EP2205756A2 - Methods of identifying modulators of an ehd polypeptide - Google Patents

Abstract

The invention relates to a method of identifying a modulator of an EHD family polypeptide, said method comprising (i) providing a first and second sample of an EHD polypeptide; (ii) contacting said first sample with a candidate modulator; (iii) contacting said first and second samples with ATP; and (iv) monitoring ATP hydrolysis in said first and second samples, wherein a difference between the ATP hydrolysis in said first and second samples identifies said candidate modulator as a modulator of an EHD family polypeptide. The invention also relates to methods of modelling molecules and to various EHD mutant polypeptides.

Description

METHODS

FIELD OF THE INVENTION

The invention relates to the field of EHD polypeptides and their structure and/or biological function(s).

BACKGROUND TO THE INVENTION

The ability to actively remodel membranes in response to nucleotide hydrolysis has largely been attributed to GTPases of the dynamin superfamily, and these have i been extensively studied . Epsin homology (EH) domain-containing proteins

(EHDs/Rme-1/pincher) comprise a less characterised class of highly conserved

2 eukaryotic ATPases implicated in clathrin-independent endocytosis , and recycling

3,4 from endosomes .

The dynamin superfamily of large GTPases are multi-domain proteins that include the classical dynamins (Dynl, Dyn2, Dyn3), dynamin-related proteins (Mx i proteins, Dip, OPA and mitofusins) and the GBP/atlastin family . The proteins have an amino-(N-)terminal guanine nucleotide binding domain (G-domain) with a low affinity for nucleotides which is followed by a helical (or middle) domain. Additional domains are involved in membrane-binding and recruitment to sites of activation. Dynamin is the best characterised member where oligomerisation- stimulated GTP hydrolysis has been proposed to lead to scission of clathrin-coated

5-8 vesicles . Other superfamily members can function in membrane tubulation and membrane scission or fusion.

EHDs comprise a highly conserved eukaryotic protein family with four members (EHD 1-4) in mammals and a single member in C. elegans, D. melanogaster and many eukaryotic parasites such as Plasmodium, Leishmania and Entamboeba. The proteins have a molecular mass of approximately 6OkD and contain an N-terminal G-domain, followed by a helical domain and a C-terminal EH-domain (Fig. Ia), although in plant homologues the EH-domain is N-terminal. The EH-domain is known to interact with asparagine-proline-phenylalanine (NPF) motifs in proteins involved in endocytosis. EHD polypeptide structure is poorly understood in the art. EHD polypeptides are regarded as GTPases in the art. EHD biological functions are largely unknown in the art. The macromolecular behaviour of EHD polypeptides is incompletely understood in the art. The design or selection/screening for inhibitors or activators of EHD is not possible based on the inadequate information regarding the structure/function of EHD in the art.

The present invention seeks to overcome problem(s) associated with the prior art.

SUMMARY OF THE INVENTION

EHD proteins are known by sequence analysis to contain a guanine nucleotide binding domain (G-domain). It has been suggested that EHD might bind to adenine nucleotides, with the attendant possibility that such nucleotides might be hydrolysed by the protein. However, there has been no accurate scientific study to date which reliably attributes ATP hydrolysis to a G domain. In the prior art, cross-nucleotide activities of that nature are typically attributed to contamination effects. The prior art view is very clearly established that G-domains have guanine nucleotide binding and/or guanine nucleotide hydrolysis activities.

The present inventors have crystallised and have studied the structure of EHD2 in unprecedented detail. This has led to a number of structural and mechanistic insights into the biology of EHD family polypeptides. A key finding is that EHD family polypeptides are in fact ATP binding polypeptides. Furthermore, we disclose how ATP binds to those polypeptides. In addition, the structural insights allowed a modelling of the likely mechanism of ATP hydrolysis by EHD. family polypeptides, which hypothesis has been demonstrated to be accurate by mutational studies of the ATP ase activity.

The invention is based on these surprising findings. In one aspect, the invention relates to a method of identifying a modulator of an EHD family polypeptide, said method comprising

(i) providing a first and second sample of an EHD polypeptide;

(ii) contacting said first sample with a candidate modulator; (iii) contacting said first and second samples with ATP; and

(iv) monitoring ATP hydrolysis in said first and second samples, wherein a difference between the ATP hydrolysis in said first and second samples identifies said candidate modulator as a modulator of an EHD family polypeptide.

Suitably if hydrolysis of ATP is greater in said first sample than in said second sample then the candidate modulator is identified as an enhancer of EHD family polypeptide activity.

Suitably if hydrolysis of ATP is lower in said first sample than in said second sample then the candidate modulator is identified as an inhibitor of EHD family polypeptide activity.

Suitably ATP hydrolysis is monitored in the presence of lipid. Suitably said lipid is in the form of liposomes. Suitably said lipid is in the form of phosphatidylserine (PS) at a final concentration of about 10%.

In another aspect, the invention relates to a method as described above further comprising the step of providing a further sample of EHD family polypeptide, said further sample comprising an EHD family polypeptide bearing a T94A mutation, said further sample being used to determine the reference or background level of spontaneous ATP hydrolysis.

In another aspect, the invention relates to a method as described above further comprising the step of providing a further sample of EHD family polypeptide, said further sample comprising an EHD family polypeptide bearing an I157Q mutation, said further sample being used to determine the reference level of ATP hydrolysis in the absence of lipids. In another aspect, the invention relates to a method as described above further comprising the step of providing a further reference sample, said further reference sample comprising a dynamin polypeptide together with GTP nucleotide and candidate modulator, said further sample being used to determine whether the candidate modulator has an EHD-specifϊc effect, or whether it is also capable of affecting dynamin GTPase activity.

In another aspect, the invention relates to a crystalline EHD family polypeptide, said polypeptide being bound to an adenosine nucleotide or an analogue thereof.

In another aspect, the invention relates to a EHD polypeptide having the structure defined by the structural coordinates as shown in Table A.

In another aspect, the invention relates to a method for identifying a candidate modulator of EHD family polypeptide activity, said method comprising

(i) providing a molecular modelling apparatus with a set of structural coordinates of an EHD family polypeptide selected from those shown in Table A;

(ii) providing said molecular modelling apparatus with a set of structural coordinates of a molecular entity of interest; and

(iii) determining whether the molecular entity of interest is expected to bind to or to affect the structure of said EHD family polypeptide, wherein an expectation of binding or affecting the structure of said EHD family polypeptide identifies said molecular entity of interest as a candidate modulator of EHD family polypeptide activity.

A molecular modelling apparatus is suitably a computer programmed with the appropriate tools for molecular modelling. Suitable programs/tools are noted in the examples section. .

Suitably the structural coordinates of at least the EH-domain are selected. The first crystal structure of an EH domain is presented herein - in the prior art only low resolution NMR structural information has been available. The crystal structure of the EH domain enables it to be effectively targeted, for example to find or test inhibitors of the interaction with the NPF motifs of the target cargo.

Suitably the structural coordinates of at least the G-domain are selected.

Suitably the structural coordinates of at least the dimerisation interface are selected.

Suitably the structural coordinates of the oligomerisation interface are selected. In particular, reference is made to figure 4a and b where key residues in oligomerisation are set out and in particular four residues are shown to abolish oligomerisation (E91Q, R167E, K193D, D198R). Thus, in modelling or studying the oligomerisation domain, attention should be advantageously focussed on those residues and their contribution to the structure.

Suitably the structural coordinates of at least the membrane binding site are selected.

The sites mentioned are described in more detail below, for example with reference to figure Ia.

Suitably each of the structural coordinates of Table A are selected.

In another aspect, the invention relates to a method for identifying a candidate therapeutic agent, said method comprising application of rational drug design to the crystal structure of EHD2.

Rational design of candidate agents likely to be able to interact with the target i protein may be based upon structural studies of the molecular shapes of the target protein as disclosed herein. These will provide guidance as to which amino acid residues form molecular contact regions. In another aspect, the invention relates to a method of manufacturing a modulator of an EHD family polypeptide, said method comprising identifying a candidate modulator as described above, and synthesising a quantity of said modulator. ■ . ^{• ■}

The candidate therapeutic agent (or candidate modulator or molecular entity of interest (interchangeably referred to as 'agent' below)) may be an organic compound or other chemical. The agent may be a compound, which is obtainable from or produced by any suitable source, whether natural or artificial. The agent may be an amino acid molecule, a polypeptide, or a chemical derivative thereof, or a combination thereof. The agent may even be a polynucleotide molecule - which may be a sense or an anti-sense molecule. The agent may be an antibody. The agent may be designed or obtained from a library of compounds, which may comprise peptides, as well as other compounds, such as small organic molecules. By way of example, the agent may be a natural substance, a biological macromolecule, or an extract made from biological materials such as bacteria, fungi, or animal (particularly mammalian) cells or tissues, an organic or an inorganic molecule, a synthetic agent, a semi-synthetic agent, a structural or functional mimetic, a peptide, a peptidomimetic, a derivatised agent, a peptide cleaved from a whole protein, or a peptide synthesised synthetically (such as, by way of example, either using a peptide synthesiser or. by recombinant techniques or combinations thereof, a recombinant agent, an antibody, a natural or a non-natural agent, a fusion protein or equivalent thereof and mutants, derivatives or combinations thereof). Typically, the agent will be an organic compound. Typically, the organic compounds will comprise two or more hydrocarbyl groups. Here, the term "hydrocarbyl group" means a group comprising at least C and H and may optionally comprise one or more other suitable substituents. Examples of such substituents may include halo-, alkoxy-, nitro-, an alkyl group, a cyclic group etc.. In addition to the possibility of the substituents being a cyclic group, a combination of substituents may form a cyclic group. If the hydrocarbyl group comprises more than one C then those carbons need not necessarily be linked to each other. For example, at least two of the carbons may be linked via a suitable element or group. Thus, the hydrocarbyl group may contain hetero atoms. Suitable hetero atoms will be apparent to those skilled in the art and include, for instance, sulphur, nitrogen and oxygen. For some applications, preferably the agent comprises at least one cyclic group. The cyclic group may be a polycyclic group, such as a non-fused polycyclic group. For some applications, the agent comprises at least the one of said cyclic groups linked to another hydrocarbyl group. The agent may be in the form of a pharmaceutically acceptable salt - such as an acid addition salt or a base salt — or a solvate thereof, including a hydrate thereof. For a review on suitable salts see Berge et al, (1977) J. Pharm. Sd. 66, 1- 19.

In another aspect, the invention relates to use of a candidate modulator of EHD family polypeptide activity identified as described above, wherein said EHD family polypeptide is EHD2, in the manufacture of a medicament for diabetes. . .

In another aspect, the invention relates to use of the atomic coordinates as shown in Table A in the modelling of an EHD family polypeptide.

In another aspect, the invention relates to a method for the design of one or more ligands of an EHD family polypeptide, said method comprising the use of coordinates as shown in Table A.

In another aspect, the invention relates to use of an EHD family polypeptide in the tabulation of a biological membrane.

In another aspect, the invention relates to a method of tubulating a biological membrane comprising contacting said membrane with an EHD family polypeptide.

In another aspect, the invention relates to a method as described above or a use as described above wherein said membrane is comprised by a liposome. Suitably said membrane comprises phosphatidylserine (PS). In another aspect, the invention relates to use of an EHD family polypeptide in membrane scission.

In another aspect, the invention relates to a method of inducing membrane scission, said method comprising contacting said membrane with an EHD family polypeptide. Suitably said method further comprises contacting said membrane- EHD family polypeptide complex with nucleotide in conditions permissive of nucleotide hydrolysis. Suitably said nucleotide is adenosine triphosphate (ATP).

Mutating has it normal meaning in the art and may refer to the substitution or truncation or deletion of the residue, motif or domain referred to. Mutation may be effected at the polypeptide level e.g. by synthesis of a polypeptide having the mutated sequence, or may be effected at the nucleotide level e.g. by making a nucleic acid encoding the mutated sequence, which nucleic acid may be - subsequently translated to produce the mutated polypeptide. Where no amino acid is specified as the replacement amino acid for a given mutation site, suitably alanine (A) is used.

In another aspectythe invention relates to a method of inhibiting dimerisation of an EHD family polypeptide, said method comprising mutating amino acid W238 of said polypeptide. In another aspect, the invention relates to a method of inhibiting dimerisation of an EHD family polypeptide, said method comprising mutating amino acids neighbouring W238 of said polypeptide, such as amino acids within

10 residues either side of W238, or amino acid residues within 5 residues either side of W238, or the immediate neighbouring residues of W238 (i.e. residues 237 and/or 239).

In another aspect, the invention relates to a method of modifying an EHD family polypeptide to permit guanine nucleotide binding thereto, said method comprising mutating said EHD polypeptide at one or more amino acid residues within the region Hl 92 to M223, wherein said mutation alleviates steric exclusion of an amino group at carbon 2 of said guanine nucleotide. In another aspect, the invention relates to a method of modifying an EHD family polypeptide to reduce or prevent membrane binding, said method comprising mutating any of K324, K327, K328, K329, K334, K341, V321 or F322. Suitably amino acid V321 and/or F322 is mutated — these are considered to have similar effects.

In another aspect, the invention relates to a method of modifying an EHD family polypeptide to reduce or prevent membrane binding, said method comprising mutating any of K324, K327, K328, K329 or F322. Suitably amino acid F322 is mutated.

hi another aspect, the invention relates to a method of modifying an EHD family polypeptide to reduce or prevent ATP hydrolysis by said polypeptide, said method comprising mutating amino acid T72A or T94 of said polypeptide, suitably T94.

In another aspect, the invention relates to a method of modifying an EHD family polypeptide to reduce or prevent breakdown of membrane structures by said polypeptide, said method comprising mutating amino acid T72 A or T94 of said polypeptide, suitably T94.

In another aspect, the invention relates to a method of modifying an EHD family polypeptide to increase ATP hydrolysis, such as to increase intrinsic ATP hydrolysis, by said polypeptide, said method comprising mutating amino acid 1157 of said polypeptide.

hi another aspect, the invention relates to a method of modifying an EHD family polypeptide to enhance breakdown of membrane structures by said polypeptide, said method comprising mutating amino acid 1157 of said polypeptide. ,

Suitably said 1157 is mutated to N, R or Q. Suitably said 1157 is mutated to Q. In another aspect, the invention relates to a method of inducing membrane fission, said method comprising contacting said membrane with an EHD family polypeptide comprising an Il 57Q mutation.

In another aspect, the invention relates to a method of modifying an EHD family polypeptide to reduce or abolish assembly stimulated ATP hydrolysis, said method comprising mutating said EHD polypeptide at E91, R167, K193, D198, F122, F 128, or by deletion of the EH domain. Suitably said mutation(s) comprise one or more of the mutations set out in Figure 4b.

In another aspect, the invention relates to an EHD family polypeptide or fragment thereof comprising one or more of the following mutations: (i) T94A; (ii) I157Q; and (iii) F322A.

A fragment is suitably at least 10 amino acids in length, suitably at least 25 amino acids, suitably at least 50 amino acids, suitably at least 100 amino acids, suitably at least 200 amino acids, suitably the majority of the EHD polypeptide of interest. Suitably a fragment comprises a whole motif or a whole domain of the EHD polypeptide of interest. Suitably a fragment comprises at least 10 amino acids either side of the given mutation of interest. When more than one mutation is discussed, suitably a fragment comprises at least 10 amino acids each side of the two or more mutations, and suitably further comprises the intemvening amino acid sequence too. Where a mutation is within 10 amino acids of the end of the polypeptide then suitably the fragment comprises the amino acids between said mutation and said end (e.g. the N- or C- terminus).

In another aspect, the invention relates to a method of destabilising a membrane, said method comprising contacting said membrane with a EHD family polypeptide and a nucleotide under conditions permissive of nucleotide hydrolysis. In another aspect, the invention relates to an EHD family polypeptide comprising one or more of the mutations described herein.

Suitably said EHD family polypeptide or fragment thereof is or is derived from mammalian EHD2.

DETAILED DESCRIPTION OF THE INVENTION

The invention provides architectural and mechanistic insights into an EHD ATPase involved in membrane remodeling. Here we show that epsin homology (EH) domain-containing proteins (EHDs) share many common features with the dynamin superfamily such as low affinity to nucleotides, the ability to tubulate liposomes in vitro, to oligomerise around lipid tubules in ring-like structures and to stimulate nucleotide hydrolysis in response to lipid binding. We present the structure of EHD2, bound to a non-hydrolysable ATP analogue, and provide evidence that EHDs are involved in nucleotide-dependent membrane scission in vivo. The nucleotide-binding domain is involved in dimerisation which creates a highly curved membrane-binding region. Oligomerisation of dimers occurs on another nucleotide-binding domain interface, and this allows us to model the EHD oligomer. We discuss the functional implications of the EHD2 structure for an understanding of membrane deformation.

Dynamins are distinguished from classical signalling GTPases by their large size, their low affinity for nucleotide and assembly-stimulated nucleotide hydrolysis. From studies of GBPl, dynamin, bacterial dynamin-like protein, and particularly the insights into EHD disclosed herein, it appears that the mechanism of assembly- stimulated nucleotide hydrolysis is also conserved. In cases where data are available assembly involves the same conserved interface in the G-domain, with the same orientation of G-domains, a phosphate cap and an activation mechanism which is dependent on a catalytic serine or- threonine from switch I. This mechanism is different for the signal-recognition particle and its receptor where the nucleotides are found anti-parallel in the dimer and GTP hydrolysis involves catalysis by the 2'-hydroxyl group of opposing nucleotides. This assembly- stimulated GTP hydrolysis mechanism has likely been maintained across the dynamin superfamily.

We disclose the first molecular understanding of two separate interfaces in the G- domain which allow us to propose how oligomers are assembled. The structure, the architecture of the membrane interaction site and the proposed oligomerisation mechanism disclosed herein each provide an initial framework to understand the . membrane remodelling function for the EHD family. EHD2 initially interacts with membrane via ionic interactions, and we disclose that the insertion of the conserved F322 at the tip of the helical domain will induce local curvature stress in the membrane. Furthermore, the highly curved membrane interaction site hi the EHD oligomer is along the flat dimension of the lipid tubule, perpendicular to its curvature (see examples and Fig. 13b), and therefore EHD2 binding will create additional curvature stress on the membrane. Both factors are likely to contribute to membrane destabilisation, a prerequisite for membrane fission and fusion. We also disclose that nucleotide hydrolysis is most likely leading to membrane scission in vivo, and thus conformational changes induced by nucleotide hydrolysis are leading to further membrane destabilisation. .

hi another aspect, the invention may be useful in the attachment of entities to biological membranes. For example, the invention may relate to a method of attaching an entity to a biological membrane, the method comprising attaching said entity to a membrane binding element of an EHD family protein, and contacting the resulting complex with a biological membrane.

The invention may involve use of an EHD family polypeptide in the hydrolysis of ATP.

A biological membrane is typically a lipid bilayer membrane. An example of a biological membrane is a plasma membrane. More in particular, the biological membranes of the invention are often intracellular membranes, for example those involved in vesicle trafficking, or those forming a part of the endocytic recycling compartment. The term liposome has its normal meaning in the art, namely a single or multi laminar vesicle. Liposomes may be made from lecithins or other lipids. Preferably liposomes are made from brain derived lipids. Preferably liposomes are made from Folch extract. In some embodiments, liposomes may be made from 100% anionic phosphatidyl serine (PS) liposomes (it is to be noted that this 100% refers to the composition of the liposomes in this particular embodiment and should not infer the proportion of lipid present overall which is discussed elsewhere herein). Suitably liposomes may contain phosphatidyl inositol 4,5 bisphosphate (PEP2).

When the invention that, is used in the tubulation of liposomes, preferably this takes place in vitro. .

EHD FAMILY POLYPEPTIDES EHDs comprise a highly conserved eukaryotic protein family. EHDs have a molecular mass of approximately 60KD.. EHD proteins contain a G domain, a helical domain, and a EH domain. Typically these domains occur in the order N terminus - G domain - helical domain - EH domain - C terminus. However, it should be noted that in plant EHDs, the EH domain may be at the N terminus.

For a polypeptide to be considered as an EHD family polypeptide, it should possess one or more of the above characteristics. More suitably, it should possess sufficient sequence identity to EHD1/2/3/4 to be classified in the same molecular family. Most suitably, it should be a mammalian EHD polypeptide. Most suitably, it should comprise mammalian EHD2 amino acid sequence. In particular, an exemplary EHD family polypeptide has the sequence shown as mmEHD2 in figure 8.

When particular amino acid residues are referred to using numeric addresses, the numbering is taken using mouse EHD2 (mmEHD2) amino acid sequence as the reference sequence. This is to be used as is well understood in the art to locate the residue of interest. This is not always a strict counting exercise — attention must be paid to the context. For example, if the protein of interest such as human EHD2.is of a slightly different length, then location of the correct residue in the human sequence correseponding to (for example) T94 may require the sequences to be aligned and the equivalent or corresponding residue picked, rather than simply taking the 94^th residue of the sequence of interest. This is well within the ambit of the skilled reader. In the unlikely event that any further guidance is needed, reference is made to figure 8 which presents a comprehensive alignment of sequences of interest with the reference sequence mrnEHD2 at the top which both illustrates the principle and provides a robust reference chart for ease of location of the correct residues.

It will be apparent to the skilled reader that the invention is exemplified predominantly by reference to EHD2. It should be noted that EHD2 exhibits high sequence homology with other EHD family polypeptides. Thus, in some aspects the invention relates to the use of EHD2 in the development of therapeutics for application to other EHD family proteins, hi particular, the crystal structure of the ATPase domain of EHD2 complexed with a bound ligand is applicable across the EHD family polypeptides since those polypeptides are also regarded as ATPases (having previously been thought to be GTPases). In some aspects of the invention, it may be desirable to employ a functional test as to whether or not a particular polypeptide is to be considered an EHD family polypeptide. In addition to, or instead of, the sequence based criteria set out above, the following functional criterion may also be used: EHD family polypeptides can rescue a C.elegans RME knockout. Thus, in order to determine whether or not a particular polypeptide is indeed to be considered an EHD family polypeptide, it may be tested whether or not that polypeptide can rescue a C.elegans RME knockout. If the knockout is rescued, the polypeptide may be regarded as an EHD family polypeptide.

Thus there is a high degree of homology between all four classes of EHD in terms of nucleotide/amino acid sequence, and all four can rescue a C.elegans mutant in the orthologue RME-I. The C. elegans EHD, Rme-1, has been shown to regulate the exit of transmembrane proteins from a tubular intracellular compartment, the so-called endocytic recycling compartment , and a similar location and role has

4,9 been demonstrated for mammalian EHDl . EHD4 / Pincher is predominantly localised to the plasma membrane and is involved in the uptake of the TrkA

2,10 receptor in response to nerve growth factor (NGF) stimulation . Overexpressioj of EHD4 leads to increased clathrm-independent macropinocytic endocytosis of

2.

TrkA in the presence of NGF . Other members of the family also mediate trafficking of various ligands and overexpression of these EHDs leads to their

4,11-14 localisation on tubules inside cells

Exemplary applications of the invention are shown in the following table:

EHDl is involved in MHC class I recycling at the membrane (Caplan et al. (2002) A tubular EHDl -containing compartment involved in the recycling of major histocompatibility complex class I molecules to the plasma membrane. EMBO J. 21 p2557-67). Overexpression of EHDl increases recycling. By inhibiting EHDl activity, for example in a transplanted organ, the transplant may be protected from effects of autorejection. Conversely, activation of EHDl activity may promote an immunological response.

Thus the invention relates to use of a candidate modulator of EHD family polypeptide activity identified as described above, wherein said EHD family polypeptide is EHDl, in the manufacture of a medicament for ameliorating or enhancing immune responses. Amelioration relates to inhibitors of EHDl, augmentation applies to activators of EHDl.

EHDl may have an involvement in cystic fibrosis. .

EHD2 is . known to be involved in insulin mediated GLUT4 transport to the membrane (Park et al. (2004) EHD2 interacts with the insulin-responsive glucose transporter (GLUT4) in rat adipocytes and may participate in insulin-induced GLUT4 recruitment. Biochemistry 43 p7552-62). Thus inhibition of EHD2 provides therapeutic benefit in the treatment of diabetes such as type II diabetes. Thus the invention relates to use of a candidate modulator of EHD family polypeptide activity identified as described above, wherein said EHD family polypeptide is EHD2, in the manufacture of a medicament for diabetes.

EHD4 mediates pinocytic endocytosis of functionally specialised nerve growth factor (NGFJ/neurotrόphic tyrosine kinase receptor type 1 (TrkA) to endosomes and TrkA-erk5 mitogen-activated protein kinase signalling (Shao et al. (2002) Pincher, a pinocytic chaperone for nerve growth factor/TrkA signaling endosomes. J. Cell Biol. 157 p679-691). Thus modulation of EHD4 has application in the treatment of pain. Thus the invention relates to use of a candidate modulator of EHD family polypeptide activity identified as described above, wherein said EHD family polypeptide is EHD4, in the manufacture of a medicament for pain, hi another aspect, the invention relates to use of a candidate modulator of EHD family polypeptide activity identified as described above, wherein said EHD family polypeptide is EHD4, in the manufacture of a medicament for cancer.

AU EHDs are involved in clathrin-independent endocytosis, which is also known to be a mechanism of entry for viruses into cells (Damm et al. (2005) Clathrin- and caveolin-1 -independent endocytosis : entry of simian virus 40 into cells devoid of caveolae. . J. Cell Biol. 168 ρ477~488). Thus broad inhibition of the EHD class finds application in viral infections. Moreover, the EHD sequence is conserved from parasites to higher mammals such as humans. By application of the methods of the invention to the isolation of parasite specific inhibitors, for example by screening parasite orthologues alongside mammalian EHDs, treatments for infections may usefully be provided. Thus in another aspect the invention provides use of a candidate modulator of EHD family polypeptide activity identified as described above, in the manufacture of a medicament for viral or parasite infection.

INDUSTRIAL APPLICATION

EHDl is involved in the recycling of MHC class 1 molecules. Thus, modulation of EHDl has application in immune modulation, for example in transplant patients or in graft versus host disease.

, EHD4 is involved in the internalisation of the TrkA receptor. This receptor responds to nerve growth factor (NGF). Thus, modulation of EHD4 is relevant to the modulation of, or treatment of, pain. NGF is also implicated in the survival and homeostatic maintenance of neurons; thus modulation of EHD4, for example EHD4 response to NGF, finds application in the treatment of neurodegeneration.

EHD2 is important in diabetes. Thus, modulation of EHD2 is important for the treatment of diabetes. More particularly, inhibition of EHD2 is important for the treatment of diabetes. Thus, the present invention particularly concerns screening for or validation of EHD2 inhibitors. Furthermore, the invention relates to the use of EHD2 inhibitors in the treatment of diabetes. In one embodiment, the invention relates to the screening for compounds capable of inhibiting EHD2, and to the use of such inhibitors in the manufacture of a medicament for diabetes.

ASSAYS There are numerous biological activities ascribed to EHD family polypeptides for the first time by the present inventors. These include oligomerisation (including dimerisation), lipid binding, nucleotide binding and nucleotide hydrolysis. The invention provides assays for modulators of one or more of these activities.

Regarding oligomerisation, without wishing to be bound by theory, this is a key target for therapeutic invention. The reason is believed to be that oligomerisation may provide specificity between different EHD family members such as EHD 1/2/3/4. These individual proteins are known to localise to different places within the cell. Thus, by targeting the dimerisation or oligomerisation of those proteins, for example by targeting the oligomerisation/dimerisation interface defined by the present study, then an advantageous specificity can be provided for molecules so identified. Thus, suitably the assays of the present invention readout or screen for factors affecting oligomerisation. . .

It must be noted that oligomerisation facilitates lipid binding. Therefore, for certain assay readouts it may be possible that one or more underlying biological effects might be detected. For example, if the readout of a particular assay was lipid binding, this would be expected to be adversely affected by anything which inhibited oligomerisation. Such factors should be borne in mind by the skilled operator.

The assays of the invention suitably monitor EHD ATP ase activity. Colorimetric ATPase assays are widely available commercially (e.g. http://www.innovabiosciences.com/products/atpase.php). The assay is suitably conducted according to the manufacturer's recommendations for ATPase assay. Suitably the assay may be conducted using regaents of InnovaBiosciences' catalogue number 601-0120. Suitably the assay is conducted essentially as set out in Innova Biosciences' Technical Bulletin number 654 (release 007; July 2005).

In vitro EHD polypeptides may exhibit a slow rate of ATP turnover - this may advantageously be enhanced by including a lipid preparation such as a liposome preparation into the assay of the invention.

Optionally, functional assay step(s) may be additionally used in order to better characterise the effect of the modulator(s) or treatment(s) being studied, or to verify the in vivo significance. An example of such an assay is to monitor internalisation of labelled NGF for candidate EHD4 modulators.

hi some embodiments, it may be desirable to perform further assay steps in order to determine more precisely the biological effect of a given compound. For example, if it is suspected that, a particular compound or treatment is affecting lipid binding, then a direct lipid binding assay might be employed. For example, a FRET based assay might be used, hi this embodiment, a first FRET element would be attached to the EHD family polypeptide of interest, and a second FRET element would be attached to the lipid of interest. Thus, if the EHD family polypeptide does indeed bind the lipid then the FRET effect (fluorescence resonance energy transfer) permits this to be detected and thereby provides some insight as to whether or not lipid binding has been affected.

If it is suspected that a particular compound or treatment is having an effect on nucleotide binding by an EHD family polypeptide, this may be directly confirmed using a nucleotide binding assay. Any nucleotide binding assay known in the art may be employed for this subsequent step or assay, for example the direct binding of a radiolabeled or a fluorescently labelled nucleotide to the EHD family polypeptide of interest under the different treatments being investigated may be assessed. In one embodiment of the invention, it is possible to apply molecular modelling aspects to the design of a nucleotide analogue. For example, it may be possible to design a nucleotide analogue which would selectively bind to an EHD family polypeptide such as EHD2. Thus, in some embodiments the invention relates to such design methods, and to a nucleotide analogue so designed.

It should be noted that the assays of the invention are likely to identify inhibitors of oligomerisation more often or more reliably than specific inhibitors of membrane binding. The reason is that the oligomerisation interface is much more extensive than the relatively much smaller interface which is believed to mediate membrane binding. Since disruption of oligomerisation leads to disruption of membrane binding, the hits which are detected by assaying for disrupted membrane binding would be expected to contain a greater proportion of hits disrupting oligomerisation and a smaller proportion of hits which directly interfere with the actual mechanism of membrane binding.

hi some embodiments, it may be advantageous to employ an optional cell based step in the assay. For example, candidate modulators of EHD family polypeptides may be applied to cells harbouring a fluorescently labelled EHD family polypeptide. The EHD family polypeptide would normally be localised to one or more membrane locations within the cell, dependent on which EHD family member was being studied. If the presence of the candidate modulator changes the expected cellular distribution of the EHD family polypeptide being studied, then this is a dramatic indicator that membrane binding had been affected by that modulator. One example of an altered distribution would be a cytosolic distribution.

hi one embodiment, the invention relates to a three step screening procedure having a. first step of a ATPase screen, a second step of a cell based localisation screen, and an optional third step of a cargo internalisation screen, hi another embodiment, the invention may relate to a two step procedure involving a first step of an ATPase screen and a second step of a cargo internalisation screen, hi another embodiment, the invention may relate to a two step procedure involving a first step of an ATPase screen and a second step of a cell based localisation screen.

DYNAMIN CONTROL In some aspects of the invention, a dynamin control may be included as a reference sample in the assay of the invention.^' Using a dynamin family polypeptide as a control provides numerous advantages. Dynamin is one of the most homologous proteins to EHD in terms of sequence identity. It is expected that dynamin works via a similar mechanism for membrane scission. The activity and affinity profile for dynamin is thought to be similar to EHD. Furthermore, the lipid specificity of dynamin is very close to the specificity of EHD family polypeptides. Thus, by including dynamin as a parallel reference sample in the assays of the invention, false positives having a general effect (rather than an EHD specific effect) may beneficially be excluded from the screen at a very early stage.

It should be noted of course that dynamin is a GTPase. Therefore, the reference sample featuring dynamin should have GTP as a substrate, and should measure the hydrolysis of GTP (rather than ATP which will of course be used in assaying EHD activity). Suitably, two dynamin controls are used, one with candidate modulator and one without. This advantageously permits internal calibration of the background for dynamin, making the dynamin control more robust.

The candidate compounds or treatments of most interest will be those which have ho effect on dynamin action, such as no effect on the GTP hydrolysis activity of dynamin, but which do affect EHD activity, such as ATP hydrolysis by EHD.

INACTIVE EHD MUTANT hi some aspects of the invention, a control or reference sample is used which comprises an inactive EHD family polypeptide. Such a polypeptide is suitably constructed by mutation of the wild type EHD sequence. For example, the catalytic residue may be substituted, residues important in activation of hydrolysis may be substituted, residues involved in ATP binding may be substituted, or any other suitable alteration to the ATP hydrolytic elements of EHD may be made. Suitably the most stable polypeptide is selected as an inactive EHD mutant.

The most suitable EHD mutant to select is that which knocks out the ATPase activity.

A most suitable mutant is a T94A or T72A mutant, more suitably a T94A mutant, of an EHD family polypeptide (or the equivalent residue). This has the advantage of binding ATP but also has the advantage of being catalytically inactive, in other words the T94A mutant does not catalyse the hydrolysis of ATP. Design of this mutant has been enabled by the structural insights into EHD presented herein. The T94A mutant has the further advantage that it is exceptionally well suited to the search for factors affecting oligomerisation. This is because this mutant actually oligomerises slightly more readily even than the wild type EHD family polypeptide family itself.

LIPID/MEMBRANE COMPONENT

The assays of the invention suitably comprise a lipid component such as a membrane component. The lipid component may comprise or contain any negatively charged lipid. The reason that the lipids should be negatively charged is due to the lysines present in the lipid binding site of EHD family polypeptides. Without wishing to be bound by theory, it is believed that the initial long range charge mediated interaction is between the negatively charged elements of the lipids and the positively charged lysine residues on the EHD family polypeptide.

Suitably the negatively charged lipid component may be phosphatidyl serine. Suitably the negatively charged lipid component may be any phosphatidyl inositol lipid. Most suitably, the negatively charged lipids may be provided in the form of liposomes such as Folch liposomes.

It should be noted that specificity for PIP2 (phosphatidyl inositol 4,5 bisphosphate) is observed for EHD family polypeptides. However, such specificity does not necessitate the use of PIP2. For example, if sufficient phosphatidyl serine (PS) is used, then it is not necessary to supply PIP2.

Any suitable concentration of negatively charged lipid may be used. Typically, lipid such as phosphatidyl serine (PS) is used at approximately 10%-20% final concentration.

I157Q

The invention provides a super-active EHD family polypeptide mutant. This mutant is suitably the I157Q mutant. EHD family polypeptides bearing this mutation are not well activated by lipids. In other words, EHD family polypeptides bearing the I157Q mutation are already very highly active in terms of

ATP hydrolysis. By "not well activated by lipids" is meant that lipids are not required in order to reach the high level of activation observed. Thus, the present invention relates to an EHD family polypeptide bearing the Il 57Q mutation.

In addition, such mutants are useful in embodiments of the assay of the invention. For example, by employing the I157Q mutant as the EHD polypeptide in the assays of the invention, the inclusion of lipids in the assay may advantageously be avoided. In another embodiment, an I157Q EHD family polypeptide may be used as a reference or control sample. In this way, if a particular compound or treatment was shown to affect ATP hydrolysis of an EHD family polypeptide both with and without the I157Q mutation, in particular when lipids were absent from the I157Q assay sample, then this effectively, provides another level of information about the action of the compound or treatment being studied. Specifically, if an I157Q mutant EHD is affected in a similar manner to a normal EHD polypeptide, then this would indicate that the action of the compound or treatment is via an ATP or an oligomerisation effect, and is far less likely to be via a lipid binding effect. Thus, the assays of the invention may employ I157Q mutants in order to distinguish between the effects on different biological aspects of the EHD family polypeptide being studied. EHD3

EHD3 may be involved in transferrin uptake. Specifically, EHD3 may inhibit transferrin uptake. Transferrin uptake is an essential biological function, and therefore it is not desirable to interfere with this function. For these reasons, preferably inhibition of transferrin uptake by EHD3 is not a target of the present invention. However, the invention may be applied to the identification or development of inhibitors of EHD3 which still allow transferrin uptake, hi another embodiment transferrin uptake may be used as a readout in a cellular screen to ensure EHD modulators do not interfere with this vital function (i.e. a counter screen).

Structure Based Design

Determination of the 3D structure of EHD provides important information about the likely active sites of EHD, particularly when comparisons are made with similar enzymes. This information may then be used for rational design of EHD inhibitors or interactors, e.g. by computational techniques which identify possible binding ligands for the active sites, by enabling linked-fragment approaches to drug design, and by enabling the identification and location of bound ligands using X-ray crystallographic analysis. These techniques are discussed in more detail below.

An iterative approach to ligand design based on repeated sequences of computer modelling, protein-ligand complex formation and X-ray analysis may be employed. EHD inhibitors may also be designed in the this way. More specifically, a ligand (e.g. a potential inhibitor) of EHD may be designed that complements the functionalities of the EHD active site(s) such as the oligomerisation site or ATP ase site. The ligand can then be synthesised, formed into a complex with EHD, and the complex then analysed by X-ray crystallography to identify the actual position of the bound ligand. The structure and/or functional groups of the ligand can then be adjusted, if necessary, in view of the results of the X-ray analysis, and the synthesis and analysis sequence repeated until an optimised ligand is obtained. Related approaches to structure-based drug design are also discussed in Bohacek et al., Medicinal Research Reviews, Vol.16, (1996), 3-50.

As a result of the determination of the EHD 3D structure, more purely computational techniques for rational drug design may also be used to design EHD inhibitors (or activators). For example, automated ligand-receptor docking programs (discussed e.g. by Jones et al. in Current Opinion in Biotechnology,

Vol.6, (1995), 652-656) which require accurate information on the atomic coordinates of target molecules may be used to design EHD inhibitors (or activators).

Linked-fragment approaches to drug design also require accurate information on the atomic coordinates of target molecules. The idea behind these approaches is to determine (computationally or experimentally) the binding locations of plural ligands to a target molecule, and then construct a molecular scaffold to connect the ligands together in such a way that their relative binding positions are preserved. The connected ligands thus form a potential lead compound that can be further refined using e.g. iterative technique(s). For a virtual linked-fragment approach see Verlinde et al., J. of Computer- Aided Molecular Design, 6, (1992), 131-147, and for NMR and X-ray approaches see Shuker et al., Science, 274, (1996), 1531-1534 and Stout et al., Structure, 6, (1998), 839-848. The use of these approaches to design EHD inhibitors is made possible by the determination of the EHD structure.

Many of the techniques and approaches to structure-based drug design described above rely at some stage on X-ray analysis to identify the binding position of a ligand in a ligand-protein complex. A common way of doing this is to perform X- ray crystallography on the complex, produce a difference Fourier electron density map, and associate a particular pattern of electron density with the ligand.

However, in order to produce the map it is necessary to know beforehand the protein 3D structure (or at least the protein structure factors). Therefore, determination of the EHD structure also allows difference Fourier electron density maps of EHD-ligand complexes to be produced, which can greatly assist the process of rational drug design.

The approaches to structure-based drug design described above all require initial identification of possible compounds for interaction with the target molecule (in this case EHD). Sometimes these compounds are known e.g. from the research literature. However, when they are not, or when novel compounds are wanted, a first stage of the drug design program may involve computer-based in silico screening of compound databases (such as the Cambridge Structural Database) with the aim of identifying compounds which interact with the active site or sites of the target bio-molecule. Screening selection criteria may be based on pharmacokinetic properties such as metabolic stability and toxicity. However, determination of the EHD structure allows the architecture and chemical nature of each active site to be identified, which in turn allows the geometric and functional constraints of a descriptor for the potential inhibitor to be derived. The descriptor is, therefore, a type of virtual 3-D pharmacophore, which can also be used as selection criteria or filter for database screening.

The invention relates to the selection and/or design and/or screening for inhibitors or activators or molecules capable of interfering with or binding to EHD polypeptides. In particular the invention relates to screening for inhibitors of EHD polypeptides.

The invention is now described by way of example. These examples are intended to be illustrative, and are not intended to limit the appended claims. Reference is made to the following figures:

BRIEF DESCRIPTION OF THE FIGURES

Figure 1 shows that EHD2 shares common properties with the dynamin superfamily: a, Domain structure of EHD proteins. Amino acid numbering corresponds to mouse EHD2. b, EHD2 binds to adenine nucleotides, as determined by ITC. For clarity, ΔΔH = ΔHn -ΔH1 is plotted. Fitted values are: ATP-γ-S (m): 13±3μM (n=0.96), ADP(Θ): 50±6μM (n=0.9), GTP-γ- S(^^") and EHD2(T72A)-ATP-γ-S(fp): no binding observed, c, Coomassie- stained gels of co-sedimentation assays in the presence of 1 mM ATP-γ-S using brain-derived Folch, 100% PS and synthetic liposomes (70% phosphatidyl-choline, 10% PS, 10% cholesterol, 10% of the indicated PIs). P-pelleted fraction, S - supernatant, d, Negative stain EM of PS liposomes in the absence (top) or presence (middle, bottom) of EHD2 and 1 mM ATP- γ-S. The bottom panel shows an intermediate in the tubulation process, surrounded by EHD2 rings of variable diameter, e, EGFP-tagged EHD2 was over-expressed in HeLa cells. Whereas the wild-type protein localised to puncta and tubular networks close to the cell surface, the T72A mutant was cytoplasmic. Images were acquired close to the basal cell surface, f, Nucleotide hydrolysis was measured by HPLC in the absence (empty symbols) or presence of Folch liposomes (filled symbols). Data represent mean and standard deviation for two (intrinisic reactions) or three

(stimulated reactions) independent experiments. Whereas the intrinsic ATP reaction was 8-fold stimulated by Folch lipids (θ,©), GTP hydrolysis was not stimulated (^, ⁷^). The nucleotide-free T72A mutant did not show stimulation of ATP hydrolysis (fp.jp). Figure 2 shows the structure of EHD2: a, Ribbon-type presentation of the EHD2 dimer. Molecule A is coloured according to the secondary structure and molecule B according to the domain structure. Disordered loops are represented by dashed lines. The GPF motif in the linker regions is drawn in purple, the localisation of the KPFxxxNPF and further motifs in the G- domain are shown, b, Topology plot of EH D2 in which circles represent α- helices and triangles represent β-strands. Comparison with the classical Ras-like G-domain (boxed) and the G-domain of dynamin indicates that EHD2 has a dynamin-related switch I extension, c, Left: Electrostatic surface representation of the EHD2 EH-domain in which red indicates negative charge and blue positive charge at neutral pH. F422 is penetrating in the non-charged peptide binding pocket. Right: Superposition of the EHD2 EH-domain (dark-green) with the second EH-domain of Eps15 22

(orange) bound to an NPF-containing peptide (pdb code 1 FF1) . Structure and peptide binding mode is very similar in both EH-domains. d, Comparison of the nucleotide-binding sites of Ras (pdb code 5p21 , left) and EHD2 (right). Residues from the NKxD motif involved in specific nucleotide recognition are shown with hydrogen bonds indicated. In EHD2, , D222 from the NKxD motif forms a salt bridge to R536 which is supplied from the opposing EH-domain (in green) into the nucleotide binding site. Figure 3 shows membrane binding and the role of ATP hydrolysis: a, Ribbon-type representation of the putative membrane-binding site with residues tested for membrane-binding in ball-and-stick representation, b, Coomassie-stained gels of sedimentation assays in the absence (lower panel) and presence of Folch liposomes using wild-type EHD2 and the indicated mutants, c, Nucleotide hydrolysis of the lipid binding mutants was carried out as described in Fig. 1f. The F322A mutant („ intrinsic, ^ stimulated reaction) showed a 40% decrease in the stimulated ATPase

-1 -1 reaction (kobs=3.0h for F322A versus 5.4h for wt), and the mutant

K328D pc,^"~) a 75% reduced rate (kobs=1,6h ). d, EGFP-tagged F322A mutant showed a completely cytoplasmic distribution when over-expressed in HeLa cells. Also mutations K324D, K327D, K328D and K329D led to a completely cytoplasmic distribution of EHD2 (data not shown), e, Affinity of the T94A mutant to ATP-γ-S was determined as described in Fig. 1 b. Nucleotide hydrolysis was measured as described in Fig. 1f. In vitro tubulation activity of PS liposomes was analysed as described in Fig. 1d. f, EGFP-tagged mutants were over-expressed in HeLa cells. Whereas the . T94A mutants showed extensive tubulation with no punctate stained, the I157Q mutant showed exclusively punctate staining, g, Quantification of the over-expression phen.otypes from Fig. 3f. For each construct, three independent experiments with «50 cells / experiments were analysed. Figure 4 shows the EHD2 oligomer: a, The alignment in Fig. 8 was used to create a surface conservation plot of the EHD2 dimer (in the same orientation as in Fig. 2a) with conserved residues shown in purple and non- conserved residues in cyan. Conserved surface-exposed residues mutated in the following experiments are indicated. A highly conserved surface patch is present in the G-domain, in between the EHD2 monomers, b, Nucleotide hydrolysis for mutants in the proposed oligomerisation interface was measured as described in Fig. 1f. Note that mutant R167E (in Switch II) showed an increased basal ATPase activity which was not further stimulated by Folch liposomes. Furthermore, deletion of the EH-domain and the mutation of the side site xPFs motif completely prevented the membrane-stimulated ATPase reaction, c, Model of the EHD2 oligomer. Top: Surface representation (orange and blue-cyan dimer) and mesh representation (two dimers on the right) of the proposed oligomer. Only the EH-domains of the second dimer are shown in blue and cyan. The linker region and the disordered KPFxxxNPF loop are shown as dotted lines. The proposed movement of the EH-domains from the top site linker to the side. site G-domain are indicated by arrows. The two EHD2 monomers which were used for the generation of this model are shown in the dotted box with the AMP-PNP molecules facing each other in a head-to-head fashion. . Bottom part: Side view of the oligomer. The membrane-binding sites are facing all in the^' same direction towards the putative membrane interface. Figure 5 shows expression and purification of mouse EHD2. Mouse EHD2 was expressed in Escherichia coli as a His-fusion protein as described in Materials and Methods. NI - Non-induced culture. I - Induced culture. SN - Soluble extract. FT - Soluble extract after application to NiNTA Sepharose. E1- EHD2 after elution from NiNTA-Sepharose. E2 - EHD2 after dialysis and thrombin cleavage. E3 - EHD2 after re-application and elution from the NiNTA column. This protein was further purified by size-exclusion chromatography using a Sephadex S200 column (data not shown). Figure 6 shows ultracentrifugation analysis indicates that EHD2 is a dimeric protein. Sedimentation velocity experiments were performed as described in methods. Selected scans (at equal, ~15min intervals), and of g(s20,w) (the amount of material sedimenting between s20,w and (s20,w+δs)) and also the residuals for fitting the data with DCDT+, were plotted with the program profit v.5.6.7 (Quantum soft, Switzerland). The fitted value is 113 ± 4kDa which corresponds well with the calculated mass of the dimer of 124kDa.

Figure 7 shows EHD2 tubulation of PS- and synthetic liposomes. EHD2 was incubated with the indicated liposomes in the presence and absence of nucleotides and analysed by EM as described in Methods, a, EHD2 deformed PS liposomes into tubular networks, here in the presence of ATP-Y-S. b, Enlarged views of the indicated area in a. Note the presence of regularly spaced EHD2 rings (some are indicated with arrows). This even spacing may be due to the curvature stress generated by an EHD2 ring along the axis of the lipid tubule which might disfavour binding of the next ring in the direct vicinity (see below), c, Some of the lipid tubules (especially at higher protein concentration) were tightly packed with EHD2 oligomeric rings. d,e In the presence of ADP and in the absence of nucleotide (f,g), EHD2 also tubulated PS liposomes and formed ring-like structures around the tubules. e,g are enlarged views of the indicated areas in d and f, respectively. We did not observe a noticeable change of size of the tubules with the different nucleotide conditions. h,i,j, Under less favourable lipid binding conditions (synthetic liposomes with no PS and only 2.5% PIP2), EHD2 tubulated liposomes in the presence of ATP-γ-S. (h) and ADP (i), but we did not observe tubulation in the absence of nucleotides Q).

Figure 8 shows alignment and secondary structure assignment. Multiple sequence alignment of the EHD family. The following sequences were aligned (expasy accession number in brackets): Mouse musculus EHD2 (Q8BH64), Homo sapiens EHD1 (Q9H4M9), Homo sapiens EHD3 (Q9NZN3), Homo sapiens EHD4 (Q9H223), Danio rerio EHD (Q6P3J7), Xenopus laevis EHD1 (Q7SYA1), Xenopus laevis EHD4 (Q7ZXE8), Drosophila melanogaster PAST-1 (Q8IGN0), Caenorhabditis elegans RME 1 (Q966F0), Schistosoma japonicum EHD (Q5DG45), Dictyostelium discoideum EHD (Q54ST5), Plasmodium falciparum EHD (Q9NLB8), Entamoeba histolytica EHD (Q515L4), Trypanosoma cruzi EHD (Q4DYK9), Leishmania major EHD (Q4QDJ3S), Arabidopsis thaliana EHD (Q3EAA4). Completely conserved residues are boxed in red, conserved residues (>50% sequence identity) are boxed in green. Helices are indicated by cylinders, β-strands as blue arrows with colours according to the domain organisation (see Fig. 1a). Residues mutated in this study are indicated with a diamond (♦).

Figure 9 shows the EHD dimer interface. The alignment in Fig. 8 was used to create a surface conservation plot of the EHD2 G-domain and helical domain, with conserved residues shown in purple and non- conserved residues shown in cyan. Helix α6 with its invariant W238 and the contiguous loop of the opposing EHD2 monomer are shown in orange interacting with the conserved surface.

2+

Figure 10 shows the Ca binding site of the EH-domain. Residues

2+ involved in Ca -binding and W490 at the bottom of the peptide binding pocket are in dark grey and the bound GPF-peptide is in light grey. Five

2+ direct ligands for Ca could be identified which are the carboxy side- chains of D494, D496, D498, E505 and one main chain oxygen from M500 (mc500). The sixth ligands might be a water molecule not seen at the current resolution. Figure 11 shows Top: Electrostatic surface representation of EHD2. Red indicates negative charge and blue positive charge at neutral pH. The orientation of EHD2 is the same as in Fig. 2a. The membrane interaction site is highly curved which is a consequence of EHD2 dimerisation. The diameter of the sphere is approximately 7nm, but this may not be so extreme if the tips of the loops (a phenylalanine and a valine residue) are inserted into the membrane. Bottom: EHD binding to liposomes of different sizes in the presence and absence of 1 mM nucleotides and 1 mM MgCI2 (P - pelleted fraction, S supernatant). In the absence of nucleotide, the protein shows a strong binding preference for highly curved membranes. The liposomes have 87.5% phosphatidyl-choline, 10% cholesterol, 2.5% phosphatidyl-inositol(4,5)P2 and no added phosphatidyl-serine. Figure 12 shows the phosphate cap. The phosphates of the AMP-PNP molecule are covered by residues from switch I and the P-loop. This cap does not allow the introduction of a catalytic residue in trans. . Figure 13 shows: a, Top and side view of the EHD2 oligomeric ring model in a surface representation. For better clarity, the EH domains are not included. The diameter of the embraced lipid tubule is «18nm and the thickness of the EHD2 ring is «10nm, in agreement to what is observed in the EM assays. Approximately twenty EHD2 dimers constitute one turn in this model, b, Arrangement of the EHD2 dimers in the oligomer. The high curvature of the membrane interaction site of EHD2 (Fig. 11 ) is oriented perpendicular to the curvature of the lipid tubule. This arrangement is predicted to induce local curvature on the lipid tubule, c, In an alternative model, the curvature of the EHD2 lipid interaction site matches the curvature of the lipid tubules. However, such an arrangement of the EHD2 oligomer was never observed in EM studies (Fig. 1d, Fig. 7).

Figure 14 shows analysis of peptide binding to the EH-domain. The affinity of hepta-peptides from EHD2 containing the indicated xPF motifs to the EH-domain of EHD2 was measured by ITC at 10°C in 10OmM HEPES (pH 7.5), 5OmM NaCl₅

118 418

200μM CaCl2. Peptides PEKPFRKL and RMGPFVER did not (show

124 detectable binding whereas binding of peptide KLNPFGNT could be fitted to an , affinity of 130±20μM (n=1.33). Figure 15 shows a table. Examples:

We disclose the structure and function of mouse EHD2 as a model for the EHD family. The following methods were generally applied:

ITC measurements were performed at 10⁰C in 2OmM HEPES (pH 7.5), 30OmM NaCl, 2mM MgC12. Liposome binding assays were performed as described previously (www.endocytosis.org). Multiple turnover ATPase assays were performed in 2OmM HEPES (pH 7.5), 135mM NaCl₅ 15mM KCl, ImM MgC12 at 30⁰C with lOμM EHD2 (or mutants) as enzyme and lOOμM ATP as substrate, in the absence or presence of lmg/ml Folch liposomes (Sigma- Aldrich). Reactions were started by the addition of the protein to the final reaction mix and

27 nucleotide hydrolysis was followed using standard HPLC measurement . Initial rates were determined by applying a linear fit to data points up to 40% nucleotide hydrolysis. For electron microscopic studies, 2.5μM EHD2 in 2OmM HEPES (pH 7.5), 15OmM NaCl, ImM MgC12 was incubated for 15min at 25°C in the presence of ImM nucleotide and 0.05mg/ml (final concentration) of the indicated liposomes. Samples were spotted on carbon-coated copper grids (Canemco and Marivac) and negatively stained with 2% uranyl acetate. Protein expression and structure determination. Mouse EHD2 full-length protein and all mutants were expressed as N-terminal His-fusions followed by a PreScission cleavage site in Escherichia coli BL21 DE3 Rosetta (Novagen) from a modified pET28 vector. Bacteria cultures in TB medium were induced at an OD of 0.2 with 40μM IPTG and grown overnight at 18°C. Bacteria were lysed in lysis buffer containing 5OmM HEPES (pH 7.5), 40OmM NaCl, 25mM Imidazole, 2.5mM β-Mercaptoethanol (β-ME), 500μM Pefablock SC (Boehringer Ingelheim) using an Emulsiflex homogeniser (Avestin, Canada). After centrifugation at 100,00Og for 45min at 4⁰C, the soluble extract was applied to, a NiNTA-column (Qiagen, Hildesheim) equilibrated with lysis buffer. The column was extensively washed with 2OmM HEPES (pH 7.5), 70OmM NaCl, 3OmM Imidazole, 2.5mM β-ME, ImM ATP, 1OmM KCl and shortly with 2OmM

HEPES (pH 7.5), 30OmM NaCl, 25mM Imidazole, 2.5mM β-ME. Bound protein was eluted with 2OmM HEPES (pH 7.5), 30OmM NaCl, 10OmM Imidazole, 2.5mM β-ME and dialysed overnight at 4°C against 2OmM HEPES (pH 7.5), 30OmM NaCl, 2.5mM β-Mercaptoethanol in the presence of 250μg PreScission protease to cleave the His-tag. The protein was re-applied to a NiNTA column to which it bound under these buffer conditions also in the absence of the His-tag. The column was extensively washed with 2OmM HEPES, 30OmM NaCl, 2.5mM β-ME, and the protein finally eluted with 2OmM HEPES, 30OmM NaCl, 2.5mM β-Me, 25mM Imidazole, concentrated and further purified using a Sephadex200 size-exclusion column (two consecutive runs for proteins used for the ATP ase assays). Typical yields were 4mg purified EHD2 / 1 bacteria culture. At 30OmM NaCl we could concentrate the protein to 40mg/ml but at lower salt concentration we observed some precipitation at this protein concentration. The protein was partially stabilised by ImM MgC12.

Crystallisation and structure determination. For crystallisation, a

30 selenomethioninesubstituted point mutant Q41 OA was prepared as described . This mutant showed identical biochemical properties as the wild-type protein but displayed less degradation in the linker region when incubated over longer periods of time. The protein was concentrated to 40mg/ml and supplemented with 4mM MgC12, 2mM AMP-PNP (Sigma-Aldrich, both final concentrations). The hanging- drop vapour-diffusion method was used for crystallisation. 2μl protein solution were mixed with an equal volume of reservoir solution containing 3% PEG2000 MME, 5OmM MES (pH 6.4), 4mM MgC12. Crystals appeared after one week at

3

4°C and had dimension of -0.2 x 0.2 x 0.05mm . For flash-freezing in liquid nitrogen, they were first transferred for lOsec in 5OmM MES (pH 6.4), 75mM NaCl, 4mM MgC12, 2mM AMP-PNP, 14% MPD before incubation in the final cryo-solution containing 5OmM MES (pH 6.4), 75mM NaCl, 4mM MgC12, 2mM AMP-PNP, 27% MPD. No crystals were obtained in the presence of ADP or in nucleotide-free conditions.

One dataset at the selenium peak wavelength was collected from a single crystal at the ESRP beamline ID14-EH4 (see Fig 15 ("Supplementary Table 1")) and

31 processed and scaled using the xds program suite . Crystals belonged to the monoclinic crystal system and contained one molecule in the asymmetric unit. 13

32 out of 16 selenium atoms were found from SHELXD using the anomalous signal of the dataset. Selenium sites were refined and initial phases were calculated using

33 the program SHARP . In the resulting electron density, the main chain was clearly

34 traceable, and an initial model could be built using the XtaϊView package . The

3₅ model was refined using Refmac5 with 3 TLS groups (Figure 15 ("Supplementary Table 1"))- The asymmetric unit contains 477 amino acids, one AMPPNP, one magnesium, one calcium and five water molecules and has an excellent geometry with all residues in the favoured and most favoured region of

36 the Ramachandran plot as judged by the program Procheck . Ribbon plots were 37 38 prepared using the program Molscript and rendered with Raster3D . Surface

39 conservation plots were prepared using the ConSurf server and ccp4 molecular

40 . graphics . Electron potential maps, were generated using ccp4 molecular graphics.

41

All other surface representations were prepared using pymol . To predict the arrangement of the EHD2 dimer in the oligomer, two EHD2 dimers were superimposed with one of the two monomers of the GBPl ^#GDP ^»AlF3-dimer (pdb

42 ^' . • code 2B92) using swisspdb viewer . The EHD2 dimers were manually re-aligned to avoid amino acid clashes in a way that the two-fold axis between the oligomerising EHD2 monomers was maintained. A high degree of shape complementarity between the EHD2 dimers in the resulting tetramer supported this approach (Fig. 13). Furthermore, the lipid binding sites of both EHD2 dimers are expected to contact the membrane, and this restraint is fulfilled in the tetramer. To obtain a 20nm ring, an 18° tilt was introduced between the dimers. We refrained from energy minimising of this structure since major conformational changes in the interface are expected to take place upon oligomerisation (ordering of switch I and switch II) and since the resolution of the structure is not appropriate for an

43 accurate prediction. The programs superpose and pdbset from ccp4 were used to generate the oligomer from the tetramer. Pdb coordinates of the proposed oligomer are found in the Supplementary Materials. Ultracentrifugation. Sedimentation velocity experiments were performed in a

Beckman Optima XLA ultracentrifuge, using an An-60Ti rotor. Centrifugation was

-1 at 50,000 rev x min and 5°C at an EHD2 concentration of 15μM, with scans as

44,45 fast as possible (~1.5min intervals). The data were analysed using DCDT+ v.2 , with the partial specific volume for the protein (from the amino acid composition)

4δ and solvent density and viscosity calculated using Sednterp . Selected scans (at equal, ~15min intervals), and of g(s20,w) (the amount of material sedimenting between s20,w and (s20,w+δs)) and also the residuals for fitting the data with DCDT+, were plotted with the program profit v.5.6.7 (Quantum soft, Switzerland). Cell biology. N-terminal EGFP -tagged EHD2 and all mutants were over-expressed in HeLa cells from the pEGFP-C3 vector (Clontech). HeLa cells were grown as per ECACC guidelines with 10% fetal bovine serum and transfected using Genejuice (Novagen) for transient protein expression. 24h after transfection, cells were fixed for lOmin at 37°C in 3% paraformaldehyde and mounted. All confocal images were taken sequentially using a BioRad Radiance system and LaserSharp software (Biorad). For real-time microscopy, transfected cells on glass-bottom Petri dishes (WiIlCo Wells BV, Amsterdam) were washed with 25mM HEPES (pH 7.5), 125mM NaCl₅ 5mM KCl, 1OmM D-glucose, ImM MgC12, 2mM CaC12), and epifiuorescence images were taken using an Olympus 1X70 microscope (Southhall, UK) and Argon laser (Melles Griot, Carlsbad, CA) with a Princeton instruments (Trenton, NJ) cooled I-PentaMAX camera with MetaMorph software (Universal imaging).

Example 1: Expression and Purification

Mouse full-length EHD2 was expressed in bacteria and purified to homogeneity (Fig. 5). The purified protein was nucleotide-free as judged by HPLC analysis. In 30OmM NaCl, EHD2 was highly soluble, eluted as a dimeric protein by size- exclusion chromatography, and was found to be a dimer in dynamic light scattering experiments and in analytical velocity centrifugation (Fig. 6). At 50μM protein concentration, the hydrodynamic radius did not change in the presence or absence of nucleotides (or in 15OmM versus 30OmM NaCl), as judged by dynamic light scattering experiments. It was previously reported that EHDs - despite having a predicted G-domain - bind to adenine nucleotides . We confirmed these results by using isothermal titration calorimetry (ITC) (Fig. Ib) and found binding of EHD2 to the non-hydrolysable ATP analogue ATP-γ-S, with an affinity of 13μM, and to ADP, with an affinity of approximately 50μM. A mutation in the phosphate binding (P-)loop, T72A, prevented binding to ATP-γ-S, similar to the effect of equivalent mutations, on nucleotide binding to other GTPases. No binding signal

15 was observed for GTP-γ-S (Fig. Ib and ). We still refer to this domain as a G- domain because the sequence and fold (see below) are clearly similar to other G- domains. We next investigated membrane-binding properties of EHD2 and found efficient binding to liposomes made from brain-derived lipids (Folch extract) and to 100% anionic phosphatidyl-serine (PS) liposomes (Fig. Ic). Using synthetic liposomes containing various different phosphatidyl-inositols (PI) (Fig. Ic) we observed best binding to liposomes containing PI(4,5)bisphosphate (PIP2). Example 2: Effects on biological membranes

The consequence of membrane-binding was analysed by electron microscopy (EM), and we found that EHD2 deforms PS liposomes in a nucleotide-independent manner into 20nm-diameter tubules and oligomerises in ring-like structures around . these tubules (Fig. Id, Fig. 7). Nucleotide-independence of liposome tubulation in

16 vitro is also observed for dynamin . No noticeable tubule fission or alteration in tubule diameter was found for EHD2 in the presence of ATP. Frequently we observed a complex network of connected tubules that had an extensive surface area implying that there is considerable fusion occurring between liposomes (Fig. 7). We also saw a few instances where EHD2 oligomeric rings were of variable diameter (Fig. Id, bottom) suggesting that the interface used for EHD2 oligomerisation is rather flexible. Folch liposomes were also tubulated by EHD2. However, with synthetic liposomes containing only 2.5% PIP2 and in the absence of PS, the amount of EHD binding was reduced, and in this less favourable binding condition we only observed tubulation in the presence of ATP-γ-S and ADP but not in the absence of nucleotides (Fig. 7). When EGFP-tagged EHD2 was over-expressed in HeLa cells it marked punctate and tubular structures that were mainly found close to the plasma membrane (Fig. Ie, endogenous EHD2 in various cell lines shows a similar peripheral

13,17 distribution ). Although the nucleptide-free T72A mutant bound to Folch liposomes in vitro (Fig. 1C), it showed a cytoplasmic distribution when over- expressed in vivo (Fig. 1 e), indicating that nucleotide binding is required for

3 oligomerisation in vivo, in agreement with previous results . Example 3: ATP binding and ATPase activity

We next monitored the effect of membrane-binding on the ATPase activity of EHD2 under multiple-turnover conditions (10-fold excess of ATP over EHD2), in the presence and absence of Folch liposomes (Fig. If). The intrinsic / background

-1 ATPase activity is extremely slow (kobs=0.7h ) but is stimulated 8-fold in the

-1 18 presence of Folch or PS liposomes (kobs=5.6h ). In contrast to GBPl we did not observe hydrolysis to nucleoside mono-phosphate. GTP was not hydrolysed in the presence or absence of Folch liposomes, and the T72A mutant did not show membrane-stimulated ATP ase activity. EHD2 displays a 600-fold slower stimulated nucleotide hydrolysis than dynamin, which hydrolyses GTP under this

-1 condition with a kcat of- lsec .

To obtain structural insights we solved the crystal structure of EHD2 in the presence of the non-hydrolysable ATP analogue AMP-PNP to a maximal resolution of 3.1 A (see Methods and Figure 15 ("Supplementary Table 1") for the statistics). The nucleotide binding domain of EHD2 possesses a typical G-domain fold with a central β-sheet surrounded by α-helices (Fig. 2a, 2b and Fig. 8). An

AMP-PNP molecule occupies the canonical nucleotide-binding site. In comparison to the Ras-like G-domain, EHD2 contains an insertion of two additional β-strands

19 in the switch I region which are also present in the G-domain of dynamin (Fig. 2b). Residues 112-129, which are distal to switch I, are disordered and contain a predicted EH-domain binding motif, KPFxxxNPF. In agreement with our biochemical analysis, EHD2 crystallises as a dimer, and the dimer axis corresponds to a crystallogfaphic two-fold axis (Fig. 2a). Dimerisation is mediated via a highly conserved, mostly hydrophobic interface of approximately 2100A in the G-domain (Fig. 9). At the centre of the interface, the entirely conserved W238 in helix α6 is buried in a hydrophobic pocket, and mutations of this residue render the protein insoluble. The high conservation of this interface suggests that it is a common feature of all EHD members. Such an interface has not been described as yet for any other large GTPase and involves a different face of the G-domain than the dimer interfaces from the structurally characterised GBPl and bacterial

18,20 dynamin-like protein (BDLP) dimers Example 4: Structural Insights

The helical domain is composed of helix αl and α2 from the N-terminal region (residues 18-55, which follow disordered residues 1-18) and helices α8, oc9, αlO, αl 1 and αl2 (residues 285-400) following the G-domain (Fig. 2a). Helix α8 of EHD is the organising scaffold against which most of the other helices fold. It has also extensive contacts with the G-domain. The dimeric G-domain together with the helical region adopts a scissor shape, where the membrane is proposed to bind between blades (see later).

Following the middle domain there is a 40-residue linker which connects the helical domain with the C-terminal EH-domain (residues 443-543). The EH- domain of EHD2 is similar to the previously determined second EH-domain of

21,22 . .

Epsl 5 solved by NMR studies with a root-mean square deviation of 1.5 A for the main-chain atoms (Fig. 2c). It is built of two closely packed perpendicular EF

2+ hands which are connected by a short β-sheet. We included a Ca -ion in the second EF hand which is ligated by four oxygens from acidic side-chains (D494, D496, D498, E505) and one main chain carbonyl oxygen of M500 (Fig. 10). This ion has been maintained during purification. The EH-domain is localised on top of

2 the G-domain (the top site position) with a buried interface of 1600 A . Eighteen disordered residues connecting the EHdomain to the helical domain means that it is ambiguous as to which EH-domain connects to which helical domain. We assign the EH-domains to opposing monomers (red EHD belongs to red helical domain in Fig. 2a) as the last visible residue of the linker from the helical domain is closer to the opposite EH-domain (distance 29A) than to the superjacent EH-domain (distance of 34A), and in this latter case the linker would have to wind around the EH-domain and thus one would expect to see some parts of this in the structure (Fig. 2a). Unexpectedly, the peptide binding sites of both EH-domains are occupied by a GPF motif (residues 420-422) from the linker region (Fig. 2a and c). The GPF motif adopts a similar conformation as an NPF-containing peptide bound

21 to the EH2 domain of Epsl 5 involving a tight turn with F422 projecting into a hydrophobic pocket which is lined by W490 at its base (Fig. 2c and Fig. 10). Example 5: Nucleiotide Binding Site

Specific guanosine recognition in GTPases is mediated by a highly conserved NKxD motif (called G4) where the asparagine side-chain forms a hydrogen bond to the carbonyl group at carbonό of the guanosine base and the aspartate side-chain forms a double hydrogen bond to nitrogenl of the guanosine base and the amine group at carbon2 (Fig. 2d, left). Aspartate has been shown to be crucial since mutating it to asparagine in Ras reduces nucleotide affinity by more than 1000- 23 fold . Directly following the NKxD motif, a large hydrophobic residue (leucine in Ras and dynamin, M223 in EHD2) lines the nucleotide binding pocket. The NKxD motif of EHD2 (starting at residue 219) is also highly conserved in EHD family members (Fig. 8). The carboxyamide group of N219 forms a hydrogen bond to the C6 amino group of the adenine base (Fig. 2d, right). M223, whose side-chain is buttressed by the side chain of H 192, is closer to the purine base than the corresponding leucine residue in Ras and sterically excludes an amino group at C2, thus explaining the inability of EHDs to bind to guanine nucleotides. Instead of forming a double hydrogen bond, the completely invariant D222 of EHD2 surprisingly forms a salt bridge with the conserved R536 which is supplied from the C-terminus of the superjacent EH-domain (Fig. 2d, right). Example 6: Membrane Binding Site

The membrane-binding properties of EHD2 are reminiscent of a subset of the small GTPase family which have recently been shown to require polybasic stretches for their PIP2- and PI(3,4,5)P3-dependent targeting to the plasma

24 membrane . We found such a polybasic stretch in EHD2 close to the tip of the helical domain, but facing the cavity between the EHD2 dimer, consisting of K324, K327, K328 and K329 on each monomer (Fig. 3a). A hydrophobic residue, F322, is located at the tip of the helical domain. We mutated K328 to aspartate and F322 to alanine, and indeed both these mutants bound less to liposomes (Fig. 3b), and showed reduced ATPase stimulation in the presence of Folch liposomes (Fig. 3c). In vivo, the F322A mutation of the membrane-binding site, and in fact any lysine to aspartate mutations in the polybasic cluster, led to a completely cytoplasmic distribution of the protein (Fig. 3d). Thus the lipid interaction site of EHD2 is composed of two closely opposing lipid-binding sites in the dimer, and this leads to a highly curved membrane interface of approximately 7nm radius (Fig. 3a and Fig. 11). Indeed EHD2 showed a binding preference for very small liposomes, consistent with this curvature, but only in the nucleotide-free form (Fig. 11). In the nucleotide-bound form EHD binding is not curvature sensitive, and this is likely due to oligomer formation along an axis perpendicular to the high curvature (see below). Example 7: Catalytic Site

In EHD2, the phosphate groups of the AMP-PNP molecule are occluded from the exterior by switch I and the P -loop, which would not allow the insertion of a catalytic residue in trans into the catalytic site (Fig. 12). This so-called "phosphate

25 cap" is also present in GBPl whose mechanism of GTP hydrolysis has been shown to involve dimerisation-dependent positioning of the attacking nucleophilic

18 water molecule by a catalytic serine in cis from switch I which corresponds to

T94 in EHD2.

In small GTPases, the role of positioning the water molecule is assigned to a

26 catalytic glutamine from switch II . We studied the role of ATP hydrolysis to gain insights into the function of EHD2 in vivo. The T94A mutant bound to ATP-γ-S with nearly wild-type affinity (Fig. 3e) and oligomerised around PS liposomes (Fig. 4e), but did not show any membrane-stimulated ATPase activity, consistent with a catalytic function for T94. When over-expressed in HeLa cells, the T94A mutant labelled extensive tubular structures with essentially no punctate staining (compare wild-type and T94A in Fig. 3d, 3f and 3g), suggesting that ATP hydrolysis is involved in the break-down of tubular structures in vivo. We previously observed severely inhibited GTP hydrolysis and a similar extensive tubulation phenotype with dynaminl when the equivalent T65 was mutated to alanine . To confirm the role of ATP hydrolysis in EHD function we re-introduced a catalytic glutamine in the active site, at the position normally found for small GTPases (Il 57Q). This mutant tubulated liposomes and hydrolysed ATP faster than wild-type, even in the absence of membranes. Furthermore, the ATPase reaction was not further stimulated by membranes (Fig. 3e). When over-expressed in HeLa cells this protein labelled only very short tubules and puncta (Fig. 3f, Fig. 3g). Many of these puncta were highly mobile as determined by live-cell microscopy. This suggests that increased ATP hydrolysis leads to increased membrane fission by EHD2. Altogether, these results are consistent with a role of ATP hydrolysis in the scission of membranes in vivo. hi a surface-conservation plot of the EHD2 dimer, a highly conserved surface patch encompasses switch I, switch II and the surrounding area (Fig. 4a). GBPl and BDLP use this same interface, with the same relative orientation of the G-

18,20 domains, for dimerisation . This interface was suggested to be a conserved

20 feature of all dynaminrelated GTPases . Thus, the EHD2 dimer may further oligomerise into the observed rings using this second G-domain interface. Using

. ^' 18 ^' the dimeric GBPl 'GDP-AlF 4 G-domain structure as a template and taking into account the observed 20-nm ring of the EHD2 coat (Fig. Ic), we predicted the arrangement of the EHD2 dimers within the oligomer in which the nucleotides of two opposing EHD monomers are facing each other in a head-to-head fashion (see Methods and Fig. 4c). The predicted oligomer has a compact structure with a high degree of shape-complementarity between the oligomerising dimers (see Supplementary coordinates). Furthermore, the membrane-binding sites are pointing in the same direction towards the putative membrane interface (Fig. 4c, Fig. 13), and the thickness of the oligomeric ring agrees well with the thickness of the rings observed by EM (~10nm, Fig. Id). We tested this model by mutagenesis of four surface-exposed conserved residues in this putative interface (Fig. 4a, 4b). As predicted, all mutants showed reduced or completely abolished assembly- stimulated ATP hydrolysis (Fig. 4b) indicating that the conserved interface is indeed involved in the assembly-stimulated ATPase reaction, hi the predicted oligomer, the highly curved membrane interface of the EHD2 dimer are oriented perpendicular to the direction of the tubule curvature (Fig. 13b), consistent with the tightly packed rings observed by EM. hi an alternative model, the oligomer could also form along the length of a tubule (parallel to its long axis) and thus maximise the use of the highly curved membrane interface of the dimer (Fig. 13 c). However, such an arrangement was never observed by EM. Furthermore, our ring-based oligomer model is consistent with the absence of any curvature-sensitive membrane binding upon oligomerisation. Example 8: EH Domains

EH-domains are low affinity protein-protein interactors normally found in endocytic multi-subunit assemblies. A likely purpose of the EH-domain is in recruitment of the protein to sites of action. In the oligomer it could further function to concentrate NPF-containing binding partners around membrane-bound EHD, but we did not observe any co-localisation of described EHD binding

27 partners, pacsinl and 2 along the length of EHD tubules in vivo (data not shown). An alternative explanation for the function of the.EH-domain in the oligomer can be proposed based on the presence of two conserved PF motifs (NPF and KPF) in a disordered surface loop at the side of the G-domain between β-sheet 2 A and 2B. hi our proposed oligomer, the EH-domains from one dimer are close to the side- site NPF motif of the adjacent dimer (Fig. 4c) and thus after oligomerisation on membranes they may switch position from the top site position in the dimer to the side site in the opposing dimer. It is interesting that only a side site NPF peptide, and not the top site GPF peptide, bound with a measurable affinity (~130μM) to the isolated EH-domain of EHD2 (Fig. 14), and this affinity is well within the

21 range of other related EH-domain interactions . In agreement with a role for the NPF motifs in stabilisation / organisation of the EHD oligomer we observed that a deletion mutant of the EH-domain (ΔEH) or a double mutant of the two side-site xPF motifs (F 122A/F 128 A) did not show any membrane-stimulated ATPase activity (Fig. 4b) and we did not find any regular oligomers on liposomes in EM studies for these mutants. A dominant negative mutant in C elegans Rmel is found in the linker between the EH-domain and the helical domain pointing to the importance of this flexible linker.

Example 9: Cell imaging studies

EHD2 wild-type was over-expressed in HeLa cells for 24h and imaged by EPI- fluorescence for approximately 30min. Some of the tubules and puncta are dynamic. EHD2 T94A was over-expressed in HeLa cells for 24h and imaged by EPI- fluorescence for approximately 30min. There a only tubules, and these are mostly static.

EHD2 I157Q was over-expressed in HeLa cells for 24h and imaged by EPI- fiuoresceήce for approximately 30min. No tubules can be found and the puncta are mostly motile. Supplementary coordinates: Pdb coordinates of the proposed EHD2 oligomer. Four EHD2 dimers (in the absence of the EH domain) were aligned as described in Methods. All lipid interaction sites point towards the putative membrane interface. Molecules B and C which have been used for the initial alignment with GBPl are related via a 2-fold axis, and the nucleotides of these molecules are oriented in a head-to-head fashion.

Example 10: Assay

This example relates to a method of identifying a modulator of an EHD family polypeptide.

A first and second sample of an EHD polypeptide are provided. In this example the EHD polypeptide is EHD2.

The first EHD sample is contacted with a candidate modulator. The candidate modulator is added to the medium containing the EHD polypeptide.

ATP reagent is added to the first and second samples. The ATP reagent is as per InnovaBiosciences' catalogue number 601-0120, permitting colorimetric readout of ATP hydrolysis.

ATP hydrolysis in said first and second samples is monitored in accordance with the manufacturer's instructions. .

A difference between the ATP hydrolysis in said first and second samples identifies said candidate modulator as a modulator of an EHD family polypeptide.

In particular, if hydrolysis of ATP is greater in said first sample than in said second sample then the candidate modulator is identified as an enhancer of EHD family polypeptide activity. Conversely, if hydrolysis of ATP is lower in said, first sample than in said second sample then the candidate modulator is identified as an inhibitor of EHD family polypeptide activity.

The ATP hydrolysis is optionally monitored in the presence of lipid, in which case liposomes and/or phosphatidylserine (PS) at a final concentration of about 10% are added to both the samples, suitably after addition of candidate modulator but before addition of ATP reagent.

