM 1788 CB PRO A 321 30. 724 -8. .655 21. 775 1. 00 22. .93 C
ATOM 1789 CG PRO A 321 30. 445 -7. 933 23. .041 1. 00 22. .72 C
ATOM 1790 CD PRO A 321 29. 486 -6. .814 22. .724 1. 00 23. ,19 C
ATOM 1791 N TYR A 322 28. 731 -8. .433 19. .264 1. 00 15. .16 N
ATOM 1792 CA TYR A 322 28. 164 -9. ,002 18. .067 1. 00 13. ,57 C
ATOM 1793 C TYR A 322 28. 139 -8. .028 16. .888 1. 00 11. ,96 C
ATOM 1794 0 TYR A 322 27. 859 -8. .461 15. .766 1. 00 11. ,72 O
ATOM 1795 CB TYR A 322 26. .730 -9. ,557 18. .294 1. 00 13. .57 C
ATOM 1796 CG TYR A 322 25. 911 -8. ,526 19. ,051 1. 00 14. ,10 C
ATOM 1797 CDl TYR A 322 25. ,350 -7. .434 18. .383 1. ,00 15. .48 C
ATOM 1798 CD2 TYR A 322 25. .744 -8. .631 20. .424 1. ,00 14. .15 c
ATOM 1799 CE1 TYR A 322 24. .637 -6. .478 19. .070 1. ,00 13. .81 c
ATOM 1800 CE2 TYR A 322 25. .027 -7. .680 21. .123 1. ,00 14. .00 c
ATOM 1801 CZ TYR A 322 24. .476 -6. .614 20. .442 1. ,00 13. .74 c
ATOM 1802 OH TYR A 322 23. .794 -5. .667 21. .153 1. ,00 12. .10 0
ATOM 1803 N THR A 323 28. .466 -6. .765 17. .062 1. ,00 12. .54 N
ATOM 1804 CA THR A 323 28. .556 -5. .824 15. .954 1. .00 14. .40 C
ATOM 1805 C THR A 323 29. .950 -5. .832 15. .330 1. ,00 17. .79 C
ATOM 1806 O THR A 323 30. .135 -5. .317 14. .222 1. .00 16. .25 O
ATOM 1807 CB THR A 323 28. .228 -4. .392 16. .386 1. .00 13. .73 c
ATOM 1808 OGl THR A 323 29. .199 -3. .931 17. .349 1. .00 15. .88 0
ATOM 1809 CG2 THR A 323 26. .847 -4. .266 17. .013 1. .00 11. .85 c
ATOM 1810 N SER A 324 30. .951 -6. .350 16. .044 1. .00 17. .37 N
ATOM 1811 CA SER A 324 32. .316 -6. .328 15. .495 1. .00 18. .42 C
ATOM 1812 C SER A 324 32. .433 -7. .144 14. .230 1. .00 17. .01 C
ATOM 1813 O SER A 324 31. .841 -8. .216 14. .129 1. .00 18. .39 0
ATOM 1814 CB SER A 324 33. .285 -6. .915 16. .544 1. .00 21. .35 C
ATOM 1815 OG SER A 324 34. .591 -6. .956 15. .984 1. .00 23. .70 0
ATOM 1816 N PRO A 325 33, .223 -6. .682 13. .263 1. .00 15. .59 N
ATOM 1817 CA PRO A 325 33. .998 -5. .463 13. .348 1. .00 14. .87 C
ATOM 1818 C PRO A 325 33. .424 -4. .245 12. .649 1. .00 13. .60 c
ATOM 1819 O PRO A 325 34. .151 -3, .395 12. .118 1. .00 11. .66 0
ATOM 1820 CB PRO A 325 35. .271 -5. .900 12. .597 1. .00 15. .85 c
ATOM 1821 CG PRO A 325 34. .738 -6. .706 11. .465 1. .00 14. .66 c
ATOM 1822 CD PRO A 325 33. .519 -7, .424 12. .009 1. .00 15. .79 c
ATOM 1823 N ASN A 326 32. .094 -4, .155 12, .570 1. .00 11. .77 N
ATOM 1824 CA ASN A 326 31, .498 -2, .995 11. .891 1. .00 12. .94 C
ATOM 1825 C ASN A 326 31, .860 -1, .739 12. .649 1. .00 11, .80 C
ATOM 1826 O ASN A 326 31, .544 -1. .610 13. .834 1. .00 12. .08 O
ATOM 1827 CB ASN A 326 29, .962 -3, .185 11, .837 1. .00 10, .46 C
ATOM 1828 CG ASN A 326 29, .261 -2, .189 10. .942 1. .00 14, .62 C
ATOM 1829 ODl ASN A 326 29, .834 -1, .170 10, .548 1. .00 10, .01 0
ATOM 1830 ND2 ASN A 326 27, .998 -2. .460 10, .588 1. .00 10, .12 N
ATOM 1831 N PRO A 327 32, .488 -0, .752 12, .015 1. .00 12, .51 N
ATOM 1832 CA PRO A 327 32, .752 0. .534 12, .617 1, .00 13, .36 C
ATOM 1833 C PRO A 327 31. .470 1. .295 12. .944 1, .00 14, .81 C
ATOM 1834 0 PRO A 327 31. .464 2 .112 13. .881 1. .00 13, .79 0
ATOM 1835 CB PRO A 327 33, .535 1 .323 11. .573 1, .00 15, .50 C
ATOM 1836 CG PRO A 327 33 .846 0 .371 10, .476 1, .00 16. .62 C
ATOM 1837 CD PRO A 327 32. .867 -0 .774 10. .574 1, .00 14, .40 C
ATOM 1838 N ASN A 328 30. .402 1 .094 12, .154 1. .00 9, .74 N
ATOM 1839 CA ASN A 328 29 .143 1 .812 12. .402 1, .00 10 .19 C
ATOM 1840 C ASN A 328 28 .243 0 .879 13, .204 1. .00 12. .18 C
ATOM 1841 0 ASN A 328 27 .390 0 .184 12. .676 1. .00 11, .06 0
ATOM 1842 CB ASN A 328 28 .527 2 .226 11 .063 1, .00 12, .80 C
ATOM 1843 CG ASN A 328 29 .456 3. .172 10 .322 1, .00 14 .33 C
ATOM 1844 ODl ASN A 328 30 .041 4 .051 10 .974 1. .00 14 .84 0
ATOM 1845 ND2 ASN A 328 29 .610 3 .035 9. .011 1. .00 11 .92 N
ATOM 1846 N TYR A 329 28 .569 0. .777 14 .497 1. .00 13 .51 N
ATOM 1847 CA TYR A 329 27 .996 -0 .189 15 .398 1 .00 13 .75 C
ATOM 1848 C TYR A 329 26 .695 0 .245 16 .045 1 .00 12 .00 C
ATOM 1849 0 TYR A 329 26 .132 -0 .570 16 .783 1 .00 12 .57 O
ATOM 1850 CB TYR A 329 29 .045 -0 .559 16 .476 1 .00 14 .67 C
ATOM 1851 CG TYR A 329 29 .444 0 .618 17 .333 1 .00 18 .64 C
ATOM 1852 CDl TYR A 329 28 .684 1 .014 18 .422 1 .00 17 .95 C ATOM 1853 CD2 TYR A 329 30.605 1.342 17.048 1..00 21..28 c
ATOM 1854 CE1 TYR A 329 29. 061 2. 101 19. 194 1. ,00 20. ,94 c
ATOM 1855 CE2 TYR A 329 30. 989 2. 428 17. .813 1. .00 21. ,04 c
ATOM 1856 CZ TYR A 329 30. 207 2. 797 18. .889 1. 00 23. ,73 c ATOM 1857 OH TYR A 329 30. 571 3. 885 19. .660 1. .00 26. ,36 0
ATOM 1858 N ASP A 330 26. 203 1. 451 15. .785 1. .00 12. ,31 N
ATOM 1859 CA ASP A 330 24. 924 1. 894 16. .347 1. .00 11. ,92 C
ATOM 1860 C ASP A 330 24. 245 2. 760 15. .284 1. ,00 12. ,73 C
ATOM 1861 O ASP A 330 24. 861 3. 070 14. .255 1. ,00 10. ,45 0 ATOM 1862 CB ASP A 330 25. 062 2. 627 17. ,675 1. .00 14. ,42 C
ATOM 1863 CG ASP A 330 26. 007 3. 802 17. .654 1. .00 15. ,78 C
ATOM 1864 ODl ASP A 330 26. 263 4. .391 16. .580 1. .00 14. ,20 o
ATOM 1865 OD2 ASP A 330 26. .522 4. 184 18. ,736 1. .00 16. ,79 0
ATOM 1866 N GLU A 331 22. 997 3. ,146 15. ,511 1. .00 12. ,67 N ATOM 1867 CA GLU A 331 22. .269 3. ,907 14. ,491 1. .00 11. ,99 C
ATOM 1868 C GLU A 331 22. .816 5. ,303 14. ,285 1. .00 12. ,65 C
ATOM 1869 0 GLU A 331 22. .811 5. .736 13. .132 1. .00 11. .93 0
ATOM 1870 CB GLU A 331 20. .757 3. .933 14. .768 1. .00 7. .16 C
ATOM 1871 CG GLU A 331 20. .195 2. .502 14. .830 1. .00 9. .29 C ATOM 1872 CD GLU A 331 20. .294 1. .816 13. .475 1. .00 10. .33 C
ATOM 1873 OE1 GLU A 331 19. .807 2. .404 12. .492 1. .00 8. .53 0
ATOM 1874 OE2 GLU A 331 20. .919 0. .742 13. .355 1. .00 10. .92 o
ATOM 1875 N LYS A 332 23. .300 5. .982 15. .324 1. .00 13. .62 N
ATOM 1876 CA LYS A 332 23. .911 7. .298 15. .125 1. .00 11. .69 C ATOM 1877 C LYS A 332 25. .101 7. .222 14. .180 1. .00 10. .86 C
ATOM 1878 O LYS A 332 25. .239 8. .051 13. .288 1. .00 11. .24 O
ATOM 1879 CB LYS A 332 24. .338 7. .919 16. .462 1. .00 13. .33 C
ATOM 1880 CG LYS A 332 25. .004 9. .292 16. .311 1. .00 15. .61 C
ATOM 1881 CD LYS A 332 25. .338 9. .875 17. .691 1. .00 15. .28 c ATOM 1882 CE LYS A 332 26. .003 11. .237 17. .515 1. .00 18. .46 c
ATOM 1883 NZ LYS A 332 26. .180 11. .941 18. .816 1. .00 20. .17 N
ATOM 1884 N HIS A 333 25. .988 6. .233 14. .325 1. .00 12. .13 N
ATOM 1885 CA HIS A 333 27. .130 6. .085 13. .430 1. .00 10. .52 C
ATOM 1886 C HIS A 333 26. .633 5. .817 12. .004 1. .00 12. .35 C ATOM 1887 O HIS A 333 27. .197 6. .351 11. .045 1. .00 11. .58 0
ATOM 1888 CB HIS A 333 28. .044 4. .918 13. .808 1. .00 12. .44 C
ATOM 1889 CG HIS A 333 29. .019 5. .254 14. .894 1. .00 15. .77 C
ATOM 1890 ND1 HIS A 333 28. .702 5. .171 16, .226 1. .00 15. .79 N
ATOM 1891 CD2 HIS A 333 30, .309 5. .698 14. .813 1. .00 14. .51 C ATOM 1892 CE1 HIS A 333 29, .761 5. .541 16. .937 1. .00 17. .94 C
ATOM 1893 NE2 HIS A 333 30, .748 5. .860 16. .108 1. .00 15. .66 N
ATOM 1894 N TYR A 334 25, .649 4. .923 11. .878 1. .00 7. .78 N
ATOM 1895 CA TYR A 334 25, .116 4, .617 10. .547 1. .00 10. .34 C
ATOM 1896 C TYR A 334 24, .563 5. .856 9. .859 1. .00 10. .74 C ATOM 1897 0 TYR A 334 24, .930 6. .168 8. .719 1. .00 12. .95 O
ATOM 1898 CB TYR A 334 24. .051 3, .518 10. .680 1. .00 8. .54 C
ATOM 1899 CG TYR A 334 23, .168 3, .218 9, .489 1, .00 7, .49 C
ATOM 1900 CDl TYR A 334 23, .622 3, .298 8, .182 1, .00 8. .36 C
ATOM 1901 CD2 TYR A 334 21, .845 2, .805 9, .696 1, .00 6. .89 C ATOM 1902 CE1 TYR A 334 22, .807 3, .020 7, .098 1, .00 9, .11 C
ATOM 1903 CE2 TYR A 334 21, .026 2, .500 8, .620 1, .00 8. .56 C
ATOM 1904 CZ TYR A 334 21. .495 2, .610 7, .334 1, .00 8, .78 C
ATOM 1905 OH TYR A 334 20, .668 2, .312 6, .265 1, .00 7, .45 0
ATOM 1906 N ILE A 335 23. .655 6. .568 10, .515 1. .00 10. .74 N ATOM 1907 CA ILE A 335 23 .033 7, .756 9. .937 1, .00 9. .79 C
ATOM 1908 C ILE A 335 23 .985 8, .909 9, .679 1, .00 13, .38 C
ATOM 1909 O ILE A 335 23 .878 9. .571 8, .629 1. .00 11, .65 O
ATOM 1910 CB ILE A 335 21 .863 8, .192 10, .845 1. .00 10. .61 C
ATOM 1911 CGI ILE A 335 20 .765 7. .133 10, .688 1, .00 12, .96 C ATOM 1912 CG2 ILE A 335 21 .366 9 .579 10, .467 1. .00 11, .76 C
ATOM 1913 CDl ILE A 335 19 .663 7. .170 11, .716 1. .00 11. .64 C
ATOM 1914 N GLU A 336 24 .939 9 .139 10, .592 1. .00 9. .63 N
ATOM 1915 CA GLU A 336 25 .935 10 .199 10, .338 1. .00 12. .73 C
ATOM 1916 C GLU A 336 26 .784 9 .920 9, .115 1. .00 13, .16 C ATOM 1917 O GLU A 336 27 .124 10 .863 8. .391 1 .00 12. .25 0
ATOM 1918 CB GLU A 336 26 .762 10 .506 11, .584 1 .00 12, .44 C
ATOM 1919 CG GLU A 336 25 .946 11 .357 12 .555 1 .00 14 .68 C
ATOM 1920 CD GLU A 336 26 .731 11 .825 13 .770 1 .00 14 .65 c
ATOM 1921 OE1 GLU A 336 27 .835 11 .294 14 .011 1 .00 15 .28 0 ATOM 1922 OE2 GLU A 336 26 .195 12 .691 14 .491 1 .00 14 .11 0
ATOM 1923 N ALA A 337 27 .061 8 .679 8 .764 1 .00 14 .58 N
ATOM 1924 CA ALA A 337 27 .803 8 .337 7 .562 1 .00 14 .30 C ATOM 1925 C ALA A 337 26.,930 8..306 6..304 1..00 15.,31 c
ATOM 1926 O ALA A 337 27. ,381 8. ,589 5. ,189 1. .00 12. .60 0
ATOM 1927 CB ALA A 337 28. .404 6. ,943 7. .746 1. ,00 14. ,02 c
ATOM 1928 N PHE A 338 25. ,680 7. ,869 6. .450 1. ,00 10. ,62 N
ATOM 1929 CA PHE A 338 24. ,738 7. ,697 5. ,365 1. ,00 9. .89 C
ATOM 1930 C PHE A 338 24. ,135 8. ,979 4. ,828 1. ,00 8. ,70 C
ATOM 1931 O PHE A 338 24. ,142 9. ,215 3. ,614 1. .00 10. ,69 o
ATOM 1932 CB PHE A 338 23. ,614 6. ,772 5. ,886 1. ,00 11. ,18 c
ATOM 1933 CG PHE A 338 22. ,667 6. ,165 4. ,897 1. .00 11. ,79 c
ATOM 1934 CDl PHE A 338 22. .982 6. ,000 3. .559 1. .00 8. .39 c
ATOM 1935 CD2 PHE A 338 21. ,447 5. ,671 5. .358 1. ,00 9. ,80 c
ATOM 1936 CE1 PHE A 338 22. ,096 5. ,399 2. .685 1. .00 8. ,73 c
ATOM 1937 CE2 PHE A 338 20. .552 5. ,070 4. ,488 1. ,00 9. ,34 c
ATOM 1938 CZ PHE A 338 20. ,877 4. ,933 3. .154 1. .00 12. ,90 c
ATOM 1939 N ARG A 339 23. ,717 9. .901 5. ,696 1. .00 6. .96 N
ATOM 1940 CA ARG A 339 23. .084 11. ,148 5. .261 1. ,00 9. ,28 C
ATOM 1941 C ARG A 339 23. .860 11. .971 4. .269 1. .00 9. .30 C
ATOM 1942 0 ARG A 339 23. .310 12. .383 3. .238 1. .00 11. .10 o
ATOM 1943 CB ARG A 339 22. .654 11. .960 6. .482 1. .00 9. .94 c
ATOM 1944 CG ARG A 339 22. .182 13. .380 6. .260 1. .00 12. .91 c
ATOM 1945 CD ARG A 339 21. .045 13. .545 5. .261 1. .00 14. .88 c
ATOM 1946 NE ARG A 339 20. .816 14. .987 5. .111 1. .00 16. .65 N
ATOM 1947 CZ ARG A 339 19. .982 15. .673 5. .878 1. .00 16. .47 C
ATOM 1948 NHl ARG A 339 19. .275 15. .042 6. .810 1. .00 14. .80 N
ATOM 1949 NH2 ARG A 339 19. .860 16. .976 5. .679 1. .00 18. .03 N
ATOM 1950 N PRO A 340 25. .137 12. .284 4. .493 1. .00 12. .84 N
ATOM 1951 CA PRO A 340 25. .916 13. .074 3. .549 1. .00 12. .72 C
ATOM 1952 C PRO A 340 25. .936 12. .483 2. .153 1. .00 12. .78 C
ATOM 1953 O PRO A 340 25. .890 13. .216 1. .150 1. .00 10. .55 O
ATOM 1954 CB PRO A 340 27. .312 13. .154 4. .171 1. .00 14. .90 C
ATOM 1955 CG PRO A 340 27. .120 12. .804 5. .606 1. .00 16. .25 C
ATOM 1956 CD PRO A 340 25. .898 11. .930 5. .708 1. .00 13. .20 C
ATOM 1957 N LEU A 341 26. .019 11. .148 2. .025 1. .00 10. .11 N
ATOM 1958 CA LEU A 341 26. .019 10. .516 0. .710 1. .00 9. .98 C
ATOM 1959 C LEU A 341 24. .670 10. .638 0. .028 1. .00 9. .00 C
ATOM 1960 0 LEU A 341 24. .592 10. .873 -1. .181 1. .00 10. .98 O
ATOM 1961 CB LEU A 341 26. .432 9. .040 0. .840 1. .00 13. .65 C
ATOM 1962 CG LEU A 341 27. .918 8, .936 1. .269 1. .00 19. .15 C
ATOM 1963 CDl LEU A 341 28. .126 7. .751 2. .186 1. .00 22. .88 C
ATOM 1964 CD2 LEU A 341 28. .770 8. .837 0. .023 1. .00 23. .80 C
ATOM 1965 N LEU A 342 23. .607 10. .496 0, .815 1. .00 8. .10 N
ATOM 1966 CA LEU A 342 22, .255 10. .660 0. .278 1. .00 11. .17 C
ATOM 1967 C LEU A 342 22, .086 12, .103 -0. .196 1. .00 10. .19 C
ATOM 1968 0 LEU A 342 21, .525 12, .363 -1. .263 1. .00 10. .33 0
ATOM 1969 CB LEU A 342 21, .224 10, .337 1. .374 1. .00 7. .92 C
ATOM 1970 CG LEU A 342 21, .098 8, .859 1. .758 1. .00 11. .33 C
ATOM 1971 CDl LEU A 342 20, .478 8, .717 3. .137 1. .00 7. .93 C
ATOM 1972 CD2 LEU A 342 20, .246 8, .117 0. .723 1. .00 8. .97 C
ATOM 1973 N GLU A 343 22, .446 13, .056 0. .667 1. .00 10. .39 N
ATOM 1974 CA GLU A 343 22, .263 14, .475 0. .381 1. .00 10. .01 C
ATOM 1975 C GLU A 343 23, .012 14, .922 -0. .857 1. .00 11. .97 C
ATOM 1976 0 GLU A 343 22, .491 15, .661 -1. .708 1. .00 12. .57 O
ATOM 1977 CB GLU A 343 22. .598 15, .318 1. .621 1. .00 12. .83 C
ATOM 1978 CG GLU A 343 22, .294 16, .798 1. .396 1, .00 18. .77 C
ATOM 1979 CD GLU A 343 22, .024 17. .582 2. .655 1. .00 19. .20 C
ATOM 1980 0E1 GLU A 343 22, .291 17. .078 3. .768 1, .00 21. .19 O
ATOM 1981 0E2 GLU A 343 21. .525 18, .727 2, .548 1, .00 21. .18 O
ATOM 1982 N ALA A 344 24, .226 14. .410 -1. .066 1, .00 11. .16 N
ATOM 1983 CA ALA A 344 25. .017 14. .719 -2, .253 1, .00 13. .43 C
ATOM 1984 C ALA A 344 24 .367 14, .212 -3, .530 1, .00 14, .55 C
ATOM 1985 0 ALA A 344 24 .661 14. .647 -4, .657 1, .00 15, .36 O
ATOM 1986 CB ALA A 344 26 .411 14. .105 -2, .079 1. .00 11, .18 C
ATOM 1987 N ARG A 345 23. .488 13 .222 -3, .423 1, .00 12, .33 N
ATOM 1988 CA ARG A 345 22 .784 12, .630 -4, .537 1, .00 13, .25 C
ATOM 1989 C ARG A 345 21 .347 13 .137 -4, .630 1, .00 14, .69 C
ATOM 1990 0 ARG A 345 20 .534 12 .511 -5, .309 1, .00 11, .15 0
ATOM 1991 CB ARG A 345 22 .841 11 .098 -4 .429 1 .00 13 .43 C
ATOM 1992 CG ARG A 345 24 .292 10 .619 -4 .534 1 .00 14 .60 C
ATOM 1993 CD ARG A 345 24 .485 9 .154 -4 .226 1 .00 17 .43 C
ATOM 1994 NE ARG A 345 25 .862 8 .730 -4 .452 1 .00 17 .71 N
ATOM 1995 CZ ARG A 345 26 .928 9 .074 -3 .738 1 .00 23 .50 C
ATOM 1996 NHl ARG A 345 26 .863 9 .864 -2 .669 1 .00 17 .69 N ATOM 1997 NH2 ARG A 345 28..114 8.,602 -4..103 1..00 23..81 N
ATOM 1998 N GLY A 346 21. .060 14. .280 -4. .010 1. .00 11. .84 N
ATOM 1999 CA GLY A 346 19. .764 14. .918 -4. .178 1. .00 12. .92 C
ATOM 2000 C GLY A 346 18. .678 14. .563 -3. .187 1. .00 11. .40 C
ATOM 2001 O GLY A 346 17. .527 15. .019 -3. .337 1. .00 8. .76 O
ATOM 2002 N PHE A 347 19. .018 13. .780 -2. .168 1. .00 12. .55 N
ATOM 2003 CA PHE A 347 17. .996 13. .385 -1. .177 1. .00 11. .96 C
ATOM 2004 C PHE A 347 18. .454 13. .708 0. .227 1. .00 11. .44 C
ATOM 2005 0 PHE A 347 19. .114 12. .896 0. .872 1. .00 11. .58 O
ATOM 2006 CB PHE A 347 17. .750 11. .876 -1. .340 1. .00 11. .24 C
ATOM 2007 CG PHE A 347 16. .637 11. .259 -0. .528 1. .00 13. .04 C
ATOM 2008 CDl PHE A 347 15. .647 12. .015 0. .069 1. .00 12. .13 C
ATOM 2009 CD2 PHE A 347 16. .586 9. .870 -0. .389 1. .00 11. .26 C
ATOM 2010 CE1 PHE A 347 14. .626 11. .425 0. .798 1. .00 13. .16 C
ATOM 2011 CE2 PHE A 347 15. .574 9. .270 0. .339 1. .00 11. .40 C
ATOM 2012 CZ PHE A 347 14. .596 10. .042 0. .925 1. .00 11. .56 C
ATOM 2013 N PRO A 348 18. .063 14. .841 0. .799 1. .00 13. .23 N
ATOM 2014 CA PRO A 348 18. .484 15. .260 2. .138 1. .00 13. .82 C
ATOM 2015 C PRO A 348 17. .563 14. .639 3. .180 1. .00 13. .97 C
ATOM 2016 O PRO A 348 16. .813 15. .285 3. .910 1. .00 12. .48 O
ATOM 2017 CB PRO A 348 18. .308 16. .785 2. .067 1. .00 13. .80 C
ATOM 2018 CG PRO A 348 17. .096 16. .939 1. .201 1. .00 14. .81 C
ATOM 2019 CD PRO A 348 17. .264 15. .889 0. .124 1. .00 13. .97 C
ATOM 2020 N ALA A 349 17. .558 13. .315 3. .208 1. .00 11. .56 N
ATOM 2021 CA ALA A 349 16. .700 12. .506 4. .034 1. .00 12. .18 C
ATOM 2022 C ALA A 349 16. .841 12. .765 5. .527 1. .00 10. .93 C
ATOM 2023 O ALA A 349 17. .917 12. .750 6. .109 1. .00 10. .86 O
ATOM 2024 CB ALA A 349 16. .965 11. .024 3. .749 1. .00 10. .43 C
ATOM 2025 N GLN A 350 15. .685 12. .985 6. .130 1. .00 9. .76 N
