GB2453341A - ATP hydrolysis by EHD family polypeptides - Google Patents

Abstract

A method of identifying a modulator of an epsin homology domain (EHD) containing polypeptide, said method comprising: providing a first and second sample of an EHD polypeptide; contacting said first sample with a candidate modulator; contacting said first and second samples with ATP; and 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. Also claimed are crystal structures comprising EHD family polypeptides bound to an adenosine nucleotide, methods of identifying therapeutic agents using said crystal structures, an EHD polypeptide, use of EHD family polypeptides in membrane modulation and mutated EHD family polypeptides.

Description

19 /20 Supplementary Table I Data collection and refinement statistics Selenomethionine derwatsve Data collection Space group C2 Cell dimensons kb,c(A) 99.9. 1341.56.1 fi P () 90. 1065. 90 Wav&ength 0.97962 CO Resotution (A) * 20-3.1 (3.2 -3.1)

C

Rsri* 7.8(36.1) 11.45(4.4) Completeness (%)* 96.4 (93.8) Redundancy * 3.4 (3.4) Refinement ResouUon (A) 20-3.1 No. reflections 12091 R, R 0.230/0.275 No, atoms Protein 3765 Ligand/ion 33 FIG. 15 20/20 Water 5 8-factors Protein 6iA Co C Ligandlion 50A2 C'J Water 51.5A2 R.m.s deviations c'J Bond lengths (A) OO19 Bond angles (°) 1.121 4f4iglest resolution shell is shown in parenthesis.

FIG. I5CONT'D

I

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 GlPases of the dynamin superfamily, and these have been extensively studied. Epsin homology (EH) domain-containing proteins (EHDsIRmC-1/pincher) comprise a less characterised class of highly conserved eukaryotic ATPases implicated in clathrin-independent endocytosis, and recycling from endosomes The dynamin superfamily of large GTPases are multi-domain proteins that include the classical dynamins (Dyni, Dyn2, Dyn3), dynamin-related proteins (Mx proteins, Dlp, 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 charactensed member where oligomerisation-stimulated GTP hydrolysis has been proposed to lead to scission of clathrin-coated 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 (EHD1-4) in mammals and a single member in C. elegans, D. melanogaster and * * many eukaryotic parasites such as Plasmodium, Leishmania and Enta,nboeba. 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. la), 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. EI{D 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 El-ID 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 andlor 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 * **S 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 AlP 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 ATPase activity.

The invention is based on these surprising findings.

In one aspect, the invention relates to a method of identifying a modulator of an El-ID family polypeptide, said method comprising (i) providing a first and second sample of an El-ID polypeptide; (ii) contacting said first sample with a candidate modulator; (iii) contacting said first and second samples with ATP; and (iv) monitoring AlP 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 El-ID 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 EFID 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 1157Q 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-specific 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 S...

family polypeptide identifies said molecular entity of interest as a candidate modulator of EHD family polypeptide activity. *5*S

S

* 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 Ntv[R 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 dimensation 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.

: 25 In another aspect, the invention relates to a method for identifying a candidate *...

S.... therapeutic agent, said method comprising application of rational drug design to the crystal structure of EHD2. S...

I

*....S * Rational design of candidate agents likely to be able to interact with the target : *::: 30 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 mo'ecules.

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. S...

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 S.....

* etc. In addition to the possibility of the substituents being a cyclic group, a :::5. 30 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 a!, (1977) J. Pharm. Sci. 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 EFID family polypeptide in the tubulation of a biological membrane. S.. S

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

S

S.....

* In another aspect, the invention relates to a method as described above or a use as ::. 30 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 El-ID family polypeptide. Suitably said method fi.trther comprises contacting said membrane-EHD family polypeptide complex with nucleotide in conditions permissive of nucleotide hydrolysis. Suitably said nucleotide is adenosine triphosphate (AT?).

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 aspect, the invention relates to a method of inhibiting dimerisation of an El-ID 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 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 S...

and/or 239). S...

In another aspect, the invention relates to a method of modifying an EHID family *SSS*S * polypeptide to permit guanine nucleotide binding thereto, said method comprising ::::. 30 mutating said El-ID polypeptide at one or more amino acid residues within the *. region H192 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.

In 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 T72A or T94 of said polypeptide, suitably T94.

In another aspect, the invention relates to a method of modifying an El-TD 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. *... * S S...

In another aspect, the invention relates to a method of modifying an EHD family *SSS * polypeptide to enhance breakdown of membrane structures by said polypeptide, S.....

* S said method comprising mutating amino acid 1157 of said polypeptide.

: .". 30 **S.

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 1157Q mutation.

In another aspect, the invention relates to a method of modifring an EHD family polypeptide to reduce or abolish assembly stimulated ATP hydrolysis, said method comprising mutating said El-ID polypeptide at E91, R167, K193, D198, F122, Fl28, 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) 1157Q; 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 END 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 S..... polypeptide then suitably the fragment comprises the amino acids between said mutation and said end (e.g. the N-or C-terminus).

S

S.....

* In another aspect, the invention relates to a method of destabilising a membrane, : * ::: 30 said method comprising contacting said membrane with a END family polypeptide and a nucleotide under conditions permissive of nucleotide hydrolysis.

In another aspect, the invention relates to an El-if) 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 dynaniin 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 El- lBs 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 defonnation.

Dynamins are distinguished from classical signalling GTPases by their large size, their low affinity for nucleotide and assembly-stimulated nucleotide hydrolysis.

From studies of GBP 1, dynamin, bacterial dynamin-like protein, and particularly : ... 25 the insights into EHD disclosed herein, it appears that the mechanism of assembly-S...

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 ::::. 30 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 in the EHD oligomer is along the flat dimension of the lipid tubule, perpendicular to its curvature (see examples and Supplementary Fig. 9b), 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.

In 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. a...

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

* A biological membrane is typically a lipid bilayer membrane. An example of a ::::. 30 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 (PIP2).

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. EFIDs have a molecular mass of approximately 6OKD. EFID 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 EHID1/2/3/4 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 supplementary figure 4. S...

**....

* 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 EHID2 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 94th 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 supplementary figure 4 which presents a comprehensive alignment of sequences of interest with the reference sequence mmEHD2 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. In particular, the crystal structure of the ATPase domain of EHD2 complexed with a bound ligand is applicable across the EHID family polypeptides since those polypeptides are also regarded as ATPases (having previously been thought to be GlPases).

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 *. ..

1** may be tested whether or not that polypeptide can rescue a C.elegans RME knockout. If the knockout is rescued, the polypeptide maybe regarded as an EHD * family polypeptide. * S

::::. 30 Thus there is a high degree of homology between all four classes of El-ID in terms * * * of nucleotide/amino acid sequence, and all four can rescue a C.elegans mutant in the orthologue RME-1. The C. elegans El-ID, Rme-l, 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 been demonstrated for mammalian El-ID I EHD4 / Pincher is predominantly localised to the plasma membrane and is involved in the uptake of the TrkA receptor in response to nerve growth factor (NGF) stimulation. Overexpression of EHD4 leads to increased clathrin-independent macropinocytic endocytosis of 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: Pathway/interaction Therapeutic Therapeutic inhibition activation EHDI MHC I Inhibit in Promote transplanted organ immunological -Protect transplant targeting -from autorejection enhance immune response EHD2 GLUT4 Diabetes E1-1D3 transfemn EHD4 Macropinocytic cancer cancer * NGF/TrkA Pain * *.* * * * a ALL Virus entry a...

a.,,,, EHDs parasites **I**I * S * ,, EHD1 is involved in MI-IC class I recycling at the membrane (Caplan et a!. (2002) A tubular EHD 1-containing compartment involved in the recycling of major * 15 histocompatibility complex class I molecules to the plasma membrane. EMIBO J. 21 p2557-67). Overexpression of EHDI increases recycling. By inhibiting El-ID I activity, for example in a transplanted organ, the transplant may be protected from effects of autorejection. Conversely, activation of EHDI activity may promote an immunological response.

Thus the invention relates to use of a candidate modulator of EHID family polypeptide activity identified as described above, wherein said EHD family polypeptide is EHD1, in the manufacture of a medicament for ameliorating or enhancing immune responses. Amelioration relates to inhibitors of El-ID 1, augmentation applies to activators of EHD 1.

EHDI may have an involvement in cystic fibrosis.

EHID2 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 11 diabetes.

Thus the invention relates to use of a candidate modulator of El-ID 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 (NGF)/neurotrophic tyrosine kinase receptor type I (TrkA) to endosomes : 25 and TrkA-erk5 mitogen-activated protein kinase signalling (Shao et al. (2002) I...

s. Pincher, a pinocytic chaperone for nerve growth factor/TrkA signaling endosomes.

s.. J. Cell Biol. 157 p679-691). Thus modulation of EFID4 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 EI-1D4, in the manufacture of a medicament for pain. In . another aspect, the invention relates to use of a candidate modulator of El-ID family polypeptide activity identified as described above, wherein said Ft-ID family polypeptide is EI-1D4, in the manufacture of a medicament for cancer.

All 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 p4T/-488). Thus broad inhibition of the EHD class finds application in viral infections. Moreover, the El-ID 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

EHDI is involved in the recycling of Mill-IC class 1 molecules. Thus, modulation of EHD I 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 EH1D4, for example * 25 EHD4 response to NGF, finds application in the treatment of neurodegeneration. * S. * S S SSS*

E1-1D2 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 EHID2 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 medicarnent 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 EHD1/2/3/4. 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 oligomerisationldimerisation 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 oligomensation.

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 * 25 operator. * ** * . * ***.

*:*. The assays of the invention suitably monitor EHD ATPase activity. Colorimetnc 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.

In 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. In this embodiment, a first FRET element would be attached to the EHID 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 : 25 nucleotide binding by an El-ID 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 radiolabelled 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 EFID 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.

In 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 S.. expected cellular distribution of the EHD family p.olypeptide being studied, then this is a dramatic indicator that membrane binding had been affected by that S.....

* 25 modulator. One example of an altered distribution would be a cytosolic : *** * distribution. S... * S *

* In 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. In another embodiment, the invention may relate to a two step procedure involving a first step of an ATPase screen arid a second step of a cargo internalisation screen. In 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 EI{D 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 dynaniin should have GTP as a substrate, and should measure the hydrolysis of GTP (rather than ATP which will of course be used in assaying EF[D 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. S.. S * S

* S. S The candidate compounds or treatments of most interest will be those which have *5SS no 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. * S. * . S S...

*:*. INACTIVE EHD MUTANT In some aspects of the invention, a control or reference sample is used which comprises an inactive El-ID 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 El-ID 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 El-ID 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 EFID 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.

* * 25 : *..* 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 El-ID 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 I 0%-20% final concentration. 1157Q

The invention provides a super-active EHD family polypeptide mutant. This mutant is suitably the 1157Q mutant. El-ID family polypeptides bearing this mutation are not well activated by lipids. In other words, EHD family polypeptides bearing the 1157Q 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 1157Q mutation.

In addition, such mutants are useful in embodiments of the assay of the invention.

For example, by employing the 1157Q 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 1157Q 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 1157Q mutation, in particular when lipids were absent from the 1157Q assay sample, then this effectively provides another level of information about the action of the compound or treatment being studied. Specifically, if an 1157Q : *** 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 1157Q mutants in order to distinguish between the effects on different biological aspects of the EHD family polypeptide being studied. EIID3

EHD3 may be involved in transferrin uptake. Specifically, EHD3 may inhibit transfemn 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. In another embodiment transferrin uptake may be used as a readout in a cellular screen to ensure El-ID 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 E}{D inhibitors or interactors, e.g. by computational techniques which identify possible binding ligarids for the active sites, by enabling linked-fragment approaches to drug design, and by enabling the identification arid 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 s'S employed. EHD inhibitors may also be designed in the this way. More specifically, * : 25 a ligand (e.g. a potential inhibitor) of EHD may be designed that complements the : s' * functionalities of the EL-ID active site(s) such as the oligomerisation site or ATPase S...

* * : site. The ligand can then be synthesised, formed into a complex with El-ID, 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 El-ID 3D structure, more purely computational techniques for rational drug design may also be used to design El-ID inhibitors (or activators). For example, automated ligand-receptor docking programs (discussed e.g. by Jones Ct 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 El-ID 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 identif' 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 phannacophore, 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: *I.. S. S * . . * I.

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, MI-I = Hn -LH1 is plotted. Fitted values are: ATP-y-S (j): 13�3pM (n0.96), ADP(0): 50�6pM (n0.9), GTP-y- S() and EHD2(T72A)-ATP-y-S(i): no binding observed. c, Coomassie-stained gels of co-sedimentation assays in the presence of 1 mM ATP-y-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 1mM ATP-v-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 Foich 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 (0,0), GTP hydrolysis was not stimulated The nucleotide-free T72A mutant did not show stimulation of ATP hydrolysis (i,i).

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 *bII " *" in purple, the localisation of the KPFXXXNPF and further motifs in the G- domain are shown. b, Topology plot of EHD2 in which circles represent a'-helices and triangles represent a-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 EpsI 5 (orange) bound to an NPF-containing peptide (pdb code IFFI) . 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 AlP 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. if. The F322A mutant (. intrinsic, stimulated reaction) showed a 40% decrease in the stimulated ATPase -1 -1 reaction (kobs=3.Oh for F322A versus 5.4h for wt), and the mutant K328D (,) 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-y-S was determined as described in Fig. lb. Nucleotide hydrolysis was measured as described in Fig. if. In vitro tubulation activity of PS liposomes was analysed as described in Fig. id. f, EGFP-tagged mutants were over-expressed in HeLa cells. Whereas the * 25 194A mutants showed extensive tubulation with no punctate stained, the a'. 1157Q mutant showed exclusively punctate staining. g, Quantification of the . .: over-expression phenotypes from Fig. 3f. For each construct, three independent experiments with 50 cells I experiments were analysed.

Figure 4 shows the EHD2 oligomer: a, The alignment in Supplementary Fig. 4 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. if. Note that mutant R167E (in Switch Il) showed an increased basal ATPase activity which was not further stimulated by Foich 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-dornain 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 alt in the same direction towards the putative membrane interface.

Supplementary Figure 1 shows expression and purification of mouse EHD2. Mouse EHD2 was expressed in Escherichia coil 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. El-EHD2 after elution from N1NTA-Sepharose. E2 -S.....

* 5 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).

Supplementary Figure 2 shows ultracentrifugation analysis indicates that EHD2 is a dimeric protein. Sedimentation velocity experiments were performed as described in methods. Selected scans (at equal, -1 5mm intervals), and of g(s20,w) (the amount of material sedimenting between s20,w and (s20,w+ós)) 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 l24kDa.

Supplementary Figure 3 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-y-S (h) and ADP (i), but we did not observe tubulation in the absence of nucleotides (j).

Supplementary Figure 4 shows alignment and secondary structure s * 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!aevis EHDI (Q7SYAI), Xenopus laevis EHD4 (Q7ZXE8), Drosophila melanogaster PAST-I (Q8l G NO), Caenorhabditis elegans RME1 (Q966F0), Schistosomajaponicum EHD (Q5DG45), Dictyostelium discoideum EHD (Q54ST5), Plasmodium falciparum EHD (Q9NLB8), Entamoeba histolytica EHD (Q51 5L4), Tiypanosoma 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, /3-strands as blue arrows with colours according to the domain organisation (see Fig. Ia). Residues mutated in this study are indicated with a diamond (,).

Supplementary Figure 5 shows the EHD dimer interface. The alignment in Supplementary Fig. 4 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 a6 with its invariant W238 and the contiguous loop of the opposing EHD2 monomer are shown in orange interacting with the conserved surface. 2+

Supplementary Figure 6 shows the Ca binding site of the EH-domain. 2+

Residues 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 2+ grey. Five direct ligands for Ca could be identified which are the carboxy side-chains of 0494, D496, 0498, E505 and one main chain oxygen from M500 (mc500). The sixth ligands might be a water molecule not seen at the current resolution.

Supplementary Figure 7 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 ** *5sS 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 1mM MgCl2 (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.

Supplementary Figure 8 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.

Supplementary Figure 9 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 (Supplementary Fig. 7) 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. Id, Supplementary Fig. .3).

Supplementary Figure 10 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 100mM HEPES (pH 118 418 7.5), 50mM NaC1, 200DM CaCI2. Peptides PEKPFRKL and RIVIGPFVER did S...

not show detectable binding whereas binding of peptide KLNPFGNT could be * fitted to an affinity of 130�20.tM (n=1.33).

Supplementary Figure 11 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: JTC measurements were performed at 10°C in 20mM HEPES (pH 7.5), 300mM NaCI, 2mM MgCI2. Liposome binding assays were performed as described previously (www.endocytosis.org). Multiple turnover ATPase assays were performed in 20mM HEPES (pH 7.5), 135m1v1 NaCI, 15mM KC1, lmlvI MgC12 at 30°C with lOi.tM EHD2 (or mutants) as enzyme and 100pM ATP as substrate, in the absence or presence of I mg/mi Foich liposomes (Sigma-Aldrich).

Reactions were started by the addition of the protein to the final reaction mix and nucleotide hydrolysis was followed using standard HPLC measurement. Initial rates were determined by applying a linear fit to data points up to 40% nucieotide hydrolysis. For electron microscopic studies, 2.5jiM EHD2 in 20mM HEPES (pH 7.5), 150mM NaCL, 1mM MgCI2 was incubated for 15mm at 25°C in the presence of 1mM nucleotide and 0. 05mg/mi (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 co/i BL21 DE3 Rosetta (Novagen) from a modified pET28 vector. Bacteria cultures in TB medium were induced at an OD of 0.2 with 4OpM IPTG and grown overnight at 18°C. Bacteria were iysed in lysis buffer containing 50mM HEPES (pH 7.5), 400mM NaC1, 25mM Imidazole, 2.5mM /3-Mercaptoethanol (/3-ME), 500MM Pefablock SC (Boebringer Ingelheim) using an Emulsiflex homogeniser (Avestin, Canada). After : centrifugation at 1 00,000g for 45mm at 4°C, the soluble extract was applied to a NiNTA-column (Qiagen, Hildesheim) equilibrated with lysis buffer. The column was extensively washed with 20mM HEPES (pH 7.5), 700mM NaC1, 30mM Imidazole 2.5mM /3-ME 1mM ATP, 10mM KC1 and shortly with 20mM *.... , , * HEPES (pH 7.5), 300mM NaCI, 25mM Imidazoie, 2.5mM /3-ME. Bound protein was eluted with 20mM HEPES (pH 7.5), 300mM NaC1, 100mM Imidazole, 2.5mM /3-ME and dialysed overnight at 4°C against 20mM HEPES (pH 7.5), 300mM NaCI, 2.5mM /3-Mercaptoethanol in the presence of 250pg 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 20mM HEPES, 300mM NaCI, 2.5mM /3-ME, and the protein finally eluted with 20mM HEPES, 300mM NaC1, 2.5mM /3-Me, 25mM Imidazole, concentrated and further purified using a Sephadex200 size-exclusion column (two consecutive runs for proteins used for the ATPase assays). Typical yields were 4mg purified EHD2 / 1 bacteria culture. At 300mM NaCI we could concentrate the protein to 40mg/mi but at lower salt concentration we observed some precipitation at this protein concentration. The protein was partially stabilised by 1mM MgCl2.

Crystallisation and structure determination. For crystallisation, a 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/mi and supplemented with 4mM MgCl2, 2mM AMP-PNP (Sigma-Aldrich, both final concentrations). The hanging-drop vapour-diffusion method was used for crystallisation. 2j.ti protein solution were mixed with an equal volume of reservoir solution containing 3% PEG2000 MME, 50mM MES (pH 6.4), 4mM MgCl2. Crystals appeared after one week at 4°C and had dimension of.2 x 0.2 x 0.05mm. For flash-freezing in liquid nitrogen, they were first transferred for I Osec in 50mM MES (pH 6.4), 75mM NaC1, 4mM MgCl2, 2mM AMP-PNP, 14% MPD before incubation in the final cryo-solution containing 50mM MES (pH 6.4), 75mM NaC1, 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 ESRF beamline 1D14-EH4 (see Supplementary Table 1) and processed and * . 25 scaled using the xds program suite. Crystals belonged to the monochnic crystal : *. system and contained one molecule in the asymmetric unit. 13 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 the program SHARP. In the resulting electron density, the main chain was clearly traceable, and an initial model could be built using the Xtal View package. The model was refined using Refmac5 with 3 TLS groups (Supplementary Table I). 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 the Ramachandran plot as judged by the program Procheck. Ribbon plots were prepared using the program 37 38 Molscript and rendered with Raster3D. Surface conservation plots were 39 40 prepared using the ConSurf server and ccp4 molecular graphics. Electron potential maps were generated using ccp4 molecular graphics. All other surface representations were prepared using pymoi. To predict the arrangement of the EHD2 dimer in the oligomer, two EI{D2 dimers were superimposed with one of the two monomers of the GBPI *GDP *A1F3-dimer (pdb code 2B92) using swisspdb viewer. The EI-1D2 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 (Supplementary Fig. 9). 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 2Onm 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 oligomensation (ordering of switch I and * switch II) and since the resolution of the structure is not appropriate for an accurate prediction. The programs superpose and pdbset from ccp4 were used to generate S...

the oligomer from the tetramer. Pdb coordinates of the proposed oligomer are *5**** * found in the Supplementary Materials.

Ultracentrifugation. Sedimentation velocity experiments were performed in a * Beckman Optima XLA ultracentrifuge, using an An-6OTi rotor. Centrifugation was at 50,000 rev x mm and 5°C at an EHD2 concentration of 1 5j.tM, with scans as fast as possible (-1.5mm intervals). The data were analysed using DCDT+ v.2 with the partial specific volume for the protein (from the amino acid composition) and solvent density and viscosity calculated using Sednterp. Selected scans (at equal, --15mm intervals), and of g(s20,w) (the amount of material sedimenting between s20,w and (s20,w+ôs)) 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 10mm 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 (WillCo Wells By, Amsterdam) were washed with 25mM HEPES (pH 7.5), 125mM NaCI, 5mM KC1, 10mM D-glucose, 1mM MgCI2, 2mM CaCl2), and epifluorescence images were taken using an Olympus 1X70 microscope (Southhall, UK) and Argon laser (Melles Griot, Carlsbad, CA) with a Princeton instruments (Trenton, NJ) cooled 1-PentaMAX camera with MetaMorph software (Universal imaging).

Example 1: Expression and Purification Mouse full-length EHD2 was expressed in bacteria and purified to homogeneity (Supplementary Fig. 1). The purified protein was nucleotide-free as judged by HPLC analysis. In 300mM NaC1, E}{D2 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 * *** (Supplementary Fig. 2). At 50DM protein concentration, the hydrodynamic radius *.* did not change in the presence or absence of nucleotides (or in 150mM versus * " 300mM NaCI), as judged by dynamic light scattering experiments. It was : *. previously reported that EHDs -despite having a predicted G-domain -bind to Is *:* . 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-y-S, with an affinity of 131.mM, and to ADP, with an affinity of approximately 50tM. A mutation in the phosphate binding (P-)loop, T72A, prevented binding to ATP-y-S, similar to the effect of equivalent mutations on nucleotide binding to other GTPases. No binding signal was observed for GTP-y-S (Fig. lb and). We still refer to this domain as a G-domain because the sequence and fold (see below) are clearly similar to other 0-domains. We next investigated membrane-binding properties of EHD2 and found efficient binding to liposomes made from brain-derived lipids (Foich extract) and to 100% anionic phosphatidyl-serine (PS) liposomes (Fig. ic). Using synthetic liposomes containing various different phosphatidyl-inositols (P1) (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 2Onm-diameter tubules and oligomerises in ring-like structures around these tubules (Fig. Id, Supplementary Fig. 3). Nucleotide-independence of liposome tubulation in 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 (Supplementary Fig. 3). 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 *I..

of ATP-'y-S and ADP but not in the absence of nucleotides (Supplementary Fig. 3).

When EGFP-tagged EI-1D2 was over-expressed in HeLa cells it marked punctate : ** and tubular structures that were mainly found close to the plasma membrane (Fig. . : le, endogenous EHD2 in various cell lines shows a similar peripheral distrubution). Although the nucleotide-free T72A mutant bound to Foich liposomes in vitro (Fig. 1C), it showed a cytoplasmic distribution when over-expressed in vivo (Fig. le), indicating that nucleotide binding is required for oligomensation 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 E1-1D2 under multiple-turnover conditions (10-fold excess of ATP over EHD2), in the presence and absence of Foich liposomes (Fig. If). The intrinsic / background ATPase activity is extremely slow (kobs=0.7h) but is stimulated 8-fold in the -I 18 presence of Folch or PS liposomes (kobs=5.6h). In contrast to GBPI 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 ATPase activity. EHD2 displays a 600-fold slower stimulated nucleotide hydrolysis than dynamin, which hydrolyses GTP under this condition with a kcat of 1sec 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. iA (see Methods and Supplementary Table I for the statistics). The nucleotide binding domain of EHD2 possesses a typical G-domain fold with a central (3-sheet surrounded by a-helices (Fig. 2a, 2b and Supplementary Fig. 4). An AIvIP-PNP molecule occupies the canonical nucleotide-binding site. In comparison to the Ras-like G-domain, EHD2 contains an insertion of two additional (3-strands 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 crystallographic two-fold axis (Fig. 2a). Dimerisation is mediated **** 2 via a highly conserved, mostly hydrophobic interface of approximately 2100A in the G-domain (Supplementary Fig. 5). At the centre of the interface, the entirely conserved W238 in helix a6 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 charactensed GBPI and bacterial dynamin-like protein (BDLP) dimers Example 4: Structural Insights The helical domain is composed of helix cr1 and c2 from the N-terminal region (residues 18-55, which follow disordered residues 1-18) and helices cr8, o9, cr10, cr1 I and cr12 (residues 285-400) following the G-domain (Fig. 2a). Helix cr8 of El-ID is the organising scaffold against which most of the other helices fold. It has also extensive contacts with the G-domain. The dimenc 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 2 1,22 EpsI5 solved by NMR studies with a root-mean square deviation of 1.5A for the main-chain atoms (Fig. 2c). It is built of two closely packed perpendicular EF 2-f hands which are connected by a short j3-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 (Supplementary Fig. 6). This ion has been maintained during purification. The EH-domain is localised on top of the G-domain (the top site position) with a buried interface of I 600A. 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 to the EH2 domain of EpsiS involving a tight turn with F422 projecting into a hydrophobic pocket which is lined by W490 at its base (Fig. 2c and Supplementary Fig. 6).

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 carbon6 of the guanosine base and the aspartate side-chain forms a double hydrogen bond to nitrogen I 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-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 (Supplementary Fig. 4). The carboxyamide group ofN2l9 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 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 and data not shown). 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 Supplementary Fig. 7). Indeed EHD2 showed a binding preference for very small liposomes, consistent with this curvature, but only in the nucleotide-free form (Supplementary Fig. 7). In the nucleotide-bound form EF[D 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, whi ch would not allow the insertion of a catalytic residue in trans into the catalytic site (Supplementary Fig. 8). This so-called "phosphate cap" is also present in GBP1 whose mechanism of GTP hydrolysis has been shown to involve dimerisation-dependent positioning of the attacking nucleophilic 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 catalytic glutamine from switch H. We studied the role of ATP hydrolysis to gain insights into the function of EHD2 in vivo. The T94A mutant bound to ATP-'y-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, and Supplementary Movies I and 2), 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 165 was mutated to alanine. To confirm the role of ATP hydrolysis in EHD function **S* we re-introduced a catalytic glutamine in the active site, at the position normally found for small GlPases (Ii 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 (Supplementary Movie 3). 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.

In a surface-conservation plot of the EHD2 dimer, a highly conserved surface patch encompasses switch I, switch II and the surrounding area (Fig. 4a). GBP 1 and BDLP use this same interface, with the same relative orientation of the G-domains, for dimerisation. This interface was suggested to be a conserved feature of all dynaminrelated GTPases. Thus, the EHD2 dimer may further oligomerise into the observed rings using this second 0-domain interface. Using -18 the dimeric GBPI'GDP'AlF 4 0-domain structure as a template and taking into account the observed 20-nm ring of the EI-[D2 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, Supplementary Fig. 9), and the thickness of the oligomenc ring agrees well with : the thickness of the rings observed by EM (l0nm, 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 ISIt abolished assembly-stimulated ATP hydrolysis (Fig. 4b) indicating that the *: 25 conserved interface is indeed involved in the assembly-stimulated ATPase * ** reaction. In the predicted oligomer, the highly curved membrane interface of the : EHD2 dimer are oriented perpendicular to the direction of the tubule curvature * (Supplementary Fig. 9b), consistent with the tightly packed rings observed by EM.

In an alternative model, the oligomer could also form along the length of a tubule @arallel to its long axis) and thus maximise the use of the highly curved membrane interface of the dimer (Supplementary Fig. 9c). 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 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 fl-sheet 2A and 2B.

In 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 dimr. It is interesting that only a side site NPF peptide, and not the top site GPF peptide, bound with a measurable affinity (30ltM) to the isolated EH-domain of EHD2 (Supplementary Fig. 10), and this affinity is well within the 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 (EH) or a double mutant of the a',, two side-site xPF motifs (F122A/F128A) did not show any membrane-stimulated S..,.. 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. * S * * S.

Example 9: Cell imaging studies EHD2 wild-type was over-expressed in HeLa cells for 24h and imaged by EPI-fluorescence for approximately 30mm. 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 30mm. There a only tubules, and these are mostly static.

EHD2 1157Q was over-expressed in HeLa cells for 24h and imaged by EPI-fluorescence for approximately 30mm. 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 GBP 1 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 S...

the EHD polypeptide is EHD2. * . *SSS

The first El-ID sample is contacted with a candidate modulator. The candidate : *. 25 modulator is added to the medium containing the El-ID polypeptide. *5** * *

* .: 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 EF[D 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 phosphatidylsenne (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. * * * *** **** * * S... * . S...

S

*55SS* * . * S. * . S *S.. SS * S * * S **

Example 11:Atomic Coordinates

Table A

ATOM I N ARGA 19 51.364-44.695-13.521 1.0058.79 N ATOM 2 CA ARGA 19 51.849-44.622-14.929 1.0058.86 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 ATOM 6 NE ARGA 19 55.299-46.949-16.261 1.0059.75 N ATOM 7 CZ A.RGA 19 56.300-46.076-16.161 1.005995 C ATOM 8 NHI ARG A 19 56.669 -45.613 -14.972 1.00 60.07 N ATOM 9 NH2 ARG A 19 56.937 -45.665 -17.252 1.00 59.86 N ATOM 10 C ARG A 19 50. 835 -45.249 -15.884 1.00 58.73 C ATOM 11 0 ARG A 19 5 1.082 -45.372 -17.083 1.00 58.69 0 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 1.00 58.46 C ATOM 14 CB THRA 20 47.790-47.226-15.302 1.00 58.50 C ATOM 15 001 THR A 20 47.104 -46.534 -14.249 1.00 58.37 0 ATOM 16 CG2 THR A 20 48.699 -48.292 -14.705 1.00 58.59 C ATOM 17 C THR A 20 47.680 -45.152 -16.697 1.00 58.32 C ATOM 18 0 THRA 20 48.020-43.965 -16.718 1.00 58.25 0 ATOM 19 N VALA 21 46.500-45.579-17.143 1.00 58.12 N ATOM 20 CA VAL A 21 45.548 -44.683 -17.800 1.00 57.89 C ATOM 21 CB VALA 21 44.611-45.447-18.756 1.00 57.93 C ATOM 22 CG1 VAL A 21 43.624 -46.293 -17.968 1.00 58.17 C ATOM 23 CG2 VAL A 21 43.872 -44.474 -19.663 1.00 57.98 C ATOM 24 C VALA 21 44.712-43.859-16.817 1.00 57.68 C ATOM 25 0 VAL A 21 44.574 -42.644 -16.983 1.00 57.39. 0 ATOM 26 N THR A 22 44.152 -44.511 -15.801 1.00 57. 46 N ATOM 27 CA THRA 22 43.359-43.792-14.806 1.00 57.30 C ATOM 28 CS 1'HR A 22 42.661 -44.740 -13.793 1.00 57.27 C ATOM 29 001 THRA 22 43.523-44.987-12.676 1.00 57.51 0 ATOM 30 CG2 THR A 22 42.280 -46.062 -14.453 1.00 57.23 C ATOM 31 C THR A 22 44.255 -42.784 -14.085 1.00 57.11 C ATOM 32 0 THRA 22 43.837-41.669-13.783 1.0057.00 0 ATOM 33 N SERA 23 45.494-43.183-13.824 1.00 56.93 N ATOM 34 CA SER A 23 46.500 -42.275 -13.297 1.00 56.79 C ATOM 35 CB SER A 23 47.849 -42.985 -13.265 1.00 56. 78 C ATOM 36 OG SERA 23 48.811-42.263-14.009 1.0057.00 0 ATOM 37 C SERA 23 46.594-41.016-14.155 1.0056.73 C * * ATOM 38 0 SERA 23 46.504-39.884-13.653 1.0056.72 0 ATOM 39 N SERA 24 46.768 -41.227 -15.456 1.00 56.67 N : *. ATOM 40 CA SERA 24 46.884-40.135-16.415 1.00 56.66 C 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 0 * " ATOM 43 C SERA 24 45.629-39.262-16.388 1.0056.55 C ATOM 44 0 SERA 24 45.710-38.031 -16.372 1.00 56.41 0 ATOM 45 N LEU A 25 44.471 -39.911 -16.373 1.00 56.64 N ATOM 46 CA LEU A 25 43.208 -39.213 -16.174 1.00 56.46 C ATOM 47 CB LEUA 25 42.067-40.216-16.016 1.0056.37 C ATOM 48 CC LEU A 25 41.205 -40.508 -17.240 1.00 56.13 C ATOM 49 CD! LEUA 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 ATOM 51 C LEUA 25 43.271 -38.320-14.940 1.00 56.49 C ATOM 52 0 LEUA 25 42.889-37.148-14.989 1.0056.42 0 ATOM 53 N LYSA 26 43.752-38.883-13.835 1.0056.45 N ATOM 54 CA LYS A 26 43.817 -38 164 -12.575 1.00 56.29 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 1.00 56.35 C ATOM 57 CD LYSA 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 1.00 56.32 C ATOM 61 0 LYS A 26 44.264 -35.8 17 -12.367 1.00 56. 34 0 ATOM 62 N GLU A 27 45.901 -37.093 -13.242 1.00 56.37 N ATOM 63 CA GLU A 27 46.764 -35.927 -13.450 1.00 56.31 C ATOM 64 CB GLU A 27 48.135 -36.332 -13.989 1.00 56.40 C ATOM 65 CO GLU A 27 49.118 -36.769 -12.907 1.00 56. 99 C ATOM 66 CD GLUA 27 49.194-35.789-11.741 1.00 57.43 C ATOM 67 OE1 GLU A 27 48.165 -35.604 -11.049 1.00 57.97 0 ATOM 68 OE2 GLU A 27 50.285 -35.218-11.504 1.00 56.59 0 ATOM 69 C GLUA 27 46.110-34.886-14.357 1.0056.16 C ATOM 70 0 GLU A 27 46.094 -33.69 1 -14.039 1.00 55.99 0 ATOM 71 N LEU A 28 45.563 -35.352.15.478 1.00 56.19 N ATOM 72 CA LEU A 28 44.827 -34.483 -16.394 1.00 56.04 C ATOM 73 CB LEU A 28 44.156 -35.295 -17.505 1.00 55 97 C ATOM 74 CO LEU A 28 44.864 -35.366.18.861 1.00 56.13 C ATOM 75 CD1 LEU A 28 46.354 -35.712 -18.746 1.00 56.25 C ATOM 76 CD2 LEU A 28 44.144 -36.321 -19.799 1.00 56.01 C ATOM 77 C LEUA 28 43.787-33.671-15.642 1.00 56.00 C ATOM 78 0 LEU A 28 43.736 -32.450 -15.767 1.00 56.01 0 ATOM 79 N TYR A 29 42.961 -34.353 -14.857 1.00 55.97 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 1.00 55.13 C ATOM 83 CDI TYR A 29 39.169 -33.320 -12.560 1.00 54.84 C ATOM 84 CE1 TYRA 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 TYR A 29 37.839 -32.111 -9. 396 1.00 55.02 0 ATOM 87 CE2 TYRA 29 39.791 -33.381 -9.875 1.00 54.94 C :. 35 ATOM 88 CD2 TYR A 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 0 TYRA 29 42.328.31.432-13.272 1.00 55.94 0 ATOM 91 N ARG A 30 43.565 -33.056 -12.311 1.00 56.07 N ATOM 92 CA ARGA 30 44.161-32.167-11.317 1.0056.16 C ATOM 93 CB ARGA 30 45.155-32.915.10.425 1.00 56.13 C ATOM 94 CO ARGA 30 45.781 -32.027 -9. 349 1.00 56.57 C ATOM 95 CD ARG A 30 46.944 -32.704 -8.639 1.00 56.62 C ATOM 96 NE ARGA 30 47.997-33.102 -9.570 1.00 57.56 N : .* ATOM 97 CZ ARGA 30 49.025-32.334 -9.915 1.00 57.96 C ATOM 98 NH! ARGA 30 49.150-31.115 -9. 404 1.0058.09 N ATOM 99 NH2ARGA 30 49.933-32.785.10.771 1.0058.17 N * ATOM 100 C ARG A 30 44.836 -30.945.11.925 1.00 56.07 C ATOM 101 0 ARGA 30 44.809-29.864-11.339 1.0056.10 0 ATOM 102 N THRA 31 45.438-31.104-13.097 1.00 5602 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 1.00 55.94 C ATOM 105 001 THR A 31 47.127 -31.427 -15.407 1.00 56.01 0 ATOM 106 CG2THRA 31 48.379-31 172-13.361 1.0055.91 C ATOM 107 C THR A 31 45.378 -29.166 -14.687 1.00 55.97 C ATOM 108 0 THRA 31 45.658-27.982 -14.883 1.00 55.91 0 ATOM 109 N LYSA 32 44.377-29.780-15.311 1.0056.00 N ATOM 110 CA LYS A 32 43.660 -29.137 -16.414 1.00 56.02 C ATOM 111 CB LYS A 32 43.701 -30.019 -17.673 1.00 56.03 C ATOM 112 CO LYS A 32 45.082 -30.162 -18.339 1.00 56.05 C ATOM 113 CD LYSA 32 45.420-28.956-19.218 1.0056.16 C ATOM 114 CE LYS A 32 46.772 -29.099 -19.924 1.00 55.96 C ATOM 115 NZ LYS A 32 46.693 -29.805 - 2 1.237 1.00 55.50 N ATOM 116 C LYS A 32 42.211 -28.750 -16.087 1.00 56.03 C ATOM 117 0 LYSA 32 41.668-27.819-16.683 1.0056.12 0 ATOM 118 N LEUA 33 41.587-29.460-15.149 1.0055.98 N ATOM 119 CA LEIJA 33 40182-29.209-14.814 1.00 55.83 C ATOM 120 CB LEU A 33 39.381 -30.508 -14.852 1.00 55.81 C ATOM 121 CO LEUA 33 38.353-30.636-15.968 1.0055.96 C ATOM 122 CDI LEUA 33 37.675-31.991 -15.893 1.00 56.34 C ATOM 123 CD2 LEU A 33 37.330 -29.526 -15.847 1.00 56.25 C ATOM 124 C LEU A 33 39.996 -28.553 -13.455 1.00 55. 75 C ATOM 125 0 LEUA 33 39.334-27.521 -13.332 1.00 55.70 0 ATOM 126 N LEUA 34 40.581 -29.171 -12.435 1.00 55.70 N ATOM 127 CA LEUA 34 40.452-28.699-11.066 1.0055.64 C ATOM 128 CB LEU A 34 41.427 -29.447 -10.154 1.00 55.58 C ATOM 129 CG LEUA 34 41.327-29.178 -8.654 1.00 55.53 C ATOM 130 CD1 LEU A 34 39.877 -29.201 -8.195 1.00 55.57 C ATOM 131 CD2 LEU A 34 42.156 -30.193 -7.882 1.00 55.60 C ATOM 132 C LEU A 34 40.638 -27. 189 -10.935 1.00 55.74 C ATOM 133 0 LEUA 34 39.868-26.536-10.231 1.0055.74 0 ATOM 134 N PROA 35 41.658-26.624-11.611 1.00 55.81 N ATOM 135 CA PRO A 35 41.887-25.187-11.486 1.00 55.89 C ATOM 136 CB PRO A 35 43.070 -24.935 -12.426 1.00 55.71 C ATOM 137 CO PRO A 35 43.742 -26.244 -12.550 1.00 55.71 C ATOM 138 CD PROA 35 42.647-27.256-12.502 1.0055.76 C ATOM 139 C PRO A 35 40.683 -24.372 -11.935 1.00 56.06 C ATOM 140 0 PROA 35 40.384-23.339-11.341 1.00 56.11 0 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 LEU A 36 38.587 -24.654 -14.936 1.00 56.61 C ATOM 144 CG LEU A 36 38.094 -23.658 -15.978 1.00 56.89 C ATOM 145 CDI LEU A 36 38.653 -24.03 1 -17.33 1 1.00 57.25 C ATOM 146 CD2 LEU A 36 36.582 -23.624 -16.011 1.00 57.53 C ATOM 147 C LEUA 36 37.648-24.229-12.646 1.00 56.79 C ATOM 148 0 LEUA 36 36.943-23.237-12.376 1.00 56.95 0 ATOM 149 N GLUA 37 37.413-25.448-12.171 1.00 57.00 N ATOM 150 CA GLIJA 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 GLU A 37 36.009-29.602-11.266 1.00 57.48 C * ATOM 154 OEI GLU A 37 35.934 -29.763 -10.026 1.00 57.98 0 * ** ATOM 155 0E2 GLU A 37 36.035 -30.557 -12.073 1.00 57.15 0 * *,*. 45 ATOM 156 C GLU A 37 36.550 -24.800 -9.958 1.00 57.50 C ** * ATOM 157 0 GLUA 37 35.595-24.154 -9.517 1.00 57.53 0 * * ATOM 158 N GLU A 38 37.767 -24.760 -9.417 1.00 57.64 N ATOM 159 CA GLU A 38 38.044 -23.989 -8.206 1.00 57.92 C ATOM 160 CB GLU A 38 39.439 -24.302 -7.661 1.00 58.10 C ATOM 161 CO GLU A 38 39.552 -25.674 -7.015 1.00 59.87 C ATOM 162 CD GLU A 38 38.818 -25.767 -5.682 1.00 62.05 C ATOM 163 OE1 GLU A 38 39.351 -25.231 -4.678 1.00 62.81 0 ATOM 164 0E2 GLU A 38 37.719 -26.384 -5.638 1.00 62.50 0 ATOM 165 C GLU A 38 37.901 -22.498 -8.441 1.00 57.70 C ATOM 166 0 GLUA 38 37.434-21.771 -7.567 1.0057.74 0 ATOM 167 N HIS A 39 38.298 -22.045 -9.624 1.00 57.50 N ATOM 168 CA HIS A 39 38.240 -20.627 -9.932 1.00 57.36 C ATOM 169 CB HIS A 39 39.053-20.289-11.186 1.00 57.49 C ATOM 170 CG HISA 39 39.414-18.837-11. 301 1.0057.86 C ATOM 171 NDIHISA 39 39.302-18.130-12.480 1.0058.15 N ATOM 172 CEI HISA 39 39.687-16.882-12.283 1.00 57.80 C ATOM 173 NE2HISA 39 40.040-16.751 -11.017 1.00 58.12 N ATOM 174 CD2HISA 39 39.879-17.959-10.381 1.0057.91 C ATOM 175 C HISA 39 36.801-20.174-10.088 1.0057.12 C ATOM 176 0 HIS A 39 36.415 -19.146 -9.542 1.00 57.14 0 ATOM 177 N TYRA 40 35.994 -20.938 -10.815 1.00 56.95 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 1.00 56.68 C ATOM 180 CG TYRA 40 35.005 -19.812 -13.382 1.00 56. 39 C ATOM 181 CDI TYR A 40 34.678 -18.482 -13.599 1.00 56.19 C ATOM 182 CEITYR.A 40 35.429-17692-14.438 1.00 56.13 C ATOM 183 CZ TYRA 40 36.532-18.227-15.072 1.00 56.27 C ATOM 184 OH TYRA 40 37.288-17.435-15. 910 1.00 56.35 0 ATOM 185 CE2 TYR A 40 36.884 -19.546 -14.866 1.00 55.86 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 0 TYRA 40 32.416-21.131 -10.219 1.00 56.80 0 ATOM 189 N ARG A 41 34.185 -21.710 -8.940 1 0057.29 N ATOM 190 CA ARGA 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 ARG A 41 33.747 -20.264 -6.192 1.00 59.24 C ATOM 193 CD ARGA 41 34.206-21.140 -5.036 1.0061.74 C ATOM 194 NE ARG A 41 35.654 -2 1.097 -4.852 1.00 63.78 N ATOM 195 CZ ARG A 41 36.369 -22.080 -4.309 1.00 65.07 C ATOM 196 NH1ARGA 41 37.684-21.953 -4.184 1.0065.94 N ATOM 197 NH2 ARG A 41 35.775 -23.194 -3.895 1.00 65.68 N ATOM 198 C ARGA 41 32.362-23.250 -8.179 1.0057.59 C ATOM 199 0 ARGA 41 31.245-23.266 -7.656 1.00 57.63 0 ATOM 200 N PHE A 42 32.761 -24.135 -9.085 1.00 57.42 N ATOM 201 CA PHEA 42 3 1.940 -25.247 -9.536 1.00 57.25 C ATOM 202 CB PHEA 42 32.803 -26.170-10.400 1.00 57.11 C ATOM 203 CG PHEA 42 32.033 -27.222 -11.132 1.00 56.65 C ATOM 204 CD1 PHE A 42 32.041 -28.533 -10.692 1.00 56.29 C ATOM 205 CE1 PHE A 42 31.340-29.506-11.365 1.00 56.21 C ATOM 206 CZ PHE A 42 30.623 -29.177 -12.498 1.00 56.63 C ATOM 207 CE2PHEA 42 30.611 -27.873-12.952 1.00 56.58 C ATOM 208 CD2 PHE A 42 31.315 -26.905 -12.271 1.00 56.58 C ATOM 209 C PHEA 42 31.366-26.027 -8.358 1.0057.37 C ATOM 210 0 PHE A 42 30.240 -26.520 -8.414 1.00 57.37 0 ATOM 211 N GLY A 43 32.149 -26.124 -7.288 1.00 57.54 N ATOM 212 CA GLY A 43 31.795 -26.943 -6.133 1.00 57.71 C ATOM 213 C GLY A 43 30.592 -26.473 -5.338 1.00 57.88 C *: 45 ATOM 214 0 GLYA 43 30.052-27.222 -4.525 1.00 58.01 0 ATOM 215 N SERA 44 30.171 -25.234 -5.563 1.00 57.99 N ATOM 216 CA SERA 44 29.037-24.680 -4.838 1.00 58.04 C ATOM 217 CR SERA 44 29.377 -23.298 -4.295 1.00 57.99 C ATOM 218 OG SERA 44 30.592 -23.328 -3.568 1. 00 58.35 0 ATOM 219 C SER A 44 27.824 -24.589 -5.739 1.00 58.15 C ATOM 220 0 SERA 44 26.838-23.930 -5.401 1.00 58.23 0 ATOM 221 N PHEA 45 27.900-25. 257 -6.887 1.0058.23 N : * ATOM 222 CA PHE A 45 26.845 -25.183 -7.888 1.00 58.33 C * ATOM 223 CB PHE A 45 27.270 -24.285 -9.051 1.00 58.38 C *. 55 ATOM 224 CG PHEA 45 27.111 -22.817 -8.782 1.0058.62 C * ATOM 225 CDI PHEA 45 25.873 -22.207 -8.899 1.00 58.76 C ATOM 226 CE1 PHEA 45 25.725-20.851 -8.657 1.00 58.85 C ATOM 227 CZ PHE A 45 26.822 -20.087 -8.30 1 1.00 58. 65 C ATOM 228 CE2 PHE A 45 28.063 -20.68 1 -8.189 1.00 58.80 C ATOM 229 CD2 PHE A 45 28.205 -22.039 -8.429 1.00 58.92 C ATOM 230 C PHE A 45 26.447 -26.549 -8.432 1.00 58.40 C ATOM 231 0 PHEA 45 25.269-26.809 -8.653 1.00 58.46 0 ATOM 232 N HIS A 46 27.424 -27.4 15 -8.669 1.00 58.47 N ATOM 233 CA HIS A 46 27.135 -28.696 -9.298 1.00 58.57 C ATOM 234 CB HIS A 46 27. 553 -28.677 -10.765 1.00 58.52 C ATOM 235 CG HISA 46 27.012-27.510-11.526 1. 00 58.40 C ATOM 236 ND1 HISA 46 25.756-27.510-12.093 1.00 58.69 N ATOM 237 CE1 HIS A 46 25.547 -26.35 1 -12.692 1.00 58.73 C ATOM 238 NE2 HIS A 46 26.622 -25.599 -12.532 1.00 58.60 N ATOM 239 CD2HISA 46 27.553-26.301 -11.806 1.00 58.47 C ATOM 240 C HISA 46 27.804-29.851 -8.577 1.0058.82 C ATOM 241 0 HIS A 46 27.13 1 -30.724 -8.041 1.00 58.94 0 ATOM 242 N SERA 47 29.130-29.859 -8.561 1.005914 N ATOM 243 CA SER A 47 29.856 -30.936 -7. 907 1.00 59.57 C ATOM 244 CB SERA 47 30.256 -32.001 -8.924 1.00 59.49 C ATOM 245 00 SER A 47 29.254 -32.992 -9.030 1.00 59.64 0 ATOM 246 C SERA 47 3 1.089 -30.454 -7.160 1.00 59.92 C ATOM 247 0 SERA 47 31.799 -29.566 -7. 632 1.00 60.08 0 ATOM 248 N PRO A 48 3 1.348 -3 1.043 -5.984 1.00 60.20 N ATOM 249 CA PRO A 48 32.579 -30.774 -5.254 1.00 60.54 C ATOM 250 CB PRO A 48 32.350 -3 1.470 -3.916 1.00 60.46 C ATOM 251 CG PROA 48 3 1.373 -32.544 -4.219 1.00 60.43 C ATOM 252 CD PRO A 48 30.483 -32.004 -5.283 1.00 60.14 C ATOM 253 C PRO A 48 33.749 -3 1.409 -5.991 1.00 60.95 C ATOM 254 0 PROA 48 33.537-32.221 -6.893 1.0061.07 0 ATOM 255 N ALAA 49 34.970-31.039 -5.624 1.0061.39 N ATOM 256 CA ALA A 49 36.149 -3 1.565 -6.306 1.00 61.81 C ATOM 257 CB ALAA 49 37.387-30.779 -5.919 1.00 61.89 C ATOM 258 C ALA A 49 36.341 -33.046 -6.011 1.00 62.05 C ATOM 259 0 ALAA 49 36.042-33.508 -4.914 1.00 61.90 0 ATOM 260 N LEUA 50 36.846-33.778 -6.999 1.00 62.63 N ATOM 261 CA LEU A 50 37.017 -35.224 -6.900 1.00 63.26 C ATOM 262 CB LEU A 50 37.169 -35.826 -8.30 1 1.00 63.16 C ATOM 263 CG LEU A 50 36.104 -35. 424 -9 330 1.00 63.07 C ATOM 264 CD1 LEU A 50 34.733 -35.875 -8.873 1.00 63. 12 C ATOM 265 CD2 LEU A 50 36.4 10 -35.978 -10.7 17 1.00 62.96 C ATOM 266 C LEU A 50 38.213 -35.607 -6.020 1.00 63.95 C ATOM 267 0 LEU A 50 39.139 -34.817 -5.836 1.00 64.09 0 ATOM 268 N GLU A 51 38.181 -36.820 -5.469 1. 00 64.70 N ATOM e269 CA GLU A 51 39.296 -37.346 -4.683 1.00 65.43 C : ... ATOM 270 CS GLUA 51 38.780-37.991 -3.401 1.00 65.54 C ATOM 271 CO GLUA 51 37.576-37.302 -2.788 1.00 66.38 C ATOM 272 CD GLUA 51 36.647-38.289 -2. 106 1.0067.59 C ATOM 273 OE1 GLU A 51 36.443 -39.386 -2.671 1.00 68.33 0 a... ATOM 274 OE2GLUA 51 36.120-37.976 -1.013 1.0068.07 0 * * *** ATOM 275 C GLUA 51 40.026-38.398 -5.510 1.0065.74 C : ATOM 276 0 GLUA 51 39.716-38.592 -6.682 1.0065.83 0 * 50 ATOM 277 N ASPA 52 40.989-39.086 -4906 1.0066.11 N ATOM 278 CA ASP A 52 4 1.614 -40.222 -5.57 1 1.00 66.50 C : *. ATOM 279 CB ASPA 52 42.961 -40.543 -4.936 1.00 66.58 C ATOM 280 CG ASPA 52 44.008-39.495 -5.242 1.00 67.19 C ATOM 281 ODI ASP A 52 43.632 -38.386 -5.689 1.00 67.73 0 * 55 ATOM 282 0D2 ASP A 52 45.210 -39.782 -5.040 1.00 67.86 0 ATOM 283 C ASP A 52 40.687 -41.420 -5.465 1.00 66.69 C ATOM 284 0 ASP A 52 40.773 -42.377 -6.245 1.00 66.73 0 ATOM 285 N ALA A 53 39.783 -41.341 -4.495 1.00 66.92 N ATOM 286 CA ALA A 53 38.878 -42.436 -4.184 1.00 67.19 C ATOM 287 CB ALAA 53 38.099-42.128 -2.914 1.00 67.25 C ATOM 288 C ALAA 53 37.930-42.772 -5.331 1.0067.26 C ATOM 289 0 ALAA 53 37.550-43.926 -5.503 1.0067.24 0 ATOM 290 N ASPA 54 37.543-41.771 -6.113 1.0067.45 N ATOM 291 CA ASP A 54 36.663 -42.028 -7.25 1 1.00 67.74 C ATOM 292 CB ASP A 54 35.641 -40.899 -7.467 1.00 67.90 C ATOM 293 CG ASPA 54 36.161 -39.544 -7.036 1.00 68.67 C ATOM 294 ODI ASPA 54 37.398-39.378 -6.970 1.00 69.79 0 ATOM 295 OD2ASPA 54 35.333-38.646 -6.758 1.0069.03 0 ATOM 296 C ASPA 54 37.458-42.329 -8.520 1.0067.62 C ATOM 297 0 ASPA 54 36.900-42.378 -9.618 1.0067.85 0 ATOM 298 N PHE A 55 38.762 -42 532 -8. 353 1.00 67.33 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 1.00 67.01 C ATOM 301 CO PHE A 55 40.448 -40.743 -10.259 1.00 66.79 C ATOM 302 CD1 PHE A 55 40.078 -39.670 -9.471 1.00 66.59 C ATOM 303 CEI PHE A 55 39.754 -38.459 -10.037 1.00 66.30 C ATOM 304 CZ PHE A 55 39.800 -38.306 -11.403 1.00 66.49 C ATOM 305 CE2PHEA 55 40.171 -39.366-12.200 1.0066.62 C ATOM 306 CD2 PHE A 55 40.495 -40.576 -11.628 1.00 66.65 C ATOM 307 C PHEA 55 40.136-44.396 -9.151 1.0066.92 C ATOM 308 0 PHE A 55 40.288 -45.209 -10.061 1.00 66.88 0 ATOM 309 N ASP A 56 40.4 15 -44.669 -7.879 1.00 66.74 N ATOM 310 CA ASP A 56 41.024 -45. 940 -7.491 1.00 66.60 C ATOM 311 CB ASPA 56 42.316-45.690 -6.707 1.0066.71 C ATOM 312 CO ASP A 56 43.344 -44.905 -7.504 1.00 67.09 C ATOM 313 ODI ASP A 56 43.364 -45.043 -8.747 1.00 67.21 0 ATOM 314 0D2 ASP A 56 44.135 -44. 153 -6.886 1.00 67.60 0 ATOM 315 C ASP A 56 40.091 -46.835 -6.674 1.00 66.36 C ATOM 316 0 ASPA 56 40.544-47.576 -5.801 1.0066.42 0 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 GLY A 57 37.046 -48.534 -7.006 1.00 65.47 C ATOM 320 0 GLY A 57 36.955 -48.408 -8.227 1.00 65.50 0 ATOM 321 N LYS A 58 36.485 -49.535 -6.331 1.00 65.22 N ATOM 322 CA LYS A 58 35.74 1 -50.602 -7.000 1.00 64.95 C ATOM 323 CB LYS A 58 35.422 -5 1.734 -6.019 1.006495 C ATOM 324 CG LYS A 58 36.409 -52.886 -6.068 1.00 65.08 C ATOM 325 CD LYS A 58 36.4 19 -53.661 -4.763 1.00 65.47 C ATOM 326 CE LYSA 58 35.019-54.076 -4.348 1.00 65.82 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 1.00 64.68 C ATOM 329 o LYSA 58 33.691 -49.365 -7.019 1.00 64.72 0 s..., 45 ATOM 330 N PROA 59 34.226-50.484 -8.913 1.00 64.36 N ATOM 331 CA PRO A 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 CO PROA 59 34.179-51.939-10.707 1.00 64.14 C ATOM 334 CD PROA 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 * S ATOM 336 0 PROA 59 31.643-51.438 -8.205 1.0063.99 0 * ** 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 1.00 63.49 C ** , ATOM 339 CB META 60 29.069-48.382 -7.572 1.0063.41 C . ,: 55 ATOM 340 CO META 60 29.977-47. 957 -6.428 1.0063.33 C ATOM 341 SD MET A 60 30.125 -46.152 -6.292 1.00 63.57 S ATOM 342 CE META 60 30.571 -45.961 -4.564 1.00 63.70 C ATOM 343 C META 60 28.435-49.986 -9.363 1.00 63.31 C ATOM 344 0 MET A 60 28.549 -49.526 -10 496 1.00 63.29 0 ATOM 345 N VALA 61 27.428-50.779 -9.012 1.0063.07 N ATOM 346 CA VAL A 61 26.204 -50.802 -9.8 10 1.0062.97 C ATOM 347 CB VALA 61 25.898-52.180-10.449 1.0062.87 C ATOM 348 CGI VALA 61 27.161-52.805-10. 997 1.00 62.90 C ATOM 349 CG2VALA 61 25241 -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 0 VALA 61 25.021 -50.612 -7.722 1.00 63.16 0 ATOM 352 N LEUA 62 24.115-49.599 -9.523 1.0062.78 N ATOM 353 CA LEU A 62 22.993 -49,062 -8.769 1.00 62.54 C ATOM 354 CB LEU A 62 22.929 -47.541 -8.896 1.00 62.51 C ATOM 355 CG LEUA 62 21.760-46.869 -8.168 1.0062.61 C ATOM 356 CDI LEUA 62 22.157-45.506 -7. 620 1.00 62.58 C ATOM 357 CD2 LEU A 62 20.545 -46.751 -9.077 1.00 62.83 C ATOM 358 C LEUA 62 21.684-49675 -9.218 1.00 62.41 C ATOM 359 0 LEUA 62 21.380-49.715-10.410 1.0062.37 0 ATOM 360 N VAL A 63 20.907 -50.148 -8. 252 1.00 62.32 N ATOM 361 CA VAL A 63 19.608 -50.73 1 -8.544 1.00 62.19 C ATOM 362 CB VALA 63 19.468-52.128 -7.927 1.0062.15 C ATOM 363 CG1 VALA 63 18.208-52.787 -8.436 1.00 62.50 C ATOM 364 CG2 VAL A 63 20.684 -52.982 -8.265 1.00 61.99 C ATOM 365 C VALA 63 18.481 -49.830 -8.046 1.00 62.07 C ATOM 366 0 VAL A 63 18.360-49.577 -6.847 1.00 61.99 0 ATOM 367 N ALAA 64 17.666-49.344 -8.978 1.0062.00 N ATOM 368 CA ALA A 64 16.562 -48.446 -8.651 1.00 61.93 C ATOM 369 CB ALA A 64 16.855 -47.043 -9.141 1.00 61.86 C ATOM 370 C ALA A 64 15.266 -48.949 -9.257 1.00 61.87 C ATOM 371 0 ALA A 64 15.275 -49.792 -10.146 1.00 62.00 0 ATOM 372 N GLYA 65 14.153-48.418 -8.777 1.0061.82 N ATOM 373 CA GLY A 65 12.838 -48.820 -9.250 1.00 62.04 C ATOM 374 C GLY A 65 11.837-48.413 -8.194 1.00 62.30 C ATOM 375 0 GLYA 65 12.228-47.955 -7.118 1.006242 0 ATOM 376 N GLN A 66 10.549 -48.562 -8.478 1.0062.45 N ATOM 377 CA GLNA 66 9.560-48.233 -7.464 1.0062.73 C ATOM 378 CB GLNA 66 8.301 -47.616 -8.067 1.00 62.81 C ATOM 379 CG GLN A 66 7.858 -48.190 -9.387 1.00 63.71 C ATOM 380 CD GLNA 66 6.754-47.355-10.012 1.00 64.68 C ATOM 381 OEI GLN A 66 5.905 -46.794 -9.305 1.00 65.17 0 ATOM 382 NE2 GLN A 66 6.760 -47.264 -11.340 1.00 65.07 N ATOM 383 C GLN A 66 9.240 -49.424 -6.577 1.00 62.78 C ATOM 384 0 GLN A 66 9.877 -50.470 -6.685 1 00 62.88 0 ATOM 385 N TYRA 67 8.263 -49.258 -5.694 1.00 62.88 N ATOM 386 CA TYR A 67 7.972 -50.258 -4.673 1.00 62.98 C : ... ATOM 387 CB TY'RA 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 CD! TYRA 67 6.105-47.566 -2.918 1.0064.41 C ATOM 390 CE! TYR A 67 6.324 -46.45! -2.112 1.00 64.56 C ATOM 39! CZ TYRA 67 7.470-46.381 -1.336 1.0064.29 C ATOM 392 OH TYRA 67 7.695 -45.278 -0.537 1.00 64.28 0 : 50 ATOM 393 CE2TYRA 67 8.389-47.414 -1.356 1.0064.30 C * ATOM 394 CD2 TYRA 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 0 TYRA 67 7.053-51.824 -6.246 1.00 62.73 0 ATOM 397 N SERA 68 8.293-52.648 -4.550 1.0062.73 N * . : 55 ATOM 398 CA SER A 68 8.040 -54.060 -4.830 1.00 62.58 C ATOM 399 CB SER A 68 6.600 -54.438 -4.459 1.00 62.63 C ATOM 400 OG SER A 68 6.339 -54.184 -3.086 1.0062 93 0 ATOM 401 C SERA 68 8.328 -54 439 -6.272 1.00 62.40 C ATOM 402 0 SERA 68 7.649-55.288 -6.848 1.0062.68 0 ATOM 403 N TI-IRA 69 9.338-53.814 -6.858 1.00 61.97 N ATOM 404 CA TI-IRA 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 406 001 THRA 69 9.623 -51.719 -8.480 1.00 61.90 0 ATOM 407 CG2 THR A 69 10.026 -53.030 -10.435 1.00 62.25 C ATOM 408 C THRA 69 10.712-55.266 -8.232 1.00 61.26 C ATOM 409 0 THRA 69 11.031 -55.832 -9. 276 1.00 61.25 0 ATOM 410 N GLY A 70 11.222 -55.596 -7.053 1.00 60.94 N ATOM 411 CA GLY A 70 12.143 -56.715 -6.910 1.00 60.52 C ATOM 412 C GLYA 70 13.612-56.350 -6.934 1.0060.22 C ATOM 413 0 GLY A 70 14.435 -57.156 -7. 334 1.00 60.21 0 ATOM 414 N LYSA 71 13.950-55.138 -6.507 1.0060.02 N ATOM 415 CA LYSA 71 15.344-54.712 -6.478 1.0059.94 C ATOM 416 CB LYSA 71 15.440-53.272 -5.986 L0059.83 C ATOM 417 CG LYSA 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 1.00 58.14 C ATOM 420 NZ LYSA 71 13.111 -50.011 -4.562 1.00 57.62 N ATOM 421 C LYSA 71 16.170-55.620 -5.570 1.0060.06 C ATOM 422 0 LYSA 71 17.156-56.244 -5.998 1.0060.25 0 ATOM 423 N THRA 72 15.754 -55.686 -4.309 1.00 60.04 N ATOM 424 CA THR A 72 16.436 -56.494 -3.3 14 1.00 60.09 C ATOM 425 CB THRA 72 15.698-56.451 -1.955 1.0060.10 C ATOM 426 001 THR A 72 15.224 -55.121 -1.703 1.00 60.02 0 ATOM 427 CG2 THR A 72 16.626 -56.878 -0.824 1.00 60.05 C ATOM 428 C THRA 72 16.548-57.931 -3.814 1.00 60.14 C ATOM 429 0 THR A 72 17.605 -58.562 -3.702 1.00 60.40 0 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 1.00 60.22 C ATOM 432 CB SER A 73 14.064 -60.131 -5.502 1.00 60.26 C ATOM 433 00 SER A 73 13.120 -60.336 -4.462 1.00 59.98 0 ATOM 434 C SERA 73 16.501 -59.901 -6.027 1.00 60.19 C ATOM 435 0 SERA 73 17.298 -60.825 -6.042 1.00 60.56 0 ATOM 436 N PHEA 74 16.496-58.942 -6.936 1.00 60.20 N ATOM 437 CA PHEA 74 17.456-58.885 -8. 016 1.0060.14 C ATOM 438 CB PHE A 74 17.294 -57.558 -8.748 1.00 60.03 C ATOM 439 CO PHE A 74 18.223 -57.383 -9.900 1.00 60.15 C ATOM 440 CDI PHE A 74 18.013 -58.066-11.083 1.00 60.37 C ATOM 441 CE1 PHE A 74 18.866 -57.899 -12.147 1.00 60.41 C ATOM 442 CZ PHE A 74 19.937 -57.033 -12.040 1.00 60.50 C ATOM 443 CE2 PHE A 74 20.148 -56.342 -10.870 1.00 60.12 C ATOM 444 CD2 PHE A 74 19.297 -56.517 -9.810 1.00 60.02 C * ATOM 445 C PHE A 74 18.876 -59.038 -7.486 1.00 60.19 C ATOM 446 0 PHE A 74 19.623 -59.913 -7.925 1.00 60.38 0 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 ILEA 75 20.862 -57.131 -4.989 1.00 60.26 C ATOM 450 CG1 ILEA 75 20.540-55.781 -5.625 1.00 60.08 C ATOM 451 CD1 ILEA 75 20.666-54.622 -4.673 1.00 59.79 C ATOM 452 CG2 ILE A 75 22.305 -57.159 -4.530 1.00 60.22 C * *, ATOM 453 C ILEA 75 20.850-59.613 -5.324 1.0060.71 C ATOM 454 0 ILEA 75 21.862-60.278 -5.584 1.0061.02 0 *. * ATOM 455 N GLNA 76 19.915 -60.007 -4.464 1.00 60.91 N *. .: 55 ATOM 456 CA GLNA 76 19.933-61.311 -3.814 1.00 61.22 C ATOM 457 CB GLN A 76 18.538 -61.595 -3.263 1.00 61.23 C ATOM 458 CO 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 OEI GLN A 76 17.409 -62.972 -0.176 1.00 63.47 0 ATOM 461 NE2 GLN A 76 18.873 -61.282 -0.471 1.00 63.36 N ATOM 462 C GLN A 76 20.292 -62.38 1 -4.840 1.00 61.30 C ATOM 463 0 GLN A 76 21.096-63. 280 -4.589 1.0061.68 0 ATOM 464 N 1'YR A 77 19.678 -62.242 -6.009 1.00 61.31 N ATOM 465 CA TYRA 77 19.786-63.181 -7.115 1.0061.46 C ATOM 466 CB TYR A 77 18.682 -62.874 -8.125 1.00 61.45 C ATOM 467 CG TYR A 77 18.636 -63.776 -9.326 1.00 61.46 C ATOM 468 CD1 TYRA 77 18.978-63.300-10.583 1.00 61.59 C ATOM 469 CE1TYRA 77 18.919-64.117-11.698 1.0061.89 C ATOM 470 CZ TYRA 77 18.512-65.428-11.559 1.006181 C ATOM 471 OH TYR A 77 18.455 -66.244 -12.661 1.00 61.74 0 ATOM 472 CE2 TYR A 77 18.163 -65.923 -10.318 1.00 61.90 C ATOM 473 CD2 TYR A 77 18.227 -65.097 -9.212 1.00 61.71 C ATOM 474 C TYRA 77 21.145-63.093 -7.791 1.0061.48 C ATOM 475 0 TYRA 77 21.713-64.112 -8.184 1.00 61.51 0 ATOM 476 N LEUA 78 21.659-61.874 -7.936 1.00 61.31 N ATOM 477 CA LEUA 78 22.991 -61.687 -8.493 1.00 61.65 C ATOM 478 CB LEU A 78 23.306 -60.206 -8.664 1.00 61.70 C ATOM 479 CO LEUA 78 22.978-59.629-10.039 1.0062.28 C ATOM 480 CD! LEUA 78 23.121-58.112-10. 024 1.00 62.88 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 1.00 61.78 C ATOM 483 0 LEUA 78 24.988-62.939 -8.069 1.0061.79 0 ATOM 484 N LEU A 79 23.837 -62.181 -6. 292 1.00 61.84 N ATOM 485 CA LEU A 79 24.798 -62.702 -5.34 1 1.00 62.22 C ATOM 486 CB LEU A 79 24.754 -61.888 -4.051 1.00 62.29 C ATOM 487 CO LEUA 79 25.012-60.386 -4.176 1.00 62.42 C ATOM 488 CDI LEU A 79 25.014 -59.736 -2.800 1.00 62.58 C ATOM 489 CD2 LEU A 79 26.324 -60.120 -4.896 1.00 62. 69 C ATOM 490 C LEUA 79 24.547-64.168 -5.032 1.00 62.47 C ATOM 491 0 LEU A 79 25.397 -64.833 -4.439 1.00 62.39 0 ATOM 492 N GLUA 80 23.383-64.668 -5. 440 1.0062.76 N ATOM 493 CA GLU A 80 22.942 -66.001 -5.034 1.00 63.58 C ATOM 494 CB GLU A 80 23.637 -67.091 -5.852 1.00 63.72 C ATOM 495 CO GLUA 80 23.051 -67.293 -7.250 1.00 65.58 C ATOM 496 CD GLU A 80 22.042 -68.443 -7.324 1.00 68.13 C ATOM 497 OEI GLUA 80 22.412-69.522 -7.867 1.00 69.12 0 ATOM 498 0E2 GLU A 80 20.888 -68.278 -6.838 1.00 68.88 0 ATOM 499 C GLUA 80 23.214-66.180 -3.544 1.00 63.57 C ATOM 500 0 GLUA 80 23.706-67.219 -3.106 1.00 63.47 0 ATOM 501 N GLNA 81 22.899-65.133 -2.784 1.00 63.78 N ATOM 502 CA GLNA 81 23.086-65.106 -1.342 1.0063.93 C ATOM 503 CB GLN A 81 24.562-64.900 -0.993 1.00 63.84 C * 45 ATOM 504 CO GLN A 81 24.847 -64. 947 0.504 1.00 63.39 C ATOM 505 CD GLN A 81 26.324-64.864 0.824 1.00 62.75 C ATOM 506 OE1GLNA 81 26.739-65.199 1.929 1.00 63.13 0 ATOM 507 NE2 GLN A 81 27.127 -64.417 -0.137 1.00 62.73 N ATOM 508 C GLNA 81 22.239-63.987 -0. 731 1.00 64.17 C ATOM 509 0 GLN A 81 22.026 -62.952 -1.361 1.00 64.15 0 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 1.00 64.72 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 1.00 65.36 C ** * 55 ATOM 514 CD GLUA 82 17.597-63.996 2.870 1.0066.14 C *. .: ATOM 515 OEI GLU A 82 17.685 -65.080 3.490 1.00 66.18 0 ATOM 516 OE2GLUA 82 16.520-63.591 2.372 1.0066.28 0 ATOM 517 C GLUA 82 21.732-62.057 1.748 1.0064.81 C ATOM 518 0 GLU A 82 22.863 -62.233 2.202 1.00 64.77 0 ATOM 519 N VA!. A 83 2 1.152 -60.862 1.705 1.00 64.99 N ATOM 520 CA VAL A 83 21. 825 -59.654 2.169 1.00 65.07 C ATOM 521 CB VAL A 83 21.294 -58.413 1.439 1.00 65.06 C ATOM 522 CG1 VALA 83 22.242-57.244 1.628 1.00 65.06 C ATOM 523 CG2 VAL A 83 21.098 -58.712 -0.036 1.00 64.87 C ATOM 524 C VALA 83 21.638-59.465 3.673 1.0065.23 C ATOM 525 0 VAL A 83 20.509 -59.404 4.157 1.00 65.10 0 ATOM 526 N PRO A 84 22.752 -59.365 4.4 14 1.00 65.51 N ATOM 527 CA PROA 84 22.753 -59.247 5.869 1.00 65.77 C ATOM 528 CB PROA 84 24.156-58.723 6.168 1.0065.66 C ATOM 529 CO PRO A 84 24.990 -59.315 5.100 1.00 65.56 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 0 PRO A 84 20.987 -58.603 7.342 1.00 66.22 0 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 1.00 67.21 C ATOM 535 C GLYA 85 19.347-56.044 5.581 1.0067.67 C ATOM 536 0 GLYA 85 18.320-55.785 6.211 1.0067.61 0 ATOM 537 N SERA 86 19.348 -56.313 4.278 1.00 68.17 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 00 SER A 86 18.520 -54.297 1.904 1.00 68.90 0 ATOM 541 C SERA 86 17.225-57.374 3.398 1.00 69.01 C ATOM 542 0 SERA 86 17.554-58.386 2.769 1.00 69.11 0 ATOM 543 N ARG A 87 16.065 -57.263 4.044 1.00 69.32 N ATOM 544 CA ARGA 87 15.015-58.266 3.918 1.00 69.63 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 0.00 50.00 C ATOM 547 CD ARGA 87 14.525-60.115 7.110 0.00 50.00 C ATOM 548 NE ARG A 87 13.769 -61.343 6. 893 0.00 50.00 N ATOM 549 CZ ARG A 87 14.263 -62.572 6.969 0.00 50 00 C ATOM 550 NH1 ARG A 87 13.467 -63.609 6.740 0.00 50.00 N ATOM 551 NH2ARGA 87 15.528-62.779 7.297 0.0050.00 N ATOM 552 C ARG A 87 14.18 1 -57.999 2.661 1.00 69.92 C ATOM 553 0 ARG A 87 14.475 -57.085 1.888 1.00 69.93 0 ATOM 554 N VAL A 88 13.143 -58.803 2.461 1.00 70.32 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 CG1 VALA 88 11.662-59.875 -0.855 1.00 70.52 C ATOM 558 CG2VALA 88 13.398-60.855 0.661 1.0070.76 C ATOM 559 C VALA 88 10.836-59.035 1.655 1.0070.97 C ATOM 560 0 VALA 88 10.594-59.997 2.389 1.0071.03 0 ATOM 561 N GLYA 89 9.881 -58.255 1.157 1.00 71.28 N *.: 45 ATOM 562 CA GLYA 89 8.480-58.471 1.506 1.0071.78 C ATOM 563 C GLYA 89 7.485-57.882 0.527 1.0072.17 C ATOM 564 0 GLY A 89 7.873 -57.243 -0.451 1.00 72.08 0 ATOM 565 N PROA 90 6.184-58.087 0.798 1.00 72.59 N ATOM 566 CA PROA 90 5.083-57.648 -0.065 1.00 72.92 C ATOM 567 CB PROA 90 3.845 -58.251 0.610 1.00 72.90 C * ATOM 568 Co PRO A 90 4.24 1 -58.441 2.04 1 1.00 72.85 C ATOM 569 CD PROA 90 5.703 -58.771 2.013 1.00 72.65 C : *. ATOM 570 C PROA 90 4977 -56.126 -0.118 1.00 73.27 C ATOM 571 0 PROA 90 5.542-55.499 -1.017 1.0073.27 0 *. 55 ATOM 572 N GLUA 91 4.254-55.546 0.838 1.0073.71 N * ATOM 573 CA GLU A 91 4.167.54.094 0.976 1.00 74 09 C ATOM 574 CB GLUA 91 3.095-53.714 2.008 1.00 74.13 C ATOM 575 CO GLU A 91 1.660 -53.941 1.538 1.00 74.32 C ATOM 576 CD GLU A 91 1.490 -53.220 -0. 578 0.00 50.00 C ATOM 577 OEI GLU A 91 0.483 -53.953 -0.666 0.00 50.00 0 ATOM 578 OE2 GLU A 91 2.188 -52.915 -1.575 0.00 50.00 0 ATOM 579 C GLUA 91 5.529-53.526 1.387 1.00 74.25 C ATOM 580 0 GLU A 91 6.255 -54.168 2.15 1 1.00 74.34 0 ATOM 581 N PRO A 92 5.874 -52.323 0.876 1.00 74.34 N ATOM 582 CA PROA 92 7.138-51.615 1.101 1.0074.34 C ATOM 583 CB PROA 92 6.734 -50.133 0.987 1.00 74.35 C ATOM 584 CG PRO A 92 5.317 -50.122 0.401 1.00 74.33 C ATOM 585 CD PROA 92 4.987-51.535 0.006 1.0074.39 C ATOM 586 C PRO A 92 7.772 -5 1.884 2.471 1.00 74.33 C ATOM 587 0 PRO A 92 7.109 -51.737 3.508 1.00 74.31 0 ATOM 588 N THR A 93 9.052 -52.260 2.465 1.00 74.15 N ATOM 589 CA TI-IRA 93 9.754-52.645 3.695 1.0073.95 C ATOM 590 CU THRA 93 10.189-54.133 3.657 1.0074.06 C ATOM 591 OGITHRA 93 10.591-54.490 2.311 1.0073.87 0 ATOM 592 CG2 THR A 93 9.031 -55.058 4.114 1.00 74.23 C ATOM 593 C THR A 93 10.968 -5 1.770 4.024 1.00 73.59 C ATOM 594 0 THR A 93 10.972 -5 1.057 5.034 1.00 73.58 0 ATOM 595 N THRA 94 11.993-51.839 3.172 1.00 73.13 N ATOM 596 CA THRA 94 13.241-51.097 3.381 1.0072.66 *C ATOM 597 CB THR A 94 14.380 -5 1.644 2.474 1.00 72.80 C ATOM 598 OGI THRA 94 13.974-51.598 1.095 1.00 72.65 0 ATOM 599 CG2THRA 94 14.720-53.088 2.846 1.00 72.95 C ATOM 600 C THRA 94 13.058-49.593 3.137 1.0072.18 C ATOM 601 0 THRA 94 12.441-49.188 2.150 1.0072.21 0 ATOM 602 N ASP A 95 13.600 -48. 767 4.03 1 1.00 71.45 N ATOM 603 CA ASPA 95 13.381 -47.320 3.956 1.00 70.73 C ATOM 604 CB ASP A 95 12.585 -46.839 5.180 1.00 70.79 C ATOM 605 CO ASP A 95 12.336 -46.932 5.763 0.00 50.00 C ATOM 606 OD1 ASP A 95 12.950 -47.842 6.397 0.00 50.00 0 ATOM 607 0D2 ASP A 95 11.658 -46.098 6.4 18 0.00 50.00 0 ATOM 608 C ASP A 95 14.665 -46.498 3.814 1.00 70.16 C ATOM 609 0 ASP A 95 14.73 8 -45.367 4.304 1 00 70.07 0 ATOM 610 N CYSA 96 15.665-47.052 3.131 1.00 69.46 N ATOM 611 CA CYS A 96 16.933 -46.343 2.957 1.00 68.81 C ATOM 612 CB CYSA 96 17.698-46.296 4.282 1.0068.91 C ATOM 613 SO CYSA 96 18.497-47.853 4.720 1.0069.45 S ATOM 614 C CYS A 96 17.834 -46.935 1.869 1.00 68.20 C ATOM 615 0 CYSA 96 17.435-47.834 1.130 1.0068.12 0 ATOM 616 N PHE A 97 19.053 -46.408 1.785 100 67.48 N ATOM 617 CA PHE A 97 20.049 -46.870 0.830 1.00 66.69 C ATOM 618 CB PHEA 97 20.914-45.706 0.345 1.0066.64 C ATOM 619 CO PI-JE A 97 20.172 -44.689 -0.467 1.00 66.32 C * 45 ATOM 620 CD1 PHE A 97 19.322 -43.780 0.142 1.00 66.08 C ATOM 621 CEI PHEA 97 18.640-42.841 -0.602 1.00 65.88 C ATOM 622 CZ PHEA 97 18.811 -42.793 -1.968 1.00 66.18 C ATOM 623 CE2PHEA 97 19.662-43.688 -2.588 1.00 66.18 C *****. ATOM 624 CD2 PHE A 97 20.339 -44.627 -1.838 1.00 66.18 C ATOM 625 C PHE A 97 20.950 -47.902 1.482 1.00 66.32 C ATOM 626 0 PHEA 97 21.532-47.657 2.538 1.0066.17 0 ATOM 627 N VAL A 98 2 1.068 -49.056 0.843 1.00 65.88 N * ** ATOM 628 CA VAL A 98 21.934 -50.108 1.335 1.00 65.43 C ATOM 629 CB VALA 98 21.178-51.438 1.474 1.00 65.36 C *. * 55 ATOM 630 CGI VALA 98 22.070-52.488 2.108 1.00 65.18 C ATOM 631 CG2 VALA 98 19.913 -51.243 2.288 1.00 65.13 C ATOM 632 C VALA 98 23.090-50.287 0.368 1.0065.26 C ATOM 633 0 VAL A 98 22.889 -50.620 -0.797 1.00 65.27 0 ATOM 634 N ALA A 99 24.30 1 -50.050 0.849 1.0065.07 N ATOM 635 CA ALA A 99 25.478 -50.225 0022 1.00 65.02 C ATOM 636 CB ALA A 99 26.521 -49.179 0. 359 1.00 65.00 C ATOM 637 C ALAA 99 26.039-51.619 0.225 1.0065.03 C ATOM 638 0 ALA A 99 26.838 -51.847 1.129 1.00 65.09 0 ATOM 639 N VALA 100 25.609-52.555 -0.609 1.00 65.12 N ATOM 640 CA VAL A 100 26.105 -53.922 -0.520 1.00 65.24 C ATOM 641 CB VAL A 100 25 193 -54.9 14 -1.267 1.00 65.20 C ATOM 642 CG1 VAL A 100 23.733 -54.672 -0.914 1.00 65.10 C ATOM 643 CG2VALA 100 25.600-56.345 -0.952 1.00 65.15 C ATOM 644 C VAL A 100 27.5 12 -53.995 -1.097 1.00 65.39 C ATOM 645 0 VALA 100 27.699-53.938 -2.313 1.0065.48 0 ATOM 646 N META 101 28.501 -54.107 -0.218 1.00 65.56 N ATOM 647 CA MET A 101 29.894 -54.16 1 -0.638 1.00 65.78 C ATOM 648 CB META 101 30.600-52.850 -0.311 1.00 65.79 C ATOM 649 CG META 101 30.252-52.294 1. 058 1.00 65.81 C ATOM 650 SD META 101 31.344 -50.959 1.580 1.00 65.65 S ATOM 651 CE META 101 31.250-49.849 0.175 1.00 65.57 C ATOM 652 C MET A 101 30. 6 10 -55.3 17 0.034 1.00 66.02 C ATOM 653 0 META 101 30.052 -55.978 0.907 1.00 66.05 0 ATOM 654 N HISA 102 31.850-55.559 -0.369 1.00 66.39 N ATOM 655 CA HISA 102 32.607-56.667 0.190 1.00 66.80 C ATOM 656 CB HISA 102 33.918-56.881 -0.569 1.00 66.73 C ATOM 657 CG HIS A 102 34.629 -58.142 -0.189 1.00 66.79 C ATOM 658 ND1 HISA 102 34.164-59.392 -0.540 1.0066.68 N ATOM 659 CE! HIS A 102 34.983 -60.3 13 -0.064 1.00 66.49 C ATOM 660 NE2 HIS A 102 35.961 -59.706 0.586 1.00 66.63 N ATOM 661 CD2 HIS A 102 35.762 -58.347 0.525 1.00 66.78 C ATOM 662 C HIS A 102 32.873 -56.459 1.678 1.00 67.13 C ATOM 663 0 HISA 102 32.449-55.465 2.262 1.00 67.23 0 ATOM 664 N GLY A 103 33.572 -57.408 2.285 1.00 67.46 N ATOM 665 CA GLYA 103 33.879-57.341 3.700 1.00 67.99 C ATOM 666 C GLYA 103 34.212-58.729 4.186 1.00 68.39 C ATOM 667 0 GLY A 103 33.727 -59.7 15 3.636 1.00 68.41 0 ATOM 668 N GLUA 104 35.045-58.812 5.216 1.0068.82 N ATOM 669 CA GLU A 104 35.493 -60.105 5.708 1.00 69.31 C ATOM 670 CB GLU A 104 36.829 -59.968 6.450 1.00 69.45 C ATOM 671 CG GLU A 104 37.433 -61.291 6.923 1.00 70.31 C ATOM 672 CD GLUA 104 37.326-62.41! 5.885 1.0071.40 C ATOM 673 OE! GLU A 104 36.942 -62.136 4.723 1.00 71.64 0 ATOM 674 OE2GLUA 104 37.624-63.575 6.240 1.00 71.78 0 ATOM 675 C GLU A 104 34.434 -60.790 6 577 1.00 69.42 C ATOM 676 0 GLU A 104 34.245 -62.007 6.501 1.00 69.49 0 * ATOM 677 N THRA 105 33.737-60.003 7.389 1.0069.53 N ATOM 678 CA THRA 105 32.69! -60.542 8.248 1.00 69.56 C ATOM 679 CB THRA 105 32.845 -60.049 9.707 1.00 69.61 C ATOM 680 OGI TI-IR A 105 32.017 -60.837 10.572 1.00 69.65 0 ATOM 681 CG2 THR A 105 32.457 -58.573 9.830 1.00 69.72 C ATOM 682 C THRA 105 31.305-60.172 7.723 1.0069.52 C ATOM 683 0 THRA!05 31.111-59.099 7.147 1.0069.53 0 ATOM 684 N GLUA 106 30.349-61.075 7.909 1.00 69.46 N * ** ATOM