Example 11: Atomic Coordinates

Table A

ATOM 1 N ARGA 19 51.364-44.695-13.521 1.0058.79 N

ATOM 2 CA ARGA 19 51.849-44.622-14.929 LOO 58.86 C

ATOM 3 CB ARGA 19 53.209-45.314-15.064 1.0058.86 C

ATOM 4 CG ARGA 19 53.148-46.838-15.011 1.0059.05 C

ATOM 5 CD ARGA 19 54.535-47.464-15.123 1.0059.14 C

10 ATOM 6 NE ARGA 19 55.299-46.949-16.261 1.0059.75 N

ATOM 7 CZ ARGA 19 56.300-46.076-16.161 1.0059.95 C

ATOM 8 NHlARGA 19 56.669-45.613-14.972 1.0060.07 N

ATOM 9 NH2ARGA 19 56.937-45.665-17.252 1.0059.86 N

ATOM 10 C ARGA 19 50.835-45.249-15.884 1.0058.73 C

15 ATOM 11 O ARGA 19 51.082-45.372-17.083 1.0058.69 O

ATOM 12 N THRA 20 49.688-45.636-15.338 1.0058.62 N

ATOM 13 CA THRA 20 48.614-46.223-16.132 1.0058.46 C

ATOM 14 CB THRA 20 47.790-47.226-15.302 1.0058.50 C

ATOM 15 OGlTHRA 20 47.104-46.534-14.249 1.0058.37 O

20 ATOM 16 CG2THRA 20 48.699-48.292-14.705 1.0058.59 C

ATOM 17 C THRA 20 47.680-45.152-16.697 1.0058.32 C

ATOM 18 O THRA 20 48.020-43.965-16.718 1.0058.25 O

ATOM 19 N VALA 21 46.500-45.579-17.143 1.0058.12 N

ATOM 20 CA VALA 21 45.548-44.683-17.800 1.0057.89 C

25 ATOM 21 CB VALA 21 44.611-45.447-18.756 1.0057.93 C

ATOM 22 CGlVALA 21 43.624-46.293-17.968 1.0058.17 C

ATOM 23 CG2VALA 21 43.872-44.474-19.663 1.0057.98 C

ATOM 24 C VALA 21 44.712-43.859-16.817 1.0057.68 ' C

ATOM 25 O VALA 21 44.574-42.644-16.983 1.0057.39 , O

30. ATOM 26 N THRA 22 44.152-44.511-15.801 1.0057.46 N

ATOM 27 CA THRA 22 43.359-43.792-14.806 1.0057.30 C

ATOM 28 CB THRA 22 .42.661 -44.740 -13.793 1.0057.27 C

ATOM 29 OGlTHRA 22 43.523-44.987-12.676 1.0057.51 O

ATOM 30 CG2 THR A 22 42.280-46.062-14.453 1.0057.23 C

35 ATOM 31 C THRA 22 44.255-42.784-14.085 1.0057.11 C

ATOM . 32 O THRA 22 43.837-41.669-13.783 1.0057.00 O

ATOM 33 N SERA 23 45.494-43.183-13.824 1.0056.93 N

ATOM 34 CA SERA 23 46.500-42.275-13.297 1.0056.79 C

ATOM 35 CB SERA 23 47.849-42.985-13.265 1.0056.78 C

40 ATOM 36 OG SERA 23 48.811-42.263-14.009 1.0057.00 O

ATOM 37 C SERA 23 46.594-41.016-14.155 1.0056.73 C

ATOM 38 O SERA 23 46.504-39.884-13.653 1.0056.72 O

ATOM 39 N SERA 24 46.768-41.227-15.456 1.0056.67 N

ATOM 40 CA SERA 24 46.884-40.135-16.415 1.0056.66 C

45 ATOM 41 CB SERA 24 47.130-40.691-17.818 1.0056.64 C

ATOM 42 OG SERA 24 47.818-39.753-18.626 1.0056.92 O

ATOM 43 C SERA 24 45.629-39.262-16.388 1.0056.55 C

ATOM 44 O SERA 24 45.710-38.031-16.372 1.0056.41 O ^•

ATOM 45 N LEUA 25 44.471-39.911-16.373 1.0056.64 N

50 ATOM 46 CA LEUA 25 43.208-39.213-16.174 1.0056.46. C

ATOM 47 CB LEUA 25 42.067-40.216-16.016 1.0056.37 C

ATOM 48 CG LEUA 25 41.205 -40.508 '-17.240 1.0056.13 C

ATOM 49 CDlLEUA 25 41.983-40.290-18.513 1.0055.71 C

ATOM 50 CD2LEUA 25 40.657-41.923-17.166 1.0056.30 C

55 ATOM 51 C LEUA 25 43.271-38.320-14.940 1.0056.49 C

ATOM 52 O LEUA 25 42.889-37.148-14.989 1.0056.42 O

ATOM 53 N LYS A 26 43.752-38.883-13.835 1.0056.45 N ATOM 54 CA LYS A 26 43.817-38.164-12.575 1.0056.29 C

ATOM 55 CB LYSA 26 44.322 -39.079 -11.456^' 1.0056.32 C

ATOM 56 CG LYS A 26 44.300-38.454-10.064 1.0056.35 C

ATOM 57 CD LYS A 26 44.278-39.516 -8.966 1.0056.35 C ATOM 58 CE LYSA 26 45.538-40.371 -8.973 1.0056.39 C

ATOM 59 NZ LYS A 26 45.407-41.557 -8.080 1.0056.13 N

ATOM 60 C LYS A 26 44.690-36.924-12.715 1.0056.32 C

ATOM 61 O LYS A 26 44.264-35.817-12.367 1.0056.34 O

ATOM 62 N GLUA 27 45.901 -37.093-13.242 1.0056.37 N ATOM 63 CA GLUA 27 46.764-35.927-13.450 1.0056.31 C

ATOM 64 CB GLU A 27 48.135-36.332-13.989 1.0056.40 C

ATOM 65 CG GLUA 27 49.118-36.769-12.907 1.0056.99 C

ATOM 66 CD GLUA 27 49.194-35.789-11.741 1.0057.43 C

ATOM 67 OEl GLUA 27 48.165-35.604-11.049 1.0057.97 O ATOM 68 OE2GLUA 27 50.285-35.218-11.504 1.0056.59 O

ATOM 69 C GLUA 27 46.110-34.886-14.357 1.0056.16 C

ATOM 70 O GLUA 27 46.094-33.691-14.039 1.0055.99 O

ATOM 71 N LEUA 28 45.563-35.352-15.478 1.00_.56.19 N

ATOM 72 CA LEU A 28 44.827-34.483-16.394 1.0056.04 C ATOM 73 CB LEU A 28 44.156-35.295-17.505 1.0055.97 C

ATOM 74 CG LEUA 28 44.864-35.366-18.861 1.0056.13 C

ATOM 75 CDlLEUA 28 46.354-35.712-18.746 1.0056.25 C

ATOM 76 CD2LEUA 28 44.144-36.321-19.799 1.0056.01 C

ATOM 77 C LEU A^' 28 43.787-33.671-15.642 1.0056.00 C ATOM 78 0 LEUA 28 43.736-32.450-15.767 1.0056.01 O

ATOM . 79 N TYRA 29 42.961 -34.353 -14.857 1.0055.97 N

ATOM 80 CA TYRA 29 41.978-33.671-14.035 1.0055.76 C

ATOM 81 CB TYRA 29 41.222-34.659-13.152 1.0055.53 C

ATOM 82 CG TYRA 29 40.319.-33.982-12.150 1.0055.13 C ATOM 83 CDlTYRA 29 39.169-33.320-12.560 1.0054.84 C

ATOM 84 CElTYRA 29 38.340-32.696-11.649 1.0054.64 C

ATOM 85 CZ TYRA 29 38.657-32.729-10.309 1.0054.85 . C

ATOM 86 OH TYRA 29 37.839-32.111 -9.396 1.0055.02 ^■ O

ATOM 87 CE2TYRA 29 39.791-33.381 -9.875 1.0054.94 C ATOM 88 CD2TYRA 29 40.617-34.000-10.796 1.0054.98 C

ATOM 89 C TYRA 29 42.640-32.618-13.163 1.0055.90 C

ATOM 90 O TYRA 29 42.328-31.432-13.272 1.0055.94 O

ATOM 91 N ARG A 30 43.565-33.056-12.311 1.0056.07 N

ATOM 92 CA ARG A 30 44.161 -32.167-11.317 1.0056.16 C ATOM 93 CB ARGA 30 45.155-32.915-10.425 1.0056.13 C

ATOM 94 CG ARGA 30 45.781-32.027 -9.349 1.0056.57 C

ATOM 95 CD ARGA 30 46.944-32.704 -8.639 1.0056.62 C

ATOM 96 NE ARGA 30 47.997-33.102 -9.570 1.0057.56 N

ATOM 97 CZ ARG A 30 49.025 -32.334 -9.915 1.0057.96 C ATOM 98 NHlARGA 30 49.150-31.115 -9.404 1.0058.09 N

ATOM 99 NH2 ARG A 30 49.933-32.785-10.771 1.0058.17 N

ATOM 100 C ARGA 30 44.836-30.945-11.925 1.0056.07 C

ATOM 101 O ARGA 30 44.809-29.864-11.339 1.0056.10 O

ATOM 102 N THRA 31 45.438-31.104-13.097 1.0056.02 . N ATOM 103 CA THRA 31 46.186-29.999-13.689 1.0055.94 ^' C

ATOM 104 CB THRA 31 47.468-30.495-14.373 1.0055.94 C

ATOM 105 OGl THRA 31 47.127-31.427-15.407 1.0056.01 O

ATOM 106 CG2THRA 31 48.379-31.172-13.361 1.0055.91 C

ATOM 107 C THRA 31 45.378-29.166-14.687 1.0055.97 C ATOM 108 O THRA 31 45.658-27.982-14.883 1.0055.91 O

^■ ATOM 109 N LYS A 32 44.377-29.780-15.311 1.0056.00 N

ATOM 110.CA LYSA 32 43.660-29.137-16.414 1.0056.02 C

ATOM 111 CB LYSA 32 43.701-30.019-17.673 1.0056.03 C ATOM 112 CG LYSA 32 45.082-30.162-18.339 1.0056.05 C

ATOM 113 CD LYSA 32 45.420-28.956-19.218 1.0056.16 C

ATOM 114 CE LYSA 32 46.772-29.099-19.924 1.0055.96 C

ATOM 115 NZ LYSA 32 46.693-29.805-21.237 1.0055.50 N ATOM 116 C LYSA 32 42.211 -28.750 -16.087 1.0056.03 ^' C

ATOM 117 O LYSA 32 41.668-27.819-16.683 1.0056.12 O

ATOM 118 N LEUA 33 41.587-29.460-15.149 1.0055.98 N

ATOM 119 CA LEUA 33 40.182-29.209-14.814 1.0055.83 C

ATOM 120 CB LEUA 33 39.381-30.508-14.852 1.0055.81 C ATOM 121 CG LEUA 33 38.353-30.636-15.968 1.0055.96 C

ATOM 122 CDl LEUA 33 37.675-31.991-15.893 1.0056.34 C

ATOM 123 CD2LEUA 33 37.330-29.526-15.847 1.0056.25 C

ATOM 124 C LEUA 33 39.996-28.553-13.455 1.0055.75 C

ATOM 125 O LEU A 33 39.334-27.521-13.332 1.0055.70 O ATOM 126 N LEUA 34 40.581-29.171-12.435 1.0055.70 N

ATOM 127 CA LEUA 34 40.452-28.699-11.066 1.0055.64 C

ATOM 128 CB LEUA 34 41.427-29.447-10.154 1.0055.58 C

ATOM 129 CG LEUA 34 41.327-29.178 -8.654 1.0055.53 C

, ATOM 130 CDlLEUA 34 39.877-29.201 -8.195 1.0055.57 C ATOM 131 CD2 LEU A 34 42.156-30.193 -7.882 1.0055.60 C

ATOM 132 C LEUA 34 40.638-27.189-10.935 1.0055.74 C

ATOM 133 O LEUA 34 39.868-26.536-10.231 1.0055.74 O

ATOM 134 N PRO A 35 41.658-26.624-11.611 1.0055.81 N

ATOM 135 CA PRO A 35 41.887-25.187-11.486 1.0055.89 C ATOM .136 CB PRO A 35 43.070-24.935-12.426 1.0055.71 C

ATOM 137 CG PROA 35 43.742-26.244-12.550 LOO 55.71 C

ATOM 138 CD PRO A 35 42.647-27.256-12.502 1.0055.76 C

ATOM 139 C PRO A 35 40.683-24.372-11.935 1.0056.06 C

ATOM 140 O PROA 35 40.384-23.339-11.341 1.0056.11 O ATOM 141 N LEUA 36 39.996-24.843-12.969 1.0056.32 N

ATOM 142 CA LEUA 36 38.876-24.111-13.545 1.0056.60 C

ATOM 143 CB LEUA 36 38.587-24.654-14.936 1.0056.61 C

ATOM 144 CG LEUA 36 38.094-23.658-15.978 1.0056.89 C

ATOM 145 CDl LEUA 36 38.653-24.031-17.331 1.0057.25 C ATOM 146 CD2 LEU A 36 36.582-23.624-16.011 1.0057.53 C

ATOM 147 C LEUA 36 37.648-24.229-12.646 1.0056.79 C

ATOM 148 O LEUA 36 36.943-23.237-12.376 1.0056.95 O

ATOM 149 N GLUA 37 37.413-25.448-12.171 1.0057.00 N

ATOM .150 CA GLUA 37 36.379-25.705-11.180 1.0057.34 C ATOM 151 CB GLUA 37 36.412-27.168-10.732 1.0057.32 C

ATOM 152 CG GLUA 37 36.068-28.182-11.809 1.0057.49 C

ATOM 153 CD GLUA 37 36.009-29.602-11.266 1.0057.48 C

ATOM 154 OEl GLUA 37 35.934-29.763-10.026 1.0057.98 O

ATOM 155 OE2GLUA 37 36.035-30.557-12.073 1.0057.15 O ATOM 156 C GLUA 37 36.550-24.800 -9.958 1.0057.50 C

ATOM 157 O GLUA 37 35.595-24.154 -9.517 1.0057.53 O

ATOM 158 N GLUA 38 37.767-24.760 -9,417 1.0057.64 .N

ATOM 159 CA GLUA 38 38.044-23.989 -8.206 1.0057.92 C

ATOM 160 CB GLUA 38 39.439-24.302 -7.661 1.0058.10 C ATOM 161 CG GLUA 38 39.552-25.674 -7.015 1.0059.87 C

ATOM 162 CD GLUA 38 38.818-25.767 -5.682 1.0062.05 C

ATOM 163 OElGLUA 38 39.351-25.231 -4.678 1.0062.81 O

ATOM 164 OE2GLUA 38 37.719-26.384 -5.638 1.0062.50 O

ATOM 165 C GLUA 38 37.901-22.498 -8.441 1.0057.70' C ATOM 166 O GLUA 38 37.434-21.771 -7.567 1.0057.74 O

ATOM 167 N HIS A 39 38.298-22.045 -9.624 1.0057.50 N

ATOM 168 CA HIS A 39 38.240-20.627 -9,932 1.0057.36 C

ATOM 169 CB HIS A 39 39.053-20.289-11.186 1.0057.49 C ATOM 170 CG HIS A 39 39,414 -18.837 -11.301 1.0057.86 C

ATOM 171 NDl HIS A 39 39.302-18.130-12.480 1.0058.15 N

ATOM 172 CEl HIS A 39 39.687-16.882-12.283 1.0057.80 C

ATOM 173 NE2 HIS A 39 40.040-16.751-11.017 1.0058.12 N ATOM 174 CD2HISA 39 39.879-17.959-10.381 1.0057.91 C

ATOM 175 C HIS A 39 36.801-20.174-10.088 1.0057.12 C

ATOM 176 O HIS A 39 36.415-19.146 -9.542 1.0057.14 O

ATOM 177 N . TYR A 40 35.994-20.938-10.815 1.0056.95 N

ATOM 178 CA TYRA 40 34.610-20.504-10.998 1.0056.80 C ATOM 179 CB TYRA 40 34.183-20.668-12.451 1.0056.68 C

ATOM 180 CG TYRA 40 35.005-19.812-13.382 1.0056.39 C

ATOM 181 CDl TYRA 40 34.678-18.482-13.599 1.0056.19 C

ATOM 182 CEl TYRA 40 35.429-17.692-14.438 1.0056.13 C

ATOM 183 CZ TYRA 40 36.532-18.227-15.072 1.0056.27 C ATOM 184 OH TYRA 40 37.288-17.435-15.910 1.0056.35 O

ATOM 185 CE2 TYR A 40 36.884-19.546-14.866 1.0055.86 C

ATOM 186 CD2TYRA 40 36.124-20.327-14.025 1.0056.00 C

ATOM 187 C TYRA 40 33.632-21.152-10.015 1.0056.98 . C

ATOM 188 O TYRA 40 32.416-21.131-10.219 1.0056.80 O ATOM 189 N ARGA 41 34.185-21.710 -8.940 1.0057.29 N

ATOM 190 CA ARG A 41 33.402-22.199 -7.801 1.0057.67 C

ATOM 191 CB ARGA 41 32.759-21.025 -7.056 1.0057.84 C

ATOM 192 CG ARGA 41 33.747-20.264 -6.192 1.0059.24 C

ATOM 193 CD ARGA 41 34.206-21.140 -5.036 1.0061.74 C ATOM 194 NE ARG A 41 35.654-21.097 -4,852 1.0063.78 . N

ATOM 195 CZ ARGA 41 36.369-22.080 -4.309 1.0065.07 C

ATOM 196 NHl ARGA 41 37.684-21.953 -4.184 1.0065.94 N

ATOM 197 NH2 ARG A 41 35.775-23.194 -3.895 1.0065.68 N

ATOM 198 C ARG A 41 32.362-23.250 -8.179 1.0057.59 C ATOM 199 O ARGA 41 31.245-23.266 -7.656 1.00.57.63 O

ATOM 200 N PHE A 42 32.761 -24.135 -9.085 1.0057.42 N

ATOM 201 CA PHE A 42 31.940-25.247 -9.536 1.0057.25 C

ATOM 202 CB PHEA 42 32.803-26.170-10.400 1.0057.11 C

ATOM 203 CG PHEA 42 32.033-27.222-11.132 1.0056.65 C ATOM 204 CDlPHEA 42 32.041-28.533-10.692 1.0056.29 C

ATOM 205 CElPHEA 42 31.340-29.506-11.365 1.0056.21 C

ATOM 206 CZ PHE A 42 30.623-29.177-12.498 1.0056.63 C

ATOM 207 CE2PHEA 42 30.611-27.873-12.952 1.0056.58 C

ATOM 208 CD2 PHE A 42 31.315-26.905-12.271 1.0056.58 C ATOM 209 C PHEA 42 31.366-26.027 -8.358 1.0057.37 C

ATOM 210 O PHEA 42 30.240-26.520 -8.414 1.0057.37 O

ATOM 211 N GLYA 43 32.149-26.124 -7.288 1.0057.54 N

ATOM 212 CA GLYA 43 31.795-26.943 -6.133 1.0057.71 C

ATOM 213 C GLYA 43 30.592-26.473 -5.338 1.0057.88 C ATOM 214 O GLYA 43 30.052-27.222 -4.525 1.0058.01 O

ATOM 215 N SERA 44 30.171-25.234 -5.563 1.0057.99 N

ATOM 216 CA SERA 44 29.037-24.680 -4.838 1.0058.04 C

ATOM 217 CB SERA 44 29.377-23.298 -4.295 1.0057.99 C

ATOM 218 OG SERA 44 30.592-23.328 -3.568 1.0058.35 O ATOM 219 C SERA 44 27.824-24.589 -5.739 1.0058.15 C

ATOM 220 O SERA 44 26.838 -23.930 -5.401 1.0058.23 O

ATOM 221 N PHEA 45 27.900-25.257 -6.887 1.0058.23 N

ATOM 222 CA PHEA 45 26.845-25.183 -7.888 1.0058.33 C

ATOM 223 CB PHE A 45 27.270-24.285 -9.051 1.0058.38 C ATOM 224 CG PHEA 45 27.111-22.817 -8.782 1.0058.62 C

ATOM 225 CDl PHE A 45 25.873-22.207 -8.899 1.0058.76 G

ATOM 226 CEl PHEA 45 25.725-20.851 -8.657 1.0058.85 C

ATOM 227 CZ PHE A 45 26.822-20.087 -8.301 1.0058.65 C ATOM 228 CE2 PHE A 45 28.063-20.681 -8.189 1.0058.80 C

ATOM 229 CD2 PHE A 45 28.205-22.039 -8.429 1.0058.92 C

ATOM 230 C PHE A 45 26.447-26.549 -8.432 1.0058.40 C

ATOM 231 O PHEA 45 25.269-26.809 -8.653 1.0058.46 O ATOM 232 N HISA 46 27.424-27.415 -8.669 1.0058.47 N

ATOM 233 CA HIS A 46 27.135-28.696 -9.298 1.0058.57 C

ATOM 234 CB HIS A 46 27.553-28.677-10.765 1.0058.52 C

ATOM 235 CG HIS A 46 27.012-27.510-11.526 1.0058.40 C

ATOM 236 NDl HIS A 46 25.756-27.510-12.093 1.0058.69 N ATOM 237 CEl HIS A 46 25.547-26.351-12.692 1.0058.73 C

ATOM 238 NE2 HIS A 46 26.622-25.599-12.532 1.0058.60 N

ATOM 239 CD2HIS A 46 27.553-26.301-11.806 1.0058.47 C

ATOM 240 C HISA 46 27:804-29.851 -8.577 1.0058.82 C

ATOM 241 O HIS A 46 27.131-30.724 -8.041 1.0058.94 O ATOM 242 N SERA 47 29.130-29.859 -8.561 1.0059.14 N

ATOM 243 CA SERA 47 29.856-30.936 -7.907 1.0059.57 C

ATOM 244 CB SERA 47 30.256-32.001 -8.924 1.0059.49 C

ATOM 245 OG SERA 47 29.254-32.992 -9.030 1.0059.64 O

ATOM 246 C SERA 47 ^•31.089-30.454 -7.160 1.0059.92 C ATOM 247 O SERA 47 31.799-29.566 -7.632 1.0060.08 O

ATOM 248 N PROA 48 31.348-31.043 -5.984 1.0060.20 N

ATOM 249 CA PROA 48 32.579-30.774 -5.254 1.0060.54 C

ATOM 250 CB PRO A 48 32.350-31.470 -3.916 1.0060.46 C

ATOM 251 CG PRO A 48 31.373-32.544 -4.219 1.0060.43 C ATOM 252 CD PRO A 48 30.483 -32.004 -5.283 1.0060.14 C

ATOM 253 C PROA 48 33.749-31.409 -5.991 1.0060.95 C

ATOM 254 O PRO A 48 33.537-32.221 -6.893 1.0061.07 O

ATOM 255 N ALAA 49 34.970-31.039 -5.624 1.0061.39 N

ATOM 256 CA ALAA 49 36.149-31.565 -6.306 1.0061.81 C ATOM 257 CB ALAA 49 37.387-30.779 -5.919 1.0061.89 C

ATOM 258 C ALAA 49 36.341-33.046 -6.011 1.0062.05 C

ATOM 259 O ALAA 49 36.042-33.508 -4.914 1.0061.90 O

ATOM 260 N LEUA 50 .36.846-33.778 -6.999 1.0062.63 N

ATOM 261 CA LEUA 50 37.017-35.224 -6.900 1.0063.26 C ATOM 262 CB LEUA 50 37.169-35.826 -8.301 1.0063.16 C

ATOM 263 CG LEUA 50 36.104-35.424 -9.330 1.0063.07 C

ATOM 264 CDlLEUA 50 34.733-35.875 -8.873 1.0063.12 C

ATOM 265 CD2LEUA 50 ^■ 36.410-35.978-10.717 1.0062.96 C

ATOM 266 C LEUA 50 38.213-35.607 -6.020 1.0063.95 . C ATOM 267 O LEUA 50 39.139-34.817 -5.836 1.0064.09 O

ATOM 268 N GLUA 51 38.181-36.820 -5.469 1.0064.70 N

ATOM 269 CA GLUA 51 39.296-37.346 -4.683 1.0065.43 C

ATOM 270 CB GLUA 51 38.780-37.991 -3.401 1.0065.54 C

ATOM 271 CG GLUA 51 37.576-37.302 -2.788 1.0066.38 C ATOM 272 CD GLUA 51 36.647-38.289 -2.106 1.0067.59 C

ATOM 273 OElGLUA 51 36.443 -39.386 -2.671 1.0068.33 O

ATOM 274 OE2 GLU A 51 36.120-37.976 -1.013 1.0068.07 O

ATOM 275 C GLUA 51 40.026-38.398 -5.510 1.0065.74 C

ATOM 276 O GLUA 51 39.716-38.592 -6.682 1.0065.83 O ATOM 277 N ASP A 52 40.989-39.086 -4.906 1.0066.11 N

ATOM 278 CA ASP A 52 41.614-40.222 -5.571 1.0066.50 C

ATOM 279 CB ASPA 52 42.961-40.543 -4.936 1.0066.58 C

ATOM 280 CG ASP A 52 44.008-39.495 -5.242 1.0067.19 C

ATOM 281 ODlASPA 52 43.632-38.386 -5.689 1.0067.73 O ATOM _.282 OD2 ASP A 52 45.210-39.782 -5.040 1.0067.86 O

ATOM 283 C ASPA 52 40.687-41.420 -5.465 1.0066.69 C

ATOM 284 O ASP A 52 40.773-42.377 -6.245 i.OO 66.73 O

ATOM 285 N ALA A -53 39.783-41.341 -4.495 1.0066.92 N ATOM 286 CA ALAA 53 38.878-42.436 -4.184 1.0067.19 C

ATOM 287 CB ALAA 53 38.099-42.128 -2.914 1.0067.25 C

ATOM 288 C ALAA 53 37.930-42.772 -5.331 1.0067.26 C

ATOM 289 O ALAA 53 37.550-43.926 -5.503 1.0067.24 O ATOM 290 N ASP A 54 37.543-41.771 -6.113 1.0067.45 N

ATOM 291 CA ASP A 54 36.663-42.028 -7.251 1.0067.74 C

ATOM 292 CB ASP A 54 35.641 -40.899 -7.467 1.0067.90 C

ATOM 293 CG ASP A 54 36.161-39.544 -7.036 1.0068.67 C

ATOM 294 ODl ASP A 54 37.398 -39.378 -6.970 1.0069.79 O ATOM 295 OD2ASPA 54 35.333-38.646 -6.758 1.0069.03 O

ATOM 296 C ASP A 54 37.458-42.329 -8.520 1.0067.62 C

ATOM 297 O ASPA 54 36.900-42.378 -9.618 1.0067.85 O

ATOM 298 N PHEA 55 38.762-42.532 -8.353 1.0067.33 N

ATOM 299 CA PHEA 55 39.616-42.994 -9.442 1.0067.04 C ATOM 300 CB PHEA 55 40.806-42.056 -9.639 1.0067.01 C

ATOM 301 CG PHEA 55 40.448-40.743-10.259 1.0066.79 C

ATOM 302 CDlPHEA 55 40.078-39.670 -9.471 1.0066.59 C

ATOM 303 CEl PHE A 55 39.754-38.459-10.037 1.0066.30 C

ATOM 304 CZ PHE A 55 39.800-38.306-11.403 1.0066.49 C ATOM 305 CE2 PHE A 55 40.171-39.366-12.200 1.0066.62 C

ATOM 306 CD2PHEA 55 40.495-40.576-11.628 1.0066.65 C

ATOM 307 C PHEA 55 40.136-44.396 -9.151 1.0066.92 C

ATOM 308 O PHEA 55 40.288-45.209-10.061 1.0066.88 O

ATOM 309 N ASP A 56 40.415-44.669 -7.879 1.0066.74 N ATOM 310 CA ASPA 56 41.024-45.940 -7.491 1.0066.60 C

ATOM 311 CB ASPA 56 42.316-45.690 -6.707 1.0066.71 C

ATOM 312 CG ASPA 56 43.344-44.905 -7.504 1.0067.09 C

ATOM 313 ODlASPA 56 43.364-45.043 -8.747 1.0067.21 O

ATOM 314 OD2ASPA 56 44.135-44.153 -6.886 1.0067.60 O ATOM 315 C ASPA 56 40.091 -46.835 -6.674 1.0066.36 C

ATOM 316 O ASPA 56 40.544-47.576 -5.801 1.0066.42 O

ATOM 317 N GLYA 57 38.796-46.777 -6.961 1.0066.00. N

ATOM 318 CA GLYA 57 37.819-47.528 -6.182 1.0065.67 C

ATOM 319 C GLYA 57 37.046-48.534 -7.006 1.0065.47 C ATOM 320 O GLYA 57 36.955-48.408 -8.227 1.0065.50 O

ATOM 321 N LYS A 58 36.485-49.535 -6.331 1.0065.22 N

ATOM 322 CA LYS A 58 35.741-50.602 -7.000 1.0064.95 C

ATOM 323 CB LYS A 58 35.422-51.734 -6.019 1.0064.95 C

ATOM 324 CG LYS A 58 36.409-52.886 -6.068 1.0065.08 C ATOM 325 CD LYSA 58 36.419-53.661 -4.763 1.0065.47 C

ATOM 326 CE LYS A 58 35.019-54.076 -4.348 1.0065.82 C

ATOM 327 NZ LYSA 58 35.015-54.712 -2.998 1.0066.10 N

ATOM 328 C LYS A 58 34.458-50.095 -7.648 1.0064.68 C

ATOM 329 O LYS A 58 33.691 -49.365 -7.019 1.0064.72 O ATOM 330 N PRO A 59 34.226 -50.484 '-8.913 1.0064.36 N

ATOM 331 CA PROA 59 33.020-50.095 -9.642 1.0064.14 C

ATOM 332 CB PRO A 59 33.087-50.937-10.927 1.0064.07 C

ATOM 333 CG PRO A 59 34.179-51.939-10.707 1.0064.14 C

ATOM 334 CD PRO A 59 35.118-51.317 -9.734 1.0064.28 C ATOM 335 C PROA 59 31.740-50.401 -8.865 1.0063.96 C

ATOM 336 O PRO A 59 31.643-51.438 -8.205 1.0063.99 O

ATOM 337 N META 60 30.777-49.488 -8.942 1.0063.71 N

ATOM 338 CA META 60 29.481-49.666 -8.301 1.0063.49 C

ATOM 339 CB META 60 29.069-48.382 -7.572 1.0063.41 C ATOM 340 CG META 60 29.977-47.957 -6.428 1.0063.33 C

ATOM 341 SD META 60 30.125 -46.152 -6.292 1.0063.57 S

ATOM 342 CE META 60 30.571-45.961 -4.564 1.0063.70 C

ATOM 343 C META 60 28.435-49.986 -9.363 1.0063.31 C ATOM 344 O META 60 28.549-49.526-10.496 1.0063.29 O

ATOM 345 N VALA 61 27.428-50.779 -9.012 1.0063.07 N

ATOM 346 CA VALA 61 26.204-50.802 -9.810 1.0062.97 C

ATOM 347 CB VALA 61 25.898-52.180-10.449 1.0062.87 C ATOM 348 CGlVALA 61 27.161 -52.805 -10.997 1.0062.90 C

ATOM 349 CG2VALA 61 25.241 -53.104 -9.458 1.0062.98 C

ATOM 350 C VALA 61 25.049-50.335 -8.929 1.0063.00 C

ATOM 351 O VALA 61 25.021 -50.612 -7.722 1.0063.16 O

ATOM 352 N LEUA 62 24.115-49.599 -9.523 1.0062.78 N ATOM 353 CA LEUA 62 22.993-49.062 -8.769 1.00.62.54 C

ATOM 354 CB LEUA 62 22.929-47.541 -8.896 1.0062.51 C

ATOM 355 CG LEUA 62 21.760-46.869 -8.168 1.0062.61 C

ATOM 356 CDlLEUA 62 22.157-45.506 -7.620 1.0062.58 C

ATOM 357 CD2LEUA 62 20.545-46.751 -9.077 1.0062.83 C ATOM 358 C LEUA 62 21.684-49.675 -9.218 1.0062.41 C

ATOM 359 O LEUA 62 21.380-49.715-10.410 1.0062.37 O ATOM 360 N VALA 63 20.907-50.148 -8.252 1.0062.32 N

ATOM 361 CA VALA 63 19.608 τ50.731 -8.544 1.0062.19 C

ATOM 362 CB VALA 63 19.468-52.128 -7.927 1.0062.15 C ATOM 363 CGlVALA 63 18.208-52.787 -8.436 1.0062.50 C

ATOM 364 CG2VALA 63 20.684-52.982 -8.265 1.0061.99 C

ATOM 365 C VALA 63 18.481-49.830 -8.046 1.0062.07 C

ATOM 366 O VALA 63 18.360-49.577 -6.847 1.0061.99 ^' O

ATOM 367 N ALAA 64 17.666-49.344 -8.978 1.0062.00 N ATOM 368 CA ALAA 64 16.562-48.446 -8.651 1.0061.93 C

ATOM 369 CB ALAA 64^' 16.855-47.043 -9.141 1.0061.86 C

ATOM 370 C ALAA 64 15.266-48.949 -9.257 1.0061.87 C

ATOM 371 O ALAA 64 ^■ 15.275-49.792-10.146 1.0062.00 O

ATOM 372 N GLYA 65 14.153-48.418 -8.777 1.0061.82 N ATOM 373 CA GLYA 65 12.838-48.820 -9.250 1.0062.04 C

ATOM 374 C GLYA 65 11.837-48.413 -8.194 1.0062.30 C

ATOM 375 O GLYA 65 12.228-47.955 -7.118 1.0062.42 O

ATOM 376 N GLNA 66 10.549-48.562 -8.478 1.0062.45 N

ATOM 377 CA GLNA 66 9.56p -48.233 -7.464 1.0062.73 C ATOM 378 CB GLNA 66 8.301-47.616 -8.067 1.0062.81 C

ATOM 379 CG GLNA 66 7.858-48.190 -9.387 1.0063.71 C.

ATOM 380 CD GLNA 66 6.754-47.355-10.012 1.0064.68 C

ATOM 381 OEl GLNA 66 5.905 -46.794 -9.305 1.0065.17 O

ATOM 382 NE2 GLN A 66 6.760-47.264-11.340 1.0065.07 N ATOM 383 C GLN A.66 9.240 -49.424 -6.577 1.0062.78 C

ATOM 384 O GLNA 66 9.877-50.470 -6.685 1.0062.88 O

ATOM 385 N TYRA 67 . 8.263-49.258 -5.694 1.0062.88 N

ATOM 386 CA TYRA 67 7.972-50.258 -4.673 1.0062.98 C

ATOM 387 CB TYRA 67 6.770-49.831 -3.825 1.0063.32 C ATOM 388 CG TYRA 67 7.016 -48.619 -2.953 1.0063.88 C

ATOM 389 CDlTYRA 67 6.105-47.566 -2.918 1.0064.41 C

ATOM 390 CEl TYRA 67 6.324-46.451 -2.112 1.0064.56 C

ATOM 391 CZ TYRA 67 7.470-46.381 -1.336 1.0064.29 C

ATOM 392 OH TYRA 67 7.695-45.278 -0.537 1.0064.28 O ATOM 393 CE2TYRA 67 8.389-47.414 -1.356 1.0064.30 C

ATOM 394 CD2 TYR A 67 8.160 -48.526- -2.162 1.0064.33 C

ATOM 395 C TYRA 67 7.728-51.655 -5.232 1.0062.84 C.

ATOM 396 O TYRA 67 7.053-51.824 -6.246 1.0062,73 O

ATOM 397 N SERA 68 8.293-52.648 -4.550 1.0062.73 N ATOM 398 CA SERA 68 8.040-54.060 -4.830 1.0062.58 C

ATOM 399 CB SERA 68 6.600-54.438 -4.459 1.0062.63 C

ATOM 400 OG SERA 68 6.339-54.184 -3.086 1.0062.93 O

ATOM 401 C SERA 68 8.328-54.439 -6.272 1.0062.40 C ATOM 402 O SERA 68 7.649-55.288 -6.848 1.0062.68 O

ATOM 403 N THRA 69 9.338-53.814 -6.858 1.0061.97 N

ATOM 404 CA THRA 69 9.697-54.129 -8.225 1.0061.63 C

ATOM 405 CB THRA 69 10.267-52.907 -8.953 1.0061.73 C ATOM 406 OGlTHRA 69 9.623-51.719 -8.480 1.0061.90 O

ATOM 407 CG2THRA 69 10.026-53.030-10.435 1.0062.25 G

ATOM 408 C THRA 69 10.712-55.266 -8.232 1.0061.26 C

ATOM 409 O THRA 69 11.031-55.832 -9.276 1.0061.25 O

ATOM 410 N. GLYA 70 11.222-55.596 -7.053 1.0060.94 N ATOM 411 CA GLYA 70 12.143-56.715 -6.910 1.0060.52 C

ATOM 412 C GLYA 70 13.612-56.350 -6.934 1.0060.22 C

ATOM 413 O GLYA 70 14.435-57.156 -7.334 1.0060.21 O

ATOM 414 N LYSA 71 13.950-55.138 -6.507 1.0060.02 N

ATOM 415 CA LYS A 71 15.344-54.712 -6.478 1.0059.94 C ATOM 416 CB LYSA 71 15.440-53.272 -5.986 1.0059.83 C

ATOM 417 CG LYS A 71 14.957-52.237 -6.980 1.0059.55 C

ATOM 418 CD LYSA 71 14.638-50.922 -6.287 1.0058.81 C

ATOM 419 CE LYS A 71 13.242-50.955 -5.692 1.0058.14 C

ATOM 420 NZ LYSA 71 13.111_T50.011 -4.562 1.0057.62 N ATOM 421 C LYS A 71 16.170-55.620 -5.570 1.0060.06 C

ATOM 422 O LYSA 71 17.156-56.244 -5.998 1.0060.25 O

ATOM 423 N THRA 72 15.754.55.686 -4.309 1.0060.04 N

ATOM 424 CA THRA 72 16.436-56.494 -3.314 1.0060.09 C

ATOM 425 CB THRA 72 15.698-56.451 -1.955 1.0060.10 C ATOM 426 OGlTHRA 72 15.224-55.121 -1.7031.0060.02 O

ATOM 427 CG2THRA 72 16.626-56.878 -0.824 1.0060.05 C

ATOM 428 C THRA 72 16.548-57.931 -3.814 1.0060.14 C

ATOM 429 O THRA 72 17.605-58.562 -3.702 1.0060.40 O

ATOM 430 N SERA 73 15.457-58.438 -4.382 1.0060.12 N ATOM 431 CA SERA 73 15.446-59.783 -4.939 1.0060.22 C

ATOM 432 CB SERA 73 14.064-60.131 -5.502 1.0060.26 C

ATOM 433 OG SERA 73 13.120-60.336 -4.462 1.0059.98 O

ATOM 434 C SERA 73 16.501-59.901 -6.027 1.0060.19 C

ATOM 435 O SERA 73 17.298-60.825 -6.042 1.0060.56 O ATOM 436 N PHEA 74 16.496-58.942 -6.936 1.0060.20 N

ATOM 437 CA PHE A 74 17.456-58.885 -8.016 1.0060.14 C

ATOM 438 CB PHEA 74 17.294-57.558 -8.748 1.0060.03 C

ATOM 439 CG PHEA 74 18.223-57.383 -9.900 1.0060.15 C

ATOM 440 CDlPHEA 74 18.013-58.066-11.083 1.0060.37 C ATOM 441 CEl PHE A 74 18.866-57.899-12.147 1.0060.41 C

ATOM 442 CZ PHEA 74 19.937-57.033-12.040 1.0060.50 C

ATOM 443 CE2PHEA 74 20.148-56.342-10.870 1.0060.12 C

ATOM 444 CD2 PHE A 74 19.297-56.517 -9.810 1.0060.02 . C

ATOM 445 C PHEA 74 18.876-59.038 -7.486 1.0060.19 C ATOM 446 O PHEA 74 19.623-59.913 -7.925 1.0060.38 O

ATOM 447 N ILEA 75 19.247-58.192 -6.532 1.0060.27 N

ATOM 448 CA ILEA 75 20.599-58.260 -5.988 1.0060.40 C

ATOM 449 CB ILE A 75 20.862-57.131 -4.989 1.0060.26 C

ATOM 450 CGl ILE A 75 20.540-55.781 -5.625 1.0060.08 C ATOM 451 CDlILEA 75 20.666-54.622 -4.673 1.0059.79 C ATOM . 452 CG2 ILE A 75 22.305-57.159 -4.530 1.0060.22 C

ATOM 453 C ILEA 75 20.850-59.613 -5.324 1.0060.71 C

ATOM 454 O ILEA 75 21.862-60.278 -5.584 1.0061.02 O

ATOM 455 N. GLNA 76 19.915-60.007 -4.464 1.0060.91 N ATOM 456 CA GLNA 76 . 19.933-61.311 -3.814 1.0061.22 C

ATOM 457 CB GLNA 76 18.538-61.595 -3.263 1.0061.23 C

ATOM 458 CG GLNA 76 18.435-62.776 -2.330 1.0062.03 C

ATOM 459 CD GLNA 76 18.200-62.353 -0.894 1.0063.06 C ATOM 460. OEl GLNA 76 17.409-62.972 -0.176 1.0063.47 O

ATOM 461 NE2GLNA 76 18.873-61.282 -0.471 1.0063.36 N

ATOM 462 C GLNA 76 20.292-62.381 -4.840 1.0061.30 C

ATOM 463 O GLNA 76 21.096-63.280 -4.589 1.0061.68 O ATOM 464 N TYRA 77 19.678-62.242 -6.009 1.0061.31 N

ATOM 465 CA TYRA 77 19.786-63.181 -7.115 1.0061.46 . C

ATOM 466 CB TYRA 77 18.682-62.874 -8.125 1.0061.45 C

ATOM 467 CG TYRA 77 18.636-63.776 -9.326 1.0061.46 . C

ATOM 468 CDlTYRA 77 18.978-63.300-10.583 1.0061.59 C ATOM 469 CEl TYRA .77 18.919-64.117-11.698 1.0061.89 C

ATOM 470 CZ TYRA 77 18.512 ^"-65.428 -11.559 1.0061.81 C

ATOM 471 OH TYRA 77 18.455-66.244-12.661 1.0061.74 O

ATOM 472 CE2TYRA 77 18.163 -65.923 -10.318 1.0061.90. C

ATOM 473 CD2TYRA 77 18.227-65.097 -9.212 1.0061.71 C ATOM 474 C TYRA 77. 21.145-63.093 -7.791 1.0061.48 C

ATOM 475 O TYRA 77 21.713-64.112 -8.184 1.0061.51 O

ATOM 476 N LEUA 78 21.659-61.874 -7.936 1.0061.31 N

ATOM 477 CA LEUA 78 22.991-61.687 -8.493 1.0061.65 C

ATOM 478 CB LEUA 78 23.306 -60.206 -8.664 1.0061.70 C ATOM 479 CG LEUA 78 22.978-59.629-10.039 1.0062.28 C ATOM '480 CDlLEUA 78 23.121-58.112-10.024 1.0062.88 C

ATOM 481 CD2LEUA 78 23.908-60.242-11.070 1.0062.72 C

ATOM 482 C LEUA 78 24.031-62.325 -7.596 1.0061.78 C

ATOM 483 O LEUA 78 24.988-62.939 -8.069 1.0061.79 O ATOM 484 N LEUA 79 23.837-62.181 -6.292 1.0061.84 N

ATOM 485 CA LEUA 79 24.798-62.702 -5.341 LOO 62.22 C

ATOM 486 CB LEUA 79 24.754-61.888 -4.051 1.0062.29 C

ATOM 487 CG LEUA 79 25.012-60.386 -4.176 1.0062.42 C

ATOM 488 CDlLEUA 79 25.014-59.736 -2.800 1.0062.58 C ATOM 489 CD2 LEU A 79 26.324-60.120 -4.896 1.0062.69 C

ATOM 490 C LEUA 79 24.547-64.168.-5.032 1.0062.47 C

ATOM 491 O LEUA 79 25.397-64.833 -4.439 1.0062.39 O

ATOM 492 N GLUA 80 23.383-64.668 -5.440 1.0062.76 N

ATOM 493 CA GLUA 80 22.942-66.001 -5.034 1.0063.58 C ATOM 494 CB GLUA 80 23.637-67.091 -5.852 1.0063.72 C

ATOM 495 CG GLUA 80 23.051-67.293 -7.250 1.0065.58 C

ATOM 496 CD GLUA 80 22.042-68.443 -7.324 1.0068.13 C

ATOM 497 OEl GLUA 80 22.412-69.522 -7.867 1.0069.12 O

ATOM 498 OE2GLUA 80 20.888-68.278 -6.838 1.0068.88 O ATOM 499 C GLUA 80 23.214 -66.180 -3.544 1.0063.57 C

ATOM 500 O GLUA 80 23.706-67.219 -3.106 1.0063.47 O

ATOM 501 N GLNA 81 22.899-65.133 -2.784 1.0063.78 N

ATOM 502 CA GLNA 81 23.086-65.106 -1.342 1.0063.93 C

ATOM 503 CB GLNA 81 24.562-64.900 -0.993 1.0063.84 C ATOM 504 CG GLNA 81 24.847-64.947 0.504 1.0063.39 C

ATOM 505 CD GLNA 81 26.324-64.864 0.824 1.0062.75 C

ATOM 506 OElGLNA 81 26.739-65.199 1.929 1.0063.13 O

ATOM 507 NE2 GLN A 81 27.127-64.417 -0.137 1.0062.73 N

ATOM 508 C GLNA 81 22.239-63.987 -0.731 1.0064.17 C ATOM 509 O GLNA 81 22.026-62.952 -1.361 1.0064.15 O

ATOM 510 N GLUA 82 21.757-64.204 0.492 1.0064.47 N

ATOM 511 CA GLUA 82 20.916-63.227 1.182 1.0064.72 ^• C

ATOM 512 CB GLUA 82 . 20.083-63.910 2.277 1.0064.74 C

ATOM 513 CG GLUA 82 18.846-63.123 2.712 1.0065.36 C ATOM 514 CD GLUA 82 17.597-63.996 2.870 1.0066.14 C

ATOM 515 OElGLUA 82 17.685 -65.080 3.490 1.0066.18 - O

ATOM 516 OE2GLUA 82 16.520 -63.591 2.372 1.0066.28 O

ATOM 517 C GLUA 82 21.732-62.057 1.748 1.0064.81 C ATOM 518.0 GLUA 82 22.863 -62.233 2.202 1.0064.77 O

ATOM 519 N VALA 83 21.152-60.862 1.705 1.0064.99 N

ATOM 520 CA VALA 83 21.825 -59.654 2.169 1.0065.07 C

ATOM 521 CB VALA 83 21.294-58.413 1.439 1.0065.06 C

ATOM 522 CGlVALA 83 22.242 -57.244 I 1.628 1.0065.06 C

ATOM 523 CG2VALA 83 21.098 -58.712 » -0.036 1.0064.87 C

ATOM 524 C VALA 83 21.638 -59.465 3.673 1.0065.23 C

ATOM 525 O VALA 83 20.509 -59.404 4.157 1.0065.10 O

ATOM 526 N PROA 84 22.752 -59.365 4.414 ^■ 1.0065.51 N

ATOM 527 CA PROA 84 22.753 -59.247 5.869 1.0065.77 C

ATOM 528 CB PROA 84 24.156-58.723 6.168 1.0065.66 C

ATOM 529 CG PRO A 84 24.990-59.315 5.100 1.0065.56 C

ATOM 530 CD PROA 84 24.120-59.365 3.867 1.0065.53 C

ATOM 531 C PROA 84 21.706-58.275 6.401 1.0066.15 C

ATOM 532 O PROA 84 20.987 -58.603 7.342 1.0066.22 O

ATOM 533 N GLYA 85 21.616-57.094 5.802 1.0066.61 N

ATOM 534 CA GLY A 85 20.694 -56.072 6.282 1.0067.21 C

ATOM 535 C GLYA 85 19.347 -56.044 5.581 1.0067.67 C

ATOM 536 O GLYA 85 18.320 -55.785 6.211 1.0067.61 O

ATOM 537 N SERA 86 19.348-56.313' 4.278 1.0068.17 N

ATOM 538 CA SERA 86 18.144-56.150 3.456 1.0068.71 C

ATOM 539 CB SERA 86 18.514-55.711 2.031 1.0068.74 C

ATOM 540 OG SERA 86 18.520 -54.297 1.904 1.0068.90 O

ATOM 541 C SERA 86 17.225 -57.374 3.398 1.0069.01 C

ATOM 542 O SERA 86 •17.554-58.386 2.769 1.0069.11 O

ATOM 543 N ARGA 87 16.065 -57.263 4.044 1.0069.32 N

ATOM 544 CA ARG A 87 15.015 -58.266 3.918 I 1.0069.63 C

ATOM 545 CB ARGA 87 14.122 -58.274 5.161 1.0069.53 C

ATOM 546 CG ARGA 87 15.231 -59.653 5.857 ' 0.0050.00 C

ATOM 547 CD ARGA 87 14.525-60.115 7.11C I 0.0050.00 C

ATOM 548 NE ARG A 87 13.769-61.343 6.893 0.0050.00 N

ATOM 549 CZ ARGA 87 14.263 -62.572 6.969 0.0050.00 C

ATOM _.550 NHl ARG A 87 13.467-63.609 6.740 0.0050.00 N

ATOM 551 NH2ARGA 87 15.528 -62.779 7.297 0.0050.00 N

ATOM 552 C ARGA 87 14.181 -57.999 2.661 1.0069.92 C

ATOM 553 O ARGA 87 14.475 -57.085 1.888 1.0069.93 O

ATOM 554 N VALA 88 13.143 -58.803 2.461 1.0070.32 N

ATOM 555 CA VALA 88 12.278 -58.678 1.289 > 1.0070.65 C

ATOM 556 CB VALA 88 12.785 -59.565 0.124 1.0070.63 C

ATOM 557 CGl VAL A 88 11.662 -59.87^ 5 -0.855 1.0070.52 C

ATOM 558 CG2VALA 88 13.398-60.85* 5 0.661 1.0070.76 C

ATOM 559 C VALA 88 10.836-59.035 1.655 1.0070.97 C

ATOM 560 O VALA 88 10.594 -59.997 2.389 1.0071.03 O

ATOM 561 N GLYA 89 9.881 -58.255 1.157 1.0071.28 N

ATOM 562 CA GLYA 89 8.480 -58.471 1.506 LOO 71.78 C

ATOM 563 C GLYA 89 7.485 -57.882 0.527 1.0072.17 C

ATOM 564 O GLYA 89 7.873-57.243 - -0.451 1.0072.08 O

ATOM 565 N PRO A 90 6.184-58.087 0.798 1.0072.59 N

ATOM 566 CA PRO A 90 5.083 -57.648 -0.065 1.0072.92 C

ATOM 567 CB PROA 90. 3.845 -58.251 0.610 1.0072.90 C

ATOM 568 CG PRO A 90 4.241 -58.441 2.041 1.0072.85 C

ATOM. 569 CD PRO A 90 5.703 -58.771 2.013 1.0072.65. C

ATOM 570 C PROA 90 4,977-56.126 -0.118 1.0073.27 C

ATOM 571 O PROA 90 5.542-55.499 - •1.017 1.0073.27 O

ATOM 572 N GLUA 91 4.254 -55.546 0.838 1.0073.71 ^'N

ATOM 573 CA GLUA 91 4.167-54.094 0.976 1.0074.09 C

ATOM 574 CB GLUA 91 3.095 -53.714 2.008 1.0074.13 C

ATOM 575 CG GLUA 91 1.660-53.941 1.538 1.0074.32 C ATOM 576 CD GLUA 91 1.490-53.220 -0.578 0.0050.00 C

ATOM 577 OEl GLUA 91 0.483 -53.953 -0.6660.0050.00 O

ATOM 578 OE2GLUA 91 2.188-52.915 -1.575 0.0050.00 O

ATOM 579 C GLUA 91 5.529-53.526 1.387 1.0074.25 C ATOM 580 O GLUA 91 6.255-54.168 2.151 1.0074.34 O

ATOM 581 N PRO A 92 5.874-52.323 0.876 1.0074.34 N

ATOM 582 CA PRO A 92 7.138-51.615 1.101 1.0074.34 C

ATOM 583 CB PRO A 92 6.734-50.133 0.987 1.0074.35 C

ATOM 584 CG PRO A 92 5.317-50.122 0.401 1.0074.33 C ATOM 585 CD PROA 92 4.987-51.535 0.006 1.0074.39 C

ATOM 586 C PROA 92 7.772-51.884 2.471 1.0074.33 C

ATOM 587 O PRO A 92 7.109-51.737 3.508 1.0074.31 O

ATOM 588 N THRA 93 9.052-52.260. 2.465 1.0074.15 N

ATOM 589 CA THRA 93 9.754-52.645 3.695 1.0073.95 C ATOM 590 CB THRA 93 10.189-54.133 3.657 1.0074.06 C

ATOM 591 OGlTHRA 93 10.591-54.490 2.311 1.0073.87 O

ATOM 592 CG2THRA 93 9.031-55.058 4.114 1.0074.23 C

ATOM 593 C THRA 93 10.968-51.770 4.024 1.0073.59 C

ATOM 594 O THRA 93 10.972-51.057 5.034 1.0073.58 O ATOM 595 N THRA 94 11.993-51.839 3.172 1.0073.13 N

ATOM 596 CA THRA 94 13.241-51.097 3.381 1.0072.66 C

ATOM 597 CB THRA 94. 14.380-51.644 2.474 1.0072.80 C

ATOM 598 OGl THRA 94 . 13.974-51.598 1.095 1.0072.65 O

ATOM 599 CG2THRA 94 14.720-53.088 2.846 1.0072.95 C ATOM 600 C THRA 94 13.058-49.593 3.137 1.0072.18 C

ATOM 601 O THRA 94 12.441-49.188 2.150 1.0072.21 O

ATOM 602 N ASP A 95 13.600-48.767 4.031 1.0071.45 N

ATOM 603 CA ASP A 95 13.381-47.320 3.956 1.0070.73 C

ATOM 604 CB ASP A 95 12.585-46.839 5.180 1.0070.79 C ATOM 605 CG ASPA 95 12.336-46.932 5.763 0.0050.00 C

ATOM 606 ODl ASPA 95 12.950-47.842 6.3970.0050.00 O

ATOM 607 OD2 ASP A 95 11.658-46.098 6.418 0.0050.00 O

ATOM 608 C ASP A 95 14.665-46.498 3.814 1.0070.16 C

ATOM 609 O ASPA 95 14.738-45.367 4.304 1.0070.07 O ATOM 610 N CYS A 96 15.665-47.052 3.131 1.0069.46 N

ATOM 611 CA CYSA 96 . 16.933-46.343 2.957 1.0068.81 C

ATOM 612 CB CYS A 96 17.698-46.296 4.282 1.0068.91 C

ATOM 613 SG CYS A 96 18.497-47.853 4.720 1.0069.45 S

ATOM 614 C CYS A 96 17.834-46.935 1.869 1.0068.20 C ATOM 615 O CYSA 96 17.435-47.834 1.130 1.0068.12 O

ATOM 616 N PHEA 97 19.053-46.408 1.785 1.0067.48 N

ATOM 617 CA PHEA 97 20.049-46.870 0.830 1.0066.69 C

^' ATOM 618 CB PHEA 97 20.914-45.706 0.345 1.0066.64 ' C

ATOM 619 CG PHEA 97 20.172-44.689 -0.467 1.0066.32 C ATOM .620 CDl PHEA 97 19.322-43.780 0.142 1.0066.08 C

ATOM 621 CElPHEA 97 18.640-42.841 -0.602 1.0065.88 C

ATOM 622 CZ PHEA 97 18.811-42.793 -1.968 1.0066.18 C

ATOM 623 CE2 PHE A 97 19.662-43.688 -2;588 1.0066.18 C

ATOM 624 CD2PHEA 97 20.339-44.627 -1.838 1.0066.18 C ATOM 625 C PHEA 97 20.950-47.902 1.482.1.0066.32 C

ATOM 626 O PHEA 97 21.532-47.657 2.538 1.0066.17 O

ATOM 627 N VALA 98 21.068-49.056 0.843 1.0065.88 N

ATOM 628 CA VALA 98 21.934-50.108 1.335 1.0065.43 C

ATOM 629 CB VALA 98 21.178-51.438 1.474 1.0065.36 C ATOM 630 CGlVALA 98 22.070-52.488 2.108 1.0065.18 . C

ATOM 631 CG2VALA 98 19.913-51.243 2.288 1.0065.13 C

ATOM 632 C VALA 98 23.090-50.287 0.368 1.0065.26 C

ATOM 633 O VALA 98 22.889-50.620 -0:797 1.0065.27 O ATOM 634 N ALAA 99 24.301 -50.050 0.849 1.0065.07 N

ATOM 635 CA ALAA 99 25.478-50.225 0.022 1.0065.02 C

ATOM 636 CB ALAA 99 26.521-49.179 0.359 1.0065.00 C

ATOM 637 C ALAA 99 26.039-51.619 0.225 1.0065.03 C ATOM 638 O ALAA 99 26.838-51.847 1.129 1.0065.09 O

ATOM 639 N VALAlOO 25.609-52.555 -0.609 1.0065.12 N

ATOM 640 CA VALAlOO 26.105-53.922 -0.520 1.0065.24 C ATOM 641 CB VALAlOO 25.193-54.914 -1.267 1.0065.20 C

ATOM 642 CGl VALA 100 23.733 -54.672 -0.914 1.0065.10 C ATOM 643 CG2VALA100 25.600-56.345 -0.952 1.0065.15 C

ATOM 644 C VALAlOO 27.512-53.995 -1.097 1.0065.39 C

ATOM 645. O VALAlOO 27.699-53.938 -2.313 1.0065.48 O

ATOM 646 N METAlOl 28.501 -54.107 -0.218 1.0065.56 N

ATOM 647 CA METAlOl 29.894-54.161 -0.638 1.0065.78 C ATOM 648 CB METAlOl 30.600-52.850 -0.311 1.0065.79 C

ATOM 649 CG METAlOl 30.252-52.294 1.058 1.0065.81 CATOM 650 SD METAlOl 31.344-50.959 L580 1.0065.65 S

ATOM 651 CE METAlOl 31.250-49.849 0.175 1.0065.57 C

ATOM 652 C METAlOl 30.610-55.317 0.034 1.0066.02 C ATOM 653 O METAlOl 30.052-55.978 0.907 1.0066.05 O

ATOM 654 N HIS A 102 31.850-55.559 -0.369 1.0066.39. N

ATOM 655 CA HIS A 102 • 32.607-56.667 0.190 1.0066.80 C

ATOM 656 CB HIS A 102 33.918-56.881 -0.569 1.0066.73 C

ATOM 657 CG HIS A 102 34.629-58.142 -0.189 1.0066.79 C ATOM 658 NDl HIS A 102 34.164-59.392 -0.540 1.0066.68 N

ATOM 659 CEl HIS A 102 34.983-60.313 -0.064 1.0066.49 C

ATOM 660 NE2 HIS A 102 35.961-59.706 0.586 1.0066.63 N

ATOM 661 GD2HISA102 35.762-58.347 0.525 1.0066.78 C

ATOM 662 C HIS A 102 32.873-56.459 1.678 1.0067.13 C ATOM 663 O HIS A 102 32.449-55.465 2.262 1.0067.23 O

ATOM 664 N GLYA 103 33.572-57.408 2.285 1.0067.46 N

ATOM 665 CA GLY A 103 33.879-57.341 3.700 1.0067.99 C

ATOM 666 C GLY A 103 34.212-58.729 4.186 1.0068.39 C

ATOM 667 O GLYA 103 33.727-59.715 3.636 1.0068.41 O ATOM 668 N GLU A 104 35.045-58.812 5.216 1.0068.82 N

ATOM 669 CA GLU A 104 35.493-60.105 5.708 1.0069.31 C

ATOM 670 CB GLU A 104 36.829 -59.968 6.450 1.0069.45 C

ATOM 671 CG GLU A 104 37.433 -61.291 6.923 1.0070.31 C

ATOM 672 CD GLU A 104 37.326-62.411 5.885 1.0071.40 C ATOM 673 OEl GLU A 104 36.942 -62.136 4.723 1.0071.64 O

ATOM 674 OE2 GLU A 104 37.624 -63.575 6.240 1.0071.78 O

ATOM 675 C GLUA 104 34.434 -60.790 6.577 1.0069.42 C

ATOM 676 O GLUA 104 34.245 -62.007.6.501 1.0069.49 O

ATOM 677 N THRA 105 33.737-60.003 7.389 1.0069.53 N ATOM 678 CA THR A 105 32.691-60.542 8.248 1.0069.56 C

ATOM 679 CB THR A 105 32.845-60.049 9.707 1.0069.61 C

ATOM 680 OGl THRA 105 32.017-60.837 10.572 1.0069.65 O

ATOM 681 CG2THRA105 32.457 -58.573 9.830.1.0069.72. C

ATOM 682 C THR A 105 31.305-60.172 7.723 1.0069.52 C ATOM 683 O THRA 105 31.111-59.099 7.147 1.0069.53 O

ATOM 684 N GLU A 106 30.349-61.075 7.909 1.0069.46 N

ATOM 685 CA GLU A 106 28.960-60.778 7.594 1.0069.46 C

ATOM 686 CB GLUA 106 28.137-62.066 7.517 1.0069.51 C ATOM 687 CG GLU A 106 28.455 -62.949 6.315 1.0069.53 C ATOM 688 CD GLUA 106 27.789-64.318 6.394 1.0069.39 C

ATOM 689 OEl GLU A 106 27.490 -64.754 7.573 1.0069.37 O

ATOM 690 OE2 GLUA 106 27.562 -64.963 5.282 1.0068.93 O

ATOM 691 C GLUA 106 28.399 -59.863 8.674 1.0069.46 C ATOM 692 O GLU A 106 28.645 -60.073 9.860 1.0069.46 O

ATOM 693 N GLY A 107 27.650 -58.845 8.265 1.0069.47 • N

ATOM 694 CA GLY A 107 27.084 -57.896 9.216 1.0069.50 C

ATOM 695 C GLYA 107 26.766-56.551 8.593 1.0069.52 C

ATOM 696 O GLYA 107 26.771 -56.407 7.370 1.0069.51 O

ATOM 697 N THRA 108 26.489 -55.562 9.439 1.0069.51 N

ATOM 698 CA THRA 108 26.095 -54.240 8.965 1.0069.49 C

ATOM 699 CB THRA 108 24.573 -54.020 9.092 1.0069.48 C

ATOM 700 OGl THRA 108 24.213 -53.964 10.478 1.0069.55 O

ATOM 701 CG2 THRA 108 23.798 -55.139 8.407 1.0069.46 C

ATOM 702 C THR A 108 26.787-53.116 9.725 1.0069.49 C

ATOM 703 O THR A 108 27.509-53.354 : 10.695 1.0069.48 O

ATOM 704 N VALA 109 26.546-51.890 9.267 1.0069.49 N

ATOM 705 CA VALA 109 27.063 -50.680 9.901 1.0069.46 C

ATOM 706 CB VALA 109 28.614 -50.660 9.921 1.0069.47 C

ATOM 707 CGl VAL A 109 29.132-49.424 10.648 1.0069.54 C

ATOM 708 CG2VALA109 29.180-50.750 8.506 1.0069.55 C

ATOM 709 C VALA 109 26.507 -49.450 9.173 1.0069.39 C

ATOM 710 O VALA 109 26.653 -49.325 7.956 1.0069.42 O

ATOM 711 N PROAIlO 25.843 -48.548 9.916 1.0069.28 N

ATOM 712 CA PROAIlO 25.193 -47.376 9.325 1.0069.20 C

ATOM 713 CB PROAIlO 24.058 -47.076 10.311 1.0069.20 C

ATOM 714 CG PROAIlO 24.501 -47.667 11.623 1.0069.19 C

ATOM 715 CD PROAIlO 25.653 -48.608 11.376 1.0069.25 C

ATOM 716 C PROAIlO 26.098 -46.150 9.166 1.0069.09 C

ATOM 717 O PROAIlO 25.916-45.155 9.869 1.0069.13 O

ATOM 718 N GLYAlIl 27.048 -46.216 8.237 1.0068.96 N

ATOM 719 CA GLYAlIl 27.942 -45.089 7.969 1.0068.85 C

ATOM 720 C GLYAlIl 28.984 -44.872 9.058 1.0068.81 C

ATOM 721 O GLYAlIl 28.844 -43.965 9.917 1.0068.65 O

ATOM 722 N ASNA 130 26.659-31.270 8.342 1.0066.96 N

ATOM 723 CA ASN A 130 25.386 -30.849 7.759 1.0067.00 C

ATOM 724 CB ASN A 130 25.594 -29.640 6.836 1.0066.96 C

ATOM 725 CG ASNA 130 24.279 -29.020 6.381 1.0066.90 C

ATOM 726 ODl ASN A 130 23.843 -28.004 6.943 1.0066.78 O

ATOM 727 ND2ASNA130 23.636 -29.635 5.364 1.0066.61 N

ATOM 728 C ASN A 130 24.650-31.973 7.012 1.0067.05 C

ATOM 729 O ASN A 130 23.429-32.106 7.132 1.0067.08 O.

ATOM 730 N THRA 131 25.399 -32.772 6.249 1.0067.04 N

ATOM 731 CA THRA 131 24.833 -33.856 5.424 1.0066.97 C

ATOM 732 CB THRA 131 25.900 -34.450 4.459 1.0066.99 C

ATOM 733 OGl THRA 131 25.543 -35.792 ! 4.101 1.0066.77 O

ATOM 734 CG2 THRA 131 27.277 -34.460 i 5.115 1.0067.17 C

ATOM 735 C. THRA 131 24.178 -34.980 6.243 1.0066.94. C

ATOM 736 O THRA 131 24.347 -35.054 7.465 1.0066.93 O

ATOM 737 N PHE A 132 23.431 -35.851 5.561 1.00.66.81 N

ATOM 738 CA PHE A 132 22.674 -36.912 6.232 1.0066.68 C

ATOM 739 CB PHE A 132 21.172-36.602 6.205 1.0066.71 C

ATOM 740 CG PHE A 132 20.815 -35.278 6.826 1.0066.79 C

ATOM 741 CDl PHE A 132 20.191 -34.290 6.077 1.0066.90 C

ATOM 742 CEl PHE A 132. 19.863 -33.064 6.649 1.0067.27 C

ATOM 743 CZ PHE A 132 20.166-32.814 7.982 1.0067.02 C

ATOM 744 CE2PHEA132 20.793 -33.791. 8.737 1.0067.01 C

ATOM 745 CD2 PHE A 132 21.116-35.015 8.158 1.0066.90 C

ATOM ^' 746 C PHEA 132 22.947-38.316 5.680 1.0066.58 C

ATOM 747 O PHE A 132 22.646 -38.620 4.521 1.0066.52 O

ATOM 748 N LEUA 133 23.516-39.165 6.534 1.0066.41 N

ATOM 749 CA LEUA 133 23.870 -40.539 6.181 1.0066.14 C ATOM 750 CB LEU A 133 25.374 -40.769 6.373 1.00 66.19 C ATOM 751 CG LEU A 133 26.382 -40.435 5.265 1.00 66.22 C ATOM 752 CDl LEU A 133 26.089 -39.104 4.584 1.00 66.32 C ATOM 753 CD2 LEU A 133 27.804 -40.457 5.821 1.00 66.13 C ATOM 754 C LEU A 133 23.101 -41.546 7.032 1.00 65.93 C ATOM 755 O LEU A 133 23.329 -42.751 6.937 1.00 65.82 O ^' ATOM 756 N ASN A 134 22.205 -41.051 7.882 1.00 65.76 N ^' ATOM 757 CA ASN A 134 21.409 -41.930 8.732 1.00 65.55 C • ATOM 758 CB ASN A 134 20.734 -41.148 9.863 1.00 65.55 C ATOM 759 CG ASN A 134 20.140 -42.057 10.930 1.00 65.49 C ATOM 760 ODl ASN A 134 19.314 -41.627 11.736 1.00 65.41 O ATOM 761 ND2 ASN A 134 20.560 -43.319 10.938 1.00 65.26 N ATOM 762 C ASN A 134 20.373 -42.672 7.900 1.00 65.39 C ATOM 763 O ASN A 134 19.824 -43.690^' 8.326 1.00 65.43 O ATOM 764 N ARG A 135 20.112 -42.146 6.707 1.00 65.09 N ATOM 765 CA ARG A 135 19.287 -42.836 5.734 1.00 64.81 C ATOM 766 CB ARG A 135 18.497 -41.831 4.894 1.00 64.75 C ATOM 767 CG ARG A 135 17.760 -40.714 5.123 0.00 50.00 C ATOM 768 CD ARG A 135 17.421 -39.538 4.310 0.00 50.00 C ATOM 769 NE ARG A 135 18.323 -38.615 3.780 0.00 50.00 N ATOM 770 CZ ARG A 135 18.391 -37.354 3.482 0.00 50.00 C ATOM 771 NHl ARG A 135 19.376 -36.980 2.625 0.00 50.00 N ATOM 772 NH2 ARG A 135 17.696 -36.373 4.013 0.00 50.00 N ATOM 773 C ARG A 135 20.213 -43.669 4.857 1.00 64.65 C ATOM 774 O ARG A 135 19.912 -43.944 3.695 1.00 64.66 O ATOM 775 N PHE A 136 21.344 -44.072 5.431 1.00 64.44 N ATOM 776 CA PHE A 136 22.377 -44.795 4.695 1.00 64.19 C ATOM 777 CB PHE A 136 23.496 -43.832 4.295 1.00 64.24 C ATOM 778 CG PHE A 136 24.064 -44.089 2.932 1.00 64.14 C ATOM 779 CDl PHE A 136 23.904 -43.155 1.919 1.00 64.00 C ATOM 780 CEl PHE A 136 24.424 -43.377 0.663 1.00 64.15 C ATOM 781 CZ PHE A 136 25.111 -44.548 0.403 1.00 64.46 C ATOM 782 CE2 PHE A 136 25.277 -45.491 1.407 1.00 64.42 C ATOM 783 CD2 PHE A 136 24.756 -45.257 2.662 1.00 64.17 C ATOM 784 C PHE A 136 22.959 -45.939 5.525 1.00 63.99 C ATOM 785 O PHE A 136 23.550 -45.718 6.586 1.00 63.97 O ATOM 786 N MET A 137 22.793 -47.160 5.028 1.00 63.68 N ATOM 787 CA MET A 137 23.301 -48.347 5.703 1.00 63.43 C ATOM 788 CB MET A 137 22.165 -49.343 5.945 1.00 63.62 C ATOM 789 CG MET A 137 21.184 -48.929 7.033 1.00 64.35 C ATOM 790 SD MET A 137 21.680 -49.495 8.676 1.00 66.23 S ATOM 791 CE MET A 137 21.543 -51.275 8.465 1.0065.88 C ATOM 792 C MET A 137. 24.384 -49.000 4.858 1.00 63.01 C ATOM 793 O MET A 137 24.486 -48.735 3.661 1.00 63.09 O ATOM 794 N CYS A 138 25.188 -49.857 5.479 1.00 62.44 N ATOM 795 CA CYS A 138 26.232 -50.576 4.757 1.00 61.94 C ATOM 796 CB CYS A 138 27.595 -49.918 4.975 1.00 62.03 C ATOM 797 SG CYS A 138 28.990 -50.936 4.439 1.00 62.33 S ATOM 798 C CYS A 138 26.295 -52.041 5.163 1.00 61.48 C ^' ATOM 799 O CYS A 138 26.422 -52.365 6.345 1.00 61.39 O ATOM 800 N ALA A 139 26.211 -52.921 4.172 1.00 60.93 N ATOM 801 CA ALA A 139 26.280 -54.357 4.408 1.00 60.47 . C ATOM 802 CB ALA A 139 25.044 -55.046 3.856 1.00 60.46 C ATOM 803 C ALA A 139 27.541 -54.939 3.783 1.00 60.13 C ATOM 804 O ALA A 139 27.987 -54.485 2.729 1.00 60.12 O ATOM 805 N GLN A 140 28.113 -55.942 4.441 1.00 59.68 N ATOM 806 CA GLN A 140 29.350 -56.562 3.985 1.00 59.22 C ATOM 807 CB GLN A 140 30.513 -56.145 4.882 1.00 59.22 C ATOM 808 CG GLN A 140 30.723 -54.656 4.993 1.0059.09 C

ATOM 809 CD GLN A 140 31.949-54.321/ 5.802 1.0059.09 C

ATOM 810 OEl GLNA 140 32.772 -55.192 6.084 1.0059.44 O

. ATOM 811 NE2GLNA140 32.080 -53.058 6.185 1.0059.05 N

5 ATOM 812 C GLNA 140 29.231 -58.074 4.025 1.0058.94 C

ATOM 813 O GLN A 140 28.591-58.624 4.920 1.0058.94 O

ATOM 814 N LEUA 141 29.860-58.747 3.067 1.0058.55 N

ATOM 815 CA LEU A 141 29.887-60.207 3.081 1.0058.30 C

ATOM 816 CB LEU A 141 28.481-60.785 2.861 1.0058,30 C

10 ATOM 817 CG LEUA 141 27.730-60.539 1.550 1.0058.25 C

ATOM 818 CDl LEU A 141 26.394-61.267 1.581 1.0058.11 C

ATOM 819 CD2LEUA141 27.524-59.056 1.278 1.0058.38 C

ATOM 820 C LEUA 141 30.890-60.810 2.099 1.0058.06 C

ATOM 821 O LEU A 141 30.953-60.403 0.942 1.0058.07 O

15 ATOM 822 N PRO A 142 31.681-61.788 2.571 1.0057.87 N

ATOM 823 CA PRO A 142 32.663-62.505 1.761 1.0057.70 C

ATOM 824 CB PRO A 142 33.217-63.554 2.728 1.0057.74 C

ATOM 825 CG PRO A 142 32.219-63.635 3.840 1.0057.78 C

ATOM 826 CD PRO A 142 31.664-62.265 3.963 1.0057.80 C 0 ATOM 827 C PRO A 142 31.999-63.187 0.578 1.0057.59 C

ATOM 828 O PRO A 142 31.212-64.109 0.759 1.0057.61 O

ATOM 829 N ASN A 143 32.327-62.729 -0.625 1.0057.52 N

ATOM 830 CA ASNA 143 31.640-63.152 -1.837 1.0057.41 C

ATOM 831 CB ASN A 143 30.167-62.745 -1.756 1.0057.34 C 5- ATOM 832 CG ASN A 143 29.403 -63.022 -3.037 1.0057.28 C

ATOM 833 ODl ASNA 143 29.960-62.987 -4.136 1.0057.32 O

ATOM 834 ND2 ASN A 143 28.109-63.281 -2.901 1.0056.70 N

ATOM 835 C ASNA 143 32.314-62.516 -3.050 1.0057.47 C

ATOM 836 O ASNA 143 32.443-61.295 -3.124 1.0057.41 O

30 ATOM 837 N GLN A 144 32.737-63.350 -3.998 1.0057.56 N

ATOM 838 CA GLNA 144 33.563-62.908 -5.129 1.0057.72 C

ATOM 839 CB GLN A 144 33.773-64.055 -6.110 1.0057.81 C

ATOM 840 CG GLN A 144 34.101 -65.378 -5.467 1.0058.02 C

ATOM 841 CD GLNA 144 34.468-66.419 -6.497 1.0058.57 C

35 ATOM 842 OEl GLN A 144 35.365-66.207 -7.317 1.0058.64 O

ATOM 843 NE2 GLN A 144 33.774-67.553 -6.466 1.0058.83 N

ATOM 844 C GLNA 144 32.996-61.713 -5.891 1.0057.73 C

ATOM 845 O GLN A 144 33.729-60.782 -6.265 1.0057.88 O

ATOM 846 N VALA 145 31.693-61.756 -6.143 1.0057.64 N

40 ATOM 847 CA VAL A 145 31.037-60.663 -6.830 1.0057.55 C

ATOM 848 CB VAL A 145 29.515-60.834 -6.849 1.0057.60 C

ATOM 849 CGl VALA 145 29.149-62.269 -7.189 1.0057.62 C

ATOM 850 CG2VALA145 28.891 -59.867 -7.844 1.0057.54 C

ATOM 851 C VAL A 145 31.396 -59.369 -6.123 1.0057.47 C

45 ATOM 852 O VALA 145 31.752-58.386 -6.764 1.0057.53. O

ATOM 853 N LEU A 146 31.325-59.386 -4.797 1.0057.46 N

ATOM 854 CA LEUA 146 31.695-58.222 -4.001 1.0057.59 C

ATOM 855 CB LEU A 146 31.218-58.367 -2.553 1.0057.59 C

ATOM 856 CG LEU A 146 29.750-58.045 -2.263 1.0057.56 C

50. ATOM 857 CDl LEUA 146 29.270-56.879 -3.U9 1.0057.23 C

ATOM 858 CD2 LEUA 146 28.882-59.266 -2.489 1.0057.83 C

ATOM 859 C LEU A 146 33.197-57.934 -4.046 1.0057.65 C

ATOM 860 O LEUA 146 33.635-56.840 -3.698 1.0057.62 O

ATOM 861 N GLU A 147 33.985-58.917 -4.466 1.0057.74 N

55 ATOM 862 CA GLUA 147 35.396-58.681 -4.719 1.0057.96 C

ATOM 863 CB GLU A 147 36.152-59.994 -4.928 1.0057.87 C

ATOM 864 CG GLU A 147 36.190-60.912 -3.725 1.0058.25 C

ATOM 865 CD GLUA 147 36.827-62.253 -4.048 1.0058.44 C ATOM 866 OEl GLU A 147 36.631 -63.217 -3.271 1.0058.79 O

ATOM 867 OE2 GLUA 147 37.520-62.343 -5.086 1.0059.30 O

ATOM 868 C GLUA 147 35.520-57.827 -5.969 1.0057.91 C

ATOM 869 O GLU A 147 36.266-56.850 -5.996 1.0058.03 O ATOM 870 N SER A 148 34.781-58.197 -7.009 1.0057.86 N

ATOM 871 CA SERA 148 34.875-57.474 -8.274 1.0057.89 C

ATOM 872 CB SERA 148 34.270-58.296 -9.409 1.0057.92 C

ATOM 873 OG SERA 148 34.858-59.582 -9.471 1.0058.15 O

ATOM 874 C SER A 148 34.220-56.091 -8.222 1.0057.91 C ATOM 875 O SERA 148 34.816-55.099 -8.641 1.0058.01 O

ATOM 876 N ILE A 149 32.995-56.031 -7.708 1.0057.82 N

ATOM 877 CA. ILE A 149 32.216-54.795 -7.699 1.0057.70 C

ATOM 878 CB ILE A 149 31.161-54.802 -8.818 1.0057.63 C

ATOM 879 CGl ILE A 149 30.180 -55.962 -8.620 1.0057.21 C ATOM 880 CDl ILE A 149 29.012-55.946 -9.580 1.0056.31 C

ATOM 881 CG2ILEA149 31.825-54.901-10.175 1.0057.78 C

ATOM 882 C ILE A 149 31.484-54.602 -6.378 1.0057.81 C

ATOM 883 O ILEA 149 31.605-55.418 -5.467 1.0058.00 O

ATOM 884 N SERA 150 30.725-53.517 -6.272 1.0057.80 N ATOM 885 CA SER A 150 29.808-53.345 -5.146 1.0057.87 C

ATOM 886 CB SER A 150 30.424-52.492 -4.031 1.0057.80 C

ATOM 887 OG SER A 150 31.122-51.381 -4.555 1.0058.07 O

ATOM 888 C SERA 150 28.472-52.780 -5.620 1.0057.82 C

ATOM 889 O SERA 150 _.28.417-51.969 -6.546 1.0057.84 O ATOM 890 N ILE A 151 27.393-53.233 -4.994 1.0057.75 N-

ATOM 891 CA ILEA 151 26.056-52.907 -5.461 1.0057.75 C

ATOM 892 CB ILE A 151 25.248-54.178 -5.733 1.0057.69 C

ATOM 893 CGl ILEA 151 26.076-55.163 -6.555 1.0057.79 C

ATOM 894 CD 1 ILE A 151 25.580-56.585 -6.471 1.0058.36 C ATOM 895 CG2ILEA151 23.946-53.837 -6.437 1.0057.61 C

ATOM 896 C ILEA 151 25.307-52.074 -4.438 1.0057.80 c^'

ATOM 897 O ILEA 151^' 25.108-52.502 -3.302 1.0057.77 O

ATOM 898 N ILE A 152 24.884-50.882 -4.838 1.0057.79 N

ATOM 899 CA ILEA 152 24.129-50.046 -3.928 1.0057.80 C ATOM 900 CB ILE A 152 24.593-48.573 -3.980 1.0057.84 C

ATOM 901 CGl ILEA 152 23.502-47.669 -4.549 1.0058.21 C

ATOM 902 CDl ILE A 152 22.496-47.213 -3.501 1.0058.80 C

ATOM 903 CG2ILEA152 25.918-48.445 -4.728 1.0057.83 C

ATOM 904 C ILE A 152 22.633-50.189 -4.214 1.0057.75 C ATOM 905 O ILE A 152 22.177-49.991 -5.340 1.0057.62 O

ATOM 906 N ASP A 153 21.886-50.564 -3.181 1.0057.80 N

ATOM 907 CA ASP A 153 20.450-50.776 -3.283 1.0057.91 C

ATOM 908 CB ASP A 153 20.048-52.005 -2.470 1.0057.99 C

ATOM 909 CG ASP A 153 18.582-52.358 -2.625 1.0058.23 C ATOM 910 ODl ASP A 153 17.831-51.554 -3.219 1.0058.41 O

ATOM 911 OD2ASPA153 18.181-53.444 -2.147 1.0058.26 O

ATOM 912 C ASP A 153 19.710-49.549 -2.770 1.0058.00 C

ATOM 913 O ASP A 153 20.084-48.975 -1.746 1.0058.18 O

ATOM 914 N THRA 154 18.652-49.160 -3.475 1.0058.02 N ATOM 915 CA THR A 154 17.958-47.904 -3.200 1.0057.95 C

ATOM 916 CB THRA 154 17.814-47.058 -4.482 1.0057.97 C

ATOM 917 OGl THRA 154 17.036-47.776 -5.454 1.0057.67 . O

ATOM 918 CG2 THRA 154 19.182-46.726 -5.059 1.0057.86 C

ATOM 919 C THRA 154 16.568-48.117 -2.617 1.0058.01 ^' C ATOM 920 O THRA 154 16.008-49.205 -2.739 1.0057.95 O

ATOM 921 N PRO A 155 16.009-47.071 -1.977 1.0058.12 N

ATOM 922 CA PRO A 155 14.614-47.083 -1.545 1.0058.12 C

ATOM 923 CB PROA 155 14.458 -45.757 ^'-0.788 1.0058.01 C ATOM 924 CG PRO A 155 15.838 -45.284 -0.511 1.00 58.04 C

ATOM 925 CD PRO A 155 . 16.684 -45.812 -1.616 1.0058.18 C

ATOM 926 C PRO A 155 13.682 -47.093 -2.747 1.00 58.22 C

ATOM 927 O PRO A 155 14.050 -46.623 -3.829 1.00 58.19 O ATOM 928 N GLY A 156 12.483 -47.628 -2.552 1.00 58.35 N

ATOM 929 CA GLY A 156 11.492 -47.689 -3.616 1.00 58.61 C

ATOM 930 C GLY A 156 10.938 -46.324 -3.963 1.00 58.79 C

ATOM 931 O GLY A 156 10.545 -45.557 -3.083 1.00 58.87 O

ATOM 932 N ILE A 157 10.916 -46.016 -5.253 1.00 58.96 N ATOM 933 CA ILE A 157 10.340 -44.769 -5.713 1.0059.18 C

ATOM 934 CB ILE A 157 10.632 -44.544 -7.199 1.00 59.11 C

ATOM 935 CGl ILE A 157 12.137 -44.645 -7.447 1.00 59.27 C

ATOM 936 CDl ILE A 157 12.551 -44.359 -8.875 1.00 59.64 C

ATOM 937 CG2 ILE A 157 10.127 -43.190 -7.640 1.00 59.13 C ATOM 938 C ILE A 157 8.838 -44.792 -5.459 1.00 59.40 C

ATOM 939 O ILE A 157 8.145 -45.715 -5.877 1.00 59.29 O

ATOM 940 N LEU A 158 8.344 -43.786 -4.745 1.00 59.83 N

ATOM 941 CA LEU A 158 6.924 -43.723 -4.408 1.00 60.23 C

ATOM 942 CB LEU A 158 6.614 -42.471 -3.580 1.00 60.13 C ATOM 943 CG LEU A 158 6.013 -41.410 -3.969 0.00 50.00 C

ATOM 944 CDl LEU A 158 5.164 -41.219 -5.172 0.00 50.00 C

ATOM 945 CD2 LEU A 158 5.392 -40.676 -2.774 0.00 50.00 C

ATOM 946 C LEU A 158 6.063 -43.761 -5.668 1.00 60.49 C

ATOM 947 O LEU A 158 6.377 -43.110 -6.666 1.00 60.52 OATOM 948 N SER A 1.59 4.984 -44.535 -5.618 1.00 60.79 N

ATOM 949 CA SER A 159 ^' 4.070 -44.651 -6.748 1.00 61.07 C

ATOM 950 CB SER A 159 3.135 -45.849 -6:561 1.00 61.20 C

ATOM 951 OG SER A 159 2.477 -46.173 -7.774 1.00 61.72 O

ATOM 952 C SER A 159 3.260 -43.364 -6.942 1.00 61.06 C ATOM 953 O SER A 159 2.043 -43.338 -6.733 1.00 61.02 O

ATOM .954 N ARG A 167 8.576 -37.115 1.268 1.00 65.73 N

ATOM 955 CA ARG A 167 9.108 -35.811 1.654 1.00 65.83 C

ATOM 956 CB ARG A 167 8.000 -34.902 2.220 1.00 65.92 C

ATOM 95fi CG ARG A 167 6.850 -34.591 1.263 1.00 66.25 C ATOM 958 CD ARG A 167 5.617 -35.448 1.553 1.00 66.72 C

ATOM 959 NE ARG A 167 5.726 -36.803 1.001 1.00 67.11 N

ATOM 960 CZ ARG A 167 4.818 -37.760 1.181 1.00 67.11 C

ATOM 961 NHl ARG A 167 3.728 -37.514 1.905 1.00 67.24 N

ATOM 962 NH2 ARG A 167 4.998 -38.961 0.640 1.00 66.65 N ATOM 963 C ARG A 167 10.217 -35.961 2.690 1.00 65.75 C

ATOM 964 O ARG A 167 10.033 -35.617 3.858 1.00 65.80 O

ATOM 965 N GLY A 168 11.367 -36.474 2.266 1.00 65.67 N

ATOM 966 CA GLY A 168 12.498 -36.639 3.172 1.00 65.55 C

ATOM 967 C GLY A 168 13.752 -35.936 2.691 1.00 65.49 C ATOM 968 O GLY A 168 14.343 -35.132 3.410 1.00 65.38 O

.ATOM 969 N TYRA 169 14.151 -36.239 1.462 1.00 65.52 ^■ N

ATOM 970 CA TYR A 169 15.392 -35.720 0.898 1.00 65.52 C

ATOM 971 CB TYR A 169 16.520 -36.744 1.084 1.00 65.60 C

ATOM 972 CG TYR A 169 16.060 -38.185 0.979 1.00 65.63 C ATOM 973 CDl TYRA 169 15.809 -38.940 2.121 1.00 65.74 C

ATOM 974 CEl TYR A 169 15.382 -40.256^' 2.032 1.00 65.83 C ATOM 975 CZ TYR A 169 15.198 -40.834 0.790 1.00 65.80 C

ATOM 976 OH TYR A 169 14.772 -42.140 0.699 1.00 65.64 O

ATOM 977 CE2 TYR A 169 15.438 -40.105 -0.360 1.00 65.77 C ATOM 978 CD2 TYR A 169 15.866 -38.788 -0.260 1.00 65.73 C

ATOM 979 C TYRA 169 15.216 -35.383 -0.585 1.00 65.44 C

ATOM 980 O TYR A 169 14.107 -35.459 -1.118 1.00 65.44 O

ATOM 981 N ASP A 170 16.312 -35.007 -1.242 1.00 65.30 N ATOM 982 CA ASP A 170 16.294-34.711 -2.674 1.0065.09 C

ATOM 983 CB ASP A 170 17.247-33.557 -2.999 1.0065.12 C

ATOM 984 CG ASP A 170 16.898-32.862 -4.304 1.0065.25 C

ATOM 985 ODl ASP A 170 17.312-31.695 -4.484 1.0065.06 O ATOM 986 OD2ASPA170 16.211-33.481 -5.149 1.0065.55 O

ATOM 987 C ASP A 170 ^• 16.637-35.965 -3.486 1.0064.95 C

ATOM 988 O ASP A 170 17.698-36.058 -4.131 1.0064.78 O

ATOM 989 N PHE A 171 15.719-36.926.-3.442 1.0064.77 N

ATOM 990 CA PHE A 171 15.907-38.217 -4.088 1.0064.63 C ATOM 991 CB PHEA 171. 14.580-38.975 -4.165 1.0064.63 C

ATOM 992 CG PHE A 171 14.728 -40.414 -4.560 1.0064,58 C

ATOM 993 CDl PHEA 171 15.480-41.283 -3.788 1.0064.37 C

ATOM 994 CEl PHE A 171 15.616-42.608 -4.146 1.0064.43 C

ATOM 995 CZ PHEA 171 14.992-43.083 -5.285 1.0064.73 C ATOM 996 CE2 PHE A 171 14.237-42.228 -6.062 1.0064.67 C

ATOM 997 CD2PHEA171 14.107-40.902 -5.697 1.0064.81 C

ATOM 998 C PHEA 171 16.534-38.064 -5.470 1.0064.56 C

ATOM 999 O PHE A 171 17.609-38.616 -5.734 1.0064.43 O

ATOM 1000 N PRO A 172 15.872-37.306 -6.357 1.0064.52 N ATOM 1001 CA PRO A 172 16.455-37.032 -7.663 1.0064.49 C

ATOM 1002 CB PRO A 172 15.573-35.907 -8.202 1.0064.54 C

ATOM 1003 CG PRO A 172 14.246-36.174 -7.585 1.0064.64 C

ATOM 1004 CD PRO A 172 14.547-36.678 -6.203 1.0064.57 C

ATOM 1005 C PRO A 172 17.916-36.583 -7.571 1.0064.39 C ATOM 1006 O PRO A 172 18.775-37.148 -8.258 1.0064.27 O ATOM 1007 N ALAA 173 18.200-35.592 -6.729 1.0064.18 N

ATOM 1008 CA ALAA 173 19.568 -35.093 -6.596 1.0064.15 C

ATOM 1009 CB ALAA 173 19.641 -33.959 -5.592 1.0064.18 C

ATOM 1010 C ALAA 173 20.547-36.206 -6.226 1.0064.15 C ATOM 1011 O ALA A 173 21.636-36.305 -6.809 1.0064.04 O ATOM, 1012 N VALA 174 20.168-37.051 -5.270 1.0064.23 N

ATOM 1013 CA VALA 174 21.045 -38.177 -4.922 1.0064.12 C

ATOM 1014 CB VAL A 174 20.627-38.899 -3.608 1.0064.14 C

ATOM 1015 CGl VALA 174 19.189-38.598 -3.246 1.0064.11 C ATOM 1016 CG2VALA174 20.874-40.397 -3.705 1.0064.15 C

ATOM 1017 C VAL A 174 21.219-39.162 -6.092 1.0064.08 C

ATOM 1018 O VAL A 174 22.340-39.617 -6.378 1.0063.98 O

ATOM 1019 N LEU A 175 20.121-39.466 -6.781 1.0064.02 N

ATOM 1020 CA LEUA 175 20.200-40.298 -7.976 1.0063.80 C ATOM 1021 CB LEU A 175 18.813-40.556 -8.557 1.0063.79 C

ATOM 1022 CG LEUA 175 18.168 -41.866 -8.103 1.0064.02 C

ATOM 1023 CDl LEUA 175 16.760-42.013 -8.663 1.0064.02 C

ATOM 1024 CD2 LEU A 175 19.034-43.050 -8.512 1.0064.22 , C

ATOM 1025 C LEU A 175 21.107-39.679 -9.034 1.0063.78 C ATOM 1026 O LEU A 175 21.733-40.386 -9.820 1.0063.66 O

ATOM 1027 N ARG A 176 21.181-38.355 -9.049 1.0063.87 N

ATOM 1028 CA ARG A 176 22.050-37.663 -9.989 1.0063.82 C

ATOM 1029 CB ARG A 176 21.579-36.223-10.186 1.0063.86 C

ATOM 1030 CG ARG A 176 22.452-35.376-11.095 1.0064.46 C ATOM 1031 CD ARG A 176 21.716-34.101-11.477 1.0065.87 C

ATOM 1032 NE ARG A 176 20.505-33.929-10.669 1.0066.91 N

ATOM 1033 CZ ARG A 176 19.918-32.760-10.423 1.0067.30 C

ATOM 1034 NHl ARG A 176 18.817-32.717 -9.679 1.0067.30 N

ATOM 1035 NH2 ARG A 176 20.435-31.635-10.912 1.0067.62 N ATOM 1036 C ARG A 176 23.510-37.722 -9.538 1.0063.65 C

ATOM 1037 O ARG A 176 24.417-37.859-10.363 1.0063.59 O

ATOM 1038 N TRP A 177 23.733-37.633 -8.229 1.0063.54 N

ATOM 1039 CA TRP A 177 25.080-37.773 -7.668 1.0063.37 ^• C ATOM 1040 CB TRP A 177 25.025-37.527 -6.160 1.0063.31 C ATOM 1041 CG TRP A 177 26.347-37.583 -5.454 1.0063.26 C ATOM 1042 CDl TRP A 177 27.218 -36.549 -5.255 1.0062.97 C ATOM 1043 NEl TRP A 177 28.317-36.985 -4.555 1.0062.77 N ATOM 1044 CE2 TRP A 177. 28.169-38.320 -4.280 1.0063.09 C ATOM 1045 CD2 TRP A 177 26.937-38.731 -4.828 1.0063.35 C ATOM 1046 CE3 TRP A 177 26.544-40.069 -4.683 1.0063.27 C ATOM 1047 CZ3 TRP A 177 27.383-40.939 -4.005 1.0063.03 C ATOM 1048 CH2TRPA177 28.604 -40.500 -3.473 1.0063.04 C ATOM 1049 CZ2 TRP A 177 29.014-39.199 -3.599 1.0063.18 C ATOM 1050 C TRP A 177 25.641-39.168 -7.971 1.0063.41 C ATOM 1051 O TRP A 177 26.780-39.331 -8.476 1.0063.24 O ATOM 1052 N PHEA 178 24.826-40.177 -7.672 1.0063.59 N ATOM 1053 CA PHE A 178 25.161 -41.545 -8.047 1.0063.57 C ATOM 1054 CB PHE A 178 24.094-42.526 -7.558 1.0063.59 C ATOM 1055 CG PHE A 178 24:285-42.971 -6.137 1.0063.89 C ATOM 1056 CDl PHE A 178 25.401-43.713 -5.772 1.0064.14 C ATOM 1057 CEl PHE A 178 25.580-44.131 -4.461 1.0064.00 C ATOM 1058 CZ PHE A 178 24.638-43.811 -3.501 1.0063.93 C ATOM 1059 CE2 PHE A 178 23.520-43.076 -3.851 1.0064.17 C ATOM 1060 CD2 PHE A 178 23.346 -42.660 -5.166 1.0064.18 C ATOM^' 1061 C PHE A 178 25.345-41.661 -9.562 1.0063.55 C ATOM 1062 O PHE A 178 26.341-42.210-10.032 1.0063.61 O. ATOM 1063 N ALA A 179 24.391-41.133-10.325 1.0063.51 N ATOM 1064 CA ALA A 179 24.479-41.170-11.783 1.0063.38 C ATOM 1065 CB ALA A 179 23.344-40.377-12.410 1.0063.38 C ATOM 1066 C ALA A 179 25.832-40.648-12.260 1.0063.30 C ATOM 1067 O ALAA 179 26.435-41.207-13.178 1.0063.20 O ATOM 1068 N GLU A 180 26.303-39.574-11.631 1.0063.33 N ATOM 1069 CA GLU A 180. 27.635-39.051-11.916 1.0063.25 C ATOM 1070 CB GLUA 180 27.923-37.789-11.102 1.0063.23 C ATOM 1071 CG GLUA 180 27.232-36.535-11.594 1.0063.57 C ATOM 1072 CD GLUA 180 27.433-35.365-10.650 1.0063.57 C ATOM 1073 OEl GLUA 180 28.083-35.556 -9.596 1.0063.87 O ATOM 1074 OE2GLUA180 26.936-34.258-10.959 1.0064.08 O ATOM 1075 C GLU A 180 28.695-40.090-11.595 1.0063.07 C ATOM 1076 O GLU A 180 29.588-40.338-12.405 1.0063.03 O ATOM 1077 N ARG A 181 28.601-40.696-10.411 i.OO 62.95 N ATOM 1078 CA ARG A 181 29.672-41.605 -9.967 1.0062.57 C ATOM 1079 CB ARG A 181 29.820-41.556 -8.447 1.0062.55 C ATOM 1080 CG ARG A 181 30.681 -40.405 -7.980 1.0062.92 C ATOM 1081 CD ARG A 181 30.191-39.845 -6.668 1.0063.49 C ATOM 1082 NE ARG A 181 30.603 -38.454 -6.494 1.0064.41 N ATOM 1083 CZ ARG A 181 29.996-37.415 -7.063 1.0064.92 C ATOM 1084 NHl ARG A 181 30.438 -36.180 -6.846 1.0065.08 N ATOM 1085 NH2 ARG A 181 28.943-37.606 -7.849 1.0065.13 N ATOM 1086 C ARG A 181 29.587-43.059-10.444 1.0062.33 C ATOM 1087 O ARG A 181 30.604-43.668-10.768 1.0062.41 O ATOM 1088 N VAL A 182 28.377-43.601-10.499 1.0062.04 N ATOM 1089 CA VALA 182 28.153-45.040-10.663 1.0061.56 C ATOM 1090 CB VALA 182 26.718-45.378-10.249 1.0061.45 C ATOM 1091 CGl VALA 182 26.198-46.552-11.030 1.0061.55 C ATOM 1092 CG2 VAL A 182 26,654-45.623 -8.752 1.0061.14 C ATOM 1093 C VAL A 182 28.430-45.596-12.065 1.0061.44 C ATOM 1094 O VALA 182 28.331-44.875-13.055 1.0061.47 O ATOM 1095 N ASP A 183 28.772-46.882-12.137 1.0061.33 N ATOM 1096 CA ASP A 183 29.076-47,554-13.415 1.0061.35 C ATOM 1097 CB ASP A 183 30.000-48.762-13.198 1.0061.39 C ATOM 1098 CG ASP A 183 31.466-48.373-13.136 1.0062.09 C ATOM 1099 ODl ASP A 183 32.248-48.863-13.981 1.0062.54 O ATOM 1100 OD2ASPA183 31.838-47.569-12.252 1.0063.12 O ATOM 1101 C ASP A 183 27.842-47.992-14.216 1.0061.13 C ATOM 1102 O ASP A 183 27.771 -47.778 -15.428 1.0061.05 O ATOM 1103 N LEU A 184 26.894-48.634-13.539 1.0060.90 N ATOM 1104 CA LEUA 184 25.651-49.082-14.164 1.0060.71 C ATOM 1105 CB LEU A 184 25.63.0-50.608-14.307 1.0060.75 C ATOM 1106 CG LEU A 184 26.126 -51.298 -15.581 1.0060.63 C ATOM 1107 CDl LEUA 184 25.747-52.774-15.537 1.0060.23 C ATOM 1108 CD2LEUA184 25.555-50.648-16.828 1.0060.26 C ATOM 1109 C LEU A 184 24.448-48.655-13.335 1.0060.59 C ATOM 1110 O LEUA 184 24.508-48.633-12.107 1.0060.73 O ATOM 1111 N ILEA 185 23.351-48.320-14.005 1.0060.33 N ATOM 1112 CA ILEA 185 22.119-47.996-13.310 1.0060.09 C ATOM 1113 CB ILE A 185 21.670-46.560-13.589 1.0059.94 C ATOM 1114 CGl ILE A 185 22.827-45.592-13.343 1.0059.84 C ATOM 1115 CDl ILE A 185 22.469-44.139-13.553 1.0059.85 C ATOM 1116 CG2 ILE A 185 20.483-46.203-12.718 1.0059.66 C ATOM 1117 C ILEA 185 21.039-48.964-13.754 1.0060.22 C ATOM 1118 O ILEA 185 20.636-48.969-14.915 1.0060.25 O ATOM 1119 N ILEA 186 20.586-49.799-12.830 1.0060.39 N ATOM 112Q CA ILEA 186 19.557-50.777-13.145 1.0060.66 C ATOM 1121 CB ILE A 186 19.785-52.100-12.400 1.0060.60 C ATOM 1122 CGl ILE A 186. 21.222-52.588-12.592 1.0060.80 C ATOM 1123 CDl ILEA 186 21.619-52.766-14.037 1.0060.97 C ATOM 1124 CG2ILEA186 18.808 -53.141 -12.881 1.0060.56 C ATOM 1125 C ILE A 186 18.188-50.230-12.768 1.0060.88 C ATOM 1126 O ILEA 186 17.935-49.911-11.603 1.0060.99 O ATOM 1127 N LEUA 187 17.312-50.107-13.757 1.0061.05 N ATOM 1128 CA LEUA 187 15.945-49.672-13.507 1.0061.25 C ATOM 1129 CB LEUA 187 15.555-48.542-14.458 1.0061.17 C ATOM 1130 CG LEUA 187 15.836-47.107-14.010 1.0060.76 C ATOM 1131 CDl LEUA 187 17.290-46.918-13.667 1.0060.58 C ATOM 1132 CD2LEUA187 15.425-46.133-15.096 1.0060.96 C ATOM 1133 C LEUA 187 14.980-50.850-13.649 1.0061.68 C ATOM 1134 O LEUA 187 14.955-51.526-14.682 1.0061.88 O. ATOM 1135 N LEU A 188 14.194-51.101-12.606 1.0061.91 N ATOM 1136 CA LEUA 188 13.260-52.216-12.627 1.0062.18 C ATOM 1137 CB LEU A.188 13.348-53.033-11.341 1.0062.05 C ATOM^' 1138 CG LEUA 188 14.662 -53.756 -11.067 1.0062.08 C ATOM 1139 CDl LEUA 188 14.375-55.091-10.405 1.0061.97 C ATOM 1140 CD2LEUA188 15.416-53.970-12.353 1.0062.07 C ATOM 1141 C LEU A 188 11.831-51.755-12.833 1.0062.53 C ATOM 1142 O LEU A 188 11.372-50.801-12.205 1.0062.71 O ATOM 1143 N PHE A 189 11.138-52.441-13.729 1.0062.88 N ATOM 1144 CA PHEA 189 9.703-52.305-13.862 1.0063.25 C ^' ATOM 1145 CB PHEA 189 9.348-51.737-15.222 1.0063.06 C ATOM 1146 CG PHE A 189 9.810-50.339-15.425 1.0063.11 C ATOM 1147 CDl PHEA 189 11.085-50.080-15.889 1.0063.21 C ATOM 1148 CEl PHE A 189 11.513-48.781-16.081 1.0063.18 C ATOM 1149 CZ PHEA 189 10.659-47.727-15.805 1.0063.21 C ATOM 1150 CE2.PHEA189 9.385-47.974-15.339 1.0063.09 C ATOM 1151 CD2PHEA189 8.966-49.274-15.152 1.0063.37 C ATOM 1152 C PHEA 189 9.168-53.707-13.755 1.0063.65 C ATOM 1153 O PHE A 189 9.798-54.631-14.257 1.0063.87 O ATOM 1154 N ASP A 190 8.028-53.895-13.104 1.0064.11 N ATOM 1155 CA ASP A 190 7.488-55.244-13.029 1.0064.78 C ATOM 1156 CB ASP A 190 7.296-55.712-11.575 1.0064.95 C ATOM 1157 CG ASP A 190 5.906-55.455-11.040 1.0065.15 C ATOM 1158 ODl ASP A 190 5.433-54.305-11.133 1.0066.38 O ATOM 1159 OD2ASPA190 5.299-56.403-10.497 1.0064.63 O ATOM 1160 C ASP A 190 6.252-55.446-13.911 1.0065.11 C ATOM 1161 O ASP A 190 5.267-54.713-13.810 1.0065.07 O ATOM 1162 N ALAA 191 6.348-56.441-14.793 1.0065.57 N ATOM 1163 CA ALAA 191 5.325-56.747-15.793 1.0065.98 C ATOM 1164 CB ALAA 191 5.777-57.918-16.644 1.0066.05 C ATOM 1165 C ALAA 191 4.001-57.076-15.143 1.006.6.33 C ATOM 1166 O ALAA 191 2.979-57.215-15.811 1.0066.29 O ATOM 1167 N HIS A 192 4.039-57.206-13.826 1.0066.88 N ATOM 1168 CA HIS A 192 2.885-57.594-13.058 1.0067.53 C ATOM 1169 CB HIS A 192 3.359-58.253-11.773 1.0067.72 C ATOM 1170 CG HIS A 192 2.252-58.756-10.912 1.0068.70 C ATOM 1171 NDl HIS A 192 1.333-59.684-11.354 1.0069.77 N ATOM 1172 CEl HIS A 192 0.476-59.947-10.383 1.0070.36 C ATOM 1173 NE2HISA192 0.812-59.227 -9:327 1.0071.03 N ATOM 1174 CD2 HIS A 192 1.921 -58.474 -9.632 1.0069.62 C ATOM 1175 C HIS A 192 2.028-56.372-12.751 1.0067.83 C ATOM 1176 O HIS A 192 0.806-56.409-12.890 1.0068.11 O ATOM 1177 N LYS A 193 2.681-55.290-12.336 1.0068.10 N ATOM 1178 CA LYS A 193 2.010-54.027-12.039 1.0068.23 C ATOM 1179 CB LYS A 193 2.029-53.736-10.536 1.0068.19 C ATOM 1180 CG LYS A 193 0.915-54.383 -9.730 1.0068.42 C ATOM 1181 CD LYS A 193 0.800-53.722 -8.360 1.0068.19 C ATOM 1182 CE LYS A 193 0.625-52.216 -8.509 1.0068.29 C ATOM 1183 NZ LYS A 193 0.868-51.484 -7.239 1.0068.54 N ATOM 1184 C LYS A 193 2.717-52.889-12.750 1.0068.36 C ATOM 1185 O LYS A 193 3.491-52.156-12.133 1.0068.44 O ATOM 1186 N LEUA 194 2.459-52.730-14.040 1.0068.56 N ATOM 1187 CA LEU A 194 3.100-51.653-14.781 1.0068.79^' C ATOM 1188 CB LEUA 194 2.892-51.826-16.282 1.0068.92 C ATOM 1189 CG LEUA 194 4.052-51.373-17.167 1.0068.90 C ATOM 1190 CDl LEU A 194 3.496-50.606-18.343 1.0069.72 C ATOM 1191 CD2LEUA194 5.038-50.514-16.405 1.0069.07 C ATOM 1192 C LEU A 194 2.570-50.294-14.335 1.0068.86 C ATOM 1193 O LEUA 194 1.387-49.994-14.484 1.0068.87 O ATOM 1194 N GLUA 195 3.459-49.479-13.781 1.0069.01 N ATOM 1195 CA GLU A 195 3.114-48.129-13.348 1.0069.24 C ATOM 1196 CB GLU A 195 2.533-48.156-11.926 1.0069.19 C ATOM 1197 CG GLUA 195 2.935-46.994-11.024 1.0069.68 C ATOM 1198 CD GLUA 195 2.265-45.679-11.395 1.0070.76 C ATOM 1199 OEl GLUA 195 2.217-45.345-12.597 1.0071.25 O ATOM 1200 OE2GLUA195 1.795-44.968-10.479 1.0070.87 O ATOM 1201 C GLU A 195 4.353-47.238-13.433 1.0069.31 C ATOM 1202 O GLUA 195 5.439-47.641-13.016 1.0069.43 O ATOM 1203 N ILE A 196 4.198-46.047-14.013 1.00 ^"69.37 N ATOM 1204 CA ILE A 196 5.286-45.058-14.048 1.0069.32 C ATOM 1205 CB ILEA 196 5.806-44.760-15.486 1.0069.37 C ATOM 1206 CGl ILE A 196 6.278-46.045-16.167 1.0069.31 C ATOM 1207 CDl ILE A 196 7.156-45.796-17.375 1.0069.52 C ATOM 1208 CG2ILEA196 6.960-43.749-15.449 1.0069.16 C ATOM 1209 C ILE A 196 4.873-43.763-13.341 1.0069.13 C ATOM 1210 O ILE A 196 4.292-42.853-13.938 1.0069.00 O , ATOM 1211 N SER A 197 5.186-43.707-12.053 1.0068.93 N ATOM 1212 CA SERA 197 4.839-42.579-11.215 1.0068.80 C ATOM 1213 CB SERA 197 5.212-42.892 -9.771 1.0068.89 ^' C ATOM 1214 OG SERA 197 6.584-43.236 -9.679 1.0068.92 O