ATOM 2026 CA GLN A 350 15. .559 13. .090 7. .576 1. .00 10. .00 C
ATOM 2027 C GLN A 350 15. .222 11. .676 8. .049 1. .00 9. .55 C
ATOM 2028 O GLN A 350 14. .642 10. .910 7. .267 1. .00 10. .83 0
ATOM 2029 CB GLN A 350 14. .492 14. .090 7. .996 1. .00 9. .57 C
ATOM 2030 CG GLN A 350 14. .922 15. .536 7. .812 1. .00 12. .31 C
ATOM 2031 CD GLN A 350 16. .092 15. .926 8. .700 1. .00 14. .64 c
ATOM 2032 OE1 GLN A 350 17. .204 16. .158 8. .231 1. .00 16. .94 o
ATOM 2033 NE2 GLN A 350 15. .868 16. .018 10. .010 1. .00 13. .88 N
ATOM 2034 N PHE A 351 15. .663 11. .305 9. .240 1. .00 8. .69 N
ATOM 2035 CA PHE A 351 15. .455 9. .939 9. .698 1. .00 8. .77 C
ATOM 2036 C PHE A 351 14. .556 9. .803 10. .896 1. .00 8. .32 C
ATOM 2037 0 PHE A 351 14. .406 10. .716 11. .711 1. .00 8. .72 0
ATOM 2038 CB PHE A 351 16. .842 9. .380 10. .117 1. .00 10. .92 C
ATOM 2039 CG PHE A 351 17. .733 9. .089 8. .945 1. .00 9. .64 C
ATOM 2040 CDl PHE A 351 18. .421 10. .103 8. .297 1. .00 11. .78 C
ATOM 2041 CD2 PHE A 351 17. .881 7. .789 8. .496 1. .00 10. .24 C
ATOM 2042 CE1 PHE A 351 19. .219 9. .810 7. .198 1. .00 10. .48 C
ATOM 2043 CE2 PHE A 351 18. .694 7. .489 7. .413 1. .00 8. .56 C
ATOM 2044 CZ PHE A 351 19. .370 8. .513 6. .771 1. .00 9. .23 C
ATOM 2045 N ILE A 352 13. .964 8. .613 11. .033 1. .00 7. .47 N
ATOM 2046 CA ILE A 352 13. .256 8. .251 12, .254 1, .00 8. .08 C
ATOM 2047 C ILE A 352 13. .897 6, .909 12, .650 1. .00 7. .08 C
ATOM 2048 O ILE A 352 14, .272 6, .129 11. .764 1. .00 8. .28 0
ATOM 2049 CB ILE A 352 11, .745 8, .145 12. .239 1. .00 7. .94 C
ATOM 2050 CGI ILE A 352 11, .278 7, .093 11. .213 1, .00 6. .92 C
ATOM 2051 CG2 ILE A 352 11. .086 9. .490 11. .954 1. .00 7. .41 C
ATOM 2052 CDl ILE A 352 9, .764 6. .881 11. .272 1. .00 10. .15 C
ATOM 2053 N VAL A 353 14, .104 6. .697 13. .944 1. .00 7. .36 N
ATOM 2054 CA VAL A 353 14. .814 5. .494 14. .390 1. .00 8. .29 C
ATOM 2055 C VAL A 353 14. .024 4. .719 15. .438 1. .00 7. .66 C
ATOM 2056 O VAL A 353 13. .646 5. .312 16. .448 1. .00 7. .89 O
ATOM 2057 CB VAL A 353 16. .174 5. .868 15. .036 1. .00 8. .48 C
ATOM 2058 CGI VAL A 353 16. .932 4. .617 15. .465 1. .00 7. .58 C
ATOM 2059 CG2 VAL A 353 17. .043 6. .710 14. .101 1. .00 11. .26 C
ATOM 2060 N ASP A 354 13. .806 3. .432 15. .194 1. .00 7. .41 N
ATOM 2061 CA ASP A 354 13. .062 2. .593 16. .147 1. .00 8. .11 C
ATOM 2062 C ASP A 354 13. .975 2. .332 17. .346 1. .00 9. .35 C
ATOM 2063 O ASP A 354 15, .160 2, .038 17. .191 1, .00 7. .62 0
ATOM 2064 CB ASP A 354 12. .633 1, .294 15, .482 1. .00 6, .20 C
ATOM 2065 CG ASP A 354 11. .586 0, .460 16, .174 1. .00 7. .49 C
ATOM 2066 ODl ASP A 354 11, .241 0, .771 17, .334 1. .00 7. .99 O
ATOM 2067 OD2 ASP A 354 11 .084 -0, .522 15, .580 1. .00 7. .38 O
ATOM 2068 N GLN A 355 13. .443 2, .571 18, .535 1. .00 11. .53 N ATOM 2069 CA GLN A 355 14.138 2.,358 19..796 1.00 11..42 c
ATOM 2070 C GLN A 355 13. 214 1. .614 20. .755 1. 00 12. 94 c
ATOM 2071 O GLN A 355 13. 517 1. .428 21. .939 1. 00 9. 56 o
ATOM 2072 CB GLN A 355 14. 598 3. .669 20. .409 1. 00 13. 21 c
ATOM 2073 CG GLN A 355 15. 724 4. .377 19. .670 1. 00 11. 58 c
ATOM 2074 CD GLN A 355 17. 038 3. 635 19. 792 1. 00 13. 08 c
ATOM 2075 OE1 GLN A 355 17. 662 3. ,659 20. .856 1. .00 11. ,07 0
ATOM 2076 NE2 GLN A 355 17. 453 2. .962 18. .722 1. .00 12. .59 N
ATOM 2077 N GLY A 356 12. 131 1. .044 20. ,203 1. .00 9. ,58 N
ATOM 2078 CA GLY A 356 11. 183 0. ,309 21. ,030 1. .00 11. ,28 C
ATOM 2079 C GLY A 356 11. 785 -0. ,859 21. ,798 1. .00 11. ,42 C
ATOM 2080 0 GLY A 356 11. 231 -1. ,286 22. ,819 1. .00 13. ,11 0
ATOM 2081 N ARG A 357 12. 845 -1. ,493 21. ,300 1. .00 9. .98 N
ATOM 2082 CA ARG A 357 13. 452 -2. ,641 21. ,980 1. .00 10. .49 C
ATOM 2083 C ARG A 357 14. 956 -2. ,432 22. ,118 1. 00 10. ,61 C
ATOM 2084 O ARG A 357 15. 712 -3. .405 22. ,096 1. .00 10. .60 O
ATOM 2085 CB ARG A 357 13. ,094 -3. .918 21. ,191 1. ,00 6. .30 C
ATOM 2086 CG ARG A 357 11. ,592 -4. .235 21. .219 1. ,00 9. .33 C
ATOM 2087 CD ARG A 357 11. ,152 -5. .573 20. .686 1. ,00 10. .11 C
ATOM 2088 NE ARG A 357 11. .503 -5. .805 19. .286 1. ,00 9. ,06 N
ATOM 2089 CZ ARG A 357 11. ,262 -6. .942 18. .642 1. ,00 11. .52 C
ATOM 2090 NHl ARG A 357 10. ,671 -7. .923 19. .318 1. .00 10. .50 N
ATOM 2091 NH2 ARG A 357 11. ,635 -7. .125 17. .372 1. ,00 7. ,18 N
ATOM 2092 N SER A 358 15. .380 -1. .170 22. .232 1. ,00 11. ,46 N
ATOM 2093 CA SER A 358 16. .805 -0. .824 22. .247 1. .00 10. ,13 C
ATOM 2094 C SER A 358 17. .370 -0. .372 23. .583 1. .00 11. .53 C
ATOM 2095 O SER A 358 18. .539 0. .066 23. .687 1. .00 12. .37 O
ATOM 2096 CB SER A 358 16. .988 0. .348 21. .245 1. .00 9. .78 C
ATOM 2097 OG SER A 358 16. .843 -0. .180 19. .916 1. .00 9. .37 O
ATOM 2098 N GLY A 359 16. .567 -0. .459 24. .631 1. .00 8. .41 N
ATOM 2099 CA GLY A 359 16. .929 0. .013 25. .945 1. .00 11. .24 C
ATOM 2100 C GLY A 359 18. .168 -0. .645 26. .556 1. .00 10. .77 C
ATOM 2101 O GLY A 359 19. .005 0. .093 27. .066 1. .00 14. .30 O
ATOM 2102 N LYS A 360 18. .317 -1. .947 26. .449 1. .00 11. .40 N
ATOM 2103 CA LYS A 360 19. .437 -2. .659 27. .063 1. .00 13. .69 C
ATOM 2104 C LYS A 360 20. .533 -2. .957 26. .044 1. .00 13. .62 C
ATOM 2105 O LYS A 360 20. .292 -3. .592 25. .016 1. .00 12. .09 0
ATOM 2106 CB LYS A 360 18. .945 -3, .982 27. .662 1. .00 12. .11 C
ATOM 2107 CG LYS A 360 19. .889 -4, .578 28. .705 1. .00 17. .84 C
ATOM 2108 CD LYS A 360 19. .223 -5, .780 29. .374 1. .00 23. .30 C
ATOM 2109 CE LYS A 360 19. .989 -6, .259 30. .595 1. .00 29. .30 C
ATOM 2110 NZ LYS A 360 21. .394 -6, .616 30. .263 1. .00 29. .46 N
ATOM 2111 N GLN A 361 21. .721 -2, .405 26. .310 1. .00 12. .86 N
ATOM 2112 CA GLN A 361 22. .870 -2, .598 25. .421 1. .00 14. .17 C
ATOM 2113 C GLN A 361 24. .094 -3, .041 26. .226 1. .00 16. .49 C
ATOM 2114 O GLN A 361 24. .384 -2, .414 27. .241 1. .00 16. .24 O
ATOM 2115 CB GLN A 361 23, .188 -1, .268 24. .731 1, .00 14. .32 C
ATOM 2116 CG GLN A 361 22, .077 -0 .680 23. .869 1, .00 9. .89 C
ATOM 2117 CD GLN A 361 21. .740 -1. .556 22, .684 1, .00 13. .07 C
ATOM 2118 OE1 GLN A 361 22. .618 -2. .284 22, .210 1. .00 13. .09 O
ATOM 2119 NE2 GLN A 361 20, .502 -1. .495 22, .177 1, .00 8. .77 N
ATOM 2120 N PRO A 362 24, .814 -4, .042 25. .762 1. .00 18. .13 N
ATOM 2121 CA PRO A 362 24, .476 -4. .805 24, .579 1. .00 16. .66 C
ATOM 2122 C PRO A 362 23, .230 -5. .656 24, .790 1. .00 17. .75 C
ATOM 2123 O PRO A 362 22, .883 -5. .897 25, .958 1. .00 15. .49 0
ATOM 2124 CB PRO A 362 25, .648 -5, .763 24, .397 1. .00 19. .10 C
ATOM 2125 CG PRO A 362 26 .715 -5 .340 25 .342 1. .00 20. .94 C
ATOM 2126 CD PRO A 362 26 .022 -4. .595 26 .441 1. .00 19, .31 C
ATOM 2127 N THR A 363 22 .642 -6. .190 23 .716 1. .00 12. .07 N
ATOM 2128 CA THR A 363 21 .485 -7 .063 23 .909 1. .00 13. .87 C
ATOM 2129 C THR A 363 21 .947 -8 .483 24 .229 1. .00 16. .38 C
ATOM 2130 O THR A 363 23 .159 -8 .740 24 .353 1. .00 17. .15 O
ATOM 2131 CB THR A 363 20 .622 -7 .100 22 .629 1, .00 14, .61 C
ATOM 2132 OGl THR A 363 21, .374 -7 .829 21, .648 1, .00 14, .52 O
ATOM 2133 CG2 THR A 363 20 .304 -5 .693 22 .129 1. .00 10, .96 C
ATOM 2134 N GLY A 364 21, .033 -9 .445 24 .237 1. .00 14, .44 N
ATOM 2135 CA GLY A 364 21 .397 -10 .842 24 .429 1. .00 16 .91 C
ATOM 2136 C GLY A 364 21 .640 -11 .562 23 .107 1. .00 15 .93 C
ATOM 2137 0 GLY A 364 21 .759 -12 .796 23 .069 1. .00 16 .01 O
ATOM 2138 N GLN A 365 21 .670 -10 .837 21 .990 1. .00 13 .92 N
ATOM 2139 CA GLN A 365 21 .895 -11 .420 20 .681 1. .00 12 .65 C
ATOM 2140 C GLN A 365 23 .294 -12 .045 20 .600 1. .00 14 .06 C ATOM 2141 O GLN A 365 24.255 -11.390 21.,010 1..00 14.,30 o
ATOM 2142 CB GLN A 365 21. 821 -10. 362 19. .565 1. .00 11. ,46 c
ATOM 2143 CG GLN A 365 20. 408 -9. 802 19. ,372 1. .00 11. ,44 c
ATOM 2144 CD GLN A 365 20. 377 -8. 530 18. ,555 1. ,00 8. .49 c
ATOM 2145 OE1 GLN A 365 20. 789 -7. .483 19. ,046 1. .00 10. ,68 o
ATOM 2146 NE2 GLN A 365 19. 935 -8. 604 17. .302 1. .00 10. .40 N
ATOM 2147 N LYS A 366 23. 376 -13. 245 20. .061 1. .00 14. .56 N
ATOM 2148 CA LYS A 366 24. 655 -13. 923 19. ,891 1. .00 16. ,55 C
ATOM 2149 C LYS A 366 25. .310 -13. 449 18. .600 1. .00 17. .19 C
ATOM 2150 O LYS A 366 26. ,529 -13. 434 18. 461 1. .00 14. .35 0
ATOM 2151 CB LYS A 366 24. 500 -15. 450 19. .865 1. .00 17. .82 C
ATOM 2152 CG LYS A 366 24. 104 -16. 000 21. .237 1. .00 25. .09 C
ATOM 2153 CD LYS A 366 25. .167 -15. 643 22. .277 1. .00 28. .19 C
ATOM 2154 CE LYS A 366 26. 095 -16. 817 22. .543 1. .00 32. .67 C
ATOM 2155 NZ LYS A 366 25. 665 -17. 535 23. .787 1. .00 36. 57 N
ATOM 2156 N GLU A 367 24. 488 -13. 163 17. .595 1. ,00 14. .58 N
ATOM 2157 CA GLU A 367 24. ,897 -12. ,661 16. .291 1. .00 16. .66 C
ATOM 2158 C GLU A 367 23. ,940 -11. ,511 15. .939 1. .00 16. ,50 C
ATOM 2159 O GLU A 367 22. .764 -11. ,520 16. .319 1. .00 11. ,08 0
ATOM 2160 CB GLU A 367 24. .900 -13. ,707 15. .190 1. .00 18. ,74 C
ATOM 2161 CG AGLU A 367 25. .785 -14. ,922 15. ,359 0. .50 19. ,66 C
ATOM 2162 CG BGLU A 367 25. .883 -14. ,840 15. ,413 0. .50 22. ,22 C
ATOM 2163 CD AGLU A 367 27. .269 -14. ,624 15. .434 0. .50 21. ,41 C
ATOM 2164 CD BGLU A 367 25. .887 -15. ,915 14. .358 0. .50 23. ,81 C
ATOM 2165 OE1AGLU A 367 27. .693 -13. ,538 14. ,986 0. .50 20. ,72 O
ATOM 2166 OE1BGLU A 367 25. .208 -15. .749 13. ,325 0. .50 26. ,57 O
ATOM 2167 OE2AGLU A 367 28. .037 -15. .479 15. .934 0. ,50 20. ,01 O
ATOM 2168 OE2BGLU A 367 26. .579 -16. ,938 14. .559 0. ,50 26. ,93 O
ATOM 2169 N TRP A 368 24. .439 -10. ,500 15. .250 1. .00 13. ,30 N
ATOM 2170 CA TRP A 368 23. .691 -9. ,304 14. .915 1. .00 13. .09 C
ATOM 2171 C TRP A 368 22. .463 -9. ,544 14. .061 1. .00 12. .80 C
ATOM 2172 O TRP A 368 21. .435 -8. ,871 14. .250 1. .00 10. .69 O
ATOM 2173 CB TRP A 368 24. .611 -8. .304 14. .183 1. .00 14. .76 C
ATOM 2174 CG TRP A 368 24. .283 -6. .859 14. .398 1. .00 13. .52 C
ATOM 2175 CDl TRP A 368 23. .175 -6. .329 14. .994 1. .00 13. .63 C
ATOM 2176 CD2 TRP A 368 25. .092 -5. .742 14. .009 1. .00 11. .73 C
ATOM 2177 NE1 TRP A 368 23. .239 -4. .957 15. .004 1. .00 12. .26 N
ATOM 2178 CE2 TRP A 368 24. .413 -4. .573 14. .397 1. .00 12. .86 C
ATOM 2179 CE3 TRP A 368 26. .327 -5. .623 13. .362 1. .00 13. .61 C
ATOM 2180 CZ2 TRP A 368 24. .922 -3. .299 14. .169 1. .00 10. .40 C
ATOM 2181 CZ3 TRP A 368 26, .834 -4. .357 13. .132 1. .00 11. .45 C
ATOM 2182 CH2 TRP A 368 26. .137 -3. .208 13. .536 1. .00 10. .27 C
ATOM 2183 N GLY A 369 22. .517 -10. .525 13. .164 1. .00 11. .73 N
ATOM 2184 CA GLY A 369 21. .417 -10. .878 12. .300 1. .00 12. .49 C
ATOM 2185 C GLY A 369 20. .338 -11. .698 13. .001 1, .00 12. .52 C
ATOM 2186 O GLY A 369 19. .412 -12. .154 12. .332 1, .00 13. .60 O
ATOM 2187 N HIS A 370 20. .440 -11. .932 14. .304 1. .00 12. .82 N
ATOM 2188 CA HIS A 370 19. .397 -12. .686 15. .022 1. .00 12. .27 C
ATOM 2189 C HIS A 370 18. .304 -11. .697 15. .409 1. .00 12. .62 C
ATOM 2190 O HIS A 370 18 .446 -10. .975 16, .397 1. .00 14, .21 O
ATOM 2191 CB HIS A 370 19 .986 -13, .391 16, .238 1 .00 10. .86 C
ATOM 2192 CG HIS A 370 20 .928 -14. .503 15, .853 1. .00 13, .37 C
ATOM 2193 ND1 HIS A 370 21 .663 -15. .203 16. .783 1. .00 15, .98 N
ATOM 2194 CD2 HIS A 370 21 .262 -15. .003 14 .637 1. .00 16, .19 C
ATOM 2195 CE1 HIS A 370 22 .387 -16. .119 16. .152 1. .00 15, .27 C
ATOM 2196 NE2 HIS A 370 22 .165 -16, .018 14 .854 1 .00 15, .58 N
ATOM 2197 N TRP A 371 17 .242 -11 .647 14 .613 1 .00 12. .56 N
ATOM 2198 CA TRP A 371 16 .209 -10 .637 14 .827 1 .00 12. .02 C
ATOM 2199 C TRP A 371 14 .955 -11. .117 15. .528 1. .00 12. .14 C
ATOM 2200 O TRP A 371 14 .091 -10 .291 15 .844 1 .00 10, .90 O
ATOM 2201 CB TRP A 371 15 .749 -10. .126 13. .438 1 .00 9, .54 C
ATOM 2202 CG TRP A 371 15 .366 -11. .188 12 .462 1. .00 11, .32 C
ATOM 2203 CDl TRP A 371 16 .152 -11. .684 11. .461 1 .00 14, .90 C
ATOM 2204 CD2 TRP A 371 14 .111 -11 .878 12, .343 1. .00 10, .64 C
ATOM 2205 NE1 TRP A 371 15 .477 -12 .637 10. .750 1. .00 15, .34 N
ATOM 2206 CE2 TRP A 371 14 .216 -12. .773 11 .274 1 .00 12, .80 C
ATOM 2207 CE3 TRP A 371 12 .913 -11 .825 13 .070 1 .00 6 .86 C
ATOM 2208 CZ2 TRP A 371 13 .185 -13 .631 10 .887 1 .00 12 .65 C
ATOM 2209 CZ3 TRP A 371 11 .879 -12 .657 12 .685 1 .00 9. .59 C
ATOM 2210 CH2 TRP A 371 12 .011 -13 .545 11 .608 1 .00 11 .86 C
ATOM 2211 N CYS A 372 14 .810 -12 .427 15 .725 1 .00 11 .94 N
ATOM 2212 CA CYS A 372 13 .564 -12 .903 16 .307 1 .00 11. .69 C ATOM 2213 C CYS A 372 13.493 -13.,035 17.,808 1.,00 12.,79 c
ATOM 2214 O CYS A 372 14. 248 -13. ,776 18. ,447 1. .00 11. ,89 o
ATOM 2215 CB CYS A 372 13. 231 -14. ,231 15. ,602 1. .00 11. .72 c
ATOM 2216 SG CYS A 372 11. .555 -14. ,776 16. ,052 1. ,00 10. .80 s
ATOM 2217 N ASN A 373 12. 580 -12. ,268 18. ,414 1. .00 10. .43 N
ATOM 2218 CA ASN A 373 12. 319 -12. ,339 19. ,851 1. ,00 11. ,60 C
ATOM 2219 C ASN A 373 13. 624 -12. ,463 20. ,630 1. ,00 11. ,60 C
ATOM 2220 0 ASN A 373 13. ,703 -13. ,286 21. ,562 1. ,00 12. ,62 0
ATOM 2221 CB ASN A 373 11. 449 -13. ,567 20. ,134 1. ,00 7. ,20 C
ATOM 2222 CG ASN A 373 10. .171 -13. ,675 19. ,356 1. ,00 10. .48 C
ATOM 2223 ODl ASN A 373 9. .466 -12. ,694 19. .079 1. ,00 11. ,46 o
ATOM 2224 ND2 ASN A 373 9. .828 -14. ,897 18. ,961 1. .00 9. .89 N
ATOM 2225 N ALA A 374 14. .529 -11. ,522 20. ,408 1. ,00 12. ,19 N
ATOM 2226 CA ALA A 374 15. 853 -11. .599 21. .013 1. ,00 13. ,32 C
ATOM 2227 C ALA A 374 15. .821 -11. .449 22. .527 1. ,00 13. ,60 C
ATOM 2228 O ALA A 374 15. .140 -10. .567 23. .058 1. .00 10. ,40 O
ATOM 2229 CB ALA A 374 16. .755 -10. .542 20. .389 1. .00 13. .95 C
ATOM 2230 N ILE A 375 16. .597 -12. .300 23. .200 1. .00 14. .26 N
ATOM 2231 CA ILE A 375 16. .675 -12. .212 24. .665 1. ,00 13. .63 C
ATOM 2232 C ILE A 375 17. .570 -11. .053 25. .067 1. .00 15. .61 C
ATOM 2233 0 ILE A 375 18. .305 -10. .489 24. .247 1. .00 14. .65 0
ATOM 2234 CB ILE A 375 17. .201 -13. .533 25. .262 1. .00 13. .82 C
ATOM 2235 CGI ILE A 375 18. .538 -13. .952 24. .636 1. .00 15. .63 C
ATOM 2236 CG2 ILE A 375 16. .152 -14. .622 25. .021 1. .00 12. .82 C
ATOM 2237 CDl ILE A 375 19. .210 -15. .159 25. .270 1. .00 15. .14 C
ATOM 2238 N GLY A 376 17. .461 -10. .639 26. .326 1. .00 14. .51 N
ATOM 2239 CA GLY A 376 18. .261 -9. .598 26. .918 1. .00 15. .11 C
ATOM 2240 C GLY A 376 18. .075 -8. .206 26. .350 1. .00 14. .35 C
ATOM 2241 0 GLY A 376 19. .008 -7. .398 26. .293 1. .00 12. .94 O
ATOM 2242 N THR A 377 16. .835 -7. .910 25. .969 1. .00 13. .43 N
ATOM 2243 CA THR A 377 16. .458 -6. .629 25. .411 1. .00 14. .16 C
ATOM 2244 C THR A 377 15. .477 -5. .919 26. .342 1. .00 14. .52 C
ATOM 2245 0 THR A 377 14. .844 -6. .566 27. .171 1. .00 13. .61 O
ATOM 2246 CB THR A 377 15. .784 -6. .781 24. .037 1. .00 14. .23 C
ATOM 2247 OGl THR A 377 14. .564 -7. .531 24. .209 1. .00 13. .57 0
ATOM 2248 CG2 THR A 377 16. .712 -7. .512 23. .063 1. .00 9. .16 C
ATOM 2249 N GLY A 378 15. .386 -4. .608 26. .215 1. .00 14. .11 N
ATOM 2250 CA GLY A 378 14. .490 -3. .827 27. .054 1. .00 13. .01 C
ATOM 2251 C GLY A 378 13. .863 -2. .667 26. .288 1. .00 12. .69 C
ATOM 2252 0 GLY A 378 14. .401 -2. .278 25. .259 1. .00 11. .68 0
ATOM 2253 N PHE A 379 12. .748 -2. .126 26. .771 1. .00 11. .50 N
ATOM 2254 CA PHE A 379 12. .139 -0. .955 26. .156 1. .00 12. .13 C
ATOM 2255 C PHE A 379 13. .146 0. .189 26. .136 1. .00 14. .61 C
ATOM 2256 0 PHE A 379 13. .843 0. .421 27. .138 1. .00 15. .51 0
ATOM 2257 CB PHE A 379 10. .910 -0. .460 26. .931 1. .00 13. .63 C
ATOM 2258 CG PHE A 379 9. .711 -1. .349 26. .771 1. .00 14. .82 C
ATOM 2259 CDl PHE A 379 9. .141 -1. .530 25. .520 1. .00 11. .34 C