685 CA GLUA 106 28.960-60.778 7.594 1.00 69.46 C ATOM 686 CB GLUA 106 28.137-62.066 7.517 1.0069.51 C ** * ATOM 687 CO GLU A 106 28.455 -62.949 6.3 15 1.00 69.53 C ATOM 688 CD GLUA 106 27.789-64.318 6.394 1.00 69.39 C ATOM 689 OE! GLUA 106 27.490-64.754 7.573 1.00 69.37 0 ATOM 690 OE2GLUA 106 27.562-64.963 5.282 1.00 68.93 0 ATOM 691 C GLU A 106 28.399 -59.863 8.674 1.00 69.46 C ATOM 692 0 GLU A 106 28.645 -60.073 9.860 1.00 69.46 0 ATOM 693 N GLY A 107 27.650 -58.845 8.265 1.00 69.47 N ATOM 694 CA GLY A 107 27.084 -57.896 9.216 1.00 69.50 C ATOM 695 C GLYA 107 26.766-56.551 8.593 1.0069.52 C ATOM 696 0 GLYA 107 26.771 -56.407 7.370 1.00 69.51 0 ATOM 697 N THRA 108 26.489-55.562 9.439 1.0069.51 N ATOM 698 CA THR A 108 26.095 -54.240 8.965 1.00 69.49 C ATOM 699 CB THR A 108 24.573 -54.020 9.092 1.00 69.48 C ATOM 700 OG1 THR A lOS 24.213 -53.964 10.478 1.00 69.55 0 ATOM 701 CG2THRA 108 23.798-55.139 8.407 1.00 69.46 C ATOM 702 C THRA 108 26.787-53.116 9.725 1.00 69.49 C ATOM 703 0 TI-IRA 108 27.509-53.354 10.695 1.00 69.48 0 ATOM 704 N VAL A 109 26.546 -5 1.890 9.267 1.00 69.49 N ATOM 705 CA VAL A 109 27.063 -50.680 9.90 1 1.00 69.46 C ATOM 706 CB VALA 109 28.614-50.660 9.921 1.00 69.47 C ATOM 707 ccii VAL A 109 29.132 -49.424 10.648 1.00 69.54 C ATOM 708 CG2 VAL A 109 29.180 -50.750 8.506 1.00 69.55 C ATOM 709 C VAL A 109 26.507 -49.450 9.173 1.00 69.39 C ATOM 710 0 VAL A 109 26.653 -49.325 7.956 1.00 69.42 0 ATOM 711 N PROA 110 25.843 -48.548 9.916 1.00 69.28 N ATOM 712 CA PRO A 110 25.193 -47.376 9.325 1.00 69.20 C ATOM 713 CB PRO A 110 24.058 -47.076 10.311 1.00 69.20 C ATOM 714 Cci PROA 110 24.501 -47.667 11.623 1.00 69.19 C ATOM 715 CD PRO A 110 25.653 -48.608 11.376 1.00 69.25 C ATOM 716 C PRO A 110 26.098 -46.150 9.166 1.00 69.09 C ATOM 717 0 PROA 110 25.916-45.155 9.869 1.0069.13 0 ATOM 718 N GLYA 111 27.048-46.216 8.237 1.0068.96 N ATOM 719 CA GLY A 111 27.942 -45.089 7.969 1.00 68.85 C ATOM 720 C GLY A 111 28. 984 -44.872 9.058 1.00 68.81 C ATOM 721 0 GLYA 111 28.844-43.965 9.917 1.0068.65 0 ATOM 722 N ASN A 130 26.659 -3 1.270 8.342 1.00 66.96 N ATOM 723 CA ASNA 130 25.386-30.849 7.759 1.00 67.00 C ATOM 724 CB ASN A 130 25.594 -29.640 6.836 1.00 66.96 C ATOM 725 CG ASN A 130 24.279 -29.020 6.38 1 1.00 66.90 C ATOM 726 OD1 ASN A 130 23.843 -28.004 6.943 1.00 66. 78 0 ATOM 727 ND2ASNA 130 23.636-29.635 5.364 1.00 66.61 N ATOM 728 C ASNA 130 24.650-31.973 7.012 1.00 67.05 C ATOM 729 0 ASNA 130 23.429-32.106 7.132 1.00 67.08 0 ATOM 730 N THRA 131 25.399-32.772 6.249 1.00 67.04 N ATOM 731 CA THR A 131 24.833 -33.856 5.424 1.00 66.97 C ATOM 732 CB THRA 131 25.900-34.450 4.459 1.00 66.99 C ATOM 733 OG1 THRA 131 25.543-35.792 4.101 1.00 66.77 0 ATOM 734 CG2 THR A 131 27.277 -34.460 5.115 1.00 67.17 C ATOM 735 C THRA 131 24.178-34.980 6.243 1.00 66.94 C : .. 45 ATOM 736 0 THRA 131 24.347-35.054 7.465 1.00 66.93 0 ATOM 737 N PHEA 132 23.431-35.851 5.561 1.0066.81 N ATOM 738 CA PHEA 132 22.674-36.912 6.232 1.00 66.68 C ATOM 739 CB PHE A 132 2 1.172 -36.602 6.205 1.00 66.71 C ATOM 740 CG PHE A 132 20.815 -35.278 6.826 1.00 66.79 C ATOM 741 CDI PHE A 132 20.191 -34.290 6.077 1.00 66.90 C ATOM 742 CE1 PHEA 132 19.863-33.064 6.649 1.00 67.27 C ATOM 743 CZ PHEA 132 20.166-32.814 7.982 1.00 67.02 C * ** ATOM 744 CE2 PHE A 132 20.793 -33.79 1 8.737 1.00 67.01 C :.. ATOM 745 CD2PHEA 132 21.116-35.015 8.158 1.0066.90 C *. * 55 ATOM 746 C PHE A 132 22.947 -38.3 16 5.680 1.00 66.58 C ATOM 747 0 PHEA 132 22.646-38.620 4. 521 1.00 66.52 0 ATOM 748 N LEU A 133 23.516 -39.165 6.534 1.00 66.41 N ATOM 749 CA LEU A 133 23.870 -40.539 6.181 1.00 66.14 C ATOM 750 CB LEUA 133 25.374-40769 6.373 1.0066.19 C ATOM 751 Co LEUA 133 26.382-40.435 5.265 1.00 66.22 C ATOM 752 CD1 LEUA 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 LEUA 133 23.101 -41.546 7.032 1.0065.93 C ATOM 755 0 LEUA 133 23.329-42.751 6937 1.00 65.82 0 ATOM 756 N ASN A 134 22.205 -41.051 7.882 1.00 65.76 N ATOM 757 CA ASNA 134 21.409-41.930 8.732 1.00 65.55 C ATOM 758 CB ASNA 134 20.734-41.148 9.863 1.00 65.55 C ATOM 759 CG ASNA 134 20.140-42.057 10. 930 1.00 65.49 C ATOM 760 OD1 ASN A 134 19.3 14 -41.627 11.736 1.00 65.41 0 ATOM 761 ND2 ASN A 134 20.560 -43.319 10.938 1.00 65.26 N ATOM 762 C ASNA 134 20.373-42.672 7.900 1.00 65.39 C ATOM 763 0 ASN A 134 19.824 -43.690 8.326 1.00 65.43 0 ATOM 764 N ARGA 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 CO ARO A 135 17.760 -40. 714 5.123 0.00 50.00 C ATOM 768 CD ARO A 135 17.42 1 -39.538 4.3 10 0.00 50. 00 C ATOM 769 NE ARGA 135 18.323-38.615 3.780 0.00 50.00 N ATOM 770 CZ ARGA 135 18.391 -37.354 3.482 0.00 50.00 C ATOM 771 NFII ARG A 135 19.376 -36.980 2.625 0.00 50.00 N ATOM 772 NH2 ARG A 135 17.696 -36.373 4.0 13 0.00 50.00 N ATOM 773 C ARGA 135 20.213-43.669 4.857 1.006465 C ATOM 774 0 ARG A 135 19.912 -43.944 3.695 1.00 64.66 0 ATOM 775 N PHEA 136 21.344-44.072 5.431 1.00 64.44 N ATOM 776 CA PHEA 136 22.377-44.795 4.695 1.0064.19 C ATOM 777 CB PHE A 136 23.496 -43.832 4.295 1.00 64.24 C ATOM 778 CO PHE A 136 24.064 -44.089 2.932 1.00 64.14 C ATOM 779 CDI PHEA 136 23.904-43.155 1.919 1.0064.00 C ATOM 780 CEI PHE A 136 24.424 -43.377 0.663 1.0064.15 C ATOM 781 CZ PHE A 136 25.111 -44.548 0.403 1.0064.46 C ATOM 782 CE2 PHE A 136 25.277 -45.491 1.407 1.0064.42 C ATOM 783 CD2PHEA 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 0 PHEA 136 23.550-45.718 6.586 1.00 63.97 0 ATOM 786 N META 137 22.793-47.160 5.028 1.00 63.68 N ATOM 787 CA META 137 23.301 -48.347 5.703 1.00 63.43 C ATOM 788 CB META 137 22.165-49.343 5. 945 1.00 63.62 C ATOM 789 CO MET A 137 21.184 -48.929 7.033 1.0064.35 C ATOM 790 SD MET A 137 2 1.680 -49.495 8.676 1.00 66.23 S ATOM 791 CE META 137 21.543-51.275 8.465 1.00 65.88 C ATOM 792 C META 137 24.384-49.000 4.858 1.0063.01 C * . ATOM 793 0 META 137 24.486-48.735 3.661 1.00 63.09 0 ATOM 794 N CYSA 138 25.188-49,857 5.479 1.00 62.44 N ATOM 795 CA CYSA 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 0 CYSA 138 26.422-52.365 6.345 1.00 61.39 0 ATOM 800 N ALAA 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 ALAA 139 25.044-55.046 3.856 10060.46 C ** * ATOM 803 C ALA A 139 27.54 1 -54.939 3.783 1.00 60.13 C * 55 ATOM 804 0 ALA A 139 27.987 -54.485 2.729 1.00 60.12 0 ATOM 805 N GLN A 140 28.113 -55.942 4.441 1.00 59.68 N ATOM 806 CA GLNA 140 29.350-56.562 3.985 1.00 59.22 C ATOM 807 CB GLNA 140 30.513-56.145 4.882 1.00 59.22 C ATOM 808 Ci GLN A 140 30.723 -54.656 4.993 1.00 59.09 C ATOM 809 CD GLN A 140 3 1.949 -54.321 5.802 1.00 59.09 C ATOM 810 OE1 GLN A 140 32.772 -55.192 6.084 1.00 59.44 0 ATOM 811 NE2GLNA 140 32.080-53.058 6.185 1.0059.05 N ATOM 812 C GLNA 140 29.231 -58.074 4.025 1.00 58.94 C ATOM 813 0 GLNA 140 28.591 -58.624 4.920 1.00 58.94 0 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 1.00 58.30 C ATOM 816 CB LEUA 141 28.481 -60.785 2.861 1.00 58.30 C ATOM 817 CG LEUA 141 27.730-60.539 1.550 1.00 58.25 C ATOM 818 CD! LEUA 141 26.394-61.267 1. 581 1.0058.11 C ATOM 819 CD2LEUA 141 27.524-59.056 1.278 1.00 58.38 C ATOM 820 C LEU A 141 30.890 -60.8 10 2.099 1.00 58.06 C ATOM 821 0 LEU A 141 30. 953 -60.403 0.942 1.00 58.07 0 ATOM 822 N PROA 142 31.681-61.788 2.571 1.0057.87 N ATOM 823 CA PROA 142 32.663-62.505 1.761 1.00 57.70 C ATOM 824 CB PROA 142 33.217-63.554 2.728 1.0057.74 C ATOM 825 CG PROA 142 32.219-63.635 3.840 1.00 57.78 C ATOM 826 CD PRO A 142 3 1.664 -62.265 3.963 1.00 57.80 C ATOM 827 C PROA 142 31.999-63.187 0.578 1.00 57.59 C ATOM 828 0 PRO A 142 31.212 -64.109 0.759 1.00 57.61 0 ATOM 829 N ASN A 143 32.327 -62.729 -0.625 1.00 57.52 N ATOM 830 CA ASNA 143 31.640-63.152 -1.837 1.00 57.4! C ATOM 831 CB ASN A 143 30.167 -62.745 -1.756 1.00 57. 34 C ATOM 832 CG ASN A 143 29.403 -63.022 -3.037 1 00 57.28 C ATOM 833 OD1 ASNA 143 29.960-62.987 -4.136 1.00 57.32 0 ATOM 834 ND2ASNA 143 28.109-63.281 -2.901 1.0056.70 N ATOM 835 C ASNA 143 32.314-62.516 -3.050 1.00 57.47 C ATOM 836 0 ASN A 143 32.443 -61.295 -3.124 1.00 57.41 0 ATOM 837 N GLN A 144 32.737 -63.350 -3 998 1.00 57.56 N ATOM 838 CA GLN A 144 33.563 -62.908 -5.129 1.00 57.72 C ATOM 839 CB GLNA 144 33.773-64.055 -6.110 1.00 57.81 C ATOM 840 CG GLN A 144 34.101 -65.378 -5.467 1.00 58. 02 C ATOM 841 CD GLNA 144 34.468-66.419 -6.497 1.00 58.57 C ATOM 842 OE1 GLN A 144 35.365 -66.207 -7.317 1.00 58.64 0 ATOM 843 NE2 GLN A 144 33.774 -67.553 -6.466 1.00 58.83 N ATOM 844 C GLN A 144 32.996 -61.7 13 -5.891 1.00 57.73 C ATOM 845 0 GLN A 144 33.729 -60.782 -6.265 1.00 57.88 0 ATOM 846 N VAL A 145 31.693 -61.756 -6.143 1.00 57.64 N ATOM 847 CA VAL A 145 31.037 -60.663 -6.830 1.00 57.55 C ATOM 848 CB VAL A 145 29.5 15 -60.834 -6.849 1.00 57.60 C ATOM 849 CG1 VALA 145 29.149 -62.269 -7.189 1.00 57. 62 C ATOM 850 CG2 VAL A 145 28.89 1 -59.867 -7.844 1.00 57.54 C :. ATOM 851 C VALA 145 31.396-59.369 -6.123 1.0057.47 C * .. 45 ATOM 852 0 VAL A 145 31.752 -58.386 -6.764 1.00 57.53 0 ATOM 853 N LEUA 146 31.325-59.386 -4.797 1.00 57.46 N ATOM 854 CA LEUA 146 31.695 -58.222 -4.001 1.00 57.59 C ATOM 855 CB LEUA 146 31.218-58.367 -2.553 1.00 57.59 C ATOM 856 CG LEU A 146 29.750 -58.045 -2.263 1.00 57.56 C ATOM 857 CD1 LEU A 146 29.270 -56.879 -3.119 1.00 57.23 C *:* ATOM 858 CD2 LEU A 146 28.882 -59.266 -2.489 1.00 57.83 C ATOM 859 C LEU A 146 33.197 -57.934 -4.046 1.00 57.65 C * ** ATOM 860 0 LEU A 146 33.635 -56.840 -3.698 1.00 57.62 0 ATOM 861 N GLUA 147 33.985-58.917 -4.466 1.0057.74 N ** * 55 ATOM 862 CA GLUA 147 35.396-58.681 -4.719 1.00 57.96 C ATOM 863 CB GLU A 147 36.152 -59.994 -4.928 1.00 57.87 C ATOM 864 CG GLU A 147 36.190 -60.9 12 -3.725 1.00 58.25 C ATOM 865 CD GLUA 147 36.827-62.253 -4.048 1.00 58.44 C ATOM 866 OEI GLUA 147 36.631 -63.217 -3.271 1.00 58.79 0 ATOM 867 OE2GLUA 147 37.520-62.343 -5.086 1.00 59.30 0 ATOM 868 C GLU A 147 35.520 -57.827 -5.969 1.00 57.91 C ATOM 869 0 GLUA 147 36.266-56.850 -5.996 1.00 58.03 0 ATOM 870 N SERA 148 34.781 -58.197 -7.009 1.00 57.86 N ATOM 871 CA SER A 148 34.875 -57 474 -8.274 1 00 57.89 C ATOM 872 CB SERA 148 34.270-58.296 -9.409 1.00 57.92 C ATOM 873 OG SERA 148 34.858-59.582 -9.471 1.00 58.15 0 ATOM 874 C SERA 148 34.220-56.091 -8.222 1.00 57.91 C ATOM 875 0 SERA 148 34.816-55.099 -8.641 1.00 58.01 0 ATOM 876 N ILE A 149 32.995 -56.031 -7.708 1.00 57.82 N ATOM 877 CA ILEA 149 32.216-54.795 -7.699 1.00 57 70 C ATOM 878 CB ILE A 149 31.161 -54.802 -8.818 1.00 57.63 C ATOM 879 CG1 ILEA 149 30.180-55.962 -8.620 1.00 57.21 C ATOM 880 CD1 ILEA 149 29.012 -55. 946 -9.580 1.00 56.31 C ATOM 881 CG2ILEA 149 31.825-54.901-10.175 1.0057.78 C ATOM 882 C ILE A 149 3 1.484 -54.602 -6.378 1.00 57.81 C ATOM 883 0 ILEA 149 31.605 -55.418 -5.467 1.00 58.00 0 ATOM 884 N SERA 150 30.725-53.517 -6.272 1.00 57.80 N ATOM 885 CA SERA 150 29.808 -53.345 -5.146 1.00 57.87 C ATOM 886 CB SER A 150 30.424 -52.492 -4.031 1.00 57.80 C ATOM 88700 SERA 150 31.122-51.381 -4.555 1.0058.07 0 ATOM 888 C SER A 150 28.472-52.780.5.620 1.00 57.82 C ATOM 889 0 SERA 150 28.417-51.969 -6.546 1.00 57.84 0 ATOM 890 N ILEA 151 27.393 -53.233 -4.994 1.00 57.75 N ATOM 891 CA ILE A 151 26.056 -52.907 -5.461 1.00 57.75 C ATOM 892 CB ILE A 151 25.248 -54.178 -5.733 1.00 57.69 C ATOM 893 CG1 ILE A 151 26.076 -55.163 -6.555 1.00 57.79 C ATOM 894 CD1 ILEA 151 25.580-56.585 -6.471 1.00 58.36 C ATOM 895 CG2ILEA 151 23.946-53.837.6.437 1.00 57.61 C ATOM 896 C ILEA 151 25.307-52.074 -4.438 1.00 57.80 C ATOM 897 0 ILEA 151 25.108-52.502.3.302 1.00 57.77 0 ATOM 898 N ILEA 152 24.884-50.882 -4.838 1.00 57.79 N ATOM 899 CA ILEA 152 24.129-50.046 -3.928 1.00 57.80 C ATOM 900 CB ILE A 152 24.593 -48.573 -3.980 1.00 57.84 C ATOM 901 CG1 ILEA 152 23.502 -47.669.4.549 1.00 58.21 C ATOM 902 CDI ILE A 152 22.496 -47.213.3.501 1.00 58.80 C ATOM 903 CG2ILEA 152 25.918-48.445 -4.728 1.00 57.83 C ATOM 904 C ILEA 152 22.633-50.189 -4.214 1.0057.75 C ATOM 905 0 ILEA 152 22.177-49.991 -5.340 1.00 57.62 0 ATOM 906 N ASPA 153 21.886-50.564 -3.181 1.00 57.80 N ATOM 907 CA ASPA 153 20.450-50.776 -3.283 1.00 57.91 C ATOM 908 CB ASP A 153 20.048.52.005 -2.470 1.00 57.99 C ATOM 909 CG ASPA 153 18.582-52.358 -2.625 1.00 58.23 C * 45 ATOM 910 ODIASPA 153 17.831-51.554 -3.219 1.0058.41 0 * ATOM 911 OD2ASPA 153 18.181-53.444 -2.147 1.0058.26 0 S... ATOM 912 C ASPA 153 19.710-49.549 -2.770 1.0058.00 C ATOM 913 0 ASPA 153 20.084-48.975 -1.746 1.0058.18 0 ATOM 914 N THRA 154 18.652-49.160 -3.475 1.0058.02 N ATOM 915 CA TI-IRA 154 17.958 -47.904 -3.200 1.00 57.95 C ATOM 916 CB THRA 154 17.814-47.058 -4.482 1.0057.97 C ATOM 917 OG1 THRA 154 17.036-47.776 -5.454 1.00 57.67 0 * .. ATOM 918 CG2THRA 154 19.182-46.726 -5.059 1.00 57.86 C ATOM 919 C THRA 154 16.568-48.117 -2.617 1.0058.01 C ATOM 920 0 THRA 154 16.008 -49.205.2.739 1.00 57.95 0 * .. ATOM 921 N PROA 155 16.009-47.071 -1.977 1.0058.12 N ATOM 922 CA PRO A 155 14.614 -47.083 -1.545 1.00 58.12 C ATOM 923 CB PRO A 155 14.458 -45.757 -0.788 1.00 58.01 C ATOM 924 CG PROA 155 15.838-45.284 -0.511 1.0058.04 C ATOM 925 CD PROA 155 16.684-45.812 -1. 616 1.00 58.18 C ATOM 926 C PRO A 155 13.682 -47.093 -2.747 1.00 58.22 C ATOM 927 0 PROA 155 14.050-46.623 -3.829 1.0058.19 0 ATOM 928 N GLY A 156 12.483 -47.628 -2.552 1.00 58.35 N ATOM 929 CA GLYA 156 11.492-47.689 -3.616 1.0058.61 C ATOM 930 C GLYA 156 10.938-46.324 -3.963 1.00 58.79 C ATOM 931 0 GLY A 156 10.545 -45.557 -3.083 1.00 58 87 0 ATOM 932 N ILEA 157 10.916-46.016 -5.253 1.00 58.96 N ATOM 933 CA ILEA 157 10.340-44.769 -5.713 1.00 59.18 C ATOM 934 CB ILEA 157 10.632-44.544 -7.199 1.00 59.11 C ATOM 935 CG1 ILEA 157 12.137-44.645 -7.447 1.00 59.27 C ATOM 936 CDI ILEA 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 ILEA 157 8.838-44.792 -5.459 1.00 59.40 C ATOM 939 0 ILE A 157 8.145 -45.715 -5.877 1.00 59.29 0 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 LEUA 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 CD! LEUA 158 5.164-41.219 -5.172 0.0050.00 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 0 LEU A 158 6.377 -43.110 -6.666 1.00 60.52 0 ATOM 948 N SERA 159 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 SERA 159 3.135 -45.849 -6.561 1. 00 61.20 C ATOM 951 06 SERA 159 2.477-46.173 -7.774 1.00 61.72 0 ATOM 952 C SER A 159 3.260-43.364 -6.942 1.00 61.06 C ATOM 953 0 SERA 159 2.043 -43.338 -6.733 1.00 61.02 0 ATOM 954 N ARGA 167 8.576-37.115 1.268 1.00 65.73 N ATOM 955 CA ARGA 167 9.108-35.811 1.654 1.0065.83 C ATOM 956 CB ARG A 167 8.000 -34.902 2.220 1.00 65.92 C ATOM 957 CO 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 ARGA 167 5.726-36.803 1.001 1.00 67.11 N ATOM 960 CZ ARGA 167 4.818-37.760 1.181 1.0067.11 C ATOM 961 NHI ARGA 167 3.728-37. 514 1.905 1.00 67.24 N ATOM 962 N}12 ARG A 167 4.998 -38.961 0.640 1.00 66.65 N ATOM 963 C ARGA 167 10.217-35.961 2.690 1.0065.75 C ATOM 964 0 ARG A 167 10.033 -35.617 3.858 1.00 65.80 0 ATOM 965 N GLYA 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 9680 GLYA 168 14.343-35.132 3.410 1.0065.38 0 ATOM 969 N TYRA 169 14.151-36.239 1.462 1.0065.52 N ATOM 970 CA TYRA 169 15.392-35.720 0.898 1.00 65.52 C **** ATOM 971 CB TYRA 169 16.520 -36.744 1.084 1.00 65.60 C ATOM 972 CO TYRA 169 16.060-38.185 0.979 1.00 65.63 C ATOM 973 CDI TYRA 169 15.809-38.940 2.121 1.0065.74 C ATOM 974 CE! TYRA 169 15.382 -40.256 2.032 1.00 65.83 C ATOM 975 CZ TYRA 169 15.198 -40.834 0.790 1.00 65.80 C : *. ATOM 976 OH TYRA 169 14.772-42.140 0.699 1.00 65.64 0 ATOM 977 CE2TYRA 169 15.438-40.105 -0.360 1.0065.77 C *. : 55 ATOM 978 CD2TYRA 169 15.866-38.788 -0.260 1.0065.73 C ATOM 979 C TYRA 169 15.216-35.383 -0.585 1.00 65.44 C ATOM 9800 TYRA 169 14.107-35.459 -1.118 1.0065.44 0 ATOM 981 N ASPA 170 16.312-35.007 -1.242 1.00 65.30 N ATOM 982 CA ASPA 170 16.294-34.711 -2.674 1.00 65.09 C ATOM 983 CB ASPA 170 17.247-33.557 -2.999 1.00 65.12 C ATOM 984 CG ASP A 170 16.898 -32.862 -4.304 1.00 65. 25 C ATOM 985 ODI ASPA 170 17.312-31.695 -4.484 1.0065.06 0 ATOM 986 0D2 ASP A 170 16.211 -33.481 -5.149 1.00 65.55 0 ATOM 987 C ASPA 170 16.637-35. 965 -3.486 1.006495 C ATOM 988 0 ASPA 170 17.698-36.058 -4.131 1.0064.78 0 ATOM 989 N PHEA 171 15.719-36.926 -3.442 1.0064.77 N ATOM 990 CA PHEA 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 CO PHEA 171 14.728-40.414 -4.560 1.0064.58 C ATOM 993 CDI PHEA 171 15.480-41.283 -3.788 1.0064.37 C ATOM 994 CE! PHE A 171 15.616 -42.608 -4 146 1.00 64.43 C ATOM 995 CZ PHE A 171 14.992 -43.083 -5.285 1.00 64.73 C ATOM 996 CE2PHEA 171 14.237-42.228 -6.062 1.00 64.67 C ATOM 997 CD2 PHE A 171 14.107 -40.902 -5.697 1.00 64.81 C ATOM 998 C PHEA 171 16.534-38.064 -5.470 1.00 64.56 C ATOM 999 0 PHEA 171 17.609-38.616 -5.734 1.00 64.43 0 ATOM 1000 N PRO A 172 15.872 -37.306 -6.357 1.00 64. 52 N ATOM 1001 CA PROA 172 16.455-37.032 -7.663 1.00 64.49 C ATOM 1002 CB PROA 172 15.573-35.907 -8.202 1.00 64.54 C ATOM 1003 CG PROA 172 14.246-36.174 -7.585 1.00 64.64 C ATOM 1004 CD PRO A 172 14.547 -36.678 -6.203 1.0064.57 C ATOM 1005 C PROA 172 17.916-36.583 -7.571 1.00 64.39 C ATOM 1006 0 PRO A 172 18.775 -37.148 -8.258 1.0064.27 0 ATOM 1007 N ALAA 173 18.200-35.592 -6.729 1.00 64.18 N ATOM 1008 CA ALA A 173 19.568 -35.093 -6.596 1.00 64.15 C ATOM 1009 CB ALAA 173 19.641 -33.959 -5.592 1.0064.18 C ATOM 1010 C ALA A 173 20.547 -36.206 -6.226 1.00 64.15 C ATOM 1011 0 ALA A 173 2 1.636 -36.305 -6.809 1.00 64.04 0 ATOM 1012 N VAL A 174 20.168 -37.051 -5.270 1.0064.23 N ATOM 1013 CA VALA 174 21.045-38.177 -4.922 1.00 64.12 C ATOM 1014 CB VAL A 174 20.627 -38.899 -3.608 1.00 64.14 C ATOM 1015 CG1VALA 174 19.189-38.598 -3.246 1.0064.11 C ATOM 1016 CG2VALA 174 20.874-40.397 -3.705 1.00 64.15 C ATOM 1017 C VALA 174 2 1. 219 -39.162 -6.092 1.00 64.08 C ATOM 1018 0 VAL A 174 22.340 -39.617 -6.378 1.00 63.98 0 ATOM 1019 N LEUA 175 20.121 -39.466 -6.781 1.00 64.02 N ATOM 1020 CA LEU A 175 20.200 -40.298 -7.976 1.00 63.80 C ATOM 1021 CB LEU A 175 18.813 -40.556 -8.557 1.00 63.79 C ATOM 3022 Co LEUA 175 18.168-41. 866 -8.103 1.00 64.02 C ATOM 1023 CD1 LEU A 175 16.760 -42.013 -8.663 1.00 64.02 C ATOM 1024 CD2 LEU A 175 19.034 -43.050 -8.5 12 1.0064.22 C : . ATOM 1025 C LEUA 175 21.107-39.679 -9.034 1.00 63.78 C ATOM 1026 0 LEU A 175 21.733 -40.386 -9.820 1.00 63.66 0 ** ATOM 1027 N ARGA 176 21.181 -38.355 -9.049 1.00 63.87 N ATOM 1028 CA ARG A 176 22.050 -37.663 -9.989 1.00 63.82 C ATOM 1029 CB ARGA 176 21.579-36.223-10.186 1.00 63.86 C ATOM 1030 CG ARGA 176 22.452-35.376-11.095 1.0064.46 C ATOM 1031 CD ARGA 176 21.716-34.101-11.477 1.0065.87 C * ATOM 1032 NE ARGA 176 20.505-33.929-10.669 1.00 66.91 N ATOM 1033 CZ ARGA 176 19.918-32.760-10.423 1.00 67.30 C ATOM 1034 NH! ARGA 176 18.817-32.717 -9.679 1.00 67.30 N ATOM 1035 NH2ARGA 176 20.435-31.635-10.912 1.0067.62 N *. 55 ATOM 1036 C ARGA 176 23.510-37.722 -9.538 1.00 63.65 C * ATOM 10370 ARGA 176 24.417-37.859-10.363 1.0063.59 0 ATOM 1038 N TRPA 177 23.733 -37.633 -8.229 1.00 63.54 N ATOM 1039 CA TRP A 177 25.080 -37.773 -7.668 1.00 63.37 C ATOM 1040 CB TRPA 177 25.025-37.527 -6.160 1.00 63.31 C ATOM 1041 CO TRPA 177 26.347-37.583 -5.454 1.00 63.26 C ATOM 1042 CDI TRP A 177 27.2 18 -36.549 -5.255 1.00 62.97 C ATOM 1043 NE! TRP A 177 28.3 17 -36.985 -4.555 1.00 62.77 N ATOM 1044 CE2 TR.P A 177 28.169 -38.320 -4. 280 1.00 63.09 C ATOM 1045 CD2 TRP A 177 26.937 -38.731 -4.828 1.00 63.35 C ATOM 1046 CE3 TRP A 177 26.544 -40.069 -4.683 1.00 63.27 C ATOM 1047 CZ3 TRP A 177 27.383 -40.939 -4.005 1.00 63.03 C ATOM 1048 CH2 TRP A 177 28.604 -40.500 -3.473 1.00 63.04 C ATOM 1049 CZ2TRPA 177 29.014-39.199 -3.599 1.00 63.18 C ATOM 1050 C TRPAI77 25.641-39.168 -7.971 1.0063.41 C ATOM 1051 0 TRPA 177 26.780-39.331 -8.476 1.00 63.24 0 ATOM 1052 N PHEA 178 24.826-40.177 -7.672 1.00 63.59 N ATOM 1053 CA PHEA 178 25.161-41.545 -8.047 1.0063.57 C ATOM 1054 CB PHEA 178 24.094-42.526 -7.558 1.00 63.59 C ATOM 1055 CO PHE A 178 24.285 -42.971 -6.137 1.00 63.89 C ATOM 1056 CD1 PHE A 178 25.401 -43.713 -5.772 1.00 64.14 C ATOM 1057 CE1PHEA 178 25.580-44.131 -4.461 1.0064.00 C ATOM 1058 CZ PHE A 178 24.638 -43.811 -3.501 1.00 63.93 C ATOM 1059 CE2 PHE A 178 23.520 -43.076 -3.85 1 1.00 64.17 C ATOM 1060 CD2PHEA 178 23.346-42.660 -5.166 1.0064.18 C ATOM 1061 C PHEA 178 25.345-41.661 -9.562 1.00 63.55 C ATOM 1062 0 PHEA 178 26.341 -42.210-10.032 1.00 63.61 0 ATOM 1063 N ALAA 179 24.391-41.133-10.325 1.0063.51 N ATOM 1064 CA ALAA 179 24.479-41.170-11.783 1.0063.38 C ATOM 1065 CB ALA A 179 23.344 -40.377 -12.4 10 1.00 63.38 C ATOM 1066 C ALA A 179 25.832 -40.648 -12.260 1.00 63.30 C ATOM 1067 0 ALA A 179 26.435 -41.207 -13.178 1.00 63.20 0 ATOM 1068 N GLUA 180 26.303 -39.574 -11.631 1.00 63.33 N ATOM 1069 CA GLU A 180 27.635 -39.051 -11.916 1.00 63.25 C ATOM 1070 CE GLU A 180 27.923 -37.789 -11.102 1.00 63.23 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 OE1 GLUA 180 28.083 -35.556 -9.596 1.00 63.87 0 ATOM 1074 OE2GLUA 180 26.936-34.258-10.959 1.00 64.08 0 ATOM 1075 C GLUA 180 28.695 -40.090-11.595 1.00 63.07 C ATOM 1076 0 GLU A 180 29.588 -40.338 -12.405 1.00 63.03 0 ATOM 1077 N ARGA 181 28.601 -40.696-10.411 1.00 62.95 N ATOM 1078 CA ARG A 181 29.672 -41.605 -9.967 1.00 62.57 C ATOM 1079 CB ARG A 181 29.820 -41.556 -8.447 1.00 62.55 C ATOM 1080 CO ARG A 181 30.68 1 -40.405 -7.980 1.00 62.92 C ATOM 1081 CD ARGA 181 30.191-39.845 -6.668 1.0063.49 C ATOM 1082 NE ARGA 181 30.603-38.454 -6.494 1.00 64.41 N : , ATOM 1083 CZ ARGA 181 29.996-37.415 -7.063 1.00 64.92 C ec.. e 45 ATOM 1084 NH! ARG A 181 30.438 -36.180 -6.846 1.00 65.08 N ATOM 1085 NH2ARGA 181 28.943-37.606 -7.849 1.00 65.13 N ATOM 1086 C ARG A 181 29.587 -43.059 -10.444 1.00 62.33 C ATOM 10870 ARGA 181 30.604-43.668-10.768 1.0062.41 0 ATOM 1088 N VALA 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 1.00 61.45 C ATOM 1091 CG1VALA 182 26.198-46.552-11.030 1.0061.55 C : ," * ATOM 1092 CG2 VAL A 182 26.654 -45.623 -8.752 1.00 61.14 C ATOM 1093 C VALA 182 28.430-45.596-12.065 1.0061.44 C ***. : 55 ATOM 1094 0 VALA 182 28.331 -44.875-13.055 1.00 61.47 0 * ATOM 1095 N ASP A 183 28.772 -46.882 -12.137 1.00 61.33 N ATOM 1096 CA ASPA 183 29.076-47.554-13.415 1.00 61.35 C ATOM 1097 CB ASP A 183 30.000 -48.762 -13.198 1.00 61.39 C ATOM 1098 CG ASPA 183 31.466-48.373-13.136 1.00 62.09 C ATOM 1099 ODI ASP A 183 32.248 -48.863 -13.981 1.00 62.54 0 ATOM 1100 OD2ASPA 183 31.838-47.569-12.252 1.0063.12 0 ATOM 1101 C ASPA 183 27.842-47.992-14.216 1.0061.13 C ATOM 1102 0 ASP A 183 27.771 -47.778 -15.428 1.00 61.05 0 ATOM 1103 N LEUA 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 LEIJ A 184 25.630 -50.608 -14.307 1.00 60.75 C ATOM 1106 CG LEUA 184 26.126-51.298-15.581 1.0060.63 C ATOM 1107 CD! LEUA 184 25.747-52.774-15.537 1.00 60.23 C ATOM 1108 CD2 LEU A 184 25.555 -50.648 -16.828 1.00 60.26 C ATOM 1109 C LEU A 184 24. 448 -48.655 -13.335 1.00 60.59 C ATOM 1110 0 LEUA 184 24.508-48.633-12.107 1.0060.73 0 ATOM 1111 N ILEA 185 23.351 -48.320-14.005 1.00 60.33 N ATOM 1112 CA ILEA 185 22.119-47.996-13.310 1.0060.09 C ATOM 1113 CB ILEA 185 21.670-46.560-13.589 1.0059.94 C ATOM 1114 COt ILE A 185 22.827 -45.592 -13.343 1.00 59.84 C ATOM 1115 CDI ILEA 185 22.469-44.139-13.553 1.00 59.85 C ATOM 1116 CG2ILEA 185 20.483-46.203-12.718 1.0059.66 C ATOM 1117 C ILE A 185 21.039 -48.964 -13.754 1.00 60.22 C ATOM 1118 0 [LE A 185 20. 636 -48.969 -14.915 1.00 60.25 0 ATOM 1119 N ILE A 186 20.586-49.799-12.830 1.00 60.39 N ATOM 1120 CA ILE A 186 19.557 -50.777 -13.145 1.00 60.66 C ATOM 1121 CB ILEA 186 19.785-52.100-12.400 1.0060.60 C ATOM 1122 Cot ILEA 186 21.222-52.588-12.592 1.00 60.80 C ATOM 1123 CDI ILE A 186 21.619 -52.766 -14.037 1.00 60.97 C ATOM 1124 CG2ILEA 186 18:80853.14142.881 1.0060.56 C ATOM 1125 C ILEA 186 18.188-50.230-12.768 1.0060.88 C ATOM 1126 0 ILE A 186 17.935 -49.911 -11.603 1.00 60.99 0 ATOM 1127 N LEUA 187 17.312-50.107-13.757 1.0061.05 N ATOM 1128 CA LFU A 187 15.945 -49.672 -13.507 1.00 61.25 C ATOM 1129 CB LEUA 187 15.555-48.542-14.458 1.0061.17 C ATOM 1130 CO LEUA 187 15.836-47.107-14.010 1.0060.76 C ATOM 1131 CD! LEUA 187 17.290-46.918 -13.667 1.00 60.58 C ATOM 1132 CD2LEUA 187 15.425-46.133-15.096 1.0060.96 C ATOM 1133 C LEUA 187 14.980-50.850-13. 649 1.00 61.68 ATOM 1134 0 LEUA 187 14.955-51.526-14.682 1.0061.88 ATOM 1135 N LEUA 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 LEUA 188 13.348-53.033-11.341 1.0062.05 C ATOM 1138 CG LEU A 188 14.662 -53.756-11.067 1.00 62.08 C ATOM 1139 CD! LEUA 188 14.375-55.091-10.405 1.00 61.97 C ATOM 1140 CD2LEUA 188 15.416-53.970-12.353 1.0062.07 C ATOM 1141 C LEUA 188 11.831 -51.755-12.833 1.00 62.53 C ATOM 1142 0 LEU A 188 11.372 -50.801 -12.205 1.00 62.71 0 ATOM 1143 N PHEA 189 11.138-2.441-13.729 1.0062.88 N ATOM 1144 CA PHEA 189 9.703 -52.305 -13.862 1.00 63.25 C ATOM 1145 CB PHEA 189 9.348 -51.737 -15.222 1.00 63.06 C ATOM 1146 CO PHEA 189 9.810-50.339-15.425 1.00 63.11 C ATOM 1147 CDI PHE A 189 11.085 -50.080 -15.889 1.00 63.21 C ATOM 1148 CE! PHEA 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 PHE A 189 9.385 -47.974 -15.339 1.00 63.09 C ATOM 1151 CD2 PHE A 189 8.966 -49.274 -15.152 1.00 63.37 C ATOM 1152 C PHEA 189 9.168-53.707-13.755 1.0063.65 C ATOM 1153 0 PHEA 189 9.798-54.631 -14.257 1.00 63.87 0 ATOM 1154 N ASPA 190 8.028-53.895-13.104 1.0064.11 N ATOM 1155 CA ASP A 190 7.488 -55.244 -13.029 1.006478 C ATOM 1156 CB ASPA 190 7.296-55.712-11.575 1.0064.95 C ATOM 1157 CO ASPA 190 5.906-55.455-11.040 1.0065.15 C ATOM 1158 OD1ASPA 190 5.433-54.305-11.133 1.0066.38 0 ATOM 1159 OD2ASPA 190 5.299-56.403-10.497 1.0064.63 0 ATOM 1160 C ASPA 190 6.252-55.446-13.911 1.0065.11 C ATOM 1161 0 ASPA 190 5.267-54.713 -13.810 1.00 65.07 0 ATOM 1162 N ALAA 191 6.348-56.441-14.793 1.00 65.57 N ATOM 1163 CA ALAA 191 5.325-56.747-15.793 1.00 65.98 C ATOM 1164 CB ALAA 191 5.777-57.918-16. 644 1.00 66.05 C ATOM 1165 C ALAA 191 4.001-57.076-15.143 1.0066.33 C ATOM 11660 ALAA 191 2.979-57.215-15.811 1.0066.29 0 ATOM 1167 N HISA 192 4.039-57.206-13.826 1.00 66.88 N ATOM 1168 CA HIS A 192 2.885 -57.594 -13.058 1.00 67.53 C ATOM 1169 CB HISA 192 3.359-58.253-11.773 1.00 67.72 C ATOM 1170 CG HISA 192 2.252-58.756-10.912 1.00 68.70 C ATOM 1171 ND! HIS A 192 1.333 -59.684-11.354 1.00 69.77 N ATOM 1172 CE1 HISA 192 0.476-59.947-10.383 1.0070.36 C ATOM 1173 NE2 HIS A 192 0.812 -59.227 -9.327 1.00 71.03 N ATOM 1174 CD2 HIS A 192 1.921 -58.474 -9.632 1.00 69.62 C ATOM 1175 C HIS A 192 2.028 -56.372 -12.75 1 1.00 67.83 C ATOM 1176 0 HISA 192 0.806-56.409-12.890 1.0068.11 0 ATOM 1177 N LYSA 193 2.681-55.290-12.336 1.0068.10 N ATOM 1178 CA LYS A 193 2.010 -54.027 -12.039 1.00 68.23 C ATOM 1179 CB LYS A 193 2.029 -53.736 -10.536 1.00 68.19 C ATOM 1180 CG LYS A 193 0.915 -54.383 -9.730 1.00 68.42 C ATOM 1181 CD LYS A 193 0.800 -53.722 -8.360 1.00 68.19 C ATOM 1182 CE LYS A 193 0.625 -52.216 -8.509 1.00 68.29 C ATOM 1183 NZ LYS A 193 0.868 -5 1.484 -7.239 1.00 68.54 N ATOM 1184 C LYS A 193 2.717 -52.889 -12.750 1.00 68. 36 C ATOM 11850 LYSA 193 3.491-52.156-12.133 1.0068.44 0 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 1.00 68.79 C ATOM 1188 CB LEUA 194 2.892-51.826-16.282 1.0068.92 C ATOM 1189 CG LEU A 194 4.052 -51.373 -17.167 1.00 68.90 C ATOM 1190 CDI LEUA 194 3.496-50.606-18.343 1.0069.72 C ATOM 1191 CD2 LEU A 194 5.038 -50.514 -16.405 1.00 69.07 C :. ATOM 1192 C LEU A 194 2.570 -50.294 -14.335 1.00 68.86 C * . ATOM 1193 0 LEUA 194 1.387-49.994-14.484 1.00 68.87 0 ** ATOM 1194 N GLUA 195 3.459-49.479-13.781 1.0069.01 N ATOM 1195 CA GLUA 195 3.114-48.129-13.348 1.0069.24 C ATOM 1196 CB GLUA 195 2.533-48.156-11.926 1.0069.19 C S...

ATOM 1197 CO GLUA 195 2.935-46.994-11.024 1.0069.68 C ATOM 1198 CD GLUA 195 2.265 -45.679 -11.395 1.00 70.76 C ATOM 1199 OE1GLUA!95 2.217-45.345-12.597 1.0071.25 0 ATOM 1200 OE2 GLU A 195 1.795 -44.968 -10.479 1.00 70.87 0 * *. ATOM 1201 C GLUA 195 4.353-47.238-13.433 1.00 69.31 C ATOM 12020 GLUA 195 5.439-47.641.13.016 1.0069.43 0 . : ATOM 1203 N ILEA 196 4.198-46.047-14.013 1.00 69.37 N * ** ATOM 1204 CA ILE A 196 5.286.45.058 -14.048 1.00 69.32 C ATOM 1205 CB ILEA 196 5.806-44.760-15.486 1.00 69.37 C ATOM 1206 CG1 ILE A 196 6.278 -46.045 -16.167 1.00 69.3! C ATOM 1207 CDI ILE A 196 7.156 -45.796 -17.375 1.00 69.52 C ATOM 1208 CG2 ILE A 196 6.960 -43.749-15.449 1.00 69.16 C ATOM 1209 C ILEA 196 4.873-43.763-13.341 1.0069.13 C ATOM 12100 ILEA 196 4.292-42.853-13.938 1.0069.00 0 ATOM 1211 N SERA 197 5.186-43.707-12.053 1.00 68.93 N ATOM 1212 CA SERA 197 4.839-42.579-11.215 1.0068.80 C ATOM 1213 CB SER A 197 5.212 -42.892 -9.771 1.00 68.89 C ATOM 1214 OG SERA 197 6.584-43.236 -9.679 1.00 68.92 0 ATOM 1215 C SERA 197 5.542 -41.299-11. 643 1.00 68.69 C ATOM 12160 SERA 197 6.556-41.331-12345 1.0068.50 0 ATOM 1217 N ASPA 198 4.988-40.174-11.201 1.0068.61 N ATOM 1218 CA ASPA 198 5.579-38.869-11.439 1.0068.54 C ATOM 1219 CB ASP A 198 4.708 -37.785 -10.802 1.00 68.63 C ATOM 1220 CG ASP A 198 5.29 1 -36.394 -10.965 1 00 69.32 C ATOM 1221 OD1 ASPA 198 6.289-36.245 -11.704 1.00 69.90 0 ATOM 1222 0D2 ASP A 198 4.747 -35.445 -10.354 1.00 70.07 0 ATOM 1223 C ASPA 198 6.996-38.830-10.866 1.00 68.35 C ATOM 1224 0 ASPA 198 7.959-38.466-11.560 1.00 68.12 0 ATOM 1225 N GLUA 199 7.116-39.220 -9.600 1.00 68.16 N ATOM 1226 CA GLUA 199 8.406-39.264 -8.926 1.00 68.12 C ATOM 1227 CB GLUA 199 8.256-39.928 -7.558 1.00 68.13 C ATOM 1228 CG GLUA 199 9.527-39.956 -6. 717 1.00 68.49 C ATOM 1229 CD GLUA 199 9.283-40.500 -5.315 1.00 68.60 C ATOM 1230 OE1 GLU A 199 8.391 -39.966 -4.618 1.00 69.43 0 ATOM 1231 0E2 GLU A 199 9.983 -41.456 -4.908 1.00 68.91 0 ATOM 1232 C GLUA 199 9.450-39.994 -9.774 1.00 67.92 C ATOM 1233 0 GLUA 199 10.610-39.567 -9.861 1.00 67.83 0 ATOM 1234 N PHE A 200 9.034 -41.082 -10.418 1.00 67.72 N ATOM 1235 CA PHEA200 9.947-41.851 -11.255 1.0067.53 C ATOM 1236 CB PHEA200 9.287-43.134-11.753 1.0067.63 C ATOM 1237 CG PHEA200 10.212-44.319-11.781 1.0067.69 C ATOM 1238 CDI PHE A 200 9.890 -45.482 -11.102 1.00 67.87 C ATOM 1239 CE! PHE A 200 10.742 -46.574 -11.129 1.00 68.11 C ATOM 1240 CZ PHE A 200 11.934 -46.505 -11.828 1.00 67.82 C ATOM 1241 CE2PHEA200 12,269-45.35! -12.499 1.00 67.56 C ATOM 1242 CD2 PHE A 200 11.411 -44.267 -12.474 1.00 67.81 C ATOM 1243 C PHE A 200 10.455 -41.020 -12.432 1.00 67.43 C ATOM 1244 0 PHE A 200 11.660-40.823 -12.581 1.00 67.23 0 ATOM 1245 N SERA 201 9.541 -40.522 -13.262 1.00 67.37 N ATOM 1246 CA SER A 201 9. 940 -39.690 -14.399 1.00 67.44 C ATOM 1247 CB SERA 201 8.729-39.271 -15.239 1.00 67.44 C ATOM 1248 OG SERA 201 7.921 -38.337-14.551 1.00 67.77 0 ATOM 1249 C SERA 201 10.758-38.471 -13.956 1.00 67.32 C ATOM 1250 0 SERA2O1 11.566-37.939-14.726 1.0067.15 0 ATOM 1251 N GLU A 202 10.546 -38.033 -12.716 1.00 67.40 N * ATOM 1252 CA GLUA 202 11.424-37.031-12.113 1.0067.29 C 40 ATOM 1253 CB GLU A 202 10.885 -36.581 -10.754 1.00 67.36 C ATOM 1254 CG GLUA2O2 9.975-35.366-10.803 1.0067.70 C ATOM 1255 CD GLU A 202 10.675 -34.096 -10.356 1.00 68.43 C ** S ****** ATOM 1256 OEIGLUA2O2 11.599-34.193 -9.520 1.0068.71 0 ATOM 1257 0E2 GLU A 202 10.296 -33.000 -10.828 1.00 68.82 0 ATOM 1258 C GLUA 202 12.832-37602-11.957 1.0067.11 C ATOM 1259 0 GLU A 202 13.824 -36.963 -12.332 1.00 66.97 0 * ** ATOM 1260 N ALAA2O3 12.916-38.811-11.411 1.0067.08 N ATOM 1261 CA ALAA2O3 14.206-39.491 -11.281 1.00 66.87 C * ATOM 1262 CB ALA A 203 14.030 -40. 842 -10.595 1.00 66.88 C ATOM 1263 C ALAA2O3 14.920-39.656-12.633 1.0066.81 C ATOM 1264 0 ALAA2O3 16.110-39.327-12.771 1.0066.36 0 ATOM 1265 N ILE A 204 14.189 -40.164 -13.627 1.00 66.84 N ATOM 1266 CA ILE A 204 14.736 -40.312 -14.977 1.00 66.68 C ATOM 1267 CB ILEA2O4 13.766-41.034-15.925 1.0066.55 C ATOM 1268 CG1 ILE A 204 13.592 -42.485 -15.493 1.00 66.77 C ATOM 1269 CDI ILEA 204 12.277-42.763-14.821 1.00 67.14 C ATOM 1270 CG2 ILE A 204 14.282 -40.998 -17.345 1.00 66.27 C ATOM 1271 C!LEA2O4 15.125-38.957-15.567 1.0066.71 C ATOM 1272 0 ILEA2O4 16.102-38.850-16.312 1.0066.75 0 ATOM 1273 N GLY A 205 14.359 -37.922 -15.235 1.00 66.74 N ATOM 1274 CA GLYA2O5 14.763-36.565-15575 1.0066.51 C ATOM 1275 C GLY A 205 16.115 -36.275 -14.946 1.00 66.38 C ATOM 1276 0 GLY A 205 16.957 -35.597 -15.541 1.00 66.39 0 ATOM 1277 N ALA A 206 16.326 -36.806 -13.743 1.00 66.29 N ATOM 1278 CA ALA A 206 17.573 -36.575 -13.006 1.00 65.87 C ATOM 1279 CR ALAA2O6 17.366-36.813-11.515 10065.95 C ATOM 1280 C ALAA2O6 18.743-37.407-13.518 1.0065.58 C ATOM 1281 0 ALAA2O6 19.900-37.072-13.280 1.00 65.48 0 ATOM 1282 N LEUA2O7 18.446-38.499-14.210 1.0065.49 N ATOM 1283 CA LEU A 207 19.506 -39.322 -14.795 1.00 65.08 C ATOM 1284 CB LEU A 207 19.040 -40.769 -14.948 1.00 65.03 C ATOM 1285 CG LEU A 207 19.398 -41.743 -13.823 1.00 65.05 C ATOM 1286 CD! LEUA2O7 19.471 -41.051 -12.472 1.00 65.29 C ATOM 1287 CD2 LEU A 207 18.398 -42.885 -13.782 1.00 65.61 C ATOM 1288 C LEUA2O7 20.009-38.785-16.136 1.0064.97 C ATOM 1289 0 LEU A 207 20.904 -39.364 -16.750 1.00 64.88 0 ATOM 1290 N ARG A 208 19.433 -37.674 -16.582 1.00 64.92 N ATOM 1291 CA ARG A 208 19.771 -37.083 -17.879 1.00 64.83 C ATOM 1292 CB ARGA2O8 19.025-35.751-18.064 1.0064.82 C ATOM 1293 CO ARG A 208 19.634 -34.791 -19.087 1.00 64.69 C ATOM 1294 CD ARG A 208 18.525 -34.039 -19.840 1.00 64.59 C ATOM 1295 NE ARGA2O8 18.746-32.581 -19.922 1.0064.85 N ATOM 1296 CZ ARGA2O8 19.843-31.934-19.505 1.0064.78 C ATOM 1297 NHL ARG A 208 20.873 -32.594 -18.958 1.00 65.02 N ATOM 1298 NH2 ARG A 208 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 0 ARG A 208 21.993 -36.423 -17.218 1.0064.84 0 ATOM 1301 N GLY A 209 2 1.753 -37.327 -19.266 1.00 64.60 N ATOM 1302 CA GLYA2O9 23.163-37.188-19.622 1.0064.23 C ATOM 1303 C GLYA2O9 23.947-38.455-19.352 1.0063.99 C ATOM 13040 GLYA2O9 25.131-38.553-19.677 1.0063.84 0 ATOM 1305 N HIS A 210 23.28! -39.431 -18.749 1.00 63.86 N ATOM 1306 CA HIS A 210 23.932 -40.685 -18.408 1.00 63.78 C ATOM 1307 CB HIS A 210 24.183 -40.769 -16.900 1.00 63.93 C ATOM 1308 CG HISA21O 25.189-39.779-16.401 1.0064.53 C * * * *** ATOM 1309 ND!HISA2!0 24.880-38.807-15.474 1.0065.05 N ATOM 1310 CE1HISA2IO 25.955-38.079-15.228 1.0065.36 C 40 ATOM 1311 NE2HISA2IO 26.949-38.540-15.967 1.0065.43 N ATOM 1312 CD2HISA2IO 26.496-39.602-16. 711 1.0065.12 C ATOM 1313 C HISA2IO 23.132-41.891-18.878 1.0063.46 C ATOM 1314 0 HISA21O 23.308-42.996-18.366 1.0063.56 0 *....: ATOM 1315 N GLUA 211 22.26! -41.682-19.860 1.00 63.02 N * 45 ATOM 1316 CA GLUA2II 21.438-42.767-20.373 1.00 62.65 C * ** ATOM 1317 CB GLUA2LI 20.582-42.298-21.548 1.0062.67 C ATOM 1318 CG GLUA2I! 21.011-40.968-22. 133 1.0063.51 C ** * ATOM 1319 CD GLUA2I1 20.239-39.803-21.542 1.00 64.41 C ATOM 1320 OEIGLUA21! 20.737-38.656-21.593 1.0064.72 0 ATOM 1321 OE2GLUA2II 19.126-40.038-21.027 1.0064.94 0 ATOM 1322 C GLU A 211 22.26! -43.999 -20.756 1.00 62.27 C ATOM 1323 0 GLUA2!1 21.780-45.128-20.648 1.0062.45 0 ATOM 1324 N ASPA2I2 23.502-43.786-21.182 1.0061.63 N ATOM 1325 CA ASPA212 24.356-44.897-21.600 1.0061.13 C ATOM 1326 CB ASPA212 25.658-44.381 -22.206 10061.30 C ATOM 1327 CG ASP A 212 26.499 -43.615 -21.207 1.00 62.39 C ATOM 1328 OD1 ASP A 212 26.292 -42.385 -21.076 1.00 63.83 0 ATOM 1329 0D2 ASP A 212 27.374 -44.239 -20.56! 1.00 63.08 0 ATOM 1330 C ASPA2I2 24.664-45.858-20.455 1.0060.47 C ATOM 1331 0 ASPA2I2 25.109-46.983-20.681 1.0060.32 0 ATOM 1332 N LYS A 213 24.427 -45.410 -19.229 1.00 59.79 N ATOM 1333 CA LYSA 213 24.701 -46.226-18.058 1.00 59.18 C ATOM 1334 CD LYSA2I3 25.212-45.361-16.909 1.0059.14 C ATOM 1335 CO LYS A 213 26.566 -44.724 -17.136 1.00 59.05 C ATOM 1336 CD LYSA2I3 27.080-44.131 -15.831 1.0059.11 C ATOM 1337 CE LYSA213 28.308-43.262-16.033 1.0058.78 C ATOM 1338 NZ LYS A 213 28.643 -42.542 -14.778 1.00 58.30 N ATOM 1339 C LYS A 213 23.456 -46.962 -17.601 1.00 58.86 C ATOM 1340 0 LYSA213 23.464-47.627-16.568 1. 00 58.84 0 ATOM 1341 N ILE A 214 22.384 -46.851 -18.372 1.00 58.47 N ATOM 1342 CA ILEA214 21.099-47.377-17.935 1.0058.17 C ATOM 1343 CB ILE A 214 19.967 -46.389 -18.249 1.00 58.12 C ATOM 1344 CG1 ILEA214 20.170-45.098-17.459 1.0058.10 C ATOM 1345 CD1ILEA214 19.152-44.022-17. 765 1.0058.21 C ATOM 1346 CG2 ILE A 214 18.622 -47.009 -17.924 1.00 58.27 C ATOM 1347 C ILEA 214 20.745 -48.735 -18.53 1 1.00 57.94 C ATOM 1348 0 ILE A 214 20.731 -48.908 -19.746 1.00 58.08 0 ATOM 1349 N ARG A 215 20.460 -49.698 -17.664 1.00 57.63 N ATOM 1350 CA AROA2I5 19.861-50.946-18.101 1.0057.37 C ATOM 1351 CB ARGA2I5 20.675-52.152-17.641 1.00 57.18 C ATOM 1352 CG ARGA2I5 22.111-52.145-18.072 1.00 56.81 C ATOM 1353 CD ARG A 215 22.266 -51.984 -19.569 1.00 56.23 C ATOM 1354 NE ARGA215 23.676-51.817-19.905 1.0056.42 N ATOM 1355 CZ ARG A 215 24.302 -50.645 -19.933 1.00 56.18 C ATOM 1356 NH! ARG A 215 23.640 -49.527 -19.664 1.00 56.41 N ATOM 1357 NH2 ARG A 215 25.590 -50.59 1 -20.234 1.00 55.83 N ATOM 1358 C ARGA2I5 18.472-51.029-17.503 1.00 57.38 C ATOM 1359 0 ARGA215 18.320-51.179-16.287 1.00 57.59 0 ATOM 1360 N VALA216 17.461-50.913-18. 357 1.0057.17 N ATOM 1361 CA VALA 216 16.075-51.040-17.934 1.00 56.79 C ATOM 1362 CB VALA 216 15.154-50.313-18.912 1.00 56.68 C ATOM 1363 CG1 VAL A 216 13.703 -50.608 -18.590 1.00 56.77 C ATOM 1364 CG2VALA216 15.431 -48.823-18.886 1.00 56.69 C ATOM 1365 C VALA216 15.688-52.506-17.941 1.0056.67 C ATOM 1366 0 VALA2L6 15.659-53.124-18.999 1.0056.91 0 :. ATOM 1367 N VALA 217 15.395 -53.079 -16.778 1.00 56.39 N * .. ATOM 1368 CA VALA 217 14.980-54.478-16.760 1.00 56.08 C ATOM 1369 CB VALA2I7 15.906-55.381-15.905 1.0056.09 C ATOM 1370 CGI VALA 217 17.104-54.600-15.412 1.00 55.83 C ATOM 1371 CG2VALA217 15.148-56.004-14.745 1.0056.09 C ATOM 1372 C VALA2I7 13.529-54.632-16.335 1.0056.01 C ATOM 1373 0 VALA2I7 13.112-54.152-15.275 1.0056.14 0 ATOM 1374 N LEUA 218 12.766-55.297-17.195 1.0055.76 N ATOM 1375 CA LEUA218 11.364-55.593-16.950 1.0055.35 C * ** ATOM 1376 CD LEU A 218 10.622 -55.634 -18.279 1.00 55.27 C ATOM 1377 CO LEUA2I8 9.189-56.137-18.354 1.0055.27 C *. : ATOM 1378 CDI LEUA 218 8.248-55.189-17.639 1.00 55.39 C *

50 ATOM 1379 CD2LEUA218 8.817-56.270-19.817 1.00 55.68 C ATOM 1380 C LEUA218 11.261-56.926-16.213 1.0055.33 C ATOM 1381 0 LEUA2I8 11.388-58.006-16.799 1.0055.26 0 ATOM 1382 N ASNA2I9 11.040-56.830-14.911 1.0055.33 N ATOM 1383 CA ASNA2I9 11.089-57.970-14.018 1.0055.16 C ATOM 1384 CB ASN A 219 11.392-57.479-12.607 1.00 55.29 C ATOM 1385 CO ASNA2I9 12.091-58.516-11.774 1.0055.94 C ATOM 1386 ODI ASNA 219 12.474-59.575-12.282 1.00 56.02 0 ATOM 1387 ND2 ASN A 219 12.266 -58.225 -10.480 1.00 56.54 N ATOM 1388 C ASNA219 9.807-58.789-14.008 1.0055.04 C ATOM 1389 0 ASNA2I9 8.796-58.388-14.582 1.0054.74 0 ATOM 1390 N LYS A 220 9.868 -59.937 -13.337 1.00 55.21 N ATOM 1391 CA LYS A 220 8.744 -60.871 -13.202 1.00 55.41 C ATOM 1392 CB LYS A 220 7.898 -60.553 -11.958 1.0055.43 C ATOM 1393 CO LYS A 220 7.902 -59.096-11.540 1.00 55.52 C ATOM 1394 CD LYS A 220 8 157 -58 922 -10.043 1.00 55.10 C ATOM 1395 CE LYS A 220 6.892 -58.547 -9.289 1.00 55.18 C ATOM 1396 NZ LYS A 220 7.203 -57. 685 -8.115 1.00 54.26 N ATOM 1397 C LYSA22O 7.873-61.022-14.446 1.0055.67 C ATOM 1398 0 LYSA22O 6.652-61.107-14.352 1.00 55.78 0 ATOM 1399 N ALAA 221 8.513-61.082-15.610 1.00 56.06 N ATOM 1400 CA ALA A221 7.809-61.285-16. 872 10056.27 C ATOM 1401 CB ALAA 221 8.736-61.039-18.041 1.00 56.15 C ATOM 1402 C ALAA 221 7.241 -62.689-16.951 1.00 56.45 C ATOM 1403 0 ALA A 221 6.458 -62.996 -17.841 1.00 56.60 0 ATOM 1404 N ASPA222 7.636-63.540-16. 014 1.0056.79 N ATOM 1405 CA ASP A 222 7.225 -64.932 -16.043 1.00 57.20 C ATOM 1406 CB ASP A 222 8.254 -65.8 17 -15.346 1.00 57.26 C ATOM 1407 CO ASP A 222 8.054 -65.865 -13.841 1.00 58.12 C ATOM 1408 ODIASPA222 7.813-66.978-13.312 1.0058.75 0 ATOM 1409 OD2ASPA222 8.117-64.791-13.191 1.0058.98 0 ATOM 1410 C ASPA222 5.891-65.106-15.353 1.0057.37 C ATOM 1411 0 ASP A 222 5.334 -66.205 -15.334 1.00 57.48 0 ATOM 1412 N MET A 223 5. 380 -64.038 -14.759 1.00 57.52 N ATOM 1413 CA META223 4.135-64.182-14.030 1.0057.98 C ATOM 1414 CB META223 4.286-63.751-12.571 1.005798 C ATOM 1415 CG META223 4.396-62.271 -12.325 1.00 58.43 C ATOM 1416 SD META 223 4.202 -61968 -10.553 1.00 59.28 S ATOM 1417 CE META223 2.734-62.938-10.188 1.0059.20 C ATOM 1418 C MET A 223 2.975 -63.489 -14.720 1.00 57.63 C ATOM 1419 0 MET A 23 2.063 -62.975 -14.076 1.00 57.84 0 ATOM 1420 N VAL A 224 3.005 -63.5 14 -16.045 1.00 57.30 N ATOM 1421 CA VALA224 1.964-62.896-16.834 1.0056.98 C ATOM 1422 CB VALA 224 2.240-61.386-17.001 1.00 56.86 C ATOM 1423 CG1 VALA 224 2.971 -61.108-18.298 1.00 56.82 C a. ATOM 1424 CG2 VALA 224 0.953 -60.602 -16.936 1.00 56.98 C : ... ATOM 1425 C VAL A 224 1.892 -63.608 -18.183 1.00 56.86 C ATOM 1426 0 VALA 224 2.917-63.957-18.764 1.00 56.87 0 ATOM 1427 N GLUA225 0.682 -63.856-18.665 1.00 56.71 N ATOM 1428 CA GLU A 225 0.513 -64.536-19.937 1.00 56.69 C ... ATOM 1429 CB GLUA225 -0.968-64.682-20.256 1.0057.01 C ATOM 1430 CG GLU A 225 -1.282 -65.935 -21.035 1.00 58.92 C ATOM 1431 CD GLUA 225 -1.499-67.130-20.129 1.00 61.73 C * 45 ATOM 1432 OE1 GLU A 225 -0.506 -67.8 12 -19.773 1.00 62.80 0 ATOM 1433 OE2GLUA225 -2.671 -67.378-19.761 1.0063.64 0 ATOM 1434 C GLUA 225 1.213-63.731 -21.029 1.00 56.21 C ** , ATOM 1435 0 GLU A 225 1.305 -62.5 12 -20.935 1.00 56.09 0 : ATOM 1436 N THRA 226 1.692-64.399-22.071 1.00 55.84 N ATOM 1437 CA THRA 226 2.587-63.730-23.022 1.00 55.74 C ATOM 1438 CB THR A 226 3.293 -64.7 15 -23.989 1.00 55.64 C ATOM 1439 001 THRA 226 3.317-64.152 -25.306 1.00 55.50 0 ATOM 1440 CG2 THR A 226 2.580 -66.054 -24.02 1 1.00 56.27 C ATOM 1441 C THRA226 2.027-62.487-23.756 1.0055.65 C ATOM 1442 0 THRA226 2.646-61.416-23.715 1.0055.72 0 ATOM 1443 N GLNA227 0.882-62.618-24.426 1.0055.48 N ATOM 1444 CA GLN A 227 0.245 -61.451 -25.055 1.00 55.18 C ATOM 1445 CB GLNA227 -1.218-61.737-25.375 1.00 55.14 C ATOM 1446 CG GLNA227 -1.496-62.165-26.797 1.0054.85 C ATOM 1447 CD GLN A 227 -2.945 -62.543 -26.991 1.00 54.43 C ATOM 1448 OEI GLN A 227 -3.545 -63.201 -26.136 1.00 53.99 0 ATOM 1449 NE2GLNA227 -3.523-62.124-28.111 1.0054.27 N ATOM 1450 C GLN A 227 0.309 -60.245 -24.126 1.00 55.20 C ATOM 1451 0 GLNA 227 0.738-59.151 -24.521 1.00 55.06 0 ATOM 1452 N GLN A 228 -0.130 -60.463 -22.888 1.00 55.21 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 1.00 55.25 C ATOM 1455 CG GLN A228 -0.485 -59.113 -19.350 1.00 55.38 C ATOM 1456 CD GLN A 228 -1.259 -57.832 -19.534 1.00 55.86 C ATOM 1457 OEI GLNA 228 -2.266-57.794-20.243 1.00 56.42 0 ATOM 1458 NE2 GLN A 228 -0.795 -56.769 -18.892 1.00 56.22 N ATOM 1459 C GLNA228 1.320-58.880-21.670 1.0055.39 C ATOM 1460 0 3LNA228 1.504-57.660-21.581 1.0055.39 0 ATOM 1461 N LEUA 229 2.316-59.761 -21.627 1.00 55.35 N ATOM 1462 CA LEUA229 3.707-59.320-21. 591 1.0055.42 C ATOM 1463 CB LEUA229 4.664-60.506-21.719 1.0055.40 C ATOM 1464 CO LEU A 229 5.986.60.430 -20.956 1.00 55.19 C ATOM 1465 CDI LEU A 229 7.025 -61.296 -2 1.644 1 00 55.13 C ATOM 1466 CD2 LEU A 229 6.476 -59.001 -20.843 1.00 54.53 C ATOM 1467 C LEU A 229 3.955 -58.334 -22.728 1.00 55.47 C ATOM 1468 0 LEU A 229 4.405 -57.209 -22.493 1.00 55.55 0 ATOM 1469 N MET A 230 3.646 -58.752 -23.955 1.00 55.41 N ATOM 1470 CA META23O 3.777-57.862-25.108 1.0055.26 C ATOM 1471 CB META23O 3.182.58.497-26.364 1.0055.44 C ATOM 1472 CO MET A 230 3.890 -59.763 -26.794 1.00 55.41 C ATOM 1473 SD MET A 230 5.663 -59.494 -26.963 1.00 56.86 S ATOM 1474 CE META 230 6.272 -61.082 -26.388 1.00 56.24 C ATOM 1475 C META 230 3.111 -56.523-24.830 1.00 55.18 C ATOM 1476 0 META23O 3.696-55.459.25.064 1.0055.12 0 ATOM 1477 N ARGA231 1.888.56.581-24.316 1.0055.12 N ATOM 1478 CA ARGA23I 1.164.55.368-23.947 1.0055.21 C ATOM 1479 CB ARG A 231 -0.186 -55.730 -23.330 1.00 55.10 C ATOM 1480 CO ARG A 231 -1.374 -55.530 -24. 259 1.00 55.70 C ATOM 1481 CD ARG A 231 -1.500.56.597 -25.332 1.00 56.51 C ATOM 1482 NE ARG A 231 -0.666 -56.309 -26.492 1.00 57.65 N ATOM 1483 CZ ARG A 231 -0.540 -57.120 -27.537 1.00 57.94 C * ATOM 1484 NHI ARG A 231.1.204 -58.268.27.570 1.0057.78 N ATOM 1485 NH2 ARG A 231 0.252.56.782 -28.546 1.00 58.31 N ATOM 1486 C ARGA231 1.969-54.457-23.005 1.0055.08 C ATOM 1487 0 ARGA231 2.166-53.258-23.284 1.0054.91. 0 ATOM 1488 N VALA232 2.443-55.032-21.901 1.0054.99 N **** ATOM 1489 CA VAL A 232 3.204 -54.267 -20.917 1.00 54.96 C ATOM 1490 CB VALA232 3.520-55.100-19.664 1.0054.88 C ATOM 1491 CG1 VALA 232 4.557-54.407-18.823 1.00 55.17 C * *. ATOM 1492 CG2VALA232 2.272-55.310-18.848 1.0055.17 C ATOM 1493 C VALA232 4.494-53.702-21.518 1.0054.91 C ** * ATOM 1494 0 VALA232 4.720-52.485-21.503 1.0054.68 0 ATOM 1495 N TYRA233 5.332-54.583-22.055 1.0054.85 N ATOM 1496 CA TYRA 233 6.549 -54.152 -22.724 1.00 54.67 C ATOM 1497 CB TYR A 233 7.164 -55.333 -23.470 1.00 54.48 C ATOM 1498 CG TYRA233 8.424-55.026-24.241 1.0054.61 C ATOM 1499 CDI TYRA 233 8.799-55.811 -25.321 1.00 54.70 C ATOM 1500 CE1 TYRA 233 9.948 -55.544 -26.035 1.00 54.44 C ATOM 1501 CZ TYRA 233 10.736-54.480-25.678 1.00 54.26 C ATOM 1502 OH TYR A 233 11.877-54.219-26.394 1.00 54.47 0 ATOM 1503 CE2 TYR A 233 10.388 -53.681 -24.612 1.00 54.50 C ATOM 1504 CD2 TYRA 233 9.237 -53.955 -23.898 1.00 54.77 C ATOM 1505 C TYR A 233 6.256 -52.964 -23.657 1.00 54.73 C ATOM 1506 0 TYRA 233 6.922 -5 1.909 -23.586 1.00 54.67 0 ATOM 1507 N GLY A 234 5.243 -53.129 -24.508 1.00 54.80 N ATOM 1508 CA GLY A 234 4.797 -52.047 -25.381 1.00 54.70 C ATOM 1509 C GLY A 234 4.565 -50.754 -24.615 1.00 54.80 C ATOM 15100 GLYA234 5.144-49.698-24.950 10054.91 0 ATOM 1511 N ALAA235 3.730-50.830-23.578 1.0054.65 N ATOM 1512 CA ALA A 235 3.434 -49.651 -22.763 1.00 54.39 C ATOM 1513 CB ALAA 235 2.500-50.015 -21.633 1.00 54.36 C ATOM 1514 C ALA A 235 4.708 -49.002 -22.216 1.00 54.45 C ATOM 1515 0 ALA A 235 4.913 -47.784 -22.345 1.00 54.48 0 ATOM 1516 N LEUA236 5.564-49.824-21.614 1.0054.43 N ATOM 1517 CA LEUA236 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 LEUA236 8.536-50.421 -19.362 1.00 54.14 C ATOM 1520 CD1 LEU A 236 8.970 -49.007 -19.059 1.00 54.03 C ATOM 1521 CD2LEUA236 9.735-51.350-19.443 1.00 53.68 C ATOM 1522 C LEU A 236 7.577 -48.558 -22.115 1.00 54.43 C ATOM 1523 0 LEU A 236 7.874 -47.383 -21.910 1.00 54.51 0 ATOM 1524 N META237 7.885-49.192-23.245 1.0054.66 N ATOM 1525 CA META 237 8.702-48.506-24.253 1.00 54.81 C ATOM 1526 CB META 237 9.112-49.435-25.395 1.00 54.86 C ATOM 1527 CG MET A 237 10.080 -50.528 -24.964 1.00 55.85 C ATOM 1528 SD MET A 237 11.647 -49.943 -24.265 1.00 57.46 S ATOM 1529 CE META 237 12.613-49.728-25.759 1.00 56.82 C ATOM 1530 C META 237 8.030-47.250-24.786 1.00 54.74 C ATOM 1531 0 META237 8.708-46.278-25.121 1.00 54.99 0 ATOM 1532 N TRPA 238 6.704-47.261 -24. 855 1.00 54.61 N ATOM 1533 CA TRP A 238 5.983 -46.061 -25.264 1.00 54.49 C ATOM 1534 CB TRPA238 4.496-46.358-25.263 1.0054.42 C ATOM 1535 CG 1'RPA238 3.815-45.961-26.503 1.0054.35 C ATOM 1536 CDI TRP A 238 3.955 -46.533 -27.733 1.00 54.85 C ATOM 1537 NE1 TRPA238 3.148-45.899-28.647 1.00 54.83 N ATOM 1538 CE2 TRP A 238 2.463 -44.903 -28.006 1.00 54.14 C ATOM 1539 CD2 TRP A 238 2.861 -44.916 -26.652 1.00 53.92 C ATOM 1540 CE3TRPA238 2.304-43.991-25.776 1.0053.71 C : ATOM 1541 CZ3 TRP A 238 1.388 -43.100 -26.265 1.00 54.62 C ATOM 1542 CH2TRPA238 1.014-43.109-27.617 1.0054.60 C ATOM 1543 CZ2 1'RP A 238 1.539 -44.004 -28.499 1.00 54.05 C ATOM 1544 C TR.P A 238 6.263 -44.921 -24.287 1.00 54.52 C ATOM 1545 0 TRPA238 6.752-43.827-24.653 1.0054.67 0 ATOM 1546 N ALAA239 5.951-45.206-23.028 1.0054.59 N ATOM 1547 CA ALA A 239 6.148 -44.262 -21.941 1.00 54.74 C S.....</p>..DTD: <p>* * 45 ATOM 1548 CB ALA A 239 5.781 -44.915 -20.617 1.00 54.68 C ATOM 1549 C ALA A 239 7.583 -43.746 -2 1.904 1.00 54.79 C ATOM 1550 0 ALAA239 7.828-42.547-22.071 1.0055.14 0 ATOM 1551 N LEUA 240 8.525-44.661 -21.680 1.00 54.72 N . : ATOM 1552 CA LEUA 240 9.939-44.311 -21.643 1.00 54.66 C * 50 ATOM 1553 CB LEUA24O 10.807-45.565-21.563 1.0054.59 C ATOM 1554 CG LEU A 240 10.956 -46.206 -20.184 1.00 54.30 C ATOM 1555 CD1 LEU A 240 11.936-47.363 -20.250 1.00 54.48 C ATOM 1556 CD2LEUA24O 11.408-45.186-19.152 1.0053.92 C ATOM 1557 C LEU A 240 10.3 17 -43.482 -22.860 1.00 54.72 C ATOM 1558 0 LEUA24O 10.939-42.429-22.729 1.0054.60 0 ATOM 1559 N GLY A 241 9.933 -43.962 -24.040 1.00 54.91 N ATOM 1560 CA GLY A 241 10.086 -43.188 -25.263 1.00 55.18 C ATOM 1561 C GLY A 241 9.742 -41.726 -25.038 1.00 55.50 C ATOM 1562 0 GLY A 241 10.590 -40.842 -25.229 1.00 55.56 0 ATOM 1563 N LYSA242 8.503-41.464-24.621 1.0055.54 N ATOM 1564 CA LYSA242 8.070-40.079-24.365 1.0055.84 C ATOM 1565 CB LYS A 242 6.564 -40.037 -24.078 1.00 55.91 C ATOM 1566 CG LYSA242 6.106-38.929-23.139 1.0056.07 C ATOM 1567 CD LYS A 242 5.977 -37.59 1 -23.848 1.00 56.51 C ATOM 1568 CE LYS A 242 5.135 -36.620 -23.03 1 1.00 56.40 C ATOM 1569 NZ LYSA242 3.736-37.109-22.882 1.0056.49 N ATOM 1570 C LYSA242 8.859-39.370-23.249 1.0056.01 C ATOM 1571 0 LYS A 242 9.107 -38.168 -23.328 1.00 55.92 0 ATOM 1572 N VALA 243 9.264 -40.121 -22.227 1.00 56. 28 N ATOM 1573 CA VALA243 9.903-39.540-21.034 1.0056.96 C ATOM 1574 CB VAL A 243 9.818 -40.487 -19.809 1.00 57.04 C ATOM 1575 CGI VALA 243 10.420-39.818-18.572 1.00 56.83 C ATOM 1576 CG2 VALA 243 8.375 -40.904 -19.550 1.00 57.52 C ATOM 1577 C VAL A 243 11.363 -39.111 -21.205 1.00 57.22 C ATOM 1578 0 VAL A 243 11.674 -37.939 -21 023 1.00 57.33 0 ATOM 1579 N VALA 244 12.256-40.051 -21 528 1.00 57.66 N ATOM 1580 CA VAL A 244 13.693 -39.748 -21.602 1.00 58.09 C ATOM 1581 CB VALA244 14.578-41.016-21.585 1.0057.99 C ATOM 1582 CG1 VALA 244 13.898-42.136-20.823 1.00 58.05 C ATOM 1583 CG2 VAL A 244 14.902 -41.459 -22.988 1.00 57.87 C ATOM 1584 C VAL A 244 14.057 -38.882 -22.8 12 1.00 58.63 C ATOM 1585 0 VAL A 244 15.063 -38.174 -22.79 1 1.00 58.67 0 ATOM 1586 N GLY A 245 13.247 -38.957 -23.866 1.00 59.32 N ATOM 1587 CA GLYA245 13.291 -37.975-24.960 1.00 60.12 C ATOM 1588 C GLY A 245 14.427 -38.053 -25.967 1.00 60.64 C ATOM 1589 0 GLY A 245 14.404 -37.358 -26.987 1.00 60.52 0 ATOM 1590 N THRA246 15.422-38.891-25.681 1.0061.23 N ATOM 1591 CA THR A 246 16.545 -39.111 -26.594 1.00 61.72 C ATOM 1592 CB THRA 246 17. 713 -39.822 -25.877 1.00 61.77 C ATOM 1593 OGI THRA 246 18.778 -40.049 -26. 807 1.00 62.38 0 ATOM 1594 CG2THRA246 17.264-41.160-25.307 1.0061.63 C ATOM 1595 C THRA246 16.109-39.947-27.803 1.0061.92 C ATOM 1596 0 THRA 246 15.279-40.838-27.666 1.00 61.87 0 ATOM 1597 N PRO A 247 16.652 -39.646-28.998 1.00 62.13 N ATOM 1598 CA PRO A 247 16.324 -40.447 -30.180 1.00 62.22 C ATOM 1599 CB PR0A247 16.935-39.644-31.338 1.0062.11 C ATOM 1600 CG PROA 247 17.223-38.284-30.771 1.00 62.24 C ATOM 1601 CD PR0A247 17.556-38.535-29.333 1.0062.13 C ATOM 1602 C PROA247 16.922-41.857-30.135 1.0062.38 C ATOM 1603 0 PR0A247 16.518-42.714-30921 1.0062.55 0 ATOM 1604 N GLU A 248 17.869 -42.095 -29.228 1.00 62.37 N : ATOM 1605 CA GLU A 248 18454-43.427-29.065 1.00 62.39 C * 45 ATOM 1606 CB GLU A 248 19.928 -43.337 -28.665 1.00 62.54 C * ** ATOM 1607 CG GLU A 248 20.752 -42.415 -29.542 1.00 63.55 C ATOM 1608 CD GLUA248 20.801 -41.000-29.002 1.0064.86 C ATOM 1609 OEI GLU A 248 20.533 -40.048 -29.772 1.00 65.06 0 ATOM 1610 OE2 GLU A 248 21.103 -40.844 -27.798 1.00 65.69 0 ATOM 1611 C GLUA248 17.687-44.235-28.030 1.0062.14 C ATOM 1612 0 GLUA 248 17.524-43.801 -26.892 1.00 62.25 0 ATOM 1613 N VALA 249 17.234-45.419-28.429 1.00 61.87 N ATOM 1614 CA VALA249 16.374-46.254-27.590 1.0061.58 C ATOM 1615 CB VALA249 15.486-47.184-28.459 1.0061.51 C ATOM 1616 CGI VALA 249 16.221 -47.608 -29.720 1.00 61.83 C ATOM 1617 CG2 VAL A 249 15.035 -48.396 -27.674 1.00 61.54 C ATOM 1618 C VALA249 17.134-47.072-26.538 1.0061.44 C ATOM 1619 0 VALA 249 18.170-47.671 -26.823 1.00 61.45 0

I

ATOM 1620 N LEU A 250 16.608 -47.082 -25.3 18 1.00 61.36 N ATOM 1621 CA LEU A 250 17.189 -47.851 -24.224 1.00 61.27 C ATOM 1622 CB LEU A 250 16.662 -47.347 -22.88 1 1.00 61.02 C ATOM 1623 CG LEU A 250 17.582 -46.481 -22.021 1.00 60.92 C ATOM 1624 CD1 LEU A 250 18.366 -45.482 -22.848 1.00 61.76 C ATOM 1625 CD2 LEU A 250 16.777 -45.765 -20.962 1.00 61.02 C ATOM 1626 C LEUA25O 16.888-49.335-24.361 1.00 61.49 C ATOM 1627 0 LEUA25O 15.789-49.725-24.754 1.0061.64 0 ATOM 1628 N ARGA251 17.871-50.161-24.025 1.0061.69 N ATOM 1629 CA ARGA 251 17.693-51.606-24.018 1.00 61.74 C ATOM 1630 CB ARG A 251 19.060 -52.294 -24.056 1.00 61.77 C ATOM 1631 CG ARG A 251 19.056 -53.780 -23.705 1.00 61.82 C ATOM 1632 CD ARGA25I 18.614-54.629-24.885 1.0061.89 C ATOM 1633 NE ARGA25I 19.429-55.833-25.010 1.0061.71 N ATOM 1634 CZ ARGA25I 19.057-57.040-24.598 1.0061.63 C ATOM 1635 NH1 ARGA251 17.874-57.216-24.030 1.00 61.74 N ATOM 1636 NH2ARGA 251 19.875-58.072-24.751 1.00 61.58 N ATOM 1637 C ARG A 251 16.946 -52.033 -22.762 1.00 61.79 C ATOM 16380 ARGA25L 17.320-51.641-21.656 1.0061.72 0 ATOM 1639 N VALA 252 15.890-52.825 -22.929 1.00 61.91 N ATOM 1640 CA VALA 252 15.265-53.487-21.778 1.00 62.11 C ATOM 1641 CB VAL A 252 13.724 -53.317 -21.741 1.0062.15 C ATOM 1642 CG1 VALA2S2 13.357-51.846-21.684 1.0062.31 C ATOM 1643 CG2 VAL A 252 13.085 -53.976 -22.949 1.00 62.44 C ATOM 1644 C VALA2S2 15,625-54.972-21.739 1.0061.92 C ATOM 1645 0 VAL A 252 15.675 -55.633 -22.776 1.00 61.98 0 ATOM 1646 N TYR A 253 15.894 -55.482 -20.541 1.00 61.76 N ATOM 1647 CA TYRA 253 16.191 -56.898 -20.351 1.00 61.60 C ATOM 1648 CB 1'YRA 253 17.414-57.072-19.449 1.00 61.60 C ATOM 1649 CG TYR A 253 18.679 -56.478 -20.036 1.00 62.19 C ATOM 1650 CDI TYR A 253 19.206 -55.293 -19.549 1.00 62.55 C ATOM 1651 CE1 TYR A 253 20.359 -54. 749 -20.091 1.00 62.44 C ATOM 1652 CZ TYRA253 20.993-55.384-21.132 1.00 61.97 C ATOM 1653 OH TYR A 253 22.139 -54.844 -21.673 1.00 62.06 0 ATOM 1654 CE2 TYR A 253 20.490 -56.557 -2 1.632 1.00 62.23 C ATOM 1655 CD2 TYRA 253 19.341 -57.098 -21.088 1.00 62.57 C ATOM 1656 C TYRA253 14.976-57.588-19.749 1.0061.37 C * .** ATOM 1657 0 TYRA 253 14.563-57.252-18.640 1.00 61.52 0 ATOM 1658 N ILE A 254 14.400 -58.539 -20.484 1.00 60.85 N ATOM 1659 CA 1LEA254 13.152-59.177-20.068 1.00 60.38 C ATOM 1660 CB ILE A 254 12.245 -59.455 -2 1.275 1.00 60.34 C ATOM 1661 CGLILEA254 12.301-58.278-22.251 1.0060.50 C **S.