ATOM 1215 C SERA 197 5.542-41.299-11.643 1.0068.69 C

ATOM 1216 O SER A 197 6:556-41.331-12.345 1.0068.50 O

ATOM 1217 N ASP A 198 4.988-40.174-11.201 1.0068.61 N ATOM 1218 CA ASP A 198 5.579-38.869-11.439 1.0068.54 C

ATOM 1219 CB ASP A 198 4.708-37.785-10.802 1.0068.63 C

ATOM 1220 CG ASP A 198 5.291-36.394-10.965 1.0069.32 C

ATOM 1221 ODl ASP A 198 6.289-36.245-11.704 1.0069.90 O

ATOM 1222 OD2ASPA198 4.747-35.445-10.354 1.0070.07 O ATOM 1223 C ASP A 198 6.996-38.830-10.866 1.0068.35 C

ATOM 1224 O ASP A 198 7.959-38.466-11.560 1.0068.12 O

ATOM 1225 N GLUA 199 7.116-39.220 -9.600 1.0068.16 N

ATOM 1226 CA GLUA 199 8.406-39.264 -8.926 1.0068.12 C

ATOM 1227 CB GLUA 199 8.256-39.928 -7.558 1.0068.13 C ATOM 1228 CG GLUA 199 9.527 -39.956 -6.717 1.0068.49 C

ATOM 1229 CD GLU A 199 9.283-40.500 -5.315 1.0068.60 C

ATOM 1230 OEl GLU A 199 8.391 -39.966 -4.618 1.0069.43 O

ATOM 1231 OE2 GLUA 199 9.983-41.456 -4.908 1.0068.91 O

ATOM 1232 C GLUA 199 9.450-39.994 -9.774 1.0067.92 C ATOM 1233 O GLU A 199 10.610-39.567 -9.861 1.0067.83 O

ATOM 1234 N PHE A 200 9.034-41.082-10.418 1.0067.72 N

ATOM 1235 CA PHE A 200 9.947-41.851-11.255 1.0067.53 C

ATOM 1236 CB PHE A 200 9.287-43.134-11.753 1.0067.63 C

ATOM 1237 CG PHE A 200 10.212-44.319-11.781 1.0067.69 C ATOM 1238 CDl PHE A 200 9.890-45.482-11.102 1.0067.87 C

ATOM 1239 CEl PHE A 200 10.742-46.574-11.129 1.0068.11 C

ATOM 1240 CZ PHE A 200 11.934-46.505-11.828 1.0067.82 C

ATOM 1241 CE2PHEA200 12.269-45.351-12.499 1.0067.56 C

ATOM 1242 CD2PHEA200 11.411-44.267-12.474 1.0067.81 C ATOM 1243 C PHE A 200 10.455-41.020-12.432 1.0067.43 C

ATOM 1244 O PHE A 200 11.660-40.823-12.581 1.0067.23 O

ATOM 1245 N SER A 201 9.541-40.522-13.262 1.0067.37 ^■ N

ATOM 1246 CA SER A 201 9.940-39.690-14.399 1.0067.44 C

ATOM 1247 CB SER A 201 8.729-39.271-15.239 1.0067.44 C ATOM 1248 OG SER A 201 7.921-38.337-14.551 1.0067.77 O

ATOM 1249 C SER A 201 10.758-38.471-13.956 1.0067.32 C

ATOM 1250 O SER A 201 11.566-37.939-14.726 1.0067.15 O

ATOM 1251 N GLU A 202 10.546-38.033-12.716 1.0067.40 N

ATOM 1252 CA GLU A 202 11.424 -37.031-12.113 1.0067.29 C ATOM 1253 CB GLU A 202 10.885 -36.581 -10.754 1.0067.36 C

ATOM 1254 CG GLU A 202 9.975-35.366-10.803 1.0067.70 C

ATOM 1255 CD GLU A 202 10.675-34.096-10.356 1.0068.43 C

ATOM 1256 OEl GLU A 202 11.599-34.193 -9.520 1.0068.71 , O

ATOM 1257 OE2GLUA202 10.296-33.000-10.828 1.0068.82 O ATOM 1258 C GLU A 202 12.832-37.602-11.957 1:0067.11 C

ATOM 1259 O GLU A 202 13.824-36.963-12.332 1.0066.97 O

ATOM 1260 N ALA A 203 12.916-38.811-11.411 1.0067.08 N

ATOM 1261 CA ALA A 203 14.206-39.491-11.281 1.0066.87 C

ATOM 1262 CB ALA A 203 14.030-40.842-10.595 1.0066.88 C ATOM 1263 C ALA A 203 14.920-39.656-12.633 1.0066.81 C

ATOM 1264 O ALAA 203 16.110-39.327-12.771 1.0066.36 9

ATOM 1265 N ILE A 204 14.189-40.164-13.627 1.0066.84 N

ATOM 1266 CA ILE A 204 14.736-40.312-14.977 1.0066.68 C

ATOM 1267 CB ILE A 204 13.766-41.034-15.925 1.0066.55 C ATOM 1268 CGl ILE A 204 13.592-42.485-15.493 1.0066.77 C

ATOM 1269 CDl ILE A 204 12.277-42.76344.821 1.0067.14 C

ATOM 1270 CG2ILEA204 14.282-40.998-17.345 1.0066.27 C

ATOM 1271 C ILE A 204 15.125-38.957-15.567 1.0066.71 C ATOM 1272 O ILE A 204 16.102-38.850-16.312 1.0066.75 O ATOM 1273 N GLY A 205 14.359-37.922-15.235 1.0066.74 N ATOM 1274 CA GLY A 205 14.763-36.565-15.575 1.0066.51 C ATOM 1275 C GLY A 205 16.115-36.275-14.946 1.0066.38 C ATOM 1276 O GLY A 205 16.957-35.597-15.541 1.0066.39 O ATOM 1277 N ALA A 206 16.326-36.806-13.743 1.0066.29 N ATOM 1278 CA ALA A 206 17.573-36.575-13.006 1.0065.87 C ATOM 1279 CB ALA A 206 17.366-36.813-11.515 1.0065.95 C ATOM 1280 C ALA A 206 18.743-37.407-13.518 1.0065.58 C ATOM 1281 O ALA A 206 19.900-37.072-13.280 1.0065.48 O ATOM 1282 N LEU A 207 18.446-38.499-14.210 1.0065.49 N ATOM 1283 CA LEU A 207 19.506-39.322-14.795 1.0065.08 C ATOM 1284 CB LEU A 207 19.040-40.769-14.948 1.0065.03 C ATOM 1285 CG LEU A 207 19.398-41.743-13.823 1.0065.05 C ATOM 1286 CDl LEU A 207 19.471-41.051-12.472 1.0065.29 C ATOM 1287 CD2LEUA207 18.398-42.885-13.782 1.0065.61 C ATOM 1288 C LEU A 207 20.009-38.785-16.136 1.0064.97 C ATOM 1289 O LEU A 207 20.904-39.364-16.750 1.0064.88 O ATOM 1290 N ARG A 208 19.433-37.674-16.582 1.0064.92 N ATOM 1291 CA ARG A 208 19.771-37.083-17.879 1.0064.83 C ATOM 1292 CB ARG A 208 19.025-35.751-18.064 1.0064.82 C ATOM 1293 CG ARG A 208 19.634-34.791-19.087 1.0064.69 C ATOM 1294 CD ARG A 208 18.525-34.039-19.840 1.0064.59 C ATOM 1295 NE ARG A 208 18.746-32.581-19.922 1.0064.85 N ATOM 1296 CZ ARG A 208 19.843-31.934-19.505 1.0064.78 C ATOM 1297 NHl ARG A 208 20.873-32.594-18.958 1.0065.02 N ATOM 1298 NH2ARGA208 19.907-30.609-19.645 1.0064.48 N ATOM 1299 C ARG A 208 21.279-36.913-18.094 1.0064.76 C ATOM 1300 O ARG A 208 21.993-36.423-17.218 1.0064.84 O ATOM 1301 N GLY A 209^' 21.753-37.327-19.266 1.00.64.60 N ATOM 1302 CA GLY A 209 23.163-37.188-19.622 1.0064.23 C ATOM 1303 C GLY A 209 23.947-38.455-19.352 1.0063.99 C ATOM 1304 O GLY A 209 25.131 -38.553 -19.677 1.0063.84 O ATOM 1305 N HIS A 210 23.281-39.431-18.749 1.0063.86 N ATOM 1306 CA HIS A 210 23.932-40.685-18.408 1.0063.78 C ATOM 1307 CB HIS A 210 24.183-40.769-16.900 1.0063.93 C ATOM 1308 CG HIS A 210 25.189-39.779-16.401 1.0064.53 C ATOM 1309 NDl HIS A 210 24.880-38.807-15.474 1.0065.05 N ATOM 1310 CEl HIS A 210 25.955-38.079-15.228 1.0065.36 C ATOM 1311 NE2 HIS A 210 26.949-38.540-15.967 1.0065.43 N ATOM 1312 CD2HISA210 26.496-39.602-16.711 1.0065.12 C ATOM 1313 C HIS A 210 23.132-41.891-18.878 1.0063.46 C ATOM 1314 O HIS A 210 23.308-42.996-18.366 1.0063.56 O ATOM 1315 N GLU A 211 22.261-41.682-19.860 1.0063.02 N ATOM 1316 CA GLU A 211 21.438-42.767-20.373 1.0062.65 ^• C ATOM 1317 CB GLU A 211 20.582-42.298-21.548 1.0062.67 C ■ ATOM 1318 CG GLU A 211 21.011-40.968-22.133 1.0063.51 C ATOM 1319 CD GLU A 211 20.239 -39.803 "-21.542 1.0064.41 C ATOM 1320 OE1GLUA211 20.737-38.656-21.593 1.0064.72 O ATOM 1321 OE2GLUA211 19.126-40.038-21.027 1.0064.94 O ATOM 1322 C GLU A 211 22.261-43.999-20.756 1.0062.27 C ATOM 1323 O GLU A 211 21.780-45.128-20.648.1.0062.45 O ATOM 1324 N ASP A 212 23.502-43.786-21.182 1.0061.63 N ATOM 1325 CA ASP A 212 24.356-44.897-21.600 1.0061.13 C ATOM 1326 CB ASP A 212 25.658-44.381-22.206 1.0061.30 C ATOM 1327 CG ASP A 212 26.499-43.615-21.207 1.0062.39 C ATOM 1328 ODl ASP A 212 26.292-42.385-21.076 1:0063.83 O ATOM 1329 OD2ASPA212 27.374-44.239-20.561 1.0063.08 O ATOM 1330 C ASP A 212 24.664-45.858-20.455 1.0060.47 C ATOM 1331 O ASP A 212 25.109-46.983-20.681 1.0060.32 O ATOM 1332 N LYS A 213 24.427-45.410-19.229 1.0059.79 N ATOM 1333 CA LYS A 213 24.701-46.226-18.058 1.0059.18 C ATOM 1334 CB LYS A 213 25.212-45.361-16.909 1.0059.14 C ATOM 1335 CG LYS A 213 26.566-44.724-17.136 1.0059.05 C ATOM 1336 CD LYS A 213 27.080-44.131-15.831 1.0059.11 C ATOM 1337 CE LYS A 213 28.308-43.262-16.033 1.0058.78 C ATOM 1338 NZ LYS A 213 28.643 -42.542 -14.778 1.0058.30 N ATOM 1339 C LYSA 213 23.456-46.962-17.601 1.0058.86 C ATOM 1340 O LYS A 213 23.464-47.627-16.568 1.0058.84 O ATOM 1341 N ILE A 214 22.384-46.851-18.372 1.0058.47 N ATOM 1342 CA ILE A 214 21.099-47.377-17.935 1.0058.17 C ATOM 1343 CB ILE A 214 19.967-46.389-18.249 1.0058.12 C ATOM 1344 CGl ILE A 214 20.170-45.098-17.459 1.0058.10 C ATOM 1345 CDl ILE A 214 19.152-44.022-17.765 1.0058.21 C ATOM 1346 CG2ILEA214 18.622-47.009-17.924 1.0058.27 C ATOM 1347 C ILE A 214 20.745-48.735-18.531 1.0057.94 C ATOM 1348 O ILE A 214 20.731-48.908-19.746 1.0058.08 O ATOM 1349 N ARG A 215 20.460-49.698-17.664 1.0057.63 N ATOM 1350 CA ARG A 215 19.861-50.946-18.101 1.0057.37 C ATOM 1351 CB ARG A 215 20.675-52.152-17.641 1.0057.18 C ATOM 1352 CG ARG A 215 22.111-52.145-18.072 1.0056.81 C ATOM 1353 CD ARG A 215 22.266-51.984-19.569 1.0056.23 C ATOM 1354 NE ARG A 215 23.676-51.817-19.905 1.0056.42 . N ATOM 1355 CZ ARG A 215 24.302-50.645-19.933 1.0056.18 C ATOM 1356 NHl ARG A 215 23.640-49.527-19.664 1.0056.41 N ATOM 1357 NH2 ARG A 215 25.590-50.591-20.234 1.0055.83 N ATOM 1358 C ARG A 215 18.472-51.029-17.503 1.0057.38 C ATOM .1359 O ARG A 215 18.320-51.179-16.287 1.0057.59 O ATOM 1360 N VAL A 216 17.461 -50.913 -18.357 1.0057.17 N ATOM 1361 CA VAL A 216 16.075-51.040-17.934 1.0056.79 C ATOM 1362 CB VAL A 216 15.154-50.313-18.912 1.0056.68 C ATOM 1363 CGl VAL A 216 13.703-50.608-18.590 lfoO 56.77 C ATOM 1364 CG2VALA216 15.431-48.823-18.886 lloO 56.69 C ATOM 1365 C VAL A 216 15.688-52.506-17.941 1.0056.67 C ATOM 1366 O VAL A 216 15.659-53.124-18.999 1.0056.91 O ATOM 1367 N VAL A 217 15.395-53.079-16.778 1.0056.39 N ATOM 1368 CA VAL A 217 14.980-54.478-16.760 1.0056.08 C ATOM 1369 CB VAL A 217 15.906-55.381-15.905 1.0056.09 C ATOM 1370 CGl VAL A 217 17.104-54.600-15.412 1,0055.83 C ATOM 1371 CG2VALA217 15.148-56.004-14.745 1.0056.09 C ATOM 1372 C VAL A 217 13.529-54.632-16.335 1.0056.01 C ATOM 1373 O VAL A 217 13.112-54.152-15.275 1.0056.14 O ; ATOM 1374 N LEU A 218 12.766-55.297-17.195 1.0055.76 N ATOM 1375 CA LEU A 218 11.364-55.593-16.950 1.0055.35 C ATOM 1376 CB LEU A 218 10.622-55.634-18.279 1.0055.27 C ATOM 1377 CG LEU A 218 9.189-56.137-18.354 1.0055.27 C ATOM 1378 CDl LEU A 218 8.248-55.189-17.639 1.0055.39 C ATOM 1379 CD2LEUA218 8.817-56.270-19.817 1.0055.68 C ATOM 1380 C LEU A 218 11.261-56.926-16.213 1.0055.33 C ATOM 1381 O LEU A 218 11.388-58.006-16.799 1.0055.26 O ATOM 1382 N ASN A 219 11.040-56.830-14.911 1.0055.33 N ATOM 1383 CA ASN A 219 11.089-57.970-14.018 1.0055.16 C ATOM 1384 CB ASN A 219 11.392-57.479-12.607 1.0055.29 C ATOM 1385 CG ASN A 219 12.091-58.516-11.774 1.0055.94 C ATOM 1386 ODl ASN A 219 12.474-59.575-12.282 1.0056.02 O ATOM 1387 ND2ASNA219 12.266-58.225-10.480 1.0056.54 N ATOM 1388 C ASN A 219 9.807-58.789-14.008 1.0055.04 C

ATOM 1389 O ASN A 219 8.796-58.388-14.582 1.0054.74 O

ATOM 1390 N LYS A 220 9.868-59.937-13.337 1.0055.21 N

ATOM 1391 CA LYS A 220 8.744-60.871-13.202 1.0055.41 C ATOM 1392 CB LYS A 220 7.898-60.553-11.958 1.0055.43 C

ATOM 1393 CG LYS A 220 7.902-59.096-11.540 1.0055.52 C

ATOM 1394 CD LYS A 220 8.157 -58.922 -10.043 1.0055.10 C

ATOM 1395 CE LYS A 220 6.892-58.547 -9.289 1.0055.18 C

ATOM 1396 NZ LYS A 220 7.203-57.685 -8.115 1.0054.26 N ATOM 1397 C LYS A 220 7.873-61.022-14.446 1.0055.67 C

ATOM 1398 O LYS A 220 6.652-61.107-14.352 1.0055.78 O

ATOM 1399 N ALA A 221 8.513-61.082-15.610 1.0056.06 N

ATOM 1400 CA ALA A 221 7.809-61.285-16.872 1.0056.27 C

ATOM 1401 CB ALA A 221 8.736 -61.039 -18.041 1.0056.15 C ATOM 1402 C ALA A 221 7.241-62.689-16.951 1.0056.45 C

ATOM 1403 O ALA A 221 6.458-62.996-17.841 1.0056.60 O

ATOM 1404 N ASP A 222 7.636 -63.540 -16.014 1.0056.79 N

ATOM 1405 CA ASP. A 222 7.225-64.932-16.043 1.0057.20 C

ATOM 1406 CB ASP A 222 8.254-65.817-15.346 1.0057.26 C ATOM 1407 CG ASP A 222 8.054-65.865-13.841 1.0058.12 C

ATOM 1408 ODl ASP A 222 7.813-66.978-13.312 1.0058.75 O

ATOM 1409 OD2ASPA222 8.117-64.791-13.191 1.0058.98- O

ATOM 1410 C ASP A 222 5.891 -65.106 -15.353 • 1.0057.37 C

ATOM 1411 O ASP A 222 5.334-66.205-15.334 1.0057.48 O ATOM 1412 N MET A 223 5.380-64.038-14.759 1.0057.52 N

ATOM 1413 CA MET A 223 4.135-64.182-14.030 1.0057.98 C

ATOM 1414 CB MET A 223 4.286-63.751-12.571 1.0057.98 C

ATOM 1415 CG MET A 223 4.396 -62.271-12.325 1.0058.43 C

ATOM 1416 SD MET A 223 4.202-61.968-10.553 1.0059.28 S ATOM 1417 CE MET A 223 2.734-62.938-10.188 1.0059.20 C

ATOM 1418 C MET A 223 2.975-63.489-14.720. 1.0057.63 C

ATOM 1419 O MET A 223 2.063-62.975-14.076 1.0057.84 O

ATOM 1420 N VAL A 224 3.005-63.514-16.045 1.0057.30 N

ATOM 1421 CA VAL A 224 1.964-62.896-16.834 1.0056.98 C ATOM 1422 CB VAL A 224 2.240-61.386-17.001 1.0056.86 C

ATOM 1423 CGl VAL A 224 2.971-61.108-18.298 1.0056.82 C

ATOM 1424 CG2VALA224 0.953-60.602-16.936 1.0056.98 C

ATOM 1425 C VAL A 224 1.892-63.608-18.183 1.0056.86 C

ATOM 1426 O VAL A 224 2.917-63.957-18.764 1.0056.87 O ATOM 1427 N GLU A 225 0.682-63.856-18.665 1.0056.71 N

ATOM 1428 CA GLU A 225 0.513-64.536-19.937 1.0056.69 C

ATOM 1429 CB GLU A 225 -0.968-64.682-20.256 1.0057.01 C

ATOM 1430 CG GLU A 225 -1.282-65.935-21.035 1.0058.92 C

ATOM 1431 CD GLU A 225 -1.499-67.130-20.129 1.0061.73 C ATOM 1432- OEl GLU A 225 -0.506-67.812-19.773 1.0062.80 O

ATOM 1433 OE2GLUA225 -2.671-67.378-19.761 1.0063.64 O

ATOM 1434 C GLU A 225 1.213-63.731-21.029 1.0056.21 C

ATOM 1435 O GLU A 225 1.305-62.512-20.935 1.0056.09 O

ATOM 1436 N THR A 226 1.692-64.399-22.071 1.0055.84 N ATOM 1437 CA THR A 226 2.587-63.730-23.022 1.0055.74 C

ATOM 1438 CB THR A 226 3.293-64.715-23.989 1.0055.64 C

ATOM 1439 OGl THR A 226 3.317-64.152-25.306 1.0055.50 O

ATOM 1440 CG2THRA226 2.580-66.054-24.021 1.0056.27 C

ATOM 1441 C THR A 226 2.027-62.487-23.756 1.0055.65 C ATOM 1442 O THR A 226 2.646-61.416-23.715 1.0055.72 O

ATOM 1443 N GLN A 227 0.882-62.618-24.426 1.0055.48 N

ATOM 1444 CA. GLN A 227 0.245-61.451-25.055 1.0055.18 C

■ ATOM 1445 CB GLN A 227 -1.218-61.737-25.375 1.0055.14 C ATOM 1446 CG GLN A 227 -1.496-62.165-26.797 1.0054.85 C ATOM 1447 CD GLN A 227 -2.945 -62.543 -26.991 1.0054.43 C ATOM 1448 OEl GLN A 227 -3.545-63.201-26.136 1.0053.99 OATOM 1449 NE2 GLN A 227 -3.523-62.124-28.111 1.0054.27 N ATOM 1450 C GLN A 227 0.309-60.245-24.126 1.0055.20 C ATOM 1451 O -GLN A 227 0.738-59.151-24.521 1.0055.06 O ATOM 1452 N GLN A 228 -0.130-60.463-22.888 1.0055.21 N ATOM 1453 CA GLN A 228 -0.091-59.450-21.848 1.00_.55.26 C ATOM 1454 CB GLN A 228 -0.604-60.039-20.538 1.0055.25 C ATOM 1455 CG GLN A 228 -0.485-59.113-19.350 1.0055.38 C ATOM 1456 CD GLN A 228 -1.259-57.832-19.534 1.0055.86 C ATOM 1457 OEl GLN A 228 -2.266-57.794-20.243 1.0056.42 O ATOM 1458 NE2 GLN A 228 -0.795-56.769-18.892 1.0056.22 N ATOM 1459 C GLN A 228 1.320-58.880-21.670 1.0055.39 C ATOM 1460 O GLN A 228 1.504-57.660-21.581 1.0055.39 O ATOM 1461 N LEU A 229 2.316-59.761-21.627 1.0055.35 N ATOM 1462 CA LEU A 229 3.707-59.320-21.591 1.0055.42 C ATOM 1463 CB LEU A 229 4.664-60.506-21.719 1.0055.40 C ATOM 1464 CG LEU A 229 5.986-60.430-20.956 1.0055.19 C ATOM 1465 CDl LEU A 229 7.025-61.296-21.644 1.0055.13 C ATOM 1466 CD2LEUA229 6.476-59.001-20.843 1.0054.53 C ATOM 1467 C LEU A 229 3.955-58.334-22.728 1.0055.47 C ATOM 1468 O LEU A 229 4.405-57.209-22.493 1.0055.55 O ATOM 1469 N MET A 230 3.646-58.752-23.955 1.0055.41 N ATOM 1470 CA MET A 230 3.777-57.862-25.108 1.0055.26 C ATOM 1471 CB MET A 230 3.182-58.497-26.364 1.0055.44 C ATOM 1472 CG MET A 230 3.890-59.763-26.794 1.0055.41 C ATOM 1473 SD MET A 230 5.663-59.494-26.963 1.0056.86 S ATOM 1474 CE MET A 230 6.272-61.082-26.388 1.0056.24 C ATOM 1475 C MET A 230 3.111-56.523-24.830 1.0055.18 C ATOM 1476 O MET A 230 3.696-55.459-25.064 1.0055.12 O ATOM 1477 N ARGA.231 1.888-56.581-24.316 1.0055.12 N ATOM 1478 CA ARG A 231 1.164-55.368-23.947 1.0055.21 C ATOM 1479 CB ARG A 231 -0.186-55.730-23.330 1.0055.10 C ATOM 1480 CG ARG A 231 -1.374-55.530-24.259 1.0055.70 C ATOM 1481 CD ARG A 231 -1.500-56.597-25.332 1.0056.51 C ATOM 1482 NE ARG A 231 -0.666-56.309-26.492 1.0057.65 N ATOM 1483 CZ ARG A 231 -0.540-57.120-27.537 1.0057.94 C ATOM 1484 NHl ARG A 231 -1.204-58.268-27,570 1.0057.78 N ATOM 1485 NH2ARGA231 0.252-56.782-28.546 1.0058.31 N ATOM 1486 C ARG A 231 1.969-54.457-23.005 1.0055.08 C ATOM 1487 O ARG A 231 2.166-53.258-23,284 1.0054.91 O ATOM 1488 N VAL A 232 2.443-55.032-21.901 1.0054.99 N ATOM 1489 CA VAL A 232 3.204-54.267-20.917 1.0054.96 C ATOM 1490 CB VAL A 232 3.520-55.100-19.664 1.0054.88 C ATOM 1491 CGl VAL A 232 4.557-54.407-18.823 1.0055.17 C ATOM 1492 CG2VALA232 2.272-55.310-18.848 1.0055.17 C ATOM.1493 C VAL A 232 4.494-53.702-21.518 1.0054.91 C ATOM 1494 O VAL A 232 4.720-52.485-21.503 1.0054.68 O ATOM 1495 N TYR A 233 5.332-54.583-22.055 1.0054.85 N ATOM 1496 CA TYR A 233 6.549-54.152-22.724 1.0054.67 C ATOM 1497 CB TYR A 233 7.164-55.333-23.470 1.0054.48 C ATOM 1498 CG TYR A 233 8.424-55.026-24.241 1.0054.61 C ATOM 1499 CDl TYR A 233 8.799-55.811-25.321 1.0054.70 C ATOM 1500 CEl TYR A 233 9.948-55.544-26.035 1.0054.44 C ATOM 1501 CZ TYR A 233 10.736-54.480-25.678 1.0054.26 C ATOM 1502 OH TYR A 233 11.877-54.219-26.394 1.0054.47 O ATOM 1503 CE2TYRA233 10.388-53.681-24.612 1.0054.50 C ATOM 1504 CD2TYRA233 9.237-53.955-23.898 1.0054.77 C

ATOM 1505 C TYR A 233 6.256-52.964-23.657 1.0054.73 C

ATOM 1506 O TYR A 233 6.922-51.909-23.586 1.0054.67 O

ATOM 1507 N GLY A 234 5.243-53.129-24.508 1.0054.80 N ATOM 1508 CA GLY A 234 4.797-52.047-25.381 1.0054.70 C

ATOM 1509 C GLY A 234 4.565-50.754-24.615 1.0054.80 C

ATOM 1510 O GLY A 234 5=144-49.698-24.950 1.0054.91 O

ATOM 1511 N ALA A 235 3.730-50.830-23.578 1.0054.65 N

ATOM 1512 CA ALA A 235 3.434-49.651-22.763 1.0054.39 C ATOM 1513 CB ALA A 235 2.500-50.015-21.633 1.0054.36 C

ATOM 1514 C ALA A 235 4.708-49.002-22.216 1.0054.45 C

ATOM 1515 O ALA A 235 4.913 -47.784 -22.345 1.0054.48 O

ATOM 1516 N LEU A 236 5.564-49.824-21.614 1.0054.43 N

ATOM 1517 CA LEU A 236 6.828-49.355-21.068 1.0054.31 C ATOM 1518 CB LEUA236 7.695-50.532-20.638 1.0054.32 C

ATOM 1519 CG LEU A 236 8.536-50.421-19.362 1.0054.14 C

ATOM 1520 CDl LEU A 236 8.970-49.007-19.059 1.0054.03 C

ATOM 1521 CD2LEUA236 9.735-51.350-19.443 1.0053.68 C

ATOM 1522 C LEU A 236 7.577-48.558-22.115 1.0054.43 C ATOM 1523 O LEU A 236 7.874-47.383-21.910 1.0054.51 O

ATOM 1524 N MET A 237 7.885-49.192-23.245 1.0054.66 N

ATOM 1525 CA MET A 237 8.702-48.506-24.253 1.0054.81 C

ATOM 1526 CB MET A 237 9.112-49.435-25.395 1.0054.86 C

ATOM 1527 CG MET A 237 10.080-50.528-24.964 1.0055.85 C ATOM 1528 SD MET A 237 11.647-49.943-24.265 1.0057.46 S .

ATOM 1529 CE MET A 237 12.613-49.728-25.759 1.0056.82 C

ATOM 1530 C MET A 237 8.030-47.250-24.786 1.0054.74 C

ATOM 1531 O MET A 237 8.708-46.278-25.121 1.0054.99 O

ATOM 1532 N TRP A 238 6.704-47.261-24.855 1.0054.61 N ATOM 1533 CA TRP A 238 5.983-46.061-25.264 1.0054.49 C

ATOM 1534 CB TRP A 238 4.496-46358-25.263 1.0054.42 C

ATOM 1535 CG TRP A 238 3.815-45.961-26.503 1.0054.35 C

ATOM 1536 CDl TRP A 238 3.955-46.533-27.733 1.0054.85 C

ATOM 1537 NEl TRP A 238 3.148-45.899-28.647 1.0054.83 N ATOM 1538 CE2TRPA238 2.463-44.903-28.006 1.0054.14 C

ATOM 1539 CD2TRPA238 2.861-44.916-26.652 1.0053.92 . C

ATOM 1540 CE3 TRP A 238 2.304-43.991-25.776 1.0053.71 C

ATOM 1541 CZ3TRPA238' 1.388-43.100-26.265 1.0054.62 C

ATOM 1542 CH2TRPA238 1.014-43.109-27.617 1.0054.60 C ATOM 1543 CZ2TRPA238 1.539-44.004-28.499 1.0054.05 C

ATOM 1544 C TRP A 238 6.263 -44.921 -24.287 1.0054.52 C

ATOM 1545 O TRP A 238 6.752-43.827-24.653 1.0054.67 O

ATOM 1546 N ALA A 239 5.951-45.206-23.028 1.0054.59 N

ATOM 1547 CA ALA A 239 6.148-44.262-21.941 1.0054.74 C ATOM 1548 CB ALA A 239 5.781-44.915-20.617 1.0054.68 C

ATOM 1549 C ALA A 239 7.583-43.746-21.904 1.0054.79 C

ATOM 1550 O ALA A 239 7.828-42.547-22.071 1.0055.14 O

ATOM 1551 N LEU A 240 8.525-44.661-21.680 1.0054.72 N

ATOM 1552 CA LEU A 240 9.939-44.311-21.643 1.0054.66 C ATOM 1553 CB LEU A 240 10.807-45.565-21.563 1.0054.59 C

ATOM 1554 CG LEU A 240 10.956-46.206-20.184 1.0054.30 C

ATOM 1555 CDl LEU A 240 11.936-47.363-20.250 1.0054.48 C

ATOM 1556 CD2LEUA240 11.408-45.186-19.152 1.0053.92 C

ATOM 1557 C LEU A 240 10.317 -43.482 -22.860 1.0054.72 C ATOM 1558 O LEU A 240 10.939-42.429-22.729 1.0054.60 O

ATOM 1559 N GLY A 241 9.933-43.962-24.040 1.0054.91 N

ATOM 1560 CA GLY A 241 10.086-43.188-25.263 1.0055.18 C

ATOM 1561 C GLY A 241 9.742-41.726-25.038 1.0055.50 C ATOM 1562 O GLY A 241 10.590-40.842-25.229 1.0055.56 O ATOM 1563 N LYS A 242 8.503-41.464-24.621 1.0055.54 . N ATOM 1564 CA LYS A 242 8.070-40.079-24.365 1.0055.84 C ATOM 1565 CB LYS A 242 6.564-40.037-24.078 1.0055.91 C ATOM 1566 CG LYS A 242 6.106-38.929-23.139 1,0056.07 C ATOM 1567 CD LYS A 242 5.977-37.591-23.848 1.0056.51 C ATOM 1568 CE LYS A 242 5.135-36.620-23.031 1.0056.40 C ATOM 1569 NZ LYS A 242 3.736-37.109-22.882 1.0056.49 N ATOM 1570 C LYS A 242 8.859-39.370-23.249 1.0056.01 C ATOM 1571 O LYS A 242 9.107 -38.168 -23.328 1.0055.92 O ATOM 1572 N VAL A 243 9.264-40.121-22.227 1.0056.28 N ATOM 1573 CA VAL A 243 9.903-39.540-21.034 1.0056.96 C ATOM 1574 CB VAL A 243 9.818-40.487-19.809 1.0057.04 C ATOM 1575 CGl VAL A 243 10.420-39.818-18.572 1.0056.83 C ATOM 1576 CG2VALA243 8.375-40.904-19.550 1.0057.52 C ATOM 1577 C VAL A 243 11.363-39.111-21.205 1.0057.22 C ATOM 1578 O VAL A 243 11.61 '4 -37.939-21..023 1.0057.33 O ATOM 1579 N VAL A 244 12.256-40.051-21.528 1.0057.66 N ATOM 1580 CA VAL A 244 13.693-39.748-21.602 1.0058.09 C ATOM 1581 CB VAL A 244 14.578-41.016-21.585 1.0057.99 C ATOM 1582 CGl VAL A 244 13.898-42.136-20.823 1.0058.05 C ATOM 1583 CG2VALA244 14.902-41.459-22.988 1.0057.87 C ATOM 1584 C VAL A 244 14.057-38.882-22.812 1.0058.63 C ATOM 1585 O VAL A 244 15.063-38.174-22.791 1.0058.67 O ATOM 1586 N GLY A 245 13.247-38.957-23.866 1.0059.32 N ATOM 1587 CA GLY A 245 13.291-37.975-24.960 1.0060.12 C ATOM 1588 C GLY A 245 14.427-38.053-25.967 1.0060.64 C ATOM 1589 O GLY A 245 14.404-37.358-26.987 1.0060.52 O ATOM 1590 N THR A 246 15.422-38.891-25.681 1.0061.23 N ATOM 1591 CA THR A 246 16.545-39.111-26.594 1.0061.72 . C ATOM 1592 CB THR A 246 17.713-39.822-25.877 1.0061.77 C ATOM 1593 OGl THR A 246 18.778-40.049-26.807 1.0062.38 O ATOM 1594 CG2THRA246 17.264 -41.160 -25.307 1.0061.63 C ATOM 1595 C THR A 246 16.109-39.947-27.803 1.0061.92 C ATOM 1596 O THR A 246 15.279-40.838-27.666 1.0061.87 O ATOM 1597 N PRO A 247 16.652-39.646-28.998 1.0062.13 N ATOM 1598 CA PRO A 247 16.324-40.447-30.180 1.0062.22 C ATOM 1599 CB PRO A 247 16.935-39.644-31.338 1.0062.11 C ATOM 1600 CG PRO A 247 17.223-38.284-30.771 1.0062.24 C ATOM 1601 CD PRO A 247 17.556-38.535-29.333 1.0062.13 C ATOM 1602 C PRO A 247 16.922-41.857-30.135 1.0062.38 C ATOM 1603 O PRO A 247 16.518-42.714-30.921 1.0062.55 O ATOM 1604 N GLU A 248 17.869-42.095-29.228 1.0062.37 N ATOM 1605 CA GLU A 248 18.454-43.427-29.065 1.0062.39 C ATOM 1606 CB GLU A 248 19.928-43.337-28.665 1.0062.54 C ATOM 1607 CG GLU A 248 20.752-42.415-29.542 1.0063.55 C ATOM 1608 CD GLU A 248 20.801-41.000-29.002 1.0064.86 C ATOM 1609 OEl GLU A 248 20.533-40.048-29.772 1.0065.06 O ATOM 1610 OE2GLUA248 21.10340.844 -27.798 1.0065.69 O ATOM 1611 C GLU A 248 17.687-44.235-28.030 1.0062.14 C ATOM 1612 O GLU A 248 17.524-43.801-26.892 1.0062.25 . O ATOM 1613 N VAL A 249 17.234-45.419-28.429 1.0061.87 N ATOM 1614 CA VAL A 249 16.374-46.254-27.590 1.0061.58 C ATOM 1615 CB VAL A 249 15.486-47.184-28.459 1.0061.51 C ATOM 1616 CGl VAL A 249 16.221-47.608-29.720 1.0061.83 C ATOM 1617 CG2 VAL A 249 15.035-48.396-27.674 1.0061.54 C ATOM 1618 C VAL A 249 17.134-47.072-26.538 1.0061.44 . C ATOM 1619 O VAL A 249 18.170-47.671-26.823 1.0061.45 O ATOM 1620 N LEU A 250 16.608-47.082-25.318 1.0061.36 N ATOM 1621 CA LEU A 250 17.189-47.851-24.224 1.0061.27 C ATOM 1622 CB LEU A 250 16.662-47.347-22.881 1.0061.02 C ATOM 1623 CG LEU A 250 17.582-46.481-22.021 1.0060.92 C ATOM 1624 CDl LEU A 250 18.366-45.482-22.848 1.0061.76 C ATOM 1625 CD2LEUA250 16.777-45.765-20.962 1.0061.02 C ATOM 1626 C LEU A 250 16.888-49.335-24.361 1.0061.49 C ATOM 1627 O LEU A 250 15.789-49.725-24.754 1.0061.64 O ATOM 1628 N ARG A 251 17.871-50.161-24.025 1.0061.69 N ATOM 1629 CA ARG A 251 17.693-51.606-24.018 1.0061.74 C ATOM 1630 CB ARG A 251 19.060-52.294-24.056 1.0061.77 C ATOM 1631 CG ARG A 251 19.056-53.780-23.705 1.0061.82 C ATOM 1632 CD ARG A 251 18.614-54.629-24.885 1.0061.89 C ATOM 1633 NE ARG A 251 19-429-55.833-25.010 1.0061.71 N ATOM 1634 CZ ARG A 251 19.057-57.040-24.598 1.0061.63 C ATOM 1635 NHl ARG A 251 17.874-57.216-24.030 1.0061.74 N ATOM 1636 NH2 ARG A 251 19.875-58.072-24.751 1.0061.58 N ATOM 1637 C ARG A 251 16.946-52.033-22.762 1.0061.79 C ATOM 1638 O ARG A 251 17.320-51.641-21.656 1.0061.72 O ATOM 1639 N VAL A 252 15.890-52.825-22.929 1.0061.91 . N ATOM 1640 CA VAL A 252 15.265 -53.487 -21.778 1.0062.11 C ATOM 1641 CB VAL A 252 13.724-53.317-21.741 1.0062.15 C ATOM 1642 CGl VAL A 252 13.357 -51.846₇21.684 1.0062.31 C ATOM 1643 CG2VALA252 13.085-53.976-22.949 1.0062.44 C ATOM 1644 C VAL A 252 15.625-54.972-21.739 1.0061.92 C ATOM 1645 O VAL A 252 15.675-55.633-22.776 1.0061.98 O ATOM 1646 N TYR A 253 15.894-55.482-20.541 1.0061.76 N ATOM 1647 CA TYR A 253 16.191 τ56.898 -20.351 1.0061.60 C ATOM 1648 CB TYR A 253. 17.414-57.072-19.449 1.0061.60 C ATOM 1649 CG TYR A 253 18.679-56.478-20.036 1.0062.19 C ATOM 1650 CDl TYR A 253 19.206-55.293-19.549 1.0062.55 G ATOM 1651 CEl TYR A 253 20.359-54.749-20.091 1.0062.44 C ATOM 1652 CZ TYR A 253 20.993-55.384-21.132 1.0061.97 C ATOM 1653 OH TYR A 253 22.139-54.844-21.673 1.0062.06 O ATOM 1654 CE2TYRA253 20.490-56.557-21.632 1.0062.23 C ATOM 1655 CD2TYRA253 19.341-57.098-21.088 1.0062.57 C ATOM 1656 C TYR A 253 14.976-57.588-19.749 1.0061.37 C ATOM 1657 O TYR A 253 14.563-57.252-18.640 1.0061.52 O ATOM 1658 N ILE A 254 14.400-58.539-20.484 1.0060.85 N ATOM 1659 CA ILE A 254 13.152-59.177-20.068 1.0060.38 C ATOM 1660 CB ILE A 254 12.245-59.455-21.275 1.0060.34 C ATOM 1661 CGl ILE A 254 12.301-58.278-22.251 1.0060.50 C ATOM 1662 CDl ILE A 254 11.238-58.319-23.329 1.0060.93 C ATOM 1663 CG2ILEA254 10.821-59.735-20.821 1.0059.77 C ATOM 1664 C ILE A 254 13.385-60.486-19.324 1.0060.21 C ATOM 1665 O ILE A 254 13.958-61.423-19,867 1.0060.30 O ATOM 1666 N GLY A 255 12.931-60.558-18.079 1.0059.92 N ATOM 1667 CA GLY A 255 13.090-61.789-17.310 1.0059.62 C ATOM 1668 C GLY A 255 12.484-61.725-15.923 1.0059.23 C ATOM 1669 O GLY A 255 11.792-60.766-15.585 1.0059.30 O ATOM 1670 N SER A 256 12.735-62.759-15.126 1.0058.78 N ATOM 1671 CA SER A 256 12.342-62.757-13.723 1.0058.69 C ATOM 1672 CB SER A 256 11.081-63.593-13.486 1.0058.72 C ATOM 1673 OG SER A 256 11.098-64.776-14.260 1.0059.59 O ATOM 1674 C SER A 256 13.500-63.204-12.829 1.0058.34 C ATOM 1675 O SER A 256 13.731-64.392-12.606 1.0058.22 O ATOM 1676 N PHE A 257 14.207-62.212-12.305 1.0058.01 N ATOM 1677 CA PHE A 257 15.459 -62.410 -11.606 1.0057.54 C ATOM 1678 CB PHE A 257 16.256-61.107-11.660 1.0057.11 C

ATOM 1679 CG PHE A 257 16.501-60.627-13.062 1.0056.81 C

ATOM 1680 CDl PHE A 257 17.747-60.763-13.651 1.0056.40 C

ATOM 1681 CEl PHE A 257 17.969-60.338-14.950 1.0055.40 C ATOM 1682 CZ PHE A 257 16.941-59.781-15.679 1.0055.70 C

ATOM 1683 CE2PHEA257 15.693-59.650-15.119 1.0055.89 C

ATOM 1684 CD2PHEA257 15.473-60.077-13.813 1.0056.91 C

ATOM 1685 C PHE A 257 15.300-62.948-10.177 1.0057.57 C

ATOM 1686 O PHE A 257 15.433-62.216 -9.193 1.0057.54 O ATOM 1687 N TRP A 258 15.008-64.243-10.090 1.0057.58 N

ATOM 1688 CA TRP A 258 14.989 -64.966 -8.821 1.0057.65 C

ATOM 1689 CB TRP A 258 13.858 -64.464 -7.917 1.0057.76 C

ATOM 1690 CG TRP A 258 12.478-64.843 -8.339 1.0057.87 C

ATOM 1691 CDl TRP A 258 12.077 -65.277 -9.572 1.0058.43 C ATOM 1692 NEl TRP A 258 10.723-65.520 -9.572 1.0058.60 N

ATOM 1693 CE2TRPA258 . 10.222-65.229 -8.329 1.0058.63 C

ATOM 1694 CD2TRPA258 11.299-64.791 -7.530 1.0058.19 C

ATOM 1695 CE3 TRP A 258 11.050-64.430 -6.201 1.0058.21 C

ATOM 1696 CZ3TRPA258 9.753-64.513 -5.720 1.0058.20 C ATOM 1697 CH2TRPA258 8.703-64.949 -6.539 1.0058.12 C

ATOM 1698 CZ2TRPA258 ^" 8.916-65.313 -7.842 1.0058.37 C

ATOM 1699 C TRP A 258 14.928-66.479 -9.058 1.0057.67 C

ATOM 1700 O TRP A 258 14.436-66.937-10.093 1.0057.71 O

ATOM 1701 N SER A 259 15.443-67.254 -8.107 1.0057.66 N ATOM 1702 CA SER A 259 15.578-68.706 -8.285 1.0057.55 C

ATOM 1703 CB SER A 259 16.660-69.255 -7.356 1.0057.60 C

ATOM 1704 OG SER A 259 17.916-68.667 -7.651 1.0058.07 O.

ATOM 1705 C SER A 259 14.274-69.478 -8.081 1.0057.36 C

ATOM 1706 O SER A 259 14.283-70.686 -7.836 1.0057.37 O ATOM 1707 N GLN A 260 13.156-68.775 -8.194 1.0057.11 N

ATOM 1708 CA GLN A 260 11.850-69.384 -8.021 1.0056.90 C

ATOM 1709 CB GLN A 260 10.841-68.302 -7.643 1.0057.05 C

ATOM 1710 CG GLN A 260 9.862-68.687 -6.541 1.0058.16 C

ATOM 1711 CD GLN A 260 10.543-68.952 -5.204 1.0059.01 C ATOM 1712 OEl GLN A 260 11.611-68.404 -4.913 1.0059.19 O

ATOM 1713 NE2 GLN A 260 9.922-69.798 -4.384 1.0058.96 N

ATOM 1714 C GLN A 260 11.441 -70.055 -9.327 1.00'56.43 C

ATOM 1715 O GLN A 260 11.879-69.640-10.396 1.0056.50 O

ATOM 1716 N PRO A 261 10.623 -71.113 -9.249 1.0056.02 N ATOM 1717 CA PRO A 261 10.059-71.724-10.452 1.0055.81 C

ATOM 1718 CB PRO A 261 9.110-72.785 -9.893 1.0055.75 C

ATOM 1719 CG PRO A 261 9.690-73.132 -8.570 1.0055.87 C

ATOM 1720 CD PRO A 261 10.223-71.832 -8.030 1.0056.03 C

ATOM 1721 C PRO A 261 9.292-70.729-11.319 1.0055.59 C ATOM 1722 O PRO A 261 8.921-69.652-10.859 1.0055.74 O

ATOM 1723 N LEU A 262 9.057-71.092-12.570 1.0055.30 N

ATOM 1724 CA LEU A 262 8.463-70.173-13.518 1.0055.12 C

ATOM 1725 CB LEU A 262 9.026-70.457-14.905 1.0055.09 C

ATOM 1726 CG LEU A 262 9.764-69.356-15.667 1.0054.85 C ATOM 1727 CDl LEU A 262 10.497-68.395-14.741 1.0054.87 C

ATOM 1728 CD2LEUA262 10.742-70.010-16.607 1.0054.29 C

ATOM 1729 C LEU A 262 6.966-70.386-13.513 1.0055.14 C

ATOM 1730. O LEU A 262 6.508-71.518-13.615 1.0055.24 O

ATOM 1731 N LEU A 263 6.198-69.309-13.379 1.0055.24 N ATOM 1732 CA LEU A 263 4.743-69.433-13.356 1.0055.20 C

ATOM 1733 CB LEU A 263 . 4.076-68.110-12.967 1.0055.14 C

ATOM 1734 CG LEU A 263 2.706-68.176-12.271 1.0055.03 C

ATOM 1735 CDl LEU A 263 2.132 -66.781 -12.099 1.00.54.72 C 16

ATOM 1736 CD2LEUA263 1.706-69.056-13.010 1.0055.07 C

ATOM 1737 C LEU A 263 4.266-69.875-14.729 1.0055.30 C

ATOM 1738 O LEU A 263 3.879.-71.025-14.921 1.0055.01 O

ATOM 1739 N VAL A 264 4.298-68.949-15.680 1.0055.62 N ATOM 1740 CA VAL A 264 3.950-69.260-17.059 1.0055.97 C

ATOM 1741 CB VAL A 264 3.016-68.194-17.669 1.0055.83 C

ATOM 1742 CGl VAL A 264 3.489-66.801-17.317 1.0055.89 C

ATOM 1743 CG2VALA264 2.898-68.376-19.175 1.0056.05 C

ATOM 1744 C VAL A 264 5.228-69.448-17.876 1.0056.23 C ■ ATOM 1745 O VAL A 264 5.8.82-68.484-18.251 1.0056.29 O

ATOM 1746 N PRO A 265 5.574-70.711-18.161 1.0056.68 N

ATOM 1747 CA PRO A 265 6.910-71.109-18.587 1.0057.10 C

ATOM 1748 CB PRO A 265 6.917-72.607-18.282 1.0057.09 C

ATOM 1749 CG PRO A 265 5.512-73.022-18.537 1.0056.77 C ATOM 1750 CD PRO A 265 4.657-71.863-18.091 1.0056.60 C

ATOM 1751 C PRO A 265 7.228-70.900-20.067 1.0057.60 C

ATOM 1752 O PRO A 265 8.402-70.934-20.449 1.0057.55 O

ATOM 1753 N ASP A 266 6.210-70.686-20.896 1.0058.11 N

ATOM 1754 CA ASP A 266 6.421 -70.770 -22.341 1.0058.60 C ATOM 1755 CB ASP A 266 5.111 -71.053-23.108 1.0058.96 C

ATOM 1756 CG ASP A 266 3.967-70.141 -22.702 1.0059.26 C

ATOM 1757 ODl ASP A 266 4.064-68.920-22.943 1.0060.12 O

ATOM 1758 OD2ASPA266 2.955-70.659-22.177 1.0059.63 O

ATOM 1759 C ASP A 266 7.205-69.617-22.951 1.0058.63 C ATOM 1760 O ASP A 266 6.978-69.238-24.092 1.0058.80 O

ATOM 1761 N ASN A 267 8.151-69.085-22.190 1.0058.79 N

ATOM 1762 CA ASN A 267 8.998-68.002-22.663 1.0058.87 C

ATOM 1763 CB ASN A 267 8.339-66.657-22.369 1.0058.66 C

ATOM 1764 CG ASN A 267 7.617-66.102-23.561 1.0058.19 C ATOM 1765 ODl ASN A 267 8.090-66.229-24.686 1.0058.89 O

ATOM 1766 ND2 ASN A 267 6.467-65.483-23.331 1.0057.38 N

ATOM 1767 C ASN A 267 10.387-68.040-22.037 1.0059.27 C

ATOM 1768 O ASN A 267 11.117-67.045-22.065 1.0059.19 O

ATOM 1769 N ARG A 268 10.763-69.187-21.477 1.0059.60 N ATOM 1770 CA ARG A 268 11.957-69.204-20.649 1.0059.99 C

ATOM 1771 CB ARG A 268 11.986-70.400-19.683 1.0060.07 C

ATOM 1772 CG ARG A 268 12.662-71.672-20.115 1.0060.90 C

ATOM 1773 CD ARG A 268 13.141-72.379-18.844 1.0063.18 C

ATOM 1774 NE ARG A 268 13.096-73.840-18.898 1.0065.28 N ATOM 1775 CZ ARG A 268 11.996-74.570-18.704 1.0066.78 C

ATOM 1776 NHl ARG A 268 10.830-73.975-18.460 1.0066.33 N

ATOM 1777 NH2ARGA268 12.057-75.902-18.764 1.0067.27 N

ATOM 1778 C ARG A 268 13.241-69.016-21.440 1.0060.01 C

ATOM 1779 O ARG A 268 14.156-68.351-20.970 1.0060.20 O ATOM 1780 N ARG A 269 13.287-69.550-22.654 1.0060.18 N

ATOM 1781 CA ARG A 269 14.414-69.298-23.548 1.0060.31 C

ATOM 1782 CB ARG A 269 14.079-69.759-24.967 1.0060.47 C

ATOM 1783 CG ARG A 269 14.873-70.966-25.444 1.0061.18 C

ATOM 1784 CD ARG A 269 16.252-70.541-25.953 1.0062.47 C ATOM 1785 NE ARG A 269 17.234-70.391-24.878 1.0062.90 N

ATOM 1786 CZ ARG A 269 18.457-70.919-24.900 1.0062.99 ^' C

ATOM 1787 NHl ARG A 269 18.866-71.619-25.952 1.0062.79 N

ATOM 1788 NH2ARGA269 19.281-70.729-23.875 1.0062.86 N

ATOM 1789 C ARG A 269 14.784-67.818-23.554 1.0060.15 C ATOM 1790 O ARG A 269 15.943-67.449-23.343 1.0060.18 O

ATOM 1791 N LEU A 270 13.781-66.978-23.789 1.0060.00 N ^•

ATOM 1792 CA LEU A 270 13.970-65.539-23.848 1.0059.87 C

ATOM 1793 CB LEU A 270 12.637-64.857-24.150 1.0059.80 C ATOM 1794 CG LEU A 270 12.602-63.460-24.777 1.0059.73 C ATOM 1795 CDl LEU A 270 12.448-62.370-23.734 1.0059.80 C ATOM 1796 CD2LEUA270 13.817-63.214-25.654 1.0059.78 C ATOM 1797 C LEU A 270 14.543-65.031-22.537 1.0059.92 C ATOM 1798 O LEU A 270 15.516-64.287-22.525 1.0060.09 O ATOM 1799 N PHE A 271 13.948-65.455-21.429 1.0060.22 N ATOM 1800 CA PHE A 271 14.377-65.006-20.109 1.0060.39 C ATOM 1801 CB PHE A 271 13.480-65.581-19.013 1.0060.47 C ATOM 1802 CG PHE A 271 12.029-65.224-19.166 1.0060.39 C ATOM 1803 CDl PHE A 271 11.653-64.051-19.811 1.0060.01 C ATOM 1804 CEl PHE A 271 10.319-63.716-19.953 1.0059.82 C ATOM 1805 CZ PHE A 271 9.341-64.546-19.432 1.0060.43 C ATOM 1806 CE2PHEA271 9.702-65.718-18.778 1.0060.27 C ATOM 1807 CD2 PHE. A 271 11.042-66.049-18.646 1.0060.08 C ATOM 1808 C PHE A 271 15.826-65.375-19.839 1.0060.56 C ATOM 1809 O PHE A 271 16.629-64.523-19.432 1.0060.91 O ATOM .1810 N GLU A 272 16.172-66.638-20.064 1.0060.53 N ATOM 1811 CA GLU A 272 17.557-67.032-19.881 1.0060.88 . C ATOM 1812 CB GLU A 272 17.780-68.554-19.987 1.0060.68 C ATOM 1813 CG GLU A 272 16.859-69.330-20.916 1.0061.39 C ATOM 1814 CD GLU A 272 17.054-70.852-20.801 1.0062.06 C ATOM 1815 OEl GLU A 272 16.525-71.608-21.655 1.0063.50 O ATOM 1816 OE2GLUA272 17.745-71.301-19.853 1.0064.06 O ATOM 1817 C GLU A 272 18.472-66.221-20.804 1.0060.54 C ATOM 1818 O GLU A 272 19.500-65.707-20.365 1.0060.78 O ATOM 1819 N LEU A 273 18.082-66.061-22.064 1.0060.28 N ATOM 1820 CA LEU A 273 18.885-65.255-22.979 1.0060.15 C ATOM 1821 CB LEU A 273 18.265-65.249-24.378 1.0060.05 C ATOM 1822 CG LEU A 273 19.067-66.013-25.429 1.0059.60 C ATOM 1823 CDl LEU A 273 20.501-65.525-25.383 1.0060.64 C ATOM 1824 CD2 LEU A 273 19.023-67.492-25.195 1.0059.04 C ATOM 1825 C LEU A 273 19.135-63.819-22.481 1.0060.30 C ATOM 1826 O LEU A 273 20.285-63.350-22.429 1.0060.39 O - ATOM' 1827 N GLU A 274 18.059-63.128-22.114 1.0060.35 N ATOM 1828 CA GLU A 274 18.162-61.747-21.656 1.0060.63 C ATOM 1829 CB GLU A 274 16.774-61.173-21.378 1.0060.61 C ATOM 1830 CG GLU A 274 15.841-61.133-22.589 1.0061.23 C ATOM 1831 CD GLU A 274 .16.125-59.970-23.531 1.0062.07. C ATOM 1832 OEl GLU A 274 15.475-58.910-23.376 1.0062.22 O ATOM 1833 OE2GLUA274 16.996-60.115-24.421 1.0062.05 O ATOM 1834 C GLU A 274 19.025-61.672-20.402 1.0060.74 C ATOM 1835 O GLU A 274 19.923-60.821-20.280 1.0060.90 O ATOM 1836 N GLU A 275 18.752-62.578-19.473 1.0060.89 N ATOM 1837 CA GLU A 275 19.561-62.697-18.276 1.0061.09 C ATOM 1838 CB GLU A 275 19.106-63.919-17.491 1.0061.28 C ATOM 1839 CG GLU A 275 19.561-63.971-16.051 1.0062.13 C ATOM 1840 CD GLU A 275 19.147-65.272-15.391 1.0063.3.8 C ATOM 1841 OEl GLU A 275 19.938-65.821-14.587 1.0063.96 O ATOM 1842 OE2GLUA275 18.033-65.757-15.698 1.0063.30 O ATOM 1843 C GLU A 275. 21.037-62.822-18.658 1.0061.04 C ATOM 1844 O GLU A 275 21.896 -62.138 -18.102 1.0060.86 O ATOM 1845 N GLN A 276 21.323-63.688-19.623 1.0061.18 N ATOM 1846 CA GLN A 276 22.689-63.863-20.110 1.0061.56 C ATOM 1847 CB GLN A 276 22.749-64.934-21.207 1.0061.86 C ATOM 1848 CG GLN A 276 22.828-66.357-20.681 1.0063.52 C ATOM 1849 CD GLN A 276 24.095-66.593-19.875 1.0066.43 C ATOM 1850 OEl GLN A 276 25.197-66.659-20.431 1.0067.98 O ATOM 1851 NE2GLNA276 23.947-66.718-18.557 1.0067.10 N ATOM 1852 C GLN A 276 23.282-62.550-20.618 1.0061.36 C ATOM 1853 O GLN A 276 24.414-62.196-20.269 1.0061.33 O ATOM 1854 N ASP A 277 22.523-61.827-21.437 1.0061.08 N ATOM 1855 CA ASP A 277 23.030-60.572-21.987 1.0061.12 C 5 ATOM 1856 CB ASP A 277 22.044-59.973-22.993 1.0061.25 C ATOM 1857 CG ASP A 277 21.989-60.757-24.307 1.0062.18 C ATOM 1858 ODl ASP A 277 22.708-61.774-24.444 1.0063.05 O ATOM 1859 OD2ASPA277 21.223-60.356-25.213 1.0063.07 O ATOM 1860 C ASP A 277 23.366-59.576-20.873 1.0060.97 C

10 ATOM 1861 O ASP A 277 24.484-59.023-20.818 1.0061.14 O ATOM 1862 N LEU A 278 22.411 -59.359 -19.969 1.0060.75 N ATOM 1863 CA LEU A 278 22.657-58.435-18.859 1.0060.28 C ATOM 1864 CB LEU A 278 21.412-58.273-17.973 1.0060.28 C ATOM 1865 CG LEU A 278 21.560-57.508-16.651 1.0059.63 C

15 . ATOM 1866 CDl LEU A 278 21.808-56.034-16.902 1.0058.86 C ATOM 1867 CD2LEUA278 20.334-57.694-15.776 1.0059.64 C ATOM 1868 C LEU A 278 23.860-58.894-18.034 1.0060.34 C ATOM 1869 O LEU A 278 • 24.730-58.091-17.684 1.0060.18 O ATOM 1870 N PHE A 279 23.916-60.190-17.735 1.0060.47 N

20 ^' ATOM 1871 CA PHE A 279 25.030-60.706-16.950 1.0060.57 C ATOM 1872 CB PHE A 279 24.897-62.197-16.662 1.0060.52 C ATOM 1873 CG PHE A 279 23.881-62.511-15.618 1.0060.50 C ATOM 1874 CDl PHE A 279 23.466-61.533-14.729 1.0060.16 C ATOM 1875 CEl PHE A 279 22.523-61.808-13.766 1.0060.38 C

25. ATOM 1876 CZ PHE A 279 21.992-63.075-13.670 1.0060.80 C ATOM 1877 CE2PHEA279 22.408-64.068-14.548 1.0060.94 C ATOM 1878 CD2PHEA279 23.346-63.783-15.514 1.0060.60 C ATOM 1879 C PHE A 279 26.350-60.418-17.630 1.0060.72 C ATOM 1880 O PHE A 279 27.261-59.888-17.007 1.0060.64 O

30 ATOM 1881 N ARG A 280 26.462-60.758-18.908 1.0060.96 N ATOM 1882 CA ARG A 280 ^'27.662-60.380-19.633 1.0061.16 C ATOM 1883 CB ARG A 280 27.549-60.714-21.123 1.0061.05 C ATOM 1884 CG ARG A 280 28.208-62.041-21.488 1.0061.56 C ATOM 1885 CD ARG A 280 28.096-62.359-22.976 1.0061.94 C

35 ATOM 1886 NE ARG A 280 26.969-63.243-23.280 1.0063.84 N ATOM 1887 CZ ARG A 280 25.713-62.833-23.459 1.0064.28 C ATOM 1888 NHl ARG A 280 25.410-61.542-23.363 1.0064.38 N ATOM 1889 NH2ARGA280 24.759-63.718-23.733 1.0064.17 N ATOM 1890 C ARG A 280 27.951-58.895-19.396 1.0061.05 C

40 ATOM 1891 O ARG A 280 29.071 -58.525 -19.027 1.0060.89 O

ATOM 1892 N ASP A 281 26.932-58.053-19.561 1.0061.18 N ^*

ATOM 1893 CA ASP A 281 27.123-56.605-19.389 1.0061.26 C

. ATOM 1894 CB ASP A 281 25.814-55.846-19.642 1.0061.67 C

ATOM 1895 CG ASP A 281 26.023-54.555-20.433 1.0062.92 C

45 ATOM 1896 ODl ASP A 281 27.161-54.026-20.453 1.0063.95 O ATOM 1897 OD2ASPA281 25.041-54.076-21.048 1.0064.41 O ATOM 1898 C ASP A 281 27.700-56.222-18.020 1.0060.84 C ATOM 1899 O ASP A 281 28.646-55.446-17.943 1.0060.76 O ATOM 1900 N ILE A 282 • 27.125-56.763-16.948 1.0060.54 N

50 ATOM 1901 CA ILE A 282 27.616-56.507-15.589 1.0060.21 C ATOM 1902 CB ILE A 282 26.726-57.185-14.534 1.0060.12 C ATOM 1903 CGl ILE A 282 25.316-56.592-14.547 1.0060.23 C ATOM 1904 CDl ILE A 282 24.299-57.415-13.778 1.0059.99 C ATOM 1905 CG2ILEA282 27.357-57.075-13.150 1.0059.55 C

55 ATOM 1906 C ILE A 282 29.009-57.077-15.409 1.0060.29 C ATOM 1907 O ILE A 282 29.945 -56.371 --15.057 1.0060.29 O ATOM 1908 N GLN A 283 29.128 -58.375 -15.651 1.0060.51 N ATOM 1909 CA GLN A 283 30.374-59.096-15.479 1.0060.54 C ATOM 1910 CB GLN A 283 30.218-60.538-15.964 1.0060.59 C ATOM 1911 CG GLN A 283. 31.250-61.500-15.404 1.0061.30 C ATOM 1912 CD GLN A 283 32.334-61.830-16.404 1.0062.16 C ATOM 1913 OEl GLN A 283 33.515-61.936-16.054 1.0062.37 O ATOM 1914 NE2 GLN A 283 31.938-61.995-17.664 1.0062.82 N ATOM 1915 C GLN A 283 31.498-58.403-16.223 1.0060.41 C ATOM 1916 O GLN A 283 32.660-58.514-15.838 1.0060.58 O ATOM 1917 N GLY A 284 31.145-57.670-17.275 1.0060.32 N ATOM 1918 CA GLY A 284 32.142-56.993-18.098 1.0059.90 C ATOM 1919 C GLYA284 32.647 -55.656 -17.576.1.0059.63 C ATOM 1920 O GLY A 284 33.536-55.052-18.175 1.0059.69 O ATOM 1921 N LEU A 285 32.096-55.194-16.458 1.0059.39 N ATOM 1922 CA LEU A 285 32.397 -53.848 -15.950 1.0059.12 C ATOM 1923 CB LEU A 285 31.494-53.498-14.761 1.0058.97 C ATOM 1924 CG LEU A 285 30.009-53.305-15.056 1.0058.44 C ATOM 1925 CDl LEU A 285 29.291-52.805-13.819 1.0058.10 C ATOM 1926 CD2LEUA285 29.822-52.345-16.210 1.0058.23 C ATOM 1927 C LEU A 285 33.864-53.581-15.588 1.0059.12 C ATOM 1928 O LEU A 285 34.466-52.638-16.110 1.0058.98 O ATOM 1929 N PRO A 286 34.444-54.409-14.698 1.0059.17 N ATOM 1930 CA PRO A 286 35.792-54.145-14.203 1.0059.19 C ATOM 1931 CB PRO A 286 36.075-55.339-13.288 1.0059.12 C ATOM 1932 CG PRO A 286 34.744-55.870-12.925 1.0059.19 C ATOM 1933 CD PRO A 286 33.888-55.648-14.127 1.0059.17 C ATOM 1934 C PRO A 286 36.789-54.132,-15.342 1.0059.26 C ATOM 1935 O PRO A 286 37.746-53.357-15.323 1.0059.19 O ATOM 1936 N ARG A 287. 36.553-54.989-16.331 1.0059.46 N ATOM 1937 CA ARG A 287 37.412-55.057-17.499 1.0059.64 C ATOM 1938 CB ARG A 287 36.797-55.921-18.592 1.0059.76 C ATOM 1939 CG ARG A 287 37.768-56.326-19.690 1.0060.10 C ATOM 1940 CD ARG A 287 37.147-57.427-20.510 1.0061.21 C ATOM 1941 NE ARG A 287 36.470-58.384-19.637 1.0062.03 N ATOM 1942 CZ ARG A 287 35.399-59.089-19.984 1.0062.52 C ATOM 1943 NHl ARG A 287 J34.852 -59.933 -19.118 1.0062.89 N ATOM 1944 NH2 ARG A 287 '34.871-58.943-21.192 1.0062.75 N ATOM 1945 C ARG A 287 37.685-53.659-18.017 1.0059.65 C ATOM 1946 O ARG A 287 38.790-53.378-18.474 1.0059.81 . O ATOM 1947 N HIS A 288 36.694-52.772-17.946 1.0059.63 N ATOM 1948 CA HIS A 288 37.017-51.366-18.161 1.0059.67 C ATOM 1949 CB HIS A 288 37.330-51.042-19.616 1.0059.99 C ATOM 1950 CG HIS A 288 38.788-50.816-19.848 1.0061.01 C ATOM 1951 NDl HIS A 288 39.584-50.164-18.929 1.0061.71 N ATOM 1952 CEl HIS A 288 40.826-50.118-19.381 1.0062.63 C ATOM 1953 NE2 HIS A 288 40.864-50.719-20.558 1.0062.85 N ATOM 1954 CD2HISA288 39.603-51.171-20.870 1.0062.15 C ATOM 1955 C HIS A 288 36.213-50.263-17.500 1.0059.26 C ATOM 1956 O HIS A 288 35.213-49.774-18.027 1.0059.07 O ATOM 1957 N ALA A 289 36.721-49.867-16.340 1.0058.88 N ATOM 1958 CA ALA A 289 36.302-48.660-15.668 1.0058.55 C ATOM 1959 CB ALA A 289 36.632-48.746-14.182 1.0058.66 C ATOM 1960 C ALA A 289 37.013-47.468-16.301 1.0058.24 C. ATOM 1961 O ALA A 289 36.464-46.372-16.359 1.0058.03 O ATOM 1962 N ALA A 290 38.233-47.688-16.781 1.0057.82 N ATOM 1963 CA ALA A 290 39.024-46.609-17.358 1.0057.55 C ATOM 1964 CB ALA A 290 40.307-47.154-17.938 1.0057.56 C ATOM 1965 C ALA A 290 38.252-45.822-18.416 1.0057.41 C ATOM 1966 O ALA A 290 38.284-44.587-18.437 1.0057.25 O ATOM 1967 N LEU A 291 37.557-46.542-19.289 1.0057.29 N ATOM 1968 CA LEU A 291 36.796-45.916-20.362 1.0057.23 C ATOM 1969 CB LEU A 291 36.243-46.984-21.308 1.0057.15 C ATOM 1970 CG LEU A 291 36.111-46.651-22.796 1.0056.86 C ATOM 1971 CDl LEU A 291 35.366-47.763-23.507 1.0056.79 C ATOM 1972 CD2LEUA291 35.407-45.328-23.016 1.0057.08 C ATOM 1973 C LEU A 291 35.658-45.059-19.802 1.0057.31 C ATOM 1974 O LEU A 291 35.502-43.894-20.180 1.0057.24 O ATOM 1975 N ARG A 292 34.866-45.629-18.897 1.0057.43 N ATOM 1976 CA ARG A 292 33.724-44.901-18.343 1.0057.57 C ATOM 1977 CB ARG A 292 32.790-45.826-17.545 1.0057.62 C ATOM 1978 CG ARG A 292 33.064-45.912-16.049 1.0057.76 C ATOM 1979 CD ARG A 292 32.064-45.093-15.239 1.0057.94 . C ATOM 1980 NE ARG A 292 32.428-45.049-13.823 1.0058.09 N ATOM 1981 CZ ARG A 292 32.935-43.984-13.209 1.0057.92 C ATOM 1982 NHl ARG A 292 33.241-44.043-11.923 1.0058.28 N ATOM 1983 NH2ARGA292 33.133-42.855-13.874 1.0058.17 N ATOM 1984 C ARG A 292 34.204-43.718-17.508 1,0057.46 C ATOM 1985 O ARG A 292 33.588-42.648-17.520 1.0057.56 O ATOM 1986 N LYS A 293 35.312-43.912-16.802 1.0057.36 N ATOM 1987 CA LYS A 293 35.942-42.831-16.067 1.0057.19 C ATOM 1988 CB LYS A 293 37.186-43.323-15.330 1.0057.19 C ATOM 1989 CG LYS A 293 36.886-44.029-14.020 1.0057.17 C ATOM 1990 CD LYS A 293 38.050-44.901-13.578 1.0057.02 C ATOM 1991 CE LYS A 293 37.757-45.577-12.248 1.0057.19 C ATOM 1992 NZ LYS A 293 38.749-46.645-11.944 1.0057.34 N ATOM 1993 C LYS A 293 36.304-41.729-17.043 1.0057.09 C ATOM 1994 O LYS A 293 35.865-40.588-16.892 1.0057.11 O ATOM 1995 N LEU A 294 37.091 -42.079 -18.055 1.0056.95 N ATOM 1996 CA LEU A 294 37.458-41.121-19.083 1.0056.84 C ATOM 1997 CB LEU A 294 38.123-41.836-20.259 1.0056.79 C ATOM 1998 CG LEU A 294 38.441-40.974-21.483 1.0056.79 C ATOM .1999 CDl LEU A 294 39.335-39.809-21.097 1.0057.30 C ATOM 2000 CD2LEUA294 39.095-41.802-22.568 1.0056.83 C ATOM 2001 C LEU A 294 36.226-40.348-19.550 1.0056.79 C ATOM 2002 O LEU A 294 36.167-39.112-19.454 1.0056.76 O ATOM 2003 N ASN A 295 35.236 -41.084 -20.039 1.0056.85 N ATOM 2004 CA ASN A 295 34.003-40.469-20.527 1.0056.94 C ATOM 2005 CB ASN A 295 32.999-41.549-20.922 1.0057.00 C ATOM 2006 CG ASN A 295 32.915-41.708-22.436 1.0057.02 C ATOM 2007 ODl ASN A 295 33.082-42.815-22.972 1.0056.80 O ATOM 2008 ND2ASNA295 32.656-40.594-23.140 1.0057.22 N ATOM 2009 C ASN A 295 33.355-39.494-19.545 1.0056.98 C ATOM 2010 O ASN A 295 33.029-38.355-19.897 1.0056.90 O ATOM 2011 N ASP A 296 33.163-39.939-18.311 1.0057.20 N ATOM 2012 CA ASP A 296 32.544-39.075-17.319 1.0057.27 C ^' ATOM 2013 CB ASP A 296 32.240-39.854-16.040 1.0057.49 C ATOM 2014 CG ASP A 296 31.232-40.978-16.270 1.0058.34 C ATOM 2015 ODl ASP A 296 31.236-41.950-15.485 1.0059.28 O ATOM 2016 OD2 ASP A 296 30.441-40.898-17.241 1.0059.32 O ATOM 2017 C ASP A 296 33.409-37.844-17.057 1.0057.08 C ATOM 2018 O ASP A 296 32.886-36.745-16.834 1.0056.96 O ATOM 2019 N LEU A 297 34.728-38.027-17.115 1.0056.92 N ATOM 2020 CA LEU A 297 35.652 -36.901 -17.027 1.0056.71 C ATOM 2021 CB LEU A 297 37.110-37.360-17.104 1.0056.70 C ATOM 2022 CG LEU A 297 38..145 -36.289 -16.736 1.0057.00 C ATOM 2023 CDl LEU A 297 38.338-36.212-15.230 1.0057.18 C ATOM 2024 CD2LEUA297 39.486-36.538-17.417 1.0057.32 C ATOM 2025 C LEU A 297 35.357-35.904-18.140 1.0056.57 C ATOM 2026 O LEU A 297 35.223-34.709-17.882 1.0056.57 O ATOM 2027 N VAL A 298 35.246-36.394-19.374 1.0056.40 N- ATOM 2028 CA VAL A 298 34.872-35.528-20.498 1.0056.20 C ATOM 2029 CB VAL A 298 34.701-36.323-21.801 1.0056.10 C ATOM 2030 CGl VAL A 298 34.213-35.414-22.920 1.0055.78 C ATOM 2031 CG2VALA298 35.994-37.011 -22.183 1.0055.98 C ATOM 2032 C VAL A 298 33.562-34.781-20.239 1.0056.34 C ATOM 2033 O VAL A 298 33.490-33.550-20.372 1.0056.51 O ATOM 2034 N LYS A 299 32.523-35.532-19.880 1.0056.48 N ATOM 2035 CA LYS A 299 31.207-34.944-19.649 1.0056.48 C ATOM 2036 CB LYS A 299 30.223-36.009-19.163 1.0056.50 C ATOM 2037 CG LYS A 299 29.928-37.118-20.171 1.0056.54 C ATOM 2038 CD LYS A 299 29.057-38.204-19.543 1.0056.73 C ATOM 2039 CE LYS A 299 28.654-39.272-20.554 1.0057.33 C ATOM 2040 NZ LYS A 299 27.703-38.749-21.571 1.0057.04 N ATOM 2041 C LYS A 299 31.312-33.824-18.623 1.0056.44 C ATOM 2042 O LYS A 299 30.872-32.676-18.860 1.0056.62 O ATOM 2043 N ARG A 300 31.910-34.158-17.482 1.0056.46 N ATOM 2044 CA ARG A 300 32.147-33.159-16.456 1.0056.31 C ATOM 2045 CB ARG A 300 32.985-33.720-15.307 1.0056.27 C ATOM 2046 CG ARG A 300 33.478-32.651-14.337 1.0056.17 C ATOM 2047 CD ARG A 300 34.274-33.246-13.191 1.0056.14 C ATOM 2048 NE ARG A 300 33.429-33.563-12.047 1.0056.16 N ATOM 2049 CZ ARG A 300 33.530-32.970-10.862 1.0056.53 C ATOM 2050 NHl ARG A 300_. 32.722-33.317 -9.870 1.0056.30 N ATOM 2051 NH2ARGA300 34.450-32.037-10.665 1.0056.98 N ATOM 2052 C ARG A 300 32.834-31.952-17.081 1.0056.37 C ATOM 2053 O ARG A 300 32.329-30.834-16.996 1.0056.39 O ATOM 2054 N ALA A 301 33.973-32.186-17.729 1.0056.45 N ATOM 2055 CA ALA A 301 34.714-31.106-18.374 1.0056.41 C ATOM 2056 CB ALA A 301 35.758-31.660-19.331 1.0056.29 C ATOM 2057 C ALA A 301 33.761-30.172-19.104 1.0056.46 C ATOM 2058 O ALA A 301 33.722-28.971-18.821 1.0056.47 O ATOM 2059 N ARG A 302 32.980-30.728-20.025 1.0056.55 N ATOM 2060 CA ARG A 302 32.035-29.923-20.808 1.0056.77 C ATOM 2061 CB ARG A 302 31.260-30.818-21.777 1.0056,86 C ATOM 2062 CG ARG A 302 32.166-31.414-22.840 1.0057.73 C ATOM 2063 CD ARG A 302 31.637-32.710-23.404 1.0059.51 C ATOM 2064 NE ARG A 302 30.704-32.490-24.503 1.0061.12 N ATOM 2065 CZ ARG A 302 29.383-32.597-24.393 1.0062.12 C ATOM 2066 NHl ARG A 302 28.831-32.927-23.228 1.0062.16 N ATOM 2067 NH2ARGA302 . 28.612 -32.381 -25.452 1.0062.71 N ATOM 2068 C ARG A 302 31.093-29.087-19.932 1.0056.68 C ^' ATOM 2069 O ARG A 302 30.924-27.862-20.149 1.0056.68 O ATOM 2070 N LEU A 303 30.503-29.735-18.927 1.0056.67 N ATOM 2071 CA LEU A 303 29.663-28.990-17.981 1.0056.63 C ATOM 2072 CB LEU A 303 29.083-29.913-16.910 1.0056.59 C ATOM 2073 CG LEU A 303 28.182-29.195-15.902 1.0056.67 C ATOM 2074 CDl LEU A 303 26.913-28.699-16.582 1.0056.50 C ATOM 2075 CD2LEUA303 27.844-30.106-14.733 1.0057.07 C ATOM 2076 C LEU A 303 30.433-27.832-17.323 1.0056.59 C ATOM 2077 O LEU A 303 29.971 -26.677 -17.307 1.0056.69 O ATOM 2078 N VAL A 304 31.606-28.149-16.781 1.0056.40 N ATOM 2079 CA VAL A 304 32.482-27.143-16.199 1.0056.15 C ATOM 2080 CB VAL A 304 33.862-27.728-15.855 1.0056.03. C ATOM 2081 CGl. VAL A 304 34.801-26.633-15.389 1.0055.85 C ATOM 2082 CG2VALA304 33.728-28.800-14.797 1.00^" 55.67 C ATOM 2083 C VAL A 304 32.655-25.971-17.159 1.0056.22 C ATOM 2084 O VAL A 304 32.319-24.832-16.825 1.0056.31 O

ATOM 2085 N ARG A 305 33.166-26.249-18.356 1.0056.24 N

ATOM 2086 CA ARG A 305 33.364-25.195-19.351 1.0056.28 C

ATOM 2087 CB ARG A 305 33.760-25.783-20.714 1.0056.25 C ATOM 2088 CG ARG A 305 33,325 -24.961 -2L919 1.0056.53 C

ATOM 2089 CD ARG A 305 34.485-24.659-22.872 1.0057.09 C

ATOM 2090 NE ARG A 305 34.903-25.757-23.746 1.0057.25 N

ATOM 2091 CZ ARG A 305 34.124-26.746-24.174 1.0057.93 C

ATOM 2092 NHl ARG A 305 34.632-27.680-24.968 1.0057.81 N ATOM 2093 NH2ARGA305 32.845-26.809-23.820 1.0058.76 N

ATOM 2094 C ARG A 305 32.126-24.303-1.9.448 1.0056.28 C

ATOM 2095 O ARG A 305 32.223-23.058-19.357 1.0056.39 O

ATOM 2096 N VAL A 306 30.956-24.931 -19.589 1.0056.35 N

ATOM 2097 CA VAL A 306 29.727-24.136-19.630 1.0056.27 C ATOM 2098 CB VAL A 306 28.487-25.017-19.682 1.0056.15 C

ATOM 2099 CGl VAL A 306 27.267-24.162-19.959 1.0056.18 C

ATOM 2100 CG2VALA306 28.652-26.085-20.738 1.0056.17 C

ATOM 2101 C VAL A 306 29.608-23.217-18.409 1.0056.36 C

ATOM 2102 O VAL A 306 29.536-21.983-18.532 1.0056.51 O ATOM 2103 N HIS A 307 29.588-23.822-17.227 1.0056.41 N

ATOM 2104 CA HIS A 307 29.471-23.049-15.993 1.0056.44 C ATOM 2105 CB HIS A 307 29.743-23.942-14.783 1.0056.45 C

ATOM 2106 CG HIS A 307 29.652-23.225-13.474 1.0055.91 C

ATOM 2107 NDl HIS A 307 28.449-22.849-12.914 1.0055.76 N ATOM 2108 CEl HIS A 307 28.672-22.245-11.760 1.0055.92 C

ATOM 2109 NE2 HIS A 307 29.976-22.221-11.548 1.0056.18 N

ATOM 2110 CD2HISA307 30.612-22.827-12.606 LOO 55.83 C

ATOM 2111 C HIS A 307 30.427-21.856-15.981 1.0056.54 C

ATOM 2112 O HIS A 307 30.023-20.712-15.705 1.0056.69 O ATOM 2113 N ALA A 308 31.696-22.138-16.281 1.0056.50 N

ATOM 2114 CA ALA A 308 32.722.-21.106-16.342 1.0056.41 C

ATOM 2115 CB ALA A 308 34.000-21.659-16.921 1.0056:25 C

ATOM 2116 C ALA A 308 32.211-19.972-17.198 1.0056.41 C

ATOM 2117 O ALA A 308 32.153-18.819-16.751 1.0056.62 O ^' ATOM 2118 N TYRA309 31.814-20.299-18.424 1.0056.40 N

ATOM 2119 CA TYR A 309 31.311-19.251-19.299 1.0056.51 C

ATOM 2120 CB TYR A 309 30.868-19.809-20.650 1.0056.57 C

ATOM 2121 CG TYR A 309 32.021-20.031-21.598 1.0056.51 C

ATOM 2122 CDl TYR A 309 32.161-21.225-22.287 1.0056.48 C ATOM 2123 CEl TYR A 309 33.219-21.429-23.150 1.0056.59 C

ATOM 2124 CZ TYR A 309 34.159-20.436-23.323 1.0056.61 C

ATOM 2125 OH TYR A 309 35.215-20.639-24.178 1.0056.68 O

ATOM 2126 CE2TYRA309 34.048-19.243-22.644 1.0056.61 C

ATOM 2127 CD2TYRA309 32.985-19.048-21.786 1.0056.59 C ATOM 2128 C TYR A 309 30.193-18.455-18.632 1.0056,61 C

ATOM 2129 O TYR A 309 30.250-17.219-18.581 1.0056.91 O

ATOM 2130 N ILE A 310 29.193-19.158-18.102 1.0056.59 N

ATOM 2131 CA ILE A 310 28.068-18.486-17.439 1.0056.63 C

ATOM 2132 CB ILE A 310 27.113-19.492-16.774 1.0056.52 C ATOM 2133 CGl ILE A 310 26.552-20.463-17.809 1.0056.47 C

ATOM 2134 CDl ILE A 310 25.786-21.610-17.202 1.0056.57 C

ATOM 2135 CG2ILEA310 . 25.980 -18.768 -16.079 1.0056.40 C ,

ATOM 2136 C ILE A 310 28.523-17.463-16.387 1.0056.78. C

ATOM 2137 O ILE A 310 28.192-16.258-16.473 1.0057.05 O ATOM 2138 N ILE A 311 29.283-17.938-15.399 1.0056.75 . N

ATOM 2139 CA ILE A 311 29.750-17.046-14.338 1.0056.82 C

ATOM 2140 CB ILE A 311 30.607-17.771-13.281 1.0056.78 C

ATOM 2141 CGl ILE A 311 29.743-18.232-12.109 1.0056.78 C ATOM 2142 CDl ILE A 311 28.714-19.266-12.461 1.0057.40 C ATOM 2143 CG2ILEA311 31.655-16.834-12.716 1.0057.09 C ATOM 2144 C ILE A 311 30.532-15.882-14.932 1.0056.87 C ATOM 2145 O ILE A 311 30.257-14.714-14.630 1.0056.99 O ATOM 2146 N SER A 312 31.495-16.205-15.792 1.0056.92 N ATOM 2147 CA SER A 312 32.304-15.181-16.436 1.0057.06 C ATOM 2148 CB SER A 312 33.181-15.797-17.521 1.0057.04 C ATOM 2149 OG SER A 312 34.124-16.687-16.952 1.0057.03 O ATOM 2150 C SER A 312 31.437-14.078-17.028 1.0057.22 • C ATOM 2151 O SERA312 31.633-12.896-16.726 1.0057.33 O ATOM 2152 N TYR A 313 30.474-14.464-17.864 1.0057.40 N ATOM 2153 CA TYR A 313 29.591-13.479-18.501 1.0057.83 C ATOM 2154 CB TYR A 313 28.638-14.142-19.503 1.0058.15 C ATOM 2155 CG TYRA 313 29.257-14.429-20.864 1.0058.84 C ATOM 2156 CDl TYR A 313 28.576-14.120-22.041 1.0059.36 C ATOM 2157 CE1TYRA313 29.137-14.383-23.290 1.0059.39 C ATOM 2158 CZ TYR A 313 30.395-14.957_^23.368 1.0059.16 C ATOM 2159 OH TYRA 313 30.957-15.219-24.597 1.0059.00 O ATOM 2160 CE2TYRA313 31.093 -15.269 -22.216 1.0059.29 C ATOM 2161 CD2TΫRA313 30.525-15.004-20.974 1.0059.34 C ATOM 2162 C TYRA313 28.815-12.657-17.471 1.0057.75 C ATOM 2163 O TYR A 313 28.734-11.423-17.578 1.0057.91 O ATOM 2164 N LEU A 314 28.257-13.328-16.465, 1.0057.51 N ATOM 2165 CA LEU A 314 27.569-12.590-15.403 1.0057.40 C ATOM 2166 CB LEU A 314 27.057-13.550-14.330 1.0057.20 C ATOM 2167 CG LEU A 314 25.894-14.430-14.790 1.0056.64 C ATOM 2168 CDl LEU A 314 25.739-15.648-13.905 1.0055.97 C ATOM 2169 CD2 LEUA 314 24.612-13.622-14.836 1.0056.28 C ATOM 2170 C LEU A 314 28.481-11.514-14.795 1.0057.49 C ATOM 2171 O LEU A 314 28.138-10.316-14.753 1.0057.84 O ATOM 2172 N LYS A 315 29.656-11.949-14.344 1.0057.46 N ATOM 2173 CA LYS A 315 30.624-11.045-13.725 1.0057.51 C ATOM 217.4 CB LYS A 315 31.880-11.804-13.290 1.0057.50 C ATOM 2175 CG LYS A 315 33.079-10.920-12.986 1.0057.23 C ATOM 2176 CD LYS A 315 32.828-10.022-11.793 1.0057.26 C ATOM 2177 CE LYS A 315 34.012 -9.103-11.556 1.0057.59 C • ATOM 2178 NZ LYS A 315 33.958 -8.446-10.218 1.0057.78 N ATOM 2179 C LYS A 315 31.003 -9.898-14.648 1.0057.60 C ATOM 2180 O LYS A 315 31.104 -8.753-14.207 1.0057.65 O ATOM 2181 N LYS A 316 31.217-10.202-15.925 1.0057.67 N ATOM 2182 CA LYS A 316 31.571 -9.156-16.880 1.0057.96 C ATOM 2183 CB LYS A 316 32.094 -9.747-18.198 1.0058.04 C ATOM 2184 CG LYS A 316 31.033-10.014-19.266 1.0058.13 C ATOM.2185 CD LYS A 316 31.633-10.748-20.463 1.0058.14 C ATOM 2186 CE LYS A 316 30.559-11.212-21.441 1.0058.37 C ATOM 2187 NZ LYS A 316 29.905-10.080-22.159 1.0058.37 N ATOM 2188 C LYS A 316 30.386 -8.223-17.128 1.0057.99 C ATOM 2189 O LYS A 316 30.559 -7.095-17.590 1.0057.89 O ATOM 2190 N GLU A 317 29.183 -8.693-16.812 1.0058.12 N ATOM 2191 CA GLUA 317 28.004 -7.848-16.967 1.0058.35 C ATOM 2192 CB GLUA 317 26.752 -8.689-17.228 1.0058.34 C ATOM 2193 CG GLU A 317 25.722 -7.983 -18.087 1.0058.29 C ATOM 2194 CD GLU A 317 26.286 -7.568 -19.434 1.0058.49 C ATOM 2195 OEl GLU A 317 25.892 -6.495 -19.943 1.0058.78 O ^' ATOM 2196 OE2 GLU A 317 27.130 -8.311-19.982 1.0058.20 O ATOM 2197 C GLU A 317 27.791 -6.929-15.765 1.0058.52 C ATOM 2198 O GLU A 317 27.312 -5.806-15.919 1.0058.43 O ATOM 2199 N MET A 318 28.147 -7.408-14.574 1.0058.76 N ATOM 2200 CA MET A 318 27.957 -6.621 -13.339 1.00 59.38 C ATOM 2201 CB MET A 318 28.350 -7.457 -12.122 1.00 59.35 C ATOM 2202 CG MET A 318 27.290 -8.450 -11.703 1.00 59.35 C ATOM 2203 SD MET A 318 25.852 -7.627 -11.000 1.00 59.21 S ATOM 2204 CE MET A 318 26.589 -6.840 -9.568 1.00 59.36 C ATOM 2205 C MET A 318 28.694 -5.273 -13.292 1.00 59.81 C ATOM 2206 O MET A 318 29.870 -5.198 -13.641 1.00 59.90 O ATOM 2207 N PRO A 319 28.001 -4.208 -12.835 1.00 60.27 N ATOM 2208 CA PRO A 319 28.570 -2.859 -12.719 1.00 60.66 C ATOM 2209 CB PRO A 319 27.330 -1.968 -12.653 1.00 60.60 C ATOM 2210 CG PRO A 319 26.311 -2.817 -11.979 1.00 60.41 C ATOM 2211 CD PRO A 319 26.597 -4.248 -12.386 1.00 60.27 C ATOM 2212 C PRO A 319 29.398 -2.698 -11.446 1.00 61.12 C ATOM 2213 O PRO A 319 29.036 -3.243 -10.399 1.00 61.23 O ATOM 2214 N THR A 320 30.488 -1.936 -11.537 1.00 61.63 N ATOM 2215 CA THR A 320 31.497 -1.880 -10.470 1.00 62.20 C ATOM 2216 CB THR A 320 32.620 -0.850 -10.777 1.00 62.25 C ATOM 2217 OGl THR A 320 32.176 0.476 -10.455 1.00 62.39 . O ATOM 2218 CG2 THR A 320 33.033 -0.914 -12.247 1.00 62.52 C ATOM 2219 C THR A 320 30.946 -1.611 -9.065 1.00 62.49 C ATOM 2220 O THR A 320 30.968 -2.492 -8.200 1.00 62.58 O ATOM 2221 N VAL A 321 30.451 -0.398 -8.840 1.00 62.79 N ATOM 2222 CA VAL A 321 30.129 0.029 -7.482 1.00 63.06 C ATOM 2223 CB VAL A 321 30.852 1.360 -7.122 1.00 63.09 C ATOM 2224 CGl VAL A 321 30.552 2.457 -8.196 1.00 63.09 C ATOM' 2225 CG2 VAL A 321 30.489 1.830 -5.677 1.0063.21 C ATOM 2226 C VAL A 321 28.625 0.097 -7.157 1.00 63.21 C ATOM 2227 O VAL A 321 28.177 -0.527 -6.190 1.00 63.23 O ATOM 2228 N PHE A 322 27.846 0.829 -7.953 1.00 63.40 N ATOM 2229 CA PHE A 322 26.411 0.966 -7.661 1.00 63.56 C ATOM 2230 CB PHE A 322 26.053 2.392 -7.207 1.00 63.65 C ATOM 2231 CG PHE A 322 26.791 3.475 -7.940 1.00 63.76 C ATOM 2232 CDl PHE A 322 27.629 4.341 -7.253 .1.00 63.84 C ATOM 2233 CEl PHE A 322 28.311 5.344 -7.919 1.00 64.14 C ATOM 2234 CZ PHE A 322 28.157 5.492 -9.289 1.00 64.13 C ATOM 2235 CE2 PHE A 322 27.322 4.636 -9.985 1.00 64.19 C ATOM 2236 CD2 PHE A 322 26.643 3.633 -9.311 1.00 64.04 C ATOM 2237 C PHE A 322 25.459 0.500 -8.764 1.00 63.57 C ATOM 2238 O PHE A 322 25.789 0.536 -9.951 1.00 63.52 O ATOM 2239 N GLY A 323 24.271 0.074 -8.341 1.00 63.63 N

ATOM 2240 CA GLY A 323 23.257^' -0.470 -9.238 1.00 63.75 C

ATOM 2241 C GLY A 323 23.131 -1.967 -9.042 1.00 63.84 C

ATOM 2242 O GLY A 323 22.124 -2.574 -9.402 1.00 63.82 O

• ATOM 2243 N LYS A 324 24.168 -2.547 -8.448^' 1.00 63.98 N ATOM 2244 CA LYS A 324 24.303 -3.993 -8.249 1.00 64.15 C ATOM 2245 CB LYS A 324 25.266 -4.263_. -7.084 1.00 64.21 C ATOM 2246 CG LYS A 324 25.336 -3.122 -6.060 1.00 64.51 C ATOM 2247 .CD LYS A 324 26.357 -3.392 -4.952 1.00 64.43 C ATOM 2248 CE LYS A 324 27.696 -3.883 -5.508 1.00 64.92 C ATOM 2249 NZ LYS A 324 28.280 -2.994 -6.560 1.00 64.78 N ATOM 2250 C LYS A 324 23.012 -4.807 -8.070 1.00 64.09 C ATOM 2251 O LYS A 324 22.825 -5.828 -8.735 1.00 64.04 O ATOM 2252 N GLU A 325 22.132 -4.361 -7.177 1.00 64.10 ^' N ATOM 2253 CA GLU A 325 20.961 -5.152 -6.781 1.00 64.12 C . ATOM 2254 CB GLU A 325 20.169 -4.416 -5.692 1.00 64.09 C ATOM 2255 CG GLU A 325 20.990 -4.058 -4.459 1.00 63.96 C ATOM 2256. CD GLU A 325 20.031 -4.963 -3.893 0,00 50.00 C ATOM 2257 OEl GLU A 325 20.090 -5.825 -4.783 0.00 50.00 O ATOM 2258 OE2GLUA325 19.664 -5.171 -2.727 0.0050.00 O

ATOM 2259 C i GLU A 325- 20.030 -5.549 -7.941 1.0064.19 C

ATOM 2260 O GLU A 325 19.810 -6.781 -8.214 1.0064.25 O

ATOM 2261 N ASN A 326 19.472 -4.524 -8.613 1.0064.26 N

ATOM 2262 CA ASN A 326 18.505 -4.812 -9.679 1.0064.33 C

ATOM 2263 CB ASN A 326 17.540 -3.633 -9.941 1.0064.30 C

ATOM 2264 CG ASN A 326 18.252 -2.335-10.279 1.0064.30 C

ATOM 2265 ODl ASN A 326 18.063 -1.317 -9.606 1.0064.17 O

ATOM 2266 ND2ASNA326 19.058 -2.357-11.338 1.0064.50 N

ATOM 2267 C . ASN A 326 19.181 -5.330-10.958 1.0064.35 C

ATOM 2268 O ASN A 326 18.546 -5.991-11.784 1.0064.40 O

ATOM 2269 N LYS A 327 20.472 -5.038-11.104 1.0064.30 N

ATOM 2270 CA LYS A 327 21.244 -5.569-12.219 1.0064.23 C

ATOM 2271 CB LYS A 327 22.638 -4.943-12.281 1.0064.22 C

ATOM 2272 CG LYS A 327 23.130 -4.643-13.699 1.0064.25 C

ATOM 2273 CD LYS A 327 22.954 -5.831-14.639 1.0064.27 C

ATOM 2274 CE LYS A 327 23.113 -5.426-16.099 1.0064.19 C

ATOM 2275 NZ LYS A 327 24.510 -5.015-16.421 1.0064.30 N

ATOM 2276 C LYS A 327 21.355 -7.072-12.042 1.0064.18 C

ATOM 2277 O LYS A 327 21.258 -7.825-13.004 1.0064.23 O

ATOM 2278 N LYS A 328 21.551 -7.503-10.801 1.0064.17 N

ATOM 2279 CA LYS A 328 21.573 -8.924 -10.490 1.0064.23 C

ATOM 2280 CB LYS A 328 22.005 -9.156 -9.040 1.0064.21 C

ATOM 2281 CG LYS A 328 21.992-10.616 -8.620 1.0064.08 C

ATOM 2282 CD LYS A 328 22.061-10.764 -7.110 1.0064.01 C

ATOM 2283 CE LYS A 328 21.635-12.160 -6.682 1.0063.97 C

ATOM 2284 NZ LYS A 328 21.527 -12.286 -5.204 1.0063.96 N

ATOM 2285 C LYS A 328 20.197 -9.536-10.744 1.0064.29 C

ATOM 2286 O LYS A 328 20.069-10.507-11.517 1.0064.33 O

ATOM 2287 N LYS A 329 19.165 -8.960-10.111 1.0064.32 N

ATOM 2288 CA LYS A 329 17.813 -9.511-10.273 1.0064.39 C

ATOM 2289 CB LYS A 329 16.788 -8.659 -9.523 1.0064.37 C

ATOM 2290 CG LYS A 329 16.688-10.172 -7.803 0.0050.00 C

ATOM 2291 CD LYS A 329 15.993 -9.545 -6.623 0.0050.00 C

ATOM 2292 CE LYS A 329 15.083-10.565 -5.937 0.0050.00 C .

ATOM 2293 NZ LYS A 329 14.752-10.177 -4.545 0.0050.00 N

ATOM _.2294 C LYS A 329 17.434 -9.631-11.757 1.0064.44 C

ATOM 2295 O LYS A 329 16.935-10.671-12.218 1.0064.52 O

ATOM 2296 N. GLN A 330 17.689 -8.557-12.498 1.0064.44 N

ATOM 2297 CA GLN A 330 17.458 -8.520-13.936 1.0064.45 C

ATOM 2298 CB GLN A 330 17.758 -7.118-14.473 1.0064.44 C

ATOM 2299 CG GLN A 330 17.843 -7.007-15.986 1.0064.39 C

ATOM 2300 CD GLN A 330 18.221 -5.608-16.440 1.0064.40 C

ATOM 2301 OEl GLN A 330 .17.777 -4.614-15.862 1.0064.30 O

ATOM 2302 NE2GLNA330 19.046 -5.524-17.479 1.0064.34 N

ATOM 2303 C GLN A 330 18.305 -9.565-14.658 1.0064.45 C

ATOM 2304 O GLN A 330 17.813 -10.287 -15.529 1.0064.60 O

ATOM 2305 N LEU A 331 19.579 -9.647-14.281 1.0064.39 N

ATOM 2306 CA LEU A 331 20.495-10.615-14.874 1.0064.37 C

ATOM 2307 CB LEU A 331 21.902-10.488-14.284 1.0064.32 C

ATOM 2308 CG LEU A 331 22.855 -9.519-14.986 1.0064.30 C

ATOM 2309 CDl LEU A 331 24.178 -9.421-14.242 1.006435 C

ATOM 2310 CD2LEUA331 23.081 -9.930-16.430 1.0064.38 C

ATOM 2311 C LEU A 331 19.983-12.039-14.718 1.0064.41 C

ATOM 2312 O LEU A 331 20.171-12.868-15.610 1.0064.39 O

ATOM 2313 ^•N ILE A 332 19.335-12.331-13.593 1.0064.44 N

ATOM 2314 CA . ILE A 332 18.744-13.660-13.438 1.0064.56 C

ATOM 2315 CB ILE A 332 18.734-14.168-11.978 1.0064.53 C ATOM 2316 CGl ILE A 332 18.252-13.081-11.022 1.0064.67 C

ATOM 2317 CDl ILE A 332 18.518-13.404 -9.570 1.0064.93 C

ATOM 2318 CG2ILEA332 20.122-14.638-11.573 1.0064.59 C

ATOM 2319 C ILE A 332 17.361-13.779-14.076 1.0064.64 C ATOM 2320 O ILE A 332 16.916-14.885-14.381 1.0064.71 O

ATOM 2321 N LEU A 333 16.681-12.653-14.286 1.0064.69 N

ATOM 2322 CA LEU A 333 15.474-12.679-15.120 1.0064.86 C

ATOM 2323 CB LEUA333 14.733-11.340-15.070 1.0064.84 C ATOM 2324 CG LEU A 333 13.377-11.329-14.357 1.0064.83 C ATOM 2325 CD1LEUA333 13.505-11.795-12.912 1.0064.93 C

ATOM 2326 CD2LEUA333 12.750 -9.944-14.431 1.0064.92 C

ATOM 2327 C LEU A 333 15.821-13.018-16.568 1.0064.95 C

ATOM 2328 O LEU A 333 15.066-13.699-17.265 1.0064.92 O

ATOM 2329 N LYS A 334 16.982-12.542-17.002 1.0065.06 N ATOM 2330 CA LYS A 334 17.410-12.645-18.390 1.0065.32 C

ATOM 2331 CB LYS A 334 18.037-11.303-18.801 1.0065.31 C

ATOM 2332 CG LYS A 334 18.859-11.279-20.084 1.0065.31 C

ATOM 2333 CD LYS A 334 19.751-10.026-20.101 1.0065.18 C.