ATOM 2260 CD2 PHE A 379 9. .133 -1. .974 27. .858 1. .00 14. .44 C
ATOM 2261 CE1 PHE A 379 8. .043 -2. .343 25. .351 1. .00 11. .61 c
ATOM 2262 CE2 PHE A 379 8. .038 -2. .797 27. .688 1. .00 14. .53 c
ATOM 2263 CZ PHE A 379 7. .485 -2. .989 26. .438 1. .00 12. .96 c
ATOM 2264 N GLY A 380 13. .236 0. .896 25. .024 1. .00 11. .68 N
ATOM 2265 CA GLY A 380 14. .203 1. .966 24. .890 1. .00 11. .35 C
ATOM 2266 C GLY A 380 13. .642 3. .372 25. .052 1. .00 10. .75 C
ATOM 2267 0 GLY A 380 12. .589 3. .562 25. .653 1. .00 12. .44 O
ATOM 2268 N MET A 381 14. .371 4. .356 24. .542 1. .00 10. .00 N
ATOM 2269 CA MET A 381 13. .951 5. .754 24. .638 1. .00 11. .50 C
ATOM 2270 C MET A 381 12. .514 5. .941 24. .142 1. .00 15. .24 C
ATOM 2271 0 MET A 381 12. .098 5. .313 23. .161 1. .00 11. .19 0
ATOM 2272 CB MET A 381 14. .891 6. .660 23. .871 1. .00 14. .46 c
ATOM 2273 CG MET A 381 16. .286 6. .838 24. .438 1. .00 18. .95 c
ATOM 2274 SD MET A 381 17, .272 7. .998 23. .460 1. .00 25. .67 s
ATOM 2275 CE MET A 381 17. .087 7, .233 21. .849 1. .00 19. .92 c
ATOM 2276 N ARG A 382 11. .739 6. .762 24. .866 1. .00 15. .63 N
ATOM 2277 CA ARG A 382 10, .352 6. .961 24. .460 1. .00 16. .59 c
ATOM 2278 C ARG A 382 10. .304 7, .814 23. .195 1. .00 12. .90 c
ATOM 2279 0 ARG A 382 11 .136 8 .698 23, .019 1, .00 11. .25 0
ATOM 2280 CB ARG A 382 9 .514 7 .662 25, .518 1, .00 19, .99 c
ATOM 2281 CG ARG A 382 9 .720 7 .274 26, .957 1. .00 24, .88 c
ATOM 2282 CD ARG A 382 9 .828 5 .763 27, .161 1. .00 25, .60 c
ATOM 2283 NE ARG A 382 10 .101 5 .566 28. .556 1. .00 31. .36 N
ATOM 2284 CZ ARG A 382 11 .039 4 .880 29, .179 1, .00 28. .51 C ATOM 2285 NHl ARG A 382 11.966 4.178 28.552 1.00 23.21 N
ATOM 2286 NH2 ARG A 382 10. 969 4. 919 30. 500 1. 00 26. 26 N
ATOM 2287 N PRO A 383 9. 266 7. 621 22. 394 1. 00 12. 79 N
ATOM 2288 CA PRO A 383 9. 091 8. .404 21. 184 1. 00 9. 96 C
ATOM 2289 C PRO A 383 9. 132 9. .890 21. ,451 1. 00 12. 67 C
ATOM 2290 0 PRO A 383 8. .525 10. ,380 22. .418 1. 00 10. 47 0
ATOM 2291 CB PRO A 383 7. .730 7. .972 20. ,634 1. 00 9. 92 C
ATOM 2292 CG PRO A 383 7. ,528 6. ,596 21. ,190 1. 00 12. .01 C
ATOM 2293 CD PRO A 383 8. ,233 6. ,575 22. ,534 1. 00 11. .26 C
ATOM 2294 N THR A 384 9. ,863 10. ,615 20. ,604 1. 00 9. ,35 N
ATOM 2295 CA THR A 384 9. 954 12. ,066 20. 773 1. 00 13. 08 C
ATOM 2296 C THR A 384 10. .452 12. .740 19. ,509 1. 00 11. 46 C
ATOM 2297 0 THR A 384 11. .211 12. ,154 18. .744 1. 00 11. 29 O
ATOM 2298 CB THR A 384 10. ,902 12. ,393 21. ,951 1. 00 13. 60 C
ATOM 2299 OGl THR A 384 11. ,023 13. ,815 22. ,086 1. 00 14. ,44 O
ATOM 2300 CG2 THR A 384 12. ,291 11. .815 21. ,716 1. 00 17. ,66 C
ATOM 2301 N ALA A 385 10. .043 13. .980 19. ,281 1. 00 11. .36 N
ATOM 2302 CA ALA A 385 10. .497 14. .786 18. ,172 1. .00 14. ,24 C
ATOM 2303 C ALA A 385 11. ,754 15. .560 18. ,587 1. .00 16. ,91 C
ATOM 2304 0 ALA A 385 12. .389 16. .192 17. .754 1. .00 18. ,52 O
ATOM 2305 CB ALA A 385 9. .420 15. .795 17. .767 1. .00 16. .27 C
ATOM 2306 N ASN A 386 12. .093 15. .543 19. .873 1. .00 16. ,95 N
ATOM 2307 CA ASN A 386 13. .268 16. ,270 20. .367 1. 00 19. 41 C
ATOM 2308 C ASN A 386 14. .431 15. ,314 20. ,530 1. 00 17. .81 C
ATOM 2309 0 ASN A 386 14. .702 14. .797 21. ,613 1. 00 17. ,23 O
ATOM 2310 CB ASN A 386 12. .912 16. .972 21. ,688 1. 00 21. .90 C
ATOM 2311 CG ASN A 386 11. .843 18. .014 21. .413 1. 00 22. .31 C
ATOM 2312 ODl ASN A 386 10. .682 17. .896 21. .800 1. .00 26. ,34 O
ATOM 2313 ND2 ASN A 386 12. .231 19. .061 20. .702 1. .00 26. ,26 N
ATOM 2314 N THR A 387 15. .106 15. .013 19. .414 1. .00 14. ,34 N
ATOM 2315 CA THR A 387 16. .162 14. .019 19. .418 1. ,00 15. .21 C
ATOM 2316 C THR A 387 17. .556 14. .542 19. .710 1. .00 17. .75 C
ATOM 2317 O THR A 387 18. .457 13. .726 19. .874 1. .00 17. .94 0
ATOM 2318 CB THR A 387 16. .211 13. .380 17. .996 1. .00 15. .42 C
ATOM 2319 OGl THR A 387 16, .616 14. .412 17. .106 1. .00 14. .59 O
ATOM 2320 CG2 THR A 387 14. .827 12. .893 17. .609 1. .00 13. .57 C
ATOM 2321 N GLY A 388 17. .755 15. .851 19. .622 1. .00 19. .77 N
ATOM 2322 CA GLY A 388 19. .091 16. .415 19. .810 1. .00 23. .06 C
ATOM 2323 C GLY A 388 19. .990 16. .134 18. .604 1. .00 24. .03 C
ATOM 2324 O GLY A 388 21. .211 16. .262 18. .719 1. .00 26. .20 0
ATOM 2325 N HIS A 389 19. .414 15, .755 17. .457 1. .00 19. .40 N
ATOM 2326 CA HIS A 389 20, .235 15, .493 16. .279 1. .00 14. .57 C
ATOM 2327 C HIS A 389 19, .573 16, .090 15. .049 1. .00 14. .06 C
ATOM 2328 O HIS A 389 18, .457 15, .686 14. .675 1. .00 12. .99 O
ATOM 2329 CB HIS A 389 20. .455 13, .979 16, .134 1. .00 13. .55 C
ATOM 2330 CG HIS A 389 21 .619 13 .721 15, .216 1, .00 13, .99 C
ATOM 2331 ND1 HIS A 389 21 .618 14 .056 13. .881 1, .00 13. .44 N
ATOM 2332 CD2 HIS A 389 22, .833 13, .177 15, .477 1. ,00 12. .87 C
ATOM 2333 CE1 HIS A 389 22, .791 13, .732 13, .345 1. .00 12. .87 c
ATOM 2334 NE2 HIS A 389 23, .540 13. .187 14, .298 1, .00 13. .79 N
ATOM 2335 N GLN A 390 20. .283 16. .950 14, .333 1, .00 14. .11 N
ATOM 2336 CA GLN A 390 19. .743 17. .625 13. .162 1. .00 16. .20 C
ATOM 2337 C GLN A 390 19 .160 16 .703 12. .094 1, .00 13. .84 C
ATOM 2338 0 GLN A 390 18 .334 17 .173 11 .298 1, .00 13, .37 0
ATOM 2339 CB GLN A 390 20 .825 18 .499 12. .505 1. .00 20, .15 C
ATOM 2340 CG GLN A 390 22 .088 17 .753 12 .106 1. .00 31. .09 C
ATOM 2341 CD GLN A 390 23 .248 18 .648 11 .720 1 .00 35, .92 C
ATOM 2342 OE1 GLN A 390 24 .432 18 .318 11 .849 1. .00 37, .48 O
ATOM 2343 NE2 GLN A 390 22 .936 19 .850 11 .225 1. .00 36. .68 N
ATOM 2344 N TYR A 391 19 .663 15 .492 11 .932 1. .00 12. .67 N
ATOM 2345 CA TYR A 391 19 .258 14 .578 10. .877 1. .00 14. .48 C
ATOM 2346 C TYR A 391 18 .093 13 .650 11. .228 1, .00 14. .99 C
ATOM 2347 O TYR A 391 17 .606 12 .886 10 .378 1, .00 12. .39 0
ATOM 2348 CB TYR A 391 20 .432 13 .624 10 .597 1. .00 15, .46 c
ATOM 2349 CG TYR A 391 21 .663 14 .210 9 .962 1 .00 17, .10 c
ATOM 2350 CDl TYR A 391 21 .685 15 .479 9 .402 1. .00 18, .66 c
ATOM 2351 CD2 TYR A 391 22 .824 13 .441 9 .903 1 .00 19. .40 c
ATOM 2352 CE1 TYR A 391 22 .840 15 .979 8 .823 1 .00 18. .42 c
ATOM 2353 CE2 TYR A 391 23 .986 13 .928 9 .325 1. .00 20 .24 c
ATOM 2354 CZ TYR A 391 23 .972 15 .200 8 .787 1 .00 21 .11 c
ATOM 2355 OH TYR A 391 25 .126 15 .679 8 .205 1 .00 19 .62 0
ATOM 2356 N VAL A 392 17 .730 13 .651 12 .493 1 .00 12 .39 N ATOM 2357 CA VAL A 392 16.714 12..748 13.032 1..00 13..23 c TOM 2358 C VAL A 392 15. 480 13. ,506 13. ,492 1. .00 14. ,92 c
ATOM 2359 O VAL A 392 15. 499 14. ,238 14. 490 1. 00 14. ,52 o
ATOM 2360 CB VAL A 392 17. 309 11. ,938 14. ,201 1. .00 11. ,35 c
ATOM 2361 CGI VAL A 392 16. ,324 10. ,883 14. ,711 1. .00 11. .19 c
ATOM 2362 CG2 VAL A 392 18. 627 11. ,253 13. .840 1. .00 10. ,63 c
ATOM 2363 N ASP A 393 14. .363 13. ,331 12. .773 1. ,00 14. .20 N
ATOM 2364 CA ASP A 393 13. ,107 13. ,965 13. ,153 1. .00 12. .15 C
ATOM 2365 C ASP A 393 12. 552 13. ,363 14. 449 1. ,00 10. .46 C
ATOM 2366 0 ASP A 393 11. .886 14. ,075 15. ,197 1. ,00 10. .32 o
ATOM 2367 CB ASP A 393 12. ,004 13. .759 12. .120 1. ,00 10. .53 c
ATOM 2368 CG ASP A 393 12. 166 14. ,596 10. .878 1. .00 10. .53 c
ATOM 2369 ODl ASP A 393 12. ,859 15. ,627 10. ,979 1. ,00 10. .17 0
ATOM 2370 OD2 ASP A 393 11. ,618 14. .244 9. .812 1. .00 9. .58 o
ATOM 2371 N ALA A 394 12. ,782 12. .067 14. ,665 1. ,00 9. .78 N
ATOM 2372 CA ALA A 394 12. ,242 11. .484 15. ,881 1. ,00 10. .04 C
ATOM 2373 C ALA A 394 12. ,788 10. .096 16. .175 1. .00 10. .84 C
ATOM 2374 O ALA A 394 13. .199 9. .323 15. .326 1. .00 11. .29 0
ATOM 2375 CB ALA A 394 10. .717 11. .284 15. ,756 1. .00 8. .93 C
ATOM 2376 N PHE A 395 12. .704 9. .829 17. .474 1. .00 11. .98 N
ATOM 2377 CA PHE A 395 12. .906 8. .457 17. .939 1. .00 10. .32 C
ATOM 2378 C PHE A 395 11. .474 7. .927 18. .057 1. ,00 9. .70 C
ATOM 2379 0 PHE A 395 10. .594 8. .655 18. .502 1. .00 8. .96 0
ATOM 2380 CB PHE A 395 13. .572 8. .451 19. .292 1. .00 10. .45 C
ATOM 2381 CG PHE A 395 15. .013 8. .896 19. ,186 1. ,00 11. ,98 C
ATOM 2382 CDl PHE A 395 15. .872 8. .196 18. ,372 1. ,00 13. .78 C
ATOM 2383 CD2 PHE A 395 15. .486 9. .985 19. .886 1. .00 17. .42 C
ATOM 2384 CE1 PHE A 395 17. .201 8. .543 18. ,243 1. ,00 17. .08 C
ATOM 2385 CE2 PHE A 395 16. .817 10. .357 19. .774 1. .00 16. .11 c
ATOM 2386 CZ PHE A 395 17. .670 9. .639 18. .950 1. .00 17. .10 c
ATOM 2387 N VAL A 396 11. .281 6. .697 17. .603 1. ,00 9. .89 N
ATOM 2388 CA VAL A 396 9. .938 6. .133 17. .603 1. .00 7. .78 C
ATOM 2389 C VAL A 396 9. .928 4. .693 18. .058 1. .00 8. .54 c
ATOM 2390 O VAL A 396 10. .959 4. .061 18. .276 1. .00 8. .53 o
ATOM 2391 CB VAL A 396 9. .408 6. .161 16. .138 1. .00 8. .91 c
ATOM 2392 CGI VAL A 396 9. .009 7. .571 15. .714 1. .00 7. .56 c
ATOM 2393 CG2 VAL A 396 10. .490 5. .628 15. .199 1. .00 3. .68 c
ATOM 2394 N TRP A 397 8. .725 4. .157 18. .225 1. .00 7. .98 N
ATOM 2395 CA TRP A 397 8. .534 2. .751 18. .552 1. .00 8. .13 C
ATOM 2396 C TRP A 397 7, .758 2, .176 17, .359 1, .00 9. .21 C
ATOM 2397 O TRP A 397 6. .548 2, .351 17. .308 1. .00 6. .97 O
ATOM 2398 CB TRP A 397 7, .771 2, .525 19. .848 1, .00 11. .38 C
ATOM 2399 CG TRP A 397 8, .576 2, .758 21, .096 1, .00 11. .04 C
ATOM 2400 CDl TRP A 397 9. .732 3, .467 21, .257 1. .00 12. .89 c
ATOM 2401 CD2 TRP A 397 8, .232 2, .286 22. .409 1, .00 11. .85 c
ATOM 2402 NE1 TRP A 397 10, .148 3. .453 22, .564 1. .00 10. .85 N
ATOM 2403 CE2 TRP A 397 9, .240 2, .719 23. .285 1. .00 11. .47 c
ATOM 2404 CE3 TRP A 397 7, .160 1, .532 22. .912 1. .00 10, .65 c
ATOM 2405 CZ2 TRP A 397 9. .205 2 .435 24, .650 1. .00 11. .88 c
ATOM 2406 CZ3 TRP A 397 7, .138 1, .234 24. .268 1. .00 12. .02 c
ATOM 2407 CH2 TRP A 397 8, .150 1, .690 25. .104 1, .00 10. .05 c
ATOM 2408 N VAL A 398 8 .495 1 .530 16, .442 1. .00 7, .88 N
ATOM 2409 CA VAL A 398 7, .776 1, .037 15. .254 1, .00 5, .08 C
ATOM 2410 C VAL A 398 7, .208 -0 .352 15, .494 1. .00 7, .54 C
ATOM 2411 O VAL A 398 6 .004 -0 .563 15, .334 1 .00 7. .53 0
ATOM 2412 CB VAL A 398 8. .663 1 .122 14, .004 1. .00 6, .33 C
ATOM 2413 CGI VAL A 398 7 .796 0 .803 12, .781 1. .00 7, .56 C
ATOM 2414 CG2 VAL A 398 9 .301 2 .503 13 .889 1 .00 6 .40 C
ATOM 2415 N LYS A 399 8 .053 -1 .312 15, .862 1. .00 6. .71 N
ATOM 2416 CA LYS A 399 7 .582 -2 .655 16. .241 1 .00 9 .29 C
ATOM 2417 C LYS A 399 7 .132 -2 .548 17 .698 1 .00 6 .47 C
ATOM 2418 O LYS A 399 7 .938 -2 .143 18, .536 1 .00 9. .48 0
ATOM 2419 CB LYS A 399 8 .778 -3 .614 16 .122 1 .00 8 .35 C
ATOM 2420 CG LYS A 399 8 .585 -4 .990 16 .741 1 .00 11 .13 C
ATOM 2421 CD LYS A 399 7 .431 -5 .741 16, .061 1 .00 12. .42 C
ATOM 2422 CE LYS A 399 7 .109 -7 .014 16 .824 1 .00 10 .44 C
ATOM 2423 NZ LYS A 399 6 .193 -7 .900 16 .051 1 .00 14 .39 N
ATOM 2424 N PRO A 400 5 .876 -2 .823 18 .016 1 .00 7 .37 N
ATOM 2425 CA PRO A 400 5 .364 -2 .695 19 .371 1 .00 8 .03 C
ATOM 2426 C PRO A 400 5 .914 -3 .786 20 .282 1 .00 9 .27 C
ATOM 2427 O PRO A 400 5 .556 -4 .936 20 .058 1 .00 7 .71 O
ATOM 2428 CB PRO A 400 3 .845 -2 .797 19 .194 1 .00 9 .60 C ATOM 2429 CG PRO A 400 3.626 -2.535 17.731 1.00 9.49 C
ATOM 2430 CD PRO A 400 4. 815 -3. 254 17. 071 1. 00 7. 21 c
ATOM 2431 N GLY A 401 6. 840 -3. 470 21. 163 1. 00 9. 35 N
ATOM 2432 CA GLY A 401 7. 481 -4. 482 22. 015 1. 00 10. 39 C
ATOM 2433 C GLY A 401 6. 416 -5. 254 22. 797 1. 00 10. 56 C
ATOM 2434 0 GLY A 401 5. 572 -4. 651 23. 440 1. 00 10. 17 0
ATOM 2435 N GLY A 402 6. 502 -6. 578 22. 746 1. 00 12. 76 N
ATOM 2436 CA GLY A 402 5. 533 -7. 434 23. 424 1. 00 11. 36 C
ATOM 2437 C GLY A 402 4. 747 -8. 227 22. .379 1. 00 14. 25 C
ATOM 2438 0 GLY A 402 4. 255 -9. 313 22. .683 1. 00 14. ,26 0
ATOM 2439 N GLU A 403 4. 627 -7. 697 21. 160 1. 00 13. 06 N
ATOM 2440 CA GLU A 403 3. 989 -8. 425 20. 060 1. 00 12. 73 C
ATOM 2441 C GLU A 403 5. 086 -9. 268 19. 399 1. 00 12. 75 C
ATOM 2442 0 GLU A 403 6. 158 -8. 763 19. 089 1. 00 11. 76 0
ATOM 2443 CB GLU A 403 3. 323 -7. 492 19. 035 1. 00 11. .21 c
ATOM 2444 CG GLU A 403 2. .201 -6. .714 19. ,718 1. .00 14. .19 c
ATOM 2445 CD GLU A 403 1. .454 -5. .720 18. .847 1. .00 15. .93 c
ATOM 2446 OE1 GLU A 403 1. .824 -5. ,584 17. ,674 1. .00 12. .13 o
ATOM 2447 OE2 GLU A 403 0. ,493 -5. ,084 19. ,329 1. .00 14. .54 0
ATOM 2448 N CYS A 404 4. ,817 -10. ,548 19. .226 1. ,00 11. ,86 N
ATOM 2449 CA CYS A 404 5. .763 -11. ,506 18. .724 1. ,00 13. ,61 C
ATOM 2450 C CYS A 404 6. .329 -11. ,302 17. .327 1. .00 13. ,64 C
ATOM 2451 0 CYS A 404 5. .632 -10. ,838 16. ,440 1. .00 12. .45 O
ATOM 2452 CB CYS A 404 5. ,069 -12. ,891 18. ,731 1. ,00 10. ,78 C
ATOM 2453 SG CYS A 404 6. ,348 -14. ,186 18. .843 1. ,00 10. .02 S
ATOM 2454 N ASP A 405 7. ,568 -11. ,748 17. ,139 1. ,00 12. ,58 N
ATOM 2455 CA ASP A 405 8. .211 -11. ,697 15. .830 1. ,00 11. ,30 C
ATOM 2456 C ASP A 405 7. .958 -12. ,975 15. .041 1. ,00 12. ,96 C
ATOM 2457 0 ASP A 405 8. .143 -12. ,984 13. .822 1. .00 11. .87 O
ATOM 2458 CB ASP A 405 9. .722 -11. .515 16. .026 1. .00 12. .67 c
ATOM 2459 CG ASP A 405 10. .085 -10. .167 16. .588 1. .00 14. .88 c
ATOM 2460 ODl ASP A 405 9. .501 -9. ,124 16. .182 1. .00 13. .52 o
ATOM 2461 OD2 ASP A 405 10. .960 -10. .152 17. .483 1. .00 12. .49 0
ATOM 2462 N GLY A 406 7. .571 -14. .072 15. .703 1. .00 11. .55 N
ATOM 2463 CA GLY A 406 7. .388 -15. .337 15. .012 1. .00 10. .92 C
ATOM 2464 C GLY A 406 7. .336 -16. .513 15. .991 1. .00 11. .09 C
ATOM 2465 O GLY A 406 7. .907 -16. .438 17. .082 1. .00 10. .50 O
ATOM 2466 N THR A 407 6. .621 -17. .564 15. .592 1. .00 12. .63 N
ATOM 2467 CA THR A 407 6. .463 -18. .725 16. .472 1. .00 13. .63 C
ATOM 2468 C THR A 407 7. .768 -19. .496 16. .592 1. .00 13. .58 C
ATOM 2469 0 THR A 407 8, .543 -19. .531 15. .636 1, .00 14, .00 O
ATOM 2470 CB THR A 407 5. .363 -19, .678 15, .962 1, .00 14, .88 C
ATOM 2471 OGl THR A 407 5. .269 -20, .817 16, .832 1, .00 15, .36 O
ATOM 2472 CG2 THR A 407 5 .642 -20. .164 14. .551 1. .00 12, .17 c
ATOM 2473 N SER A 408 7 .998 -20. .112 17 .758 1. .00 13. .91 N
ATOM 2474 CA SER A 408 9 .200 -20 .921 17 .934 1 .00 13 .96 C
ATOM 2475 C SER A 408 8 .883 -22 .394 17 .664 1 .00 18 .94 C
ATOM 2476 O SER A 408 9 .746 -23. .266 17, .777 1. .00 18, .78 O
ATOM 2477 CB SER A 408 9 .773 -20. .761 19, .340 1. .00 17, .90 C
ATOM 2478 OG SER A 408 8 .765 -21 .027 20, .306 1, .00 21. .37 0
ATOM 2479 N ASP A 409 7 .614 -22 .691 17 .383 1 .00 18. .86 N
ATOM 2480 CA ASP A 409 7 .227 -24 .074 17 .088 1 .00 20 .41 C
ATOM 2481 C ASP A 409 7 .796 -24 .460 15 .732 1 .00 21 .46 C
ATOM 2482 0 ASP A 409 7 .283 -24 .085 14 .674 1 .00 21 .42 0
ATOM 2483 CB ASP A 409 5 .719 -24 .246 17 .124 1 .00 19 .32 C
ATOM 2484 CG ASP A 409 5 .209 -25 .619 16 .735 1 .00 19 .94 C
ATOM 2485 ODl ASP A 409 5 .950 -26 .476 16 .230 1 .00 18 .83 O
ATOM 2486 OD2 ASP A 409 3 .992 -25 .837 16 .926 1 .00 22 .26 0
ATOM 2487 N THR A 410 8 .814 -25 .319 15 .731 1 .00 20 .78 N
ATOM 2488 CA THR A 410 9 .483 -25 .741 14 .511 1 .00 20 .71 C
ATOM 2489 C THR A 410 8 .594 -26 .480 13 .529 1 .00 20 .75 C
ATOM 2490 O THR A 410 8 .950 -26 .616 12 .341 1 .00 21 .83 O
ATOM 2491 CB THR A 410 10 .740 -26 .587 14 .805 1 .00 22 .31 C
ATOM 2492 OGl THR A 410 10 .353 -27 .871 15 .314 1 .00 21 .56 0
ATOM 2493 CG2 THR A 410 11 .635 -25 .916 15 .836 1 .00 19 .75 C
ATOM 2494 N THR A 411 7 .457 -26 .997 13 .952 1 .00 21 .25 N
ATOM 2495 CA THR A 411 6 .543 -27 .698 13 .067 1 .00 21 .65 C
ATOM 2496 C THR A 411 5 .487 -26 .771 12 .469 1 .00 20 .71 C
ATOM 2497 0 THR A 411 4 .799 -27 .221 11 .556 1 .00 20 .88 o
ATOM 2498 CB THR A 411 5 .826 -28 .862 13 .785 1 .00 24 .84 c
ATOM 2499 OGl THR A 411 4 .821 -28 .357 14 .673 1 .00 24 .15 0