ATOM 1662 CDI ILE A 254 11.238-58.319-23.329 1.00 60.93 C ATOM 1663 CG2 ILE A 254 10.82 1 -59.735 -20.821 1.00 59.77 C ATOM 1664 C ILE A 254 13.385 -60.486 -19.324 1.00 60.21 C * ** ATOM 1665 0 1LEA254 13.958-61.423-19.867 1.0060.30 0 ATOM 1666 N GLYA255 12.931-60.558-18.079 1.0059.92 N *. . ATOM 1667 CA GLY A 255 13.090 -61.789 -17.3 10 1.00 59. 62 C ATOM 1668 C GLYA255 12.484-61.725-15.923 1.0059.23 C ATOM 1669 0 0LYA255 11.792-60.766-15.585 1.0059.30 0 ATOM 1670 N SERA256 12.735-62.759-15.126 1.0058.78 N ATOM 1671 CA SER A 256 12.342 -62.757 -13.723 1.00 58.69 C ATOM 1672 CB SERA 256 11.081-63.593-13.486 1.00 58.72 C ATOM 1673 OG SERA256 11.098-64.776-14.260 1.0059.59 0 ATOM 1674 C SERA256 13.500-63.204-12.829 1.0058.34 C ATOM 1675 0 SERA 256 13.73 1 -64.392-12.606 1.00 58.22 0 ATOM 1676 N PHE A 257 14.207 -62.2 12 -12.305 1.00 58.01 N ATOM 1677 CA PHE A 257 15.459 -62.410 -11.606 1.00 57.54 C ATOM 1678 CB PHE A 257 16.256-61.107-11.660 1.0057.11 C ATOM 1679 CG PITEA 257 16.501 -60.627-13.062 1.00 56.81 C ATOM 1680 CDI PHE A 257 17.747 -60.763 -13.65 1 1.00 56.40 C ATOM 1681 CE! PHE A 257 17.969 -60.338 -14.950 1.00 55.40 C ATOM 1682 CZ PHEA 257 16.941 -59.781 -15.679 1.00 55.70 C ATOM 1683 CE2PHEA257 15.693-59.650-15.119 1.0055.89 C ATOM 1684 CD2 PHE A 257 15.473 -60.077 -13.813 1.00 56.91 C ATOM 1685 C PHE A 257 15.300 -62.948 -10.177 1.00 57.57 C ATOM 1686 0 PHE A 257 15.433 -62.2 16 -9.193 1.00 57.54 0 ATOM 1687 N TRPA258 15.008-64.243-10.090 1.0057.58 N ATOM 1688 CA TRP A 258 14.989 -64.966 -8.821 1.00 57.65 C ATOM 1689 CB TRP A 258 13.858 -64.464 -7.917 1.00 57.76 C ATOM 1690 CG TRP A 258 12.478 -64.843 -8.339 1.00 57.87 C ATOM 1691 CD! TRP A 258 12.077 -65.277 -9.572 1.00 58.43 C ATOM 1692 NEI TRPA 258 10.723 -65.520 -9.572 1.00 58.60 N ATOM 1693 CE2 TRP A 258 10.222 -65.229 -8.329 1.00 58.63 C ATOM 1694 CD2 TRP A 258 11.299-64.791 -7.530 1.00 58.19 C ATOM 1695 CE3TR.PA258 11.050-64.430 -6.201 1.0058.21 C ATOM 1696 CZ3 TRP A 258 9.753 -64.5 13 -5.720 1.00 58.20 C ATOM 1697 CH2TRPA258 8.703 -64.949 -6.539 1.00 58.12 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 00 57.67 C ATOM 1700 0 TRPA 258 14.436-66.937-10.093 1.00 57.71 0 ATOM 1701 N SER A 259 15.443 -67.254 -8.107 1.00 57.66 N ATOM 1702 CA SER A 259 15.578 -68.706 -8.285 1.00 57.55 C ATOM 1703 CB SER A 259 16.660 -69.255 -7.356 1.00 57.60 C ATOM 1704 OG SERA259 17.916-68.667 -7.651 1.0058.07 0 ATOM 1705 C SERA 259 14.274 -69.478 -8.081 1.00 57.36 C ATOM 1706 0 SERA259 14.283-70.686 -7.836 1.0057.37 0 ATOM 1707 N GLNA 260 13.156-68.775 -8.194 1.00 57.1! N ATOM 1708 CA GLN A 260 11.850 -69.384 -8.021 1.00 56.90 C ATOM 1709 CB GLN A 260 10.841 -68.302 -7.643 1.00 57.05 C ATOM 1710 CG GLN A 260 9.862 -68.687 -6.541 1.00 58.16 C ATOM 1711 CD GLN A 260 10.543 -68.952 -5.204 1.00 59.01 C ATOM 1712 OE1GLNA26O 11.611-68.404 -4.913 1.0059.19 0 ATOM 1713 NE2 GLN A 260 9.922 -69.798 -4.384 1.00 58.96 N ATOM 1714 C GLN A 260 11.441 -70.055 -9.327 1.00 56.43 C :. ATOM 1715 0 GLNA26O 11.879-69.640-10.396 1.00 56.50 0 * ATOM 1716 N PROA 261 10.623-71.113 -9.249 1.00 56.02 N ". 40 ATOM 1717 CA PROA 261 10.059-71.724-10.452 1.00 55.81 C **)* ATOM 1718 CB PROA 261 9.110-72.785 -9.893 1.00 55,75 C ATOM 1719 CG PROA261 9.690-73.132 -8.570 1.0055.87 C ATOM 1720 CD PRO A 261 10.223 -71.832 -8.030 1.00 56.03 C ATOM 172! C PROA26I 9.292-70.729-11. 319 1.00 55.59 C ATOM 1722 0 PROA261 8.921 -69.652-10.859 1.00 55.74 0 ATOM 1723 N LEUA262 9.057-71.092-12.570 1.0055.30 N * ** ATOM 1724 CA LEU A 262 8.463 -70.173 -13.518 1.00 55.12 C ** S **** ATOM 1725 CB LEU A 262 9.026 -70.457 -14.905 1.00 55.09 C *. : ATOM 1726 CG LEU A 262 9.764 -69.356 -15.667 1.00 54.85 C * . 50 ATOM 1727 CD! LEU A 262 10.497 -68.395 -14.74 1 1.00 54.87 C ATOM 1728 CD2 LEU A 262 10.742 -70.010 -16.607 1.00 54.29 C ATOM 1729 C LEU A 262 6.966 -70.386 -13.513 1.00 55.14 C ATOM 1730 0 LEUA262 6.508-71.518-13.615 1.0055.24 0 ATOM 1731 N LEUA263 6.198-69.309-13.379 1.0055.24 N ATOM 1732 CA LEU A 263 4.743 -69.433 -13.356 1.00 55.20 C ATOM 1733 CB LEU A 263 4.076 -68.110 -12.967 1.00 55.14 C ATOM 1734 CG LEU A 263 2.706 -68.176 -12.271 1.00 55.03 C ATOM 1735 CD! LEUA263 2.132-66.781 -12.099 1.00 54.72 C ATOM 1736 CD2 LEU A 263 1 706 -69.056 -13.010 1.00 55.07 C ATOM 1737 C LEU A 263 4.266 -69.875 -14.729 1.00 55.30 C ATOM 1738 0 LEUA263 3.879-71.025-14.921 1.0055.01 0 ATOM 1739 N VALA264 4.298-68.949-15.680 1.0055.62 N ATOM 1740 CA VALA264 3.950-69.260-17.059 1.0055.97 C ATOM 1741CB VALA264 3.016-68.194-17.669 1.0055.83 C ATOM 1742 CGI VALA 264 3.489-66.801 -17.317 1.00 55.89 C ATOM 1743 CG2VALA264 2.898-68.376-19.175 1.0056.05 C ATOM 1744 C VALA 264 5. 228 -69.448 -17.876 1.00 56.23 C ATOM 1745 0 VALA 264 5.882 -68.484 -18.251 1.00 56.29 0 ATOM 1746 N PR0A265 5.574-70.711-18.161 1.0056.68 N ATOM 1747 CA PROA 265 6.910-71.109-18.587 1.00 57.10 C ATOM 1748 CB PR0A265 6.917-72.607-18.282 1.0057.09 C ATOM 1749 CO PROA 265 5.512-73022-18.537 1.00 56.77 C ATOM 1750 CD PRO A 265 4.657 -7 1.863 -18.091 1.00 56.60 C ATOM 1751 C PRO A 265 7.228 -70.900 -20.067 1.00 57.60 C ATOM 1752 0 PRO A 265 8.402 -70.934 -20.449 1.00 57.55 0 ATOM 1753 N ASPA266 6.210-70.686-20.896 1.0058.11 N ATOM 1754 CA ASP A 266 6.421 -70.770 -22.341 1.00 58.60 C ATOM 1755 CB ASPA266 5.111-71.053-23.108 1.0058.96 C ATOM 1756 CG ASP A 266 3.967 -70.141 -22.702 1.00 59.26 C ATOM 1757 OD1 ASP A 266 4.064 -68.920 -22.943 1.00 60.12 0 ATOM 1758 OD2ASPA266 2.955-70.659-22.177 1.0059.63 0 ATOM 1759 C ASP A 266 7.205 -69.617 -22.951 1.00 58.63 C ATOM 1760 0 ASPA266 6.978-69.238-24.092 1.0058.80 0 ATOM 1761 N ASN A 267 8.151 -69.085 -22.190 1.00 58.79 N ATOM 1762 CA ASNA267 8.998 -68.002 -22.663 1.00 58.87 C ATOM 1763 CB ASN A 267 8.339 -66.657 -22.369 1.00 58.66 C ATOM 1764 CG ASN A 267 7.617 -66.102 -23.561 1.00 58.19 C ATOM 1765 ODI ASN A 267 8.090 -66.229 -24.686 1.00 58.89 0 ATOM 1766 ND2 ASNA 267 6.467 -65.483 -23.331 1.00 57.38 N ATOM 1767 C ASN A 267 10.387 -68.040 -22.037 1.00 59.27 C ATOM 1768 0 ASNA 267 11.117 -67.045 -22.065 1.00 59.19 0 ATOM 1769 N ARG A 268 10.763 -69.187 -2 1. 477 1.00 59.60 N ATOM 1770 CA ARG A 268 11.957-69.204-20.649 1.00 59.99 C ATOM 1771 CB ARGA26S 11.986-70.400-19.683 1.0060.07 C ATOM 1772 CG ARG A 268 12.662 -71.672 -20.115 1.00 60.90 C ATOM 1773 CD ARGA268 13.141-72.379-18.844 1.0063.18 C ATOM 1774 NE ARG A 268 13.096 -73.840 -18.898 1.00 65.28 N ATOM 1775 CZ ARG A 268 11.996-74.570-18.704 1.00 66.78 C ATOM 1776 NH1 ARG A 268 10.830 -73.975 -18.460 1.00 66.33 N ATOM 1777 NH2 ARG A 268 12.057 -75.902 -18.764 1.00 67.27 N ATOM 1778 C ARGA268 13.241-69.016-21.440 1.0060.01 C ATOM 1779 0 ARGA 268 14.156-68.351 -20.970 1.00 60.20 0 ATOM 1780 N ARG A 269 13.287 -69.550 -22.654 1.00 60.18 N ATOM 1781 CA ARGA269 14.414-69.298-23.548 1.00 60.31 C ATOM 1782 CB ARG A 269 14.079 -69.759 -24.967 1.00 60.47 C ATOM 1783 CO ARGA269 14.873-70.966-25.444 1.00 61.18 C S.... ATOM 1784 CD ARG A 269 16.252 -70.541 -25.953 1.00 62.47 C ATOM 1785 NE ARG A 269 17.234 -70.391 -24. 878 1.00 62.90 N ATOM 1786 CZ ARGA 269 18.457-70.919-24,900 1.00 62.99 C ATOM 1787 NHIARGA 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 ARGA269 14.784-67.818-23.554 1.0060.15 C : 55 ATOM 1790 0 ARGA269 15.943-67.449-23.343 1.0060.18 0 * S. ATOM 1791 N LEU A 270 13.781 -66. 978 -23.789 1.00 60.00 N ATOM 1792 CA LEUA27O 13.970-65.539-23.848 1.0059.87 C ATOM 1793 CB LEUA27O 12.637-64.857-24.150 1.0059.80 C ATOM 1794 CG LEU A 270 12.602 -63.460 -24 777 1.00 59.73 C ATOM 1795 CD1 LEU A 270 12.448 -62.370 -23.734 1.00 59.80 C ATOM 1796 CD2LEUA27O 13.817-63.214-25.654 1.00 59.78 C ATOM 1797 C LEU A 270 14.543 -65.031 -22.537 1.00 59.92 C ATOM 1798 0 LEU A 270 15.5 16 -64.287 -22.525 1.00 60.09 0 ATOM 1799 N PHE A 271 13.948 -65.455 -2 1.429 1.00 60.22 N ATOM 1800 CA PHEA 271 14.377-65.006-20.109 1.00 60.39 C ATOM 1801 CB PHEA27I 13.480-65.581-19.013 1.0060.47 C ATOM 1802 CG PHEA 271 12.029-65.224-19.166 1.00 60.39 C ATOM 1803 CDIPHEA27I 11.653-64.051-19.811 1.0060.01 C ATOM 1804 CE1PHEA27I 10319-63.716-19.953 1.0059.82 C ATOM 1805 CZ PHE A 271 9.341 -64.546 -19.432 1.00 60.43 C ATOM 1806 CE2PHEA27I 9.702-65.718-18.778 1.0060.27 C ATOM 1807 CD2PHEA27I 11.042-66.049-18.646 1.0060.08 C ATOM 1808 C PHEA27I 15.826-65.375-19.839 1.0060.56 C ATOM 1809 0 PHE A 271 16.629 -64.523 -19.432 1.00 60.91 0 ATOM 1810 N GLU A 272 16.172 -66.638 -20.064 1.0060.53 N ATOM 1811 CA GLUA272 17.557-67.032-19.881 1.00 60.88 C ATOM 1812 CB GLU A 272 17.780 -68.554 -19.987 1.00 60.68 C ATOM 1813 CO GLUA272 16.859-69.330-20.916 1.00 61.39 C ATOM 1814 CD GLUA272 17.054-70.852-20.801 1.0062.06 C ATOM 1815 OEI GLUA 272 16.525-71.608-21.655 1.00 63.50 0 ATOM 1816 OE2GLUA272 17.745-71.301-19.853 1.0064.06 0 ATOM 1817 C GLUA 272 18.472-66.221 -20.804 1.00 60.54 C ATOM 1818 0 GLU A 272 19.500 -65.707 -20.365 1.00 60.78 0 ATOM 1819 N LEU A 273 18.082 -66.061 -22.064 1.00 60.28 N ATOM 1820 CA LEU A 273 18.885 -65.255 -22.979 1.00 60.15 C ATOM 1821 CB LEU A 273 18.265 -65.249 -24.378 1.00 60.05 C ATOM 1822 CG LEU A 273 19.067 -66.013 -25.429 1.00 59.60 C ATOM 1823 CDI LEU A 273 20.50 1 -65.525 -25.383 1.00 60.64 C ATOM 1824 CD2 LEU A 273 19.023 -67.492 -25.195 1.00 59.04 C ATOM 1825 C LEU A 273 19.135 -63.8 19 -22.481 1.00 60.30 C ATOM 1826 0 LEU A 273 20.285 -63.350 -22.429 1.00 60.39 0 ATOM 1827 N GLUA 274 18.059-63.128-22.114 1.00 60.35 N ATOM 1828 CA GLU A 274 18.162 -61.747 -21.656 1.00 60.63 C ATOM 1829 CB GLU A 274 16.774 -61.173 -21.378 1.00 60.61 C ATOM 1830 CO GLU A 274 15.841 -61.133 -22.589 1.00 61.23 C ATOM 1831 CD GLUA 274 16.125 -59.970-23.531 1.00 62.07 C ATOM 1832 OEI GLU A 274 15.475 -58.910 -23.376 1.00 62.22 0 ATOM 1833 OE2GLUA274 16.996-60.115-24.421 1.0062.05 0 ATOM 1834 C GLU A 274 19.025 -61.672 -20.402 1.00 60.74 C ATOM 1835 0 GLUA274 19.923-60.821 -20.280 1.0060.90 0 :. ATOM 1836 N GLUA275 18.752-62.578-19.473 1.0060.89 N * ATOM 1837 CA GLUA275 19.561-62.697-18.276 1.0061.09 C ATOM 1838 CB 0LUA275 19.106-63.919-17.491 1.0061.28 C ATOM 1839 CG 0LUA275 19.561-63.971-16. 051 1.0062.13 C ATOM 1840 CD GLU A 275 19.147 -65.272 -15.391 1.00 63.38 C ATOM 1841 OEIGLUA275 19.938-65.821-14.587 1.0063.96 0 ATOM 1842 OE2GLUA 275 18.033-65.757-15.698 1.00 63.30 0 *....: 50 ATOM 1843 C 6LUA275 21.037-62.822-18.658 1.0061.04 C * * ATOM 1844 0 GLUA275 21.896-62.138-18.102 1.0060.86 0 * *, ATOM 1845 N GLN A 276 21.323 -63. 688 -19.623 1.0061.18 N ATOM 1846 CA GLNA 276 22.689-63.863-20.110 1.00 61.56 C ** , ATOM 1847 CB GLN A 276 22.749-64.934 -21.207 1.00 61,86 C *. .: 55 ATOM 1848 CO GLNA276 22.828-66.357-20.681 1.0063.52 C ATOM 1849 CD GLN A 276 24.095 -66.593 -19.875 1.00 66.43 C ATOM 1850 OE1 GLN A 276 25.197 -66.659 -20.431 1.00 67.98 0 ATOM 1851 NE2GLNA276 23.947-66.718-18.557 1.0067.10 N ATOM 1852 C GLNA276 23.282-62.550-20.618 1.0061.36 C ATOM 1853 0 GLN A 276 24.4 14 -62.196 -20.269 1.00 61.33 0 ATOM 1854 N ASPA277 22.523-61.827-21.437 1.0061.08 N ATOM 1855 CA ASPA277 23.030-60.572 -21.987 1.00 61.12 C ATOM 1856 CB ASP A 277 22.044 -59.973 -22.993 1.00 61.25 C ATOM 1857 CG ASPA277 21.989-60.757-24.307 1.0062.18 C ATOM 1858 ODI ASP A 277 22.708 -6 1.774 -24.444 1.00 63.05 0 ATOM 1859 OD2 ASP A 277 21.223 -60.356 -25.213 1.00 63.07 0 ATOM 1860 C ASP A 277 23.366 -59.576 -20.873 1.00 60.97 C ATOM 1861 0 ASPA277 24.484-59.023-20.818 1.0061.14 0 ATOM 1862 N LEUA278 22.411 -59.359-19.969 1.0060.75 N ATOM 1863 CA LEU A 278 22.657 -58.435 -18.859 1.00 60.28 C ATOM 1864 CB LEU A 278 21.412 -58.273 -17.973 1.00 60.28 C ATOM 1865 CG LEU A 278 2 1.560 -57.508 -16. 65 1 1.00 59.63 C ATOM 1866 CD! LEU A 278 21.808 -56.034 -16.902 1.00 58.86 C ATOM 1867 CD2 LEIJ A 278 20.334.57.694 -15.776 1.00 59.64 C ATOM 1868 C LEUA278 23.860-58.894-18.034 1.0060.34 C ATOM 1869 0 LEU A 278 24.730 -58.091 -17.684 1.00 60.18 0 ATOM 1870 N PHE A 279 23.916 -60.190 -17.735 1.00 60.47 N ATOM 1871 CA PHE A 279 25.030 -60.706 -16.950 1.00 60.57 C ATOM 1872 CB PHE A 279 24.897 -62.197 -16.662 1.00 60.52 C ATOM 1873 CG PHE A 279 23.881 -62.511 -15.618 1.00 60.50 C ATOM 1874 CD1 PHEA279 23.466-61.533-14.729 1.0060.16 C ATOM 1875 CEI PIlE A 279 22.523 -61.808 -13.766 1.00 60.38 C ATOM 1876 CZ PHEA279 21.992-63.075-13.670 1.00 60.80 C ATOM 1877 CE2 PHE A 279 22.408 -64.068 -14.548 1.00 60.94 C ATOM 1878 CD2 PHE A 279 23.346 -63.783 -15.5 14 1.00 60.60 C ATOM 1879 C PHE A 279 26.350 -60.418 -17.630 1.00 60.72 C ATOM 1880 0 PHE A 279 27.261 -59.888 -17.007 1.00 60.64 0 ATOM 1881 N ARGA28O 26.462-60.758-18.908 1.0060.96 N ATOM 1882 CA ARG A 280 27.662 -60.380 -19.633 1.00 61.16 C ATOM 1883 CB ARGA 280 27.549-60.714-21.123 1.00 61.05 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 1.00 61.94 C ATOM 1886 NE ARG A 280 26.969 -63.243 -23.280 1.00 63.84 N ATOM 1887 CZ ARG A 280 25.7 13 -62.833 -23.459 1.00 64.28 C ATOM 1888 NHIARGA28O 25.410-61.542-23.363 1.0064.38 N ATOM 1889 NH2ARGA28O 24.759-63.718-23.733 1.00 64.17 N ATOM 1890 C ARG A 280 27.951 -58.895 -19.396 1.00 61.05 C ATOM 1891 0 ARG A 280 29.07 1 -58.525.19.027 1.00 60.89 0 ATOM 1892 N ASPA281 26.932-58.053-19.561 1.0061.18 N ATOM 1893 CA ASPA28I 27.123-56.605-19.389 1.0061.26 C ** ATOM 1894 CB ASP A281 25.814-55.846-19.642 1.00 61.67 C : **. ATOM 1895 CG ASPA28I 26.023-54.555-20.433 1.0062.92 C ATOM 1896 OD 1 ASP A 281 27.161 -54.026 -20.453 1.00 63.95 0 ATOM 1897 OD2ASPA281 25.041 -54.076-21.048 1.0064.41 0 ATOM 1898 C ASPA281 27.700-56.222-18.020 1.0060.84 C ATOM 1899 0 ASPA281 28.646-55.446-17.943 1.00 60.76 0 S's ATOM 1900 N ILE A 282 27.125.56.763 -16.948 1.00 60.54 N ATOM 1901 CA ILEA 282 27.616-56.507-15.589 1.00 60. 21 C * ATOM 1902 CB ILE A 282 26.726 -57.185 -14.534 1.00 60.12 C * ** ATOM 1903 CGI 1LEA282 25.316-56.592-14.547 1.0060.23 C ATOM 1904 CDIILEA282 24.299-57.415-13.778 1.0059.99 C ** * ATOM 1905 CG2 ILE A 282 27.357 -57.075 -13.150 1.00 59.55 C ATOM 1906 C 1LEA282 29.009-57.077-15.409 1. 00 60.29 C ATOM 1907 0 ILE A 282 29.945 -56.371 -15.057 1.00 60.29 0 ATOM 1908 N GLNA283 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 1.00 60.59 C ATOM 1911 CG GLN A 28 3 31.250 -61.500 -15.404 1.0061.30 C ATOM 1912 CD GLNA 283 32.334-61.830-16.404 1.00 62.16 C ATOM 1913 OE1GLNA283 33.515-61.936-16.054 1.0062.37 0 ATOM 1914 NE2 GLN A 283 3 1.938 -61.995 -17.664 1.00 62.82 N ATOM 1915 C GLNA 283 31.498-58.403-16.223 10060.41 C ATOM 1916 0 GLNA283 32.660-58.514-15.838 1.0060.58 0 ATOM 1917 N GLYA 284 31.145-57.670-17.275 1.00 60.32 N ATOM 1918 CA GLYA284 32.142-56.993-18,098 1.0059.90 C ATOM 1919 C GLYA 284 32.647-55.656-17.576 1.00 59.63 C ATOM 1920 0 GLY A 284 33.536 -55.052 -18.175 1.00 59.69 0 ATOM 1921 N LEUA285 32.096-55.194-16.458 1.0059.39 N ATOM 1922 CA LEU A 285 32.397 -53.848 -15.950 1.00 59.12 C ATOM 1923 CB LEU A 285 3 1.494 -53.498 -14.761 1.00 58.97 C ATOM 1924 CG LEU A 285 30.009 -53.305 -15.056 1.00 58.44 C ATOM 1925 CD1 LEU A 285 29.291 -52 805 -13.819 1.00 58.10 C ATOM 1926 CD2 LEUA 285 29.822 -52.345 -16.210 1.00 58.23 C ATOM 1927 C LEUA285 33.864-53.581-15.588 1.0059.12 C ATOM 1928 0 LEUA285 34.466-52.638-16.110 1.0058.98 0 ATOM 1929 N PRO A 286 34.444 -54.409 -14.698 1.00 59.17 N ATOM 1930 CA PRO A 286 35.792 -54.145 -14. 203 1.00 59.19 C ATOM 1931 CB PRO A 286 36.075 -55.339 -13.288 1.00 59.12 C ATOM 1932 CG PR0A286 34.744-55.870-12.925 1.0059.19 C ATOM 1933 CD PRO A 286 33.888 -55.648 -14.127 1.00 59.17 C ATOM 1934 C PR0A286 36.789-54.132-15.342 1.0059.26 C ATOM 1935 0 PRO A 286 37.746 -53.357 -15.323 1.00 59.19 0 ATOM 1936 N ARG A 287 36.553 -54.989 -16.331 1.00 59.46 N ATOM 1937 CA AR0A287 37.412-55.057-17.499 1.0059.64 C ATOM 1938 CB ARG A 287 36.797 -55.921 -18.592 1.00 59.76 C ATOM 1939 CG ARGA 287 37.768-56.326-19.690 1.00 60.10 C ATOM 1940 CD ARGA287 37.147-57.427-20.510 1.0061.21 C ATOM 1941 NE ARGA 287 36.470-58.384-19.637 1.00 62.03 N ATOM 1942 CZ ARG A 287 35.399 -59.089 -19.984 1.00 62.52 C ATOM 1943 NH1ARGA287 34.852-59.933-19.118 1.0062.89 N ATOM 1944 NH2 ARG A 287 34.871 -58.943 -21.192 1.00 62.75 N ATOM 1945 C ARO A 287 37.685 -53.659 -18.0 17 1.00 59.65 C ATOM 1946 0 ARGA287 38.790-53.378-18.474 1.0059.81 0 ATOM 1947 N HIS A 288 36.694 -52.772 -17.946 1.00 59.63 N ATOM 1948 CA HISA 288 37.017-51.366-18.161 1.00 59. 67 C ATOM 1949 CB HISA28S 37.330-51.042-19.616 1.0059.99 C ATOM 1950 CG H1SA288 38.788-50.816-19.848 1.0061.01 C ATOM 1951 ND! HIS A 288 39.584 -50.164 -18.929 1.00 61.71 N ATOM 1952 CEIHISA288 40.826-50.118-19.381 1.0062.63 C : ATOM 1953 NE2HISA288 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 H1SA288 36.213-50.263-17.500 1.0059.26 C ATOM 1956 0 HIS A 288 35.213 -49.774 -18.027 1.00 59.07 0 ATOM 1957 N ALAA289 36.721-49.867-16.340 1.0058.88 N ATOM 1958 CA ALAA289 36.302-48.660-15.668 1.0058.55 C ATOM 1959 CB ALAA2S9 36.632-48.746-14.182 1.0058.66 C * S *S.

* * ATOM 1960 C ALAA2S9 37.013-47.468-16.301 1.00 58.24 C ATOM 1961 0 ALA A 289 36.464 -46.372 -16.359 1.00 58.03 0 : *. ATOM 1962 N ALAA29O 38.233-47.688-16.781 1.0057.82 N ATOM 1963 CA ALAA29O 39.024-46.609-17.358 1.0057.55 C *. : 55 ATOM 1964 CB ALAA 290 40.307-47.154-17.938 1.00 57.56 C * ATOM 1965 C ALA A 290 38.252 -45.822 -18.416 1.00 57.41 C ATOM 1966 0 ALA A 290 38.284 -44.587 -18.437 1.00 57.25 0 ATOM 1967 N LEU A 291 37.557 -46.542 -19.289 1.00 57.29 N ATOM 1968 CA LEUA29I 36.796-45.916-20.362 1.0057.23 C ATOM 1969 CB LEUA29I 36.243-46.984-21.308 1.0057.15 C ATOM 1970 Co LEUA29I 36.111 -46.651 -22.796 1.0056.86 C ATOM 1971 CDI LEU A 291 35.366 -47.763 -23.507 1.00 56.79 C ATOM 1972 CD2 LEU A 291 35.407 -45.328 -23.016 1.00 57.08 C ATOM 1973 C LEUA29I 35.658-45.059-19.802 1.0057.31 C ATOM 1974 0 LEUA29I 35.502-43.894-20.180 1.0057.24 0 ATOM 1975 N ARGA292 34.866-45.629-18.897 1.0057.43 N ATOM 1976 CA ARGA292 33.724-44.901-18.343 1.0057.57 C ATOM 1977 CS ARG A 292 32.790 -45.826 -17.545 1.00 57.62 C ATOM 1978 CG ARO A 292 33.064 -45.912 -16.049 1.00 57.76 C ATOM 1979 CD ARG A 292 32.064 -45.093 -15.239 1.00 57.94 C ATOM 1980 NE ARO A 292 32.428 -45.049 -13. 823 1 00 58.09 N ATOM 1981 CZ ARO A 292 32.935 -43.984 -13.209 1.00 57.92 C ATOM 1982 N}IIARGA292 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 ARO A 292 34.204 -43.718 -17.508 1.00 57.46 C ATOM 1985 0 AR0A292 33.588-42.648-17.520 1.0057.56 0 ATOM 1986 N LYSA 293 35.312-43.912-16.802 1.00 57.36 N ATOM 1987 CA LYSA 293 35.942-42.831 -16.067 1.00 57.19 C ATOM 1988 CB LYS A 293 37.186 -43.323 -15.330 1.00 57.19 C ATOM 1989 CG LYS A 293 36.886 -44.029 -14.020 1.00 57.17 C ATOM 1990 CD LYS A 293 38.050 -44.901 -13.578 1.00 57.02 C ATOM 1991 CE LYS A 293 37.757-45.577-12.248 1.00 57.19 C ATOM 1992 NZ LYSA293 38.749-46645-11.944 1.0057.34 N ATOM 1993 C LYS A 293 36.304 -41.729 -17.043 1.00 57.09 C ATOM 1994 0 LYS A 293 35.865 -40.588 -16.892 1.00 57.11 0 ATOM 1995 N LEU A 294 37.091 -42.079 -18.055 1.00 56.95 N ATOM 1996 CA LEU A 294 37.458 -41.121 -19.083 1.00 56.84 C ATOM 1997 CE LEU A 294 38.123 -41.836 -20.259 1.00 56.79 C ATOM 1998 Co LEU A 294 38.441 -40.974 -2 1.483 1.00 56.79 C ATOM 1999 CDI LEU A 294 39.335 -39.809 -21.097 1.00 57.30 C ATOM 2000 CD2 LEU A 294 39 095 -41.802 -22.568 1.00 56.83 C ATOM 2001 C LEU A 294 36.226 -40.348 -19.550 1.00 56.79 C ATOM 2002 0 LEU A 294 36.167 -39.112 -19.454 1.00 56.76 0 ATOM 2003 N ASN A 295 35.236 -4 1.084 -20.039 1.00 56.85 N ATOM 2004 CA ASN A 295 34.003 -40.469 -20.527 1.00 56.94 C ATOM 2005 CE ASN A 295 32.999 -41.549 -20.922 1.00 57.00 C ATOM 2006 CO ASN A 295 32.915 -41.708 -22. 436 1.00 57.02 C ATOM 2007 ODI ASN A 295 33.082 -42.8 15 -22.972 1.00 56.80 0 ATOM 2008 ND2ASNA295 32.656-40.594-23 140 1.00 57.22 N ATOM 2009 C ASN A 295 33.355 -39.494 -19.545 1.00 56.98 C ATOM 2010 0 ASNA295 33.029-38.355-19.897 1.00 56.90 0 : ,** ATOM 2011 N ASPA 296 33.163-39.939-18.311 1.00 57.20 N ATOM 2012 CA ASP A 296 32.544 -39.075 -17.3 19 1.00 57.27 C ATOM 2013 CB ASP A 296 32.240 -39.854 -16.040 1.00 57.49 C ATOM 2014 CO ASP A 296 3 1.232 -40.978 -16.270 1.00 58.34 C ATOM 2015 OD1ASPA296 31.236-41.950-15.485 1.0059.28 0 ATOM 2016 OD2ASPA 296 30.441 -40.898-17.241 1.00 59.32 0 ATOM 2017 C ASP A 296 33.409 -37.844 -17.057 1.00 57.08 C ** S...

* ATOM 2018 0 ASPA296 32.886-36.745-16.834 1.0056.96 0 ATOM 2019 N LEUA 297 34.728 -38.027 -17.115 1.00 56.92 N ATOM 2020 CA LEUA297 35.652-36.901 -17.027 1.00 56.71 C ATOM 2021 CB LEU A 297 37.110-37.360-17.104 1.00 56.70 C *. 55 ATOM 2022 CO LEU A 297 38.145 -36.289 -16.736 1.00 57.00 C * " ATOM 2023 CD1 LEU A 297 38.338 -36.212 -15.230 1.00 57.18 C ATOM 2024 CD2 LEU A 297 39.486 -36.538 -17.417 1.00 57.32 C ATOM 2025 C LEUA297 35.357-35.904-18.140 1.0056.57 C ATOM 2026 0 LEU A 297 35.223 -34.709 -17.882 1.00 56.57 0 ATOM 2027 N VAL A 298 35. 246 -36.394 -19.374 1.00 56.40 N ATOM 2028 CA VALA298 34.872-35.528-20.498 1.0056.20 C ATOM 2029 CB VALA 298 34.701 -36.323-21.801 1.00 56.10 C ATOM 2030 CG1 VALA 298 34.213 -35.414 -22.920 1.00 55.78 C ATOM 2031 CG2VALA 298 35.994-37.011-22.183 1.0055.98 C ATOM 2032 C VAL A 298 33.562 -34.78 1 -20.239 1.00 56.34 C ATOM 2033 0 VAL A 298 33.490 -33.550 -20.372 1.00 56.51 0 ATOM 2034 N LYS A 299 32.523 -35.532 -19.880 1.00 56.48 N ATOM 2035 CA LYS A 299 31.207 -34.944 -19.649 1.00 56.48 C ATOM 2036 CB LYS A 299 30.223 -36.009 -19.163 1.00 56.50 C ATOM 2037 CG LYSA299 29.928-37.118-20.171 1.0056.54 C ATOM 2038 CD LYS A 299 29.057 -38.204 -19.543 1.00 5673 C ATOM 2039 CE LYS A 299 28.654 -39.272 -20.554 1.00 57.33 C ATOM 2040 NZ LYS A 299 27.703 -38.749 -21.571 1.00 57.04 N ATOM 2041 C LYS A 299 31.312 -33.824 -18.623 1.00 56.44 C ATOM 2042 0 LYS A 299 30.872 -32.676 -18.860 1.00 56.62 0 ATOM 2043 N A.RGA300 31.910-34.158-17.482 1.0056.46 N ATOM 2044 CA ARG A 300 32.147 -33.159 -16.456 1.00 56.31 C ATOM 2045 CB A.RG A 300 32.985 -33.720 -15.307 1.00 56.27 C ATOM 2046 CG ARG A 300 33.478 -32.651 -14.337 1.00 56.17 C ATOM 2047 CD ARGA300 34.274-33.246-13.191 1.0056.14 C ATOM 2048 NE ARGA 300 33.429 -33.563 -12.047 1.00 56.16 N H ATOM 2049 CZ ARGA300 33.530-32.970-10.862 1.0056.53 C ATOM 2050 NH1 A.RG A 300 32.722 -33.3 17 -9.870 1.00 56.30 N ATOM 2051 NH2 ARG A 300 34.450 -32.037 -10.665 1.00 56.98 N ATOM 2052 C ARGA300 32.834-31.952-17.081 1.0056.37 C ATOM 2053 0 ARGA300 32.329-30.834-16.996 1.0056.39 0 ATOM 2054 N ALA A 301 33.973 -32.186 -17.729 1.00 56.45 N ATOM 2055 CA ALAA3OI 34.714-31.106-18.374 1.00 56.41 C ATOM 2056 CB ALA A 301 35.758 -31.660 -19.331 1.00 56.29 C ATOM 2057 C ALAA 301 33.761-30.172-19.104 1.00 56.46 C ATOM 2058 0 ALAA 301 33.722-28.971 -18.821 1.00 56.47 0 ATOM 2059 N ARG A 302 32.980 -30.728 -20.025 1.00 56.55 N ATOM 2060 CA ARG A 302 32.035 -29.923 -20. 808 1.00 56.77 C ATOM 2061 CB ARG A 302 31.260 -30.818 -21.777 1.00 56.86 C ATOM 2062 CG ARGA3O2 32.166-31.414-22.840 1.0057.73 C ATOM 2063 CD ARGA3O2 31.637-32.710-23.404 1.0059.51 C ATOM 2064 NE ARG A 302 30.704 -32.490 -24.503 1.00 61.12 N ATOM 2065 CZ ARG A 302 29.383 -32.597 -24.393 1.00 62.12 C ATOM 2066 NH1 ARG A 302 28.83 1 -32.927 -23.228 1.00 62.16 N ATOM 2067 NH2ARGA 302 28.612-32.381 -25.452 1.00 62.71 N ATOM 2068 C ARG A 302 3 1.093 -29.087 -19.932 1.00 56.68 C :. ATOM 2069 0 ARG A 302 30.924 -27.862 -20.149 1.00 56.68 0 ATOM 2070 N LEUA 303 30.503 -29.735 -18.927 1.00 56.67 N ATOM 2071 CA LEU A 303 29.663 -28.990 -17.981 1.00 56.63 C ATOM 2072 CB LEU A 303 29.083 -29.913 -16.910 1.00 56.59 C ATOM 2073 CG LEIJ A 303 28.182 -29.195 -15.902 1.00 56.67 C ATOM 2074 CD1LEUA3O3 26.913-28.699-16.582 1.00 56.50 C ATOM 2075 CD2 LEU A 303 27.844 -30.106 -14.733 1.00 57.07 C ATOM 2076 C LEUA3O3 30.433-27.832-17.323 1.0056.59 C ATOM 2077 0 LEUA 303 29.971 -26.677-17.307 1.00 56.69 0 : *. ATOM 2078 N VAL A 304 31.606 -28.149 -16.781 1.00 56.40 N ATOM 2079 CA VALA3O4 32.482-27.143-16.199 1.0056.15 C . : 55 ATOM 2080 CB VAL A 304 33.862 -27.728 -15.855 1.00 56.03 C * ATOM 2081 CGI VAL A 304 34.801 -26.633 -15.389 1.00 55.85 C ATOM 2082 CG2 VAL A 304 33.728 -28.800 -14.797 1.00 55.67 C ATOM 2083 C VALA 304 32.655 -25.971 -17.159 1.00 56.22 C ATOM 2084 0 VALA 304 32.319 -24.832 -16.825 1.00 56.31 0 ATOM 2085 N ARG A 305 33.166 -26.249 -18.356 1.00 56.24 N ATOM 2086 CA ARG A 305 33.364 -25.195 -19.35 1 1.00 56.28 C ATOM 2087 CB ARG A 305 33.760 -25.783 -20.714 1.00 56.25 C ATOM 2088 CG ARGA3O5 33.325-24.961 -21.919 1.0056.53 C ATOM 2089 CD ARG A 305 34485 -24.659 -22.872 1.00 57.09 C ATOM 2090 NE ARG A 305 34,903 -25 757 -23.746 1.00 57.25 N ATOM 2091 CZ ARG A 305 34.124 -26.746 -24.174 1.00 57.93 C ATOM 2092 NHI ARG A 305 34.632 -27.680 -24.968 1.00 57.81 N ATOM 2093 NH2 ARG A 305 32.845 -26.809 -23.820 1.00 58.76 N ATOM 2094 C ARG A 305 32.126 -24.303 -19.448 1.00 56.28 C ATOM 2095 0 ARG A 305 32.223 -23.058 -19.357 1.00 56.39 0 ATOM 2096 N VALA 306 30.956 -24.93 1 -19.589 1.00 56.35 N ATOM 2097 CA VALA3O6 29.727-24.136-19.630 1.0056.27 C ATOM 2098 CB VALA3O6 28.487-25.017-19.682 1.0056.15 C ATOM 2099 CG1 VALA 306 27.267-24.162-19.959 1.00 56.18 C ATOM 2100 CG2 VALA 306 28.652 -26.085 -20.738 1.00 56.17 C ATOM 2101 C VALA 306 29.608-23.217-18.409 1.00 56.36 C ATOM 2102 0 VALA 306 29.536 -21.983 -18.532 1.00 56.51 0 ATOM 2103 N HIS A 307 29.588 -23.822 -17.227 1.00 56.41 N ATOM 2104 CA HIS A 307 29.471 -23.049 -15.993 1.00 56.44 C ATOM 2105 CB HIS A 307 29.743 -23.942 -14.783 1.00 56.45 C ATOM 2106 CG HIS A 307 29.652 -23.225 -13. 474 1.00 55.91 C ATOM 2107 ND1 HIS A 307 28.449 -22.849 -12.914 1.00 55.76 N ATOM 2108 CE! HISA 307 28.672-22.245-11.760 1.00 55.92 C ATOM 2109 NE2 HIS A 307 29.976 -22.221 -11.548 1.00 56.18 N ATOM 2110 CD2HISA3O7 30.612-22.827-12.606 1.00 55.83 C ATOM 2111 C HISA3O7 30.427-21.856-15. 981 1.0056.54 C ATOM 2112 0 HIS A 307 30.023 -20.712 -15.705 1.00 56.69 0 ATOM 2113 N ALAA3O8 31.696-22.138-16.281 1.00 56.50 N ATOM 2114 CA ALA A 308 32.722 -21.106 -16.342 1.00 56.41 C ATOM 2115 CB ALA A 308 34.000 -21.659 -16.921 1.00 56.25 C ATOM 2116 C ALAA3O8 32.211-19.972-17.198 1.0056.41 C ATOM 2117 0 ALAA 308 32.153-18.819-16.751 1.0056.62 0 ATOM 2118 N TYRA 309 31.814-20.299-18.424 1.00 56.40 N ATOM 2119 CA TYRA3O9 31.311-19.251-19.299 1.0056.51 C ATOM 2120 CR TYR A 309 30.868 -19.809 -20.650 1.00 56.57 C ATOM 2121 CG TYRA3O9 32.021-20.031-21.598 1.0056.51 C ATOM 2122 CD1 TYR A 309 32.161 -21.225 -22.287 1.00 56.48 C ATOM 2123 CE1TYRA3O9 33.219-21.429-23.150 1.0056.59 C ATOM 2124 CZ TYRA3O9 34.159-20.436-23.323 1.00 56.61 C ATOM 2125 OH TYRA3O9 35.215-20.639-24.178 1.0056.68 0 ATOM 2126 CE2TYRA3O9 34.048-19.243-22. 644 1.0056.61 C : ATOM 2127 CD2TYRA 309 32.985 -19.048-21.786 1.00 56.59 C ATOM 2128 C TYRA 309 30.193-18.455-18.632 1.00 56.61 C ATOM 2129 0 TYRA 309 30.250-17.219-18.581 1.00 56.91 0 ATOM 2130 N ILEA 310 29.193-19.158-18.102 1.00 56.59 N ATOM 2131 CA ILEA 310 28.068-18.486-17.439 1.00 56.63 C ATOM 2132 CB ILEA 310 27.113-19.492-16.774 1.00 56.52 C : 50 ATOM 2133 CG1 ILE A 310 26.552 -20.463 -17.809 1.00 56.47 C * ATOM 2134 CDIILEA31O 25.786-21.610-17.202 1.0056.57 C ATOM 2135 CG2ILEA31O 25.980-18.768-16.079 1.0056.40 C *, ATOM 2136 C ILEA3IO 28.523-17.463-16.387 1.0056.78 C ATOM 2137 0 ILEA3IO 28.192-16.258-16.473 1.0057.05 0 *. : 55 ATOM 2138 N ILE A 311 29.283 -17.938 -15.399 1.00 56.75 N * ATOM 2139 CA ILEA 311 29.750-17.046-14.338 1.00 56.82 C ATOM 2140 CB ILEA3!1 30.607-17.771-13.281 1.0056.78 C ATOM 2141 CGIILEA3I1 29.743-18.232-12.109 1.0056.78 C ATOM 2142 CDIILEA3II 28.714-19.266-12.461 1.0057.40 C ATOM 2143 CG2ILEA31I 31.655-16.834-12. 716 1.00 57.09 C ATOM 2144 C ILE A 311 30.532 -15.882 -14.932 1.00 56.87 C ATOM 2145 0 ILE A 311 30.257 -14.714.14.630 1.00 56.99 0 ATOM 2146 N SERA 312 3 1.495 -16.205 -15.792 1.00 56.92 N ATOM 2147 CA SERA312 32.304-15.181-16.436 1.0057.06 C ATOM 2148 CB SERA3I2 33.181-15.797-17. 521 1.0057.04 C ATOM 2149 OG SER A 312 34.124 -16.687 -16.952 1.00 57.03 0 ATOM 2150 C SERA312 31.437-14.078-17.028 1.0057.22 C ATOM 2151 0 SERA 312 31.633 -12.896-16.726 1.00 57.33 0 ATOM 2152 N TYR A 313 30.474 -14.464 -17.864 1.00 57.40 N ATOM 2153 CA TYRA313 29.591-13.479-18.501 1.0057.83 C ATOM 2154 CB TYRA 313 28.638-14.142-19.503 1.00 58.15 C ATOM 2155 CG TYRA313 29.257-14.429-20.864 1.0058.84 C ATOM 2156 CD1 TYRA 313 28.576-14.120-22.041 1.00 59.36 C ATOM 2157 CE1TYRA313 29.137-14.383-23.290 1.0059.39 C ATOM 2158 CZ TYRA 313 30.395-14.957-23.368 1.00 59.16 C ATOM 2159 OH TYRA3I3 30.957-15.219-24.597 1.0059.00 0 ATOM 2160 CE2TYRA313 31.093-15.269-22. 216 1.0059.29 C ATOM 2161 CD2 TYRA 313 30.525 -15.004 -20.974 1.00 59.34 C ATOM 2162 C TYRA 313 28.815-12.657-17.471 1.00 57.75 C ATOM 2163 0 TYRA 313 28.734-11.423-17.578 1.00 57.91 0 ATOM 2164 N LEUA3I4 28.257-13.328-16.465 1.0057.51 N ATOM 2165 CA LEUA314 27.569-12.590-15. 403 1.00 57.40 C ATOM 2166 CB LEUA3I4 27.057-13.550-14.330 1.0057.20 C ATOM 2167 CG LEUA314 25.894-14.430.14.790 1.0056.64 C ATOM 2168 CD1LEUA314 25.739-15.648-13.905 1.0055.97 C ATOM 2169 CD2LEUA314 24.612-13.622-14. 836 1.00 56.28 C ATOM 2170 C LEUA314 28.481-11.514-14.795 1.0057.49 C ATOM 2171 0 LEUA3I4 28.138-10.316-14.753 1.0057.84 0 ATOM 2172 N LYSA3L5 29.656-11.949-14.344 1.0057.46 N ATOM 2173 CA LYSA315 30.624-11.045-13. 725 1.00 57.51 C ATOM 2174 CB LYSA315 31.880-11.804-13.290 1.0057.50 C ATOM 2175 CG LYS A 315 33.079 -10.920 -12.986 1.00 57.23 C ATOM 2176 CD LYS A 315 32.828 -10.022 -11.793 1.0057.26 C ATOM 2177 CE LYSA3I5 34.012 -9.103-11.556 1.0057.59 C ATOM 2178 NZ LYSA3I5 33.958 -8.446-10.218 1.00 57.78 N ATOM 2179 C LYSA 315 31.003 -9.898-14.648 1.00 57.60 C ATOM 2180 0 LYSA3I5 31.104 -8.753-14.207 1.00 57.65 0 ATOM 2181 N LYSA 316 31.217-10.202-15.925 1.00 57.67 N ATOM 2182 CA LYSA316 31.571 -9.156-16.880 1.0057.96 C ATOM 2183 CB LYSA316 32.094 -9.747-18.198 1.0058.04 C ATOM 2184 CO LYSA316 31.033-10.014-19.266 1.00 58.13 C :. ATOM 2185 CD LYS A 316 31.633 -10.748 -20.463 1.00 58.14 C ATOM 2186 CE LYSA3I6 30.559-11.212-21.441 1.00 58.37 C ATOM 2187 NZ LYS A 316 29.905 -10.080 -22.159 1.00 58.37 N ATOM 2188 C LYS A 316 30.386 -8.223 -17.128 1.00 57.99 C ATOM 2189 0 LYSA316 30.559 -7.095-17.590 1.0057.89 0 ATOM 2190 N GLUA 317 29.183 -8.693-16.812 1.00 58.12 N ATOM 2191 CA GLU A 317 28.004 -7.848 -16.967 1.00 58.35 C ATOM 2192 CB GLUA317 26.752 -8.689-17.228 1.0058.34 C ATOM 2193 CO GLU A 317 25 722 -7.983 -18.087 1.00 58.29 C : " ATOM 2194 CD GLU A 317 26.286 -7.568 -19.434 1.00 58.49 C ATOM 2195 OEIGLUA3I7 25.892 -6.495-19.943 1.0058.78 0 . : 55 ATOM 2196 OE2GLUA3I7 27.130 -8.311-19.982 1.0058.20 0 * ATOM 2197 C 0LUA317 27.791 -6.929-15.765 1.0058.52 C ATOM 2198 0 GLUA3I7 27.312 -5.806-15.919 1.0058.43 0 ATOM 2199 N META318 28.147 -7.408-14.574 1.0058.76 N ATOM 2200 CA META 318 27.957 -6.621 -13.339 1.00 59.38 C ATOM 2201 CB META318 28. 350 -7.457-12.122 1.0059.35 C ATOM 2202 CG META 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 META 318 26.589 -6.840 -9.568 1.00 59.36 C ATOM 2205 C META3I8 28.694 -5.273-13.292 1.0059.81 C ATOM 2206 0 MET A 318 29.870 -5.198 -13.641 1.00 59.90 0 ATOM 2207 N PROA319 28.001 -4.208-12.835 1.0060.27 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 PROA 319 26.311 -2.817-11.979 1.00 60.41 C ATOM 2211 CD PROA 319 26.597 -4.248-12386 1.00 60.27 C ATOM 2212 C PRO A 319 29.398 -2.698 -11.446 1.00 61.12 C ATOM 2213 0 PROA 319 29.036 -3.243-10.399 1.0061.23 0 ATOM 2214 N THRA32O 30.488 -1.936-11.537 1.0061.63 N ATOM 2215 CA THRA 320 31.497 -1.880-10.470 1.00 62.20 C ATOM 2216 CB 1'HRA 320 32.620 -0.850-10.777 1.00 62.25 C ATOM 2217 OG1 THRA 320 32.176 0.476-10.455 1.00 62.39 0 ATOM 2218 CG2 THR A 320 33.033 -0.914 -12.247 1.00 62.52 C ATOM 2219 C THRA 320 30.946 -1.611 -9.065 1.00 62.49 C ATOM 2220 0 THRA32O 30.968 -2.492 -8.200 1.0062.58 0 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 0063.09 C ATOM 2224 CGI 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 1.00 63.21 C ATOM 2226 C VAL A 321 28.625 0.097 -7.157 1.00 63.21 C ATOM 2227 0 VALA321 28.177 -0.527 -6.190 1.0063.23 0 ATOM 2228 N PHE A 322 27.846 0.829 -7.953 1.00 63.40 N ATOM 2229 CA PHEA 322 26.411 0.966 -7.661 1.0063.56 C ATOM 2230 CB PHEA322 26.053 2.392 -7.207 1.0063.65 C ATOM 2231 CG PHE A 322 26.791 3.475 -7. 940 1.00 63.76 C ATOM 2232 CDI PHE A 322 27.629 4.34 1 -7.253 1.00 63.84 C ATOM 2233 CEI 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 PHEA322 25.459 0.500 -8.764 1.0063.57 C ATOM 2238 0 PHEA322 25.789 0.536 -9.951 1.0063.52 0 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 0 GLY A 323 22.124 -2.574 -9.402 1.00 63.82 0 : ,, ATOM 2243 N LYSA324 24.168 -2.547 -8.448 1.0063.98 N ATOM 2244 CA LYS A 324 24.303 -3.993 -8.249 1.0064.15 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 1.0064.51 C *.* ATOM 2247 CD LYSA324 26.357 -3.392 -4.952 1.0064.43 C ATOM 2248 CE LYSA324 27.696 -3.883 -5.508 1.00 64.92 C : 50 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 0 LYSA324 22.825 -5.828 -8.735 1.0064.04 0 ATOM 2252 N GLUA 325 22.132 -4.361 -7.177 1.00 64.10 N ATOM 2253 CA GLU A 325 20.961 -5.152 -6.781 1.0064.12 C *, 55 ATOM 2254 CB GLUA325 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 OEI GLUA325 20090 -5.825 -4.783 0.00 50.00 0 ATOM 2258 OE2GLUA325 19.664 -5.171 -2.727 0.0050.00 0 ATOM 2259 C GLUA 325 20.030 -5.549 -7.941 1.0064.19 C ATOM 2260 0 GLUA325 19.810 -6.781 -8.214 1.0064.25 0 ATOM 2261 N ASN A 326 19.472 -4.524 -8.6 13 1.00 64.26 N ATOM 2262 CA ASN A 326 18.505 -4.812 -9.679 1.00 64.33 C ATOM 2263 CB ASN A 326 17.540 -3.633 -9.94 1 1.0064 30 C ATOM 2264 CO ASN A 326 18.252 -2.335 -10.279 1.00 64.30 C ATOM 2265 OD1 ASNA 326 18.063 -1.317 -9.606 1.00 64.17 0 ATOM 2266 ND2 ASN A 326 19.058 -2.357 -11.338 1.0064.50 N ATOM 2267 C ASNA326 19. 181 -5.330-10.958 1.0064.35 C ATOM 2268 0 ASNA 326 18.546 -5.991 -11.784 1.00 64.40 0 ATOM 2269 N LYSA327 20.472 -5.038-11.104 1.0064.30 N ATOM 2270 CA LYSA327 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 CO LYS A 327 23.130 -4643 -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 1.00 64.30 N ATOM 2276 C LYSA327 21.355 -7.072-12.042 1.0064.18 C ATOM 2277 0 LYS A 327 2 1.258 -7.825 -13.004 1.00 64.23 0 ATOM 2278 N LYS A 328 21.551 -7.503 -10.801 1.00 64.17 N ATOM 2279 CA LYS A 328 21.573 -8.924 -10.490 1.00 64.23 C ATOM 2280 CB LYS A 328 22.005 -9 156 -9.040 1.0064.21 C ATOM 2281 CO LYSA328 21.992-10.616 -8.620 1.0064.08 C ATOM 2282 CD LYS A 328 22.06 1 -10.764 -7.110 1.00 64.01 C ATOM 2283 CE LYS A 328 21.635 -12.160 -6.682 1.00 63.97 C ATOM 2284 NZ LYSA328 21.527-12.286 -5.204 1.0063.96 N ATOM 2285 C LYSA328 20.197 -9.536-10.744 1.00 64.29 C ATOM 2286 0 LYS A 328 20.069-10.507-11.517 1.00 64.33 0 ATOM 2287 N LYSA329 19.165 -8.960-10. 111 1.0064.32 N ATOM 2288 CA LYS A 329 17.813 -9.5 11 -10.273 1.0064.39 C ATOM 2289 CB LYS A 329 16.788 -8.659 -9.523 1.00 64.37 C ATOM 2290 CG LYS A 329 16.688 -10.172 -7.803 0.00 50.00 C ATOM 2291 CD LYS A 329 15.993 -9.545 -6.623 0.00 50.00 C ATOM 2292 CE LYS A 329 15.083 -10.565 -5.937 0.00 50.00 C ATOM 2293 NZ LYS A 329 14.752 -10.177 -4.545 0.00 50.00 N ATOM 2294 C LYS A 329 17.434 -9.631 -11.757 1.00 64.44 C ATOM 2295 0 LYS A 329 16.935 -10.671 -12.2 18 1.0064.52 0 ATOM 2296 N GLNA 330 17.689 -8.557-12.498 1.00 64.44 N ATOM 2297 CA GLNA33O 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 1.00 64.39 C ATOM 2300 CD GLN A 330 18.22 1 -5.608 -16.440 1.0064.40 C : ATOM 2301 OE1GLNA33O 17.777 -4.614-15.862 1.0064.30 0 ATOM 2302 NE2 GLN A 330 19.046 -5.524 -17.479 1.00 64.34 N ATOM 2303 C GLNA33O 18.305 -9.565-14.658 1.0064.45 C ATOM 2304 0 GLNA33O 17.813-10.287-15.529 1.006460 0 ATOM 2305 N LEUA331 19.579 -9.647-14.281 1.0064.39 N ATOM 2306 CA LEUA331 20.495-10.615-14.874 1. 0064 37 C ATOM 2307 CB LEUA33I 21.902-10.488-14.284 1.0064.32 C * * ATOM 2308 CG LEUA331 22.855 -9.519-14.986 1.0064.30 C ATOM 2309 CDI LEU A 331 24. 178 -9.421 -14.242 1.0064.35 C : *** ATOM 2310 CD2LEUA33I 23.081 -9.930-16. 430 1.0064.38 C ATOM 2311 C LEUA33I 19.983-12.039-14.718 1.0064.41 C **. : 55 ATOM 2312 0 LEUA331 20.171-12.868-15.610 1.0064.39 0 * ATOM 2313 N 1LEA332 19.335-12.331-13.593 1.0064.44 N ATOM 2314 CA 1LEA332 18.744-13.660-13. 438 1.0064.56 C ATOM 2315 CB 1LEA332 18.734-14.168-11.978 1.0064.53 C ATOM 2316 CGIILEA332 18.252-13.081-11.022 1.0064.67 C ATOM 2317 CDIILEA332 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 1LEA332 17.361-13.779-14.076 10064.64 C ATOM 2320 0 ILE A 332 16.916 -14.885 -14.381 1.00 64.71 0 ATOM 2321 N LEUA 333 16.681 -12.653-14.286 1.0064.69 N ATOM 2322 CA LEUA333 15.474-12.679-15.120 1.0064.86 C ATOM 2323 CB LEUA 333 14.733-11.340-15.070 1.0064.84 C ATOM 2324 CG LEUA333 13.377-11.329-14. 357 1.0064.83 C ATOM 2325 CDILEUA333 13.505-11.795-12.912 1.0064.93 C ATOM 2326 CD2 LEU A 333 12.750 -9.944 -14.43 1 1.0064.92 C ATOM 2327 C LEUA333 15.821-13.018-16.568 1.0064.95 C ATOM 2328 0 LEUA333 15.066-13.699-17.265 1.0064.92 0 ATOM 2329 N LYSA334 16.982-12.542-17.002 1.0065.06 N ATOM 2330 CA LYSA334 17.410-12.645-18.390 1.0065.32 C ATOM 2331 CB LYSA334 18.037-11.303-18.801 1.0065.31 C ATOM 2332 CG LYSA334 18.859-11.279-20. 084 1.0065.31 C ATOM 2333 CD LYSA 334 19.751 -10.026-20.101 1.00 65.18 C ATOM 2334 CE LYS A 334 20.825 -10.098 -21.178 1.00 64.74 C ATOM 2335 NZ LYSA334 21.839 -9.010-21.016 1.0064.46 N ATOM 2336 C LYS A 334 18.385 -13.813 -18.589 1.00 65.54 C ATOM 2337 0 LYSA334 19.241 -13.778-19.474 1.00 65.57 0 ATOM 2338 N LEU A 335 18.243 -14.855 -17.772 1.00 65.83 N ATOM 2339 CA LEUA335 19.176-15.984-17.815 1.0066.16 C ATOM 2340 CR LEUA335 19.092-16.826-16.537 1.0066.09 C ATOM 2341 CO LEUA 335 20.406-17.326-15.917 1.00 66.13 C ATOM 2342 CD! LEU A 335 20.204 -18.673 -15.232 1.00 66.05 C ATOM 2343 CD2 LEU A 335 21.536 -17.420 -16.93 1 1.00 65.95 C ATOM 2344 C LEU A 335 18.990 -16.877 -19.044 1.00 66.47 C ATOM 2345 0 LEUA 335 19.964-17.217-19.710 1.00 66.51 0 ATOM 2346 N PRO A 336 17.739 -17.263 -19.354 1.00 66.81 N ATOM 2347 CA PROA 336 17.544 -18.144 -20.503 1.00 67.08 C ATOM 2348 CB PRO A 336 16.028 -18.367 -20.526 1.00 67.05 C ATOM 2349 CO PR0A336 15.458-17.221 -19.762 1.00 66.99 C ATOM 2350 CD PRO A 336 16.465 -16.916 -18.702 1.00 66.85 C ATOM 235! C PR0A336 18.010-17.486-21.797 1.0067.39 C ATOM 2352 0 PR0A336 18.262-18.175-22.786 1.0067.44 0 ATOM 2353 N VALA337 18.123-16.162-21.781 1.0067.78 N ATOM 2354 CA VAL A 337 18.655 -15.42! -22.917 1.00 68.20 C ATOM 2355 CB VALA 337 18.258-13.931-22.857 1.00 68.20 C ATOM 2356 CGIVALA337 18.443-13.275-24.221 1.0068.26 C ATOM 2357 CG2 VAL A 337 16.817 -13.779 -22.384 1.00 68.27 C ATOM 2358 C VALA337 20.177-15.540-22.917 1.0068.46 C ATOM 2359 0 VALA 337 20.796-15.754-23.964 1.00 68.80 0 ATOM 2360 N ILEA 338 20.769-15.408-21.733 1.00 68.70 N a.. ATOM 2361 CA 1LEA338 22.210-15.578-21.561 1.0068.88 C ATOM 2362 CB ILE A 338 22.627 -15.468 -20.077 1.00 68.80 C ATOM 2363 CG! ILEA 338 22.408-14.045-19.557 1.00 68.70 C ATOM 2364 CD1ILEA338 23.413-13.035-20.078 1.0068.75 C ATOM 2365 CG2 ILE A 338 24.082 -15.865 -19.900 1.00 68.67 C * ATOM 2366 C ILEA 338 22.66! -16.929-22.114 1.00 69.11 C ATOM 2367 0 ILE A 338 23.575 -16.995 -22.939 1.00 69.27 0 ATOM 2368 N PHEA339 22.007-17.999-21.664 1.0069.30 N ATOM 2369 CA P1-lEA 339 22.327 -19.346-22.133 1.00 69.45 C **. : 55 ATOM 2370 CB PHE A 339 21.395 -20.390 -21.503 1.00 69.45 C ATOM 2371 CO PHE A 339 21.613 -20.598 -20.024 1.00 69.55 C ATOM 2372 CD! PHE A 339 22.744 -20.104 -19.391 1.00 69.69 C ATOM 2373 CEI PHE A 339 22.944 -20.304 -18.035 1.00 69.63 C ATOM 2374 CZ PHEA 339 22.019-21.017-17.299 1.00 69. 58 C ATOM 2375 CE2 PHE A 339 20.893.21.524 -17.919 1.00 69.60 C ATOM 2376 CD2 PHE A 339 20.695 -21.3 18 -19.273 1.00 69.56 C ATOM 2377 C PHE A 339 22.248 -19.427 -23.656 1.00 69.52 C ATOM 2378 0 PHEA339 23.170-19.923-24.314 1.0069.66 0 ATOM 2379 N ALAA34O 21.146-18.926-24.208 1.0069.56 N ATOM 2380 CA ALA A 340 20.949 -18.908 -25.653 1.00 69.59 C ATOM 2381 CB ALA A 340 19.633 -18.214 -26.000 1.00 69.61 C ATOM 2382 C ALAA 340 22.119-18.218-26.351 1.00 69.61 C ATOM 2383 0 ALA A 340 22.683 -18.750 -27.3 19 1.00 69.74 0 ATOM 2384 N LYS A 341 22.486 -17.035 -25. 848 1.00 69.49 N ATOM 2385 CA LYS A 341 23.574 -16.263 -26.446 1.00 69.65 C ATOM 2386 CB LYS A 341 23.660 -14.861 -25.828 1.00 69.67 C ATOM 2387 CG LYS A 341 22.479 -13.952 -26.189 1.00 69.92 C ATOM 2388 CD LYS A 341 22.774 -12.477 -25.902 1.00 69.78 C ATOM 2389 CE LYSA34I 21.518-11.612-26.045 1.0069.77 C ATOM 2390 NZ LYS A 341 20.889 -11.703 -27.400 1.00 69.59 N ATOM 2391 C LYS A 341 24.914 -16.993 -26.352 1.00 69.57 C ATOM 2392 0 LYSA34I 25.626-17.142-27.354 1.0069.70 0 ATOM 2393 N 1LEA342 25.248-17.463-25.152 1.0069.50 N ATOM 2394 CA ILEA 342 26.494 -18.200-24.950 1.00 69.48 C ATOM 2395 CB 1LEA342 26.709-18.597-23.478 1.0069.39 C ATOM 2396 CGI ILE A 342 26.707 -17.354 -22.587 1.00 69.17 C ATOM 2397 CDIILEA342 27.110-17.626-21.159 1.0068.85 C ATOM 2398 CG2 ILE A 342 28.024 -19.337 -23.320 1.00 69.32 C ATOM 2399 C [LE A 342 26.565 -19.437 -25.846 1.00 69.61 C ATOM 2400 0 ILE A 342 27.632 -19.764 -26.364 1.00 69.60 0 ATOM 2401 N GLNA343 25.436-20.123-26.027 1.0069.77 N ATOM 2402 CA GLN A 343 25.359 -21.194 -27.031 1.00 69.99 C ATOM 2403 CB GLN A 343 23.974 -2 1.856 -27.044 1.00 69.96 C ATOM 2404 CG GLNA343 23.772-22.873-25.937 1.0070.15 C ATOM 2405 CD GLN A 343 22.383 -23.483 -25.957 1.00 70.33 C ATOM 2406 OEI GLN A 343 21.783 -23.669 -27.044 1.00 71.09 0 ATOM 2407 NE2GLNA343 21.876-23.816-24.732 1.0070.53 N ATOM 2408 C GLNA343 25.669-20.640-28.416 1.0070.01 C ATOM 2409 0 GLNA 343 26.512-21.177-29.138 1.00 70.02 0 ATOM 2410 N LEU A 344 24.977 -19.562 -28.778 1.00 70.01 N ATOM 2411 CA LEU A 344 25.165 -18.934 -30.082 1.00 70.13 C ATOM 2412 CB LEU A 344 24.382 -17.615 -30.176 1.00 70.20 C ATOM 2413 CG LEIJ A 344 22.866 -17.683 -30.411 1.00 70.29 C ATOM 2414 CDI LEU A 344 22.234 -16.303 -30.260 1.00 70.28 C ATOM 2415 CD2 LEUA 344 22.543 -18.278 -3 1.778 1.00 70.32 C ATOM 2416 C LEUA344 26.640-18.682-30.384 1.0070.13 C ATOM 2417 0 LEUA344 27.154-19.142-31.405 1.00 70.23 0 ATOM 2418 N GLU A 345 27.323 -17.959 -29.496 1.00 70.00 N * ATOM 2419 CA GLUA345 28.670-17.481-29.815 1.0070.11 C ATOM 2420 CB GLU A 345 28.849 -16.036 -29.34 1 1.00 70.11 C ATOM 2421 CG GLUA 345 28.436-15.805 -27.898 1.00 70.34 C 1*** ATOM 2422 CD GLUA345 28.662-14.378-27.452 1.0070.34 C ATOM 2423 OEI GLU A 345 29.828 -14.018 -27.182 1.00 70.78 0 * ATOM 2424 0E2 GLU A 345 27.672 -13.618 -27.364 1.00 70.66 0 ATOM 2425 C GLU A 345 29.830 -18.345 -29.313 1.00 70.06 C : .. ATOM 2426 0 GLU A 345 30.985 -17.922 -29.375 1.00 70.05 0 ATOM 2427 N HIS A 346 29.537 -19.545 -28.823 1.00 70.09 N ATOM 2428 CA H1SA346 30.597-20.438-28.341 1.0070.11 C * ATOM 2429 CB HISA 346 30.676-20.431 -26.811 1.00 70.05 C ATOM 2430 CG HIS A 346 3 1.545 -19.349 -26.253 1.00 69.94 C ATOM 2431 ND1 H1SA346 32.919-19.371 -26.358 1.0069.85 N ATOM 2432 CEI HISA 346 33.419-18.296-25.775 1.0070.02 C ATOM 2433 NE2 HIS A 346 32.419 -17.581 -25.289 1.00 69.91 N ATOM 2434 CD2HISA346 31.236-18.218-25.574 1.0070.00 C ATOM 2435 C H1SA346 30.444-21.869-28.841 1.0070.14 C ATOM 2436 0 HIS A 346 31.236 -22.744 -28.486 1.00 70.16 0 ATOM 2437 N H1SA347 29.425-22.099-29.661 1.0070.14 N ATOM 2438 CA HIS A 347 29.158 -23.422 -30.208 1.00 70.21 C ATOM 2439 CB HIS A 347 30.145 -23.753 -3 1.329 1.00 70.15 C ATOM 2440 CG HISA 347 30.172-22.738-32.427 1.00 70.25 C ATOM 2441 NDI HIS A 347 31.071 -21.693 -32.451 1.00 70.27 N ATOM 2442 CE1 HIS A 347 30.861 -20.961 -33.532 1.00 70.36 C ATOM 2443 NE2 HIS A 347 29.859 -21.494 -34.208 1.00 70.39 N ATOM 2444 CD2 HIS A 347 29.409 -22.606 -33.538 1.00 70.34 C ATOM 2445 C HIS A 347 29.219 -24.505 -29.138 1.00 70.23 C ATOM 2446 0 HIS A 347 30.208 -25.230 -29.032 1.00 70.29 0 ATOM 2447 N 1LEA348 28.165-24.603-28.336 1.0070.25 N ATOM 2448 CA ILE A 348 28.0 14 -25.743 -27.44 1 1.00 70.37 C ATOM 2449 CB ILEA 348 28.329-25.401 -25.961 1.00 70.40 C ATOM 2450 CGI ILE A 348 27.603 -24.131 -25.524 1.00 70.55 C ATOM 2451 CDI 1LEA348 28.426-22.879-25.700 1.0070.97 C ATOM 2452 CG2 ILE A 348 29.829 -25.226 -25.759 1.00 70.45 C ATOM 2453 C ILE A 348 26.6 14 -26.336 -27.566 1.00 70.38 C ATOM 2454 0 ILEA348 25.644-25.618-27.818 1.0070.43 0 ATOM 2455 N SER A 349 26.523 -27.653 -27.407 1.00 70.37 N ATOM 2456 CA SER A 349 25.248 -28.352 -27.479 1.00 70.38 C ATOM 2457 CS SERA 349 25.471-29.867-27.539 1.00 70.40 C ATOM 2458 00 SER A 349 24.237 -30.566 -27.596 1.00 70.52 0 ATOM 2459 C SER A 349 24.382 -28.006 -26.275 1.00 70.34 C ATOM 2460 0 SER A 349 24.880 -27.934 -25.149 1.00 70.27 0 ATOM 2461 N PROA35O 23.078-27.779-26.511 1.0070.29 N ATOM 2462 CA PRO A 350 22.123 -27.530 -25.43 I 1.00 70.22 C ATOM 2463 CB PROA3SO 20.777-27.495-26.160 1.0070.23 C ATOM 2464 CC PRO A 350 2 1.122 -27.067 -27.546 1.00 70.27 C ATOM 2465 CD PROA35O 22.439-27.722-27.837 1.0070.21 C ATOM 2466 C PROA35O 22.130-28.634-24.364 1.0070.13 C ATOM 2467 0 PRO A 350 21.642 -28.421 -23.253 1.00 70.22 0 ATOM 2468 N GLYA3SI 22.689-29.795-24.695 1.0069.88 N * ATOM 2469 CA GLYA 351 22.773-30.899-23.746 1.00 69.54 C ** ATOM 2470 C GLYA 351 23.820-30.680-22.669 1.00 69.38 C *S..