ATOM 2334 CE LYS A 334 20.825-10.098-21.178 1.0064.74 C ATOM 2335 NZ LYS A 334 21.839 -9.010-21.016 1.0064.46 N

ATOM 2336 C LYS A 334 18.385-13.813-18.589 1.0065.54 C

ATOM 2337 0 LYS A 334 19.241-13.778-19.474 1.0065.57 O

ATOM 2338 N LEU A 335 18.243-14.855-17.772 1.0065.83 N

ATOM 2339 CA LEU A 335 19.176-15.984-17.815 1.0066.16 C ATOM 2340 CB LEU A 335 19.092-16.826-16.537 1.0066.09 C

ATOM 2341 CG LEU A 335 20.406-17.326-15.917 1.0066.13 C

ATOM 2342 CDl LEU A 335 20.204-18.673-15.232 1.0066.05 C

ATOM 2343 CD2LEUA335 21.536-17.420-16.931 1.0065.95 C

ATOM 2344 C LEUA335 18.990-16.877-19.044 1.0066.47 C ATOM 2345 O LEU A 335 19.964-17.217-19.710 1.0066.51 O

ATOM 2346 N PRO A 336 17.739-17.263-19.354 1.0066.81 N

ATOM 2347 CA PRO A 336 17.544-18.144-20.503 1.0067.08 C

ATOM 2348 CB PRO A 336 16.028-18.367-20.526 1.0067.05 C

ATOM 2349 CG PRO A 336. 15.458-17.221-19.762 1.0066.99 C ATOM 2350 CD PRO A 336 16.465-16.916-18.702 1.0066.85 C

ATOM 2351 C PRO A 336 18.010-17.486-21.797 1.0067.39 C

ATOM 2352 O PROA336 18.262-18.175-22.786 1.0067.44 O

ATOM 2353 N VALA337 18.123-16.162-21.781 1.0067.78 ^' N

ATOM 2354 CA VAL A 337 18.655-15.421-22.917 1.0068.20 C ATOM 2355 CB VAL A 337 18.258-13.931-22.857 1.0068.20 C

ATOM 2356 CGl VAL A 337 18.443-13.275-24.221 1.0068.26 C

ATOM 2357 CG2VALA337 16.817-13.779-22.384 1.0068.27 C

ATOM 2358 C VAL A 337 20.177-15.540-22.917 1.0068.46 C

ATOM 2359 O VAL A 337 20.796-15.754-23.964 1.0068.80 O. ATOM 2360 N ILE A 338 20.769-15.408-21.733 1.0068.70 N

ATOM 2361 CA ILE A 338 22.210-15.578-21.561 1.0068.88 C

ATOM 2362 CB ILE A 338 22.627-15.468-20.077 1.0068.80 C

ATOM 2363 CGl ILE A 338 22.408-14.045-19.557 1.0068.70 C

ATOM 2364 CDl ILE A 338 23.413-13.035-20.078 1.0068.75 C ATOM 2365 CG2ILEA338 24.082-15.865-19.900 1.0068.67 C

ATOM 2366 C ILEA338 22.661-16.929-22.114 1.0069.11 C

ATOM 2367 O ILE A 338 23.575-16.995-22.939 1.0069.27 O

ATOM 2368 N PHE A 339 22.007-17.999-21.664 1.0069.30 N

ATOM 2369 CA PHE A 339 22.327-19.346-22.133 1.0069.45 C ATOM 2370 CB PHE A 339 21.395-20.390-21.503 1.0069.45 C

ATOM 2371 CG PHE A 339 21.613-20.598-20.024 1.0069.55 . C

ATOM 2372 CDl PHE A 339 22.744-20.104-19.391 1.0069.69 C

ATOM 2373 CEl PHE A 339 22.944-20.304-18.035 1.0069.63 C ATOM 2374 CZ PHE A 339 22.019-21.017-17.299 1.0069.58 C

ATOM 2375 CE2PHEA339 20.893-21.524-17.919 1.0069.60 C

ATOM 2376 CD2PHEA339 20.695-21.318-19.273 1.0069.56 C

ATOM 2377 C PHE A 339 22.248-19.427-23.656 1.0069.52 C ATOM 2378 O PHE A 339 23.170-19.923-24.314 1.0069.66 O

ATOM 2379 N ALAA340 21.146-18.926-24.208 1.0069.56 N

ATOM 2380 CA ALA A 340 20.949-18.908-25.653 1.0069.59 C

ATOM 2381 CB ALAA340 19.633-18.214-26.000 1.0069.61 C

ATOM 2382 C ALAA340 22.119-18.218-26.351 1.0069.61 C ATOM 2383 O ALAA340 22.683-18.750-27.319 1.0069.74 -O

ATOM 2384 N LYS A 341 22.486-17.035-25.848 1.0069.49 N

ATOM 2385 CA LYS A 341 23.574-16.263-26.446 1.0069.65 C

ATOM 2386 CB LYS A 341 23.660-14.861-25.828 1.0069.67 C

ATOM .2387 CG LYS A 341 22.479-13.952-26.189 1.0069.92 C ATOM 2388 CD LYS A 341 22.774-12.477-25.902 1.0069.78 C

ATOM 2389 CE LYS A 341 21.518-11.612-26.045 1.0069.77 C

ATOM 2390 NZ LYS A 341 20.889-11.703-27.400 1.0069.59 N ATOM 2391 C LYS A 341 24.914-16.993-26.352 1.0069.57 C

ATOM 2392 O LYS A 341 25.626-17.142-27.354 1.0069.70 O ATOM 2393 N ILEA 342 25.248-17.463-25.152 1.0069.50 N

ATOM 2394 CA ILE A 342 26.494-18.200-24.950 1.0069.48 C

ATOM 2395 CB ILE A 342 26.709-18.597-23.478 1.0069.39 C

ATOM 2396 CGl ILE A 342 26.707-17.354-22.587 1.0069.17 C

ATOM 2397 CDl ILE A 342 27.110-17.626-21.159 1.0068.85 C . ATOM 2398 CG2ILEA342 28.024-19.337-23.320 1.0069.32 C

ATOM 2399 C ILE A 342 26.565-19.437-25.846 1.0069.61 C

ATOM 2400 O ILE A 342 27.632-19.764-26.364 1.0069.60 O

ATOM 2401 N GLN A 343 25.436-20.123-26.027 1.0069.77 N

ATOM 2402 CA GLN A 343 25.359-21.194-27.031 1.0069.99 C ATOM 2403 CB GLN A 343 23.974-21.856-27.044 1.0069.96 C

ATOM 2404 CG GLN A 343 23.772-22.873-25.937 1.0070.15 ^• C,

ATOM 2405 CD GLN A 343 22.383-23.483-25.957 1.0070.33 C

ATOM 2406 OEl GLN A 343 21.783-23:669-27.044 1.0071.09 O

ATOM 2407 NE2 GLN A 343 21.876-23.816-24.732 1.0070.53 N ATOM 2408 C GLN A 343 25.669-20.640-28.416 1.0070.01 C

ATOM 2409 O GLNA343 26.512-21.177-29.138 1.0070.02 O

ATOM 2410 N LEU A 344 24.977-19.562-28.778 1.0070.01 N

ATOM.2411 CA LEU A 344 25.165-18.934-30.082 1.0070.13 C

ATOM 2412 CB LEUA344 24.382-17.615-30.176 1.0070.20 C ATOM 2413 CG LEU A 344 22.866-17.683-30.411 1.0070.29 C

ATOM 2414 CDl LEU A 344 22.234-16.303-30.260 1.0070.28 C

ATOM 2415 CD2 LEU A 344 22.543-18.278-31.778 1.0070.32 C

ATOM 2416 C LEUA344 26.640-18.682-30.384 1.0070.13 C

ATOM 2417 O LEUA344 27.154.-19.142-31.405 1.0070.23 O ATOM 2418 N GLU A 345 27323-17.959-29.496 1.0070.00 N

ATOM 2419 CA GLU A 345 28.670-17.481-29.815 1.0070.11 C

ATOM 2420 CB GLU A 345 28.849-16.036-29.341 1.0070.11 C

ATOM 2421 CG GLU A 345 28.436-15.805-27.898 1.0070.34 C

ATOM 2422 CD GLU A 345 28.662-14.378-27.452 1.0070.34 C ATOM 2423 OEl GLU A 345 29.828-14.018-27.182 1.0070.78 O

ATOM 2424 OE2 GLU A 345 27.672-13.618-27.364 1.0070.66 O

ATOM 2425 C GLU A 345 29.830-18.345-29.313 1.0070.06 C

ATOM 2426 O GLU A 345 30.985-17.922-29.375 1.0070.05 O

ATOM 2427 N HIS A 346 29.537-19.545-28.823 1.0070.09 N ATOM 2428 CA HIS A 346 30.597-20.438-28.341 1.0070.11 C

ATOM 2429 CB HIS A 346 30.676-20.431-26.811 1.0070.05 C

ATOM 2430 CG HIS A 346 31.545-19.349-26.253 1.0069.94 C

ATOM 243.1 NDl HIS A 346 32.919-19.371.-26.358 1.0069.85 N ATOM 2432 CEl HIS A 346 33.419-18.296-25.775 1.0070.02 C ATOM 2433 NE2HISA346 32.419-17.581-25.289 1.0069.91 N ATOM 2434 CD2HISA346 31.236-18.218-25.574 1.0070.00 C ATOM 2435 C HIS A 346 30.444-21.869-28.841 1.0070.14 C ATOM 2436 O HIS A 346 31.236-22.744-28.486 1.0070.16 O ATOM 2437 N HIS A 347 29.425-22.099-29.661 1.0070.14 N ATOM 2438 CA HIS A 347 29.158-23.422-30.208 1.0070.21 C ATOM 2439 CB HIS A 347 30.145-23.753-31.329 1.0070.15 C ATOM 2440 CG HIS A 347 30.172-22.738-32.427 1.0070.25 C ATOM ^' 2441 NDl HIS A 347 31.071-21.693-32.451 1.0070.27 N ATOM 2442 CEl HIS A 347 30.861-20.961-33.532 1.0070.36 C ATOM 2443 NE2HISA347 29.859-21.494-34.208 1.0070.39 N ATOM 2444 CD2HISA347 29.409-22.606-33.538 1.0070.34 C ATOM 2445 C HIS A 347 29.219-24.505-29.138 1.0070.23 C ATOM 2446 O HIS A 347 30.208-25.230-29.032 1.0070.29 O ATOM 2447 N ILE A 348 28.165-24.603-28.336 1.0070.25 N ATOM 2448 CA ILE A 348 28.014-25.743-27.441 1.0070.37 C ATOM 2449 CB ILE A 348 28.329-25.401-25.961 1.0070.40 C ATOM 2450 CGl ILE A 348 27.603 -24.131 -25.524 1.0070.55 C ATOM 2451 CDl ILE A 348 28.426-22.879-25.700 1.0070.97 C ATOM 2452 CG2ILEA348 . 29.829-25.226-25.759 1.0070.45 " C ATOM 2453 C. ILE A 348 26.614-26.336-27.566 1.0070.38 C ATOM 2454 O ILE A 348 25.644-25.618-27.818 1.0070.43 O ATOM 2455 N SER A 349 26.523-27.653-27.407 1.0070.37 N ATOM 2456 CA SER A 349 25.248-28.352-27.479 1.0070.38 C ATOM 2457 CB SER A 349 25.471-29.867-27.539 1.0070.40 C ATOM 2458 OG SER A 349 24.237-30.566-27.596 1.0070.52 O ATOM 2459 C SER A 349 24.382-28.006-26.275 1.0070.34 C ATOM 2460 O SER A 349 24.880-27.934-25.149 1.0070.27 O ATOM 2461 N PRO A 350 23.078-27.779-26.511 1.0070.29 N ATOM 2462 CA PRO A 350 22.123-27.530-25.431 1.0070.22 C ATOM 2463 CB PRO A 350 20.777-27.495-26.160 1.0070.23 C ATOM 2464 CG PRO A 350 21.122-27.067-27.546 1.0070.27 C ATOM 2465 CD PRO A 350 22.439-27.722-27.837 1.0070.21 C ATOM 2466 C PRO A 350 22.130-28.634-24.364 1.0070.13 C ATOM 2467 O . PRO A 350 21.642-28.421-23.253 1.0070.22 O ATOM 2468 N GLY A 351 22.689-29.795-24.695 1.0069.88 N ATOM 2469 CA GLY A 351 22.773-30.899-23.746 1.0069.54 C ATOM 2470 C GLY A 351 23.820-30.680-22.669 1.0069.38 C ATOM 2471 O GLY A 351 24.040-31.547-21.818 1.0069.41 O ATOM 2472 N ASP A 352 24.468-29.516-22.700 1.0069.15 N ATOM 2473 CA ASP A 352 25.539-29.207-21.755 1.0068.90 C ATOM 2474 CB ASP A 352 26.748-28.614-22.482 1.0068.94 C ATOM 2475 CG ASP A 352 27.470-29.629-23.340 1.0069.10 C ATOM 2476 ODl ASP A 352 28.721-29.587-23.386 1.0069.17 O ATOM 2477 OD2ASPA352 26.788-30.470-23.969 1.0069.78 O ATOM 2478 C ASP A 352 25.097-28.251-20.653 1.0068.71 C ATOM 2479 O ASP A 352 25.743-28.157-19.610 1.0068.69 O ATOM 2480 N PHE A 353 24.000-27.541-20.890 1.0068.50 N ATOM 2481 CA PHE A 353 23.536-26.519-19.955 1.0068.34 C ATOM 2482 CB PHE A 353 22.700-25.470-20.683 1.0068.32 C ATOM 2483 CG PHE A 353 23.518-24.413-21.348 1.0068.40 C ATOM 2484 CDl PHE A 353 23.773-23.213-20.704 1.0068.54 C ATOM 2485 CEl PHE A 353 24.534 -22.233 --21.312 1.0068.49 C ATOM 2486 CZ PHE A_.353 25.053-22.448-22.571 1.0068.51 . C ATOM 2487 CE2PHEA353 24.811-23.646-23.220 1.0068.68 C ATOM 2488 CD2PHEA353 24.049-24.620-22.608 1.0068.56 C ATOM 2489 C PHE A 353 22.761-27.066-18.763 1.0068.21 C ATOM 2490 O PHE A 353 21.997-28.021-18.896 1.0068.28 O ATOM 2491 N PRO A 354 22.949-26.445-17.589 1.0068.04 N ATOM 2492 CA PRO A 354 22.224-26.839-16.385 1.0067.82 C ATOM 2493 CB PRO A 354 22.931-26.057-15.267 1.0067.87 C ATOM 2494 CG PRO A 354 24.145-25.426-15.899 1.0067.91 C ATOM 2495 CD PRO A 354 23.859-25.313-17.348 1.0067.93 C ATOM 2496 C PRO A 354 20.773-26.392-16.476 1.0067.54 C ATOM 2497 O PRO A 354 20.406-25.682-17.412 1.0067.44 O ATOM 2498 N ASP A 355 19.956-26.806-15.512 1.0067.25 N ATOM 2499 CA ASP A 355 18.591-26.307-15.419 1.0066.95 C ATOM 2500 CB ASP A 355 17.806-27.057-14.341 1.0066.98 C ATOM 2501 CG ASP A 355 16.373-26.569-14.216 1.0067.19 C ATOM 2502 ODl ASP A 355 15.459-27.421-14.187 1.0067.62 O ATOM 2503 OD2ASPA355 16.155-25.338-14.148 1.0067.10 O ATOM 2504 C ASP A 355 18.627-24.813-15.111 1.0066.67 C ATOM 2505 O ASP A 355 19.260-24.383-14.144 1.0066.78 O ATOM 2506 N CYS A 356 17.945-24.029-15.940 1.0066.16 ^' N ATOM 2507 CA CYS A 356 17.977-22.576-15.834 1.0065.72 C ATOM 2508 CB CYS A 356 17.156-21.950-16.964 1.0065.76 C ATOM 2509 SG CYS A 356 17.529-20.216-17.290 1.0065.98 S ATOM 2510 C CYS A 356 17.470-22.090-14.478 1.0065.43 C ATOM 2511 O CYS A 356 18.068-21.203-13.864 1.0064.92 . O ATOM 2512 N GLN A 357 16.378-22.689-14.010 1.0065.25 N ATOM 2513 CA GLN A 357 15.719-22.247-12.780 1.0065.06 C ATOM 2514 CB GLN A 357 14.262-22.723-12.746 1.0065.11 C ATOM 2515 CG GLNA357 13.336-21.874-13.615 1.0065.39 C ATOM 2516 CD GLN A 357 12.050-22.588-13.988 1.0065.96 C ATOM 2517 OEl GLN A 357 11.004-21.939-14.178 1.0066.00 O ATOM 2518 NE2 GLN A 357 12.123-23.933-14.100 LOO 66.01 N ATOM 2519 C GLN A 357 16.466-22.615-11.492 1.0064.82 C ATOM 2520 O GLN A 357 16.503-21.825-10.541 1.0064.50 O ATOM 2521 N LYS A 358 17.061-23.805-11.458 1.0064.56 N ATOM 2522. CA LYS A 358 17.898-24.192-10.327 1.0064.41 C ATOM |523 CB LYS A 358 18.410-25.623-10.501 1.0064.55 C ATOM 2524 CG LYS A 358 19.047-26.218 -9.249 1.0065.05 C ATOM 2525 CD LYS A 358 18.000-26.546 -8.187 1.0065.74 C ATOM 2526 CE LYS A 358 18.640-27.141 -6.936 1.0066.04 C ATOM 2527 NZ LYS A 358 / 17.621-27.613 -5.948 1.0066.17 N ATOM 2528 C LYS A 358 19.067-23.215-10.243 1.0064.12 C ATOM 2529 O LYS A 358 19.329-22.600 -9.193 1.0063.78 O ATOM 2530 N MET A 359 19.752-23.074-11.374 1.0063.91 N ATOM 2531 CA MET A 359 20.818-22.101-11.531 1.0063.82 C ATOM 2532 CB MET A 359 21.298-22.083-12.984 1.0063.91 C ATOM 2533 CG MET A 359 22.634-21.389-13.214 1.0064.20 C ATOM 2534 SD MET A 359 24.047-22.269-12.508 1.0065.02 S ATOM 2535 CE MET A 359 25.409-21.348-13.220 1.0064.30 C ATOM 2536 C MET A 359 20.322-20.719-11,117 1.0063.69 C ATOM 2537 O MET A 359 21.086-19.907-10.602 1.0063.41 O ATOM 2538 N GLN A 360 19.037-20.459-11.328 1.0063.78 N ATOM 2539 CA GLN A 360 18.454-19.186-10.916 1.0063.51 C ATOM 2540 CB GLN A 360 17.126-18.937-11.632 1.0063.59 C ATOM 2541 CG GLN A 360 17.299-18.365-13.029 1.0063.62 C ATOM 2542 CD GLN A 360 16.031-18.412-13.856 1.0063.50 C ATOM 2543 OEl GLN A 360 15.815-17.566-14.722 1.0063.52 O ATOM 2544 NE2 GLN A 360 15.187 -19.403 -13.595 1.0063.46 N ATOM 2545 C GLN A 360 18.297-19.059 -9:399 1.0063.40 C ATOM 2546 O GLN A 360 18.546-17.991 -8.834 1.0063.16 O ATOM 2547 N GLU A 361 17.895-20.144 -8.741 1.0063.45 N ATOM 2548 CA GLU A 361 17.802-20.151 -7.279 1.0063.14 C ATOM 2549 CB GLU A 361 17.142-21.442 -6.790 1.0063.14 C ATOM 2550 CG GLU A 361 15.901 -22.350 -6.363 0.0050.00 C ATOM 2551 CD GLU A 361 15.696 -23.530 -5.435 0.0050.00 C ATOM 2552 OEl GLU A 361 16.150-24.642 -5.776 0.0050.00 O ATOM 2553 OE2GLUA361 15.081-23.346 -4.363 0.0050.00 O ATOM 2554 C GLU A 361 19.184-19.978 -6.637 1.0063.01 C ATOM 2555 O GLU A 361 19.382-19.152 -5.715 1.0062.82 O ATOM 2556 N LEU A 362 20.148-20.751 -7.138 1.0062.93 N ATOM 2557 CA LEU A 362 21.511-20.662 -6.617 1.0062.55 C ATOM 2558 CB LEU A 362 22.361 -21.809 -7.164 1.0062.51 C ATOM 2559 CG LEU A 362 21.784-23.205 -6.916 1.0062.22 C ATOM 2560 CDl LEU A 362 22.741 -24.272 -7.416 1.0061.94 C ATOM 2561 CD2LEUA362 21.471 -23.409 -5.440 1.0061.87 C ATOM 2562 C LEU A 362 22.154-19.299 -6.921 1.0062.44 C ATOM _.2563 O LEU A 362 22.811-18.678 -6.052 1.0062.11 O ATOM 2564 N LEU A 363 21.960-18.832 -8.156 1.0062.56 N . ATOM 2565 CA LEU A 363 22.412-17.501 -8.530 1.0062.37 C ATOM 2566 CB LEU A 363 22.080-17.199 -9.993 1.0062.32 C ATOM 2567 CG LEU A 363 23.212-17.346-11.013 1.0062.11 C ATOM 2568 CDl LEU A 363 24.325-16.381-10.684 1.0062.15 C ATOM 2569 CD2LEUA363 23.753-18.759-11.056 1.0061.97 C ATOM 2570 C LEU A 363 21.759-16.483 -7.609 1.0062.38 C ATOM 2571 O LEU A 363 22.362-15.468 -7.261 1.0062.29 O ATOM 2572 N MET A 364 20.521-16.770 -7.213 1.0062.56 N

ATOM 2573 CA MET A 364 19.821-15.949 -6.229 1.0062.46 C

ATOM 2574 CB MET A 364 18.376-16.436 -6.047 1.0062.50 C

ATOM 2575 CG MET A 364 17.449-15.444 -5.357 1.0062.64 C

■ ATOM 2576 SD MET A 364 17.255-13.900 -6.279 1.0063.45 S ATOM 2577 CE MET A 364 15.974-13.066 -5.331 1.0063.02 C ATOM 2578 C MET A 364 20.576-16.000 -4.903 1.0062.32 C ATOM 2579 O MET A 364 20.579-15.030 -4.142 1.0062.24 O ATOM 2580 N ALA A 365 21.227-17.132 .4.638 1.0062.25 N ATOM 2581 CA ALA A 365 22.014-17.277 -3.401 1.0061.89 C ATOM 2582 CB ALA A 365 22.130-18.749 -3.012 1.0061.88 C ATOM 2583 C ALA A 365 23.406-16.615 -3.399 1.0061.73 C ATOM 2584 O ALA A 365 23.901-16.219 -2.344 1.0061.65 O ATOM 2585 N HIS A 366 24.039-16.491 -4.565 1.0061.58 N ATOM 2586 CA HIS A 366 25.428-15.979 -4.623 1.0061.07 C ATOM 2587 CB HIS A 366 26.178-16.621 -5.786 1.0061.07 C ATOM 2588 CG HIS A 366 26.701 -17.983 -5.478 1.0060.77 C ATOM 2589 NDl HIS A 366 25.881-19.026 -5.107 1.0060.88 N ATOM 2590 CEl HIS A 366 26.613-20.104 -4.894 1.0061.03 C ATOM 2591 NE2HISA366 27.879-19.796 -5.114 1.0061.08 N ATOM 2592 CD2HISA366 27.961 -18.475 -5.481 1.0060.66 C ATOM 2593 C HIS A 366 25.606-14.462 -4.714 1.0060.91 C ATOM 2594 O HIS A 366 24.659-13.732 -4.999 1.0060.95 O ATOM 2595 N ASP A 367 26.837-14.001 -4.476 1.0060.67 N ATOM 2596 CA ASP A 367 27.209-12.600 -4.702 1.0060.54 C ATOM 2597 CB ASP A 367 28.089-12.052 -3.576 1.0060.59 C ATOM 2598 CG ASP A 367 28.551 -10.615 -3.839 1.0060.69 C ATOM 2599 ODl ASP A 367 29.141 -9.993 -2.927 1.0060.49 O ATOM 2600 OD2ASPA367 28.324-10.103 -4.958 1.0060.90 O ATOM 2601 C ASP A 367 27.947-12.442 -6.020 1.0060.51 C ATOM 2602 O ASP A 367 28.946-13.117 -6.273 1.0060.68 O ATOM 2603 N PHE A 368 27.468-11.519 -6.845 1.0060.30 N ATOM 2604 CA PHE A 368 27.980-11.376 -8.194 1.0060.01 C ATOM 2605 CB PHE A 368 26.956-10.666 -9.076 1.0060.10 C ATOM 2606 CG PHEA368 25.846-11.562 -9.547 1.0060.32 C

ATOM 2607 CDl PHE A 368 25.315-12.532 -8.707 1.0060.54 C

ATOM 2608 CEl PHE A 368 24.295-13.358 -9.133 1.0060.45 C

ATOM 2609 CZ PHE A 368 23.784-13.217-10.408 1.0060.53 C ATOM 2610 CE2 PHE A 368 24.299-12.251-11.256 1.0060.66 C

ATOM.2611 CD2PHEA368 25.323-11.430-10.823 1.0060.62 C

ATOM 2612 C PHE A 368 29.324-10.673 -8.238 1.0059.80 C

ATOM 2613 O PHE A 368 30.204-11.067 -8.998 1.0059.86 O

ATOM 2614 N THR A 369 29.486 -9.641 -7.417 1.0059.53 N ATOM 2615 CA THR A 369 30.717 -8.854 -7.432 1.0059.25 C

ATOM 2616 CB THR A 369 30.613 -7.593 -6.543 1.0059.18 C

ATOM 2617 OGl THR A 369 30.494 -7.974 -5.167 1.0059.25 O

ATOM 2618 CG2THRA369 29.407 -6.761 -6.943 1.0059.10 C

ATOM 2619 C THR A 369 31.927 -9.691 -7.025 1.0059.10 C ATOM 2620 O THRA369 33:068 -9.311 -7.280 1.0058.97 O

ATOM 2621 N LYS A 370 31.670-10.840 -6.407 1.0059.01 N

ATOM 2622 CA LYS A 370 32.740-11.725 -5.960 1.0058.97 C

ATOM 2623 CB LYS A 370 32.318-12.482 -4.699 1.0059.01 C

ATOM 2624 CG LYS A 370 31.859-11.596 -3.550 1.0059.07 C ATOM 2625 CD LYSA370 33.008-11.175 -2.649 1.0059.12 C

ATOM 2626 CE LYS A 370 32.490-10.481 -1.392 LOO 59.61 C

ATOM 2627 NZ LYS A 370 31.488-11.309 -0.638 1.0059.98 N

ATOM 2628 C LYS A 370 33.152-12.715 -7.047 1.0058.95 C

ATOM 2629 0 LYS A 370 34.235-13.292 -6.982 1.0058.95 O ATOM 2630 N PHE A 371 32.285-12.914 -8.039 1.0058.98 N

ATOM 2631 CA PHE A 371 32.595-13.790 -9.170 1.0059.03 C

ATOM 2632 CB PHE A 371 31.474-13.759-10.214 1.0058.86 C

ATOM 2633 CG PHE A 371 30.216-14.459 -9.785 1.0058.79 C

ATOM 2634 CDl PHE A 371 28.979-14.003-10.210 1.0058.52 C ATOM 2635 CEl PHE A 371 27.818-14.644 -9.823 1.0058.30 C

ATOM 2636 CZ PHE A 371 27.883-15.752 -9.000 1.0058.32 C

ATOM 2637 CE2PHEA371 29.106-16.218 -8.569 1.0058.37 C

ATOM 2638 CD2PHEA371 30.266-15.574 -8.961 1.0058.75 C

ATOM 2639 C PHE A 371 33.902-13.386 -9.840 1.0059.21 C ATOM 2640 O PHE A 371 34.291-12.223 -9.804 1.0059.25^" O

ATOM 2641 N HIS A 372 34.579-14.346-10.456 1.0059.50 N

ATOM 2642 CA HIS A 372 35.789-14.040-11.206 1.0059.80 C

ATOM 2643 CB HIS A 372 36.798-15.180-11.093 1.0059.85 c^'

ATOM 2644 CG HIS A 372 37.463 -15.261- -9.756 1.0059.95 C ATOM 2645 NDl HIS A 372 38.399-14.342 -9.335 1.0059.92 N

ATOM 2646 CEl HIS A 372 38.814-14.663 -8.123 1.0060.28 C

ATOM 2647 NE2 HIS A 372 38.178-15.756 -7.741 1.0060.47 N

ATOM 2648 CD2HISA372 37.327-16.150 -8.744 1.0060.21 C

ATOM 2649 C HIS A 372 35.468-13.754-12.668 1.0059.98 C ATOM 2650 O HIS A 372 34.385-14.092-13.149 1.0060.08 O

ATOM 2651 N SER A 373 36.413-13.130-13.370 1.0060.16 N

ATOM 2652 CA SER A 373 36.231-12.788-14.783 1.0060.24 ^: C

ATOM 2653 CB SERA373 37.012-11.521-15.135 1.0060.28 C

ATOM 2654 OG SER A 373 36.688-10.461-14.252 1.0060.74 O ATOM 2655 C SER A 373 36.664-13.918-15.705 1.0060.17 C

ATOM 2656 O SER A 373 37.354-14.847-15.291 1.0060.00 O

ATOM 2657 N LEU A 374 36.259-13.828-16.964 1.0060.35 N

ATOM 2658 CA LEU A 374 36.661-14.813-17.955 1.0060.62 C

ATOM 2659 CB LEU A 374 36.125-14.424-19.333 1.0060.56 C ATOM 2660 CG LEU A 374 36.072-15.531-20.384 1.0060.72 C

ATOM 2661 CD1LEUA374 34.981-15.247-21.409 1.0061.21 C

ATOM 2662 CD2 LEU A 374 37.420-15.707-21.060 1.0060.74 C

ATOM 2663 C LEU A 374 38.184-14.936-17.972 1.0060.76 C ATOM 2664 O LEU A 374 38.894-13.933-17.917 1.0060.93 O

ATOM 2665 N LYS A 375 38.682-16.167-18.030 1.0060.82 N

ATOM 2666 CA LYS A 375 40.120-16.420-18.015 1.0060.84 C

ATOM 2667 CB LYS A 375 40.535-17.002-16.664 1.0060.91 C

ATOM 2668 CG LYS A 375 40.369-16.044-15.498 1.0061.48 C

ATOM 2669 CD LYS A 375 41.697-15.434-15.084 1.0062.71 C

ATOM 2670 CE LYS A 375 42.553-16.457-14.337 1.0063.51 C

ATOM 2671 NZ LYS A 375 43.854-15.899-13.868 1.0063.82 N

ATOM 2672 C LYS A 375 40.491-17.381-19.138 1.0060.68 C

ATOM 2673 O LYS A 375 40.479-18.595-18.946 1.0060.73 O

ATOM 2674 N PRO A 376 40.838-16.837-20.313 1.0060.57 N

ATOM 2675 CA PRO A 376 41.018-17.632-21.526 1.0060.57 C

ATOM 2676 CB PRO A 376 41.521-16.607-22.545 1.0060.60 C

ATOM 2677 CG PRO A 376 41.046-15.295-22.034 1.0060.61 C

ATOM 2678 CD PRO A 376 41.097-15.407-20.544 1.0060.55 C

ATOM 2679 C PRO A 376 42.042-18.746-21.353 1.0060.59 C

ATOM 2680 O PRO A 376 41.907-19.809-21.956 1.0060.69 O

ATOM 2681 N LYS A 377 43.050-18.495-20.525 1.0060.59 N

ATOM 2682 CA LYS A 377 44.131-19.446-20.285 1.0060.71 C

ATOM 2683 CB LYS A 377 45.129-18.839-19.295 1.0060.74 C

ATOM 2684 CG LYS A 377 44.517-17.771-18.384 1.0061.05 C

ATOM 2685 CD LYS A 377 45.457-17.378-17.246 1.0061.19 C

ATOM 2686 CE LYS A 377 45.573-18.489-16.201 1.0061.82 C

ATOM 2687 NZ LYS A 377 46.528-18.146-15.102 1.0062.06 N

ATOM 2688 C LYS A 377 43.654-20.821-19.798 1.0060.59 C

ATOM 2689 O LYS A 377 43.932-21.849-20.429 1.0060.69 O

ATOM 2690 N LEU A 378 42.935-20.834-18.678 1.0060.51 N

ATOM 2691 CA LEU A 378 42.450-22.076-18.077 1.0060.41 C

ATOM 2692 CB LEUA 378 4^'1.743 -21.783 -16.757 1.0060.35 C

ATOM 2693 CG LEU A 378 42.521-20.939-15.743 1.0060.12 C

ATOM 2694 CDl LEU A 378 41.617-20.552-14.588 1.0059.86 C

ATOM 2695 CD2LEUA378 43.767-21.663-15.242 1.0059.70 C

ATOM 2696 C LEU A 378 41.507-22.807-19.022 1.0060.42 C

ATOM 2697 O LEU A 378 41.628-24.019-19.238 1.0060.64 O

ATOM 2698 N LEU A 379 40.564-22.056-19.578 1.0060.36 N

ATOM 2699 CA LEU A 379 39.686-22.568-20.617 1.0060.34 C

ATOM 2700 CB LEU A 379 38.868-21.425-21:214 1.0060.18 C

ATOM 2701 CG LEU A 379 37.657-21.020-20.372 1.0059.81 C

ATOM 2702 CDl LEU A 379 37.524-19.515-20.250 1.0059.39 C

ATOM 2703 CD2LEUA379 36.394-21.632-20.952 1.0059.83 C

ATOM 2704 C LEU A 379 40.493-23.284-21.695 1.0060.50 C

ATOM 2705 O LEU A 379 40.278-24.470-21.961 1.0060.81 O

ATOM 2706 • N GLU A 380 41.432-22.567-22.304 1.0060.65 N

ATOM 2707 CA GLU A 380 42.308-23.167-23.303 1.0060.83 C

ATOM 2708 CB GLU A 380 43.438-22.214-23.691 1.0060.85 C

ATOM 2709 CG GLU A 380 43.118-21.304-24.858 1.0060.88 C

ATOM 2710 CD GLU A 380 44.355-20.937-25.648 1.0061.03 C

ATOM 2711 OEl GLU A 380 44.281-20.931-26.892 1.0061.38 O

ATOM 2712 OE2GLUA380 45.407-20.673-25.029 1.0061.20 O

ATOM 2713 C GLU A 380 42.896-24.470-22.786 1.0060.92 C

ATOM 2714 O GLU A 380 42.872-25.499-23.481 1.0061.26 O

ATOM 2715 N ALA A 381 43.424-24.420-21.564 1.0060.89 N

ATOM 2716 CA . ALA A 381 43.984.-25.606 -20.931 1.0061.02 C

ATOM 2717 CB ALA A 381 44.320-25.322-19.480 1.0060.97 C

ATOM 2718 C ALA A 381 42.991-26.754-21.036 1.0061.14 C

ATOM 2719 O ALA A 381 43.344-27.872-21.425 1.0061.43 O

ATOM 2720 N LEU A 382 41.741-26.460-20.701 1.0061.13 N

ATOM 2721 CA . LEU A 382 40.666-27.438-20.800 1.0061.34 C ATOM 2722 CB^' LEU A 382 39.365-26.808-20.291 1.0061.35 C ATOM 2723 CG LEU A 382 38.199-27.671-19.802 1.0061.48 C ATOM 2724 CDl LEU A 382 37.136-27.835-20.885 1.0061.27 C ATOM 2725 CD2LEUA382 38.694-29.019-19.281 1.0062.11 C ATOM 2726 C LEU A 382 40.506-27.964-22.236 1.0061.46 C ATOM 2727 O LEU A 382 40.736-29.157-22.509 1.0061.78 O ATOM 2728 N ASP A 383 40.127-27.070-23.150 1.0061.44 N ATOM 2729 CA ASP A 383 39.867-27.453-24.543 1.0061.75 C ATOM 2730 CB ASP A 383 39.743-26.209-25.431 1.0061.77 C ATOM 2731 CG ASP A 383 38.778-25.172-24.868 1.0061.90 C ATOM 2732 ODl ASP A 383 38.498-25.208-23.654 1.0062.19 O ATOM 2733 OD2ASPA383 38.302-24.311-25.640 1.0062.06 O ATOM 2734 C ASP A 383 40.974-28.358-25.074 1.0061.90 C ATOM 2735 O ASP A 383 40.722-29.471-25.589 1.0062.21 O ATOM 2736 N ASP A 384 42.204-27.870-24.934 1.0061.93 N ATOM 2737 CA ASP A 384 43.377-28.633-25.329 1.0062.20 C ATOM 2738 CB ASP A 384 44.659-27.857-25.012 1.0062.22 C ATOM 2739 CG ASP A 384 45.905-28.552-25.527 1.0062.42 C ATOM 2740 ODl ASP A 384 46.168 -28.477 -26.747 1.0062.53 O ATOM 2741 OD2ASPA384 46.625-29.168-24.711 1.0062.70 O ATOM 2742 C . ASP A 384 43.387-29.985-24.621 1.0062.27 C ATOM 2743 O ASP A 384 43.630 -31.022 r25.261 1.0062.50 O ATOM 2744 N MET A 385 43.109-29.969-23.310 1.0062.20 N ATOM 2745 CA MET A 385 43.094-31.206-22.531 1.0062.37 C ATOM 2746 CB MET A 385 42.531-31.035-21.114 1.0062.38 C ATOM 2747 CG MET A 385 42.451-32.383-20.351 1.0062.39 C ATOM 2748 SD MET A 385 41.135-32.605-19.117 1.0062.11 S ATOM 2749 CE MET A 385 39.727-33.021-20.153 1.0061.97 C ATOM 2750 C MET A 385 42.244-32.216-23.244 1.0062.48 C ATOM 2751 O MET A 385 42.760-33.215-23.768 1.0062.86 O , ATOM 2752 N LEU A 386 40.937-31.958-23.272 1.0062.43 N ATOM 2753 CA LEU A 386 40.058-32.982-23.813 1.0062.76 C ATOM 2754 CB LEU A 386 38.556-32.642-23.723 1.0062.76 C ATOM 2755 CG LEU A 386 37.940-31.254-23.928 1.0062.69 C ATOM 2756 CDl LEU A 386 36.474-31.394-24.317 1.0062.40 C ATOM 2757 CD2LEUA386 38.072-30.425-22.665 1.0062.82 C ATOM 2758 C LEU A 386 40.515-33.334-25.217 1.0062.86 C ATOM 2759 O LEU A 386 40.936-34.480-25.461 1.0063.18 O ATOM 2760 N ALA A 387 40.506-32.335-26.104 1.0062.84 N ATOM 2761 CA ALA A 387 40.937-32.545-27.487 1.0063.11 . C ATOM 2762 CB ALA A 387 41.213-31.207-28.168 1.0062.92 C ATOM 2763 C ALA A 387 42.163-33.465-27.585 1.0063.24 C ATOM 2764 O ALA A 387 42.042-34.694-27.776 1.0063.61 O ATOM 2765 N GLN A 388 43.343-32.877-27.416 1.0063.14 N ATOM 2766 CA GLNA 388 44.582-33.594-27.698 1.0063143 C ATOM 2767 CB GLN A 388 45.744-32.603-27.824 1.0063.49 C ATOM 2768 CG GLN A 388 45.354-31.297-28.512 1.0063.57 C ATOM 2769 CD GLN A 388 46.408-30.790-29.481 1.0063.61 C ATOM 2770 OEl GLN A 388 47.175-31.570-30.053 1.0063.36 O ATOM 2771 NE2GLNA388 46.441-29.477-29.681 1.0063.79 N ATOM 2772 C GLN A 388 44.906-34.688-26.676 1.0063.52 C ATOM 2773 O GLN A 388 45.198-35.850-27.041 1.0063.82 O ATOM- 2774 N ASP A 389 44.844-34.323-25.397 1.0063.47 N ATOM 2775 CA ASP A 389 45.269-35.242-24.354 1.0063.75 C ATOM 2776 CB ASP A 389 45.274.-34.549-22.992 1.0063.76 C ATOM 2777 CG ASP A 389 46.351-33.484-22.888 1.0064.01 C ATOM 2778 ODl ASP A 389 47.535-33.801-23.137 1.0064.41 O ATOM 2779 OD2ASPA389 46.017-32.328-22,554 1.0064.29 O ATOM 2780 C ASP A 389 44.395-36.491-24.338 1.0063.83 C ATOM 2781 O ASP A 389 44.909-37.633-24.114 1.0064.19 O ATOM 2782 N ILE A 390 43.082-36.290-24.600 1.0063.79 N ATOM 2783 CA ILE A 390 42.202-37.449-24.564 1.0064.00 C ATOM 2784 CB ILE A 390 40.757 -37.051 -24.238 1.0063.95 C ATOM 2785 CGl ILE A 390 40.670-36.707-22.748 1.0063.71 C ATOM 2786 CDl ILE A 390 39.357-36.139-22.318 1.0063.77 C ATOM 2787 CG2ILEA390 39.789-38.171-24.600 1.0063.97 C ATOM 2788 C ILE A 390 42.349-38.215-25.875 1.0064.14 C ATOM 2789 O ILE A 390 42.347 -39.465-25.896 1.0064.58 O ATOM 2790 N ALA A 391 42.530-37.458-26.958 1.0064.14 N ATOM 2791 CA ALAA 391 42.907-38.063-28.225 1.0064.26 C ATOM 2792 CB ALA A 391 43.364 -37.001 -29.210 1.0064.25 C ATOM 2793 C ALA A 391 43.998-39.120-28.018 1.0064.38 C ATOM 2794 O ALA A 391 43.828-40.265-28.427 1.0064.34 O ATOM 2795 N LYS A 392 45.100-38.750-27.361 LOO 64.51 N ATOM 2796 CA LYS A 392 46.252-39.681-27.211 1.0065.03 C ATOM 2797 CB LYS A 392 47.541-38.900-26.844 1.0065.00 C ATOM 2798 CG LYS A 392 48.702-39.822-26.461 1.0065.42 C ATOM 2799 CD LYS A 392 49.804-39.084-25.687 1.0065.51 C ATOM 2800 CE LYS A 392 49.376-38.797-24.226 1,0066.25 C. ATOM 2801 NZ LYS A 392 50.460-38.108-23.435 1.0066.63 N ATOM 2802 C LYS A 392 46.064-40.824-26.164 1.0065.09 C ATOM 2803 O LYS A 392 46.422 -42.067 -26.150 1.0065.53 O ^• ATOM 2804 N LEU A 393 45.000-40.372-25.222 1.0065.09 N ATOM 2805 CA LEU A 393 44.770-41.413-24.203 1.0065.41 C ATOM 2806 CB LEU A 393 44.067-40.850-22.966 1.0065.35 C ATOM 2807 CG LEUA 393 45.072-40.402-21.908 1.0065.48 C ATOM 2808 CDl LEU A 393 44.354-39.831-20.708 1.0065.63 C ATOM 2809 CD2LEUA393 45.954-41.576-21.502 1.0065.50 C ATOM 2810 C LEU A 393 43.969-42.559-24.811 1.0065.64 C ATOM 2811 O LEU A 393. 44.037-43.692-24.318 1.0065.90 O ATOM 2812 N MET A 394 43.227-42.276-25.889 1.0065.68 N ATOM 2813 CA MET A 394 42.453-43.350-26.532 1.0066.07 C ATOM 2814 CB MET A 394 41.660-42.822-27.736 1.0066.11 C ATOM 2815 CG MET A 394 40.545-41.845-27.371 1.0066.43 C ATOM 2816 SD MET A 394 39.379-42.505-26.151 1.0067.28 S ATOM 2817 CE MET A 394 38.146-41.197-26.108 1.0066.63 C ATOM 2818 C MET A 394 43.334-44.552-26.932 1.0066.21 C ATOM 2819 O MET A 394 43.125 -45.678 -26.449.1.0066.49 O ATOM 2820 N PRO A 395 44.324-44.319-27.820 1.0066.35 N ATOM 2821 CA PRO A 395 45.221-45.400-28.246 1.0066.36 C ATOM 2822 CB PRO A 395 46.359-44.656-28.950 1.0066.30 C ATOM 2823 CG PRO A 395 45.708-43.450-29.505 1.0066.32 C ATOM 2824 CD PRO A 395 44.637-43.024-28:496 1.0066.42 C ATOM 2825 C PRO A 395 45.788-46.183-27.065 1.0066.38 C ATOM 2826 O PRO A 395 45.847-47.571-27.111 1.0066.53 O ATOM 2827 N LEU A 396 45.997-45.303-25.853 1.0066.35 N ATOM 2828 CA LEU A 396 46.746-46.083-24.821 1.0066.51 . C ATOM 2829 CB LEU A 396 47.352-45.178-23.729 1.0066.52 ^• C ATOM 2830 CG LEU A 396 48.412-45.758-22.772 1.0066.50 C ATOM 2831 CDl LEU A 396 48.815-44.715-21.728 1.0066.78 C ATOM 2832 CD2LEUA396 47.966-47.05.1-22.076 1.0066.41 C ATOM 2833 C LEU A 396 45.701-47.020-24.189 1.0066.56 C ATOM 2834 O LEU A 396 45.970-48.217-23.789 1.0066.72 O ATOM .2835 N LEU A 397 44.490-46.430-24.125 1.0066.57 N ATOM 2836 CA LEU A 397 43.335-47.098-23.570 1.0066.81 C ATOM 2837 CB LEU A 397 42.107-46.199-23.695 1.0066.77 C ATOM 2838 CG LEU A 397 40.789-46.797-23.217 1.0066.74 C ATOM 2839 CDl LEU A 397 40.828-47.016-21.711 1.0066.79 C ATOM 2840 CD2LEUA397 39.643-45.884-23.609 1.0066.83 C ATOM 2841 C LEU A 397 43.082-48.420-24.267 1.0066.95 C ATOM 2842 O LEU A 397 42.883-49.426-23.605 1.0067.22 O ^'• ATOM 2843 N ARG A 398 43.092-48.416-25.599 1.0067.02 N ATOM 2844 CA ARG A 398 42.836-49.643-26.369 1.0067.30 C ATOM 2845 CB ARG A 398 42.850-49.332-27.868 1.0067.36 C ATOM 2846 CG ARG A 398 41.808-48.309-28.301 1.0067.98 C ATOM 2847 CD ARG A 398 42.319-47.456-29.459 1.0068.97 C ATOM 2848 NE ARG A 398 42.794-48.259-30.583 1.0069.67 N ATOM 2849 CZ ARG A 398 42.005-48.760-31.532 1.0070.33 C ATOM 2850 NHl ARG A 398 42.528-49.478-32.520 1.0070.67 N ATOM 2851 NH2ARGA398 40.693-48.547-31.494 1.0070.46 N ATOM 2852 C ARG A 398 43.866-50.744-26.069 1.0067.28 C ATOM 2853 O ARG A 398 43.504-52.040-25.930 1.0067.55 O ATOM 2854 N GLN A 399 45.149-50.229-25.856 1.0067.15 N ATOM 2855 CA GLN A 399 46.206-51.190-25.539 1.0067.22 C ATOM 2856 CB GLN A 399 47.589-50.529-25.575 1.0067.21 C ATOM 2857 CG GLN A 399 48.756-51.484-25.318 1.0067.20 C ATOM 2858 CD GLN A 399 48.755-52.683-26.261 1.0067.24 C ATOM 2859 OEl GLN A 399 48.822-53.832-25.813 1.0067.09 O ATOM 2860 NE2 GLN A 399 48.674-52.421-27.571 1.0067.33 N ATOM 2861 C GLN A 399 45.927-51.801-24.170 1.0067.26 C ATOM 2862 O GLN A 399 46.229-52.973-23.925 1.0067.20 O ATOM 2863 N GLU A 400 45.333-51.006-23.282 1.0067.33 N ATOM 2864 CA GLU A 400 44.948-51.520-21.970 1.0067.67 C ATOM 2865 CB GLU A 400 44.770-50.383-20.966 1.0067.73 C ATOM 2866 CG GLU A 400 46.081-49.853-20.396 1.0068.29 C ATOM 2867 CD GLU A 400 45.856-49.020-19.145 1.0068.96 C ATOM 2868 OEl GLU A 400 46.798-48.311-18.724 1.0069.08 O ATOM 2869 OE2GLUA400 44.735-49.077-18.586 1.0069.03 O ATOM 2870 C GLU A 400 43.681-52.374-22.016 1.0067.75 C ATOM 2871 O GLU A 400 43.505-53.276-21.197 1.0067.75 O ATOM 2872 N . GLU A 401 42.802-52.089-22.974 1.0067.83 N ATOM 2873 CA GLU A 401 41.535-52.807-23.088 1.0068.15 C ATOM 2874 CB GLU A 401 40.515-52.036-23.945 1.0068.25 C ATOM 2875 CG GLU A 401 39.080-52.606-23.881 1.0068.55 C ATOM 2876 CD GLU A 401 38.001-51.549-24.104 1.0068.79 C ATOM 2877 OEl GLU A 401 38.129-50.435-23.549 1.0068.79 O ATOM 2878 OE2GLUA401 37.017-51.839-24.824 1.0068.49 O ATOM 2879 C GLU A 401 41.775-54.218-23.626 1.0068.19 C ATOM 2880 O GLU A 401 40.863-55.103-23.541 1.0068.20 O ATOM 2881 N LEU A 402 43.014-54.443-24.161 LOO 68.10 N ATOM 2882 CA LEU A 402 43.360-55.876-24.349 1.0068.26 C ATOM 2883 CB LEU A 402 43.651-56.248-25.818 1.0068.22 C ATOM 2884 CG LEU A 402 44.480-55.386-26.774 1.0068.29 C ATOM 2885 CDl LEU A 402 45.951-55.301-26.369 1.0068.15 C ATOM 2886 CD2LEUA402 44.340-55.954-28.185 1.0068.27 C ATOM 2887 C LEU A 402 44.480-56.322-23.386 1.0068.35 C ATOM 2888 O LEU A 402 45.647-56.557-23.789 1.0068.28 O ^' ATOM 2889 N GLU A 403 44.107-56.428-22.102 1.0068.52 N ATOM 2890 CA GLU A 403 45.088-56.755-21.065 1.0068.65 C ATOM 2891 CB GLU A 403 45.431-55.521-20.224 1.0068.70 C ATOM 2892 CG GLU A 403 46.491-54.639-20.862 1.0068.74 C ATOM 2893 CD GLU A 403 47.715-55.426-21.293 1.0068.53 C ATOM 2894 OEl GLU A 403 47.701-56.670-21.161 1.0068.11 O ATOM 2895 OE2GLUA403 48.691 -54.802-21.761 1.0068.50 O ATOM 2896 C GLU A 403 44.714-57.924-20.161 1.0068.69 C

ATOM 2897 O GLU A 403 45.249-59.023-20.320 1.0068.78 O

ATOM 2898 N SER A 404 43.817-57.699-19.204 1.0068.70 N

ATOM 2899 CA SER A 404 43.474-58.768-18.266 1.0068.71 C

ATOM 2900 CB SER A 404 44.240-58.599-16.944 1.0068.72 C

ATOM 2901 OG SER A 404 44.441-59.853-16.305 1.0068.64 O

ATOM 2902 C SER A 404 41.970-58.933-18.010 1.0068.68 C

ATOM 2903 O SER A 404 41.344-58.123-17.318 1.0068.72 O

ATOM 2904 N VAL A 405 41.405-59.999-18.576 1.0068.52 N

ATOM 2905 CA VAL A 405 40.014-60.373-18.330 1.0068.31 C

ATOM 2906 CB VAL A 405 39.515-61.401-19.382 1.0068.37 C

ATOM 2907 CGl VAL A 405 38.017-61.661-19.226 1.0068.42 C

ATOM 2908 CG2VALA405 40.316-62.702-19.301 1.0068.30 C

ATOM 2909 C VAL A 405 39.859-60.941-16.914 1.0068.09 C

ATOM 2910 O VAL A 405 38.742-61.172-16.440 1.0068.12 O

ATOM 2911 N GLU A 406 40.994-61.154-16.249 1.0067.77 N

ATOM 2912 CA GLU A 406 41.041-61.660-14.875 1.0067.37 C

ATOM 2913 CB GLU A 406 42.492-61.732-14.388 1.0067.50 C

ATOM 2914 CG GLU A 406 42.647-62.138-12.926 1.0067.80 C

ATOM 2915 CD GLU A 406 43.569-61.202-12.160 1.0068.31 C

ATOM 2916 OEl GLU A 406 44.561-61.685-11.570 1.0068.29 O

ATOM 2917 OE2GLUA406 43.301-59.978-12.151 1.0068.51 O

ATOM 2918 C GLU A 406 40.234-60.777-13.926 1.0066.93 C

ATOM 2919 O GLU A 406 39.662-61.265-12.946 1.0066.98 O

ATOM 2920 N ALA A 407 40.197-59.479-14.224 1.0066.23 N

ATOM 2921 CA ALA A 407 39.443-58.516-13.424 1.0065.47 C

ATOM 2922 CB ALA A 407 39.721-57.094-13.907 1.0065.49 C

ATOM 2923 C ALA A 407 37.940-58.813-13.441 1.0064.85 C

ATOM 2924 O ALA A 407 37.202-58.369-12.555 1.0064.84 O

ATOM 2925 N GLY A 408 37.504-59.576-14.444 1.0064.00 N

ATOM 2926 CA GLY A 408 36.098-59.936-14.617 1.0062.91 C

ATOM 2927 C GLY A 408 35.433-60.428-13.348 1.0062.16 C

ATOM 2928 O GLY A 408 36.082-61.020-12.486 1.0062.11 O

ATOM 2929 N VAL A 409 34.133 -60.180 -13.234 jl 0061.40 N

ATOM 2930 CA VAL A 409 33.380 -60.595 -12.059 1.0060.66 C

ATOM 2931 CB VAL A 409 31.952-60.013-12.059 1.0060.68 C

ATOM 2932 CGl VAL A 409 31.345-60.103-10.670 1.0060.53 C

ATOM 2933 CG2VALA409 31.973-58.573-12.521 1.0060.66 C

ATOM 2934 C VAL A 409 33.329-62.117-11.964 1.0060.21 C

ATOM 2935 O VAL A 409 32.927-62.803-12.909 1.0060.00 ' O

ATOM 2936 N ALA A 410 33.750-62.638-10.817 1.0059.67 N

ATOM 2937 CA ALA A 410 33.824-64.077-10.612 1.0059.13 C

ATOM 2938 CB ALA A 410 35.019-64.425 -9.741 1.0059.26 C

ATOM 2939 C ALA A 410 32.543-64.616 -9.998 1.0058.71 C.

ATOM 2940 O ALA A 410 31.774-63.875 -9.392 1.0058.61 O

ATOM 2941 N GLY A 411 32.338.65.919₇10.160 1.0058.33 N

ATOM 2942 CA GLYA411 31.135-66.617 -9.709 1.0057.74 C

ATOM 2943 C GLY A 411 30.218 -65.930 -8.713 1.0057.25 C

ATOM 2944 O GLY A 411 30.664-65.273 -7.770 1.0057.29 O

ATOM 2945 N GLY A 412 28.920-66.103 -8.937 1.0056.81 N

ATOM 2946 CA . GLY A 412 27.885-65.639 -8.023 1.0056.24 C

ATOM 2947 C GLY A 412 26.593 -66.100 -8.654 1.0055.88 C

ATOM 2948 O GLY A 412 26.023-67.115 -8.267 1.0055.87 O

ATOM 2949 N ALA A 413 26.149-65.349 -9.651 1.0055.53 N

ATOM 2950 CA . ALA A 413 25.119-65.806-10.564 1.0055.19 C

ATOM 2951 CB ALA A 413 23.952-64.844-10.570 1.0055.14 • C

ATOM 2952 C ALA A 413 25.763-65.865-11.937 1.0054.97 C

ATOM 2953 O ALAA 413 25.107-66.140-12.938 1.0055.00 O ATOM 2954 N PHE A 414 27.066-65.613-11.968 1.0054.73 N

ATOM 2955 CA PHE A 414 27.791-65.468-13.220 1.0054.57 C

^■ ATOM 2956 CB PHE A 414 28.869-64.387-13.090 1.0054.59 C

ATOM 2957 CG PHE A 414 28.326-63.027-12.744 1.0054.41 C ATOM 2958 CDl PHE A 414 27.851 -62.184-13.735 1.0054.25 C

ATOM 2959 CEl PHE A 414 27.351-60.941-13.421 1.0054.27 C

ATOM 2960 CZ PHE A 414 27.322-60.521-12.105 1.0054.38 C

ATOM 2961 CE2PHEA414 27.792-61.350-11.109 1.0054.20 C

ATOM 2962 CD2PHEA414 28.291-62.594-11.429 1.0054.24 C ATOM 2963 C PHE A 414 28.421.-66.771-13.689 1.0054.51 . C

ATOM 2964 O PHE A 414 28.536-67.005-14.892 1.0054.59 O

ATOM 2965 N GLU A 415 28.827-67.612-12.740 1.0054.32 N

ATOM 2966 CA GLU A 415 29.498-68.872-13.056 1.0054.13 C

ATOM 2967 CB GLU A 415 29.668-69.713-11.796 1.0054.25 C ATOM 2968 CG GLU A 415 28.358-70.145-11.184 1.0055.37 C

ATOM 2969 CD GLU A 415 28.459-70.379 -9.691 1.0057.16 C

ATOM 2970 OEl GLU A 415 27.487-70.912 -9.105 1.0057.92 O

ATOM 2971 OE2GLUA415 29.507 -7θ!θ25 -9.104 1.0057.82 O

ATOM 2972 C GLU A 415 28.758-69.664-14.133 1.0053.71 C ATOM 2973 O GLU A 415 27.527-69.672-14.179 1.0053.58 O

ATOM 2974 N GLY A 416 29.523-70.325-14.997 1.0053.38 N

ATOM 2975 CA GLY A 416 28.966-70.999-16.165 1.0052.98 C

ATOM 2976 C GLY A 416 28.302-72.320-15.844 1.0052.72 C

ATOM 2977 O GLY A 416 27.353-72.729-16.516 1.0052.60 ^' O ATOM 2978 N THR A 417 28.805-72.985-14.808 1.0052.54 N

ATOM 2979 CA THR A 417 28.274-74.275-14.382 1.0052.37 C

ATOM 2980 CB THR A 417 29.094-74.865-13.219 1.0052.27 C

ATOM 2981 OGl THR A 417 29.438-73.824-12.299 1.0051.98 O

ATOM 2982 CG2THRA417 30.369-75.497-13.736 1.0052.29 C ATOM 2983 C THR A 417 26.803-74.199-13.977 1.0052.41 C

ATOM 2984 O THR A 417 26.166-75.226-13.746 1.0052.44 O

ATOM 2985 N ARG A 418 26.269-72.982-13.899 1.0052.48 N

ATOM 2986 CA ARG A 418 24.876-72.768-13.518 1.0052.60 C

ATOM 2987 CB ARG A 418 24.659-71.335-13.031 1.0052.61 C ATOM 2988 CG ARGA418 25.100-71.097-11.597 1.0053.27 ' C

ATOM 2989 CD ARG A 418 24.677-69.722-11.083 1.0054.81 C

ATOM 2990 NE ARG A 418 23.237-69.623-10.850 1.0055.96 N

ATOM 2991 CZ ARG A 418 22.371-69.084-11.706 1.0056.80 C

ATOM 2992 NHl ARG A 418 21.077-69.038-11.405 1.0057.11 N ATOM 2993 NH2ARGA418 22.795-68.589-12.864 1.0056.93 N

ATOM 2994 C ARG A 418 23.916-73.077-14.657 1:0052.65 C

ATOM 2995 O ARG A 418 22.722-73.271-14.439 1.0052.59 O

ATOM 2996 N MET A 419 24.443-73.129-15.873 1.0052.86 N

ATOM 2997 CA MET A 419 23.613-73.399-17.037 1.0053.06 . C ATOM 2998 CB MET. A 419 24.176-72.685-18.273 1.0053.29 C

ATOM 2999 CG MET A 419 23.147-72.383-19.370 1.0054.17 C

ATOM 3000 SD MET A 419 21.616-71.599-18.788 1.0055.92 S

ATOM 3001 CE MET A 419 20.494-72.997-18.721 1.0055.37 C

ATOM 3002 C MET A 419 23.462-74.904-17.280 1.0052.89 C ATOM 3003 O MET A 419 22.750-75.326-18.190 1.0052.78 O

ATOM 3004 N GLY A 420 24.124-75.707-16.452 1.0052.86 N

ATOM 3005 CA GLY A 420 24.028-77.161-16.549 1.0052.96 C

ATOM 3006 C GLY A 420 25.303^' -77.821 -17.045 1.0053.03 C

ATOM 3007 O GLY A 420 26.231-77.138-17.476 1.0053.13 O ATOM 3008 N PRO A 421 25.364-79.161-16.972 1.0053.04 N

ATOM 3009 CA PRO A 421 26.537-79.878-17.412 1.0053.09 C

ATOM 3010 CB PRO A 421 26.673-80.952-16.335 1.0052.99 C

ATOM 3011 CG PRO A 421 25.217-81.301-15.998 1.0052.91 C ATOM 3012 CD PRO A 421 24.357-80.087-16.418 1.0053.05 C ATOM 3013 C PRO A 421 26.348-80.558-18.768 1.0053.26 C ATOM 3014 O PRO A 421 27.242-81.294-19.215 1.0053.35 O ATOM 3015 N PHE A 422 25.210-80.321-19.424 1.0053.47 N ATOM 3016 CA PHE A 422 24.861 -81.125 -20.599 1.0053.71 C ATOM 3017 CB PHE A 422 23.439^' -81.673 -20.491 1.0053.51 C ATOM 3018 CG PHE A 422 23.360-82.947-19.722 1.0053.01 C ATOM 3019 CDl PHE A 422 23.056-82.939-18.377 1.0052.78 C ATOM 3020 CEl PHE A 422 23.000-84.113-17.662 1.0052.83 C ATOM 3021 CZ PHE A 422 23.260-85.312-18.287 1.0052.98 C ATOM 3022 CE2PHEA422 23.577-85.331-19.627 1.0052.93 C ATOM 3023 CD2PHEA422 23.631-84.153-20.336 1.0052.79 C ATOM 3024 C PHE A 422 25.106-80.504-21.970 1.0054.16 C ATOM 3025 O PHE A 422 25.548-81.193-22.894 1.0054.20 O ATOM 3026 N VAL A 423 24.814-79.217-22.116 1.0054.72 N ATOM 3027 CA VAL A 423 25.103-78.540-23.376 1.0055.30 C ATOM 3028 CB VAL A 423 23.829-77.988-24.055 1.0055.35 . C ATOM 3029 CGl VAL A 423 24.187-77.283-25.358 1.0055.52 C ATOM 3030 CG2VALA423 22.840-79.119-24.324 1.0055.43 C ATOM 3031 C VAL A 423 26.133-77.434-23.179 1.0055.57 C ^' ATOM 3032 O VAL A 423 25.864-76.444-22.496 1.0055.56 O ATOM 3033 N GLU A 424 27.308-77.627-23.783 1.0056.06 N ATOM 3034 CA GLU A 424 28.436-76.685-23.709 1.0056.34 C ATOM 3035 CB GLU A 424 28.105-75.352-24.420 1.0056.44 C ATOM 3036 CG GLU A 424 29.293-74.350-24.581 1.0056.50 C ATOM 3037 CD GLU A 424 29.181 -73.133 -23.625 1.0057.30 C ATOM 3038 OEl GLU A 424 27.963-72.749-23.245 1.0057.51 . O ATOM 3039 OE2GLUA424 30.250-72.545-23.247 1.0057.40 O ATOM 3040 C GLU A 424 28.929-76.440-22.273 1.0056.48 C ATOM 3041 O GLU A 424 28.279-75.721-21.495 1.0056.64 O ATOM 3042 N GLU A 443 15.905-85.521-51.072 1,0065.60 N ATOM 3043 CA GLU A 443 14.889-84.482-51.179 1.0065.73 C ATOM 3044 CB GLU A 443 14.210-84.527-52.553 1.0066.04 C ATOM 3045 CG GLU A 443 13.123-83.462-52.765 1.0067.13 C ATOM 3046 CD GLU A 443 13.687-82.071-53.033 1.0068.58 C ATOM 3047 OEl GLU A 443 14.867-81.816-52.699 1.0069.01 O ATOM 3048 OE2GLUA443 12.942-81.229-53.583 1.0069.27 O ATOM 3049 C GLU A 443 13.847-84.609-50.074 1.0065.36 C ATOM 3050 O GLU A 443 14.126-84.292-48.918 1.0065.51 O ATOM 3051 N- TRP A 444 12.652-85.071-50.441 1.0064.83 N ATOM 3052 CA TRP A 444 11.546 -85.228 -49.500 1.0064.28 C ATOM 3053 CB TRP A 444 10.269-84.611-50.076 1.0064.11 C ATOM 3054 CG TRP A 444 9.181-84.393-49.063 1.0063.96 C ATOM 3055 CDl TRP A 444 9.343-84.086-47.744 1.0063.74 C ATOM 3056 NEl TRP A 444 8.118-83.952-47.135 1.0063.50 N ATOM 3057 CE2.TRPA444 7.133-84.164-48.062 1.0063.49 C ATOM 3058 CD2TRPA444 7.764-84.438-49.292 1.0063.81 C ATOM 3059 CE3 TRP A 444 6.970-84.694-50.414 1.0063.77 C ATOM 3060 CZ3TRPA444 5.591-84.665-50.271 1.0063.70 C ATOM 3061 CH2TRPA444 4.995-84.386-49.037 1.0063.62 C ATOM 3062 CZ2TRPA444 5.747-84.137-47.923 1.0063.59 C ATOM 3063 C TRP A 444 11.342-86.707-49.211 1.0064.04 C ATOM 3064 O TRP A 444 11.421-87.531-50.116 1.0064.09 O ATOM 3065 N VAL A 445 11.074-87.043-47.953 1.0063.74 N ATOM 3066 CA VAL A 445 11.078-88.445-47.534 1.0063.47 C ATOM 3067 CB VAL A 445 11.343-88.591-46.016 1.0063.49 C ATOM 3068 CGl VAL A 445 12.100-89.891-45.746 1.0063.40 C ATOM 3069 CG2VALA445 12.153-87.410-45.501 1.0063.67 C ATOM 3070 C VAL A 445 9.814 -89;236 -47.888 1.0063.28 C

ATOM 3071 O VAL A 445 9.848-90.466-47.930 1.0063.22 O

ATOM 3072 N VAL A 446 8.703-88.549-48.141 1.0063.03 N

ATOM 3073 CA VAL A 446 7.432-89.251-48.345 1.0062.82 C

5 ATOM 3074 CB VAL A 446 6.242-88.540-47.646 1.0062.73 C

ATOM 3075 CGl VAL A 446 6.725-87.739-46.447 1.0062.74 C

ATOM 3076 CG2VALA446 5.508-87.644-48.612 1.0062.62 C

ATOM 3077 C VAL A 446 7.100-89.527-49.817 1.0062.78 C

ATOM 3Q78 O VAL A 446 6.157-90.263-50.119 1.0062.73 O

10 ATOM 3079 N THR A 447 7.8.84-88.954-50.728 1.0062.71 N

ATOM 3080 CA THR A 447 7.650-89.148-52.161 1.0062.74 C

ATOM 3081 CB THR A 447 8.638-88.339-53.025 1.0062.72 C

ATOM 3082 OGl THR A 447 9.861-88.163-52.305 1.0063.01 O

ATOM 3083 CG2THRA447 8.062-86.972-53.357 1.0062.66 C

15 ATOM 3084 C THR A 447 7.680-90.620-52.582 1.0062.71 C

ATOM 3085 O THR A 447 7.073-90.991-53.588 1.0062.63 O

ATOM 3086 N LYS A 448 8.379-91.453-51.813 1.0062.74 N

ATOM 3087 CA LYS A 448 8.381-92.895-52.061 1.0062.80 C

ATOM 3088 CB LYS A 448 9.370-93.628-51.148 1.0062.76 C

20 ATOM 3089 CG LYS A 448 10.789-93.108-5.1.197 1.0063.05 C

ATOM 3090 CD LYS A 448 11.108-92.289-49.960 1.0063.48 C

ATOM 3091 CE LYS A 448 12.245-91.319-50.222 1.0063.64 C

ATOM 3092 NZ LYS A 448 11.832-90.275-51.202 1.0063.53 N

ATOM 3093 C LYS A 448 6.986-93.490-51.874 1.0062.83 C

25 . ATOM 3094 O LYS A 448 6.543-94.314-52.674 1.0063.01 O

ATOM 3095 N ASP A 449 6.297-93.070-50.818 1.0062.70 N

ATOM 3096 CA ASP A 449 4.993-93.632-50.493 1.0062.64 C

ATOM 3097 CB ASP A 449 4,882-93.837-48.981 1.0062.80 C

ATOM 3098 CG ASP A 449 5.951-94.782-48.439 1.0063.19 C

30 ATOM 3099 ODl ASP A 449 6.122-95.890-49.006 1.0063.74 O

ATOM 3100 OD2ASPA449 6.619 -94.419 -47.444 1.0063.29 O ATOM 3101 C ASP A 449 3.868-92.743-51.014 1.0062.46 C ATOM 31020 ASP A 449 2.684-92.959-50.717 1.0062.44 O ATOM 3103 N LYS A 450 4.253-91.756-51.817 1.0062.30 N

35 ATOM 3104 CA LYS A 450 3.326-90.744-52.305 1.0062.13 C ATOM 3105 CB LYS A 450 4.051-89.734-53.196 1.0062.11 C ATOM 3106 CG LYS A 450 3.695-88.274-52.916 1.0061.77 C ATOM 3107 CD LYS A 450 2.292-87.897-53.378 1.0060.83 C ATOM 3108 ^• CE LYS A 450 1.970-86.454-53.009 1.0059.97 C

40 ATOM 3109 NZ LYS A 450 0.604-86.047-53.420 1.0059.33 N ATOM 3110 C LYS A 450 2.140-91.352-53.050 1.0062.15 C ATOM 3111 O LYS A 450 1.013-91.248-52.589 1.0062.07 O

ATOM 3112 N SERA451 2.394-91.983-54.193 1.0062.16 N

ATOM 3113 CA SER A 451 1.320-92.559-55.008 1.0062.17 C

45 ATOM 3114 CB SER A 451 1.913-93.360-56.164 LOO 62.12 C

ATOM 3115 OG SER A 451 3.202-93.834-55.821 1.0062.06 O

ATOM 3116 C SER A 451 0.346-93.415-54.186 1.0062.26 C

ATOM 3117 O SER A 451 -0.870-93.404-54.419 1.0062.26 O

ATOM 3118 N LYSA452 0.895-94.144-53.221 1.0062.25 N

50 ATOM 3119 CA LYS A 452 0.125-94.923-52.257 1.0062.40 C

ATOM 3120 CB LYS A 452 1.131-95.657-51.364 1.0062.38 C

ATOM 3121 CG LYS A 452 0.596-96.422-50.166 1.0062.84 C

ATOM 3122 CD LYS A 452 1.727-97.330-49.630 1.0063.07 C

ATOM 3123 CE LYS A 452 1.511 -97.788 -48.181 1.0064.07 C

55 ATOM 3124 NZ LYS A 452 2.122-96.868-47.174 1.0063.97 N

ATOM 3125 C LYS A 452 -0.812-94.016-51.434 1.0062.22 C

ATOM 3126 O LYS A 452 -2.075-94.152-51.457 1.0062.21 ^' O

ATOM 3127 N TYR A 453 -0.196-93.076-50.719 1.0062.12 N ATOM 3128 CA TYR A 453 -0.965-92.110-49.949 1.0061.83 C

ATOM 3129 CB TYRA453 -0.041-91.057-49.352 1.0061.96 C

ATOM 3130 CG TYR A 453 0.911-91.611-48.324 1.0062.18 C

ATOM 3131 CD1TYRA453 0.622-92.789-47.652 1.0062.45 C ATOM 3132 CEl TYR A 453 1.484-93.298-46.704 1.0062.52 C

ATOM 3133 CZ TYR A 453 2.645-92.622-46.408 1.0062.28 C

ATOM 3134 OH TYR A 453 3.496-93.133-45.464 1.0062.68 O

ATOM 3135 CE2TYRA453 2.957-91.445-47.053 1.0062.18 C

ATOM 3136 CD2TYRA453 2.089-90.945-48.005 1.0062.43 C ATOM 3137 C TYRA453 -2.047-91.449-50.801 1.0061.73 C

ATOM 3138 O TYRA453 -3-.196 -91.346 -50.379 1.0061.52 O

ATOM 3139 N ASPA454 -1.667-91.011-52.000 1.0061.76 N

ATOM 3140 CA ASP A 454 -2.583-90.401-52.962 1.0061.68 C

ATOM 3141 CB ASP A 454 -1.859-90.082-54.269 1.0061.75 C ATOM 3142 CG ASP A 454 -1.090-88.786-54.208 1.0062-.05 C

ATOM 3143 OD1ASPA454 -0.533-88.378-55.250 1.0062.30 O

ATOM 3144 OD2ASPA454 -1.045-88.176-53.119 1.0063.12 O

ATOM 3145 C ASP A 454 -3.761-91.304-53.267 1.0061.60 C

ATOM 3146 O ASPA454 -4.908-90.860-53.236 1.0061.46 O ATOM 3147 N GLUA455 -3.474-92.565-53.581 1.0061.64 N

ATOM 3148 CA GLU A 455 -4.538-93.540-53.775 1.0061.50 C

ATOM 3149 CB GLUA455 -3.972-94.962-53.839 1.0061.52 C

ATOM 3150 CG GLU A 455 -4.800-95.931-54.675 1.0061.62 C

ATOM 3151 CD GLU A 455 -3.526-96.015-55.853 0.0050.00 C ATOM 3152 OEl GLU A 455 -4.004-96.674-56.795 0.0050.00 O

ATOM 3153 OE2 GLU A 455 -2.549-95.268-55.967.0.0050.00 O

ATOM 3154 C. GLU A 455 -5.543-93.399-52.630 1.0061.47 C

ATOM 3155 O GLUA455 -6.770-93.244-52.874 1.0061.39 O

ATOM 3156 N ILEA456 -5.034-93.395-51.379 1.0061.57 N ATOM 3157 CA ILE A 456 -6.005-93.246-50.263 1.0061.40 C

ATOM 3158 CB ILE A 456 -5.373-93.420-48.849 1.0061.41 C

ATOM 3159 CGl ILE A 456 -5.081-94.894-48.547 1.0061.57 C

ATOM 3160 CDl ILE A 456 _^3.780 -95.411 -49.117 1.0061.87 C

ATOM 3161 CG2ILEA456 . -6.319-92.913-47.775 1.0060.97 C ATOM 3162 C ILEA456 -6.732-91.892-50.326 1.0061.33 C

ATOM 3163 O ILEA456 -7.973-91.817-50.396 1.0061.32 O

ATOM 3164 N PHEA457 -5.939-90.826-50.315 1.0061.28 N

ATOM 3165 CA PHE A 457 -6.451-89.462-50.304 1.0061.18 C

ATOM 3166 CB PHE A 457 -5.325-88.478-50.619 1.0061.10 C ATOM 3167 CG PHE A 457 -5.788-87.059-50.805 1.0061.06 C

ATOM 3168 CD1PHEA457 -6.014-86.240-49.710 1.0060.72 C

ATOM 3169 CEl PHE A 457 -6.425-84.930-49.878 1.0060.37 C

ATOM 3170 CZ PHE A 457 -6.609-84.424-51.146 1.0060.51 C

ATOM 3171 CE2PHEA457 -6.384-85.228-52.248 1.0060.56 C ATOM 3172 CD2PHEA457 -5.976-86.536-52.077 1.0060.85 C

ATOM 3173 C PHEA457 -7.583 -89.275 -5L295 1.0061.08 C

ATOM 3174 O PHE A 457 -8.642-88.746-50.955 1.0061.04 O

ATOM 3175 N TYRA458 -7.352-89.710-52.526 1.0061.12 N

ATOM 3176 CA TYR A 458 -8.345-89.535-53.570 1.0060.96 C ATOM 3177 CB TYR A 458 -7.707-89.605-54.954 1.0060.87 C

ATOM 3178 CG TYR A 458 -6.880-88.380-55.257 1.0060.78 C

ATOM 3179 CD1TYRA458 -7.477-87.135-55.376 1.0060.62 C ATOM 3180 CEl TYR A 458 -6.733-86.009-55.644 1.0060.72 C

ATOM 3181 CZ TYR A 458 -5.370-86.115-55.793 1.0060.91 C ATOM 3182 OH TYR A 458 -4.624-84.987-56.061 1.0061.14 O

ATOM 3183 CE2TYRA458 -4.750-87.340-55.676 1.0060.97 C

ATOM 3184 CD2 TYR A 458 -5.505-88.463-55.404 1.0060.82 C

ATOM 3.185 C TYR A 458 -9.497-90.509-53.423 1.0060.98 C ATOM 3186 O TYR A 458 -10.613-90.212-53.844 1.0060.99 O

ATOM 3187 N ASNA459 -9.246-91.663-52.807 1.0061.12 N

ATOM 3188 CA ASN A 459 -10.374-92.529-52.457 1.0061.04 C

ATOM 3189 CB ASN A 459 -9.935-93.967-52.193 1.0061.02 C

ATOM 3190 CG ASN A 459 -10.182-94.868-53.382 1.0061.15 C

ATOM 3191 ODl ASN A 459 -9.353-95.713-53.720 1.0061.72 O

ATOM 3192 ND2ASNA459 -11.326-94.682-54.035 1.0061.27 N

ATOM 3193 C ASN A 459 -11.225-91.986-51.310 1.0061.02 C

ATOM 3194 O ASN A 459 -12.307-92.503-51.037 1.0060.90 O

ATOM 3195 N LEU A 460 -10.738-90.936-50.649 1.0061.16 N,

ATOM 3196 CA LEU A 460 -11.536-90.256-49.614 1.0061.21 C

ATOM 3197 CB LEU A 460 -10.644-89.735-48.484 1.0061.18 C

ATOM 3198 CG LEU A 460 -10.441 -90.651 -47.276 1.0061.31 C

ATOM 3199 CDl LEU A 460 -10.126-92.081-47.695 1.0061.70 C

ATOM 3200 CD2LEUA460 -9.353-90.103-46.3.64 1.0061.36 C

ATOM 3201 C LEU A 460 -12.427-89.118-50.132 1.0061.21 C

ATOM 3202 O LEU A 460 -13.042-88.401-49.341 1.0061.15 , O

ATOM 3203 N ALA A 461 -12.490-88.958-51.452 1.0061.30 N

ATOM 3204 CA ALA A 461 -13.332-87.933-52.092 1.0061.39 C .

ATOM 3205 CB ALA A 461 -14.810-88.328-52.035 1.0061.32 C

ATOM 3206 C ALA A 461 -13.132-86.526-51.527 1.0061.46 C

ATOM 3207 O ALA A 461 -13.989-86.016-50.803 1.0061.46 O

ATOM 3208 N PRO A 462 -11.998-85.891-51.868 1.0061.52 N

ATOM 3209 CA PRO A 462 -11.692-84.538-51.427 1.0061.50 C

ATOM 3210 CB PRO A 462 -10.172-84.439-51.605 1.0061.48 C

ATOM 3211 CG PRO A 462 -9.724-85.764-52.182 1.0061.39 C

ATOM 3212 CD PRO A 462 -10.929-86.437-52.716 1.0061.48 C

ATOM 3213 C PRO A 462 -12.388-83.514-52.310 LOO 61.55 C

ATOM 3214 O PRO A 462 -12.933-83.873-53.351 1.0061.39 O

ATOM 3215 N ALA A 463 -12.359-82.252-51.891 1.0061.78 N

ATOM 3216 CA ALA A 463 -13.067-81.176-52.582 1.0061.99 C

ATOM 3217 CB ALA A 463 -12.888-79.860-51.840 1.0062.09 C

ATOM 3218 C ALA A 463 -12.611-81.031-54.023 1.0062.16 C

ATOM 3219 O ALA A 463 -13.233-81.565-54.938 1.0062.42 O

ATOM 3220 N ASP A 464 -11.528-80.293-54.226 1.0062.26 N

ATOM 3221 CA ASP A 464 -10.959-80.154-55.556 1.0062.40 C

ATOM 3222 CB ASP A 464 -11.255-78.767-56.133 1.0062.60 C

ATOM 3223 CG ASP A 464 -10.538-77.651-55.385 1.0063.34 C

ATOM 3224 ODl ASP A 464 -10.634-76.485-55.835 1.0063.76 O

ATOM 3225 OD2ASPA464 -9.880-77.936-54.354 1.0064.06 O

ATOM 3226 C ASP A 464 -9.464-80.382-55.468 1.0062.23 C

ATOM 3227 O ASP A 464 -8.707-79.934-56.317 1.0062.39 O

ATOM 3228 N GLY A 465 -9.049-81.083-54.424 1.0062.02 N

ATOM 3229 CA GLY A 465 -7.640-81.324-54.177 1.0061.82 C

ATOM 3230 C GLY A 465 -7.398-81.127-52.700 1.0061.70 ^' C

ATOM 3231 O GLY A 465 -6.284-81.310-52.205 1.0061.73 O

ATOM 3232 N LYS A 466 -8.460-80.752-51.996 1.0061.43 N

ATOM 3233 CA . LYS A 466 -8.379-80.507-50.572 1.0061.22 C

ATOM 3234 CB LYS A 466 -8.571-79.023-50.279 1.0061.21 C

ATOM 3235 CG LYS A 466 -7.437-78.154-50.775 1.0061.05 C

ATOM 3236 CD LYS A 466 -7.845-76.698-50.831 1.0061.32 C

ATOM 3237 CE LYS A 466 -6.793-75.881-51.549 1.0061.80 C

ATOM 3238 NZ LYS A 466 -6.444 -76.494 -52.864 1.0062.20 N

ATOM 3239 C LYS A 466 -9.417-81.323-49.830 1.0061.12 C

ATOM 3240 O LYS A 466 -10.613-81.218-50.091 1.0061.13 O

ATOM 3241 N LEU A 467 -8.948-82.144-48.903 1.0061.00 N

ATOM 3242 CA . LEU A 467 -9.841-82.926-48.074 1.0060.88 C

ATOM 3243 CB L¹EU A 467 -9.118-84.164-47.542 1.0060.79 C ATOM 3244 CG LEU A 467 -9.961-85.111-46.693 1.0060.87 C

ATOM 3245 CDl LEU A 467 -11.113 -85.658 -47.518 1.0061.30 C

ATOM 3246 CD2LEUA467 -9.114-86.240-46.140 1.0060.91 C

ATOM 3247 c : LEU A 467 -10.339-82.065-46.917 1.0060.83 C

ATOM 3248 O LEU A 467 -9.544-81.491-46.171 1.0060.86 O

ATOM 3249 N SER A 468 -11.658-81.966-46.784 1.0060.71 N

ATOM 3250 CA SER A 468 -12.277-81.277-45.656 1.0060.55 C

ATOM 3251 CB SERA468 -13.787-81.522-45.672 1.0060.68 C

ATOM 3252 OG SER A 468 -14.306-81.658-44.359 1.0061.03 O

ATOM 3253 C SER A 468 -11.682-81.727-44.319 1.0060.34 C

ATOM 3254 O SER A 468 -11.179-82.846-44.201 1.0060.29 O

ATOM 3255 N GLY A 469 -11.746-80.852-43.318 1.0060.13 N

ATOM 3256 CA GLY A 469 -11.213-81.153-41.989 1.0059.92 C

ATOM 3257 C GLY A 469 -11.948-82.273-41.272 1.0059.86 C

ATOM 3258 O GLY A 469 -11.335-83.108-40.605 1.0059.75 O

ATOM 3259 N SER A 470 -13.267-82.298-41.412 1.0059.92 N.

ATOM 3260 CA SER A 470 -14.080-83.316-40.755 1.0060.13 C

ATOM 3261 CB SER A 470 -15:570-82.996-40.911 1.0060.18 C

ATOM 3262 OG SER A 470 -15.909-82.804-42.273 1.0060.39 O

ATOM 3263 C SER A 470 -13.771-84.730-41.262 1.0060.16- C

ATOM 3264 O SER A 470 -13.628-85.667-40.468 1.0060.19 O

ATOM 3265 N LYS A 471 -13.665-84.875-42.582 1.0060.16 N

ATOM 3266 CA LYS A 471 -13.353-86.160-43.203 1.0060.23 C

ATOM 3267 CB LYS A 471 -13.418-86.032-44.726 1.0060.32 C

ATOM 3268 CG LYS A 471 -14.215-84.826-45.209 1.0060.75 C

ATOM 3269 CD LYS A 471 -15.690-85.140-45.412 1.0061.90 C

ATOM 3270 CE LYS A 471 -16.083-85.072-46.889 1.0062.37 C

ATOM 3271 NZ LYS A 471 -15.249-85.959-47.753 1.0062.88 N

ATOM 3272 C LYS A 471 -11.952-86.600-42.777 1.0060.16 C

ATOM 3273 O LYS A 471 -11.723-87.758-42.368 1.0060.14 O

ATOM 3274 N ALA A 472 -11.021-85.654-42.869 1.0060.13 N

ATOM 3275 CA ALA A 472 -9.655-85.868-42.425 1.0060.03 C

ATOM 3276 CB ALA A 472 -8.853-84.582-42.529 1.0059.90 C

ATOM 3277 C ALA A 472 -9.670-86.382-40.993 1.0059.97 C.

ATOM 3278 O ALA A 472 -8.988-87.358-40.665 1.0060.05 O

ATOM 3279 N LYS A 473 -10.466-85.741-40.144 1.0059.85 N

ATOM 3280 CA LYS A 473 -10.563-86.203-38.771 1.0059.96 C

ATOM 3281 CB LYS A 473 -11.393-85.269-37.895 1.0059.91 C

ATOM 3282 CG LYS A 473 -11.375-85.683-36.428 1.0059.67 C

ATOM 3283 CD LYS A 473 -12.269-84.800-35.574 1.0059.75 C

ATOM 3284 CE LYS A 473 -11.937-84.943-34.095 1.0059.64 C

ATOM 3285 NZ LYS A 473 -12.834-84.122-33.234 1.0059.71 N

ATOM 3286 C LYS A 473 -11.111-87.620-38.700 1.0060.14 C

ATOM 3287 O LYS A 473 -10.441-88.495-38.164 1.0060.26 O

ATOM 3288 NT THR A 474 -12.306-87.866-39.243 1.0060.16 N

ATOM 3289 CA THR A 474 -12.872-89.219-39.144 1.0060.24 C

ATOM 3290 CB THR A 474 -14.257-89.402-39.852 1.0060.23 C

ATOM 3291 OGl THR A 474 -14:300 -88.662 ^'-41.075 1.0060.62 O

ATOM 3292 CG2THRA474 -15.394-88.933-38.952 1.0060.37 C

ATOM 3293 C THR A 474 -11.864-90.289-39.582 1.0060.23 C

ATOM 3294 O THR A 474 -11.719-91.319-38.917 1.0060.25 O

ATOM 3295 N TRP A 475 -11.145-90.037-40.672 1.0060.28 N

ATOM 3296 CA . TRP A 475 -10.106-90.978-41.096 1.0060.42 C

ATOM 3297 CB TRP A 475 -9.523-90.535-42.438 1.0060.84 C

ATOM 3298 CG TRP A 475 -8.313-91.301-42.870 1.0061.18 C

ATOM 3299 CDl TRP A 475 -8.275-92.585-43.318 1.0061.70 C

ATOM 3300 NEl TRP A 475 -6.985-92.942-43.627 1.0061.88 N

ATOM 3301 CE2TRPA475 -6.160 -91.878 -43.383 1.0061.50 C ATOM 3302 CD2TRPA475 -6.963-90.823-42.907 1.0061.57 C ATOM 3303 CE3TRPA475 -6.354-89.606-42.577 1.0062.24 C ATOM 3304 CZ3 TRP A 475 -4.977-89.484-42.734 1.0062.05 C ATOM 3305 CH2TRPA475 -4.207-90.555-43.212 1.0061.82 C ATOM 3306 CZ2TRPA475 -4.780-91.756-43.540 1.0061.71 C ATOM 3307 C TRP A 475 -8.998-91.098-40.043 1.0060.37 C ATOM 3308 O TRP A 475 -8.652-92.206-39.568 1.0060.28 O ATOM 3309 N MET A 476 -8.444-89.948-39.674 1.0060.24 N ATOM 3310 CA MET A 476 -7.358-89.927-38.717 1.0060.43 C ATOM 3311 CB MET A 476 .-6.936-88.492-38.400 1.0060.35 C ATOM 3312 CG MET A 476 -6.136-87.837-39.519 1.0060.65 C ATOM 3313 SD MET A 476 -5.609-86.145-39.154 1.0060.97 S ATOM 3314 CE MET A 476 -4.147-86.452-38.158 1.0061.19 . C ATOM 3315 C MET A 476 -7.739-90.692-37.452 1.0060.37 C ATOM 3316 O MET A 476 -7.049-91.632-37.055 1.0060.37 O ATOM 3317 N VAL A 477 -8.847-90.304-36.830 1.0060.31 N ATOM 3318 CA VAL A 477 -9.308-90.980-35.630 1.0060.18 C ATOM 3319 CB VAL A 477 -10.572-90.317-35.039 1.0060.16 C ATOM 3320 CGl VAL A 477 -11.834-91.039-35.497 1.0060.18 C ATOM 3321 CG2VALA477 -10.491-90.304-33.519 1.0060.61 C ATOM 3322 C VAL A 477 -9.553-92.442-35.979 1.0060.04 C ATOM 3323 O VAL A 477 -9.463-93.322-35.124 1.0059.92 O ATOM 3324 N GLY A 478 -9.836-92.689-37.255 1.0060.05 N ATOM 3325 CA GLY A 478 -9.937-94.048-37.773 1.0059.87 C ATOM 3326 C GLY A 478 -8.652-94.826-37.573 1.0059.75 C ATOM 3327 O GLY A 478 -8.683-96.039-37.375 1.0059.64. O ATOM 3328 N THR A 479 -7.512-94.139-37.618 1.0059.79 N ATOM 3329 CA THR A 479 -6.230-94.827-37.337 1.0059.54 C ATOM 3330 CB THR A 479 -5.012-93.965-37.682 1.0059.50 C ATOM 3331 OG1THRA479 -4.708-93.109-36.572 1.0059.40 O ATOM 3332 CG2 THR A 479 -5.274-93.142-38.930 1.0059.72 C ATOM 3333 C THR A 479 -6.044-95.280-35.881 1.0059.41 C ATOM 3334 O THR A 479 -4.929-95.606-35.467 1.0059.36 O ATOM 3335 N LYS A 480 ^■-7.126-95.279-35.111 1.0059.24 N ATOM 3336 CA LYS A 480 -7.102-95.706-33.708 1.0059.00 C ATOM 3337 CB LYS A 480 -7.107-97.236-33.602 1.0058.90 C ATOM 3338 CG LYS A 480 -8.720 -97.582 τ33.472 0.0050.00 , C ATOM 3339 CD LYS A 480 -8.884 -99.002 -33.9640.0050.00 C ATOM 3340 CE LYS A 480 -7.623-99.825-33.831 0.0050.00 C ATOM 3341 NZ LYS A 480 -7.163-100.001-32.431 0.0050.00 N ATOM 3342 C LYS A 480 -5.952-95.120-32.883 1.0058.86 C ATOM 3343 O LYS A 480 -5.432-95.778-31.985 1.0059.02 O ATOM 3344 N LEU A 481 -5.562-93.884-33.184 1.0058.63 N ATOM 3345 CA LEU A 481 -4.589 -93.169 -32.361 1.0058.40 C ATOM 3346 CB LEU A 481 -3.644-92.336-33.233 1.0058.41 C ATOM 3347 CG LEU A 481 -2.448-93.045-33.870 1.0058.17 C ATOM 3348 CDl LEU A 481 -1.516-92.033-34.503 1.0057.72 C ATOM 3349 CD2LEUA481 -1.700-93.871-32.840 1.0057.96 C ATOM 3350 C LEU A 481 -5.303-92.264-31.359 1.0058.27 C ATOM 3351 O LEU A 481 -6.429-91.835-31.607 1.0058.35 O ATOM 3352 N PRO A 482 -4.656-91.980-30.216 1.0058.15 N ATOM 3353 CA PRO A 482 -5.239-91.080-29.221 1.0058.10 C ATOM 3354 CB PRO A 482 -4.232-91.119-28.068 1.0058.03 C ATOM 3355 CG PRO A 482 -2.965-91.591-28.671 1.0058.03 C ATOM 3356 CD PRO A 482 -3.349-92.507 -29.787 1.0058.12 C ATOM 3357 C PRO A 482 -5.389-89.658-29.749 1.0058.13 C ATOM 3358 O PRO A 482 -4.523-89.170-30.476 1.0058.05 O ATOM 3359 N ASN A 483 r6.490 -89.010 -29.375 1.0058.25 N ATOM 3360 CA ASN A 483 -6.826-87.673-29.865 1.0058.27 C ATOM 3361 CB ASN A 483 -7.966-87.069-29.037 1.0058.41 C ATOM 3362 CG ASN A 483 -8.680-85.936-29.761 1.0058.98 C ATOM 3363 ODl ASN A 483 -8.648-84.782-29.323 1.0058.96 O ATOM 3364 ND2ASNA483 -9.328-86.264-30.878 1.0059.69 N ATOM 3365 C ASN A 483 -5.630-86.730-29.872 1.0057.99 C ATOM 3366 O ASN A 483 -5.249-86.219-30.912 1.0057.84 O ATOM 3367 N SER A 484 -5.048-86.515-28.698 1.0057.91 N ATOM 3368 CA SER A 484 -3.895-85.634-28.518 1.0057.86 C ATOM 3369 CB SER A 484 -3.279-85.891-27.137 1.0057.83 C ATOM 3370 OG SER A 484 -1.867-85.789-27.157 LOO 58.63 O ATOM 3371 C SER A 484 -2.851-85.771-29.634 1.0057.69 C ATOM 3372 O SER A 484 -2.538-84.801 -30.341 1.0057.89 O ATOM 3373 N VAL A 485 -2.323-86.978-29.798 1.0057.50 N ATOM 3374 CA VAL A 485 -1.368-87.246-30.858 1.0057.27 C ATOM 3375 CB VAL A 485 -1.034-88.746-30.950 1.0057.16 C ATOM 3376 CGl VAL A 485 -0.287-89.050-32.233 1.0056.97 C ATOM 3377 CG2VALA485 -0.213-89.173-29.750 1.0056.96 C ATOM 3378 C VAL A 485 -1.925-86.756-32.186 1.0057.35 C ATOM 3379 O VAL A 485 -1.303-85.944-32.866 1.0057.43 O ATOM 3380 N LEU A 486 -3.113-87.233-32.542 1.0057.54 N ATOM 3381 CA LEU A 486 -3.739-86.843-33.803 1.0057.77 C ATOM 3382 CB LEU A 486 -5.138-87.454-33.937 1.0057.88 C ATOM 3383 CG LEU A 486 -5.229-88.972-34.109 1.0058.42 C ATOM 3384 CDl LEU A 486 -6.672-89.447-33.979 1.0058.66 C ATOM 3385 CD2LEUA486 -4.638-89.407-35.444 1.0058.90 C ATOM 3386 C LEU A 486 -3.803-85.325-33.975 1.0057.80 C ATOM 3387 O LEU A 486 -3.455-84.808-35.033 1.0057.86 O ATOM 3388 N GLY A 487 -4.249-84.618-32.938 1.0057.71 N ATOM 3389 CA GLYA.487 -4.357-83.163-32.979 1.0057.64 C ATOM 3390 C GLY A 487 -3.016-82.531-33.282 1.0057.70 C ATOM 3391 O GLY A 487 -2.906-81.638-34.142 1.0057.71 O ATOM 3392 N ARG A 488 -1.988-83.010-32.585 1.0057.78 N ATOM 3393 CA ARG A 488 -0.628-82.544-32.841 1.0057.97 C ATOM 3394 CB ARG A 488 0.348-83.209-31.870 1.0058.06 C ATOM 3395 CG ARG A 488 1.529-82.338-31.468 1.0059.39 C ATOM 3396 CD ARG A 488 1.890-82.573-30.002 1.0061.62 C ATOM 3397 NE ARG A 488 2.408-83.923-29.761 1.0063.12 N ATOM 3398 CZ ARG A 488 2.051-84.695-28.733 1.0063.38 C ATOM 3399 NHl ARG A 488 . 2.580-85.907-28.598 1.0063.40 N ATOM 3400 NH2ARGA488 1.153-84.266-27.850 1.0063.17 N ATOM 3401 C ARG A 488 -0.227-82.814-34.300 1.0057.81 C ATOM 3402 O ARG A 488 0.355-81.947-34.979 1.0057.77 O ATOM 3403 N ILE A 489 -0.564-84.008-34.784 1.0057.58 N ATOM 3404 CA ILE A 489 -0.257-84.377-36.159 LOO 57.48 C ATOM 3405 CB ILE A 489 -0.663-85.815-36.470 1.0057.33 C ATOM 3406 CGl ILE A 489 0.244-86.784-35.716 1.0057.24 C ATOM 3407 CDl ILE A 489 -0.047-88.239-35.980 1.0057.50 C ATOM 3408 CG2ILEA489 -0.568-86.066-37.958 1.0057.45 C ATOM 3409 C ILE A 489 -0.953-83.441-37.128 1.0057.56 C ATOM 3410 O ILE A 489 -0.344-82.935-38.070 1.0057.63 ^' O ATOM 3411 N TRPA490 -2.236-83.206-36.895 1.0057.67 N ATOM 3412 CA TRP A 490 -2.970-82.265-37.711 1.0057.64 C ATOM 3413 CB TRP A 490 -4.367-82.008-37.152 1.0057.40 C ATOM 3414 CG TRP A 490 -4.998-80.874-37.862 1.0057.22 C ATOM 3415 CDl TRP A 490 -4.966-79.563-37.500 1.0056.97 C ATOM 3416 NEl TRP A^' 490 -5.628-78.800-38.430 1.0057.04 N ATOM 3417 CE2TRPA490 -6.092 -79.619 -39.425 1.0057.10 C ATOM 3418 CD2TRPA490 -5.704-80.933-39.103 1.0057.28 C ATOM 3419 CE3TRPA490 -6.056-81.974-39.970 1.0057.40 C ATOM 3420 CZ3TRPA490 ^■ -6.780-81.672-41.109 1.0057.15 C ATOM 3421 CH2TRPA490 -7.154-80.354-41.400 1.0057.10 C ATOM 3422 CZ2TRPA490 -6.820-79.316-40.573 1.0057.08 C ATOM 3423 C TRP A 490 -2.208-80.950-37.754 1.0057.62 C ATOM 3424 O TRP A 490 -1.865 -80.442-38.833 1.0057.65 O ATOM 3425 N LYS A 491 -1.942-80.409-36.568 1.0057.68 N ATOM 3426 CA LYS A 491- -.1.302-79.103-36.485 1.0057.74 C ATOM 3427 CB LYS A 491 -1.059-78.684-35.036 1.0057.75 C ATOM 3428 CG LYS A 491 -0.483-77.286-34.909 1.0058.40 C ATOM 3429 CD LYS A 491 -0.964-76.592-33.647 1.0060.09 C ATOM 3430 CE LYS A 491 ^• -2.402-76.107-33.804 1.0061.13 C ATOM 3431 NZ LYS A 491 -2.486-75.022-3_.4.833 1.0062.38 N ATOM 3432 C LYS A 491 -0.009-79.077-37.281 1.0057.58 C ATOM 3433 O LYS A 491 0.285-78.090-37.958 1.0057.50 O ATOM 3434 N LEU A 492 0.754-80.166-37.203 1.0057.51 N ATOM 3435 CA LEU A 492 1.982-80.287-37.988 1.0057.34 C ATOM 3436 CB LEU A 492 2.773-81.513-37.538 1.0057.12 C ATOM 3437 CG LEU A 492 4.058-81.329-36.735 1.0056.50 C ATOM 3438 CDl LEU A 492 4.013-80.090-35.863 1.0056.61 C ATOM 3439 CD2LEUA492 4.317-82.581-35.908 1.0056.14 C ATOM 3440 C LEU A 492 1.722-80.363-39.500 1.0057.59 C ATOM 3441 O LEU A 492 2.471-79.801-40.301 1.0057.53 O ATOM 3442 N SER A 493 0.653-81.051-39.885 1.0057.77 N ATOM 3443 CA SER A 493 0.421-81.357-41.288 1.0058.08 C ATOM 3444 CB SER A 493 -0.393 -82.641 -4.1.427 1.0058.12 C ATOM 3445 OG SER A 493 0.344-83.746-40.936 1.0058.62 O ATOM 3446 C SER A 493 -0.238-80.231 -42.071 1.0058.20 C ATOM 3447 O SER A 493 0.068-80.036-43.249 1.0058.25 O ATOM 3448 N ASP A 494 -1.150-79.499-41.440 1.0058.27 N ATOM 3449 CA ASP A 494 -1.797-78.397-42.148 1.0058.62 C ATOM 3450 CB ASP A 494 -3.062-77.935-41.434 1.0058.56 C ATOM 3451 CG ASP A 494 -3.824-76.894-42.226 1.0058.70 C ATOM 3452 ODl ASP A 494 -3.470-76.661-43.405 1.0058.46 O ATOM 3453 OD2ASPA494 -4.777-76.308-41.668 1.0059.37 O ATOM 3454 C ASP A 494 -0.821 -77.238 -42.302.1.0058.87 C ATOM 3455 O ASP A 494 -0.883-76.250-41.568 1.0058.88 O ATOM 3456 N VAL A 495 0.078-77.368-43.269 1.0059.15 N ATOM 3457 CA VAL A 495 1.182-76.438-43.406 1.0059.38 C ATOM 3458 CB VAL A 495 2.219-76.921-44.439 1.0059.37 C ATOM 3459 CGl VAL A 495 3.314-75.883-44.618 1.0059.25 C ATOM 3460 CG2VALA495 2.819-78.234-43.989 1:0059.21 C ATOM 3461 C VAL A 495 0.721-75.025-43.728 1.0059.65 C ATOM 3462 O VAL A 495 1.173-74.077-43.089 1.0060.04 O ATOM 3463 N ASP A 496 -0.171-74.869-44.703 1.0059.85 N ATOM 3464 CA ASP A 496 -0.668-73.525-45.031 1.0060.04 C ATOM 3465 CB ASP A 496 -1.133-73.422-46.488 1.0060.09 C ATOM 3466 CG ASP A 496 -2.176-74.455-46.847 1.0060.31 C ATOM 3467 ODl ASP A 496 -2.344-75.432-46.082 1.0060.71 O ATOM 3468 OD2ASPA496 -2.825-74.289-47.904 1.0060.45 O ATOM 3469 C ASP A 496 -1.771-73.111-44.066 1.0060.06 C ATOM 3470 O ASP A 496 . -2.373-72.046-44.210 1.0059.85 O ATOM 3471 N ARG A 497 -1.999-73.980-43.081 1.0060.35 N ATOM 3472 CA ARG A 497 -2.962-73.785-41.992 1.0060.65 C ATOM 3473 CB ARG A 497 -2.285-73.166-40.754 1.0060.76 C ATOM 3474 CG ARG A 497 -2.301-71.656-40.649 1.0062.10 C ATOM 3475 CD ARG A 497 -1.067-71.162-39.908 1.0064.37 C ATOM 3476 NE ARG A 497 0.050-70.975-40.832 1.0066.05 N ATOM 3477 CZ ARG A 497 0.345-69.817-41.420 1.0067.08 C ATOM 3478 NHl ARG A 497 1.375-69.738-42.255 1.0067.52 N ATOM 3479. NH2 ARG A 497 -0.385-68.733-41.170 1.0067.06 N ATOM 3480 C ARG A 497 -4.271-73.097-42.402 1.0060.58 C ATOM 3481 O ARG A 497 -4.638-72.036-41.889 1.0060.38 O ATOM 3482 N ASP A 498 -4.976-73.740-43.331 1.0060.75 N ATOM 3483 CA ASP A 498 -6.248-73.227-43.821 1.0060.92 C ATOM 3484 CB ASP A 498 -6.279-73.207-45.358 1.0060.94 C ATOM 3485 CG ASP A 498 -6.136-74.597-45.961 1.0060.96 C ATOM 3486 ODl ASP A 498 -5.577-75.493-45.290 1.0061.07 O ATOM 3487 OD2ASPA498 -6.578-74.792-47.115 1.0060.82 O ATOM 3488 C ASP A 498 -7.435-74.025-43.273 1.0061.06 C ATOM 3489 O ASP A 498 -8.584-73.496-43.189 1.0061.39 O ATOM 3490 N GLY A 499 -7.172-75.293-42.902 1.0061.04 • N ATOM 3491 CA GLY A 499 -8.246-76.100-42.330 1.0061.21 C ATOM 3492 C GLY A 499 -8.543-77.366-43.108 1.0061.37 C ATOM 3493 O GLY A 499 -9.301.-78.229-42.648 1.0061.52 O ATOM 3494 N MET A 500 -7.948-77.476-44.291 1.0061.28 N ATOM 3495 CA MET A 500 -8.092-78.669-45.105 1.0061.23 C ATOM 3496 CB MET A 500 -8.669-78.304-46.467 1.0061.21 C ATOM 3497 CG MET A 500 -10.072-77.741-46.410 1.0061.10 C ATOM 3498 SD MET A 500 -10.597-77.079-48.004 1.0061.13 S ATOM 3499 CE MET A 500 -12.361-76.890-47.731 1.0061.68 C ATOM 3500 C MET A 500 -6.737-79.338-45.277 1.0061.33 C ATOM 3501 O MET A 500 -5.721-78.816-44.820 1.0061.29 O ATOM 3502 N LEU A 501 -6.727-80.500-45.927 1.0061.45 N ATOM 3503 CA LEU A 501 -5.477-81.158-46.298 1.0061.49 C ATOM 3504 CB LEU A 501 -5.259-82.432-45.475 1.0061.41 C ATOM 3505 CG LEU A 501 -5.099-82.291-43.959 1.0061.24 C. ATOM 3506 CDl LEU A 501 -5.182-83.646-43.272 1.0060.96 C ATOM 3507 CD2LEUA501 -3.792-81.603-43.617 1.0061.45 C ATOM 3508 C LEU A 501 -5.480-81.494-47.788 1.0061.59 C ATOM 3509 O LEU A 501 f -6.352-82.220-48.264 1.0061.52 O ATOM 3510 N ASP A 502 ' -4.515-80.952-48.525 1.0061.72 N ATOM 3511 CA ASP A 502 -4.353-81.329-49.919 1.0061.94 C ATOM 3512 CB ASP A 502 -3.736-80.192-50.739 1.0062.06 C ATOM 3513 CG ASP A 502 -2.315-79.857-50.315 1.0062.72 C ATOM 3514 ODl ASP A 502 -1.539-80.784-49.993 1.0063.46 O ATOM 3515 OD2ASPA502 -1.966-78.655-50.326 1.0063.58 O ATOM 3516 C ASP A 502 -3.505-82.590-49.981 1.0061.99 C ATOM 3517 O ASP A 502 -3.095-83.111-48.946 1.0062.07 O ATOM 3518 N ASP A 503 -3.242-83.079-51.188 1.0062.08 N ATOM 3519 CA ASP A 503 -2.516-84.337-51.362 1.0062.21 C ATOM 3520 CB ASP A 503 -2.278-84.611-52.844 1.0062.34 C ATOM 3521 CG ASP A 503 -1.514-83.495-53:525 1.0062.98 C ATOM 3522 ODl ASP A 503 -1.726-82.315-53.165 1.0063.16 O ATOM 3523 OD2ASPA503 -0.703-83.803-54.425 1.0064.06 O ATOM 3524 C ASP A 503 -1.193-84.407-50.593 1.0062.12 C ATOM 3525 O ASP A 503 -0.955-85.360-49.843 1.0062.04 O ATOM 3526 N GLU A 504 -0.337-83.405-50.779 1.0062.02 N ATOM 3527 CA GLU A 504 0.969-83.400-50.126 1.0062.12 C ATOM 3528 CB GLU A 504 1.813 -82.201 -50.574 1.0062.02 ^' C ATOM 3529 CG GLU A 504 1.840-81.992-52.089 1.0062.68 C ATOM 3530 CD GLU A 504 3.004-81.120-52.556 1.0062.81 C ATOM 3531 OEl GLU A 504 2.797-79.905-52.791 1.0063.40 O ATOM 3532 OE2GLUA504 4.130-81.652-52.694 1.0063.95 O ATOM 3533 C GLU A 504 0.793-83.410-48.614 1.0061.85 C ATOM 3534 O. GLU A 504 1.286-84.308-47.927 1.0061.84 O