ATOM 2500 CG2 THR A 411 6 .840 -29 .693 14 .565 1 .00 24 .12 c ATOM 2501 N ALA A 412 5.368 -25.533 12..934 1.00 18.34 N
ATOM 2502 CA ALA A 412 4. 351 -24. 629 12. ,395 1. 00 17. 63 C
ATOM 2503 C ALA A 412 4. 635 -24. 172 10. ,973 1. 00 18. 97 C
ATOM 2504 0 ALA A 412 5. 764 -23. 901 10. ,561 1. 00 15. 98 O
ATOM 2505 CB ALA A 412 4. 192 -23. 407 13. .292 1. 00 18. 31 C
ATOM 2506 N ALA A 413 3. 575 -24. 031 10. ,184 1. .00 17. 60 N
ATOM 2507 CA ALA A 413 3. 653 -23. 587 8. ,805 1. 00 21. .03 C
ATOM 2508 C ALA A 413 4. 491 -22. 321 8. ,632 1. 00 21. 07 C
ATOM 2509 O ALA A 413 5. 343 -22. 276 7. .737 1. .00 22. 24 0
ATOM 2510 CB ALA A 413 2. 245 -23. 281 8. ,288 1. .00 18. .70 C
ATOM 2511 N ARG A 414 4. 275 -21. .317 9. ,477 1. ,00 18. .99 N
ATOM 2512 CA ARG A 414 5. .015 -20. .061 9. .328 1. ,00 19. ,30 C
ATOM 2513 C ARG A 414 6. ,351 -19. .995 10. .047 1. .00 19. ,29 C
ATOM 2514 O ARG A 414 6. 942 -18. ,912 10. .163 1. ,00 15. ,93 0
ATOM 2515 CB ARG A 414 4. .102 -18. ,916 9. .809 1. ,00 22. ,81 C
ATOM 2516 CG AARG A 414 2. ,677 -19. ,063 9. .278 0. .50 20. ,76 C
ATOM 2517 CG ; BARG A 414 2. 786 -18. 787 9. ,061 0. .50 24. 56 C
ATOM 2518 CD AARG A 414 1. 943 -17. 737 9. .281 0. 50 22. 28 C
ATOM 2519 CD ! BARG A 414 1. 923 -17. 686 9. .673 0. 50 26. .51 C
ATOM 2520 NE AARG A 414 1. 743 -17. 207 10. ,620 0. 50 18. .79 N
ATOM 2521 NE : BARG A 414 0. 679 -17. 499 8. ,942 0. 50 27. .44 N
ATOM 2522 CZ AARG A 414 1. ,418 -15. 944 10. ,873 0. 50 20. .76 C
ATOM 2523 cz : BARG A 414 0. .472 -16. .727 7. ,885 0. .50 30. ,07 C
ATOM 2524 NHlAARG A 414 1. .277 -15. .085 9. .866 0. ,50 21. .84 N
ATOM 2525 NHlBARG A 414 1. .434 -15. .980 7. .357 0. .50 30. ,38 N
ATOM 2526 NH2AARG A 414 1. ,246 -15. ,526 12. ,118 0. ,50 17. ,69 N
ATOM 2527 NH2BARG A 414 -0. .737 -16. ,674 7. .336 0. ,50 30. ,89 N
ATOM 2528 N TYR A 415 6. ,851 -21. ,123 10. .551 1. ,00 16. .76 N
ATOM 2529 CA TYR A 415 8. ,092 -21. ,127 11. .305 1. ,00 16. ,15 C
ATOM 2530 C TYR A 415 9. ,283 -20. .586 10. .525 1. ,00 15. ,10 C
ATOM 2531 O TYR A 415 9. .565 -21. .006 9. .408 1. .00 14. ,92 0
ATOM 2532 CB TYR A 415 8. .404 -22. .559 11. .775 1. ,00 14. .85 c
ATOM 2533 CG TYR A 415 9. .711 -22. .671 12. .527 1. ,00 14. .79 c
ATOM 2534 CDl TYR A 415 9. .840 -22. .118 13. .791 1. ,00 14. .80 c
ATOM 2535 CD2 TYR A 415 10. .807 -23. .310 11. .974 1. .00 16. .26 c
ATOM 2536 CE1 TYR A 415 11. .029 -22. .213 14. .501 1. .00 17. .75 c
ATOM 2537 CE2 TYR A 415 12. .001 -23. .410 12. .666 1. .00 16. .07 c
ATOM 2538 CZ TYR A 415 12. .102 -22. .857 13. .929 1. .00 15. .93 c
ATOM 2539 OH TYR A 415 13. .272 -22. .955 14. .629 1. .00 15. .69 0
ATOM 2540 N ASP A 416 10. .028 -19. .692 11. .161 1. .00 14. .36 N
ATOM 2541 CA ASP A 416 11. .270 -19. .162 10. .595 1. .00 15. .54 c
ATOM 2542 C ASP A 416 12. .364 -19. .687 11, .520 1. .00 15. .69 c
ATOM 2543 O ASP A 416 12. .244 -19. .414 12, .727 1. .00 15. .39 0
ATOM 2544 CB ASP A 416 11. .263 -17. .629 10, .596 1. .00 13. .93 c
ATOM 2545 CG ASP A 416 12, .503 -17. .056 9. .930 1. .00 17. .71 c
ATOM 2546 ODl ASP A 416 13, .645 -17, .413 10. .296 1, .00 14. .36 0
ATOM 2547 OD2 ASP A 416 12, .319 -16, .230 9. .005 1, .00 16. .35 0
ATOM 2548 N TYR A 417 13, .418 -20, .349 11 .056 1, .00 14. .52 N
ATOM 2549 CA TYR A 417 14, .439 -20. .884 11 .946 1, .00 15. .93 C
ATOM 2550 C TYR A 417 15. .086 -19. .865 12 .865 1, .00 14. .32 C
ATOM 2551 O TYR A 417 15, .628 -20. .217 13 .939 1, .00 14, .33 0
ATOM 2552 CB TYR A 417 15 .540 -21. .642 11 .168 1, .00 16, .81 c
ATOM 2553 CG TYR A 417 16 .541 -20, .724 10 .494 1. .00 20, .04 c
ATOM 2554 CDl TYR A 417 17 .627 -20 .235 11 .208 1 .00 20, .88 c
ATOM 2555 CD2 TYR A 417 16 .400 -20 .328 9 .171 1, .00 21. .55 c
ATOM 2556 CE1 TYR A 417 18 .541 -19 .371 10 .638 1 .00 20. .95 c
ATOM 2557 CE2 TYR A 417 17 .325 -19 .485 8 .582 1 .00 22. .81 c
ATOM 2558 CZ TYR A 417 18 .395 -19 .023 9 .314 1 .00 21. .34 c
ATOM 2559 OH TYR A 417 19 .311 -18 .175 8 .744 1 .00 23 .68 0
ATOM 2560 N HIS A 418 15 .130 -18 .583 12 .513 1 .00 10 .49 N
ATOM 2561 CA HIS A 418 15 .625 -17 .553 13 .424 1 .00 10 .60 c
ATOM 2562 C HIS A 418 14 .864 -17 .517 14 .745 1 .00 11 .16 c
ATOM 2563 O HIS A 418 15 .403 -17 .133 15 .785 1 .00 11 .75 0
ATOM 2564 CB HIS A 418 15 .527 -16 .146 12 .805 1 .00 12 .33 c
ATOM 2565 CG HIS A 418 16 .405 -15 .928 11 .618 1 .00 13 .49 c
ATOM 2566 ND1 HIS A 418 15 .984 -16 .202 10 .344 1 .00 14 .03 N
ATOM 2567 CD2 HIS A 418 17 .678 -15 .457 11 .512 1 .00 17. .01 C
ATOM 2568 CE1 HIS A 418 16 .951 -15 .914 9 .484 1 .00 17 .13 C
ATOM 2569 NE2 HIS A 418 17 .973 -15 .463 10 .166 1 .00 17 .38 N
ATOM 2570 N CYS A 419 13 .593 -17 .920 14 .773 1. .00 11 .97 N
ATOM 2571 CA CYS A 419 12 .797 -17 .924 15 .985 1 .00 11 .38 C
ATOM 2572 C CYS A 419 13 .059 -19 .153 16 .851 1 .00 13 .76 C ATOM 2573 0 CYS A 419 12..586 -19.,168 17..988 1.,00 15.,28 o
ATOM 2574 CB CYS A 419 11. ,311 -17. ,770 15. .624 1. .00 14. .89 c
ATOM 2575 SG CYS A 419 11. ,078 -16. ,183 14. .736 1. .00 9. .92 s
ATOM 2576 N GLY A 420 13. .820 -20. ,128 16. ,385 1. ,00 14. .63 N
ATOM 2577 CA GLY A 420 14. .216 -21. ,270 17. .192 1. ,00 17. .14 C
ATOM 2578 C GLY A 420 15. ,661 -21. .199 17. .670 1. .00 17. .33 C
ATOM 2579 0 GLY A 420 16. ,100 -22. .119 18. .379 1. .00 18. .09 0
ATOM 2580 N LEU A 421 16. .413 -20. ,130 17. .439 1. .00 16. .44 N
ATOM 2581 CA LEU A 421 17. ,797 -20. ,054 17. .897 1. ,00 17. .26 C
ATOM 2582 C LEU A 421 17. ,883 -19. .936 19. .418 1. .00 17. .93 C
ATOM 2583 0 LEU A 421 16. .933 -19. .554 20. .111 1. .00 15. .23 0
ATOM 2584 CB LEU A 421 18. .490 -18. .850 17. .252 1. .00 19. .03 c
ATOM 2585 CG LEU A 421 18. ,537 -18. .852 15. .714 1. ,00 18. .09 c
ATOM 2586 CDl LEU A 421 19. ,043 -17. .505 15. .216 1. .00 15. .42 c
ATOM 2587 CD2 LEU A 421 19. .391 -20. .003 15. .222 1. .00 16. .17 c
ATOM 2588 N GLU A 422 19. .077 -20. .155 19. .955 1. .00 19. .82 N
ATOM 2589 CA GLU A 422 19. .362 -20. .089 21. .379 1. .00 21. .55 C
ATOM 2590 C GLU A 422 19. .103 -18. .731 22. .009 1. .00 18. .27 C
ATOM 2591 O GLU A 422 18. .814 -18. .633 23. .210 1. .00 18. .28 0
ATOM 2592 CB GLU A 422 20. .816 -20. .501 21. .680 1. .00 28. .44 C
ATOM 2593 CG GLU A 422 21. .858 -19. .465 21. .298 1. .00 34. .64 C
ATOM 2594 CD GLU A 422 23. .283 -19. .756 21. .724 1. .00 40. .13 c
ATOM 2595 OE1 GLU A 422 23. .508 -20. .174 22. .884 1. .00 40. .63 0
ATOM 2596 OE2 GLU A 422 24. .200 -19. .557 20. .890 1. .00 39. .34 o
ATOM 2597 N ASP A 423 19. .199 -17. .648 21. .248 1. .00 15. .87 N
ATOM 2598 CA ASP A 423 18. .961 -16. .326 21. .824 1. ,00 15. .75 C
ATOM 2599 C ASP A 423 17. .572 -15. .788 21. .516 1. ,00 14. .49 C
ATOM 2600 O ASP A 423 17. .354 -14. .575 21. .628 1. ,00 13. .81 O
ATOM 2601 CB ASP A 423 20. .051 -15. .348 21. ,374 1. .00 14. .73 C
ATOM 2602 CG ASP A 423 20. .189 -15. .332 19. .865 1. .00 17. .03 C
ATOM 2603 ODl ASP A 423 19. .298 -15. .870 19. .164 1. ,00 18. .38 0
ATOM 2604 OD2 ASP A 423 21. .185 -14. .765 19. .375 1. .00 18. .33 0
ATOM 2605 N ALA A 424 16. .653 -16. .628 21. .073 1. .00 15. .63 N
ATOM 2606 CA ALA A 424 15. .267 -16. .220 20. .826 1. .00 15. .39 C
ATOM 2607 C ALA A 424 14. .431 -16. .759 21. .990 1. ,00 16. .55 C
ATOM 2608 O ALA A 424 14. .564 -17. .940 22. .324 1. .00 15. .95 O
ATOM 2609 CB ALA A 424 14. .740 -16. .793 19. .521 1. .00 14. .10 C
ATOM 2610 N LEU A 425 13. .624 -15. .918 22. .605 1. .00 14. .20 N
ATOM 2611 CA LEU A 425 12. .811 -16. .351 23. .734 1. .00 17, .25 C
ATOM 2612 C LEU A 425 11. .750 -17. .347 23. .322 1. .00 16. .76 C
ATOM 2613 O LEU A 425 11. .023 -17. .180 22. .338 1. .00 14. .13 O
ATOM 2614 CB LEU A 425 12. .173 -15. .139 24. .432 1. .00 14. .23 C
ATOM 2615 CG LEU A 425 11. .530 -15. .462 25. .794 1. .00 16. .28 C
ATOM 2616 CDl LEU A 425 12. .589 -15, .822 26, .830 1. .00 13, .47 C
ATOM 2617 CD2 LEU A 425 10. .699 -14. .276 26. .275 1. .00 11, .04 C
ATOM 2618 N LYS A 426 11. .687 -18. .484 24. .030 1. .00 19, .88 N
ATOM 2619 CA LYS A 426 10, .716 -19. .525 23. .688 1. .00 21, .65 C
ATOM 2620 C LYS A 426 10, .037 -20. .042 24, .957 1, .00 24, .87 C
ATOM 2621 O LYS A 426 10. .554 -19. .857 26. .061 1. .00 25, .02 0
ATOM 2622 CB LYS A 426 11. .353 -20. .704 22. .973 1, .00 22, .22 C
ATOM 2623 CG LYS A 426 12, .301 -20, .470 21. .820 1, .00 25 .86 C
ATOM 2624 CD LYS A 426 13, .131 -21. .720 21, .534 1, .00 24. .57 C
ATOM 2625 CE LYS A 426 14 .537 -21. .372 21 .131 1. .00 22 .74 C
ATOM 2626 NZ LYS A 426 15, .360 -20, .784 22, .223 1. .00 19. .12 N
ATOM 2627 N PRO A 427 8, .875 -20, .650 24, .779 1, .00 24, .38 N
ATOM 2628 CA PRO A 427 8 .231 -20. .812 23, .484 1, .00 23 .90 C
ATOM 2629 C PRO A 427 7 .534 -19. .528 23. .070 1. .00 20 .95 C
ATOM 2630 O PRO A 427 7, .078 -18, .785 23, .937 1. .00 21, .24 0
ATOM 2631 CB PRO A 427 7. .200 -21. .915 23, .737 1. .00 25. .67 C
ATOM 2632 CG PRO A 427 6 .778 -21, .658 25. .151 1, .00 26 .78 C
ATOM 2633 CD PRO A 427 8. .050 -21 .245 25. .866 1, .00 27 .38 C
ATOM 2634 N ALA A 428 7 .433 -19 .256 21 .776 1. .00 17 .93 N
ATOM 2635 CA ALA A 428 6, .834 -18, .004 21, .307 1, .00 17, .59 C
ATOM 2636 C ALA A 428 5 .612 -18. .293 20, .440 1, .00 16 .73 C
ATOM 2637 O ALA A 428 5 .598 -19 .276 19. .698 1. .00 14 .70 0
ATOM 2638 CB ALA A 428 7 .896 -17 .272 20 .477 1, .00 14 .41 C
ATOM 2639 N PRO A 429 4 .581 -17. .459 20, .552 1, .00 16. .24 N
ATOM 2640 CA PRO A 429 3 .359 -17 .630 19, .782 1, .00 15 .56 C
ATOM 2641 C PRO A 429 3 .503 -17 .189 18 .339 1. .00 17 .33 C
ATOM 2642 O PRO A 429 4 .597 -16 .771 17 .953 1 .00 18 .47 O
ATOM 2643 CB PRO A 429 2 .370 -16 .766 20 .545 1 .00 15 .22 C
ATOM 2644 CG PRO A 429 3 .202 -15 .655 21, .093 1, .00 16 .97 C ATOM 2645 CD PRO A 429 4 . 541 - 16 . 273 21 . 445 1 . 00 14 . 34 c
ATOM 2646 N GLU A 430 2. 424 -17. 134 17. 555 1. .00 17. 54 N
ATOM 2647 CA GLU A 430 2. 515 -16. 678 16. 174 1. 00 18. 00 C
ATOM 2648 C GLU A 430 2. 930 -15. 213 16. 053 1. 00 17. 87 C
ATOM 2649 O GLU A 430 2. 727 -14. 430 16. 984 1. 00 16. 31 O
ATOM 2650 CB GLU A 430 1. 178 -16. 888 15. 458 1. .00 19. 98 c
ATOM 2651 CG GLU A 430 0. 909 -18. .344 15. .123 1. ,00 23. 53 c
ATOM 2652 CD GLU A 430 1. 798 -18. 890 14. 029 1. 00 25. 88 c
ATOM 2653 OE1 GLU A 430 2. 298 -18. 118 13. 177 1. 00 24. 55 o
ATOM 2654 OE2 GLU A 430 1. 988 -20. 125 14. 001 1. ,00 23. 45 o
ATOM 2655 N ALA A 431 3. 558 -14. .862 14. .928 1. ,00 14. 19 N
ATOM 2656 CA ALA A 431 3. 987 -13. 479 14. 726 1. 00 14. 89 C
ATOM 2657 C ALA A 431 2. 811 -12. 525 14. 944 1. .00 14. 00 C
ATOM 2658 O ALA A 431 1. ,729 -12. .886 14. .482 1. .00 12. 71 0
ATOM 2659 CB ALA A 431 4. ,454 -13. .236 13. ,297 1. ,00 13. .64 C
ATOM 2660 N GLY A 432 3. ,016 -11. .376 15. ,558 1. .00 13. .17 N
ATOM 2661 CA GLY A 432 1. .951 -10. 409 15. 763 1. .00 13. 80 C
ATOM 2662 C GLY A 432 1. .089 -10. 628 16. .996 1. ,00 17. 04 C
ATOM 2663 O GLY A 432 0. .360 -9. .710 17. ,409 1. ,00 16. .26 0
ATOM 2664 N GLN A 433 1. .144 -11. ,803 17. ,615 1. .00 14. ,84 N
ATOM 2665 CA GLN A 433 0. .380 -12. ,142 18. .801 1. .00 16. .45 C
ATOM 2666 C GLN A 433 1. .096 -11. ,700 20. ,060 1. .00 14. 64 C
ATOM 2667 O GLN A 433 2. .313 -11. ,528 20. ,066 1. .00 15. .80 O
ATOM 2668 CB GLN A 433 0. .121 -13. ,666 18. ,842 1. .00 16. .97 C
ATOM 2669 CG GLN A 433 0. .722 -14. ,148 17. .672 1. .00 21. .15 C
ATOM 2670 CD GLN A 433 2. .152 -13. .657 17. .859 1. .00 26. .58 C
ATOM 2671 OE1 GLN A 433 2. ,785 -13. ,900 18. ,885 1. .00 30. .03 O
ATOM 2672 NE2 GLN A 433 2. ,665 -12. ,937 16. ,878 1. .00 27. ,04 N
ATOM 2673 N TRP A 434 0. .300 -11. ,412 21. .091 1. .00 13. .63 N
ATOM 2674 CA TRP A 434 0. .914 -10. .957 22. .328 1. .00 13. .82 C
ATOM 2675 C TRP A 434 1. ,836 -12. ,050 22. .868 1. .00 14. ,46 C
ATOM 2676 O TRP A 434 1. .502 -13. .228 22. .850 1. .00 10. ,69 O
ATOM 2677 CB TRP A 434 •0. .154 -10. .593 23. .346 1. .00 15. .85 C
ATOM 2678 CG TRP A 434 0. .428 -9. .807 24. .484 1. .00 15. .45 C
ATOM 2679 CDl TRP A 434 0. .526 -10. .224 25. .782 1. .00 16. ,09 c
ATOM 2680 CD2 TRP A 434 0. .986 -8. .495 24. .434 1. .00 15. ,80 c
ATOM 2681 NE1 TRP A 434 1. .096 -9. .237 26. .546 1. .00 15. .71 N
ATOM 2682 CE2 TRP A 434 1. .406 -8. .170 25. .737 1. .00 15. .27 C
ATOM 2683 CE3 TRP A 434 1. .165 -7. .546 23. .413 1. .00 13. .90 C
ATOM 2684 CZ2 TRP A 434 1. .954 -6. .928 26. .064 1. .00 13. .43 C
ATOM 2685 CZ3 TRP A 434 1. .730 -6. .334 23. .736 1. .00 12. .47 C
ATOM 2686 CH2 TRP A 434 2. .113 -6. .025 25. .050 1. .00 10. .96 C
ATOM 2687 N PHE A 435 3. .007 -11. .614 23. .306 1, .00 15. .80 N
ATOM 2688 CA PHE A 435 4. .010 -12. .527 23. .875 1. .00 17. .64 C
ATOM 2689 C PHE A 435 4. .340 -11. .975 25. .258 1, .00 15. .88 C
ATOM 2690 O PHE A 435 5, .267 -11. .206 25. .504 1, .00 16. .07 O
ATOM 2691 CB PHE A 435 5, .198 -12. .625 22, .948 1 .00 16. .11 C
ATOM 2692 CG PHE A 435 6. .263 -13, .636 23, .222 1 .00 17. .40 C
ATOM 2693 CDl PHE A 435 6, .222 -14, .491 24. .314 1, .00 17. .26 C
ATOM 2694 CD2 PHE A 435 7, .366 -13, .698 22, .372 1. .00 13. .51 C
ATOM 2695 CE1 PHE A 435 7, .232 -15, .406 24, .545 1 .00 16. .81 C
ATOM 2696 CE2 PHE A 435 8 .384 -14. .610 22. .607 1 .00 18. .11 C
ATOM 2697 CZ PHE A 435 8, .321 -15. .462 23. .693 1. .00 16. .99 C
ATOM 2698 N ASN A 436 3. .505 -12, .379 26. .236 1 .00 14. .43 N
ATOM 2699 CA ASN A 436 3 .603 -11. .789 27. .558 1. .00 15. .23 C
ATOM 2700 C ASN A 436 4 .959 -11 .953 28 .216 1 .00 13, .48 C
ATOM 2701 O ASN A 436 5 .474 -10 .996 28 .800 1 .00 15, .55 O
ATOM 2702 CB ASN A 436 2 .453 -12, .265 28. .469 1. .00 15, .43 C
ATOM 2703 CG ASN A 436 2 .294 -11 .217 29 .567 1 .00 21, .94 C
ATOM 2704 ODl ASN A 436 2 .047 -10 .048 29 .251 1 .00 19, .99 O
ATOM 2705 ND2 ASN A 436 2 .495 -11 .633 30 .819 1 .00 16 .63 N
ATOM 2706 N GLU A 437 5 .575 -13 .115 28 .065 1 .00 14. .81 N
ATOM 2707 CA GLU A 437 6 .906 -13 .383 28 .615 1 .00 16, .35 C
ATOM 2708 C GLU A 437 7 .913 -12 .371 28 .067 1 .00 15. .03 C
ATOM 2709 O GLU A 437 8 .773 -11 .859 28 .771 1 .00 12 .30 0
ATOM 2710 CB GLU A 437 7 .312 -14 .802 28 .223 1 .00 20 .49 C
ATOM 2711 CG GLU A 437 6 .478 -15 .940 28 .755 1 .00 27, .91 C
ATOM 2712 CD GLU A 437 5 .164 -16 .216 28 .064 1 .00 31 .40 C
ATOM 2713 OE1 GLU A 437 4 .791 -15 .602 27 .043 1 .00 27 .37 0
ATOM 2714 OE2 GLU A 437 4 .424 -17 .103 28 .559 1 .00 34 .05 0
ATOM 2715 N TYR A 438 7 .784 -12 .043 26 .782 1 .00 15 .08 N
ATOM 2716 CA TYR A 438 8 .656 -11 .055 26 .150 1 .00 14 .63 C ATOM 2717 C TYR A 438 8.387 -9.641 26.633 1..00 13..43 C
ATOM 2718 O TYR A 438 9. 282 -8. 804 26. 842 1. 00 12. 18 o
ATOM 2719 CB TYR A 438 8. 508 -11. 159 24. 615 1. 00 12. 75 c
ATOM 2720 CG TYR A 438 9. 747 -10. ,558 23. .964 1. ,00 13. .57 c
ATOM 2721 CDl TYR A 438 10. 865 -11. .352 23. .764 1. .00 13. 67 c
ATOM 2722 CD2 TYR A 438 9. 792 -9. .227 23. .574 1. ,00 12. ,63 c
ATOM 2723 CE1 TYR A 438 11. 992 -10. .814 23. .176 1. .00 11. .80 c
ATOM 2724 CE2 TYR A 438 10. 918 -8. ,682 22. .992 1. .00 9. .14 c
ATOM 2725 CZ TYR A 438 12. 029 -9. .495 22. ,807 1. .00 10. .92 c
ATOM 2726 OH TYR A 438 13. 167 -8. ,988 22. ,229 1. ,00 10. .89 0
ATOM 2727 N PHE A 439 7. 099 -9. ,312 26. ,821 1. ,00 12. ,19 N
ATOM 2728 CA PHE A 439 6. 710 -8. ,006 27. ,329 1. ,00 10. ,75 c
ATOM 2729 C PHE A 439 7. .365 -7. .791 28. ,685 1. ,00 12. .57 c
ATOM 2730 0 PHE A 439 7. ,995 -6. ,774 28. ,939 1. ,00 12. ,06 0
ATOM 2731 CB PHE A 439 5. ,174 -7. .920 27. ,453 1. ,00 11. ,52 c
ATOM 2732 CG PHE A 439 4. ,700 -6. .632 28. .050 1. .00 14. .98 c
ATOM 2733 CDl PHE A 439 4. 668 -5. .480 27. 283 1. .00 12. 52 c
ATOM 2734 CD2 PHE A 439 4. 299 -6. ,571 29. .382 1. 00 15. 07 c
ATOM 2735 CE1 PHE A 439 4. 238 -4. ,270 27. ,792 1. .00 10. 83 c