ATOM 2471 0 GLYA35I 24.040-31.547-21.818 1.0069.41 0 ATOM 2472 N ASP A 352 24.468 -29.516 -22.700 1.00 69.15 N ATOM 2473 CA ASP A 352 25.539 -29.207 -21.755 1.00 68.90 C ATOM 2474 CB ASP A 352 26.748 -28.614 -22.482 1.00 68.94 C ATOM 2475 CG ASP A 352 27.470 -29.629 -23.340 1.00 69.10 C ATOM 2476 ODI ASPA 352 28.721 -29.587-23.386 1.00 69.17 0 : *.** ATOM 2477 OD2 ASP A 352 26.788 -30.470 -23.969 1.00 69.78 0 ATOM 2478 C ASP A 352 25.097 -28.251 -20.653 1.00 68.71 C *. : ATOM 2479 0 ASPA352 25.743-28.157-19.610 1.0068.69 0 * ATOM 2480 N PHE A 353 24.000 -27 541 -20.890 1.00 68.50 N ATOM 2481 CA PHEA353 23.536-26.519-19.955 1.0068.34 C ATOM 2482 CB PHE A 353 22.700 -25.470 -20.683 1.00 68.32 C ATOM 2483 CG PHE A 353 23.518 -24.413 -21.348 1.00 68.40 C ATOM 2484 CD1 PHEA 353 23.773 -23.213 -20.704 1.00 68.54 C ATOM 2485 CE1 PHE A 353 24.534 -22. 233 -21.312 1.00 68.49 C ATOM 2486 CZ PHEA 353 25.053-22.448-22.571 1.00 68. 51 C ATOM 2487 CE2PHEA 353 24.811-23.646-23.220 10068.68 C ATOM 2488 CD2 PHE A 353 24.049 -24.620 -22.608 1.00 68.56 C ATOM 2489 C PHEA 353 22.761 -27.066-18.763 1.00 68.21 C ATOM 2490 0 PHEA,353 21.997-28.021 -18.896 1.00 68.28 0 ATOM 2491 N PROA 354 22.949 -26.445 -17.589 1.00 68.04 N ATOM 2492 CA PR0A354 22.224-26.839-16.385 1.0067.82 C ATOM 2493 CB PROA 354 22.931-26.057-15.267 1.0067.87 C ATOM 2494 CG PRO A 354 24.145 -25.426 -15.899 1.00 67.91 C ATOM 2495 CD PRO A 354 23.859 -25.313 -17.348 1.00 67.93 C ATOM 2496 C PROA 354 20.773 -26.392 -16.476 1.00 67.54 C ATOM 2497 0 PRO A 354 20.406 -25.682 -17.4 12 1.00 67.44 0 ATOM 2498 N ASPA355 19.956-26.806-15.512 1.0067.25 N ATOM 2499 CA ASP A355 18.591 -26.307-15,419 1.00 66.95 C ATOM 2500 CB ASP A 355 17.806 -27.057 -14.34 1 1.00 66.98 C ATOM 2501 CG ASP A 355 16.373 -26.569 -14.2 16 1.00 67.19 C ATOM 2502 ODI ASP A 355 15.459 -27.421 -14.187 1.00 67.62 0 ATOM 2503 OD2ASPA355 16.155-25.338-14.148 1.0067.10 0 ATOM 2504 C ASPA355 18.627 -24.813 -15.111 1.00 66.67 C ATOM 2505 0 ASPA355 19.260-24.383-14.144 1.0066.78 0 ATOM 2506 N CYS A 356 17.945 -24.029 -15.940 1.00 66.16 N ATOM 2507 CA CYSA356 17.977-22.576-15.834 1.0065.72 C ATOM 2508 CB CYS A 356 17.156 -21.950 -16.964 1.00 65.76 C ATOM 2509 SG CYS A 356 17.529 -20.216 -17.290 1.00 65.98 S ATOM 2510 C CYSA356 17.470-22.090-14.478 1.0065.43 C ATOM 2511 0 CYS A 356 18.068 -21.203 -13.864 1.00 64.92 0 ATOM 2512 N GLN A 357 16.378 -22.689 -14.010 1.00 65.25 N ATOM 2513 CA 0LNA357 15.719-22.247-12.780 10065.06 C ATOM 2514 CB GLN A 357 14.262 -22.723 -12.746 1.00 65.11 C ATOM 2515 CG GLNA 357 13.336-21.874-13.615 1.0065.39 C ATOM 2516 CD GLNA357 12.050-22.588-13.988 1.0065.96 C ATOM 2517 OEI GLNA357 11.004-21.939-14.178 1.00 66.00 0 ATOM 2518 NE2GLNA357 12.123-23.933-14.100 1.0066.01 N ATOM 2519 C GLNA357 16.466-22.615-11.492 1.0064.82 C ATOM 2520 0 GLN A 357 16.503 -2 1.825 -10.54 1 1.00 64.50 0 ATOM 2521 N LYSA 358 17.061-23.805-11.458 1.0064.56 N ATOM 2522 CA LYS A 358 17.898 -24.192 -10.327 1.00 64.41 C ATOM 2523 CB LYS A 358 18.410 -25.623 -10.501 1.00 64.55 C ATOM 2524 CG LYS A 358 19.047 -26.2 18 -9. 249 1.00 65.05 C ATOM 2525 CD LYS A 358 18.000 -26.546 -8.187 1.00 65.74 C * * ATOM 2526 CE LYSA358 18.640-27.141 -6.936 1.0066.04 C ATOM 2527 NZ LYS A 358 17.621 -27.613 -5.948 1.00 66.17 N ATOM 2528 C LYSA358 19.067-23.215-10.243 1.0064.12 C ATOM 2529 0 LYS A 358 19.329 -22.600 -9.193 1.00 63.78 0 **** ATOM 2530 N META359 19.752-23.074-11.374 1.0063.91 N ATOM 2531 CA META 359 20.818-22.101 -11.531 1.00 63.82 C ATOM 2532 CB META359 21.298-22.083-12.984 1.0063.91 C ATOM 2533 CG META359 22.634-21.389-13.214 1.0064.20 C ATOM 2534 SD META 359 24.047 -22.269-12.508 1.00 65.02 S : ** ATOM 2535 CE META359 25.409-21.348-13. 220 1.0064.30 C ATOM 2536 C META 359 20.322-20.719-11.117 1.00 63.69 C *. ATOM 2537 0 META 359 21.086-19.907-10.602 1.00 63.41 0 * ATOM 2538 N GLN A 360 19.037 -20.459-11.328 1.00 63.78 N ATOM 2539 CA OLNA 360 18.454-19.186-10.916 1.00 63.51 C ATOM 2540 CB GLNA36O 17.126-18.937-11.632 1.0063.59 C ATOM 2541 CG GLNA36O 17.299-18.365-13. 029 1.0063.62 C ATOM 2542 CD GLNA36O 16.031-18.412-13.856 10063.50 C ATOM 2543 OE1GLNA36O 15.815-17.566-14.722 1.0063.52 0 ATOM 2544 NE2 GLN A 360 15. 187 -19.403 -13.595 1.00 63.46 N ATOM 2545 C GLN A 360 18.297 -19.059 -9.399 1.00 63.40 C ATOM 2546 0 GLNA36O 18.546-17.991 -8.834 1.0063.16 0 ATOM 2547 N GLUA36I 17.895-20.144 -8.741 1.0063.45 N ATOM 2548 CA GLU A 361 17.802 -20.151 -7.279 1.00 63.14 C ATOM 2549 CB GLUA36I 17.142-21.442 -6.790 1.0063.14 C ATOM 2550 CO GLU A 361 15.901 -22.350 -6.363 0.00 50. 00 C ATOM 2551 CD GLUA361 15.696-23.530 -5.435 0.0050.00 C ATOM 2552 OEI GLUA 361 16.150-24.642 -5.776 0.00 50.00 0 ATOM 2553 0E2 GLU A 361 15.081 -23.346 -4.363 0.00 50.00 0 ATOM 2554 C GLU A 361 19.184 -19.978 -6.637 1.00 63.01 C ATOM 2555 0 GLU A 361 19.382 -19.152 -5.715 1.00 62.82 0 ATOM 2556 N LEUA 362 20.148 -20.751 -7.138 1.00 62.93 N ATOM 2557 CA LEUA362 21.511 -20.662 -6.617 1.00 62.55 C ATOM 2558 CB LEUA362 22.361-21.809-7.164 1.0062.51 C ATOM 2559 CG LEUA362 21.784-23.205 -6.916 1.0062.22 C ATOM 2560 CDI LEU A 362 22.74 1 -24.272 -7.4 16 1.00 61.94 C ATOM 2561 CD2 LEU A 362 21.471 -23.409 -5.440 1.00 61.87 C ATOM 2562 C LEUA362 22.154-19.299 -6.921 1.0062.44 C ATOM 2563 0 LEUA 362 22.811 -18.678 -6.052 1.00 62.11 0 ATOM 2564 N LEU A 363 21.960 -18.832 -8.156 1.00 62.56 N ATOM 2565 CA LEU A 363 22.412 -17.501 -8.530 1.00 62.37 C ATOM 2566 CB LEU A 363 22.080 -17.199 -9.993 1.00 62.32 C ATOM 2567 CG LEUA363 23.212-17.346-11.013 1.0062.11 C ATOM 2568 CD1 LEU A 363 24.325 -16.381 -10.684 1.00 62.15 C ATOM 2569 CD2LEUA 363 23.753-18.759-11.056 1.00 61.97 C ATOM 2570 C LEU A 363 2 1.759 -16.483 -7.609 1.00 62.38 C ATOM 2571 0 LEUA363 22.362-15.468 -7.261 1.0062.29 0 ATOM 2572 N META 364 20.521 -16.770 -7.213 1.00 62.56 N ATOM 2573 CA META 364 19.821 -15.949 -6.229 1.00 62.46 C ATOM 2574 CB MET A 364 18.376 -16.436 -6.047 1.00 62.50 C ATOM 2575 Co MET A 364 17.449 -15.444 -5.357 1.00 62.64 C ATOM 2576 SD META 364 17.255-13.900 -6.279 1.00 63.45 S ATOM 2577 CE META 364 15.974-13.066 -5.331 1.00 63.02 C ATOM 2578 C META364 20.576-16.000 -4. 903 1.0062.32 C ATOM 2579 0 META364 20.579-15.030 -4.142 1.0062.24 0 ATOM 2580 N ALAA 365 21.227-17.132 -4.638 1.00 62.25 N ATOM 2581 CA ALAA 365 22.014-17.277 -3.401 1.00 61.89 C ATOM 2582 CB ALAA 365 22.130-18.749 -3.012 1.00 61.88 C ATOM 2583 C ALAA365 23.406-16.615 -3.399 1.0061.73 C ATOM 2584 0 ALAA365 23.901 -16.219 -2.344 1.00 61.65 0 * ATOM 2585 N H1SA366 24.039-16.491 -4.565 1.0061.58 N *. ATOM 2586 CA HISA 366 25.428-15.979 -4.623 1.0061.07 C ATOM 2587 CB H1SA366 26.178-16.621 -5. 786 1.00 61.07 C ATOM 2588 Co HIS A 366 26.701 -17.983 -5.478 1.00 60.77 C ATOM 2589 ND1HISA366 25.881-19.026 -5.107 1.0060.88 N ATOM 2590 CEI HIS A 366 26.6 13 -20.104 -4.894 1.00 61.03 C ATOM 2591 NE2HISA366 27.879-19. 796 -5.114 1.00 61.08 N ATOM 2592 CD2 HIS A 366 27.961 -18.475 -5.48 1 1.00 60.66 C * ** ATOM 2593 C H1SA366 25.606-14.462 -4.714 1.0060.91 C ATOM 2594 0 HIS A366 24.659-13.732 -4.999 1.00 60.95 0 . : ATOM 2595 N ASPA367 26.837-14.001 -4.476 1.0060.67 N * ATOM 2596 CA ASP A 367 27.209 -12.600 -4.702 1.00 60.54 C ATOM 2597 CB ASP A 367 28.089 -12.052 -3.576 1.00 60.59 C ATOM 2598 CO ASP A 367 28.551 -10.615 -3.839 1.00 60.69 C ATOM 2599 OD1 ASP A 367 29.141 -9.993 -2.927 1.00 60.49 0 ATOM 2600 0D2 ASP A 367 28.324 -10.103 -4.958 1.00 60.90 0 ATOM 2601 C ASP A 367 27.947 -12.442 -6.020 1.00 60.51 C ATOM 2602 0 ASP A 367 28.946-13.117 -6.273 1.00 60.68 0 ATOM 2603 N PHE A 368 27.468 -11.519 -6.845 1.00 60.30 N ATOM 2604 CA PHEA 368 27.980-11.376 -8.194 1.00 60.01 C ATOM 2605 CB PHE A 368 26.956 -10.666 -9.076 1.00 60.10 C ATOM 2606 CG PHEA368 25.846-11.562 -9.547 1.0060.32 C ATOM 2607 CDI PHE A 368 25.3 15 -12.532 -8.707 1.00 60.54 C ATOM 2608 CEI PHEA 368 24.295-13.358 -9.133 1.00 60.45 C ATOM 2609 CZ PHE A 368 23.784 -13.217 -10.408 1.00 60.53 C ATOM 2610 CE2PHEA368 24.299-12.251 -11.256 1.0060.66 C ATOM 2611 CD2 PHE A 368 25.323 -11.430-10.823 1.00 60.62 C ATOM 2612 C PHE A 368 29.324 -10.673 -8.238 1.00 59.80 C ATOM 2613 0 PHEA368 30.204-11.067 -8.998 1.0059.86 0 ATOM 2614 N THR A 369 29.486 -9.641 -7.417 1.00 59.53 N ATOM 2615 CA THRA 369 30.717 -8.854 -7.432 1.00 59.25 C ATOM 2616 CB THRA369 30.613 -7.593 -6.543 1.0059.18 C ATOM 2617 OG1 TI-IRA 369 30.494 -7.974 -5.167 1.00 59.25 0 ATOM 2618 CG2THRA369 29.407 -6.761 -6.943 1.005910 C ATOM 2619 C THR A 369 3 1.927 -9.69 1 -7.025 1.00 59.10 C ATOM 2620 0 THRA 369 33.068 -9.311 -7.280 1.00 58.97 0 ATOM 2621 N LYS A 370 3 1.670 -10.840 -6.407 1.00 59.01 N ATOM 2622 CA LYS A 370 32.740-11.725 -5.960 1.00 58.97 C ATOM 2623 CR LYS A 370 32.3 18 -12.482 -4.699 1.00 59.01 C ATOM 2624 CG LYSA37O 31.859-11.596 -3.550 1.0059.07 C ATOM 2625 CD LYS A 370 33.008-11.175 -2.649 1.00 59.12 C ATOM 2626 CE LYS A 370 32.490 -10.481 -1.392 1.00 59.61 C ATOM 2627 NZ LYS A 370 31.488 -11.309 -0.638 1.00 59.98 N ATOM 2628 C LYSA37O 33.152-12.715 -7.047 1.00 58.95 C ATOM 2629 0 LYS A 370 34.235 -13.292 -6,982 1.00 58.95 0 ATOM 2630 N PHEA37I 32.285-12.914 -8.039 1.00 58.98 N ATOM 2631 CA PHEA371 32.595-13.790 -9.170 1.0059.03 C ATOM 2632 CB PHEA 371 31.474-13.759-10.214 1.00 58.86 C ATOM 2633 CG PHEA371 30.216-14.459 -9.785 1.0058.79 C ATOM 2634 CDI PHE A 371 28.979 -14.003 -10.210 1.00 58.52 C ATOM 2635 CE! PHE A 371 27.818 -14.644 -9. 823 1.00 58.30 C ATOM 2636 CZ PHE A 371 27.883 -15.752 -9.000 1.00 58.32 C ATOM 2637 CE2PHEA37I 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 37! 33.902 -13.386 -9.840 1.00 59.21 C ATOM 2640 0 PHEA 371 34.291 -12.223 -9.804 1.00 59.25 0 ATOM 2641 N H1SA372 34.579-14.346-10.456 1.0059.50 N : ***, ATOM 2642 CA HIS A 372 35.789 -14.040 -11.206 1.00 59.80 C ATOM 2643 CB HIS A 372 36.798 -15.180 -11.093 1.00 59.85 C S..... ATOM 2644 CG HIS A 372 37.463 -15.261 -9.756 1.00 59.95 C ATOM 2645 ND! H1SA372 38.399-14.342 -9.335 1.00 59.92 N ATOM 2646 CEIHISA372 38.814-14.663 -8.123 1.0060.28 C ATOM 2647 NE2HISA372 38.178-15.756 -7.741 1.00 60.47 N ATOM 2648 CD2 HIS A 372 37.327 -16.150 -8.744 1.00 60.21 C * * ATOM 2649 C HIS A 372 35.468 -13.754 -12.668 1.00 59.98 C ATOM 2650 0 HISA 372 34.385-14.092-13.149 1.00 60.08 0 ATOM 2651 N SERA 373 36.413-13.130-13.370 1.0060.16 N ATOM 2652 CA SERA 373 36.231 -12.788-14.783 1.00 60.24 C . : ATOM 2653 CB SERA 373 37.012-11.521 -15.135 1.00 60.28 C * ATOM 2654 OG SERA 373 36.688-10.461 -14.252 1.00 60.74 0 ATOM 2655 C SERA 373 36.664 -13.918-15.705 1.00 60.17 C ATOM 2656 0 SERA 373 37.354-14.847-15.291 1. 00 60.00 0 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 1.00 60.62 C ATOM 2659 CB LEU A 374 36.125 -14.424 -19.333 1.00 60.56 C ATOM 2660 CG LEUA374 36.072-15.531 -20.384 1.00 60.72 C ATOM 2661 CDI LEUA 374 34.98! -15.247-21.409 1.00 61.21 C ATOM 2662 CD2 LEt) A 374 37.420 -15.707 -21.060!.00 60.74 C ATOM 2663 C LEU A 374 38.184 -14.936 -17.972 1.00 60.76 C ATOM 2664 0 LEUA 374 38.894 -13.933 -17.917 1.00 60.93 0 ATOM 2665 N LYSA375 38.682-16.167-18.030 1.0060.82 N ATOM 2666 CA LYS A 375 40.120 -16.420 -18.015 1.00 60.84 C ATOM 2667 CB LYS A 375 40.535 -17.002 -16.664 1.00 60.91 C ATOM 2668 CG LYS A 375 40.369 -16.044 -15.498 1.00 61.48 C ATOM 2669 CD LYS A 375 41.697 -15.434 -15.084 1.00 62.71 C ATOM 2670 CE LYS A 375 42.553 -16.457 -14.337 1.00 63.51 C ATOM 2671 NZ LYS A 375 43.854 -15.899 -13.868 1.00 63.82 N ATOM 2672 C LYSA375 40.491-17.381-19.138 1.0060.68 C ATOM 2673 0 LYSA375 40.479-18.595-18.946 1.0060.73 0 ATOM 2674 N PR0A376 40.838-16.837-20.313 1.0060.57 N ATOM 2675 CA PR0A376 41.018-17.632-21526 1.0060.57 C ATOM 2676 CB PR0A376 41.521-16.607-22.545 1.00 60.60 C ATOM 2677 CO PRO A 376 41.046 -15.295 -22.034 1.00 60.61 C ATOM 2678 CD PR0A376 41.097-15.407-20.544 1.0060.55 C ATOM 2679 C PRO A 376 42.042 -18.746 -2 1.353 1.00 60.59 C ATOM 2680 0 PROA 376 41.907 -19.809 -21.956 1.00 60.69 0 ATOM 2681 N LYS A 377 43.050 -18.495 -20.525 1.00 60.59 N ATOM 2682 CA LYS A 377 44.13 1 -19.446 -20.285 1.00 60.71 C ATOM 2683 CB LYSA377 45.129-18.839-19.295 1.0060.74 C ATOM 2684 CO LYSA377 44.517-17.771 -18.384 1.00 61.05 C ATOM 2685 CD LYSA377 45.457-17.378-17.246 1.0061.19 C ATOM 2686 CE LYS A 377 45.573 -18.489 -16.201 1.00 61.82 C ATOM 2687 NZ LYSA377 46.528-18.146-15.102 1.0062.06 N ATOM 2688 C LYS A 377 43.654 -20.82 1 -19.798 1.00 60.59 C ATOM 2689 0 LYS A 377 43.932 -2 1.849 -20.429 1.00 60.69 0 ATOM 2690 N LEUA 378 42.935-20.834-18.678 1.00 60.51 N ATOM 2691 CA LEU A 378 42.450 -22.076 -18.077 1.00 60.41 C ATOM 2692 CB LEUA 378 41.743 -21.783 -16.757 1.00 60.35 C ATOM 2693 CO LEU A 378 42.521 -20.939 -15.743 1.00 60.12 C ATOM 2694 CDI LEUA 378 41.617-20.552-14.588 1.00 59.86 C ATOM 2695 CD2LEUA378 43.767-21.663-15.242 1.0059.70 C ATOM 2696 C LEU A 378 4 1.507 -22.807 -19.022 1.00 60.42 C ATOM 2697 0 LEU A 378 41.628 -24.019 -19.238 1.00 60.64 0 ATOM 2698 N LEU A 379 40.564 -22.056 -19.578 1.00 60.36 N ATOM 2699 CA LEUA379 39.686-22.568-20.617 1.0060.34 C a.

* *** ATOM 2700 CB LEU A 379 38.868 -21.425 -21.214 1.00 60.18 C ATOM 2701 CO LEUA379 37.657-21.020-20.372 1.0059.81 C ATOM 2702 CD1LEUA379 37.524-19.515-20.250 1.0059.39 C ATOM 2703 CD2 LEU A 379 36.394 -21.632 -20.952 1.00 59.83 C ATOM 2704 C LEUA 379 40.493-23.284-21.695 1.0060.50 C ATOM 2705 0 LEUA 379 40.278-24.470-21.961 1.00 60.81 0 ATOM 2706 N GLUA 380 41.432 -22.567 -22.304 1.00 60.65 N * ATOM 2707 CA GLU A 380 42,308 -23.167 -23.303 1.00 60.83 C * ** 45 ATOM 2708 CB GLUA38O 43.438-22.214-23.691 1.0060.85 C ATOM 2709 CO GLUA38O 43118-21.304-24.858 1.00 60.88 C ATOM 2710 CD GLU A 380 44.355 -20.937 -25.648 1.00 61.03 C ATOM 2711 OE1GLUA38O 44.281-20.931-26.892 1.0061.38 0 ATOM 2712 0E2 GLU A 380 45.407 -20.673 -25.029 1.0061.20 0 ATOM 2713 C GLUA38O 42.896-24.470-22.786 1.0060.92 C ATOM 2714 0 GLU A 380 42.872 -25.499 -23.481 1.00 61.26 0 ATOM 2715 N ALAA381 43.424-24.420-21.564 1.0060.89 N ATOM 2716 CA ALA A 381 43.984 -25.606 -20.931 1.00 61.02 C ATOM 2717 CU ALAA3SI 44.320-25.322-19.480 1.0060.97 C ATOM 2718 C ALAA 381 42.991 -26.754-21.036 1.00 61.14 C ATOM 2719 0 ALA A 381 43.344 -27.872 -21.425 1.00 61.43 0 ATOM 2720 N LEUA 382 41.741 -26.460-20.701 1.00 61.13 N ATOM 2721 CA LEU A 382 40.666 -27.438.20.800 1.00 61.34 C ATOM 2722 CB LEU A 382 39.365 -26.808 -20.291 1.00 61.35 C ATOM 2723 cci LEUA382 38.199-27.671-19.802 1.0061.48 C ATOM 2724 CDI LEU A 382 37.136 -27.835 -20.885 1.00 61.27 C ATOM 2725 CD2 LEU A 382 38.694 -29.019 -19.281 1.00 62.11 C ATOM 2726 C LEU A 382 40.506.27964 -22.236 1.00 61.46 C ATOM 2727 0 LEU A 382 40.736 -29.157 -22.509 1.0061 78 0 ATOM 2728 N ASPA 383 40.127-27.070-23.150 1.00 61.44 N ATOM 2729 CA ASPA383 39.867-27.453-24.543 1.00 61.75 C ATOM 2730 CB ASP A 383 39.743 -26.209 -25.431 1.00 61.77 C ATOM 2731 Cci ASP A383 38.778-25.172-24.868 1.00 61.90 C ATOM 2732 OD1 ASPA 383 38.498-25.208-23.654 1.00 62.19 0 ATOM 2733 OD2 ASP A 383 38.302 -24.311 -25.640 1.00 62.06 0 ATOM 2734 C ASPA383 40.974-28.358-25.074 1.0061.90 C ATOM 2735 0 ASP A 383 40.722 -29.47 1 -25.589 1.00 62.21 0 ATOM 2736 N ASPA 384 42.204-27.870-24.934 1.00 61.93 N ATOM 2737 CA ASP A 384 43.377 -28 633 -25.329 1.00 62.20 C ATOM 2738 CB ASPA384 44.659-27.857-25.012 1.0062.22 C ATOM 2739 Cci ASP A 384 45,905 -28.552.25.527 1.00 62.42 C ATOM 2740 OD1 ASP A 384 46.168 -28.477 -26. 747 1.00 62.53 0 ATOM 2741 0D2 ASP A 384 46.625 -29.168 -24.711 1.00 62.70 0 ATOM 2742 C ASP A 384 43.387 -29.985 -24.621 1.00 62.27 C ATOM 2743 0 ASP A 384 43.630 -3 1.022 -25.261 1.00 62.50 0 ATOM 2744 N META 385 43.109 -29.969 -23.310 1.00 62.20 N ATOM 2745 CA MET A 385 43.094 -31.206 -22. 531 1.00 62.37 C ATOM 2746 CB META 385 42.531 -31 035 -21.1 14 1.00 62.38 C ATOM 2747 CG MET A 385 42.451 -32.383 -20.351 1.00 62.39 C ATOM 2748 SD META 385 41.135-32.605-19.117 1.00 62.11 S ATOM 2749 CE META 385 39.727-33.021 -20.153 1.00 61.97 C ATOM 2750 C MET A 385 42.244 -32.2 16 -23.244 1.00 62.48 C ATOM 2751 0 META385 42.760-33.215-23.768 1.0062.86 0 ATOM 2752 N LEUA386 40.937-31.958-23.272 1.0062.43 N ATOM 2753 CA LEUA3S6 40.058-32.982-23.813 1.0062.76 C ATOM 2754 CB LEU A 386 38.556 -32.642 -23.723 1.00 62.76 C ATOM 2755 Cci LEU A 386 37.940 -3 1.254 -23.928 1.00 62.69 C ATOM 2756 CDI LEU A 386 36.474 -3 1.394 -24.3 17 1.00 62.40 C ATOM 2757 CD2 LEU A 386 38.072 -30.425 -22.665 1.00 62.82 C ATOM 2758 C LEUA 386 40.515-33.334-25.217 1.0062.86 C * . ATOM 2759 0 LEUA386 40.936-34.480-25.461 1.0063.18 0 ATOM 2760 N ALA A 387 40.506 -32.335 -26.104 1.00 62.84 N ATOM 2761 CA ALA A 387 40.937 -32.545 -27.487 1.00 63.11 C ATOM 2762 CB ALAA 387 41.213 -31.207 -28.168 1.00 62.92 C * ATOM 2763 C ALAA 387 42.163-33.465-27.585 1.0063.24 C ATOM 2764 0 ALAA387 42.042-34.694-27.776 1.0063.61 0 ATOM 2765 N GLNA 388 43.343-32.877-27. 416 1.00 63.14 N ATOM 2766 CA GLN A 388 44.582 -33 594 -27.698 1.00 63.43 C * ** ATOM 2767 CB GLN A 388 45.744 -32.603.27.824 1.00 63.49 C ATOM 2768 Cci GLNA 388 45.354-31.297-28.512 1.00 63.57 C * ATOM 2769 CD GLNA388 46.408-30.790-29.481 1.0063.61 C ATOM 2770 OE1GLNA388 47.175-31.570-30. 053 1.00 63.36 0 ATOM 2771 NE2 GLN A 388 46.44 1.29.477 -29.681 1.00 63.79 N ATOM 2772 C GLN A 388 44.906 -34.688 -26.676 1.00 63.52 C ATOM 2773 0 GLN A 388 45.198 -35.850 -27.041 1.00 63.82 0 ATOM 2774 N ASP A 389 44.844 -34.323 -25.397 1.00 63.47 N ATOM 2775 CA ASP A 389 45.269 -35.242 -24. 354 1.00 63.75 C ATOM 2776 CB ASP A389 45.274-34.549-22.992 1.00 63.76 C ATOM 2777 Cci ASP A 389 46.351 -33.484 -22.888 1.0064.01 C ATOM 2778 ODI ASP A 389 47.535 -33.801 -23.137 1.00 64.41 0 ATOM 2779 OD2 ASP A 389 46.017 -32.328 -22.554 1.0064.29 0 ATOM 2780 C ASP A 389 44 395 -36.491 -24.338 1.00 63.83 C ATOM 2781 0 ASPA389 44.909-37.633-24.114 1.0064.19 0 ATOM 2782 N ILE A 390 43.082 -36.290 -24.600 1.00 63.79 N ATOM 2783 CA ILE A 390 42.202 -37.449 -24.564 1.00 64.00 C ATOM 2784 CB ILE A 390 40.757 -37.05 1 -24.238 1.00 63.95 C ATOM 2785 CG1 ILEA 390 40.670-36.707-22.748 1.0063.71 C ATOM 2786 CD1 ILE A 390 39.357 -36.139 -22.3 18 1.00 63.77 C ATOM 2787 CG2 ILE A 390 39.789 -38 171 -24.600 1.00 63.97 C ATOM 2788 C JLE A 390 42.349 -38.215 -25.875 1.00 64.14 C ATOM 2789 0 ILEA39O 42.347-39.465 -25.896 1.00 64.58 0 ATOM 2790 N ALA A 391 42.530 -37.458 -26.958 1.00 64.14 N ATOM 2791 CA ALA A 391 42.907 -38.063 -28.225 1.00 64.26 C ATOM 2792 CB ALA A 391 43.364 -37.001 -29.2 10 1.00 64.25 C ATOM 2793 C ALA A 391 43.998 -39.120 -28.018 1.00 64.38 C ATOM 2794 0 ALA A 391 43.828 -40.265 -28.427 1.00 64.34 0 ATOM 2795 N LYSA392 45.100-38.750-27.361 1.0064.51 N ATOM 2796 CA LYSA 392 46.252-39.681 -27.211 1.00 65.03 C ATOM 2797 CB LYSA 392 47.541 -38.900-26.844 1.00 65.00 C ATOM 2798 CO LYS A 392 48.702 -39.822 -26.46 1 1.00 65.42 C ATOM 2799 CD LYS A 392 49.804 -39.084 -25.687 1.00 65.51 C ATOM 2800 CE LYS A 392 49.376 -38.797 -24.226 1.00 66.25 C ATOM 2801 NZ LYS A 392 50.460 -38.108 -23.435 1.00 66.63 N ATOM 2802 C LYS A 392 46.064 -40.824 -26.164 1.00 65.09 C ATOM 2803 0 LYS A 392 46.422 -42.067 -26.150 1.00 65.53 0 ATOM 2804 N LEU A 393 45.000 -40.372 -25.222 1.00 65.09 N ATOM 2805 CA LEU A 393 44.770 -41.413 -24.203 1.00 65.41 C ATOM 2806 CB LEU A 393 44.067 -40.850 -22.966 1.00 65.35 C ATOM 2807 CG LEU A 393 45.072 -40.402 -2 1.908 1.00 65.48 C ATOM 2808 CD1 LEU A 393 44.354 -39.831 -20.708 1.00 65.63 C ATOM 2809 CD2LEUA393 45.954-41.576-21.502 1.0065.50 C ATOM 2810 C LEUA 393 43.969-42559-24.811 1.0065.64 C ATOM 2811 0 LEUA393 44.037-43.692-24.318 1.0065.90 0 ATOM 2812 N META394 43.227-42.276-25.889 1.0065.68 N ATOM 2813 CA META394 42.453-43.350-26.532 1.0066.07 C ATOM 2814 CB META394 41.660-42.822-27.736 1.0066.11 C ATOM 2815 CG MET A 394 40.545 -41.845 -27.371 1.00 66.43 C : ... ATOM 2816 SD META 394 39.379-42.505-26.151 1.00 67.28 S ATOM 2817 CE META 394 38.146-41.197-26.108 1.00 66.63 C ATOM 2818 C META 394 43.334-44.552-26.932 1.00 66.21 C ATOM 2819 0 META 394 43.125-45.678-26.449 1.00 66.49 0 ATOM 2820 N PROA 395 44.324-44.319-27.820 1.0066.35 N ATOM 2821 CA PRO A 395 45.221 -45.400 -28.246 1.00 66.36 C ATOM 2822 CB PRO A 395 46.359 -44.656 -28.950 1.00 66.30 C * ATOM 2823 CO PRO A 395 45.708 -43.450 -29.505 1.00 66.32 C ATOM 2824 CD PRO A 395 44.637 -43.024 -28.496 1.00 66.42 C ATOM 2825 C PROA395 45.788-46.183-27.065 1.0066.38 C ATOM 2826 0 PROA 395 45.847-47.571 -27.111 1.00 66.53 0 . . ATOM 2827 N LEUA 396 45.997-45.303-25.853 1.00 66.35 N ATOM 2828 CA LEU A 396 46.746 -46.083 -24.821 1.00 66.51 C ATOM 2829 CB LEUA396 47.352-45.178-23.729 1.0066.52 C ATOM 2830 CO LEU A 396 48.412 -45.758 -22.772 1.00 66.50 C ATOM 2831 CD1 LEUA396 48.815-44.715-21.728 1.0066.78 C ATOM 2832 CD2 LEU A 396 47.966 -47.051 -22.076 1.00 66.41 C ATOM 2833 C LEUA 396 45.701 -47.020-24.189 1.0066.56 C ATOM 2834 0 LEU A 396 45.970 -48.217 -23.789 1.00 66.72 0 ATOM 2835 N LEU A 397 44.490 -46.430 -24.125 1.00 66.57 N ATOM 2836 CA LEU A 397 43.335 -47.098 -23.570 1.00 66.81 C ATOM 2837 CB LEU A 397 42.107 -46.199 -23.695 1.00 66.77 C ATOM 2838 CO LEU A 397 40.789 -46.797 -23 217 1.00 66.74 C ATOM 2839 CD1 LEU A 397 40.828 -47.016 -21.711 1.00 66.79 C ATOM 2840 CD2 LEU A 397 39.643 -45.884 -23.609 1.00 66.83 C ATOM 2841 C LEUA397 43.082-48.420-24.267 1.0066.95 C ATOM 2842 0 LEU A 397 42.883 -49.426 -23.605 1.0067.22 0 ATOM 2843 N ARG A 398 43.092 -48.416 -25.599 1.00 67.02 N ATOM 2844 CA ARG A 398 42.836-49.643 -26.369 1.00 67.30 C ATOM 2845 CB ARG A 398 42.850 -49.332 -27.868 1.00 67.36 C ATOM 2846 CO ARGA398 41.808-48.309-28.301 1.0067.98 C ATOM 2847 CD ARGA398 42.319-47.456-29. 459 1.0068.97 C ATOM 2848 NE ARG A 398 42.794 -48.259 -30.583 1.00 69.67 N ATOM 2849 CZ ARGA398 42.005-48.760-31.532 1.00 70.33 C ATOM 2850 NH! ARG A 398 42.528 -49.478 -32.520 1.00 70.67 N ATOM 2851 NH2 ARG A 398 40.693 -48.547 -31.494 1.00 70.46 N ATOM 2852 C ARGA398 43.866-50744-26.069 1.0067.28 C ATOM 2853 0 ARG A 398 43.504 -52.040 -25.930 1.00 67.55 0 ATOM 2854 N GLNA 399 45.149-50.229-25.856 1.00 67.15 N ATOM 2855 CA GLN A 399 46.206 -5 1.190 -25.539 1.00 67.22 C ATOM 2856 CB GLN A 399 47.589 -50. 529 -25.575 1.00 67.21 C ATOM 2857 CO GLNA399 48.756-51.484-25.318 1.0067.20 C ATOM 2858 CD GLN A 399 48.755 -52.683 -26.261 1.00 67.24 C ATOM 2859 OEI GLN A 399 48.822 -53.832 -25.8 13 1.00 67.09 0 ATOM 2860 NE2GLNA399 48.674-52.421 -27.571 1.0067.33 N ATOM 2861 C GLN A 399 45.927 -51.801 -24.170 1.00 67.26 C ATOM 2862 0 GLN A 399 46.229 -52.973 -23.925 1.00 67.20 0 ATOM 2863 N GLU A 400 45.333 -5 1.006 -23.282 1.00 67.33 N ATOM 2864 CA GLU A 400 44.948 -5 1.520 -21.970 1.00 67.67 C ATOM 2865 CB GLU A 400 44.770 -50.383 -20.966 1.00 67.73 C ATOM 2866 CG GLU A 400 46.081 -49.853 -20.396 1.00 68.29 C ATOM 2867 CD GLU A 400 45.856 -49.020 -19. 145 1.00 68.96 C ATOM 2868 OE1 GLU A 400 46.798 -48.311 -18.724 1.00 69.08 0 ATOM 2869 0E2 GLU A 400 44.735 -49.077 -18.586 1.00 69.03 0 ATOM 2870 C GLU A 400 43.681 -52.374 -22.016 1.00 67.75 C ATOM 2871 0 GLUA400 43.505-53276-21.197 1.00 67.75 0 ATOM 2872 N GLUA4OI 42.802-52.089-22.974 1.0067.83 N ATOM 2873 CA GLUA 401 41.535 -52.807-23.088 1.00 68.15 C : ,, ATOM 2874 CB GLU A 401 40.515 -52.036 -23.945 1.00 68.25 C ATOM 2875 CG GLUA4O1 39.080-52.606-23.881 1.0068.55 C *1* ATOM 2876 CD GLUA4O1 38.001-51.549-24.104 1.0068.79 C ATOM 2877 OEI GLU A 401 38.129 -50.435 -23.549 1.00 68.79 0 ATOM 2878 OE2GLUA4OI 37.017-51.839-24.824 1.0068.49 0 ATOM 2879 C GLUA4OI 41.775-54.218-23.626 1.0068.19 C : ATOM 2880 0 GLUA4O1 40.863-55.103-23.541 1.0068.20 0 * ATOM 2881 N LEUA 402 43.014-54.443-24.161 1.00 68.10 N ATOM 2882 CA LEU A 402 43.360 -55.876 -24.349 1.00 68.26 C : *. ATOM 2883 CB LEU A 402 43.651 -56.248 -25.818 1.00 68.22 C ATOM 2884 CG LEU A 402 44.480 -55.3 86 -26.774 1.00 68.29 C *. ATOM 2885 CDI LEU A 402 45.951 -55.301 -26.369 1.00 68.15 C * ATOM 2886 CD2 LEU A 402 44.340 -55.954 -28.185 1.00 68.27 C ATOM 2887 C LEU A 402 44.480 -56.322 -23.386 1.00 68.35 C ATOM 2888 0 LEUA4O2 45.647-56.557-23.789 1.0068.28 0 ATOM 2889 N GLU A 403 44.107 -56.428 -22.102 1.00 68.52 N ATOM 2890 CA GLUA4O3 45.088-56.755-21 065 1.00 68.65 C ATOM 2891 CB GLUA 403 45.431 -55.521 -20.224 1.00 68.70 C ATOM 2892 CG GLU A 403 46.49 1 -54.639 -20.862 1.00 68.74 C ATOM 2893 CD GLU A 403 47. 7 15 -55.426 -2 1.293 1.00 68.53 C ATOM 2894 OE1 GLU A 403 47.701 -56.670 -21.161 1.00 68.11 0 ATOM 2895 OE2 GLU A 403 48.691 -54.802 -21.761 1.00 68.50 0 ATOM 2896 C GLU A 403 44.7 14 -57.924 -20.161 1.00 68.69 C ATOM 2897 0 GLUA4O3 45.249-59.023-20.320 1.0068.78 0 ATOM 2898 N SERA 404 43.817-57.699-19.204 1.00 68.70 N ATOM 2899 CA SER A 404 43.474 -58.768 -18.266 1.00 68.71 C ATOM 2900 CB SER A 404 44.240 -58.599.16.944 1.00 68.72 C ATOM 2901 OG SER A 404 44.441 -59.853 -16.305 1 0068 64 0 ATOM 2902 C SER A 404 4 1.970 -58.933 -18.010 1.00 68.68 C ATOM 2903 0 SERA 404 41.344-58.123 -17.318 1.00 68.72 0 ATOM 2904 N VAL A 405 4 1.405 -59.999 -18.576 1.00 68.52 N ATOM 2905 CA VALA 405 40.014 -60.373 -18.330 1.00 68.31 C ATOM 2906 CB VAL A 405 39.5 15 -61.401 -19.382 1 0068.37 C ATOM 2907 CGI VALA4O5 38.017-61.661 -19.226 1.00 68.42 C ATOM 2908 CG2 VAL A 405 40.3 16 -62.702 -19.301 1.00 68.30 C ATOM 2909 C VALA 405 39.859-60.941.16.914 1.00 68.09 C ATOM 2910 0 VALA4O5 38.742-61.172-16. 440 1.0068.12 0 ATOM 2911 N GLU A 406 40.994 -6 1.154 -16.249 1.00 67.77 N ATOM 2912 CA GLUA4O6 41.041 -61.660-14.875 1.0067.37 C ATOM 2913 CB GLU A 406 42.492 -61.732 -14.388 1.00 67.50 C ATOM 2914 CG GLU A 406 42.647 -62.138 -12.926 1.00 67.80 C ATOM 2915 CD GLUA 406 43.569-61.202-12.160 1.00 68.31 C ATOM 2916 OE1 GLUA4O6 44.561 -61.685-11.570 1.0068.29 0 ATOM 2917 OE2GLUA4O6 43.301 -59.978-12.151 1.00 68.51 0 ATOM 2918 C GLU A 406 40.234 -60.777 -13.926 1.00 66.93 C ATOM 2919 0 GLUA4O6 39.662-61.265.12.946 1.0066.98 0 ATOM 2920 N ALA A 407 40.197.59.479 -14.224 1.00 66.23 N ATOM 2921 CA ALA A 407 39.443 -58.5 16 -13.424 1.00 65.47 C ATOM 2922 CB ALA A 407 39.721 -57.094 -13.907 1.00 65.49 C ATOM 2923 C ALA A 407 37.940 -58.813 -13.441 1.00 64.85 C ATOM 2924 0 ALA A 407 37.202 -58.369 -12.555 1.00 64.84 0 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 -14.6 17 1.00 62.9 1 C ATOM 2927 C GLY A 408 35.433.60.428 -13.348 1.00 62.16 C ATOM 2928 0 GLYA4O8 36.082-61.020-12.486 1.0062.11 0 ATOM 2929 N VAL A 409 34.133 -60.180 -13.234 1.00 61.40 N ATOM 2930 CA VALA 409 33.380-60.595-12.059 1.00 60.66 C ATOM 2931 CB VAL A 409 31.952 -60.013 -12.059 1.00 60.68 C :

. ATOM 2932 CGI VAL A 409 31.345 -60.103 -10.670 1.00 60.53 C ATOM 2933 CG2VALA4O9 31.973-58.573-12.521 1.0060.66 C ATOM 2934 C VALA 409 33.329-62.117-11.964 1.00 60.21 C ATOM 2935 0 VALA 409 32.927 -62.803 -12.909 1.00 60.00 0 ATOM 2936 N ALA A 410 33.750 -62.638.10.817 1.00 59.67 N * * ATOM 2937 CA ALAA41O 33.824-64.077-10.612 1.0059.13 C : ATOM 2938 CB ALAA41O 35.019-64.425 -9.741 1.0059.26 C * ATOM 2939 C ALA A 410 32.543 -64.616 -9.998 1.00 58.71 C ATOM 2940 0 ALAA4IO 31.774-63.875 -9.392 1.0058.61 0 : .. ATOM 2941 N GLYA4I1 32.338-65.919-10.160 1.0058. 33 N ATOM 2942 CA GLYA 411 31.135-66.617.9.709 1.00 57.74 C **) ATOM 2943 C GLYA41I 30.218-65.930.8.713 1.00 57.25 C ATOM 2944 0 GLYA4L1 30.664-65. 273 -7.770 1.0057.29 0 ATOM 2945 N GLYA4I2 28.920-66.103 -8.937 1.0056.81 N ATOM 2946 CA GLY A 412 27.885 -65.639 -8.023 1.00 56.24 C ATOM 2947 C 0LYA412 26.593 -66.100.8.654 1.00 55.88 C ATOM 2948 0 GLYA412 26.023-67.115 -8.267 1.00 55.87 0 ATOM 2949 N ALA A 413 26.149 -65.349 -9.65 1 1.00 55.53 N ATOM 2950 CA ALAA4L3 25.119-65.806-10.564 1.00 55.19 C ATOM 2951 CB ALA A 413 23.952 -64.844 -10.570 1.00 55.14 C ATOM 2952 C ALA A 413 25.763 -65.865 -11.937 1.00 54.97 C ATOM 2953 0 ALAA 413 25.107-66.140-12.938 1.00 55.00 0 ATOM 2954 N PHE A 414 27.066 -65.613 -11.968 1.00 54.73 N ATOM 2955 CA PHE A 414 27.791 -65.468 -13.220 1.00 54.57 C ATOM 2956 CB PHEA414 28.869-64.387-13.090 1.0054.59 C ATOM 2957 CG PHEA4I4 28.326-63.027-12.744 1.0054.41 C ATOM 2958 CD1 PHEA 414 27.851 -62.184-13.735 1.0054.25 C ATOM 2959 CEI PHEA4I4 27.351 -60.941 -13.421 1.00 54.27 C ATOM 2960 CZ PHE A 414 27.322 -60.52 I -12.105 1.00 54.38 C ATOM 2961 CE2PHEA4I4 27792-61.350-11.109 1.0054.20 C ATOM 2962 CD2 PHE A 414 28.291 -62.594-11.429 1.00 54.24 C ATOM 2963 C PHEA4I4 28.421 -66.771 -13.689 1.00 54.51 C ATOM 2964 0 PHE A 414 28.536 -67.005 -14.892 1.00 54.59 0 ATOM 2965 N GLUA4I5 28.827-67.612-12.740 1.0054.32 N ATOM 2966 CA GLU A415 29.498 -68.872 -13.056 1.00 54.13 C ATOM 2967 CB GLUA4I5 29.668 -69.713-11.796 1.00 54.25 C ATOM 2968 CG GLUA415 28.358-70.145-11.184 1. 00 55.37 C ATOM 2969 CD GLU A 415 28.459 -70.379 -9.691 1.00 57.16 C ATOM 2970 OE1 GLU A 415 27.487 -70.912 -9.105 1.00 57.92 0 ATOM 2971 0E2 GLU A 415 29.507 -70.025 -9.104 1.00 57.82 0 ATOM 2972 C GLU A 415 28.758 -69.664 -14.133 1.00 53.71 C ATOM 2973 0 GLU A 415 27.527 -69.672 -14.179 1.00 53.58 0 ATOM 2974 N GLY A 416 29.523 -70.325 -14.997 1.00 53.38 N ATOM 2975 CA GLYA416 28.966-70.999-16.165 1.0052.98 C ATOM 2976 C GLY A 416 28.302 -72.320 -15.844 1.00 52.72 C ATOM 2977 0 GLYA 416 27.353 -72.729-16.516 1.00 52.60 0 ATOM 2978 N THR A 417 28.805 -72.985 -14.808 1.00 52.54 N ATOM 2979 CA THRA 417 28.274-74.275-14.382 1.00 52.37 C ATOM 2980 CB THR A 417 29.094 -74.865 -13.2 19 1.00 52.27 C ATOM 2981 OG1 T} LRA 417 29.438 -73.824 -12.299 1.00 51.98 0 ATOM 2982 CG2THRA417 30.369-75.497-13.736 1.0052.29 C ATOM 2983 C THRA 417 26.803-74.199-13. 977 1.00 52.41 C ATOM 2984 0 THR A 417 26.166 -75.226 -13.746 1.00 52.44 0 ATOM 2985 N ARGA418 26.269-72.982-13.899 1.00 52.48 N ATOM 2986 CA ARGA 418 24.876-72.768-13.518 1.00 52.60 C ATOM 2987 CR ARGA4I8 24.659-71.335-13.031 1.00 52.61 C ATOM 2988 CG ARGA4I8 25.100-71.097-11.597 1.0053.27 C ATOM 2989 CD ARG A 418 24.677 -69.722-11.083 1.00 54.81 C ATOM 2990 NE ARGA418 23.237-69.623-10.850 1.0055.96 N * * ATOM 2991 CZ ARGA418 22.371-69.084-11.706 1.0056.80 C ATOM 2992 NHIARGA418 21.077-69.038-11.405 1.0057.11 N ATOM 2993 NH2 ARG A 418 22.795 -68.589-12.864 1.00 56.93 N ATOM 2994 C ARGA4I8 23.916-73.077-14.657 1.0052.65 C ATOM 2995 0 ARGA4I8 22.722-73.271 -14. 439 1.00 52.59 0 ATOM 2996 N META4I9 24.443-73.129-15.873 1.00 52.86 N ATOM 2997 CA META4I9 23.613-73.399-17.037 1.0053.06 C * 45 ATOM 2998 CB META419 24.176-72.685-18.273 1.0053.29 C * ** ATOM 2999 CG MET A 419 23.147 -72.383 -19.370 1.00 54.17 C ATOM 3000 SD META4I9 21.616-71.599-18.788 1.0055.92 S * ATOM 3001 CE META4I9 20.494-72.997-18.721 10055.37 C ATOM 3002 C META 419 23.462-74.904-17.280 1.00 52.89 C ATOM 3003 0 META419 22.750-75.326-18.190 1.0052.78 0 ATOM 3004 N GLY A 420 24.124 -75.707 -16.452 1.00 52.86 N ATOM 3005 CA GLY A 420 24.028 -77.161 -16.549 1.00 52.96 C ATOM 3006 C GLY A 420 25.303 -77.821 -17.045 1.00 53.03 C ATOM 3007 0 GLY A 420 26.231 -77.138 -17.476 1.00 53.13 0 ATOM 3008 N PROA42I 25.364-79.161-16972 1.0053.04 N ATOM 3009 CA PRO A421 26.537 -79.878 -17.412 1.00 53.09 C ATOM 3010 CB PRO A 421 26.673 -80.952 -16.335 1.00 52.99 C ATOM 3011 CG PROA42I 25.217-81.301-15.998 1.0052.91 C ATOM 3012 CD PROA42I 24.357-80.087-16.418 1.0053.05 C ATOM 3013 C PROA42I 26.348-80.558-18.768 1.0053.26 C ATOM 3014 0 PROA42I 27.242-81.294-19.215 1.0053.35 0 ATOM 3015 N PHEA422 25.210-80.321 -19.424 1.00 53.47 N ATOM 3016 CA PHEA422 24.861 -81.125-20.599 1.0053.71 C ATOM 3017 CB PHEA422 23.439-81.673-20.491 1.0053.51 C ATOM 3018 CO PHEA422 23.360-82.947-19. 722 1.0053.01 C ATOM 3019 CD1 PHEA422 23.056-82.939-18.377 1.00 52.78 C ATOM 3020 CE1 PHEA 422 23.000-84.113-17.662 1.00 52.83 C ATOM 3021 CZ PHEA422 23.260-85.312-18.287 1.0052.98 C ATOM 3022 CE2 PHE A 422 23.577 -85.33 1 -19.627 1.00 52.93 C ATOM 3023 CD2 PHE A 422 23.63 1 -84.153 -20.336 1.00 52.79 C ATOM 3024 C PHEA422 25.106-80.504-21.970 1.0054.16 C ATOM 3025 0 PHE A 422 25.548 -8 1.193 -22.894 1.00 54.20 0 ATOM 3026 N VALA423 24.814-79.217-22.116 1.0054.72 N ATOM 3027 CA VALA 423 25.103 -78.540-23.376 1.00 55.30 C ATOM 3028 CB VALA423 23.829-77.988-24.055 1.0055.35 C ATOM 3029 CGI VALA423 24.187-77.283-25.358 1.0055.52 C ATOM 3030 CG2 VALA423 22.840-79.119 -24.324 1.00 55.43 C ATOM 3031 C VALA423 26.133-77.434-23.179 1.0055.57 C ATOM 3032 0 VALA423 25.864-76.444-22.496 1.0055.56 0 ATOM 3033 N GLUA424 27.308 -77.627 -23.783 1.00 56.06 N ATOM 3034 CA GLU A 424 28.436 -76.685 -23.709 1.00 56.34 C ATOM 3035 CB GLU A 424 28.105 -75.352 -24.420 1.00 56.44 C ATOM 3036 CG 0LUA424 29.293 -74.350-24.581 1.00 56.50 C ATOM 3037 CD GLU A 424 29.18 1 -73.133 -23. 625 1.00 57.30 C ATOM 3038 OE1 GLUA424 27.963-72.749-23.245 1.00 57.51 0 ATOM 3039 OE2 GLU A 424 30.250 -72.545 -23.247 1.00 57.40 0 ATOM 3040 C GLU A 424 28.929 -76.440 -22.273 1.00 56.48 C ATOM 3041 0 GLUA424 28.279-75.721 -21.495 1.0056.64 0 ATOM 3042 N GLU A 443 15.905 -85.52 1 -5 1.072 1.00 65.60 N ATOM 3043 CA GLUA443 14.889-84.482-51.179 1.0065.73 C ATOM 3044 CB GLUA443 14.210-84.527-52.553 1.0066.04 C ATOM 3045 CG GLUA443 13.123 -83.462 -52.765 1.00 67.13 C ATOM 3046 CD GLUA 443 13.687-82.071 -53.033 1.0068.58 C ATOM 3047 OE1 GLUA 443 14.867-81.816-52.699 1.00 69.01 0 ATOM 3048 0E2 GLU A 443 12.942 -8 1.229 -53.583 1.00 69.27 0 : ... ATOM 3049 C GLU A 443 13.847 -84.609 -50.074 1.00 65.36 C ATOM 3050 0 GLUA443 14.126-84.292-48.918 1.00 65.51 0 ATOM 3051 N TRPA444 12.652-85.071-50. 441 1.0064.83 N ATOM 3052 CA TRP A 444 11.546 -85.228 -49 500 1.00 6428 C ATOM 3053 CB TRPA444 10.269-84.611-50.076 1.0064.11 C ATOM 3054 CO TRP A 444 9.181 -84.393 -49.063 1.00 63.96 C ATOM 3055 CD1 TRP A 444 9.343 -84.086 -47.744 1.00 63.74 C * 45 ATOM 3056 NE1 TRPA444 8.118-83.952-47.135 1.0063.50 N * * ATOM 3057 CE2 TRP A 444 7.133 -84.164-48.062 1.00 63.49 C ATOM 3058 CD2 TRP A 444 7.764 -84.438 -49.292 1.00 63.81 C * ATOM 3059 CE3 TRP A 444 6.970-84.694 -50.414 1.00 63.77 C * ATOM 3060 CZ3 TRP A 444 5.591 -84.665 -50.271 1.00 63.70 C ATOM 3061 CH2TRPA444 4.995-84.386-49.037 1.0063.62 C ATOM 3062 CZ2 TRP A 444 5.747 -84.137 -47.923 1.00 63.59 C ATOM 3063 C TRP A 444 11.342 -86.707 -49.211 1.0064.04 C ATOM 3064 0 TRP A 444 11.421 -87.531 -50.116 1.00 64.09 0 ATOM 3065 N VAL A 445 11.074 -87.043 -47.953 1.00 63.74 N ATOM 3066 CA VAL A 445 11.078 -88.445 -47.534 1.00 63.47 C ATOM 3067 CB VALA 445 11.343 -88.591 -46.016 1.00 63.49 C ATOM 3068 CG1 VALA 445 12.100-89.891 -45.746 1.00 63.40 C ATOM 3069 CG2 VAL A 445 12.153 -87.4 10 -45.501 1.00 63.67 C ATOM 3070 C VALA445 9.814-89.236-47.888 1.0063.28 C ATOM 3071 0 VAL A 445 9.848 -90.466 -47.930 1.00 63.22 0 ATOM 3072 N VALA 446 8.703 -88.549-48.141 1.00 63.03 N ATOM 3073 CA VAL A 446 7.432 -89.251 -48.345 1.00 62.82 C ATOM 3074 CB VAL A 446 6.242 -88.540 -47.646 1.00 62.73 C ATOM 3075 CG1 VAL A 446 6.725 -87.739 -46.447 1 00 62.74 C ATOM 3076 CG2 VAL A 446 5.508 -87.644 -48.612 1.00 62.62 C ATOM 3077 C VALA446 7.100-89.527-49.817 1.0062.78 C ATOM 3078 0 VALA446 6.157-90.263 -50.119 1.00 62.73 0 ATOM 3079 N THR A 447 7.884 -88.954 -50.728 1.00 62.71 N ATOM 3080 CA THRA 447 7.650-89.148-52.161 1.00 62.74 C ATOM 3081 CB THRA447 8.638-88.339-53.025 1.0062.72 C ATOM 3082 OGI THR A447 9.861 -88.163 -52.305 1.00 63.01 0 ATOM 3083 CG2 THR A 447 8.062 -86.972 -53.357 1.00 62.66 C ATOM 3084 C THRA447 7.680-90.620-52.582 1.0062.71 C ATOM 3085 0 THRA447 7.073-90991-53.588 1.0062.63 0 ATOM 3086 N LYSA 448 8.379-91.453-51.813 1.00 62.74 N ATOM 3087 CA LYSA448 8.381 -92.895-52. 061 1.00 62.80 C ATOM 3088 CB LYSA448 9.370-93.628-51.148 1.0062.76 C ATOM 3089 CG LYS A 448 10.789 -93.108 -51.197 1.00 63.05 C ATOM 3090 CD LYS A 448 11.108 -92.289 -49.960 1.00 63.48 C ATOM 3091 CE LYSA448 12.245-91.319-50.222 1.0063.64 C ATOM 3092 NZ LYS A 448 11.832 -90.275 -5 1.202 1.00 63.53 N ATOM 3093 C LYSA448 6.986-93.490-51.874 1.0062.83 C ATOM 3094 0 LYS A 448 6.543 -94.3 14 -52.674 1.00 63.01 0 ATOM 3095 N ASP A 449 6.297 -93.070 -50.818 1.00 62.70 N ATOM 3096 CA ASP A449 4.993-93.632-50.493 1.00 62.64 C ATOM 3097 CB ASP A 449 4.882 -93.837 -48.981 1.00 62.80 C ATOM 3098 CG ASP A 449 5.95 1 -94.782 -48.439 1.00 63.19 C ATOM 3099 OD1 ASP A 449 6.122 -95.890 -49.006 1.00 63.74 0 ATOM 3100 OD2ASPA449 6.619-94.419-47.444 1.0063.29 0 ATOM 3101 C ASPA449 3.868-92.743-51.014 1.0062.46 C ATOM 3102 0 ASP A 449 2.684 -92.959 -50.7 17 1.00 62.44 0 ATOM 3103 N LYSA4SO 4.253-91.756-51.817 1.00 62.30 N ATOM 3104 CA LYS A 450 3.326-90.744 -52.305 1.00 62.13 C ATOM 3105 CB LYSA45O 4.051 -89.734-53.196 1.00 62.11 C ATOM 3106 CG LYS A 450 3.695 -88.274 -52.916 1.00 61.77 C ATOM 3107 CD LYSA45O 2.292-87.897-53.378 1.0060.83 C ATOM 3108 CE LYS A 450 1.970 -86.454 -53.009 1.00 59.97 C ATOM 3109 NZ LYS A 450 0.604 -86.047 -53.420 1.00 59.33 N ATOM 3110 C LYSA 450 2.140-91.352-53.050 1.00 62.15 C ATOM 3111 0 LYS A 450 1.013 -91.248 -52.589 1.00 62.07 0 ATOM 3112 N SERA 451 2.394-91.983-54.193 1.00 62.16 N * ATOM 3113 CA SERA451 1.320-92.559-55.008 1.0062.17 C *. 45 ATOM 3114 CB SERA4SI 1.913-93.360-56.164 1.00 62.12 C S...</p>..DTD: <p>ATOM 3115 OG SERA451 3.202-93.834-55.821 1.0062.06 0 ATOM 3116 C SERA 451 0.346-93.415-54.186 1.00 62.26 C ATOM 3117 0 SERA451 -0.870-93.404-54.419 1.0062.26 0 ATOM 3118 N LYSA4S2 0.895-94.144-53.221 1.0062.25 N ATOM 3119 CA LYS A 452 0.125 -94.923 -52.257 1.00 62.40 C ATOM 3120 CB LYSA452 1.131-95.657-51.364 1.00 62.38 C * .. ATOM 3121 CG LYSA452 0.596-96.422-50.166 1.0062.84 C ATOM 3122 CD LYS A 452 1.727 -97.330-49.630 1.00 63.07 C . : ATOM 3123 CE LYSA452 1.511-97.788-48.181 1.0064.07 C ATOM 3124 NZ LYSA452 2.122-96.868-47.174 1.0063.97 N ATOM 3125 C LYSA452 -0.812-94.016-51.434 1.0062.22 C ATOM 3126 0 LYS A 452 -2.075 -94.152 -51.457 1.00 62.21 0 ATOM 3127 N TYRA453 -0.196-93076-50.719 1.00 62.12 N ATOM 3128 CA TYR A 453 -0.965-92.110 -49.949 1.00 61.83 C ATOM 3129 CB TYR A 453 -0.041 -91.057 -49.352 1.00 61.96 C ATOM 3130 CG TYRA453 0.911-91.611-48.324 1.0062.18 C ATOM 3131 CD1 TYRA 453 0.622 -92.789 -47.652 1.00 62.45 C ATOM 3132 CE! TYRA 453 1.484-93.298-46.704 1.0062.52 C ATOM 3133 CZ TYRA 453 2.645-92.622-46.408 1.00 62.28 C ATOM 3134 OH TYRA453 3.496-93.133-45.464 1.00 62.68 0 ATOM 3135 CE2TYRA453 2.957-91.445-47.053 1.0062.18 C ATOM 3136 CD2 TYRA 453 2.089 -90.945 -48.005 1.00 62.43 C ATOM 3137 C TYR A 453 -2.047 -91.449 -50.80! 1 0061.73 C ATOM 3138 0 TYRA453 -3.196-91.346-50.379 1.0061.52 0 ATOM 3139 N ASPA 454 -1.667-91.011 -52.000 1.00 61.76 N ATOM 3140 CA ASP A454 -2.583 -90401 -52.962 1.00 61.68 C ATOM 3141 CB ASPA454 -1.859-90.082-54.269 1.0061.75 C ATOM 3142 CO ASPA454 -1.090-88.786-54.208 1.0062.05 C ATOM 3143 0D1 ASP A 454 -0.533 -88.378 -55.250 1.00 62.30 0 ATOM 3144 OD2ASPA454 -1.045-88.176-53.119 1.0063.12 0 ATOM 3145 C ASPA 454 -3.761 -91.304-53.267 1.00 61.60 C ATOM 3146 0 ASP A 454 -4.908 -90.860 -53.236 1.00 61.46 0 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 1.00 61.50 C ATOM 3149 CB GLUA455 -3.972-94.962-53.839 1.00 61.52 C ATOM 3150 CG GLUA455 -4.800-95.931 -54.675 1.0061.62 C ATOM 3151 CD GLU A 455 -3.526 -96.015 -55.853 0.00 50.00 C ATOM 3152 OE1 GLU A 455 -4.004 -96.674 -56.795 0.00 50.00 0 ATOM 3153 0E2 GLU A 455 -2.549 -95.268 -55.967 0.00 50.00 0 ATOM 3154 C GLUA4S5 -5.543-93.399-52.630 1.0061.47 C ATOM 3155 0 GLUA455 -6.770-93.244-52.874 1.0061.39 0 ATOM 3156 N 1LEA456 -5.034-93.395-51.379 1.00 61.57 N ATOM 3157 CA 1LEA456 -6.005-93.246-50.263 1.0061.40 C ATOM 3158 CB ILE A 456 -5.373 -93.420 -48.849 1.00 61.41 C ATOM 3159 CG1 ILE A 456 -5.08 1 -94.894 -48.547 1.00 61.57 C ATOM 3160 CD1ILEA456 -3.780-95.411-49.117 1.0061.87 C ATOM 3161 CG2 ILE A 456 -6.319 -92.913 -47.775 1.006097 C ATOM 3162 C ILE A 456 -6.732 -91.892 -50.326 1.00 61.33 C ATOM 3163 0 1LEA456 -7.973-91.817-50.396 1.00 61.32 0 ATOM 3164 N PilE A 457 -5.939 -90.826 -50.315 1.00 61.28 N ATOM 3165 CA PHEA 457 -6.451 -89.462 -50.304 1.00 61.18 C ATOM 3166 CB PHEA457 -5.325-88.478-50.619 1.0061.10 C ATOM 3167 Co PHE A 457 -5.788 -87.059 -50.805 1.00 61.06 C ATOM 3168 CDI PHE A 457 -6.014 -86.240 -49.710 1.00 6072 C ATOM 3169 CE1 PilE A 457 -6.425 -84. 930 -49.878 1.00 60.37 C : ... ATOM 3170 CZ PHEA 457 -6.609-84.424-51.146 1. 00 60.51 C ATOM 3171 CE2PHEA457 -6.384-85.228-52.248 1.0060.56 C ATOM 3172 CD2 PHE A 457 -5.976 -86.536 -52.077 1.00 60.85 C ATOM 3173 C PHE A 457 -7.583 -89.275 -51.295 1.00 61.08 C ATOM 3174 0 PHE A 457 -8.642 -88.746 -50.955 1.00 61.04 0 ATOM 3175 N TYRA 458 -7.352-89.710-52.526 1.00 61.12 N : ATOM 3176 CA 1'YR A 458 -8.345 -89.535 -53.570 1.00 60.96 C * . 50 ATOM 3177 CB TYRA458 -7.707 -89.605 -54.954 1.00 60.87 C ATOM 3178 Co TYR A 458 -6.880 -88.380 -55.257 1.00 60.78 C : *, ATOM 3179 CD! TYR A 458 -7.477 -87.135 -55.376 1.00 60.62 C ATOM 3180 CE1 TYRA458 -6.733-86.009-55.644 1.00 60.72 C *. ATOM 3181 CZ TYRA 458 -5.370-86.115-55.793 1.00 60.91 C * 55 ATOM 3182 OH TYRA 458 -4.624-84.987-56.061 1.00 61.14 0 ATOM 3183 CE2 TYR A 458 -4.750 -87.340 -55.676 1.00 60.97 C ATOM 3184 CD2 TYR A 458 -5.505 -88.463 -55.404 1.00 60.82 C ATOM 3185 C TYR A 458 -9.497 -90.509 -53.423 1.00 60.98 C ATOM 3186 0 TYRA458 -10.613-90.212-53.844 1.0060.99 0 ATOM 3187 N ASNA 459 -9.246-91.663-52.807 1.00 61.12 N ATOM 3188 CA ASNA459 -10.374-92.529-52.457 1.00 61.04 C ATOM 3189 CB ASNA459 -9.935-93.967-52.193 1.0061.02 C ATOM 3190 CO ASNA459 -10.182-94.868-53.382 1.0061.15 C ATOM 3191 ODI ASN A 459 -9.353 -95.713 -53.720 1.00 61.72 0 ATOM 3192 ND2ASNA459 -11.326-94.682 -54.035 1.00 61.27 N ATOM 3193 C ASN A 459 -11.225-91.986-51.310 1.00 61.02 C ATOM 3194 0 ASNA459 -12.307-92.503-51.037 1.0060.90 0 ATOM 3195 N LEU A 460 -10.738 -90.936 -50.649 1.00 61.16 N ATOM 3196 CA LEUA46O -11.536-90.256-49.614 1.00 61.21 C ATOM 3197 CB LEU A 460 -10.644 -89.735 -48.484 1 0061.18 C ATOM 3198 CG LEUA46O -10.441 -90.651 -47.276 1.00 61.31 C ATOM 3199 CD! LEU A 460 -10.126 -92.081 -47.695 1.00 61.70 C ATOM 3200 CD2 LEU A 460 -9.353 -90.103 -46.364 1.00 61.36 C ATOM 3201 C LEU A 460 -12.427 -89.118 -50.132 1.00 61.21 C ATOM 3202 0 LEU A 460 -13.042 -88.401 -49.341 1.00 61.15 0 ATOM 3203 N ALAA461 -12.490-88.958-51.452 1.0061.30 N ATOM 3204 CA ALA A 461 -13.332 -87.933 -52.092 1.00 61.39 C ATOM 3205 CB ALAA461 -14.810-88.328-52.035 1.0061.32 C ATOM 3206 C ALA A 461 -13.132 -86.526 -51.527 1.00 61.46 C ATOM 3207 0 ALA A 461 -13.989 -86.016 -50.803 1.00 61.46 0 ATOM 3208 N PRO A 462 -11.998-85.891 -5 1.868 1.00 61.52 N ATOM 3209 CA PRO A462 -11.692 -84.538 -5 1.427 1.00 61.50 C ATOM 3210 CB PRO A 462 -10.172 -84.439 -5 1.605 1.00 61.48 C ATOM 3211 CO PR0A462 -9.724-85.764-52.182 1.0061.39 C ATOM 3212 CD PRO A 462 -10.929 -86.437 -52.716 1.00 61.48 C ATOM 3213 C PROA462 -12.388-83.514-52.310 1.0061.55 C ATOM 3214 0 PRO A 462 -12.933 -83.873 -53.351 1.00 61.39 0 ATOM 3215 N ALAA463 -12.359-82.252-51.891 1.0061.78 N ATOM 3216 CA ALAA463 -13.067-81.176-52.582 1.00 61.99 C ATOM 3217 CB ALAA463 -12.888-79860-51.840 1.00 62.09 C ATOM 3218 C ALAA 463 -12.611 -81.031 -54.023 1.00 62.16 C ATOM 3219 0 ALA A 463 -13.233 -81.565 -54.938 1.00 62.42 0 ATOM 3220 N ASPA464 -11.528-80.293-54.226 1.0062.26 N ATOM 3221 CA ASP A 464 -10.959 -80.154 -55.556 1.00 62.40 C ATOM 3222 CB ASPA464 -11.255-78.767-56.133 1.0062.60 C ATOM 3223 CO ASP A 464 -10.538 -77.65 1 -55.385 1.00 63.34 C ATOM 3224 OD! ASP A 464 -10.634 -76.485 -55.835 1.00 63.76 0 ATOM 3225 0D2 ASP A 464 -9.880 -77.936 -54.354 1.00 64.06 0 ATOM 3226 C ASPA464 -9.464-80.382-55.468 1.0062.23 C ATOM 3227 0 ASP A 464 -8.707 -79.934 -56.3 17 1.00 62.39 0 ATOM 3228 N GLYA465 -9.049-81.083-54.424 1.0062.02 N * ATOM 3229 CA GLY A 465 -7.640 -8 1.324 -54.177 1.00 61.82 C * * 45 ATOM 3230 C GLY A 465 -7.398 -81.127 -52.700 1.00 61.70 C ATOM 3231 0 GLY A 465 -6.284 -81.310 -52.205 1.00 61.73 0 ATOM 3232 N LYS A 466 -8.460 -80.752 -5 1.996 1.00 61.43 N *S.* ATOM 3233 CA LYSA466 -8.379-80.507-50.572 1.0061.22 C ATOM 3234 CB LYS A 466 -8.571 -79.023 -50.279 1.00 61.21 C ATOM 3235 CG LYSA466 -7.437-78.154-50.775 1.0061.05 C ATOM 3236 CD LYSA466 -7.845-76.698-50.831 1.0061.32 C * ** ATOM 3237 CE LYS A 466 -6.793 -75.881 -51.549 1.00 61.80 C ATOM 3238 NZ LYS A 466 -6.444-76.494-52.864 1.00 62.20 N * ATOM 3239 C LYSA 466 -9.417-81.323-49.830 1.00 61.12 C ATOM 3240 0 LYSA 466 -10.613-81.218-50.091 1.00 61.13 0 ATOM 3241 N LEU A 467 -8.948 -82.144 -48.903 1.00 61.00 N ATOM 3242 CA LEU A 467 -9.841 -82.926 -48.074 1.00 60.88 C ATOM 3243 CB LEU A467 -9.118 -84.164 -47.542 1.00 60.79 C ATOM 3244 CG LEU A 467 -9.961 -85.111 -46.693 1.00 60.87 C ATOM 3245 CDI LEU A 467 -11.113 -85.658 -47.518 1.00 61.30 C ATOM 3246 CD2 LEU A 467 -9.114 -86.240 -46.140 1.00 60.91 C ATOM 3247 C LEU A 467 -10.339 -82.065 -46. 917 1.00 60.83 C ATOM 3248 0 LEU A 467 -9.544 -8 1.491 -46.171 1.00 60.86 0 ATOM 3249 N SERA468 -11.658-81.966-46.784 1.0060.71 N ATOM 3250 CA SERA468 -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 00 SERA46S -14.306-81.658-44.359 1.0061.03 0 ATOM 3253 C SERA468 -11.682-81.727-44.319 1.0060.34 C ATOM 3254 0 SERA46S -11.179-82.846-44.201 1.0060.29 0 ATOM 3255 N GLYA469 -11.746-80.852-43.318 1.0060.13 N ATOM 3256 CA GLYA469 -11.213-81.153-41.989 10059.92 C ATOM 3257 C GLYA469 -11.948-82.273-41. 272 1.0059.86 C ATOM 3258 0 GLYA 469 -11.335 -83.108-40.605 1.00 59.75 0 ATOM 3259 N SER A 470 -13.267 -82.298 -41.412 1.00 59.92 N ATOM 3260 CA SERA47O -14.080-83.316-40.755 1.0060.13 C ATOM 3261 CB SER A 470 -15.570 -82.996 -40.911 1.00 60.18 C ATOM 3262 00 SERA47O -15.909-82.804-42.273 1.0060.39 0 ATOM 3263 C SER A 470 -13.771 -84.730 -41.262 1.0060.16 C ATOM 3264 0 SER A 470 -13.628 -85.667 -40.468 1.00 60.19 0 ATOM 3265 N LYS A 471 -13.665 -84.875 -42.582 1.00 60.16 N ATOM 3266 CA LYS A 471 -13.353 -86.160 -43.203 1.00 60.23 C ATOM 3267 CB LYS A 471 -13.418 -86.032 -44.726 1.00 60.32 C ATOM 3268 CO LYS A 471 -14.2 15 -84.826 -45.209 1.00 60.75 C ATOM 3269 CD LYS A 471 -15.690 -85.140 -45.412 1.00 61.90 C ATOM 3270 CE LYS A 471 -16.083 -85.072 -46.889 1.00 62.37 C ATOM 3271 NZ LYSA471 -15.249-85.959-47.753 1.0062.88 N ATOM 3272 C LYS A 471 -11.952 -86.600 -42.777 1.00 60.16 C ATOM 3273 0 LYS A 471 -11.723 -87.758 -42. 368 1.00 60.14 0 ATOM 3274 N ALA A 472 -11.021 -85.654 -42.869 1.00 60.13 N ATOM 3275 CA ALA A 472 -9.655 -85.868 -42.425 1.00 60.03 C ATOM 3276 CB ALA A 472 -8.853 -84.582 -42.529 1.00 59.90 C ATOM 3277 C ALA A 472 -9. 670 -86.382 -40.993 1.00 59.97 C ATOM 3278 0 ALA A 472 -8.988 -87.358 -40.665 1.00 60.05 0 ATOM 3279 N LYS A 473 -10.466 -85.741 -40.144 1.00 59.85 N ATOM 3280 CA LYS A 473 -10.563 -86.203 -38.771 1.00 59.96 C ATOM 3281 CB LYS A 473 -11.393 -85.269 -37.895 1.00 59.91 C ATOM 3282 CG LYS A 473 -11.375 -85.683 -36.428 1.00 59.67 C ATOM 3283 CD LYSA473 -12.269-84.800-35.574 1.0059.75 C ATOM 3284 CE LYS A 473 -11.937 -84.943 -34.095 1.00 59.64 C ATOM 3285 NZ LYS A 473 -12.834 -84.122 -33.234 1.00 59.71 N ** ATOM 3286 C LYSA473 -11.111 -87.620-38.700 1.0060.14 C : ATOM 3287 0 LYS A 473 -10.441 -88.495 -38.164 1.00 60.26 0 ATOM 3288 N THRA 474 -12.306-87.866-39.243 1.00 60.16 N ATOM 3289 CA THR A 474 -12.872 -89.219 -39.144 1.00 60.24 C ATOM 3290 CB THR A 474 -14.257 -89.402 -39.852 1.00 60.23 C . ATOM 3291 001 TI-IR A 474 -14.300 -88.662 -41.075 1.0060.62 0 ATOM 3292 CG2THRA474 -15.394-88.933-38.952 1.0060.37 C ATOM 3293 C THRA474 -11.864-90.289-39.582 1.0060.23 C * ATOM 3294 0 THRA474 -11.719-91.319-38.917 1.0060.25 0 * ,* ATOM 3295 N TRP A 475 -11.145 -90.037 -40.672 1.00 60.28 N * ATOM 3296 CA TRP A 475 -10.106 -90.978 -41.096 1.00 60.42 C ** * ATOM 3297 CB TRP A 475 -9.523 -90.535 -42.438 1.00 60.84 C ATOM 3298 CG TRPA475 -8.313-91.301-42.870 1.0061.18 C ATOM 3299 CDI TRPA475 -8.275 -92.585 -43.318 1.00 61.70 C ATOM 3300 NEI TRP A475 -6.985 -92.942 -43.627 1.00 61.88 N ATOM 3301 CE2TRPA475 -6.160-91.878-43.383 1.0061.50 C ATOM 3302 CD2 TRP A 475 -6.963 -90.823 -42.907 1.00 61.57 C ATOM 3303 CE3 TRP A 475 -6.354 -89.606 -42.577 1.00 62.24 C ATOM 3304 CZ3 TRP A 475 -4.977 -89.484 -42.734 1.00 62.05 C ATOM 3305 CH2 TRP A 475 -4.207 -90.555 -43.212 1.00 61.82 C ATOM 3306 CZ2TRPA475 -4.780-91.756-43.540 1.00 61.71 C ATOM 3307 C TRP A 475 -8.998 -91.098 -40.043 1.00 60.37 C ATOM 3308 0 TRP A 475 -8.652 -92.206 -39.568 1 00 60.28 0 ATOM 3309 N MET A 476 -8.444 -89.948 -39.674 1.00 60.24 N ATOM 3310 CA META476 -7.358-89.927-38.717 1.0060.43 C ATOM 3311 CB META476 -6.936-88.492-38.400 1.0060.35 C ATOM 3312 CG MET A 476 -6.136 -87.837 -39.5 19 1.00 60.65 C ATOM 3313 SD META 476 -5.609 -86.145 -39.154 1.00 60.97 S ATOM 3314 CE MET A476 -4.147 -86.452 -38.158 1.00 61.19 C ATOM 3315 C META476 -7.739-90.692-37.452 1.0060.37 C ATOM 3316 0 MET A 476 -7.049 -91.632 -37.055 1.00 60.37 0 ATOM 3317 N VALA 477 -8.847 -90.304-36.830 1.00 60.31 N ATOM 3318 CA VAL A 477 -9.308 -90.980 -35.630 1.00 60.18 C ATOM 3319 CB VAL A 477 -10.572 -90.317 -35.039 1.00 60.16 C ATOM 3320 CG1 VALA 477 -11.834-91.039-35.497 1.00 60.18 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 1.00 60.04 C ATOM 3323 0 VAL A 477 -9.463 -93.322 -35.124 1.00 59.92 0 ATOM 3324 N GLYA478 -9.836-92.689-37.255 1.0060.05 N ATOM 3325 CA GLY A 478 -9.937 -94.048 -37.773 1.00 59.87 C ATOM 3326 C GLYA478 -8.652-94.826-37.573 1.0059.75 C ATOM 3327 0 GLY A 478 -8.683 -96.039 -37.375 1.00 59.64 0 ATOM 3328 N TFIRA479 -7.512-94.139-37.618 1.0059.79 N ATOM 3329 CA THR A 479 -6.230 -94.827 -37.337 1.00 59.54 C F ATOM 3330 CB THRA479 -5.012-93.965-37.682 1.0059.50 C ATOM 3331 OG1 THRA479 -4.708-93.109-36.572 1.0059.40 0 ATOM 3332 CG2 THR A 479 -5.274 -93.142 -38.930 1.00 59.72 C ATOM 3333 C THRA479 -6.044-95.280-35.881 1.0059.41 C ATOM 3334 0 THR A 479 -4.929 -95.606 -35.467 1.00 59.36 0 ATOM 3335 N LYS A 480.7.126 -95.279 -35.111 01.00 59.24 N ATOM 3336 CA LYS A 480 -7.102 -95.706 -33.708 1.00 59.00 C ATOM 3337 CB LYSA48O -7.107-97.236-33.602 1.0058.90 C ATOM 3338 CG LYS A 480 -8.720 -97.582.33.472 0.00 50.00 C ATOM 3339 CD LYS A 480 -8.884 -99.002 -33.964 0.00 50.00 C ATOM 3340 CE LYS A 480 -7.623 -99.825 -33.83 1 0.00 50.00 C ATOM 3341 NZ LYS A 480 -7.163-100.001 -32.43 1 0.00 50.00 N ATOM 3342 C LYSA48O -5.952-95.120-32.883 1.0058.86 C ATOM 3343 0 LYS A 480.5.432 -95.778 -3 1.985 1.00 59.02 0 ATOM 3344 N LEUA 481 -5.562-93.884-33.184 1.00 58.63 N ATOM 3345 CA LEUA4SI -4.589-93.169-32.361 1.0058.40 C ATOM 3346 CB LEUA481 -3.644-92.336-33.233 1.0058.41 C ATOM 3347 CG LEUA48I -2.448-93.045-33. 870 1.0058.17 C ATOM 3348 CD1LEUA48I -1.516-92.033-34.503 1.0057.72 C ATOM 3349 CD2 LEU A 481 -1.700 -93.871 -32.840 1.00 57.96 C ATOM 3350 C LEUA48I -5.303-92.264-31.359 1.0058.27 C * 50 ATOM 3351 0 LEUA48I -6.429-91.835-31.607 1.0058.35 0 ATOM 3352 N PRO A 482 -4.656 -9 1.980 -30.2 16 1.00 58.15 N : *. ATOM 3353 CA PROA482 -5.239-91.080-29.221 1.0058.10 C ATOM 3354 CB PR0A482 -4.232-91.119-28.068 1.0058.03 C S. * ** * . ATOM 3355 CG PR0A482 -2.965-91.591-28.671 1.00 58.03 C ATOM 3356 CD PROA482 -3.349-92.507-29.787 1.0058.12 C ATOM 3357 C PR0A482 -5.389-89.658-29.749 1.0058.13 C ATOM 3358 0 PRO A 482 -4.523 -89.170 -30.476 1.00 58.05 0 ATOM 3359 N ASNA483 -6.490-89.010-29.375 1.0058.25 N ATOM 3360 CA ASNA483 -6.826-87.673-29.865 1.00 58.27 C ATOM 3361 CR ASNA483 -7.966-87.069-29.037 1.0058.41 C ATOM 3362 CG ASN A 483 -8.680 -85.936 -29.761 1.00 58.98 C ATOM 3363 OD1 ASN A 483 -8.648 -84 782 -29.323 1.00 58.96 0 ATOM 3364 ND2 ASN A 483 -9.328 -86.264 -30.878 1.00 59.69 N ATOM 3365 C ASN A 483 -5.630 -86.730 -29.872 1.00 57.99 C ATOM 3366 0 ASNA483 -5.249-86.219-30.912 1.00 57.84 0 ATOM 3367 N SER A 484 -5.048 -86.515 -28.698 1.00 57.91 N ATOM 3368 CA SERA 484 -3.895-85.634-28.518 1.00 57.86 C ATOM 3369 CB SERA 484 -3.279-85.891 -27.137 1.00 57.83 C ATOM 3370 OG SERA484 -1.867-85.789-27.157 1.00 58.63 0 ATOM 3371 C SERA 484 -2.851 -85.771 -29.634 1.00 57.69 C ATOM 3372 0 SER A 484 -2.538 -84.801 -30.341 1.00 57.89 0 ATOM 3373 N VAL A 485 -2.323 -86.978 -29.798 1.00 57.50 N ATOM 3374 CA VALA485 -1.368-87.246-30.858 1.0057.27 C ATOM 3375 CB VALA485 -1.034-88.746-30.950 1.0057.16 C ATOM 3376 CGI VAL A 485 -0.287 -89.050 -32.233 1.00 56.97 C ATOM 3377 CG2 VAL A 485 -0.2 13 -89.173 -29.750 1.00 56.96 C ATOM 3378 C VALA485 -1.925-86.756-32.186 1.00 57.35 C ATOM 3379 0 VALA 485 -1.303 -85.944-32.866 1.00 57.43 0 ATOM 3380 N LEU A 486 -3.113 -87.233 -32.542 1.00 57.54 N ATOM 3381 CA LEU A 486 -3.739 -86.843 -33.803 1.00 57.77 C ATOM 3382 CR LEUA4S6 -5.138-87.454-33.937 1.0057.88 C ATOM 3383 Co LEUA486 -5.229-88.972-34.109 1.0058.42 C ATOM 3384 CDI LEU A 486 -6.672 -89.447 -33.979 1.00 58.66 C ATOM 3385 CD2 LEU A 486 -4.638 -89.407 -35.444 1.00 58.90 C ATOM 3386 C LEU A 486.3.803 -85.325 -33.975 1.00 57.80 C ATOM 3387 0 LEUA486 -3.455-84.808-35.033 1.0057.86 0 ATOM 3388 N GLYA487 -4.249-84.618-32.938 1.0057.71 N ATOM 3389 CA GLY A 487 -4.357 -83.163 -32.979 1.00 57.64 C ATOM 3390 C GLYA487 -3.016-82.531 -33.282 1.0057.70 C ATOM 3391 0 GLY A 487 -2.906 -8 1.638 -34.142 1.00 57.71 0 ATOM 3392 N ARG A 488 -1.988 -83.010 -32.585 1.00 57.78 N ATOM 3393 CA ARGA488 -0.628-82.544-32.841 1.0057.97 C ATOM 3394 CB ARG A 488 0.348 -83.209 -31.870 1.00 58.06 C ATOM 3395 CO ARG A 488 1.529 -82.338 -3 1.468 1.00 59.39 C ATOM 3396 CD ARG A 488 1.890 -82.573 -30.002 1.00 61.62 C ATOM 3397 NE ARG A 488 2.408 -83.923 -29.761 1.00 63.12 N ATOM 3398 CZ ARG A 488 2.05 1 -84.695 -28.733 1.00 63.38 C ATOM 3399 NH1 ARG A 488 2.580 -85.907 -28.598 1.00 63.40 N ATOM 3400 N}12ARGA488 1.153-84.266-27.850 1.0063.17 N ATOM 3401 C ARG A 488 -0227 -82.814 -34.300 1.00 57.81 C ATOM 3402 0 ARG A 488 0.355 -81.947 -34.979 1.00 57.77 0 ATOM 3403 N 1LEA489 -0.564-84.008-34.784 1.00 57.58 N ATOM 3404 CA 1LEA489 -0.257-84.377-36.159 1.0057.48 C ATOM 3405 CB 1LEA489 -0.663 -85.815 -36.470 1.00 57.33 C ATOM 3406 CG1 ILE A 489 0.244 -86.784 -35.7 16 1.00 57.24 C ATOM 3407 CDI JLEA4S9 -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 1LEA489 -0.953-83.441-37.128 1.0057.56 C * ATOM 3410 0 1LEA489 -0.344-82.935-38.070 1.00 57.63 0 ATOM 3411 N TRPA49O -2.236-83.206-36. 895 1.0057.67 N : ***. ATOM 3412 CA TRPA49O -2.970-82.265-37.711 1.0057.64 C ATOM 3413 CB TR.PA490 -4.367-82.008-37.152 1.0057.40 C 55 ATOM 3414 CO TRPA49O -4.998-80.874-37.862 1.00 57.22 C ATOM 3415 CDI TRP A 490 -4.966 -79.563 -37.500 1.00 56.97 C ATOM 3416 NE! TRP A 490 -5.628 -78.800 -38.430 1.00 57.04 N ATOM 3417 CE2 TRP A 490 -6.092 -79.619.39.425 1.00 57.10 C ATOM 3418 CD2 TRP A 490 -5.704 -80.933 -39.103 1.00 57.28 C ATOM 3419 CE3 TRP A 490 -6.056 -81.974 -39.970 1.00 57.40 C ATOM 3420 CZ3TRPA49O -6.780-81.672-41.109 1.0057.15 C ATOM 3421 CH2TRPA49O -7.154-80.354-41.400 1.0057.10 C ATOM 3422 CZ2 TRP A 490 -6.820-79.316 -40.573 1.00 57.08 C ATOM 3423 C TRP A 490 -2.208 -80.950 -37.754 1.00 57.62 C ATOM 3424 0 TRP A 490 -1.865 -80.442 -38.833 1.0057.65 0 ATOM 3425 N LYS A 491 -1.942 -80.409 -36.568 1.00 57.68 N ATOM 3426 CA LYS A 491 -1.302 -79.103 -36.485 1.00 57.74 C ATOM 3427 CB LYS A 491 -1.059 -78.684 -35.036 1.00 57.75 C ATOM 3428 CG LYS A 491 -0.483 -77.286 -34.909 1.00 58.40 C ATOM 3429 CD LYSA49I -0.964-76.592-33.647 1.0060.09 C ATOM 3430 CE LYSA49I -2.402-76.107-33.804 1.0061.13 C ATOM 3431 NZ LYSA491 -2.486-75.022-34.833 1.0062.38 N ATOM 3432 C LYSA491 -0.009-79.077-37.281 1.0057.58 C ATOM 3433 0 LYS A 491 0.285 -78.090 -37.958 1.00 57.50 0 ATOM 3434 N LEU A 492 0.754 -80.166 -37.203 1.00 57.51 N ATOM 3435 CA LEUA492 1.982-80.287-37.988 1.0057.34 C ATOM 3436 CB LEUA492 2.773-81.513-37.538 1.0057.12 C ATOM 3437 CG LEUA492 4.058-81.329-36.735 1.0056.50 C ATOM 3438 CD1 LEU A 492 4.013 -80.090 -35.863 1.00 56.61 C ATOM 3439 CD2 LEU A 492 4.3 17 -82.581 -35.908 1.00 56.14 C ATOM 3440 C LEU A 492 1.722 -80.363 -39.500 1.00 57.59 C ATOM 3441 0 LEUA 492 2.471 -79.801 -40.301 1.00 57. 53 0 ATOM 3442 N SERA 493 0.653-81.051-39.885 1.00 57.77 N ATOM 3443 CA SERA 493 0.421 -81.357-41.288 1.00 58.08 C ATOM 3444 CB SERA493 -0.393-82.641-41.427 1.0058.12 C ATOM 3445 OG SER A 493 0.344 -83.746 -40.936 1.00 58.62 0 ATOM 3446 C SERA 493 -0.238-80.231 -42.071 1.00 58. 20 C ATOM 3447 0 SERA493 0.068-80.036-43.249 1.0058.25 0 ATOM 3448 N ASP A 494 -1.150 -79.499 -41.440 1.00 58.27 N ATOM 3449 CA ASP A 494 -1.797 -78.397 -42.148 1.00 58.62 C ATOM 3450 CB ASPA494 -3.062-77.935-41.434 1.0058.56 C ATOM 3451 CG ASP A 494 -3.824 -76 894 -42.226 1.00 58 70 C ATOM 3452 OD1 ASP A 494 -3.470 -76.661 -43.405 1.00 58.46 0 ATOM 3453 0D2 ASP A 494 -4.777 -76.308 -41.668 1.00 59.37 0 ATOM 3454 C ASP A 494 -0.82 1 -77.238 -42.302 1.00 58.87 C ATOM 3455 0 ASP A 494 -0.883 -76.250 -4 1.568 1.00 58.88 0 ATOM 3456 N VALA495 0.078-77.368-43.269 1.0059.15 N ATOM 3457 CA VAL A495 1.182 -76.438 -43.406 1.00 59.38 C ATOM 3458 CB VALA 495 2.219-76.921-44.439 1.00 59.37 C ATOM 3459 CG1 VALA 495 3.314-75.883-44.618 1.00 59.25 C :. ATOM 3460 CG2VALA495 2.819-78.234-43.989 1.0059.21 C * ATOM 3461 C VALA 495 0.721 -75.025 -43.728 1.00 59.65 C ATOM 3462 0 VALA495 1.173 -74.077 -43.089 1.00 60.04 0 ATOM 3463 N ASP A 496 -0.171 -74.869-44.703 1.00 59.85 N ATOM 3464 CA ASP A 496 -0.668 -73.525 -45.031 1.00 60.04 C ATOM 3465 CB ASP A 496 -1.133 -73.422 -46.488 1.00 60.09 C ATOM 3466 CG ASP A496 -2.176-74.455-46.847 1.00 60.31 C ATOM 3467 ODI ASP A496 -2.344-75.432-46.082 1.00 60.71 0 ATOM 3468 0D2 ASP A 496 -2.825 -74.289 -47.904 1.00 60.45 0 : ** ATOM 3469 C ASPA496 -1.771 -73.111 -44.066 1.0060.06 C ATOM 3470 0 ASPA496 -2.373 -72.046-44.210 1.0059.85 0 : ATOM 3471 N ARGA497 -1.999-73.980-43.081 1.0060.35 N * ** 55 ATOM 3472 CA ARG A 497 -2.962 -73.785 -41.992 1.00 60.65 C ATOM 3473 CB ARG A 497 -2.285 -73.166 -40.754 1.00 60.76 C ATOM 3474 CG ARG A 497 -2.301 -7 1.656 -40.649 1.00 62.10 C ATOM 3475 CD ARG A 497 -1.067 -71.162 -39.908 1.00 64.37 C ATOM 3476 NE ARG A 497 0.050 -70.975 -40.832 1.00 66.05 N ATOM 3477 CZ ARG A 497 0.345 -69.817 -41.420 1.00 67.08 C ATOM 3478 NH! ARG A 497 1.375 -69.738 -42.255 1.00 67.52 N ATOM 3479 NH2ARGA497 -0.385-68.733-41.170 1.0067.06 N ATOM 3480 C ARG A 497 -4.271 -73.097 -42.402 1.00 60.58 C ATOM 3481 0 ARGA497 -4.638-72.03641.889 1.0060.38 0 ATOM 3482 N ASPA498 -4.976-73.740-43.331 1.0060.75 N ATOM 3483 CA ASP A498 -6.248-73.227-43.821 1.00 60.92 C ATOM 3484 CB ASP A 498 -6.279 -73.207 -45.358 1.00 60.94 C ATOM 3485 CG ASPA498 -6.136-74.597-45.961 1.0060.96 C ATOM 3486 OD1 ASP A 498 -5 577 -75.493 -45.290 1.00 61.07 0 ATOM 3487 OD2ASPA498 -6.578-74.792-47.115 1.0060.82 0 ATOM 3488 C ASPA498 -7.435-74.025-43.273 1.0061.06 C ATOM 3489 0 ASPA498 -8.584-73.496-43.189 1.0061.39 0 ATOM 3490 N GLY A 499 -7.172 -75.293 -42.902 1.00 61.04 N ATOM 3491 CA GLYA499 -8.246-76.100-42.330 1.0061.21 C ATOM 3492 C GLY A 499 -8.543 -77.366 -43.108 1.00 61.37 C ATOM 3493 0 GLY A 499 -9.301 -78.229 -42.648 1.00 61.52 0 ATOM 3494 N MET A 500 -7.948 -77.476 44.29 1 1.00 61.28 N ATOM 3495 CA MET A 500 -8.092 -78.669 -45.105 1.00 61.23 C ATOM 3496 CB MET A 500 -8.669 -78.304 -46.467 1.00 61.21 C ATOM 3497 CG MET A 500 -10.072 -77.741 -46.410 1.00 61.10 C ATOM 3498 SD MET A 500 -10.597 -77.079 -48.004 1.00 61.13 S ATOM 3499 CE MET A 500 -12.36! -76.890 -47.731 1.00 61.68 C ATOM 3500 C META 500 -6.737-79.338-45.277 1.00 61.33 C ATOM 3501 0 META 500 -5.721 -78.816-44.820 1.00 61.29 0 ATOM 3502 N LEU A 501 -6.727 -80.500 -45.927 1.00 61.45 N ATOM 3503 CA LEU A 501 -5.477 -81.158 -46.298 1.00 61.49 C ATOM 3504 CB LEU A 501 -5.259 -82.432 -45. 475 1.00 61.41 C ATOM 3505 CO LEU A 501 -5.099 -82.291 -43.959 1.00 61.24 C ATOM 3506 CD! LEUA 501 -5.182-83.646-43.272 1.00 60.96 C ATOM 3507 CD2LEUA5OI -3.792-81.603-43.617 1.0061.45 C ATOM 3508 C LEUA5O1 -5.480-81.494-47.788 1.0061.59 C ATOM 3509 0 LEU A 501 -6.352 -82.22048.264 1.00 61.52 0 ATOM 3510 N ASP A 502 -4.515 -80.952 -48.525 1 0061.72 N ATOM 3511 CA ASPASO2 -4.353-81.329-49.919 1.00 61.94 C ATOM 3512 CB ASP A 502 -3.736 -80.192 -50.739 1.00 62.06 C ATOM 3513 CG ASP A 502 -2.315 -79.857 -50.315 1.00 62.72 C ATOM 3514 OD1 ASP A 502 -1 539 -80. 784 -49.993 1.00 63.46 0 ATOM 3515 OD2ASPASO2 -1.966-78.655-50.326 1.0063.58 0 ATOM 3516 C ASP A 502 -3.505 -82,590 -49.98! 1.00 61.99 C ATOM 3517 0 ASP A 502 -3.095 -83.111 -48.946 1.00 62.07 0 :. ATOM 3518 N ASPA5O3 -3.242-83.079-51.188 1.0062.08 N ATOM 3519 CA ASPA5O3 -2.516-84.337-51. 362 1.0062.21 C ATOM 3520 CB ASP A503 -2.278-84.611 -52.844 1.00 62.34 C ATOM 3521 CG ASP A 503 -1.5 14 -83.495 -53.525 1.00 62.98 C ATOM 3522 OD1 ASPA 503 -1.726-82.315-53.165 1.00 63.16 0 ATOM 3523 0D2 ASP A 503 -0.703 -83.803 -54.425 1.00 64.06 0 ATOM 3524 C ASP A 503 -1.193 -84.407 -50.593 1.00 62.12 C ATOM 3525 0 ASPA 503 -0.955-85.360-49.843 1.00 62.04 0 ATOM 3526 N GLU A 504 -0.337 -83.405 -50.779 1.00 62.02 N : **. ATOM 3527 CA GLU A 504 0.969 -83.400 -50.126 1.00 62.12 C ATOM 3528 CB GLU A 504 1.813 -82.201 -50.574 1.00 62.02 C . : ATOM 3529 CO GLU A 504 1.840 -81.992 -52.089 1.00 62.68 C * 55 ATOM 3530 CD GLUA5O4 3.004-81.120-52.556 1.0062.81 C ATOM 3531 OE1 GLU A 504 2.797 -79.905 -52.79 1 1.00 63.40 0 ATOM 3532 OE2 GLU A 504 4.130 -8 1.652 -52.694 1.00 63.95 0 ATOM 3533 C GLU A 504 0.793 -83.4 10 -48.614 1.00 61.85 C ATOM 3534 0 GLUASO4 1.286-84.308-47.927 1.0061.84 0 ATOM 3535 N GLUASO5 0.069-82.420-48.102 1.0061.64 N ATOM 3536 CA GLU A 505 -0.204 -82.340 -46.677 1.00 61.43 C ATOM 3537 CB GLUA5O5 -1.201-81.228-46.390 1.0061.18 C ATOM 3538 CO GLU A 505 -0.588 -79.85 1 -46.381 1.00 60.83 C ATOM 3539 CD GLU A 505 -1.631 -78.753 -46.286 1.00 60.55 C ATOM 3540 OE1 GLU A 505 -2.627 -78 807 -47.043 1.00 60.25 0 ATOM 3541 0E2 GLU A 505 -1.457 -77.832 -45.456 1.00 60.26 0 ATOM 3542 C GLU A 505 -0.735 -83.667 -46.149 1.00 61.67 C ATOM 3543 0 GLU A 505 -0.357 -84.106 -45.056 1.00 61.83 0 ATOM 3544 N PHEA5O6 -1.604-84.309-46.927 1.0061.68 N ATOM 3545 CA PHEA5O6 -2.180-85.586-46. 521 1.0061.63 C ATOM 3546 CB PHEASO6 -3.294-86.020-47.474 1.00 61.56 C ATOM 3547 CO PHE A 506 -3.985 -87.290 -47.056 1.00 61.67 C ATOM 3548 CD! PHEA 506 -3.470-88.528-47.414 1.00 61.62 C ATOM 3549 CE1 PHE A 506 -4.098 -89.695 -47.024 1.00 61.32 C ATOM 3550 CZ PHE A 506 -5.257 -89.633 -46. 273 1.00 61.44 C ATOM 3551 CE2PHEA5O6 -5.781 -88.409-45.912 1.00 61.14 C ATOM 3552 CD2PHEA5O6 -5.147-87.247-46.299 1.0061.51 C ATOM 3553 C PHEASO6 -1.102-86.658-46.443 1.0061.66 C ATOM 3554 0 PHEA5O6 -1.048-87.430-45.482 1.0061.70 0 ATOM 3555 N ALA A 507 -0.245 -86.705 -47.458 1.00 61.76 N ATOM 3556 CA ALA A 507 0.876 -87.636 -47.447 1.00 61.66 C ATOM 3557 CB ALAA5O7 1.706-87.488-48.706 1.0061.65 C ATOM 3558 C ALA A 507 1.732 -87.405 -46.204 1.00 61.68 C ATOM 3559 0 ALA A 507 2.156 -88.36! -45.551 1.00 61.70 0 ATOM 3560 N LEUA 508 1.969-86.133-45.878 1.00 61.60 N ATOM 3561 CA LEUA5O8 2.695-85.767-44.661 1.0061.54 C ATOM 3562 CB LEU A 508 2.778 -84.247 -44.530 1.00 61.44 C ATOM 3563 CG LEUA5O8 4.018-83.623 -43.886 1.0061.08 C ATOM 3564 CD! LEUA 508 3.712-82.195-43.481 1.00 60.85 C ATOM 3565 CD2 LEU A 508 4.505 -84.417 -42.691 1.00 60.65 C ATOM 3566 C LEU A 508 1.991 -86.346-43.433 1.00 61.70 C ATOM 3567 0 LEU A 508 2.595 -87.063 -42.621 1.00 61.61 0 ATOM 3568 N ALAA5O9 0.708-86.026-43.30! 1.0061.77 N ATOM 3569 CA ALA A 509 -0.093 -86.572 -42.221 1.00 61.78 C ATOM 3570 CB ALA A 509 -1.560 -86.243 -42.434 1.00 61.77 C ATOM 3571 C ALAA 509 0.122-88.082-42.115 1.00 61.87 C ATOM 3572 0 ALA A 509 0.550 -88.585 -41.073 1.00 61.97 0 ATOM 3573 N SERA 510 -0.154 -88.798 -43.202 1.00 61.83 N ATOM 3574 CA SER A 510 0.004 -90.251 -43.226 1.00 61.95 C ATOM 3575 CB SER A 510 -0.249 -90.793 -44.634 1.00 62.00 C ATOM 3576 OG SER A 510 -1.493 -90.333 -45.135 1.00 62.65 0 * ATOM 3577 C SERA 510 1.390 -90.673 -42.748 1.00 61.79 C . 45 ATOM 3578 0 SERA51O 1.522-91.562-41.896 1.0061.78 0 ATOM 3579 N HISA5II 2.416-90.030-43.304 1.0061.62 N ATOM 3580 CA HISA 511 3.793-90.302-42.913 1.00 61.40 C ATOM 3581 CB HISA51I 4.758-89.312-43.576 1.0061.24 C ATOM 3582 CG HIS AS!! 6.183 -89.470 -43.139 1.00 60.84 C ATOM 3583 ND1HISA5!1 7.110-90.185-43.867 1.0060.78 N ATOM 3584 CEI HIS A 511 8.275 -90.155 -43.244 1.00 60.24 C * *. ATOM 3585 NE2HISA5I1 8.137-89.449-42.136 1.0060.07 N ATOM 3586 CD2HISA5I1 6.838-89.009-42.047 1.0060.36 C ** * ATOM 3587 C HISA 511 3.906-90.212-41.404 1.00 61.38 C ATOM 3588 0 HISA51I 4.408-91.124-40.751 1.0061.56 0 ATOM 3589 N LEUA 512 3.417-89.109-40.852 1.00 61.36 N ATOM 3590 CA LEU A 512 3.499 -88.88! -39.419 1.00 61.37 C ATOM 359! CB LEU A 512 3.011 -87.469 -39.097 1.00 61.22 C ATOM 3592 CG LEU A 512 4 034 -86.435 -39.573 1.00 60.86 C ATOM 3593 CDI LEUA 512 3.482 -85.018-39.516 1.0060.51 C ATOM 3594 CD2 LEU A 512 5.3 15 -86.565 -38.760 1.00 59.84 C ATOM 3595 C LEUA512 2.749-89.938-38.605 1.0061.48 C ATOM 3596 0 LEUA512 3.236-90.422-37.574 1.0061.48 0 ATOM 3597 N ILE A 513 1.571 -90.309 -39.090 1.00 61.74 N ATOM 3598 CA ILE A 513 0.791 -91.371 -38.468 1.00 61.83 C ATOM 3599 CB ILEA513 -0.579-91.518-39.155 1.0061.81 C ATOM 3600 CG1 ILE A 513 -1.325 -90.181 -39.084 1.00 61.73 C ATOM 3601 CD1 ILEA 513 -2.782-90.257-39.456 1.00 62.12 C ATOM 3602 CG2 ILE A 513 -1.382 -92.645 -38.518 1.00 61.68 C ATOM 3603 C ILEA5I3 1.554-92.705-38.444 1.0061.89 C ATOM 3604 0 ILE A 513 1.683 -93.333 -37.391 1.00 61.85 0 ATOM 3605 N GLUA514 2.071-93.124-39.598 1.0061.92 N ATOM 3606 CA GLU A 514 2.911 -94. 3 17 -39.660 1.00 62.03 C ATOM 3607 CB GLUAS14 3.456-94.519-41.069 1.00 62.08 C ATOM 3608 CG GLUA5I4 2.396-94.778-42.118 1.0062.83 C ATOM 3609 CD GLUA 514 2.944-95.511 -43.333 1.00 63.54 C ATOM 3610 OE1GLUA5I4 3.998-96.181-43.216 1.0063.39 0 ATOM 3611 OE2GLUA 514 2.310-95.420-44.407 1.0064.11 0 ATOM 3612 C GLUA 514 4.077 -94.201 -38.689 1.00 62.07 C ATOM 3613 0 GLUA 514 4.345-95.108-37.894 1.0062.33 0 ATOM 3614 N ALA A 515 4.775 -93.072 -38.767 1.00 61.99 N ATOM 3615 CA ALA A 515 5.88 1 -92.794 -37.865 1.00 61.95 C ATOM 3616 CB ALAA515 6.338-91.346-38.007 1.00 61.86 C ATOM 3617 C ALAA 515 5.477 -93.091 -36.426 1.00 61.91 C ATOM 3618 0 ALAA515 6.134-93.878-35.746 1.0061.89 0 ATOM 3619 N LYSA516 4.389-92.472-35.972 1.0061.87 N ATOM 3620 CA LYS A 516 3.946 -92.658 -34.592 1.00 61.79 C ATOM 3621 CB LYS A 516 2.753 -91.760 -34.258 1.00 61.68 C ATOM 3622 CG LYSA516 2.874-91.054-32.915 1.00 61.28 C ATOM 3623 CD LYS A 516 2.859 -92.024 -31.750 1.00 61.20 C ATOM 3624 CE LYSAS16 3.802-91.567-30.647 1.0061.34 C ATOM 3625 NZ LYS A 516 3.687 -90.108 -30.377 1.00 61.19 N ATOM 3626 C LYS A 516 3.598-94.113 -34.336 1.00 61. 88 C ATOM 3627 0 LYS A 516 3.898 -94.645 -33.269 1.00 62.04 0 ATOM 3628 N LEUA5I7 2.975-94.761-35.315 1.0061.97 N ATOM 3629 CA LEU A517 2.643 -96.176 -35.178 1.00 62.25 C ATOM 3630 CB LEU A 517 1.868 -96.690 -36.396 1.00 62.24 C ATOM 3631 CG LEU A 517 0.436-96.164 -36.551 1.00 62.30 C ATOM 3632 CD! LEU A 517 -0.225 -96.729 -37.800 1.00 62.24 C ATOM 3633 CD2 LEU A 517 -0.395 -96.473 -35.313 1.00 62.23 C ATOM 3634 C LEU A 517 3.893