ATOM 3535 N GLU A 505 0.069-82.420-48.102 1.0061.64 N

ATOM 3536 CA GLU A 505 -0.204-82.340-46.677 1.0061.43 C

ATOM 3537 CB GLU A 505 -1.201-81.228-46.390 1.0061.18 C ATOM 3538 CG GLU A 505 -0.588-79.851-46.381 1.0060.83 C

ATOM 3539 CD_.GLUA505 -1.631-78.753-46.286 1.0060.55 C ATOM 3540 OEl GLU A 505 -2.627-78.807-47.043 1.0060.25 O

ATOM 3541 OE2GLUA505 -1.457-77.832-45.456 1.0060.26 O

ATOM 3542 C GLU A 505 -0.735-83.667-46.149 1.0061.67 C ATOM 3543 O GLU A 505 -0.357-84.106-45.056 1.0061.83 O

ATOM 3544 N PHE A 506 -1.604-84.309-46.927 1.0061.68 N

ATOM 3545 CA PHE A 506 -2.180-85.586-46.521 1.0061.63 C

ATOM 3546 CB PHE A 506 -3.294-86.020-47.474 1.0061.56 C

ATOM 3547 CG PHE A 506 -3.985-87.290-47.056 1.0061.67 C ATOM 3548 CDlPHE A 506 -3.470-88.528-47.414 1.0061.62 C

ATOM 3549 CEl PHE A 506 -4.098-89.695-47.024 1.0061.32 C

ATOM 3550 CZ PHE A 506 -5.257-89.633-46.273 1.0061.44 C

ATOM 3551 CE2PHEA506 -5.781-88.409-45.912 1.0061.14 C

ATOM 3552 CD2PHEA506 -5.147-87.247-46.299 1.0061.51 C ATOM 3553 C PHE A 506 -1.102-86.658-46.443 1.0061.66 C

ATOM 3554 O PHE A 506 -1.048-87.430-45.482 1.0061.70 O

ATOM 3555 N ALAA507 -0.245-86.705-47.458 1.0061.76 N

ATOM 3556 CA ALA A 507 0.876-87.636-47.447 1.0061.66 C

ATOM 3557 CB ALA A 507 1.706-87.488-48.706 1.0061.65 C ATOM 3558 C ALA A 507 1.732-87.405-46.204 1.0061.68 C

ATOM 3559 0 ALAA507 2.156-88.361-45.551 1.0061.70 O

ATOM 3560 N LEU A 508 1.969-86.133-45.878 1.0061.60 N

ATOM .3561 CA LEU A 508 2.695-85.767-44.661 1.0061.54 C

ATOM 3562 CB LEU A 508 2.778-84.247-44.530 1.0061.44 C ATOM 3563 CG LEU A 508 4.018-83.623-43.886 1.0061.08 C

ATOM 3564 CDl LEU A 508 3.712-82.195-43.481 1.0060.85 C

ATOM 3565 CD2LEUA508 4.505-84.417-42.691 1.0060.65 C

ATOM 3566 C LEUA508 1.991-86.346-43.433 1.0061.70 . C

ATOM 3567 O LEU A 508 2.595-87.063-42.621 1.0061.61 O ATOM 3568 N ALA A 509 0.708-86.026-43.301 1.0061.77 N

ATOM 3569 CA ALA A 509 -0.093-86.572-42.221 1.0061.78 C

ATOM 3570 CB ALA A 509 -1.560-86.243-42.434 1.0061.77 C

ATOM 3571 C ALAA509 0.122-88.082-42.115 1.0061.87 O

ATOM 3572 O ALA A 509 0.550-88.585-41.073 1.0061.97 O ATOM 3573 N SER A 510 -0.154-88.798-43.202 1.0061.83 N

ATOM 3574 CA SER A 510 0.004-90.251-43.226 1.0061.95 C

ATOM 3575 CB SER A 510 -0.249-90.793-44.634 1.0062.00 C

ATOM 3576 OG SER A 510 -1.493-90.333-45.135 1.0062.65 O

ATOM 3577 C SER A 510 1.390-90.673-42.748 1.0061.79 C ATOM 3578 O SERA510 1.522-91.562-41.896 1.0061.78 O

ATOM 3579 N HISA511 2.416-90.030-43.304 1.0061.62 N

ATOM 3580 CA HIS A 511 3.793-90.302.-42.913 1.0061.40 C

ATOM 3581 CB HIS A 511 4.758-89.312-43.576 1.0061.24 C

ATOM 3582 CG HIS A 511 6.183-89.470-43.139 1.0060.84 C ATOM 3583 NDl HIS A 511 7.110-90.185-43.867 1.0060.78. N

ATOM 3584 CEl HIS A 511 8.275-90.155-43.244 1.0060.24 C

ATOM 3585 NE2 HIS A 511 8.137 -89.449 -42.136 1.0060.07 N

ATOM 3586 CD2HISA511 6.838-89.009-42.047 1.0060.36 C

ATOM 3587 C HIS A 511 3.906-90,212 -41.404 1.0061,38 C ATOM 3588 O HIS A 511 4.408-91.124-40.751 1.0061.56 O

ATOM 3589 N LEU A 512 3.417-89.109-40.852 1.0061.36 N

ATOM 3590 CA LEU A 512 3.499-88.881-39.419 1.0061.37 C

ATOM 3591 CB LEU A 512 3.011-87.469-39.097 1.0061.22 C ATOM 3592 CG LEU A 512 4.034-86.435-39.573 1.0060.86 C

ATOM 3593 CDl LEU A 512 3.482-85.018-39.516 1.0060.51 • C

ATOM 3594 CD2LEUA512 5.315-86.565-38.760 1.0059.84 C

ATOM 3595 C LEU A 512 2.749-89.938-38.605 1.0061.48 C ATOM 3596 O LEU A 512 3.236-90.422-37.574 1.0061.48 O

ATOM 3597 N ILE A 513 1.571 -90.309- -39.090 1.0061.74 N

ATOM 3598 CA ILE A 513 0.791-91.371-38.468 1.0061.83 C

ATOM 3599 CB ILE A 513 -0.579-91.518-39.155 1.0061.81 C

ATOM 3600 CGl ILE A 513 -1.325-90.181-39.084 1.0061.73 C ATOM 3601 CDl ILE A 513 -2.782-90.257-39.456 1.0062.12 C

ATOM 3602 CG2ILEA513 -1.382-92.645-38.518 1.0061.68 C

ATOM 3603 C ILE A 513 1.554 -92.705 -38.444- 1.0061.89 C

ATOM 3604 O ILE A 513 1.683-93.333-37.391 1.0061.85 O

ATOM 3605 N GLU A 514 2.071-93.124-39.598 1.0061.92 N ATOM 3606 CA GLU A 514 2.911-94317-39.660 1.0062.03 C

ATOM 3607 CB GLU A 514 3.456-94.519-41.069 1.0062.08 C

ATOM 3608 CG GLU A 514 2.396-94.778-42.118 1.0062.83 C

ATOM 3609 CD GLU A 514 2.944-95.511-43.333 1.0063.54 C

ATOM 3610 OEl GLU A 514 3.998-96.181-43.216 1.0063.39 O ATOM 3611 OE2GLUA514 2.310-95.420-44.407 1.0064.11 O

. ATOM 3612 C GLU A 514 4.077-94.201-38.689 1.0062.07 C

ATOM 3613 O GLU A 514 4.345 -95.108 -37.894 1.0062.33 O

ATOM 3614 N ALA A 515 4.775-93.072-38.767 1.0061.99 N

ATOM 3615 CA ALA A 515 5.881-92.794-37.865 1.0061.95 C ATOM 3616 CB ALA A 5.15 6.338-91.346-38.007 1.0061.86 C

ATOM 3617 C ALAA 515 5.477-93.091-36.426 1.0061.91 C

ATOM 3618 O ALA A 515 6.134-93.878-35.746 1.0061.89 O

ATOM 3619 N LYS A 516 4.389-92.472-35.972 1.0061.87 N

ATOM 3620 CA LYS A 516 3.946-92.658-34.592 1.0061.79 C ATOM 3621 CB LYS A 516 2.753-91.760-34.258 1.0061.68 C

ATOM 3622 CG LYS A 516 2.874-91.054-32.915 1.0061.28 C

ATOM 3623 CD LYS A 516 2.859-92.024-31.750 1.0061.20 C

ATOM 3624 CE LYS A 516 3.802-91.567-30.647 1.0061.34 C

ATOM 3625 NZ LYS A 516 3.687-90.108-30.377 1.0061.19 N ATOM 3626 C LYS A 516 3.598-94.113-34.336 1.0061.88 C

ATOM 3627 O LYSA516 3.898-94.645-33.269 1.0062.04 O

ATOM 3628 N LEU A 517 2.975-94.761-35.315 1.0061.97 N

ATOM 3629 CA LEU A 517 2.643-96.176-35.178 1.0062.25 C

* ATOM 3630 CB LEUA 517 1.868-96.690-36.396 1.0062.24 C ATOM 3631 CG LEU A 517 0.436-96.164-36.551 1.0062.30 C

ATOM 3632 CDl LEU A 517 -0.225-96.729-37.800 1.0062.24 C

ATOM 3633 CD2LEUA517 -0.395-96.473-35.313 1.0062.23 C

ATOM 3634 C LEU A 517 3.893-97.019-34.935 1.0062.46 C

ATOM 3635 O LEU A 517 3.871-97.939-34.123 1.0062.42 O ATOM 3636 N- GLU A 518 4:983-96.698-35.628 1.0062.79 N

ATOM 3637 CA GLU A 518 6.252-97.404-35.418 1.0063.31 C

ATOM 3638 CB GLU A 518 7.314-96.944-36.421 1.0063.45 C

ATOM 3639 CG GLU A 518 7.738-98.010-37.419 1.0063.87 C

ATOM 3640 CD GLU A 518 6.782-98.127-38.581 1.0064.37 C ATOM 3641 OEl GLU A 518 6.048-99.135-38.645 1.0064.42 O

• ATOM 3642. OE2 GLU A 518 6.759-97.205-39.426 1.0064.82 O

ATOM 3643 C GLU A 518. 6.799-97.252-34.001 1.0063.54 C

ATOM 3644 O GLU A 518 7.571-98.091-33.532 1.0063.50 O

ATOM 3645 N GLY A 519 6.406-96.175-33.329 1.0063.92 N ATOM 3646 CA GLY A 519 6.916-95.872.-31.995 1.0064.42 C

ATOM 3647 C GLY A 519 7.909 -94.725 -32.008.1.0064.74 C

ATOM 3648 O GLY A 519 9.012-94.834-31.468 1.0064.74 O

ATOM 3649 N HIS A 520 7.513-93.620-32.633 1.0065.16 N ATOM 3650 CA HIS A 520 8.361-92.438-32.716 1.0065.57 C ATOM 3651 CB HIS A 520 8.735-92.143-34.169 1.0065.67 C ATOM 3652 CG HIS A 520 9.840-93,003-34.691 1.0066.10 C ATOM 3653 NDl HIS A 520 11.163-92.796-34.357 1.0066.58 N ATOM 3654 CEl HIS A 520 11.911-93.707-34.955 1.0066.72 C ATOM 3655 NE2HISA520 11.121-94.495-35.666 1.0066.89 N ATOM 3656 CD2HISA520 9.820-94.077-35.517 1.0066.36 C ATOM 3657 C HIS A 520 7.678-91.219-32.126 1.0065.70 C ATOM 3658 O HIS A 520 6.576-90.855-32.538 1.0065.77 O ATOM 3659 N GLY A 521 8.335-90.583-31.163 1.0065.86 N ATOM 3660 CA GLY A 521 7.867-89.296-30.678 1.0066.01 C ATOM 3661 C GLY A 521 7.715-88.376-31.873 1.0066.07 C ATOM^' 3662 O GLY A 521 8.524-88.416-32.802 1.0066.13 O ATOM 3663 N LEU A 522 6.663-87.569-31.874 1.0066.10 ^' N ATOM 3664 CA LEU A 522 6.483-86.582-32.929 1.0066.04 C ATOM 3665 CB LEU A 522 5.019 -86.174 -33.043.1.0066.08 C ATOM 3666 CG LEU A 522 4.179-86.795-34.157 1.0066.47 C ATOM 3667 CDl LEU A 522 4.642-88.202-34.519 1.0066.89 C ATOM 3668 CD2LEUA522 2.724-86.798-33.720 1.0066.94 _. C ATOM 3669 C LEU A 522 7.322-85.351-32.639 1.0065.97 C ATOM 3670 O LEU A 522 7.534-84.999-31.478 1.0065.87 O ATOM 3671 N PRO A 523 7.808-84.690-33.699 1.0065.92 N ATOM 3672 CA PRO A 523 8.473-83.409-33.516 1.0065.84 C ATOM 3673 CB PRO A 523 8.849-82.993-34.943 1.0065.78 C ATOM 3674 CG PRO A 523 8.792 -84.241.-35.750 1.0065.95 ■ C ATOM 3675 CD PRO A 523 7.751 -85.097-35.113 1.0065.96 C ATOM 3676 C PRO A 523 7.476-82.414-32.939 1.0065.77 C ATOM 3677 O PRO A 523 6.272-82.685-32.901 1.0065.97 O ATOM 3678 N THR A 524 7.965-81.272-32.484 1.0065.48 N ATOM 3679 CA THR A 524 7.065-80.238-32.020 1.0065.17 C ATOM 3680 CB THR A 524 7.481-79.717-30.623 1.0065.20 C ATOM 3681 OGl THR A 524 7.177 -78.323 -30.514 1.0065.65 O ATOM 3682 CG2THRA524 8.974-79.937-30.389 1.0065.23 C ATOM 3683 C THR A 524 6.952-79.137-33.084 1.0064.84 C ATOM 3684 O THR A 524 5.974-78.392-33.122 1.0064.93 O ATOM 3685 N ASN A 525 7.946-79.070-33.966 1.0064.41 N ATOM 3686 CA ASN A 525 7.941-78.137-35.095 1.0063.87 C ATOM 3687 CB ASN A 525 8.818-76.920-34.805 1.0063.88 C ATOM 3688 CG ASN A 525 8.167-75.948-33.854 1.0063.78 C ATOM 3689 ODl ASN A 525 8.737-75.603-32.820 1.0063.84 O ATOM 3690 ND2 ASN A 525 6.961-75.502-34.194 1.0063.55 N ATOM 3691 C ASN A 525 8.422-78.805-36.374 1.0063.51 C ATOM 3692 O ASN A 525 9.530-79.340-36.428 1.0063.55 O ATOM 3693 N LEU A 526 7.583-78.761-37.401 1.0062.99 N ATOM 3694 CA LEU A 526 7.882-79.378-38.681 1.0062.43 C ATOM 3695 CB LEU A 526 6.694-79.165-39.615 1.0062.46 C ATOM 3696 CG LEU A 526 6.369-80.239-40.650 1.0062.26 C ATOM 3697 CDl LEU A 526 7.395-80.225-41.753 1.0062.66 C ATOM. 3698 CD2LEUA526 6.303-81.602-39.996 1.0062.13 C ATOM 3699 C LEU A 526 9.146-78.766-39.286 1.0062.24 C

ATOM 3700 O LEU A 526 9.145-77.599-39.674 1.0062.21 O

ATOM 3701 N PRO A 527 10.234-79:554-39.371 1.0061.99 N

. ATOM 3702 CA PRO A 527 11.486-79.062-39.942 1.0061.70 C

ATOM 3703 CB PRO A 527 12.503-80.112-39.495 1.0061.70 C ATOM 3704 CG PRO A 527 11.722-81.364-39.395 1.0061.61 C ATOM 3705 CD PRO A 527 10.340-80.961-38.941 1.0061.99 C ATOM 3706 C PRO A 527 11.417-79.005-41.466 1.0061.51 C ATOM 3707 O PRO A 527 10.651 -79.751 -42.079 1.0061.49 O ATOM 3708 N ARG A 528 12.221-78.133-42.069 1.0061.27 N

ATOM 3709 CA ARG A 528 12.154-77.888-43.510 1.0061.10 C

ATOM 3710 CB ARG A 528 13.334-77.024-43.968 1.0061.10 C

ATOM 3711 CG ARG A 528 13.363-76.776-45.472 1.0061.06 C

ATOM 3712 CD ARG A 528 14.621-76.043-45.903 ϊ .0061.02 C

ATOM 3713 NE ARG A 528 14.650-75.823-47.347 1.0060.86 N

ATOM 3714 CZ ARG A 528 14.282-74.691-47.945 1.0060.65 C

ATOM 3715 NHl ARG A 528 1-4.343-74:592-49.267 1.0060.39 . N

ATOM 3716 NH2ARGA528 13.855-73.658-47.227 1.0060.55 N

ATOM 3717 C ARG A 528 12.091-79.163-44.355 1.0061.02 C

ATOM 3718 O ARG A 528 11.282-79.270-45.277 1.0060.96 O

ATOM 3719 N ARG A 529 12.948-80.125-44.032 1.0060.92 N

ATOM 3720 CA ARG A 529 13.097-81.325-44.848 1.0060.87 C

ATOM 3721 CB ARG A 529 14.249-82.189-44.328 1.0061.05 C

ATOM 3722 CG ARG A 529 14.118-82.565-42.867 1.0061.92 C

ATOM 3723 CD ARG A 529 15.338-83.315-42.367 1.0063.40 C

ATOM 3724 NE ARG A 529 15.130-83.798-41.006 1.0064.56 N

ATOM 3725 CZ ARG A 529 14.453-84.901-40.702 1.0065.44 C

ATOM 3726 NHl ARG A 529 14.311-85.259-39.432 1.0065.89 N

ATOM 3727 NH2 ARG A 529 13.916-85.646-41.665 1.0065.76 N

ATOM 3728 C ARG A 529 11.817 -82.142 -44.925 1.0060.59 C

ATOM 3729 O ARG A 529 11.665-82.979-45.817 1.0060.74 O

ATOM 3730 N LEU A 530 10.901-81.907-43.991 1.0060.16 N

ATOM 3731 CA LEU A 530 9.623-82.605-44.003 1.0059.71 C

ATOM 3732 CB LEU A 530 9.209-83.023-42.591 1.0059.65 C

ATOM 3733 CG LEU A 530 9.701-84.382-42.092 1.0059.14 C

ATOM 3734 CDl LEU A 530 9.103-84.693-40.730 1.0058.59 C

ATOM 3735 CD2LEUA530 9.345-85.472-43.082 1.0058.67 C

ATOM 3736 C LEU A 530 8.520-81.784-44.664 1.0059.56 C

ATOM 3737 O LEU A 530 7.468-82.318-45.009 1.0059.51 O

ATOM 3738 N VALA531 8.756-80.488-44.840 1.0059.45 N

ATOM 3739 CA VAL A 531 7.784-79.637-45.519 1.0059.44 C

ATOM .3740 CB VAL A 531 8.167-78.142-45.438 1.0059.28 C

ATOM 3741 CGl VAL A 531 7.067-77.283-46.024 1.0058.89 C

ATOM 3742 CG2.VALA531 8.443-77.735-44.006 1.0059.32 C

ATOM 3743 C VALA 531 7.685-80.033-46.989 1.0059.61 C

ATOM 3744 O VAL A 531 8.700-80.081-47.685 1.0059.64 O

ATOM 3745 N PRO A 532 6.464-80.329-47.467 1.0059.71 N

ATOM 3746 CA PRO A 532 6.282-80.580-48.891 1.0059.85 C

ATOM 3747 CB PRO A 532 4.776-80.410-49.079 1.0059.82 C

ATOM 3748 CG PRO A 532 . 4.193 -80.816 -47.766 1.0059.65 C

ATOM 3749 CD - PRO A 532 5.203-80.447-46.713 1.0059.60 C

ATOM 3750 C PRO A 532 7.044-79.537-49.707 1.0060.13 C

ATOM 3751 O PRO A 532 7.085-78.370-49.322 1.0060.15 O

ATOM 3752 N PRO A 533 7.648-79.960-50.829 1.0060.38 N

ATOM 3753 CA . PRO A 533 8.535-79.145-51.659 1.0060;52 C

ATOM 3754 CB PRO A 533 8.659-79.971-52.938 1.0060.55 C

ATOM 3755 CG PRO A 533 8.543-81.366-52.458 1.0060.51 C

ATOM 3756 CD PRO A 533 7.498-81.321-51.373 1.0060.41 C

ATOM 3757 C PRO A 533 8.031-77.729-51.965 1.0060.72 C

ATOM 3758 O PRO A 533 8.842-76.825-52.156 1.0060.82 O

ATOM 3759 N SER A 534 6.717-77.532-52.022 1.0061.01 N

ATOM 3760 CA . SER A 534 6.176-76.176-52.028 1.0061.33 C

ATOM 3761 CB SER A 534 4.719-76.179-52.469 1.0061.27 C

ATOM 3762 OG f SER A 534 4.535-77.089-53.541 1.0061.06 O

ATOM 3763 C SER A 534 6.320-75.634-50.606 1.0061.73 C

ATOM 3764 O SER A 534 5.342 -75.532 -49.849 1.0061.49 O

ATOM 3765 N LYS A 535 7.561 -75.302-50.248 1.0062.26 N ATOM 3766 CA LYS A 535 7.909-75.061-48.849 1.0062.66 C ATOM 3767 CB LYS A 535 9.019-76.020-48.362 1.0062.74 ^• C ATOM 3768 CG LYS A 535 10.263-76.121-49.239 1.0062.63 C ATOM 3769 CD LYS A 535 11.276-77.127-48.668 1.0062.53 C ATOM 3770 CE LYS A 535 10.889-78.574-48.974 1.0062.10 C ATOM 3771 NZ LYS A 535 11.955-79.555-48.612 1.0061.50 N ATOM 3772 C LYS A 535 8.221-73.624-48.467 1.0062.89 C ATOM 3773 O LYS A 535 7.423-73.007-47.763 1.0063.20 O ATOM 3774 N ARG A 536 9.356-73.086-48.915 1.0062.87 N ATOM 3775 CA ARGA.536 9.820-71.790-48.411 1.0062.96 C ATOM 3776 CB ARG A 536 10.355-71.935-46.981 1.0063.00 C ATOM 3777 CG ARG A 536 9.589-71.160-45.920 1.0062.88 C ATOM 3778 CD ARG A 536 10.104-69.730-45.785 1.0062.78 C ATOM 3779 NE ARG A 536 9.513-69.039-44.637 1.0062.80 N ATOM 3780 CZ ARG A 536 9.662-67.741-44.378 1.0062.71 C ATOM 3781 NHl ARG A 536 9.085-67.202-43.312 1.0062.64 N ATOM 3782 NH2 ARG A 536 10.385-66.977-45.186 1.0062.73 N ATOM 3783 C ARG A 536 10.907-71.172-49.261 1.0063.09 C ATOM 3784 O ARG A 536 12.064-71.595-49.195 1.0063.09 O ATOM 3785 N ARG A 537 10.536-70.154-50.040 1.0063.37 N ATOM 3786 CA ARG A 537 11.507-69.382-50.808 1.0063.60 C ATOM 3787 CB ARG A 537 10.803-68.242-51.556 1.0063.66 C ATOM 3788 CG ARG A 537 11.370-67.921-52.949 1.0064.02 C ATOM 3789 CD ARG A 537 12.815-67.398-52.901 1.0064.23 C ATOM 3790 NE ARG A 537 13.276-66.952-54.216 1.0064.87 N ATOM 3791 CZ ARG A 537 13.586-65.692-54.516 1.0065.30 C ATOM 3792 NHl ARG A 537 13.493-64.746-53.591 1.0065.61 N ATOM 3793 NH2ARGA537 13.998-65.373-55.739 1.0064.97 N ATOM 3794 C ARG A 537 12.530 -68.816 -49.820 1.0063.69 C ATOM 3795 O ARG A 537 12.202-68.553-48.657 1.0063.76 O ATOM 3796 N GLN A 538 13.766-68.641-50.275 1.0063.75 N ATOM 3797 CA GLN A 538 14.834-68.177-49.394 1.0063.87 C ATOM 3798 CB GLN A 538 15.457-69.363-48.658 1.0063.84 C ATOM 3799 CG GLN A 538 15.906-70.488-49.582 1.0063.92 C ATOM 3800 CD GLN A 538 16.296-71.738-48.817 1.0064.01 C ATOM 3801 OEl GLN A 538 16.303-71.751-47.584 1.0064.15 O ATOM 3802 NE2 GLN A 538 16.622-72.802-49.545 1.0064.37 N ATOM 3803 C GLN A 538 15.909-67.416-50.160 1.0063.88 C ^■ ATOM 3804 O GLNA 538 17.043-67.243-49.647 1.0063.92 O. ATOM 3805 O2AANPA600 11.527-56.574 -1.805 1.0048.61 O ATOM 3806 PA ANP A 600 11.448-57.106 -3.213 1.0048.08 P ATOM 3807 O1AANPA600 12.590-57.937 -3.742 1.0048.41 O ATOM 3808 O3AANPA600 11.221-55.854 -4.189 1.0049.01 O ATOM 3809 PB ANP A 600 11.878-54.443 -3.787 1.0049.55 P ATOM 3810 O1B ANP A 600 12.072-53.654 -5.058 1.0049.44 ■ O ATOM 3811 O2BANPA600 13.088-54.721 -2.926 1.0049.32 O ATOM 3812 N3BANPA600 10.688-53.641 -2.803 1.0049.69 N ATOM 3813 PG ANP A 600 11.161 -52.172 -2.006 1.0050.29 P ATOM 3814 O3GANPA600 11.033-51.114 -3.076 1.0050.68 O ATOM 3815 O2GANPA600 10.150-52.031 -0.893 1.0050.99 O ATOM 3816 O1GANPA600 12.579-52.435 -1.551 1.0049.88 O ATOM 3817 O5* ANP A 600 10.094-57.950 -3.373 1.0048.33 O ATOM 3818 C5* ANP A 600 9.065-57.592 -4.286 1.0049.10 C ATOM 3819 C4* ANP A 600 7.956 -58.626 -4.134.1.0050.21 C ATOM 3820 C3* ANP A 600 8.309-59.661 -3.080 1.0050.31 C ATOM 3821 03* ANP A 600 7.105-60.157 -2.491 1.0050.26 O ATOM 3822 C2* ANP A 600 8.963-60.782 -3.853 1.0050.21 C ATOM 3823 O2* ANP A 600 8.705-62.044 -3.239 1.0050.10 O ATOM 3824 Cl* ANP A 600 8.291 -60.692 -5.208 1.0050.66 C ATOM 3825 04* ANP A 600 7.807-59.354 -5.353 1.0050.80 O ATOM 3826 N9 ANP A 600 9.253-60.938 -6.296 1.0050.73 N ATOM 3827 C4 ANP A 600 8.946-61.536 -7.443 1.0050.52 C ATOM 3828 C5 ANP A 600 10.180-61.565 -8.228 1.0050.67 C ATOM 3829 N7 ANP A 600 11.130-60.971 -7.480 1.0051.15 N ATOM 3830 C8 ANP A 600 10.552-60.592 -6.309 1.0050.79 C ATOM 3831 N3 ANP A 600 7.823-62.071 -7.962 1.0050.46 N ATOM 3832 C2 ANP A 600 7.828-62.625 -9.184 1.0050.75 C ATOM 3833 Nl ANP A 600. 8.920-62.692 -9.963 1.0050.79 N ATOM 3834 C6 ANP A 600 10.108-62.188 -9.564 1.0050.80 C ATOM 3835 N6 ANP A 600 11.205 -62.253 -10.3561.0050.98 N ATOM 3836 MG MG A 700 13.847-53.618 -0.877 1.0049.55 MG ATOM 3837 CA CA A 701 -4.087-77.142-45.879 LOO 46.71 CA ATOM 1 N ARGB 19 -35.864-44.695-40.362 1.0058.79 N ATOM 2 CA ARGB 19 -36.349-44.622-38.954 1.0058.86 C ATOM 3 CB ARGB 19 -37.709-45.314-38.819 1.0058.86 C ATOM 4 CG ARGB 19 -37.648-46.838-38.872 1.0059.05 C ATOM 5 CD ARGB 19 -39.035-47.464-38.760 1.0059.14 C ATOM 6 NE ARGB 19 -39.799-46.949-37.622 1.0059.75 N- ATOM 7 CZ ARGB 19 -40.800-46.076-37.722 1.0059.95 . C ATOM 8 NHlARGB 19 -41.169-45.613-38.911 1.0060.07 N ATOM 9 NH2ARGB 19 -41.437-45.665-36.631 1.0059.86 N ATOM 10 C ARGB 19 -35.335-45.249-37.999 1.0058.73 C ATOM 11 O ARGB 19 -35.582-45.372-36.800 1.0058.69 O ATOM 1 N THRB 20 -34.188-45.636-38.545 1.0058.62 N ATOM 2 CA THRB 20 -33.114-46.223-37.751 1.0058.46 C ATOM 3 CB THRB 20. -32.290-47.226-38.581 1.0058.50 C ATOM 4 OGlTHRB 20 -31.604-46.534-39.634 1.0058.37 O ATOM 5 CG2THRB 20 -33.199-48.292-39.178 1.0058.59 C ATOM 6 C THRB 20 -32.180-45.152-37.186 1.0058.32 C ATOM 7 O THRB 20 -32.520-43.965-37.165 1.0058.25 O ATOM 1 N VALB 21 -31.000-45.579-36.740 1.0058.12 N ATOM 2 CA VALB 21 -30.048 -44.683 -36.083 1.0057.89 C ATOM 3 CB VALB 21 -29.111-45.447-35.127 1.0057.93 C ATOM 4 CGlVALB 21 -28.124-46.293-35.915 1.0058.17 C ATOM 5 CG2VALB 21 -28.372-44.474-34.220 1.0057.98 C ATOM 6 C VALB 21 -29.212-43.859-37.066 1.0057.68 C ATOM 7 O VALB 21 -29.074-42.644-36.900 1.0057.39 O ATOM 1 N THRB 22 -28.652-44.511-38.082 1.0057.46 N ATOM 2 CA THRB 22 -27.859-43.792-39.077 1.0057.30 C ATOM 3 CB THRB 22 -27.161-44.740-40.090 1.0057.27 C ATOM 4 OGlTHRB 22 -28.023-44.987-41.207 1.0057.51 O ATOM 5 CG2THRB 22 -26.780-46.062-39.430 1.0057.23 C ATOM 6 C THRB 22 -28.755-42.784-39.798 1.0057.11 C ATOM 7 O THRB 22 -28.337-41.669-40.100 1.0057.00 O ATOM 1 N SERB 23 -29.994-43.183-40.059 1.0056.93 N ATOM 2 CA SERB 23 -31.000-42.275-40.586 1.0056.79 C ATOM 3 CB SERB 23 -32.349-42.985-40.618 1.0056.78 C ATOM 4 OG SERB 23 -33.311-42.263-39.874 1.0057.00 O ATOM 5 C SERB 23 -31.094-41.016-39.728 1.0056.73 C ATOM 6 O SERB 23 -31.004-39.884-40.230 1.0056.72 O ATOM 1 N SERB 24 -31.268-41.227-38.427 1.0056.67 N ATOM. 2 CA SERB 24 -31.384-40.135-37.468 1.0056.66 C ATOM 3 CB SERB 24 -31.630-40.691-36.065 1.0056.64 C ATOM 4 OG SERB 24 -32.318-39.753-35.257 1.0056.92 O ATOM 5 C SERB 24 -30.129-39.262-37.495 1.0056.55 C ATOM 6 O SERB 24 -30.210-38.031-37.511 1.0056.41 O ATOM 1 N LEUB 25 -28.971-39.911-37.510 1.0056.64 N

ATOM 2 CA LEUB 25 -27.708-39.213-37.709 1.0056.46 C

ATOM 3 CB LEUB 25 -26.567-40.216-37.867 1.0056.37 C

ATOM 4 CG LEUB 25 -25.705-40.508-36.643 1.0056.13 C

ATOM 5 CDlLEUB 25 -26.483-40.290-35.370 1.0055.71 C

ATOM 6 GD2LEU.B 25 -25.157-41.923-36.717 1.0056.30 C

ATOM 7 C LEUB 25 -27.771-38.320-38.943 1.0056.49 C

ATOM 8 O LEUB 25 -27.389-37.148-38.894 1.0056.42 O

ATOM 1 N LYSB 26 -28.252-38.883-40.048 1.0056.45 N

ATOM 2 CA LYS B 26 -28.317-38.164-41.308 1.0056.29 C

ATOM 3 CB LYSB 26 -28.822-39.079-42.427 1.0056.32 C

ATOM 4 CG LYSB 26 -28.800-38.454-43.819 1.0056.35 C

ATOM 5 CD LYSB 26 -28.778-39.516-44.917 1.0056.35 C

ATOM 6 CE LYS B 26 -30.038-40.371-44.910 1.0056.39 C

ATOM 7 NZ LYS B 26 -29.907-41.557-45.803 1.0056.13- N

ATOM 8 C LYS B 26 -29.190-36.924-41.168 1^".OO 56.32 C

ATOM 9 O LYSB 26 -28.764-35.817-41.516 1.0056.34 O

ATOM 1 N GLUB 27 -30.401-37.093-40.641 1.0056.37 N

ATOM 2 CA GLUB 27 -31.264-35.927-40.433 1.0056.31 C

ATOM 3 CB GLUB 27 -32.635-36.332-39.894 1.0056.40 C

ATOM 4 CG GLUB 27 -33.618-36.769-40.976 1.0056.99 C

ATOM 5 CD GLUB 27 -33.694-35.789-42.142 1.0057.43 C

ATOM 6 OElGLUB 27 -32.665-35.604-42.834 1.0057.97 O

ATOM 7 OE2GLUB 27 -34.785-35.218-42.379 1.0056.59 O- ATOM 8 C GLUB 27 -30.610-34.886-39.526 1.0056.16 C

ATOM 9 O GLUB 27 -30.594 -33.691 -39.844 1.0055.99 O

ATOM 1 N LEUB 28 -30.063-35.352-38.405 1.0056.19 N

ATOM 2 CA LEUB 28 -29.327-34.483-37.489 1.0056.04 C

ATOM 3 CB LEUB 28 -28.656-35.295-36.378 1.0055.97 C

ATOM 4 CG LEUB 28 -29.364-35.366-35.022 1.0056.13 C

ATOM 5 CDlLEUB 28 -30.854-35.712-35.137 1.0056.25 C

ATOM 6 CD2LEUB 28 -28.644-36.321-34.084 1.0056.01 C

ATOM 7 C LEUB 28 -28.287-33.671-38.241 1.0056.00 C

ATOM 8 O LEUB 28 -28.236-32.450-38.116 1.0056.01 O

ATOM 1 N TYRB 29 -27.461-34353-39.026 1.0055.97 N

ATOM 2 CA TYRB 29 -26.478-33.671-39.848 1.0055.76 C

ATOM 3 CB TYRB 29 -25.722-34.659-40.731 1.0055.53 C

ATOM 4 CG TYRB 29 -24.819-33.982-41.733 1.0055.13 C

ATOM 5 CDlTYRB 29 -23.669-33.320-41.323 1.0054.84 C

ATOM 6 CEl TYR B 29 -22.840-32.696-42.234 1.0054.64 C

ATOM 7 CZ TYRB 29 -23.157-32.729-43.574 1.0054.85 C

ATOM 8 OH TYRB 29 -22.339-32.111 -44.487 1.0055.02 O

ATOM 9 CE2TYRB 29 -24.291-33.381-44.008 1.0054.94 C

ATOM 10 CD2TYRB 29 -25.117-34.000-43.087 1.0054.98 C

ATOM 11 C TYRB 29 -27.140-32.618-40.720 1.0055.90 C

ATOM 12 O TYRB 29 -26.828-31.432-40.611 1.0055.94 O

ATOM 1 N ARGB 30 -28.065-33.056-41.572 1.0056.07 N

ATOM 2 CA ARG B 30 -28.661-32.167-42.566 1.0056.16 C

ATOM 3 CB ARGB 30 -29.655-32,915-43.458 1.0056.13 C

ATOM . 4 CG ARGB 30 -30.281-32.027-44.534 1.0056.57 C

ATOM 5 CD ARGB 30 -31.444-32.704-45.244 1.0056.62 C

ATOM 6 NE ARG B 30 -32.497-33.102-44.313 1.0057.56 N

ATOM 7 CZ ARG B 30 -33.525-32:334-43.968 1.0057.96 C

ATOM 8 NHl ARG B 30 -33.650-31.115-44.479 1.0058.09 N

ATOM 9 NH2ARGB 30 -34.433-32.785-43.112 1.0058.17 N

ATOM 10 C ARGB 30 -29.336-30.945-41.958 1.0056.07 C

ATOM 11 O ARGB 30 -29.309-29.864-42.544 1.0056.10 O

ATOM 1 N THRB 31 -29.938-31.104-40.786 1.0056.02 N ATOM 2 CA THRB 31 -30.686-29.999-40.194 1.0055.94 C

ATOM 3 CB THRB 31 -31.968-30.495-39.510 1.0055.94 C

ATOM 4 OGlTHRB 31 -31.627-31.427-38.476 1.0056.01 O

ATOM 5 CG2THRB 31 -32.879-31.172-40.522 1.0055.91 C

ATOM 6 C THRB 31 -29.878-29.166-39.196 1.0055.97 C

ATOM 7 O THRB 31 -30.158-27.982-39.000 1.0055.91 O

ATOM 1 N LYSB 32 -28.877-29.780-38.572 1.0056.00 N

ATOM 2 CA LYS B 32 -28.160-29.137-37.469 1.0056.02 C

ATOM 3 CB LYSB 32 -28.201-30.019-36.210 LOO 56.03 C

ATOM 4 CG LYS B.32 -29.582-30.162-35.544 1.0056.05 C

ATOM 5 CD LYSB 32 -29.920-28.956-34.665 1.0056.16 C

ATOM 6 CE LYSB 32 -31.272-29.099-33.959 1.0055.96 C

ATOM 7 NZ LYSB 32 -31.193-29.805-32.646 1.0055.50 N

ATOM 8 C LYSB 32 -26.711-28.750-37.796 1.0056.03 C

ATOM 9 O LYS B 32. -26.168-27.819-37.200 1.0056.12 O

ATOM 1 N LEUB 33 -26.087-29.460-38.734 1.0055.98 N

ATOM 2 CA LEUB 33 -24.682-29.209-39.069 1.0055.83 C

ATOM ^■ 3 CB LEUB 33 -23.881-30.508-39.031 1.0055.81 C

ATOM 4 CG LEUB 33 -22.853-30.636-37.915 1.0055.96 C

ATOM 5 CDlLEUB 33 -22.175-31.991-37.990 1.0056.34 C

ATOM 6 CD2LEUB 33 -21.830-29.526-38.036 1.0056.25 C

ATOM 7 C LEUB 33 -24.496-28.553-40.428 1.0055.75 C

ATOM 8 O LEUB 33 -23.834-27.521-40.551 1.0055.70 O

ATOM 1 N LEUB 34 -25.081-29.171-41.448 1.0055.70 N

ATOM 2 CA LEUB 34 -24.952-28.699-42.817 1.0055.64 C

ATOM 3 CB LEUB 34 -25.927-29.447-43.729 1.0055.58 C

ATOM 4 CG LEUB 34 -25.827-29.178-45.229 1.0055.53 C

ATOM 5 CDlLEUB 34 -24.377-29.201-45.688 1.0055.57 C

ATOM 6 CD2LEUB 34 -26.656-30.193-46.001 1.0055.60 C

ATOM 7 C LEUB 34 -25.138-27.189-42.948 1.0055.74 C

ATOM 8 O LEUB 34 -24.368-26.536-43.652 1.0055.74 O,

ATOM 1 N PROB 35 -26.158-26.624-42.272 1.0055.81 N

ATOM 2 CA PRO B 35 -26.387-25.187-42.397 1.0055.89 C

ATOM 3 CB PROB 35 -27.570-24.935-41.457 1.0055.71 C

ATOM 4 CG PROB 35 -28.242-26.244-41.333 1.0055.71 C

ATOM 5 CD PROB 35 -27.147-27.256-41.381 1.0055.76 C

ATOM 6 C PROB 35 -25.183-24.372-41.948 1.0056.06 C

ATOM 7 O PROB 35 -24.884-23.339-42.542 1.0056.11 O

ATOM 1 N LEUB 36 -24.496 -24.843 -40.914 1.0056.32 N

ATOM 2 CA LEUB 36 -23.376-24.111-40.338 1.0056.60 C

ATOM 3 CB LEUB 36 -23.087-24.654-38.947 1.0056.61 C

ATOM 4 CG LEUB 36 -22.594-23.658-37.905 1.0056.89 C

ATOM 5 CDlLEUB 36 -23.153-24.031-36.552 1.0057.25 C

ATOM 6 CD2LEUB 36 -21.082-23.624-37.872 1.0057.53 C

ATOM 7 G LEUB 36 -22.148-24.229-41.237 1.0056.79 C

ATOM 8 O LEUB 36 -21.443-23.237-41.507 1.0056.95 O

ATOM 1 N GLUB 37 -21.913-25.448-41.712 1.0057.00 N

ATOM 2 CA GLUB 37 -20.879-25.705-42.703 1.0057.34 C

ATOM 3 CB GLUB 37 -20.912-27.168-43.151 1.0057.32 C

ATOM 4 CG GLUB 37 -20.568-28.182-42.074 1.0057.49 C

ATOM 5 CD GLUB 37 -20.509-29.602-42.617 1.0057.48 C

ATOM 6 OElGLUB 37 -20.434-29.763-43.857 1.0057.98 O

ATOM 7 0E2GLUB 37 -20.535-30.557-41.810 1.0057.15 O

ATOM 8 C GLUB 37 -21.050-24.800-43.925 1.0057.50 C

ATOM 9 O GLUB 37 -20.095-24.154-44.366 1.0057.53 O

ATOM 1 N GLUB 38 -22.267-24.760-44.466 1.0057.64 N

ATOM 2 CA GLUB 38 -22.544-23.989-45.677 1.0057.92 C

ATOM 3 CB GLUB 38 -23.939-24.302-46.222 1.0058.10 C ATOM 4 CG GLUB 38 -24.052-25.674-46.868 1.0059.87 C

ATOM 5 CD GLUB 38 -23.318-25.767-48.201 1.0062.05 C

ATOM 6 OElGLUB 38 -23.851-25.231-49.205 1.0062.81 O

ATOM 7 OE2GLUB 38 -22.219-26.384-48.245 1.0062.50 O

ATOM 8 C GLUB : 38 -22.401 -22.498 -45.442 1.0057.70 C

ATOM 9 O GLUB : 38 -21.934-21.771-46.316 1.0057.74 O

ATOM 1 N HISB 39 ■ ■22.798-22.045-44.259 1.0057.50 N

ATOM 2 CA HIS B : 39 -22.740-20.627-43.951 1.0057.36 C

ATOM .3 CB HISB : 39 -23.553-20.289-42.697 1.0057.49 C

ATOM 4 CG HISB : 39 -23.914 -18.837 -42.582 1.0057.86 C

ATOM 5 NDlHISB 39 -23.802-18.130-41.403 1.0058.15 N

ATOM 6 CEl HIS B 39 -24.187-16.882-41.600 1.0057.80 C

ATOM 7 NE2 HIS B 39 -24.540-16.751-42.866 1.0058.12 N

ATOM 8 CD2 HIS B 39 -24.379-17.959-43.502 1.0057.91 C

ATOM 9 C HISB 39 ■ •21.301-20.174-43.795 1.0057.12 C

ATOM 10 O HISB 39 . -20.915 -19.146 -44.341 ^• 1.0057.14 O

ATOM 1 N TYRB - W -20.494-20.938-43.068 1.0056.95 N

ATOM 2 CA TYRB 40 -19.110-20.504-42.885 1.0056.80 C

ATOM 3 CB TYRB 40 -18.683-20.668-41.432 1.0056.68 C

ATOM 4 CG TYRB 40 -19.505-19.812-40.501 1.0056.39 C

ATOM 5 CDlTYRB 40 -19.178-18.482-40.284 1.0056.19 C

ATOM 6 CElTYRB 40 -19.929-17.692-39.445 1.0056.13 C

ATOM 7 CZ TYRB 40 -21.032-18.227-38.811 1.0056.27 C

ATOM 8 OH TYRB 40 -21.788-17.435-37.973 1.0056.35 O

ATOM 9 CE2TYRB 40 -21.384-19.546-39.017 1.0055.86 C .

ATOM 10 CD2TYRB 40 -20.624-20.327-39.858 1.0056.00 C

ATOM 11 C TYRB 40 -18.132-21.152-43.868 1.0056.98 C

ATOM 12 O TYRB 40 -16.916-21.131-43.664 1.0056.80 O

ATOM 1 N ARGB 41 -18.685-21.710-44.943 1.0057.29 N

ATOM 2 CA ARGB 41 -17.902-22.199-46.082 1.0057.67 C

ATOM 3 CB ARGB 41 -17.259-21.025-46.827 1.0057.84 C

ATOM 4 CG ARGB 41 -18.247-20.264-47.691 1.0059.24 C

ATOM 5 CD ARGB 41 -18.706-21.140-48.847 1.0061.74 C

ATOM 6 NE ARGB 41 -20.154-21.097-49.031 1.0063.78 N

ATOM 7 CZ ARGB 41 -20.869-22.080-49.574 1.0065.07 C

ATOM 8 NHl ARG E \ 41 -22.184-21.953-49.699 1.0065.94 N

ATOM 9 NH2ARGB 41 -20.275-23.194-49.988 1.0065.68 N

ATOM 10 C ARGB 41 -16.862-23.250-45.704 1.0057.59 C

ATOM 11 O ARGB 41 -15.745-23.266-46.227 1.0057.63 O

ATOM 1 N PHEB ' \2 -17.261 -24.135 -44.798 1.0057.42 N .

ATOM 2 CA PHEB 42 -16.440-25.247-44.347 1.0057.25 C

ATOM 3 CB PHEB 42 -17.303-26.170-43.483 1.0057.11 C

ATOM 4 CG PHEB 42 -16.533-27.222-42.751 1.0056.65 C

ATOM 5 CDlPHEB 42 -16.541-28.533-43.191 1.0056.29 C

ATOM 6 CElPHEB 42 -15.840-29.506-42.518 1.0056.21 C

ATOM 7 CZ PHEB 42 -15.123-29.177-41.385 1.0056.63 C

ATOM 8 CE2PHEB 42 -15.111-27.873-40.931 1.0056.58 C

ATOM 9 CD2PHEB 42 -15.815 -26.905 -41.612 1.0056.58 C

ATOM 10 C PHEB 42 -15.866-26.027-45.525 1.0057.37 C

ATOM 11 O PHEB 42 -14.740-26.520-45.469 1.0057.37 O

ATOM 1 N GLYB 43 -16.649-26.124-46.595 1.0057.54 N

ATOM 2 CA GLYB 43 -16.295-26.943-47.750 1.0057.71 C

ATOM 3 C GLYB 43 -15.092-26.473-48.545 1.0057.88 C

ATOM 4- O GLYB 43 -14.552-27.222-49.358 1.0058.01 O

ATOM 1 N SERB ' -14.671-25.234-48.320 1.0057.99 N

ATOM 2 CA SERB 44 -13.537 -24.680 -49.045 1.0058.04 C

ATOM 3 CB SERB 44 -13.877-23.298-49.588 1.0057.99 C

ATOM 4 OG SERB 44 -15.092-23.328-50.315 1.0058.35 O ATOM 5 C SERB 44 -12.324-24.589-48.144 1.0058.15 C

ATOM 6 O SERB 44 -11.338-23.930-48.482 1.0058.23 O

ATOM 1 N PHEB 45 -12.400-25.257-46.996 1.0058.23 N

ATOM 2 CA PHEB 45 -11.345-25.183-45.995 1.0058.33 C

ATOM 3 CB PHEB 45 -11.770-24.285-44.832 1.0058.38 C

ATOM 4 CG PHEB 45 -11.611-22.817-45.101 1.0058.62 C

ATOM 5 CDlPHEB 45 -10.373-22.207-44.984 1.0058.76 C

ATOM 6 CEl PHE B 45 -10.225-20.851-45.226 1.0058.85 C

ATOM 7 CZ PHEB 45 -11.322-20.087-45.582 1.0058.65 C

ATOM 8 CE2PHEB 45 -12.563-20.681-45.694 1.0058.80 C

ATOM 9 CD2PHEB 45 -12.705-22.039-45.454 1.0058.92 C

ATOM 10 C PHEB 45 -10.947-26.549-45.451 1.0058.40 C

ATOM 11 O PHE B 45 -9.769-26.809-45.230 1.0058.46 O

ATOM 1 N HISB 46 -11.924-27.415-45.214 1.0058.47 N

ATOM 2 CA HIS B 46 -11.635-28.696-44.585 1.0058.57 C

ATOM 3 CB HISB 46 -12.053-28.677-43.118 1.0058.52 C

ATOM 4 CG HISB 46 -11.512-27.510-42.357 1.0058.40 ^" C

ATOM 5 NDl HIS B 46 -10.256 -27.510 -41.790 1.0058.69 . N ,

ATOM 6 CEl HIS B 46 -10.047-26.351-41.191 1.0058.73 C

ATOM 7 NE2HISB 46 -11.122-25.599-41.351 1.0058.60 N

ATOM 8 CD2HISB 46 -12.053-26.301-42.077 1.0058.47 C

ATOM 9 C HISB 46 -12.304-29.851-45.306 1.0058.82 C

ATOM 10 O HISB 46 -11.631-30.724-45.842 1.0058.94 O

ATOM 1 N SERB 47 -13.630-29.859-45.322 1.0059.14 N

ATOM 2 CA SERB 47 -14.356-30.936-45.976 1.0059.57 C

ATOM 3 CB SERB 47 -14.756-32.001-44.959 1.0059.49 C

ATOM 4 OG SERB 47 -13.754-32.992-44.853 1.0059.64 O

ATOM 5 C SERB 47 -15.589-30.454-46.723 1.0059.92 C

ATOM 6 O SERB 47 -16.299-29.566-46.251 1.0060.08 O

ATOM 1 N PROB 48 -15.848-31.043-47.899 1.0060.20 N

ATOM 2 CA PRO B 48 -17.079-30.774-48.629 1.0060.54 C

ATOM 3 CB PROB 48 -16.850-31.470-49.967 1.0060.46 C

ATOM 4 CG PROB 48 -15.873-32.544-49.664 1.0060.43 C

ATOlfϊ 5 CD PROB 48 -14.983-32.004-48.600 1.0060.14 C

ATOM 6 C PROB 48 -18.249-31.409-47.892 1.0060.95 C

ATOM 7 O PROB 48 -18.037-32.221-46.990 1.0061.07 O

ATOM 1 N ALAB 49 -19.470-31.039-48.259 1.0061.39 - N

ATOM 2 CA ALAB 49 -20.649-31.565-47.577 1.0061.81 C

ATOM 3 CB ALAB 49 -21.887-30.779-47.964 1.0061.89 C

ATOM 4 C ALAB 49 -20.841-33.046-47.872 1.0062.05 C

ATOM 5 O ALAB 49 -20.542-33.508-48.969 1.0061.90 O

ATOM 1 N LEUB 50 -21.346-33.778-46.884 1.0062.63 N

ATOM 2 CA LEUB 50 -21.517-35.224-46.983 1.0063.26 C

ATOM 3 CB LEUB 50 -21.669-35.826-45.582 1.0063.16 C

ATOM 4 CG LEUB 50 -20.604-35.424-44.553 1.0063.07 C

ATOM 5 CDlLEUB 50 -19.233-35.875-45.010 1.0063.12 C

ATOM 6 CD2LEUB 50 -20.910-35.978-43.166 1.0062.96 C

ATOM 7 C LEUB 50 -22.713-35.607-47.863 1.0063.95 C

ATOM 8 O LEUB 50 -23.639-34.817-48.047 1.0064.09 O

ATOM 1 N GLUB 51 -22.681-36.820-48.414 1.0064.70 N

ATOM 2 CA GLUB 51 -23.796-37.346-49.200 1.0065.43 C

ATOM 3 CB GLUB 51 -23.280-37.991-50.482 1.0065.54 C

ATOM 4 CG GLUB 51 -22.076-37.302-51.095 1.0066.38 C

ATOM 5 CD GLUB 51 -21.147-38.289-51.777 1.0067.59 C

ATOM 6 OElGLUB 51 -20.943-39.386-51.212 1.0068.33 O

ATOM 7 OE2GLUB 51 -20.620-37.976-52.870 1.0068.07 O

ATOM 8 C GLUB 51 -24.526-38.398-48.373 1.0065.74 C

ATOM 9 O GLUB 51 -24.216-38.592-47.201 1.0065.83 O ATOM 1 N ASPB 52 . -25.489-39.086-48.977 1.0066.11 N

ATOM 2 CA ASP B 52 -26.114-40.222-48.312 1.0066.50 C

ATOM 3 CB ASPB 52 -27.461-40.543-48.947 1.0066.58 C

ATOM 4 CG ASP B 52 -28.508-39.495-48.641 1.0067.19 C

ATOM 5 ODl ASP B 52 -28.132-38.386-48.194 1.0067.73 O

ATOM 6 OD2 ASP B 52 -29.710-39.782-48.843 1.0067.86 O

ATOM 7 C ASPB 52 -25.187-41.420-48.418 1.0066.69 C

ATOM 8 O ASPB i 52 -25.273-42.377-47.638 1.0066.73 O

ATOM 1 N ALAB 53 -24.283-41.341-49.388 1.0066.92 N

ATOM 2 CA ALAB 53 -23.378-42.436-49.699 1.0067.19 C

ATOM 3 CB ALAB 53 -22.599-42.128-50.969 1.0067.25 C

ATOM 4 C ALAB ; 53 -22.430-42.772-48:552 1.0067.26 C

ATOM 5 O ALAB 53 -22.050-43.926-48.380 1.0067.24 O

ATOM 1 N ASPB i 54 -22.043-41.771-47.770 1.0067.45 N

ATOM 2 CA ASP B 54 -21.163 -42.028 -46.632 1.0067.74 C

ATOM ^'3 CB ASPB 54 ■ -20.141 -40.899 -46.416 1.0067.90 C

ATOM 4 CG ASP B 54- -20.661-39.544-46.847 1.0068.67 C

ATOM 5 ODl ASP B 54 -21.898-39.378-46.913 1.0069.79 O

ATOM 6 OD2 ASP B 54 -19.833-38.646-47.125 1.0069.03 O

ATOM 7 C ASPB 54 -21.958-42.329-45.363 .1.0067.62 C

ATOM 8 O ASPB . ' 54 -21.400^' -42.378 -44.265 1.0067.85 O

ATOM 1 N PHEB ; 55 -23.262-42.532-45.530 1.0067.33 N

ATOM 2 CA PHEB 55 -24.116-42.994-44.441 1.0067.04 C

ATOM 3 CB PHEB 55 .-25.306-42.056-44.244 1.0067.01 C

ATOM 4 CG PHEB 55 -24.948-40.743-43.624 1.0066.79 C

ATOM 5 CDlPHEB .55 -24.578-39.670-44.412 1.0066.59 C

ATOM 6 CEl PHE B ^■55 -24.254-38.459-43.846 1.0066.30 C

ATOM 7 CZ PHEB 55 -24.300-38.306-42.480 1.0066.49 C

ATOM 8 CE2PHEB 55 -24.671 -39.366 -41.683 1.0066.62 C

ATOM 9 CD2PHEB 55 -24.995-40.576-42.255 1.0066.65 C

ATOM 10 C PHEB 55 -24.636-44.396-44.732 1.0066.92 C

ATOM 11 O PHEB 55 -24.788-45.209-43.822 1.0066.88 O

ATOM 1 N ASPB : 56 -24.915-44.669-46.004 LOO 66.74 N

ATOM 2 CA ASP B 56 -25.524-45.940-46.392 1.0066.60 C

ATOM 3 CB ASP B 56 . -26.816 τ45.690 -47.176 LOO 66.71 C

ATOM 4 CG ASP B 56 -27.844-44.905-46.379 1.0067.09 C

ATOM 5 ODl ASP B 1 56 -27.864-45.043-45.136 1.0067.21 O

ATOM 6 OD2 ASP B i 56 -28.635-44.153-46.997 1.0067:60 O

ATOM ^'V C ASPB : 56 -24.591-46.835-47.209 1.0066.36 C

ATOM 8 O ASPB ; 56 -25.044-47.576-48.082 1.0066.42 O

ATOM 1 N GLYB 57 -23.296-46.777-46.922 1.0066.00 N

ATOM 2 CA GLYB 57 -22.319-47.528-47.701 1.0065.67 C

ATOM 3 C GLYB 57 -21.546-48.534-46.877 1.0065.47 C

ATOM 4 O GLYB 57 -21.455-48.408-45.656 1.0065.50 O

ATOM 1 N LYSB 58 -20.985-49.535-47.552 1.0065.22 N

ATOM 2 CA LYS B 58 . -20.241-50.602-46.883 1.0064.95 G

ATOM 3 CB LYSB 58 -19.922-51,734-47.864 1.0064.95 C

ATOM 4 CG LYSB 58 -20.909-52.886-47.815 1.0065.08 C

ATOM 5 CD LYSB 58 . -20.919-53.661-49.120 1.0065.47 C

ATOM 6 CE LYS B 58 -19.519-54.076-49.535 1.0065.82 C

ATOM 7 NZ LYS B 58 -19.515-54.712-50.885 1.0066.10 N

ATOM 8 C LYSB 58 -18.958-50.095-46.235 1.0064.68 C

ATOM 9 O LYSB 58 -18.191-49.365-46.864 1.0064.72 O

ATOM 1 N PROB 59 -18.726-50.484-44.970 1.0064.36 N

ATOM 2 CA PRO B 59 -17.520-50.095-44.241 1.0064.14 C

ATOM 3 CB PROB 59 -17.587-50.937-42.956 1.0064.07 C

ATOM 4 CG PROB 59 . -18.679-51.939-43.176 1.0064.14 C

ATOM 5 CD PROB 59 -19.618-51.317-44.149 1.0064.28 C ATOM 6 C PROB 59 -16.240-50.401-45.018 1.0063.96 C

ATOM 7 O PROB 59 -16.143-51.438-45.678 1.0063.99 O

ATOM 1 N METB 60 -15.277-49.488-44.941 1.0063.71 N

ATOM 2 CA METB 60 -13.981-49.666-45.582 1.0063.49 C

ATOM 3 CB METB 60 -13.569-48.382-46.311 1.0063.41 C

ATOM 4 CG METB 60 .14.477-47.957-47.455 1.0063.33 C

ATOM^" 5 SD METB 60 -14.625-46.152-47.591 1.0063.57 S

ATOM .6 CE MET B 60 -15.07.1-45.961-49.319 1.0063.70 C

ATOM 7 C METB 60 -12.935-49.986-44.520 1.0063.31 C

ATOM 8 O METB 60 -13.049-49.526-43.387 1.0063.29 O

ATOM 1 N VALB 61 -11.928-50.779-44.871 1.0063.07 N

ATOM 2 CA VALB 61 -10.704-50.802-44.073 1.0062.97 C

ATOM 3 CB VALB 61 -10.398-52.180-43.434 1.0062.87 C

ATOM 4 CGlVALB 61 -11.661 -52.805 -42.886 1.0062.90 C

ATOM 5 CG2VALB 61 -9.741-53.104-44.425 1.0062.98 C

ATOM 6 C VALB 61 -9.549-50.335-44.954 1.00.63.00 C

ATOM 7 O VALB 61 -9.521-50.612-46.161 1.0063.16 O

ATOM 1 N LEUB 62 -8.615-49.599-44.360 1.0062.78 N

ATOM 2 CA LEUB 62 -7.493-49.062-45.114 1.0062.54 C

ATOM ^' 3 CB LEUB 62 -7.429-47.541-44.987 1.0062.51 C

ATOM 4 CG LEUB 62 -6.260-46.869-45.715 1.0062.61 C

ATOM 5 CDlLEUB 62 -6.657-45.506-46.263 1.0062.58 C

ATOM 6 CD2LEUB 62 -5.045-46.751-44.806 1.0062.83 . C

ATOM 7 C LEUB 62 -6.184-49.675-44.665 1.0062.41 C

ATOM 8 O LEUB 62 -5.880-49.715-43.473 1.0062.37 O

ATOM 1 N VALB 63 -5.407-50.148-45.631 1.0062.32 N

ATOM 2 CA VALB 63 -4.108-50.731-45.339 1.0062.19 C

ATOM 3 CB VALB 63 -3.968-52.128-45.956 1.0062.15 C

ATOM 4 CGlVALB 63 -2.708-52.787-45.447 1.0062.50 C

ATOM 5 CG2VALB 63 -5.184-52.982-45.618 1.0061.99 C

ATOM 6^" C VALB 63 -2.981-49.830-45.837 1.0062.07 C

ATOM 7 O VALB 63 -2.860-49.577-47.036 1.0061.99 O

ATOM 1 N ALAB 64 -2.166-49.344-44.905 1.0062.00 N

ATOM 2 CA ALAB 64 -1.062-48.446-45.232 1.0061.93 C

ATOM 3 CB ALAB 64 -1.355-47.043-44.742 1.0061.86 C

ATOM 4 C ALAB 64 0.234-48.949-44.626 1.0061.87 C

ATOM 5 O ALAB 64 0.225-49.792-43.737 1.0062.00 O

ATOM 1 N GLYB 65 1.347-48.418-45.106 1.0061.82 N

ATOM 2 CA GLYB 65 2.662 -48.820 -44.633.1.0062.04 C

ATOM 3 C GLYB 65 3.663-48.413-45.689 1.0062.30 C

ATOM 4 O GLYB 65 3.272-47.955-46.765 1.0062.42 O

ATOM 1 N GLNB 66 4.951 -48.562 -45.405 1.0062.45 N

ATOM 2 CA GLNB 66 5.940-48.233-46.419 1.0062.73 C

ATOM 3 CB GLNB 66 7.199-47.616-45.816 1.0062.81 C

ATOM 4 CG GLNB 66 7.642-48.190-44.496 1.0063.71 C

ATOM 5 CD GLNB 66 8.746-47.355-43.871 1.0064.68 C

ATOM 6 OElGLNB 66 9.595-46.794-44.578 1.0065.17 O

ATOM 7 NE2GLNB 66 8.740-47.264-42.543 1.0065.07 N

ATOM 8 C GLNB 66 6.260-49.424-47.306 1.0062.78 C

ATOM 9 O GLNB 66 5.623-50.470-47.198 1.0062.88 O

ATOM 1 N TYRB 67 7.237-49.258-48.189 1.0062.88 N

ATOM 2 CA TYRB 67 7.528 -50.258 -49.210 1.0062.98 C

ATOM 3 CB TYRB 67 8.730-49.831-50.058 1.0063.32 C

ATOM 4 CG TYRB 67 8.484-48.619-50.930 1.0063.88 C

ATOM 5 CDlTYRB 67 9.395-47.566-50.965 1.0064.41 C

ATOM 6 CElTYRB 67 9.176-46.451-51.771 1.0064.56 C

ATOM 7 CZ TYRB 67 8.030-46.381-52.547 1.0064.29 C

ATOM 8 OH TYRB 67 7.805-45.278-53.346 1.0064.28 O ATOM 9 CE2TYRB 67 7.111-47.414-52.527 1.0064.30 C

ATOM 10 CD2TYRB 67 7.340-48.526-51.721 1.0064.33 C

ATOM 11 C TYRB 67 7.772-51.655-48.651 1.0062.84 C

ATOM 12 O TYRB 67 8.447-51.824-47.637 1.0062.73 O

ATOM 1 N SERB < 58 7.207-52.648-49.333 1.0062.73 N

ATOM 2 CA SERB 68 7.460-54.060-49.053 1.0062.58 C

ATOM 3 CB SERB 68 8.900-54.438-49.424 1.0062.63 C

ATOM 4 OG SERB 68 9.161-54.184-50.797 1.0062.93 O

ATOM 5 C SERB ( 58 7.172-54.439-47.611 1.0062.40 C

ATOM 6 O SERB i 58 7.851 -55.288-47.035 1.0062.68 O

ATOM 1 N THRB 69 6.162-53.814-47.025 1.0061.97 N

ATOM 2 CA THRB 69 5.803-54.129-45.658 1.0061.63 C

ATOM 3 CB THRB 69 5.233-52.907-44.930 1.0061.73 C

ATOM 4 OGlTHRB 69 5.877-51.719-45.403 1.0061.90 O

ATOM 5 CG2THRE ! 69. 5.474-53.030-43.448 1.0062.25 C

ATOM 6 C THRB 69 4.788-55.266-45.651 1.0061.26 C

ATOM 7 O THRB 69 4.469-55.832-44.607 1.0061.25 O

ATOM 1 N GLYB 70 4.278-55.596-46.830 1.0060.94 N

ATOM 2 CA GLYB 70 3.357-56.715-46.973 1.0060.52 C

ATOM 3 C GLYB 70 1.888-56.350-46.949 1.0060.22 C

ATOM 4 O GLYB 70 1.065-57.156-46.549 1.0060.21 O

ATOM . 1 N LYSB 7.1 1.550-55.138-47.376 1.0060.02 N

ATOM 2 CA LYS B 71 0.156-54.712-47.405 1.0059.94 C

ATOM 3 CB LYSB 71 0.060-53.272-47.897 1.0059.83 C

ATOM •4 CG LYSB. 71 0.543-52.237-46.903 1.0059.55 C

ATOM 5 CD LYSB 71 ^• 0.862-50.922-47.596 1.0058.81 C

ATOM 6 CE LYS B 71 2.258-50.955-48.191 1.0058.14 C

ATOM 7 NZ LYS B 71 2.389-50.011-49.321 1.0057.62 N

ATOM 8 C LYSB 71 -0.670-55.620-48.313 1.0060.06 C

ATOM 9 O LYSB 71 -1.656-56.244-47.885 1.0060.25 O

ATOM 1 N THRB 72 -0.254-55.686-49.574 1.0060.04 N

ATOM 2 CA THRB 72 -0.936-56.494-50.569 1.0060.09 C

ATOM 3 CB THRB 72 -0.198-56.451-51.928 1.0060.10 C

ATOM 4 OGlTHRB 72 0.276-55.121-52.180 1.0060.02 O

ATOM 5 CG2THRB 72 -1.126-56.878-53.059 1.0060.05 C

ATOM 6 C THRB 72 -1.048-57.931-50.069 1.0060.14 C

ATOM 7 O THRB 72 • -2.105 -58.562 -50.181 1.0060.40 O

ATOM 1 N SERB 73 0.043-58.438-49.501 1.0060.12 N

ATOM 2 CA SERB 73 0.054-59.783-48.944 1.0060.22 C

ATOM 3 CB SERB 73 1.436-60.131-48.381 1.0060.26 C

ATOM 4 OG SERB 73 2.380-60.336-49.421 1.0059.98 O

ATOM 5 C SERB 73 -1.001-59.901-47.856 1.0060.19 C

ATOM 6 O SERB 73 -1.798-60.825-47.841 1.0060.56 O

ATOM 1 N PHEB 74 -0.996-58.942-46.947 1.0060.20 N

ATOM 2 CA PHEB 74 -1.956-58.885-45.867 1.0060.14 C.

ATOM 3 CB PHEB 74 -1.794-57.558-45.135 1.0060.03 C

ATOM 4 CG PHEB 74 -2.723-57.383-43.983 1.0060.15 C

ATOM 5 CDlPHEB 74 -2.513-58.066-42.800 1.0060.37 C

ATOM 6 CElPHEE ! 74 -3.366-57.899-41.736 1.0060.41 C

ATOM 7 CZ PHEB 74 -4.437-57.033-41.843 1.0060.50 C

ATOM 8 CE2PHEE ! 74 -4.648-56.342-43.013 1.0060.12 C

ATOM 9 CD2PHEB 74 -3.797-56.517-44.073 1.0060.02 C

ATOM 1C ) C PHEB 74 -3.3.76-59.038-46.397 1.0060.19 C

ATOM 11 O PHEB 74 -4.123-59.913-45.958 1.0060.38 O

ATOM 1 N ILEB : 75 -3.747-58.192-47.351 1.0060.27 N

ATOM 2 CA ILEB 75 -5.099-58.260-47.895 1.0060.40 C

ATOM 3 CB ILEB 75 -5.362-57.131-48.894 1.0060.26 C

ATOM 4 CGlILEB 75 -5.040-55.781-48.258 1.0060.08 C ATOM 5 CDlILEB 75 -5.166-54.622-49.210 1.0059.79 C

ATOM 6 CG2ILEB 15 -6.805-57.159-49.353 1.0060.22 C

ATOM 7 C ILEB 75 ^■5.350-59.613-48.559 1.0060.71 C

ATOM 8 O ILEB 75 -6.362-60.278-48.299 1.0061.02 O

ATOM 1 N GLNB 76 -4.415-60.007-49.419 1.0060.91 N

ATOM 2 CA GLNB 76 -4.433-61.311-50.069 1.0061.22 . C

ATOM 3 CB GLNB 76 -3.038-61.595-50.620 1.0061.23 C

ATOM 4 CG GLNB 76 -2.935-62.776-51.553 1.0062.03 C

ATOM 5 CD GLNB 76 • -2.700 -62.353 -52.989 1.0063.06 C

ATOM 6 OEl GLNB 76 -1.909-62.972-53.707 1.0063.47 O

ATOM 7 NE2GLNB 76 -3.373-61.282-53.412 1.0063:36 N

ATOM 8 C GLNB 76 -4.792-62.381-49.043 1.0061.30 C

ATOM 9 O GLNB 76 -5.596-63.280-49.294 1.0061.68 O

ATOM 1 N TYRB 77 -4.178-62.242-47.874 1.0061.31 N

ATOM 2 CA TYRB 77 -4.286-63.181-46.768 1.0061.46 C

ATOM 3 CB TYRB 77 -3.182-62.874-45.758 1.0061.45 C

ATOM 4 CG TYRB 77 -3.136-63.776-44.557 1.0061.46 C

ATOM 5 CDlTYRB 77 -3.478-63.300-43.300 1.0061.59 C

ATOM 6 CElTYRB 77 -3.419-64.117-42.185 1.0061.89 C

ATOM 7 CZ TYRB 77 -3.012-65.428-42.324 1.0061.81 C

ATOM 8 OH TYRB 77 -2.955-66.244-41.222 1.0061.74 O

ATOM 9 CE2TYRB 77 -2.663-65.923-43.565 1.0061.90 C

ATOM .10 CD2TYRB 77 -2.727-65.097-44.671 1.0061.71 C

ATOM 11 C TYRB 77 -5.645-63.093-46.092 1.0061.48 C

ATOM 12 O TYRB 77 -6.213-64.112-45.699 1.0061.51 O

ATOM 1 N LEUB 78 -6.159-61.874-45.947 1.0061.31 N

ATOM 2 CA LEU B 78 -7.491 -61.687 -45.390 1.0061.65 C

ATOM 3 CB LEUB 78 -7.806-60.206-45.219 1.0061.70 C

ATOM 4 CG LEUB 78 -7.478-59.629-43.844 1.0062.28 C

ATOM 5 CDlLEUB 78 -7.621-58.112-43.859 1.0062.88 C

ATOM 6 CD2LEUB 78 -8.408-60.242-42.813 1.0062.72 C

ATOM 7 C LEUB 78 -8.531-62.325-46.287 1,0061.78 C

ATOM 8 O LEUB 78 -9.488-62.939-45.814 1.0061.79 O

ATOM 1 N LEUB 79 -8.337-62.181-47.591 1.0061.84 N

ATOM 2 CA LEUB 79 -9.298-62.702-48.542 1.0062.22 C

ATOM 3 CB LEUB 79 -9.254-61.888-49.832 1.0062.29 C

ATOM 4 CG LEUB 79 -9.512-60.386-49.707 1.0062.42 C

ATOM 5 CDlLEUB 79 -9.514-59.736-51.083 1.0062.58 C

ATOM 6 CD2LEUB 79 -10.824-60.120-48.987 1.0062.69 C

ATOM 7 C LEUB 79 -9.047-64.168-48.851 1.0062.47 C

ATOM 8 O LEUB 79 -9.897-64.833-49.444 1.0062.39 O

ATOM 1 N GLUB 80 -7.883-64.668-48.443 1.0062.76 N

ATOM 2 CA GLUB 80 -7.442-66.001-48.849 1.0063.58 C

ATOM 3 CB GLUB 80 -8.137-67.091-48.031 1.0063.72 C

ATOM 4 CG GLUB 80 -7.551-67.293-46.633 1.0065.58 C

ATOM 5 CD GLUB 80 -6.542-68.443-46.559 1.0068.13 C

ATOM 6 OElGLUB 80 -6.912-69.522-46.016 1.0069.12 O

ATOM 7 OE2GLUB 80 -5.388-68.278-47.045 1.0068.88 O

ATOM 8 C GLUB 80 -7.714-66.180-50.339 1.0063.57 C

ATOM 9 O GLUB 80 -8.206-67.219-50.777 1.0063.47 O

ATOM 1 N GLNB 81 -7.399-65.133-51.099 1.0063.78 N

ATOM 2 CA GLNB 81 -7.586-65.106-52.541 1.0063.93 C

ATOM 3 CB GLNB 81 -9.062-64.900-52.890 1.0063.84 C

ATOM 4 CG GLNB 81 -9.347-64.947-54.387 1.0063.39 C

ATOM 5 CD GLNB 81 -10.824-64.864-54.707 1.0062.75 C

ATOM 6 OElGLNB 81 -11.239-65.199-55.812 1.0063.13 O

ATOM 7 NE2GLNB 81 -11.627-64.417-53.746 1.0062.73 N

ATOM 8 C GLNB 81 -6.739-63.987-53.152 1.Q064.17 C ATOM 9 O GLNB 81 -6.526-62.952-52.522 1.0064.15 O

ATOM 1 N GLUB 82 -6.257-64.204-54.375 1.0064.47 N

ATOM 2 CA GLUB 82 -5.416-63.227-55.065 1.0064.72 C

ATOM 3 CB GLUB 82 -4.583-63.910-56.160 1.0064.74 C

ATOM 4 CG GLUB 82 -3.346 -63.123 -56.595 ^'1.0065.36 C

ATOM 5 CD GLUB 82 -2.097-63.996-56.753 1.0066.14 C

ATOM 6 OElGLUB 82 -2.185-65.080-57.373 1.0066.18 O

ATOM 7 OE2GLUB 82 -1.020-63.591-56.255 1.0066.28 O

ATOM 8 C GLUB 82 -6.232-62.057-55.631 1.0064.81 C

ATOM 9 O GLUB 82 -7.363-62.233-56.085 1.0064.77 O

ATOM 1 N VALB 83 -5.652-60.862-55.588 1.0064.99 N

ATOM 2 CA VALB 83 -6.325-59.654-56.052 1.0065.07 C

ATOM 3 CB VALB 83 -5.794-58.413-55.322 1.0065.06 C

ATOM 4 CGlVALB 83 -6.742-57.244-55.511 1.0065.06 _. C .

ATOM 5 CG2VALB 83 -5.598-58.712-53.847 1.0064.87 C

ATOM 6 C VALB 83 -6.138-59.465-57.556 1.0065.23 C

ATOM 7 O VALB 83 -5.009-59.404-58.040 1.0065.10 O

ATOM 1 N PROB 84 -7.252-59.365-58.297 1.0065.51 N

ATOM 2 CA PRO B 84 -7.253-59.247-59.752 1.0065.77 C

ATOM 3 CB PROB 84 -8.656-58.723-60.051 1.0065.66 C

ATOM 4 CG PRO B 84 -9.490-59.315-58.983 1.0065.56 C

ATOM 5 CD PROB 84 -8.620-59.365-57.750 1.0065.53 C

ATOM 6 C PROB 84 -6.206-58.275-60.284 1.0066.15 C

ATOM 7 O PROB 84 -5.487-58.603-61.225 1.0066.22 O

ATOM 1 N GLYB 85 -6.116-57.094-59.685 1.0066.61 N

ATOM 2 CA GLYB 85 -5.194-56.072-60.165 1.0067.21 C

ATOM 3 C GLYB 85 -3.847-56.044-59.464 1.0067.67 C

ATOM 4 O GLYB 85 -2.820 -55.785 -60.094 1.0067.61 O

ATOM 1 N SERB 86 -3.848-56.313-58.161 1.0068.17 N

ATOM 2 CA SERB 86 -2.644-56.150-57.339 1.0068.71 C

ATOM 3 CB SERB 86 -3.014-55.711-55.914 1.0068.74 C

ATOM^' 4 OG SERB 86 ^• -3.020-54.297-55.787 1.0068.90 O

ATOM 5 C SERB 86 -1.725-57.374-57.281 1.0069.01 C

ATOM 6 O SERB 86 -2.054-58.386-56.652 1.0069.11 O

ATOM 1 N ARGB 87 -0.565-57.263-57.927 1.0069.32 N

ATOM 2 CA ARG B 87 0.485-58.266-57.801 1.0069.63 C

ATOM 3 CB ARGB 87 1.378-58.274-59.044 1.0069.53 ■ C

ATOM 4 CG ARGB 87 0.269 -59.653 -59.740 0.0050.00 C

ATOM 5 CD ARGB 87 0.975-60.115-60.993 0.0050.00 C

ATOM 6 NE ARG B 87 1.731 -61.343 -60.776 0.0050.00 N

ATOM ^'7 CZ ARGB 87 1.237-62.572-60.852 0.0050.00 C

ATOM 8 NHlARGB 87 2.033 --63.609 -60.623 0.0050.00 N

ATOM 9 NH2ARGB 87 -0.028-62.779-61.180 0.0050.00 N

ATOM 10 C ARGB 87 1.319 -57.999 -56.544 1.0069.92 C

ATOM 11 O ARGB 87 1.025-57.085-55.771 1.0069.93 O

ATOM 1 N VALB 88 2.357-58.803-56.344 1.0070.32 N

ATOM 2 CA VALB 88 3.222-58.678-55.172 1.0070.65 C

ATOM 3 CB VALB 88 2.715-59.565-54.007 1.0070.63 C

ATOM 4 CGlVALB 88 3.838-59.875-53.028 1.0070.52 C

ATOM 5 CG2VALB 88 2.102-60.855-54.544 1.0070.76 C

ATOM 6 C VALB 88 4.664-59.035-55.538 1.0070.97 C

ATOM 7 O VALB 88 4.906-59.997-56.272 1.0071.03 O

ATOM 1 N GLYB 89 5.619-58.255-55.040 1.0071.28 N

ATOM 2 CA GLYB 89 7.020-58.471-55.389 1.0071.78 C

ATOM 3 C GLYB 89 8.015-57.882-54.410 1.0072.17 C

ATOM 4 O GLYB 89 7.627 -57.243 -53.432 ,1.0072.08 O

ATOM 1 N PROB 90 9.316-58.087 -54.681 1.0072.59 N

ATOM 2 CA PRO B 90 10.417-57.648-53.818 1.0072.92 C ATOM 3 CB PROB 90 11.655-58.251-54.493 1.0072.90 C

ATOM 4 CG PRO B 90 11.259-58.441-55.924 1.0072.85 C

ATOM 5 CD PROB 90 9.797-58.771-55.896 1.0072.65 C

ATOM 6 C PROB 90 10.523-56.126-53.765 1.0073.27 C

ATOM 7 O PROB 90 9.958-55.499-52.866 1,0073.27 O

ATOM 1 N GLUB 91 11.246-55.546-54.721 1.0073.71 N

ATOM 2 CA GLUB 91 11.333-54.094-54.859 1.0074.09 C

ATOM 3 CB GLUB 91 12.405-53.714-55.891 1.0074.13 C

ATOM 4 CG GLUB 91 13.840-53.941-55.421 1.0074.32 C

ATOM 5 CD GLUB 91 14.010-53.220-53.305 0.0050.00 C

ATOM 6 OElGLUB 91 15.017-53.953-53.217 0.0050.00 O

ATOM 7 OE2GLUB 91 13.312-52.915-52.3080.0050.00 O

ATOM 8 C GLUB 91 9.971-53.526-55.270 1.0074.25 C

ATOM 9 O GLUB 91 9.245-54.168-56.034 1.0074.34 O

ATOM 1 N PROB 92 .9.626-52.323-54.759 1.0074.34 N

ATOM 2 CA PRO B 92 8.362-51.615-54.984 1.0074.34 C

ATOM 3 CB PROB 92 8.766-50.133-54.870 1.0074.35 C

ATOM 4 CG PROB 92 10.183-50.122-54.284 1.0074.33 C

ATOM 5 CD PROB 92 10.513-51.535-53.889 1.0074.39 C

ATOM 6 C PROB 92 7.728-51.884-56.354 1.0074.33 C

ATOM 7 O PROB 92 8.391-51.737-57.391 1.0074.31 O

ATOM 1 N THRB 93 6.448-52.260-56.348 1.0074.15 N

ATOM 2 CA THRB 93 5.746-52.645-57.578 1.0073.95 C

ATOM 3 CB THRB 93 5.311-54.133-57.540 1.0074.06 C

ATOM 4 OGlTHRB 93 4.909-54.490-56.194 1.0073.87 O

ATOM 5 CG2THRB 93 6.469-55.058-57.997 1.0074.23 C

ATOM 6 C THRB 93 4.532-51.770-57.907 1.0073.59 C

ATOM 7 O THRB 93 4.528-51.057-58.917 1.0073.58 O

ATOM 1 N THRB 94 3.507-51.839-57.055 1.0073.13 N

ATOM 2 CA THRB 94 2.259-51.097-57.264 1.0072.66 C

ATOM 3 CB THRB 94 1.120-51.644-56.357 1.0072.80 C

ATOM 4 OGlTHRB 94 1.526-51.598-54.978 1.0072.65 O

ATOM 5 CG2THRB 94 0.780-53.088-56.729 1.0072.95 C

ATOM 6 C THRB 94 2.442-49.593-57.020 1.0072.18 C

ATOM 7 O THRB 94 3.059-49.188-56.033 1.0072.21 O

ATOM 1 N ASPB 95 1.900-48.767-57.914 1.0071.45 N

ATOM 2 CA ASP B 95 2.119-47.320-57.839 1.0070.73 C

ATOM 3 CB ASPB 95 2.915-46.839-59.063 1.0070.79 C

ATOM 4 CG ASPB 95 3.164-46.932-59.6460.0050.00 C

ATOM 5 ODlASPB 95 2.550-47.842-60.2800.0050.00 O

ATOM 6 0D2ASPB 95 3.842-46.098-60.301 0.0050.00 O

ATOM 7 C ASPB 95 0.835-46.498-57.697 1.0070.16 C

ATOM 8 O ASPB 95 0.762-45.367-58.187 1.0070.07 O

ATOM 1 N CYSB 96 -0.165-47.052-57.014 1.0069.46 N

ATOM 2 CA CYSB 96 -1.433-46.343-56.840 1.0068.81 C

ATOM 3 CB CYSB 96 -2.198-46.296-58.165 1.0068.91 C

ATOM 4 SG CYSB 96 -2.997-47.853-58.603 1.0069.45 S

ATOM 5 C CYSB 96 -2.334-46.93.5-55.752 1.0068.20 C

ATOM 6 O CYSB 96 -1.935-47.834-55.013 1.0068.12 O

ATOM 1 N PHEB 97 -3.553-46.408-55.668 1.0067.48 N

ATOM 2 CA PHEB 97 -4.549-46.870-54.713 1.0066.69 C

ATOM 3 CB PHEB 97 -5.414-45.706-54.228 1.0066.64 C

ATOM 4 CG PHEB 97 -4.672-44.689-53.416 1.0066.32 C

ATOM 5 CDlPHEB 97 -3.822-43.780-54.025 1.0066.08 C

ATOM 6 CElPHEB 97 -3.140 -42.841 -53.281 1.0065.88 C

ATOM 7 CZ PHEB 97 -3.311-42.793 -51.915 1.0066.18 C

ATOM 8 CE2PHEB 97 -4.162-43.688-51.295 1.0066.18 C

ATOM 9 CD2PHEB 97 -4.839-44.627-52.045 1.0066.18 C ATOM 10 C PHEB 97 -5.450-47.902-55.365 1.0066.32 C

ATOM 11 O PHEB 97 -6.032 -47.657 -56.421 1.0066.17 O

ATOM 1 N VALB 98 -5.568-49.056-54.726 1.0065.88 N

ATOM 2 CA VALB 98 -6.434-50.108-55.218 1.0065.43 C

ATOM 3 CB VALB 98 -5.678-51.438-55.357 1.0065.36 C

ATOM 4 CGlVALB 98 -6.570-52.488-55.991 1.0065.18 C

ATOM 5 CG2VALB 98 -4.413-51.243-56.171 1.0065.13 C

ATOM 6 C VALB 98 -7.590-50.287-54.251 1.0065.26 C

ATOM 7 O VALB 98 -7.389-50.620-53.086 1.0065.27 O

ATOM 1 N ALAB 99 -8.801-50.050-54.732 1.0065.07 N

ATOM 2 CA ALAB 99 -9.978-50.225-53.905 1.0065.02 C

ATOM 3 CB ALAB 99 -11.021-49.179-54.242 1.0065.00 C

ATOM 4 C ALAB 99 -10.539-51.619-54.108 1.0065.03 C

ATOM 5 O ALAB 99 -11.338-51.847-55.012 1.0065.09 O

ATOM 1 N VALB lOO -10.109-52.555-53.274 1.0065.12 N

ATOM ^•2 CA VALB lOO -10.605-53.922-53.363 1.0065.24 C

ATOM 3 CB VALB 100 -9.693-54.914-52.616 1.0065.20 C

ATOM 4 CGl VALB lOO -8.233-54.672-52.969 1.0065.10 C

ATOM 5 CG2VALB 100 -10.100-56.345-52.931 1.0065.15 C

ATOM 6 C VALBlOO -12.012-53.995-52.786 1.0065.39 C

ATOM 7 O VALB lOO -12.199-53.938-51.570 1.0065.48 O

ATOM 1 N MET B 101 -13.001-54.107-53.665 1.0065.56 N

ATOM 2 CA METB 101 -14.394-54.161-53.245 1.0065.78 C

ATOM 3 CB MET B 101 -15.100-52.850-53.572 1.0065.79 C

ATOM 4 CG METB lOl -14.752-52.294-54.941 1.0065.81 C

ATOM 5 SD METB lOl -15.844-50.959-55.463 1.0065.65 S

ATOM 6 CE METB lOl -15.750-49.849-54.058 1.0065.57 C

ATOM 7 C METB 101 -15.110-55.317-53.917 1.0066.02 C

ATOM 8 O METB 101 -14.552-55.978-54.790 1.0066.05 O

ATOM 1 N HIS B 102 -16.350-55.559-53.514 1.0066.39 N

ATOM 2 CA HIS B 102 -17.107-56.667-54.073 1.0066.80 C.