ATOM 2736 CE2 PHE A 439 3. 875 -5. ,360 29. .902 1. .00 15. .85 c
ATOM 2737 CZ PHE A 439 3. 837 -4. ,225 29. .120 1. .00 17. .96 c
ATOM 2738 N ILE A 440 7. ,270 -8. ,800 29. ,564 1. ,00 13. .60 N
ATOM 2739 CA ILE A 440 7. ,880 -8. ,684 30. ,899 1. ,00 15. ,56 c
ATOM 2740 C ILE A 440 9. ,379 -8. ,474 30. ,838 1. ,00 13. ,18 c
ATOM 2741 O ILE A 440 9. .933 -7. .613 31. ,536 1. ,00 12. ,86 o
ATOM 2742 CB ILE A 440 7. .449 -9. .889 31. .753 1. ,00 17. ,52 c
ATOM 2743 CGI ILE A 440 5. ,941 -9. .728 32. .037 1. ,00 20. ,09 c
ATOM 2744 CG2 ILE A 440 8. .219 -9. .975 33. .064 1. .00 21. .38 c
ATOM 2745 CDl ILE A 440 5. .229 -11. .002 32. .413 1. .00 26. .81 c
ATOM 2746 N GLN A 441 10. .054 -9. .168 29. .935 1. .00 15. .58 N
ATOM 2747 CA GLN A 441 11. .500 -9. .003 29. .745 1. .00 13. .59 C
ATOM 2748 C GLN A 441 11. .819 -7. .557 29. .395 1. .00 14. .18 c
ATOM 2749 0 GLN A 441 12. .640 -6. .877 30. .021 1. .00 12. .66 0
ATOM 2750 CB GLN A 441 11. .964 -9. .943 28. .630 1. ,00 14. .14 c
ATOM 2751 CG GLN A 441 13. .398 -9. .670 28. .184 1. .00 15. .65 c
ATOM 2752 CD GLN A 441 13. .776 -10. .439 26. .941 1. .00 14. .60 c
ATOM 2753 OE1 GLN A 441 13. .805 -11. .662 26. .927 1. .00 14. .87 0
ATOM 2754 NE2 GLN A 441 14. .084 -9. .731 25. .857 1. .00 16. .49 N
ATOM 2755 N LEU A 442 11. .139 -7. ,043 28. .368 1. .00 14. .07 N
ATOM 2756 CA LEU A 442 11. .309 -5. .656 27. .952 1. .00 13. .76 C
ATOM 2757 C LEU A 442 11. .091 -4. .676 29. .090 1. .00 12. .15 C
ATOM 2758 0 LEU A 442 11. .770 -3. .669 29. .233 1. .00 12. .54 0
ATOM 2759 CB LEU A 442 10. .287 -5. .340 26. .835 1. .00 12. .65 C
ATOM 2760 CG LEU A 442 10. .619 -5, .944 25. .466 1. .00 11. .47 C
ATOM 2761 CDl LEU A 442 9. .473 -5, .788 24. .482 1. .00 9. .63 C
ATOM 2762 CD2 LEU A 442 11. .882 -5, .315 24. .863 1, .00 13. .55 C
ATOM 2763 N LEU A 443 10, .044 -4. .896 29, .862 1, .00 14. .68 N
ATOM 2764 CA LEU A 443 9, .700 -4. .061 31, .011 1, .00 16. .59 C
ATOM 2765 C LEU A 443 10, .769 -4, .104 32, .090 1, .00 17, .12 C
ATOM 2766 0 LEU A 443 11, .197 -3. .063 32, .607 1. .00 15, .83 O
ATOM 2767 CB LEU A 443 8. .369 -4, .585 31. .559 1. .00 19. .47 C
ATOM 2768 CG LEU A 443 7. .559 -3, .671 32. .463 1, .00 25. .52 C
ATOM 2769 CDl LEU A 443 7, .216 -2, .382 31. .733 1, .00 24. .26 C
ATOM 2770 CD2 LEU A 443 6, .312 -4. .407 32, .951 1. .00 21, .92 c
ATOM 2771 N ARG A 444 11, .275 -5. .295 32, .414 1. .00 17, .80 N
ATOM 2772 CA ARG A 444 12. .342 -5 .386 33, .411 1. .00 20, .45 C
ATOM 2773 C ARG A 444 13, .620 -4 .717 32, .931 1. .00 20, .40 C
ATOM 2774 0 ARG A 444 1 .287 -4 .023 33. .701 1 .00 20. .97 O
ATOM 2775 CB ARG A 444 12 .601 -6 .854 33 .790 1. .00 25, .22 C
ATOM 2776 CG ARG A 444 11 .356 -7 .405 34 .478 1 .00 32 .03 C
ATOM 2777 CD ARG A 444 11 .655 -8 .431 35 .541 1 .00 37 .10 C
ATOM 2778 NE ARG A 444 11 .534 -9 .784 35 .020 1 .00 41 .19 N
ATOM 2779 CZ ARG A 444 10 .917 -10 .767 35 .666 1 .00 44 .17 C
ATOM 2780 NHl ARG A 444 10 .357 -10 .560 36 .852 1 .00 44 .37 N
ATOM 2781 NH2 ARG A 444 10 .861 -11 .969 35 .100 1 .00 45 .89 N
ATOM 2782 N ASN A 445 13 .941 -4 .846 31 .641 1 .00 16 .93 N
ATOM 2783 CA ASN A 445 15 .161 -4 .244 31 .113 1 .00 16. .96 C
ATOM 2784 C ASN A 445 14 .980 -2 .840 30. .568 1 .00 15. .44 C
ATOM 2785 0 ASN A 445 15 .878 -2 .345 29 .884 1 .00 13. .79 O
ATOM 2786 CB ASN A 445 15 .707 -5 .162 30 .014 1 .00 18 .47 C
ATOM 2787 CG ASN A 445 16 .137 -6 .538 30 .488 1 .00 18 .89 C
ATOM 2788 ODl ASN A 445 16 .055 -7 .537 29 .770 1 .00 17 .39 O ATOM 2789 ND2 ASN A 445 16.647 -6.588 31..708 1..00 18.02 N
ATOM 2790 N ALA A 446 13. 878 -2. 159 30. 845 1. 00 15. .51 N
ATOM 2791 CA ALA A 446 13. 648 -0. 829 30. 296 1. .00 15. 51 C
ATOM 2792 C ALA A 446 14. 752 0. 154 30. 621 1. .00 17. 57 C
ATOM 2793 0 ALA A 446 15. 188 0. 268 31. ,771 1. ,00 16. ,35 0
ATOM 2794 CB ALA A 446 12. .303 -0. 293 30. .787 1. .00 14. .81 C
ATOM 2795 N ASN A 447 15. 126 0. 981 29. 647 1. .00 16. 64 N
ATOM 2796 CA ASN A 447 16. .098 2. 052 29. ,902 1. .00 16. .00 C
ATOM 2797 C ASN A 447 15. 844 3. 208 28. .950 1. .00 17. 83 C
ATOM 2798 O ASN A 447 16. .012 3. 038 27. ,732 1. .00 18. .83 0
ATOM 2799 CB ASN A 447 17. .522 1. 518 29. ,728 1. .00 17. .65 C
ATOM 2800 CG ASN A 447 18. .566 2. 597 29. .929 1. .00 23. 38 C
ATOM 2801 ODl ASN A 447 18. ,419 3. 452 30. .797 1. .00 22. 77 O
ATOM 2802 ND2 ASN A 447 19. ,650 2. 601 29. ,162 1. .00 24. .43 N
ATOM 2803 N PRO A 448 15. ,540 4. 380 29. .478 1. .00 18. ,20 N
ATOM 2804 CA PRO A 448 15. .366 4. 620 30. .890 1. ,00 17. .16 C
ATOM 2805 C PRO A 448 14. .176 3. ,878 31. .473 1. .00 18. .21 C
ATOM 2806 O PRO A 448 13. .243 3. ,420 30. .799 1. .00 16. .91 O
ATOM 2807 CB PRO A 448 15. .154 6. ,119 31. .013 1. .00 19. ,04 C
ATOM 2808 CG PRO A 448 14. .668 6. ,558 29. .674 1. .00 20. .73 C
ATOM 2809 CD PRO A 448 15. .292 5. ,619 28. .686 1. .00 20. .31 C
ATOM 2810 N PRO A 449 14. .220 3. ,677 32. .782 1. .00 18. .86 N
ATOM 2811 CA PRO A 449 13. .201 2. .918 33. .477 1. .00 19. ,10 C
ATOM 2812 C PRO A 449 11. .848 3. ,614 33. .430 1. .00 20. .78 C
ATOM 2813 O PRO A 449 11. .788 4. .827 33. .243 1. .00 20. .62 0
ATOM 2814 CB PRO A 449 13. .712 2. .856 34. .914 1. .00 20. .85 C
ATOM 2815 CG PRO A 449 15. .155 3. .208 34. .851 1. .00 21. .46 C
ATOM 2816 CD PRO A 449 15. .289 4. .170 33. .697 1. .00 19. .58 C
ATOM 2817 N PHE A 450 10. .782 2. .854 33. .601 1. .00 21. .46 N
ATOM 2818 CA PHE A 450 9. .438 3. .389 33. .709 1. .00 28. .61 C
ATOM 2819 C PHE A 450 9. .072 3. .431 35. .204 1. .00 33. .92 C
ATOM 2820 O PHE A 450 8. .942 4. .534 35. .775 1. .00 36. .20 0
ATOM 2821 CB PHE A 450 8. .401 2. .527 32. .994 1. .00 27. .81 C
ATOM 2822 CG PHE A 450 8. .420 2. .651 31. .498 1. .00 25. .37 C
ATOM 2823 CDl PHE A 450 7. .693 3. .645 30. .865 1. .00 24. .79 C
ATOM 2824 CD2 PHE A 450 9. .145 1. .756 30. .730 1. .00 26. .22 C
ATOM 2825 CE1 PHE A 450 7. .696 3. .765 29. .488 1. .00 24. .38 C
ATOM 2826 CE2 PHE A 450 9. .152 1. .871 29. .352 1. .00 26. .70 C
ATOM 2827 CZ PHE A 450 8. .427 2. .870 28. .731 1. .00 26. .67 c
ATOM 2828 OXT PHE A 450 9, .364 2. .398 35. .866 1. .00 39. .79 0
ATOM 2829 MG IUM A 500 28. .946 14. .438 16. .660 1. .00 33. .17 MG
ATOM 2831 Cl MAN A 600 5. .668 -11. .308 42. .166 1. .00 49. .14 C
ATOM 2832 C2 MAN A 600 7. .120 -11. .237 41. .573 1, .00 49. .77 C
ATOM 2833 02 MAN A 600 8, .041 -11. .026 42. .620 1. .00 50. .50 O
ATOM 2834 C3 MAN A 600 7, .409 -12. .514 40. .808 1, .00 50. .61 C
ATOM 2835 03 MAN A 600 8, .746 -12. .457 40. .289 1, .00 52. .29 O
ATOM 2836 C4 MAN A 600 7. .214 -13. .771 41, .606 1, .00 49. .83 C
ATOM 2837 04 MAN A 600 7, .152 -14. .888 40, .732 1, .00 49. .25 O
ATOM 2838 C5 MAN A 600 5. .938 -13. .737 42. .478 1, .00 49. .49 C
ATOM 2839 C6 MAN A 600 6. .030 -14. .691 43, .660 1, .00 48. .90 C
ATOM 2840 06 MAN A 600 7, .004 -14. .235 44, .570 1, .00 49. .55 O
ATOM 2841 05 MAN A 600 5 .598 -12, .455 42, .966 1. .00 48. .82 0
ATOM 2842 Cl MAN A 650 -1. .019 0. .389 36, .281 1 .00 33. .59 c
ATOM 2843 C2 MAN A 650 -1. .735 -0, .910 36, .785 1 .00 35. .19 c
ATOM 2844 02 MAN A 650 -1 .810 -0, .926 38, .207 1 .00 35. .56 0
ATOM 2845 C3 MAN A 650 -3, .139 -0, .988 36, .208 1 .00 36, .76 c
ATOM 2846 03 MAN A 650 -3. .775 -2. .175 36. .706 1 .00 37, .15 o
ATOM 2847 C4 MAN A 650 -3 .976 0. .239 36 .472 1 .00 38. .33 c
ATOM 2848 04 MAN A 650 -5 .154 0, .218 35 .687 1 .00 40, .01 0
ATOM 2849 C5 MAN A 650 -3. .171 1, .500 36 .088 1 .00 38, .36 c
ATOM 2850 C6 MAN A 650 -3 .775 2, .831 36 .470 1 .00 39, .68 c
ATOM 2851 06 MAN A 650 -3 .054 3 .827 35 .766 1 .00 42, .08 0
ATOM 2852 05 MAN A 650 -1. .856 1, .461 36 .634 1 .00 35 .94 0
ATOM 2853 Cl NAG A 800 -8 .073 -6 .145 -0, .318 1 .00 9. .79 c
ATOM 2854 C2 NAG A 800 -8 .690 -7. .157 -1. .282 1 .00 10. .36 c
ATOM 2855 N2 NAG A 800 -7 .691 -7 .663 -2 .243 1 .00 10. .16 N
ATOM 2856 C7 NAG A 800 -7 .477 -8 .997 -2 .458 1 .00 13 .26 c
ATOM 2857 07 NAG A 800 -8 .065 -9 .803 -1 .898 1 .00 14 .95 0
ATOM 2858 C8 NAG A 800 -6 .428 -9 .300 -3 .464 1 .00 11 .06 c
ATOM 2859 C3 NAG A 800 -9 .811 -6 .520 -2 .083 1 .00 11 .55 c
ATOM 2860 03 NAG A 800 -10 .512 -7 .519 -2 .816 1 .00 11 .95 0
ATOM 2861 C4 NAG A 800 -10 .844 -5 .826 -1 .139 1 .00 11 .32 c ATOM 2862 04 NAG A 800 11.756 -5.115 -1.996 1.00 11.09 o
ATOM 2863 C5 NAG A 800 10. 060 -4. 839 -0. 256 1. 00 9. 16 c
ATOM 2864 05 NAG A 800 -9. 147 -5. 613 0. 503 1. 00 7. 61 0
ATOM 2865 C6 NAG A 800 10. 905 -4. 025 0. 707 1. 00 8. 71 c
ATOM 2866 06 NAG A 800 10. 129 -3. 168 1. 504 1. 00 10. 07 o
ATOM 2867 Cl GOL G 700 5. 971 -7. 474 13. 148 1. 00 56. 20 c
ATOM 2868 01 GOL G 700 6. 763 -8. 674 13. .072 1. 00 56. .59 0
ATOM 2869 C2 GOL G 700 4. 604 -7. 678 12. .511 1. 00 56. 76 c
ATOM 2870 02 GOL G 700 3. 707 -6. 678 13. ,053 1. .00 57. .19 o
ATOM 2871 C3 GOL G 700 4. 726 -7. .533 10. ,989 1. .00 55. .80 c
ATOM 2872 03 GOL G 700 3. 721 -8. 314 10. 310 1. 00 55. 24 0
ATOM 2873 OWO WAT W 1 -4. 468 16. 654 2. 524 1. 00 5. 60 o
ATOM 2874 OWO WAT W 2 -9. 324 -4. 136 3. 963 1. 00 6. 10 o
ATOM 2875 OWO WAT W 3 -7. 470 -3. 307 -2. .246 1. 00 5. 86 o
ATOM 2876 OWO WAT W 4 12. 860 0. 177 1. ,787 1. 00 5. .96 o
ATOM 2877 OWO WAT W 5 -5. 097 10. .396 6. ,971 1. 00 6. .32 o
ATOM 2878 OWO WAT W 6 8. 197 -5. ,100 2. ,595 1. .00 6. .05 0
ATOM 2879 OWO WAT W 7 -0. 886 -12. ,491 -4. ,926 1. ,00 7. ,07 0
ATOM 2880 OWO WAT W 8 10. 318 -7. .987 -10. ,336 1. .00 7. ,50 0
ATOM 2881 OWO WAT w 9 14. .305 -0. .911 18. ,902 1. 00 7. ,40 o
ATOM 2882 OWO WAT w 10 6. .478 5. ,872 17. ,995 1. ,00 7. ,57 0
ATOM 2883 OWO WAT w 11 2. ,423 -9. .736 0. .365 1. .00 7. .92 0
ATOM 2884 OWO WAT w 12 1. .030 -0. .380 18. .240 1. .00 8. .32 o
ATOM 2885 OWO WAT w 13 13. 819 -1. ,981 3. ,118 1. .00 8. ,36 0
ATOM 2886 OWO WAT w 14 10. 400 1. ,638 1. ,169 1. .00 8. ,17 0
ATOM 2887 OWO WAT w 15 -5. .766 -9. ,753 4. ,360 1. .00 8. ,35 0
ATOM 2888 OWO WAT w 16 5. .966 -14. .827 -7. .223 1. ,00 8. ,55 o
ATOM 2889 OWO WAT w 17 7. .007 -11. .847 6. .999 1. .00 8. ,79 o
ATOM 2890 OWO WAT w 18 13. ,826 -7. .905 -10. .918 1. ,00 8. .81 o
ATOM 2891 OWO WAT w 19 14. ,539 -0. .383 9. .398 1. ,00 9. .03 0
ATOM 2892 OWO WAT w 20 -0. .933 2. .266 23. .257 1. .00 9. .17 o
ATOM 2893 OWO WAT w 21 12. .170 -3. .479 17. .651 1. .00 9. .27 o
ATOM 2894 OWO WAT w 22 0. .705 -12. .567 -11. .769 1. .00 9. .37 0
ATOM 2895 OWO WAT w 23 11. .229 -17. .196 19. .443 1. .00 9. .19 o
ATOM 2896 OWO WAT w 24 10. .620 -1. .566 18. .573 1. .00 9. .42 o
ATOM 2897 OWO WAT w 25 -7. .475 -2. .684 0. .505 1. .00 9. .78 o
ATOM 2898 OWO WAT w 26 -8. .958 18. .273 6. .515 1. .00 9. .87 0
ATOM 2899 OWO WAT w 27 17. .557 -3. .737 24. .225 1. .00 10. .25 o
ATOM 2900 OWO WAT w 28 23. .059 -3. .505 19. .890 1. .00 10. .29 o
ATOM 2901 OWO WAT w 29 4. .767 16. .031 5, .354 1. .00 10. .53 o
ATOM 2902 OWO WAT w 30 8. .485 -1, .312 22, .058 1, .00 10. .47 0
ATOM 2903 OWO WAT w 31 9. .567 -7. .077 1, .426 1, .00 10. .47 0
ATOM 2904 OWO WAT w 32 6. .081 -15, .169 -3, .110 1, .00 10, .80 0
ATOM 2905 OWO WAT w 33 -6. .029 -5. .578 -3, .194 1, .00 10, .73 0
ATOM 2906 OWO WAT w 34 -0, .551 -8 .403 -11, .160 1, .00 10, .64 0
ATOM 2907 OWO WAT w 35 21. .193 -4. .885 18. .347 1, .00 10, .94 o
ATOM 2908 OWO WAT w 36 16. .703 -14 .576 15 .763 1 .00 10, .99 o
ATOM 2909 OWO WAT w 37 27. .431 6 .691 19 .167 1. .00 11, .25 0
ATOM 2910 OWO WAT w 38 17. .711 12, .202 -5, .183 1, .00 11, .51 0
ATOM 2911 OWO WAT w 39 -3. .425 15, .550 13. .219 1, .00 11, .38 o
ATOM 2912 OWO WAT w 40 1, .926 -9. .415 -10 .379 1. .00 11, .20 0
ATOM 2913 OWO WAT w 41 10. .725 -12 .796 -6 .900 1, .00 11, .29 0
ATOM 2914 OWO WAT w 42 4. .586 -12 .320 -0 .004 1 .00 11. .22 0
ATOM 2915 OWO WAT w 43 31 .723 -3 .146 16 .036 1. .00 11 .36 0
ATOM 2916 OWO WAT w 44 -2 .405 -2 .392 16 .337 1 .00 11 .79 0
ATOM 2917 OWO WAT w 45 9 .550 -0 .217 -0 .443 1 .00 11 .72 0
ATOM 2918 OWO WAT w 46 7 .087 -13 .703 -0 .019 1 .00 12 .00 0
ATOM 2919 OWO WAT w 47 1 .840 16 .199 -0 .689 1 .00 12 .05 0
ATOM 2920 OWO WAT w 48 8 .160 -7 .933 20 .936 1 .00 11 .91 0
ATOM 2921 OWO WAT w 49 -7 .538 19 .875 9 .498 1 .00 12 .29 o
ATOM 2922 OWO WAT w 50 9 .058 -10 .668 20 .774 1. .00 11 .78 o
ATOM 2923 OWO WAT w 51 16 .826 3 .308 23 .487 1 .00 12 .38 0
ATOM 2924 OWO WAT w 52 -0 .582 -2 .790 18 .365 1 .00 12 .92 0
ATOM 2925 OWO WAT w 53 1 .832 19 .649 3 .061 1 .00 12 .83 0
ATOM 2926 OWO WAT w 54 12 .706 -8 .455 14 .301 1 .00 12 .82 0
ATOM 2927 OWO WAT w 55 -11 .536 9 .535 -0 .312 1 .00 13 .19 0
ATOM 2928 OWO WAT w 56 -6 .032 15 .160 0 .690 1 .00 13 .88 0
ATOM 2929 OWO WAT w 57 19 .162 -5 .707 15 .994 1 .00 14 .13 0
ATOM 2930 OWO WAT w 58 -1 .239 4 .561 14 .826 1 .00 14 .56 o
ATOM 2931 OWO WAT w 59 8 .708 -18 .310 13 .262 1 .00 14 .09 o
ATOM 2932 OWO WAT w 60 17 .937 3 .773 25 .959 1 .00 13 .94 0
ATOM 2933 OWO WAT w 61 5 .763 2 .778 -10 .531 1 .00 14 .20 0 ATOM 2934 OWO WAT W 62 4.818 16.514 -4.288 1.00 14.46 o
ATOM 2935 OWO WAT W 63 15.604 -2.866 10.842 1. 00 14. 30 o
ATOM 2936 OWO WAT W 64 31.308 4.387 6.863 1. 00 14. 65 o
ATOM 2937 OWO WAT W 65 10.455 15.524 -0.294 1. 00 14. 43 o
ATOM 2938 OWO WAT W 66 3.496 1.048 22.599 1. 00 14. 74 o
ATOM 2939 OWO WAT W 67 -8.496 -0.107 -4.629 1. 00 14. 14 o
ATOM 2940 OWO WAT W 68 -11.241 8.767 20.443 1. 00 14. 78 0
ATOM 2941 OWO WAT W 69 -1.634 -4.976 12.452 1. 00 14. 74 o
ATOM 2942 OWO WAT W 70 17.087 -13.910 18.326 1. 00 14. 95 0
ATOM 2943 OWO WAT W 71 -0.612 -3.043 14.265 1. 00 15. 69 0
ATOM 2944 OWO WAT W 72 -13.481 -4.288 3.399 1. 00 15. 73 o
ATOM 2945 OWO WAT W 73 5.936 13.080 -7.676 1. 00 15. 27 o
ATOM 2946 OWO WAT W 74 0.494 2.739 20.969 1. 00 15. 30 o
ATOM 2947 OWO WAT W 75 23.631 -1.239 18.248 1. 00 15. 65 o
ATOM 2948 OWO WAT W 76 13.244 8.375 26.887 1. 00 15. 66 0
ATOM 2949 OWO WAT W 77 30.009 2.397 0.481 1. 00 15. 32 o
ATOM 2950 OWO WAT w 78 14.697 -24.524 18.449 1. 00 16. 10 o
ATOM 2951 OWO WAT w 79 9.865 -14.692 0.881 1. .00 15. 61 o
ATOM 2952 OWO WAT w 80 -6.700 3.255 18.580 1. ,00 15. .95 o
ATOM 2953 OWO WAT w 81 0.226 -10.358 4.396 1. 00 16. 43 o
ATOM 2954 OWO WAT w 82 -14.277 -3.237 7.387 1. 00 16. 55 0
ATOM 2955 OWO WAT w 83 -14.273 10.136 14.220 1. ,00 16. .35 o
ATOM 2956 OWO WAT w 84 16.995 -22.459 14.478 1. .00 16. .89 0
ATOM 2957 OWO WAT w 85 8.800 -18.470 -1.262 1. .00 16. .06 0
ATOM 2958 OWO WAT w 86 -9.771 -2.396 -3.663 1. ,00 16. .79 0
ATOM 2959 OWO WAT w 87 31.994 -3.122 5.019 1. ,00 16. .44 o
ATOM 2960 OWO WAT w 88 -5.716 -11.410 -0.377 1. 00 17. .08 0
ATOM 2961 OWO WAT w 89 -7.576 -6.091 -5.437 1. ,00 16. .49 o
ATOM 2962 OWO WAT w 90 -8.105 0.245 -7.257 1. ,00 16. ,85 o
ATOM 2963 OWO WAT w 91 1.936 -21.294 11.415 1. ,00 17. ,49 o
ATOM 2964 OWO WAT w 92 26.647 15.826 1.455 1. ,00 17. ,25 0
ATOM 2965 OWO WAT w 93 12.689 9.940 24.738 1. .00 17. ,13 o
ATOM 2966 OWO WAT w 94 -13.521 -5.945 7.221 1. .00 17. ,80 o
ATOM 2967 OWO WAT w 95 8.448 15.744 3.637 1. .00 17. .75 o
ATOM 2968 OWO WAT w 96 -8.192 15.467 13.488 1. .00 17. .91 o
ATOM 2969 OWO WAT w 97 3.604 -6.629 15.807 1. .00 17. .79 o
ATOM 2970 OWO WAT w 98 0.291 6.882 16.524 1. .00 18. .12 0
ATOM 2971 OWO WAT w 99 15.287 -17.536 -3.539 1. .00 17. .85 o
ATOM 2972 OWO WAT w 100 14.184 -10.300 3.235 1. .00 18. .33 o
ATOM 2973 OWO WAT w 101 -2.364 2.671 30.993 1. .00 17. .88 o
ATOM 2974 OWO WAT w 102 3.745 -8.895 -12.356 1. .00 18. .47 o
ATOM 2975 OWO WAT w 103 -6.245 -7.090 -7.683 1. .00 18. .81 0
ATOM 2976 OWO WAT w 104 1.436 -14.284 25.817 1. .00 18. .52 0
ATOM 2977 OWO WAT w 105 12.268 -4.305 9.772 1. .00 18. .81 o
ATOM 2978 OWO WAT w 106 -0.224 -18.011 18.615 1. .00 19. .25 o
ATOM 2979 OWO WAT w 107 -11.552 -5.720 4.596 1, .00 19. .42 o