-97.019 -34.935 1.00 62.46 C : ... ATOM 3635 0 LEUA5I7 3.871-97.939-34. 123 1.0062.42 0 ATOM 3636 N GLUA 518 4.983-96.698-35.628 1.00 62.79 N ATOM 3637 CA GLU A 518 6.252 -97.404 -35.418 1.00 63.31 C ATOM 3638 CB GLUA5I8 7.314-96.944-36.421 1.0063.45 C ATOM 3639 CO GLU A 518 7.738 -98.010 -37.419 1.00 63.87 C ATOM 3640 CD GLUA 518 6.782-98.127-38.581 1.00 64.37 C ATOM 3641 OE1 GLUA 518 6.048-99.135-38.645 1.00 64.42 0 ATOM 3642 OE2 OLU A 518 6.759 -97.205 -39.426 1.00 64.82 0 * ** ATOM 3643 C GLUA 518 6.799 -97.252 -34.001 1.00 63.54 C ATOM 36440 GLUA5I8 7.571-98.091-33.532 1.0063.50 0 ** * ATOM 3645 N GLYA 519 6.406 -96.175 -33.329 1.00 63.92 N ATOM 3646 CA GLY A 519 6.916 -95.872 -31.995 1.00 64.42 C ATOM 3647 C GLY A 519 7.909 -94.725 -32.008 1.00 64.74 C ATOM 3648 0 GLY A 519 9.012 -94.834 -31.468 1.0064.74 0 ATOM 3649 N HISA52O 7.513-93.620-32.633 1.0065.16 N ATOM 3650 CA HIS A 520 8.361 -92.438 -32.716 1.00 65.57 C ATOM 3651 CB HISA52O 8.735-92.143-34.169 1.0065.67 C ATOM 3652 CG HIS A 520 9.840 -93.003 -34.69 1 1.00 66.10 C ATOM 3653 ND1 HIS A 520 11.163 -92. 796 -34.357 1.00 66.58 N ATOM 3654 CEI HIS A 520 11.911 -93.707 -34.955 1.00 6672 C ATOM 3655 NE2HISA52O 11.121 -94.495-35.666 1.00 66.89 N ATOM 3656 CD2 HIS A 520 9 820 -94 077 -35.5 17 1.00 66.36 C ATOM 3657 C HISA 520 7.678-91.219-32.126 1.00 65.70 C ATOM 3658 0 HIS A 520 6.576 -90.855 -32.538 1.00 65.77 0 ATOM 3659 N GLY A 521 8.335 -90.583 -31.163 1.00 65.86 N ATOM 3660 CA GLYA52I 7.867 -89 296-30.678 1.00 66.01 C ATOM 3661 C GLY A 521 7.715 -88.376 -31.873 1.00 66.07 C ATOM 3662 0 GLYA521 8.524-88.416-32.802 1.00 66.13 0 ATOM 3663 N LEU A 522 6.663 -87.569 -3 1.874 1.00 66.10 N ATOM 3664 CA LEU A 522 6.483 -86.582 -32.929 1.00 66. 04 C ATOM 3665 CB LEU A 522 5.019 -86.174 -33.043 1.00 66.08 C ATOM 3666 CG LEU A 522 4.179 -86.795 -34.157 1.00 66.47 C ATOM 3667 CDI LEU A 522 4. 642 -88.202 -34.5 19 1.00 66.89 C ATOM 3668 CD2 LEU A 522 2.724 -86.798 -33.720 1.00 66.94 C ATOM 3669 C LEU A 522 7.322 -85.351 -32.639 1.00 65.97 C ATOM 3670 0 LEU A 522 7.534 -84.999 -3 1.478 1.00 65.87 0 ATOM 3671 N PRO A 523 7.808 -84.690 -33.699 1.00 65.92 N ATOM 3672 CA PROA523 8.473-83.409-33.516 1.0065.84 C ATOM 3673 CB PRO A 523 8.849 -82.993 -34.943 1.00 65.78 C ATOM 3674 CG PROA 523 8.792-84.241 -35.750 1.00 65. 95 C ATOM 3675 CD PROA 523 7.751 -85.097-35.113 1.00 65.96 C ATOM 3676 C PRO A 523 7.476 -82.414 -32.939 1.00 65.77 C ATOM 3677 0 PRO A 523 6.272 -82.685 -32.901 1.00 6597 0 ATOM 3678 N THR A 524 7.965 -8 1.272 -32.484 1.00 65.48 N ATOM 3679 CA THR A 524 7.065 -80.238 -32.020 1.00 65.17 C ATOM 3680 CB THRA 524. 7.481 -79.717-30.623 1.00 65.20 C ATOM 3681 OGI TIiRA 524 7.177-78.323-30.514 1.00 65.65 0 ATOM 3682 CG2 T} A 524 8.974 -79.937 -30.389 1.00 65.23 C ATOM 3683 C TI-ER A 524 6.952 -79.137 -33. 084 1.0064.84 C ATOM 3684 0 THRA524 5.974-78.392-33.122 1.0064.93 0 ATOM 3685 N ASN A 525 7.946 -79.070 -33.966 1.0064.41 N ATOM 3686 CA ASN A 525 794 I -78.137 -35.095 1.00 63.87 C ATOM 3687 CB ASNA525 8.818-76.920-34.805 1.0063.88 C ATOM 3688 CG ASNA525 8.167-75.948-33.854 1.0063.78 C ATOM 3689 OD1 ASN A 525 8.737 -75.603 -32.820 1.00 63.84 0 ATOM 3690 ND2 ASN A 525 6.961.75.502 -34.194 1.00 63.55 N ATOM 3691 C ASN A 525 8.422 -78.805 -36.374 1.00 63.51 C : * ATOM 3692 0 ASN A 525 9.530 -79.340 -36.428 1.00 63.55 0 ATOM 3693 N LEU A 526 7.583 -78.761 -37.401 1.00 62.99 N ATOM 3694 CA LEUA 526 7.882-79.378-38 681 1.00 62.43 C ATOM 3695 CB LEU A 526 6.694 -79.165 -39.6 15 1.00 62.46 C ATOM 3696 CG LEU A 526 6.369 -80.239 -40. 650 1.00 62.26 C ATOM 3697 CD1 LEU A 526 7.395.80.225 -41.753 1.00 62.66 C ATOM 3698 CD2 LEU A 526 6.303 -81.602 -39.996 1.00 62.13 C * 50 ATOM 3699 C LEUA526 9.146-78.766-39.286 1.0062.24 C ATOM 3700 0 LEU A 526 9.145 -77.599.39.674 1.00 62.21 0 : *. ATOM 3701 N PROA 527 10.234-79.554-39. 371 1.00 61.99 N ATOM 3702 CA PRO A 527 11.486 -79.062 -39.942 1.00 61.70 C *. : ATOM 3703 CB PROA 527 12.503-80.112-39.495 1.00 61.70 C * 55 ATOM 3704 CG PRO A 527 11.722.81.364 -39.395 1.00 61.61 C ATOM 3705 CD PRO A 527 10.340 -80.961 -38.94 I 1.00 61.99 C ATOM 3706 C PRO A 527 11.417-79.005 -41.466 1.00 61.51 C ATOM 3707 0 PRO A 527 10.65 1 -79.75 1 -42079 1.00 61.49 0 ATOM 3708 N ARGA528 12.221-78.133-42.069 1.0061.27 N ATOM 3709 CA ARGA 528 12.154-77.888-43.510 1.0061.10 C ATOM 3710 CB ARGA 528 13.334-77.024-43.968 1.00 61.10 C ATOM 3711 Co ARG A 528 13.363 -76.776 -45.472 1.00 61.06 C ATOM 3712 CD ARG A 528 14.621 -76.043 -45.903 1.00 61.02 C ATOM 3713 NE ARG A 528 14.650 -75.823 -47.347 1.00 60.86 N ATOM 3714 CZ ARG A 528 14.282 -74.691 -47.945 1.00 60.65 C ATOM 3715 NH! ARG A 528 14.343 -74.592 -49.267 1.00 60.39 N ATOM 3716 NH2 ARG A 528 13.855 -73.658 -47.227 1.00 60.55 N ATOM 3717 C ARGA528 12.091-79.163-44.355 1.0061.02 C ATOM 3718 0 ARG A 528 11.282-79.270-45.277 1.00 60.96 0 ATOM 3719 N ARGA 529 12.948-80.125 -44.032 1.00 60.92 N ATOM 3720 CA ARG A 529 13.097 -8 1.325 -44.848 1.00 60.87 C ATOM 3721 CB ARGA529 14.249-82.189-44.328 1.0061.05 C ATOM 3722 CG ARGAS29 14.118-82.565-42. 867 1.0061.92 C ATOM 3723 CD ARG A 529 15.338 -83.3 15 -42.367 1.00 63.40 C ATOM 3724 NE ARG A 529 15.130 -83.798 -41.006 1.00 64.56 N ATOM 3725 CZ A.RG A 529 14.453 -84.901 -40.702 1.00 65.44 C ATOM 3726 NH! ARGA 529 14.311 -85.259-39.432 1.00 65.89 N ATOM 3727 NH2ARGA529 13.916-85.646-41.665 1.0065.76 N ATOM 3728 C ARGA529 11.817-82.142-44.925 1.0060.59 C ATOM 3729 0 A.RG A 529 11.665 -82 979 -45.817 1.00 60.74 0 ATOM 3730 N LEUA53O 10.901-81.907-43.991 10060.16 N ATOM 3731 CA LEU A 530 9.623 -82.605 -44.003 1.00 59.71 C ATOM 3732 CB LEU A 530 9.209 -83.023 -42.59! 1.00 59.65 C ATOM 3733 CG LEU A 530 9.701 -84.382 -42.092 1.00 59.14 C ATOM 3734 CD1 LEU A 530 9.103 -84.693 -40.730 1.00 58.59 C ATOM 3735 CD2 LEU A 530 9.345 -85.472 -43.082 1.00 58.67 C ATOM 3736 C LEU A 530 8.520 -8 1.784 -44.664 1.00 59.56 C ATOM 3737 0 LEUA53O 7.468-82.318-45.009 1.0059.51 0 ATOM 3738 N VAL A 531 8.756 -80.488 -44.840 1.00 59.45 N ATOM 3739 CA VALA 531 7.784-79.637-45.519 1.00 59.44 C ATOM 3740 CB VAL A 531 8.167 -78.142 -45.438 1.00 59.28 C ATOM 3741 CG1 VAL A 531 7.067 -77.283 -46.024 1.00 58.89 C ATOM 3742 CG2VALA53I 8.443-77.735-44.006 1.0059.32 C ATOM 3743 C VAL A 531 7.685 -80.033 -46.989 1.00 59.61 C ATOM 3744 0 VAL A 531 8.700 -80.081 -47.685 1.00 59.64 0 ATOM 3745 N PRO A 532 6.464 -80.329 -47.467 1.00 59.71 N ATOM 3746 CA PRO A 532 6.282 -80.580 -48.89 1 1.00 59.85 C ATOM 3747 CB PRO A 532 4.776 -80.4 10 -49.079 1.00 59.82 C ATOM 3748 CG PROA 532 4.193-80.816-47.766 1.00 59.65 C ATOM 3749 CD PRO A 532 5.203 -80.447 -46.713 1.00 59.60 C : ATOM 3750 C PRO A 532 7.044 -79.537 -49.707 1.00 60.13 C ATOM 3751 0 PROAS32 7.085-78.370-49.322 1.0060.15 0 ATOM 3752 N PR0A533 7.648-79.960-50.829 1.0060.38 N ATOM 3753 CA PRO A 533 8.535 -79.145 -51.659 1.00 60.52 C ATOM 3754 CB PROA 533 8.659 -79.971 -52.938 1.00 60.55 C ATOM 3755 CG PRO A 533 8.543 -81.366 -52.458 1.00 60.51 C ATOM 3756 CD PROA533 7.498 -81.321 -51.373 1.00 60.41 C * * 50 ATOM 3757 C PROA 533 8.031 -77.729-51.965 1.00 60.72 C ATOM 3758 0 PRO A 533 8.842 -76.825 -52.156 1.00 60.82 0 : *. ATOM 3759 N SERA 534 6.717-77.532-52. 022 1.00 61.01 N ATOM 3760 CA SERA 534 6.176-76.176-52.028 1.00 61.33 C *. : ATOM 3761 CB SERA 534 4.719-76.179-52.469 1.0061.27 C * 55 ATOM 3762 OG SERA534 4.535-77.089-53.541 1.0061.06 0 ATOM 3763 C SERA534 6.320-75.634-50.606 1.0061.73 C ATOM 3764 0 SER A 534 5.342 -75.532 -49.849 1.00 61.49 0 ATOM 3765 N LYS A 535 7.56 1 -75.302 -50.248 1.00 62.26 N ATOM 3766 CA LYS A 535 7.909 -75.061 -48.849 1.00 62.66 C ATOM 3767 CB LYS A 535 9.0 19 -76.020 -48.362 1.00 62.74 C ATOM 3768 CG LYSA535 10.263-76.121 -49.239 1.00 62.63 C ATOM 3769 CD LYSA535 11.276-77.127-48.668 1.0062.53 C ATOM 3770 CE LYS A 535 10.889 -78.574

-48.974 1.00 62.10 C ATOM 3771 NZ LYS A 535 11.955-79.555 -48.612 1.00 61.50 N ATOM 3772 C LYS A 535 8.22 1 -73.624 -48.467 1.00 62.89 C ATOM 3773 0 LYS A 535 7.423 -73.007 -47.763 1.00 63.20 0 ATOM 3774 N ARGA536 9.356-73.086-48.915 1.0062.87 N ATOM 3775 CA ARGA536 9.820-71.790-48.411 1.0062.96 C ATOM 3776 CB ARGA 536 10.355 -71.935 -46.981 1.00 63.00 C ATOM 3777 CO ARGA536 9.589-71.160-45.920 1.0062.88 C ATOM 3778 CD ARG A 536 10.104 -69.730-45.785 1.00 62.78 C ATOM 3779 NE ARGA.536 9.513-69.039-44.637 1.0062.80 N ATOM 3780 CZ ARGA536 9.662-67. 741 -44.378 1.00 62.71 C ATOM 3781 NI-Il ARG A 536 9.085 -67.202 -43.3 12 1. 00 62.64 N ATOM 3782 NH2 ARG A 536 10.385 -66 977 -45.186 1.00 62.73 N ATOM 3783 C ARG A 536 10.907 -7 1.172 -49.261 1.00 63.09 C ATOM 3784 0 ARG A 536 12.064 -71.595 -49.195 1.00 63.09 0 ATOM 3785 N ARGAS37 10.536-70.154-50.040 1.0063.37 N ATOM 3786 CA ARG A 537 11.507 -69.382 -50.808 1.00 63.60 C ATOM 3787 CB ARG A 537 10.803 -68.242 -5 1.556 1.00 63.66 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 1.00 64.23 C ATOM 3790 NE ARG A 537 13.276 -66.952 -54.216 1.0064.87 N ATOM 3791 CZ ARGA537 13.586-65.692-54.516 1.00 65.30 C ATOM 3792 NH1 ARG A 537 13.493 -64.746-53.591 1.00 65.61 N ATOM 3793 NH2 ARG A 537 13.998 -65.373 -55. 739 1.00 64.97 N ATOM 3794 C ARG A 537 12.530 -68.8 16 -49.820 1.00 63.69 C ATOM 3795 0 ARGA537 12.202-68.553-48.657 1.0063.76 0 ATOM 3796 N GLN A 538 13.766 -68.64 I -50.275 1.00 63.75 N ATOM 3797 CA GLNA538 14.834-68.177-49.394 1.0063.87 C ATOM 3798 CB GLN A 538 15.457 -69.363 -48.658 1.00 63.84 C ATOM 3799 CG GLN A 538 15.906 -70.488 -49.582 1.00 63.92 C ATOM 3800 CD GLN A 538 16.296 -71.738 -48.817 1.0064.01 C ATOM 3801 OEIGLNA538 16.303-71.751-47.584 1.0064.15 0 ATOM 3802 NE2 GLN A 538 16.622 -72.802 -49.545 1.00 64.37 N ATOM 3803 C GLNA538 15.909-67.416-50.160 1.0063.88 C ATOM 3804 0 GLN A 538 17.043 -67.243 -49.647 1.00 63.92 0 ATOM 3805 O2AANPA600 11.527-56.574 -1.805 1.0048.61 0 ATOM 3806 PA ANPA 600 11.448-57.106 -3.213 1.0048.08 P ATOM 3807 O1AANPA600 12.590-57.937 -3.742 1.0048.41 0 :. ATOM 3808 03A AMP A 600 11.221 -55.854 -4.189 1.00 49.01 0 * *** ATOM 3809 PB AMP A 600 11.878 -54.443 -3.787 1.00 49.55 P ATOM 3810 OIBANPA600 12.072-53.654 -5.058 1.0049.44 0 ATOM 3811 O2BANPA600 13.088-54.721 -2.926 1.0049.32 0 ATOM 3812 N3B AMP A 600 10.688 -53.641 -2.803 1.00 49.69 N ATOM 3813 PG ANPA600 11.161-52.172 -2.006 1.0050.29 P ATOM 3814 030 ANPA 600 11.033-51.114 -3.076 1.00 50.68 0 ATOM 3815 O2GANPA 600 10.150-52.031 -0.893 1.00 50.99 0 * S ATOM 3816 OIGANPA600 12.579-52.435 -1.551 1.0049.88 0 * ,* ATOM 3817 O5*ANPA600 10.094-57.950 -3.373 1.0048.33 0 ATOM 3818 C5*ANPA600 9.065-57.592 -4.286 1.0049.10 C * ATOM 3819 C4 ANP A 600 7.956 -58.626 -4.134 1.00 50.21 C ATOM 3820 C3*ANPA600 8.309-59.661 -3.080 1.00 50.31 C ATOM 3821 03* ANP A 600 7.105 -60.157 -2.491 1.00 50.26 0 ATOM 3822 C2* AMP A 600 8.963 -60.782 -3.853 1.00 50.21 C ATOM 3823 02* AMP A 600 8.705 -62.044 -3.239 1.00 50.10 0 ATOM 3824 C1*ANPA600 8.291 -60.692 -5.208 1. 00 50.66 C ATOM 3825 04 ANP A 600 7.807 -59.354 -5.353 1.00 50.80 0 ATOM 3826 N9 ANP A 600 9.253 -60.938 -6.296 1.00 50.73 N ATOM 3827 C4 ANPA600 8.946-61.536 -7.443 1.0050.52 C ATOM 3828 C5 ANPA600 10.180-61.565 -8.228 1.0050.67 C ATOM 3829 N7 ANPA 600 11.130-60.971 -7.480 1.0051.15 N ATOM 3830 C8 ANPA600 10.552-60.592 -6.309 1.00 50.79 C ATOM 3831 N3 ANP A 600 7.823 -62.07 I -7.962 1 00 50.46 N ATOM 3832 C2 ANP A 600 7.828 -62.625 -9.184 1.00 50.75 C ATOM 3833 Ni ANPA600 8.920-62.692 -9.963 1.0050.79 N ATOM 3834 C6 ANP A 600 10.108 -62.188 -9.564 1.00 50.80 C ATOM 3835 N6 ANP A 600 11,205 -62.253 -10.356 1.00 50.98 N ATOM 3836 MG MGA700 13.847- 53618 -0.877 1.0049.55 MG ATOM 3837 CA CA A 701 -4.087 -77.142 -45.879 1.00 46.71 CA ATOM I N ARGB 19 -35.864-44.695-40.362 1.0058.79 N ATOM 2 CA ARG B 19 -36.349 -44.622 -38.954 1.00 58.86 C ATOM 3 CB ARG B 19 -37.709 -45 314 -38.8 19 1.00 58.86 C ATOM 4 CG ARG B 19 -37.648 -46.838 -38.872 1.00 59.05 C ATOM 5 CD ARG B 19 -39.035 -47.464 -38.760 1.00 59.14 C ATOM 6 NE ARG B 19 -39.799 -46.949 -37.622 1.00 59.75 N ATOM 7 CZ ARG B 19 -40.800 -46.076 -37.722 1.00 59.95 C ATOM 8 NH! AROB 19 -41.169-45.613-38.911 1.0060.07 N ATOM 9 NH2 ARG B 19 -41.437 -45.665 -36.631 1.00 59.86 N ATOM 10 C ARGB 19 -35.335-45.249-37.999 1.0058.73 C ATOM 11 0 ARGB 19 -35.582-45.372-36.800 1.0058.69 0 ATOM I N THRB 20 -34.188-45.636-38.545 1.0058.62 N ATOM 2 CA THR B 20 -33.114 -46.223 -37.751 1.00 58.46 C ATOM 3 CB THRB 20 -32.290-47.226-38.581 1.0058.50 C ATOM 4 OGI THRB 20 -31.604 -46.534 -39.634 1.00 58.37 0 ATOM 5 CG2 THR B 20 -33.199 -48.292 -39.178 1.00 58.59 C ATOM 6 C THRB 20 -32.180 -45.152 -37.186 1.00 58.32 C ATOM 7 0 THR B 20 -32.520 -43.965 -37.165 1.00 58.25 0 ATOM 1 N VAL B 21 -31.000-45.579-36.740 1.00 58.12 N ATOM 2 CA VALB 21 -30.048 -44.683 -36.083 1.00 57.89 C ATOM 3 CB VALB 21 -29.111-45.447-35.127 1.00 57.93 C ATOM 4 CG1 VAL B 21 -28.124 -46.293 -35.915 1.00 58.17 C ATOM 5 CG2VALB 21 -28.372-44.474-34.220 1.0057.98 C ATOM 6 C VAL B 21 -29.212 -43.859 -37.066 1.00 57.68 C ATOM 7 0 VALB 21 -29.074-42.644-36.900 1.0057.39 0 ATOM 1 N THR B 22 -28.652 -44.511 -38.082 1.00 57.46 N ATOM 2 CA THR B 22 -27.859 -43 792 -39.077 1.00 57.30 C ATOM 3 CB THRB 22 -27.161 -44.740 -40.090 1.00 57.27 C : * ATOM 4 OGI THRB 22 -28.023 -44.987-41.207 1.00 57.51 0 * * ATOM 5 CG2 THR B 22 -26.780 -46.062 -39.430 1.00 57.23 C ATOM 6 C THRB 22 -28.755 -42.784-39.798 1.00 57.11 C ATOM 7 0 THRB 22 -28.337 -41.669 -40.100 1.00 57.00 0 ATOM 1 N SERB 23 -29.994-43.183 -40.059 1.00 56.93 N ** *. ATOM 2 CA SER B 23 -31.000 -42.275 -40.586 1.00 56.79 C * ATOM 3 CB SERB 23 -32.349-42.985-40.618 1.0056.78 C I.....

* * 50 ATOM 4 OG SER B 23 -33.311 -42.263 -39.874 1.00 57.00 0 ATOM 5 C SERB 23 -31.094-41.016-39.728 1.00 56.73 C * * ATOM 6 0 SER B 23 -31.004 -39.884 -40.230 1.00 56.72 0 ATOM 1 N SER B 24 -31.268 -41.227 -38.427 1.00 56.67 N *. ATOM 2 CA SER B 24 -31.384 -40.135 -37.468 1.00 56.66 C * 55 ATOM 3 CB SER B 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 0 ATOM S C SERB 24 -30.129-39.262-37.495 1.0056.55 C ATOM 6 0 SERB 24 -30.210-38.031 -37.511 1.00 56.41 0 ATOM 1 N LEUB 25 -28.971.39.911 -37.510 1.0056.64 N ATOM 2 CA LEU B 25 -27.708 -39 213 -37.709 1.00 56.46 C ATOM 3 CB LEUB 25 -26.567-40.216-37.867 1.00 56.37 C ATOM 4 CG LEUB 25 -25.705-40.508-36. 643 1.0056.13 C ATOM 5 CDI LEUB 25 -26.483-40.290-35.370 1.00 55.71 C ATOM 6 CD2 LEU B 25 -25.157 -41.923 -36.717 1.00 56.30 C ATOM 7 C LEUB 25 -27. 771 -38.320-38.943 1.00 56.49 C ATOM 8 0 LEU B 25 -27.389 -37.148 -38.894 1. 00 56.42 0 ATOM I N LYS B 26 -28.252 -38.883 -40.048 1.00 56.45 N ATOM 2 CA LYS B 26 -28.317-38.164 -41.308 1.00 56.29 C ATOM 3 CB LYS B 26 -28.822 -39.079 -42.427 1.00 56.32 C ATOM 4 CO LYSB 26 -28.800-38.454-43.819 1.0056.35 C ATOM 5 CD LYS B 26 -28.778 -39.516 -44.917 1.00 56.35 C ATOM 6 CE LYS B 26 -30.038 -40.371 -44.910 1.00 56.39 C ATOM 7 NZ LYSB 26 -29.907-41.557-45.803 1.00 56.13 N ATOM 8 C LYSB 26 -29.190-36.924-41.168 1.0056.32 C ATOM 9 0 LYS B 26 -28.764 -35.817 -41.516 1.00 56.34 0 ATOM 1 N GLUB 27 -30.401 -37.093-40.641 1.00 56.37 N ATOM 2 CA GLU B 27 -31.264 -35.927 -40.433 1.00 56.31 C ATOM 3 CB GLU B 27 -32.635 -36.332 -39.894 1.00 56.40 C ATOM 4 CG GLU B 27 -33.618 -36.769 -40.976 1.00 56.99 C ATOM 5 CD GLU B 27 -33.694 -35.789 -42.142 1.00 57.43 C ATOM 6 OE1 GLU B 27 -32.665 -35.604 -42.834 1.00 57.97 0 ATOM 7 0E2 GLU B 27 -34.785 -35.2 18 -42.379 1.00 56.59 0 ATOM 8 C GLU B 27 -30.610 -34.886 -39.526 1.00 56.16 C ATOM 9 0 GLU B 27 -30.594 -33.691 -39.844 1.00 55.99 0 ATOM 1 N LEU B 28 -30.063 -35.352 -38.405 1.00 56.19 N ATOM 2 CA LEU B 28 -29.327 -34.483 -37.489 1.00 56.04 C ATOM 3 CB LEU B 28 -28.656 -35.295 -36.378 1.00 55. 97 C ATOM 4 CO LEUB 28 -29.364-35.366-35.022 1.0056.13 C ATOM 5 CD1 LEU B 28 -30.854 -35.7 12 -35.137 1.00 56.25 C ATOM 6 CD2 LEU B 28 -28.644 -36.321 -34.084 1.00 56.01 C ATOM 7 C LEUB 28 -28.287-33.671 -38.241 1.00 56.00 C ATOM 8 0 LEUB 28 -28.236-32.450-38.116 1.0056.01 0 ATOM I N TYRB 29 -27.461 -34.353-39.026 1.00 55.97 N ATOM 2 CA TYRB 29 -26.478-33.671 -39.848 1.00 55.76 C ATOM 3 CB TYR B 29 -25.722 -34.659 -40.731 1.00 55. 53 C ATOM 4 CG TYRB 29 -24.819-33.982-41.733 1.00 55.13 C ATOM 5 CDI TYR B 29 -23.669 -33.320 -41.323 1.00 54.84 C ATOM 6 CE1 TYR B 29.22.840 -32.696 -42.234 1.00 54.64 C ATOM 7 CZ TYR B 29 -23.157 -32.729 -43.574 1.00 54. 85 C ATOM 8 OH TYR B 29 -22.339 -32.111 -44.487 1.00 55.02 0 :. ATOM 9 CE2 TYR B 29 -24.291 -33.381 -44.008 1.00 54.94 C * ATOM 10 CD2 TYR B 29 -25.117 -34.000 -43.087 1.00 54.98 C ATOM 11 C TYRB 29 -27.140-32.618-40.720 1.0055.90 C * . ATOM 12 0 TYR B 29 -26.828 -31.432 -40.611 1.00 55.94 0 ATOM I N ARG B 30 -28.065 -33.056 -41.572 1.00 56.07 N ATOM 2 CA ARGB 30 -28.661-32.167-42.566 10056.16 C ATOM 3 CB ARGB 30 -29.655-32.915-43.458 1.00 56.13 C *:: 50 ATOM 4 CO ARG 13 30 -30.281 -32.027 -44.534 1.00 56.57 C ATOM 5 CD ARG B 30 -3 1.444 -32.704 -45.244 1.00 56.62 C * ** ATOM 6 NE ARG B 30 -32.497 -33.102 -44.313 1.00 57.56 N ATOM 7 CZ ARGB 30 -33.525-32.334-43.968 1.00 57.96 C * ATOM 8 NH1ARGB 30 -33.650-31.115-44.479 1.0058 09 N * * 55 ATOM 9 NH2 ARG B 30 -34.433 -32.785 -43.112 1.00 58.17 N ATOM 10 C ARG B 30 -29.336 -30.945 -41.958 1.00 56.07 C ATOM 11 0 ARGB 30 -29.309-29.864-42.544 1.0056.10 0 ATOM 1 N THRB 31.29.938 -31.104.40.786 1.00 56.02 N ATOM 2 CA THR B 31 -30.686 -29.999 -40.194 1.00 55.94 C ATOM 3 CB THRB 31 -3 1.968 -30.495 -39.510 1.00 55.94 C ATOM 4 001 THRB 31 -31.627-31.427-38.476 1.0056.01 0 ATOM 5 C02 THR B 31 -32.879 -31.172 -40.522 1.00 55.91 C ATOM 6 C THRB 31 -29.878-29.166-39.196 1.0055.97 C ATOM 7 0 THR B 31 -30.158 -27.982 -39.000 1.00 55.91 0 ATOM I N LYS B 32 -28.877 -29.780 -38.572 1.00 56.00 N ATOM 2 CA LYS B 32 -28.160 -29.137 -37.469 1.00 56.02 C ATOM 3 CB LYSB 32 -28.201 -30.019-36.210 1.00 56.03 C ATOM 4 CU LYS B 32 -29.582 -30.162 -35.544 1.00 56.05 C ATOM 5 CD LYSB 32 -29.920-28.956-34.665 1.0056.16 C ATOM 6 CE LYS B 32 -3 1.272 -29.099 -33.959 1.00 55.96 C ATOM 7 NZ LYS B 32 -3 1.193 -29.805 -32.646 1.00 55.50 N ATOM 8 C LYSB 32 -26.711 -28.750-37.796 1.00 56.03 C ATOM 9 0 LYSB 32 -26.168-27.819-37.200 1.0056.12 0 ATOM I N LEUB 33 -26.087-29.460-38.734 1.0055.98 N ATOM 2 CA LEU B 33 -24.682 -29.209 -39.069 1.00 55.83 C ATOM 3 CB LEUB 33 -23.881 -30.508-39.031 1.00 55.81 C ATOM 4 CG LEU B 33 -22.853 -30.636 -37.9 15 1.00 55.96 C ATOM 5 CDI LEU B 33 -22.175 -3 1.991 -37.990 1.00 56.34 C ATOM 6 CD2 LEU B 33 -2 1.830 -29.526 -38.036 1.00 56.25 C ATOM 7 C LEU B 33 -24.496 -28.553 -40.428 1.00 55.75 C ATOM 8 0 LEU B 33 -23.834 -27.52 1 -40.551 1.00 55.70 0 ATOM 1 N LEU B 34 -25.081 -29.171 -41.448 1.00 55.70 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 CD1 LEU B 34 -24.377 -29.201 -45.688 1.00 55.57 C ATOM 6 CD2 LEU B 34 -26.656 -30.193 -46.001 1.00 55.60 C ATOM 7 C LEU B 34 -25.138 -27.189 -42.948 1.00 55.74 C ATOM 8 0 LEU B 34 -24.368 -26.536 -43.652 1.00 55.74 0 ATOM I N PRO B 35 -26.158 -26.624 -42.272 1.00 55.81 N ATOM 2 CA PROB 35 -26.387-25.187-42.397 1.00 55.89 C ATOM 3 CR 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 PRO B 35 -25.183 -24.372 -4 1.948 1.00 56.06 C ATOM 7 0 PROB 35 -24.884-23.339-42.542 1.0056.11 0 ATOM 1 N LEU B 36 -24.496 -24.843 -40.914 1.00 56.32 N ATOM 2 CA LEUB 36 -23.376-24.111 -40.338 1.0056.60 C * . ATOM 3 CR LEU B 36 -23.087 -24.654 -38.947 1.00 56.61 C ** ATOM 4 CG LEUB 36 -22.594-23.658-37.905 1.0056.89 C * ATOM 5 CDI LEU B 36 -23.153 -24.031 -36.552 1.00 57.25 C ATOM 6 CD2 LEU B 36 -2 1.082 -23.624 -37.872 1.00 57.53 C *. 45 ATOM 7 C LEUB 36 -22.148-24.229-41.237 1.00 5679 C ATOM 8 0 LEUB 36 -21.443-23.237-41.507 1.0056.95 0 ATOM 1 N GLUB 37 -21.913-25.448-41.712 1.0057.00 N ATOM 2 CA GLU B 37 -20.879 -25.705 -42.703 1.00 57.34 C * ** ATOM 3 CB GLUB 37 -20.912-27.168-43.151 1.00 57.32 C *.:.. 50 ATOM 4 CG GLUB 37 -20.568-28.182-42.074 1.0057.49 C ** * ATOM 5 CD GLU B 37 -20.509 -29.602 -42.617 1.00 57.48 C ATOM 6 OEI GLU B 37 -20.434 -29.763 -43.857 1.00 57.98 0 ATOM 7 0E2 GLU B 37 -20.535 -30.557 -41.810 1.00 57.15 0 ATOM 8 C GLUB 37 -21.050-24.800-43.925 1.0057.50 C ATOM 9 0 GLU B 37 -20.095 -24.154 -44.366 1.00 57.53 0 ATOM I N GLU B 38 -22.267 -24.760 -44.466 1.00 57.64 N ATOM 2 CA GLU B 38 -22. 544 -23.989 -45.677 1.00 57.92 C ATOM 3 CB GLUB 38 -23.939-24.302-46.222 1.0058.10 C ATOM 4 CG GLU B 38.24.052 -25.674 -46.868 1.00 59.87 C ATOM 5 CD GLUB 38 -23.318-25.767-48.201 1.0062.05 C ATOM 6 OE1 GLU B 38 -23.851 -25.231 -49.205 1.00 62.81 0 ATOM 7 0E2 GLU B 38 -22.2 19 -26.384 -48.245 1.00 62.50 0 ATOM 8 C GLU B 38 -22.401 -22.498 -45.442 1.00 57.70 C ATOM 9 0 GLUB 38 -21.934-21.771 -46.316 1.00 57.74 0 ATOM 1 N HIS B 39 -22.798 -22.045 -44.259 1.00 57.50 N ATOM 2 CA HISB 39 -22.740-20.627-43.951 1.0057.36 C ATOM 3 CB HISB 39 -23.553 -20.289-42.697 1.00 57.49 C ATOM 4 CG HIS B 39 -23.914 -18.837 -42.582 1.00 57.86 C ATOM 5 NDI 1-IISB 39 -23.802-18.130-41.403 1.0058.15 N ATOM 6 CE1 HIS B 39 -24.187 -16.882 -41.600 1.00 57.80 C ATOM 7 NE2 HIS B 39.24.540 -16 751 -42.866 1.00 58. 12 N ATOM 8 CD2 HIS B 39.24.379 -17.959 -43.502 1.00 57.91 C ATOM 9 C HIS B 39 -21.301 -20.174 -43.795 1.00 57.12 C ATOM 10 0 HIS B 39 -20.915 -19. 146 -44.341 1.00 57.14 0 ATOM I N TYR B 40 -20.494 -20.938 -43.068 1.00 56.95 N ATOM 2 CA TYRB 40 -19.110-20.504-42.885 1.0056.80 C ATOM 3 CB TYR B 40 -18.683 -20.668 -41.432 1.00 56.68 C ATOM 4 03 TYRB 40 -19.505-19.812-40.501 1.00 56.39 C ATOM 5 CD! TYRB 40 -19.178 -18.482 -40.284 1.00 56.19 C ATOM 6 CE1 TYR B 40 -19.929 -17.692 -39.445 1.00 56.13 C ATOM 7 CZ TYR B 40 -21.032-18.227-38.811 1.00 56.27 C ATOM 8 OH TYRB 40 -21.788-17.435-37.973 1.0056.35 0 ATOM 9 CE2TYRB 40 -21.384-19,546-39.017 1.0055.86 C ATOM 10 CD2 TYR B 40 -20.624 -20.327 -39.858 1.00 56.00 C ATOM 11 C TYRB 40 -18.132-21.152-43.868 1.00 56.98 C ATOM 12 0 TYR B 40 -16.916 -21.131 -43.664 1.00 56.80 0 ATOM I N ARG B 41 -18.685 -21.710-44.943 1.00 57.29 N ATOM 2 CA ARG B 41 -17.902 -22.199 -46.082 1.00 57.67 C ATOM 3 CB ARG B 41 -17.259 -2 1.025 -46.827 1.00 57.84 C ATOM 4 CG ARG B 41 -18.247 -20.264 -47.691 1.00 59.24 C ATOM 5 CD ARGB 41 -18.706-21.140-48.847 1.00 61.74 C ATOM 6 NE ARG B 41.20.154 -21.097 -49.031 1.00 63.78 N ATOM 7 CZ ARG B 41 -20.869 -22.080 -49.574 1.00 65.07 C ATOM 8 NHI ARG B 41 -22.184 -21.953 -49.699 1.00 65.94 N ATOM 9 NH2 ARG B 41 -20.275 -23.194 -49.988 1.00 65.68 N ATOM 10 C ARG B 41 -16.862 -23.250 -45.704 1.00 57.59 C ATOM 11 0 ARG B 41 -15.745 -23.266 -46.227 1.00 57.63 0 ATOM 1 N PHEB 42 -17.261 -24.135-44.798 1.00 57.42 N * . ATOM 2 CA PHE B 42.16.440 -25.247 -44.347 1.00 57.25 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 1.00 56.65 C ATOM 5 CDI PHEB 42 -16.541 -28.533 -43.191 1.00 56.29 C *:* 45 ATOM 6 CEI PHE B 42 -15.840 -29.506 -42.518 1.00 56.21 C ATOM 7 CZ PHEB 42 -15123-29.177-41.385 1.0056.63 C ATOM 8 CE2PHEB 42 -15.111-27.873-40.931 1.0056.58 C ATOM 9 CD2 PHE B 42 -15.815 -26.905 -41.612 1.00 56.58 C * *, ATOM 10 C PHEB 42 -15.866-26.027-45.525 1.0057.37 C ATOM 11 0 PHEB 42 -14.740-26.520-45.469 1.0057.37 0 ** * ATOM 1 N GLYB 43 -16.649-26.124-46.595 1.00 57.54 N ATOM 2 CA GLY 13 43 -16. 295 -26.943 -47.750 1.00 57.71 C ATOM 3 C GLY B 43 -15.092 -26.473 -48.545 1.00 57.88 C ATOM 4 0 GLYB 43 -14.552-27.222-49.358 1.0058.01 0 ATOM I N SERB 44 -14.671 -25.234-48.320 1.00 57.99 N ATOM 2 CA SER B 44 -13.537 -24.680 -49.045 1.00 58.04 C ATOM 3 CB SER B 44 -13.877 -23.298 -49.588 1.00 57.99 C ATOM 4 OG SERB 44 -15.092-23.328-50.315 1.0058.35 0 ATOM 5 C SERB 44 -12.324-24.589-48.144 1.0058.15 C ATOM 6 0 SERB 44 -11.338-23.930-48.482 1.0058.23 0 ATOM I N PHEB 45 -12.400-25.257-46.996 1.0058.23 N ATOM 2 CA PHE B 45 -11.345 -25.183 -45.995 1.00 58.33 C ATOM 3 CB PHE B 45 -11.770-24.285 -44.832 1.00 58.38 C ATOM 4 Co PHEB 45 -11.611-22.817-45.101 1.0058.62 C ATOM 5 CDI PHE B 45 -10.373 -22.207 -44.984 1.00 58.76 C ATOM 6 CE! PHEB 45 -10.225-20.851 -45.226 1.00 58.85 C ATOM 7 CZ PHE B 45 -11.322 -20.087 -45.582 1.00 58.65 C ATOM 8 CE2 PHE B 45 -12.563 -20.681 -45.694 1.00 58.80 C ATOM 9 CD2 PHE B 45 -12.705 -22.039-45.454 1.00 58.92 C ATOM 10 C PHEB 45 -10.947-26.549-45.451 1.0058.40 C ATOM ii 0 PHEB 45 -9769-26.809-45.230 1.0058.46 0 ATOM I N HIS B 46 -11.924 -27.415 -45.214 1.00 58.47 N ATOM 2 CA HIS B 46 -II 635 -28.696 -44.585 1.00 58.57 C ATOM 3 CB HIS B 46 -12.053 -28.677 -43.118 1.00 58.52 C ATOM 4 CG HISB 46 -11.512-27.510-42.357 1.00 58.40 C ATOM 5 ND! HISB 46 -10.256-27.510-41.790 1.005869 N ATOM 6 CEI HIS B 46 -10.047 -26.351 -41.191 1.00 58.73 C ATOM 7 NE2HISB 46 -11.122-25.599-41.351 1.00 58.60 N ATOM 8 CD2 HIS B 46 -12.053 -26.301 -42.077 1.00 58.47 C ATOM 9 C HIS B 46 -12.304 -29.851 -45.306 1.00 58.82 C ATOM 10 0 HISB 46 -11.631 -30.724-45.842 1.00 58.94 0 ATOM I N SERB 47 -13.630-29.859-45.322 1.00 59.14 N ATOM 2 CA SERB 47 -14.356-30.936-45.976 1.0059.57 C ATOM 3 CB SER B 47 -14.756 -32.001 -44.959 1.00 59.49 C ATOM 4 OG SER B 47 -13.754 -32.992 -44.853 1.00 59.64 0 ATOM 5 C SER B 47 -15.589 -30.454 -46.723 1.00 59.92 C ATOM 6 0 SERB 47 -16.299-29.566-46.251 1.0060.08 0 ATOM I N PRO B 48 -15.848 -3 1.043 -47.899 1.00 60.20 N ATOM 2 CA PRO B 48 -17.079 -30.774 -48.629 1.00 60.54 C ATOM 3 CR PRO B 48 -16.850 -31 470 -49.967 1.00 60.46 C ATOM 4 CG PRO B 48 -15.873 -32.544 -49.664 1.00 60.43 C ATOM 5 CD PRO B 48 -14.983 -32.004 -48.600 1.00 60.14 C ATOM 6 C PROB 48 -18.249-31.409-47.892 1.00 60.95 C ATOM 7 0 PRO B 48 -18.037 -32.221 -46.990 1.00 61.07 0 ATOM 1 N ALAB 49 -19.470-31.039-48.259 1.0061.39 N ATOM 2 CA ALA B 49 -20.649 -31.565 -47.577 1.00 61.81 C ATOM 3 CB ALA B 49 -2 1.887 -30.779 -47.964 1.00 61.89 C :. 40 ATOM 4 C ALAB 49 -20.841 -33.046-47.872 1.00 62..05 C ATOM 5 0 ALAB 49 -20.542 -33.508-48.969 1.00 61.90 0 ATOM 1 N LEUB 50 -21.346-33.778-46.884 1.0062.63 N ATOM 2 CA LEU B 50 -21.517 -35.224 -46.983 1.00 63.26 C ATOM 3 CB LEU B 50 -21.669 -35. 826 -45.582 1.00 63.16 C ATOM 4 CO LEU B 50 -20.604 -35.424 -44.553 1.00 63. 07 C ATOM 5 CDI LEUB 50 -19.233-35.875-45.010 1.00 63.12 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 0 LEUB 50 -23.639-34.817-48.047 1.0064.09 0 ATOM I 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 1.00 65.54 C ATOM 4 CG GLU B 51 -22.076 -37.302 -51.095 1.00 66. 38 C ATOM 5 CD GLU B 51 -21.147 -38.289 -51.777 1.00 67.59 C ATOM 6 0E1 GLU B 51 -20.943 -39.386 -5 1.212 1.00 68.33 0 ATOM 7 0E2 GLU B 51 -20.620 -37.976 -52.870 1.00 68.07 0 ATOM 8 C GLUB 51 -24.526-38.398-48.373 1.0065.74 C ATOM 9 0 GLUB 51 -24.216-38.592-47.201 1.00 65.83 0 ATOM I 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 1.00 66.50 C ATOM 3 CB ASP B 52 -27.461 -40.543 -48.947 1.00 66.58 C ATOM 4 CG ASP B 52 -28.508 -39.495 -48.641 1.00 67.19 C ATOM 5 OD1 ASP B 52 -28.132 -38.386 -48.194 1.00 67.73 0 ATOM 6 OD2ASPB 52 -29.710-39.782-48.843 1.0067.86 0 ATOM 7 C ASPB 52 -25.187-41.420-48.418 1.0066.69 C ATOM 8 0 ASP B 52 -25.273 -42.377 -47 638 1.00 66.73 0 ATOM I N ALAB 53 -24.283 -41.341 -49.388 1.00 66.92 N ATOM 2 CA ALA B 53 -23.378 -42.436 -49.699 1.00 67.19 C ATOM 3 CB ALAB 53 -22.599-42.128-50.969 1.0067.25 C ATOM 4 C ALA B 53 -22.430 -42.772 -48.552 1.00 67.26 C ATOM 5 0 ALAB 53 -22.050-43.926-48.380 1.0067.24 0 ATOM 1 N ASP B 54 -22.043 -41.771 -47.770 1.00 67.45 N ATOM 2 CA ASP B 54 -21.163 -42.028 -46.632 1.00 67.74 C ATOM 3 CB ASPB 54 -20.141 -40.899 -46.416 1.00 67.90 C ATOM 4 CG ASPB 54 -20.661 -39.544-46.847 1.0068.67 C ATOM 5 ODI ASP B 54 -21.898 -39.378 -46.913 1.00 69.79 0 ATOM 6 0D2 ASP B 54 -19.833 -38.646-47.125 1.00 69.03 0 ATOM 7 C ASP B 54 -2 1.958 -42.329 -45 363 1.00 67.62 C ATOM 8 0 ASPB 54 -21.400-42.378-44.265 1.0067.85 0 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 PHE B 55 -24.948 -40.743 -43.624 1.00 66.79 C ATOM 5 CDI PHEB 55 -24.578-39.670-44.412 1.00 66.59 C ATOM 6 CE1 PHE B 55 -24.254 -38.459 -43.846 1.00 66.30 C ATOM 7 CZ PHE B 55 -24.300 -38.306 -42.480 1.00 66. 49 C ATOM 8 CE2 PHE B 55 -24.671 -39.366 -41.683 1.00 66.62 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 0 PHEB 55 -24.788-45.209-43.822 1.0066.88 0 ATOM 1 N ASP B 56 -24.915 -44.669 -46.004 1.00 66.74 N ATOM 2 CA ASP B 56 -25.524 -45.940 -46.392 1.00 66.60 C ATOM 3 CB ASPB 56 -26.816-45.690-47.176 1.0066.71 C ATOM 4 CG ASP B 56 -27.844 -44.905 -46.379 1.00 67.09 C ATOM 5 OD1 ASP B 56 -27.864 -45.043 -45.136 1.00 67.21 0 ATOM 6 OD2 ASP B 56 -28.635 -44.153 -46.997 1.00 67.60 0 ATOM 7 C ASP B 56 -24.591 -46.835 -47.209 1.00 66.36 C ATOM 8 0 ASPB 56 -25.044-47.576-48.082 1.0066.42 0 * ATOM 1 N GLY B 57 -23.296 -46.777 -46.922 1.00 66.00 N ATOM 2 CA GLY B 57 -22.319 -47.528 -47.701 1.00 65. 67 C ATOM 3 C GLYB 57 -21.546-48.534-46.877 1.0065.47 C ATOM 4 0 GLY B 57 -2 1.455 -48.408 -45.656 1.00 65.50 0 45 ATOM 1 N LYSB 58 -20.985 -49.535-47.552 1.00 65.22 N ATOM 2 CA LYSB 58 -20.241 -50.602-46.883 1.00 64.95 C ATOM 3 CB LYSB 58 -19.922-51.734-47.864 1.00 64.95 C ATOM 4 CG LYS B 58 -20.909 -52.886 -47.815 1.00 65.08 C * ** ATOM 5 CD LYS B 58 -20.919 -53.661 -49.120 1.00 65.47 C ATOM 6 CE LYSB 58 -19.519-54.076-49.535 1.0065.82 C ATOM 7 NZ LYS B 58 -19.515 -54.712 -50.885 1.00 66.10 N ATOM 8 C LYSB 58 -18.958-50.095 -46.235 1.00 64.68 C ATOM 9 0 LYSB 58 -18.191-49.365-46.864 1.00 64.72 0 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 PRO B 59 -17.587 -50.937 -42.956 1.00 64.07 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 1.00 64.28 C ATOM 6 C PROB 59 -16.240-50.401 -45.018 1.00 63.96 C ATOM 7 0 PROB 59 -16.143 -5 1.438 -45.678 1.00 63.99 0 ATOM I N MET B 60 -15.277 -49.488 -44.941 1.00 63.71 N ATOM 2 CA METS 60 -13.981 -49.666-45.582 1. 00 63.49 C ATOM 3 CB MET B 60 -13.569 -48.382 -46.311 1.00 63.41 C ATOM 4 CG MET B 60 -14.477 -47.957 -47.455 1.00 63.33 C ATOM 5 SD METB 60 -14.625-46.152-47.591 1.0063.57 S ATOM 6 CE METB 60 -15.071 -45.961 -49.319 1.00 63.70 C ATOM 7 C MET B 60 -12.935 -49.986 -44.520 1.00 63.31 C ATOM 8 0 MET B 60 -13.049 -49.526 -43.387 1.00 63.29 0 ATOM I N VALB 61 -11.928-50.779-44.871 1.0063.07 N ATOM 2 CA VAL B 61 -10.704 -50.802 -44.073 1.00 62.97 C ATOM 3 CB VAL B 61 -10.398 -52.180-43.434 1.00 62.87 C ATOM 4 CG1 VALB 61 -11.661 -52.805 -42.886 1.00 62.90 C ATOM 5 CG2VALB 61 -9.741 -53.104-44.425 1.00 62.98 C ATOM 6 C VAL B 61 -9.549 -50.335 -44.954 1.00 63.00 C ATOM 7 0 VALB 61 -9.521 -50.612-46.161 1.00 63.16 0 ATOM 1 N LEU B 62 -8.615 -49.599-44.360 1.00 62.78 N ATOM 2 CA LEUB 62 -7.493-49.062-45.114 1.0062.54 C ATOM 3 CB LEU B 62 -7.429 -47.541 -44. 987 1.00 62.51 C ATOM 4 CG LEU B 62 -6.260 -46.869 -45.715 1.00 62.61 C ATOM 5 CDI LEU B 62 -6.657 -45.506 -46.263 1.00 62.58 C ATOM 6 CD2 LEU B 62 -5.045 -46.751 -44.806 1.00 62.83 C ATOM 7 C LEU B 62 -6.184 -49.675 -44.665 1.00 62.41 C ATOM 8 0 LEU B 62 -5.880-49.715-43.473 1.00 62.37 0 ATOM I N VAL B 63 -5.407 -50.148 -45.631 1.00 62.32 N ATOM 2 CA VALB 63 -4.108-50.731 -45.339 1.00 62.19 C ATOM 3 CB VALB 63 -3.968-52.128-45.956 1.0062.15 C ATOM 4 CG1 VAL B 63 -2.708 -52.787 -45.447 1.00 62.50 C ATOM 5 CG2VALB 63 -5.184-52.982-45.618 1.0061.99 C ATOM 6 C VAL B 63 -2.98 1 -49.830 -45.837 1.00 62.07 C ATOM 7 0 VALB 63 -2.860-49.577-47.036 1.00 61.99 0 ATOM 1 N ALA B 64 -2.166-49.344-44.905 1.00 62.00 N ATOM 2 CA ALA B 64 -1.062 -48.446 -45.232 1.00 61.93 C ATOM 3 CB ALA B 64 -1.355 -47. 043 -44.742 1.00 61.86 C ATOM 4 C ALA B 64 0.234 -48.949 -44.626 1.00 61.87 C ATOM 5 0 ALA B 64 0.225 -49.792 -43.737 1.00 62.00 0 ATOM 1 N GLY B 65 1.347 -48.418 -.45.106 1.00 61.82 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 0 GLY B 65 3.272 -47.955 -46.765 1.00 62.42 0 *, 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 1.00 62.73 C ATOM 3 CB GLNB 66 7.199-47.616-45.816 1.0062.81 C 45 ATOM 4 CG GLNB 66 7.642-48.190-44.496 1.00 63.71 C ATOM S CD GLNB 66 8.746-47.355-43.871 1.0064.68 C * : ATOM 6 OE1 GLN B 66 9.595 -46.794 -44.578 1.0065.17 0 ATOM 7 NE2 GLN B 66 8.740 -47.264 -42.543 1.00 65.07 N * ** ATOM 8 C GLNB 66 6.260-49424-47.306 1.0062.78 C ATOM 9 0 GLNB 66 5.623 -50.470-47.198 1.00 62.88 0 * ATOM 1 N TYRB 67 7.237-49.258-48.189 1.0062.88 N *.: ATOM 2 CA I'YR B 67 7.528 -50.258 -49.210 1.00 62.98 C ATOM 3 CB TYR B 67 8.730 -49.831 -50.058 1.00 63.32 C ATOM 4 CO TYRB 67 8.484-48.619-50.930 1.0063.88 C ATOM 5 CDI TYR B 67 9.395 -47.566 -50.965 1.0064.41 C ATOM 6 CEI TYRB 67 9.176-46.451 -51.771 1.0064.56 C ATOM 7 CZ TYRB 67 8.030-46.381 -52.547 1.00 64.29 C ATOM 8 OH TYRB 67 7.805-45.278-53.346 1.0064.28 0 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 TYR B 67 7.772 -51.655 -48.651 1.00 62.84 C ATOM 12 0 TYRB 67 8.447-51.824-47.637 1.0062.73 0 ATOM I N SER B 68 7.207 -52.648 -49.333 1.00 62.73 N ATOM 2 CA SERB 68 7460-54.060-49.053 1.0062.58 C ATOM 3 CB SER B 68 8.900 -54.438 -49.424 1.00 62.63 C ATOM 4 00 SER B 68 9.161 -54.184 -50.797 1.00 62.93 0 ATOM 5 C SERB 68 7.172-54.439-47.611 1.0062.40 C ATOM 6 0 SERB 68 7.851 -55.288-47.035 1.00 62.68 0 ATOM I N THRB 69 6.162-53.814-47.025 1.0061.97 N ATOM 2 CA THR B 69 5.803 -54.129 -45.658 1.00 61.63 C ATOM 3 CB THRB 69 5.233-52907-44.930 1.0061.73 C ATOM 4 001 THRB 69 5.877-51.719-45.403 1.00 61.90 0 ATOM 5 CG2THRB 69 5.474-53.030-43.448 1.0062.25 C ATOM 6 C THRB 69 4.788 -55.266 -45.651 1.00 61.26 C ATOM 7 0 THR B 69 4.469 -55.832 -44.607 1.00 61.25 0 ATOM 1 N GLY B 70 4.278 -55.596 -46.830 1.00 60.94 N ATOM 2 CA GLY B 70 3.357 -56. 7 15 -46.973 1.00 60.52 C ATOM 3 C GLY B 70 1.888 -56.350 -46.949 1.00 60. 22 C ATOM 4 0 GLY B 70 1.065 -57.156 -46.549 1.00 60.21 0 ATOM I N LYS B 71 1.550 -55.138 -47.376 1.00 60.02 N ATOM 2 CA LYS B 71 0.156 -54.712 -47.405 1.00 59.94 C ATOM 3 CB LYS B 71 0.060 -53.272 -47.897 1.00 59.83 C ATOM 4 CG LYS B 71 0.543 -52.237 -46.903 1.00 59.55 C ATOM 5 CD LYS B 71 0.862 -50.922 -47.596 1.00 58.81 C ATOM 6 CE LYS B 71 2.258 -50.955 -48.191 1.00 58 14 C ATOM 7 NZ LYSB 71 2.389-50.011 -49.321 1.00 57.62 N ATOM 8 C LYSB 71 -0.670-55.620-48.313 1.0060.06 C ATOM 9 0 LYSB 71 -1.656-56.244-47.885 1.0060.25 0 ATOM 1 N THR B 72 -0.254 -55.686-49.574 1.00 60.04 N ATOM 2 CA THR B 72 -0.936 -56.494 -50.569 1.00 60.09 C ATOM 3 CB THR B 72 -0.198 -56.451 -5 1.928 1.00 60.10 C ATOM 4 OG1 THR B 72 0. 276 -55.121 -52.180 1.00 60.02 0 ATOM 5 CG2 THR B 72 -1.126 -56.878 -53.059 1.00 60.05 C ATOM 6 C THRB 72 -1.048 -57.931 -50.069 1.00 60.14 C ATOM 7 0 THRB 72 -2.105 -58.562 -50.181 1.00 60.40 0 ATOM 1 N SER B 73 0.043 -58.438 -49.501 1.00 60.12 N ATOM 2 CA SER B 73 0.054 -59.783 -48.944 1. 00 60.22 C : ... 40 ATOM 3 CB SER B 73 1.436 -60.131 -48.381 1.00 60.26 C ATOM 4 OG SERB 73 2.380-60.336-49.421 1.0059.98 0 ATOM 5 C SERB 73 -1.001 -59.901 -47.856 1.00 60.19 C ATOM 6 0 SER B 73 -1.798 -60.825 -47.841 1. 00 60.56 0 ATOM I N PHE B 74 -0.996 -58.942 -46.947 1.00 60.20 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 1.00 60.03 C * ATOM 4 CG PHE B 74 -2.723 -57.383 -43.983 1.00 60.15 C ATOM 5 CD1 PHE B 74 -2.5 13 -58.066 -42.800 1.00 60.37 C : .. ATOM 6 CE1 PHE B 74 -3.366-57.899 -41.736 1.00 60.41 C ATOM 7 CZ PHE B 74 -4.437-57.033 -41.843 1.00 60.50 C *. : ATOM 8 CE2 PHE B 74 -4.648 -56.342 -43.013 1.00 60.12 C * ATOM 9 CD2 PHE B 74 -3.797 -56.5 17 -44.073 1.00 60.02 C ATOM 10 C PHEB 74 -3.376-59.038-46.397 1.0060.19 C ATOM 11 0 PHE B 74 -4.123 -59.9 13 -45.958 1.00 60.38 0 ATOM 1 N ILE B 75 -3.747 -58.192 -47.351 1.00 60.27 N ATOM 2 CA ILE B 75 -5.099 -58.260 -47.895 1.00 60.40 C ATOM 3 CB ILE B 75 -5.362 -57.13 1 -48.894 1.00 60. 26 C ATOM 4 CG1 ILE B 75 -5.040 -55.781 -48.258 1.00 60.08 C ATOM 5 CDI ILE B 75 -5.166 -54.622 -49.210 1.00 59.79 C ATOM 6 CG2 ILE B 75 -6.805 -57.159 -49.353 1.00 60.22 C ATOM 7 C ILE B 75 -5.350 -59.613 -48.559 1.00 60.71 C ATOM 8 0 ILE B 75 -6.362 -60.278 -48.299 1.00 61.02 0 ATOM I N GLN B 76 -4.415 -60.007 -49.419 1.00 60.91 N ATOM 2 CA GLNB 76 -4.433 -61.311 -50.069 1.00 61.22 C ATOM 3 CB GLN B 76 -3.038 -61.595 -50.620 1.00 61.23 C ATOM 4 CG GLNB 76 -2.935-62.776-51.553 1.0062.03 C ATOM 5 CD GLN B 76 -2.700 -62.353 -52.989 1.00 63.06 C ATOM 6 OEI GLNB 76 -1.909-62.972-53.707 1.00 63.47 0 ATOM 7 NE2 OLN B 76 -3.373 -6 1.282 -53.4 12 1.00 63.36 N ATOM 8 C GLN B 76 -4.792 -62.381 -49.043 1.00 61.30 C ATOM 9 0 GLNB 76 -5.596-63.280-49.294 1.0061.68 0 ATOM 1 N TYR B 77 -4.178 -62.242 -47.874 1.00 61.31 N ATOM 2 CA TYR B 77 -4.286 -63.181 -46.768 1.00 61.46 C ATOM 3 CB TYR B 77 -3.182 -62.874 -45.758 1.00 61.45 C ATOM 4 CG TYRB 77 -3.136-63.776-44.557 1.0061.46 C ATOM 5 CDI TYRB 77 -3.478-63.300-43.300 1.00 61.59 C ATOM 6 CE1 TYR B 77 -3.419 -64.117 -42.185 1.00 61.89 C ATOM 7 CZ TYR B 77 -3.012 -65.428 -42.324 1.0061 81 C ATOM 8 OH TYR B 77 -2.955 -66.244 -41.222 1.00 61.74 0 ATOM 9 CE2 TYR B 77 -2.663 -65.923 -43.565 1.00 61.90 C ATOM 10 CD2 TYR B 77 -2.727 -65.097 -44.671 1.00 61.71 C ATOM 11 C TYR B 77 -5.645 -63.093 -46.092 1.00 61.48 C ATOM 12 0 TYRB 77 -6.213-64.112-45.699 1.0061.51 0 ATOM I N LEU B 78 -6.159 -61.874 -45.947 1.00 61.31 N ATOM 2 CA LEU B 78 -7.491 -61.687 -45.390 1.00 61.65 C ATOM 3 CB LEU B 78 -7.806-60.206 -45.219 1.00 61.70 C ATOM 4 CO LEU B 78 -7.478 -59.629 -43.844 1.00 62.28 C ATOM 5 CDI LEUB 78 -7.621 -58.112-43.859 1.00 62.88 C ATOM 6 CD2 LEU B 78 -8.408 -60.242 -42.813 1.00 62.72 C ATOM 7 C LEUB 78 -8.531 -62.325 -46.287 1.00 61.78 C ATOM 8 0 LEU B 78 -9.488 -62.939 -45.814 1.00 61.79 0 ATOM 1 N LEU B 79 -8.337 -62.181 -47.591 1.00 61.84 N ATOM 2 CA LEU B 79 -9.298 -62.702 -48.542 1.00 62.22 C ATOM 3 CB LEU B 79 -9.254 -61.888 -49.832 1.00 62.29 C ATOM 4 CO LEU B 79 -9.512 -60.386 -49.707 1.00 62.42 C ATOM S CD1 LEU B 79 -9.514 -59.736 -51.083 1.00 62.58 C ATOM 6 CD2 LEU B 79 -10.824 -60. 120 -48.987 1.00 62.69 C :"... 40 ATOM 7 C LEU B 79 -9.047 -64.168 -48.851 1.00 62.47 C ATOM 8 0 LEU B 79 -9.897 -64.833 -49.444 1.00 62.39 0 ATOM I N GLU B 80 -7.883 -64.668 -48.443 1.00 62.76 N ATOM 2 CA GLU B 80 -7.442 -66.00 1 -48.849 1.00 63.58 C *. ATOM 3 CB GLUB 80 -8.137 -67.091 -48.031 1.00 63.72 C ATOM 4 CG GLUB 80 -7.551 -67.293-46.633 1.00 65.58 C ATOM 5 CD GLU B 80 -6.542 -68.443 -46.559 1.00 68.13 C * * ATOM 6 OE1 GLU B 80 -6.912 -69.522 -46.016 1.00 69.12 0 ATOM 7 0E2 GLU B 80 -5.388 -68.278 -47.045 1.00 68.88 0 : .. ATOM 8 C GLUB 80 -7.714-66.180-50.339 1.0063.57 C ATOM 9 0 GLUB 80 -8.206-67.219-50.777 1.00 63.47 0 : ATOM 1 N GLNB 81 -7.399-65.133-51.099 1.00 63.78 N * ATOM 2 CA GLN B 81 -7.586 -65.106 -52.54 1 1.00 63.93 C ATOM 3 CB GLN B 81 -9.062 -64.900-52.890 1.00 63.84 C ATOM 4 CO GLN B 81 -9.347 -64.947 -54.387 1.00 63.39 C ATOM S CD GLN B 81 -10.824 -64.864 -54.707 1.00 62.75 C ATOM 6 OEIGLNB 81 -11.239-65.199-55.812 1.0063.13 0 ATOM 7 NE2GLNB 81 -11.627-64.417-53.746 1.00 62.73 N ATOM 8 C GLN B 81 -6.739 -63.987 -53 152 1.00 64.17 C ATOM 9 0 GLN B 81 -6 526 -62.952 -52.522 1.00 64.15 0 ATOM I N GLU B 82 -6.257 -64.204 -54.375 1.00 64 47 N ATOM 2 CA GLUB 82 -5.416-63.227-55.065 1.0064.72 C ATOM 3 CB GLU B 82 -4.583 -63.910 -56.160 1.00 64.74 C ATOM 4 CG GLU B 82 -3.346 -63.123 -56.595 1.00 65.36 C ATOM 5 CD GLU B 82 -2.097 -63.996 -56.753 1.00 66.14 C ATOM 6 OEI GLU B 82 -2.185 -65.080 -57.373 1.00 66.18 0 ATOM 7 OE2GLUB 82 -1.020-63.591.56.255 1.00 66.28 0 ATOM 8 C GLU B 82 -6.232 -62.057 -55.631 1.00 64.81 C ATOM 9 0 GLUB 82 -7.363 -62.233 -56.085 1.00 64.77 0 ATOM I N VALB 83 -5.652-60.862-55.588 1.0064.99 N ATOM 2 CA VAL B 83 -6.325 -59.654 -56.052 1.00 65.07 C ATOM 3 CB VALB 83 -5.794-58.413-55.322 1.0065.06 C ATOM 4 CGI VAL B 83 -6.742 -57.244 -55.511 1.00 65.06 C ATOM 5 CG2 VAL B 83 -5.598 -58.712 -53.847 1.00 64.87 C ATOM 6 C VAL B 83 -6.138 -59.465 -57.556 1.00 65.23 C ATOM 7 0 VALB 83 -5.009 -59.404 -58.040 1.00 65.10 0 ATOM 1 N PRO B 84 -7.252 -59.365 -58.297 1.00 65.51 N ATOM 2 CA PRO B 84 -7.253 -59.247 -59.752 1.00 65.77 C ATOM 3 CB PRO B 84 -8.656 -58.723 -60.05 1 1.00 65.66 C ATOM 4 CG PRO B 84 -9.490 -59.3 15 -58.983 1.00 65.56 C ATOM 5 CD PRO B 84 -8.620 -59.365 -57.750 1.00 65.53 C ATOM 6 C PRO B 84 -6.206 -58.275 -60.284 1.00 66.15 C ATOM 7 0 PRO B 84 -5.487 -58.603 -61.225 1.00 66.22 0 ATOM I N GLY B 85 -6.116-57.094-59.685 1.00 66.61 N ATOM 2 CA GLY B 85 -5.194 -56.072 -60.165 1.00 67.21 C ATOM 3 C GLYB 85 -3.847-56.044-59.464 1.006767 C ATOM 4 0 GLY B 85 -2.820 -55.785 -60.094 1.00 67.61 0 ATOM I N SER B 86 -3.848 -56.313 -58.161 1.00 68.17 N ATOM 2 CA SER B 86 -2.644 -56.150 -57.339 1.00 68.71 C ATOM 3 CB SERB 86 -3.014-55.711 -55.914 1.00 68.74 C ATOM 4 00 SER B 86 -3.020 -54.297 -55.787 1.00 68.90 0 ATOM 5 C SER B 86 -1.725 -57.374 -57.281 1.00 69.01 C ATOM 6 0 SERB 86 -2.054-58.386-56.652 1.0069.11 0 ATOM I N ARG B 87 -0.565 -57.263 -57.927 1.00 69.32 N ATOM 2 CA ARG B 87 0.485 -58.266 -57.801 1.00 69.63 C ATOM 3 CB ARG B 87 1.378 -58.274 -59.044 1.00 69.53 C ATOM 4 CG ARG B 87 0.269 -59.653 -59.740 0.00 50.00 C ATOM 5 CD ARG B 87 0.975 -60.115 -60.993 0. 00 50.00 C : 40 ATOM 6 NE ARG B 87 1.731 -61.343 -60.776 0.00 50.00 N ATOM 7 CZ ARG B 87 1.237 -62.572 -60.852 0.00 50.00 C ATOM 8 NH1 ARGB 87 2.033 -63.609-60.623 0.00 50.00 N ATOM 9 NH2 ARG B 87 -0.028 -62.779 -61.180 0.00 50.00 N *** ATOM 10 C ARG B 87 1.319 -57.999 -56.544 1.00 69.92 C ATOM 11 0 ARGB 87 1.025-57.085-55.771 1.00 69.93 0 ATOM I N VALB 88 2.357-58.803-56.344 1.007032 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 CG1 VALB 88 3.838 -59.875 -53.028 1.00 70.52 C ATOM S CG2 VAL B 88 2.102 -60.855 -54.544 1.00 70.76 C *. ATOM 6 C VAL B 88 4.664-59.035 -55.538 1.00 70.97 C * ATOM 7 0 VALB 88 4.906-59.997-56.272 1.0071.03 0 ATOM I N GLY B 89 5.619 -58.255 -55.040 1.00 71.28 N ATOM 2 CA GLY B 89 7.020 -58.471 -55.389 1.00 71.78 C ATOM 3 C GLYB 89 8.015-57.882-54.410 1.0072.17 C ATOM 4 0 GLY B 89 7.627 -57.243 -53.432 1.00 72.08 0 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 1.00 72.92 C ATOM 3 CB PRO B 90 11.655 -58.25 1 -54.493 1.00 72. 90 C ATOM 4 CG PROB 90 11.259-58.441 -55.924 1.00 72.85 C ATOM 5 CD PROB 90 9.797-58.771 -55.896 1.00 72.65 C ATOM 6 C PRO B 90 10.523 -56.126 -53. 765 1.00 73.27 C ATOM 7 0 PRO B 90 9.958 -55.499 -52.866 1.00 73.27 0 ATOM I 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 GLU B 91 12.405 -53.714 -55. 891 1.00 74.13 C ATOM 4 Co GLU B 91 13.840 -53.941 -55.421 1.00 74.32 C ATOM 5 CD GLU B 91 14.0 10 -53.220 -53.305 0.00 50.00 C ATOM 6 OEI GLU B 91 15.017 -53.953 -53.217 0.00 50.00 0 ATOM 7 OE2 GLU B 91 13.3 12 -52.915 -52.308 0.00 50.00 0 ATOM 8 C GLUB 91 9.971 -53.526-55.270 1.00 74.25 C ATOM 9 0 GLU B 91 9.245 -54.168 -56.034 1.00 74.34 0 ATOM 1 N PROB 92 9.626-52.323-54.759 1.0074.34 N ATOM 2 CA PRO B 92 8.362 -5 1.615 -54.984 1.00 74.34 C ATOM 3 CD PRO B 92 8.766 -50.133 -54.870 1.00 74.35 C ATOM 4 CG PRO B 92 10.183 -50 122 -54.284 1.00 74.33 C ATOM 5 CD PRO B 92 10.5 13 -5 1.535 -53.889 1.00 74.39 C ATOM 6 C PRO B 92 7.728 -51.884 -56.354 1. 00 74.33 C ATOM 7 0 PRO B 92 8.391 -51.737 -57.391 1.00 74.31 0 ATOM 1 N T} IR B 93 6.448.52.260 -56.348 1.00 74.15 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 1.00 74.06 C ATOM 4 001 THRB 93 4.909 -54.490 -56.194 1.00 73.87 0 ATOM 5 CG2 THR B 93 6.469 -55.058 -57.997 1.00 74.23 C ATOM 6 C THR B 93 4.532 - 5 1.770 -57.907 1.00 73.59 C ATOM 7 0 THRB 93 4.528 -51.057 -58.917 1.00 73.58 0 ATOM 1 N THRB 94 3.507-51.839-57.055 1.0073.13 N ATOM 2 CA THE. B 94 2.259 -5 1.097 -57.264 1.00 72.66 C ATOM 3 CB THE. B 94 1.120 -51.644 -56.357 1.00 72.80 C ATOM 4 001 THE. B 94 1.526 -51.598 -54.978 1.00 72. 65 0 ATOM 5 CG2 THR B 94 0.780 -53.088 -56.729 1.00 72.95 C ATOM 6 C THR B 94 2.442 -49.593 -57.020 1.00 72.18 C ATOM 7 0 THE. B 94 3.059 -49.188 -56.033 1.00 72.21 0 ATOM 1 N ASP B 95 1.900 -48.767 -57.914 1.00 71.45 N ATOM 2 CA ASP B 95 2.119 -47.320 -57.839 1.00 70.73 C ATOM 3 CB ASP B 95 2.915 -46.839 -59.063 1.00 70.79 C ATOM 4 CO ASP B 95 3.164.46.932 -59. 646 0.00 50.00 C : .*. 40 ATOM 5 OD1 ASP B 95 2.550 -47.842 -60.280 0.00 50. 00 0 ATOM 6 OD2ASPB 95 3.842-46.098-60.301 0.0050.00 0 ATOM 7 C ASP B 95 0.835 -46.498 -57.697 1.00 70.16 C ATOM 8 0 ASP B 95 0.762 -45.367 -58. 187 1.00 70.07 0 *... ATOM I N CYS B 96 -0.165 -47.052.57.014 1.00 69.46 N ATOM 2 CA CYS B 96 -1.433 -46.343 -56.840 1.00 68.81 C ATOM 3 CB CYSB 96 -2.198-46.296-58.165 1.00 68.91 C * ATOM 4 So cys B 96 -2.997 -47.853 -58.603 1.00 69.45 S ATOM 5 C CYS B 96 -2.334 -46.935 -55.752 1.00 68.20 C : *. ATOM 6 0 CYS B 96 -1.935 -47.834 -55.013 1.00 68.12 0 ATOM I N PHEB 97 -3.553-46.408-55.668 1.00 67.48 N *. : ATOM 2 CA PHEB 97 -4.549-46.870-54.713 1.0066.69 C * ATOM 3 CB PHE B 97 -5.414 -45.706 -54.228 1.0066.64 C ATOM 4 CO PHEB 97 -4.672-44.689-53.416 1.0066.32 C ATOM 5 CDI PHE B 97 -3.822 -43.780 -54.025 1.00 66.08 C ATOM 6 CE1 PHE B 97 -3.140 -42.841 -53.281 1.00 65.88 C ATOM 7 CZ PHEB 97 -3.311 -42.793 -51.915 1.00 66.18 C ATOM 8 CE2 PHE B 97 -4.162 -43.688 -51.295 1.00 66. 18 C ATOM 9 CD2 PHE B 97 -4.839 -44.627 -52.045 1.00 66.18 C ATOM 10 C PHE B 97 -5 450 -47.902 -55.365 1.00 66.32 C ATOM 11 0 PHEB 97 -6.032-47.657-56.421 1.0066.17 0 ATOM 1 N VAL B 98 -5.568 -49.056 -54.726 1.00 65.88 N ATOM 2 CA VALB 98 -6.434-50.108-55.218 1.0065.43 C ATOM 3 CB VALB 98 -5.678-51438-55.357 10065.36 C ATOM 4 CGI VALB 98 -6.570-52.488-55.991 1.0065.18 C ATOM 5 CG2 VAL B 98 -4.413 -51.243 -56.171 1.00 65.13 C ATOM 6 C VALB 98 -7.590-50.287-54.251 1.0065.26 C ATOM 7 0 VAL B 98 -7.3 89 -50.620 -53.086 1.00 65.27 0 ATOM I N ALA B 99 -8.801 -50.050 -54.732 1.00 65.07 N ATOM 2 CA ALA B 99 -9.978 -50.225 -53.905 1.00 65.02 C ATOM 3 CB ALA B 99 -11.021 -49.179 -54.242 1.00 65. 00 C ATOM 4 C ALAB 99 -10.539-51.619-54.108 1.00 65.03 C ATOM 5 0 ALAB 99 -11.338-51.847-55.012 1.0065.09 0 ATOM 1 N VALB 100 -10.109 -52.555 -53.274 1.00 65.12 N ATOM 2 CA VALB 100 -10.605-53.922-53.363 1.00 65.24 C ATOM 3 CB VAL B 100 -9.693 -54.914 -52.616 1.00 65.20 C ATOM 4 CGI VAL B 100 -8.233 -54.672 -52.969 1.00 65.10 C ATOM 5 CG2 VAL B 100 -10.100 -56.345 -52.931 1.00 65.15 C ATOM 6 C VALB 100 -12.012-53.995-52.786 1.00 65.39 C ATOM 7 0 VALB 100 -12.199-53.938-51.570 1.00 65.48 0 ATOM I N METB 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 METB 101 -15.100-52.850-53.572 1.0065.79 C ATOM 4 CG MET B 101 -14.752 -52.294 -54.941 1.00 65.81 C ATOM 5 SD METB 101 -15.844-50.959-55.463 1.00 65.65 5 ATOM 6 CE METB 101 -15.750-49.849-54.058 1.00 65.57 C ATOM 7 C METB 101 -15.110-55.317-53. 917 1.0066.02 C ATOM 8 0 MET B 101 -14.552 -55.978 -54.790 1.00 66.05 0 ATOM 1 N HISB 102 -16.350-55.559-53.514 1.00 66.39 N ATOM 2 CA HIS B 102 -17.107 -56.667 -54.073 1.00 66.80 C ATOM 3 CB HISB 102 -18.418-56.881 -53.314 1.00 66.73 C ATOM 4 CG HISB 102 -19.129-58.142-53.694 1.0066.79 C ATOM 5 NDI HIS B 102 -18.664 -59.392 -53.343 1.00 66.68 N ATOM 6 CE1 HIS B 102 -19.483 -60.313 -53.819 1.00 66.49 C ATOM 7 NE2 HIS B 102 -20.46 1 -59. 706 -54.469 1.00 66.63 N ATOM 8 CD2 HIS B 102 -20.262 -58.347 -54.408 1.00 66.78 C ATOM 9 C HIS B 102 -17.373 -56.459 -55.561 1.00 67.13 C ATOM 10 0 HIS B 102 -16.949 -55.465 -56.145 1.00 67.23 0 ATOM 1 N GLY B 103 -18.072 -57.408 -56.168 1.00 67.46 N *.s. ATOM 2 CA GLYB 103 -18.379-57341-57.583 1.0067.99 C ATOM 3 C GLYB 103 -18.712-58.729-58.069 1.006839 C ATOM 4 0 GLY B 103 -18.227 -59.715 -57.519 1.00 68.41 0 ATOM 1 N GLUB 104 -19.545-58.812-59.099 1.00 68.82 N *as 45 ATOM 2 CA GLU B 104 -19.993 -60.105 -59.591 1.00 69.31 C : ATOM 3 CB GLUB 104 -21.329-59.968-60.333 1.0069.45 C * ATOM 4 CG GLU B 104 -21.933 -61.291 -60.806 1.00 70.31 C ATOM 5 CD GLU B 104 -21.826 -62.411 -59.768 1.00 71.40 C : .. ATOM 6 OE1 GLU B 104 -21.442 -62.136 -58.606 1.00 71.64 0 ::. 50 ATOM 7 OE2GLUB 104 -22.124-63.575-60.123 1.0071.78 0 ATOM 8 C GLU B 104 -18.934 -60.790 -60.460 1.00 69.42 C ATOM 9 0 GLU B 104 -18.745 -62.007 -60.384 1.00 69. 49 0 ATOM 1 N THRB 105 -18.237 -60.003 -61.272 1.00 69.53 N ATOM 2 CA THRB 105 -17.191-60.542-62.131 1.0069.56 C ATOM 3 CB THR. B 105 -17.345 -60. 049 -63.590 1.00 69.61 C ATOM 4 OGI THR B 105 -16.5 17 -60.837 -64.455 1.00 69.65 0 ATOM 5 CG2THRB 105 -16.957-58.573-63.713 1.00 69.72 C ATOM 6 C THRB 105 -15.805-60.172-61.606 1.00 69.52 C ATOM 7 0 THR B 105 -15.611 -59.099 -61.030 1.00 69.53 0 ATOM 1 N GLU B 106 -14.849 -61.075 -61.792 1.00 69.46 N ATOM 2 CA GLU B 106 -13.460 -60.778 -61.477 1.00 69.46 C ATOM 3 CB GLU B 106 -12.637 -62.066 -61.400 1.00 69.51 C ATOM 4 CG GLU B 106 -12.955 -62.949 -60.198 1.0069 53 C ATOM 5 CD GLU B 106 -12.289 -64.318 -60.277 1.00 69.39 C ATOM 6 OEI GLUB 106 -11.990-64.754-61.456 1.00 69.37 0 ATOM 7 0E2 GLU B 106 -12.062 -64.963 -59.165 1.00 68.93 0 ATOM 8 C GLUB 106 -12.899-59.863-62.557 1.00 69.46 C ATOM 9 0 GLU B 106 -13.145 -60.073 -63.743 1.00 69.46 0 ATOM I N GLY B 107 -12.150 -58.845 -62.148 1.00 69. 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 1.00 69.52 C ATOM 4 0 GLYB 107 -11.271 -56.407-61.253 1.00 69.51 0 ATOM I N TI-JR B 108 -10.989 -55.562 -63.322 1.00 69.51 N ATOM 2 CA THR B 108 -10.595 -54.240 -62.848 1.00 69.49 C ATOM 3 CB THRB 108 -9.073 -54.020-62.975 1.0069.48 C ATOM 4 OG1 THRB 108 -8. 713 -53.964 -64.361 1.00 69.55 0 ATOM 5 CG2THRB 108 -8.298-55.139-62.290 1.00 69.46 C ATOM 6 C THR B 108 -11.287 -53.116 -63.608 1.00 69.49 C ATOM 7 0 ThRB 108 -12.009 -53.354 -64.578 1.00 69.48 0 ATOM 1 N VAL B 109 -11.046 -51.890 -63.150 1.00 69.49 N ATOM 2 CA VAL B 109 -11.563 -50.680 -63.784 1.00 69.46 C ATOM 3 CB VAL B 109 -13.114 -50.660 -63.804 1.00 6947 C ATOM 4 CG1 VAL B 109 -13.632 -49.424 -64.531 1.00 69.54 C ATOM 5 CG2VALB 109 -13.680-50.750-62.389 1.00 69.55 C ATOM 6 C VAL B 109 -11.007 -49.450 -63.056 1.00 69.39 C ATOM 70 VALB 109 -11.153-49.325-61.839 1.0069.42 0 ATOM I N PROB 110 -10.343-48.548-63.799 1.00 69.28 N ATOM 2 CA PRO B 110 -9.693 -47.376 -63.208 1.00 69.20 C ATOM 3 CB PRO B 110 -8.558 -47.076 -64.194 1.00 69.20 C ATOM 4 CG PRO B 110 -9.001 -47.667 -65.506 1.00 69. 19 C ATOM 5 CD PROB 110 -10.153 -48.608 -65.259 1.00 69.25 C ATOM 6 C PRO B 110 -10.598 -46.150 -63.049 1.00 69.09 C ATOM 70 PROB 110 -10.416-45.155-63.752 1.0069.13 0 ATOM I N GLYB 111 -11.548-46.216-62.120 1.0068.96 N ATOM 2 CA GLY B 111 -12.442 -45.089 -6 1.852 1.00 68.85 C ATOM 3 C GLY B 111 -13.484 -44.872 -62.941 1.00 68.81 C ATOM 4 0 GLY B 111 -13.344 -43.965 -63.800 1.00 68.65 0 : *... 40 TER 4 GLYB 111 **** ATOM I