ATOM 3 CB HIS B 102 -18.418-56.881-53.314 1.0066.73 C

ATOM 4 CG HIS B 102 -19.129-58.142-53.694 1.0066.79 C

ATOM 5 KDl HIS B 102. -18.664 -59.392 -53.3f3 1.0066.68 N

ATOM 6 CEl HIS B 102 -19.483-60.313-53.819 1.0066.49 C

ATOM 7 NE2 HIS B 102 -20.461-59.706-54.469 1.0066.63 N

ATOM 8 CD2 HIS B 102 -20.262-58.347-54.408 1.0066.78 C

ATOM 9 C HIS B 102 -17.373-56.459-55.561 1.0067.13 C

ATOM 10 O HIS B 102 -16.949-55.465-56.145 1.0067.23 O

ATOM 1 N GLYB 103 -18.072-57.408-56.168 1.0067.46 N

ATOM 2 CA GLYB 103 -18.379-57.341-57.583 1.0067.99 C

ATOM 3 C GLYB 103 -18.712-58.729-58.069 1.0068.39 ^' C

ATOM 4 O GLYB 103 -18.227-59.715-57.519 1.0068.41 O

ATOM 1 N GLUB 104 -19.545-58.812-59.099 1.0068.82 N

ATOM 2 CA GLUB 104 -19.993-60.105-59.591 1.0069.31 C

ATOM 3 CB GLUB 104 -21.329-59.968-60.333 1.0069.45 C

ATOM 4 CG GLUB 104 -21.933-61.291-60.806 1.0070.31 C

ATOM 5 CD GLUB 104 -21.826-62.411-59.768 1.0071.40 C

ATOM 6 OEl GLUB 104 -21.442-62.136-58.606 1.0071.64 O

ATOM 7 OE2 GLUB 104 -22.124-63.575-60.123 1.0071.78 O

ATOM 8 C GLUB 104 -18.934-60.790-60.460 1.0069.42 C

ATOM 9 O GLUB 104 -18.745-62:007-60.384 1.0069.49 O

ATOM 1 N THRB 105 -18.237-60.003-61.272 1.0069.53 N

ATOM 2 CA THRB 105 -17.191 -60.542-62.131 1.0069.56 C

ATOM 3 CB THRB 105 -17.345-60.049-63.590 1.0069.61 C

ATOM 4 OGl THRB 105 -16.517 -60.837 -64.455 1.0069.65 O

ATOM 5 CG2THRB 105 -16.957-58.573-63.713 1.0069.72 C

ATOM 6 C THRB 105 -15.805-60.172-61.606 1.0069.52 C ATOM .7 O, THRB 105 -15.611-59.099-61.030 1.0069.53 O

ATOM 1 N GLUB 106 -14.849-61.075-61.792 1.0069.46 N

ATOM 2 CA GLUB 106 -13.460-60.778-61.477 1.0069.46 C

ATOM 3 CB GLUB 106 -12.637-62.066-61.400 1.0069.51 C

ATOM 4 CG GLUB 106 -12.955-62:949-60.198 1.0069.53 C

ATOM 5 CD GLUB 106 -12.289-64.318-60.277 1.0069.39 C

ATOM 6 OElGLUB 106. -11.990-64.754-61.456 1.0069.37 O

ATOM 7 OE2 GLUB 106 -12.062-64.963-59.165 1.0068.93 O

ATOM 8 C GLUB 106 rl2.899 -59.863 -62.557 1.0069.46 C

ATOM 9 O GLUB 106 -13.145-60.073-63.743 1.0069.46 O

ATOM 1 N GLYB 107 -12.150-58.845-62.148 1.0069.47 N

ATOM 2 CA GLYB 107 -11.584-57.896-63.099 1.0069.50 C

ATOM 3 C GLYB 107 -11.266-56.551-62.476 1.0069.52 C

ATOM 4 O GLYB 107 -11.271-56.407-61.253 1.0069.51 O

ATOM 1 N TBDR. B 108 -10.989-55.562-63.322 1.0069.51 N

ATOM 2 CA THRB 108 -10.595-54.240-62.848 1.0069.49 C

ATOM 3 CB THRB 108 -9.073-54.020-62.975 1.0069.48 C

ATOM 4 OGlTHRB 108 -8.713-53.964-64.361 1.0069.55 O

ATOM 5 CG2THRB 108 -8.298-55.139-62.290 1.0069.46 C

ATOM 6 C THRB 108 -11.287-53.116-63.608 1.0069.49 C

ATOM ^' 7 O THRB 108 -12.009-53.354-64.578 1.0069.48 O

ATOM 1 N VALB 109 -11.046-51.890-63.150 1.0069.49 N

ATOM 2 CA VALB 109 -11.563-50.680-63.784 1.0069.46 C

ATOM 3 CB VAL B 109 -13.114-50.660-63.804 1.0069.47 C

ATOM 4 CGl VALB 109 -13.632-49.424-64.531 1.0069.54 C

ATOM. 5 CG2VALB 109 -13.680-50.750-62.389 1.0069.55 C

ATOM 6 C VALB 109 -11.007-49.450-63.056 1.0069.39 C

ATOM 7 O VALB 109 -11.153-49.325-61.839 1.0069.42 O

ATOM 1 N PROB IlO -10.343-48.548-63.799 1.0069.28 N

ATOM 2 CA PROB IlO -9.693-47.376-63.208 1.0069.20 C

ATOM 3 CB PROB 110 -8.558-47.076-64.194 1.0069.20 C

ATOM 4 CG PROB IlO -9.001-47.667-65.506 1.0069.19 C

ATOM 5 CD PROB IlO -10.153-48.608-65.259 1.0069.25 C

ATOM 6 C PROB 110 -10.598-46.150-63.049 1.0069.09 C

ATOM 7 O PROB IlO -10.416-45.155-63.752 1.0069.13 O

ATOM 1 N GLYB 111 -11.548-46.216-62.120 1.0068.96 N

ATOM 2 CA GLYB lIl -12.442-45.089-61.852 1.0068.85 C

ATOM 3 C GLYB lIl -13.484-44.872-62.941 1.0068.81 C

ATOM 4 O GLYB 111 -13.344-43.965-63.800 1.006S.65 O

TER 4 GLYB lIl

ATOM 1 N ASN B 130 -11.159-31.270-62.225 1.0066.96 N

ATOM 2 CA ASNB 130 -9.886-30.849-61.642 1.0067.00 C

ATOM 3 CB ASNB 130 -10.094 -29.640 -60.719- 1.0066.96 C

ATOM ^■ 4 CG ASNB 130 -8.779-29.020-60.264 1.0066.90 C

ATOM 5 ODl ASNB 130 -8.343-28.004-60.826 1.0066.78 O

ATOM 6 ND2ASNB 130 -8.136-29.635-59.247 1.0066.61 N

ATOM 7 C ASNB 130 -9.150-31.973-60.895 1.0067.05 C

ATOM 8 O ASNB 130 -7.929-32.106-61.015 1.0067.08 O_.

ATOM 1 N THRB 131 -9.899-32.772-60.132 1.0067.04 N

ATOM 2 CA THRB 131 -9.333 Λ33.856 -59.307 1.0066.97 C

ATOM 3 CB THRB 131 -10.400-34.450-58.342 1.0066.99 C

ATOM 4 OGl THRB 131 -10.043-35.792-57.984 1.0066.77 O

ATOM 5 CG2THRB 131 -11.777-34.460-58.998 1.0067.17 C

ATOM 6 C THRB 131 -8.678-34.980-60.126 1.0066.94 C

ATOM 7 O THRB 131 -8.847-35.054-61.348 1.0066.93 O

ATOM 1 N PHEB 132^: -7.931-35.851-59.444 1.0066.81 N

ATOM 2 CA PHE B 132 -7.174-36.912-60.115 1.0066.68 C

ATOM 3 CB PHEB 132 -5.672-36.602-60.088 1.0066.71 C ATOM 4 CG PHEB 132 -5.315-35.278-60.709 1.0066.79 C

ATOM 5 CDl PHE B 132 -4.691-34.290-59.960 1.0066.90 C

ATOM 6 CEl PHE B 132 -4.363-33.064-60.532 1.0067.27 C

ATOM 7 CZ PHEB 132 -4.666-32.814-61.865 1.0067.02 C

ATOM 8 CE2PHEB132 -5.293-33.791-62.620 1.0067.01 C

ATOM 9 CD2PHEB 132 -5.616-35.015-62.041 1.0066.90 C

ATOM 10 C PHEB 132 -7.447-38.316-59.563 1.0066.58 C

ATOM 11 O PHEB 132 -7.146-38.620-58.404 1.0066.52 O

ATOM, 1 N LEUB 133 -8.016-39.165-60.417 1.0066.41 N

ATOM 2 CA LEUB 133 -8.370-40.539-60.064 1.0066.14 C

ATOM 3 CB LEUB 133 -9.874-40.769-60.256 1.0066.19 C

ATOM 4 CG LEUB 133 -10.882-40.435-59.148 1.0066.22 C ^■

ATOM 5 CDlLEUB 133 -10.589-39.104-58.467 1.0066.32 C

ATOM 6 CD2LEUB133 -12.304-40.457-59.704 1.0066.13 C

ATOM 7 C LEUB 133 -7.601-41.546-60.915 1.0065.93 C.

ATOM 8 O LEUB 133 -7.829-42.751-60.820 1.0065.82 O

ATOM 1 K ASN B 134 -6.705-41.051-61.765 1.0065.76 N

ATOM 2 CA ASNB 134 -5.909-41.930-62.615 1.0065.55 ^■ C

ATOM 3 CB ASNB 134 -5.234-41.148-63.746 1.0065.55 C

ATOM 4 CG ASNB 134 -4.640-42.057-64.813 1.0065.49 C

ATOM 5 ODl ASN B 134 -3.814-41.627-65.619 1.0065.41 O

ATOM 6 ND2ASNB134 -5.060-43.319-64.821 1.0065.26 , N

ATOM 7 C ASNB 134 -4.873-42.672-61.783 1.0065.39 C

ATOM 8 O ASNB 134 -4.324-43.690-62.209 1.0065.43 O

ATOM 1 N ARG B 135 -4.612 -42.146 -60.590 1.0065.09 N

ATOM 2 CA ARGB 135 -3.787-42.836-59.617 1.0064.81 C

ATOM 3 CB ARGB 135 -2.997r-41.831 -58.777 1.0064.75 C

ATOM 4 CG ARG B 135 -2.260 -40.714 -59.0060.0050.00 C

ATOM 5 CD ARG B 135 -1.921-39.538-58.193 0.0050.00 C

ATOM 6 NE ARG B 135 -2.823-38.615-57.663 0.0050.00 N

ATOM 7 CZ ARGB 135 -2.891 -37.354 -57.365 0.0050.00 C

ATOM 8 NHl ARG B 135 -3.876-36.980-56.508 0.0050.00 N

ATOM 9 NH2 ARG B 135 -2.196,-36:373 -57.8960.0050.00 N

ATOM ^' 10 C ARGB 135 -4.713-43.669-58.740 1.0064.65 C

ATOM 11 O ARGB 135 -4.412-43.944-57.578 1.0064.66 O

ATOM 1 N PHE B 136 -5.844-44.072-59.314 1.0064.44 N

ATOM 2 CA PHEB 136 -6.877-44.795-58.578 1.0064.19 C

ATOM 3 CB PHEB 136 -7.996-43.832-58.178 1.0064.24 C

ATOM 4 CG PHEB 136 -8.564-44.089-56.815 1.0064.14 C

ATOM 5 CDl PHEB 136 -8.404-43.155-55.802 1.0064.00 C

ATOM 6 CEl PHEB 136 -8.924-43.377-54.546 1.0064.15 C

ATOM 7 CZ PHEB 136 -9.611-44.548-54.286 1.0064.46 C

ATOM 8 CE2PHEB136 -9.777-45.491-55.290 1.0064.42 C

ATOM .9 CD2 PHE B 136 -9.256 -45.257 -56.545 1.0064.17 C

ATOM 10 C PHE B 136 -7.459-45.939-59.408 1.0063.99 C

ATOM 11 O PHEB 136 -8.050-45.718-60.469 1.0063.97 O

ATOM 1 N METB 137 -7.293-47.160-58.911 1.0063.68 N

ATOM 2 CA MET B 137 -7.801-48.347-59.586 1.0063.43 . C

ATOM ^■ 3 CB METB 137 -6.665-49.343-59.828 1.0063.62 C

ATOM 4 CG METB 137 -5.684-48.929-60.916 1.0064.35 C

ATOM 5 SD METB 137 -6.180-49.495-62.559 1.0066.23 S

ATOM 6 CE METB 137 -6.043-51.275-62.348 1.0065.88 C

ATOM 7 C METB 137 -8.884-49.000-58.741 1.0063.01 C

ATOM 8 O METB 137 -8.986-48.735-57.544 1.0063.09 O

ATOM 1 N CYS B 138 -9.688-49.857-59.362 1.0062.44. N

ATOM 2 CA CYS B 138 -10.732-50.576-58.640 1.0061.94 C

ATOM 3 CB CYSB 138 -12.095-49.918-58.858 1.0062.03 C

ATOM 4 SG CYS B 138 -13.490-50.936-58.322 1.0062.33 S ATOM 5 C CYSB 138 -10.795-52.041-59.046 1.0061.48 C

ATOM 6 O CYS B 138 -10.922-52.365-60.228 1.0061.39 O

ATOM 1 N ALAB 139 -10.711-52.921-58.055 1.0060.93 N

ATOM 2 CA ALAB 139 -10.780-54.357-58.291 1.0060.47 C

ATOM 3 CB ALAB 139 -9.544-55.046-57.739 1.0060.46 C

ATOM 4 C ALAB 139 -12.041-54.939-57.666 1.0060.13 C

ATOM 5 O ALAB 139 -12.487-54.485-56.612 1.0060.12 O

ATOM 1 N GLNB 140 -12.613 -55.942 -58.324 1.0059.68 ^' . N

ATOM 2 CA GLNB 140 -13.850-56.562-57.868 1.0059.22 ^' C

ATOM 3 CB GLNB 140 -15.013-56.145-58.765 1.0059.22 C

ATOM 4 CG GLNB 140 -15.223-54.656-58.876 1.0059.09 C

ATOM 5 CD GLNB 140 -16.449-54.321-59.685 1.0059.09 C

ATOM 6 OEl GLNB 140 -17.272-55.192-59.967 1.0059.44 O

ATOM 7 NE2GLNB140 -16.580-53.058-60.068 1.0059.05 N

ATOM 8 C GLNB 140 -13.731-58.074-57.908 1.0058.94 C

ATOM 9 O GLNB 140 -13.091-58.624-58.803 1.0058.94 O

ATOM 1 N LEUB 141 -14.360-58.747-56.950 1.0058.55 N

ATOM 2 CA LEUB 141 -14.387-60.207-56.964 1.0058.30 C

ATOM 3 CB LEUB 141 -12.981-60.785-56.744 1.0058.30 C

ATOM 4 CG LEUB 141 -12.230-60.539-55.433 1.0058.25 C

ATOM 5 CDl LEUB 141 -10.894-61.267-55.464 1.0058.11 C

ATOM 6 CD2LEUB141 -12.024-59.056-55.161 1.0058.38 C

ATOM 7 C LEUB 141 -15.390-60.810-55.982 1.0058.06 C

ATOM 8 O LEUB 141 -15.453-60.403-54.825 1.0058.07 O

ATOM 1 N PRO B 142 -16.181-61.788-56.454 1.0057.87 N

ATOM 2 CA PROB 142 -17.163-62.505-55.644 1.0057.70 C

ATOM 3 CB PRO B 142 -17.717-63.554-56.611 1.0057.74 C

ATOM 4 CG PRO B 142 -16.719-63.635-57.723 1.0057.78 C

ATOM 5 CD PRO B 142 -16.164-62.265-57.846 1.0057.80 C

ATOM 6 C PRO B 142 -16.499-63.187-54.461 1.0057.59 C

ATOM 7 O PRO B 142 -15.712-64.109-54.642 1.0057.61 O

ATOM 1 N ASNB 143 -16.827-62.729-53.258 1.0057,52 N

ATOM 2 CA ASNB 143 -16.140-63.152-52.046 1.0057.41 C

ATOM 3 CB ASNB 143 -14.667-62.745-52.127 1.0057.34 C

ATOM 4 CG ASNB 143 -13.903-63.022-50.846 1.0057.28 ■ C

ATOM 5 ODl ASN B 143 -14.460-62.987-49.747 1.0057.32 O

ATOM 6 ND2ASNB143 -12.609-63.281-50.982 1.0056.70 N

ATOM 7 C ASNB 143 -16.814-62.516-50.833 1.0057.47 • C

ATOM 8 O ASNB 143 -16.943-61.295-50.759 1.0057.41 O

ATOM 1 N GLNB 144 -17.237-63.350-49.885 1.0057.56, N

ATOM 2 CA GLNB 144 -18.063-62.908-48.754 1.0057.7.2 C

ATOM 3 CB GLNB 144 -18.273-64.055-47.773 1.0057.81 C

ATOM 4 CG GLNB 144 -18.601-65.378-48.416 1.0058.02 C

ATOM 5 CD GLNB 144 -18.968-66.419-47.386 1.0058.57 C

ATOM 6 OEl GLNB 144 -19.865-66.207-46.566 1.0058.64 O

ATOM 7 NE2GLNB144 -18.274-67.553-47.417 1.0058.83 N

ATOM 8 C GLNB 144 -17.496-61.713-47.992 1.0057.73 C

ATOM 9 O GLNB 144 -18.229-60.782-47.618 1.0057.88 O

ATOM 1 N VALB 145 -16.193-61.756-47.740 1.0057.64 N

ATOM 2 CA VALB 145 -15.537-60.663-47.053 1.0057.55 C

ATOM 3 CB VALB 145 -14.015-60.834-47.034 1.0057.60 C

ATOM 4 CGlVALB 145 -13.649-62.269-46.694 1.0057.62 C

ATOM 5 CG2VALB145 -13.391-59.867-46.039 1.0057.54 C

ATOM 6 C VALB 145 -15.896-59.369-47.760 1.0057.47 C

ATOM 7 O VALB 145 -16.252-58386-47.119 1.0057.53 O

ATOM 1 N LEUB 146 -15.825-59.386-49.086 1.0057.46 N

ATOM 2 CA LEUB 146 -16.195-58.222-49.882 1.0057.59 C

ATOM 3 CB LEUB 146 -15.718-58.367-51.330 1.0057.59 C ATOM 4 CG LEUB 146 -14.250-58.045-51.620 1.0057.56 C

ATOM 5 CDl LEUB 146 -13.770-56.879-50.764 1.0057.23 C

ATOM 6 CD2LEUB 146 -13.382-59.266-51.394 1.0057.83 C

ATOM 7 C LEUB 146 -17.697-57.934-49.837 1.0057.65 C

ATOM 8 O LEUB 146 -18.135-56.840-50.185 1.0057.62 O

ATOM 1 N GLUB 147 -18.485-58.917-49.417 1.0057.74 N

ATOM 2 CA GLUB 147 -19.896-58.681-49.164 1.0057.96 C

ATOM 3 CB GLUB 147 -20.652-59.994-48.955 1.0057.87 C

ATOM 4 CG GLUB 147 -20.690-60.912-50.158 1.0058.25 C

ATOM 5 CD GLUB 147 -21.327-62.253-49.835 1.0058.44 C

ATOM 6 OEl GLUB 147 -21.131-63.217-50.612 1.0058.79 O

ATOM- 7 OE2 GLUB 147 -22.020-62.343-48.797 1.0059.30 O

ATOM 8 C GLUB 147 -20.020-57.827-47.914 1.0057.91 C

ATOM 9 O GLUB 147 -20.766-56.850-47.887 1.0058.03 O

ATOM 1 N SERB 148 -19.281-58.197-46.874 1.0057.86 N

ATOM 2 CA SERB 148 -19.375-57.474-45.609 1.0057.89 C

ATOM 3 CB SERB 148 -18.770-58.296-44.474 1.0057.92 C

ATOM 4 OG SERB 148 -19.358-59.582-44.412 1.0058.15 O

ATOM 5 C SERB 148 -18.720-56.091-45.661 1.0057.91 C

ATOM 6 O SERB 148 -19.316-55.099-45.242 1.0058.01 O

ATOM 1 N ILEB 149 -17.495-56.031-46.175 1.0057.82 N

ATOM 2 CA ILEB 149 -16.716-54.795-46.184 1.0057.70 C

ATOM 3 CB ILE B 149 -15.661-54.802-45.065 1.0057.63 C

ATOM 4 CGl ILEB 149 -14.680-55.962-45.263 1.0057.21 C

ATOM 5 CDl ILE B 149 -13.512-55.946-44.303 1.0056.31 ^■ C

ATOM 6 CG2ILEB 149 -16.325-54.901-43.708 1.0057.78 C

ATOM 7 C ILEB 149 -15.984-54.602-47.505 1.0057.81 C

ATOM 8 O ILE B 149 -16.105-55.418-48.416 1.0058.00 O

ATOM 1 N SERB 150 -15.225-53.517-47.611 1.0057.80 N

ATOM 2 CA SERB 150 -14.308 -53.345 -48.737 ^' 1.0057.87 C

ATOM 3 CB SERB 150 -14.924-52.492-49.852 1.0057.80 C

ATOM 4 OG SERB 150 -15.622-51.381-49.328 1.0058.07 O

ATOM 5 C SERB 150 τl2.972 -52.780 -48.263 1.0057.82 C

ATOM 6 O SERB 150 -12.917-51.969-47.337 1.0057.84 O

ATOM 1 N ILEB 151 -11.893-53.233-48.889 1.0057.75 N

ATOM 2 CA ILEB 151 -10.556-52.907-48.422 1.0057.75 C

ATOM 3 CB ILEB 151 -9.748-54.178-48.150 1.0057.69 C

ATOM 4 CGl ILE B 151 -10.576-55.163-47.328 1.0057.79 C

ATOM 5 CDlILEB 151 -10.080-56.585-47.412 r.00.58.36 C

ATOM 6 CG2ILEB 151 -8^446-53.837-47.446 1.0057.61 C

ATOM 7 C ILEB 151 -9.807-52.074-49.445 1.0057.80 C

ATOM 8 O ILEB 151 -9.608-52.502-50.581 1.0057.77 O

ATOM 1 N ILEB 152 -9.384-50.882-49.045 1.0057.79 N

ATOM 2 CA ILEB 152 -8.629 -50.046 -.49.955 1.0057.80 C

ATOM 3 CB ILEB 152 -9.093-48.573-49.903 1.0057.84 C

ATOM 4 CGl ILEB 152 -8.002-47.669-49.334 1.0058.21 C

ATOM 5 CDlILEB 152 -6.996-47.213-50.382 1.0058.80 C

ATOM 6 CG2ILEB 152 -10.418-48.445-49.155 1.0057.83 C

ATOM 7 C ILEB 152 -7.133-50.189-49.669 1.0057.75_. C

ATOM 8 O ILEB 152 -6.677-49.991 -48.543 1.0057:62 O

ATOM 1 N ASP B 153 -6.386-50.564-50.702 1.0057.80 N

ATOM 2 CA ASP B 153 -4.950 -50.776 r50.600 1.0057.91 C

ATOM 3 CB ASP B 153 -4.548-52.005-51.413 1.0057.99 C

ATOM 4 CG ASP B 153 -3.082-52.358-51.258 1.0058.23 C

ATOM 5 ODlASPB 153 -2.331-51.554-50.664 1.0058.41 O

ATOM 6 OD2 ASP B 153 -2.681-53.444-51.736 1.0058.26 O

ATOM 7 C ASP B 153 -4.210-49.549-51.113 1.0058.00 ^' C

ATOM 8 O ASPB 153 -4.584-48.975-52.137 1.0058.18 O ATOM 1 N THRB 154 -3.152-49.160-50.408 1.0058.02 N

ATOM 2 CA THRB 154 -2.458-47.904-50.683 1.0057.95 C

ATOM 3 CB THRB 154 -2.314-47.058-49.401 1.0057.97 C

ATOM 4 OGl THRB 154 -1.536-47.776-48.429 1.0057.67 O

ATOM 5 CG2THRB154 -3.682-46.726-48.824 1.0057.86 C

ATOM 6 C THRB 154 -1.068-48.117-51.266 1.0058.01 C

ATOM 7 O THRB 154 -0.508-49.205-51.144 1.0057.95 O

ATOM 1. N PRO B 155 -0.509-47.071-51.906 1.0058.12 N

ATOM 2 CA PROB 155 0.886-47.083-52.338 1.0058.12 C

ATOM 3 CB PROB 155 1.042-45.757-53.095 1.0058.01 C

ATOM 4 CG PROB 155 -0.338-45.284-53.372 1.0058.04 C

ATOM 5 CD PRO B 155 -1.184-45.812-52.267 1.0058.18 C

ATOM 6 C PROB 155 1.818-47.093-51.136 1.0058.22 C

ATOM 7 O PROB 155 1.450-46.623-50.054 1.0058.19 O

ATOM 1 N GLYB 156 3.017-47.628-51.331 1.0058.35 N^'

ATOM 2 CA GLYB 156 4.008-47.689-50.267 1.0058.61 C

ATOM 3 C GLYB 156 4.562-46.324-49.920 1.0058.79 C

ATOM 4 O GLYB 156 4.955-45.557-50.800 1.0058.87 O

ATOM 1 N ILEB 157 4.584-46.016-48.630 1.0058.96 N

ATOM 2 CA ILE B 157 5.160-44.769-48.170 1.0059.18 C

ATOM 3 CB ILEB 157 4.868-44.544-46.684 1.0059.11 C

ATOM 4 CGl ILEB 157 3.363-44.645-46.436 1.0059.27 C

ATOM 5 CDlILEB 157 2.949-44.3.59-45.008 1.0059.64 C

ATOM^' 6 CG2ILEB157 5.373-43.190-46.243 1.0059.13 C

ATOM 7 C ILEB 157 6.662-44.792-48.424 1.0059.40 C

ATOM 8 O ILEB 157 7.355-45.715-48.006 1.0059.29 O

ATOM 1 N LEUB 158 7.156-43.786-49.138 1.0059.83 N

ATOM 2 CA LEUB 158 8.576-43.723-49.475 1.0060.23 C

ATOM 3 CB LEU B 158. 8.886 -42.471 -50.303' 1.0060.13 C

ATOM 4 CG LEUB 158 9.487-41.410-49.914 0.0050.00 C

ATOM 5 CDl LEUB 158 10.336-41.219-48.711 0.0050.00 C

ATOM 6 CD2LEUB158 10.108-40.676-51.109 0.0050.00 C

ATOM 7 C LEUB 158 9.437-43.761-48.215 1.0060.49 C

ATOM 8 O LEUB 158 9.123-43.110-47.217 1.0060.52 O

ATOM 1 N SERB 159 10.516-44.535-48.265 1.0060.79 N

ATOM 2 CA SERB 159 11.430-44.651-47.135 1.0061.07 C

ATOM 3 CB SERB 159 12.365-45.849-47.322 1.0061.20 C

ATOM 4 OG SERB 159 13.023-46.173-46.109 1.0061.72 O

ATOM 5 C SERB 159 12.240-43.364-46.941 1.0061.06 C

ATOM 6 O SERB 159 13.457-43.338-47.150 1.0061.02 O

TER 6 SERB 159

ATOM 1 N ARGB 167 6.924-37.115-55.151 1.0065.73 N

ATOM 2 CA ARGB 167 6.392-35.811-55.537 1.0065.83 C

ATOM 3 CB ARGB 167 7.500-34.902-56.103 1.0065.92 C

ATOM 4 CG ARGB 167 8.650-34.591-55.146 1.0066.25 C

ATOM 5 CD ARGB 167 9.883-35.448-55.436 1.0066.72 C

ATOM 6 NE ARGB 167 9.774-36.803-54.884 1.0067.11 N

ATOM 7 CZ ARGB 167 10.682-37.760-55.064 1.0067.11 C

ATOM 8 NHl ARG B 167 11.772-37.514-55.788 1.0067.24 N

ATOM 9 NH2ARGB167 10.502 -38.961 -54.523 1.0066.65 N

ATOM 10 ' C ARGB 167 5.283-35.961-56.573 1.0065.75 . C

ATOM 11 O ARG B 167 5.467-35.617-57.741 1.0065.80 O ^'

ATOM 1 N GLYB 168 4.133-36.474-56.149 1.0065.67 N

ATOM 2 CA GLYB 168 3.002-36.639-57.055 1.0065.55 C

ATOM 3 C GLYB 168 1.748-35.936-56.574 1.0065.49 C

ATOM 4 O GLYB 168 1.157-35.132-57.293 1.0065.38 ^' O

ATOM 1 N TYRB 169 1.349-36.239-55.345 1.0065.52 N

ATOM 2 CA TYRB 169 0.108-35.720-54.781 1.0065.52 C ATOM 3 CB TYRB 169 -1.020-36.744-54.967 1.0065.60 C

ATOM 4 CG TYRB 169 -0.560-38.185-54,862 1.0065.63 C

ATOM 5 CDlTYRB 169 -0.309-38.940-56.004 1.0065.74 C

ATOM 6 CEl TYRB 169 0.118-40.256-55.915 1.0065.83 C

ATOM 7 CZ TYRB 169 0.302-40.834-54.673 1.0065.80 C

ATOM 8. OH TYRB 169 0.728-42.140-54.582 1.0065.64 O

ATOM 9 CE2TYRB 169 0.062-40.105-53.523 1.0065.77 C

ATOM 10 CD2TYRB 169 -0.366-38.788-53.623 1.0065.73 C

ATOM 11 C TYRB 169 0.284-35.383-53.298 1.0065.44 C

ATOM 12 O TYRB 169 1.393 -35.459 -52.765 1.0065.44 O

ATOM 1 N ASP B 170 -0.812-35.007-52.641 1.0065.30 N

ATOM 2 CA ASP B 170 -0.794-34.7.11-51.209 1.0065.09 C

ATOM 3 CB ASP B 170 -1.747-33.557-50.884 1.0065.12 C

ATOM 4 CG ASP B 170 -1.398-32.862-49.579 1.0065.25 C

ATOM 5 ODl ASP B 170 ^' -1.812-31.695-49.399 1.0065.06 O

ATOM 6 OD2 ASP B 170 -0.711-33.481-48.734 1.0065.55 O

ATOM 7 C ASP B 170 -1.137-35.965-50.397 1.0064.95 C

ATOM 8 O ASPB 170 -2.198-36.058-49.752 1.0064.78 O

ATOM l^' N PHEB 171 -0.219-36.926-50.441 1.0064.77 N

ATOM 2 CA PHEB 171 -0.407-38.217-49.795 1.0064.63 C

ATOM 3 CB PHEB 171 0.920-38.975-49.718 1.0064.63 C

ATOM 4 CG PHEB 171 0.772-40.414-49.323 1.0064.58 C

ATOM 5 CDlPHEB 171 0.020-41.283-50.095 1.0064.37 C

ATOM 6 CEl PHEB 171 -0.116-42.608-49.737 1.0064.43 C

ATOM- 7 CZ PHEB 171 0.508-43.083-48.598 1.0064.73 C

ATOM 8 CE2PHEB 171 .1.263-42.228-47.821 1.0064.67 C

ATOM 9 CD2PHEB 171 1.393-40.902-48.186 1.0064.81 C

ATOM 10 C PHEB 171 -1.034-38.064-48.413 1.0064.56 C

ATOM 11 O PHEB 171 -2.109-38.616-48.149 1.0064.43 O

ATOM 1 N PRO B 172 -0.372-37.306-47.526 1.0064.52 N

ATOM 2 CA PROB 172 -0.955-37.032-46.220 1.0064.49 C

ATOM 3 CB PRO B 172 -0.073-35.907-45.681 1.0064.54 C

ATOM 4 CG PRO B 172 1.254-36.174-46.298 1.0064.64 C

ATOM 5 CD PRO B 172 0.953-36.678-47.680 1.0064.57 C

ATOM 6 C PRO B 172 -2.416-36.583-46.312 1.0064.39 C

ATOM 7 O PRO B 172 -3.275-37.148-45.625 1.0064.27 O

ATOM 1 N ALAB 173 -2.700-35.592-47.154 1.0064.18 N

ATOM 2 CA ALAB 173 -4.068-35.093-47.287 1.0064.15 C

ATOM 3 CB ALA B.173 -4.141-33.959-48.291 1.0064.18 C

ATOM 4 C ALAB 173 -5.047-36.206-47.657 1.0064.15 C

ATOM 5 O ALAB 173 -6.136-36.305-47.074 1.0064.04 O

ATOM 1 N VALB 174 -4.668-37.051-48.613 1.0064.23 N

ATOM 2 CA VALB 174 -5.545-38.177-48.96.1 1.0064.12 C

ATOM 3 CB VALB 174 -5.127-38.899-50.275 1.0064.14 C

ATOM 4 CGl VAL B 174 -3.689-38.598-50.637 1.0064.11 C

ATOM 5 CG2VALB 174 -5.374-40.397-50.178 1.0064.15 C

ATOM 6 C VALB 174 -5.719-39.162-47.791 1.0064.08 C

ATOM 7 O VALB 174 -6.840-39.617-47.505 1.0063.98 O

ATOM 1 N LEUB 175 -4.621-39.466-47.102 1.0064.02 N

ATOM 2 CA LEUB 175 -4.700 -40.298 -45.907 1.0063.80 C

ATOM 3 CB LEUB 175 -3.313-40.556-45.326 LOO 63.79 C

ATOM 4 CG LEUB 175 -2.668-41.866-45.780 1.0064.02 C

ATOM 5 CDl LEUB 175 -1.260-42.013-45.220 1.0064.02 C

ATOM 6 CD2LEUB175 -3.534-43.050-45.371 1.0064.22 C

ATOM 7 C LEUB 175 -5.607-39.679-44.849 1.0063.78 C

ATOM 8 O LEUB 175 -6.233-40.386-44.063 1.0063.66 O

ATOM 1 N ARG B 176 -5.681-38.355-44.834 1.0063.87 N

ATOM ■ 2 CA ARGB 176 -6.550-37.663-43.894 1.0063.82 C ATOM 3 CB ARG B 176 -6.079-36.223-43.697 1.0063.86 C

ATOM 4 CG ARG B 176 -6.952-35.376-42.788 1.0064.46 C

ATOM 5 CD ARG B 176 -6.216-34.101-42.406 1.0065.87 C

ATOM 6 NE ARG B 176 -5.005-33.929-43.214 1.0066.91 N

ATOM 7 CZ ARG B 176 -4.418-32.760-43.460 1.0067.30 C

ATOM 8 NHl ARG B 176 -3.317-32.717-44.204 1.0067.30 N

ATOM 9 NH2ARGB 176 -4.935-31.635-42.971 1.0067.62 N

ATOM 10 C ARG B 176 -8.010-37.722-44.345 1.0063.65 C

ATOM 11 O ARG B 176 -8÷917 -37.859 -43.520 1.0063.59 O

ATOM 1 N TRPB 177 -8.233-37.633-45.654 1.0063.54 N

ATOM 2 CA TRP B 177 -9.580-37.773-46.215 1.0063.37 C

ATOM 3 CB TRP B 177 -9.525-37.527-47.723 1.0063.31 ^'C

ATOM 4 CG TRP B 177 -10.847-37.583-48.429 1.0063.26 C

ATOM 5 CDl TRP B 177 -11.718-36.549-48.628 1.0062.97 C

ATOM. ^• 6 NEl TRP B 177 -12.817-36.985-49.328 1.0062.77 N

ATOM 7 CE2 TRP B 177 -12.669-38.320-49.603 1.0063.09 C

ATOM 8 CD2 TRP B 177 -11.437-38.731-49.055 1.0063.35 C

ATOM 9 GE3TRPB 177 -11.044-40.069-49.200 1.0063.27 C

ATOM 10 CZ3 TRP B 177 -11.883-40.939-49.878 1.0063.03 C

ATOM 11 CH2 TRP B 177 -13.104-40.500-50.410 1.0063.04 C

ATOM 12 CZ2 TRP B 177 -13.514-39.199-50.284 1.0063.18 C

ATOM 13 C TRP B 177 -10.141-39.168-45.912 1.0063.41 C

ATOM 14 O TRPB 177 -11.280-39.331-45.407 1.0063.24 O

ATOM 1 N PHE B 178 -9.326-40.177-46.211 1.0063.59 N

ATOM 2 CA PHEB 178 -9.661-41.545-45.836 1.0063.57 C

ATOM 3 CB PHEB 178 -8.594-42.526-46.325 1.0063.59 C

ATOM 4 CG PHEB 178 -8.785-42.971-47.746 1.0063.89 C

ATOM 5 CDl PHEB 178 -9.901-43.713-48.111 1.0064.14 C

ATOM 6 CEl PHEB 178 -10.080-44.131-49.422 1.0064.00 C

ATOM 7 CZ PHE B 178 -9.138-43.811 -50.382 1.0063.93 C

ATOM 8 CE2PHEB 178 -8.020-43.076-50.032 1.0064.17 C

ATOM 9 CD2PHEB 178 -7.846-42.660-48.717 1.0064.18 C

ATOM 10 C PHE B 178 -9.845-41.661-44.321 1.0063.55 C

ATOM 11 O PHEB 178 -10.841-42.210-43.851 1.0063.61 O

ATOM ' 1 N ALAB 179 -8.891-41.133-43.558 1.0063.51 N

ATOM 2 CA ALAB 179 -8.979-41.170-42.100 1.0063.38 C

ATOM 3 CB ALAB 179 -7.844-40.377-41.473 1.0063.38 C

ATOM 4 C ALAB 179 -10.332-40.648-41.623 1.0063.30 C

ATOM 5 O ALAB 179 -10.935-41.207-40.705 1.0063,20 O

ATOM 1 N GLUB 180 -10.803-39.574-42.252 1.0063.33 N

ATOM 2 CA GLUB 180 -12.135 -39.051 -41.967 1.0063.25 C

ATOM 3 CB GLUB 180 -12.423-37.789-42.781 1.0063.23 C

ATOM 4 CG GLUB 180 -11.732-36.535-42.289 1.0063.57 C

ATOM 5 CD GLUB 180 -11.933-35.365-43.233 1.0063.57 C

ATOM 6 OEl GLUB 180 -12.583-35.556-44.287 1.0063.87 O

ATOM 7 OE2GLUB 180 -11.436-34.258-42.924 1.0064.08 O

ATOM 8 C GLUB 180 -13.195-40.090-42.288 1.0063.07 C

ATOM 9 O GLUB 180 -14.088-40.338-41.478 1.0063.03 O

ATOM 1 N ARGB 181 -13.101-40:696-43.472 1.0062.95 N

ATOM 2 CA ARGB 181 -14.172-41.605-43.916 1.0062.57 C

ATOM 3 CB ARGB 181 -14.320-41.556-45.436 1.0062.55 C

ATOM 4 CG ARGB 181 -15.181-40.405-45.903 1.0062.92 C

ATOM 5 CD ARGB 181 -14.691-39.845-47.215 1.0063.49 C

ATOM 6 NE ARGB 181 -15.103-38.454-47.389 1.0064.41 N

ATOM 7 CZ ARGB 181 -14.496-37.415-46.820 1.0064.92 - C

ATOM 8 NHl ARG B 181 -14.938-36.180-47.037 1.0065.08 N

ATOM 9 NH2ARGB 181 -13.443-37.606-46.034 1.0065.13 N

ATOM 10 C ARGB 181 -14.087-43.059-43.439 1.0062.33 C ATOM 11 O ARGB 181 -15.104-43.668-43.115 1.0062.41 O

ATOM 1 N VALB 182 -12.877-43.601-43.384 1.0062.04 N

ATOM 2 CA VALB 182 -12.653-45.040-43.220 1.0061.56 C

ATOM 3 CB VALB 182 -11.218-45.378-43.634 1.0061.45 C

ATOM 4 CGl VALB 182 -10.698-46.552-42.853 1.0061.55 C

ATOM 5 CG2VALB182 -11.154-45.623-45.131 1.0061.14 C

ATOM 6 C VALB 182 -12.930-45.596-41.818 1.0061.44 C

ATOM 7 O VALB 182 -12.831-44.875-40.828 1,0061.47 O

ATOM 1 N ASP B 183 -13.272-46.882-41.746 1.0061.33 N

ATOM 2 CA ASPB 183 -13.576-47.554-40.468 1.0061.35 C

ATOM 3 CB ASP B 183 -14.500-48.762-40.685 1.0061.39 C

ATOM 4 CG ASP B 183 -15.966-48.373-40.747 1.0062.09 C

ATOM 5 ODl ASP B 183 -16.748-48.863-39.902 1.0062.54 O

ATOM 6 OD2ASPB183 -16.338-47.569-41.631 1.0063.12 O

ATOM 7 C ASP B 183 -12.342-47.992-39.667 1.0061.13 C

ATOM 8 O ASP B 183 -12.271-47.778-38.455 1.0061.05 . O

ATOM 1 N LEUB 184 -11.394-48.634-40.344 1.0060.90 N

ATOM 2 CA LEUB 184 -10.151-49.082-39.719 1.0060.71 C

ATOM 3 CB LEUB 184 -10.130-50.608-39.576 1.0060.75 C

ATOM 4 CG LEUB 184 -10.626-51.298-38.302 1.0060.63 C

ATOM 5 CDl LEUB 184 -10.247-52.774-38.346 1.0060.23 C

ATOM 6 CD2LEUB184 -10.055-50.648-37.055 1.0060.26 C

ATOM 7 C LEUB 184 -8.948-48.655-40.548 1.0060.59 C

ATOM 8 O LEUB 184 -9.008-48.633-41.776 1.0060.73 O

ATOM 1 N ILEB 185 -7.851-48.320-39.878 1.0060.33 N

ATOM 2 CA ILEB 185 -6.619-47.996-40.573 1.0060.09 C

ATOM 3 CB ILEB 185 -6.170-46.560-40.294 1.0059.94. C

ATOM 4 CGlILEB 185 -7.327-45.592-40.540 1.0059.84 C

ATOM 5 CDl ILEB 185 -6.969-44.139-40.330 1.0059.85 , C

ATOM 6 CG2ILEB185 -4.983-46.203-41.165 1.0059.66 C

ATOM 7 C ILEB 185 -5.539-48.964-40.129 1.0060.22 C

ATOM 8 O ILEB 185 -5.136-48.969-38.968 1.0060.25 O

ATOM 1 N ILEB 186 -5.086-49.799-41.053 1.0060.39 N

ATOM 2 CA ILEB 186 -4.057-50.777-40.738 1.0060.66 C

ATOM 3 CB ILEB 186 -4.285-52.100-41.483 1.0060.60 C

ATOM 4 CGl ILE B 186 -5.722-52.588-41.291 1.0060.80 C

ATOM 5 CDl ILEB 186 -6.119-52.766-39.846 1.0060.97 C

ATOM 6 CG2ILEB186 -3.308-53.141-41.002 1.0060.56 C

ATOM ^•7 C ILEB 186 -2.688-50.230-41.115 1.0060.88 C

ATOM 8 O ILEB 186 -2.435-49.911-42.280 1.0060.99 O

ATOM 1 N LEUB 187 -1.812-50.107-40.126 1.0061.05 N

ATOM 2 CA LEUB 187 -0.445-49.672-40.376 1.0061.25 C

ATOM 3 CB LEUB 187 -0.055-48.542-39.425 1.0061.17 C .

ATOM 4 CG LEUB 187 -0.336-47.107-39.873 1.0060.76 C

ATOM 5 CDl LEUB 187 -1.790-46.918-40.216 1.0060.58 C

ATOM 6 CD2LEUB187 0.075-46.133-38.787 1.0060.96 C

ATOM 7 C LEUB 187 0.520-50.850-40.234 1.0061.68 C

ATOM 8 O LEUB 187 0.545-51.526-39.201 1.0061.88 O

ATOM 1 N LEUB 188 1.306-51.101-41.277 1.0061.91 N

ATOM 2 CA LEUB 188 2.240-52.216-41.256 1.0062.18 C

ATOM 3 CB LEUB 188 2.152-53.033-42.542 1.0062.05 C

ATOM 4 CG LEUB 188 0.838-53.756-42.816 1.0062.08 C

ATOM 5 CDl LEUB 188 1.125-55.091-43.478 1.0061.97 C

ATOM 6 CD2LEUB188 0.084-53.970-41.530 1.0062.07 C

ATOM 7 C LEUB 188 3.669-51.755-41.050 1.0062.53 C

ATOM 8 O LEUB 188 4.128-50.801-41.678 1.0062.71 O

ATOM 1 N PHEB 189 4.362 -52.441 -40.154 1.0062.88 N

ATOM 2 CA PHEB 189 5.797-52.305-40.021 1.0063.25 C ATOM 3 CB PHEB 189 6.152-51.737-38.661 1.0063.06 C

ATOM 4 CG PHEB 189 5.690-50.339-38.458 1.0063.11 C

ATOM 5 CDlPHEB 189 4.415-50.080-37.994 1.0063.21 C

ATOM 6 CEl PHEB 189 3.987-48.781-37.802 1.0063.18 C

ATOM 7 CZ PHEB 189 4.841-47.727-38.078 1.0063.21 C

ATOM 8 CE2PHEB189 6.115-47.974-38.544 1.0063.09 C

ATOM 9 CD2PHEB 189 6.534-49.274-38.731 1.0063.37 C

ATOM 10 C PHEB 189 6.332-53.707-40.128 1.0063.65 C

ATOM 11 O PHEB 189 5.702-54.631-39.626 1.0063.87 O

ATOM 1 N ASP B 190 7.472-53.895-40.779 1.0064.11 N

ATOM. 2 CA ASP B 190 8.012-55.244-40.854 1.0064.78 C

ATOM 3 CB ASP B 190 8.204-55.712-42.308 1.0064.95 C

ATOM 4 CG ASP B 190 9.594-55.455-42.843 1.0065.15 C

ATOM 5 ODl ASP B 190 10.067-54.305-42.750 1.0066.38 O

ATOM 6 OD2 ASP B 190 10.201-56.403-43.386 LOO 64.63 O

ATOM 7 C ASP B 190 9.248-55.446-39.972 1.0065.11 C

ATOM 8 O ASP B 190 10.233-54.713-40.073 1.0065.07 O

ATOM 1 N ALAB 191 9.152-56.441-39.090 1.0065.57 N

ATOM 2 CA ALAB 191 10.175-56.747-38.090 1.0065.98 C

ATOM 3 CB ALAB 191 9.723-57.918-37.239 1.0066.05 C

ATOM 4 C ALAB 191 11.499-57.076-38.740 1.0066.33 C

ATOM 5 O ALAB 191 12.521-57.215-38.072 1.0066.29 O

ATOM 1 N HIS B 192 11.461-57.206-40.057 1.0066.88 N

ATOM 2 CA HIS B 192 12.615-57.594-40.825 1.0067.53 C .

ATOM 3 CB HIS B 192 12.141-58.253-42.110 1.0067.72 C

ATOM 4 CG HISB 192 13.248-58.756-42.971 1.0068.70 C

ATOM 5 NDl HIS B 192 14.167-59.684-42.529 1.0069.77 N .

ATOM 6 CEl HIS B 192 15.024-59.947-43.500 1.0070.36 C .

ATOM 7 KE2 HIS B 192 14.688-59.227-44.556 1.0071.03 N

ATOM 8 CD2 HIS B 192 13.579-58.474-44.251 1.0069.62 C

ATOM 9 C HIS B 192 13.472-56.372-41.132 1.0067.83 C

ATOM 10 O HIS B 192 14.694-56.409-40.993 1.0068.11 O

ATOM 1 N LYS B 193 12.819-55.290-41.547 1.0068.10 N

ATOM 2 CA LYSB 193 13.490-54.027-41.844 1.0068.23 C

ATOM 3 CB LYS B 193 13.471-53.736-43.347 1.0068.19 C

ATOM 4 CG LYS B 193 14.585-54.383-44.153 1.0068.42 C

ATOM 5 CD LYS B 193 14.700 -53.722 -45.523 1.0068.19 C

ATOM 6 CE LYS B 193 14.875-52.216-45.374 1.0068.29 C

ATOM 7 NZ LYS B 193 14.632-51.484-46.644 1.0068.54 N

ATOM 8 C LYSB 193 12.783-52.889-41.133 1.0068.36 C

ATOM 9 O LYS B 193 12.009-52.156-41.750 1.0068.44 O

ATOM 1 N LEUB 194 13.041-52.730-39.843 1.0068.56 N

ATOM 2 CA LEUB 194 12.400-51.653-39.102 1.0068.79 C

ATOM 3 CB LEUB 194 12.608-51.826-37.601 1.0068.92 C

ATOM 4 CG LEUB 194 11.448-51.373-36.716 1.0068.90 C

ATOM 5 CDl LEUB 194 12.004-50.606-35.540 1.0069.72 C

ATOM 6 CD2 LEUB 194 10.462-50.514-37.478 1.0069.07 C

ATOM 7 C LEUB 194 12.930-50.294-39.548 1.0068.86 C.

ATOM 8 O LEUB 194 14.113-49.994-39.399 1.0068.87 O

ATOM 1 N GLUB 195 12.041-49.479-40.102 1.0069.01 N

ATOM 2 CA GLUB 195 12.386-48.129-40.535 1.0069.24 C

ATOM 3 CB GLUB 195 12.967-48.156-41.957 1.0069.19 C

ATOM 4 CG GLUB 195 12.565-46.994-42.859 1.0069.68 C

ATOM 5 CD GLUB 195 13.235-45.679-42.488 1.0070.76 C

ATOM 6 OEl GLUB 195 13.283-45.345-41.286 1.0071.25 O

ATOM 7 OE2GLUB195 13.705-44.968-43.404 1.0070.87 O

ATOM 8 C GLUB 195 11.147-47.238-40.450 1.0069.31 C

ATOM 9 O GLUB 195 10.061-47.641-40.867 1.0069.43 O ATOM 1 N ILEB 196 11.302-46.047-39.870 1.0069.37 N

ATOM 2 CA ILEB 196 10.214-45.058-39.835 1.0069.32 C

ATOM 3 CB ILEB 196 9.694-44.760-38.397 1.0069.37 C

ATOM 4 CGl ILEB 196 9.222-46.045-37.716 1.0069.31 C

ATOM 5 CDl ILEB 196 8.344-45.796-36.508 1.0069.52 C .

ATOM 6 CG2 ILEB 196 8.540-43.749-38.434 1.0069.16 C

ATOM 7 C ILEB 196 10.627-43.763-40.542 1.0069.13 C •

ATOM 8 O ILEB 196 11.208-42.853-39.945 1.0069.00 O

ATOM 1 N SERB 197 10.314-43.707-41.830 1.0068.93 N

ATOM 2 CA SERB 197 10.661 -42.579-42.668 1.0068.80 C

ATOM • 3 CB SERB 197 10.288-42.892-44.112 1.0068.89 C

ATOM 4 OG SERB 197 8.916-43.236-44.204 1.0068.92 O

ATOM 5 C SERB 197 9.958-41.299-42.240 1.0068.69 C

ATOM 6 O SERB 197 8.944-41.331-41.538 1.0068.50 O

ATOM 1 N ASP B 198 10.512-40.174-42.682 1.0068.61 N

ATOM 2 CA ASP B 198 9.921-38.869-42.444 1.0068.54 C

ATOM 3 CB ASP B 198 10.792-37.785-43.081 1.0068.63 C

ATOM 4 CG ASP B 198 10.209-36.394-42.918 1.0069.32 C

ATOM 5 ODl ASP B 198 9.211-36.245-42.179 1.0069.90 O

ATOM 6 OD2 ASP B 198 10.753-35.445-43.529 1.0070.07 O

ATOM 7 C ASP B 198 8.504-38.830-43.017 1.0068.35 C

ATOM 8 O ASP B 198 7.541-38.466-42.323 1.0068.12 O

ATOM 1 N GLUB 199 8.384-39.220-44.283 1.0068.16 N

ATOM 2 CA GLUB 199 7.094-39.264-44.957 1.0068.12 C

ATOM 3 CB GLUB 199 7.244-39.928-46.325 1.0068.13 C

ATOM 4 CG GLUB 199 5.973-39.956-47.166 1.0068.49 C

ATOM 5 CD GLUB 199 6.217-40.500-48.568 1.0068.60 C

ATOM 6 OEl GLUB 199 7.109 -39.966 -49.265 ^'1.0069.43 O

ATOM 7 OE2 GLUB 199 5.517-41.456-48.975 1.0068.91 O

ATOM 8 C GLUB 199 6.050-39.994-44.109 1.0067.92 C

ATOM 9 O GLUB 199 4.890-39.567-44.022 1.0067.83 O

ATOM 1 N PHE B 200 6.466-41.082-43.465 1.0067.72 N

ATOM 2 CA PHE B 200 5.553 -41.851 -42.628 1.0067.53 C

ATOM 3 CB PHE B 2Op 6.213-43.134-42.130 1.0067.63 C

ATOM 4 CG PHE B 200 5.288-44.319-42.102 1.0067.69 C

ATOM 5 CDl PHEB 200 5.610-45.482-42.781 1.0067.87 C

ATOM 6 CEl PHE B 200 • 4.758 -46.574 -42.754 1.0068.11 C

ATOM 7 CZ PHE B 200 3.566-46.505-42.055 1.0067.82 C

ATOM 8 CE2 PHE B 200 3.231-45.351-41.384 1.0067.56 C

ATOM 9 CD2PHEB200 4.089-44.267-41.409 1.0067.81 C

ATOM 10 C PHE B 200 5.045-41.020-41.451 1.0067.43 C

ATOM 11 O PHE B 200 3.840-40.823-41.302 1.0067.23 O

ATOM 1 N SERB 201 5.959-40.522-40.621 1.0067.37 N

ATOM 2 CA SER B 201 5.560-39.690-39.484 1,0067.44 C

ATOM 3 CB SERB 201 6.771-39.271-38.644 1.0067.44 C

ATOM 4 OG SERB 201 7.579-38.337-39.332 1.0067.77 O

ATOM 5 C SERB 201 4.742-38.471-39.927 1.0067.32 C

ATOM 6 O SERB 201 3.934-37.939-39.157 1.0067.15 O

ATOM 1 N GLU B 202 4.954-38.033-41.167 1.0067.40 N

ATOM 2 CA GLU B- 202 4.076-37.031-41.770 1.0067.29 C

ATOM 3 CB GLU B 202 4.615-36.581-43.129 1.0067.36 C

ATOM 4 CG. GLUB 202 _. 5.525-35.366-43.080 1.0067.70 C

ATOM 5- CD GLU B 202 4.825-34.096-43.527 1.0068.43 C

ATOM 6 OEl GLU B 202 3.901-34.193-44.363 1.0068.71 O

ATOM 7 OE2GLUB202 5.204-33.000-43.055 1.0068.82 O

ATOM 8 C GLU B 202 2.668-37.602-41.926 1.0067.11 C

ATOM ^• 9 O GLU B 202 1.676-36.963-41.551 1.0066.97 O

ATOM 1 N ALA B 203 2.584-38.811-42.472 1.0067.08 N ATOM 2 CA ALA B 203 . 1.294-39.491-42.602 1.0066.87 C

ATOM 3 CB ALA B 203 1.470-40.842-43.288 1.0066.88 C .

ATOM 4 C ALA B 203 0.580-39.656-41.250 1.0066.81 C

ATOM 5 O ALA B 203 -0.610-39.327-41.112 1.0066.36 O

ATOM 1 N ILE B 204 1.311-40.164-40.256 1.0066.84 N

ATOM 2 CA ILE B 204 0.764-40.312-38.906 1.0066.68 C

ATOM 3 CB ILE B 204 1.734-41.034-37.958 1.0066.55 C

ATOM 4 CGl ILE B 204 1.908-42,485-38.390 1.0066.77 C^:

ATOM 5 CDl ILEB 204 3.223-42.763-39.062 1.0067.14 C

ATOM 6 CG2ILEB204 1.218-40.998-36.538 1.0066.27 C

ATOM 7 C ILE B 204 0.375-38.957-38.316 1.0066.71 C

ATOM 8 O ILE B 204 -0.602-38.850-37.571 1.0066.75 O

ATOM 1 N GLY B 205 1.141-37.922-38.648 1.0066.74 N

ATOM 2 CA GLY B 205 0.737-36.565-38.308 1.0066.51 C

ATOM 3 C GLY B 205 -0.615-36.275-38.937 1.0066.38 C

ATOM 4 O GLY B 205 -1.457-35.597-38.342 1.0066.39 O

ATOM 1 N ALA B 206 -0.826-36.806-40.140 1.0066.29 N

ATOM 2 CA ALA B 206 -2.073-36.575-40.877 1.0065.87 C

ATOM 3 CB ALA B 206 -1.866-36.813-42.368 1.0065.95 C

ATOM 4 C ALA B 206 -3.243-37.407-40.365 1.0065.58 C

ATOM 5 O ALAB 206 -4.400-37.072-40.603 1.0065.48 O

ATOM 1 N LEU B 207 -2.946-38.499-39.673 1.0065.49 N

ATOM 2 CA LEU B 207 -4.006-39.322-39.088 1.0065.08 C

ATOM 3 CB LEU B 207 -3.540-40.769-38.935 1.0065.03 C

ATOM 4 CG LEU B 207 -3.898-41.743-40.060 1.0065.05 C

ATOM 5 CDl LEUB 207 -3.971 -41.051 -41.411 1.0065.29 C

ATOM 6 CD2LEUB207 -2.898-42.885-40.101 1.0065.61 C

ATOM. 7 C LEU B 207 -4.509-38.785-37.747 1.0064.97 C

ATOM 8 O LEU B 207 -5.404-39.364-37.133 1.0064.88 O

ATOM 1 N ARG B 208 -3.933-37.674-37.301 1.0064.92 N

ATOM 2 CA ARGB 208 -4.271-37.083-36.004 1.0064.83 C

ATOM 3 CB ARG B 208 -3.525-35.751-35.819 1.0064.82 C

ATOM 4 CG ARG B 208 -4.134-34.791-34.796 1.0064.69 C

ATOM 5 CD ARG B 208 -3.025-34.039-34.043 1.0064.59 C

ATOM 6 NE ARG B 208 -3.246-32.581-33.961 1.0064.85 N

ATOM 7 CZ ARG B 208 -4.343-31.934-34.378 1.0064.78 C

ATOM 8 NHl ARG B 208 -5.373 -32.594 -3.4.925- 1.0065.02 N

ATOM 9 NH2 ARG B 208 -4.407-30.609-34.238 1.0064.48 N

ATOM 10 C ARG B 208 -5.779-36.913-35.789 1.0064.76 C

ATOM 11 O ARG B 208 -6.493-36.423-36.665 1.0064.84 O

ATOM 1 N GLY B 209 -6.253-37.327-34.617 1.0064.60 N

ATOM 2 CA GLY B 209 -7.663-37.188-34.261 1.0064.23 C

ATOM 3 C GLY B 209 -8.447-38.455-34.531 1.0063.99 C

ATOM 4 O GLY B 209 -9.631-38.553-34.206 1.0063.84 O

ATOM 1 N HIS B 210 -7.781-39.431-35.134 1.0063.86 N

ATOM 2 CA HIS B 210 -8.432-40.685-35.475 1.0063.78 C

ATOM 3 CB HIS B 210 -8.683-40.769-36.983 1.0063.93 C

ATOM 4 CG HIS B 210 -9.689-39.779-37.482 1.0064.53 C

ATOM 5 NDl HIS B 210 -9.380-38.807-38.409 1.0065.05 N

ATOM 6 CEl HIS B 210 -10.455-38.079-38.655 1.0065.36 C

ATOM 7 NE2 HIS B 210 -11.449-38.540-37.916 1.0065.43 N

ATOM 8 CD2 HIS B 210 -10.996-39.602-37.172 1.0065.12 C

ATOM 9 C HIS B 210 -7.632-41.891-35.005 1.0063.46 C

ATOM 10 O HIS B 210 -7.808-42.996-35.517 1.0063.56 O

ATOM 1 N GLUB 211 -6.761-41.682-34.023 1.0063.02 N

ATOM 2 CA GLUB 211 -5.938-42.767-33.510 1.0062.65 C

ATOM 3 CB GLUB 211 -5.082-42.298-32:335 1.0062.67 C

ATOM 4 CG GLUB 211 -5.511-40.968-31.750 1.0063.51 C ATOM 5 CD GLUB 211 -4.739-39.803-32.341 1.0064.41 C

ATOM 6 OEl GLUB 211 -5.237-38.656-32.290 1.0064.72 - O

ATOM 7 OE2 GLUB 211 -3.626-40.038-32.856 1.0064.94 O

ATOM 8 C GLUB 211 -6.761-43.999-33.127 1.0062.27 C

ATOM 9 O GLUB 211 -6.280-45.128-33.235 1.0062.45 O

ATOM 1 N ASP B 212 -8.002-43.786-32.701 1.0061.63 N

ATOM 2 CA ASP B 212 -8.856-44.897-32.283 1.0061.13 C

ATOM 3 CB ASP B 212 -10.158-44.381-31.677 1.0061.30 C

ATOM 4 CG ASP B 212 -10.999-43.615-32.676 1.0062.39 C

ATOM 5 ODl ASP B 212 -10.792-42.385-32.807 1.0063.83 O

ATOM 6 OD2 ASP B 212^" -11.874-44.239-33.322 1.0063.08 O

ATOM 7 C ASP B 212 -9.164-45.858-33.428 1.0060.47 C

ATOM^' 8 O ASP B 212 -9.609-46.983-33.202 1.0060.32 O

ATOM 1 N LYS B 213 -8.927-45.410-34.654 1.0059.79 N

ATOM 2 CA LYS B 213 -9.201-46.226-35.825 1.0059.18 C

ATOM 3 CB LYS B 213 -9.712-45.361-36.974 1.0059.14 C

ATOM 4 CG LYS B 213 -11.066-44.724-36.747 1.0059.05 C,

ATOM. 5 CD LYS B 213 -11.580-44.131-38.052 1.0059.11 C

ATOM 6 CE LYS B 213 -12.808-43.262-37.850 1.0058.78 C

ATOM 7 NZ LYS B 213 -13.143-42.542-39.105 1.0058.30 N

ATOM 8 C LYS B 213 -7.956-46.962-36.282 1.0058.86 C

ATOM 9 O LYS B 213 -7.964-47.627-37.315 1.0058.84 O

ATOM 1 N ILE B 214 -6.884-46.851-35.511 1.0058.47 N

ATOM 2 CA ILE B 214 -5.599-47.377-35.948 1.0058.17 C

ATOM 3 CB ILE B 214 -4.467-46.389-35.634 1.0058.12 C

ATOM 4 CGl ILE B 214 -4.670-45.098-36.424 1.0058.10 C

ATOM 5 CDl ILEB 214 -3.652-44.022-36.118 1.0058.21 C

ATOM 6 CG2ILEB214 -3.122-47.009-35.959 1.0058.27 C

ATOM 7 C ILE B 214 -5.245-48.735-35.352 1.0057.94 C

ATOM 8. O ILE B 214 -5.231-48.908-34.137 1.0058.08 O

ATOM 1 N. ARG B 215 -4.960-49.698-36.219 1.0057.63 N

ATOM 2 CA ARG B 215 -4.361-50.946-35.782 1.0057.37 C

ATOM 3 CB ARG B 215 -5.175-52.152-36.242 1.0057.18 C

ATOM 4 CG ARG B 215 -6.611-52.145-35.811 1.0056.81 C

ATOM 5 CD ARG B 215 -6.766-51.984-34.314 1.0056.23 C

ATOM 6 NE ARG B 215 -8.176-51.817-33.978 1.0056.42 N

ATOM 7 CZ ARG B 215 -8.802-50.645-33.950 1.0056.18 C

ATOM 8 NHl ARG B 215 -8.140-49.527-34.219 1.0056.41 N

ATOM 9 NH2ARGB215 -10.090-50.591-33.649 1.0055.83 N

ATOM 10 C ARG B 215 -2.972-51.029-36.380 1.0057.38 C

ATOM 11 O ARG B 215 -2.820-51.179-37.596 1.0057.59 O

ATOM 1 N. VALB 216 -1.961-50.913-35.526 1.0057.17 N

ATOM 2 CA VALB 216 -0.575-51.040-35.949 1.0056.79 C

ATOM 3 CB VAL B 216 0.346-50.313-34.971 1.0056.68 C

ATOM 4 CGl VAL B 216 1.797-50.608-35.293 1.0056.77 C

ATOM 5 CG2VALB216 0.069-48.823-34.997 1.0056.69 C

ATOM 6 C VAL B 216 -0.188-52.506-35.942 1.0056.67 C

ATOM 7 O VALB 216 -0.159-53.124-34.884 1.0056.91 O

ATOM 1 N VALB 217 0.105-53.079-37.105 1.0056.39 N

ATOM 2 CA VALB 217. 0.520-54.478-37.123 1.0056.08 C

ATOM 3 CB VALB 217 -0.406-55.381-37.978 1.0056.09 C

ATOM 4 CGl VALB 217 -1.604-54.600-38.471 1.0055.83 C

ATOM 5 CG2 VALB 217 ^■0.352-56.004-39.138 1.0056.09 C

ATOM 6 C VAL B 217 1.971-54.632-37.548 1.0056.01 C

ATOM 7 O VALB 217 2.388-54.152-38.608 1.0056.14 O

ATOM 1 N LEU B 218 2.734-55.297-36.688 1.0055.76 N

ATOM 2 CA LEU B 218 4.136-55.593-36.933 1.0055.35 C

ATOM 3 CB LEUB 218 4.878-55.634-35.604 1.0055.27 C ATOM 4 CG LEUB 218 6.311-56.137-35.529 1.0055.27 C

ATOM 5 CDl LEUB 218 7.252-55.189-36.244 1.0055.39 C

ATOM 6 CD2LEUB218 6.683-56.270-34.066 1.0055.68 C

ATOM 7 C LEUB 218 4.239-56.926-37.670 1.0055.33 C

ATOM 8 O LEUB 218 4.112-58.006-37.084 1.0055.26 O

ATOM 1 N ASNB 219 4.460-56.830-38.972 1.0055:33 N

ATOM 2 CA ASNB 219 4.411-57.970-39.865 1.0055.16 C

ATOM 3 CB ASNB 219 4.108-57.479-41.276 1.0055.29 C

ATOM 4 CG ASNB 219 3.409-58.516-42.109 1.0055.94 C

ATOM 5 ODl ASNB 219 3.026-59.575-41.601 1.0056.02 O

ATOM 6 ND2ASNB219 3.234-58.225-43.403 1.0056.54 N

ATOM 7 C ASNB 219 5.693-58.789-39.875 1.0055.04 C

ATOM 8 O ASNB 219 6.704-58.388-39.301 1.0054.74 O

ATOM 1 N LYS B 220 5.632-59.937-40.546 1.0055.21 N

ATOM 2 CA LYS B 220 6.756-60.871-40.681 1.0055.41 C

ATOM 3 CB LYS B 220 7.602-60.553-41.925 1.0055.43 C

ATOM 4 CG LYS B 220 7.598-59.096-42.343 1.0055.52 C

ATOM 5 CD LYS B 220 7.343-58.922-43.840 1.0055.10 C

ATOM 6 CE LYS B 220 8.608-58.547-44.594 1.0055.18 C

ATOM 7 NZ LYS B 220 8.297-57.685-45.768 1.0054.26 N

ATOM 8 C LYS B 220 7.627-61.022-39.437 1.0055.67 C

ATOM 9 O LYS B 220 8.848-61.107-39.531 1.0055.78 O

ATOM 1 N ALAB 221 6.987-61.082-38.273 1.0056.06 N

ATOM 2 CA ALAB 221 7.691-61.285-37.011 1.0056.27 C

ATOM. 3 CB ALAB 221 6.764-61.039-35.842 1.0056.15 C

ATOM 4 C ALAB 221 8.259-62.689-36.932 1.0056.45 C

ATOM 5 O ALAB 221 9.042-62.996-36.042 1.0056.60 O

ATOM 1 N ASP B 222 7.864-63.540-37.869 1.0056.79 N

ATOM 2 CA ASP B 222 8.275-64.932-37.840 1.0057.20 C

ATOM 3 CB ASP B 222 7.246-65.817-38.537 1^".OO 57.26 C

ATOM 4 CG ASP B 222 7.446-65.865-40.042 1.0058.12 C

ATOM 5 ODl ASP B 222 7.687-66.978-40.571 1.0058.75 O

ATOM 6 OD2ASPB222 7.383-64.791-40.692 1.0058.98 O

ATOM 7 C ASP B 222 9.609-65.106-38.530 1.0057:37 C

ATOM 8 O ASP B 222 10.166-66.205-38.549 1.0057.48 O

ATOM 1 N MET B 223 10.120-64.038-39.124 1.0057.52 N

ATOM 2 CA MET B 223 11.365-64.182-39.853 1.0057.98 C

ATOM 3 CB MET B 223 11.214-63.751-41.312 1.0057.98 C

ATOM 4 CG MET B 223 11.104-62.271-41.558 1.0058.43 C

ATOM 5 SD MET B 223 11.298-61.968-43.330 1.0059.28 S

ATOM 6 CE MET B 223 12.766-62.938-43.695 1.0059.20 C

ATOM 7 C MET B 223 12.525-63.489-39.163 1.0057.63 C

ATOM 8 O MET B 223 13.437 -62.975 r39.807 1.0057.84 O

ATOM 1 N VAL B 224 12.495-63.514-37.838 1.0057.30 N ^•

ATOM 2 CA VAL B 224 13.536-62.896-37.049 1.0056.98 C

ATOM 3 CB VAL B 224 13.260-61.386-36.882 1.0056.86 C

ATOM 4 CGl VAL B 224 12.529-61.108-35.585 1.0056.82 C

ATOM 5 CG2VALB224 14.547-60.602-36.947 1.0056.98 C

ATOM 6 C VAL B 224 13.608-63.608-35.700 1.0056.86 C

ATOM 7 O VAL B 224 12.583-63.957-35.119 1.0056.87 O

ATOM 1 N GLU B 225 14.818-63.856-35.218 1.0056.71 N

ATOM 2 CA GLU B 225 14.987-64.536-33.946 1.0056.69 C

ATOM 3 CB GLU B 225 16.468-64.682-33.627 1.0057.01 C

ATOM 4 CG GLU B 225 16.782-65.935-32.848 1.0058.92 C

ATOM 5 CD GLU B 225 16.999-67.130-33.754 1.0061.73 C

ATOM 6 OEl GLUB 225 16.006-67.812-34.110 1.0062.80 O

ATOM ^•7 OE2GLUB225 18.171 -67.378 -34.122 1.0063.64 O

ATOM 8 C GLU B 225 14.287 -63.731 -32.854 1.0056.21 C ATOM 9 O GLU B 225 14.195-62.512-32.948 1.0056.09 O

ATOM 1 N THR B 226 13.808-64.399-31.812 1.0055.84 N

ATOM. 2 CA THR B 226 12.913-63.730-30.861 1.0055.74 C

ATOM 3 CB THR B 226 12.207-64.715-29.894 1.0055.64 C

ATOM 4 OGl THRB 226 12.183-64.152-28.577 1.0055.50 O

ATOM 5 CG2THRB226 12.920-66.054-29.862 1.0056.27 C

ATOM 6 C THR B 226 13.473-62.487-30.127 1.0055.65 C

ATOM 7 O THR B 226 12.854-61.416-30.168 1.0055.72 O

ATOM 1 N GLN B 227 14.618-62.618-29.457 1.0055.48 N

ATOM 2 CA GLN B 227 15.255-61.451-28.828 1.0055.18 C

ATOM 3 CB GLN B 227 16.718-61.737-28.508 1.0055.14 C

ATOM 4 CG GLN B 227 16.996-62.165-27.086 1.0054.85 C

ATOM 5 CD GLN B 227 18.445-62.543-26.892 1.0054.43 C

ATOM 6 OEl GLN B 227. 19.045 -63.201 -27.747- 1.0053.99 O

ATOM 7 NE2GLNB227 19.023-62.124-25.772 1.0054.27 N

ATOM 8 C GLN B 227 15.191-60.245-29.757 1.0055.20 C

ATOM 9 O GLN B 227 14.762-59.151-29.362 1.0055.06 O

ATOM 1 N GLN B 228 15.630-60.463-30.995 1.0055.21 N

ATOM 2 CA GLNB 228 15.591-59.450-32.035 1.0055.26 C

ATOM 3 CB GLNB 228 16.104-60.039-33.345 1.0055.25 C

ATOM 4 CG GLN B 228 15.985-59.113-34.533 1.0055.38 C

ATOM 5 CD GLN B 228 16.759-57.832-34.349 1.0055.86 C

ATOM 6 OEl GLNB 228 17.766-57.794-33.640 1.0056.42 ■ O

.ATOM 7 NE2GLNB228 16.295-56.769-34.991 1.0056.22 N

ATOM 8 C GLN B 228 14.180-58.880-32.213 1.0055.39 C

ATOM ,9 O GLN B 228 13.996-57.660-32.302 1.0055.39 O

ATOM 1 N LEU B 229 13.184-59.761-32.256 1.0055.35 N .

ATOM ^' 2 CA LEU B 229 11.793-59.320-32.292 1.0055.42 C

ATOM 3 CB LEU B 229 10.836-60.506-32.164 1.0055.40 C

ATOM 4 CG LEU B 229 9.514-60.430-32.927 1.0055.19 C

ATOM 5 CDl LEU B 229 8.475-61.296-32.239 1,0055.13 C

ATOM 6 CD2LEUB229 9.024-59.001-33.040 1.0054.53 C

ATOM 7 C LEU B 229 11.545-58.334-31.155 1.0055.47 C

ATOM 8 O LEU B 229 11.095-57.209-31.390 1.0055.55. O

ATOM 1 N MET B 230 11.854-58.752-29,928 1.0055.41 N

ATOM 2 CA MET B 230 11.723-57.862-28.775 1.0055.26 C

ATOM 3 CB MET B 230 12.318-58.497-27.519 1.0055.44 C

ATOM 4 CG MET B 230 11.610 -59.763 -27.089 1.0055.41. C

ATOM 5 SD MET B 230 9.837-59.494-26.920 1.0056.86 S

ATOM 6 CE MET B 230 9.228-61.082-27.495 1.0056.24 C

ATOM 7 C MET B 230 12.389-56.523-29.053 1.0055.18 C

ATOM 8 O MET B 230 11.804-55.459-28.819 1.0055.12 O

ATOM 1 N ARG B 231 13.612-56.581-29.567 1.0055.12 N.

ATOM 2 CA ARGB 231 14.336-55.368-29.936 1.0055.21 C

ATOM 3 CB ARGB 231 15.686-55.730-30.553 1.0055.10 C

ATOM 4 CG ARGB 231 16.874-55.530-29.624 1.0055.70 C

ATOM 5 CD ARGB 231 17.000-56.597-28.551 1.0056.51 C

ATOM 6 NE ARG B 231 16.166-56.309-27.391 1.0057.65 N

ATOM 7 CZ ARGB 231 16.040-57.120-26.346 1.0057.94 C

ATOM 8 NHl ARGB 231 16.704-58.268-26.313 1.0057.78 N

ATOM 9 NH2ARGB231 15.248-56.782-25.337 1.0058.31 N

ATOM 10 C ARGB231 13.531-54.457-30.878 1.0055.08 C

ATOM 11 O ARG B 231 13.334 -53.258 -30.599 1.0054.91 O

ATOM 1 N VAL B 232 13.057-55.032-31.982 1.0054.99 N

ATOM 2 CA VALB 232 12.296-54.267-32.966 1.0054.96 C

ATOM 3 CB VAL B 232 11.980-55.100-34.219 1.0054.88 ^' C

ATOM 4 CGl VAL B.232 10.943-54.407-35.060 1.0055.17 C

ATOM 5 CG2VALB232 13.228-55.310-35.035 1.0055.17 C ATOM 6 C VAL B 232 11.006-53.702-32.365 1.0054.91 C

ATOM 7 O VAL B 232 10.780-52.485-32.380 1.0054.68 O

ATOM 1 N TYR B 233 10.168-54.583-31.828 1.0054.85 N

ATOM 2 CA TYR B 233 8.951-54.152-31.159 1.0054.67 C

ATOM 3 CB TYRB 233 8.336-55.333-30.413 1.0054.48 C

ATOM 4 CG TYRB 233 7.076-55.026-29.642 1.0054.61 C

ATOM 5 CDl TYRB 233 6.701-55.811-28.562 1.0054.70 C

ATOM ^•6 CEl TYRB 233 5.552-55.544-27.848 1.0054.44 C

ATOM 7 CZ TYRB 233 4.764-54.480-28.205 1.0054.26 C

ATOM 8 OH TYR B 233 3.623-54.219-27.489 1.0054.47 ^' O

ATOM 9 CE2TYRB233 5.112-53.681-29.271 1.0054.50 C

ATOM 10 CD2 TYRB 233 6.263-53.955-29.985 1.0054.77 C

ATOM 11 C TYR B 233 9.244-52.964-30.226 1.0054.73 C

ATOM 12 O TYRB 233 8.578-51.909-30.297 1.0054.67 O

ATOM 1 N GLY B 234 10.257-53.129-29.375 1.0054.80 N

ATOM 2 CA GLY B 234 10.703-52.047-28.502 1.0054.70 C

ATOM 3 C GLY B 234 10.935-50.754-29.268 1.0054.80 C

ATOM 4 O GLY B 234 10.356-49.698-28.933 1.0054.91 O

ATOM 1 N ALA B 235 11.770-50.830-30.305 1.0054.65 N

ATOM 2 CA ALAB 235 12.066-49.651-31.120 1.0054.39 C

ATOM 3 CB ALA B 235 13.000-50.015-32.250 1.0054.36 C

ATOM 4 C ALAB 235 10.792-49.002-31.667 1.0054.45 C

ATOM 5 O ALA B 235 10.587-47.784-31.538 1.0054.48 O

ATOM 1 N LEU B 236 9.936-49.824-32.269 1.0054.43 _, N

ATOM 2 CA LEU B 236 8.672-49.355-32.815 1.0054.31 C

ATOM ^■ 3 CB LEU B 236 7.805-50.532-33.245 1.0054.32 C

ATOM 4 CG LEUB 236 6.964-50.421-34.521 1.0054.14 C

ATOM 5 CDl LEUB 236 6.530-49.007-34.824 1.0054.03 C

ATOM 6 CD2LEUB236 5,765-51.350-34.440 1.0053.68 C .

ATOM 7 C LEU B 236 7.923-48.558-31.768 1.0054.43 C

ATOM 8 O LEUB 236 7.626-47.383-31.973 1.0054.51 O

ATOM 1 N MET B 237 7.615-49.192-30.638 1.0054.66 N

ATOM 2 CA MET B 237 6.798-48.506-29.630 1.0054.81 C

ATOM 3 CB MET B 237 6.388-49.435-28.488 1.0054.86 C

ATOM 4 CG MET B 237 5.420-50.528-28.919 1.0055.85 • C

ATOM 5 SD MET B 237 3.853-49.943-29.618 1.0057.46 S

ATOM 6 CE MET B 237 2.887-49.728-28.124 1.0056.82 C

ATOM 7 C MET B 237 7.470-47.250-29.097 1.0054.74 C

ATOM 8 O MET B 237 6.792-46.278-28.762 1.0054.99 O

ATOM 1 N TRP B 238 8.796-47.261-29.028 1.0054.61 N

ATOM . 2 CA TRP B 238 9.517-46.061-28.619 1.0054.49 C

ATOM 3 CB TRP B 238 11.004-46.358-28.620 1.0054.42 C

ATOM 4 CG TRP B 238 11.685-45.961-27.380 1.0054.35 C

ATOM 5 CDl TRP B 238 11.545-46.533-26.150 1.0054.85 C

ATOM 6 NEl TRP B 238 12.352-45.899-25.236 1.0054.83 N

ATOM 7 CE2 TRP B 238 13.037-44.903-25.877 1.0054.14 C

ATOM 8 CD2 TRP B 238 12.639-44.916-27.231 1.0053.92 C

ATOM 9 CE3 TRP B 238 13.196-43.991-28.107 1.0053.71. C

ATOM 10 CZ3 TRP B 238 14.112-43.100-27.618 1.0054.62 C

ATOM 11 CH2 TRP B 238 14.486-43.109-26.266 1.0054.60 C

ATOM 12 CZ2 TRP B 238 13.961-44.004-25.384 1.0054.05 C

ATOM 13 C TRP B 238 9.237 -44.921 -29.596 1.0054.52 C

ATOM 14 O TRP B 238 8.748-43.827-29.230 1.0054.67 O

ATOM 1 N ALAB 239 9.549-45.206-30.855 1.0054.59 N

ATOM 2 CA ALA B 239 9.352-44.262-31.942 1.0054.74 C

ATOM ^'3 CB ALAB 239 9.719-44.915-33.266 1.0054.68 C

ATOM 4 C ALAB 239 7.917-43.746-31.979 1.0054.79 C

ATOM 5 O ALA B 239 7.672-42.547-31.812 1.0055.14 O ATOM 1 N LEU B 240 6.975-44.661-32.203 1.0054.72 N

ATOM 2 CA LEU B 240 5.561 -44.311 -32.240 1.0054.66 C

ATOM 3 CB LEU B 240 4.693-45.565-32.320 1.0054.59 C

ATOM 4 CG LEU B 240 4.544-46.206-33.699 1.0054.30 C

ATOM 5 CDl LEU B 240 3.564-47.363-33.633 1.0054.48 C

ATOM 6 CD2LEUB240 4.092-45.186-34.731 1.0053.92 C

ATOM 7 C LEU B 240 5.183-43.482-31.023 1.0054.72 . C

ATOM 8 O LEU B 240 4.561-42.429-31.154 1.0054.60 O

ATOM 1 N GLY B 241 5.567-43.962-29.843 1.0054.91 ^" N

ATOM 2 CA GLY B 241 5.414-43.188-28.620 1.0055.18 C

ATOM 3- C GLY B 241 5.758-41.726-28.845 1.0055.50 C

ATOM 4 O GLY B 241 4.910-40.842-28.654 1.0055.56 O

ATOM 1 N LYS B 242 6.997-41.464-29.262 1.0055.54 N

ATOM 2 CA LYS B 242 7.430-40.079-29.518 1.0055.84 C

ATOM 3 CB LYS B 242 8.936-40.037-29.805 1.0055.91 C

ATOM 4 CG LYS B 242 9.394-38.929-30.744 1.0056.07 C

ATOM 5 CD LYS B 242 9.523-37.591-30.035 1.0056.51 C

ATOM 6 CE LYS B 242 10.365-36.620-30.852 1.0056.40 . C

ATOM 7 NZ LYS B 242 11.764-37.109-31.001 1.0056.49 N

ATOM 8 C LYS B 242 6.641-39.370-30.634 1.0056.01 C

ATOM 9 O LYS B 242 6.393-38.168-30.555 1.0055.92 O

ATOM 1 N VAL B 243 6.236-40.121-31.656 1.0056.28 N

ATOM 2 CA VAL B 243 5.597-39.540-32.849 1.0056.96 C

ATOM 3 CB VAL B 243 5.682-40.487-34.074 1.0057.04 C

ATOM 4 CGl VALB 243 5.080-39.818-35.311 1.0056.83 C

ATOM 5 CG2VALB243 7.125-40.904-34.333 1.0057.52 C

ATOM 6 C VAL B 243 4.137-39.111-32.678 1.0057.22 C

ATOM 7 O VAL B 243 3.826-37.939-32.860 1.0057.33 O

ATOM 1 N VAL B 244 3.244-40.051-32.355 1.0057.66 N

ATOM 2 CA VAL B 244 1.807-39.748-32.281 1.0058.09 C

ATOM 3 CB VAL B 244 0.922-41.016-32.298 1.0057.99 C

ATOM 4 CGl VALB 244 1.602-42.136-33.060 1.0058.05 C

ATOM 5 CG2VALB244 0.598-41.459-30.895 1.0057.87 C

ATOM 6 C VAL B 244 1.443-38.882-31.071 1.0058.63 C

ATOM ^•7 O VAL B 244 0.437-38.174-31.092 1.0058.67 O

ATOM 1 N GLY B 245 2.253-38.957-30.017 1.0059.32 N

ATOM 2 CA GLY B 245 2.209-37.975-28.923 1.0060.12 C

ATOM 3 C GLY B 245 1.073-38.053-27.916 1.0060.64 C

ATOM 4 O GLY B 245 1.096-37.358-26.896 1.0060.52 O

ATOM 1 N THR B 246 0.078-38.891-28.202 1.0061.23 N

ATOM 2 CA THR B 246 -1.045-39.111-27.289 1.0061.72 C

ATOM 3 CB THR B 246 -2.213-39.822-28.006 1.0061.77 C

ATOM 4 OGl THR B 246 -3.278-40.049-27.076 1.0062.38 O

ATOM 5 CG2THRB246 -1.764-41.160-28.576 1.0061.63 C

ATOM 6 C THR B 246 -0.609-39.947-26.080 1.0061.92 C

ATOM 7 O THR B 246 0.221-40.838-26.217 1.0061.87 O

ATOM 1 N PRO B 247 -1.152-39.646-24.885 1.0062.13 N

ATOM 2 CA PRO B 247 -0.824-40.447-23.703 1.0062.22 C

ATOM 3 CB PRO B 247 -1.435-39.644-22.545 1.0062.11 C

ATOM 4 CG PRO B 247 -1.723-38.284-23.112 1.0062.24 C

ATOM 5 CD PRO B 247 -2.056-38.535-24.550 1.0062.13 C

ATOM 6 C PRO B 247 -1.422-41.857-23.748 1.0062.38 C

ATOM 7 O PRO B 247 -1.018-42.714-22.962 i.0062.55 O

ATOM 1 N GLU B 248 -2.369-42.095-24.655 1.0062.37 N

ATOM 2 CA GLU B 248 -2.954-43.427-24.818 1.0062.39 C

ATOM 3 CB GLU B 248 -4.428-43.337-25.218 1.0062.54 C

ATOM 4 CG GLU B 248 -5.252-42.415-24.341 1.0063.55 C

ATOM 5 CD GLU B 248 -5.301-41.000-24.881 1.0064.86 C ATOM 6 OEl GLU B 248 -5.033-40.048-24.111 1.0065.06 O

ATOM 7 OE2 GLUB 248 -5.603-40.844-26.085 1.0065.69 O

ATOM 8 C GLU B 248 -2.187-44.235-25.853 1.0062.14 C

ATOM 9 O GLU B 248 -2.024-43.801-26.991 1.0062.25 O

ATOM 1 N VAL B 249 -1.734-45.419-25.454 1.0061.87 N

ATOM 2 CA VAL B 249 -0.874-46.254-26.293 1.0061.58 C

ATOM 3 CB VAL B 249 0.014-47.184-25.424 1.0061.51 C

ATOM 4 CGl VALB 249 -0.721-47.608-24.163 1.0061.83 C

ATOM 5 CG2VALB249 0.465-48.396-26.209 1.0061.54 C

ATOM 6 C VAL B 249 -1.634-47.072-27.345 1.0061.44 C

ATOM 7 O VAL B 249 -2.670-47.671-27.060 1.0061.45 O

ATOM 1 N LEU B 250 -1.108-47.082-28.565 1.0061.36 N

ATOM 2 CA LEU B 250 -1.689-47.851 -29.659 1.0061.27 C

ATOM 3 CB LEU B 250 -1.162-47.347-31.002 1.0061.02 C

ATOM 4 CG LEU B 250 -2.082-46.481-31.862 1.0060.92 C

ATOM 5 CDl LEUB 250 -2.866-45.482-31.035 1.0061.76 C

ATOM 6 CD2 LEU B 250 -1.277-45.765-32.921 1.0061.02 C

ATOM 7 C LEU B 250 -1,388-49.335-29.522 1.0061.49 C

ATOM 8 O LEU B 250 -0.289-49.725-29.129 1.0061.64 O

ATOM 1 N ARG B 251 -2.371-50.161-29.858 1.0061.69 N

ATOM 2 CA ARG B 251 -2.193-51.606-29.865 1.0061.74 C

ATOM 3 CB ARGB 251 -3.560-52.294-29.827 1.0061.77 C

ATOM 4 CG ARG B 251 -3.556-53.780-30.178 1.0061.82 C

ATOM 5 CD ARGB 251 -3.114-54.629-28.998 1.0061.89 C

ATOM 6 NE ARGB 251 -3.929-55.833-28.873 1.0061.71 N

ATOM 7 CZ ARGB 251 -3.557-57.040-29.285 1.0061.63 C

ATOM .8 NHl ARG B 251 -2.374-57.216-29.853 1.0061.74 N

ATOM 9 NH2ARGB251 -4.375-58.072-29.132 1.0061.58 N

ATOM 10 C ARG B 251 -1.446-52.033-31.121 1.0061.79 C

ATOM 11 O ARGB 251 -1.820-51.641-32.227 1.0061.72 O

ATOM 1 N VAL B 252 -0.390-52.825-30.954 1.0061.91 N

ATOM 2 CA VAL B 252 0.235-53.487-32.105 1.0062.11 C

ATOM 3 CB VAL B 252 1.776-53.317-32.142 1.0062.15 C

ATOM 4 CGl VAL B.252 2.143-51.846-32.199 1.0062.31 Cf!