ATOM 2980 OWO WAT w 108 14.435 -15.325 7.825 1, .00 19. .06 o
ATOM 2981 OWO WAT w 109 5.457 14.376 18.532 1, .00 19. .25 o
ATOM 2982 OWO WAT w 110 33.159 -5.641 1.172 1. .00 19, .33 o
ATOM 2983 OWO WAT w 111 21.488 -7.744 27.377 1. .00 18. .85 o
ATOM 2984 OWO WAT w 112 -0.732 12.133 -4.438 1 .00 20. .00 o
ATOM 2985 OWO WAT w 113 -0.539 4.054 17.863 1. .00 19, .83 o
ATOM 2986 OWO WAT w 114 -7.316 5.876 -4.772 1 .00 19. .57 0
ATOM 2987 OWO WAT w 115 10.104 -8.684 13.464 1. .00 19, .36 o
ATOM 2988 OWO WAT w 116 -6.373 -10.853 -7.428 1 .00 19 .77 o
ATOM 2989 OWO WAT w 117 23.367 12.977 18.804 1 .00 20 .58 o
ATOM 2990 OWO WAT w 118 4.173 10.724 23.922 1 .00 20 .44 o
ATOM 2991 OWO WAT w 119 4.605 -16.994 13.371 1 .00 19 .72 0
ATOM 2992 OWO WAT w 120 -13.086 -1.205 0.262 1 .00 19 .75 o
ATOM 2993 OWO WAT w 121 22.657 -7.291 -3.700 1 .00 20 .26 0
ATOM 2994 OWO WAT w 122 29.490 7.752 11.469 1 .00 20 .15 o
ATOM 2995 OWO WAT w 123 6.233 20.091 3.312 1 .00 20 .58 o
ATOM 2996 OWO WAT w 124 16.002 -4.377 8.845 1 .00 19 .99 0
ATOM 2997 OWO WAT w 125 -14.036 6.248 16.420 1 .00 20 .32 o
ATOM 2998 OWO WAT w 126 24.954 -10.530 23.514 1 .00 20 .20 0
ATOM 2999 OWO WAT w 127 -5.026 -3.016 -9.151 1 .00 19 .86 0
ATOM 3000 OWO WAT w 128 22.890 17.427 15.518 1 .00 20 .21 0
ATOM 3001 OWO WAT w 129 7.124 -16.580 8.309 1 .00 21 .04 0
ATOM 3002 OWO WAT w 130 -11.004 -2.388 13.243 1 .00 20 .24 0
ATOM 3003 OWO WAT w 131 3.527 8.031 26.930 1 .00 20 .59 0
ATOM 3004 OWO WAT w 132 -2.513 -12.076 20.838 1 .00 21 .55 0
ATOM 3005 OWO WAT w 133 -13.855 10.661 6.699 1 .00 20 .52 0 ATOM 3006 OWO WAT W 134 6.324 9.299 23.766 1.00 21.47 O
ATOM 3007 OWO WAT W 135 13.982 17.723 12.601 1.00 21.83 O
ATOM 3008 OWO WAT W 136 7.589 -2.515 44.700 1.00 21.84 O
ATOM 3009 OWO WAT W 137 18.823 -8.635 13.064 1.00 21.59 O
ATOM 3010 OWO WAT W 138 7.675 -18.108 2.858 1.00 21.94 0
ATOM 3011 OWO WAT W 139 10.142 -13.484 -9.453 1.00 22.79 0
ATOM 3012 OWO WAT W 140 -8.748 -4.033 13.606 1.00 22.15 0
ATOM 3013 OWO WAT W 141 28.299 8.450 16.957 1.00 23.12 0
ATOM 3014 OWO WAT W 142 -0.123 8.590 25.377 1.00 22.65 0
ATOM 3015 OWO WAT W 143 4.305 5.196 -10.573 1.00 22.59 0
ATOM 3016 OWO WAT W 144 3.216 18.707 -3.341 1.00 23.01 O
ATOM 3017 OWO WAT W 145 23.235 -8.140 10.628 1.00 22.81 O
ATOM 3018 OWO WAT W 146 22.644 -9.297 3.639 1.00 23.06 0
ATOM 3019 OWO WAT W 147 8.467 11.734 24.878 1.00 22.90 0
ATOM 3020 OWO WAT W 148 26.741 14.179 16.573 1.00 23.03 0
ATOM 3021 OWO WAT W 149 29.370 12.527 16.019 1.00 23.20 O
ATOM 3022 OWO WAT W 150 -2.593 8.779 22.944 1.00 23.78 0
ATOM 3023 OWO WAT w 151 13.042 11.744 0.631 1.00 23.23 0
ATOM 3024 OWO WAT w 152 3.415 21.470 13.104 1.00 23.05 O
ATOM 3025 OWO WAT w 153 6.048 8.207 26.173 1.00 22.63 O
ATOM 3026 OWO WAT w 154 24.730 -11.926 11.981 1.00 23.13 O
ATOM 3027 OWO WAT w 155 11.681 -16.410 -7.159 1.00 23.40 O
ATOM 3028 OWO WAT w 156 31.087 14.581 17.102 1.00 23.88 0
ATOM 3029 OWO WAT w 157 -7.485 -9.642 1.513 1.00 23.54 O
ATOM 3030 OWO WAT w 158 22.874 0.702 -5.440 1.00 23.80 O
ATOM 3031 OWO WAT w 159 -5.044 15.418 -2.039 1.00 23.87 O
ATOM 3032 OWO WAT w 160 33.616 3.503 14.918 1.00 24.08 0
ATOM 3033 OWO WAT w 161 ■10.872 15.052 4.563 1.00 24.14 0
ATOM 3034 OWO WAT w 162 -4.606 -13.215 2.312 1.00 24.40 0
ATOM 3035 OWO WAT w 163 27.070 17.927 -2.306 1.00 23.99 0
ATOM 3036 OWO WAT w 164 9.893 -5.746 10.263 1.00 24.76 0
ATOM 3037 OWO WAT w 165 17.078 3.189 -7.107 1.00 24.03 0
ATOM 3038 OWO WAT w 166 15.062 14.379 19.475 1.00 24.70 0
ATOM 3039 OWO WAT w 167 22.032 -0.623 28.407 1.00 24.25 0
ATOM 3040 OWO WAT w 168 12.181 -23.786 18.858 1.00 24.75 0
ATOM 3041 OWO WAT w 169 -0.705 -14.765 22.543 1.00 24.49 0
ATOM 3042 OWO WAT w 170 28.955 8.903 14.322 1.00 24.45 0
ATOM 3043 OWO WAT w 171 3.695 12.616 -6.193 1.00 24.55 0
ATOM 3044 OWO WAT w 172 19.538 -12.070 9.591 1.00 24.48 0
ATOM 3045 OWO WAT w 173 14.310 14.805 24.317 1.00 24.67 0
ATOM 3046 OWO WAT w 174 29.093 11.564 -1.788 1.00 25.43 0
ATOM 3047 OWO WAT w 175 3.832 6.619 29.580 1.00 24.64 0
ATOM 3048 OWO WAT w 176 -4.607 -13.078 -5.569 1.00 25.32 0
ATOM 3049 OWO WAT w 177 2.173 -10.201 8.127 1.00 25.57 0
ATOM 3050 OWO WAT w 178 4.802 -21.672 20.497 1.00 25.35 0
ATOM 3051 OWO WAT w 179 -5.652 -2.528 34.399 1.00 24.99 0
ATOM 3052 OWO WAT w 180 4.922 -18.387 6.576 1.00 25.41 0
ATOM 3053 OWO WAT w 181 19.039 18.090 8.296 1.00 24.90 0
ATOM 3054 OWO WAT w 182 14.030 -16.520 -0.839 1.00 25.24 0
ATOM 3055 OWO WAT w 183 13.952 -13.251 29.217 1.00 24.95 0
ATOM 3056 OWO WAT w 184 13.863 -3.287 7.648 1.00 25.30 0
ATOM 3057 OWO WAT w 185 12.660 14.016 -9.979 1.00 26.21 0
ATOM 3058 OWO WAT w 186 12.317 9.016 29.374 1.00 25.87 0
ATOM 3059 OWO WAT w 187 16.730 -11.987 28.683 1.00 26.21 0
ATOM 3060 OWO WAT w 188 12.915 7.477 33.524 1.00 25.68 0
ATOM 3061 OWO WAT w 189 20.307 19.532 0.156 1.00 26.22 0
ATOM 3062 OWO WAT w 190 -4.141 -5.926 13.308 1.00 26.52 0
ATOM 3063 OWO WAT w 191 3.650 -16.192 3.024 1.00 26.09 0
ATOM 3064 OWO WAT w 192 18.931 -8.114 10.486 1.00 25.84 0
ATOM 3065 OWO WAT w 193 6.544 -16.595 11.718 1.00 26.72 0
ATOM 3066 OWO WAT w 194 -9.642 -4.382 -5.721 1.00 26.51 0
ATOM 3067 OWO WAT w 195 25.077 18.264 7.448 1.00 27.66 0
ATOM 3068 OWO WAT w 196 22.062 -10.277 28.364 1.00 26.91 0
ATOM 3069 OWO WAT w 197 21.527 7.834 -6.777 1.00 27.25 0
ATOM 3070 OWO WAT w 198 -15.429 6.005 10.514 1.00 26.27 0
ATOM 3071 OWO WAT w 199 21.193 -21.187 18.252 1.00 26.89 0
ATOM 3072 OWO WAT w 200 19.949 -14.230 -7.811 1.00 26.83 0
ATOM 3073 OWO WAT w 201 27.179 3.904 26.254 1.00 27.22 0
ATOM 3074 OWO WAT w 202 28.930 13.425 18.572 1.00 26.37 0
ATOM 3075 OWO WAT w 203 25.676 -3.621 -3.154 1.00 26.88 0
ATOM 3076 OWO WAT w 204 -3.469 -3.163 39.209 1.00 27.42 0
ATOM 3077 OWO WAT w 205 -6.999 18.655 15.387 1.00 27.04 0 ATOM 3078 OWO WAT W 206 -9.951 2.021 -4..039 1.00 27..29 o
ATOM 3079 OWO WAT W 207 16. 128 17. 390 14. .219 1. 00 27. ,01 o
ATOM 3080 OWO WAT W 208 5. 742 20. 405 11. .966 1. 00 27. ,24 o
ATOM 3081 OWO WAT W 209 3. 407 -14. 359 31. ,337 1. 00 26. ,97 o
ATOM 3082 OWO WAT W 210 13. 943 16. 430 15. .607 1. 00 26. .52 0
ATOM 3083 OWO WAT W 211 1. 033 -24. 205 11. ,563 1. 00 26. .74 o
ATOM 3084 OWO WAT W 212 8. ,538 -6. ,820 12. ,252 1. .00 27. .10 o
ATOM 3085 OWO WAT W 213 26. .428 -6. ,873 4. ,061 1. ,00 28. .64 0
ATOM 3086 OWO WAT W 214 12. ,793 -21. ,553 8. .586 1. ,00 27. .33 o
ATOM 3087 OWO WAT W 215 1. ,409 -1. .041 41. ,300 1. ,00 27. .91 o
ATOM 3088 OWO WAT W 216 16. ,429 -18. .470 25. ,150 1. .00 28. ,26 o
ATOM 3089 OWO WAT W 217 23. .448 -5. ,569 28. ,728 1. .00 27. .68 0
ATOM 3090 OWO WAT W 218 3. ,804 12. ,359 21. ,721 1. .00 27. .98 0
ATOM 3091 OWO WAT W 219 12. .182 -21. .534 27. .485 1. .00 28. .34 o
ATOM 3092 OWO WAT W 220 -2. .839 14. .075 -5. ,590 1. .00 29. .01 o
ATOM 3093 OWO WAT W 221 6. 291 -7. .332 -11. ,913 1. .00 27. ,59 o
ATOM 3094 OWO WAT W 222 27. .232 -10. ,868 14. .704 1. ,00 27. .74 o
ATOM 3095 OWO WAT w 223 22. .832 -12. ,419 1. .056 1. ,00 28. .27 0
ATOM 3096 OWO WAT w 224 24. .905 16. .204 16. .657 1. .00 27. .46 o
ATOM 3097 OWO WAT w 225 6. .998 -16. .116 1. .072 1. .00 28. .54 0
ATOM 3098 OWO WAT w 226 8. .341 -14. .756 11. .628 1. ,00 28. .02 o
ATOM 3099 OWO WAT w 227 31. .699 8. ,814 7. .083 1. .00 28. .53 o
ATOM 3100 OWO WAT w 228 1. ,326 12. .873 24. .228 1. ,00 28. .34 o
ATOM 3101 OWO WAT w 229 26. .343 10. .267 21. .240 1. ,00 28. .97 o
ATOM 3102 OWO WAT w 230 -8. ,226 8. .444 -4. .190 1. ,00 28. .02 0
ATOM 3103 OWO WAT w 231 1. .037 10. ,354 23. .234 1. ,00 27. .68 0
ATOM 3104 OWO WAT w 232 31. ,351 9. .070 15. .681 1. ,00 28. .94 0
ATOM 3105 OWO WAT w 233 9. ,961 -13. .191 30. .741 1. ,00 28. .63 0
ATOM 3106 OWO WAT w 234 -1. ,017 -12. .518 14. .553 1. ,00 29. .46 o
ATOM 3107 OWO WAT w 235 7. ,281 16. .086 5. .949 1. .00 28. .91 o
ATOM 3108 OWO WAT w 236 12. ,010 -1. .097 -12. .003 1. .00 29. .09 o
ATOM 3109 OWO WAT w 237 14. .446 0. .903 -0. .623 1. .00 28. .57 o
ATOM 3110 OWO WAT w 238 20. .658 -12. .467 27. .357 1. .00 28. .27 0
ATOM 3111 OWO WAT w 239 29. .938 9. .464 5. .006 1. .00 28. .75 o
ATOM 3112 OWO WAT w 240 14. .494 -1. .249 33. .932 1. .00 28. .76 0
ATOM 3113 OWO WAT w 241 -6. .225 20. .349 11. .888 1. .00 28. .93 0
ATOM 3114 OWO WAT w 242 -4. .947 -14. .577 -8, .496 1. .00 30, .30 o
ATOM 3115 OWO WAT w 243 20. .235 17. .364 -1. .556 1. .00 30, .70 0
ATOM 3116 OWO WAT w 244 -1. .673 -9. .217 19, .036 1. .00 30, .74 0
ATOM 3117 OWO WAT w 245 10. .607 17. .610 3, .903 1. .00 29, .81 0
ATOM 3118 OWO WAT w 246 18. .328 -2. .427 30, .996 1. .00 29, .71 0
ATOM 3119 OWO WAT w 247 15. .186 10. .698 24, .086 1. .00 30, .00 0
ATOM 3120 OWO WAT w 248 25. .589 -12, .660 25, .077 1. .00 29, .38 0
ATOM 3121 OWO WAT w 249 5. .811 -10. .320 38, .194 1. .00 29, .86 o
ATOM 3122 OWO WAT w 250 -9, .482 14. .737 23, .332 1. .00 29, .60 o
ATOM 3123 OWO WAT w 251 -9, .452 -8, .084 -5, .246 1. .00 29, .57 o
ATOM 3124 OWO WAT w 252 27 .981 -2 .018 24 .047 1. .00 29 .85 o
ATOM 3125 OWO WAT w 253 9 .480 -14 .704 9 .232 1, .00 29 .91 o
ATOM 3126 OWO WAT w 254 29. .170 15 .410 15 .105 1, .00 30 .52 0
ATOM 3127 OWO WAT w 255 -1 .073 20 .472 15 .287 1, .00 30 .04 0
ATOM 3128 OWO WAT w 256 25. .041 16 .369 4 .043 1, .00 30. .10 0
ATOM 3129 OWO WAT w 257 8 .526 -10 .719 12 .264 1, .00 30. .73 0
ATOM 3130 OWO WAT w 258 ■11. .777 -9 .547 -1 .114 1, .00 30 .39 0
ATOM 3131 OWO WAT w 259 15 .217 -24 .589 13 .732 1. .00 31 .76 0
ATOM 3132 OWO WAT w 260 ■10. .571 15 .562 -1 .155 1. .00 31 .49 0
ATOM 3133 OWO WAT w 261 24, .233 -10 .206 -3 .316 1, .00 30 .98 0
ATOM 3134 OWO WAT w 262 22 .801 -14 .479 24 .909 1 .00 32 .54 o
ATOM 3135 OWO WAT w 263 0 .353 -5 .061 15 .605 1 .00 32 .91 0
ATOM 3136 OWO WAT w 264 0 .183 -9 .444 12 .256 1 .00 32 .18 o
ATOM 3137 OWO WAT w 265 -9 .240 4 .480 -6 .104 1 .00 32 .08 o
ATOM 3138 OWO WAT w 266 22 .177 -16 .298 0 .412 1 .00 31 .68 0
ATOM 3139 OWO WAT w 267 20 .544 -0 .803 30 .714 1 .00 31 .12 0
ATOM 3140 OWO WAT w 268 ■13 .097 -2 .924 16 .924 1 .00 32 .23 0
ATOM 3141 OWO WAT w 269 -2 .339 21 .164 17 .490 1. .00 33 .07 0
ATOM 3142 OWO WAT w 270 14 .787 -12 .634 7 .535 1. .00 31 .57 0
ATOM 3143 OWO WAT w 271 19 .163 -23 .079 12 .690 1. .00 32 .33 0
ATOM 3144 OWO WAT w 272 26 .398 16 .860 -4 .892 1 .00 31 .30 0
ATOM 3145 OWO WAT w 273 -1 .037 -13 .317 26 .276 1 .00 32 .40 0
ATOM 3146 OWO WAT w 274 31 .761 -9 .534 9 .316 1 .00 31 .45 0
ATOM 3147 OWO WAT w 275 ■14 .962 6 .438 8 .019 1 .00 32 .22 0
ATOM 3148 OWO WAT w 276 16 .902 -22 .232 24 .082 1 .00 32 .50 0
ATOM 3149 OWO WAT w 277 31 .999 3 .938 -0 .687 1 .00 32 .98 0 ATOM 3150 OWO WAT W 278 10.882 -24.863 20.835 1.00 33.,00 o
ATOM 3151 OWO WAT W 279 16. 312 8. 681 27. .021 1. 00 32. .18 0
ATOM 3152 OWO WAT W 280 20. 408 2. 341 23. .733 1. 00 31. ,64 o
ATOM 3153 OWO WAT W 281 3. 089 -16. 183 24. .860 1. 00 32. ,92 0
ATOM 3154 OWO WAT W 282 12. 145 -8. 651 -12. .952 1. 00 33. ,48 o
ATOM 3155 OWO WAT W 283 30. 869 -10. .078 15. ,970 1. 00 32. ,04 0
ATOM 3156 OWO WAT W 284 26. 112 0. .524 27. ,149 1. 00 33. ,28 0
ATOM 3157 OWO WAT W 285 32. 955 3. ,269 26. ,482 1. 00 31. ,92 0
ATOM 3158 OWO WAT W 286 -4. 349 15. ,468 25. ,028 1. 00 33. ,76 0
ATOM 3159 OWO WAT W 287 0. 543 -19. ,994 6. ,822 1. 00 33. ,30 0
ATOM 3160 OWO WAT W 288 7. 232 18. ,822 6. ,235 1. 00 33. .25 0
ATOM 3161 OWO WAT W 289 30. 793 -0. ,744 -2. ,106 1. 00 32. .41 0
ATOM 3162 OWO WAT W 290 14. .044 4. .412 4. ,984 1. 00 34. .64 o
ATOM 3163 OWO WAT W 291 7. .935 -21. ,433 7. ,051 1. .00 33. .93 o
ATOM 3164 OWO WAT W 292 9. .487 17. ,785 1. ,224 1. 00 33. .09 0
ATOM 3165 OWO WAT W 293 ■11. .530 17. .332 12. .202 1. 00 32. .80 0
ATOM 3166 OWO WAT W 294 11. 972 20. ,874 7. .981 1. 00 33. ,70 0
ATOM 3167 OWO WAT W 295 2. 330 1. ,272 42. .628 1. 00 32. ,68 0
ATOM 3168 OWO WAT W 296 17. 157 10. .127 9. ,956 1. 00 32. ,92 o
ATOM 3169 OWO WAT W 297 20. 408 -14. .578 9. .046 1. 00 34. ,48 0
ATOM 3170 OWO WAT W 298 -5. 731 -5. ,219 34. ,259 1. 00 34. ,02 o
ATOM 3171 OWO WAT W 299 28. 823 -8. ,458 13. .197 1. 00 34. ,10 0
ATOM 3172 OWO WAT W 300 18. 168 10. .098 25. ,967 1. 00 34. ,11 0
ATOM 3173 OWO WAT W 301 2. .189 -27. .221 14. ,252 1. 00 33. .96 0
ATOM 3174 OWO WAT W 302 4. .440 18. ,298 20. ,498 1. 00 33. .98 o
ATOM 3175 OWO WAT W 303 18. .342 -18. .763 -1. ,284 1. ,00 33. .67 o
ATOM 3176 OWO WAT W 304 -4. .335 -4. .252 15. .976 1. ,00 33. .57 o
ATOM 3177 OWO WAT W 305 -5. ,704 -11. .489 9. .366 1. .00 34. .26 o
ATOM 3178 OWO WAT W 306 8. ,129 -11. .682 -12. .784 1. ,00 33. .48 o
ATOM 3179 OWO WAT W 307 20. .227 10. .579 -7. .226 1. ,00 34. .37 0
ATOM 3180 OWO WAT W 308 5. .761 -19. .412 28. .762 1. ,00 36. .02 o
ATOM 3181 OWO WAT W 309 •13. .370 2. .801 17. .564 1. .00 34. .60 o
ATOM 3182 OWO WAT W 310 17. ,448 -16. .784 1. .721 1. .00 33. .97 0
ATOM 3183 OWO WAT W 311 30. .754 11. .892 4. .112 1. .00 33. .96 0
ATOM 3184 OWO WAT W 312 9. .298 7. .216 31. .177 1. .00 33. .72 0
ATOM 3185 OWO WAT W 313 3. .963 5. .346 37. .294 1. ,00 35. .91 0
ATOM 3186 OWO WAT W 314 -0. .537 -3. .858 -13. .509 1. ,00 35. .50 0
ATOM 3187 OWO WAT W 315 29. .546 12. .636 1. .125 1. .00 35. .28 0
ATOM 3188 OWO WAT W 316 16. .641 -10. .279 30. .641 1. .00 36. .00 0
ATOM 3189 OWO WAT W 317 3. .375 1. .212 -11. .626 1. .00 35. .75 0
ATOM 3190 OWO WAT W 318 4. .176 -22, .783 27. .673 1. .00 34. .95 0
ATOM 3191 OWO WAT W 319 -7. .882 0, .661 24. .793 1. .00 35. .32 o
ATOM 3192 OWO WAT W 320 -4. .779 7, .582 23, .450 1. .00 34, .46 o
ATOM 3193 OWO WAT W 321 4. .365 -18, .587 24, .470 1. .00 34, .61 0
ATOM 3194 OWO WAT W 322 1. .204 12, .181 -7, .096 1. .00 36, .26 o
ATOM 3195 OWO WAT W 323 -3. .540 -2. .303 -11, .595 1. .00 35, .37 0
ATOM 3196 OWO WAT W 324 -8. .444 -11. .343 25, .966 1. .00 34, .16 0
ATOM 3197 OWO WAT W 325 -9. .197 -3. .147 27. .671 1. .00 34, .91 0
ATOM 3198 OWO WAT W 326 -5, .861 6. .821 -7, .982 1. .00 35. .73 0
ATOM 3199 OWO WAT W 327 10, .062 -1. .946 -13. .617 1. .00 36 .61 0
ATOM 3200 OWO WAT W 328 ■10, .656 -3 .956 29 .828 1. .00 35 .98 0
ATOM 3201 OWO WAT W 329 27. .520 13 .568 9 .092 1. .00 34 .52 o
ATOM 3202 OWO WAT W 330 ■13 .835 20 .571 21 .432 1. .00 35 .55 0
ATOM 3203 OWO WAT W 331 8. .763 17 .704 -6. .219 1. .00 35 .66 0
ATOM 3204 OWO WAT W 332 8 .791 19 .547 -1 .536 1. .00 35 .85 0
ATOM 3205 OWO WAT W 333 1. .972 -24 .287 16 .659 1. .00 36 .07 0
ATOM 3206 OWO WAT W 334 1. .764 6 .531 -9 .997 1. .00 35 .95 o
ATOM 3207 OWO WAT W 335 26 .115 -21 .431 23 .463 1. .00 35 .92 o
ATOM 3208 OWO WAT W 336 3. .092 -20 .316 22 .836 1 .00 36 .59 0
ATOM 3209 OWO WAT W 337 9 .317 -26 .480 18 .754 1 .00 35 .55 0
ATOM 3210 OWO WAT W 338 21 .231 19 .662 18 .051 1 .00 37 .21 o
ATOM 3211 OWO WAT W 339 6 .594 19 .484 19 .344 1 .00 37 .53 0
ATOM 3212 OWO WAT W 340 7 .477 14 .635 20 .823 1 .00 37 .91 0
ATOM 3213 OWO WAT W 341 -11 .937 10 .574 22 .349 1 .00 36 .41 0
ATOM 3214 OWO WAT W 342 7 .548 -25 .143 8 .852 1 .00 37 .20 0
ATOM 3215 OWO WAT W 343 -15 .112 10 .366 11 .747 1 .00 37 .44 0
ATOM 3216 OWO WAT W 344 1. .187 10 .146 -10 .133 1. .00 37 .90 0
ATOM 3217 OWO WAT W 345 27 .638 -9 .538 23 .200 1. .00 37 .98 0
ATOM 3218 OWO WAT W 346 11. .116 -26 .606 10 .512 1 .00 38 .07 0
ATOM 3219 OWO WAT W 347 30 .049 12 .630 12 .175 1. .00 36 .48 o
ATOM 3220 OWO WAT W 348 2 .579 -21 .238 16 .750 1. .00 37 .11 o
ATOM 3221 OWO WAT W 349 11 .496 16 .342 -9 .873 1 .00 39 .00 o ATOM 3222 OWO WAT W 350 -1.466 -16.623 20.756 1.00 36.99 0
ATOM 3223 OWO WAT W 351 -0. 545 -19. 843 10. 447 1. 00 38. 11 0
ATOM 3224 OWO WAT W 352 21. 379 12. 373 20. 657 1. 00 37. 85 o
ATOM 3225 OWO WAT W 353 28. 638 1. 283 26. 152 1. 00 38. 39 0