N ASN B 130 -11.159 -31.270 -62.225 1.00 66.96 N * * ** * ATOM 2 CA ASN B 130 -9.886 -30.849 -61.642 1.00 67.00 C ATOM 3 CB ASN B 130 -10.094 -29.640-60.719 1.00 66.96 C ATOM 4 CO ASN B 130 -8.779-29.020-60.264 1.00 66.90 C ATOM 5 ODI ASN B 130 -8.343 -28.004 -60.826 1.0066 78 0 ATOM 6 ND2ASNB 130 -8.136-29.635-59.247 1.00 66.61 N * ATOM 7 C ASN B 130 -9.150 -31.973 -60.895 1.00 67.05 C * ATOM 8 0 ASNB 130 -7.929-32.106-61.015 1. 00 67.08 0 ATOM I N THRB 131 -9.899-32.772-60.132 1.0067.04 N ** * 50 ATOM 2 CA THRB 131 -9.333-33.856-59.307 1.00 66.97 C ATOM 3 CB THRB 131 -10.400-34.450-58.342 1.00 66.99 C ATOM 4 0G1 THRB 131 -10.043 -35.792 -57.984 1.00 66.77 0 ATOM 5 CG2 THR B 131 -11.777 -34.460 -58.998 1.00 67.17 C ATOM 6 C THRB 131 -8.678-34.980-60.126 1.00 66.94 C ATOM 7 0 THRB 131 -8.847-35.054-61.348 1.00 66.93 0 ATOM I N PHE B 132 -7.931 -35.851 -59.444 1.00 66.81 N ATOM 2 CA PHEB 132 -7.174-36.912-60.115 1.006668 C ATOM 3 CB PHE B 132 -5.672 -36.602 -60.088 1.00 66 71 C ATOM 4 CG PHE B 132 -5.315 -35.278 -60.709 1.00 66.79 C ATOM 5 CDI PHEB 132 -4.691 -34.290-59.960 1.0066.90 C ATOM 6 CEI PHE B 132 -4.363 -33.064 -60.532 1.00 67.27 C ATOM 7 CZ PHE B 132 -4.666 -32.8 14 -61.865 1.00 67.02 C ATOM 8 CE2PHEB 132 -5.293-33.791 -62.620 1.00 67.01 C ATOM 9 CD2 PHE B 132 -5.616 -35.015 -62.041 1.00 66.90 C ATOM 10 C PHEB 132 -7.447-38.316-59.563 1.00 66.58 C ATOM 11 0 PHEB 132 -7.146-38.620-58.404 1.00 66.52 0 ATOM I N LEUB 133 -8.016-39.165-60.417 1.00 66.41 N ATOM 2 CA LEUB 133 -8.370-40.539-60.064 1.00 66.14 C ATOM 3 CB LEU B 133 -9.874 -40.769 -60.256 1.00 66.19 C ATOM 4 CG LEU B 133 -10.882 -40.435 -59.148 1.00 66.22 C ATOM 5 CDI LEU B 133 -10.589 -39.104 -58.467 1.00 66.32 C ATOM 6 CD2 LEU B 133 -12.304 -40.457 -59.704 1.00 66.13 C ATOM 7 C LEUB 133 -7.601 -41.546-60.915 1.00 65.93 C ATOM 8 0 LEUB 133 -7.829-42.751 -60.820 1.00 65.82 0 ATOM I N ASN B 134 -6.705 -41.051 -61.765 1.00 65.76 N ATOM 2 CA ASNB 134 -5.909-41.930-62.615 1.00 65.55 C ATOM 3 CB ASN B 134 -5.234 -41.148 -63.746 1.00 65.55 C ATOM 4 CG ASNB 134 -4.640-42.057-64.813 1.00 65.49 C ATOM 5 OD1 ASN B 134 -3.814 -41.627 -65.619 1.00 65.41 0 ATOM 6 ND2ASNB 134 -5.060-43.319-64.821 1.0065.26 N ATOM 7 C ASN B 134 -4.873 -42.672 -61.783 1.00 65.39 C ATOM 8 0 ASNB 134 -4.324-43.690-62.209 1.0065.43 0 ATOM I N ARG B 135 -4.6 12 -42.146 -60.590 1.00 65.09 N ATOM 2 CA ARGB 135 -3.787-42.836-59.617 1.00 64.81 C ATOM 3 CB ARGB 135 -2.997-41.831 -58.777 1.00 64.75 C ATOM 4 CG ARG B 135 -2.260 -40.714 -59.006 0.00 50.00 C ATOM 5 CD ARG B 135 -1.921 -39.538 -58.193 0.00 50.00 C ATOM 6 NE ARG B 135 -2.823 -38.615 -57.663 0.00 50. 00 N ATOM 7 CZ ARG B 135 -2.891 -37.354 -57.365 0.00 50.00 C ATOM 8 N}11 ARG B 135 -3.876 -36.980 -56.508 0.00 50.00 N ATOM 9 NIH2 ARG B 135 -2.196 -36.373 -57.896 0.00 50.00 N ATOM 10 C ARG B 135 -4.713 -43.669 -58.740 1.0064.65 C ATOM 11 0 ARGB 135 -4.412-43.944-57.578 1.0064.66 0 ATOM I N PHE B 136 -5.844 -44.072 -59.314 1.00 64.44 N ATOM 2 CA PHE B 136 -6.877 -44.795 -58.578 1.00 64.19 C ATOM 3 CB PHE B 136 -7.996 -43.832 -58.178 1.00 64.24 C ATOM 4 CG PHE B 136 -8.564 -44.089 -56.815 1.00 64.14 C *** 40 ATOM 5 CD1 PHEB 136 -8.404-43.155-55.802 1.0064.00 C ATOM 6 CE1 PHEB 136 -8.924-43.377-54.546 1.0064.15 C ATOM 7 CZ PHE B 136 -9.611 -44.548 -54.286 1.00 64.46 C ATOM 8 CE2 PHE B 136 -9.777 -45.491 -55.290 1.00 64.42 C ATOM 9 CD2 PHE B 136 -9.256 -45.257 -56.545 1.00 64.17 C ATOM 10 C PHE B 136 -7.459 -45.939-59.408 1.00 63.99 C * ATOM 11 0 PHE B 136 -8.050 -45.718 -60.469 1.00 63.97 0 ATOM 1 N METB 137 -7.293-47.160-58.911 1.0063.68 N ATOM 2 CA METB 137 -7.801-48.347-59.586 1.00 63.43 C ATOM 3 CB METB 137 -6.665-49.343-59.828 1.00 63.62 C * 50 ATOM 4 CG METB 137.5.684-48.929-60.916 1.00 64.35 C ATOM 5 SD MET B 137 -6.180 -49.495 -62.559 1.00 66.23 S ATOM 6 CE MET B 137 -6.043 -5 1.275 -62.348 1.00 65.88 C ATOM 7 C METB 137 -8.884 -49.000 -58.741 1.00 63.01 C ATOM 8 0 METB 137 -8.986-48.735-57.544 1.00 63.09 0 ATOM 1 N CYSB 138 -9.688-49.857-59.362 1.00 62.44 N ATOM 2 CA CYS B 138 -10.732 -50.576-58.640 1.00 61.94 C ATOM 3 CB CYS B 138 -12.095 -49.918 -58.858 1.00 62.03 C ATOM 4 SG CYSB 138 -13.490-50.936-58.322 1.00 62.33 S ATOM 5 C CYSB 138.10.795-52.041 -59.046 1.0061.48 C ATOM 6 0 CYSB 138 -10.922-52.365-60.228 1.00 61.39 0 ATOM 1 N ALA B 139 -10.711 -52.921 -58.055 1.00 60.93 N ATOM 2 CA ALA B 139 -10.780 -54.357 -58.291 1.00 60.47 C ATOM 3 CB ALA B 139 -9.544 -55.046 -57.739 1.00 60.46 C ATOM 4 C ALAB 139 -12.041-54.939-57.666 1.0060.13 C ATOM 5 0 ALA B 139 -12.487 -54.485 -56.612 1.00 60.12 0 ATOM I N GLN B 140 -12.613 -55.942 -58.324 1.00 59.68 N ATOM 2 CA GLN B 140 -13.850 -56.562 -57.868 1.00 59.22 C ATOM 3 CB GLN B 140 -15.013 -56.145 -58.765 1.00 59.22 C ATOM 4 CG GLNB 140 -15.223-54.656-58.876 1.00 59.09 C ATOM 5 CD GLN B 140 -16.449 -54.321 -59.685 1.005909 C ATOM 6 OE1 GLNB 140 -17.272 -55.192 -59.967 1.00 59.44 0 ATOM 7 NE2 GLN B 140 -16.580 -53.058 -60.068 1.00 59.05 N ATOM 8 C GLNB 140 -13.731 -58.074-57.908 1.00 58.94 C ATOM 9 0 GLNB 140 -13.091 -58.624-58.803 1.00 58.94 0 ATOM 1 N LEU B 141 -14.360 -58.747 -56.950 1.00 58.55 N ATOM 2 CA LEU B 141 -14.387 -60.207 -56.964 1.00 58.30 C ATOM 3 CB LEU B 141 -12.98 1 -60.785 -56.744 1.00 58.30 C ATOM 4 CG LEUB 141 -12.230-60.539-55.433 1.00 58.25 C ATOM S CD1 LEUB 141 -10.894-61.267-55.464 1.00 58.11 C ATOM 6 CD2 LEU B 141 -12.024 -59.056 -55.161 1.00 58.38 C ATOM 7 C LEUB 141 -15.390-60.810-55.982 1.00 58.06 C ATOM 8 0 LEU B 141 -15.453 -60.403 -54.825 1.00 58.07 0 ATOM I N PRO B 142 -16.181 -61.788 -56.454 1.00 57.87 N ATOM 2 CA PRO B 142 -17.163 -62.505 -55.644 1.00 57.70 C ATOM 3 CB PROB 142 -17.717-63.554-56.611 1.0057.74 C ATOM 4 CG PRO B 142 -16.719 -63.635 -57.723 1.00 57.78 C ATOM 5 CD PRO B 142 -16.164 -62.265 -57.846 1.00 57.80 C ATOM 6 C PROB 142 -16.499-63.187-54.461 1.00 57.59 C ATOM 7 0 PROB 142 -15.712-64.109-54. 642 1.00 57.61 0 ATOM 1 N ASNB 143 -16.827-62.729-53.258 1.00 57.52 N ATOM 2 CA ASN B 143 -16.140 -63.152 -52.046 1.00 57.41 C ATOM 3 CB ASN B 143.14.667 -62.745 -52.127 1.00 57.34 C ATOM 4 CG ASN B 143 -13.903 -63.022 -50.846 1.00 57.28 C ATOM 5 OD1 ASN B 143 -14.460 -62.987 -49.747 1.00 57.32 0 ATOM 6 ND2 ASN B 143 -12.609 -63.281 -50.982 1.00 56.70 N ATOM 7 C ASNB 143 -16.814-62.516-50.833 1.00 57.47 C ATOM 8 0 ASN B 143 -16.943 -61.295 -50.759 1.00 57.41 0 : .. 40 ATOM I N GLNB 144 -17.237-63.350-49.885 1.00 57.56 N **** ATOM 2 CA GLN B 144 -18.063 -62.908 -48.754 1.00 57.72 C * * **** ATOM 3 CB GLN B 144 -18.273 -64.055 -47.773 1.00 57.81 C ATOM 4 CG GLN B 144 -18.601 -65.378 -48.416 1.00 58.02 C ATOM 5 CD GLNB 144 -18.968-66.419-47.386 1.0058.57 C ATOM 6 OE1 GLN B 144 -19.865 -66.207 -46.566 1.00 58.64 0 ATOM 7 NE2GLNB 144 -18.274 -67.553 -47.417 1.00 58.83 N * ATOM 8 C GLNB 144 -17.496-61.713 -47.992 1.00 57.73 C ATOM 9 0 GLNB 144 -18.229-60.782-47.618 1.00 57.88 0 ::. ATOM 1 N VALB 145 -16.193-61.756-47.740 1.0057.64 N ** * 50 ATOM 2 CA VALS 145 -15.537-60.663-47.053 1.00 57.55 C ATOM 3 CS VALB 145 -14.015-60.834-47.034 1.00 57.60 C ATOM 4 CGI VALB 145 -13.649 -62.269 -46.694 1.00 57.62 C ATOM 5 CG2VALB 145 -13.391 -59.867-46.039 1.00 57.54 C ATOM 6 C VALB 145 -15.896-59.369-47.760 1.00 57.47 C ATOM 7 0 VALS 145 -16.252-58.386-47.119 1.00 57.53 0 ATOM 1 N LEU B 146 -15.825 -59.386 -49.086 1.00 57.46 N ATOM 2 CA LEU B 146 -16.195 -58.222 -49.882 1.00 57.59 C ATOM 3 CB LEUB 146 -15.718-58.367-51.330 1.0057.59 C ATOM 4 CG LEU B 146 -14.250 -58.045 -5 1.620 1.00 57.56 C ATOM 5 CDI LEUB 146 -13.770-56.879-50.764 1.00 57.23 C ATOM 6 CD2 LEU B 146 -13.382 -59.266 - 5 1.394 1.00 57.83 C ATOM 7 C LEU B 146 -17.697 -57.934 -49.837 1.00 57.65 C ATOM 8 0 LEU B 146 -18.135 -56.840 -50.185 1.00 57.62 0 ATOM 1 N GLU B 147 -18.485 -58.917 -49.417 1.00 57.74 N ATOM 2 CA GLUB 147 -19.896-58.681 -49.164 1.00 57.96 C ATOM 3 CB GLU B 147 -20.652 -59.994 -48,955 1.00 57.87 C ATOM 4 CG GLU B 147 -20.690 -60.912 -50.158 1.00 58.25 C ATOM 5 CD GLU B 147 -2 1.327 -62.253 -49.835 1.00 58.44 C ATOM 6 OEI GLUB 147 -21.131 -63.217-50.612 1.00 58.79 0 ATOM 7 OE2GLUB 147 -22.020-62.343-48.797 1.00 59.30 0 ATOM 8 C GLUB 147 -20.020-57.827-47. 914 1.00 57.91 C ATOM 9 0 GLU B 147 -20.766 -56.850 -47.887 1.00 58.03 0 ATOM I N SERB 148 -19.281 -58.197-46.874 1.00 57.86 N ATOM 2 CA SERB 148 -19.375 -57.474 -45.609 1.00 57.89 C ATOM 3 CB SERB 148 -18.770-58.296-44.474 1.00 57.92 C ATOM 4 OG SERB 148 -19.358-59.582-44.412 1.00 58.15 0 ATOM 5 C SER B 148 -18.720 -56.091 -45.661 1.00 57.91 C ATOM 6 0 SERB 148 -19.316-55.099-45.242 1.005801 0 ATOM 1 N ILE B 149 -17.495 -56.031 -46.175 1.00 57.82 N ATOM 2 CA ILE B 149 -16.716 -54.795 -46.184 1.00 57.70 C ATOM 3 CB ILE B 149 -15.661 -54.802 -45.065 1.00 57.63 C ATOM 4 CGL ILE B 149 -14.680 -55.962 -45.263 1.00 57.21 C ATOM 5 CDI ILE B 149 -13.5 12 -55.946-44.303 1.00 56.31 C ATOM 6 CG2 ILE B 149 -16.325 -54.901 -43.708 1.00 57.78 C ATOM 7 C ILE B 149 -15.984 -54.602 -47.505 1.00 57.81 C ATOM 8 0 ILEB 149 -16.105-55.418-48.416 1.00 58.00 0 ATOM I N SER B 150 -15.225 -53.5 17 -47.611 1.00 57.80 N ATOM 2 CA SERB 150 -14.308-53.345-48.737 1.00 57.87 C ATOM 3 CB SER B 150 -14.924 -52.492 -49.852 1.00 57.80 C ATOM 4 OG SER B 150 -15.622 -5 1.381 -49.328 1.00 58.07 0 ATOM 5 C SERB 150 -12.972-52.780-48.263 1.00 57.82 C ATOM 6 0 SERB 150 -12.917-51.969-47. 337 1.00 57.84 0 ATOM 1 N ILEB 151 -11.893 -53.233 -48.889 1.00 57.75 N ATOM 2 CA ILEB 151 -10.556-52.907-48.422 1.00 57.75 C ATOM 3 CR ILE B 151 -9.748 -54.178 -48.150 1.00 57.69 C ATOM 4 CG1 ILEB 151 -10.576-55.163-47.328 1.0057.79 C ATOM 5 CDI ILE B 151 -10.080 -56.585 -47.412 1.00 58.36 C ATOM 6 CG2 ILE B 151 -8.446 -53.837 -47.446 1.00 57.61 C **** ATOM 7 C ILEB 151 -9.807-52.074-49.445 1.00 57.80 C ATOM 8 0 ILEB 151 -9.608-52.502-50.581 1.00 57.77 0 ATOM I N ILE B 152 -9.384 -50.882 -49.045 1.00 57.79 N ATOM 2 CA ILE B 152 -8.629-50.046-49.955 1.00 57.80 C ATOM 3 CB ILE B 152 -9.093 -48.573 -49.903 1.00 57.84 C ATOM 4 CGI ILE B 152 -8.002-47.669-49.334 1.00 58.21 C * ATOM 5 CDI ILE B 152 -6.996 -47.2 13 -50.382 1.00 58.80 C ATOM 6 CG2 ILE B 152 -10.418 -48.445 -49.155 1.00 57.83 C ATOM 7 C ILEB 152 -7.133-50.189-49.669 1.00 57.75 C ATOM 8 0 ILE B 152 -6.677 -49.991 -48.543 1.00 57.62 0 ATOM I N ASPB 153 -6.386-50.564-50.702 1.00 57.80 N ATOM 2 CA ASP 8 153 -4.950 -50.776 -50.600 1.00 57.91 C ATOM 3 CB ASP B 153 -4.548 -52.005 -5 1.413 1.00 57.99 C ATOM 4 CG ASPB 153 -3.082-52.358-51.258 1.00 58.23 C ATOM 5 ODI ASP B 153 -2.331 -51.554 -50.664 1.00 58.41 0 ATOM 6 OD2ASPB 153 -2.681 -53.444-51.736 1.00 58.26 0 ATOM 7 C ASPB 153 -4.210-49.549-51.113 1.0058.00 C ATOM 80 ASPB 153 -4.584-48.975-52.137 1.0058.18 0 ATOM I N THRB 154 -3.152 -49.160 -50.408 1.00 58.02 N ATOM 2 CA THRB 154 -2.458-47.904-50.683 1.00 57.95 C ATOM 3 CB THR B 154 -2.314 -47.058 -49.401 1.00 57.97 C ATOM 4 OGL THRB 154 -1.536-47.776-48.429 1.00 57.67 0 ATOM 5 CG2 THR B 154 -3.682 -46.726 -48.824 1.00 57.86 C ATOM 6 C T}IRB 154 -1.068-48.117-51.266 1.0058.01 C ATOM 7 0 THRB 154 -0.508 -49.205 -51.144 1.00 57.95 0 ATOM 1 N PROB 155 -0.509-47.071 -51.906 1.00 58.12 N ATOM 2 CA PRO B 155 0.886 -47.083 -52.338 1.00 58.12 C ATOM 3 CB PRO B 155 1.042 -45.757-53.095 1.00 58.01 C ATOM 4 CG PROB 155 -0.338-45.284-53.372 1.00 58.04 C ATOM 5 CD PROB 155 -1.184-45.812-52.267 1.00 58.18 C ATOM 6 C PRO B 155 1.818 -47.093 -51. 136 1.00 58.22 C ATOM 7 0 PRO B 155 1.450 -46.623 -50.054 1.00 58.19 0 ATOM I N GLYB 156 3.017-47.628-51.331 1.00 58.35 N ATOM 2 CA GLY B 156 4.008 -47.689 -50.267 1.00 58.61 C ATOM 3 C GLY B 156 4.562 -46.324 -49.920 1. 00 58.79 C ATOM 4 0 GLY B 156 4.955 -45.557 -50.800 1.00 58.87 0 ATOM 1 N ILEB 157 4.584-46016-48.630 1.0058.96 N ATOM 2 CA ILE B 157 5.160 -44.769 -48.170 1.00 59.18 C ATOM 3 CB ILEB 157 4.868-44.544-46.684 1.0059.11 C ATOM 4 CGI ILE B 157 3.363 -44.645 -46.436 1.00 59.27 C ATOM 5 CDt ILE B 157 2.949 -44.359 -45.008 1.00 59.64 C ATOM 6 CG2ILEB 157 5.373-43.190-46.243 1.00 59.13 C ATOM 7 C ILE B 157 6.662 -44.792 -48.424 1.00 59.40 C ATOM 8 0 ILE B 157 7.355 -45.715 -48.006 1.00 59.29 0 ATOM 1 N LEUB 158 7.156-43.786-49.138 1.00 59.83 N ATOM 2 CA LEUB 158 8.576-43.723-49.475 1.00 60.23 C ATOM 3 CB LEU B 158 8.886 -42.471 -50. 303 1.00 60.13 C ATOM 4 CG LEU B 158 9.487 -41.410 -49.914 0.00 50.00 C ATOM 5 CD1 LEU B 158 10.336 -41.219 -48.711 0.00 50.00 C ATOM 6 CD2LEUB 158 10.108-40.676-51.109 0.0050.00 C ATOM 7 C LEU B 158 9.437 -43.761 -48.215 1.00 60.49 C ATOM 80 LEUB 158 9.123-43.110-47.217 1.0060.52 0 ATOM 1 N SER B 159 10.5 16 -44.535 -48.265 1.00 60.79 N ATOM 2 CA SERB 159 11.430-44.651 -47.135 1.00 61.07 C ATOM 3 CB SERB 159 12.365 -45.849-47.322 1.00 61.20 C ATOM 4 OG SER B 159 13.023 -46.173 -46.109 1.00 61.72 0 *. ATOM 5 C SERB 159 12.240-43.364-46.941 1.0061.06 C : ... 40 ATOM 6 0 SERB 159 13.457-43.338-47.150 1.00 61.02 0 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 1.00 65.83 C ATOM 3 CB ARGB 167 7.500-34.902-56.103 1.00 65.92 C ATOM 4 CG AROB 167 8.650-34.591 -55.146 1.00 66.25 C : ATOM 5 CD ARGB 167 9.883-35.448-55.436 1.00 66.72 C * ATOM 6 NE ARGB 167 9.774-36.803-54.884 1.00 67.11 N * ** ATOM 7 CZ ARG B 167 10.682 -37.760-55.064 1.00 67.11 C ATOM 8 NHIARGB 167 11.772-37.514-55.788 1.0067.24 N ** * 50 ATOM 9 NH2ARGB 167 10.502-38.961 -54.523 1.00 66.65 N ATOM 10 C ARGB 167 5.283-35.961-56.573 1.0065.75 C ATOM II 0 ARGB 167 5.467-35.617-57.741 1.00 65.80 0 ATOM I N GLY B 168 4.133 -36.474 -56.149 1.00 65.67 N ATOM 2 CA GLYB 168 3.002-36.639-57.055 1.00 65.55 C ATOM 3 C GLYB 168 1.748-35.936-56.574 1.00 65.49 C ATOM 4 0 GLY B 168 1.157 -35. 132 -57.293 1.00 65.38 0 ATOM I N TYR B 169 1.349 -36.239 -55.345 1.00 65.52 N ATOM 2 CA TYR B 169 0.108 -35.720 -54.781 1.00 65.52 C ATOM 3 CB TYRB 169 -1.020-36.744-54.967 1.00 65.60 C ATOM 4 CO TYRB 169 -0.560-38.185 -54. 862 1.00 65.63 C ATOM S CD1 TYR B 169 -0.309 -38.940 -56.004 1.00 65.74 C ATOM 6 CE! TYRB 169 0.118-40.256-55.915 1.00 65.83 C ATOM 7 CZ TYR B 169 0.302 -40.834 -54.673 1.00 65.80 C ATOM 8 OH TYRB 169 0,728-42.140-54.582 1.0065.64 0 ATOM 9 CE2 TYR B 169 0.062 -40.105 -53.523 1.00 65.77 C ATOM 10 CD2TYRB 169 -0.366-38.788-53.623 1.00 65.73 C ATOM 1! C TYRB 169 0.284-35.383-53.298 1.00 65.44 C ATOM 12 0 TYR B 169 1.393 -35.459 -52. 765 1.00 65.44 0 ATOM 1 N ASPB 170 -0.812-35.007-52.641 1.00 65.30 N ATOM 2 CA ASP B 170 -0.794 -34.711 -51.209 1.00 65.09 C ATOM 3 CB ASPB 170 -1.747-33.557-50.884 1.00 65.12 C ATOM 4 CO ASPB 170 -1.398-32.862-49.579 1.00 65.25 C ATOM 5 OD1 ASPB 170 -1.812-31.695-49.399 1.00 65.06 0 ATOM 6 0D2 ASP B 170 -0.711 -33.48 1 -48.734 1.00 65.55 0 ATOM 7 C ASP B 170 -1.137 -35.965 -50.397 1.00 64.95 C ATOM 8 0 ASP B 170 -2.198 -36.058 -49.752 1.00 64.78 0 ATOM 1 N PHEB 171 -0.219-36.926-50.441 1.0064.77 N ATOM 2 CA PHEB 171 -0.407-38.217-49.795 1.00 64.63 C ATOM 3 CB PHE B 171 0.920 -38.975 -49.718 1.00 64.63 C ATOM 4 CG PHE B 171 0.772 -40 414 -49.323 1.00 64.58 C ATOM 5 CD1 PHE B 171 0.020 -41.283 -50.095 1.00 64. 37 C ATOM 6 CE1 PHE B 171 -0.116-42.608 -49.737 1.00 64.43 C ATOM 7 CZ PHE B 171 0.508 -43.083 -48.598 1.00 64.73 C ATOM 8 CE2 PHE B 171 1.263 -42.228 -47.821 1.0064.67 C ATOM 9 CD2 PHE B 171 1.393 -40.902 -48.186 1.00 64.81 C ATOM 10 C PHE B 171 -1.034 -38.064 -48.413 1.0064.56 C ATOM 11 0 PHEB 171 -2.109-38.616-48.149 1.0064.43 0 ATOM I N PROB 172 -0.372-37.306-47.526 1.00 64.52 N ATOM 2 CA PRO B 172 -0.955 -37.032 -46.220 1.00 64.49 C ATOM 3 CB PRO B 172 -0.073 -35.907 -45.681 1.00 64. 54 C ATOM 4 CG PROB 172 1.254 -36.174 -46.298 1.0064.64 C ATOM S CD PRO B 172 0.953 -36.678 -47.680 1.00 64.57 C ATOM 6 C PRO B 172 -2.416 -36.583 -46.312 1.00 64.39 C ATOM 7 0 PROB 172 -3.275-37.148-45.625 1.0064.27 0 ATOM 1 N ALA B 173 -2.700 -35.592 -47.154 1.00 64.18 N ATOM 2 CA ALA B 173 -4.068 -35.093 -47.287 1.00 64.15 C ATOM 3 CB ALA B 173 -4.14! -33.959 -48.291 1.00 64.18 C ATOM 4 C ALA B 173 -5.047 -36.206 -47.657 1.0064.15 C ATOM 5 0 ALA B 173 -6.136 -36.305 -47.074 1.00 64.04 0 ATOM I N VALB 174 -4.668-37.051 -48.613 1.00 64.23 N ATOM 2 CA VAL B 174 -5.545 -38.177 -48.961 1.00 64.12 C ATOM 3 CB VAL B 174 -5.127.38.899 -50.275 1.00 64.14 C ATOM 4 CG1 VALB 174 -3 689-38.598-50.637 1.00 64.11 C * ATOM 5 CG2 VAL B 174 -5.374 -40.397 -50.178 1.0064.15 C * ATOM 6 C VALB 174 -5.719-39.162-47.791 1.00 64.08 C ATOM 7 0 VAL B 174 -6.840 -39.617 -47.505 1.00 63 98 0 ATOM I N LEUB 175 -4.62! -39.466-47.102 1.00 64.02 N ATOM 2 CA LEU B 175 -4.700 -40.298 -45.907 1.00 63.80 C : ATOM 3 CB LEU B 175 -3.313 -40.556-45.326 1.00 63.79 C ATOM 4 CG LEU B 175 -2.668 -41.866 -45.780 1.00 64.02 C ATOM 5 CD1 LEUB 175 -1.260-42.013-45.220 1.0064.02 C ATOM 6 CD2LEUB 175 -3.534-43.050-45.371 1.00 64.22 C ATOM 7 C LEU B 175 -5.607 -39.679 -44.849 1.00 63.78 C ATOM 8 0 LEU B 175.6.233 -40.386 -44.063 1.00 63.66 0 ATOM I N ARG B 176 -5.681 -38.355 -44.834 1.00 63.87 N ATOM 2 CA ARG B 176 -6.550 -37.663 -43.894 1.00 63.82 C ATOM 3 CB ARG B 176 -6.079 -36.223 -43.697 1.00 63.86 C ATOM 4 CG ARGB 176 -6.952-35.376-42.788 1.006446 C ATOM 5 CD ARG B 176 -6.216 -34.101 -42. 406 1.00 65.87 C ATOM 6 NE ARG B 176 -5.005 -33.929 -43.214 1.00 66.91 N ATOM 7 CZ ARG B 176 -4.418 -32.760-43.460 1.00 67.30 C ATOM 8 NHI ARG B 176 -3.317 -32.717 -44.204 1.00 67.30 N ATOM 9 NH2 ARG B 176 -4.935 -31.635 -42.971 1.00 67.62 N ATOM 10 C ARGB 176 -8.010-37.722-44.345 1.00 63.65 C ATOM 11 0 ARGB 176 -8.917-37.859-43.520 1.00 63.59 0 ATOM I N TRP B 177 -8.233 -37.633 -45.654 1.00 63.54 N ATOM 2 CA TRP B 177 -9.580 -37.773 -46.215 1.00 63.37 C ATOM 3 CB TRP B 177 -9.525 -37.527 -47.723 1.00 63. 31 C ATOM 4 CG TRPB 177 -10.847-37.583-48.429 1.00 63.26 C ATOM 5 CDI TRP B 177 -11.718 -36.549 -48.628 1.00 62.97 C ATOM 6 NE1 TRPB 177 -12.817-36.985 -49.328 1.00 62.77 N ATOM 7 CE2 TRP B 177 -12.669 -38.320 -49.603 1.00 63.09 C ATOM 8 CD2TRPB 177 -11.437-38.731 -49.055 1.00 63.35 C ATOM 9 CE3 TRP B 177 -11.044 -40.069 -49.200 1.00 63.27 C ATOM 10 CZ3 TRP B 177 -11.883 -40.939 -49.878 1.00 63.03 C ATOM 11 CH2 TRP B 177 -13.104 -40.500 -50.4 10 1.00 63.04 C ATOM 12 CZ2 TRP B 177 -13.514 -39.199 -50.284 1.00 63.18 C ATOM 13 C 1'RPB 177 -10.141-39.168-45.912 1.0063.41 C ATOM 14 0 TRPB 177 -11.280-39.331-45.407 1.0063.24 0 ATOM I N PHE B 178 -9.326 -40.177 -46.211 1.00 63.59 N ATOM 2 CA PHE B 178 -9.661 -41.545 -45.836 1.00 63.57 C ATOM 3 CB PHEB 178 -8.594-42.526-46.325 1.00 63.59 C ATOM 4 CG PHEB 178 -8.785-42.971 -47.746 1.00 63.89 C ATOM 5 CDI PHE B 178 -9.901 -43.713 -48.111 1.00 64.14 C ATOM 6 CEI PHEB 178 -10.080-44.131 -49.422 1.00 64.00 C ATOM 7 CZ PHEB 178 -9.138-43.811 -50.382 1.00 63.93 C ATOM 8 CE2 PHE B 178 -8.020 -43.076 -50.032 1.0064. 17 C ATOM 9 CD2 PHE B 178 -7.846 -42.660 -48.717 1.00 64.18 C ATOM 10 C PHEB 178 -9.845-41.661 -44.321 1.00 63.55 C ATOM 11 0 PHEB 178 -10.841-42.210-43.851 1.0063.61 0 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 1.00 63.38 C ATOM 3 CB ALAS 179 -7.844-40.377-41.473 1.00 63.38 C ATOM 4 C ALA B 179 -10.332 -40.648 -41.623 1.00 63.30 C ATOM 5 0 ALA B 179 -10.935 -41.207 -40.705 1.00 63.20 0 s's 40 ATOM 1 N GLUB 180 -10.803-39.574-42.252 1.00 63.33 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 1.00 63.23 C ATOM 4 CG GLUB 180 -11.732 -36.535 -42.289 1.00 63.57 C ATOM 5 CD GLUB 180 -11.933 -35.365 -43.233 1.00 63. 57 C ATOM 6 OEI GLUB 180 -12.583-35.556-44.287 1.00 63.87 0 ATOM 7 0E2 GLU B 180 -11.436-34.258 -42.924 1.0064.08 0 ATOM 8 C GLU B 180 -13.195 -40.090 -42.288 1.00 63.07 C ATOM 9 0 GLU B 180 -14.088 -40.338 -41.478 1.00 63. 03 0 ATOM 1 N ARGB 181 -13.101-40.696-43.472 1.0062.95 N . : 50 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 1.00 62.55 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 1.00 63.49 C ATOM 6 NE AROB 181.15.103-38.454-47.389 1.00 64.41 N ATOM 7 CZ ARG B 181 -14.496 -37.415 -46.820 1.00 64.92 C ATOM 8 NI-il ARGB 181.14.938-36.180-47.037 1.00 65.08 N ATOM 9 NH2 ARG B 181 -13.443 -37. 606 -46.034 1.00 65.13 N ATOM 10 C ARGB 181 -14.08743.059-43.439 1.00 62.33 C ATOM 110 ARGB 18! -15.104-43.668-43.115 1.0062.41 0 ATOM I N VALB 182 -12.877-43601 -43.384 1.0062.04 N ATOM 2 CA VAL B 182 -12.653 -45.040 -43.220 1.00 61.56 C ATOM 3 CB VALB 182 -11.218-45.378-43.634 1.0061.45 C ATOM 4 CG1 VAL B 182 -10.698 -46.552 -42.853 1.00 61.55 C ATOM 5 CG2VALB 182 -11.154-45623-45.131 1.0061.14 C ATOM 6 C VAL B 182 -12.930 -45.596 -41.818 1.00 61.44 C ATOM 7 0 VALB 182 -12.831 -44.875-40.828 1.00 61.47 0 ATOM 1 N ASP B 183 -13.272 -46.882 -41.746 1.00 61.33 N ATOM 2 CA ASPB 183 -13.576-47.554-40.468 1.00 61.35 C ATOM 3 CB ASP B 183 -14.500 -48.762 -40.685 1.00 61.39 C ATOM 4 Cci ASP B 183 -15.966 -48.373 -40.747 1.00 62.09 C ATOM 5 OD! ASP B 183 -16.748 -48.863 -39.902 1.00 62.54 0 ATOM 6 OD2ASPB 183 -16.338-47.569-41.631 1.00 63.12 0 ATOM 7 C ASPB 183 -12.342-47.992-39.667 1.00 61.13 C ATOM 8 0 ASP B 183 -12.271 -47.778 -38.455 1.00 61.05 0 ATOM 1 N LEU B 184 -11.394-48.634 -40.344 1.00 60.90 N ATOM 2 CA LEU B 184 -10.151 -49.082 -39.719 1.00 60.71 C ATOM 3 CB LEU B 184 -10.130 -50.608 -39.576 1.00 60.75 C ATOM 4 Cci LEU B 184 -10.626 -5 1.298 -38.302 1.00 60.63 C ATOM 5 CD1 LEU B 184 -10.247 -52.774 -38.346 1.00 60.23 C ATOM 6 CD2 LEU B 184 -10.055 -50.648 -37.055 1.00 60.26 C ATOM 7 C LEU B 184 -8.948 -48.655 -40.548 1.00 60.59 C ATOM 8 0 LEU B 184 -9.008 -48.633 -41.776 1.00 60.73 0 ATOM 1 N ILE B 185 -7.85 1 -48.320 -39.878 1.00 60.33 N ATOM 2 CA ILE B 185 -6.619 -47.996 -40.573 1.00 60. 09 C ATOM 3 CB ILE B 185 -6.170 -46.560 -40.294 1.00 59.94 C ATOM 4 Ccii ILE B 185 -7.327 -45.592 -40.540 1.00 59.84 C ATOM 5 CD! ILE B 185 -6.969 -44.139 -40.330 1.00 59.85 C ATOM 6 CG2 ILE B 185 -4.983 -46.203 -41.165 1.00 59.66 C ATOM 7 C ILEB 185 -5.539-48.964-40.129 1.00 60.22 C ATOM 8 0 ILEB 185 -5.136-48.969-38.968 1.00 60.25 0 ATOM 1 N ILE B 186 -5.086-49.799 -41.053 1.00 60.39 N ATOM 2 CA ILE B 186 -4.057 -50.777 -40.738 1.00 60.66 C ATOM 3 CB ILE B 186 -4.285 -52.100 -41.483 1.00 60. 60 C ATOM 4 Ccii ILE B 186 -5.722 -52.588 -41.291 1.00 60.80 C ATOM 5 CDI ILEB 186 -6.119-52.766-39.846 1.00 60.97 C ATOM 6 CG2 ILE B 186 -3.308 -53.141 -41.002 1.00 60.56 C ATOM 7 C ILEB 186 -2.688-50.230-41.115 1.00 60.88 C ATOM 8 0 ILE B 186 -2.435 -49.911 -42.280 1.00 60.99 0 ATOM I N LEUB 187 -1.812-50.107-40.126 1.00 61.05 N ATOM 2 CA LEU B 187 -0.445 -49.672 -40.376 1.00 61.25 C ATOM 3 CB LEU B 187 -0.055 -48.542 -39.425 1.00 61.17 C ATOM 4 Cci LEUB 187 -0.336-47.107-39.873 1.00 60.76 C ATOM 5 CD! LEU B 187 -1.790 -46.918 -40.216 1.00 60.58 C ATOM 6 CD2 LEU B 187 0.075 -46.133 -38.787 1.00 60.96 C ATOM 7 C LEU B 187 0.520 -50.850 -40.234 1.0061.68 C ATOM 8 0 LEU B 187 0.545 -51.526 -39.201 1.00 61.88 0 ATOM IN LEUB 188 1.306-51.101-41.277 1.0061.91 N . : 50 ATOM 2 CA LEUB 188 2.240-52.216-41.256 1.0062.18 C * ATOM 3 CB LEU B 188 2.152 -53.033 -42.542 1.00 62.05 C ATOM 4 Cci LEU B 188 0.838 -53.756 -42.8 16 1.00 62.08 C ATOM 5 CD! LEUB 188 1.125-55.091 -43.478 1.00 61.97 C ATOM 6 CD2 LEU B 188 0.084 -53.970 -41.530 1.00 62.07 C ATOM 7 C LEUB 188 3.669-51.755-41.050 1.00 62.53 C ATOM 8 0 LEU B 188 4.128 -50.801 -41.678 1.00 62.71 0 ATOM I N PHE B 189 4.362 -52.44! -40.154 1.00 62.88 N ATOM 2 CA PHE B 189 5.797 -52.305 -40.021 1.00 63.25 C ATOM 3 CB PHE B 189 6152 -51.737 -38.661 1.00 63.06 C ATOM 4 CG PHEB 189 5.690-50.339-38.458 1.0063.11 C ATOM 5 CDI PHE B 189 4.4 15 -50.080 -37.994 1.00 63.21 C ATOM 6 CEI PHEB 189 3.987-48.781 -37.802 1.00 63.18 C ATOM 7 CZ PHEB 189 4.841 -47.727-38.078 1.00 63.21 C ATOM 8 CE2 PHE B 189 6.115 -47.974 -38.544 1.00 63.09 C ATOM 9 CD2 PHE B 189 6.534 -49.274 -38.731 1.00 63.37 C ATOM 10 C PHEB 189 6.332-53.707-40.128 1.0063.65 C ATOM 11 0 PHE B 189 5.702 -54.631 -39.626 1.00 63.87 0 ATOM I N ASPB 190 7.472-53.895 -40.779 1.0064.11 N ATOM 2 CA ASP B 190 8.012 -55.244 -40.854 1.00 64.78 C ATOM 3 CB ASPB 190 8.204-55.712-42.308 1.0064.95 C ATOM 4 CO ASP B 190 9.594 -55.455 -42.843 1.00 65.15 C ATOM 5 ODI ASPB 190 10.067-54.305-42.750 1. 00 66.38 0 ATOM 6 OD2ASPB 190 10.201 -56.403-43.386 1.00 64.63 0 ATOM 7 C ASPB 190 9.248-55.446-39.972 1.00 65.11 C ATOM 8 0 ASP B 190 10.233 -54.7 13 -40.073 1.00 65.07 0 ATOM I N ALA B 191 9 152 -56.44 1 -39.090 1.00 65.57 N ATOM 2 CA ALA B 191 10.175 -56.747 -38.090 1.00 65.98 C ATOM 3 CB ALA B 191 9.723 -57.918 -37.239 1.00 66.05 C ATOM 4 C ALAB 191 11.499-57.076-38.740 1.0066.33 C ATOM 5 0 ALA B 191 12.521 -57.215 -38. 072 1 .00 66.29 0 ATOM 1 N HISB 192 11.461 -57.206-40.057 1.00 66.88 N ATOM 2 CA HIS B 192 12.615 -57.594 -40.825 1.00 67.53 C ATOM 3 CB HISB 192 12.141-58.253-42.110 1.0067.72 C ATOM 4 CG HIS B 192 13.248 -58.756 -42.971 1.00 68.70 C ATOM 5 ND1 HISB 192 14.167-59.684-42.529 1.00 69.77 N ATOM 6 CE1 HIS B 192 15.024 -59.947 -43.500 1.00 70.36 C ATOM 7 NE2 HIS B 192 14.688 -59.227 -44.556 1.00 71.03 N ATOM 8 CD2 HIS B 192 13.579 -58.474 -44.251 1.00 69.62 C ATOM 9 C HIS B 192 13.472 -56.372 -41.132 1.00 67.83 C ATOM 10 0 HIS B 192 14.694 -56.409 -40.993 1.00 68.11 0 ATOM 1 N LYSB 193 12.819-55.290-41.547 1.0068.10 N ATOM 2 CA LYS B 193 13.490-54.027 -41.844 1.00 68.23 C ATOM 3 CB LYS B 193 13.471 -53.736 -43.347 1.00 68.19 C ATOM 4 CO LYS B 193 14.585 -54.383 -44.153 1.00 68. 42 C ATOM 5 CD LYSB 193 14.700-53.722-45.523 1.0068.19 C ATOM 6 CE LYS B 193 14.875 -52.2 16 -45.374 1.00 68.29 C ATOM 7 NZ LYSB 193 14.632-51.484-46.644 1.00 68.54 N ATOM 8 C LYS B 193 12.783 -52.889 -41.133 1.00 68.36 C *... ATOM 9 0 LYS B 193 12.009 -52.156 -41.750 1.00 68.44 0 ATOM 1 N LEUB 194 13.041 -52.730-39.843 1.0068.56 N ATOM 2 CA LEU B 194 12.400 -51.653 -39.102 1.00 68.79 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 CD1 LEU B 194 12.004 -50.606-35.540 1.00 69.72 C * ATOM 6 CD2 LEU B 194 10.462 -50.514 -37.478 1.00 69.07 C ATOM 7 C LEU B 194 12.930 -50.294 -39 548 1.00 68.86 C : *. ATOM 8 0 LEUB 194 14.113-49.994-39.399 1.0068.87 0 ATOM 1 N GLU B 195 12.041 -49.479 -40. 102 1.00 69.01 N *. : ATOM 2 CA GLU B 195 12.386 -48.129 -40.535 1.00 69.24 C * ATOM 3 CB GLUB 195 12.967-48.156-41.957 1.00 69.19 C ATOM 4 CG GLU B 195 12.565 -46.994 -42.859 1.00 69.68 C ATOM 5 CD GLU B 195 13.235 -45.679 -42.488 1.00 70.76 C ATOM 6 OEI GLU B 195 13.283 -45.345 -41.286 1.00 71.25 0 ATOM 7 0E2 GLU B 195 13.705 -44.968 -43.404 1.00 70.87 0 ATOM 8 C GLU B 195 11.147 -47.238 -40.450 1.00 69.31 C ATOM 9 0 GLUB 195 10.061 -47.641 -40.867 1.00 69.43 0 ATOM I N ILE B 196 11.302 -46.047 -39.870 1.00 69.37 N ATOM 2 CA ILEB 196 10.214-45.058-39.835 1.0069.32 C ATOM 3 CB ILE B 196 9.694 -44.760 -38.397 1.00 69.37 C ATOM 4 CG1 ILE B 196 9.222 -46.045 -37.716 1.00 69.31 C S ATOM 5 CDI ILEB 196 8.344-45.796-36.508 1.00 69.52 C ATOM 6 CG2 ILE B 196 8.540 -43.749 -38.434 1.00 69.16 C ATOM 7 C ILE B 196 10.627 -43.763 -40.542 1.00 69.13 C ATOM 8 0 ILE B 196 11.208-42.853 -39.945 1.00 69.00 0 ATOM I N SERB 197 10.314-43.707-41.830 1.0068.93 N ATOM 2 CA SERB 197 10.661 -42.579-42.668 1.00 68.80 C ATOM 3 CB SERB 197 10.288-42.892-44.112 1.0068.89 C ATOM 4 00 SER B 197 8.9 16 -43.236 -44.204 1.00 68.92 0 ATOM 5 C SER B 197 9.958 -41.299 -42.240 1. 00 68.69 C ATOM 6 0 SERB 197 8.944-41.331 -41.538 1.00 68.50 0 ATOM I N ASP B 198 10.512 -40.174 -42.682 1.00 68.61 N ATOM 2 CA ASPB 198 9.921 -38.869-42.444 1.00 68.54 C ATOM 3 CB ASP B 198 10.792 -37.785 -43.081 1.00 68.63 C ATOM 4 CG ASP B 198 10.209 -36.394 -42.918 1.00 69.32 C ATOM 5 ODI ASP B 198 9.211 -36.245 -42.179 1.00 69.90 0 ATOM 6 OD2 ASP B 198 10.753 -35.445 -43.529 1.00 70.07 0 ATOM 7 C ASPB 198 8.504-38.830-43.017 1.00 68.35 C ATOM 8 0 ASPB 198 7.541 -38.466-42.323 1.00 68.12 0 ATOM 1 N GLUB 199 8.384-39.220-44.283 1.00 68.16 N ATOM 2 CA GLU B 199 7.094 -39.264 -44.957 1.00 68.12 C ATOM 3 CB GLUB 199 7.244-39.928-46.325 1.00 68.13 C ATOM 4 CG GLUB 199 5.973 -39.956-47.166 1.00 68.49 C ATOM 5 CD GLUB 199 6.217-40.500-48.568 1.00 68.60 C ATOM 6 OEI GLU B 199 7.109 -39.966 -49.265 1.00 69.43 0 ATOM 7 OE2GLUB 199 5.517-41.456-48.975 1.0068.91 0 ATOM 8 C GLU B 199 6.050 -39.994 -44.109 1.00 67.92 C ATOM 9 0 GLUB 199 4.890-39.567-44.022 1.00 67.83 0 ATOM 1 N PHE B 200 6.466 -41. 082 -43.465 1.00 67.72 N ATOM 2 CA PHE B 200 5.553 -41.851 -42.628 1.00 67.53 C ATOM 3 CB PHE B 200 6.213 -43.134 -42.130 1.00 67.63 C ATOM 4 CO PHE B 200 5.288 -44.319 -42.102 1.00 67.69 C ATOM 5 CD1 PHE B 200 5.610 -45.482 -42.781 1.00 67.87 C ATOM 6 CEI PHE B 200 4.758 -46.574 -42.754 1.00 68. 11 C ATOM 7 CZ PHE B 200 3.566 -46.505 -42.055 1.00 67.82 C ATOM 8 CE2PHEB 200 3.231 -45.351 -41.384 1.00 67.56 C : 40 ATOM 9 CD2 PHE B 200 4.089 -44.267 -41.409 1.00 67.81 C ATOM C PHE B 200 5.045 -41.020 -41.451 1.00 67.43 C ATOM 11 0 PHEB200 3.840-40.823-41.302 1.0067.23 0 ATOM I N SERB2O1 5.959-40.522-40.621 1.0067.37 N ATOM 2 CA SER B 201 5.560 -39.690 -39.484 1.00 67.44 C ATOM 3 CS SERB 201 6.771 -39.271 -38.644 1.00 67.44 C ATOM 4 OG SERB2OI 7.579-38.337-39.332 1.0067.77 0 * ATOM 5 C SERB 201 4.742-38.471 -39.927 1.00 67.32 C ATOM 6 0 SERB 201 3.934 -37.939 -39.157 1.00 67.15 0 *... ATOM I N GLU B 202 4.954 -38.033 -41.167 1.00 67.40 N ATOM 2 CA GLU B 202 4.076 -37.031 -41.770 1.00 67.29 C ATOM 3 CB GLUB2O2 4.615-36.581-43.129 1.0067.36 C ATOM 4 CO GLU B 202 5.525 -35.366 -43.080 1.00 67.70 C ATOM S CD GLU B 202 4.825 -34.096 -43.527 1.00 68.43 C ATOM 6 OEI GLUB 202 3.901-34.193-44.363 1.00 68.71 0 ATOM 7 OE2GLUB2O2 5.204-33.000-43.055 1.0068.82 0 ATOM 8 C GLUB2O2 2.668-37.602-41.926 1.0067.11 C ATOM 9 0 GLUB 202 1.676-36.963 -41.551 1.00 66.97 0 ATOM I N ALAB 203 2.584-38.811 -42.472 1.0067.08 N ATOM 2 CA ALA B 203 1.294 -39. 49 1 -42.602 1.00 66.87 C ATOM 3 CB ALA B 203 1.470 -40.842 -43.288 1.00 66.88 C ATOM 4 C ALA B 203 0.580 -39.656 -41.250 1.00 66.81 C ATOM 5 0 ALA B 203 -0.6 10 -39.327 -41.112 1.00 66.36 0 ATOM I N ILEB 204 1.311 -40.164-40.256 1.00 66.84 N ATOM 2 CA ILE B 204 0.764 -40.312 -38 906 1. 00 66.68 C ATOM 3 CB ILEB2O4 1.734-41.034-37.958 1.0066.55 C ATOM 4 CGI ILE B 204 1.908 -42.485 -38.390 1.00 66.77 C ATOM 5 CDI ILEB 204 3.223-42.763-39.062 1.00 67.14 C ATOM 6 CG2 ILE B 204 1.218 -40.998 -36.538 1.00 66.27 C ATOM 7 C ILE B 204 0.375 -38.957 -38.3 16 1.00 66.71 C ATOM 8 0 ILE B 204 -0.602 -38.850 -37.571 1 0066.75 0 ATOM I N GLY B 205 1.141 -37.922 -38.648 1.00 66.74 N ATOM 2 CA GLY B 205 0.737 -36.565 -38.308 1.00 66.51 C ATOM 3 C GLY B 205 -0.615 -36.275 -38.937 1 0066.38 C ATOM 4 0 GLY B 205 -1.457 -35.597 -38.342 1.00 66.39 0 ATOM I N ALA B 206 -0.826 -36.806 -40.140 1.00 66.29 N ATOM 2 CA ALA B 206 -2.073 -36.575 -40.877 1.00 65.87 C ATOM 3 CB ALA B 206 -1.866 -36.8 13 -42.368 1.00 65.95 C ATOM 4 C ALA B 206 -3.243 -37.407 -40.365 1.00 65.58 C ATOM 5 0 ALA B 206 -4.400 -37.072 -40.603 1.00 65.48 0 ATOM 1 N LEUB2O7 -2.946-38.499-39.673 1.0065.49 N ATOM 2 CA LEU B 207 -4.006 -39.322 -39.088 1.00 65.08 C ATOM 3 CB LEUB2O7 -3.540-40.769-38.935 1.0065.03 C ATOM 4 CG LEU B 207 -3.898 -41.743 -40.060 1.00 65.05 C ATOM 5 CD1 LEU B 207 -3.971 -41.051 -41.411 1.00 65.29 C ATOM 6 CD2 LEU B 207 -2.898 -42.885 -40.101 1.00 65.61 C ATOM 7 C LELI B 207 -4.509 -38.785 -37.747 1.00 64.97 C ATOM 8 0 LEU B 207 -5.404 -39.364 -37.133 1.00 64.88 0 ATOM 1 N ARG B 208 -3.933 -37.674 -37.301 1.00 64.92 N ATOM 2 CA ARG B 208 -4. 271 -37.083 -36.004 1.00 64.83 C ATOM 3 CR 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 1.00 64.69 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 -32.58 1 -33.961 1.00 64.85 N ATOM 7 CZ ARG B 208 -4.343 -3 1.934 -34.378 1.00 64.78 C ATOM 8 NH1 ARG B 208 -5.373 -32.594 -34.925 1.00 65.02 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 . 40 ATOM 11 0 ARG B 208 -6.493 -36. 423 -36.665 1.00 6484 0 ATOM I N GLY B 209 -6.253 -37.327 -34 617 1.0064.60 N a...

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 1.00 63.99 C ATOM 4 0 GLY B 209 -9.631 -38.553 -34.206 1.00 63.84 0 ATOM I N HISB 210 -7.781 -39.431 -35.134 1. 00 63.86 N ATOM 2 CA I-US B 210 -8.432 -40.685 -35.475 1.00 63.78 C ATOM 3 CB HIS B 210 -8.683 -40.769 -36.983 1.00 63.93 C ATOM 4 CG HIS B 210 -9.689 -39.779 -37.482 1.0064.53 C ATOM 5 NDI HIS B 210 -9.380 -38.807 -38.409 1.00 65.05 N . : 50 ATOM 6 CE! HIS B 210 -10.455 -38.079 -38.655 1.00 65.36 C * S. ATOM 7 NE2HISB2IO -11.449-38.540-37.916 1.0065.43 N ATOM 8 CD2HISB2IO -10.996-39.602-37.172 1.0065.12 C ATOM 9 C HIS B 210 -7.632 -41.891 -35.005 1.00 63.46 C ATOM 10 0 HISB 210 -7.808-42.996-35.517 1.00 63.56 0 ATOM 1 N GLUB 211 -6.761 -41.682 -34.023 1.00 63.02 N ATOM 2 CA GLU B 211 -5.938 -42.767 -33.510 1.00 62.65 C ATOM 3 CB GLUB2II -5082-42.298-32335 1.0062.67 C ATOM 4 CG GLU B 211 -5 511 -40.968 -3 1. 750 1.00 63.51 C ATOM 5 CD GLU B 211 -4.739 -39.803 -32.341 1.00 64.41 C ATOM 6 OEI GLU B 211 -5.237 -38.656 -32.290 1.00 64.72 0 ATOM 7 OE2GLUB2II -3.626-40.038-32.856 1.0064.94 0 ATOM 8 C GLUB 211 -6.761 -43.999-33.127 1.00 62.27 C ATOM 9 0 GLU B 211 -6.280 -45.128 -33.235 1.00 62.45 0 ATOM I N ASP B 212 -8.002 -43.786 -32.701 1.00 61.63 N ATOM 2 CA ASPB2I2 -8.856-44.897-32.283 1.0061.13 C ATOM 3 CB ASPB 212 -10.158-44.381-31.677 1.0061.30 C ATOM 4 CG ASP B 212 -10.999 -43.615 -32.676 1.00 62.39 C ATOM 5 OD1 ASP B 212 -10.792 -42.385 -32.807 1.00 63.83 0 ATOM 6 OD2ASPB2I2 -11.874-44.239-33.322 1.0063.08 0 ATOM 7 C ASP B 212 -9.164 -45.858 -33.428 1.00 60.47 C ATOM 8 0 ASP B 212 -9.609 -46.983 -33.202 1.00 60.32 0 ATOM I N LYS B 213 -8.927 -45.4 10 -34.654 1.00 59.79 N ATOM 2 CA LYS B 213 -9.201 -46.226-35.825 1.00 59.18 C ATOM 3 CB LYS B 213 -9.712 -45.361 -36.974 1.00 59.14 C ATOM 4 CG LYS B 213 -11.066-44.724 -36.747 1.00 59. 05 C ATOM 5 CD LYSB 213 -11.580-44.131-38.052 1.0059.11 C ATOM 6 CE LYS B 213 -12.808 -43.262 -37.850 1.00 58.78 C ATOM 7 NZ LYSB2I3 -13.143-42.542-39.105 1.0058.30 N ATOM 8 C LYS B 213 -7.956 -46.962 -36.282 1.00 58.86 C ATOM 9 0 LYS B 213 -7.964 -47.627 -37.3 15 1.00 58. 84 0 ATOM I N ILEB 214 -6.884 -46.851 -35.511 1.00 58.47 N ATOM 2 CA ILEB2I4 -5.599-47.377-35.948 1.0058.17 C ATOM 3 CB ILE B 214 -4.467 -46.389 -35.634 1.00 58.12 C ATOM 4 CG1 ILE B 214 -4.670 -45.098 -36.424 1.00 58.10 C ATOM 5 CDI ILEB 214 -3.652-44.022-36.118 1.00 58.21 C ATOM 6 CG2 ILE B 214 -3.122 -47.009 -35.959 1.00 58.27 C ATOM 7 C ILE B 214 -5.245 -48.735 -35.352 1.00 57.94 C ATOM 8 0 ILE B 214 -5.231 -48.908 -34.137 1.00 58.08 0 ATOM 1 N A.RG B 215 -4.960 -49.698 -36.219 1.00 57.63 N ATOM 2 CA ARG B 215 -4.361 -50.946 -35.782 1.00 57.37 C ATOM 3 CB ARG B 215 -5.175 -52.152 -36.242 1.00 57.18 C ATOM 4 CG ARGB2I5 -6.611-52.145-35. 811 1.0056.81 C ATOM 5 CD ARGB2I5 -6.766-51.984-34.314 1.0056.23 C ATOM 6 NE ARGB215 -8.176-51.817-33.978 1.0056.42 N ATOM 7 CZ ARC B 215 -8.802 -50.645 -33.950 1.00 56.18 C ATOM 8 NH1 ARG B 215 -8.140 -49.527 -34.219 1.00 56.41 N ATOM 9 N}12 ARG B 215 -10.090 -50.59 1 -33.649 1.00 55.83 N ATOM 10 C ARGB2I5 -2.972-51.029-36.380 1.0057.38 C *** ATOM 11 0 ARGB215 -2.820-51.179-37.596 1.0057.59 0 ATOM 1 N VALB 216 -1.961-50.913-35.526 1.0057.17 N ATOM 2 CA VAL B 216 -0.575 -5 1.040 -35.949 1.00 56.79 C ATOM 3 CB VAL B 216 0.346 -50.313 -34.971 1.00 56.68 C a.. 45 ATOM 4 CG1 VAL B 216 1.797 -50.608 -35.293 1.00 56.77 C : ATOM 5 CG2 VAL B 216 0.069 -48.823 -34.997 1.00 56.69 C ATOM 6 C VALB 216 -0.188 -52.506 -35.942 1. 00 56.67 C ATOM 7 0 VAL B 216 -0.159 -53.124 -34.884 1.00 56.91 0 :. ATOM 1 N VALB 217 0.105-53.079-37.105 10056.39 N * * 50 ATOM 2 CA VALB2I7 0.520-54.478-37.123 1.0056.08 C ATOM 3 CB VAL B 217 -0.406 -55.381 -37. 978 1.00 56.09 C ATOM 4 CG1 VALB 217 -1.604-54.600-38.471 1.00 55.83 C ATOM 5 CG2 VAL B 217 0.352 -56.004 -39.138 1.00 56.09 C ATOM 6 C VAL B 217 1.971 -54.632 -37,548 1.00 56.01 C ATOM 7 0 VAL B 217 2.388 -54.152 -38.608 1. 00 56.14 0 ATOM 1 N LEU B 218 2.734 -55.297 -36.688 1.00 55.76 N ATOM 2 CA LEU B 218 4.136 -55.593 -36.933 1.00 55.35 C ATOM 3 CB LEU B 218 4.878 -55.634 -35.604 1.00 55.27 C ATOM 4 CG LEU B 218 6.311 -56.137 -35.529 1.00 55.27 C ATOM 5 CDI LEU B 218 7.252 -55.189 -36.244 1.00 55.39 C ATOM 6 CD2 LEU B 218 6.683 -56.270 -34.066 1.00 55.68 C ATOM 7 C LEUB2I8 4.239-56.926-37.670 L0055.33 C ATOM 8 0 LEUB21S 4.112-58.006-37.084 1.0055.26 0 ATOM I N ASN B 219 4.460 -56.830 -38.972 1.00 55.33 N ATOM 2 CA ASNB 219 4.411 -57.970-39.865 1.00 55.16 C ATOM 3 CB ASN B 219 4.108 -57.479 -41.276 1.00 55.29 C ATOM 4 CG ASNB219 3.409-58,516-42.109 1.0055.94 C ATOM 5 OD1 ASN B 219 3.026 -59.575 -41.601 1.00 56.02 0 ATOM 6 ND2 ASN B 219 3.234 -58.225 -43.403 1.00 56 54 N ATOM 7 C ASN B 219 5.693 -58.789 -39.875 1.00 55.04 C ATOM 8 0 ASN B 219 6.704 -58.388 -39 301 1. 00 54.74 0 ATOM I N LYS B 220 5.632 -59.937 -40.546 1.00 55.21 N ATOM 2 CA LYS B 220 6.756 -60.871 -40.681 1.005541 C ATOM 3 CB LYS B 220 7.602 -60.553 -41.925 1.00 55.43 C ATOM 4 CG LYS B 220 7.598 -59.096 -42.343 1.00 55.52 C ATOM 5 CD LYS B 220 7.343 -58.922 -43.840 1.00 55.10 C ATOM 6 CE LYSB 220 8.608-58.547-44.594 1.00 55.18 C ATOM 7 NZ LYS B 220 8.297 -57.685 -45.768 1.00 54.26 N ATOM 8 C LYS B 220 7.627 -61.022 -39.437 1. 00 55.67 C ATOM 9 0 LYS B 220 8.848 -61.107 -39.53 1 1.00 55.78 0 ATOM 1 N ALA B 221 6.987 -61.082 -38.273 1.00 56.06 N ATOM 2 CA ALAB 221 7.691 -61.285 -37.011 1.00 56.27 C ATOM 3 CB ALA B 221 6.764 -61.039 -35.842 1.00 56.15 C ATOM 4 C ALA B 221 8.259 -62.689 -36.932 1.00 56.45 C ATOM 5 0 ALA B 221 9.042 -62.996 -36.042 1.00 56.60 0 ATOM I N ASP B 222 7.864 -63.540 -37.869 1.00 56.79 N ATOM 2 CA ASP B 222 8.275 -64.932 -37.840 1.00 57.20 C ATOM 3 CB ASP B 222 7.246 -65.8 17 -38.537 1.00 57.26 C ATOM 4 CG ASP B 222 7.446 -65.865 -40.042 1.00 58.12 C ATOM 5 OD1 ASP B 222 7.687 -66.978 -40.571 1.00 58.75 0 ATOM 6 0D2 ASP B 222 7.383 -64.791 -40.692 1.00 58.98 0 ATOM 7 C ASPB222 9.609-65.106-38.530 1.0057.37 C ATOM 8 0 ASP B 222 10.166 -66.205 -38.549 1.00 57.48 0 ATOM 1 N MET B 223 10.120-64.038 -39.124 1.00 57.52 N ATOM 2 CA METB 223 11.365-64.182-39. 853 1.00 57.98 C ATOM 3 CB METB 223 11.214 -63.751 -41.312 1.00 57.98 C ATOM 4 CG METB 223 11.104-62.271 -41.558 1.00 58.43 C * 40 ATOM 5 SD METB 223 11.298 -61.968 -43.330 1.00 59.28 S S. ATOM 6 CE METB 223 12.766 -62.938 -43.695 1.00 59.20 C S'S.