ATOM 5 CG2VALB252 2.415-53.976-30.934 1.0062.44 C

ATOM 6 C VAL B 252 -0.125-54.972-32.144 1.0061.92 C

ATOM 7 O VAL B 252 -0.175-55.633-31.107 1.0061.98 O

ATOM 1 N TYRB 253 -0.394-55.482-33.342 1.0061.76 N

ATOM 2 CA TYR B 253 -0.691 -56.898 -33.532 1.0061.60 C

ATOM 3 CB TYRB 253 -1.914-57.072-34.434 1.0061.60 C

ATOM 4 CG TYR B 253 -3.179-56.478-33.847 1.0062.19 C

ATOM 5 CDl TYR B 253 -3.706-55.293-34.334 1.0062.55 C

ATOM 6 CEl TYR B 253 -4.859-54.749-33.792 1.0062.44 C

ATOM 7 CZ TYR B 253 -5.493-55.384-32.751 1.0061.97 C

ATOM 8 OH TYR B 253 -6,639-54.844-32.210 1.0062.06 O

ATOM 9 CE2 TYRB 253 -4.990-56.557-32.251 1.0062.23 C

ATOM 10 CD2TYRB253 -3.841-57.098-32.795 1.0062.57 C

ATOM 11 C TYR B 253 0.524-57.588-34.134 1.0061.37 C

ATOM 12 O TYRB 253 0.937-57.252-35.243 1.0061.52 O

ATOM 1 N ILE B 254 1.100-58.539-33.399 1.0060.85 N

ATOM 2 CA ILE B 254 2.348-59.177-33.815 1.0060.38 C

ATOM 3 CB ILE B 254 3.255-59.455-32.608 1.00.60.34 C

ATOM 4 CGl ILEB 254 3.199-58.278-31.632 1.0060.50 . C

ATOM 5 CDl ILEB 254 4.262-58.319-30.554 1.0060.93^' C

ATOM 6 CG2ILEB254 4.679-59.735-33.062 1.0059.77 C

ATOM 7 C ILE B 254 2.115 -60.486 -34.559 1.0060.21 ^' C

ATOM 8 O ILE B 254 1.542-61.423-34.016 1.0060.30 O

ATOM 1 N GLY B 255 2.569-60.558-35.804 1.0059.92 N ATOM 2 CA GLY B 255 2.410-61.789-36.573 1.0059.62 C

ATOM 3 C GLY B 255 3.016-61.725-37.960 1.0059.23 C

ATOM 4 O GLY B 255 3.708-60.766-38.298 1.0059.30 O

ATOM 1 N SER B 256 2.765-62.759-38.757 1.0058.78 N

ATOM 2 CA SER B 256 3.158-62.757-40.160 1.0058.69 C

ATOM 3 CB SERB 256 4.419-63.593-40.397 1.0058.72 C

ATOM 4 OG SER B 256 4.402-64.776-39.623 1.0059.59 O

ATOM 5 C SERB 256 2.000-63.204-41.054 1.0058.34 C

ATOM 6 O SERB 256 1.769-64.392-41.277. 1.0058.22 O

ATOM 1 N PHE B 257 1.293-62.212-41.578 1.0058.01 N

ATOM 2 CA PHE B 257 0.041 -62.410 -42.277 1.0057.54 C

ATOM 3 CB PHE B 257 -0.756-61.107-42.223 1.0057.11 C

ATOM 4 CG PHE B 257 -1.001-60.627-40.821 1.0056.81 C

ATOM 5 CDl PHE B 257 -2.247-60.763-40.232 1.0056.40 C

ATOM 6 CEl PHE B 257 -2.469-60.338-38.933 1,0055.40 C

ATOM 7 CZ PHE B 257 -1.441-59.781-38.204 1.0055.70 C

ATOM 8 CE2 PHE B 257 -0.193-59.650-38.764 1.0055.89 C

ATOM 9 CD2PHEB257 0.027-60.077-40.070 1.0056.91 C

ATOM 10 C PHE B 257 0.200-62.948-43.706 1.0057.57 C

ATOM 11 O PHE B 257 0.067-62.216-44.690 1.0057.54 O

ATOM 1 N TRP B 258 0.492-64.243-43.793 1.0057.58 N

ATOM 2 CA TRP B 258 0.511-64.966-45.062 1.0057.65 • C

ATOM 3 CB TRP B 258 1.642-64.464-45.966 1.0057.76 C

ATOM 4 CG TRP B 258 3.022-64.843-45.544 1.0057.87 C

ATOM 5 CDl TRP B 258 3.423-65.277-44.311 1.0058.43 C

ATOM 6 NEl TRP B 258 4.777 -65.520 -44.311 1.0058.60 N

ATOM 7 CE2 TRP B 258 5.278-65.229-45.554 1.0058.63 C

ATOM 8 CD2 TRP B 258 4.201 -64.791 -46.353 1.0058.19 C

ATOM 9 CE3 TRP B 258 4.450-64.430-47.682 1.0058.21 C

ATOM 10 CZ3 TRP B 258 5.747-64.513-48.163 1.0058.20 C

ATOM 11 CH2 TRP B 258 6.797-64.949-47.344 1.0058.12 „ C

ATOM 12 CZ2TRPB258 6.584-65.313-46.041 1.0058.37 C

ATOM 13 C TRP B 258 0.572-66.479-44.825 1.0057.67 C

ATOM 14 O TRP B 258 1.064-66.937-43.790 1.0057.71 O

ATOM 1 N SERB 259 0.057-67.254-45.776 1.0057.66 N

ATOM 2 CA SER B 259 -0.078-68.706-45.598 1.0057.55 C

ATOM 3 CB SERB 259 -1.160-69.255-46.527 1.0057.60 C

ATOM 4 OG SER B 259 -2.416-68.667-46.232 1.0058.07 O

ATOM 5 C SERB 259 1.226-69.478-45.802 1.0057.36 C

ATOM 6 O SER B 259 1.217-70.686-46.047 1.0057.37 O

ATOM 1 N GLN B 260 2.344-68.775-45.689 1.0057.11 N

ATOM 2 CA GLN B 260 3.650-69.384-45.862 1.0056.90 C

ATOM 3 CB GLN B 260 4.659-68.302-46.240 1.0057.05 C

ATOM 4 CG GLN B 260 5.638-68.687-47.342 1.0058.16 C

ATOM 5 CD GLN B 260 4.957-68.952-48.679 1.0059.01 C

ATOM 6 OEl GLN B 260 3.889-68.404-48.970 1.0059.19 O

ATOM 7 NE2GLNB260 5.578-69.798-49.499 1.0058.96 N

ATOM 8 C GLN B 260 4.059-70.055-44.556 1.0056.43 C

ATOM 9 O GLN B 260 3.621-69.640-43.487 1.0056.50 O

ATOM 1 N PRO B 261 4.877-71.113-44.634 1.0056.02 N

ATOM 2 CA PRO B 261 5.441-71.724-43.431 1.0055.81 C

ATOM 3 CB PRO B 261 6.390-72.785-43.990 1.0055.75 C

ATOM. ' 4 CG PRO B 261 5.810-73.132-45.313 1.0055.87 C

ATOM 5 CD PRO B 261 5.277-71.832-45.853 1.0056.03 C

ATOM 6 C PRO B 261 6.208-70.729-42.564 1.0055.59 C

ATOM ^' 7 O PRO B 261 6.579-69.652-43.024 1.0055.74 O

ATOM 1 N LEU B 262 6.443-71.092-41.313 1.0055.30 N

ATOM 2 CA LEU B 262 7.037-70.173-40.365 1.0055.12 ^' C ATOM 3 CB LEU B 262 6.474-70.457-38.978 1.0055.09 . C

ATOM 4 CG LEU B 262 5.736-69.356-38.216 1.0054.85 C

ATOM 5 CDl LEU B 262 5.003-68.395-39.142 1.0054.87 C

ATOM 6 CD2LEUB262 4.758-70.010-37.276 1.0054.29 C

ATOM 7 C LEU B 262 8.534-70.386-40.370 1.0055.14 C

ATOM 8 O LEU B 262 8.992-71.518-40.268 1.0055.24 O

ATOM 1 N LEU B 263 9.302-69.309-40.504 1.0055.24 N

ATOM 2 CA LEU B 263 10.757 -69.433 -40.527 1.0055.20 C

ATOM 3 CB LEU B 263 11.424-68.110-40.916 1.0055.14 C

ATOM 4 CG LEU B 263 12.794-68.176-41.612 1.0055.03 C

ATOM 5 CDl LEUB 263 13.368-66.781-41.784 1.0054.72 C

ATOM 6 CD2LEUB263 13.794-69.056-40.873 1.0055.07 C

ATOM 7 C LEU B 263 11.234-69.875-39.154 1.0055.30 C

ATOM 8 O LEU B 263 11.621-71.025-38.962 1.0055.01 O

ATOM 1 N VAL B 264 11.202-68.949-38.203 1.0055.62 N

ATOM 2 CA VAL B 264 11.550-69.260-36.824 1.0055.97 C

ATOM 3 CB VAL B 264 12.484-68.194-36.214 1.0055.83 C,

ATOM 4 CGl VALB 264 12.011-66.801 -36.566 1.0055.89 C

ATOM 5 CG2VALB264 12.602-68.376-34.708 1.0056.05 C

ATOM 6 C VAL B 264 10.272-69.448-36.007 1.0056.23 C

ATOM 7 O VAL B 264 9.618-68.484-35.632 1.0056.29 O

ATOM 1 N PRO B 265 9.926-70.711_.-35.722 1.0056.68 N

ATOM 2 CA PRO B 265 8.590-71.109-35.296 1.0057.10 C

ATOM 3 CB PRO B 265 8.583-72.607-35.601 1.0057.09 C

ATOM 4 CG PRO B 265 9.988-73.022-35.346 1.0056.77 C

ATOM 5 CD PRO B 265 10.843-71.863-35.792 1.0056.60 C

ATOM 6 C PRO B 265 8.272-70.900-33.816 1.0057.60 C

ATOM 7 O PRO B 265 7.098-70.934-33.434 1.0057.55 O

ATOM 1 N ASP B 266 9.290-70.686-32.987 1.0058.11 N

ATOM 2 CA ASP B 266 9.079-70.770-31.542 1.0058.60 C

ATOM 3 CB ASP B 266 10.389-71.053-30.775 1.0058.96 C

ATOM 4 CG ASP B 266 11.533-70.141-31.181 1.0059.26 C

ATOM 5 ODl ASP B 266 11.436-68.920-30.940 1.0060.12 O

ATOM .6 OD2 ASP B 266 12.545-70.659-31.706 1.0059.63 O

ATOM 7 C ASP B 266 8.295-69.617-30.932 1.0058.63 C

ATOM 8 O ASP B 266 8.522-69.238-29.791 1.0058.80 O

ATOM 1 N ASN B 267 7.349-69.085-31.693 1.0058.79 N

ATOM 2 CA ASN B 267 6.502-68.002-31.220 1.0058.87 C

ATOM 3 CB ASN B 267 7.161-66.657-31.514 1.0058.66 C

ATOM 4 CG ASN B 267 7.883-66.102-30.322 1.0058.19 C

ATOM 5 ODl ASN B 267 7.410-66.229-29.197 1.0058.89 O

ATOM 6 ND2ASNB267 9.033-65.483-30.552 1.0057.38 N

ATOM 7 C ASN B 267 5.113-68.040-31.846 1.0059.27 C

ATOM 8 O ASN B 267 4.383-67.045-31.818 1.0059.19 O

ATOM 1 N ARG B 268 4.737-69.187-32.406 1.0059.60 N

ATOM 2 CA ARG B 268 3.543-69.204-33.234 1.0059.99 C

ATOM 3 CB ARG B 268 3.514-70.400-34.200 1.0060.07 C

ATOM 4 CG ARG B 268 2.838-71.672-33.768 1.0060.90 C

ATOM 5 CD ARG B 268 2.359-72.379-35.039 1.0063.18 C

ATOM 6 NE ARG B 268 2.404-73.840-34.985 1.0065.28 N

ATOM 7 CZ ARG B 268 3.504-74.570-35.179 1.0066.78 C

ATOM 8 NHl ARG B 268 4.670-73.975-35.423 1.0066.33 N

ATOM 9 NH2ARGB268 3.443-75.902-35.119 1.0067.27 N

ATOM 10 C ARG B 268 2.259-69.016-32.443 1.0060.01 C

ATOM 11 O ARG B 268 1.344-68.351-32.913 1.0060.20 O

ATOM 1 N ARG B 269 2.213-69.550-31.229 1.0060.18 N

ATOM 2 CA ARG B 269 1.086-69.298-30.335 1.0060.31 C

ATOM 3 CB ARG B 269 1.421 -69.759-28.916 1.0060.47 C ATOM 4 CG ARG B 269 0.627-70.966-28.439 1.0061.18 C

ATOM 5 CD ARG B 269 -0.752-70.541-27.930 1.0062.47 C

ATOM 6 NE ARG B 269 -1.734-70.391-29.005 1.0062.90 N

ATOM 7 CZ ARG B 269 -2.957-70.919-28.983 1.0062.99 C

ATOM 8 NHl ARG B 269 -3.366-71.619-27.931 1.0062.79 N

ATOM 9 NH2 ARG B 269 -3.781-70.729-30.008 1.0062.86 N

ATOM 10 C ARG B 269 0.716 -67.818 --30.329 1.0060.15 C

ATOM 11 O ARG B 269 -0.443-67.449-30.540 1.0060.18 O

ATOM 1 N LEU B 270 1.719-66.978-30.094 1.0060.00 N

ATOM 2 CA LEU B 270 1.530-65.539-30.035 1.0059.87 C

ATOM 3 CB LEU B 270 2.863-64.857-29.733 1.0059.80 C

ATOM 4 CG LEU B 270 2.898-63.460-29.106 1.0059.73 C

ATOM 5 CDl LEUB 270 3.052-62.370-30.149 1.0059.80 C

ATOM 6 CD2 LEU B 270 1.683-63.214-28.229 1.0059.78 C

ATOM 7 C LEU B 270 0.957-65.031-31.346 1.0059.92 C

ATOM 8 O LEU B 270 -0.016-64.287-31.358 1.0060.09 O

ATOM 1 N PHE B 271 1.552-65.455-32.454 1.0060.22 N

ATOM 2 CA PHE B 271 1.123-65.006-33.774 1.0060.39 C

ATOM 3 CB PHEB 271 2.020-65.581-34.870 1.0060.47 C

ATOM 4 CG PHE B 271 3.471-65.224-34.717 1.0060.39 C

ATOM 5 CDl PHE B 271 3.847-64.051-34.072 1.0060.01 C

ATOM 6 CEl PHE B 271 5.181-63.716-33.930 1.0059.82 C

ATOM 7 CZ PHE B 271 6.159-64.546-34.451 1.0060.43 C

ATOM 8 CE2PHEB271 5.798 -65.718 -35.105 1.0060.27 C

ATOM 9 CD2PHEB271 4.458-66.049-35.237.1.0060.08 C

ATOM 10 C PHE B 271 -0.326-65.375-34.044 l'.OO 60.56 C

ATOM 11 O PHEB 271 -1.129-64.523-34.451 1.0060.91 O

ATOM 1 N GLU B 272 -0.672-66.638-33.819 1.0060.53 N

ATOM 2 CA GLU B 272 -2.057-67.032-34.002 1.0060.88 C

ATOM 3 CB GLU B 272 -2.280-68.554-33.896 1.0060.68 C

ATOM 4 CG GLU B 272 -1.359-69.330-32.967 1.0061.39 C

ATOM 5 CD GLU B 272 -1.554-70.852-33.082 1.0062.06 C

ATOM 6 OEl GLUB 272 -1.025-71.608-32.228 1.0063.50 O

Af¹OM 7 OE2GLUB272 -2.245-71.301-34.030 1.0064.06 O

ATOM 8 C GLU B 272 -2.972-66.221-33.079 1.0060.54 C

ATOM 9 O GLU B 272 -4.000-65.707-33.518 1.0060.78 O

ATOM 1 N LEU B 273 -2.582-66.061-31.819 1.0060.28 N

ATOM 2 CA LEU B 273 -3.385-65.255-30.904 1.0060.15 C

ATOM 3 CB LEU B 273 -2.765-65.249-29.505 1.0060.05 C

ATOM 4 CG LEU B 273 -3.567-66.013-28.454 1.0059.60 C

ATOM 5 CDl LEUB 273 -5.001-65.525-28.500 1.0060.64 C

ATOM 6 CD2LEUB273 -3.523-67.492-28.688 1.0059.04 C

ATOM 7 C LEU B 273 -3.635-63.819-31.402 1.0060.30 C

ATOM 8 O LEU B 273 -4.785-63.350-31.454 1.0060.39 O

ATOM 1 N GLU B 274 -2.559-63.128-31.769 1.0060.35 N

ATOM 2 CA GLU B 274 -2.662-61.747-32.227 1.0060.63 C

ATOM 3 CB GLU B 274 -1.274-61.173-32.505 1.0060.61 C

ATOM 4 CG GLU B 274 -0.341-61.133-31.294 1.0061.23 C

ATOM 5 CD GLU B 274 -0.625-59.970-30.352 1.0062.07 C

ATOM 6 OEl GLU B 274 0.025-58.910-30.507 1.0062.22 O

ATOM 7 OE2GLUB274 -1.496-60.115-29.462 1.0062.05 O

ATOM 8 C GLU B 274 -3.525-61.672-33.481 1.0060.74 C

ATOM 9 O GLU B 274 -4.423-60.821-33.603 1.0060.90 O

ATOM 1 N GLU B 275 -3.252-62.578-34.410 1.0060.89 N

ATOM 2 CA GLU B 275 -4.061-62.697-35.607 1.0061.09 C,

ATOM 3 CB GLU B 275 -3.606-63.919-36.392 1.0061.28 C

ATOM 4 CG GLtJ B 275 -4.061-63.971-37.832 1.0062.13 C

ATOM 5 CD GLU B 275 -3.647-65.272-38.492 1.0063.38 C ATOM 6 OEl GLU B 275 -4.438-65.821-39.296 1.0063.96 O

ATOM 7 OE2GLUB275 -2.533-65.757-38.185 1.0063.30 O

ATOM 8 C GLU B 275 -5.537-62.822-35.225 1.0061.04 C

ATOM 9 O GLU B 275 -6.396-62.138-35.781 1.0060.86 O

ATOM 1 N GLN B 276 -5.823-63.688-34.260 1.0061.18 N

ATOM 2 CA GLNB 276 -7.189-63.863-33.773 1.0061.56 C

ATOM 3 CB GLN B 276 -7.249-64.934-32.676 1.0061.86 C

ATOM 4 CG GLNB 276 -7.328-66.357-33.202 1.0063.52 C

ATOM 5 CD GLN B 276 -8.595-66.593-34.008 1.0066.43 C

ATOM 6 OEl GLN B 276 -9.697-66.659-33.452 1.0067.98 O

ATOM 7 NE2GLNB276 -8.447-66.718-35.326 1.0067.10 N

ATOM 8 C GLN B 276 -7.782-62.550-33.265 1.0061.36 C

ATOM 9 O GLN B 276 -8.914-62.196-33.614 1.0061.33 O

ATOM 1 N ASP B 277 -7.023-61.827-32.446 1.0061.08 N

ATOM 2 CA ASP B 277 -7.530-60.572.-31.896 1.0061.12 C

ATOM 3 CB ASP B 277 -6.544-59.973-30.890 1.0061.25 C

ATOM 4 CG ASP B 277 -6.489-60.757-29.576 1.0062.18 C

ATOM 5 ODl ASP B 277 -7.208-61.774-29.439 1.0063.05 O

ATOM 6 OD2 ASP B 277 -5.723-60.356-28.670 1.0063.07 O

ATOM 7 C ASP B 277 -7.866-59.576-33.010 1.0060.97 C

ATOM 8 O ASP B 277 -8.984-59.023-33.065 1.0061.14 O

ATOM 1 N LEU B 278 -6.911-59.359-33.914 1.0060.75 N

ATOM 2 CA LEU B 278 -7.157-58.435-35.024 1.0060.28 C

ATOM 3 CB LEU B 278 -5.912-58.273-35.910 1.0060.28 C

ATOM 4 CG LEUB 278 -6.060-57.508-37.232 1.0059.63 C

ATOM 5 CDl LEUB 278 -6.308-56.034-36.981 1.0058.86 C

ATOM 6 CD2LEUB278 -4.834-57.694-38.107 1.0059.64 C

ATOM 7 C LEU B 278 -8.360-58.894-35.849 1.0060.34 C

ATOM 8 O LEUB 278 -9.230-58.091-36.199 1.0060.18 O

ATOM 1 N PHE B 279 -8.416-60.190-36.148 1.0060.47 N

ATOM 2 CA PHE B 279 -9.530-60.706-36.933 1.0060.57 C

ATOM 3 CB PHE B 279 -9.397-62.197-37.221 1.0060.52_, C

ATOM 4 CG PHE B 279 -8.381 -62.511 -38.265 1.0060.50 C

ATOM 5 CDl PHEB 279 -7.966-61.533-39.154 1.0060.16 C

ATOM 6 CEl PHE B 279 -7.023-61.808-40.117 1.0060.38 C

ATOM 7 CZ PHE B 279 -6.492-63.075-40.213 1.0060.80 C

ATOM 8 CE2PHEB279 -6.908-64.068-39.335 1.0060.94 C

ATOM 9 CD2PHEB279 -7.846-63.783-38.369 1.0060.60 C

ATOM 10 C PHE B 279 -10.850-60.418-36.253 1.0060.72 C

ATOM 11 O PHE B 279 -11.761-59.888-36.876 1.0060.64 O

ATOM 1 N ARG B 280 -10.962-60.758-34.975 1.0060.96 N

ATOM 2 CA ARG B 280 -12.162-60.380-34.250 1.0061.16 C

ATOM 3 CB ARG B 280 -12.049-60.714-32.760 1.0061.05 C

ATOM 4 CG ARG B 280 -12.708-62.041,-32.395 1.0061.56 . C

ATOM 5 CD ARG B 280 -12.596-62.359-30.907 1.0061.94 C

ATOM 6 NE ARG B 280 -11.469-63.243-30.603 1.0063.84 N

ATOM 7 CZ ARG B 280 -10.213-62.833-30.424 1.0064.28 C

ATOM 8 NHl ARG B 280 -9.910-61.542-30.520 1.0064.38 N

ATOM 9 NH2ARGB-280 -9.259-63.718-30.150 1.0064.17 N

ATOM 10 C ARG B 280 -12.451-58.895-34.487 1.0061.05 C

ATOM 11 O ARG B 280 -13.571-58.525-34.856 1.0060.89 O

ATOM 1 N ASP B 281 -11.432-58.053-34.322 1.0061.18 N

ATOM 2 CA ASP B 281 -11.623-56.605-34.494 1.0061.26 C

ATOM 3 CB ASP B 281 -10.314-55.846-34.241 1.0061.67 C

ATOM 4 CG ASP B 281 -10.523-54.555-33.450 1.0062.92 C

ATOM 5 ODl ASP B 281 -11.661-54.026-33.430 1.0063.95 O

ATOM 6 OD2ASPB281 -9.541-54.076-32.835 1.0064.41 O

ATOM 7 C ASP B 281 -12.200-56.222-35.863 1.0060.84 C ATOM 8 O ASP B 281 -13.146-55.446-35.940 1.0060.76 O

ATOM 1 N ILE B 282 ^■ -11.625-56.763-36.935 1.0060.54 N

ATOM 2 CA ILE B 282 -12.116-56.507-38.294 1.0060.21 C

ATOM 3 CB ILE B 282 -11.226-57.185-39.349 1.0060.12 C

ATOM 4 CGl ILE B 282 -9.816-56.592-39.336 1.0060.23 C

ATOM 5 CDl ILE B 282 -8.799-57.415-40.105 1.0059.99 C

ATOM 6 CG2ILEB282 -11.857-57.075-40.733 1.0059.55 C

ATOM 7 C ILE B 282 ■ -13.509-57.077-38.474 1.0060.29 C

ATOM 8 O ILE B 282 -14.445-56.371-38.826 1.0060.29 O

ATOM 1 N GLN B 283 -13.628-58.375-38.232 1.0060.51 N

ATOM 2 CA GLN B 283 ^■ -14.874-59.096-38.404 1.0060.54 C

ATOM 3 CB GLNB 283 -14.718-60.538-37.919 1.0060.59 C

ATOM 4 CG GLN B 283 -15.750-61.500-38.479 1.0061.30 C

ATOM 5 CD GLN B 283 -16.834-61.830-37.479 1.0062.16 C

ATOM 6 OEl GLN B 283 -18.015-61.936-37.829 1.0062.37 O

ATOM 7 NE2 GLN B 283 -16.438-61.995-36.219 1.0062.82 N

ATOM 8 C GLN B 283 -15.998-58.403-37.660 1.0060.41 C

ATOM 9 O GLN B 283 -17.160-58.514-38.045 1.0060.58 O

ATOM 1 N GLY B 284 -15.645-57.670-36.608 1.0060.32 N

ATOM 2 CA GLY B 284 -16.642-56.993-35.785 1.0059.90 . C

ATOM 3 C GLY B 284 -17.147-55.656-36.307 1.0059.63 C

ATOM 4 O GLY B 284 -18.036-55.052-35.708 1.0059.69 O

ATOM 1 N LEUB 285 -16.596-55.194-37.425 1.0059.39, N

ATOM 2 CA LEU B 285 -16.897-53.848-37.933 1.0059.12 C

ATOM 3 CB LEU B 285 -15.994-53.498-39.122 1.0058.97 C

ATOM 4 CG LEU B 285 -14.509-53.305-38.827 1.0058.44 C

ATOM 5 CDl LEUB 285 -13.791 -52.805 -40.064 1.0058.10 C

ATOM 6 CD2LEUB285 -14.322 -52.345 -37.673.1.0058.23 C

ATOM 7 C LEU B 285 -18.364-53.581-38.295 1.0059.12 C

ATOM 8 O LEUB 285 -18.966-52.638-37.773 1.0058.98 O

ATOM 1 N PRO B 286 -18.944-54.409-39.185 1.0059.17 N

ATOM 2 CA PRO B 286 -20.292-54.145-39.680 1.0059.19 C

ATOM 3 CB PRO B 286 -20.575-55.339-40.595 1.0059.12 C

ATOM 4 CG PRO B 286 -19.244-55.870-40.958 1.0059.19 C

ATOM 5 CD PRO B 286 -18.388-55.648-39.756 1.0059.17 C

ATOM 6 C PRO B 286 -21.289-54.132-38.541 1.0059.26 C

ATOM 7 O PRO B 286 -22.246-53.357-38.560 1.0059.19 O

ATOM 1 N ARG B 287 -21.053-54.989-37.552 1.0059.46 N

ATOM 2 CA ARG B 287 -21.912-55.057-36.384 1.0059.64 C

ATOM 3 CB ARG B 287 -21.297-55.921-35.291 1.0059.76 C

ATOM 4 CG ARG B 287 -22.268-56.326-34.193 1.0060.10 C

ATOM 5 CD ARG B 287 -21.647-57.427-33.373 1.0061.21 C

ATOM 6 NE ARG B 287 -20.970-58.384-34.246 1.0062.03 N

ATOM 7 CZ ARG B 287 -19.899-59.089-33.899 1.0062.52 C

ATOM 8 NHl ARG B 287 -19.352 -59.933 -34.765 1.0062.89 N

ATOM 9 NH2 ARG B 287 -19.371-58.943-32.691 1.0062.75 N

ATOM 10 C ARG B 287 -22.185-53.659-35.866 1.0059.65 C

ATOM 11 O ARG B 287 -23.290-53.378-35.409 1.0059.81 O

ATOM 1 N HIS B 288 -21.194-52.772-35.937 1.0059.63 N

ATOM 2 CA HIS B 288 -21.517-51.366-35.722 1.0059.67 . C

ATOM 3 CB HIS B 288 -21.830-51.042-34.267 1.0059.99 C

ATOM 4 CG HIS B 288 -23.288 -50.816 -34.035 1.0061.01 C

ATOM. 5 NDl HIS B 288 -24.084-50.164-34.954 1.0061.71 N

ATOM 6 CEl HIS B 288 -25.326-50.118-34.502 1.0062.63 C

ATOM 7 NE2 HIS B 288 -25.364-50.719-33.325 1.0062.85 N

ATOM 8 CD2 HIS B 288 -24.103-51.171-33.013 1.0062.15 C

ATOM 9 C HIS B 288 -20.713-50.263-36.383 1.0059.2.6 C

ATOM 10 O HIS B 288 -19.713-49.774-35.856 1.0059.07 O ATOM 1 N . ALAB 289 -21.221-49.867-37.543 1.0058.88 N

ATOM 2 CA ALA B 289 -20.802-48.660-38.215 1.0058.55 C

ATOM 3 CB ALA B 289 -21.132-48.746-39.701 1.0058.66 C

ATOM 4 C . ALA B 289 -21.513-47.468-37.582 1.0058.24 C

ATOM 5 O ALA B 289 -20.964-46.372-37.524 1.0058.03 O

ATOM 1 N^'. ALA B 290 -22.733-47.688-37.102 1.0057.82 N

ATOM 2 CA ALAB 290. -23.524-46.609-36.525 1.0057.55 C

ATOM 3 CB ALAB 290 -24.807-47.154-35.945 1.0057.56 C

ATOM 4 C . ALAB 290 -22.752-45.822-35.467 1.0057.41 C

ATOM 5 O ALA B 290 -22.784-44.587-35.446 1.0057.25 O

ATOM 1 N LEU B 291 -22.057-46.542-34.594 1.0057.29 N

ATOM 2 CA LEU B 291 -21.296-45.916-33.521 1.0057.23 C

ATOM 3 CB LEUB 291 -20.743-46.984-32.575 1.0057.15 C

ATOM 4 CG LEU B 291 -20.611-46.651-31.087 1.0056.86 C

ATOM 5 CDl LEU B 291 -19.866-47.763-30.376 1.0056.79 C

ATOM 6 CD2LEUB291 -19.907-45.328-30.867 1.0057.08 C

ATOM 7 C LEU B 291 -20.158-45.059-34.081 1.0057.31 C

ATOM 8 O LEU B 291 -20.002-43.894-33.703 1.0057.24 O

ATOM 1 N ARG B 292 -19.366-45.629-34.986 1.0057.43 N

ATOM 2 CA ARG B 292 -18.224-44.901-35.540 1.0057.57 C

ATOM 3 CB ARG B 292 -17.290-45.826-36.338 1.0057.62 C

ATOM 4 CG ARG B 292 -17.564-45.912-37.834 1.0057.76 C

ATOM 5 CD ARG B 292 -16.564-45.093-38.644 1.0057.94 C

ATOM 6 NE ARG B 292 -16.928-45.049-40.060 1.0058.09 N

ATOM 7 CZ ARG B 292 -17.435-43.984-40.674 1.0057.92 C

ATOM 8 NHl ARG B 292 -17.741-44.043-41.960 1.0058.28 ^' N

ATOM 9 NH2 ARG B 292 -17.633-42.855-40.009 1.0058.17 N

ATOM 10 C ARG B 292 -18.704-43.718-36.375 1.0057.46 C

ATOM 11 O ARG B 292 -18.088-42.648-36.363 1.0057.56 O

ATOM 1 N LYS B 293 -19.812-43.912-37.081 1.0057.36 N

ATOM 2 CA LYS B 293 -20.442-42.831-37.816 1.0057.19 C

ATOM 3 CB LYS B 293 -21.686-43.323-38.553 1.0057.19 C

ATOM 4 CG LYS B 293 -21.386-44.029-39.863 1.0057.17 C

ATOM 5 CD LYS B 293 -22.550-44.901-40.305 1.0057.02 C

ATOM 6 CE LYS B 293 -22.257-45.577-41.635 1.0057.19 C

ATOM . 7 NZ LYS B 293 -23.249-46.645-41.939 1.0057.34 N

ATOM 8 C LYS B 293. -20.804-41.729-36.840 1.0057.09 C

ATOM 9 O LYS B 293 -20.365-40.588-36.991 1.0057.11 O

ATOM 1 N LEU B 294 -21.591-42.079-35.828 1.0056.95 N

ATOM 2 CA LEU B 294 -21.958-41.121-34.800 1.0056.84 C

ATOM 3 CB LEU B 294 -22.623-41.836-33.624 1.0056.79 C

ATOM 4 CG LEU B 294 -22.941-40.974-32.400 1.0056.79 C

ATOM 5 CDl LEUB 294 -23.835-39.809-32.786 1.0057.30 C

ATOM 6 CD2LEUB294 -23.595-41.802-31.3.15 1.0056.83 C

ATOM 7 C LEU B 294 -20.726-40.348-34.333 1.0056.79 C

ATOM 8 O LEU B 294 -20.667-39.112-34.429 1.0056.76 O

ATOM 1 N ASN B 295 -19.736-41.084-33.844 1.0056.85 N

ATOM 2 CA ASN B 295 : -18.503 -40.469 -33.356 1.0056.94 C

ATOM 3 CB ASN B 295 -17.499-41.549-32.961 1.0057.00 C

ATOM 4 CG ASN B 295 -17.415-41.708-31.447 1.0057.02 C

ATOM 5 ODl ASNB 295 -17.582-42.815-30.911 1.0056.80 O

ATOM 6 ND2ASNB295 -17.156-40.594-30.743 1.0057.22 N

ATOM 7 C ASNB 295 -17.855-39.494-34.338 1.0056.98 C

ATOM 8 O ASN B 295 -17.529-38.355-33.986 1.0056.90 O

ATOM 1 N ASP B 296 -17.663-39.939-35.572 1.0057.20 N

ATOM 2 CA . ASP B 296 -17.044-39.075-36.564 1.0057.27 C

ATOM 3 CB ASP B 296 -16.740-39.854-37.843 1.0057.49 C

ATOM 4 CG ASP B 296 -15.732-40.978-37.613 1.0058.34 C ATOM 5 ODl ASP B 296 -15.736-41.950-38.398 1.0059.28 O

ATOM 6 OD2 ASP B 296 -14.941-40.898-36.642 1.0059.32 O

ATOM 7 C ASP B 296 -17.909-37.844-36.826 1.0057.08 C

ATOM 8 O ASP B 296 -17.386-36.745-37.049 1.0056.96 O

ATOM 1 N LEU B 297 -19.228-38.027-36.768 1.0056.92 N

ATOM 2 CA LEU B 297 -20.152-36.901-36.856 1.0056.71 C

ATOM 3 CB LEU B 297 -21.610-37.360-36.779 1.0056.70 C

ATOM 4 CG LEU B 297 -22.645-36.289-37.147 1.0057.00 C

ATOM 5 CDl LEU B 297 -22.838-36.212-38.653 1.0057.18 C

ATOM 6 CD2LEUB297 -23.986-36.538-36.466 1.0057.32 C

ATOM 7 C LEU B 297 -19.857-35.904-35.743 1.0056.57 C

ATOM 8 O LEU B 297 -19.723-34.709-36.001 1.0056.57 , O

ATOM . 1 N VAL B 298 -19.746-36.394-34.509 1.0056.40 N

ATOM 2 CA VAL B 298 -19.372-35.528-33.385 1.0056.20 C

ATOM 3 CB VAL B 298 -19.201-36.323-32.082 1.0056.10 C

ATOM 4 CGl VALB 298 -18.713-35.414-30.963 1.0055.78 C

ATOM 5 CG2VALB298 -20.494-37.011-31.700 1.0055.98 C

ATOM 6 C VAL B 298 -18.062-34.781-33.644 1.0056.34 C

ATOM 7 O VAL B 298 -17.990-33.550-33.511 1.0056.51 O

ATOM 1 N LYS B 299 -17.023-35.532-34.003 1.0056.48 N

ATOM 2 CA LYS B 299 -15.707-34.944-34.234 1.0056.48 C

ATOM 3 CB LYS B 299 -14.723-36.009-34.720 1.0056.50 C

ATOM 4 CG LYS B 299 -14.428-37.118-33.712 1.0056.54 C

ATOM 5 CD LYS B 299 -13.557-38.204-34.340 1.0056.73 C

ATOM 6 CE LYS B 299 -13.154-39.272-33.329 1.0057.33 C

ATOM 7 NZ LYS B 299 -12.203-38.749-32.312 1.0057.04 N

ATOM 8 C LYS B 299 -15.812-33.824-35.260 1.0056.44 C

ATOM 9 O LYS B 299 -15.372-32.676-35.023 1.0056.62 O

ATOM 1 N ARG B 300 -16.410-34.158-36.401 1.0056.46 N

ATOM 2 CA ARG B 300 -16.647-33.159-37.427 1.0056.31 C

ATOM 3 CB ARG B 300 -17.485-33.720-38.576 1.0056.27 C

ATOM 4 CG ARG B 300 -17.978-32.651-39.546 1.0056.17 C

ATOM 5 CD ARG B 300 -18.774-33.246-40.692 1.0056.14 C

ATOM 6 NE ARG B 300 -17.929-33.563-41.836 1.0056.16 N

ATOM 7 CZ ARG B 300 -18.030-32.970-43.021 1.0056.53 C

ATOM 8 NHl ARG B 300 -17.222-33.317-44.013 1.0056.30 N

ATOM 9 NH2 ARG B 300 -18.950-32.037-43.218 1.0056.98 N

ATOM 10 C ARG B 300 -17.334-31.952-36.802 1.0056.37 C

ATOM 11 O ARG B 300 -16.829-30.834-36.887 1.0056.39 O

ATOM 1 N ALAB 301 -18.473-32.186-36.154 1.0056.45 N

ATOM 2 CA ALAB 301 -19.214-31.106-35.509 1.0056.41 C

ATOM 3 CB ALA B 301 -20.258-31.660-34.552 1.0056.29 C

ATOM 4 C ALAB 301 -18.261-30.172,-34.779 1.0056.46 C

ATOM 5 O ALAB 301 -18.222-28.971-35.062 1.0056.47 O

ATOM 1 N ARG B 302 -17.480 -30.728 -33.858 1.0056.55 N

ATOM 2 CA ARG B 302 -16.535-29.923-33.075 1.0056.77 C

ATOM 3 CB ARG B 302 -15.760-30.818-32.106 1.0056.86 C

ATOM 4 CG ARG B 302 -16.666-31.414-31.043 1.0057.73 C

ATOM 5 CD ARG B 302 -16.137-32.710-30.479 1.0059.51 C

ATOM 6 NE ARG B 302 -15.204-32.490-29.380 1.0061.12 N

ATOM 7 CZ ARG B 302 -13.883-32.597-29.490 1.0062.12 C

ATOM 8 NHl ARG B 302 -13.331-32.927-30.655 1.0062.16 ^• N

ATOM 9 NH2ARGB302 -13.112-32.381-28.431 1.0062.71 ^' N

ATOM 10 C ARG B 302 -15.593-29.087-33.951 1.0056.68 C

ATOM 11 O ARG B 302 -15.424-27.862-33.734 1.0056.68- O

ATOM 1 N LEUB 303 -15.003-29.735-34.956 1.0056.67 N

ATOM 2 CA LEUB 303 -14.163-28.990-35.902 1.0056.63 C

ATOM 3 CB LEU B 303 -13.583-29.913-36.973 1.0056.59 C ATOM 4 CG LEUB 303 -12.682-29.195-37.981 1.0056.67 C

ATOM 5 CDl LEU B 303 -11.413-28.699-37.301 1.0056.50 C

ATOM 6 CD2LEUB303 -12.344-30.106-39.150 1.0057.07 C

ATOM .7 C LEU B 303 -14.933-27.832-36.560 1.0056.59 C

ATOM 8 O LEU B 303 -14.471-26.677-36.576 1.0056.69 O

ATOM 1 N VAL B 304 -16.106-28.149-37.102 1.0056.40 N

ATOM 2 CA VAL B 304 -16.982-27.143-37.684 1.0056.15 C

ATOM 3 CB VAL B 304 -18.362 -27.728 -38.028 1.0056.03 C

ATOM 4 CGl VALB 304 -19.301-26.633-38.494 1.0055.85 C

ATOM 5 CG2VALB304 -18.228-28.800-39.086 1.0055.67 C

ATOM 6 C VAL B 304 -17.155 -25.971 -36.724 1.0056.22 C

ATOM 7 O VAL B 304 -16.819-24.832-37.058 1.0056.31 O

ATOM 1 N ARG B 305 -17.666-26.249-35.527 1.0056.24 N

ATOM 2 CA ARG B 305 .-17.864-25.195-34.532 1.0056.28 C

ATOM 3 CB ARG B 305 -18.260-25.783-33.169 1.0056.25 C

ATOM 4 CG ARG B 305 -17.825-24.961-31.964 1.0056.53 C

ATOM 5 CD ARG B 305 -18.985-24.659-31.011 1.0057.09 C

ATOM 6 NE ARG B 305 -19.403-25.757-30.137 1.0057.25 N

ATOM 7 CZ ARG B 305 -18.624-26.746-29.709 1.0057.93 C

ATOM 8 NHl ARG B 305 -19.132-27.680-28.915 1.0057.81 N

ATOM 9 NH2 ARG B 305 -17.345-26.809-30.063 1.0058.76 . N

ATOM 10 C ARG B 305 -16.626-24.303-34.435 1.0056.28 C

ATOM 11 O ARG B 305 -16.723-23.058-34.526 1.0056.39 O

ATOM 1 N VAL B 306 -15.456-24.931-34.294 1.0056.35 N

ATOM 2 CA VAL B 306 -14.227-24.136-34.253 1.0056.27 C

ATOM 3 CB VALB 306 -12.987-25.017-34.201 1.0056.15 C

ATOM 4 CGl VAL B 306 -11.767-24.162-33.924 1.0056.18 C

ATOM 5 CG2 VALB 306 -13.152-26.085-33.145 1.0056.17 ^' C

ATOM 6 C VAL B 306 -14.108-23.217-35.474 1.0056.36 . C

ATOM 7 O VAL B 306 -14.036-21.983-35.351 1.0056.51 O

ATOM 1 N HIS B 307 ■ -14.088-23.822-36.656 1.0056.41 N

ATOM 2 CA HIS B 307 -13.971-23.049-37.890 1.0056.44 C

ATOM 3 CB HIS B 307 -14.243-23.942-39.100 1.0056.45 C

ATOM 4 CG HIS B 307 -14.152-23.225-40.409 1,0055.91 C

ATOM 5 NDl HIS B 307 -12.949-22.849-40.969 1.0055.76 N

ATOM 6 CEl HIS B 307 -13.172-22.245-42.123 1.0055.92 C

ATOM 7 NE2 HIS B 307 -14.476-22.221-42.335 1.0056.18 N

ATOM 8 CD2 HIS B 307 -15.112-22.827-41.277 1.0055.83 C

ATOM 9 C HIS B 307 ^■ -14.927-21.856-37.902 1.0056.54 C

ATOM 10 O HIS B 307 -14.523-20.712-38.178 1.0056.69 O

ATOM 1 N ALA B 308 -16.196-22.138-37.602 1.0056.50 N

ATOM 2 CA ALAB 308 -17.222-21.106-37.541 1.0056.41 C

ATOM 3 CB ALAB 308 -18.500-21.659-36.962 1.0056.25 C

ATOM 4 C ALAB 308 -16.711-19.972-36.685 1.0056.41 C

ATOM 5 O ALAB 308 -16.653-18.819-37.132 1.0056.62 O

ATOM 1 N TYRB 309 -16.314-20.299-35.459 1.0056.40 N

ATOM 2 CA TYRB 309 -15.811-19.251-34.584 1.0056.51 C

ATOM 3 CB TYR B 309 -15.368-19.809-33.233 1.0056.57 C

ATOM 4 CG TYR B 309 -16.521-20.031-32.285 1.0056.51 C

ATOM 5 CDl TYRB 309 -16.661-21.225-31.596 1.0056.48 C

ATOM 6 CEl TYRB 309 -17.719-21.429-30.733 1.0056.59 C

ATOM 7 CZ TYR B 309 -18.659-20.436-30.560 1.0056.61 C

ATOM 8 OH TYRB 309 -19.715-20.639-29.705 1.0056.68 O

ATOM 9 CE2 TYRB 309 -18.548-19.243-31.239 1.0056.61 C

ATOM 10 CD2TYRB309 -17.485-19.048-32.097 1.0056.59 C

ATOM 11 C TYRB 309 -14.693-18.455-35.251 1.0056.61 C

ATOM 12 O TYRB 309 -14.750-17.219-35.302 1.0056.91 O

ATOM 1 N ILEB 310 -13.693-19.158-35.781 1.0056.59 N ATOM 2 CA ILEB 310 -12.568-18.486-36.444 1.0056.63 C

ATOM 3 CB ILEB 310 -11.613-19.492-37.109 1.0056.52 C .

ATOM 4 CGl ILEB 310 -11.052-20.463-36.074 1.0056.47 C

ATOM 5 CDl ILEB 310 -10.286-21.610-36.681 1.0056.57 C

ATOM 6 CG2ILEB310 -10.480-18.768-37.804 1.0056.40 C

ATOM 7 C ILEB 310 - 13.023-17.463-37.496 1.0056.78 C

ATOM 8 O ILEB 310 ^■ ■12.692-16.258-37.410 1.0057.05 O

ATOM 1 N ILEB 311 ■ ■13.783-17.938-38.484 1.0056.75 N

ATOM 2 CA ILEB 311 -14.250-17.046-39.545 1.0056.82 C

ATOM 3 CB ILEB 311 -15.107-17.771-40.602 1.0056.78 C

ATOM 4 CGl ILEB 311 -14.243-18.232-41.774 1.0056.78. C

ATOM 5 CDl ILEB 311 -13.214-19.266-41.422 1.0057.40 . C

ATOM 6 CG2 ILEB 311 -16.155-16.834-41.167 1.0057.09 C

ATOM 7 C ILEB 311 ■ ■15.032-15.882-38.951 1.0056.87 C

ATOM 8 O ILEB 311 • ■14.757-14.714-39.253 1.0056.99 O

ATOM 1 N SERB 312 -15.995-16.205-38.091 1.0056.92 N

ATOM 2 CA SERB 312 -16.804-15.181-37.447 1.0057.06 C

ATOM 3 CB SERB 312 -17.681-15.797-36.362 1.0057.04 C

ATOM 4 OG SERB 312 -18.624-16.687-36.931 1.0057.03 O

ATOM 5 C SERB 312 -15.937-14.078-36.855 1.0057.22 C

ATOM 6 O SERB 312 -16.133-12.896-37.157 1.0057.33 O

ATOM 1. N TYRB 313 -14.974-14.464-36.019 1.0057.40 N

ATOM 2 CA TYRB 313 -14.091-13.479-35.382 1.0057.83 C

ATOM 3 CB TYRB 313 -13.138-14.142-34.380 1.0058.15 C

ATOM 4 CG TYRB 313 -13.757-14.429-33.019 1.0058.84 C

ATOM 5 CDl TYRB 313 -13.076-14.120-31.842 1.0059.36 C

ATOM 6 CEl TYRB 313 -13.637 -14.383 -30.593, 1.0059.39 C

ATOM 7 CZ TYRB 313 -14.895-14.957-30.515 1.0059.16 C

ATOM 8 OH TYRB 313 -15.457-15.219-29.286 1.0059.00 O

ATOM 9 CE2 TYRB 313 -15.593-15.269-31.667 1.0059.29 C

ATOM 10 CD2 TYRB 313 -15.025-15.004-32.909 1.0059.34 C

ATOM 11 C TYRB 313 -13.315-12.657-36.412 1.0057.75 C

ATOM 12 O TYRB 313 -13.234-11.423-36.305 1.0057.91 O

ATOM 1 N, LEUB 314 -12.757-13.328-37.418 1.0057.51 N

ATOM 2 CA LEU B 314 -12.069-12:590-38.480 1.0057.40 C

ATOM 3 CB LEUB 314 -11.557-13.550-39.553 1.0057.20 C

ATOM 4 CG LEU B 314 -10.394-14.430-39.093 1.0056.64 C

ATOM 5 CDl LEUB 314 -10.239-15.648-39.978 1.0055.97 C

ATOM 6 CD2 LEUB 314 -9.112-13.622-39.047 1.0056.28 C

ATOM 7 C LEUB 314 -12.981-11.514-39.088 1.0057.49 C

ATOM 8 O LEUB 314 -12.638-10.316-39.130 1.0057.84 O

ATOM 1 N LYS B 315 -14.156-11.949-39.539 1.0057.46 . N

ATOM 2 CA LYS B 315 -15,124-11.045-40.158 1.0057.51 C

ATOM. 3 CB LYS B 315 -16.380-11.804-40.593 1.0057.50 C

ATOM 4 CG LYSB 315 -17.579 -10.920 -40.897 1.0057.23 C

ATOM 5 CD LYS B 315 -17.328-10.022-42.090 1.0057.26 C

ATOM 6 CE LYS B 315 -18.512 -9.103-42.327 1.0057.59 C

ATOM 7 NZ LYS B 315 -18.458 -8.446-43.665 1.0057.78 N

ATOM .8 C LYS B 315 -15.503 -9.898-39.235 1.0057.60 C

ATOM 9 O LYS B 315 -15.604 -8.753-39.676 1.0057.65 O

ATOM 1 N LYSB 316 -15.717-10.202-37.958 1.0057.67 N

ATOM 2 CA LYS B 316 -16.071 -9.156-37.003 1.0057.96 C

ATOM 3 CB LYS B 316 -16.594 -9.747 -35.685 1.0058.04 . C

ATOM 4 CG LYS B 316 -15.533-10.014-34.617 1.0058.13 C

ATOM 5 CD LYSB 316 -16.133-10.748-33.420 1.0058.14 C

ATOM 6 CE LYS B 316 -15.059-11.212-32.442 1.0058.37 C

ATOM 7 NZ LYS B 316 -14.405-10.080-31.724 1.0058.37 N

ATOM 8 C LYS B 316 -14.886 -8.223-36.755 1.0057.99 C ATOM 9 O LYS B 316 -15.059 -7.095-36.293 1.0057.89 O

ATOM 1 N GLUB 317 -13.683 -8.693-37.071 1.0058.12 N

ATOM 2 CA GLUB 317 -12.504 -7.848-36.916 1.0058.35 C

ATOM 3 CB GLUB 317 -11.252 -8.689-36.655 1.0058.34 C

ATOM . 4 CG GLUB 317 -10.222 -7.983 -35.796 1.0058.29 C

ATOM 5 CD GLUB 317 -10.786 -7.568-34.449 1.0058.49 C

ATOM 6 OEl GLUB 317 -10.392 -6.495-33.940 1.0058.78 O

ATOM 7 OE2GLUB317 -11.630 -8.311-33.901 1.0058.20 O

ATOM 8 C GLUB 317 -12.291 -6.929-38.118 1.0058.52 C

ATOM 9 O GLUB 317 -11.812 -5.806-37.964 1.0058.43 O

ATOM 1 N MET B 318 -12.647 -7.408 -39.309 1.0058.76 N

ATOM 2 CA METB 318 -12.457 -6.621-40.544 1.0059.38 C

ATOM 3 CB METB 318 -12.850 -7.457-41.761 1.0059.35 C

ATOM 4 CG METB 318 -11.790 -8.450-42.180 1.0059.35 C

ATOM 5 SD METB 318 -10.352 -7.627-42.883 1.0059.21 S

ATOM 6 CE METB 318 -11.089 -6.840-44.315 1.0059.36 C

ATOM 7 C MET B 318 -13.194 -5.273 -40.591 1.0059.81 C

ATOM 8 O MET B 318 -14.370 -5.198-40.242 1.0059.90 O

ATOM 1 N PRO B 319 -12.501 -4.208-41.048 1.0060.27 N

ATOM 2 CA PRO B 319 -13.070 -2.859-41.164 1.0060.66 C

ATOM 3 CB PRO B 319 -11.830 -1.968-41.230 1.0060.60 C

ATOM 4 CG PRO B 319 -10.811 -2.817-41.904 1.0060.41 C

ATOM 5 CD PRO B 319 -11.097 -4.248-41.497 1.0060.27 C

ATOM 6 C PRO B 319 -13.898 -2.698-42.437 1.0061.12 C

ATOM 7 O PRO B 319 -13.536 -3.243 -43.484 1.0061.23 O

ATOM. 1 N THRB 320 -14.988 -1.936-42.346 1.0061.63 N

ATOM 2- CA THRB 320 -15.997 -1.880-43.413 1.0062.20 C

ATOM 3 CB THRB 320 -17.120 -0.850-43.106 1.0062.25 C

ATOM 4 OGl THRB 320 -16.676 0.476-43.428 1.0062.39 O

ATOM 5 CG2THRB320 -17.533 -0.914-41.636 1.0062.52 C

ATOM 6 C THRB 320 -15.446 -1.611-44.818 1.0062.49 C

ATOM 7 O THRB 320 -15.468 -2.492-45.683 1.0062.58 O

ATOM 1 N VALB 321 -14.951 -0.398-45.043 1.0062.79 N

ATOM 2 CA VALB 321 -14.629 0.029 -4f 401 1.0063.06 ^• C

ATOM 3 CB VAL B 321 -15.352 1.360-46.761 1.0063.09 C

ATOM 4 CGl VALB 321 -15.052 2.457-45.687 1.0063.09 C

ATOM 5 CG2 VALB 321 -14.989 1.830-48.206 1.0063.21 C

ATOM 6 C VALB 321 -13.125 0.097-46.726 1.0063.21 C

ATOM 7 O VALB 321 -12.677 -0.527-47.693 1.0063.23 O

ATOM I N PHEB 322 -12.346 0.829-45.930 1.0063.40 N

ATOM 2 CA PHE B 322 -10.911 0.966-46.222 1.0063.56 C

ATOM 3 CB PHE B 322 -10.553 2.392-46.676 1.0063.65 C

ATOM 4 CG PHE B 322 -11.291 3.475-45.943 1.0063.76 C

ATOM 5 CDl PHE B 322 -12.129 4.341-46.630 1.0063.84 C

ATOM 6 CEl PHE B 322 -12.811 5.344-45.964 1.0064.14 C

ATOM 7 CZ PHE B 322 -12.657 5.492-44.594 1.0064.13 C

ATOM 8 CE2PHEB322 -11.822 4.636-43.898 1.0064.19 C

ATOM 9 CD2PHEB322 -11.143 3.633-44.572 1.0064.04 C

ATOM 10 C PHE B 322 -9.959 0.500-45.119 1.0063.57 C

ATOM 11 O PHEB 322 -10.289 0.536-43.932 1.0063.52 O

ATOM 1 N GLY B 323 -8.771 0.074-45.542 1.0063.63 N

ATOM 2 CA GLY B 323 -7.757 -0.470-44.645 1.0063.75 C

ATOM 3 C GLYB 323 -7.631 -1.967-44.841 1.0063.84 C

ATOM 4 O GLY B 323 -6.624 -2.574-44.481 1.0063.82 O

ATOM 1 N LYS B 324 -8.668 -2.547-45.435 1.0063.98 N

ATOM . 2 CA LYS B 324 -8.803 -3.993-45.634 1.0064.15 C

ATOM 3 CB LYS B 324 ^• -9.766 -4.263-46.799 1.0064.21 C

ATOM 4 CG LYS B 324 -9.836 -3.122-47.823 1.0064.51 C ATOM 5 CD LYS B 324 -10.857 -3.392-48.931 1.0064.43 C

ATOM 6 CE LYS B 324 -12.196 -3.883-48.375 1.0064.92 C

ATOM 7 NZ LYS B 324 -12.780 -2.994 -47.323 1.0064.78 N

ATOM 8 c : LYS B 324 -7.512 -4.807-45.813 1.0064.09 C

ATOM 9 O LYS B 324 -7.325 -5.828-45.148 1.0064.04 O

ATOM 1 N GLU B 325 -6.632 -4.361-46.706 1.0064.10 N

ATOM 2 CA GLUB 325 -5.461 -5.152-47.102 1.0064.12 C

ATOM 3 CB GLU B 325 -4.669 --4.416 -48.191 1.0064.09 C

ATOM 4 CG GLUB 325 -5.490 -4.058-49.424 1.0063.96 C

ATOM 5 CD GLU B 325 -4.531 -4.963-49.990 0.0050.00 C

ATOM 6 OEl GLU B 325 -4.590 -5.825 -49.100 0.0050.00 O

ATOM 7 OE2GLUB325 -4.164 -5.171 -51.156 0.0050.00 O

ATOM 8 C GLUB 325 -4.530 -5.549-45.942 1.0064.19 C

ATOM 9 O GLUB 325 -4.310 -6.781-45.669 1.0064.25 O

ATOM 1 N ASN B 326 -3.972 -4.524-45.270 1.0064.26 N

ATOM 2 CA ASN B 326 -3.005 -4.812-44.204 1.0064.33 ' C

ATOM 3 CB ASN B 326 -2.040 -3.633 -43.942 1.0064.30 C

ATOM 4 CG ASN B 326 -2.752 -2.335-43.604 1.0064.30 C

ATOM 5 ODl ASNB 326 ^• -2.563 -1.317-44.277 1.0064.17 O

ATOM 6 ND2ASNB326 -3.558 -2.357-42.545 1.0064.50 N

ATOM 7 C ASNB 326 -3.681 -5.330-42.925 LOO 64.35 C

ATOM 8 O ASNB 326 -3.046 -5.991-42.099 1.0064.40 O

ATOM 1 N LYS B 327 -4.972 -5.038-42.779 1.0064.30 N

ATOM 2 CA LYS B 327 .5.744 -5.569 -41.664 1.0064.23 C

ATOM 3 CB LYS B 327 -7.138 -4.943-41.602 1.0064.22 C

ATOM 4 CG LYS B 327 -7.630 -4.643-40.184 1.0064.25 C

ATOM 5 CD LYS B 327 -7.454 -5.831-39.244 1.0064.27 C

ATOM 6 CE LYS B 327 -7.613 -5.426-37.784 1.0064.19 C

ATOM 7 NZ LYS B 327 -9.010 -5.015-37.462 1.0064.30 N

ATOM 8 C LYS B 327 -5.855 -7.072-41.841 1.0064.18 G

ATOM 9 O LYS B 327 -5.758 -7.825.-40.879 1.0064.23 O

ATOM 1 N LYS B 328 -6.051 -7.503-43.082 1.0064.17 N

ATOM 2 CA LYS B 328 -6.073 -8.924-43.393 1.0064.23 C

ATOM 3 CB LYS B 328 -6.505 -9.156-44.843 1.0064.21 C

ATOM 4 CG LYS B 328 -6.492-10.616-45.263 1.0064.08 . C

ATOM 5 CD LYS B 328 -6.561-10.764-46.773 1.0064.01 C

ATOM 6 CE LYS B 328 -6.135-12.160-47.201 1.0063.97 C

ATOM ^■7 NZ LYS B 328 -6.027-12.286-48.679 1.0063.96 N

ATOM 8 C LYS B 328 -4.697 -9.536-43.139 1.0064.29 C

ATOM 9 O LYS B 328 -4.569-10.507-42.366 1.0064.33 O

ATOM 1 N LYS B 329 -3.665 -8.960-43.772 1.0064.32 N

ATOM 2 CA LYS B 329 -2.313 -9.511 -43.610 1.0064.39 C

ATOM 3 CB LYS B 329 -1.288 -8.659-44.360 1.0064.37 C

ATOM 4 CG LYS B 329 -1.188-10.172-46.080 0.0050.00 C

ATOM 5 CD LYS B 329 -0.493 -9.545 -47.260 0.0050.00 C

ATOM 6 CE LYS B 329. 0.417-10.565-47.946 0.0050.00 C

ATOM 7^' NZ LYS B 329 0.748 -10.177 ^'-49.338 0.0050.00 N

ATOM 8 C LYS B 329 -1.934 -9.631-42.126 1.0064.44 C

ATOM 9 O LYS B 329 -1.435-10.671-41.665 1.0064.52 O

ATOM 1 N GLNB 330 -2.189 -8.557-41.385 1.0064.44 N

ATOM 2 CA GLNB 330 -1.958 -8.520-39.947 1.0064.45 C-

ATOM 3 CB GLNB 330 -2.258 -7.118-39.410 1.0064.44 C

ATOM 4 CG GLN B 330 -2.343 -7.007-37.897 1.0064.39 C

ATOM 5 CD ■ GLNB 330 -2.721 -5.608-37.443 1.0064.40 C

ATOM 6 OEl GLNB 330 -2.277^' -4.614 -38.021 1.0064.30 O.

ATOM 7 NE2GLNB330 -3.546 -5.524-36.404 1.0064.34 N

ATOM 8 C GLNB 330 -2.805 -9.565-39.225 1.0064.45 C

ATOM 9 O GLN B 330 -2.313-10.287-38.354 1.0064.60 O ATOM 1 N LEUB 331 -4.079 -9.647-39.602 1.0064.39 N

ATOM 2 CA LEUB 331 -4.995 -10.615 -39.009 1.0064.37 C

ATOM 3 CB LEUB 331 -6.402-10.488-39.599 1.0064.32 C

ATOM 4 CG LEUB 331 -7.355 -9.519-38.897 1.0064.30 C

ATOM 5 CDl LEUB 331 -8.678 -9.421-39.641 1.0064.35 C

ATOM 6 CD2LEUB331 -7.581 -9.930-37.453 1.0064.38 C

ATOM 7 C LEUB 331 -4.483-12.039-39.165 1.0064.41 C

ATOM 8 O LEUB 331 -4.671-12.868-38.273 1.0064.39 O

ATOM 1 N ILEB 332 -3.835-12.331-40.290 1.0064.44 N .

ATOM 2 CA ILE B 332 -3.244-13.660-40.445 1.0064.56 C

ATOM 3 CB ILE B 332 -3.234-14.168-41.905 1.0064.53 C

ATOM 4 CGl ILE B 332 -2.752-13.081-42.861 1.0064.67 C

ATOM 5 CDl ILEB 332 -3.018-13.404-44.313 1.0064.93 C

ATOM 6 CG2ILEB332 -4.622-14.638-42.310 1.0064.59 C

ATOM 7 C ILE B 332 -1.861-13.779-39.807 1.0064.64 C

ATOM 8 O ILE B 332 -1.416-14.885-39.502 1.0064.71 O

ATOM 1 N LEUB 333 -1.181-12.653-39.597 1.0064.69 N

ATOM 2 CA LEU B 333 0;026 -12.679 -38.763 1.0064.86 C

ATOM 3 CB LEU B 333 0.767-11.340-38.813 1,0064.84 C

ATOM 4 CG LEU B 333 2.123-11.329-39.526 1.0064.83 C

ATOM 5 CDl LEU B 333 1.995-11.795-40.971 1.0064.93 C

ATOM 6 CD2LEUB333 2.750 -9.944-39.452 1.0064.92 C

ATOM 7 C LEUB 333 -0.321-13.018-37.315 1.0064.95 C

ATOM 8 O LEU B 333 0.434-13.699-36.618 1.0064.92 O

ATOM 1 N LYS B 334 -1.482-12.542-36.881 1.0065.06 N

ATOM 2 CA LYS B 334 -1.910-12.645-35.493 1.0065.32 C

ATOM 3 CB LYS B 334 -2.537-11.303-35.082 1.0065.31 C

ATOM 4 CG LYS B 334 -3.359-11.279-33.799 1.0065.31 C

ATOM 5 CD LYS B 334 -4.251-10.026-33.782 1.0065.18 C

ATOM 6 CE LYS B 334 -5.325-10.098-32.705 1.0064.74 C

ATOM 7 NZ LYS B 334 -6.339 -9.010-32.867 1.0064.46 N

ATOM 8 C . LYS B 334 -2.885-13.813-35.294 1.0065.54 C

ATOM 9 O LYS B 334 -3.741 -13.778 -34.409 1.0065.57. O

ATOM 1 N LEU B 335 -2.743-14.855-36.111 1.0065.83 N

ATOM 2 CA LEU B 335 -3.676-15.984-36.068 1.0066.16 C

ATOM 3 CB LEUB 335 -3.592-16.826-37.346 1.0066.09 C

ATOM 4 CG LEU B 335 -4.906-17.326-37.966 1.0066.13 C

ATOM 5 CDl LEUB 335 -4.704-18.673-38.651 1.0066.05 C

ATOM 6 CD2 LEUB 335 -6.036 -17.420 -36.952 1.0065.95 C

ATOM 7 C LEUB 335 -3.490-16.877-34.839 1.0066.47 C

ATOM 8 O LEU B 335 -4.464-17.217-34.173 1.0066.51 O

ATOM 1 N PRO B 336 -2.239-17.263-34.529 1.0066.81 N

ATOM 2 CA PRO B 336 -2.044-18.144-33.380 1.0067.08 C

ATOM 3 CB PRO B 336 -0.528-18.367-33.357 1.0067.05 C

ATOM 4 CG PRO B 336 0.042-17.221-34.121 1.0066.99 C

ATOM 5 CD PRO B 336 -0.965-16.916-35.181 1.0066.85 C

ATOM 6 C PRO B 336 -2.510-17.486-32.086 1.0067.39 C

ATOM 7 O PRO B 336 -2.762-18.175-31.097 1.0067.44 O

ATOM 1 N VAL B 337 -2.623-16.162-32.102 1.0067.78 N

ATOM 2 CA VALB 337 -3.155 -15.421 -30.966 1.0068.20 C

ATOM 3 CB VAL B 337 -2.758-13.931-31.026 1.0068.20 C

ATOM 4 CGl VALB 337 -2.943-13.275-29.662 1.0068.26 C

ATOM 5 CG2VALB337 -1.317-13.779-31.499 1.0068.27 C

ATOM 6 C VAL B 337 -4.677-15.540-30.966 1.0068.46 C

ATOM 7 O VAL B 337 -5.296-15.754-29.919 1.0068.80 O

ATOM 1 N ILE B 338 -5.269-15.408-32.150 1.0068.70 N

ATOM 2 CA ILE B 338 -6.710-15.578-32.322 1.0068.88 C

ATOM 3 CB ILE B 338 -7.127-15.468-33.806 1.0068.80 C ATOM 4 CGl ILE B 338 -6.908-14.045-34.326 1.0068.70 C

ATOM, 5 CDl ILEB 338 -7.913-13.035-33.805 1.0068.75 C

ATOM 6 CG2ILEB338 -8.582-15.865-33.983 1.0068.67 C

ATOM 7 C ILEB 338 -7.161-16.929-31.769 1.0069.11 C

ATOM 8 O ILE B 338 -8.075-16.995-30.944 1.0069.27 O

ATOM 1 N PHE B 339 -6.507-17.999-32.219 1.0069.30 N

ATOM 2 CA PHE B 339 -6.827-19.346-31.750 1.0069.45 C

ATOM 3- CB PHE B 339 -5.895-20.390-32.380 1.0069.45 C

ATOM 4 CG PHE B 339 -6.113-20.598-33.859 1.0069.55 C

ATOM 5 CDl PHEB 339 -7.244-20.104-34.492 1.0069.69 C

ATOM 6 CEl PHE B 339 -7.444-20.304-35.848 1.0069.63 C

ATOM 7 CZ PHE B 339 -6.519-21.017-36.584 1.0069.58 C .

ATOM 8 CE2 PHE B 339 -5.393-21.524-35.964 1.0069.60 C

ATOM 9 CD2PHEB339 -5.195-21.318-34.610 1.0069.56 C

ATOM 10 C PHE B 339 -6.748-19.427-30.227 1.0069.52 C

ATOM 11 O PHE B 339 -7.670-19.923-29.569 1.0069.66 O

ATOM 1 K ALAB 340 -5.646-18.926-29.675 1.0069.56 N

ATOM 2 CA ALA B 340 -5.449-18.908-28.230 1.0069.59 C

ATOM 3 CB ALAB 340 -4.133-18.214-27.883 1.0069.61 C

ATOM 4 C ALA B 340 -6.619-18.218-27.532 1.0069.61 C

ATOM 5 O ALA B 340 -7.183-18.750-26.564 1.0069.74 O

ATOM 1 N LYS B 341 -6.986-17.035-28.035 1.0069.49 N

ATOM 2 CA LYS B 341 -8.074-16.263-27.437 1.0069.65 C

ATOM 3 CB LYS B 341 -8.160-14.861-28.055 1.0069.67 C

ATOM 4 CG LYS B 341. -6.979-13.952-27.694 1.0069.92 . C

ATOM 5 CD LYS B 341 -7.274-12.477-27.981 1.0069.78 C

ATOM 6 CE LYS B 341 -6.018-11.612-27.838 1.0069.77 C

ATOM 7 NZ LYS B 341 -5.389-11.703-26.483 1.0069.59 N

ATOM 8 C LYS B 341 -9.414-16.993-27.531 1.0069.57 C

ATOM 9 O LYS B 341 -10.126-17.142-26.529 1.0069.70 O

ATOM 1 N ILE B 342 -9.748-17.463-28.731 1.0069.50 N

ATOM 2 CA ILE B 342 -10.994-18.200-28.933 1.0069.48 C

ATOM 3 CB ILE B 342 -11.209-18.597-30.405 1.0069.39 C

ATOM 4 CGl ILE B 342 -11.207-17.354-31.296 1.0069.17 C

ATOM 5 CDl ILEB 342 -11.610-17.626-32.724 1.0068.85 C

ATOM 6 CG2 ILE B 342 -12.524-19.337-30.563 1.0069.32 C

ATOM 7 C ILE B 342 -11.065-19.437-28.037 1.0069.61 C

ATOM 8 O ILE B 342 -12.132-19.764-27.519 1.0069.60 O

ATOM 1 N GLN B 343 -9.936-20.123-27.856 1.0069.77 N

ATOM 2 CA GLN B 343 -9.859-21.194-26.852 1.0069.99 . C

ATOM 3 CB GLN B 343 -8.474^21.856-26.839 1.0069.96 C

ATOM 4 CG GLN B 343 -8.272-22.873-27.946 1.0070.15 C

ATOM 5 CD GLN B 343 -6.883-23,483-27.926 1.0070.33 C

ATOM 6 OEl GLNB 343 -6.283 -23.669 -26.839 1.0071.09 O

ATOM 7 NE2GLNB343 -6.376-23.816-29.151 1.0070.53 N

ATOM 8 C GLN B 343 -10.169-20.640-25.467 1.0070.01 C

ATOM 9 O GLN B 343 -11.012-21.177-24.745 1.0070.02 O

ATOM 1 N LEU B 344 -9.477-19.562-25.105 1.0070.01 N

ATOM 2 CA LEU B 344 -9.665-18.934-23.801 1.0070.13 C

ATOM 3 CB LEU B 344 -8.882-17.615-23.707 1.0070.20 C

ATOM 4 CG LEU B 344 -7.366-17.683-23.472 1.0070.29 C

ATOM 5 CDl LEU B 344 -6.734-16.303-23.623 1.0070.28 C

ATOM 6 CD2LEUB344 -7.043 -18.278 -22.105 1.0070.32 C ^'

ATOM ^*7 C LEU B 344 -11.140-18.682-23.499 1.0070.13 C

ATOM 8 O LEUB 344 -11.654-19.142-22.478 1.0070.23 O

ATOM 1 N GLU B 345 -11.823-17.959-24.387 1.0070.00 N

ATOM 2 CA GLU B 345 -13.170 -17.481 -24.068 1.0070.11 C

ATOM 3 CB GLU B 345 -13.349-16.036-24.542 1.0070.11 C ATOM 4 CG GLU B 345 -12.936-15.805-25.985 1.0070.34 C

ATOM 5 CD GLU B 345 -13.162-14.378-26.431 1.0070.34 C

ATOM 6 OEl GLU B 345 -14.328-14.018-26.701 1.0070.78 O

ATOM 7 OE2GLUB345 -12.172-13.618-26.519 1.0070.66 O

ATOM 8 C GLU B 345 -14.330-18.345-24.570 1.0070.06 C

ATOM 9 O GLU B 345 -15.485-17.922-24.508 1.0070.05 O

ATOM 1 N HIS B 346. -14.037-19.545-25:060 1.0070.09 N

ATOM 2 CA HIS B 346 -15.097-20.438-25.542 1.0070.11 C •

ATOM 3 CB HIS B 346, -15.176-20.431-27.072 1.0070.05 C-

ATOM 4 CG HIS B 346 -16.045-19.349-27.630 1.0069.94 C

ATOM 5 NDl HIS B 346 -17.419-19.371-27.525 1.0069.85 N

ATOM 6. CEl HIS B 346 -17.919-18.296-28.108 1.0070.02 C

ATOM 7 NE2 HIS B 346. -16.919-17.581-28.594 1.0069.91 N

ATOM 8 CD2 HIS B 346 -15.736-18.218-28.309 1.0070.00 C

ATOM 9 C HIS B 346 -14.944 -21.869 -25.042 1.0070.14 C

ATOM 10 O HIS B 346 -15.736-22.744-25.397 1.0070.16 O

ATOM 1 N HIS B 347 -13.925-22.099-24.222 1.0070.14 N

ATOM 2 CA HIS B 347 -13.658-23.422-23.675 1.0070.21 C

ATOM 3 CB HIS B 347 -14.645-23.753-22.554 1.0070.15 C

ATOM 4 CG HIS B 347 -14.672-22.738-21.456 1.0070.25 C

ATOM 5 NDl HIS B 347 -15.571 -21.693 -2L432 1.0070.27 N

ATOM 6 CEl HIS B 347 -15.361-20.961-20.351 1.0070.36 C

ATOM 7 NE2 HIS B 347 -14.359-21.494.-19.675 1.0070.39 N

ATOM 8 CD2 HIS B 347 -13.909-22.606-20.345 1.0070.34 C

ATOM 9 C HIS B 347 -13.719-24.505-24.745 1.0070.23 C

ATOM 10 O HIS B 347 -14.708-25.230-24.851 1.0070.29 O

ATOM 1 N ILE B 348 -12.665-24.603-25.547 1.0070.25 N

ATOM 2 CA ILE B 348 -12.514-25.743-26.442 1.0070.37 C

ATOM 3 CB ILE B 348 -12.829-25.401-27.922 1.0070.40 C

ATOM 4 CGl ILE B 348 -12.103-24.131-28.359 1.0070.55 C

ATOM 5 CDl ILE B 348 -12.926 -22.879 -28.183 1.0070.97 C

ATOM 6 CG2ILEB348 -14.329-25.226-28.124 1.0070.45 C

ATOM 7 C ILE B 348. -11.114-26.336-26.317 1.0070.38 C

ATOM 8 O ILE B 348 -10.144-25.618-26.065 1.0070.43 O

ATOM 1 N SER B 349 -11.023 -27.653 -26.476 1.0070.37 N

ATOM 2 CA SER B 349 -9.748-28.352-26.404 1.0070.38 C

ATOM 3 CB SER B 349 -9.971-29.867-26.344 1.0070.40 C

ATOM 4 OG SER B 349 -8.737-30.566-26.287 1.0070.52 O

ATOM 5 C SER B 349 -8.882-28.006-27.608 1.0070.34 C

ATOM 6 O SERB 349 -9.380-27.934-28.734 1.0070.27 O

ATOM 1 N PRO B 350 -7 '.578 -27.779 -27 '.372 1.0070.29 N

ATOM 2 CA PRO B 350 -6.623-27.530-28.452 1.0070.22 C

ATOM 3 CB PRO B 350 -5.277 -27 '.495 -27.723 1.0070.23 C

ATOM 4 CG PROB 350 -5.622-27.067-26.337 1.0070.27 C

ATOM 5 CD PRO B 350 -6.939-27.722-26.046 1.0070.21 C

ATOM. 6 C PRO B 350 -6.630-28.634-29.519 1.0070.13 C

ATOM 7 O PRO B 350 -6.142-28.421-30.630 1.0070.22 O

ATOM 1 N GLYB 351 -7.189-29.795-29.188 1.0069.88 N

ATOM 2 CA GLY B 351 -7.273-30.899-30.137 1.0069.54 C

ATOM 3 C GLY B 351 -8.320-30.680-31.214 1.0069.38 C

ATOM 4 O GLYB 351 -8.540-31.547-32.065 1.0069.41 O

ATOM 1 N ASP B 352 -8.968-29.516-31.183 1.0069.15 N

ATOM 2 CA ASP B 352 -10.039-29.207-32.128 1.0068.90 C

ATOM 3 CB ASP B 352 -11.248-28.614-31.401 1.0068.94 C

ATOM 4 CG ASP B 352 -11.970-29.629-30.543 1.0069.10 C

ATOM 5 ODl ASP B 352 -13.221-29.587-30.497 1.0069.17 O

ATOM 6 OD2 ASP B 352 -11.288-30.470-29.914 1.0069.78 O

ATOM 7 C. ASP B 352 -9.597 -28.251 -33.230 1.0068.71 C ATOM 8 O ASP B 352 -10.243 -28.157 -34.273 1.0068.69 O

ATOM 1 N : PHE B 353 -8.500 -27.541 -32.993 1.0068.50 N

ATOM 2 CA PHE B 353 -8.036-26.519-33.928 1.0068.34 C

ATOM 3 CB PHE B 353 -7.200-25.470-33.200 1.0068.32 C

ATOM 4 CG PHE B 353 -8.018-24.413-32.535 1.0068.40 C

ATOM 5 CDl PHEB 353 -8.273-23.213-33.179 1.0068.54 C

ATOM 6 CEi I PHE B 353 -9.034-22.233-32.571 1.0068.49 C

ATOM . 7 CZ PHE B 353 -9.553-22.448-31.312 1.0068.51 C

ATOM 8 CE2PHEB353 -9.311-23.646-30.663 1.0068.68 C

ATOM 9 CD2PHEB353 -8.549-24.620-31.275 1.0068.56 C

ATOM 10 C PHE B 353 -7.261-27.066-35.120 1.0068.21 C

ATOM 11 O PHE B 353 -6.497-28.021-34.987 1.0068.28 O

ATOM 1 N PRO B 354 -7.449-26.445-36.294 1.0068.04 N

ATOM 2 CA PRO B 354 -6.724-26.839-37.498 1.0067.82 C

ATOM 3 CB PRO B 354 -7.431-26.057-38.616 1.0067.87 C

ATOM 4 CG PRO B 354 -8.645-25.426-37.984 1.0067.91 C

ATOM 5 CD PRO B 354 -8.359-25.313-36.535 1.0067.93 C

ATOM 6 C PRO B 354 -5.273-26.392-37.407 1.0067.54 C

ATOM 7 O PRO B 354 -4:906-25.682-36.471 1.0067.44 O

ATOM ^•1 N ASP B 355 -4.456-26.806-38.371 1.0067.25 N

ATOM 2 CA ASP B 355 -3.091-26.307-38.464 1.0066.95 C .

ATOM 3 CB ASP B 355 -2.306-27.057-39.542 1.0066.98 C

ATOM 4 CG ASP B 355 -0.873-26.569.-39.667 1.0067.19 C

ATOM 5 ODl ASP B 355 0.041-27.421-39.696 1.0067.62 O

ATOM 6 OD2 ASP B 355 -0.655-25.338-39.735 1.0067.10 O

ATOM 7 C ASP B 355 -3.127-24.813-38.772 1.0066.67 C

ATOM 8 O ASP B 355 -3.760-24.383-39.739 1.0066.78 O

ATOM 1 N CYS B 356 .-2.445-24.029-37.943 1.0066.16 N

ATOM 2 CA CYS B 356 -2.477-22.576-38.049 1.0065.72 C

ATOM 3 CB CYS B 356 -1.656-21.950-36.919 1.0065.76 C

ATOM 4 SG CYS B 356 -2.029-20.216-36.593 1.0065.98 S

ATOM 5 C CYS B 356 -1.970-22.090-39.405 1.0065.43 C

ATOM 6 O CYS B 356 -2.568-21.203-40.019 1.0064.92 O

ATOM 1 N GLN B 357 -0.878-22.689-39.873 1.0065.25 N

ATOM 2 CA GLNB 357 -0.219-22.247-41.103 1.0065.06 C

ATOM 3 CB GLNB 357 1.238-22.723-41.137 1.0065.11 C

ATOM 4 CG GLN B 357 2.164-21.874-40.268 1.0065.39 C

ATOM 5 CD GLNB 357 3.450-22.588-39.895 1.0065.96 C .

ATOM 6 OEl GLNB 357 4.496-21.939-39.705 1.0066.00 O

ATOM 7 NE2GLNB357 3.377-23.933-39.783 1.0066.01 N

ATOM 8 C GLNB 357 -0.966-22.615-42.391 1.0064.82 C

ATOM 9 O GLNB 357 -1.003-21.825-43.342 1.0064.50 O

ATOM 1 N LYS B 358 -1.561-23.805-42.425 1.0064.56 N

ATOM 2 CA LYS B 358 -2.398-24.192-43.556 1.0064.41 C

ATOM 3 CB LYS B 358 -2.910-25.623-43.382 1.0064.55 C

ATOM 4 CG LYS B 358 -3.547-26.218-44.634 1.0065.05 C

ATOM 5 CD LYS B 358 .-2.500 -26.546 -45.696 1.0065.74 C

ATOM 6 CE LYS B 358 -3.140-27.141-46.947 1.0066.04 C

ATOM 7 NZ LYS B 358 -2.121-27.613-47.935 1.0066.17 N

ATOM 8 C LYS B 358 -3.567-23.215-43.640 1.0064.12 C

ATOM 9 O LYS B 358 -3.829-22.600-44.690 1.0063.78 O

ATOM 1 N MET B 359 -4.252-23.074-42.509 1.0063.91 N

ATOM 2 CA . MET B 359 -5.318-22.101-42.352 1.0063.82 C

ATOM 3 CB MET B 359 -5.798-22.083-40.899 1.0063.91 C

ATOM 4 CG METB 359 -7.134-21.389-40.669 1.0064.20 C

ATOM 5 SD MET B 359 -8.547-22.269-41.375 1.0065.02 .S

ATOM 6 CE MET B 359 -9.909-21.348-40.663 1.0064.30 C

ATOM 7 C MET B 359 -4.822-20.719-42.766 1.0063.69 C ATOM 8 O MET B 359 -5.586-19.907-43.281 1.0063.41 O

ATOM 1 N GLN B 360 -3.537-20.459-42.555 1.0063.78 N

ATOM 2 CA GLNB 360 -2.954-19.186-42.967 1.0063.51 C

ATOM 3 CB GLN B 360 -1.626-18.937-42.251 1.0063.59 C

ATOM 4 CG GLN B 360 -1.799-18.365-40.854 1.0063.62 C

ATOM 5 CD GLN B 360 -0.531-18.412-40.027 1.0063.50 C

ATOM 6 OEl GLNB 360 -0.315 -17.566 -39.161 1.0063.52 O

ATOM 7 NE2 GLN B 360 0.313-19.403-40.288 1.0063.46 N

ATOM 8 C GLN B 360 -2.797-19.059-44.484 1.0063.40 C

ATOM 9 O GLNB 360 -3.046-17.991-45.049 1.0063.16 O

ATOM 1 N GLU B 361 -2.395-20.144-45.142 1.0063.45 N

ATOM 2 CA GLUB 361 -2.302-20.151-46.604 1.0063.14 C

ATOM 3 CB GLU B 361 -1.642-21.442-47.093 1.0063.14 C .

ATOM 4 CG GLU B 361 -0.401 -22.350 -47.5200.0050.00 C

ATOM 5 CD GLUB 361 -0.196-23.530-48.448 0.0050.00 C

ATOM 6 OEl GLU B 361 -0.650-24.642-48.107 0.0050.00 O

ATOM 7 OE2GLUB361 0.419-23.346-49.520 0.0050.00 O

ATOM 8 C GLUB 361 -3.684-19.978-47.246 1.0063.01 C

ATOM 9 O GLUB 361 -3;882 -19.152 -48.168 1.0062.82 O

ATOM 1 N LEU B 362 -4.648-20.751-46.745 1.0062.93 N-

ATOM 2 CA LEU B 362 -6.011 -20.662 -47.266.1.0062.55 C

ATOM 3 CB LEU B 362 .6.861 -21.809 -46.719 1.0062.51 C

ATOM 4 CG LEU B 362 -6.284-23.205-46.967 1.0062.22 C

ATOM 5 CDl LEU B 362 -7.241-24.272-46.467 1.0061.94 C

ATOM 6 GD2 LEUB 362 -5.971-23.409-48.443 1.0061.87 C

ATOM 7 C LEUB 362 -6.654-19.299-46.962 1.0062.44 C

ATOM 8 O LEUB 362 -7.311-18.678-47.831 1.0062.11 O

ATOM 1 N LEU B 363 -6.460-18.832-45.727 1.0062.56 N

ATOM 2 CA LEUB 363 -6.912-17.501-45.353 1.0062.37 C

ATOM 3 CB LEU B 363 -6.580-17.199-43.890 1.0062.32 C

ATOM 4 CG LEUB 363 -7.712-17.346-42.870 1.0062.11 C

ATOM 5 CDl LEUB 363 -8.825-16.381-43.199 1.0062.15 C

ATOM 6 CD2LEUB363 -8.253-18.759-42.827 1.0061.97 C

ATOM 7 C LEU B 363 -6.259 -16.483 -46.274 1.0062.38 C

ATOM 8 O LEU B 363 -6.862-15.468-46.622 1.0062.29 O

ATOM 1 N MET B 364 -5.021-16.770-46.670 1.0062.56 N

ATOM 2 CA MET B 364 -4.321-15.949-47.654 1.0062.46 C

ATOM 3 CB MET B 364 -2.876-16.436-47.836 1.0062.50 C

ATOM 4 CG MET B 364 -1.949-15.444-48.526 1.0062.64 C

ATOM 5 SD MET B 364 -1.755-13.900-47.604 1.0063.45 S

ATOM 6 CE MET B 364 -0.474-13.066-48.552 1.0063.02 C

ATOM 7 C MET B 364 -5.076-16.000-48.980 1.0062.32 C

ATOM 8 O MET B 364 -5.079-15.030-49.741 1.0062.24 O

ATOM 1 N ALAB 365 -5.727-17.132-49.245 1.0062.25 N

ATOM 2 CA ALAB 365 -6.514-17.277-50.482 1.0061.89 C

ATOM 3 CB ALAB 365 -6.630-18.749-50.871 1.0061.88 C

ATOM 4 C ALA B 365 -7.906-16.615-50.484 1.0061.73 C

ATOM 5 O ALAB 365 -8.401-16.219-51.539 1.0061.65 O

ATOM 1 N HIS B 366 -8.539-16.491-49.318 1.0061.58 N

ATOM .2 CA HIS B 366 -9.928-15.979-49.260 1.00.61.07 C

ATOM 3 CB HIS B 366 -10.678-16.621-48.097 1.0061.07 C

ATOM 4 CG HIS B 366 -11.201-17.983-48.405 1.0060.77 C

ATOM . 5 NDl HIS B 366 -10.381-19.026-48.776 1.0060.88 N

ATOM 6 CEl HIS B 366 -11.113-20.104-48.989 1.0061.03 C

ATOM 7 NE2 HIS B 366 -12.379-19.796-48.769 1.0061.08 N

ATOM 8 CD2 HIS B 366 -12.461-18.475-48.402 1.0060.66 C

ATOM 9 C HIS B 366 -10.106-14.462-49.169 1.0060.91 C

ATOM 1C ) O HIS B 366 -9.159-13.732-48.884 1.0060.95 O ATOM 1 N ASP B 367 -11.337-14.001-49.407 1.0060.67 N

ATOM 2 CA ASP B 367 -11.709-12.600-49.181 1.0060.54 C

ATOM 3 CB ASP B 367 -12.589-12.052-50.307 1.0060.59 C

ATOM 4 CG ASP B 367 -13.051-10.615-50.044 1.0060.69 C

ATOM 5 ODl ASP B 367 -13,641 -9.993-50.956 1.0060.49 O

ATOM 6 OD2 ASP B 367 -12.824-10.103-48.925 1.0060.90 O

ATOM 7 C ASP B 367 -12.447-12.442-47.863 1.0060.51 C

ATOM 8 O ASP B 367 -13.446-13.117-47.610 1.0060.68 O

ATOM ■1 N. PHE B 368 -11.968-11.519-47.038 1.0060.30 N

ATOM 2 CA PHEB 368 -12.480-11.376-45.689 1.0060.01 C

ATOM 3 CB PHE B 368 -11.456-10.666-44.807 1.0060.10 C

ATOM 4 CG PHE B 368 -10.346-11.562-44.336 1.0060.32 C

ATOM 5 CDl PHE B 368 -9.815-12.532-45.176 1.0060.54 C

ATOM 6 CEl PHEB 368 -8.795-13.358-44.750 1.0060.45 C

ATOM 7 CZ PHE B 368 -8.284-13.217-43.475 1.0060.53 C

ATOM 8 CE2PHEB368 -8.799-12.251-42.627 1.0060.66 C

ATOM 9 CD2PHEB368 -9.823-11.430-43.060 1.0060.62 C

ATOM 10 C PHEB 368 -13.824-10.673-45.645 1.0059.80 C

ATOM 11 O PHE B 368 -14.704-11.067-44.885 1.0059.86 O

ATOM 1 N THR B 369 -13.986 -9.641 -46.466 1.0059.53 N

ATOM 2 CA THRB 369 -15.217 -8.854-46.451 1.0059.25 C

ATOM 3 CB THRB 369 -15.113 -7.593-47.340 1.0059.18 C

ATOM 4 OGl THRB 369 -14.994 -7.974-48.716 1.0059.25 O

ATOM 5 CG2THRB369 -13.907 -6.761-46.940 1.0059.10 C

ATOM 6 C THRB 369 -16.427 -9.691-46.858 1.0059.10 C

ATOM 7 O THRB 369 -17.568 -9.311-46.603 1.0058.97 O

ATOM 1 N LYSB 370 -16.170 -10.840 -47.476, 1.0059.01 N

ATOM 2 CA LYS B 370 -17.240-11.725-47.923 1.0058.97 C

ATOM 3 CB LYS B 370 -16.818-12.482-49.184 1.0059.01 C

ATOM 4 CG LYS B 370 -16.359-11.596-50.333 1.0059.07 C

ATOM 5 CD LYS B 370 -17.508-11.175-51.234 1.0059.12 C

ATOM 6 CE LYS B 370 -16.990-10.481-52.491 1.0059.61 C

ATOM 7 NZ LYS B 370 -15.988-11.309-53.245 1.0059.98 N

ATOM 8 C LYS B 370 -17.652-12.715-46.836 1.0058.95 C

ATOM 9 O LYS B 370 -18.735-13.292-46.901 1.0058.95 O

ATOM 1 N PHE B 371 -16.785-12:914-45.844 1.0058.98 N

ATOM 2 CA PHEB 371 -17.095-13.790-44.713 1.0059.03 C

ATOM 3 CB PHEB 371 -15.974-13.759-43.669 1.0058.86 C

ATOM 4 CG PHE B 371 -14.716-14.459-44.098 1.0058.79 C

ATOM 5 CDl PHEB 371 -13.479-14.003-43.673 1.0058.52 C

ATOM 6 CEl PHE B 371. -12.318-14.644-44.060 1.0058.30 C

ATOM 7 CZ PHEB 371 -12.383-15.752-44.883 1.0058.32 C

ATOM 8 CE2PHEB371 -13.606-16.218-45.314 1.0058.37 C

ATOM 9 CD2PHEB371 -14.766-15.574-44.922 1.0058.75 C

ATOM 10 C PHEB 371 -18.402-13.386-44.043 1.0059.21 C

ATOM 11 O PHEB 371 -18.791-12.223-44.079 1.0059.25 O

ATOM 1 N HIS B 372 -19.079-14.346-43.427 1.0059.50 N

ATOM 2 CA HIS B 372 -20.289-14.040-42.677 1.0059.80 C

ATOM 3 CB HIS B 372 -21.298-15.180-42.790 1.0059.85 C .

ATOM 4 CG HIS B 372 -21.963-15.261-44.127 1.0059.95- C

ATOM 5 NDl HIS B 372 -22.899-14.342-44.548 1.0059.92 N

ATOM 6 CEl HIS B 372 -23.314-14.663-45.760 1.0060.28 C

ATOM 7 NE2 HIS B 372 -22.678-15.756-46.142 1.0060.47 N

ATOM 8 CD2 HIS B 372 -21.827-16.150-45.139 1.0060.21 C

ATOM 9 C HIS B 372 . -19.968-13.754-41.215 1.0059.98 C

ATOM 10 O HIS B 372 -18.885-14.092-40.734 1.0060.08 O

ATOM 1. N SERB 373 -20.913-13.130-40.513 1.0060.16 N

ATOM 2 CA SER B 373 -20.731-12.788-39.100 1.0060.24 C ATOM 3 CB SER B 373 -21.512-11.521-38.748 1.0060.28 C

ATOM 4 OG SER B 373 -21.188-10.461-39.631 1.0060.74 O

ATOM 5 C SER B 373 -21.164-13.918-38.178 1.0060.17 C

ATOM 6 O SERB 373 -21.854-14.847-38.592 1.0060.00 . O

ATOM 1 N LEU B 374 -20.759-13.828-36.919 1.0060.35 N

ATOM 2 CA LEU B 374 -21.161-14.813-35.928 1.0060.62 C

ATOM 3 CB LEU B 374 -20.625-14.424-34.550 1.0060.56 C

ATOM 4 CG LEU B 374 -20.572-15.531-33.499 1.0060.72 C

ATOM 5 CDl LEUB 374 -19.481-15.247-32.474 1.0061.21 C

ATOM 6 CD2LEUB374 -21.920-15.707-32.823 1.0060.74 C

ATOM 7 C LEU B 374 -22.684-14.936-35.911 1.0060.76 C

ATOM 8 O LEU B 374 -23.394-13.933-35.966 1.0060.93 O

ATOM 1 N LYS B 375 -23.182-16.167-35.853 1.0060.82 N

ATOM 2 CA LYS B 375 -24.620-16.420-35.868 1.0060.84 C

ATOM 3 CB LYS B 375 -25.035-17.002-37.219 1.0060.91 C

ATOM 4 CG LYS B 375 -24.869-16.044-38.385 1.0061.48 C

ATOM 5 CD LYS B 375 -26.197 -15.434 -38.799 1.0062.71 C

ATOM 6 CE LYS B 375 -27.053-16.457-39.546 1.00.63.51 C

ATOM 7 NZ LYS B 375 -28.354-15.899-40.015 1.0063.82 N

ATOM 8 C LYS B 375 -24.991-17.381-34.745 1.0060.68 C

ATOM 9 O LYS B 3.75 -24.979-18.595-34.937 1.00.60.73 O

ATOM 1 N PRO B 376 -25.338-16.837-33,570 1.0060.57 N

ATOM 2 CA PRO B 376 -25.518-17.632-32.357 1.0060.57 C

ATOM 3 CB PRO B 376 -26.021-16.607-31.338 1.0060.60 C

ATOM 4 CG PRO B 376 -25.546-15.295-31.849 1.0060.61 C

ATOM 5 CD PRO B 376 -25.597-15.407-33.339 1.0060.55 C

ATOM 6 C PRO B 376 -26.542-18.746-32.530 1.0060.59 C

ATOM 7 O PRO B 376 -26.407-19.809-31.927 1.0060.69 O

ATOM 1 N LYS B 377 -27.550-18.495-33.358 1.0060.59 N

ATOM 2 CA LYS B 377 -28.631-19.446-33.598 1.0060.71 ' C

ATOM 3 CB LYS B 377 -29.629-18.839-34.588 1.0060.74 C

ATOM 4 CG LYS B 377 -29.017-17.771-35.499 1.0061.05 C

ATOM 5 CD LYS B 377 -29.957-17.378-36.637 1.0061.19 C

ATOM 6 CE LYS B 377 -30.073-18.489-37.682 1.0061.82 C

ATOM 7 NZ LYS B 377 -31.028-18.146-38.781 1.0062.06 N

ATOM 8 C LYS B 377 -28.154-20.821-34.085 1.0060.59 C

ATOM 9 O LYS B 377 -28.432-21.849-33.454 1.0060.69 O

ATOM 1 N LEU B 378 -27.435-20.834-35.205 1.0060.51 N

ATOM 2 CA LEU B 378 -26.950-22.076-35.80.6 1.0060.41 C

ATOM 3 CB LEU B 378 -26.243-21.783-37.126 1.0060.35 C

ATOM 4 CG LEUB 378 -27.021 -20.939-38.140 1.0060.12 C

ATOM 5 CDl LEUB 378 -26.117-20.552-39.295 1.0059.86 C

ATOM 6 CD2LEUB378 -28.267-21.663-38.641 1.0059.70 C

ATOM 7 C LEUB 378 -26.007-22.807-34.861 1.0060.42 C

ATOM 8 O LEU B 378 -26.128-24.019-34.645 1.0060.64 O

ATOM 1 N LEU B 379 -25.064-22.056-34.305 1.0060.36 N

ATOM 2 CA LEUB 379 -24.186-22.568-33.266 1.0060.34 C

ATOM 3 CB LEUB 379 -23.368-21.425-32.669 1.0060.18 C

ATOM 4 CG LEU B 379 -22.157-21.020-33.511 1.0059.81 C

ATOM 5 CDl LEU B 379 -22.024-19.515-33.633 1.0059.39 C

ATOM 6 CD2LEUB379 -20.894-21.632-32.931 1.0059.83 C

ATOM 7 C LEU B 379 -24.993 -23:284 -32.188 1.0060.50 C

ATOM 8 O LEUB 379 -24.778-24.470-31.922 1.0060.81 O

ATOM 1 N GLU B 380 -25.932-22.567-31.579 1.0060.65 N

ATOM 2 CA GLUB 380 -26.808-23.167-30.580 1.0060.83 C

ATOM 3 CB GLUB 380 -27.938-22.214-30.192 1.0060.85 C

ATOM •4 CG GLUB 380 -27.618-21.304-29.025 1.0060.88 C

ATOM 5 CD GLU B 380 -28.855-20.937-28.235 1.0061.03 . C ATOM 6 OEl GLUB 380 -28.781-20.931-26.991 1.0061.38 O

ATOM 7 OE2 GLUB 380 ^'-29.907-20.673-28.854 1.0061.20 O

ATOM 8 C GLUB 380 -27.396-24.470-31.097 1.0060.92 C

ATOM ^■9 O GLUB 380 -27.372-25.499-30.402 1.0061.26 O

ATOM 1 N ALAB 381 -27.924-24.420-32.319 1.0060.89 N

ATOM 2 CA ALAB 381 -28.484-25.606-32.952 1.0061.02 C

ATOM 3 CB ALAB 381 -28.820-25.322-34.403 1.0060.97 C

ATOM 4 C ALAB 381 -27.491-26.754-32.847 1.0061.14. C

ATOM 5 O ALAB 381 -27.844-27.872-32.458 1.0061.43 O

ATOM 1 N LEUB 382 -26.241-26.460-33.182 1.0061.13 N

ATOM 2 CA LEUB 382 -25.166-27.438-33.083 1.0061.34 C

ATOM 3 CB LEUB 382 -23.865-26.808-33.592 1.0061.35 C

ATOM 4 CG LEUB 382 -22.699-27.671-34.081 1.0061.48 C

ATOM 5 CDl LEU B 382 -21.636-27.835-32.998 1.0061.27 C

ATOM 6 CD2LEUB382 -23.194-29.019-34.602 1.0062.11 C

ATOM 7 C LEU B 382 -25.006-27.964-31.647 1.0061.46 C

ATOM 8 O LEUB 382 -25.236-29.157-31.374 1.0061.78 O

ATOM 1 N ASP B 383 -24.627-27.070-30.733 1.0061.44 N

ATOM 2 CA ASP B 383 -24.367-27.453-29.340 1.0061.75 C

ATOM 3 CB ASP B 383 -24.243-26.209-28.452 1.0061.77 C

ATOM 4 CG ASP B 383 -23.278-25.172-29.015 1.0061.90 C

ATOM 5 ODl ASP B 383 -22.998-25.208-30.229 1.0062.19 O

ATOM 6 OD2 ASP B 383 -22.802 -24.311 -28.243.1.0062.06 . O

ATOM 7 C ASP B 383 -25.474-28.358-28.809 1.0061.90 C

ATOM 8 O ASP B 383 -25.222-29.471-28.294 1.0062.21 O

ATOM 1 N ASP B 384 -26.704-27.870-28.949 1.0061.93 N

ATOM 2 CA ASP B 384 -27.877-28.633-28.554 1.0062.20 C

ATOM 3 CB ASP B 384 -29.159-27.857-28.871 1.0062.22 C

ATOM 4 CG ASP B 384 -30.405-28.552-28.356 1.0062.42 C

ATOM 5 ODl ASP B 384 -30.668-28.477-27.136 1.0062.53 O

ATOM 6 OD2 ASP B 384 -31.125-29.168-29.172 1.0062.70 O

ATOM 7 C ASP B 384 -27.887-29.985-29.262 1.0062.27 C

ATOM 8 O ASP B 384 -28.130-31.022-28.622 1.0062.50 O

ATOM 1 N MET B 385 -27.609-29.969-30.573 1.0062.20 N .