ATOM 3226 OWO WAT W 354 26. 602 -18. 054 17. 223 1. 00 37. 87 0
ATOM 3227 OWO WAT W 355 7. 428 6. 106 33. 816 1. 00 38. 44 0
ATOM 3228 OWO WAT W 356 8. 893 23. 527 6. 272 1. 00 38. 41 o
ATOM 3229 OWO WAT W 357 10. 471 9. 875 -2. 931 1. 00 36. 99 0
ATOM 3230 OWO WAT W 358 -0. 662 -13. 392 29. 705 1. 00 38. 39 o
ATOM 3231 OWO WAT W 359 -2. 749 -13. 844 23. 936 1. 00 36. 78 o
ATOM 3232 OWO WAT W 360 -6. 451 -7. 989 -11. 128 1. 00 38. 41 0
ATOM 3233 OWO WAT W 361 9. 700 20. 358 0. 772 1. 00 39. 26 o
ATOM 3234 OWO WAT W 362 -7. 793 -2. 309 -8. 870 1. 00 38. 33 0
ATOM 3235 OWO WAT W 363 6. 887 20. 392 -3. 210 1. 00 38. 80 o
ATOM 3236 OWO WAT W 364 17. 753 6. 950 20. 616 1. 00 40. 01 o
ATOM 3237 OWO WAT W 365 28. 379 16. 628 17. 436 1. 00 37. 42 o
ATOM 3238 OWO WAT W 366 9. 825 -12. 183 6. 908 1. 00 38. 16 0
ATOM 3239 OWO WAT W 367 5. 690 6. 886 -12. 186 1. ,00 40. 11 0
ATOM 3240 OWO WAT W 368 -2. 055 -16. 092 31. 328 1. .00 39. 36 0
ATOM 3241 OWO WAT W 369 ■11. 775 -1. .154 -2. .246 1. .00 37. 59 0
ATOM 3242 OWO WAT W 370 -3. 450 4. .262 -10. 734 1. .00 38. .16 o
ATOM 3243 OWO WAT W 371 ■14. .001 -3. .955 -0. 918 1. .00 38. .31 o
ATOM 3244 OWO WAT W 372 8. .159 3. ,321 -11. .997 1. ,00 37. .67 o
ATOM 3245 OWO WAT W 373 16. .327 17. .648 5. ,170 1. .00 39. .07 0
ATOM 3246 OWO WAT W 374 13. .238 -12. .480 -13. .011 1. .00 38. ,95 0
ATOM 3247 OWO WAT W 375 19. ,726 2. ,965 -8. ,515 1. ,00 38. ,29 o
ATOM 3248 OWO WAT W 376 19. ,310 -9. ,518 5. .350 1. .00 38. ,81 o
ATOM 3249 OWO WAT W 377 •15. ,073 10. ,383 1. ,720 1. .00 41. ,26 o
ATOM 3250 OWO WAT W 378 1. .833 3. ,909 36. .312 1. .00 40. .71 0
ATOM 3251 OWO WAT W 379 7. .669 -2. .701 -13. ,009 1. .00 38. .35 0
ATOM 3252 OWO WAT W 380 -0. .042 22. .891 13. ,930 1. .00 38. .98 0
ATOM 3253 OWO WAT W 381 18. .209 -4. .980 33. ,399 1. .00 39. .29 0
ATOM 3254 OWO WAT W 382 13. .374 15. .788 3. .831 1. .00 39. .95 o
ATOM 3255 OWO WAT W 383 •10. .327 -7. .958 3. .125 1. .00 38. .85 o
ATOM 3256 OWO WAT W 384 -3. .650 3. .813 32. .973 1. .00 39. .43 0
ATOM 3257 OWO WAT W 385 20. .875 4. .704 22. .603 1. .00 38. .60 o
ATOM 3258 OWO WAT W 386 14. .314 17. .681 -1. .839 1. .00 41. .17 0
ATOM 3259 OWO WAT W 387 19. .223 15. .552 -7. .262 1. .00 41. .68 o
ATOM 3260 OWO WAT W 388 33. .270 4. .365 19. ,865 1. .00 40. .05 o
ATOM 3261 OWO WAT W 389 9. .325 20. .619 21. ,151 1. .00 39. .90 0
ATOM 3262 OWO WAT W 390 -13. .091 15. .620 6. .000 1. .00 40. .38 o
ATOM 3263 OWO WAT W 391 23, .491 19. .179 -2. .503 1. .00 39. .94 0
ATOM 3264 OWO WAT W 392 -12, .773 6. .682 5. .403 1. .00 39. .84 o
ATOM 3265 OWO WAT W 393 28, .152 1. .672 -5. .763 1, .00 40. .15 0
ATOM 3266 OWO WAT W 394 0, .217 0. .249 39. .323 1, .00 39. .21 o
ATOM 3267 OWO WAT W 395 -8, .727 22, .236 15. .741 1. .00 42. .52 o
ATOM 3268 OWO WAT W 396 16, .483 18, .099 -4. .316 1. .00 41. .15 0
ATOM 3269 OWO WAT W 397 6, .198 3, .825 37. .356 1, .00 40. .82 0
ATOM 3270 OWO WAT W 398 7, .009 -19, .419 5, .120 1, .00 39, .84 0
ATOM 3271 OWO WAT W 399 10. .448 18. .227 -3, .279 1, .00 41, .40 0
ATOM 3272 OWO WAT W 400 12. .628 19. .457 14. .821 1 .00 39, .84 0
ATOM 3273 OWO WAT W 401 37 .879 -8 .908 11. .587 1 .00 40, .44 0
ATOM 3274 OWO WAT W 402 -1. .899 8 .875 27, .727 1 .00 41. .39 o
ATOM 3275 OWO WAT W 403 24 .296 3 .299 -8. .463 1 .00 40. .53 o
ATOM 3276 OWO WAT W 404 6 .867 1 .412 38 .573 1 .00 41 .40 0
ATOM 3277 OWO WAT W 405 22 .366 -14 .528 11 .597 1 .00 43 .11 o
ATOM 3278 OWO WAT W 406 23 .833 -18 .708 17 .699 1. .00 41 .98 0
ATOM 3279 OWO WAT W 407 1 .838 -15 .790 33 .526 1 .00 41 .48 0
ATOM 3280 OWO WAT W 408 27 .474 -3 .804 -1. .240 1 .00 40 .65 0
ATOM 3281 OWO WAT W 409 -5 .174 19 .174 25 .726 1 .00 41 .76 o
ATOM 3282 OWO WAT W 410 0 .062 25 .053 24 .310 1 .00 41 .70 0
ATOM 3283 OWO WAT W 411 4 .471 -12 .096 -12. .960 1 .00 43 .28 0
ATOM 3284 OWO WAT W 412 20 .256 -13 .113 2 .826 1 .00 41 .10 0
ATOM 3285 OWO WAT W 413 -5 .840 -5 .661 21 .921 1 .00 41 .92 0
ATOM 3286 OWO WAT W 414 8 .684 -13 .645 34 .794 1 .00 42 .54 0
ATOM 3287 OWO WAT W 415 13 .914 -6 .916 -13 .882 1 .00 41 .71 0
ATOM 3288 OWO WAT W 416 14 .187 -11 .282 31 .629 1 .00 41 .23 o
ATOM 3289 OWO WAT W 417 12 .561 17 .391 1 .764 1 .00 43 .57 0
ATOM 3290 OWO WAT W 418 3 .232 17 .233 22 .744 1 .00 42 .83 o
ATOM 3291 OWO WAT W 419 27 .314 7 .198 23 .397 1 .00 41 .34 o
ATOM 3292 OWO WAT W 420 -12 .751 1 .882 -3 .237 1 .00 40 .27 0
ATOM 3293 OWO WAT W 421 0 .590 -24 .813 14 .244 1 .00 41 .89 0 ATOM 3294 OWO WAT W 422 -4.431 25.628 20.657 .00 42.92 O
ATOM 3295 OWO WAT W 423 10.735 -29.632 13.177 ,00 41.34 O
ATOM 3296 OWO WAT W 424 818 -18.271 26.821 ,00 41.70 O
ATOM 3297 OWO WAT W 425 544 -5.854 -14.071 ,00 42.37 O
ATOM 3298 OWO WAT W 426 -10.926 0.955 20.550 00 43.69 O
ATOM 3299 OWO WAT W 427 971 15.314 -3.312 .00 43.61 O
ATOM 3300 OWO WAT W 428 504 15.490 -5.176 .00 42.78 O
ATOM 3301 OWO WAT W 429 24.825 -9.368 26.783 .00 42.64 O
ATOM 3302 OWO WAT W 430 14.033 -20.188 1.211 .00 43.44 O
ATOM 3303 OWO WAT W 431 23.267 -17.669 12.770 ,00 44.56 O
ATOM 3304 OWO WAT W 432 17.150 -15.960 5.707 ,00 44.54 O
ATOM 3305 OWO WAT W 433 -2.139 5.153 37.892 .00 44.88 O
ATOM 3306 OWO WAT W 434 21.785 -9.480 6.297 ,00 44.18 O
ATOM 3307 OWO WAT W 435 25.968 -8.622 10.348 ,00 42.33 O
ATOM 3308 OWO WAT W 436 -3.314 -13.078 5.090 ,00 43.68 O
ATOM 3309 OWO WAT W 437 -10.754 6.347 21.686 ,00 43.50 O
ATOM 3310 OWO WAT w 438 0.943 22.569 17.840 ,00 44.44 O
ATOM 3311 OWO WAT w 439 24.968 8.402 -7.324 ,00 43.13 O
ATOM 3312 OWO WAT w 440 16.500 -6.946 9.700 .00 44.41 O
ATOM 3313 OWO WAT w 441 0.557 17.044 23.824 .00 44.16 0
ATOM 3314 OWO WAT w 442 1.825 16.199 29.076 ,00 45.60 o
ATOM 3315 OWO WAT w 443 32.689 -8.004 5.401 ,00 44.79 o
ATOM 3316 OWO WAT w 444 22.281 -16.173 27.002 .00 45.83 o
ATOM 3317 OWO WAT w 445 23.674 1.373 27.678 .00 45.60 0
ATOM 3318 OWO WAT w 446 13.387 -27.439 12.003 1.00 45.57 0
ATOM 3319 OWO WAT w 447 23.380 .087 30.367 1.00 44.29 0
ATOM 3320 OWO WAT w 448 25.870 .427 29.466 1.00 45.76 o
ATOM 3321 OWO WAT w 449 28.230 -12.183 20.780 .00 46.33 0
ATOM 3322 OWO WAT w 450 0.525 -12.459 8.685 .00 46.37 o
ATOM 3323 OWO WAT w 451 0.049 3.073 38.476 .00 44.20 0
ATOM 3324 OWO WAT w 452 15.358 -25.408 11.134 .00 45.34 0
ATOM 3325 OWO WAT w 453 -7.126 10.457 -5.602 .00 46.42 0
ATOM 3326 OWO WAT w 454 -15.541 12.545 14.559 .00 44.77 o
ATOM 3327 OWO WAT w 455 9.733 -8.250 9.274 .00 46.50 o
ATOM 3328 OWO WAT w 456 15.819 -14.661 -10.184 .00 48.29 0
ATOM 3329 OWO WAT w 457 24.696 -7.742 6.017 1.00 45.66 o
ATOM 3330 OWO WAT w 458 -10.468 19.247 26.127 .00 47.46 o
ATOM 3331 OWO WAT w 459 12.789 -8.545 10.918 .00 45.92 0
ATOM 3332 OWO WAT w 460 -13.715 6.091 1.705 .00 48.27 o
ATOM 3333 OWO WAT w 461 29.183 -12.218 16.919 .00 48.14 o
ATOM 3334 OWO WAT w 462 .173 6.902 28.600 ,00 47.42 o
ATOM 3335 OWO WAT w 463 .020 22.830 14.837 .00 48.29 o
ATOM 3336 OWO WAT w 464 .629 27.213 10.934 1.00 45.82 o
ATOM 3337 OWO WAT w 465 10.448 11.702 -11.581 1.00 47.52 0
ATOM 3338 OWO WAT w 466 25.475 0.155 -6.203 00 46.75 0
ATOM 3339 OWO WAT w 467 11.999 19.475 -5.519 00 46.73 0
ATOM 3340 OWO WAT w 468 29.707 -3.847 25.273 00 50.07 0
ATOM 3341 OWO WAT w 469 20.987 -8.262 8.572 00 46.30 0
ATOM 3342 OWO WAT w 470 25.831 15.569 12.286 00 49.36 o
ATOM 3343 OWO WAT w 471 -9.628 18.946 14.121 00 49.44 o
ATOM 3344 OWO WAT w 472 -14.232 19.028 24.748 00 49.03 o
ATOM 3345 OWO WAT w 473 26.936 13.463 12.361 00 48.35 0
ATOM 3346 OWO WAT w 474 -9.922 399 24.487 00 48.05 0
ATOM 3347 OWO WAT w 475 20.086 651 23.257 00 47.80 0
ATOM 3348 OWO WAT w 476 8.200 10.319 -11.614 00 48.09 o
ATOM 3349 OWO WAT w 477 6.799 7.061 29.352 00 48.85 0
ATOM 3350 OWO WAT w 478 10.735 -0.632 34.142 1.00 48.01 0
ATOM 3351 OWO WAT w 479 -6.739 13.322 24.757 1.00 47.80 o
ATOM 3352 OWO WAT w 480 33.317 -5.038 21.142 .00 48.61 0
ATOM 3353 OWO WAT w 481 16.742 18.491 19.979 .00 48.67 0
ATOM 3354 OWO WAT w 482 -3.257 -8.684 14.796 .00 48.30 0
ATOM 3355 OWO WAT w 483 -5.635 12.310 6.861 .00 47.68 0
ATOM 3356 OWO WAT w 484 -6.546 -7.324 23.953 .00 48.00 0
ATOM 3357 OWO WAT w 485 -16.417 11.786 18.852 .00 49.45 0
ATOM 3358 OWO WAT w 486 8.671 -23.459 21.434 .00 48.92 o
ATOM 3359 OWO WAT w 487 5.235 -11.988 16.287 .00 51.42 o
ATOM 3360 OWO WAT w 488 19.211 5.233 32.606 .00 48.01 0
ATOM 3361 OWO WAT w 489 3.094 22.345 20.038 .00 47.93 o
ATOM 3362 OWO WAT w 490 15.806 -10.355 6.028 1.00 48.03 0
ATOM 3363 OWO WAT w 491 -6.950 -2.187 14.967 1.00 48.57 0
ATOM 3364 OWO WAT w 492 12.467 21.040 -0.832 1.00 50.56 0
ATOM 3365 OWO WAT w 493 0.205 16.980 -3.263 1.00 49.08 0 ATOM 3366 OWO WAT W 494 -0..236 -13..180 11.,296 1.00 49..99 o
ATOM 3367 OWO WAT W 495 6. .150 -23. .964 20. ,680 1. .00 48. .18 o
ATOM 3368 OWO WAT W 496 13. ,719 7. ,872 -0. ,329 1. .00 48. ,87 o
ATOM 3369 OWO WAT W 497 12. ,209 15. .214 0. .936 1. .00 50. ,57 o
ATOM 3370 OWO WAT W 498 -2. .924 -9. .799 -15. .659 1. ,00 51. .19 o
ATOM 3371 OWO WAT W 499 6. .248 -11. .289 9. .950 1. .00 49. .69 0
ATOM 3372 OWO WAT W 500 17. .344 -18. .775 4. .262 1. .00 50. .03 0
ATOM 3373 OWO WAT W 501 16. .733 -8. ,345 33. .918 1. .00 50. .77 0
ATOM 3374 OWO WAT W 502 18. .913 19. .056 -3. .412 1. .00 52. .40 o
ATOM 3375 OWO WAT W 503 19. .260 -16. .015 -9. .840 1. .00 52. .05 o
ATOM 3376 OWO WAT W 504 27. .834 12. .908 -5. .570 1. .00 53. .02 o
ATOM 3377 OWO WAT W 505 24. .475 -19. .432 26. .879 1. .00 49. .42 o
ATOM 3378 OWO WAT W 506 8. .968 -29. .748 10. .541 1. .00 51. .81 o
ATOM 3379 OWO WAT W 507 11. .867 -10. .300 -5. .857 1. .00 49. .98 0
ATOM 3380 OWO WAT W 508 -0. .894 -7. .386 15. .813 1. .00 53. .61 o
ATOM 3381 OWO WAT W 509 -6. .619 1. .184 16. .728 1. .00 51. .96 0
ATOM 3382 OWO WAT w 510 -7. .892 -6. .118 11. .419 1. .00 51. .35 o
ATOM 3383 OWO WAT w 511 35. .158 3. .849 21. .698 1. .00 49. .52 o
ATOM 3384 OWO WAT w 512 30. .968 1. .931 -2. .551 1. .00 53. .02 0
ATOM 3385 OWO WAT w 513 14. .962 20. .345 -5. .321 1. .00 51. .10 o
ATOM 3386 OWO WAT w 514 10. .299 20. .332 3. .887 1. .00 51. .28 o
ATOM 3387 OWO WAT w 515 9. .136 -4. .930 -14. .241 1. .00 55. .74 0
ATOM 3388 OWO WAT w 516 16, .017 18. .130 16. .960 1. .00 52. .99 0
ATOM 3389 OWO WAT w 517 •10, .226 -2. .977 -7. .939 1. .00 52. .52 o
ATOM 3390 OWO WAT w 518 -7. .913 -1, .057 33. .785 1. .00 55. .56 o
ATOM 3391 OWO WAT w 519 -4. .603 9. .544 27. .704 1. .00 53. .84 o
ATOM 3392 OWO WAT w 520 36, .037 -9. .066 14, .613 1. .00 54. .07 0
ATOM 3393 OWO WAT w 521 -2, .613 -5, .713 -15. .830 1. .00 56. .11 0
ATOM 3394 OWO WAT w 522 22, .102 17, .648 -5, .091 1. .00 55. .53 0
ATOM 3395 OWO WAT w 523 -4. .113 -12, .228 31. .460 1. .00 57, .69 0
ATOM 3396 OWO WAT w 524 12 .219 -5, .923 -5 .197 1. .00 56, .14 o
ATOM 3397 OWO WAT w 525 8. .378 -6 .929 44 .771 1. .00 55, .77 o
ATOM 3398 OWO WAT w 526 21. .973 -11. .541 8. .343 1. .00 58. .28 0
ATOM 3399 OWO WAT w 527 7 .445 -9, .109 -13. .773 1. .00 59. .63 0
ATOM 3400 OWO WAT w 528 6. .357 -28. .394 18. .254 1. .00 58. .45 0
ATOM 3401 OWO WAT w 529 24 .736 -10 .387 1 .413 1. .00 59. .79 0
ATOM 3402 OWO WAT w 530 17 .122 -2. .581 -8 .119 1. .00 59, .43 0
ATOM 3403 OWO WAT w 531 18 .599 -24 .379 17 .004 1. .00 60 .10 o
ATOM 3404 OWO WAT w 532 20 .743 6 .549 24, .623 1. .00 62, .58 o
ATOM 3405 OWO WAT w 533 30 .196 -6 .698 5. .283 1, .00 61, .40 0
ATOM 3406 OWO WAT w 534 30 .992 9. .365 -2. .158 1 .00 62. .44 0
SEQUENCE LISTING
(1) GENERAL INFORMATION: (i) APPLICANT: (A) NAME: NOVO NORDISK A/S
(B) STREET: Novo Alle
(C) CITY: Bagsvaerd
(E) COUNTRY: Denmark
(F) POSTAL CODE (ZIP): DK-2880 (G) TELEPHONE: +45 44 44 88 88
(H) TELEFAX: +45 44 49 32 56
(ii) TITLE OF INVENTION: FAMILY 6 ENDO-1 , 4-BETA-GLUCANASE VARIANTS AND CLEANING COMPOSITIONS CONTAINING THEM
(iii) NUMBER OF SEQUENCES: 4
(iv) COMPUTER READABLE FORM:
(A) MEDIUM TYPE: Floppy disk (B) COMPUTER: IBM PC compatible
(C) OPERATING SYSTEM: PC-DOS/MS-DOS
(D) SOFTWARE: Patentin Release #1.0, Version #1.30 (EPO)
(2) INFORMATION FOR SEQ ID NO: 1: (i) SEQUENCE CHARACTERISTICS:
(A) LENGTH: 1422 base pairs
(B) TYPE: nucleic acid
(C) STRANDEDNESS: single (D) TOPOLOGY: linear
(ii) MOLECULE TYPE: DNA (genomic) (vi) ORIGINAL SOURCE:
(A) ORGANISM: Humicola insolens DSM 1800
(xi) SEQUENCE DESCRIPTION: SEQ ID NO: 1:
ATGGCCAAGT TTTTCCTTAC TGCTGCCTTT GCGGCTGCCG CTCTCGCCGC TCCCGTTGTT 60 GAGGAGCGCC AGAACTGTGC CTCGACTTGG GGCCAGTGCG GTGGCATCGG CTTCAATGGC 120
CCGACTTGCT GCCAGTCTGG TAGCACTTGC GTGAAGCAGA ACGACTGGTA CTCCCAGTGC 180
CTGCCTGGCA GCCAGGTGAC GACGTCGACC ACCTCGAGCT CGTCGACGAC GTCTCGCGCC 240
ACCTCCACCA CCAGCGCTGG TGGCGTGACC TCGATCACCA CTGCTCCCAC CCGCACCGTC 300
ACCATCCCCG GCGGTGCCTC GACCACTGCC AGCTACAACG GCAACCCCTT CGAGGGTGTT 360
CAGCTTTGGG CCAACAACTA CTACCGGTCC GAAGTTCACA CTCTTGCCAT CCCTCAGATC 420
ACTGACCCTG CCCTGAGGGC TGCGGCCTCT GCTGTTGCCG AGGTTCCCAG CTTCCAGTGG 480
CTCGACCGGA ACGTCACCGT CGACACCCTG CTCGTCCAGA CCCTCTCTGA GATCCGCGAG 540
GCGAACCAAG CGGGCGCGAA TCCCCAATAT GCTGCCCAAA TCGTCGTTTA CGACTTGCCT 600
GACCGCGACT GCGCTGCCGC GGCTTCGAAC GGCGAGTGGG CCATCGCCAA CAACGGCGTC 660
AACAACTACA AGGCATACAT CAACCGCATC CGCGAGATTC TCATTTCCTT CTCGGATGTC 720
CGCACCATTC TGGTCATTGA GCCCGACTCG CTGGCCAACA TGGTCACCAA CATGAACGTT 780
CCCAAGTGCA GCGGTGCCGC CTCGACCTAC CGCGAGTTGA CCATCTATGC CCTCAAGCAG 840
CTCGACCTCC CGCACGTCGC CATGTACATG GACGCCGGCC ACGCTGGCTG GCTTGGCTGG 900
CCCGCCAACA TCCAGCCCGC CGCTGAGCTC TTCGCCAAGA TCTACGAGGA TGCCGGCAAG 960
CCCCGCGCCG TCCGCGGTCT CGCCACCAAC GTCGCCAACT ACAACGCCTG GAGCGTCTCG 1020
AGCCCGCCGC CCTACACCAG CCCCAACCCC AACTACGACG AGAAGCACTA CATCGAGGCC 1080
TTCCGCCCCC TCCTCGAGGC CCGCGGCTTC CCCGCCCAGT TCATCGTCGA CCAGGGCCGC 1140
AGCGGCAAGC AGCCCACCGG CCAGAAGGAA TGGGGCCACT GGTGTAATGC TATCGGTACG 1200
GGCTTCGGTA TGCGCCCTAC TGCCAACACC GGCCACCAGT ACGTCGATGC CTTCGTCTGG 1260 GTCAAGCCCG GCGGTGAGTG CGACGGCACC AGCGACACGA CCGCTGCCCG CTACGACTAC 1320
CACTGCGGTC TCGAGGACGC CCTCAAGCCC GCCCCTGAAG CTGGTCAGTG GTTTAATGAA 1380
TATTTTATTC AGTTGCTGCG TAACGCCAAC CCGCCGTTCT AG 1422
(2) INFORMATION FOR SEQ ID NO: 2: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 473 amino acids
(B) TYPE: amino acid
(C) STRANDEDNESS: single
(D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (vi) ORIGINAL SOURCE:
(A) ORGANISM: Humicola insolens DSM 1800
(xi) SEQUENCE DESCRIPTION: SEQ ID NO: 2:
Met Ala Lys Phe Phe Leu Thr Ala Ala Phe Ala Ala Ala Ala Leu Ala
1 5 10 15
Ala Pro Val Val Glu Glu Arg Gin Asn Cys Ala Ser Thr Trp Gly Gin 20 25 30
Cys Gly Gly lie Gly Phe Asn Gly Pro Thr Cys Cys Gin Ser Gly Ser 35 40 45
Thr Cys Val Lys Gin Asn Asp Trp Tyr Ser Gin Cys Leu Pro Gly Ser 50 55 60
Gin Val Thr Thr Ser Thr Thr Ser Ser Ser Ser Thr Thr Ser Arg Ala 65 70 75 80
Thr Ser Thr Thr Ser Ala Gly Gly Val Thr Ser lie Thr Thr Ala Pro
85 90 95
Thr Arg Thr Val Thr lie Pro Gly Gly Ala Ser Thr Thr Ala Ser Tyr 100 105 110 Asn Gly Asn Pro Phe Glu Gly Val Gin Leu Trp Ala Asn Asn Tyr Tyr 115 120 125
Arg Ser Glu Val His Thr Leu Ala He Pro Gin He Thr Asp Pro Ala 130 135 140
Leu Arg Ala Ala Ala Ser Ala Val Ala Glu Val Pro Ser Phe Gin Trp 145 150 155 160
Leu Asp Arg Asn Val Thr Val Asp Thr Leu Leu Val Gin Thr Leu Ser 165 170 175
Glu He Arg Glu Ala Asn Gin Ala Gly Ala Asn Pro Gin Tyr Ala Ala 180 185 190
Gin He Val Val Tyr Asp Leu Pro Asp Arg Asp Cys Ala Ala Ala Ala 195 200 205
Ser Asn Gly Glu Trp Ala He Ala Asn Asn Gly Val Asn Asn Tyr Lys 210 215 220
Ala Tyr He Asn Arg He Arg Glu He Leu He Ser Phe Ser Asp Val 225 230 235 240
Arg Thr He Leu Val He Glu Pro Asp Ser Leu Ala Asn Met Val Thr 245 250 255
Asn Met Asn Val Pro Lys Cys Ser Gly Ala Ala Ser Thr Tyr Arg Glu 260 265 270
Leu Thr He Tyr Ala Leu Lys Gin Leu Asp Leu Pro His Val Ala Met 275 280 285