ATOM 7 C METB 223 12.525 -63.489-39.163 1.00 57.63 C ATOM 8 0 METB223 13.437-62.975-39.807 1.0057.84 0 ATOM 1 N VALB224 12.495-63.514-37.838 1.0057.30 N ATOM 2 CA VAL B 224 13.536 -62.896 -37.049 1.00 56.98 C :: ATOM 3 CB VAL B 224 13.260 -61.386 -36.882 1.00 56.86 C ATOM 4 CG1 VAL B 224 12.529 -61.108 -35.585 1.00 56.82 C : ** ATOM 5 CG2 VAL B 224 14.547 -60.602 -36.947 1.00 56.98 C ATOM 6 C VAL B 224 13.608 -63.608 -35.700 1.00 56.86 C . : 50 ATOM 7 0 VALB224 12.583-63.957-35.119 1.0056.87 0 * ATOM 1 N GLUB225 14.818-63.856-35.218 1.0056.71 N ATOM 2 CA GLU B 225 14.987 -64.536 -33.946 1.00 56.69 C ATOM 3 CB GLU B 225 16.468 -64.682 -33.627 1.00 57.01 C ATOM 4 CG 0LUB225 16.782-65.935-32.848 1.0058.92 C ATOM 5 CD GLU B 225 16.999 -67.130 -33.754 1.00 61.73 C ATOM 6 OE1 GLU B 225 16.006-67.812-34.110 1.00 62.80 0 ATOM 7 0E2 GLU B 225 18.171 -67.378 -34.122 1.00 63.64 0 ATOM 8 C GLU B 225 14.287 -63.73 1 -32.854 1.00 56.21 C ATOM 9 0 GLU B 225 14.195 -62. 512 -32.948 1.00 56.09 0 ATOM 1 N THRB226 13.808-64.399-31.812 1.0055.84 N ATOM 2 CA THR B 226 12.913 -63.730 -30.861 1.00 55.74 C ATOM 3 CB THR B 226 12.207 -64.715 -29.894 1.00 55.64 C ATOM 4 OGI THR B 226 12.183 -64.152 -28.577 1.00 55.50 0 ATOM 5 CG2 THR B 226 12.920 -66 054 -29.862 1.00 56.27 C ATOM 6 C THR B 226 13.473 -62 487 -30.127 1.00 55.65 C ATOM 7 0 THRB 226 12.854-61.416-30.168 1.00 55.72 0 ATOM 1 N GLNB227 14.618-62.618-29.457 1.0055.48 N ATOM 2 CA GLN B 227 15.255 -61.451 -28.828 1.00 55.18 C ATOM 3 CB GLNB 227 16.718-61.737-28.508 1.00 55.14 C ATOM 4 CG GLN B 227 16.996 -62.165 -27.086 1.00 54.85 C ATOM 5 CD GLN B 227 18.445 -62.543 -26.892 1.00 54.43 C ATOM 6 OEI GLN B 227 19.045 -63. 20 1 -27.747 1.00 53.99.0 ATOM 7 NE2 GLN B 227 19.023 -62.124 -25.772 1.00 54.27 N ATOM 8 C GLN B 227 15.191 -60.245 -29.757 1.00 55.20 C ATOM 9 0 GLNB 227 14.762-59.151 -29.362 1.00 55.06 0 ATOM I N GLN B 228 15.630 -60.463 -30.995 1.00 55.21 N ATOM 2 CA GLN B 228 15.591 -59.450 -32.035 1.00 55.26 C ATOM 3 CB GLNB228 16.104-60.039-33.345 1.0055.25 C ATOM 4 CO GLN B 228 15.985 -59.113 -34.533 1.00 55.38 C ATOM 5 CD GLN B 228 16.759 -57.832 -34.349 1.00 55.86 C ATOM 6 OE1 GLN B 228 17.766-57.794-33.640 1.00 56.42 0 ATOM 7 NE2 GLN B 228 16.295 -56.769 -34.991 1.00 56.22 N ATOM 8 C GLNB228 14.180-58.880-32.213 1.0055.39 C ATOM 9 0 GLN B 228 13.996 -57.660 -32.302 1.00 55.39 0 ATOM I N LEUB 229 13.184-59.761 -32.256 1.00 55.35 N ATOM 2 CA LEUB229 11.793-59.320-32.292 1.0055.42 C ATOM 3 CB LEU B 229 10.836 -60.506 -32.164 1.00 55.40 C ATOM 4 CO LEUB229 9.514-60.430-32.927 1.0055.19 C ATOM 5 CDI LEUB 229 8.475-61.296-32.239 1.00 55.13 C ATOM 6 CD2 LEU B 229 9.024 -59.001 -33.040 1.00 54.53 C ATOM 7 C LEUB229 11.545-58.334-31.155 1.00 55.47 C ATOM 8 0 LEU B 229 11.095 -57.209 -3 1.390 1.00 55.55 0 ATOM 1 N MET B 230 11.854 -58.752 -29.928 1.00 55.41 N ATOM 2 CA MET B 230 11.723 -57.862 -28.775 1.00 55.26 C ATOM 3 CB METB23O 12.318-58.497-27.519 1,0055.44 C ATOM 4 CO MET B 230 11.610-59.763 -27.089 1.00 55.41 C :. ATOM 5 SD MET B 230 9.837 -59.494 -26.920 1.00 56.86 S ATOM 6 CE MET B 230 9.228 -61.082 -27.495 1.00 56.24 C ATOM 7 C METB 230 12.389-56.523-29.053 1.0055.18 C ATOM 8 0 METB23O 11.804-55.459-28.819 1.0055.12 0 ATOM I N ARGB23I 13.612-56.581-29.567 1.0055.12 N ATOM 2 CA AROB 231 14.336-55.368-29.936 1.00 55.21 C ATOM 3 CB ARGB231 15.686-55.730-30.553 1.0055.10 C ATOM 4 CO ARGB231 16.874-55.530-29.624 1.0055.70 C ATOM 5 CD ARGB231 17.000-56.597-28.551 1.0056.51 C ATOM 6 NE AROB231 16.166-56.309-27.391 1.00 57.65 N ATOM 7 CZ ARGB23I 16.040-57.120-26.346 1.00 57.94 C ATOM 8 NH! ARGB 231 16.704-58.268-26.313 1.00 57.78 N * ATOM 9 N1-12 ARG B 231 15.248 -56.782 -25.337 1.00 58.31 N ATOM 10 C ARGB 231 13.531-54.457-30.878 1.00 55.08 C ATOM 11 0 AROB23I 13.334-53.258-30.599 1.0054.91 0 ATOM 1 N VALB232 13.057-55.032-31.982 1.0054.99 N ATOM 2 CA VAL B 232 12.296 -54.267 -32.966 1.00 54.96 C ATOM 3 CB VALB232 11.980-55.100-34.219 1.0054.88 C ATOM 4 CGI VAL B 232 10.943 -54.407 -35.060 1.00 55.17 C ATOM 5 CG2 VALB 232 13.228 -55.310-35.035 1.00 55.17 C ATOM 6 C VAL B 232 11.006-53.702 -32.365 1.00 54.91 C ATOM 7 0 VALB232 10.780-52.485-32.380 1.0054.68 0 ATOM I N TYRB233 10.168-54.583-31.828 1.0054.85 N ATOM 2 CA TYRB233 8.951-54.152-31.159 1.0054.67 C ATOM 3 CB TYR B 233 8.336 -55.333 -30.4 13 1.00 54.48 C ATOM 4 CG TYR B 233 7.076 -55.026 -29.642 1.00 54.61 C ATOM 5 CDI TYR B 233 6.701 -55.81 I -28.562 1.00 54.70 C ATOM 6 CEI TYR B 233 5.552 -55.544 -27.848 1.00 54.44 C ATOM 7 CZ TYRB 233 4.764-54.480-28.205 1.00 54.26 C ATOM 8 OH TYR B 233 3.623 -54.2 19 -27.489 1.00 54.47 0 ATOM 9 CE2TYRB233 5.112-53.681 -29.271 1.00 54.50 C ATOM 10 CD2 TYR B 233 6. 263 -53.955 -29.985 1.00 54.77 C ATOM ii C TYR B 233 9.244 -52.964 -30.226 1.00 54.73 C ATOM 12 0 TYR B 233 8.578 -5 1.909 -30.297 1.00 54.67 0 ATOM I N GLYB234 10.257-53.129-29.375 10054.80 N ATOM 2 CA GLY B 234 10.703 -52.047 -28.502 1.00 54.70 C ATOM 3 C GLY B 234 10.935 -50.754 -29.268 1.00 54.80 C ATOM 4 0 GLY B 234 10.356 -49.698 -28.933 1.00 54.91 0 ATOM I N ALA B 235 11.770-50.830 -30.305 1.00 54.65 N ATOM 2 CA ALA B 235 12.066 -49.651 -31.120 1.00 54.39 C ATOM 3 CB ALA B 235 13.000 -50.0 15 -32.250 1.00 54.36 C ATOM 4 C ALA B 235 10.792 -49.002 -3 1.667 1.00 54.45 C ATOM 5 0 ALA B 235 10.587 -47.784 -3 1.538 1.00 54.48 -0 ATOM 1 N LEU B 236 9.936 -49.824 -32.269 1.00 54.43 N ATOM 2 CA LEU B 236 8.672 -49.355-32.815 1.00 54.31 C ATOM 3 CB LEU B 236 7.805 -50.532 -33.245 1. 00 54.32 C ATOM 4 CG LEU B 236 6.964 -50.42 1 -34.521 1.00 54.14 C ATOM 5 CDI LEU B 236 6.530 -49.007 -34.824 1.00 54.03 C ATOM 6 CD2 LEU B 236 5.765 - 5 1.350 -34.440 1.00 53.68 C ATOM 7 C LEU B 236 7.923 -48.558 -3 1.768 1.00 54.43 C ATOM 8 0 LEU B 236 7.626 -47.383 -3 1.973 1.00 54.51 0 ATOM 1 N METB 237 7.615-49.192-30.638 1.00 54.66 N ATOM 2 CA MET B 237 6.798 -48.506 -29.630 1.00 54.81 C ATOM 3 CB MET B 237 6.388 -49.435 -28.488 1.00 54.86 C ATOM 4 CG MET B 237 5.420 -50.528 -28.9 19 1.00 55.85 C ATOM 5 SD MET B 237 3.853 -49.943-29.618 1.00 57.46 S ATOM 6 CE MET B 237 2. 887 -49.728 -28.124 1.00 56.82 C ATOM 7 C MET B 237 7.470 -47.250 -29.097 1. 00 54.74 C ATOM 8 0 METB 237 6.792 -46.278 -28.762 1.00 54.99 0 ATOM I N TRP B 238 8.796 -47.261 -29.028 1.00 54.61 N ATOM 2 CA TRPB238 9.517-46.061-28.619 1.0054.49 C ATOM 3 CB TRPB238 11.004-46.358-28.620 1.0054.42 C ATOM 4 CG TRP B 238 11.685 -45.961 -27.380 1.00 54.35 C ATOM 5 CD1TRPB 238 11.545-46.533-26.150 1.00 54.85 C ATOM 6 NEI TRPB 238 12.352-45.899-25.236 1.00 54.83 N ATOM 7 CE2TRPB23S 13.037-44.903-25.877 1.0054.14 C ATOM 8 CD2 TRP B 238 12.639 -44.916 -27.23 1 1.00 53.92 C : *, ATOM 9 CE3TRPB 238 13.196-43.991 -28.107 1.0053.71 C ATOM 10 CZ3TRPB 238 14.112-43.100-27.618 1.0054.62 C : 50 ATOM 11 CH2TRPB 238 14.486-43.109-26.266 1.00 54.60 C * ATOM 12 CZ2 TRP B 238 13.961 -44.004 -25.384 1.00 54.05 C ATOM 13 C TRP B 238 9.237 -44.921 -29.596 1.00 54.52 C ATOM 14 0 TRP B 238 8.748 -43.827 -29.230 1.00 54.67 0 ATOM I N ALA B 239 9.549 -45.206 -30.855 1.00 54.59 N ATOM 2 CA ALA B 239 9.352 -44.262 -3 1.942 1.00 54.74 C ATOM 3 CB ALA B 239 9.719 -44.915 -33.266 1.00 54. 68 C ATOM 4 C ALA B 239 7.917 -43.746 -31.979 1.00 54.79 C ATOM 5 0 ALAB239 7.672-42.547-31.812 1.0055.14 0 ATOM I N LEU B 240 6.975 -44.661 -32.203 1.00 54.72 N ATOM 2 CA LEUB24O 5.561 -44.311 -32.240 1.0054.66 C ATOM 3 CB LW B 240 4.693 -45.565 -32.320 1.00 54.59 C ATOM 4 CO LEU B 240 4.544 -46.206 -33.699 1.00 54.30 C ATOM 5 CDI LEUB240 3.564-47.363-33.633 1.0054.48 C ATOM 6 CD2 LEU B 240 4.092 -45.186 -34.73 1 1.00 53.92 C ATOM 7 C LEU B 240 5.183 -43.482 -31.023 1.00 54.72 C ATOM 8 0 LEU B 240 4.561 -42.429 -31.154 1.00 54.60 0 ATOM I N GLY B 241 5.567 -43.962 -29.843 1. 00 54.91 N ATOM 2 CA GLY B 241 5.414 -43.188 -28.620 1.00 55.18 C ATOM 3 C GLY B 241 5.758 -41.726 -28.845 1.00 55.50 C ATOM 4 0 GLY B 241 4.910 -40.842 -28.654 1.00 55.56 0 ATOM 1 N LYSB242 6.997-41.464-29262 1.0055. 54 N ATOM 2 CA LYSB242 7.430-40.079-29.518 1.0055.84 C ATOM 3 CB LYS B 242 8.936 -40.037 -29.805 1.00 55.91 C ATOM 4 CG LYS B 242 9.394 -38.929 -30.744 1.00 56.07 C ATOM 5 CD LYS B 242 9.523 -37.59 1 -30.035 1.00 56. 51 C ATOM 6 CE LYS B 242 10.365 -36.620 -30.852 1.00 56.40 C ATOM 7 NZ LYSB 242 11.764-37.109-31.001 1.00 56.49 N ATOM 8 C LYSB242 6.641 -39.370-30.634 1.00 56.01 C ATOM 9 0 LYS B 242 6.393 -38.168 -30.555 1.00 55.92 0 ATOM I N VAL B 243 6.236 -40.121 -3 1.656 1.00 56.28 N ATOM 2 CA VAL B 243 5.597 -39.540 -32.849 1.00 56.96 C ATOM 3 CB VAL B 243 5.682 -40.487 -34.074 1.00 57.04 C ATOM 4 CGI VALB 243 5.080-39.818-35.311 1.00 56.83 C ATOM 5 CG2 VAL B 243 7.125 -40.904 -34.333 1.00 57.52 C ATOM 6 C VAL B 243 4.137 -39.111 -32.678 1.00 57.22 C ATOM 7 0 VAL B 243 3.826 -37.939 -32.860 1.00 57.33 0 ATOM I N VALB 244 3.244-40.051 -32.355 1.00 57.66 N ATOM 2 CA VALB244 1.807-39.748-32.281 1.0058.09 C ATOM 3 CB VAL B 244 0.922 -41.016 -32.298 1.00 57.99 C ATOM 4 CGI VAL B 244 1.602 -42.136 -33 060 1.00 58.05 C ATOM 5 CG2 VAL B 244 0.598 -41.459 -30.895 1.00 57. 87 C ATOM 6 C VAL B 244 1.443 -38.882 -31.071 1.00 58.63 C ATOM 7 0 VAL B 244 0.437 -38.174 -31.092 1.00 58.67 0 ATOM 1 N GLY B 245 2.253 -38.957 -30.017 1.00 59.32 N ATOM 2 CA GLY B 245 2.209 -37.975 -28.923 1.00 60.12 C ATOM 3 C GLY B 245 1.073 -38.053 -27.916 1.00 60.64 C ATOM 4 0 GLYB245 1.096-37.358-26.896 1.0060.52 0 : ... 40 ATOM I N THR B 246 0.078 -38.891 -28.202 1.00 61.23 N ATOM 2 CA THRB246 -1.045-39.111-27.289 1.0061.72 C ATOM 3 CB THR B 246 -2.213 -39.822 -28.006 1.00 61.77 C ATOM 4 001 THRB 246 -3.278 -40.049 -27.076 1.00 62.38 0 ATOM 5 CG2 THIRB 246 -1.764-41.160-28.576 1.00 61.63 C ATOM 6 C THR B 246 -0.609 -39.947.26. 080 1.00 61.92 C ATOM 7 0 THR B 246 0.221 -40.838 -26.217 1.00 61.87 0 * ATOM I N PRO B 247 -1.152-39.646-24.885 1.00 62.13 N ATOM 2 CA PRO B 247 -0. 824 -40.447 -23.703 1.00 62.22 C ATOM 3 CB PR0B247 -1.435-39.644-22.545 1.006211 C ** * 50 ATOM 4 CO PRO B 247 -1.723-38.284-23.112 1.00 62.24 C ATOM 5 CD PRO B 247 -2.056 -38.535 -24.550 1.00 62.13 C ATOM 6 C PRO B 247.1.422 -41.857 -23.748 1.00 62.38 C ATOM 7 0 PR0B247 -1.018-42.714-22.962 1.0062.55 0 ATOM I N GLU B 248 -2.369 -42.095 -24. 655 1.00 62.37 N ATOM 2 CA GLU B 248.2.954 -43.427.24.8 18 1.00 62.39 C ATOM 3 CB GLU B 248 -4.428 -43.337.25.2 18 1.00 62.54 C ATOM 4 CG GLU B 248 -5.252 -42.415 -24.341 1.00 63.55 C ATOM 5 CD GLU B 248 -5.301 -41.000 -24.881 1.0064.86 C ATOM 6 OEI GLUB 248 -5.033-40.048-24.111 1.00 65.06 0 ATOM 7 0E2 GLU B 248 -5.603 -40.844 -26.085 1.00 65.69 0 ATOM 8 C GLUB248 -2.187-44.235-25.853 1.0062.14 C ATOM 9 0 GLUB248 -2.024-43801 -26.991 1.0062.25 0 ATOM 1 N VALB249 -1.734-45.419-25.454 1.0061.87 N ATOM 2 CA VAL B 249 -0.874 -46.254 -26.293 1.00 61.58 C ATOM 3 CB VALB249 0.014-47.184-25.424 1.0061.51 C ATOM 4 CG1 VAL B 249 -0.72 1 -47.608 -24.163 1.00 61.83 C ATOM 5 CG2 VAL B 249 0.465 -48.396 -26.209 1.00 61. 54 C ATOM 6 C VALB249 -1.634-47.072-27.345 1.0061.44 C ATOM 7 0 VALB 249 -2.670-47.671 -27.060 1.00 61.45 0 ATOM 1 N LEUB25O -1.108-47.082-28.565 1.0061.36 N ATOM 2 CA LEU B 250 -1.689 -47.851 -29.659 1.00 61.27 C ATOM 3 CB LEU B 250 -1.162 -47.347 -31.002 1.00 61.02 C ATOM 4 CG LEU B 250 -2.082 -46.481 -31.862 1.00 60.92 C ATOM 5 CD1 LEU B 250 -2.866 -45.482 -31.035 1.00 61.76 C ATOM 6 CD2 LEU B 250 -1 277 -45.765 -32.921 1.00 61.02 C ATOM 7 C LEU B 250 -1.388 -49.335 -29.522 1.00 61.49 C ATOM 8 0 LEU B 250 -0.289 -49.725 -29.129 1.00 61.64 0 ATOM 1 N ARG B 251 -2.371 -50.161 -29.858 1.00 61.69 N ATOM 2 CA ARG B 251 -2.193 -51.606 -29.865 1.00 61.74 C ATOM 3 CB ARO B 251 -3.560 -52.294 -29.827 1.00 61.77 C ATOM 4 CG ARG B 251 -3.556 -53.780 -30.178 1.00 61.82 C ATOM 5 CD ARG B 251 -3.114 -54.629 -28.998 1.00 61.89 C ATOM 6 NE ARG B 251 -3.929 -55.833 -28.873 1.00 61.71 N ATOM 7 CZ ARG B 251 -3.557 -57.040 -29.285 1.00 61. 63 C ATOM 8 NH1 ARG B 251 -2.374 -57.216 -29.853 1.00 61.74 N ATOM 9 NH2 ARG B 251 -4.375 -58.072 -29.132 1.00 61.58 N ATOM 10 C ARGB251 -1.446-52.033-31.121 10061.79 C ATOM 11 0 ARG B 251 -1.820 -51.641 -32. 227 1.00 61.72 0 ATOM 1 N VAL B 252 -0.390 -52.825 -30.954 1.00 61.91 N ATOM 2 CA VAL B 252 0.235 -53 487 -32.105 1.00 62.11 C ATOM 3 CB VALB252 1.776-53.317-32.142 1.0062.15 C ATOM 4 CG1 VAL B 252 2.143 -51.846 -32. 199 1.00 62.31 C ATOM 5 CG2 VAL B 252 2.4 15 -53.976 -30.934 1.00 62.44 C ATOM 6 C VAL B 252 -0.125 -54.972 -32.144 1.00 61.92 C ATOM 7 0 VAL B 252 -0.175 -55.633 -31.107 1.00 61.98 0 ATOM 1 N TYRB 253 -0.394 -55.482 -33.342 1.00 61.76 N : **, ATOM 2 CA TYR B 253 -0.691 -56.898 -33.532 1. 00 61.60 C ATOM 3 CB TYR B 253 -1.914 -57.072 -34.434 1.00 61.60 C ATOM 4 CG TYRB 253 -3.179-56.478-33.847 1.00 62.19 C ATOM 5 CDI TYR B 253 -3.706 -55.293 -34.334 1.00 62.55 C ATOM 6 CE1 TYRB 253 -4.859-54.749-33.792 1. 00 62.44 C ATOM 7 CZ TYR B 253 -5.493 -55.384 -32.751 1.00 61.97 C ATOM 8 OH TYR B 253 -6.639 -54.844 -32.210 1.00 62.06 0 * ATOM 9 CE2 TYR B 253 -4.990 -56.557 -32.25 1 1.00 62.23 C ATOM 10 CD2 TYR B 253 -3.84 1 -57. 098 -32.795 1.00 62.57 C ATOM 11 C TYRB 253 0.524-57.588-34.134 1.00 61.37 C ATOM 12 0 TYRB 253 0.937 -57.252 -35.243 1.00 61.52 0 *. 50 ATOM 1 N 1LEB254 1.100-58.539-33.399 1.0060.85 N * ATOM 2 CA 1LEB254 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 CG1 ILE B 254 3.199 -58.278 -31.632 1.00 60.50 C ATOM 5 CDI ILE B 254 4.262 -58.3 19 -30.554 1.00 60.93 C ATOM 6 CG2 ILE B 254 4.679 -59.735 -33.062 1.00 59.77 C ATOM 7 C 1LEB254 2.115-60.486-34.559 1.0060.21 C ATOM 8 0 ILEB 254 1.542-61.423-34.016 1.00 60.30 0 ATOM 1 N GLY B 255 2.569 -60.558 -35.804 1.00 59.92 N ATOM 2 CA GLY B 255 2.4 10 -61.789 -36.573 1.00 59.62 C ATOM 3 C GLY B 255 3.016 -61.725 -37.960 1. 00 59.23 C ATOM 4 0 GLY B 255 3.708 -60.766 -38.298 1.00 59.30 0 ATOM I N SER B 256 2.765 -62.759 -38.757 1.00 58.78 N ATOM 2 CA SERB 256 3.158 -62.757 -40.160 1.00 58.69 C ATOM 3 CB SER B 256 4.4 19 -63593 -40.397 1.00 58.72 C ATOM 4 OG SER B 256 4.402 -64.776 -39.623 1.00 59.59 0 ATOM 5 C SERB256 2.000-63.204-41.054 1.0058.34 C ATOM 6 0 SERB256 1.769.64.392-41.277 1.0058.22 0 ATOM 1 N PHE B 257 1.293 -62.212 -41.578 1.00 58.01 N ATOM 2 CA PHE B 257 0.041 -62.4 10 -42.277 1.00 57.54 C ATOM 3 CB PHEB257 -0.756-61.107-42.223 1.0057.11 C ATOM 4 CG PHEB 257 -1.001 -60.627-40.821 1.00 56.81 C ATOM 5 CD1 PHE B 257 -2.247 -60.763 -40.232 1.00 56.40 C ATOM 6 CE1 P1-1EB257 -2.469-60.338-38.933 1.005540 C ATOM 7 CZ PHE B 257 -1.44 1 -59.781 -38.204 1.00 55.70 C ATOM 8 CE2 PHE B 257 -0.193 -59.650-38.764 1.00 55.89 C ATOM 9 CD2 PHE B 257 0.027 -60.077 -40.070 1.00 56.91 C ATOM 10 C PHEB257 0.200-62.948-43.706 1.0057.57 C ATOM 11 0 PHE B 257 0.067 -62.216 -44.690 1.00 57.54 0 ATOM 1 N TRP B 258 0.492 -64.243 -43.793 1. 00 57.58 N ATOM 2 CA TRP B 258 0.511 -64.966 -45.062 1.00 57 65 C ATOM 3 CB TRP B 258 1.642 -64.464 -45.966 1.00 57.76 C ATOM 4 CG TRP B 258 3.022 -64.843 -45.544 1.00 57.87 C ATOM 5 CDI TRP B 258 3.423 -65.277 -44.311 1.00 58.43 C ATOM 6 NE1 TRP B 258 4.777 -65.520 -44.311 1.00 58.60 N ATOM 7 CE2 TRP B 258 5.278 -65.229-45.554 1.00 58.63 C ATOM 8 CD2TRPB 258 4.201-64.791-46.353 1.00 58.19 C ATOM 9 CE3 TRP B 258 4.450 -64.430-47. 682 1.00 58.21 C ATOM 10 CZ3TRPB 2S8 5.747-64.513-48.163 1.00 58.20 C ATOM 11 CH2 TRP B 258 6.797 -64.949 -47.344 1.00 58.12 C ATOM 12 CZ2 TRP B 258 6.584 -65.3 13 -46.041 1.00 58.37 C ATOM 13 C TRPB258 0.572-66.479-44.825 1.0057.67 C ATOM 14 0 TRP B 258 1.064 -66.937 -43.790 1.00 57.71 0 ATOM 1 N SERB259 0.057-67.254.45.776 1.0057.66 N ATOM 2 CA SER B 259 -0.078 -68.706 -45.598 1.00 57.55 C ATOM 3 CB SERB259 -1.160-69.255-46.527 1.0057.60 C ATOM 4 OG SER B 259 -2.4 16 -68.667 -46.232 1.00 58.07 0 ATOM 5 C SER B 259 1.226 -69.478 -45.802 1.00 57.36 C ATOM 6 0 SERB 259 1.217 -70.686..46047 1.00 57.37 0 ATOM I N GLN B 260 2.344 -68.775 -45.689 1.00 57.11 N ATOM 2 CA GLN B 260 3.650 -69.384 -45.862 1.00 56.90 C ATOM 3 CB GLN B 260 4.659 -68.302 -46.240 1.00 57.05 C ATOM 4 CG GLNB 260 5.638-68.687-47.342 1.00 58.16 C ATOM 5 CD GLN B 260 4.957 -68.952 -48. 679 1.00 59.01 C ATOM 6 OE1 GLN B 260 3.889 -68.404 -48.970 1.00 59.19 0 ATOM 7 NE2 GLN B 260 5.578 -69.798 -49.499 1.00 58.96 N ATOM 8 C GLN B 260 4.059 -70.055 -44.556 1.00 56.43 C ATOM 9 0 GLN B 260 3.621 -69.640-43. 487 1.00 56.50 0 ATOM I N PRO B 261 4.877 -71.113 -44.634 1.00 56.02 N ATOM 2 CA PROB261 5.441-71.724-43.431 1.0055.81 C ATOM 3 CB PRO B 261 6.390 -72.785 -43.990 1.00 55.75 C ATOM 4 CG PROB261 5.810-73.132-45.313 1.0055.87 C ATOM 5 CD PRO B 261 5.277 -7 1.832 -45.853 1.00 56.03 C ATOM 6 C PRO B 261 6.208 -70.729 -42.564 1.00 55.59 C ATOM 7 0 PRO B 261 6.579 -69.652 -43.024 1.00 55.74 0 ATOM I N LEU B 262 6.443 -71.092 -41.313 1. 00 55.30 N ATOM 2 CA LEUB262 7.037-70.173-40.365 1.0055.12 C ATOM 3 CB LEU B 262 6.474 -70.457 -38.978 1.00 55.09 C ATOM 4 CG LEU B 262 5.736 -69.356 -38.2 16 1.00 54.85 C ATOM 5 CD1 LEUB 262 5.003-68.395-39.142 1.00 54.87 C ATOM 6 CD2 LEU B 262 4.758 -70.0 10 -37.276 1.00 54.29 C ATOM 7 C LEUB262 8.534-70.386-40.370 1.0055.14 C ATOM 8 0 LEU B 262 8.992 -71.518 -40.268 1.00 55.24 0 ATOM 1 N LEU B 263 9.302 -69.309 -40.504 1.00 55.24 N ATOM 2 CA LEU B 263 10.757 -69.433 -40.527 1.00 55.20 C ATOM 3 CB LEUB263 11.424-68.110-40.916 1.0055.14 C ATOM 4 CG LEUB 263 12.794-68.176-41.612 1.00 55.03 C ATOM 5 CDI LEU B 263 13.368 -66.781 -41.784 1.00 54.72 C ATOM 6 CD2 LEU B 263 13.794 -69.056 -40.873 1.00 55.07 C ATOM 7 C LEU B 263 11.234-69.875 -39.154 1.00 55.30 C ATOM 8 0 LEU B 263 11.621 -71.025 -38.962 1.00 55.01 0 ATOM I N VAL B 264 11.202-68.949-38.203 1.00 55.62 N ATOM 2 CA VALB264 11.550-69.260-36.824 1.0055.97 C ATOM 3 CB VAL B 264 12.484 -68.194 -36.214 1.00 55.83 C ATOM 4 CG1 VALB 264 12.011 -66.801 -36.566 1.00 55.89 C ATOM 5 CG2 VAL B 264 12.602 -68.376 -34.708 1.00 56.05 C ATOM 6 C VAL B 264 10.272 -69.448 -36.007 1.00 56.23 C ATOM 7 0 VALB264 9.618-68.484-35.632 1.0056.29 0 ATOM I N PRO B 265 9.926 -70.711 -35.722 1.00 56.68 N ATOM 2 CA PR0B265 8.590-71.109-35.296 1.0057.10 C ATOM 3 CB PRO B 265 8.583 -72.607 -35.601 1.00 57.09 C ATOM 4 CC PRO B 265 9.988 -73.022 -35.346 1.00 56.77 C ATOM 5 CD PRO B 265 10.843 -7 1.863 -35.792 1.00 56.60 C ATOM 6 C PR0B265 8.272-70.900-33.816 1.0057.60 C ATOM 7 0 PRO B 265 7.098 -70.934 -33.434 1.00 57.55 0 ATOM 1 N ASP B 266 9.290 -70.686 -32.987 1.00 58.11 N ATOM 2 CA ASP B 266 9.079 -70.770 -3 1.542 1.00 58.60 C ATOM 3 CB ASP B 266 10.389 -71.053 -30.775 1.00 58.96 C ATOM 4 CC ASP B 266 11.533 -70.141 -31.181 1.00 59.26 C ATOM 5 OD1 ASP B 266 11.436-68.920-30.940 1.00 60.12 0 ATOM 6 0D2 ASP B 266 12.545 -70.659 -3 1.706 1.00 59.63 0 ATOM 7 C ASP B 266 8.295 -69.6 17 -30.932 1.00 58.63 C ATOM 8 0 ASPB266 8.522-69.238-29.791 1.0058.80 0 ATOM I N ASN B 267 7.349 -69.085 -3 1.693 1.00 58.79 N ATOM 2 CA ASN B 267 6.502 -68.002 -3 1.220 1.00 58.87 C ATOM 3 CB ASN B 267 7.161 -66.657 -31.514 1.00 58.66 C * 40 ATOM 4 CG ASNB267 7.883-66.102-30.322 1.0058.19 C ATOM 5 OD1ASNB 267 7.410-66.229-29.197 1.0058.89 0 ATOM 6 ND2 ASN B 267 9.033 -65.483 -30. 552 1.00 57.38 N ATOM 7 C ASNB267 5.113-68.040-31.846 1.0059.27 C * ATOM 8 0 ASNB 267 4.383-67.045-31.818 1.00 59.19 0 ATOM 1 N ARG B 268 4.737 -69. 187 -32.406 1.00 59.60 N ATOM 2 CA ARG B 268 3.543 -69.204 -33.234 1.00 59.99 C ATOM 3 CB ARG B 268 3.5 14 -70.400 -34.200 1.00 60.07 C * ** ATOM 4 CG ARGB268 2.838-71.672-33.768 1.0060.90 C ATOM 5 CD ARGB268 2.359-72.379-35.039 1.0063.18 C * * 50 ATOM 6 NE ARGB268 2.404-73.840-34.985 1.0065.28 N ATOM 7 CZ ARGB268 3.504-74.570-35.179 1. 00 66.78 C ATOM 8 NHI ARG B 268 4.670 -73.975 -35.423 1.00 66.33 N ATOM 9 NH2ARGB268 3.443-75.902-35.119 1.0067.27 N ATOM 10 C A.RG B 268 2.259 -69.016 -32.443 1.00 60.01 C ATOM 11 0 ARG B 268 1.344 -68.351 -32.913 1.00 60.20 0 ATOM I N ARG B 269 2.2 13 -69.550 -3 1.229 1.00 60.18 N ATOM 2 CA ARC B 269 1.086 -69.298 -30 335 1.00 60.31 C ATOM 3 CB ARGB 269 1. 421 -69.759-28.916 1.00 60.47 C ATOM 4 CO ARG B 269 0.627 -70.966 -28.439 1. 00 61.18 C ATOM 5 CD ARG B 269 -0.752 -70.541 -27.930 1.00 62.47 C ATOM 6 NE ARG B 269 -1.734 -70.39 1 -29.005 1 00 62.90 N ATOM 7 CZ ARG B 269 -2.957 -70.9 19 -28.983 1.00 62.99 C ATOM 8 NH1 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 1.00 62.86 N ATOM 10 C ARG B 269 0.716 -67.818 -30.329 1.00 60.15 C ATOM 11 0 ARGB269 -0.443-67.449-30.540 1.0060.18 0 ATOM 1 N LEU B 270 1.719 -66.978 -30.094 1.00 60.00 N ATOM 2 CA LEU B 270 1.530 -65.539 -30.035 1.00 59.87 C ATOM 3 CB LEU B 270 2.863 -64.857 -29.733 1.00 59.80 C ATOM 4 CG LEU B 270 2.898 -63.460 -29.106 1.00 59.73 C ATOM 5 CD1 LEU B 270 3.052 -62.370 -30.149 1.00 59.80 C ATOM 6 CD2'LEU B 270 1.683 -63.2 14 -28.229 1.00 59.78 C ATOM 7 C LEUB 270 0.957-65.031 -31.346 1.00 59.92 C ATOM 8 0 LEU B 270 -0.016 -64.287 -31.358 1.00 60.09 0 ATOM I N PHE B 271 1.552 -65.455 -32.454 1. 00 60.22 N ATOM 2 CA PHE B 271 1.123 -65.006 -33.774 1.00 60.39 C ATOM 3 CB PHE B 271 2.020 -65.58 1 -34.870 1.00 60.47 C ATOM 4 CO PHE B 271 3.47 1 -65.224 -34.7 17 1.00 60.39 C ATOM 5 CD1 PHE B 271 3.847 -64.05 1 -34.072 1.00 60.01 C ATOM 6 CE1 PilE B 271 5.181 -63.716 -33.930 1.00 59.82 C ATOM 7 CZ PHE B 271 6.159 -64.546 -34.451 1.00 60.43 C ATOM 8 CE2PHEB271 5.798-65.718-35.105 1.0060.27 C ATOM 9 CD2 PHE B 271 4.458 -66.049 -35. 237 1.00 60.08 C ATOM 10 C PHE B 271 -0.326 -65.375 -34.044 1.00 60.56 C ATOM 11 0 PHEB 271 -1129-64.523-34.451 1.0060.91 0 ATOM 1 N GLU B 272 -0.672 -66.638 -33.8 19 1.00 60.53 N ATOM 2 CA GLU B 272 -2.057 -67.032 -34.002 1.00 6088 C ATOM 3 CB GLU B 272 -2.280 -68.554 -33.896 1.00 60.68 C ATOM 4 CO GLU B 272 -1.359 -69.330 -32.967 1.00 61.39 C ATOM 5 CD GLU B 272 -1.554 -70.852 -33,082 1.00 62.06 C ATOM 6 OEI GLU B 272 -1.025 -71.608 -32.228 1.00 63.50 0 ATOM 7 0E2 GLU B 272 -2.245 -71.301 -34.030 1.0064. 06 0 ATOM 8 C GLU B 272 -2.972 -66.221 -33.079 1.00 60.54 C ATOM 9 0 GLUB272 -4.000-65.707-33.518 1.0060.78 0 ATOM 1 N LEUB 273 -2.582-66.061 -31.819 1.00 60.28 N ATOM 2 CA LEU B 273 -3.385 -65.255 -30.904 1.00 60.15 C ATOM 3 CB LEU B 273 -2.765 -65.249 -29.505 1.00 60.05 C * 40 ATOM 4 CO LEUB 273 -3.567 -66.013 -28.454 1.00 59.60 C * *** *** ** ATOM S CD1 LEU B 273 -5.001 -65.525 -28.500 1.0060.64 C ATOM 6 CD2 LEU B 273 -3.523 -67.492 -28.688 1.00 59.04 C ATOM 7 C LEU B 273 -3.635 -63.819 -31.402 1.00 60.30 C ATOM 8 0 LEUB273 -4.785-63.350-31.454 1.0060.39 0 * 45 ATOM I N GLUB274 -2.559-63.128-31.769 1.0060.35 N ATOM 2 CA GLU B 274 -2.662 -61.747 -32.227 1.00 60.63 C ATOM 3 CB GLU B 274 -1,274 -61.173 -32.505 1.00 60. 61 C : *"* ATOM 4 CO GLU B 274 -0.341 -61.133 -31.294 1.00 61.23 C ATOM 5 CD GLU B 274 -0.625 -59.970 -30.352 1.00 62.07 C ATOM 6 OEI GLUB274 0.025-58.910-30.507 1.0062.22 0 * ATOM 7 0E2 GLU B 274 -1.496 -60.115 -29.462 1.00 62.05 0 ATOM 8 C GLU B 274 -3.525 -61.672 -33.481 1.00 60.74 C ATOM 9 0 GLU B 274 -4.423 -60.82 1 -33.603 1.00 60.90 0 ATOM I N GLU B 275 -3.252 -62.578 -34.4 10 1.00 60.89 N ATOM 2 CA GLU B 275 -4.061 -62.697 -35.607 1.00 61.09 C ATOM 3 CB GLU B 275 -3.606 -63.919 -36.392 1.00 61.28 C ATOM 4 CO GLU B 275 -4.061 -63.971 -37.832 1.00 62.13 C ATOM 5 CD GLU B 275 -3.647 -65.272 -38.492 1.00 63.38 C ATOM 6 OEI GLU B 275 -4.438 -65.821 -39.296 1.00 63.96 0 ATOM 7 0E2 GLU B 275 -2.533 -65.757 -38.185 1.00 63.30 0 ATOM 8 C GLUB275 -5.537-62.822-35.225 1.0061.04 C ATOM 9 0 GLUB275 -6.396-62.138-35.781 1.0060.86 0 ATOM I N GLN B 276 -5.823 -63.688 -34.260 1.00 61.18 N ATOM 2 CA GLNB276 -7.189-63.863-33. 773 1.0061.56 C ATOM 3 CB GLN B 276 -7.249 -64.934 -32.676 1.00 61.86 C ATOM 4 CG GLN B 276 -7.328 -66.357 -33.202 1.00 63.52 C ATOM 5 CD GLN B 276 -8.595 -66.593 -34008 1.00 66.43 C ATOM 6 OEL GLN B 276 -9.697 -66.659 -33.452 1.00 67.98 0 ATOM 7 NE2 GLN B 276 -8.447 -66.718 -35.326 1.00 67.10 N ATOM 8 C GLN B 276 -7.782 -62.550 -33.265 1.00 61.36 C ATOM 9 0 GLNB 276 -8.914-62.196-33.614 1.0061.33 0 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. 00 61.12 C ATOM 3 CB ASP B 277 -6.544 -59.973 -30.890 1.00 61.25 C ATOM 4 CG ASP B 277 -6.489 -60.757 -29.576 1.00 62.18 C ATOM 5 OD1 ASP B 277 -7.208 -61.774 -29.439 1.00 63.05 0 ATOM 6 0D2 ASP B 277 -5.723 -60.356 -28.670 1.00 63.07 0 ATOM 7 C ASP B 277 -7.866 -59.576 -33.010 1.00 60.97 C ATOM 8 0 ASP B 277 -8.984 -59.023 -33.065 1.00 61.14 0 ATOM I N LEUB 278 -6,911 -59.359-33.914 1.00 60.75 N ATOM 2 CA LEU B 278 -7.157 -58.435 -35.024 1.00 60.28 C ATOM 3 CB LEU B 278 -5.912 -58.273 -35.910 1.00 60.28 C ATOM 4 CG LEU B 278 -6.060 -57.508 -37.232 1.00 59.63 C ATOM 5 CD! LEU B 278 -6.308 -56.034 -36.98 1 1.00 58.86 C ATOM 6 CD2 LEU B 278 -4.834 -57.694 -38.107 1.00 59.64 C ATOM 7 C LEU B 278 -8.360 -58.894 -35.849 1.00 60.34 C ATOM 8 0 LEU 8278 -9.230 -58.091 -36.199 1.00 60.18 0 ATOM I N PHE B 279 -8.416 -60.190 -36.148 1.00 60.47 N ATOM 2 CA PHE B 279 -9.530 -60.706 -36.933 1.00 60.57 C ATOM 3 CB PHE8279 -9.397-62.197-37.221 1.0060.52 C ATOM 4 CG PHEB 279 -8.381 -62.511 -38.265 1.00 60.50 C ATOM 5 CD! PHE B 279 -7.966 -61.533 -39.154 1.00 60.16 C ATOM 6 CE! PHE B 279 -7.023 -61.808 -40.117 1.00 60.38 C ATOM 7 CZ PHE B 279 -6.492 -63.075 -40.213 1.00 60.80 C ATOM 8 CE2 PHE B 279 -6.908 -64.068 -39.335 1.00 60.94 C ATOM 9 CD2 PHE B 279 -7.846 -63.783 -38.369 1.00 60.60 C :. ATOM 10 C PHE B 279 -10.850 -60.418 -36.253 1.00 60.72 C * 40 ATOM 11 0 PHE B 279 -11.761 -59.888 -36.876 1.00 60.64 0 ATOM 1 N ARG B 280 -10.962 -60.758 -34.975 1.00 60.96 N ATOM 2 CA ARG B 280 -12.162 -60.380 -34.250 1.00 61.16 C ATOM 3 CB ARGB28O -12.049-60.714-32.760 1.00 61.05 C I... ATOM 4 CG ARGB28O -12.708-62.041-32.395 1.0061 56 C * 45 ATOM 5 CD ARG B 280 -12.596 -62. 359 -30.907 1.00 61.94 C ATOM 6 NE ARG 8280 -11.469 -63.243 -30.603 1.00 63. 84 N ATOM 7 CZ ARG B 280 -10.2 13 -62.833 -30.424 1.00 64.28 C : *s* ATOM 8 NH! ARG B 280 -9.910 -61.542 -30.520 1.0064.38 N ATOM 9 NI-I2ARGB28O -9.259-63.718-30.150 1.0064.17 N *. 50 ATOM 10 C ARGB28O -12.451-58.895-34.487 1.0061.05 C * ATOM 11 0 ARG 8 280 -13.571 -58.525 -34.856 1.00 60.89 0 ATOM 1 N ASP B 281 -11.432 -58.053 -34.322 1.00 61. 18 N ATOM 2 CA ASPB 281 -11.623 -56.605 -34.494 1.00 61.26 C ATOM 3 CB ASP B 28! -10.3 14 -55.846 -34.241 1.00 61.67 C ATOM 4 CG ASP B 281 -10.523 -54.555 -33.450 1.00 62.92 C ATOM 5 OD1 ASPB28I -11.661 -54.026-33.430!.0063.95 0 ATOM 6 0D2 ASP B 281 -9.541 -54.076 -32.835 1. 00 64.41 0 ATOM 7 C ASPB28I -12.200-56.222-35.863 1.0060.84 C ATOM 8 0 ASPB 281 -13.146-55.446-35.940 1.0060.76 0 ATOM 1 N ILE B 282 -11.625 -56.763 -36.935 1.00 60.54 N ATOM 2 CA 1LEB282 -12.116-56.507-38.294 1.0060.21 C ATOM 3 CB 1LEB282 -11.226-57.185-39.349 1.0060.12 C ATOM 4 COl ILE B 282 -9.8 16 -56.592 -39.336 1.00 60.23 C ATOM 5 CDI ILE B 282 -8.799 -57.4 15 -40.105 1.00 59.99 C ATOM 6 CG2 ILE B 282 -11.857 -57.075 -40.733 1.00 59.55 C ATOM 7 C ILE B 282 -13 509 -57.077 -38 474 1.00 60.29 C ATOM 8 0 ILE B 282 -14.445 -56.371 -38.826 1.00 60.29 0 ATOM I N GLN B 283 -13.628 -58.375 -38.232 1.00 60.51 N ATOM 2 CA GLNB283 -14.874-59.096-38.404 1.0060.54 C ATOM 3 CB GLNB283 -14.718-60.538-37.919 1.0060.59 C ATOM 4 CG GLN B 283 -15 750 -61.500 -38.479 1.00 61.30 C ATOM 5 CD GLNB283 -16.834-61.830-37.479 1.0062.16 C ATOM 6 OE1 GLN B 283 -18.015 -61.936 -37.829 1.00 62.37 0 ATOM 7 NE2 GLN B 283 -16.438 -61.995 -36.219 1.00 62.82 N ATOM S C GLN B 283 -15.998 -58.403 -37.660 1.00 60.41 C ATOM 9 0 GLN B 283 -17.160 -58.514 -38.045 1.00 60.58 0 ATOM I N GLY 13 284 -15. 645 -57.670 -36.608 1.00 60.32 N ATOM 2 CA GLY B 284 -16 642 -56.993 -35.785 1.00 59.90 C ATOM 3 C GLY B 284 -17.147 -55.656 -36.307 1.00 59.63 C ATOM 4 0 GLY B 284 -18.036 -55.052 -35.708 1.00 59.69 0 ATOM I N LEU B 285 -16.596 -55.194 -37.425 1.00 59.39 N ATOM 2 CA LEUB285 -16.897-53.848-37.933 1.0059.12 C ATOM 3 CB LEU B 285 -15.994 -53.498 -39.122 1.00 58.97 C ATOM 4 CG LEU B 285 -14.509 -53.305 -38.827 1.00 58.44 C ATOM 5 CD1 LEU 13 285 -13.791 -52.805 -40.064 1.00 58.10 C ATOM 6 CD2 LEU B 285 -14.322 -52.345 -37.673 1.00 58.23 C ATOM 7 C LEUB 285 -18.364-53.581 -38.295 1.00 59.12 C ATOM 8 0 LEU B 285 -18.966 -52.638 -37.773 1.00 58.98 0 ATOM I N PRO B 286 -18.944 -54.409 -39.185 1.00 59. 17 N ATOM 2 CA PRO B 286 -20.292 -54.145 -39.680 1.00 59.19 C ATOM 3 CE PR0B286 -20.575-55.339-40.595 1.0059.12 C ATOM 4 CG PROB286 -19.244-55.870-40.958 1.0059.19 C ATOM 5 CD PRO B286 -18.388-55.648-39. 756 1.00 59.17 C ATOM 6 C PRO B 286 -21.289 -54.132 -38.541 1.00 59.26 C ATOM 7 0 PRO B 286 -22.246 -53.357 -38.560 1.00 59.19 0 ATOM 1 N ARG B 287 -2 1.053.54.989 -37.552 1.00 59.46 N ATOM 2 CA ARG B 287 -2 1.912 -55.057 -36.384 1.0059.64 C ATOM 3 CE ARGB 287 -21.297-55.921 -35.291 1.00 59.76 C ATOM 4 CG ARG B 287 -22.268 -56.326 -34.193 1.00 60.10 C ATOM 5 CD ARGB 287 -21.647-57.427-33.373 1.00 61.21 C ATOM 6 NE ARG B 287 -20.970 -58. 384 -34.246 1.00 62.03 N ATOM 7 CZ ARG B 287 -19.899 -59.089 -33.899 1.00 62.52 C ATOM 8 N}I1 ARG B 287 -19.352 -59.933 -34.765 1.00 62.89 N ATOM 9 NH2 ARG B 287 -19.371 -58.943 -32.691 1.00 62.75 N ATOM 10 C ARGB 287 -22.185.53.659-35.866 1.00 59.65 C : ATOM 11 0 ARGB287.23.290-53.378-35.409 1.0059.81 0 ATOM I N H1SB288.21.194-52.772-35.937 1.0059.63 N ATOM 2 CA HIS B 288.21.5 17 -5 1.366 -35.722 1.00 59.67 C ATOM 3 CB HIS B 288 -21.830 -51.042 -34.267 1.00 59.99 C * ATOM 4 CG H1SB288 -23.288-50.816-34.035 1.0061.01 C ATOM 5 NDI HIS B 288 -24.084 -50.164.34.954 1.00 61.71 N ATOM 6 CEI HIS B 288.25.326 -50.118 -34.502 1.00 62.63 C ATOM 7 NE2 HIS B 288.25.364-50. 719 -33.325 1.00 62.85 N ATOM 8 CD2HISB288 -24.103-51.171-33.013 1.0062.15 C ATOM 9 C HIS B 288 -20.7 13 -50.263 -36.383 1.00 59.26 C ATOM 10 0 HIS B 288 -19.713 -49.774 -35.856 1.00 59.07 0 ATOM I N ALA B 289 -21.221 -49.867 -37.543 1.00 58.88 N ATOM 2 CA ALA B 289 -20.802 -48.660 -38.2 15 1.00 58.55 C ATOM 3 CB ALA B 289 -21.132 -48.746 -39.701 1.00 58.66 C ATOM 4 C ALA B 289 -21.5 13 -47.468 -37.582 1.00 58.24 C ATOM 5 0 ALA B 289 -20.964 -46.372 -37.524 1.00 58.03 0 ATOM 1 N ALA B 290 -22.733 -47.688 -37.102 1.00 57.82 N ATOM 2 CA ALA B 290 -23.524 -46.609 -36.525 1.00 57.55 C ATOM 3 CB ALA B 290 -24.807 -47.154 -35.945 1.00 57.56 C ATOM 4 C ALA B 290 -22.752 -45.822 -35.467 1.00 57.41 C ATOM 5 0 ALAB29O -22.784-44.587-35.446 1.0057.25 0 ATOM 1 N LEUB29I -22.057-46.542-34.594 1.0057.29 N ATOM 2 CA LEU B 291 -21.296 -45.916 -33.521 1.00 57.23 C ATOM 3 CB LE1J B 291 -20.743 -46.984 -32.575 1.00 57.15 C ATOM 4 CO LEU B 291 -20.611 -46.65 1 -31 087 1.00 56.86 C ATOM 5 CDI LEU B 291 -19.866 -47. 763 -30.376 1.00 56.79 C ATOM 6 CD2 LEU B 291 -19.907 -45.328 -30.867 1.00 57.08 C ATOM 7 C LEU B 291 -20.158 -45.059 -34.081 1.00 57.31 C ATOM 8 0 LEU B 291 -20.002 -43.894 -33.703 1.00 57.24 0 ATOM I N ARG B 292 -19.366 -45.629 -34.986 1.00 57.43 N ATOM 2 CA ARG B 292 -18.224 -44.901 -35.540 1.00 57.57 C ATOM 3 CB ARG 13 292 -17.290 -45.826 -36.338 1.00 57.62 C ATOM 4 CO ARG B 292 -17.564 -45.912 -37.834 1.00 57.76 C ATOM 5 CD ARG B 292 -16.564 -45.093 -38.644 1.00 57.94 C ATOM 6 NE ARG B 292 -16.928 -45.049 -40.060 1.00 58.09 N ATOM 7 CZ ARGB292 -17.435-43.984-40.674 1.0057.92 C ATOM 8 NIh ARG B 292 -17.741 -44.043 -41.960 1.00 58.28 N ATOM 9 NH2ARGB292 -17.633-42.855-40.009 1.00 58.17 N ATOM 10 C ARG B 292 -18.704 -43.718 -36.375 1.00 57.46 C ATOM 11 0 ARG B 292 -18.088 -42.648 -36.363 1.00 57.56 0 ATOM 1 N LYS B 293 -19.812 -43.912 -37.081 1.00 57. 36 N ATOM 2 CA LYS B 293 -20.442 -42.831 -37.8 16 1.00 57.19 C ATOM 3 CB LYS B 293 -2 1.686 -43.323 -38.553 1.00 5719 C ATOM 4 CG LYSB293 -21.386-44.029-39.863 1.0057.17 C ATOM 5 CD LYSB 293 -22.550-44.901 -40.305 1.00 57.02 C ATOM 6 CE LYSB293 -22.257-45.577-41.635 1.0057.19 C ATOM 7 NZ LYS B 293 -23.249-46.645 -41.939 1.00 57.34 N ATOM 8 C LYS B 293 -20.804 -41.729 -36.840 1.00 57.09 C ATOM 9 0 LYSB293 -20.365-40.588-36.991 1.0057.11 0 ATOM 1 N LEU B 294 -2 1.591 -42.079 -35.828 1.00 56.95 N ATOM 2 CA LEU B 294 -21.958 -41.121 -34 800 1.00 56.84 C ATOM 3 CB LEU B 294 -22 623 -41.836 -33.624 1.00 56.79 C ATOM 4 CO LEU B 294 -22.941 -40.974 -32.400 1.00 56.79 C S.'.. ATOM 5 CD! LEUB 294 -23.835-39.809-32.786 1.00 57.30 C ATOM 6 CD2LEUB294 -23.595-41.802-31. 315 1.00 56.83 C ATOM 7 C LEU B 294 -20.726 -40.348 -34.333 1.00 56.79 C ATOM 8 0 LELJ B 294 -20.667 -39.112-34.429 1.00 56.76 0 ATOM 1 N ASN B 295 -19.736 -4 1.084 -33.844 1.00 56.85 N ATOM 2 CA ASN B 295 -18.503 -40.469 -33.356 1.00 56.94 C ATOM 3 CB ASN B 295 -17.499 -41.549 -32.961 1.00 57.00 C ATOM 4 CG ASN B 295 -17.415 -41.708 -31.447 1.00 57.02 C :.. ATOM 5 ODI ASNB295 -17.582-42.815-30.911 1.0056.80 0 * ATOM 6 ND2 ASN B 295 -17.156 -40.594 -30.743 1.00 57.22 N : ATOM 7 C ASNB295 -17.855-39.494-34.338 1.0056.98 C ATOM 8 0 ASN B 295 -17.529 -38.355 -33.986 1.00 56.90 0 ATOM 1 N ASP B 296 -17.663 -39.939 -35.572 1.00 57. 20 N ATOM 2 CA ASP B 296 -17.044 -39.075 -36.564 1.00 57.27 C ATOM 3 CB ASP B 296 -16.740 -39.854 -37.843 1.00 57.49 C ATOM 4 CO ASP B 296 -15.732 -40.978 -37.613 1.00 58.34 C ATOM 5 OD1 ASPB296 -15.736-41.950-38.398 1. 00 59.28 0 ATOM 6 OD2ASPB296 -14.941 -40.898-36.642 1.0059.32 0 ATOM 7 C ASP B 296 -17.909 -37.844 -36.826 1.00 57 08 C ATOM 8 0 ASP B 296 -17.386 -36.745 -37 049 1.00 5696 0 ATOM I N LEU B 297 -19.228 -38.027 -36.768 1.00 56.92 N ATOM 2 CA LEUB 297 -20.152-36.901 -36.856 1.00 56.71 C ATOM 3 CB LEU B 297 -2 1.610 -37.360 -36.779 1.00 56.70 C ATOM 4 CC LEUB297 -22.645-36.289-37.147 1.0057.00 C ATOM 5 CDI LEUB297 -22.838-36212-38.653 1.0057.18 C ATOM 6 CD2 LEt) B 297 -23.986 -36.538 -36.466 1.00 57.32 C ATOM 7 C LEU B 297 -19.857 -35.904 -35.743 1.00 56.57 C ATOM 8 0 LEU B 297 -19.723 -34.709 -36.001 1.00 56.57 0 ATOM 1 N VAL B 298 -19.746 -36.394 -34.509 1.00 56.40 N ATOM 2 CA VALB298 -19.372-35.528-33.385 1.0056.20 C ATOM 3 CB VAL B 298 -19.201 -36.323 -32.082 1.00 56.10 C ATOM 4 CG1 VAL B 298 -18.713 -35.414 -30.963 1.00 55.78 C ATOM 5 CG2 VA!. 13 298 -20.494 -37.011 -3 1.700 1.00 55.98 C ATOM 6 C VAL B 298 -18.062 -34.781 -33.644 1.00 56.34 C ATOM 7 0 VALB298 -17.990-33.550-33.511 1.0056.51 0 ATOM 1 N LYS B 299 -17.023 -35.532 -34.003 1.00 56.48 N ATOM 2 CA LYS B 299 -15. 707 -34.944 -34.234 1.00 56.48 C ATOM 3 CB LYS B 299 -14.723 -36.009 -34.720 1.00 56.50 C ATOM 4 CC LYSB299 -14.428-37.118-33.712 1.0056.54 C ATOM 5 CD LYS B 299 -13.557 -38.204 -34.340 1.00 56.73 C ATOM 6 CE LYS B 299 -13. 154 -39.272 -33.329 1.00 57.33 C ATOM 7 NZ LYS B 299 -12.203 -38.749 -32.3 12 1.00 57.04 N ATOM 8 C LYS B 299 -15.812 -33.824 -35.260 1.00 56.44 C ATOM 9 0 LYS B 299 -15.372 -32.676 -35.023 1.00 56.62 0 ATOM I N ARGB300 -16.410-34.158-36.401 1.0056.46 N ATOM 2 CA ARGB300 -16.647-33.159-37.427 1.0056.31 C ATOM 3 CB ARG B 300 -17.485 -33.720 -38.576 1.00 56.27 C ATOM 4 CC ARG 13300 -17.978 -32.651 -39.546 1.00 56.17 C ATOM 5 CD ARG B 300 -18.774 -33.246 -40.692 1.00 56.14 C ATOM 6 NE ARC B 300 -17.929 -33.563 -41.836 1.00 56.16 N ATOM 7 CZ ARGB300 -18.030-32.970-43.021 1.0056.53 C ATOM 8 NI-Il ARG B 300 -17.222 -33.317 -44.013 1.00 56.30 N ATOM 9 NH2ARGB300 -18.950-32.037-43.218 1.0056.98 N ATOM 10 C ARC B 300 -17.334 -3 1.952 -36.802 1.00 56.37 C ATOM 11 0 ARG B 300 -16.829 -30.834 -36.887 1.00 56.39 0 ATOM 1 N ALA B 301 -18.473 -32.186 -36.154 1.00 56.45 N :. ATOM 2 CA ALAS 301 -19.214-31.106-35.509 1.00 56.41 C * ATOM 3 CB ALA B 301 -20.258 -31.660 -34.552 1.00 56.29 C ATOM 4 C ALA B 301 -18.261 -30.172 -34.779 1.00 56.46 C ATOM 5 0 ALAB 301 -18.222-28.971-35.062 1.00 56.47 0 ATOM 1 N ARGB3O2 -17.480-30.728-33.858 1.0056.55 N ATOM 2 CA ARG B 302 -16.535 -29.923 -33.075 1.00 56.77 C ATOM 3 CB ARC B 302 -15.760 -30. 8 18 -32.106 1.00 56.86 C *:: ATOM 4 CG ARC B 302 -16.666 -31.4 14 -31.043 1.00 57.73 C ATOM 5 CD ARGB3O2 -16.137-32.710-30.479 1.0059.51 C : ,** 50 ATOM 6 NE ARGB3O2 -15.204-32.490-29.380 1.0061.12 N ATOM 7 CZ ARGB3O2 -13.883-32.597-29.490 1.0062.12 C *. : ATOM 8 NH1 ARGB 302 -13.331 -32.927-30.655 1.00 62.16 N * * ATOM 9 NH2ARGB3O2 -13.112-32.381-28.431 1.0062.71 N ATOM 10 C ARC B 302 -15.593 -29.087 -33.951 1.00 56.68 C ATOM 11 0 ARC B 302 -15.424 -27.862 -33.734 1.00 56.68 0 ATOM 1 N LEU B 303 -15.003 -29.735 -34.956 1.00 56.67 N ATOM 2 CA LEUB3O3 -14.163-28.990-35.902 1.0056.63 C ATOM 3 CS LEU B 303 -13.583 -29.913 -36.973 1.00 56.59 C ATOM 4 CG LEU B 303 -12.682 -29.195 -37.981 1.00 56.67 C ATOM 5 CD! LEU B 303 -11.413 -28.699 -37.301 1.00 56.50 C ATOM 6 CD2 LEU B 303 -12.344 -30.106 -39.150 1.00 57.07 C ATOM 7 C LEU B 303 -14.933 -27.832 -36.560 1.00 56.59 C ATOM 8 0 LEU B 303 -14.471 -26.677 -36.576 1.00 56.69 0 ATOM 1 N VALB3O4 -16.106-28.149-37.102 1.0056.40 N ATOM 2 CA VAL B 304 -16.982 -27.143 -37.684 1.00 56.15 C ATOM 3 CB VAL B 304 -18.362 -27.728 -38.028 1.00 56.03 C ATOM 4 CG1 VAL B 304 -19.301 -26.633 -38.494 1.00 55.85 C ATOM 5 CG2VALB3O4 -18.228-28.800-39.086 1.0055.67 C ATOM 6 C VAL B 304 -17.155 -25.971 -36.724 1.00 56.22 C ATOM 7 0 VAL B 304 -16.819 -24.832 -37.058 1.00 56.31 0 ATOM I N ARG B 305 -17.666 -26.249 -35.527 1.00 56.24 N ATOM 2 CA ARG B 305 -17.864 -25.195 -34.532 1.00 5628 C ATOM 3 CB ARG B 305 -18.260-25.783 -33.169 1.00 56.25 C ATOM 4 CG ARG B 305 -17.825 -24.96 I -31.964 1.00 56.53 C ATOM 5 CD ARG B 305 -18.985 -24.659 -3 1.011 1.00 57.09 C ATOM 6 NE ARG B 305 -19.403 -25.757 -30.137 1.00 57.25 N ATOM 7 CZ ARG B 305 -18.624 -26.746 -29.709 1.00 57.93 C ATOM 8 NH! ARG B 305 -19.132 -27.680 -28.915 1.00 57.81 N ATOM 9 N1-12 ARO B 305 -17.345 -26.809 -30.063 1.00 58.76 N ATOM 10 C ARGB 305 -16.626-24.303-34.435 1.00 56.28 C ATOM 11 0 ARGB 305 -16.723 -23.058-34.526 1.00 56.39 0 ATOM I N VAL B 306 -15.456 -24.931 -34.294 1.00 56.35 N ATOM 2 CA VAL B 306 -14.227 -24.136 -34.253 1.00 56.27 C ATOM

3 CB VALB3O6 -12.987-25.017-34.201 1.0056.15 C ATOM 4 CG1 VALB 306 -11.767-24.162-33.924 1.0056.18 C ATOM 5 CG2VALB3O6 -13.152-26.085-33.145 1.0056.17 C ATOM 6 C VALB3O6 -14.108-23.217-35.474 1.0056.36 C ATOM 7 0 VALB3O6 -14.036-21.983-35.351 1.00 56.51 0 ATOM 1 N HIS B 307 -14.088 -23.822 -36.656 1.00 56.41 N ATOM 2 CA HISB3O7 -13.971-23.049-37.890 1.005644 C ATOM 3 CB HIS B 307 -14.243 -23.942 -39.100 1.00 56.45 C ATOM 4 CG HIS B 307 -14.152 -23.225 -40.409 1.00 55.91 C ATOM 5 ND1 HISB 307 -12.949-22.849-40.969 1.00 55.76 N ATOM 6 CE1 HIS B 307 -11172 -22.245 -42.123 1.00 55.92 C ATOM 7 NE2 HIS B 307 -14.476 -22.221 -42.335 1.00 56.18 N ATOM 8 CD2HISB3O7 -15.112-22.827-41.277 1.0055.83 C ATOM 9 C HISB3O7 -14.927-21.856-37.902 1.0056.54 C ATOM 10 0 HIS B 307 -14.523 -20.712 -38.178 1.00 56.69 0 * ATOM 1 N ALAB3O8 -16.196-22.138-37.602 1.0056.50 N **.

ATOM 2 CA ALA B 308 -17.222 -21.106 -37.541 1.00 56.41 C ** ATOM 3 CB ALA B 308 -18.500 -21.659 -36.962 1.00 56.25 C ATOM 4 C ALA B 308 -16.711 -19.972 -36.685 1.00 56.41 C ATOM 5 0 ALA B 308 -16.653 -18.819-37.132 1.00 56.62 0 s's. ATOM 1 N TYRB3O9 -16.314-20.299-35.459 1.0056.40 N *....: ATOM 2 CA TYRB3O9 -15.811-19.251-34.584 1.0056.51 C * * ATOM 3 CB TYRB3O9 -15.368-19.809-33.233 1.0056.57 C ATOM 4 CG TYRB 309 -16.521 -20.031 -32.285 1.00 56.51 C : *". 50 ATOM 5 CDI TYRB 309 -16.661 -21.225 -31.596 1.00 56.48 C ATOM 6 CEITYRB3O9 -17.719-21.429-30.733 1.0056.59 C * . : ATOM 7 CZ TYR B 309 -18.659 -20.436 -30.560 1.00 56.61 C ATOM 8 OH TYRB 309 -19.715-20.639-29.705 1.00 56.68 0 ATOM 9 CE2 TYR B 309 -18.548 -19.243 -3 1.239 1.00 56.61 C ATOM 10 CD2 TYR B 309 -17.485 -19.048 -32.097 1.00 56.59 C ATOM 1! C TYR B 309 -14.693 -18.455 -35.251 1.00 56.61 C ATOM 12 0 TYRB3O9 -14.750-17.219-35.302 1.0056.91 0 ATOM 1 N ILEB 310 -13.693-19.158-35.781 1.00 56.59 N ATOM 2 CA ILE B 310 -12.568 -18.486 -36.444 1.00 56.63 C ATOM 3 CB ILEB3IO -11.613-19.492-37.109 1.0056.52 C ATOM 4 CG1 ILE B 310 -11.052-20.463 -36.074 1.00 56.47 C ATOM 5 CD1 ILE B 310 -10.286 -2 1.610 -36.681 1.00 56.57 C ATOM 6 CG2 ILE B 310 -10.480 -18.768 -37.804 1.00 56.40 C ATOM 7 C ILE B 310 -13.023 -17.463 -37.496 1.00 56.78 C ATOM 8 0 ILE B 310 -12.692 -16.258 -37.410 1.00 57. 05 0 ATOM I N ILE B 311 -13.783 -17.938 -38.484 1.00 56.75 N ATOM 2 CA ILE B 311 -14.250 -17.046 -39.545 1.00 56.82 C ATOM 3 CB ILE B 311 -15.107 -17.771 -40.602 1.00 56.78 C ATOM 4 CGI ILEB 311 -14.243-18.232-41.774 1.00 56.78 C ATOM 5 CDIILEB3II -13.214-19.266-41.422 1.0057.40 C ATOM 6 CG2ILEB3II -16.155-16.834-41.167 1.00 57.09 C ATOM 7 C ILE B 311 -15.032 -15.882 -38.951 1.00 56.87 C ATOM 8 0 ILE B 311 -14.757 -14.7 14 -39.253 1.00 56.99 0 ATOM I N SER B 312 -15.995 -16.205 -38.091 1.00 56.92 N ATOM 2 CA SERB3I2 -16.804-15.181-37.447 1.005706 C ATOM 3 CB SERB 312 -17.681 -15.797-36.362 1.00 57.04 C ATOM 4 OG SER B 312 -18.624 -16.687 -36.931 1.00 57.03 0 ATOM 5 C SER B 312 -15.937 -14.078 -36.855 1.00 57.22 C ATOM 6 0 SER B 312 -16.133 -12.896 -37.157 1.00 57.33 0 ATOM I N TYRB3I3 -14.974-14.464-36.019 1.0057.40 N ATOM 2 CA TYRB3I3 -14.091-13.479-35.382 1.0057.83 C ATOM 3 CB TYRB 313 -13.138-14.142-34.380 1.00 58.15 C ATOM 4 CG TYRB 313 -13.757-14.429-33.019 1.0058.84 C ATOM S CD! TYRB 313 -13.076-14.120-31.842 1.0059.36 C ATOM 6 CEI 1'YR B 313 -13.637 -14.383 -30.593 1.00 59.39 C ATOM 7 CZ TYRB 313 -14.895-14.957-30.515 1.00 59.16 C ATOM 8 OH TYR B 313 -15.457 -15.219 -29.286 1.00 59.00 0 ATOM 9 CE2 1'YR B 313 -15.593 -15.269 -31.667 1.00 59.29 C ATOM 10 CD2 TYR B 313 -15.025 -15.004 -32.909 1.00 59.34 C ATOM 11 C TYRB3I3 -13.315-12.657-36.412 1.0057.75 C ATOM 12 0 TYR B 313 -13.234-11.423 -36.305 1.00 57.91 0 ATOM I N LEUB3I4 -12.757-13.328-37.418 1.0057.51 N ATOM 2 CA LEU B 314 -12.069 -12.590 -38.480 1.00 57.40 C ATOM 3 CB LEU B 314 -11.557-13.550-39.553 1.00 57.20 C ATOM 4 CU LEU B 314 -10.394 -14.430 -39.093 1.00 56.64 C ATOM 5 CDI LEU B 314 -10.239 -15.648 -39.978 1.00 55.97 C ATOM 6 CD2LEUB314 -9.112-13.622-39.047 1.00 56.28 C ATOM 7 C LEUB314 -12.981-11.514-39.088 1.0057.49 C ATOM 8 0 LEUB 314 -12.638-10.316-39.130 1.0057.84 0 ATOM I N LYSB3I5 -14.156-11.949-39.539 1.0057.46 N ATOM 2 CA LYSB 315 -15.124-11.045-40.158 1.00 57.51 C ATOM 3 CB LYS B 315 -16.380-11.804 -40.593 1.00 57.50 C ATOM 4 CG LYSB3IS -17.579-10.920-40.897 1.0057.23 C ATOM 5 CD LYSB 315 -17.328-10.022-42.090 1.00 57.26 C ATOM 6 CE LYSB 315 -18.512 -9.103-42.327 1.00 57.59 C ATOM 7 NZ LYSB3I5 -18458 -8.446-43.665 1.005778 N ATOM 8 C LYS B 315 -15.503 -9.898 -39.235 1.00 57.60 C *** 50 ATOM 9 0 LYS B 315 -15.604 -8.753 -39.676 1.00 57.65 0 ATOM 1 N LYSB316 -15.717-10.202-37.958 1.0057.67 N ATOM 2 CA LYS B 316 -16.071 -9.156 -37.003 1.00 57.96 C ATOM 3 CB LYS B 316 -16.594 -9.747 -35.685 1.00 58. 04 C ATOM 4 CU LYSB 316 -15.533-10.014-34.617 1.00 58.13 C ATOM 5 CD LYSB3I6 -16.133-10.748-33.420 1.0058.14 C ATOM 6 CE LYSB 316 -15.059-11.212-32. 442 1.00 58.37 C ATOM 7 NZ LYS B 316 -14.405 -10.080 -3 1.724 1.00 58.37 N ATOM 8 C LYS B 316 -14.886 -8.223 -36.755 1.00 57.99 C ATOM 9 0 LYS B 316 -15.059 -7.095 -36.293 1.00 57.89 0 ATOM 1 N GLUB3I7 -13.683 -8.693-37. 071 1.0058.12 N ATOM 2 CA GLU B 317 -12.504.7.848 -36.916 1.00 58.35 C ATOM 3 CR GLU B 317 -11.252 -8.689 -36.655 1.00 58.34 C ATOM 4 CG GLU B 317 -10.222 -7.983 -35.796 1.00 58.29 C ATOM 5 CD GLU B 317 -10.786 -7.568 -34.449 1.00 58.49 C ATOM 6 OEI GLU B 317 -10.392 -6.495 -33.940 1.00 58.78 0 ATOM 7 OE2GLUB3I7 -11.630 -8.311 -33.901 1.0058.20 0 ATOM 8 C GLUB317 -12.291 -6.929-38.118 1.0058.52 C ATOM 9 0 GLUB3I7 -11.812 -5.806-37.964 1.0058.43 0 ATOM I N METB3I8 -12.647 -7.408-39.309 1.0058. 76 N ATOM 2 CA METB 318 -12.457 -6.621 -40.544 1.00 59.38 C ATOM 3 CB METB3I8 -12.850 -7.457-41.761 1.0059.35 C ATOM 4 CO METB3I8 -11.790 -8.450-42.180 1.0059.35 C ATOM 5 SD METB 318 -10.352 -7627 -42.883 1.00 59.21 S ATOM 6 CE METB3I8 -11.089 -6.840-44.315 1.0059.36 C ATOM 7 C MET B 318 -13.194 -5.273 -40.591 1.00 59.81 C ATOM 8 0 MET B 318 -14.370 -5.198 -40.242 1. 00 59.90 0 ATOM I N PROB319 -12.501 -4.208-41.048 1.0060.27 N ATOM 2 CA PRO B 319 -13.070 -2.859 -41.164 1.00 60.66 C ATOM 3 CR PRO B 319 -11.830 -1. 968 -41.230 1.00 60.60 C ATOM 4 CO PROB319 -10.811 -2.817-41.904 1.0060.41 C ATOM 5 CD PROB 319 -11.097 -4.248 -41.497 1.00 60.27 C ATOM 6 C PROB319 -13.898 -2.698-42.437 1.0061.12 C ATOM 7 0 PROB319 -13.536 -3.243-43.484 1.0061.23 0 ATOM I N THRB32O -14.988 -1.936-42.346 1.0061.63 N ATOM 2 CA THR B 320 -15.997 -1.880 -43.413 1.00 62.20 C ATOM 3 CB THRB32O -17 120 -0.850-43.106 1.0062.25 C ATOM 4 OGI THRB 320 -16.676 0.476-43.428 1.00 62.39 0 ATOM 5 CG2TH RB32O -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 0 THRB 320 -15.468 -2.492 -45.683 1.00 62.58 0 ATOM I N VAL B 321 -14.951 -0.398 -45.043 1.00 62.79 N ATOM 2 CA VAL B 321 -14.629 0.029 -46.401 1.00 63.06 C ATOM 3 CB VAL B 321 -15.352 1.360 -46.761 1.00 63.09 C ATOM 4 CGI VAL B 321 -15.052 2.457 -45.687 1.00 63.09 C ATOM 5 CG2 VAL B 321 -14.989 1.830 -48.206 1.00 63. 21 C ATOM 6 C VALB32I -13.125 0.097-46.726 1.0063.21 C ATOM 7 0 VALB321 -12.677 -0.527-47.693 1.0063.23 0 ATOM I N PHE B 322 -12.346 0.829 -45. 930 1.00 63.40 N * ATOM 2 CA PHE B 322 -10.911 0.966 -46.222 1.00 63.56 C * *..

ATOM 3 CB PHE B 322 -10.553 2.392 -46.676 1.00 63.65 C ATOM 4 CG PHEB 322 -11.291 3.475 -45.943 1.00 63.76 C ATOM 5 CD1 PHE B 322 -12.129 4.341 -46.630 1.00 63.84 C ATOM 6 CEIPHEB322 -12.811 5.344-45.964 1.0064.14 C ATOM 7 CZ PHEB 322 -12.657 5.492-44.594 1.00 64.13 C : ATOM 8 CE2 PHE B 322 -11.822 4.636 -43.898 1.00 64.19 C * * ATOM 9 CD2 PHE B 322 -11.143 3.633 -44.572 1.0064.04 C ATOM 10 C PHE B 322 -9.959 0.500-45.119 1.00 63.57 C : *. 50 ATOM 11 0 PHEB322 -10.289 0.536-43.932 1.0063.52 0 ATOM I N GLYB323 -8.771 0.074-45.542 1.0063.63 N **. : ATOM 2 CA GLY B 323 -7.757 -0.470 -44.645 1.00 63.75 C ATOM 3 C GLY B 323 -7.631 -1.967 -44.841 1.00 63.84 C ATOM 4 0 GLY B 323 -6.624 -2.574 -44.481 1.00 63.82 0 ATOM I N LYSB324 -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 CO LYS B 324 -9.836 -3.122 -47.823 1.00 64.51 C ATOM 5 CD LYSB324 -10.857 -3.392-48.931 1.0064.43 C ATOM 6 CE LYS B 324 -12 196 -3.883 -48.375 1.00 64.92 C ATOM 7 NZ LYS B 324 -12.780 -2.994 -47.323 1.00 64.78 N ATOM 8 C LYSB324 -7.512 -4.807-45.813 1.0064.09 C ATOM 9 0 LYS B 324 -7.325 -5.828 -45.148 1 00 64.04 0 ATOM I N GLU B 325 -6.632 -4.361 -46.706 1.00 64.10 N ATOM 2 CA GLU B 325 -5.46 1 -5.152 -47.102 1.00 64.12 C ATOM 3 CB GLUB325 -4.669 -4.416-48.191 1.0064.09 C ATOM 4 CG GLUB325 -5.490 -4.058-49.424 1.00 63.96 C ATOM 5 CD GLU B 325 -4.531 -4.963 -49.990 0.00 50.00 C ATOM 6 OE1 GLU B 325 -4.590 -5.825 -49.100 0.00 50.00 0 ATOM 7 0E2 GLU B 325 -4.164 -5.171 -51.156 0.00 50. 00 0 ATOM 8 C GLU B 325 -4.530 -5.549 -45.942 1 00 64.19 C ATOM 9 0 GLUB 325 -4.310 -6.781 -45.669 1.00 64.25 0 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 ASNB 326 -2.040 -3.633-43.942 1.00 64.30 C ATOM 4 CG ASN B 326 -2.752 -2.335 -43.604 1.00 64.30 C ATOM 5 OD1 ASN B 326 -2.563 -1.317 -44.277 1.00 64.17 0 ATOM 6 ND2 ASN B 326 -3.558 -2.357 -42.545 1.0064.50 N ATOM 7 C ASNB326 -3.681 -5.330-42.925 1.0064.35 C ATOM 8 0 ASN B 326 -3.046 -5.991 -42.099 1.00 64.40 0 ATOM 1 N LYS B 327 -4.972 -5.038 -42.779 1.00 64.30 N ATOM 2 CA LYS B 327 -5.744 -5.569 -41.664 1.00 64.23 C ATOM 3 CB LYS B 327 -7.138 -4.943 -41.602 1.00 64.22 C ATOM 4 CO LYS B 327 -7.630 -4.643 -40.184 1.00 64.25 C ATOM 5 CD LYSB 327 -7.454 -5.831 -39.244 1.00 64.27 C ATOM 6 CE LYS B 327 -7.6 13 -5.426 -37.784 1.00 64. 19 C ATOM 7 NZ LYSB327 -9.010 -5.015-37.462 1.0064.30 N ATOM 8 C LYSB327 -5.855 -7.072-41.841 1.0064.18 C ATOM 9 0 LYS B 327 -5.758 -7.825 -40.879 1.0064.23 0 ATOM 1 N LYS B 328 -6.05 1 -7.503 -43.082 1.00 64.17 N ATOM 2 CA LYS B 328 -6.073 -8.924 -43.393 1.00 64.23 C ATOM 3 CB LYS B 328 -6. 505 -9.156 -44.843 1.0064.21 C ATOM 4 CO LYS B 328 -6.492 -10.616 -45.263 1. 00 64.08 C ATOM 5 CD LYS B 328 -6.561 -10.764 -46.773 1.00 64.01 C ATOM 6 CE LYS B 328 -6.135 -12.160 -47.201 1.00 63.97 C ATOM 7 NZ LYS B 328 -6.027 -12.286 -48.679 1.00 63.96 N ATOM 8 C LYSB328 -4.697 -9.536-43.139 1.0064.29 C ATOM 9 0 LYS B 328 -4.569 -10.507 -42.366 1.00 64.33 0 ATOM 1 N LYS B 329 -3.665 -8.960 -43.772 1.0064.32 N ATOM 2 CA LYS B 329 -2.3 13 -9.511 -43.610 1.00 64.39 C ** ATOM 3 CB LYS B 329 -1.288 -8.659 -44.360 1.00 64.37 C ATOM 4 CG LYS B 329 -1.188 -10.172 -46.080 0.00 50.00 C ATOM 5 CD LYS B 329 -0.493 -9.545 -47.260 0.00 50.00 C ATOM 6 CE LYS B 329 0.417 -10.565 -47.946 0.00 50.00 C ATOM 7 NZ LYS B 329 0.748 -10.177 -49.338 0.00 50.00 N ATOM 8 C LYS B 329 -1.934 -9.631 -42.126 1.006444 C ATOM 9 0 LYSB 329 -1.435-10.671 -41.665 1.00 64.52 0 s. 50 ATOM 1 N GLNB 330 -2.189 -8.557-41.385 1.00 64.44 N ATOM 2 CA GLN B 330 -1.958 -8.520 -39.947 1.00 64.45 C : ATOM 3 CB GLNB33O -2.258 -7.118-39.410 1.006444 C ATOM 4 CO GLNB33O -2.343 -7.007-37.897 1.0064.39 C ATOM 5 CD GLN B 330 -2.72 1 -5.608 -37.443 1.0064.40 C ATOM 6 OEI GLN B 330 -2.277 -4.6 14 -38.02 1 1.0064.30 0 ATOM 7 NE2 GLN B 330 -3.546 -5.524 -36.404 1.0064.34 N ATOM 8 C GLN B 330 -2.805 -9.565 -39.225 1.00 64.45 C ATOM 9 0 GLN B 330 -2.3 13 -10.287 -38.354 1.00 64.60 0 ATOM I N LEUB33I -4.079 -9.647-39. 602 1.0064.39 N ATOM 2 CA LEU B 331 -4.995 -10.615 -39.009 1.00 64.37 C ATOM 3 CB LEUB33I -6.402-10.488-39.599 1.0064.32 C ATOM 4 CG LEU B 331 -7.355 -9.5 19 -38.897 1.00 64.30 C ATOM 5 CDI LEU B 331 -8.678 -9.421 -39.641 1.00 64.35 C ATOM 6 CD2LEUB33I -7.581 -9.930-37.453 1.0064.38 C ATOM 7 C LEUB33I -4.483-12.039-39.165 1.0064.41 C ATOM 8 0 LEU B 331 -4.671 -12. 868 -38.273 1.00 64.39 0 ATOM 1 N ILE B 332 -3.835 -12.331 -40.290 1 00 64.44 N ATOM 2 CA 1LEB332 -3.244-13.660-40.445 1.00 64.56 C ATOM 3 CD ILE B 332 -3.234 -14.168 -41.905 1.0064.53 C ATOM 4 CG1 ILE B 332 -2.752 -13.081 -42.861 1.00 64.67 C ATOM 5 CDIILEB332 -3.018-13.404-44.313 1.0064.93 C ATOM 6 CG2 ILE B 332 -4.622 -14.638 -42.310 1.0064.59 C ATOM 7 C 1LEB332 -1861-13.779-39.807 1006464 C ATOM 8 0 1LEB332 -1.416-14.885-39.502 1.0064.71 0 ATOM 1 N LEU B 333 -1.181 -12.653 -39.597 1.00 64.69 N ATOM 2 CA LEU B 333 0.026 -12.679 -38.763 1.00 64.86 C ATOM 3 CB LEUB333 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 CD1 LEU B 333 1.995 -11.795 -40.971 1.00 64.93 C ATOM 6 CD2 LEU B 333 2.750 -9.944 -39.452 1.00 64.92 C ATOM 7 C LEU B 333 -0.321 -13.018 -37.3 15 1.0064.95 C ATOM 8 0 LEU B 333 0.434 -13.699 -36.618 1. 00 64.92 0 ATOM I N LYSB334 -1.482-12.542-36.881 1.0065.06 N ATOM 2 CA LYSB 334 -1.910-12.645-35.493 1.0065.32 C ATOM 3 CB LYS B 334 -2.537 -11.303 -35.082 1.00 65.31 C ATOM 4 CG LYSB334 -3.359-11.279-33.799 1.0065.31 C ATOM 5 CD LYS B 334 -4.25 1 -10.026 -33.782 1.00 65.18 C ATOM 6 CE LYSB334 -5.325-10.098-32.705 1.0064.74 C ATOM 7 NZ LYSB 334 -6.339 -9.010-32.867 1.00 64.46 N ATOM 8 C LYS B 334 -2.885 -13.813 -35.294 1.00 65.54 C ATOM 9 0 LYS B 334 -3.741 -13.778 -34.409 1.00 65.57 0 ATOM I N LEU B 335 -2.743 -14.855 -36.111 1.00 65.83 N ATOM 2 CA LEUB335 -3.676-15.984-36.068 1.0066.16 C ATOM 3 CB LEU B 335 -3.592 -16.826 -37.346 1.00 66.09 C ATOM 4 CG LEU B 335 -4.906 -17.326 -37.966 1.00 66.13 C ATOM 5 CDI LEU B 335 -4.704 -18.673 -38.651 1.00 66.05 C ATOM 6 CD2 LEU B 335 -6.036 -17.420 -36.952 1.00 65.95 C ATOM 7 C LEUB335 -3.490-16.877-34.839 1.0066.47 C ATOM 8 0 LEUB335 -4.464-17.217-34.173 1.0066.51 0 ATOM 1 N PR0B336 -2.239-17.263-34.529 1.0066.81 N ATOM 2 CA PR0B336 -2.044-18.144-33.380 1.0067.08 C ATOM 3 CB PR0B336 -0.528-18.367-33.357 1.0067.05 C ATOM 4 CG PRO B 336 0.042 -17.221 -34.121 1.00 66.99 C ATOM 5 CD PROB 336 -0.965-16.916-35.181 1.00 66.85 C ATOM 6 C PR0B336 -2.510-17.486-32.086 1.0067.39 C ATOM 7 0 PR0B336 -2.762-18.175-31.097 1.0067.44 0 ATOM 1 N VAL B 337 -2.623 -16.162 -32.102 1.00 67.78 N ATOM 2 CA VALB 337 -3.155-15. 421 -30.966 1.00 68.20 C ATOM 3 CB VALB 337 -2.758-13.931 -31.026 1.00 68.20 C . : ATOM 4 CGI VALB 337 -2.943-13.275-29.662 1.00 68.26 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 1.00 68.46 C ATOM 7 0 VAL B 337 -5.296 -15.754 -29.919 1.00 68.80 0 ATOM I N 1LEB338 -5.269-15.408-32.150 1.0068.70 N ATOM 2 CA ILE B 338 -6.7 10 -15.578 -32.322 1.00 68.88 C ATOM 3 CB ILE B 338 -7.127 -15.468 -33.806 1.00 68.80 C ATOM 4 CGI ILE B 338 -6908 -14.045 -34.326 1.00 68.70 C ATOM 5 CDI ILE B 338 -7.913 -13.035 -33.805 1.00 68.75 C ATOM 6 CG2 ILE B 338 -8.582 -15.865 -33.983 1.00 68.67 C ATOM 7 C ILEB 338 -7.161 -16.929-31.769 1.00 69.11 C ATOM 8 0 ILE B 338 -8.075 -16.995 -30.944 1.00 69.27 0 ATOM 1 N PHE B 339 -6.507 -17.999 -32.2 19 1 0069.30 N ATOM 2 CA PHE B 339 -6.827 -19.346 -3 1.750 1.00 69.45 C ATOM 3 CB PHE B 339 -5.895 -20.390 -32.380 1.00 69.45 C ATOM 4 CG PHE B 339 -6.113 -20. 598 -33.859 1.00 69.55 C ATOM 5 CD1 PHE B 339 -7.244 -20.104 -34.492 1.00 69,69 C ATOM 6 CE1 PHE B 339 -7.444 -20.304 -35.848 1.00 69.63 C ATOM 7 CZ PHE B 339 -6.519 -21.017 -36.584 1.00 69.58 C ATOM 8 CE2 PHE B 339 -5.393 -2 1.524 -35.964 1.00 69.60 C ATOM 9 CD2 PHE 13 339 -5.195 -21.318 -34. 610 1.00 69.56 C ATOM 10 C PHE B 339 -6.748 -19 427 -30.227 1.00 69.52 C ATOM 11 0 PHEB339 -7.670-19.923-29.569 1.0069.66 0 ATOM I N ALA B 340 -5.646 -18.926 -29.675 1.00 69.56 N ATOM 2 CA ALA B 340 -5.449 -18.908 -28.230 1.00 69.59 C ATOM 3 CB ALAB34O -4.133-18.214-27.883 1.0069.61 C ATOM 4 C ALA B 340 -6.619 -18.2 18 -27.532 1.00 69.61 C ATOM 5 0 ALAB34O -7.183-18.750-26.564 1.0069.74 0 ATOM I N LYS B 341 -6.986 -17.035 -28. 035 1.00 69.49 N ATOM 2 CA LYS B 341 -8.074 -16.263 -27.437 1.00 69.65 C ATOM 3 CB LYS B 341 -8.160 -14.861 -28.055 1.00 69.67 C ATOM 4 CG LYS B 341 -6.979 -13.952 -27.694 1 00 69.92 C ATOM 5 CD LYS B 341 -7.274 -12.477 -27.981 1.00 69.78 C ATOM 6 CE LYS B 341 -6.018 -11.612 -27.838 1.00 69. 77 C ATOM 7 NZ LYS B 341 -5.389-11.703 -26.483 1.00 69.59 N ATOM 8 C LYS B 341 -9.414 -16.993 -27.531 1.00 69.57 C ATOM 9 0 LYS B 341 -10.126 -17. 142 -26.529 1.00 69.70 0 ATOM I N ILE B 342 -9.748 -17.463 -28.73 1 1.00 69. 50 N ATOM 2 CA ILE B 342 -10.994 -18.200 -28.933 1.00 69.48 C ATOM 3 CB ILE B 342 -11.209 -18.597 -30.405 1.00 69.39 C ATOM 4 CG1ILEB342 -11.207-17.354-31.296 1.0069.17 C ATOM 5 CD! ILEB 342 -11.610-17.626-32.724 1.00 68.85 C ATOM 6 CG2 ILE B 342 -12.524 -19.337 -30.563 1.00 69.32 C ATOM 7 C ILE B 342 -11.065 -19.437 -28.037 1.00 69. 61 C ATOM 8 0 1LE2342 -12.132-19.764-27.519 1.0069.60 0 ATOM 1 N GLNB 343 -9.936-20.123 -27.856 1.00 69.77 N ATOM 2 CA GLN B 343 -9.859 -21.194 -26.852 1.00 69.99 C : * ATOM 3 CB GLN B 343 -8.474 -2 1.856 -26.839 1.00 69.96 C ATOM 4 CG GLN B 343 -8.272 -22.873 -27.946 1.00 70.15 C ATOM 5 CD GLN B 343 -6.883 -23.483 -27.926 1.00 70.33 C ATOM 6 OEI GLN B 343 -6.283 -23.669 -26.839 1.00 71.09 0 *... 45 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 1.00 70.01 C ATOM 9 0 GLN B 343 -11.012 -21.177 -24.745 1.00 70.02 0 ATOM 1 N LEUB 344 -9.477-19.562-25.105 1.00 70.01 N ATOM 2 CA LEU B 344 -9.665 -18.934 -23.801 1 00 70.13 C : *. 50 ATOM 3 CB LELJ B 344 -8.882 -17.615 -23.707 1.00 70.20 C ATOM 4 CG LEUB344 -7.366-17.683-23.472 1.0070.29 C *. : ATOM 5 CD1 LEU B 344 -6.734 -16.303 -23.623 1.00 70.28 C * ATOM 6 CD2 LEU B 344 -7.043 -18.278 -22.105 1.00 70.32 C ATOM 7 C LEU B 344 -11.140-18.682-23.499 1.00 70.13 C ATOM 8 0 LEUB344 -11.654-19.142-22.478 1.0070.23 0 ATOM I N GLU B 345 -11.823 -17.959 -24.387 1.00 70.00 N ATOM 2 CA GLU B 345 -13.170 -17.481 -24.068 1.00 70.11 C ATOM 3 CB GLU B 345 -13.349 -16.036 -24.542 1.00 70.11 C ATOM 4 CG GLU B 345 -12.936 -15.805 -25.985 1.00 70.34 C ATOM 5 CD GLU B 345 -13.162 -14.378 -26.43 1 1.00 70.34 C ATOM 6 OEI GLU B 345 -14.328 -14.018 -26.701 1.00 70.78 0 ATOM 7 0E2 GLU B 345 -12.172 -13.618 -26.519 1.00 70.66 0 ATOM 8 C GLUB345 -14.330-18.345-24.570 1.0070.06 C ATOM 9 0 GLU B 345 -15.485 -17.922 -24.508 I 0070.05 0 ATOM 1 N HIS B 346 -14.037 -19.545 -25.060 1.00 70.09 N ATOM 2 CA HIS B 346 -15.097 -20.438 -25.542 1.00 70.11 C ATOM 3 CB HIS B 346 -15.176.20.43 1 -27.072 1.00 70.05 C ATOM 4 CG HIS B 346 -16.045 -19.349 -27.630 1.00 69.94 C ATOM 5 ND1 HIS B 346.17.419 -19.371 -27,525 1.00 69.85 N ATOM 6 CE! HIS B 346 -17.919 -18.296 -28.108 1.00 70.02 C ATOM 7 NE2 HIS B 346 -16.919 -17.581 -28.594 1.00 69.91 N ATOM 8 CD2 HIS B 346 -15.736.18.218 -28.309 1.00 70.00 C ATOM 9 C HIS B 346 -14.944 -21. 869 -25.042 1.00 70.14 C ATOM 10 0 HIS B 346 -15.736 -22.744 -25.397 1.00 70.16 0 ATOM 1 N HIS B 347 -13.925 -22.099 -24.222 1.00 70.14 N ATOM 2 CA HIS B 347 -13.658.23.422.23.675 1.00 70.21 C ATOM 3 CB HIS B 347.14.645 -23.753.22.554 1.00 70.15 C ATOM 4 CG HIS B 347 -14.672 -22.738 -2 1.456 1.00 70.25 C ATOM 5 NDI HIS B 347 -15.571 -21.693 -21.432 1.00 70.27 N ATOM 6 CEI HIS B 347 -15.36 1 -20.961 -20.351 1.00 70.36 C ATOM 7 NE2 HIS B 347 -14.359 -2 1.494 -19.675 1.00 70.39 N ATOM 8 CD2 HIS B 347 -13.909.22.606 -20.345 1.00 70.34 C ATOM 9 C HIS B 347.13.719.24.505 -24.745 1.00 70.23 C ATOM 10 0 HIS B 347 -14.708 -25.230 -24.85 1 1.00 70.29 0 ATOM 1 N ILE B 348 -12.665 -24.603 -25.547 1.00 70.25 N ATOM 2 CA ILE B 348 -12.5 14 -25.743 -26.442 1.00 70.37 C ATOM 3 CB ILE B 348.12. 829 -25.401 -27.922 1.00 70.40 C ATOM 4 CG1ILEB348 -12.103-24.131-28.359 1.0070.55 C ATOM 5 CD! ILE B 348 -12.926 -22.879 -28.183 1.00 70.97 C ATOM 6 CG2 ILE B 348.14.329.25.226 -28.124 1.00 70.45 C ATOM 7 C ILE B 348 -11114 -26.336 -26.3 17 1.00 70.38 C ATOM 8 0 ILE B 348 -10.144 -25.618 -26.065 1.00 70.43 0 ATOM 1 N SERB 349 -11.023 -27.653 -26.476 1.00 70.37 N ATOM 2 CA SER B 349 -9.748 -28.352 -26.404 1.00 70.38 C ATOM 3 CB SER B 349 -9.971 -29.867 -26.344 1.00 70.40 C ATOM 4 OG SER B 349.8.737 -30.566 -26.287 1.00 70.52 0 ATOM 5 C SERB349 -8.882-28.006-27.608 1.0070.34 C ATOM 6 0 SER B 349.9.380 -27.934 -28.734 1.00 70.27 0 * ATOM 1 N PRO B 350 -7.578 -27.779 -27.372 1.00 70.29 N * *..