ATOM 2 CA METB 385 -27.594-31.206-31.352 1.0062.37 C

ATOM 3 CB MET B 385- -27.031-31.035-32.769 1.0062.38 C

ATOM 4 CG MET B 385 -26.951-32.383-33.532 1.0062.39 C

ATOM 5 SD MET B 385 -25.635-32.605-34.766 1.0062.11 S

ATOM 6 CE MET B 385 -24.227-33.021-33.730 1.0061.97 ^• C

ATOM 7 C MET B 385 -26.744-32.216-30.639 1.0062.48 C

ATOM 8 O METB 385 -27.260-33.215-30.115 1.0062.86 O

ATOM 1 N LEUB 386 -25.437-31.958-30.611 1.0062.43 N

ATOM 2 CA LEUB 386 -24.558-32.982-30.070 1.0062.76 C

ATOM 3 CB LEUB 386 -23.056-32.642-30.160 1.0062.76 C

ATOM 4 CG LEUB 386 -22.440-31.254-29.955 1.0062.69 C

ATOM 5 CDl LEUB 386 -20.974-31.394-29.566 1.0062.40 C

ATOM 6 CD2.LEUB386 -22.572-30.425-31.218 1.0062.82 C

ATOM ^• 7 C LEUB 386 -25.015-33.334-28.666 1.0062.86 C

ATOM 8 O LEUB 386 -25.436-34.480-28.422 1.0063.18 O

ATOM 1 N ALAB 387 -25.006-32.335-27.779 1.0062.84 N

ATOM 2 CA ALAB 387 -25.437-32.545-26.396 1.0063.11 C

ATOM 3 CB ALAB 387 -25.713-31.207-25.715 1.0062.92 C

ATOM 4 C ALAB387 -26.663-33.465-26.298 1.0063.24 C

ATOM 5 O ALAB 387 -26.542-34.694-26.107 1.0063.61 O

ATOM 1 N GLNB 388 -27.843-32.877-26.467 1.0063.14 ^'N

ATOM 2 CA GLN B 388 -29.082-33.594-26.185 1.0063.43 C

ATOM 3 CB GLNB 388 -30.244-32.603-26.059 1.0063.49 C

ATOM. 4 CG GLNB 388 -29.854-31.297-25.371 1.0063.57 C ATOM 5 CD GLN B 388 -30.908-30.790-24.402 1.0063.61 C

ATOM 6 OEl GLN B 388 -31.675 -31.570 -23.830 1.0063.36 O

ATOM 7 NE2GLNB388 -30.941-29.477-24.202 1.0063.79 N

ATOM 8 C GLNB 388 -29.406-34.688-27.207 1.0063.52 C

ATOM 9 O GLNB 388 -29.698-35.850-26.842 1.0063.82 O

ATOM 1 N ASP B 389 -29.344-34.323-28.486 1.0063.47 N

ATOM 2 CA ASP B 389 -29.769-35.242-29.529 1.0063.75 C

ATOM 3 CB ASP B 389 -29.774-34.549-30.891 1.0063.76 C

ATOM 4 CG ASP B 389 -30.851-33.484-30.995 1.0064.01 C

ATOM 5 ODl ASP B 389 -32.035-33.801-30.746 1.0064.41 O

ATOM 6 OD2 ASP B 389 -30.517-32.328-31.329 1.0064.29 O

ATOM 7 C ASP B 389 -28.895-36.491-29.545 1.0063.83 C

ATOM 8 O ASP B 389 -29.409-37.633-29.769 1.0064.19 O

ATOM 1 N ILE B 390 -27.582-36.290-29.283 1.0063.79 N

ATOM 2 CA ILE B 390 -26.702-37.449-29.319 1.0064.00 C

ATOM 3 CB ILE B 390 -25.257-37.051-29.645 1.0063.95 C

ATOM 4 CGl ILE B 390 -25.170-36.707-31.135 1.0063.71 C

ATOM 5 CDl ILE B 390 -23.857-36.139-31.565 1.0063.77 C

ATOM 6 CG2ILEB390 -24.289-38.171-29.283 1.0063.97 C

ATOM 7 C ILE B 390 -26.849-38.215-28.008 1.0064.14 . C

ATOM 8 O ILE B 390 -26.847-39.465-27.987 1.0064.58 O

ATOM 1 N ALAB 391 -27.030-37.458-26.925 1.0064.14 N

ATOM 2 CA ALAB 391 -27.407-38.063-25.658 1.0064.26 C

ATOM 3 CB ALAB 391 -27.864-37.001-24.673 1.0064.25 C

ATOM 4 C ALAB 391 -28.498-39.120-25.865 1.0064.38 C

ATOM 5 O ALAB 391 -28.328-40.265-25.456 1.0064.34 O

ATOM 1 N LYS B 392 -29.600-38.750-26.522 1.0064.51 N

ATOM 2 CA LYS B 392 -30.752-39.681-26.672 1.0065.03 C

ATOM ^' 3 CB LYS B 392 -32.041-38.900-27.039 1.0065.00 C

ATOM 4 CG LYS B 392 -33.202-39.822-27.422 1.0065.42 C

ATOM 5 CD LYS B 392 -34.304-39.084-28.196 1.0065.51 C

ATOM 6 CE LYS B 392 -33.876-38.797-29.657 1.0066.25 C

ATOM 7 NZ LYS B 392 -34.960-38.108-30.448 1.0066.63 N

ATOM 8 C LYS-B J892 -30.564-40.824-27.719 1.0065.09 C

ATOM 9 O LYS B 392 -30.922-42.067-27.733 1.0065.53 O

ATOM 1 N LEU B 393 -29.500-40.372-28.661 1.0065.09 N

ATOM 2 CA LEU B 393 -29.270-41.413-29.680 1.0065.41 C

ATOM 3 CB LEUB 393 -28.567-40.850-30.917 1.0065.35 C

ATOM 4 CG LEU B 393 -29.572-40.402.-31.975 1.0065.48 C

ATOM 5 CDl LEUB 393 -28.854-39.831-33.175 1.0065.63 C

ATOM 6 CD2LEUB393 -30.454-41.576-32.381 1.0065.50 C

ATOM 7 C LEU B 393 -28.469-42.559-29.072 1.0065.64 C

ATOM 8 O LEU B 393 -28.537-43.692-29.565 1.0065.90 O

ATOM 1 N MET B 394 -27.727-42.276-27.994 1.0065.68 N

ATOM 2 CA MET B 394 -26.953-43.350-27.351 1.0066.07 C

ATOM 3 CB MET B 394 -26.160-42.822-26.147 1.0066.11 C

ATOM 4 CG MET B 394 -25.045-41.845-26.512 1.0066.43 C

ATOM 5 SD MET B 394 -23.879-42.505-27.732 1:0067.28 S

ATOM 6 CE MET B 394 -22.646-41.197-27.775 1.0066.63 C

ATOM 7 C METB394 -27.834-44.552-26.951 1.0066.21 C

ATOM 8 O MET B 394 -27.625-45.678-27.434 1.0066.49 O

ATOM l^' N PRO B 395 -28.824-44.319-26.063 1.0066.35 N

ATOM 2 CA PRO B 395 -29.721-45.400-25.637 1.0066.36 C

ATOM 3 CB PRO B 395 -30.859-44.656-24.933 1.0066.30 C

ATOM 4 CG PRO B 395 -30.208-43.450-24.378 1.0066.32 C

ATOM 5 CD PRO B 395 -29.137-43.024-25.387 1.0066.42 C

ATOM 6 C PRO B 395 -30.288-46.183-26.818 1.0066.38 C

ATOM 7 O PRO B 395 -30.347-47.571-26.772 1.0066.53 O ATOM 1 N LEU B 396 -30.497-45.303-28.030 1.0066.35 N

ATOM 2 CA LEU B 396 -31.246-46.083-29.062 1.0066.51 C

ATOM 3 CB LEUB 396 -31.852-45.178-30.154 1.0066.52 C

ATOM 4 CG LEU B 396 -32.912-45.758-31.111 1.0066.50 C

ATOM 5 CDl LEUB 396 -33.315-44.715-32.155 1.0066.78 C

ATOM 6 CD2LEUB396 -32.466-47.051-31.807 1.0066.41 C

ATOM 7 C LEUB 396 -30.201-47.020-29.694 1.0066.56 C

ATOM 8 O LEU B 396 -30.470-48.217-30.094 1.0066.72 O

ATOM 1 N LEU B 397 -28.990-46.430-29.758 1.0066.57 N

ATOM 2 CA LEU B 397 -27.835-47.098-30.313 1.0066.81 C

ATOM 3 CB LEU B 397 -26.607-46.199-30.188 1.0066.77 C -

ATOM 4 CG LEU B 397 -25.289-46.797-30.666 1.0066.74 C

ATOM 5 CDl LEUB 397 -25.328-47.016-32.172 1.0066.79 C

ATOM 6 CD2 LEU B 397 -24.143-45.884-30.274 1.0066.83 C

ATOM 7 C LEU B 397 -27.582-48.420-29.616 1.0066.95 C

ATOM 8 O LEU B 397 -27.383-49.426-30.278 1.0067.22 O

ATOM 1 N ARG B 398 -27.592-48.416-28.284 1.0067.02 N

ATOM 2 CA ARG B 398 -27.336-49.643-27.514 1.0067.30 C

ATOM 3 CB ARG B 398 -27.350.-49.332-26.015 1.0067.36 C

ATOM 4 CG ARG B 398 -26.308-48.309-25.582 1.0067.98 C

ATOM 5 CD ARG B 398 -26.819-47.456-24.424 1.0068.97 C

ATOM 6 NE ARG B 398 -27.294-48.259-23.300 1.0069.67 N

ATOM 7 CZ ARG B 398 -26.505-48.760-22.351 1.0070.33 C

ATOM 8 NHl ARG B 398 -27.028-49.478-21.363 1.0070.67 N

ATOM 9 NH2ARGB398 -25.193-48.547-22.389 1.0070.46 N

ATOM 10 C ARG B 398 -28.366-50.744-27.814 1.0067.28 C

ATOM 11 O ARG B 398 -28.004-52.040-27.953 1.0067.55 O

ATOM 1 N GLN B 399 -29.649-50.229-28.027 1.0067.15 N

ATOM 2 CA GLN B 399 -30.706-51.190-28.344 1.0067.22 C

ATOM 3 CB GLN B 399 -32.089-50.529-28.308 1.0067.21 C

ATOM 4 CG GLN B 399 -33.256-51.484-28.565 1.0067.20 C

ATOM 5 CD GLN B 399 -33.255-52.683-27.622 1.0067.24 C

ATOM 6 OEl GLNB 399 -33.322-53.832-28.070 1.0067.09 O

ATOM 7 NE2GLNB399 -33.174-52.421-26.312 1.0067.33 N

ATOM 8 C GLN B 399 -30.427-51.801-29.713 1.0067.26 C

ATOM 9 O GLN B 399 -30.729-52.973-29.958 1.0067.20 O

ATOM 1 N GLU B 400 -29.833-51.006-30.601 1.0067.33 N

ATOM 2 CA GLU B 400 -29.448-51.520-31.913 1.0067.67 C

ATOM 3 CB GLU B 400 -29.270-50.383-32.917 1.0067.73 . C

ATOM 4 CG GLU B 400 -30.581-49.853-33.487 1.0068.29 C

ATOM 5 CD GLU B 400 -30.356-49.020-34.738 1.0068.96 C

ATOM 6 OEl GLU B 400 -31.298-48.311-35.159 1.0069.08 O

ATOM 7 OE2GLUB400 -29.235-49.077-35.297 1.0069.03 O

ATOM 8 C GLU B 400 -28.181-52.374-31.867 1.0067.75 C

ATOM 9 O GLU B 400 -28.005-53.276-32.686 1.0067.75 O

ATOM 1 N GLUB 401 -27.302-52.089-30.909 1.0067.83 N

ATOM 2 CA GLU B 401 -26.035-52.807-30.795 1.0068.15 C

ATOM 3 CB GLU B 401 -25.015-52.036-29.938 1.0068.25 C

ATOM 4 CG GLU B 401 -23.580-52.606-30.002 1.0068.55. C

ATOM 5 CD GLU B 401 -22.501-51.549-29.779 1.0068.79 C

ATOM 6 OEl GLU B 401 -22.629-50.435-30,334 1.0068.79 O

ATOM 7 OE2 GLUB 401 -21.517-51.839-29.059 1.0068.49 O

ATOM 8 C GLU B 401 -26.275-54.218-30.257 1.0068.19 C

ATOM 9 O GLU B 401 -25.363-55.103-30.342 1.0068.20 O

ATOM 1 N LEU B 402 -27.514-54.443-29.722 1.0068.10 N

ATOM 2 CA LEU B 402 -27.860-55.876-29.534 1.0068.26 C

ATOM 3 CB LEU B 402 -28.151-56.248-28.065 1.0068.22 C

ATOM 4 CG LEU B 402 -28.980-55.386-27.109 1.0068.29 C ATOM 5 CDl LEUB 402 -30.451-55.301-27.514 1.0068.15 C

ATOM 6 CD2LEUB402 -28.840-55.954-25.698 1.0068.27 C

ATOM T C LEU B 402 -28.980-56.322-30.497 1.0068.35 C

ATOM 8 O LEU B 402 -30.147-56.557-30.094 1.0068.28 O

^■ 5 ATOM 1 N GLU B 403 -28.607-56.428-31.781 1.0068.52 N

ATOM 2 CA GLU B 403 -29.588-56.755-32.818 1.0068.65 C

ATOM 3 CB GLU B 403 -29.931-55.521-33.659 1.0068.70 C

ATOM 4 CG GLU B 403 -30.991 -54.639 -33.021.1.0068.74 C

ATOM 5 CD GLU B 403 -32.215-55.426-32.590 1.0068.53 C

10 ATOM 6 OEl GLU B 403 -32.201 -56.670 -32.722 1.0068.11 O

ATOM 7 OE2GLUB403 -33.191-54.802-32.122 1.0068.50 O

ATOM 8 C GLU B 403 -29.214-57,924-33.722 1.0068.69 C

ATOM 9 O GLU B 403 -29.749-59.023-33.563 1.0068.78 O

ATOM .1 N SER B 404 -28.317-57.699-34.679 1.0068.70 N

15 ATOM 2 CA SER B 404 -27.974-58.768-35.617 1.0068.71 C

ATOM 3 CB SER B 404 -28.740-58.599-36.939 1.0068.72 C

ATOM 4 OG SER B 404 -28.941-59.853-37.578 1.0068.64 O

ATOM 5 C SER B 404 -26.470-58.933-35.873 1.0068.68 C

ATOM 6 O SER B 404 -25.844-58.123-36.565 1.0068.72 O

20 ATOM. 1 N VAL B 405 -25.905-59.999-35.307 1.0068.52 N

ATOM 2 CA VAL B 405 -24.514-60.373-35.553 1.0068.31 C

ATOM 3 CB VAL B 405 -24.015-61.401-34.501 1.0068.37 C

ATOM 4 CGl VAL B 405 -22.517-61.661-34.657 1.0068.42 C

ATOM 5 CG2VALB405 -24.816-62.702-34.582 1.0068.30 C

25 ATOM 6 C VAL B 405 -24.359-60.941-36.969 1.0068.09 C

ATOM 7 O VAL B 405 -23.242-61.172-37.443 1.0068.12 O

ATOM 1 N GLU B 406 -25.494-61.154-37.634 1.0067.77 N

ATOM 2 CA GLU B 406 -25.541-61.660-39.008 1.0067.37 C

ATOM 3 CB GLU B 406 -26.992-61.732-39.495 1.0067.50 C

30 ATOM 4 CG GLU B 406 -27.147-62.138-40.957 1.0067.80 C

ATOM 5 CD GLU B 406 -28.069-61.202-41.723 1.0068.31 C

ATOM 6 OEl GLU B 406 -29.061 -61.685 -42.313.1.0068.29 O

ATOM 7 OE2GLUB406 -27.801-59.978-41.732 1.0068.51 O

ATOM 8 C GLU B 406 -24.734-60.777-39.957 1.0066.93 C

35 ATOM 9 O GLU B 406 -24.162-61.265-40.937 1.0066.98 O

ATOM 1 N ALA B 407 -24.697-59.479-39.659 1.0066.23 N

ATOM 2 CA ALA B 407 -23.943-58.516-40.459 1.0065.47 C

ATOM 3 CB ALA B 407 -24.221 -57.094 -39.976 1.0065.49 C

ATOM 4 C ALA B 407 -22.440-58.813-40.442 1.0064.85 C

40 ATOM 5 O ALA B 407 -21.702-58.369-41.328 1.0064.84 O

ATOM 1 N GLY B.408 -22.004-59.576-39.439 1.0064.00 N

ATOM 2 CA GLY B 408 -20.598-59.936-39.266 1.0062.91 C

ATOM 3 C GLY B 408 -19.933-60.428-40.535 1.0062.16 C

ATOM 4 O GLY B 408 -20.582 -61.020 -41.397 1.0062.11 O

45. ATOM 1 N VALB 409 -18.633-60.180-40.649 1.0061.40 N

ATOM 2 CA VAL B 409 -17.880-60.595-41.824 1.0060.66 C

ATOM 3 CB VAL B 409 -16.452-60.013-41.824 1.0060.68 C

ATOM 4 CGl VALB 409 -15.845-60.103-43.213 1.0060.53 C

ATOM 5 CG2VALB409 -16.473-58.573-41.362 1.0060.66 C

50 ATOM .6 C VALB 409 -17.829-62.117-41.919 1.0060.21 C

ATOM 7 O VAL B 409 -17.427-62.803-40.974 1.0060.00 O

ATOM 1 N ALA B 410 -18.250-62.638-43.066 1.0059.67 , N

ATOM 2 CA ALAB 410 -18.324-64.077-43.271 1.0059.13 C

ATOM 3 CB ALA B 410 -19.519-64.425-44.142 1.0059.26 C

55 ATOM 4 C ALA B 410 -17.043-64.616-43.885 1.0058.71 C

ATOM 5 O ALAB 410 -16.274-63.875-44.491 1.0058.61 O

ATOM 1 N GLYB 411 -16.838-65.919-43.723 1.0058.33 N

ATOM ^•2 CA GLY B 411 -15.635-66.617-44.174 1.0057.74 C ATOM 3 C GLYB 411 . -14.718-65.930-45.170 1.0057.25 . C

ATOM 4 O GLYB 411 -15.164-65.273-46.113 1.00.57.29 O

ATOM 1 N GLY B 412 -13.420-66.103-44.946 1.0056.81 N

ATOM 2 CA GLY B 412 -12.385-65.639-45.860 1.0056.24 C

ATOM 3 C GLY B 412 -11.093-66.100-45.229 1.0055.88 C

ATOM 4 O GLY B 412 -10.523-67.115-45.616 1.0055.87 O

ATOM 1 N ALAB 413 -10.649-65.349-44.232 1.0055.53 N

ATOM 2 CA ALAB 413 -9.619-65.806-43.319 1.0055.19 C

ATOM 3 CB ALAB 413 -8.452-64.844-43.313 1.0055.14 C

10 ATOM 4 C ALA B 413 -10.263-65.865-41.946 1.0054.97 C

ATOM 5 O ALAB 413 -9.607-66.140-40.945 1.0055.00 O

ATOM 1 N PHE B 414 -11.566-65.613-41.915 1.0054.73 N

ATOM 2 CA PHE B 414 -12.291-65.468-40.663 1.0054.57 C

ATOM 3 CB PHE B 414 -13.369-64.387-40.793 1.0054.59 C

15 ATOM 4 CG PHE B 414 -12.826-63.027-41.139 1.0054.41 C

ATOM 5 CDl PHE B 414 -12.351-62.184-40.148 1.0054.25 C

ATOM 6 CEl PHE B 414 -11.851-60.941-40.462 1.0054.27 C

ATOM 7 CZ PHE B 414 -11.822-60.521-41.778 1.0054.38 C

ATOM 8 CE2PHEB414 -12.292-61.350-42.774 1.0054.20 • C

20 ATOM 9 CD2PHEB414 -12.791-62.594-42.454 1.0054.24 C

ATOM 10 C PHE B 414 -12.921-66.771-40.194 1.0054.51 C

ATOM 11 O PHE B 414 -13.036-67.005-38.991 1.0054.59 O

ATOM 1 N GLU B 415 -13.327-67.612-41.143 1.0054.32 N

ATOM 2 CA GLU B 415 -13.998-68.872-40.827 1.0054.13 C

25 ATOM 3 CB GLU B 415 -14.168-69.713-42.087 1.0054.25 C

ATOM 4 CG GLUB 415 -12.858-70.145-42.699 1.0055.37 C

ATOM 5 CD GLU B 415 -12.959-70.379-44.192 1.0057.16 C

ATOM 6 OEl GLUB 415 -11.987-70.912-44.778 1.0057.92 O

ATOM 7 OE2 GLUB 415 -14.007-70.025-44.779 1.0057.82 O

30. ATOM 8 C GLU B 415 -13.258 -69.664 -39.750 1.0053.71 . C

ATOM 9 O GLU B 415 -12.027-69.672-39.704 1.0053.58 O

ATOM 1 N GLY B 416 -14.023-70.325-38.886 1.0053.38 N

ATOM 2 CA GLY B 416 -13.466-70.999-37.718 1.0052.98 C

ATOM 3 C GLYB 416 -12.802 -72.320' -38.039 1.0052.72 C

35 ATOM. 4 O GLY B 416 -11.853-72.729-37.367 1.0052.60 O

ATOM 1 N THRB 417 -13.305-72.985-39.075 1.0052.54 N

ATOM 2 CA THRB 417 -12.774-74.275-39.501 1.0052.37 C

ATOM 3 CB THRB 417 -13.594-74.865-40.664 1.0052.27 C

ATOM 4 OGl THR B 417 -13.938-73.824-41.584 1.0051.98 O

40 ATOM 5 CG2 THRB 417 -14.869-75.497-40.147 1.0052.29 C

ATOM 6 C THRB 417 -11.303-74.199-39.906 1.0052.41 C

ATOM 7 O THRB 417 -10.666 r75.226 -40.137 1.0052.44 O

ATOM 1 N ARG B 418 -10.769-72.982-39.984 1.0052.48 N

ATOM 2 CA ARG B 418 -9.376-72.768-40.365 1.0052.60 C

45 ATOM 3 CB ARGB 418 -9.159-71.335-40.852 1.0052.61 _. C

ATOM 4 CG ARG B 418 -9.600-71.097-42.286 1.0053.27 C

ATOM 5 CD ARG B 418 -9.177-69.722-42.800 1.0054.81 C

ATOM 6 NE ARG B 418 -7.737-69.623-43.033 1.0055.96 N

ATOM 7 CZ ARG B 418 -6.871 -69;084 -42.177 1.0056.80 C

50 ATOM 8 NHl ARGB 418 -5.577-69.038-42.478 1.0057.11 N

ATOM 9 NH2ARGB418 -7.295-68.589-41.019 1.0056.93 N

ATOM 10 C ARG B 418 -8.416-73.077-39.226 1.0052.65 C

ATOM 11 O ARG B 418 -7.222-73.271-39.444 1.0052.59 O

ATOM 1 N MET B 419 -8.943-73.129-38.010 1.0052.86 N

55 ATOM 2 CA MET B 419 -8.113-73.399-36.846 1.0053.06 C

ATOM 3 CB MET B 419 -8.676-72.685-35.610 1.0053.29 C

ATOM 4 CG MET B 419 -7.647-72.383-34.513 1.0054.17 C

ATOM 5 SD MET B 419 -6.116-71.599-35.095 1.0055.92 S ATOM 6 CE MET B 419 -4.994-72.997-35.162 1.0055.37 C

ATOM 7 C METB 419 -7.962-74.904-36.603 1.0052.89 C

ATOM 8 O MET B 419 -7.250-75.326-35.693 1.0052.78 O

ATOM 1 N GLY B 420 -8.624-75.707-37.431 1.0052.86 N

ATOM 2 CA GLY B 420 -8.528-77.161-37.334 1.0052.96 C

ATOM 3 C GLY B 420 -9.803-77.821-36.838 1.0053.03 C

ATOM 4 O GLY B 420 -10.731-77.138-36.407 1.0053.13 O

ATOM 1 N PRO B 421 -9.864-79.161-36.911 1.0053.04 N

ATOM 2 CA PRO B 421 -11.037-79.878-36.471 1.0053.09 C

ATOM 3 CB PRO B 421 -11.173-80.952-37.548 1.0052.99 C

ATOM 4 CG PRO B 421 -9.717-81.301-37.885 1.0052.91 C

ATOM 5 CD PRO B 421 -8.857-80.087-37.465 1.0053.05 C

ATOM 6 C PRO B 421 -10.848-80.558-35.115 1.0053.26 C

ATOM • 7 O PRO B 421 -11.742-81.294-34.668 1.0053.35 O

ATOM 1 N PHE B 422 -9.710-80.321-34.459 1.0053.47 N

ATOM 2 CA PHE B 422 -9.361-81.125-33.284 1.0053.71 C

ATOM 3 CB PHE B 422 -7.939-81.673-33.392 1.0053.51 C

ATOM 4 CG PHE B 422 -7.860-82.947-34.161 1.0053.01 C

ATOM 5 CDl PHE B 422 -7.556-82.939-35.506 1.0052.78 C

ATOM 6 CEl PHE B 422 -7.500-84.113-36.221 1.0052.83 C

ATOM 7 CZ PHE B 422 -7.760-85.312-35.596 1.0052.98 C

ATOM 8 CE2 PHE B 422 -8.077-85.331-34.256 1.0052.93 C

ATOM 9 CD2 PHE B 422 -8.131-84.153-33.547 1.0052.79 C

ATOM 10 C PHE B 422 -9.606-80.504-31.913 1.0054.16 C

ATOM 11 O PHE B 422 -10:048 -81.193 -30.989 1.0054.20 O

ATOM 1 N VAL B 423 -9.314-79.217-31.767 1.0054.72 N

ATOM 2 CA VAL B 423 -9.603-78.540-30.507 1.0055.30 C

ATOM 3 CB VAL B 423 -8.329-77.988-29.828 1.0055.35 C

ATOM 4 CGl VAL B 423 -8.687-77.283-28.525 1.0055.52 C

ATOM 5 CG2VALB423 -7.340-79.119-29.559 1.0055.43 C

ATOM 6 C VAL B 423 -10.633-77.434-30.704 1.0055.57 C

ATOM 7 O VAL B 423 -10.364-76.444-31.387 1.0055.56 O

ATOM 1 N GLU B 424 -11.808-77.627-30.100 1.0056.06 N

ATOM 2 CA GLU B 424 -12.936-76.685-30.174 1.0056.34 C

ATOM 3 CB GLU B 424 -12.605-75.352-29.463 1.0056.44 C

ATOM 4 CG GLU B 424 -13.793-74.350-29.302 1.0056.50 C

ATOM 5 CD GLU B 424 -13.681-73.133-30.258 1.0057.30 C

ATOM 6 OEl GLUB 424 -12.463-72.749-30.638 1.0057.51 O

ATOM ^■ 7 OE2GLUB424 -14.750-72.545-30.636 1.0057.40 O

ATOM 8 C GLU B 424 -13.429-76.440-31.610 1.0056.48 C

ATOM 9 O GLU B 424 -12.779-75.721-32.388 1.0056.64 O

TER 9 GLU B 424

ATOM 1 N GLU B 443 -0.405-85.521 -2.811 1.0065.60 N

ATOM 2 CA GLU B 443 0.611-84.482 -2.704 1.0065.73 C

ATOM 3 CB GLU B 443 1.290-84.527 -1.330 1.0066.04 C

ATOM 4 CG GLU B 443 2.377-83.462 -1.118 1.0067.13 C

ATOM 5 CD GLU B 443 1.813-82.071 -0.850 1.0068.58 C

ATOM 6 OEl GLU B 443 0.633-81.816 -1.184 1.0069.01 O

ATOM 7 OE2GLUB443 ^■ 2.558 -81.229 -0.300 1.0069.27 O

ATOM 8 C GLU B 443 1.653-84.609 -3.809 1.0065.36 C

ATOM 9 O GLU B 443 1.374-84.292 -4.965 1.0065.51 O

ATOM 1 N TRP B 444 2.848-85.071 -3.442 1.0064.83 N

ATOM 2 CA TRP B 444 3.954-85.228 -4.383 1.0064.28 C

ATOM 3 CB TRP B 444 5.231-84.611 -3.807 1.0064.11 C

ATOM 4 CG TRP B 444 6.319-84.393 -4.820 1.0063.96 C

ATOM 5 CDl TRP B 444 6.157-84.086 -6.139 1.0063.74 C

ATOM 6 ISlEl TRP B 444 7.382 -83.952 -6.748 1.0063.50 N

ATOM 7 CE2TRPB444 8.367-84.164 -5.821 1.0063.49 C ATOM 8 CD2 TRP B 444 7.736-84.438 -4.591 1.0063.81 C

ATOM 9 CE3 TRP B 444 8.530-84.694 -3.469 1.0063.77 C

ATOM 10 CZ3 TRP B 444 9.909-84.665 -3.612 1.0063.70 C

ATOM 11 CH2 TRP B 444 10.505-84.386. -4.846 1.0063.62 C

ATOM 12 CZ2 TRP B 444 9.753-84.137 -5.960 1.0063.59 C

ATOM 13 C TRP B 444 4.158-86.707 -4.672 1.0064.04 C

ATOM 14 O TRP B 444 4.079-87.531 -3.767 1.0064.09 O

ATOM 1 N VAL B 445 4.426-87.043 -5.930 1.0063.74 N

ATOM 2 CA VAL B 445 4.422-88.445 -6.349 1.0063.47 C

ATOM 3 CB VAL B 445 4.157-88.591 -7.867 1.0063.49 C

ATOM 4 CGl VAL B 445 3.400-89.891 -8.137 1.0063.40 C

ATOM 5 CG2VALB445 3.347-87.410 -8.382 1.0063.67 C

ATOM 6 C VAL B 445 5.686-89.236 -5.995 1.0063.28 C

ATOM 7 O VAL B 445 5.652-90.466 -5.953 1.0063.22 O

ATOM 1 N VAL B 446 6.797-88.549 -5.742 1.0063.03 N

ATOM 2 CA VAL B 446 8.068-89.251 -5.538 1.0062.82 C

ATOM 3 CB VAL B 446 9.25.8-88.540 -6.237 1.0062.73 C

ATOM 4 CGl VAL B 446 8.775-87.739 -7.436 1.0062.74 C

ATOM ^•5 CG2VALB446 9.992-87.644 -5.271 1.0062.62 C

ATOM 6 C VAL B 446 8.400-89.527 -4.066 1.0062.78 C

ATOM 7 O VAL B 446 9.343-90.263 -3.764 1.0062.73 O

ATOM 1 N THR B 447 7.616-88.954 -3.155 1.0062.71 • N

ATOM 2 CA THR B 447 7.850-89.148 -1.722 1.0062.74 C

ATOM 3 CB THR B 447 6.862-88.339 -0.858 1.0062.72 C

ATOM 4 OGt THRB 447 5.639-88.163 -1.578 1.0063.01 O

ATOM 5 CG2THRB447 7.438-86.972 -0.526 1.0062.66 C

ATOM 6 C THR B 447 7.820-90.620 -1.301 1.0062.71 C

ATOM 7 O THR B 447 8.427-90.991 -0.295 1.0062.63 O

ATOM 1 N LYS B 448 7.121 -91.453 -2.070 1.0062.74 N

ATOM 2 CA LYS B 448 7.119-92.895. -1.822 1.0062.80 C

ATOM 3 CB LYS B 448 6.130-93.628 -2.735 1.0062.76 C

ATOM 4 CG LYS B 448 4.711-93.108 -2.686 1.0063.05 C

ATOM 5 CD LYS B 448 4.392-92.289 -3.923 1.0063.48 C

ATOM 6 CE LYS B 448 3.255-91.319 -3.661 1.0063.64 C

ATOM 7 NZ LYS B 448 3.668-90.275 -2.681 1.0063.53 N

ATOM 8 C LYS B 448 8.514-93.490 -2.009 1.0062.83 C

ATOM 9 O LYS B 448 8.957-94.314 -1.209 1.0063.01 O

ATOM 1 N ASP B 449 9.203-93.070 -3.065 1.0062.70 N

ATOM 2 CA ASP B 449. 10.507-93.632 -3.390 1.0062.64 C

ATOM 3 CB ASP B 449 10.618-93.837 -4.902 1.0062.80 C

ATOM 4 CG ASP B 449 9.549-94.782 -5.444 1.0063.19 C

ATOM 5 ODl ASP B 449 9.378-95.890 -4.877 1.0063.74 O

ATOM 6 OD2 ASP B 449 8.881 -94.419 -6.439 1.0063.29 O

ATOM 7 C ASP B 449 11.632-92.743 -2.869 1.0062.46 C

ATOM 8 O ASP B 449 12.816-92.959 -3.166 1.0062.44 O

ATOM 1 N LYS B 450 11.247-91.756 -2.066 1.0062.30 N

ATOM 2 CA LYS B 450 12.174-90.744 -1.578 1.0062.13 C

ATOM 3 CB LYS B 450 11.449-89.734 -0.687 1.0062.11 C

ATOM 4 CG LYS B 450 11.805-88.274 -0.967 1.0061.77 C

ATOM 5 CD LYS B 450 13.208-87.897 -0.505 1.0060.83 C

ATOM 6 CE LYS B 450 13.530-86.454 -0.874 1.0059.97 C

ATOM 7 NZ LYS B 450 14.896-86.047 -0.463 1.0059.33 N

ATOM 8 C LYS B 450 13.360-91.352 -0.833 1.0062.15 C

ATOM 9 O LYS B 450 14.487-91.248 -1.294 1.0062.07 O

ATOM 1 N SERB 451 13.106-91.983 0.310 1.0062.16 N

ATOM 2 CA SER B 451 14.180-92.559 1.125 1.0062.17 C

ATOM 3 CB SER B 451 13.587-93.360 2.281 1.0062.12 C

ATOM 4 OG SERB 451 12.298-93.834 1.938 1.0062.06 O ATOM 5 C SERB 451 15.154-93.415 0.303 1.0062.26 C

ATOM 6 O SER B 451 16.370-93.404 0.536 1.0062.26 O

ATOM 1 N LYS B 452 14.605-94.144 -0.662 1.0062.25 N

ATOM 2 CA LYS B 452 15.375-94.923 -1.626 1.0062.40 . C

ATOM 3 CB LYS B 452 14.369-95.657 -2.519 1.0062.38 C

ATOM 4 CG LYS B 452 14.904-96.422 -3.717 1.0062.84 C

ATOM 5 CD LYS B 452 13.773-97.330 -4.253 1.0063.07 C

ATOM 6 CE LYS B 452 13.989-97.788 -5.702 1.0064.07 C

ATOM 7 NZ LYS B 452 13.378-96.868 -6.709 1.0063.97 N

ATOM 8 C LYS B 452 16.312-94.016 -2.449 1.0062.22 C

ATOM 9 O LYS B 452 17.575-94.152 -2.426 1.0062.21 O

ATOM 1 N TYR B 453 15.696-93.076 -3.164 1.0062.12 N

ATOM 2 CA TYR B 453 16.465-92.110 -3.934 1.0061.83 C

ATOM 3 CB TYR B 453 15.541-91.057 -4.531 1.0061.96 C

ATOM 4 CG TYR B 453 14.589-91.611 -5.559 1.0062.18 C

ATOM 5 CDl TYRB 453 14.878-92.789 -6.231 1.0062.45 C

ATOM 6 CEl TYR B 453. 14.016-93.298 -7.179 1.0062.52 C

ATOM 7 CZ TYR B 453 12.855 -92.622 -7.475 1.0062.28 C

ATOM 8 OH TYR B 453 12.004-93.133 -8.419 1.0062.68 O

ATOM 9 CE2TYRB453 12.543-91.445 -6.830 1.0062.18 C

ATOM 10 CD2 TYRB 453 13.411-90.945 -5.878 1.0062.43 C

ATOM 11 C TYR B 453 17.547-91.449 -3.082 1.0061.73 C

ATOM 12 O TYR B 453 18.696-91.346 -3.504 1.0061.52 O

ATOM 1 N ASP B 454 17.167-91.011 -1.883 1.0061.76 N

ATOM 2 CA ASP B 454 18.083-90.401 -0.921 1.0061.68 C

ATOM 3 CB ASP B 454 17.359-90.082 0.386 1.0061.75 C

ATOM 4 CG ASP B 454 16.590-88.786 0.325 1.0062.05 C

ATOM 5 ODl ASP B 454 16.033-88.378 1.367 1.0062.30 O

ATOM 6 OD2 ASP B 454 16.545-88.176 -0.764 1.0063.12 . O

ATOM 7 C ASP B 454 19.261-91.304 -0.616 1.0061.60 C

ATOM 8 O ASP B 454 20.408-90.860 -0.647 1.0061.46 O

ATOM 1 N GLU B 455 18.974-92.565 -0.302 1.0061.64 N

ATOM 2 CA GLU B 455 20.038-93.540 -0.108 1.0061.50 C

ATOM 3 CB GLU B 455 19.472-94.962 -0.044 1.0061.52 C

ATOM 4 CG GLU B 455 20.300-95.931 0.792 1.0061.62 C

ATOM 5 CD GLU B 455 19.026-96.015 1.970 0.0050.00 C

ATOM 6 OEl GLU B 455 19.504 -96.674 2.912 0.0050.00 O

ATOM 7 OE2GLUB455 18.049-95.268 2.084 0.0050.00 O

ATOM 8 C GLU B 455 21.043-93.399 -1.253 1.0061.47 C

ATOM 9 O GLU B 455 22.270-93.244 -1.009 1.0061.39 O

ATOM 1 N ILE B₁456 20.534-93.395 -2.504 1.0061.57 N

ATOM 2 CA ILE B 456 21.505-93.246 -3.620 1.0061.40 C

ATOM 3 CB ILE B 456 20.873 -93.420 -5.034 1.0061.41 C

ATOM 4 CGl ILE B 456 20.581-94.894 -5.336 1.0061.57 C

ATOM 5 CDl ILEB 456 19.280-95.411 -4.766 1.0061.87 C

ATOM 6 CG2ILEB456 21.819-92.913 -6.108 1.0060.97 C

ATOM 7 C ILE B 456 22.232 -91.892 --3.557 1.0061.33 C

ATOM 8 O ILE B 456 23.473-91.817 -3.487 1.0061.32 O

ATOM 1 N PHE B 457 21.439-90.826 -3.568 1.0061.28 N

ATOM 2 CA PHE B 457 21.951 -89.462 -3.579 1.0061.18 C

ATOM 3 CB PHE B 457 20.825-88.478 -3.264 1.0061.10 C

ATOM 4 CG PHE B 457 21.288-87.059 -3.078 1.0061.06 C

ATOM 5 CDl PHE B 457 21.514-86.240 -4.173 1.0060.72 . C

ATOM 6 CEl PHE B 457 21.925-84.930 -4.005 1.0060.37 C

ATOM 7 CZ PHE B 457 22.109-84.424 -2.737 1.0060.51 C

ATOM 8 CE2PHEB457 21.884-85.228 -1.635 1.0060.56 C

ATOM 9 CD2PHEB457 21.476-86.536 -1.806 1.0060.85 C ■

ATOM 10 C PHE B 457 23.083-89.275 -2.588 1.0061.08 C ATOM 11 O PHE B 457 24.142-88.746 -2.928 1.0061.04 O

ATOM 1 N TYRB 458 22.852-89.710 -1.357 1.0061.12 . N

ATOM 2 CA TYRB 458 23.845-89.535 -0.313 1.0060.96 C

ATOM 3 CB TYR B 458 23.207-89.605 1.071 1.0060.87 C

ATOM 4 CG TYRB 458 22.380 -88.380 1.374 1.0060.78 C

ATOM 5 CDl TYRB 458 22.977 -87.135 1.493 1.0060.62 C

ATOM 6 CEl TYRB 458 22.233 -86.009 1.761 1.0060.72 C

ATOM 7 CZ TYRB 458 20.870-86.115 1.910 1.0060.91 C

ATOM 8 OH TYR B 458 20.124-84.987 2.178 1.0061.14 O

ATOM 9 CE2TYRB458 20.250 -87.340 1.793 1.0060.97 C

ATOM 10 CD2 TYRB 458 21.005 -88.463 1.521 1.0060.82 C

ATOM 11 C TYR B 458 24.997-90.509 -0.460 1.0060.98 C

ATOM 12 O TYR B 458 26.113-90.212 -0.039 1.0060.99 O

ATOM 1 N ASN B 459 24.746-91.663 -1.076 1.0061.12 N

ATOM 2 CA ASN B 459 25.874-92.529 -1.426 1.0061.04 C

ATOM ^■ 3 CB ASN B 459 25.435-93.967 -1.690 1.0061.02 C

ATOM 4 CG ASN B 459 25.682-94.868 -0.501 1.0061.15 C

ATOM 5 ODl ASN B 459 24.853-95.713 -0.163 1.0061.72 O

ATOM 6 ND2ASNB459 26.826-94.682 0.152 1.0061.27 N

ATOM 7 C ASN B 459 26.725-91.986 -2.573 1.0061.02 C

ATOM 8 O ASN B 459 27.807-92.503 -2.846 1.0060.90 O

ATOM 1 N LEU B 460 26.238 -90.936 -3.234 1.0061.16 N

ATOM 2 CA LEU B 460 27.036-90.256 -4.269 1.0061.21 C

ATOM 3 CB LEU B 460 26.144-89.735 -5.399 1.0061.18 P

ATOM 4 CG LEU B 460 25.941-90.651 -6.607 1.0061.31 C

ATOM 5 CDl LEU B 460 25.626-92.081 -6.188 1.0061.70 C

ATOM 6 CD2LEUB460 24.853-90.103 -7.519 1.0061.36 C

ATOM 7 C LEU B 460 27.927-89.118 -3.751 1.0061.21 C

ATOM 8 O LEU B 460 28.542-88.401 -4.542 1.00_.61.15 O

ATOM 1 N ALA B 461 27.990-88.958 -2.431 1.0061.30 N

ATOM 2 CA ALA B 461 28.832-87.933 -1.791 1.0061.39 C

ATOM 3 CB ALAB 461 30.310-88.328 -1.848 1.0061.32 C

ATOM 4 C ALAB 461 28.632-86.526 -2.356 1.0061.46 C

ATOM 5 O ALAB 461 29.489-86.016 -3.080 1.0061.46 P

ATOM 1 N PRO B 462 27.498-85.891 -2.015 1.0061.52 N

ATOM 2 CA PRO B 462 27.192-84.538 -2.456 1.0061.50 C

ATOM 3 CB PRO B 462 25.672-84.439 -2.278 1.0061.48 C

ATOM 4 CG PRO B 462 25.224-85.764 -1.701 1.0061.39 C

ATOM 5 CD PRO B 462 26.429-86:437 -1.167 1.0061.48 C

ATOM 6 C PRO B 462 27.888 -83.514 -1.573 1.0061.55 C

ATOM 7 O PRO B 462 28.433-83.873 -0.532 1.0061.39 O

ATOM 1 N ALA B 463 27.859-82.252 -1.992 1.0061.78 N

ATOM 2 CA ALAB 463 28.567-81.176 -1.301 1.0061.99 C

ATOM 3 CB ALA B 463 28.388-79.860 -2.043 1.0062.09 C

ATOM 4 C ALA B 463 28.111-81.031 0.140 1.0062.16 C^*

ATOM 5 O ALA B 463 28.733 -81.565 .1.055 1.0062.42 O

ATOM 1 N ASP B 464 27.028 -80.293 0.343 1.0062.26 N

ATOM 2 CA ASP B 464 26.459 -80.154 1.673 1.0062.40 C

ATOM 3 CB ASP B 464 26.755 -78.767 2.250 1.0062.60 C

ATOM 4 CG ASP B 464 26.038 -77.651 1.502 1.0063.34 C

ATOM 5 ODl ASP B 464 26.134-76.485 1.952 1.0063.76 O

ATOM 6 OD2 ASP B 464 25.380-77.936 0.471 1.0064.06 O

ATOM 7 C ASP B 464 24.964-80.382 1.585 1.0062.23 C

ATOM 8 O ASP B 464 24.207-79.934 2.434 1.0062.39 O

ATOM i N GLY B 465 24.549-81.083 0.541 1.0062.02 N

ATOM. 2 CA GLY B 465 23.140-81.324 0.294 1.0061.82 C

ATOM 3 C GLY B 465 22.898-81.127 -1.183 1.0061.70 C

ATOM 4 O GLY B 465 21.784-81.310 -1.678 1.0061.73 O ATOM 1 N LYS B 466 23.960-80.752 -1.887 1.0061.43 N

ATOM 2 CA LYS B 466 23.879-80.507 -3.311 1.0061.22 C

ATOM 3 CB LYS B 466 24.071 -79.023 -3.604 1.0061.21 C

ATOM 4 CG LYS B 466 22.937-78.154 -3.108 1.PO 61.05 C,

ATOM 5 CD LYS B 466 23.345-76.698 -3.052 1.0061.32 C

ATOM 6 CE LYS B 466 22.293-75.881 -2.334 1.0061.80 C

ATOM 7 NZ LYS B 466 21.944-76.494 -1.019 1.0062.20 N

ATOM 8 c : LYS B 466 24.917-81.323 -4.053 1.0061.12 C

ATOM 9 O LYS B 466 26.113-81.218 -3.792 1.0061.13 O

ATOM 1 N LEU B 467 24.448-82.144 -4.980 1.0061.00 N

ATOM 2 CA LEU B 467 25.341-82.926 -5.809 1.0060.88 C

ATOM 3 CB LEU B 467 24.618-84.164 -6.341 1.0060.79 C

ATOM 4 CG LEU B 467 25.461-85.111 .7.190 1.0060.87 C

ATOM 5 CDl LEU B 467 26.613-85.658 -6.365 1.0061.30 C

ATOM 6 CD2LEUB467 24.614-86.240 -7.743 1.0060.91 C

ATOM 7 C LEU B 467 25.839-82.065 -6.966 1.0060.83 C

ATOM 8 O LEU B 467 25.044-81.491 -7.712 1.0060.86 O

ATOM 1 N SER B 468 27.158-81.966 -7.099 1.0060.71 N

ATOM 2 CA SER B 468 27.777-81.277 -8.227 1.0060.55 C

ATOM 3 CB SER B 468 29.287-81.522 -8.211 1.0060.68 C

ATOM 4 OG SER B 468 29.806-81.658 -9.524 1.0061.03 O

ATOM 5 C SER B 468 27.182-81.727 -9.564 1.0060.34 C

ATOM 6 O SER B 468 26.679-82.846 -9.682 1.0060.29 O

ATOM 1 N GLY B 469 27.246-80.852-10.565 1.0060.13 N

ATOM 2 CA GLY B 469 26.713-81.153-11.894 1.0059.92 C

ATOM 3 C GLY B 469 27.448-82.273-12.611 1.0059.86 . C

ATOM 4 O GLY B 469 26.835-83.108-13.278 1.0059.75 O

ATOM 1 N SER B 470 28.767-82.298-12.471 1.0059.92 N

ATOM 2 CA SER B 470 29.580-83.316-13.128 1.0060.13 C

ATOM 3 CB SER B 470 31.070-82.996-12.972 1.0060.18 C

ATOM 4 OG SER B 470 31.409-82.804-11.610 1.0060.39, O

ATOM 5 C SER B 470 29.271-84.730-12.621 1.0060.16 C

ATOM 6 O SER B 470 29.128-85.667-13.415 1.0060.19 O

ATOM 1 N LYS B 471^' 29.165-84.875-11.301 1.0060.16 ' N

ATOM 2 CA LYS B 471 28.853-86.160-10.680 1.0060.23 C

ATOM 3 CB LYS B 471 28.918-86.032 -9.157 1.0060.32 C

ATOM 4 CG LYS B 471 29.715-84.826 -8.674 1.0060.75 C

ATOM 5 CD LYS B 471 31.190-85.140 -8.471 1.0061.90 C

ATOM 6 CE LYS B 471 31.583-85.072 -6.994 1.0062.37 C

ATOM 7 NZ LYS B 471 30.749-85.959 -6.130 1.0062.88 N

ATOM 8 C LYS B 471 27.452-86.600-11.106 1.0060.16 C

ATOM 9 O LYS B 471 27.223-87.758-11,515 1.0060.14 O

ATOM 1 N ALA B 472 26.521-85.654-11.014 1.0060.13 N

ATOM 2 CA ALA B 472 25.155-85.868-11.458 1.0060.03 C

ATOM 3 CB ALA B 472 24.353-84.582-11.354 1.0059.90 C

ATOM 4 C ALA B 472 25.170-86.382-12.890 1.0059.97 C

ATOM 5 O ALA B 472 24.488-87.358-13.218 1.0060.05 O

ATOM 1 N LYS B 473 25.966-85.741-13.739 1.0059.85 N

ATOM 2 CA . LYS B 473 26.063-86.203-15.112 1.0059.96 C

ATOM 3 CB LYS B 473 26.893-85.269-15.988 1.0059.91 C

ATOM 4 CG LYS B 473 26.875-85.683-17.455 1.0059.67 C

ATOM 5 CD LYS B 473 27.769-84.800-18.309 1.0059.75 C

ATOM 6 .CE LYS B 473 27.437-84.943-19.788 1.0059.64 C

ATOM 7 NZ LYS B 473 28.334-84.122-20.649 1.0059.71 N

ATOM 8 C LYS B 473 26.611 -87.620 -15.183 1.0060.14 C

ATOM 9 O LYS B 473 25.941-88.495-15.719 1.0060.26 O

ATOM 1 N THR B 474 27.806-87.866-14.640 1.0060.16 N

ATOM 2 CA . THR B 474 28.372-89.219-14.739 1.0060.24 C ATOM 3 CB THR B 474 29.757-89.402-14.031 1.0060.23 C

ATOM 4 OGl THR B 474 29.800-88.662-12.808 1.0060.62 O

ATOM 5 CG2THRB474 30.894-88.933-14.931 1.0060.37 C

ATOM 6 C THR B 474 27.364-90.289-14.301 1.0060.23 C

ATOM 7 O THR B 474 27.219-91.319-14.966 1.0060.25 O

ATOM 1 N TRP B 475 26.645-90.037-13.211 1.0060.28 N

ATOM 2 CA TRP B 475 25.606-90.978-12.787 1.0060.42 C

ATOM 3 CB TRP B 475 25.023-90.535-11.445 1.0060.84 C

ATOM 4 CG TRP B 475 23.813-91.301-11.013 1.0061.18 C

ATOM 5 CDl TRP B 475 23.775-92.585-10.565 1.0061.70 C

ATOM 6 NEl TRP B 475 22.485-92.942-10.256 1.0061.88 N

ATOM 7 CE2 TRP B 475 21.660-91.878-10.500 1.0061.50 C

ATOM 8 CD2 TRP B 475 22.463-90.823-10.976 1.0061.57 C

ATOM 9 CE3 TRP B 475 21.854-89.606-11.306 1.0062.24 C

ATOM 10 CZ3 TRP B 475 20.477-89.484-11.149 1.0062.05 C

ATOM 11 CH2 TRP B 475 19.707-90.555-10.671 1.0061.82 C

ATOM 12 CZ2 TRP B 475 20.280-91.756-10.343 1.0061.71 C

ATOM 13 C TRP B 475 24.498-91.098-13.840 1.0060.37 C

ATOM 14 O TRP B 475 24.152-92.206-14.315 1.0060.28 O

ATOM 1 N MET B 476 23.944-89.948-14.209 1.0060.24 N

ATOM 2 CA MET B 476 22.858-89.927-15.166 1.0060.43 C

ATOM 3 CB MET B 476 22.436-88.492-15.483 1.0060.35 C

ATOM 4 CG MET B 476 21.636-87.837-14.364 1.0060.65 C

ATOM 5 SD MET B 476 21.109-86.145-14.729 1.0060.97 S

ATOM 6 CE MET B 476 19.647-86.452-15.725 1.0061.19 C

ATOM 7 C MET B 476 23.239-90.692-16.431 1.0060.37 C

ATOM 8 O MET B 476 22.549-91.632-16.828 1.0060.37 O

ATOM 1 N VAL B 477 24.347-90.304-17.053 1.0060.31 N

ATOM 2 CA VAL B 477 24.808-90.980-18.253 1.0060.18 C

ATOM 3 CB VAL B 477 26.072-90.317-18.844 1.0060.16 C

ATOM 4 CGl VALB 477 27.334-91.039-18.386 1.0060.18 C

ATOM 5 CG2VALB477 25.991-90.304-20.364 1.0060.61 C

ATOM 6 C VAL B 477 25.053-92.442-17.904 1.0060.04 C

ATOM 7 O VAL B 477 24.963-93.322-18.759 1.0059.92 O

ATOM 1 N GLY B 478 25.336-92.689-16.628 1.0060.05 N

ATOM 2 CA GLY B 478 25.437-94.048-16.110 1.0059.87 . C

ATOM 3 C GLY B 478 24.152-94.826-16.310 1.0059.75 C

ATOM 4 O GLY B 478 24.183-96.039-16.508 1.0059.64 O

ATOM 1 N THR B 479 23.012-94.139-16.265 1.0059.79 N

ATOM , 2 CA THR B 479 21.730-94.827-16.546 1.0059.54 C

ATOM 3 CB THR B 479 20.512-93.965-16.201 1.0059.50 C

ATOM 4 OGl THR B 479 . 20.208-93.109-17.311 1.0059.40 O

ATOM 5 CG2THRB479 20.774-93.142-14.953 1.0059.72 C

ATOM 6 C THR B 479 21.544-95.280-18.002 1.0059.41 C

ATOM 7 O THR B 479 20.429-95.606-18.416 1.0059.36 O

ATOM 1 N LYS B 480 22.626-95.279-18.772 1.0059.24 N

ATOM 2 CA LYS B 480 22.602-95.706-20.175 1.0059.00 C

ATOM 3 CB LYS B 480 22.607-97.236-20.281 1:0058.90 C

ATOM 4 CG LYS B 480 24.220-97.582-20.411 0.0050.00 C

ATOM 5 CD LYS B 480 24.384-99.002-19.919 0.0050.00 C

ATOM 6 CE LYS B 480 23.123-99.825-20.052 0.0050.00 C

ATOM 7 NZ LYS B 480 22.663-100.001-21.452 0.0050.00 N

ATOM 8 C LYS B 480 21.452-95.120-21.000 1.0058.86 C

ATOM 9 O LYS B 480 20.932-95.778-21.898 1.0059.02 O

ATOM 1 N LEUB 481 21.062-93.884-20.699 1.0058.63 N

ATOM 2 CA LEUB 481 20.089-93.169-21.522 1.0058.40 C

ATOM 3 CB LEUB 481 19.144-92.336-20.650 1.0058.41 C

ATOM 4 CG LEUB 481 17.948-93.045-20.013 1.0058.17 C ATOM 5 CDl LEU B 481 17.016-92.033-19.380 1.0057.72 C

ATOM 6 CD2LEUB481 17.200-93.871-21.043 1.0057.96 C

ATOM 7 C LEU B 481 20.803-92.264-22.524 1.0058.27 C

ATOM 8 O LEUB 481 21.929-91.835-22.276 1.0058.35 O

ATOM 1 N PRO B 482 20.156-91.980-23.667 1.0058.15 N

ATOM 2 CA PRO B 482 20.739-91.080-24.662 1.0058.10 C

ATOM 3 CB PRO B 482 19.732-91.119-25.815 1.0058.03 C

ATOM 4 CG PRO B 482 18.465-91.591-25.212 1.0058.03 C

ATOM 5 CD PRO B 482 18.849-92.507-24.096 1.0058.12 C

ATOM 6 C PRO B 482 20.889-89.658-24.134 1.0058.13 C

ATOM 7 O PRO B 482 20.023-89.170-23.407 1.0058.05 O

ATOM 1 N ASN B 483 21.990-89.010-24.508 1.0058.25 N

ATOM 2 CA ASN B 483 22.326-87.673-24.018 1.0058.27 C

ATOM 3 CB ASN B 483 23.466-87.069-24.846 1.0058.41 C

ATOM 4 CG ASN B 483 24.180-85.936-24.122 1.0058.98 C

ATOM 5 ODl ASN B 483 24.148-84.782-24.560 1.0058.96 O

ATOM 6 ND2ASNB483 24.828-86.264-23.005 1.0059.69 N

ATOM 7 C ASN B 483 21.130-86.730-24.011 1.0057.99 . C

ATOM 8 O ASN B 483 20.749-86.219-22.971 1.0057.84 O

ATOM 1 N SER B 484 20.548-86.515-25.185 1.0057.91 N ,

ATOM 2 CA SER B 484 19.395-85.634-25.365 1.0057.86 C

ATOM 3 CB SER B 484 18.779-85.891-26.746 1.0057.83 C

ATOM 4 OG SER B 484 17.367-85.789-26.726 1.0058.63 O

ATOM 5 C SER B 484 18.351-85.771-24.249 1.0057.69 C

ATOM 6, O SER B 484 .18.038-84.801-23.542 1.0057.89 O

ATOM 1 N VAL B 485 17.823-86.978-24.085 1.0057.50 N

ATOM 2 CA VAL B 485 16.868-87.246-23.025 1.0057.27 C

ATOM 3 CB VAL B 485 16.534-88.746-22.933 1.0057.16 C

ATOM 4 CGl VAL B 485 15.787-89.050-21.650 1.0056.97 C

ATOM 5 CG2VALB485 15.713 -89.173 -24.133 1.0056.96 C

ATOM 6 C VAL B 485 17.425-86.756-21.697 1.0057.35 C

ATOM 7 O VAL B 485 16.803-85.944-21.017 1.0057.43 .0

ATOM 1 N LEUB 486 18.613-87.233-21.341 1.0057.54 N

ATOM 2 CA LEU B 486 19,239-86.843-20.080 1.0057.77 C

ATOM 3 CB LEU B 486 20.638-87.454-19.946 1.0057.88 C

ATOM 4 CG LEUB 486 20.729-88.972-19.774 1.0058.42 C

ATOM 5 CDl LEU B 486 22.172-89.447-19.904 1.0058.66 C

ATOM 6 CD2LEUB486 20.138-89.407-18.439 1.0058.90 C

ATOM 7 C LEU B 486 19.303-85.325-19.908 1.0057.80 C

ATOM 8 O LEU B 486 18.955-84.808-18.850 1.0057.86 O

ATOM 1 N GLY B 487 19.749-84.618-20.945 1.0057.71 N

ATOM 2 CA GLY B 487 19.857-83.163-20.904 1.0057.64 C

ATOM 3 C GLY B 487 18.516-82.531-20.601 1.0057.70 C

ATOM 4 O GLY B 487 18.406-81.638-19.741 1.0057.71 O

ATOM 1 N ARG B 488 17.488-83.010-21.298 1.0057/78 N

ATOM 2 CA ARG B 488 16.128-82.544-21.042 1.0057^97 C

ATOM 3 CB ARG B 488 15.152-83.209-22.013 1.0058.06 C

ATOM 4 CG ARG B 488 13.971-82.338-22.415 1.0059.39 C

ATOM 5 CD ARG B 488 13.610-82.573-23.881 1.0061.62 C

ATOM 6 NE ARG B 488 13.092-83.923-24.122 1.0063.12 N

ATOM 7 CZ ARG B 488 13.449-84.695-25.150 1.0063.38 C

ATOM 8 NHl ARG B 488 12.920-85.907-25.285 1.0063.40 N

ATOM 9 NH2ARGB488 14.347 -84.266 -26.033 1.0063.17 ^' N

ATOM 1C I C ARGB 488 15.727-82.814-19.583 1.0057.81 C

ATOM 11 O ARGB 488 15.145-81.947-18.904 1.0057.77 O

ATOM 1 N ILE B 489 16.064-84.008-19.099 1.0057.58 N

ATOM 2 CA ILE B 489 15.757-84.377-17.724 1.0057.48 C

ATOM • 3 CB ILE B 489 16.163-85.815-17.413 1.005733 C ATOM 4 CGl ILE B 489 15.256-86.784-18.167 1.0057.24 C

ATOM 5 CDl ILE B 489 15.547-88.239-17.903 1.0057.50 C

ATOM 6 CG2 ILE B 489 16.068-86.066-15.925 1.0057.45 C

ATOM 7 C ILE B 489 16.453-83:441-16.755 1.0057.56 C

ATOM 8 O ILE B 489 15.844-82.935-15.813 1.0057.63 O

ATOM 1 N TRP B 490 17.736-83.206-16.988 1.0057.67 N

ATOM 2 CA TRP B 490 18.470-82.265-16.172 1.0057.64 C

ATOM 3 CB TRP B 490 19.867-82.008-16.731 1.0057.40 C

ATOM 4 CG TRP B 490 20.498-80.874-16.021 1.0057.22 C

ATOM 5 CDl TRP B 490 20.466-79.563-16.383 1.0056.97 C

ATOM 6 NEl TRP B 490 21.128-78.800-15.453 1.0057.04 N

ATOM 7. CE2 TRP B 490 21.592-79.619-14.458 1.0057.10 C

ATOM 8 CD2 TRP B 490 21.204-80.933-14.780 1.0057.28 C

ATOM 9 CE3 TRP B 490 21.556-81.974-13.913 1.0057.40 C

ATOM 10 CZ3.TRPB490 22.280.-81.672-12.774 1.0057.15 C

ATOM 11 CH2 TRP B 490 22.654-80.354-12.483 1.0057.10 C

ATOM 12 CZ2 TRP B 490 22.320-79.316-13.310 1.0057.08 C

ATOM 13 C TRP B 490 17.708-80.950-16.129 1.0057.62 C

ATOM 14 O TRP B 490 17.365-80.442-15.050 1.0057.65 O

ATOM 1 N LYS B 491 17.442-80.409-17.315 1.0057.68 N

ATOM 2 CA LYS B 491 16.802-79.103-17.398^' 1.0057.74 C

ATOM 3 CB LYS B 491 16.559-78.684-18.847 1.0057.75 C

ATOM 4 CG LYS B 491 15.983-77.286-18.974 1.0058.40 C

ATOM 5 CD LYS B 491 16.464-76.592-20.236 1.0060.09 C

ATOM 6 CE LYS B 491 17.902-76.107-20.079 1.0061.13 C

ATOM 7 NZ LYS B 491 17.986-75.022-19.050 1.0062.38 N

ATOM 8 C LYS B 491 15.509-79.077-16.602 1.0057.58 C

ATOM 9 O LYS B 491 15.215-78.090-15.925 1.0057.50 O

ATOM 1 N LEU B 492 14.746-80.166-16.680 1.0057.51 N

ATOM 2 CA LEU B 492 13.518-80.287-15.895 1.0057.34 C

ATOM 3 CB LEU B 492 12.727-81.513-16.345 1.0057.12 C

ATOM 4 CG LEU B 492 11.442-81.329-17.148 1.00.56.50 C

ATOM 5 CDl LEUB 492 11.487-80.090-18.020 1.0056.61 C

ATOM 6 CD2LEUB492 11.183 -82.581 -17.975 1.0056.14 C

ATOM 7 C LEU B 492 13.778-80.363-14.383 1.0057.59 C '

ATOM 8 O LEU B 492 13.029-79.801-13.582 1.0057.53 O

ATOM 1 N SER B 493 14.847-81.051-13.998 1.0057.77 N

ATOM 2 CA SER B 493 15.079-81.357-12.595 1.0058.08 C

ATOM 3 CB SER B 493 15.893-82.641 -12.456 1.0058.12 C

ATOM 4 OG SER B 493 15.156-83.746-12.947 1.0058.62 O

ATOM 5 C SER B 493 15.738-80.231-11.812 1.0058.20 C

ATOM 6 O SER B 493 15.432-80.036-10.634 1.0058.25 O

ATOM 1 N ASP B 494 16.650-79.499-12.443 1.0058.27 N

ATOM 2 CA ASP B 494 17.297-78.397-11.735 1.0058.62 C

ATOM 3 CB ASP B 494 18.562-77.935-12.449 1.0058.56 C

ATOM 4 CG ASP B 494 19.324-76.894-11.657 1.0058.70 C

ATOM 5 ODl ASP B 494 18.970 -76.661 -10.478 1.0058.46 O

ATOM 6 OD2 ASP B 494 20.277-76.308-12.215 1.0059.37 O

ATOM 7 C ASP B 494 16.321-77.238-11.581 1.0058.87 C

ATOM 8 O ASP B 494 16.383-76.250-12.315 1.0058.88 O

ATOM 1 N VAL B 495 15.422-77.368-10.614 1.0059.15 N

ATOM 2 CA VAL B 495 14.318-76.438-10.477 1.0059.38 C

ATOM 3 CB VAL B 495 13.281-76.921 -9.444 1.0059.37 C

ATOM 4 CGl VAL B 495 12.186-75.883 -9.265 1.0059.25 C

ATOM 5 CG2VALB495 12.681 -78.234 -9.894 1.0059.21 C

ATOM 6 C VAL B 495 14.779-75.025-10.155 1.0059.65 C

ATOM 7 O VAL B 495 14.327-74.077-10.794 1.0060.04 O

ATOM 1 N ASP B 496 15.671-74.869 -9.180 1.0059.85 N ATOM 2 CA ASP B 496 16.168-73.525 -8.852 1.0060.04 C

ATOM 3 CB ASP B 496 16.633-73.422 -7.395 1.0060.09 C

ATOM 4 CG ASP B 496 17.676-74.455 -7.036 1.0060.31 C

ATOM 5 ODl ASP B 496 17.844-75.432 -7.801 1.0060.71 O

ATOM 6 OD2 ASP B 496 18.325-74.289 -5.979 1.0060.45 O

ATOM 7 C ASP B 496 17.271-73.111 -9.817 1.0060.06 C

ATOM 8 O ASP B 496 17.873-72.046 -9.673 1.0059.85 O

ATOM 1 N ARG B 497 17.499-73.980-10.802 1.0060.35 N

ATOM 2 CA ARG B 497 18.462-73.785-11.891 1.0060.65 C

ATOM 3 CB ARG B 497 17.785-73.166-13.129 1.0060.76 C

ATOM 4 CG ARG B 497 17.801-71.656-13.234 1.0062.10 C

ATOM 5 CD ARG B 497 16.567-71.162-13.975 1.0064.37 C

ATOM 6 NE ARG B 497 15.450-70.975-13.051 1.0066.05 N

ATOM 7 CZ ARG B 497 15.155-69.817-12.463 1.0067.08 C

ATOM 8 NHl ARG B 497 14.125-69.738-11.628 1.0067.52 N

ATOM 9 NH2 ARG B 497 15.885-68.733-12.713 1.0067.06 N

ATOM 10 C ARG B 497 19.771-73.097-11.481 1.0060.58 C

ATOM 11 O ARG B 497 20.138-72.036-11.994 1.0060.38 O

ATOM 1 N ASP B 498 20.476-73.740-10.552 1.0060.75 N

ATOM 2 CA ASP B 498 21.748-73.227-10.062 1.0060.92 C

ATOM 3 CB ASP B 498 21.779-73.207 -8.525 1.0060.94 C

ATOM 4 CG ASP B 498 21.636-74.597 -7.922 1.0060.96 C

ATOM 5 ODl ASP B 498 21.077-75.493 -8.593 1.0061.07 O

ATOM 6 OD2 ASP B 498 22.078-74.792 -6.768 1.0060.82 O

ATOM 7 C ASP B 498 22.935-74.025-10.610 1.0061.06 C

ATOM 8 O ASP B 498 24.084-73.496-10.694 1.0061.39 O

ATOM 1 N GLY B 499 22.672-75.293-10.981 1.0061.04 N

ATOM 2 CA GLY B 499 23.746-76.100-11.553 1.0061.21 C

ATOM 3 C GLY B 499 24.043-77.366-10.775 1.0061.37 C

ATOM 4 O GLY B 499 24.801-78.229-11.235 1.0061.52 O

ATOM 1 N MET B 500 23.448 -77.476 -9.592 1.0061.28 N

ATOM 2 CA MET B 500 23.592-78.669 -8.778 1.0061.23 C

ATOM 3 CB MET B 500 24.169-78.304 -7.416 1.0061.21 C

ATOM 4 CG MET B 500 25.572-77.741 -7.473 1.0061.10 C

ATOM 5 SD MET B 500 26.097-77.079 -5.879 1.0061.13 S

ATOM 6 CE MET B 500 27.861-76.890 -6.152 1.0061.68 C

ATOM 7 C MET B 500 22.237-79.338 -8.606 1.0061.33 C

ATOM 8 O MET B 500 21.221 -78.816 -9.063 1.0061.29 O

ATOM .1 N LEUB 501 22.227-80.500 -7.956 1.0061.45 N

ATOM 2 CA LEUB 501 20.977-81.158 -7.585 1.0061.49 C

ATOM 3 CB^" LEUB 501 20.759-82.432 -8.408 1.0061.41 C

ATOM 4 CG LEUB 501 20.599-82.291 -9.924 1.0061.24 C

ATOM 5 CDl LEUB 501 20.682-83.646-10.611 1.0060.96 C

ATOM 6 CD2 LEUB 501 19.292-81.603-10.266 1.0061.45 C

ATOM 7 C LEUB 501 20.980-81.494 -6.095 1.0061.59 C

ATOM 8 O LEUB 501 21.852-82.220 -5.619 1.0061.52 O

ATOM 1 N ASP B 502 20.015 -80.952 -5.358^' 1.0061.72 N

ATOM 2 CA ASP B 502 19.853-81.329 -3.964 1.0061.94 C ^>

ATOM 3 CB ASP B 502 19.236-80.192 -3:144 1.0062.06 C

ATOM 4 CG ASP B 502 17.815-79.857 -3.568 1.0062.72 C

ATOM 5 ODl ASP B 502 17.039-80.784 -3.890 1.0063.46 O

ATOM 6 OD2 ASP B 502 17.466-78.655 -3.557 1.0063.58 O

ATOM 7 C ASP B 502 19.005-82.590 -3.902 1.0061.99 C

ATOM 8 O ASP B 502 18.595-83.111 -4.937 1.0062.07 O

ATOM 1 N ASP B 503 18.742-83.079 -2.695 1.0062.08 N

ATOM 2- CA ASPB 503 18.016 -84.337 -2.521 1.0062.21 C

ATOM 3 CB ASP B 503 17.778-84.611 -1.039 1.0062.34 C

ATOM 4 CG ASP B 503 17.014-83.495 -0.358 1.0062.98 C ATOM 5 ODl ASP B 503 17.226-82.315 -0.71S 1.0063.16 O

ATOM 6 OD2 ASP B 503 16.203-83.803 0.542 1.0064.06 O

ATOM 7 C ASP B 503 16.693-84.407 -3.290 1.0062.12 C

ATOM 8 O ASP B 503 16.455-85.360 -4.040 1.0062.04 O

ATOM 1 N GLU B 504 15.837-83.405 -3.104 1.0062.02 N

ATOM 2 CA GLUB 504 14.531-83.400 -3.757 1.0062.12 C

ATOM 3 CB GLU B 504 13.687-82.201 -3.309 1.0062.02 C

ATOM 4 CG GLUB 504 13.660-81.992 -1.794 1.0062.68 C

ATOM 5 CD GLUB 504 12.496-81.120 -1.327 1.0062.81 C

ATOM 6 OEl GLU B 504 12.703-79.905 -1.092 1.0063.40 O

ATOM T OE2GLUB504 11.370-81.652 -1.189 1.0063.95 O

ATOM 8 C GLUB 504 14.707-83.410 -5.269 1.0061.85 C

ATOM 9 O GLU B 504 14.214-84.308 -5.956 1.0061.84 O

ATOM 1 N GLUB 505 15.431 -82.420 -5.781 1.0061.64 N

ATOM 2 CA GLU B 505 15.704-82.340 -7.206 1.0061.43 C

ATOM 3 CB GLU B 505 ^'16.701 -81.228 -7.493 1.0061.18 C

ATOM 4 CG GLU B 505 16.088-79.851 -7.502 1.0060.83 C

ATOM 5 CD GLU B 505 17.131-78.753 -7.597 1.0060.55 C ^'

ATOM 6 OEl GLU B 505 18.127-78.807 -6.840 1.0060.25 O

ATOM 7 OE2GLUB505 16.957 τ77.832 -8.427 1.0060.26 O

ATOM 8 C GLU B 505 16.235-83.667 -7.734 1.0061.67 C

ATOM 9 O GLUB 505 15.857-84.106 -8.827 1.0061.83 O

ATOM 1 N PHE B 506 17.104-84.309 -6.956 1.0061.68 N

ATOM 2 CA PHE B 506 17.680-85.586 -7.362 1.0061.63 C

ATOM 3 CB. PHE B 506 18.794-86.020 -6.409 1.0061.56 C

ATOM 4 CG PHE B 506 19.485-87.290 -6.827 1.0061.67 C

ATOM 5 CDl PHE B 506 18.970-88.528 -6.469 1.0061.62 C

ATOM 6 CEl PHE B 506 19.598-89.695 -6.859 1.0061.32 C

ATOM 7 CZ PHE B 506 20.757-89.633 -7.610 1.0061.44 C

ATOM 8 CE2 PHE B 506 21.281 -88.409 -7.971 1.0061.14 C

ATOM 9 CD2PHEB506 20.647-87.247 -7.584 1.0061.51 C

ATOM 10 C PHE B 506 16.602-86.658 -7.440 1.0061.66 C

ATOM 11 O PHE B 506 16.548-87.430 -8.401 1.0061.70 O

ATOM 1 N ALAB 507 15.745-86.705 -6.425 1.0061.76 N

ATOM 2 CA ALA B 507 14.624-87.636 -6.436 1.0061.66 C

ATOM 3 CB ALA B 507 13.794-87.488 -5.177 1.0061.65 C

ATOM 4 C ALAB 507 13.768-87.405 -7.679 1.0061.68 C

ATOM 5 O ALAB 507 13.344-88.361 -8.332 1.0061.70 O

ATOM 1 N LEU B 508 13.531-86.133 -8.005 1.0061.60 N

ATOM 2 CA LEUB 508 12.805-85.767 -9.222 1.0061.54 C

ATOM 3 CB LEU B 508 12.722-84.247 -9.353 1.0061.44 C

ATOM 4 CG LEU B 508 11.482-83.623 -9.997 1.0061.08 C

ATOM 5 CDl LEU B 508 11.788-82.195-10.402 1.0060.85 C

ATOM 6 CD2LEUB508 10.995-84.417-11.192 1.0060.65 C

ATOM 7 C LEU B 508 13.509.-86.346-10.450 1.0061.70 C

ATOM 8 O LEUB 508 12.905-87.063-11.262 1.0061.61 O

ATOM 1 N ALAB 509 14.792-86.026-10.582 1.0061.77 N

ATOM 2 CA ALAB 509 15.593-86.572-11.662 1.0061.78 C

ATOM 3 CB ALA B 509 17.060-86.243-11.449 1.0061.77 C

ATOM 4 C ALA B 509 15.378-88.082-11.768 1.0061.87 C

ATOM 5 O ALAB 509 14.950-88.585-12.810 1.0061.97 O

ATOM 1 N SERB 510 15.654-88.798-10.681 1.0061.83 N

ATOM 2 CA SERB 510 . 15.496-90.251-10.657 1.0061.95 C

ATOM 3 CB SERB 510 15.749-90.793 -9.249 1.0062.00 C

ATOM 4 OG SERB 510 16.993-90.333 -8.748 1.0062.65 O

ATOM 5 C SERB 510 14.110-90.673 -11.135 1.0061.79 C

ATOM 6 O SERB 510 13.978-91.562-11.987 1.0061.78 O

ATOM 1 N HIS B 511 13.084-90.030-10.579 1.0061.62 N ATOM 2 CA HIS B 511 11.707-90.302-10.970 1.0061.40 C

ATOM 3 CB HISB 511 10.742-89.312-10.307 1.0061.24 C

ATOM 4 CG HIS B 511 9.317-89.470-10.744 1.0060.84 C

ATOM 5 NDl HIS B 511 8.390-90.185-10.016 1.0060.78 N

ATOM 6 CEl HIS B 511 7.225-90.155-10.639 1.0060.24 C

ATOM 7 NE2HISB511 7.363-89.449-11.747 1.0060.07 N

ATOM 8 CD2HISB511 8.662-89.009-11.836 1.0060.36 C

ATOM 9 C HIS B 511 11.594-90.212-12.479 1.0061.38 C

ATOM 10 O HIS B 511 11.092-91.124-13.132 1.0061.56 O

ATOM 1 N LEUB 512 12.083-89.109-13.031 1.0061.36 N

ATOM 2 CA LEUB 512 12.001-88.881-14.464 1.0061.37 C

ATOM . 3 CB LEUB 512 12.489-87.469-14.786 1.0061.22 C

ATOM 4 CG LEUB 512 11.466-86.435-14.310 1.0060.86 C

ATOM 5 CDl LEUB 512 12.018-85.018-14.367 1.0060.51 C

ATOM 6 CD2LEUB512 10.185-86.565-15.123 1.0059.84 C

ATOM 7 C LEUB 512 12.751 -89.938 -15.278 1.0061.48 C '

ATOM 8 O LEUB 512 12.264-90.422-16.309 1.0061.48 O

ATOM 1 N ILEB 513 13.929-90.309-14.793 1.0061.74 N

ATOM 2 CA ILEB 513 14.709-91.371-15.415 1.0061.83 C

ATOM 3 CB ILEB 513 16.079-91.518-14.728 1.0061.81 . C

ATOM 4 CGl ILEB 513 16.825-90.181-14.799 1.0061.73 C

ATOM 5 CDl ILE B 513 18.282-90.257-14.427 1.0062.12 C

ATOM 6 CG2ILEB513 16.882-92.645-15.365 1.0061.68 C

ATOM 7 C ILEB 513 13.946-92.705-15.439^' 1.0061.89 C

ATOM 8 O ILEB^'513 13.817-93.333-16.492 1.0061.85 O

ATOM 1 N GLUB 514 13.429-93.124-14.285 1.0061.92 N

ATOM 2 CA GLUB 514 12.589-94.317-14.223 1.0062.03 C

ATOM 3 CB GLUB 514 12.044-94.519-12.814 1.0062.08 C

ATOM 4 CG GLUB 514 13.104-94.778-11.765 1.0062.83 C

ATOM 5 CD GLUB 514 12.556-95.511-10.550 1.0063.54 C

ATOM 6 OEl GLUB 514 11.502-96.181-10.667 1.0063.39 O

ATOM 7 OE2 GLUB 514 13.190-95.420 -9.476 1.0064.11 O.

ATOM 8 C GLUB 514 11.423-94.201-15.194 1.0062.07 C

ATOM 9 O GLUB 514 11.155-95.108-15.989 1.0062.33 O

ATOM 1 N ALAB 515 10.725-93.072-15.116 1.0061.99 • N

ATOM 2 CA ALAB 515 9.619-92.794-16.018 1.0061.95 C

ATOM 3 CB ALAB 515 9.162-91.346-15.876 1.0061.86 C

ATOM 4 C ALAB 515 10.023-93.091-17.457 1.0061.91 C

ATOM 5 O ALA B 515 9.366-93.878-18.137 1.0061.89 O

ATOM 1 N LYS B 516 11.111-92.472-17.911 1.0061.87 . N

ATOM 2 CA LYS B 516 11.554-92.658-19.291 1.0061.79 C

ATOM 3 CB LYS B 516 12.747-91.760-19.625 1.0061.68 C

ATOM 4 CG LYS B 516 12.626 -91.054 -20.968 1.0061.28 C

ATOM 5 CD LYS B 516 12.641-92.024-22.133 1.0061.20 C

ATOM 6 CE LYS B 516 11.698-91.567-23.236 1.0061.34 C

ATOM 7 NZ LYS B 516 11.813-90.108-23.506 LOO 61.19 N

ATOM 8 C LYS B 516 11.902-94.113-19.547 1.0061.88 C

ATOM 9 O LYS B 516 11.602-94.645-20.614 1.0062.04 O

ATOM 1 N LEUB 517 12.525-94.761-18.568 1.0061.97 N

ATOM 2 CA LEUB 517 12.857-96.176-18.705 1.0062.25 C

ATOM 3 CB LEUB 517 13.632-96.690-17.487 1.0062.24 . C

ATOM 4 CG LEU B 517 15.064-96.164-17.332 1.0062.30 C

ATOM 5 CDl LEUB 517 15.725-96.729-16.083 1.0062.24 C

ATOM 6 CD2LEUB517 15.895-96.473-18.570 1.0062.23 C

ATOM 7 C LEUB 517 11.607-97.019-18.948 1.0062.46 C

ATOM 8 O LEUB 517 11.629-97.939-19.760 1.0062.42 O

ATOM 1 N GLUB 518 10.517-96.698-18.255 1.0062.79 N

ATOM . 2 CA GLUB 518 9.248-97.404-18.465 1.0063.31 C ATOM 3 CB GLUB 518 8.186 -96.944 -17.462 1.0063.45 C

ATOM 4 CG GLUB 518 7.762-98.010-16.464 1.0063.87 C

ATOM 5 CD GLU B 518 8.718 -98.127 -15.302 1.0064.37 C

ATOM 6 OEl GLUB 518 9.452-99.135-15.238 1.0064.42 O

ATOM 7 OE2GLUB518 8.741 -97.205 -14.457 1.0064.82 O

ATOM 8 C GLUB 518 8.701-97.252-19.882 1.0063.54 C

ATOM 9 O GLUB 518 7.929 -98.091 -20.351 1.0063.50 O

ATOM 1 N GLY B 519 9.094-96.175-20.554 1.0063.92 N

ATOM 2 CA GLYB 519 8.584-95.872-21.888 1.0064.42 C

ATOM 3 C GLYB 519 7.591-94.725-21.875 1.0064.74 C

ATOM 4 O GLYB 519 6.488-94.834-22.415 1.0064.74 O

ATOM 1 N HIS B 520 7.987 -93.620 -21.250 1.0065.16 N

ATOM 2 CA HIS B 520 .7.139-92.438-21.167 1.0065.57 C

ATOM 3 CB HIS B 520 6.765-92.143-19.714 1.0065.67 C

ATOM 4 CG HIS B 520 5.660 -93.003 -19.192 1.0066.10 C

ATOM 5 NDl HIS B 520 4.337-92.796-19.526 1.0066.58 N

ATOM 6 CEl HIS B 520 3.589-93.707-18.928 1.0066.72 C

ATOM 7 NE2 HIS B 520 4.379-94.495-18.217 1.0066.89 .N

ATOM 8 CD2 HIS B 520 5.680-94.077-18.366 1.0066.36 C

ATOM 9 C HIS B 520 7.822-91.219-21.757 1.0065.70 C

ATOM 10 O HIS B 520 8.924-90.855-21.345 1.0065.77 O

ATOM 1 N GLYB 521 7.165 -90.583 -22.720 1.0065.86 N

ATOM 2 CA GLY B 521 7.633 -89.296 -23.205 1.0066.01 C

ATOM 3 C GLYB 521 7.785-88.376-22.010 1.0066.07 C

ATOM 4 O GLY B 521 6.976-88.416-21.081 1.0066.13 O

ATOM 1 N LEU B 522 8.837 -87.569 -22.009 1.0066.10 N

ATOM 2 CA LEU B 522 9.017 -86.582 -20.954 1,0066.04 C

ATOM 3 CB LEU B 522 10.481 -86.174 -20.840 1.0066.08 C

ATOM 4 CG LEU B 522 11.321-86.795-19.726 1.0066.47 C

ATOM 5 CDl LEUB 522 10.858-88.202-19.364 1.0066.89 C

ATOM 6 CD2LEUB522 12.776-86.798-20.163 1.0066.94 C

ATOM 7 C LEU B 522 8.178-85.351-21.244 1.0065.97 C

ATOM 8 O LEU B 522 . 7.966 -84.999 -22.405 1.0065.87 O

ATOM 1 N PRO B 523 7.692-84.690-20.184 1.0065.92 N

ATOM 2 CA PRO B 523 7.027-83.409-20.367 1.0065.84 C

ATOM 3 CB PRO B 523 6.651-82.993-18.940 1.0065.78 C

ATOM 4 CG PRO B 523 6.708 -84.241 -18.133 1.0065.95 C

ATOM 5 CD PRO B 523 7.749-85.097-18.770 1.0065.96 C

ATOM 6 C PRO B 523 8.024 -82.414 -20.944 1.0065.77 C

ATOM 7 O PRO B 523 9.228-82.685-20.9.82 1.0065.97 O

ATOM 1 N THR B 524 7.535-81.272-21.399 1.0065.48 N

ATOM 2 CA THRB 524 8.435 -80.238 -21.863- 1.0065.17 C

ATOM 3 CB THRB 524 8.019-79.717-23.260 1.0065.20 C

ATOM 4 OGl THR B 524 8.323 -78.323 -23.369 1.0065.65 O

ATOM 5 CG2THRB524 6.526 -79.937 -23.494 1.0065.23 C

ATOM 6 C THRB 524 8.548-79.137-20.799 1.0064.84 C

ATOM 7 O THR B 524 9.526-78.392-20.761 1.0064.93 O

ATOM 1 N ASN B 525 7.554-79,070-19.917 1.0064.41 N

ATOM 2 CA ASN B 525 7.559-78.137-18.788 1.0063.87 C

ATOM 3 CB ASN B 525 6.682-76.920-19.078 1.0063.88 C

ATOM 4 CG ASN B 525 7.333 -75.948 -20.029 1.0063.78 C

ATOM 5 ODl ASNB 525 6.763-75.603-21.063 1.0063.84 O

ATOM 6 ND2ASNB525 8.539-75.5O2-19.689 1.0063.55 ^■ N

ATOM 7 C ASNB 525 7.078-78.805-17.509 1.0063.51 C

ATOM 8 O ASN B 525 5.970-79.340-17.455 1.0063.55 O

ATOM 1 N LEU B 526 7.917 -78.761 -16.482 1.0062.99 N

ATOM 2 CA LEU B 526 7.618-79.378-15.202 1.0062.43 C

ATOM 3 CB LEU B 526 8.806-79.165-14.268 1.0062.46 C ATOM 4 CG LEU B 526 9.131-80.239-13.233 1.0062.26 C

ATOM 5 CDl LEU B 526 8.105-80.225-12.130 1.0062.66 C

ATOM 6 CD2LEUB526 9.197-81.602-13.887 1.0062.13 C

ATOM 7 C LEU B 526 6.354-78.766-14.597 1.0062.24 C •

ATOM 8 O LEU B 526 6.355-77.599-14.209 1.0062.21 O

ATOM 1 N PRO B 527 5.266-79.554-14.512 1.0061.99 N

ATOM 2 CA PRO B 527 4.014-79.062-13.941 1.0061.70 C

ATOM 3. CB PRO B 527 2.997-80.112-14.388 1.0061.70 C

ATOM 4 CG PRO B 527 3.778-81.364-14.488 1.0061.61 C

ATOM 5 CD PRO B 527 5.160-80.961-14.942 1.0061.99 C

ATOM 6. C PRO B 527 4.083 -79.005 -12.417 1.0061.51 C

ATOM 7 O PRO B 527 4.849-79.751 -11.804 1.0061.49 O

ATOM 1 N ARG B 528 3.279-78.133-11.814 1.0061.27 N

ATOM 2 CA ARG B 528 3.346-77.888-10.373 1.0061.10 C

ATOM 3 CB ARG B 528 2.166-77.024 -9.915 1.0061.10 C

ATOM 4 CG ARG B 528 2.137-76.776 -8.411 1.0061.06 C

ATOM 5 CD ARG B 528 0.879-76.043 -7.980 1.0061.02 C

ATOM 6 NE ARG B 528 0.850-75.823 -6.536 1.0060.86 N

ATOM 7 CZ ARG B 528 1.218-74.691 -5.938 1.0060.65 C

ATOM 8 NHl ARGB 528 1.157-74.592 -4.616 1.0060.39 N

ATOM 9 NH2 ARG B 528 1.645-73.658 -6.656 1.0060.55 N

ATOM 10 C ARG B 528 3.409-79.163 -9.528 1.0061.02 C

ATOM 11 O ARG B 528 4.21.8-79.270 -8.606 1.0060.96 O

ATOM 1 N ARG B 529 2.552-80.125 -9.851 1.0060.92 N

ATOM 2 CA ARG B 529 2.403-81.325 -9.035 1.0060.87 C

ATOM 3 CB ARG B 529 1.251-82.189 -9.555 1.0061.05 C

ATOM 4 CG ARG B 529 1.382-82.565-11.016 1.0061.92 C

ATOM 5 CD ARG B 529 0.162 -83.315 -11.516.1.0063.40 C

ATOM 6 NE ARG B 529 0.370-83.798-12.877 1.0064.56 N

ATOM 7 CZ ARG B 529 1.047-84.901-13.181 1.0065.44 C

ATOM 8 NHl ARGB 529 1.189-85.259-14.451 1.0065.89 N

ATOM .9 NH2ARGB529 1.584-85.646-12.218 1.0065.76 N

ATOM 10 C ARG B 529 3.683-82.142 -8.958 1.0060.59 C

ATOM 11 O ARG B 529 3.835-82.979 -8.066 1.0060.74 O

ATOM 1 N LEUB 530 4.599-81.907 -9.892 1.0060.16 N

ATOM 2 CA LEU B 530 5.877-82.605 -9.880 1.0059.71 C

ATOM 3 CB LEUB 530 6.291-83.023-11.292 1.0059.65 C

ATOM 4 CG LEUB 530 5.799-84.382-11.791 1.0059.14 C

ATOM 5 CDl LEUB 530 6.397-84.693-13.153 1.0058.59 C

ATOM 6 CD2LEUB530 6.155-85.472-10.801 1.0058.67 C

ATOM 7 C LEUB 530 6.980-81.784 -9.219 1.0059.56 C

ATOM 8 O LEUB 530 8.032-82.318 -8.874 1.0059.51 O

ATOM ^' 1 N VALB 531 6.744-80.488 -9.043 1.0059.45 N

ATOM . 2 CA VALB 531 7.716-79.637 -8.364 1.0059.44 C

ATOM 3 CB VALB 531 7.333-78.142 -8.445 1.0059.28 C

ATOM 4 CGl VALB 531 8.433-77.283 -7.859 1.0058.89 C

ATOM 5 CG2 VALB 531 7.057-77.735 -9.877 1.0059.32 C

ATOM 6 C VALB 531 7.815-80.033 -6.894 1.0059.61 C

ATOM 7 O VALB 531 6.800-80.081 -6.198 1.0059.64 O

ATOM 1 N PRO B 532 9.036-80.329 -6.416 1.0059.71 N

ATOM 2 CA PRO B 532 9.218-80.580 -4.992 1.0059.85 C

ATOM 3 CB PRO B 532 10.724-80.410 -4.804 1.0059.82 C

ATOM 4 CG PRO B 532 11.307-80.816 -6.117 1.0059.65 C

ATOM 5 CD PRO B 532 10.297-80.447 -7.170 1.0059.60 C

ATOM 6 C PRO B 532 8.456-79.537 -4.176 1.0060.13 C

ATOM 7 O PRO B 532 8.415-78.370 -4.561 1.0060.15 O

ATOM. 1 N PROB 533 7.852-79.960.-3.054 1.0060.38 N

ATOM. 2 CA PRO B 533 6.965-79.145 -2.224 1.0060.52 C ATOM 3 CB PRO B 533 6.841-79.971 -0.945 1.0060.55 C

ATOM 4 CG PRO B 533 6.957-81.366 -1.425 1.0060.51 C

ATOM 5 CD PRO B 533 8.002-81.321 -2.510 1.0060.41 C

ATOM 6 C PRO B 533 7.469-77.729 -1.918 1.0060.72 C

ATOM 7. O PRO B 533 6.658-76.825 -1.727 1.0060.82 O

ATOM 1 N SER B 534 8.783-77.532 -1.861 1.0061.01 N

ATOM 2 CA SERB 534 9.324-76.176 -1.855 1.0061.33 C

ATOM 3 CB SERB 534 10.781 -76.179 -1.414 1.0061.27 C

ATOM ^' 4 OG SER B 534 10.965-77.089 -0.342 1.0061.06 O

ATOM 5 C SERB 534 9.180-75:634 -3.277 1.0061.73 C

ATOM 6 O SERB 534 10.158-75.532 -4-034 1.0061.49 O

ATOM 1 N LYS B 535 7.939-75.302 -3.635 1.0062.26 N

ATOM 2 CA LYS B 535 7.591-75.061 -5.034 1.0062.66 C

ATOM 3 CB LYS B 535 6.481 -76.020 -5.521 1.0062.74 C

ATOM 4 CG LYS B 535 5.237-76.121 -4.644 1.0062.63. C

ATOM 5 CD LYS B 535 4.224-77.127 -5.215 1.0062.53 C

ATOM 6 CE LYS B 535 4.611-78.574 -4.909 1.0062.10 C

ATOM 7 NZ LYS B 535 3.545-79.555 -5.271 1.00.61.50 N

ATOM 8 C LYS B 535 7.279-73.624 -5.416 1.0062.89 C

ATOM 9 O LYS B 535 8.077-73.007 -6.120 1.0063.20 O

ATOM 1 N ARG B 536 6.144-73.086 -4.968 1.0062.87 N

ATOM 2 CA ARG B 536 5.680-71.790 -5.472 1.0062.96 C

ATOM 3 CB ARG B 536 5.145-71.935 -6.902 1.0063.00 C

ATOM 4 CG ARG B 536 5.911-71.160 -7.963 1.0062.88 C

ATOM 5 CD ARG B 536 5.396-69.730 -8.098 1.00.62.78 C

ATOM 6 NE ARG B 536 5.987-69.039 -9.246 1.0062.80 N

ATOM 7 CZ ARG B 536 5.838-67.741 -9.505 1.0062.71 C

ATOM 8 NHl ARG B 536 6.415-67.202-10.571 1.0062.64 N

ATOM 9 NH2 ARG B 536 5.115-66.977 -8.697 1.0062.73 N

ATOM 10 C ARG B 536 4.593-71.172 -4.622 1.0063.09 C

ATOM 11 O ARG B 536 3.436-71.595 -4.688 1.0063.09 O

ATOM 1 N ARG B 537 4.964-70.154 -3.843 1.0063.37 N

ATOM 2 CA ARG B 537 3.993-69.382 -3.075 1.0063.60 C

ATOM 3 CB ARG B 537 4.697 -68.24f -2.327 1.0063.66 C

ATOM 4 CG ARG B 537 4.130-67.921 -0.934 1.0064.02 C

ATOM 5 CD ARG B 537 2.685-67.398 -0.982 1.0064.23 C

ATOM 6 NE ARG B 537 2.224-66.952 0.333 1.0064.87 -N

ATOM 7 CZ ARGB 537 1.914-65.692 0.633 1.0065.30 C

ATOM 8 NHl ARG B 537 2.007-64.746 -0.292 1.0065.61 N

ATOM _. 9 NH2ARGB537 1.502-65.373 1.856 1.0064.97 N

ATOM 10 C ARG B 537 2.970-68.816 -4.063 1.0063.69 C

ATOM 11 O ARG B 537 3.298-68.553 -5,226 1.0063.76 O ^■

ATOM ^' 1 N GLNB 538 1.734-68.641 -3.608 1.0063.75 N

ATOM 2 CA GLNB 538 0:666-68.177 -4.489 1.0063.87 C

ATOM 3 CB GLNB 538 0.043-69.363 -5.225 1.0063.84 C

ATOM 4 CG GLNB 538 -0.406-70.488 -4.301 1.0063.92 C

ATOM 5 CD GLNB 538 -0.796-71.738 -5.066 1.0064.01 C

ATOM 6 OEl GLNB 538 -0.803 -71.751^" -6.299 1.0064.15 O

ATOM 7 NE2 GLNB 538 -1.122-72.802 -4.338 1.0064.37 N

ATOM 8 C GLNB 538 -0.409-67.416 -3.723 1.0063.88 C

ATOM 9 O GLNB 538 -1.543 -67.243 -4.236 1.0063.92 . O

TER 9 GLNB 538

HETATM 1 O2AANPB600 3.973-56.574-52.078 1.0048.61 O

HETATM 2 PA ANP B 600 4.052-57.106-50.670 1.0048.08 P

HETATM 3 O1AANPB600 2.910-57.937-50.141 1.0048.41 O

HETATM 4 O3AANPB600 4.279-55.854-49.694 1.0049.01 O

HETATM 5 PB ANP B 600 3.622-54.443-50.096 1.0049.55 P

HETATM 6 O1B ANP B 600 3.428-53.654-48.825 1.0049.44 O HETATM 7 O2BANPB600 2.412-54.721-50.957 1.0049.32 O HETATM 8 N3B ANP B 600 4.812-53.641-51.080 1.0049.69 N HETATM 9 PG ANP B 600 4.339-52.172-51.877 1.0050.29 P HETATM 10 O3GANPB600 4.467-51.114-50.807 1.0050.68 O HETATM 11 O2GANPB600 5.350-52.031-52.990 1.0050.99 O HETATM 12 O1GANPB600 2.921-52.435-52.332 1.0049.88 O HETATM 13 05* ANP B 600 5.406-57.950-50.510 1.0048.33 O HETATM 14 C5* ANP B 600 6.435-57.592-49.597 1.0049.10 C HETATM 15 C4* ANP B 600- 7.544-58.626-49.749 1.0050.21 C HETATM 16 C3* ANP B 600 7.191-59.661-50.803 1.0050.31 C HETATM 17 03* ANP B 600 8.395-60.157-51.392 1.0050.26 O HETATM 18 C2* ANP B 600 6.537-60.782-50.030 1.0050.21 C HETATM 19 O2* ANP B 600 6.795-62.044-50.644 1.0050.10 O HETATM 20 Cl* ANP B 600 7.209-60.692-48.675 1.0050.66 C HETATM 21 O4* ANP B 600 7.693-59.354-48.530 1.0050.80 O HETATM 22 N9 ANP B 600 6.247-60.938-47.587 1.0050.73 N HETATM 23 C4 ANP B 600 6.554-61.536-46.440 1.0050.52 C HETATM 24 C5 ANP B 600 5.320-61.565-45.655 1.0050.67 C HETATM 25 N7 ANP B 600 4.370-60.971-46.403 1.0051.15 N HETATM 26 CS ANP B 600 4.948 -60.592 -47.574 1.0050.79 C HETATM 27 N3 ANP B 600 7.677-62.071-45.921 1.0050.46 N HETATM 28 C2 ANP B 600 7.672-62.625-44.699 1.0050.75 C HETATM 29 Nl ANP B 600 6.580-62.692-43.920 1.0050.79 N HETATM 30 C6 ANP B 600 5.392-62.188-44.319 1.0050.80 C HETATM 31 N6 ANP B 600 4.295-62.253-43.527 1.0050.98 N HETATM 1 MG MG B 700 1.653-53.618-53.006 1.0049.55 MG HETATM 1 CA CA B 701 19.587-77.142 -8.004 1.0046.71 CA

References

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All publications mentioned in the above specification are herein incorporated by reference. Various modifications and variations of the described aspects and embodiments of the present invention will be apparent to those skilled in the art without departing from the scope of the present invention. Although the present invention has been described in connection with specific preferred embodiments, it should be understood that the invention as claimed should not be unduly limited to such specific embodiments. Indeed, various modifications of the described modes for carrying out the invention which are apparent to those skilled in the art are intended to be within the scope of the following claims.

Claims

1. A method of identifying a modulator of an EHD family polypeptide, said • method comprising (i) providing a first and second sample of an EHD polypeptide;

(ii) contacting said first sample with a candidate modulator; (iii) contacting said first and second samples with ATP; and (iv) monitoring ATP hydrolysis in said first and second samples, wherein a difference between the ATP hydrolysis in said first and second samples identifies said candidate modulator as a modulator of an EHD family polypeptide.

2. A method according to claim 1 wherein if hydrolysis of ATP is greater in said first sample than in said second sample then the candidate modulator is identified as an enhancer of EHD family polypeptide activity.

3. A method according to claim 1 wherein if hydrolysis of ATP is lower in said first sample than in said second sample then the candidate modulator is identified as an inhibitor of EHD family polypeptide activity.

4. A method according to any of claims 1 to 3 wherein ATP hydrolysis is monitored in the presence of lipid.

.

5. A method according to claim 4 wherein said lipid is in the form of liposomes.

6. A method according to claim 4 or claim 5 wherein said lipid is in the form of phosphatidylserine (PS) at a final concentration of about 10%.

7. A method according to any preceding claim further comprising the step of providing a further sample of EHD family polypeptide, said further sample comprising an EHD family polypeptide bearing a T94A mutation, said further sample being used to determine the reference or background level of spontaneous ATP hydrolysis.

8. A method according to any preceding claim further comprising the step of providing a further sample of EHD family polypeptide, said further sample comprising an EHD family polypeptide bearing an I157Q mutation, said further sample being used to determine the reference level of ATP hydrolysis in the absence of lipids.

9. A method according to any preceding claim further comprising the step of providing a further reference sample, said further reference sample comprising a dynamin polypeptide together with GTP nucleotide and candidate modulator, said further sample being used to determine whether the candidate modulator has an EHD-specific effect, or whether it is also capable of affecting dynamin GTPase activity.

10. A crystalline EHD family polypeptide, said polypeptide being bound to an adenosine nucleotide or an analogue thereof.

11. EHD polypeptide having the structure defined by the structural coordinates as shown in Table A.

12. A method for identifying a candidate modulator of EHD family polypeptide activity, said method comprising (i) providing a molecular modelling apparatus with a set of structural coordinates of an EHD family polypeptide selected from those shown in Table A;

(ii) providing said molecular modelling apparatus with a set of structural coordinates of a molecular entity of interest; and

(iii) determining whether the molecular entity of interest is expected to bind to or to affect the structure of said EHD family polypeptide, wherein an expectation of binding or affecting the structure of said EHD family polypeptide identifies said molecular entity of interest as a candidate modulator of EHD family polypeptide activity.

13. A method according to claim 12 wherein the structural coordinates of at least the EH-domain are selected.

14. A method according to claim 12 wherein the structural coordinates of at least the G-domain are selected.

15. A method according to claim 12 wherein the structural coordinates of at least the dimerisation interface are selected.

16. A method according to claim 12 wherein the structural coordinates of at least the membrane binding site are selected.

17. A method according to claim 12 wherein each of the structural coordinates of Table A are selected. .

18. A method for ident ^'if:ying a candidate therapeutic agent, said meth . o fd comprising application of rational drug design to the crystal structure of EHD2.

19. A method of manufacturing a modulator of an EHD family polypeptide, said method comprising identifying a candidate modulator according to any of claims 12 to 18, and synthesising a quantity of said modulator.

20. Use of a candidate modulator of EHD family polypeptide activity identified according to any of claims 12 to 18, wherein said EHD family polypeptide is EHD2, in the manufacture of a medicament for diabetes.

21. Use of the atomic coordinates as shown in Table A in the modelling of an EHD family polypeptide.

22. A method for the design of one or more ligands of an EHD family polypeptide, said method comprising the use of coordinates as shown in Table A.

23. Use of an EHD family polypeptide in the tabulation of a biological membrane.

24. A method of tubulating a biological membrane comprising contacting said membrane with an EHD family polypeptide.

25. A method according to claim 24 or a use according to claim 23 wherein said membrane is comprised by a liposome.

26. A method according to claim 24 or a use according to claim 23 wherein said membrane comprises phosphatidylserine (PS).

27. Use of an EHD family polypeptide in membrane scission.

28. A method of inducing membrane scission, said method comprising contacting said membrane with an EHD family polypeptide.

29. A method according to claim 28, said method further comprising contacting said membrane-EHD family polypeptide complex with nucleotide in conditions permissive of nucleotide hydrolysis.

30. A method according to claim 29 wherein said nucleotide is adenosine triphosphate (ATP).

31. A method of inhibiting dimerisation of an EHD family polypeptide, said method comprising mutating amino acid W238 of said polypeptide.

32. A method of modifying an EHD family polypeptide to permit guanine nucleotide binding thereto, said method comprising mutating said EHD polypeptide at one or more amino acid residues within the region Hl 92 to M223, wherein said mutation alleviates steric exclusion of an amino group at carbon 2 of said guanine nucleotide.

33. A method of modifying an EHD family polypeptide to reduce or prevent membrane binding, said method comprising mutating any of K324, K327, K328, . K329, K334, K341, V321 or F322.

34. A method according to claim 33 wherein amino acid V321 and/or F322 is mutated.

35. A method of modifying an EHD family polypeptide to reduce or prevent ATP hydrolysis by said polypeptide, said method comprising mutating amino acid

T94. of said polypeptide.

36. A method of modifying an EHD family polypeptide to reduce or prevent breakdown of membrane structures by said polypeptide, said method comprising mutating amino acid T94 of said polypeptide.

37. A method of modifying an EHD family polypeptide to increase ATP hydrolysis by said polypeptide, said method comprising mutating amino acid 1157 of said polypeptide. • . .

38. A method of modifying an EHD family polypeptide to enhance breakdown of membrane structures by said polypeptide, said method comprising mutating amino acid Il 57 of said polypeptide.

39. A method according to claim 37 or claim 38, wherein said Il 57 is mutated to Q.

40. A method of inducing membrane fission, said method comprising contacting said membrane with an EHD family polypeptide comprising an I157Q mutation.

41. A method of modifying an EHD family polypeptide to reduce or abolish assembly stimulated ATP hydrolysis, said method comprising mutating said EHD ^' polypeptide at E91, Rl 67, K193, D198, Fl 22, F128, or by deletion of the EH domain.

42. A method according to claim 41 wherein said mutation(s) comprise one or more of the mutations set out in Figure 4b.

43. An EHD family polypeptide or fragment thereof comprising one or more of the following mutations: (i) T94A;

(ii) I157Q; and (iii) F322A.

44. A methodjpf destabilising a membrane, said method comprising contacting said membrane with a EHD family polypeptide and a nucleotide under conditions permissive of nucleotide hydrolysis.

45. An EHD family polypeptide comprising one or more of the mutations described herein.

46. A method, use or polypeptide according to any preceding claim wherein said EHD family polypeptide or fragment thereof is or is derived from mammalian EHD2.