Tyr Met Asp Ala Gly His Ala Gly Trp Leu Gly Trp Pro Ala Asn He 290 295 300
Gin Pro Ala Ala Glu Leu Phe Ala Lys He Tyr Glu Asp Ala Gly Lys 305 310 315 320 Pro Arg Ala Val Arg Gly Leu Ala Thr Asn Val Ala Asn Tyr Asn Ala 325 330 335
Trp Ser Val Ser Ser Pro Pro Pro Tyr Thr Ser Pro Asn Pro Asn Tyr
340 345 350
Asp Glu Lys His Tyr He Glu Ala Phe Arg Pro Leu Leu Glu Ala Arg 355 360 365
Gly Phe Pro Ala Gin Phe He Val Asp Gin Gly Arg Ser Gly Lys Gin 370 375 380
Pro Thr Gly Gin Lys Glu Trp Gly His Trp Cys Asn Ala He Gly Thr 385 390 395 400
Gly Phe Gly Met Arg Pro Thr Ala Asn Thr Gly His Gin Tyr Val Asp 405 410 415
Ala Phe Val Trp Val Lys Pro Gly Gly Glu Cys Asp Gly Thr Ser Asp
420 425 430
Thr Thr Ala Ala Arg Tyr Asp Tyr His Cys Gly Leu Glu Asp Ala Leu 435 440 445
Lys Pro Ala Pro Glu Ala Gly Gin Trp Phe Asn Glu Tyr Phe He Gin 450 455 460
Leu Leu Arg Asn Ala Asn Pro Pro Phe 465 470
INFORMATION FOR SEQ ID NO : 3 : ( i ) SEQUENCE CHARACTERISTICS :
(A) LENGTH : 1483 base pairs (B) TYPE : nucleic acid
(C) STRANDEDNESS: single
(D) TOPOLOGY: linear
(ii) MOLECULE TYPE: DNA (genomic) (vi) ORIGINAL SOURCE: (A) ORGANISM: Humicola insolens DSM 1800
(xi) SEQUENCE DESCRIPTION: SEQ ID NO: 3:
CCTAGGTCGC CCACCATGCG CGTTTCTCTT GCTCTCCTCG CCTACCTGCT CAGCGCCGCC 60
GGCGCCTCGC CCGTCCCGGA GCTCGAGCCC CGGCAGTCCG GCAACCCCTT CTCCGGCCGC 120
ACCCTGCTGG TCAACTCGGA CTATAGCAGC AAGCTCGACC AGACGCGCCA GGCCTTCCTG 180
TCCCGCGGCG ACCAGACCAA CGCTGCCAAG GTCAAGTACG TCCAGGAGAA GGTTGGCACC 240
TTCTATTGGA TCTCCAACAT CTTCCTCCTG CGCGACATCG ACGTTGCCAT CCAGAATGCG 300
CGCGCCGCCA AGGCCCGCGG CGAGAACCCC ATCGTCGGTC TCGTCCTGTA CAACCTCCCC 360
GACCGCGACT GCAGCGCCGG CGAGTCCTCT GGCGAGCTTA AGCTCTCCCA GAACGGCCTG 420
AACCGGTACA AGAACGAGTA CGTCAACCCG TTCGCCCAGA AGCTCAAGGC CGCGTCCGAC 480
GTGCAGTTCG CCGTCATCCT CGAGCCCGAT GCCATCGGCA ACATGGTCAC GGGCACCAGC 540
GCCTTCTGCC GCAACGCCCG CGGCCCTCAG CAGGAGGCCA TCGGCTATGC TATCTCTCAG 600
CTCCAGGCCA GCCACATCCA CCTCTACCTG GATGTCGCCA ACGGCGGCTG GCTCGGCTGG 660
GCCGATAAGC TCGAGCCAAC TGCCCAGGAG GTCGCCACCA TCCTCCAAAA GGCCGGTAAC 720
AACGCCAAGA TCCGCGGCTT CTCCAGCAAC GTCTCCAACT ACAACCCCTA TTCCACCAGC 780
AACCCGCCGC CCTACACCTC GGGCAGCCCG TCGCCCGACG AGTCGCGCTA CGCCACCAAC 840
ATCGCCAACG CCATGCGCCA GCGCGGCCTG CCGACCCAGT TCATCATCGA CCAGAGCCGC 900
GTCGCGCTCA GCGGCGCCCG CAGCGAGTGG GGCCAATGGT GCAACGTGAA CCCCGCCGGC 960
TTCGGCCAGC CCTTCACCAC CAACACCAAC AACCCCAACG TCGACGCCAT CGTCTGGGTC 1020
AAGCCCGGCG GCGAGTCGGA CGGCCAGTGC GGCATGGGCG GCGCCCCGGC CGCCGGCATG 1080 TGGTTCGACG CGTACGCGCA GATGCTGACG CAGAACGCCC ACGACGAGAT CGCCCGCGGC 1140
GCTGCCGGCA GTGGTGGTGG CAACAACGGC GGCGGCAACA ACCCCAACCC GACCCCGACC 1200
AACCCGACAA ACCCGGGCCC GACCAGCAAC CCGGGCGGCG GCAACTGCGC CAGCAAGTGG 1260
GGCCAGTGCG GTGGTCAGGG ATGGGCCGGC CCGACCTGCT GCGAGGCTGG GTCGACTTGC 1320
ACCCGCCAGA ACGAGTGGTA CTCACAGTGC CTGTAAAGAA AAAAGAGTGC GGTTGCTGTC 1380
ACGGGTGTGA CGTTGTATAT AGCACGTCCC CGGTTAGGCT TTAGAGCACA CTGGCGGCCG 1440
CTCGAGCATG CATCTAGAGG GTGACTGACA CCTGGCGGTA GAC 1483
(2) INFORMATION FOR SEQ ID NO: 4: (i) SEQUENCE CHARACTERISTICS:
(A) LENGTH: 446 amino acids
(B) TYPE: amino acid (C) STRANDEDNESS: single
(D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (vi) ORIGINAL SOURCE:
(A) ORGANISM: Humicola insolens DSM 1800
(xi ) SEQUENCE DESCRIPTION : SEQ ID NO : 4 :
Met Arg Val Ser Leu Ala Leu Leu Ala Tyr Leu Leu Ser Ala Ala Gly 1 5 10 15
Ala Ser Pro Val Pro Glu Leu Glu Pro Arg Gin Ser Gly Asn Pro Phe 20 25 30
Ser Gly Arg Thr Leu Leu Val Asn Ser Asp Tyr Ser Ser Lys Leu Asp 35 40 45
Gin Thr Arg Gin Ala Phe Leu Ser Arg Gly Asp Gin Thr Asn Ala Ala 50 55 60 Lys Val Lys Tyr Val Gin Glu Lys Val Gly Thr Phe Tyr Trp He Ser 65 70 75 80
Asn He Phe Leu Leu Arg Asp He Asp Val Ala He Gin Asn Ala Arg 85 90 95
Ala Ala Lys Ala Arg Gly Glu Asn Pro He Val Gly Leu Val Leu Tyr 100 105 110
Asn Leu Pro Asp Arg Asp Cys Ser Ala Gly Glu Ser Ser Gly Glu Leu 115 120 125
Lys Leu Ser Gin Asn Gly Leu Asn Arg Tyr Lys Asn Glu Tyr Val Asn 130 135 140
Pro Phe Ala Gin Lys Leu Lys Ala Ala Ser Asp Val Gin Phe Ala Val 145 150 155 160
He Leu Glu Pro Asp Ala He Gly Asn Met Val Thr Gly Thr Ser Ala 165 170 175
Phe Cys Arg Asn Ala Arg Gly Pro Gin Gin Glu Ala He Gly Tyr Ala 180 185 190
He Ser Gin Leu Gin Ala Ser His He His Leu Tyr Leu Asp Val Ala 195 200 205
Asn Gly Gly Trp Leu Gly Trp Ala Asp Lys Leu Glu Pro Thr Ala Gin 210 215 220
Glu Val Ala Thr He Leu Gin Lys Ala Gly Asn Asn Ala Lys He Arg 225 230 235 240
Gly Phe Ser Ser Asn Val Ser Asn Tyr Asn Pro Tyr Ser Thr Ser Asn 245 250 255
Pro Pro Pro Tyr Thr Ser Gly Ser Pro Ser Pro Asp Glu Ser Arg Tyr 260 265 270 Ala Thr Asn He Ala Asn Ala Met Arg Gin Arg Gly Leu Pro Thr Gin 275 280 285
Phe He He Asp Gin Ser Arg Val Ala Leu Ser Gly Ala Arg Ser Glu 290 295 300
Trp Gly Gin Trp Cys Asn Val Asn Pro Ala Gly Phe Gly Gin Pro Phe 305 310 315 320
Thr Thr Asn Thr Asn Asn Pro Asn Val Asp Ala He Val Trp Val Lys
325 330 335
Pro Gly Gly Glu Ser Asp Gly Gin Cys Gly Met Gly Gly Ala Pro Ala 340 345 350
Ala Gly Met Trp Phe Asp Ala Tyr Ala Gin Met Leu Thr Gin Asn Ala 355 360 365
His Asp Glu He Ala Arg Gly Ala Ala Gly Ser Gly Gly Gly Asn Asn 370 375 380
Gly Gly Gly Asn Asn Pro Asn Pro Thr Pro Thr Asn Pro Thr Asn Pro 385 390 395 400
Gly Pro Thr Ser Asn Pro Gly Gly Gly Asn Cys Ala Ser Lys Trp Gly
405 410 415
Gin Cys Gly Gly Gin Gly Trp Ala Gly Pro Thr Cys Cys Glu Ala Gly 420 425 430
Ser Thr Cys Thr Arg Gin Asn Glu Trp Tyr Ser Gin Cys Leu 435 440 445

Claims

1. Cleaning composition comprising one or more enzymes having cellulolytic activity wherein at least 25% of the total weight of cellulolytic active protein derives from the presence of a
Humicola endo-1, 4-╬▓-glucanase or Humicola-like cellulase of the glycosyl hydrolase family 6.
2. Cleaning composition according to claim 1, wherein the Humi- cola-like cellulase comprises a catalytically core domain which has an amino acid sequence being at least 35% homologous to SEQ ID NO: 4.
3. Cleaning composition according to claim 1 or 2 , wherein the endo-l,4-╬▓-glucanase comprises one or two cellulose binding domains (CBD) operably linked to the catalytically active domain.
4. Cleaning composition according to any of the claims 1-3 wherein the composition is a detergent composition.
5. Cleaning composition according to claim 4 wherein the detergent composition comprises one or more components selected from anionic, nonionic, cationic, amphoteric, ampholytic and zwitterionic surfactants, bleaching agents, additional enzymes, sud suppressores, dispersants, soil suspension and anti-redeposition agents, smectite clays, and builder components.
6. Cleaning composition according to claim 4 or 5 wherein the detergent composition is a granular detergent composition con- taining no more than 40% by weight of inorganic filler salt.
7. Cleaning composition according to claim 6 wherein the granular detergent composition contains no more than 15% by weight of inorganic filler salt.
8. Cleaning composition according to claim 5 wherein the detergent composition is a heavy duty liquid composition.
9. Cleaning composition according to any of the claims 4-8 wherein the enzymes are selected from the group consisting of proteases, cellulases, ╬▓-glucanases, hemicellulases, lipases, peroxidases, laccases, ╬▒-amylase, glucoamylases, cutinases, 5 pectinases, reductases, oxidases, phenoloxidases, ligninases, pullulanases, arabinosidases or mixtures thereof.
10. Cleaning composition according to any of the claims 4-9 which is a laundry detergent additive.
10
11. Cleaning composition according to any of the claims 1-3 wherein the composition is a fabric softener or fabric conditioning composition for the treatment of fabrics.
15 12. Cleaning composition according to claim 11 wherein the fabric softener composition comprises from about 1% to about 90% of one or more cationic fabric softening agents, nonionic fabric softening agents, or mixtures thereof.
20 13. Cleaning composition according to claim 12 comprising from about 2% to about 50% by weight of one or more fabric softening agents .
14. Cleaning composition according to claim 12 or 13 wherein the 25 cationic fabric softening agents comprise quaternary ammonium softening agent or amine precursor thereof.
15. Cleaning composition according to claim 14 wherein the quaternary ammonium softening agent is N,N-di (2-tallowoyl-oxy-
30 ethyl) -N,N-dimethyl ammonium chloride.
16. Cleaning composition according to any of the claims 1-15 wherein endo-1, 4-╬▓-glucanase is derived or derivable from the fungus Orpinomyce╬╡ ╬╡p.
35
17. Cleaning composition according to any of the claims 1-15 wherein endo-1, 4-╬▓-glucanase is derived or derivable from the fungus Neocallima╬╡tix patriciarum .
18. Cleaning composition according to any of the claims 1-15 wherein endo-1, 4-╬▓-glucanase is derived or derivable from the fungus Trichoderma ree╬╡ei .
5
19. Cleaning composition according to any of the claims 1-15 wherein endo-1, 4-╬▓-glucanase is derived or derivable from the fungus Fu╬╡arium oxy╬╡porum .
10 20. Cleaning composition according to any of the claims 1-19 which comprises the family 6 endo-1, 4-╬▓-glucanase in an amount corresponding to from about 1 ECU to about 100000 ECU per liter washing or rinsing solution.
15 21. Cleaning composition according to any of the claims 1-20 which further comprises an endo-1, 4-╬▓-glucanase of the glycosyl hydrolase family 5, or an endo-1, 4-╬▓-glucanase of the glycosyl hydrolase family 7, or an endo-1, 4-╬▓-glucanase of the glycosyl hydrolase family 8, or an endo-l,4-╬▓-glucanase of the glycosyl
20 hydrolase family 9, or an endo-1, 4-╬▓-glucanase of the glycosyl hydrolase family 44, or an endo-l,4-╬▓-glucanase of the glycosyl hydrolase family 45, or an endo-1, 4-╬▓-glucanase of the glycosyl hydrolase family 48, or an endo-1, 4-╬▓-glucanase of the glycosyl hydrolase family 12 optionally being operably linked to a cellu- 25 lose binding domain, or any mixture thereof.
22. A process for machine treatment of fabrics which process comprises treating fabric during a rinse cycle of a machine washing process with a rinse solution containing the composition
30 according to any of the claims 11-21.
23. A method of constructing a variant of a parent Humicola fami 1' 6 endo-beta-l,4-glucanase, which variant has endo-beta-1,4- glucanase activity and improved detergent compability as compared
35 to the parent endo-beta-l,4-glucanase, which method comprises i) analysing the structure of the parent Humicola family 6 endo- beta-1,4-glucanase to identify at least one amino acid residue or at least one structural part of the Humicola family 6 endo-beta- 5 1,4-glucanase catalytically core domain structure, which amino acid residue or structural part is believed to be of relevance for altering the detergent compatibility of the parent Humicola family 6 endo-beta-1, 4-glucanase as evaluated on the basis of structural or functional considerations, 10 ii) constructing a Humicola family 6 endo-beta-l,4-glucanase variant, which as compared to the parent Humicola family 6 endo- beta-l,4-glucanase has been modified in the amino acid residue or structural part identified in i) so as to alter the detergent 15 compatibility, and, optionally,
iii) testing the resulting Humicola family 6 endo-beta-1,4- glucanase variant with respect to detergent compatibility.
20 24. The method according to claim 23, wherein the structural part to be modified is the binding cleft, the loop region encompassing the binding cleft, or the side chain of the catalytic acid Aspl39.
25. A variant of a parent Humicola family 6 endo-beta-1,4-
25 glucanase, which comprises a mutation in a position corresponding to at least one of the following positions in SEQ ID NO: 4: K20, S56, S94, A95, K103, A182, N183 and Q318.
26. The variant according to claim 25, which comprises at least 30 one of the mutations:
K20E S56D S94D A95G 35 K103E K103Q A182G N183E A182G+N183H Q318E
27. A method of constructing a variant of a parent Humicola-like family 6 cellulase, which variant has endo-beta-1,4-glucanase activity and improved detergent compatibility as compared to the parent cellulase, which method comprises i) comparing the three-dimensional structure of the Humicola endo- beta-l,4-glucanase with the structure of a Humicola-like cellulase, ii) identifying a part of the Humicola-like cellulase structure which is different from the Humicola endo-beta-1, 4-glucanase structure and which from structural or functional considerations is contemplated to be responsible for differences in the detergent compatibility of the Humicola endo-beta-1, 4-glucanase and Humicola-like cellulase, iii) modifying the part of the Humicola-like cellulase identified in ii) whereby a Humicola-like endo-beta-l,4-glucanase variant is obtained, which has an improved detergent compatibility compared to the parent Humicola-like cellulase , and optionally, iv) testing the resulting Humicola-like endo-beta-1,4-glucanase variant with respect to detergent compatibility.
28. The method according to claim 27, wherein, in step iii), the part of the Humicola-like cellulase is modified so as to resemble the corresponding part of the Humicola family 6 endo-beta-1,4- glucanase.
29. The method according to claim 27 or 28, wherein, in step iii), the modification is accomplished by deleting one or more amino acid residues of the part of the Humicola-like cellulase to be modified; or the modification is accomplished by replacing one or more amino acid residues of the part of the Humicola-like cellulase to be modified with the amino acid residues occupying corresponding positions in the Humicola endo-beta-1,4-glucanase; ΓÇó or the modification is accomplished by insertion of one or more amino acid residues present in the Humicola endo-beta-1,4- glucanase into a corresponding position in the Humicola-like cellulase.
30. The method according to any of claims 27-29, wherein the Humicola-like cellulase is selected from the group consisting of Neocallima╬╡tix patriciarum endo-beta-1,4-glucanase, Orpinomyce╬╡ ╬╡p. endo-beta-1,4-glucanase, Trichoderma re╬╡eei exoglucanase, Agaricu╬╡ bi╬╡pora exoglucanase, Phanerochaete chry╬╡o╬╡porium exoglucanse, Penicillium purpurogenum exoglucanase, Acremonium cellulyticu╬╡ exoglucanase, Fu╬╡arium oxy╬╡porum exoglucanase and homologues thereof.
10
31. The method according to claim 23 or 27, wherein the parent Humicola endo-beta-1, 4-glucanase is derived from a strain of Humicola in╬╡olen╬╡ .
15 32. The method according to claim 31, wherein the parent Humicola endo-beta-l,4-glucanase is derived from Humicola in╬╡olen╬╡, DSM 1800.
33. An isolated polynucleotide molecule comprising a DNA sequence 20 encoding an endo-beta-1, 4-glucanase variant according to claim 26.
34. A recombinant expression vector which carries the polynucleotide molecule according to claim 33.
25 35. A cell which is transformed with the polynucleotide molecule according to claim 33 or a vector according to claim 34.
36. The cell according to claim 35, which is a microorganism.
30 37. The cell according to claim 36, which is a bacterium or a fungus .
38. A cell according to claim 37, which is a Fu╬╡arium oxy╬╡porum, an A╬╡pergillu╬╡ niger or an A╬╡pergillu╬╡ oryzae cell.
35
39. Cleaning composition comprising an endo-beta-1, 4-glucanase which is constructed using the method according to any of the claims 23, 24 and 27-32.
EP98929249A 1997-07-04 1998-07-02 FAMILY 6 ENDO-1,4-$g(b)-GLUCANASE VARIANTS AND CLEANING COMPOSIT IONS CONTAINING THEM Withdrawn EP1002061A1 (en)

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