ATOM 2 CA PRO B 350.6.623 -27.530 -28.452 1.00 70.22 C ATOM 3 CB PROB35O -5.277-27.495-27.723 1.0070.23 C ATOM 4 CO PRO B 350 -5.622 -27.067 -26.337 1.00 70.27 C ATOM 5 CD PRO B 350 -6.939 -27.722 -26.046 1.00 70.21 C **** ATOM 6 C PRO B 350.6.630 -28.634 -29.519 1.00 70.13 C ATOM 7 0 PRO B 350 -6.142 -28.421 -30.630 1.00 70.22 0 * * ATOM 1 N GLY B 351 -7.189 -29.795 -29.188 1.00 69.88 N ATOM 2 CA GLYB35I -7.273-30.899-30.137 1.0069.54 C ATOM 3 C GLY B 351 -8.320.30.680.31.2 14 1.00 69.38 C ATOM 4 0 GLY B 351 -8.540 -3 1.547 -32.065 1.00 69.41 0 . : ATOM 1 N ASP B 352.8.968 -29.516.31.183 1.00 69.15 N * ATOM 2 CA ASP B 352 -10.039 -29.207 -32.128 1.00 68.90 C ATOM 3 CB ASPB352 -11.248-28.614-31.401 1.0068.94 C ATOM 4 CG ASPB352.11.970-29.629-30.543 1.0069.10 C ATOM 5 OD1 ASP B 352 -13.22 1 -29.587 -30.497 1.00 69.17 0 ATOM 6 0D2 ASP B 352 -11.288 -30.470 -29.914 1.00 69.78 0 ATOM 7 C ASP B 352 -9.597 -28.251 -33.230 1.00 68.71 C ATOM 8 0 ASPB 352.10.243 -28.157-34.273 1.00 68.69 0 ATOM I N PHEB353 -8.500-27.541 -32.993 1.0068.50 N ATOM 2 CA PHEB353 -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 PHEB353 -8.018-24413-32.535 1.0068.40 C ATOM 5 CDI PHE B 353 -8.273 -23.213 -33.179 1.00 68.54 C ATOM 6 CEI PHE B 353 -9.034 -22.233 -32 571 1.00 68.49 C ATOM 7 CZ PHEB 353 -9.553-22.448-31.312 1.0068.51 C ATOM 8 CE2PHEB353 -9.311 -23646-30.663 10068.68 C ATOM 9 CD2 PHE B 353 -8.549 -24.620 -3 1.275 1.00 68.56 C ATOM 10 C PHE B 353 -7.261 -27.066 -35.120 1.00 68.21 C ATOM 11 0 PHEB 353 -6.497-28.021 -34.987 1.00 68.28 0 ATOM I N PRO B 354 -7.449 -26.445 -36.294 1.00 68.04 N ATOM 2 CA PROB3S4 -6.724-26.839-37.498 1.0067.82 C ATOM 3 CB PROB 354 -7.431-26.057-38.616 1.00 67.87 C ATOM 4 CG PRO B 354 -8.645 -25.426 -37.984 1.00 67.91 C ATOM 5 CD PRO B 354 -8.359 -25.3 13 -36.535 1.00 67.93 C ATOM 6 C PRO B 354 -5.273 -26.392 -37.407 1.00 67.54 C ATOM 7 0 PRO B 354 -4.906 -25.682 -36.471 1.00 67.44 0 ATOM 1 N ASPB3S5 -4.456-26.806-38.371 1.0067.25 N ATOM 2 CA ASP B 355 -3.09 1 -26.307 -38.464 1.00 66.95 C ATOM 3 CB ASP B 355 -2.306 -27.057 -39.542 1.00 66.98 C ATOM 4 CG ASP B 355 -0.873 -26. 569 -39.667 1.00 67.19 C ATOM 5 OD1 ASP B 355 0.041 -27.421 -39.696 1.00 67. 62 0 ATOM 6 OD2 ASP B 355 -0.655 -25.338 -39.735 1.00 67.10 0 ATOM 7 C ASPB355 -3.127-24.813-38.772 1.0066.67 C ATOM 8 0 ASP B 355 -3.760 -24. 383 -39.739 1.00 66.78 0 ATOM 1 N CYSB356 -2.445-24.029-37.943 1.0066.16 N ATOM 2 CA CYS B 356 -2.477 -22.576 -38.049 1.00 65.72 C ATOM 3 CB CYSB356 -1.656-21.950-36.919 1.0065.76 C ATOM 4 SG CYS B 356 -2.029 -20.2 16 -36.593 1.00 65.98 S ATOM S C CYS B 356 -1.970 -22.090 -39.405 1.00 65.43 C ATOM 6 0 CYS B 356 -2.568 -2 1.203 -40.019 1.00 64.92 0 ATOM 1 N GLN B 357 -0.878 -22.689 -39.873 1.00 65.25 N ATOM 2 CA GLN B 357 -0.2 19 -22.247 -41.103 1.00 65.06 C ATOM 3 CB GLNB357 1.238-22.723-41.137 1.0065.11 C ATOM 4 CG GLN B 357 2.164 -2 1.874 -40.268 1.00 65.39 C ATOM 5 CD GLN B 357 3.450 -22.588 -39.895 1.00 65.96 C ATOM 6 OEI GLN B 357 4. 496 -2 1.939 -39.705 1.00 66.00 0 ATOM 7 NE2GLNB357 3.377-23.933-39.783 1.0066.01 N ATOM 8 C GLN B 357 -0.966 -22.615 -42.391 1.00 64.82 C ATOM 9 0 GLN B 357 -1.003 -21.825 -43.342 1.0064.50 0 **..* ATOM 1 N LYS B 358 -1.561 -23.805 -42.425 1.00 64.56 N ATOM 2 CA LYSB358 -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 1.00 65.05 C ATOM S CD LYSB358 -2.500-26.546-45.696 1.0065.74 C p ATOM 6 CE LYS B 358 -3.140 -27.14 1 -46.947 1.00 66.04 C ATOM 7 NZ LYS B 358 -2.121 -27.613 -47.935 1.00 66. 17 N ATOM 8 C LYS B 358 -3.567 -23.215 -43.640 1.00 64.12 C ATOM 9 0 LYSB358 -3.829-22.600-44.690 1.00 63.78 0 * ATOM I N METB359 -4.252-23.074-42.509 1.0063.91 N ATOM 2 CA MET B 359 -5.3 18 -22.101 -42.352 1.00 63.82 C ATOM 3 CB METB359 -5.798-22.083-40.899 1.0063.91 C ATOM 4 CG MET B 359 -7.134 -2 1.389 -40.669 1.0064.20 C ATOM 5 SD MET B 359 -8.547 -22.269 -41.375 1.00 65.02 S ATOM 6 CE MET B 359 -9.909 -21.348 -40.663 1.00 64.30 C ATOM 7 C MET B 359 -4.822 -20.7 19 -42.766 1.00 63.69 C ATOM 8 0 MET5359 -5.586-19.907-43.281 1.0063.41 0 ATOM I N GLN B 360 -3.537 -20.459 -42. 555 1.00 63.78 N ATOM 2 CA GLN B 360 -2.954 -19.186 -42.967 1.00 63.51 C ATOM 3 CB GLNB36O -1.626-18.937-42.251 1.0063.59 C S ATOM 4 CG GLN B 360 -J 799 -18.365 -40.854 1.00 63.62 C ATOM 5 CD GLN B 360 -0531 -18.412 -40.027 1.00 63.50 C ATOM 6 OE1 GLN B 360 -0.3 15 -17.566 -39.161 1.00 63.52 0 ATOM 7 NE2GLNB360 0.313-19.403-40.288 1.0063.46 N ATOM 8 C GLNB36O -2.797.19.059-44.484 1.006340 C ATOM 9 0 GLN S 360 -3.046-17.991 -45.049 1.0063 16 0 ATOM I N GLU B 361 -2.395 -20. 144 -45.142 1.00 63,45 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 1.00 63.14 C ATOM 4 CG GLU B 361 -0.401 -22.350 -47.520 0.00 50.00 C ATOM 5 CD GLUB36I -0.196.23.530-48.448 0.0050.00 C ATOM 6 OE1 GLU B 361 -0.650 -24.642 -48.107 0.00 50.00 0 ATOM 7 0E2 GLU B 361 0.4 19 -23.346 -49.520 0.00 50.00 0 ATOM 8 C GLU B 361 -3.684 -19.978 -47.246 1.00 63.01 C ATOM 9 0 GLU B 361 -3 882 -19.152 -48.168 1.00 62 82 0 ATOM I N LEU B 362 -4.648 -20.751 -46.745 I 00 62.93 N ATOM 2 CA LEU B 362 -6. 011 -20.662 -47.266 1.00 62.55 C ATOM 3 CB LEU 13 362 -6.861 -2 1.809 -46.719 1.00 62.51 C ATOM 4 CG LEU B 362 -6.284 -23.205 -46.967 1.00 62.22 C ATOM 5 CD1 LEU B 362 -7.24 1 -24.272 -46.467 1.00 61.94 C ATOM 6 CD2 LEU B 362 -5.971 -23.409 -48.443 1.00 61.87 C ATOM 7 C LEU B 362 -6.654 -19.299 -46.962 1.00 62.44 C ATOM 8 0 LEU B 362 -7.311.18.678 -47.831 1.00 62.11 0 ATOM 1 N LEU B 363 -6.460 -18.832 -45.727 1.00 62.56 N ATOM 2 CA LEU B 363 -6.912 -17.501 -45.353 1.00 62.37 C ATOM 3 CB LEUB363.6.580-17.199-43.890 1.0062.32 C ATOM 4 CG LEUB 363 -7.712-17.346-42.870 1.00 62.11 C ATOM 5 CDI LEU B 363 -8.825 -16.381 -43.199 1.00 62.15 C ATOM 6 CD2 LEU B 363 -8.253 -18.759 -42.827 1.00 61.97 C ATOM 7 C LEU B 363 -6.259 -16.483 -46.274 1.00 62.38 C ATOM 8 0 LEU B 363 -6.862 -15.468 -46.622 1.00 62.29 0 ATOM I N METB 364 -5.021 -16.770-46.670 1.00 62.56 N ATOM 2 CA MET B 364 -4.321 -15.949 -47.654 1.00 62 46 C ATOM 3 CB METB364 -2.876-16.436-47. 836 1.0062.50 C ATOM 4 CG MET B 364 -1.949 -15.444 -48.526 1.00 62.64 C ATOM 5 SD METB364 -1.755-13.900-47.604 1.0063.45 S ATOM 6 CE METB 364 -0.474 -13.066-48.552 1.00 63.02 C ATOM 7 C METB364 -5.076.16.000-48.980 1.0062.32 C ATOM 8 0 METB 364 -5.079-15.030-49.741 1.00 62.24 0 ATOM 1 N ALA B 365.5.727 -17.132 -49.245 1.00 62.25 N ATOM 2 CA ALA B 365 -6.514 -17.277 -50.482 1.00 61.89 C ATOM 3 CS ALA B 365 -6.630 -18.749 -50.871 1.00 61.88 C *...: ATOM 4 C ALA B 365 -7.906 -16.615 -50.484 1.00 61.73 C * 1 ATOM 5 0 ALA B 365 -8.401 -16.219 -51.539 1.00 61.65 0 ATOM I N HIS B 366 -8.539 -16.491 -49.318 1.00 61.58 N : . 50 ATOM 2 CA HIS B 366 -9.928 -15.979 -49.260 1.00 61.07 C ATOM 3 CB HIS B366 -10.678-16.621 -48.097 1.00 61.07 C *:* : ATOM 4 CG H1SB366 -11.201-17983-48.405 1.006077 C ATOM 5 NDI HIS B 366 -10.381 -19.026 -48.776 1.00 60.88 N ATOM 6 CE1 HISB 366 -11.113 -20.104-48.989 1.00 61.03 C ATOM 7 NE2 HIS B 366 -12.379 -19.796 -48.769 1.00 61.08 N ATOM 8 CD2 HIS B 366 -12.461.18.475 -48.402 1.00 60.66 C ATOM 9 C HISS 366 -10.106 -14.462 -49.169 1.00 60.91 C ATOM 10 0 HIS B 366 -9.159.13.732 -48.884 1 0060.95 0 ATOM I N ASPB 367.11.337-14.001 -49.407 1.0060.67 N ATOM 2 CA ASPB 367 -11.709-12.600-49.181 1.0060.54 C ATOM 3 CR ASP B 367 -12.589 -12.052 -50.307 1.00 60.59 C ATOM 4 CO ASP B 367 -13.051 -10.615.50.044 1.006069 C ATOM 5 ODI ASP B 367 -13.641 -9.993 -50.956 1.00 60.49 0 ATOM 6 0D2 ASP B 367 -12.824 -10.103 -48.925 1.00 60.90 0 ATOM 7 C ASP B 367 -12.447.12. 442 -47.863 1.00 60.51 C ATOM 8 0 ASP B 367 -13.446-13.117-47.610 1.00 60.68 0 ATOM 1 N PHEB368 -11.968-11.519-47.038 1.0060.30 N ATOM 2 CA PHE B 368 -12.480-11.376-45.689 1.00 60.01 C ATOM 3 CB PHEB 368 -11.456-10.666-44.807 1.00 60.10 C ATOM 4 Co PHEB 368 -10.346-11.562 -44.336 1.00 60.32 C ATOM 5 CDL PHEB 368 -9.815-12.532-45.176 1.0060.54 C ATOM 6 CEI PHE B 368 -8.795 -13.358 -44.750 1.00 60.45 C ATOM 7 CZ PHEB 368 -8.284-13.217-43.475 1.00 60.53 C ATOM 8 CE2 PHE B 368 -8.799 -12.251.42.627 1.00 60.66 C ATOM 9 CD2 PHE B 368 -9.823 -11.430-43.060 1.00 60.62 C ATOM 10 C PHE B 368 -13.824 -10.673 -45.645 1.00 59.80 C ATOM 11 0 PHE B 368 -14.704 -11.067 -44.885 1.00 59.86 0 ATOM 1 N THR B 369 -13.986 -9.641 -46.466 1.00 59.53 N ATOM 2 CA THRB 369 -15.217 -8.854-46.451 1.0059.25 C ATOM 3 CR THRB 369 -15.113 -7.593 -47.340 1.00 59.18 C ATOM 4 OG1 THR B 369 -14.994 -7.974.48.716 1.00 59.25 0 ATOM 5 CG2 THRB 369 -13.907 -6.761 -46.940 1.00 59.10 C ATOM 6 C THRB 369 -16.427 -9.691 -46.858 1.00 59.10 C ATOM 7 0 THR B 369 -17.568 -9.311 -46.603 1. 00 58.97 0 ATOM I N LYS B 370 -16.170 -10.840 -47.476 1.00 59.01 N ATOM 2 CA LYS B 370 -17.240-11.725 -47.923 1.00 58.97 C ATOM 3 CB LYS B 370 -16.818 -12.482 -49.184 1.00 59.01 C ATOM 4 CO LYS B 370 -16.359.11.596 -50.333 1.00 59.07 C ATOM 5 CD LYS B 370 -17.508 -11.175.51.234 1.00 59.12 C ATOM 6 CE LYSB 370 -16.990-10.481 -52.491 1.00 59.61 C ATOM 7 NZ LYS B 370 -15.988 -11.309 -53.245 1.00 59.98 N ATOM 8 C LYSB37O -17.652-12.715-46.836 1.0058.95 C ATOM 9 0 LYSB37O -18.735-13.292-46.901 1.0058.95 0 ATOM 1 N PHEB371 -16.785-12.914-45.844 1.0058.98 N ATOM 2 CA PHEB 371 -17.095 -13.790 -44.713 1.00 59.03 C ATOM 3 CB PHEB37I -15.974-13.759-43.669 1.0058.86 C ATOM 4 CG PHEB371 -14.716-14.459-44.098 1.0058.79 C ATOM 5 CDI PHEB 371 -13.479-14.003-43.673 1.00 58.52 C *** ATOM 6 CEIPHEB37L -12.318-14.644-44.060 1.0058.30 C ATOM 7 CZ PHEB 371 -12.383-15.752-44.883 1.00 58.32 C ATOM 8 CE2PHEB371 -13.606-16.218-45. 314 1.0058.37 C ATOM 9 CD2PHEB37I -14.766-15.574-44.922 1.0058.75 C ATOM 10 C PHEB37I.18,402-13.386.44.043 1.00 59.21 C ATOM 11 0 PHEB37I -18791 -12.223-44.079 1.00 59.25 0 ATOM 1 N H1SB372 -19.079-14.346-43.427 1.0059.50 N * ATOM 2 CA HIS B 372 -20.289 -14.040 -42.677 1.00 59.80 C ATOM 3 CB HIS B 372 -21.298 -15.180 -42.790 1.00 59.85 C : .. 50 ATOM 4 CO HIS B 372 -21.963 -15.261 -44.127 1.00 59.95 C ATOM 5 NDI HIS B 372 -22.899 -14.342 -44.548 1.00 59.92 N * ATOM 6 CEI HIS B 372 -23.3 14 -14.663 -45.760 1.00 60.28 C ATOM 7 NE2 HIS B 372 -22.678 -15.756 -46.142 1.00 60.47 N ATOM 8 CD2HISB372 -21.827-16.150-45.139 1.0060.21 C ATOM 9 C H1SB372 -19.968-13.754-41.215 1.0059.98 C ATOM 10 0 HIS B 372 -18.885 -14.092 -40.734 1.00 60.08 0 ATOM 1 N SERB 373 -20.913-13.130-40.513 1.00 60.16 N ATOM 2 CA SERB 373 -20.731 -12.788 -39 100 1.00 60.24 C ATOM 3 CB SER B 373 -21.512 -11.521 -38.748 1.00 60.28 C ATOM 4 OG SER B 373 -21. 188 -10.461.39.63 1 1.00 60.74 0 ATOM 5 C SERB 373 -21.164-13.918-38.178 1.0060.17 C ATOM 6 0 SERB 373 -21.854-14.847-38.592 1.0060.00 0 ATOM 1 N LEU B 374 -20.759 -13 828 -36.919 1.00 60.35 N ATOM 2 CA LEUB374 -21.161-14.813-35.928 1.006062 C ATOM 3 CB LEU B 374 -20.625 -14.424 -34.550 1.00 60.56 C ATOM 4 CO LEUB 374 -20.572-15.531 -33.499 1.00 60.72 C ATOM 5 CDI 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 1.00 60.76 C ATOM 8 0 LEU B 374 -23.394 -13.933 -35.966 1.00 60. 93 0 ATOM 1 N LYSB375 -23.182-16.167-35.853 1.0060.82 N ATOM 2 CA LYSB375 -24.620-16.420-35.868 1.0060.84 C ATOM 3 CB LYS B 375 -25.035 -17.002 -37.219 1.00 60.91 C ATOM 4 CG LYS B 375 -24.869 -16.044 -38.385 1.00 61 48 C ATOM 5 CD LYS B 375 -26.197 -15.434 -38.799 1.00 62.71 C ATOM 6 CE LYS B 375 -27.053 -16.457 -39.546 1.0063.51 C ATOM 7 NZ LYSB 375 -28.354-15.899-40.015 1.00 63.82 N ATOM 8 C LYS B 375 -24.991 -17.381 -34.745 1.00 60.68 C ATOM 9 0 LYS B 375 -24.979 -18.595 -34.937 1.00 60. 73 0 ATOM 1 N PRO B 376 -25.338 -16.837 -33.570 1.00 60.57 N ATOM 2 CA PRO B 376 -25.5 18 -17.632 -32.357 1.00 60.57 C ATOM 3 CB PRO B 376 -26.02 1 -16.607 -3 1.338 1.00 60.60 C ATOM 4 CO PRO B 376 -25.546.15.295 -3 1.849 1.00 60.61 C ATOM 5 CD PRO B 376 -25.597 -15.407 -33.339 1.00 60.55 C ATOM 6 C PROB376 -26.542-18.746-32.530 1.0060.59 C ATOM 7 0 PRO B 376 -26.407 -19.809 -3 1.927 1.00 60.69 0 ATOM I N LYS B 377 -27.550 -18.495 -33 358 1.00 60.59 N ATOM 2 CA LYS B 377 -28.631 -19.446 -33.598 1.00 60.71 C ATOM 3 CB LYS B 377 -29,629 -18.839 -34.588 1.00 60.74 C ATOM 4 CO LYSB 377 -29.017-17.771 -35.499 1.00 61.05 C ATOM 5 CD LYS B 377 -29.957 -17.378 -36.637 1.00 61.19 C ATOM 6 CE LYS B 377 -30.073 -18.489 -37.682 1.00 61.82 C ATOM 7 NZ LYS B 377 -3 1.028 -18.146 -38.781 1.00 62.06 N ATOM 8 C LYS B 377 -28.154 -20.821 -34.085 1.00 60.59 C ATOM 9 0 LYS B 377 -28.432 -2 1.849 -33.454 1.00 60.69 0 ATOM 1 N LEU B 378 -27.435 -20.834 -35.205 1.00 60.51 N ATOM 2 CA LEUB378 -26.950-22.076-35.806 1.0060.41 C ATOM 3 CB LEU B 378 -26.243 -21.783 -37.126 1.00 60.35 C : .. ATOM 4 CO LEU B 378 -27.021 -20.939 -38.140 1.00 60.12 C ATOM 5 CD! LEUB378 -26.117-20.552-39.295 1.0059.86 C * .** ATOM 6 CD2 LEU B 378 -28.267 -21.663 -38.641 1.00 59.70 C ATOM 7 C LEU B 378 -26.007 -22.807 -34.861 1.00 60.42 C *.. 45 ATOM 8 0 LEU B 378 -26.128 -24.019-34.645 1.0060.64 0 ATOM I N LEU B 379 -25.064 -22.056 -34.305 1.00 60.36 N ATOM 2 CA LEUB379 -24.186-22.568-33.266 1.0060.34 C * ATOM 3 CB LEUB 379 -23.368 -21.425 -32.669 1.00 60.18 C ATOM 4 CG LEUB379 -22.157-21.020-33.511 1.0059.81 C :

50 ATOM 5 CD! LEU B 379 -22.024 -19.515 -33.633 1.00 59.39 C ATOM 6 CD2 LEU B 379 -20.894 -2 1.632 -32.93 1 1.00 59.83 C * * : ATOM 7 C LEU B 379 -24.993 -23.284 -32.188 1.00 60.50 C ATOM 8 0 LEU B 379 -24.778 -24.470 - 3 1.922 1.00 60.81 0 ATOM 1 N GLU B 380 -25.932 -22.567 -31.579 1.00 60.65 N ATOM 2 CA GLU B 380 -26.808 -23.167 -30.580 1.00 60.83 C ATOM 3 CB GLUB38O -27.938-22.214-30.192 1.0060.85 C ATOM 4 CG GLU B 380 -27.618 -21.304 -29.025 1.00 60.88 C ATOM 5 CD GLUB3SO -28.855-20.937-28.235 1.00 61.03 C ATOM 6 OEI GLUB38O -28.781 -20.931 -26.991 1.0061.38 0 ATOM 7 0E2 GLU B 380 -29.907 -20.673 -28.854 1.00 61.20 0 ATOM 8 C GLU B 380 -27.396 -24.470 -3 1.097 1.0060.92 C ATOM 9 0 GLUB38O -27.372-25.499-30.402 1.0061.26 0 ATOM 1 N ALAB381 -27.924-24.420-32.319 1.0060.89 N ATOM 2 CA ALA B 381 -28.484 -25.606 -32 952 1.00 61.02 C ATOM 3 CB ALAB38I -28.820-25.322-34.403 1.0060.97 C ATOM 4 C ALAB 381 -27.491-26.754-32.847 1.00 61.14 C ATOM 5 0 ALAB381 -27.844-27.872-32.458 1.0061.43 0 ATOM 1 N LEUB 382 -26.241 -26.460-33.182 1.00 61.13 N ATOM 2 CA LEUB382 -25.166-27.438-33.083 1.0061.34 C ATOM 3 CB LEU B 382 -23.865 -26.808 -33.592 1.00 61.35 C ATOM 4 CG LEU B 382 -22.699 -27.67 1 -34.081 1.00 61.48 C ATOM 5 CD1 LEU B 382 -2 1.636 -27.835 -32.998 1.00 61.27 C ATOM 6 CD2LEUB382 -23.194-29.019-34.602 10062.11 C ATOM 7 C LEU B 382 -25.006 -27.964 -3 1.647 1.00 61.46 C ATOM 8 0 LEUB382 -25.236-29.157-31.374 1.0061.78 0 ATOM 1 N ASP B 383 -24.627 -27.070 -30.733 1.00 61.44 N ATOM 2 CA ASP B 383 -24.367 -27.453 -29.340 1.00 61.75 C ATOM 3 CB ASP B 383 -24.243 -26.209 -28.452 1.00 61.77 C ATOM 4 CG ASP B 383 -23.278 -25.172 -29.015 1.00 61.90 C ATOM 5 ODI ASP B 383 -22.998 -25.208 -30.229 1.00 62.19 0 ATOM 6 OD2 ASP B 383 -22.802 -24.311 -28.243 1.00 62.06 0 ATOM 7 C ASP B 383 -25.474 -28.358 -28.809 1.00 61.90 C ATOM 8 0 ASPB 383 -25.222-29.471 -28.294 1.00 62.21 0 ATOM I N ASP B 384 -26.704 -27.870 -28.949 1.00 61.93 N ATOM 2 CA ASP B 384 -27.877 -28.633 -28.554 1.00 62.20 C ATOM 3 CB ASP B 384 -29.159 -27.857 -28.871 1.00 62.22 C ATOM 4 CO ASP B 384 -30.405 -28.552 -28.356 1.00 62.42 C ATOM 5 OD1 ASP B 384 -30.668 -28.477 -27.136 1.00 62.53 0 ATOM 6 OD2ASPB384 -31.125-29.168-29.172 1.0062.70 0 ATOM 7 C ASP B 384 -27.887 -29.985 -29.262 1.00 62.27 C ATOM 8 0 ASP B 384 -28.130 -3 1 .022 -28.622 1.00 62.50 0 ATOM I N MET B 385 -27.609 -29.969 -30.573 1.00 62.20 N ATOM 2 CA MET B 385 -27.594 -31.206 -31.352 1.00 62.37 C ATOM 3 CB MET B 385 -27. 031 -31.035 -32.769 1.00 62.38 C ATOM 4 CO MET B 385 -26.951 -32.383 -33.532 1.00 62.39 C ATOM 5 SD MET B 385 -25.635 -32.605 -34.766 1.00 62.11 S ATOM 6 CE MET B 385 -24.227 -33.02 1 -33.730 1.00 61.97 C ATOM 7 C MET B 385 -26.744 -32.216 -30.639 1.00 62.48 C * ATOM 8 0 MET B 385 -27.260 -33.215 -30 115 1.00 62.86 0 ATOM 1 N LEU B 386 -25.437 -3 1.958 -30.611 1.00 62.43 N ATOM 2 CA LEUB386 -24.558-32.982-30.070 1.0062.76 C ATOM 3 CB LEU B 386 -23.056 -32.642 -30.160 1.00 62.76 C ATOM 4 CO LEU B 386 -22.440-31.254 -29.955 1.00 62.69 C ATOM 5 CD! LEU B 386 -20.974 -31.394 -29.566 1.00 62.40 C ATOM 6 CD2 LEU B 386 -22.572 -30.425 -31.218 1.00 62.82 C ATOM 7 C LEU B 386 -25.015 -33.334 -28.666 1.00 62.86 C ATOM 8 0 LEIJ B 386 -25.436 -34.480 -28.422 1.00 63.18 0 ATOM I N ALA8387 -25.006-32.335-27.779 1.0062.84 N ATOM 2 CA ALA B 387 -25.437 -32.545 -26.396 1.00 63.11 C ATOM 3 CB ALA B 387 -25.713 -31.207 -25.715 1.00 62.92 C ATOM 4 C ALA B 387 -26.663 -33.465 -26.298 1.00 63.24 C ATOM 5 0 ALA B 387 -26.542 -34.694 -26.107 1.00 63.61 0 ATOM I N GLNB388 -27.843-32.877-26.467 1.0063.14 N ATOM 2 CA GLN B 388 -29.082 -33.594 -26.185 1.00 63.43 C ATOM 3 CB GLN B 388 -30.244 -32.603.26.059 1.00 63. 49 C ATOM 4 CG GLNB38S -29.854-31.297-25.371 1.0063.57 C ATOM 5 CD GLN B 388 -30.908 -30.790 -24.402 1.00 63.61 C ATOM 6 OEI GLN B 388 -31.675 -31.570 -23.830 1.00 63.36 0 ATOM 7 NE2 GLN B 388 -30.941 -29.477 -24.202 1.00 63.79 N ATOM 8 C GLN B 388 -29.406 -34.688 -27.207 1.00 63.52 C ATOM 9 0 GLNB388 -29.698-35.850-26.842 1.0063.82 0 ATOM I N ASP B 389 -29.344 -34.323 -28.486 1.00 63.47 N ATOM 2 CA ASP B 389 -29.769 -35.242 -29.529 1.00 63.75 C ATOM 3 CB ASP B 389 -29.774 -34.549 -30.89 1 1.00 63.76 C ATOM 4 CG ASP B 389 -30.851 -33.484 -30.995 1.00 64.01 C ATOM 5 ODI ASP B 389 -32.035 -33.801 -30.746 1.00 64.41 0 ATOM 6 0D2 ASP B 389 -30.517 -32.328 -31.329 1.00 64.29 0 ATOM 7 C ASPB 389 -28.895-36 491 -29.545 1. 00 63.83 C ATOM 8 0 ASP B 389 -29.409 -37.633 -29.769 1.00 64.19 0 ATOM I N ILEB39O -27.582-36.290-29.283 1.0063.79 N ATOM 2 CA ILEB39O -26.702-37.449-29.319 1.0064.00 C ATOM 3 CB ILE B 390 -25.257 -37.051 -29.645 1.00 63.95 C ATOM 4 CG1 ILE B 390 -25.170 -36.707 -31.135 1.00 63.71 C ATOM 5 CDI ILEB 390 -23.857-36.139-31.565 1.00 63.77 C ATOM 6 CG2 ILE B 390 -24.289 -38.171 -29.283 1.00 63.97 C ATOM 7 C ILE B 390 -26.849 -38.215 -28.008 1.0064.14 C ATOM 8 0 ILE B 390 -26.847 -39.465 -27.987 1.00 64.58 0 ATOM 1 N ALA B 391 -27.030 -37.458 -26.925 1.00 64.14 N ATOM 2 CA ALA B 391 -27.407 -38.063 -25.658 1.00 64.26 C ATOM 3 CE ALA B 391 -27.864 -37.001 -24.673 1.00 6425 C ATOM 4 C ALAB39I -28.498-39120-25.865 1.0064.38 C ATOM 5 0 ALA B 391 -28328 -40.265 -25.456 1.00 64.34 0 ATOM I N LYS B 392 -29.600 -38.750 -26.522 1.00 64.51 N ATOM 2 CA LYS B 392 -30.752 -39.68 1 -26.672 1.00 65.03 C ATOM 3 CB LYS B 392 -32.041 -38.900 -27.039 1.00 65.00 C ATOM 4 CG LYS B 392 -33.202 -39.822 -27.422 1.00 65.42 C ATOM 5 CD LYSB392 -34.304-39.084-28.196 1.0065.51 C ATOM 6 CE LYS B 392 -33.876 -38.797 -29.657 1.00 66.25 C ATOM 7 NZ LYS B 392 -34.960 -38.108 -30.448 1.00 66.63 N ATOM 8 C LYS B 392 -30.564 -40.824 -27.719 1.00 65.09 C ATOM 9 0 LYS B 392 -30.922 -42.067 -27.733 1.00 65.53 0 ATOM 1 N LEU B 393 -29.500 -40.372 -28.661 1.00 65.09 N ATOM 2 CA LEU B 393 -29.270 -41.413 -29.680 1.00 65.41 C ATOM 3 CB LEU B 393 -28.567 -40.850 -30.917 1.00 65.35 C ATOM 4 CG LEU B 393 -29.572 -40.402 -3 1.975 1.00 65.48 C ATOM 5 CDI LEUB 393 -28.854-39.831 -33.175 1.00 65.63 C ATOM 6 CD2 LEU B 393 -30.454 -41.576 -32.381 1.00 65.50 C ATOM 7 C LEU B 393 -28.469 -42.559 -29.072 1.00 65.64 C ATOM 8 0 LEU B 393 -28.537 -43.692 -29.565 1.00 65.90 0 ATOM I N MET B 394 -27.727 -42.276 -27.994 1.00 65.68 N ATOM 2 CA METE 394 -26.953 -43.350-27.351 1.00 66.07 C ATOM 3 CB MET B 394 -26.160 -42.822 -26.147 1.00 66.11 C ATOM 4 CG METB 394 -25.045 -41.845 -26.512 1.00 66.43 C ATOM 5 SD METB394 -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 : 50 ATOM 7 C METB 394 -27.834 -44.552 -26.951 1.00 66.21 C ** * ATOM 8 0 METB 394 -27.625 -45.678 -27.434 1.00 66.49 0 ATOM I N PR0B395 -28.824-44.319-26.063 1.0066.35 N ATOM 2 CA PRO B 395 -29.721 -45.400 -25.637 1.00 66.36 C ATOM 3 CB PRO B 395 -30.859 -44.656 -24.933 1.00 66.30 C ATOM 4 CG PRO B 395 -30.208 -43.450 -24.378 1.00 66.32 C ATOM 5 CD PRO B 395 -29.137 -43.024 -25.387 1.00 66.42 C ATOM 6 C PRO B 395 -30.288 -46.183 -26.818 1.00 66. 38 C ATOM 7 0 PR0B395 -30347-47.571-26.772 1.00 66.53 0 ATOM I N LEU B 396 -30.497 -45.303 -28.030 1.00 66.35 N ATOM 2 CA LEU B 396 -3 1.246 -46.083 -29.062 1.00 66.51 C ATOM 3 CB LEUB396 -31.852-45.178-30.154 1.0066.52 C ATOM 4 CO LEUB396 -32.912-45.758-31.111 1.0066.50 C ATOM 5 CDI LEU B 396 -33.315 -44.715 -32.155 1.00 66.78 C ATOM 6 CD2 LEU B 396 -32.466 -47.051 -31.807 1.00 66.41 C ATOM 7 C LEU B 396 -30.201 -47.020 -29.694 1.00 66. 56 C ATOM 8 0 LEU B 396 -30.470 -48.217 -30.094 1.00 66.72 0 ATOM I N LEU B 397 -28.990 -46.430 -29.758 1.00 66.57 N ATOM 2 CA LEUB397 -27.835-47.098-30.313 1.0066.81 C ATOM 3 CB LEU B 397 -26.607 -46.199 -30.188 1.00 66.77 C ATOM 4 CG LEU B 397 -25.289 -46.797 -30.666 1.00 66.74 C ATOM 5 CD1 LEUB397 -25.328-47.016-32.172 1.00 66.79 C ATOM 6 CD2 LEU B 397 -24.143 -45.884 -30.274 1.00 66.83 C ATOM 7 C LEUB397 -27.582-48.420-29.616 1.0066.95 C ATOM 8 0 LEU B 397 -27.383 -49.426 -30.278 1.00 67.22 0 ATOM I N ARG B 398 -27.592 -48.416 -28.284 1.00 67. 02 N ATOM 2 CA ARG B 398 -27.336 -49.643 -27.5 14 1.00 67.30 C ATOM 3 CB ARG B 398 -27.350 -49.332 -26.0 15 1.00 67.36 C ATOM 4 CO ARG B 398 -26.308 -48.309 -25.582 1.00 67.98 C ATOM 5 CD ARG B 398 -26.819 -47.456 -24.424 1.00 68.97 C ATOM 6 NE ARO B 398 -27.294 -48.259 -23.300 1.00 69.67 N ATOM 7 CZ AROB 398 -26.505-48.760-22.351 1.00 70.33 C ATOM 8 NH1 ARO B 398 -27.028 -49.478 -2 1.363 1.00 70.67 N ATOM 9 NH2 ARO B 398 -25.193 -48. 547 -22.389 1.00 70.46 N ATOM 10 C ARG B 398 -28.366 -50.744 -27.814 1.00 67.28 C ATOM 11 0 ARGB398 -28.004-52.040-27.953 1.0067.55 0 ATOM I N GLN B 399 -29.649 -50.229 -28.027 1.00 67.15 N ATOM 2 CA GLN B 399 -30.706 -51.190 -28.344 1.00 67.22 C ATOM 3 CB GLN B 399 -32.089 -50.529 -28.308 1.00 67.21 C ATOM 4 CO GLNB399 -33.256-51.484-28.565 1.0067.20 C ATOM 5 CD GLN B 399 -33.255 -52.683 -27.622 1.00 67.24 C ATOM 6 OEI GLNB 399 -33.322-53.832-28.070 1.0067.09 0 ATOM 7 NE2GLNB 399 -33.174-52.421 -26.312 1.00 67.33 N ATOM 8 C GLNB 399 -30.427-51.801 -29.713 1.00 67.26 C ATOM 9 0 GLN B 399 -30.729 -52.973 -29.958 1.00 67.20 0 ATOM 1 N GLU B 400 -29.833 -51.006 -30.601 1.00 67.33 N ATOM 2 CA GLU B 400 -29.448 -5 1.520 -3 1.913 1.00 67.67 C ATOM 3 CR GLU B 400 -29.270 -50.383 -32.9 17 1.00 67.73 C ATOM 4 CO GLUB400 -30.581 -49.853-33.487 1.00 68.29 C ATOM 5 CD OLUB400 -30.356-49.020-34.738 1.0068.96 C ATOM 6 OEI GLUB400 -31.298-48.311 -35.159 1.0069.08 0 ATOM 7 0E2 GLU B 400 -29.235 -49.077 -35.297 1.00 69.03 0 ATOM 8 C GLU B 400 -28.181 -52.374 -31.867 1.00 67. 75 C ATOM 9 0 GLU B 400 -28.005 -53.276 -32.686 1.00 67.75 0 ATOM 1 N GLUB 401 -27.302 -52.089 -30.909 1.00 67.83 N ATOM 2 CA GLU B 401 -26.035 -52.807 -30.795 1.00 68.15 C ATOM 3 CB GLUB4O1 -25.015-52.036-29.938 1.0068.25 C ATOM 4 CO GLU B 401 -23.580 -52.606 -30.002 1.00 68 55 C : **. 50 ATOM 5 CD GLUB4O1 -22.501 -51.549-29.779 1.00 68.79 C ATOM 6 OE1 GLUB4O1 -22.629-50.435-30.334 1.00 68.79 0 . : ATOM 7 0E2 GLU B 401 -21.517 -51.839 -29.059 1.00 68.49 0 * ATOM 8 C GLU B 401 -26.275 -54.218 -30.257 1.00 68.19 C ATOM 9 0 GLUB4OI -25.363-55.103-30.342 1.0068.20 0 ATOM I N LEU B 402 -27.514 -54.443 -29.722 1.00 68.10 N ATOM 2 CA LEUB4O2 -27.860-55.876-29.534 1.0068.26 C ATOM 3 CB LEU B 402 -28.15 1 -56.248.28.065 1.00 68.22 C ATOM 4 CO LEUB4O2 -28.980-55.386-27.109 1.0068.29 C ATOM 5 CDI LEUB4O2 -30.451 -55.301 -27.514 1.0068.15 C ATOM 6 CD2 LEU B 402 -28.840 -55.954 -25.698 1.00 68.27 C ATOM 7 C LEU B 402 -28.980 -56.322 -30.497 1.00 68.35 C ATOM 8 0 LEUB4O2 -30.147-56.557-30.094 1.0068.28 0 ATOM I N GLUB4O3 -28.607-56.428-31.781 1.0068.52 N ATOM 2 CA GLU B 403 -29.588 -56.755 -32.818 1.00 68.65 C ATOM 3 CB GLU B 403 -29.93 1 -55.52 1 -33.659 1.00 68.70 C ATOM 4 CO GLUB4O3 -30.991 -54.639-33.021 1.00 68.74 C ATOM 5 CD GLUB4O3 -32.215-55.426-32.590 1.00 68.53 C ATOM 6 OE1 GLU B403 -32.201 -56.670-32.722 1.00 68.11 0 ATOM 7 0E2 GLU B 403 -33.191 -54.802 -32.122 1.00 68.50 0 ATOM 8 C GLU B 403 -29.2 14 -57.924 -33.722 1.00 68.69 C ATOM 9 0 GLU B 403 -29.749 -59.023 -33.563 1.00 68.78 0 ATOM I N SERB4O4 -28.317-57.699-34.679 1.0068.70 N ATOM 2 CA SERB4O4 -27.974-58.768-35.617 1.0068.71 C ATOM 3 CB SER B 404 -28.740 -58.599 -36.939 1.00 68.72 C ATOM 4 OG SERB 404 -28.941 -59.853-37.578 1.00 68.64 0 ATOM 5 C SER B 404 -26.470 -58.933 -35.873 1.00 68.68 C ATOM 6 0 SER B 404 -25.844 -58.123 -36.565 1.00 68.72 0 ATOM I N VAL B 405 -25.905 -59.999 -35.307 1.00 68. 52 N ATOM 2 CA VAL B 405 -24.5 14 -60.373 -35.553 1.00 68.31 C ATOM 3 CB VAL B 405 -24.015 -61.401 -34.501 1.00 68.37 C ATOM 4 CG1 VAL B 405 -22.5 17 -61.661 -34.657 1.00 68.42 C ATOM 5 CG2 VAL B 405 -24.8 16 -62.702 -34. 582 1.00 68.30 C ATOM 6 C VAL B 405 -24.359 -60.941 -36.969 1.00 68.09 C ATOM 7 0 VAL B 405 -23.242 -61.172 -37.443 1.00 68.12 0 ATOM I N GLU B 406 -25.494 -61.154 -37.634 1.00 67.77 N ATOM 2 CA GLU B 406 -25.541 -61.660 -39.008 1.00 67.37 C ATOM 3 CB GLU B 406 -26.992 -6 1.732 -39.495 1.00 67.50 C ATOM 4 CO GLU B 406 -27.147 -62.138 -40.957 1.00 67.80 C ATOM 5 CD GLU B 406 -28.069 -61.202 -41.723 1.00 68.31 C ATOM 6 OEI GLU B 406 -29.061 -61.685 -42.313 1.00 68.29 0 ATOM 7 0E2 GLU B 406 -27.801 -59.978 -41.732 1.00 68.51 0 ATOM 8 C GLU B 406 -24.734 -60.777 -39.957 1.00 66. 93 C ATOM 9 0 GLUB4O6 -24.162-61.265-40.937 1.0066.98 0 ATOM I N ALA B 407 -24.697 -59.479 -39.659 1.00 66.23 N ATOM 2 CA ALA B 407 -23.943 -58.5 16 -40.459 1.00 65.47 C ATOM 3 CB ALA B 407 -24.221 -57.094 -39.976 1.00 65.49 C ATOM 4 C ALAS 407 -22.440 -58.8 13 -40.442 1.00 64.85 C ATOM 5 0 ALA B 407 -2 1.702 -58.369 -41.328 1.0064.84 0 ATOM I N GLYB4O8 -22.004-59.576-39.439 1.0064.00 N ATOM 2 CA GLY B 408 -20.598 -59.936 -39.266 1.00 62.91 C ATOM 3 C GLYB4O8 -19.933-60.428-40.535 1.0062.16 C ATOM 4 0 GLYB4O8 -20.582 -61,020-41.397 1.00 62.11 0 ATOM I N VAL B 409 -18.633 -60.180 -40.649 1.00 61.40 N ATOM 2 CA VAL B 409 -17.880 -60.595 -41.824 1.00 60.66 C ATOM 3 CB VAL B 409 -16.452 -60.013 -41.824 1.00 60.68 C * ATOM 4 CGI VALB 409 -15.845-60.103-43.213 1.00 60.53 C ATOM 5 CG2 VAL B 409 -16.473 -58.573 -41.362 1.00 60.66 C : *. 50 ATOM 6 C VAL B 409 -17.829 -62.117-41.919 1.00 60.21 C ATOM 7 0 VAL B 409 -17.427 -62. 803 -40.974 1.00 60.00 0 *. ATOM 1 N ALAB41O -18.250-62.638-43.066 1.0059.67 N * ATOM 2 CA ALA B 410 -18.324 -64.077 -43.271 1.00 59.13 C ATOM 3 CB ALA B 410 -19.519 -64.425 -44.142 1.00 59.26 C ATOM 4 C ALA B410 -17.043-64.616-43.885 1.0058.71 C ATOM 5 0 ALA B 410 -16.274 -63.875 -44.491 1.00 58.61 0 ATOM I N GLYB4II -16.838-65.919-43.723 1.0058.33 N ATOM 2 CA GLYB411 -15.635-66.617-44.174 1.00 57.74 C ATOM 3 C GLYB4I1 -14.718-65.930-45.170 1.0057.25 C ATOM 4 0 GLY B 411 -15.164-65.273-46. 113 1.00 57.29 0 ATOM I N GLY B 412 -13.420 -66.103 -44.946 1.00 56.81 N ATOM 2 CA GLYB4I2 -12.385-65.639-45.860 1.0056.24 C ATOM 3 C GLYB4I2 -11.093 -66.100-45.229 1.00 55.88 C ATOM 4 0 GLYB412 -10.523-67.115-45.616 1.00 55.87 0 ATOM 1 N ALA B 413 -10 649 -65.349 -44.232 1.00 55.53 N ATOM 2 CA ALAB 413 -9.619-65.806-43.319 1.0055.19 C ATOM 3 CB ALA B 413 -8.452 -64.844 -43.313 1.00 55.14 C ATOM 4 C ALA B 413 -10.263 -65.865 -41.946 1.00 54.97 C ATOM 5 0 ALA B 413 -9.607 -66.140 -40.945 1.00 55.00 0 ATOM I N PHEB414 -11.566-65.613-41.915 1.0054.73 N ATOM 2 CA PHEB 414 -12.291 -65.468-40.663 1.00 54.57 C ATOM 3 CB PHEB414 -13.369-64.387-40.793 1.0054.59 C ATOM 4 CG PHEB4I4 -12.826-63.027-41.139 1.0054.41 C ATOM 5 CDI PHEB4I4 -12.351 -62.184-40.148 1.00 54.25 C ATOM 6 CE1 PHE B 414 -11.851 -60.941 -40.462 1.00 54.27 C ATOM 7 CZ PHEB 414 -11.822-60.521 -41.778 1.0054.38 C ATOM 8 CE2PHEB414 -12.292-61.350-42.774 1.0054.20 C ATOM 9 CD2 PHE B 414 -12.791 -62.594 -42.454 1.00 54.24 C ATOM 10 C PHEB414 -12.921-66.771-40.194 1.0054.51 C ATOM Ii 0 PHEB4I4 -13.036-67.005-38.991 1.0054.59 0 ATOM I N GLUB415 -13.327-67.612-41.143 1.0054.32 N ATOM 2 CA GLUB415 -13.998-68.872-40.827 1.0054.13 C ATOM 3 CB GLU B 415 -14 168 -69.7 13 -42.087 1.00 54.25 C ATOM 4 CG GLUB415 -12.858-70.145-42.699 1. 00 55.37 C ATOM 5 CD GLU B 415 -12.959 -70.379 -44.192 1.00 57.16 C ATOM 6 OE1GLUB4I5 -11.987-70.912-44.778 1.0057.92 0 ATOM 7 OE2 GLU B 415 -14.007 -70.025 -44.779 1.00 57.82 0 ATOM 8 C GLU B 415 -13.258 -69.664 -39.750 1.00 53.71 C ATOM 9 0 GLU B 415 -12.027 -69.672 -39.704 1.00 53.58 0 ATOM I N GLYB416 -14.023-70.325-38.886 1.0053.38 N ATOM 2 CA GLY B 416 -13.466 -70.999 -37.718 1.00 52.98 C ATOM 3 C GLY B 416 -12.802 -72.320 -38.039 1.00 52.72 C ATOM 4 0 GLY B 416 -11.853 -72.729 -37.367 1.00 52.60 0 ATOM 1 N THR B 417 -13.305 -72.985 -39.075 1.00 52.54 N ATOM 2 CA TFIR B 417 -12.774 -74.275 -39.501 1.00 52.37 C ATOM 3 CB THR B 417 -13.594 -74.865 -40.664 1.00 52.27 C ATOM 4 OGI THR B 417 -13.938 -73.824 -41.584 1.00 51.98 0 ATOM 5 CG2THRB417 -14.869-75.497-40.147 1.0052.29 C ATOM 6 C THRB 417 -11.303-74.199-39.906 1.00 52.41 C 5'. ATOM 7 0 THRB4I7 -10.666-75.226-40.137 1.0052.44 0 ATOM I N ARC B 418 -10.769 -72.982 -39.984 1.00 52.48 N ATOM 2 CA ARC B 418 -9.376 -72.768 -40.365 1.00 52. 60 C "s 45 ATOM 3 CB ARGB4I8 -9.159-71.335-40.852 1.0052.61 C ATOM 4 CG ARGB4I8 -9.600-71.097-42.286 1.0053.27 C ATOM 5 CD ARC B418 -9.177-69.722-42.800 1.00 54.81 C ATOM 6 NE ARGB4I8 -7.737-69.623-43.033 1.0055.96 N ATOM 7 CZ ARG B 418 -6.871 -69.084 -42.177 1.00 56.80 C ATOM 8 N1-IIARGB4I8 -5.577-69.038-42.478 1.0057.11 N ATOM 9 NH2 ARG B 418 -7.295 -68.589 -41.019 1.00 56.93 N ATOM 10 C ARGB418 -8.416-73.077-39.226 1.0052.65 C ATOM 11 0 ARGB4I8 -7.222-73.271-39.444 1.0052.59 0 ATOM 1 N MET B 419 -8.943 -73.129 -38.010 1.00 52.86 N ATOM 2 CA METB4I9 -8.113-73.399-36.846 1.0053.06 C ATOM 3 CB METB4I9 -8.676-72.685-35.610 1.0053.29 C ATOM 4 CG MET B 419 -7.647 -72.383 -34.513 1.00 54.17 C ATOM 5 SD MET B 419 -6.116 -7 1.599 -35.095 1.00 55.92 S ATOM 6 CE METB4I9 -4.994-72.997-35.162 1.0055.37 C ATOM 7 C MET B 419.7.962 -74.904 -36.603 1.00 52.89 C ATOM 8 0 MET B 419 -7.250 -75.326 -35.693 1.00 52.78 0 ATOM I N GLY B 420 -8.624 -75.707 -37.43 1 1.00 52.86 N ATOM 2 CA GLY.B420 -8.528-77.161 -37.334 1.0052.96 C ATOM 3 C GLY B 420 -9.803 -77.82 1 -36.838 1.00 53.03 C ATOM 4 0 GLYB42O -10.731 -77.138-36.407 1.00 53.13 0 ATOM 1 N PRO B 421 -9.864 -79.161 -36.911 1.00 53.04 N ATOM 2 CA PRO B 421 -11.037 -79.878 -36471 1.00 53.09 C ATOM 3 CB PRO B 421 -11.173 -80.952 -37.548 1.00 52.99 C ATOM 4 CO PRO B 421 -9.717 -81.301 -37.885 1 00 52. 91 C ATOM 5 CD PRO B 421 -8.857 -80.087 -37.465 1.00 53.05 C ATOM 6 C PROB42I -10.848-80.558-35.115 1.0053.26 C ATOM 7 0 PRO B421 -11.742-81.294-34.668 1.00 53.35 0 ATOM I N PHEB422 -9.710-80.321 -34.459 1.00 53.47 N ATOM 2 CA PUB B 422 -9.361 -81 125 -33.284 1.00 53.71 C ATOM 3 CB PHEB422 -7.939-81.673-33.392 1.0053.51 C ATOM 4 CG PHE B 422 -7.860 -82.947 -34.161 1.00 53.01 C ATOM 5 CD! PHE B 422 -7.556 -82.939 -35.506 1.00 52.78 C ATOM 6 CEI PHEB422 -7.500 -84.113 -36.221 1.00 52.83 C ATOM 7 CZ PHEB422 -7.760-85.312-35.596 1.00 52.98 C ATOM 8 CE2 PHE B 422 -8.077 -85.33 1 -34.256 1.00 52.93 C ATOM 9 CD2 PHE B 422 -8.131 -84.153 -33.547 1.00 52.79 C ATOM 10 C PHE B 422 -9.606 -80.504 -31.913 1.00 54.16 C ATOM 11 0 PHEB422 -10.048-81.193-30.989 1.0054.20 0 ATOM 1 N VAL B 423 -9.3 14 -79.2 17 -31.767 1.00 54.72 N ATOM 2 CA VAL B 423 -9.603 -78.540 -30.507 1.00 55.30 C ATOM 3 CB VALB423 -8.329-77.988-29.828 1.0055.35 C ATOM 4 CGI VAL B 423 -8.687 -77.283 -28.525 1.00 55.52 C ATOM 5 CG2 VAL B 423 -7.340 -79.119 -29.559 1.00 55.43 C ATOM 6 C VAL B 423 -10.633 -77.434 -30.704 1.00 55.57 C ATOM 7 0 VAL B 423 -10.364 -76.444 -3 1.387 1.00 55.56 0 ATOM I N GLU B 424 -11.808 -77.627 -30.100 1.00 56.06 N ATOM 2 CA GLU B 424 -12.936.76.685 -30.174 1.00 56.34 C ATOM 3 CB GLU B 424 -12.605 -75.352 -29.463 1.00 56.44 C ATOM 4 CG GLU B 424 -13.793 -74.350 -29.302 1.00 56.50 C ATOM 5 CD GLU B 424 -13.681 -73.133 -30.258 1.00 57.30 C ATOM 6 OEI GLU B 424 -12.463 -72.749 -30.638 1.00 57.51 0 ATOM 7 0E2 GLU B 424 -14.750 -72.545 -30.636 1.00 57.40 0 ATOM 8 C GLUB424 -13.429-76.440-31.610 1.0056.48 C ATOM 9 0 GLU B 424 -12.779 -75.721 -32.388 1.00 56.64 0 a..'. TER 9 GLUB424 ATOM I N GLUB443 -0.405-85.521 -2.811 1.0065.60 N ATOM 2 CA GLU B 443 0.611 -84.482 -2.704 1.00 65.73 C . . 45 ATOM 3 CB GLU B 443 1.290 -84.527 -1.330 1.00 66.04 C a...</p>..DTD: ATOM 4 CG GLU B 443 2.377 -83.462 -1.118 1.00 67.13 C ATOM 5 CD GLUB443 1.813-82.071 -0.850 1.0068.58 C ATOM 6 OE! GLU B 443 0.633 -81.816.1.184 1.00 69.01 0 ATOM 7 OE2 GLU B 443 2.558.81.229 -0.300 1.00 69.27 0 ATOM 8 C GLU B 443 1.653 -84.609 -3.809 1.00 65.36 C ATOM 9 0 GLUB443 1.374-84.292 -4.965 1.0065.51 0 . .: ATOM I N TRP B 444 2.848 -85.071 -3.442 1.00 64.83 N ATOM 2 CA TRPB444 3.954-85.228 -4.383 1.0064.28 C ATOM 3 CB TRPB444 5.231 -84.611 -3.807 1.0064.11 C ATOM 4 CG TRP B 444 6.3 19 -84.393 -4.820 1.00 63.96 C ATOM 5 CD! TRP B 444 6.157 -84.086 -6.139 1.0063.74 C ATOM 6 NEI TRP B 444 7.382 -83.952 -6.748 1.00 63.50 N ATOM 7 CE2 TRP B 444 8.367 -84.164 -5.821 1.00 63.49 C ATOM 8 CD2 TR.P B 444 7.736 -84.438 -4.591 1.00 63.81 C ATOM 9 CE3 TR.P B 444 8.530 -84.694 -3.469 1.00 63.77 C ATOM 10 CZ3 TRP B 444 9.909 -84.665 -3.612 1.00 63.70 C ATOM 11 CH2TR.PB444 10.505-84.386 -4.846 1.0063.62 C ATOM 12 CZ2TRPB444 9.753-84.137 -5.960 1.0063.59 C ATOM 13 C TRP B 444 4,158 -86.707 -4.672 1 006404 C ATOM 14 0 TRP B 444 4.079 -87.53 1 -3.767 1.00 64.09 0 ATOM 1 N VAL B 445 4.426 -87.043 -5.930 1.00 63.74 N ATOM 2 CA VAL B 445 4.422 -88.445 -6.349 1.00 63.47 C ATOM 3 CB VAL B 445 4.157 -88.591 -7.867 1.00 63.49 C ATOM 4 CG1 VALB 445 3.400-89.891 -8.137 1.00 63.40 C ATOM 5 CG2 VAL B 445 3.347 -87.4 10 -8.382 1.00 63.67 C ATOM 6 C VALB445 5.686-89.236 -5.995 1.0063.28 C ATOM 7 0 VAL B 445 5.652 -90.466 -5.953 1.00 63.22 0 ATOM I N VALB446 6.797-88.549 -5.742 1.0063.03 N ATOM 2 CA VALB446 8.068-89.251 -5.538 1.0062.82 C ATOM 3 CB VAL B 446 9.258 -88.540 -6.237 1.00 62.73 C ATOM 4 CGI VALB446 8.775-87.739 -7.436 1.0062.74 C ATOM 5 CG2 VAL B 446 9.992 -87.644 -5.27 1 1.00 62.62 C ATOM 6 C VALB446 8.400-89.527 -4.066 1.0062.78 C ATOM 7 0 VAL B 446 9.343 -90.263 -3.764 1.00 62.73 0 ATOM I N THR B 447 7.616 -88.954 -3.155 1.0062 71 N ATOM 2 CA THRB447 7.850-89.148 -1.722 1.0062.74 C ATOM 3 CB THRB447 6.862-88.339 -0.858 1.0062.72 C ATOM 4 OGI THR B 447 5.639 -88.163 -1.578 1.00 63.01 0 ATOM 5 CG2 THR B 447 7.438 -86.972 -0.526 1.00 62.66 C ATOM 6 C THR B 447 7.820 -90.620 -1.301 1.00 62.71 C ATOM 7 0 THRB 447 8.427 -90.991 -0.295 1.00 62.63 0 ATOM I N LYS B 448 7.121 -91.453 -2.070 1.00 62.74 N ATOM 2 CA LYSB448 7.119-92.895 -1.822 1.0062.80 C ATOM 3 CB LYSB448 6.130-93.628 -2.735 1.0062.76 C ATOM 4 CO LYSB448 4.711 -93.108 -2.686 1.0063.05 C ATOM 5 CD LYSB448 4.392-92.289 -3.923 1.0063.48 C ATOM 6 CE LYS B 448 3.255 -91.319 -3.661 1.00 63.64 C ATOM 7 NZ LYSB 448 3.668-90.275 -2.681 1.00 63.53 N ATOM 8 C LYS B 448 8.5 14 -93.490 -2.009 1.00 62.83 C ATOM 9 0 LYS B 448 8.957 -94.3 14' -1.209 1.00 63.01 0 ATOM I N ASP B 449 9.203 -93. 070 -3.065 1.00 62.70 N ATOM 2 CA ASP B 449 10.507 -93.632 -3.390 1.00 62.64 C ATOM 3 CB ASPB449 10.618-93.837 -4.902 1.0062.80 C ATOM 4 CG ASPB449 9.549-94.782 -5.444 1.0063.19 C : ... ATOM 5 ODI ASP B 449 9.378 -95.890 -4.877 1.00 63.74 0 ATOM 6 0D2 ASP B 449 8.881 -94.419 -6.439 1.00 63.29 0 ATOM 7 C ASPB449 11.632-92.743 -2.869 1.00 62.46 C ATOM 8 0 ASPB449 12.816-92.959 -3.166 1.0062.44 0 ATOM 1 N LYSB45O 11.247-91.756 -2.066 1.0062.30 N ATOM 2 CA LYSB45O 12.174-90.744 -1.578 1.0062.13 C : ATOM 3 CB LYS B 450 11.449 -89.734 -0.687 1.00 62.11 C * ATOM 4 CG LYS B 450 11.805 -88.274 -0.967 1.00 61.77 C ATOM 5 CD LYS B 450 13.208 -87.897 -0.505 1. 00 60.83 C ** ATOM 6 CE LYS B 450 13.530 -86,454 -0.874 1.00 59.97 C ATOM 7 NZ LYSB45O 14.896-86.047 -0.463 1.00 59.33 N ATOM 8 C LYSB45O 13.360-91.352 -0.833 1.00 62.15 C ATOM 9 0 LYS B 450 14.487 -9 1.248 -1.294 1,00 62.07 0 ATOM I N SERB45I 13.106-91.983 0.310 1.0062.16 N ATOM 2 CA SERB451 14.180-92.559 1.125 1.0062.17 C ATOM 3 CB SERB451 13.587-93.360 2.281 1.0062.12 C ATOM 4 OG SERB451 12.298-93.834 1.938 1.0062.06 0 ATOM 5 C SER B 451 15.154 -93.4 15 0.303 1.00 62.26 C ATOM 6 0 SERB45I 16.370-93.404 0.536 1.0062.26 0 ATOM I N LYS8452 14.605-94.144 -0.662 1.0062.25 N ATOM 2 CA LYSB452 15.375-94.923.1.626 1.0062.40 C ATOM 3 CB LYS B 452 14.369 -95.657 -2.519 1.00 62.38 C ATOM 4 CG LYSB452 14.904-96.422 -3.717 1.0062.84 C ATOM 5 CD LYS B 452 13.773 -97.330 -4. 253 1.00 63.07 C ATOM 6 CE LYS B 452 13.989 -97.788 -5.702 1.00 6407 C ATOM 7 NZ LYSB452 13.378-96.868 -6.709 1.0063.97 N ATOM 8 C LYSB452 16.312-94. 016 -2.449 1.0062.22 C ATOM 9 0 LYS B 452 17.575 -94.152 -2.426 1.00 62.21 0 ATOM I N TYRB453 15.696-93.076 -3.164 1.00 62.12 N ATOM 2 CA TYRB 453 16.465 -92.110 -3.934 1.00 61.83 C ATOM 3 CB TYRB 453 15.541 -91.057 -4.531 1.00 61.96 C ATOM 4 CO TYRB453 14.589-91.611 -5.559 1.0062.18 C ATOM 5 CD1 TYR. B 453 14.878 -92.789 -6.231 1.00 62.45 C ATOM 6 CEI TYRB 453 14.016-93.298 -7.179 1.00 62.52 C ATOM 7 CZ TYR B 453 12.855 -92.622 -7.475 1.00 62.28 C ATOM 8 011 TYR B 453 12.004 -93.133 -8.419 1.00 62.68 0 ATOM 9 CE2 TYR B 453 12.543 -91445 -6.830 1.00 62.18 C ATOM 10 CD2TYRB 453 13.411 -90.945 -5.878 1.00 62.43 C ATOM 11 C TYR B 453 17.547 -91.449 -3.082 1.00 61.73 C ATOM 12 0 TYRB 453 18.696-91.346 -3.504 1.0061.52 0 ATOM 1 N ASP B454 17.167-91.011 -1.883 1.00 61.76 N ATOM 2 CA ASP B 454 18.083 -90.401 -0.921 1.00 61.68 C ATOM 3 CB ASP B 454 17.359 -90.082 0.386 1.00 61.75 C ATOM 4 CO ASP B 454 16.590 -88.786 0.325 1.00 62.05 C ATOM 5 ODI ASP B 454 16.033 -88.378 1.367 1.00 62.30 0 ATOM 6 OD2ASPB4S4 16.545-88.176 -0.764 1.0063.12 0 ATOM 7 C ASP B 454 19.261 -91.304 -0.616 1.00 61.60 C ATOM 8 0 ASP B 454 20.408 -90.860 -0.647 1.00 61.46 0 ATOM I 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 1.00 61.50 C ATOM 3 CB GLUB 455 19.472 -94.962 -0.044 1.00 61.52 C ATOM 4 CO GLUB455 20.300-95.931 0.792 1.0061.62 C ATOM 5 CD OLU B 455 19.026 -96.015 1.970 0.00 50.00 C ATOM 6 OE1 GLU B 455 19.504 -96.674 2.9 12 0.00 50.00 0 ATOM 7 0E2 GLU B 455 18.049 -95.268 2.084 0.00 50.00 0 ATOM 8 C GLU B 455 21.043 -93.399 -1.253 1.00 61.47 C ATOM 9 0 GLU B 455 22.270 -93.244 -1.009 1.00 61.39 0 ATOM I N ILEB456 20.534-93.395 -2.504 1.0061.57 N ATOM 2 CA ILE B 456 21.505 -93.246 -3.620 1.00 61.40 C S...

ATOM 3 CB ILE B 456 20.873 -93.420 -5.034 1.00 61.41 C ATOM 4 COl ILE B 456 20.581 -94.894 -5.336 1.00 61.57 C *. 45 ATOM 5 CDI ILE B 456 19.280 -95.411 -4.766 1.00 61.87 C S.... ATOM 6 CG2ILEB456 21.819-92.913 -6.108 1.00 60.97 C ATOM 7 C 1LEB456 22.232-91.892 -3.557 1.0061.33 C *:: ATOM 8 0 1LEB456 23.473-91.817 -3.487 1.00 61.32 0 ATOM 1 N PHE B 457 21.439 -90.826 -3.568 1.00 61.28 N : 50 ATOM 2 CA PHEB457 21.951-89.462 -3.579 1.0061.18 C ATOM 3 CB PHEB 457 20.825 -88.478 -3.264 1.00 61.10 C . : ATOM 4 CO PHEB457 21.288-87.059 -3.078 1.00 61.06 C * . ATOM 5 CDIPHEB457 21.514-86.240 -4.173 1.0060.72 C ATOM 6 CEI PHE B 457 21.925 -84.930 -4.005 1.00 60.37 C ATOM 7 CZ PHE B 457 22.109 -84.424 -2.737 1.00 60.51 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 1.00 61.08 C ATOM 11 0 PHEB457 24.142-88.746 -2.928 1.0061.04 0 ATOM I N TYRB 458 22.852-89.710 -1.357 1.0061.12 N ATOM 2 CA TYR B 458 23.845 -89.535 -0.3 13 1.00 60.96 C ATOM 3 CB TYR B 458 23.207 -89.605 1.071 1.00 60.87 C ATOM 4 CG TYR B 458 22.380 -88.380 1.374 1.00 60.78 C ATOM 5 CD1 TYR B 458 22.977 -87.135 1.493 1.00 60.62 C ATOM 6 CEI TYR B 458 22.233 -86.009 1.76 I 1.00 60.72 C ATOM 7 CZ TYRB 458 20.870 -86.115 1.910 1.00 60.91 C ATOM 8 OH TYRB 458 20.124-84.987 2.178 1.00 61.14 0 ATOM 9 CE2 TYR B 458 20.250 -87.340 1.793 1.00 60.97 C ATOM 10 CD2TYRB458 21.005-88.463 1.521 1.0060.82 C ATOM 11 C TYR B 458 24.997 -90.509 -0.460 1.00 60.98 C ATOM 12 0 TYRB 458 26.113-90.212 -0.039 1.00 60.99 0 ATOM 1 N ASN B 459 24.746 -91.663 -1 076 1.00 61.12 N ATOM 2 CA ASN B 459 25874-92.529 -1.426 1.00 61.04 C ATOM 3 CB ASN B 459 25.435 -93.967 -1.690 1.00 61.02 C ATOM 4 CG ASN8459 25.682-94.868 -0.501 1.0061.15 C ATOM 5 OD1 ASN B 459 24.853 -95.713.0.163 1.00 61.72 0 ATOM 6 ND2 ASN B 459 26.826.94.682 0.152 1.00 61.27 N ATOM 7 C ASNB4S9 26.725-91.986 -2.573 1.0061.02 C ATOM 8 0 ASN B 459 27.807 -92.503 -2.846 1.00 60.90 0 ATOM I N LEU B 460 26.238 -90.936 -3.234 1.00 61.16 N ATOM 2 CA LEU B 460 27.036 -90 256 -4.269 1.00 61.21 C ATOM 3 CB LEU B 460 26. 144 -89.735 -5.399 1.00 61.18 C ATOM 4 CO LEU B 460 25.941 -90.65 1 -6.607 1.00 61.31 C ATOM 5 CDI LEU B 460 25.626 -92.08 1 -6.188 1.00 61.70 C ATOM 6 CD2 LEU B 460 24.853 -90.103 -7.5 19 1.00 61.36 C ATOM 7 C LEUB46O 27.927-89.118 -3.751 1.0061.21 C ATOM 8 0 LEU B 460 28.542 -88.401 -4.542 1.00 61.15 0 ATOM I N ALAB461 27.990-88.958 -2.431 1.0061.30 N ATOM 2 CA ALA B461 28.832-87.933 -1.791 1.00 61.39 C ATOM 3 CB ALAB46I 30.310-88. 328 -1.848 1.0061.32 C ATOM 4 C ALA B 461 28.632 -86.526 -2.356 1.00 61.46 C ATOM 5 0 ALAB 461 29.489-86.016 -3.080 1.00 61.46 0 ATOM 1 N PRO B 462 27.498 -85.891 -2.015 1.00 61.52 N ATOM 2 CA PRO B 462 27.192 -84.538 -2.456 1.00 61.50 C ATOM 3 CB PRO B 462 25.672 -84.439 -2.278 1.00 61.48 C ATOM 4 CO PRO B 462 25.224 -85.764 -1.701 1.00 61.39 C ATOM 5 CD PR0B462 26.429-86.437 -1.167 1.0061.48 C ATOM 6 C PROB 462 27.888-83.514 -1573 1.00 61.55 C ATOM 7 0 PRO B 462 28.433 -83.873 -0.532 1.00 61.39 0 * ATOM 1 N ALA B 463 27.859 -82.252 -1.992 1.00 61.78 N ATOM 2 CA ALAB 463 28.567-81.176 -1.301 1.00 61.99 C ATOM 3 CB ALA B 463 28.388 -79.860 -2.043 1.00 62.09 C ATOM 4 C ALAB463 28.111-81.031 0.140 1.0062.16 C ATOM 5 0 ALAB463 28.733-81.565 1.055 1.0062.42 0 ATOM 1 N ASP B 464 27.028 -80.293 0.343 1.00 62.26 N ATOM 2 CA ASP B 464 26.459 -80.154 1.673 1.00 62.40 C ATOM 3 CB ASP B 464 26.755 -78.767 2.250 1.00 62 60 C * *. 50 ATOM 4 CG ASP B 464 26.038 -77.65 1 1.502 1.00 63.34 C ATOM 5 OD1ASPB464 26.134-76.485 1.952 1.0063.76 0 *. : ATOM 6 OD2ASPB464 25.380-77.936 0. 471 1.0064.06 0 * ATOM 7 C ASP B 464 24.964-80.382 1.585 1.00 62.23 C ATOM 8 0 ASP B 464 24.207 -79.934 2.434 1.00 62.39 0 ATOM 1 N GLY B 465 24.549 -8 1.083 0.541 1.00 62.02 N ATOM 2 CA GLY B 465 23. 140 -81.324 0.294 1.00 61.82 C ATOM 3 C GLYB46S 22.898-81.127 -1.183 1.0061.70 C ATOM 4 0 GLY B 465 21.784 -8 1.310 -1.678 1.00 61.73 0 ATOM 1 N LYS B 466 23.960 -80.752 -1.887 1.00 61.43 N ATOM 2 CA LYSB466 23.879-80.507 -3.311 10061.22 C ATOM 3 CB LYS B 466 24 071 -79.023 -3.604 1.00 61.21 C ATOM 4 CG LYS B 466 22.937 -78.154 -3.108 1.00 61.05 C ATOM 5 CD LYS B 466 23.345 -76.698 -3.052 1.00 61.32 C ATOM 6 CE LYS B 466 22.293 -75.881 -2.334 1.00 61.80 C ATOM 7 NZ LYS B 466 2 1.944 -76.494 -1 019 1.00 62.20 N ATOM 8 C LYS B 466 24.917 -81.323 -4.053 1.00 61.12 C ATOM 9 0 LYSB466 26.113-81.218 -3.792 1.0061.13 0 ATOM I N LEIJ B 467 24.448 -82.144 -4.980 1.00 61.00 N ATOM 2 CA LEUB 467 25.341 -82.926 -5.809 1.00 60.88 C ATOM 3 CB LEU B 467 24.618 -84.164 -6.341 1.00 60.79 C ATOM 4 CG LEUB467 25.461 -85.111 -7.190 1.00 60.87 C ATOM 5 CDI LEU B 467 26.613 -85.658 -6.365 1.00 61.30 C ATOM 6 CD2 LEU B 467 24.614 -86.240 -7.743 1.00 60.91 C ATOM 7 C LEU B 467 25.839 -82.065 -6.966 1 00 60.83 C ATOM 8 0 LEUB467 25.044-81.491 -7.712 1.0060.86 0 ATOM I N SER B 468 27.158 -81.966 -7.099 1.00 60.71 N ATOM 2 CA SER B 468 27.777 -81.277 -8.227 1.00 60.55 C ATOM 3 CB SER B 468 29. 287 -81.522 -8.211 1.00 60.68 C ATOM 4 OG SERB468 29.806-81.658 -9.524 1.0061.03 0 ATOM 5 C SER B 468 27.182 -81.727 -9.564 1.00 60.34 C ATOM 6 0 SER B 468 26.679 -82.846 -9.682 1.00 60.29 0 ATOM 1 N GLY B 469 27.246 -80.852 -10.565 1.00 60.13 N ATOM 2 CA GLY B 469 26.713 -81.153 -11.894 1.00 59.92 C ATOM 3 C GLY B 469 27.448 -82.273 -12.611 1.00 59.86 C ATOM 4 0 GLY B 469 26.835 -83.108 -13.278 1.00 59.75 0 ATOM 1 N SER B 470 28.767 -82.298 -12.471 1.00 59.92 N ATOM 2 CA SERB 470 29.580-83.316-13.128 1.00 60.13 C ATOM 3 CB SERB47O 31.070-82.996-12.972 1.0060.18 C ATOM 4 OG SER B 470 31.409 -82.804 -11.610 1.00 60.39 0 ATOM 5 C SERB 470 29.271 -84.730 -12.621 1.00 60.16 C ATOM 6 0 SERB 470 29.128-85.667-13.415 1.00 60.19 0 ATOM I N LYS B 471 29.165 -84.875 -11.301 1.00 60.16 N ATOM 2 CA LYS B 471 28.853 -86.160 -10.680 1.00 60.23 C ATOM 3 CB LYS B 471 28.918 -86.032 -9.157 1.00 60.32 C ATOM 4 CG LYS B 471 29.715 -84.826 -8.674 1.00 60.75 C ATOM 5 CD LYS B 471 31.190 -85.140 -8.471 1.00 61.90 C ATOM 6 CE LYS B 471 31.583 -85.072 -6.994 1.00 62.37 C ATOM 7 NZ LYS B 471 30.749 -85.959 -6.130 1.00 62.88 N ATOM 8 C LYSB47I 27.452-86.600-11.106 1.0060.16 C * "S ATOM 9 0 LYSB471 27.223-87.758-11.515 1.0060.14 0 ATOM I N ALAB472 26.521-85.654-11.014 1.0060.13 N ATOM 2 CA ALA B472 25.155-85.868-11.458 1.00 60.03 C ATOM 3 CB ALA B 472 24.353 -84.582 -11.354 1.00 59.90 C ATOM 4 C ALA B 472 25.170 -86.382 -12.890 1.00 59.97 C ATOM 5 0 ALA B 472 24.488 -87.358 -13.218 1.00 60.05 0 ATOM I N LYSB473 25.966-85.741-13.739 1.0059.85 N ATOM 2 CA LYSB 473 26.063 -86.203 -15.112 1.00 59.96 C * *, 50 ATOM 3 CB LYSB473 26.893-85.269-15.988 1.0059.91 C ATOM 4 CG LYS B 473 26.875 -85.683 -17.455 1.00 59.67 C ** * ATOM 5 CD LYSB473 27.769-84.800-18.309 1.0059.75 C ATOM 6 CE LYS B 473 27.437 -84.943 -19.788 1.00 59.64 C ATOM 7 NZ LYS B 473 28.334 -84.122 -20.649 1.00 59. 71 N ATOM 8 C LYSB473 26.611 -87.620-15.183 1.00 60.14 C ATOM 9 0 LYS B 473 25.941 -88.495 -15.719 1.00 60.26 0 ATOM I N THR B 474 27.806 -87.866 -14.640 1.00 60.16 N ATOM 2 CA THRB 474 28.372-89.219-14.739 1.00 60.24 C ATOM 3 CB THRB474 29.757-89.402-14.031 1.0060.23 C ATOM 4 001 THR B 474 29.800 -88.662 -12.808 1.00 60.62 0 ATOM 5 CO2THRB474 30.894-88.933-14. 931 1.0060.37 C ATOM 6 C THRB474 27.364-90.289-14.301 1.0060.23 C ATOM 7 0 THRB474 27.219-91.319-14.966 1.0060.25 0 ATOM 1 N TRP B 475 26.645 -90. 037 -13 211 1.00 60.28 N ATOM 2 CA TRY B 475 25.606 -90.978 -12.787 1.00 60. 42 C ATOM 3 CB TRPB 475 25.023-90.535-11.445 1.0060.84 C ATOM 4 CG TRPB475 23.813-91.301-11.013 1.0061.18 C ATOM 5 CD1 TRP B 475 23.775 -92.585 -10.565 1.00 61.70 C ATOM 6 NEI TRP B 475 22.485 -92.942 -10.256 1.00 61.88 N ATOM 7 CE2TRPB475 21.660-91.878-10.500 1.00 61.50 C ATOM 8 CD2 TRY B 475 22.463 -90.823 -10.976 1.00 61.57 C ATOM 9 CE3TRPB475 21.854-89.606-11.306 1.0062.24 C ATOM 10 CZ3 TRY B 475 20.477 -89.484 -11.149 1.0062.05 C ATOM 11 CH2TRPB475 19.707-90.555-10.671 1.0061.82 C ATOM 12 CZ2TRPB475 20.280-91.756-10.343 1.0061.71 C ATOM 13 C TRPB475 24.498-91.098-13.840 1.0060.37 C ATOM 14 0 TRPB475 24.152-92.206-14.315 1.0060.28 0 ATOM 1 N MET B 476 23.944 -89.948 -14.209 1.00 60.24 N ATOM 2 CA MET B 476 22.858 -89.927 -15.166 1.00 60.43 C ATOM 3 CB METB476 22.436-88.492-15.483 1.0060.35 C ATOM 4 CO MET B 476 2 1.636 -87.837 -14.364 1.00 60.65 C ATOM 5 SD MET B 476 2 1.109 -86.145 -14.729 1.00 60.97 S ATOM 6 CE MET B 476 19.647-86.452 -15.725 1.00 61.19 C ATOM 7 C MET B 476 23.239 -90.692 -16.43 1 1.00 60.37 C ATOM 8 0 MET B 476 22.549 -9 1.632 -16.828 1.00 60.37 0 ATOM I N VAL B 477 24.347 -90.304 -17.053 1.00 60.31 N ATOM 2 CA VAL B 477 24.808 -90.980 -18.253 1.00 60.18 C ATOM 3 CB VALB477 26.072-90.317-18.844 1.0060.16 C ATOM 4 CG1 VALB 477 27.334-91.039-18.386 1.00 60.18 C ATOM 5 CG2 VAL B 477 25.991 -90.304 -20.364 1.00 60.61 C ATOM 6 C VAL B 477 25.053 -92.442 -17.904 1.00 60.04 C ATOM 7 0 VAL B 477 24.963 -93.322 -18.759 1.00 59.92 0 ATOM 1 N GLY B 478 25.336 -92.689 -16.628 1.00 60.05 N ATOM 2 CA GLY B 478 25.437 -94. 048 -16.110 1.00 59.87 C ATOM 3 C GLY B 478 24.152 -94.826 -16.3 10 1.00 59. 75 C ATOM 4 0 GLY B 478 24.183 -96.039 -16.508 1.00 59.64 0 ATOM 1 N THRB 479 23.012-94.139-16.265 1.00 59.79 N ATOM 2 CA THR B 479 21.730 -94.827 -16.546 1.00 59.54 C **** ATOM 3 CB THRB479 20.512-93.965-16.201 1.00 59.50 C ATOM 4 OG1 THR B 479 20.208 -93.109-17.311 1.00 59.40 0 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 1.00 59.41 C ATOM 7 0 THRB 479 20.429 -95.606 -18.416 1. 00 59.36 0 ATOM I N LYSB48O 22.626-95.279-18.772 1.0059.24 N ATOM 2 CA LYS B 480 22.602 -95.706 -20.175 1.00 59.00 C ATOM 3 CB LYSB48O 22.607-97.236-20.281 1.0058.90 C ATOM 4 CO LYS B 480 24.220 -97.582 -20.411 0.00 50.00 C ATOM 5 CD LYS B 480 24.384 -99.002 -19.919 0.00 50. 00 C "S ATOM 6 CE LYS B 480 23.123 -99.825 -20.052 0.00 50.00 C : ATOM 7 NZ LYS B 480 22.663-100.001 -21.452 0.00 50.00 N S ATOM 8 C LYSB48O 21.452-95.120-21.000 1.00 58.86 C ATOM 9 0 LYS B 480 20.932 -95.778 -2 1.898 1.00 59.02 0 ATOM I N LEU B 481 2 1.062 -93.884 -20.699 1.00 58.63 N ATOM 2 CA LEU B 481 20.089 -93.169 -21.522 1.00 58.40 C ATOM 3 CB LEU B 481 19.144 -92.336 -20.650 1.00 58.41 C ATOM 4 CG LEU B 481 17.948 -93. 045 -20.0 13 1.00 58.17 C ATOM 5 CDI LEU B 481 17.016 -92.033 -19.380 1.00 57.72 C ATOM 6 CD2 LEU B 481 17.200 -93.871 -21.043 1.00 57.96 C ATOM 7 C LEUB48I 20.803-92.264-22.524 1.0058.27 C ATOM 8 0 LEUB48I 21.929-91.835-22.276 1.0058.35 0 ATOM I N PR0B482 20.156-91.980-23.667 1.0058.15 N ATOM 2 CA PR0B482 20.739-91.080-24.662 1.0058.10 C ATOM 3 CB PROB482 19.732-91.119-25.815 1.0058.03 C ATOM 4 CO PROB 482 18.465-91.591 -25.212 1.0058.03 C ATOM 5 CD PRO B 482 18.849 -92.507 -24.096 1.00 58.12 C ATOM 6 C PR0B482 20.889-89.658-24.134 1.0058.13 C ATOM 7 0 PRO B 482 20.023 -89.170 -23.407 1.00 58.05 0 ATOM 1 N ASN B 483 21.990 -89.010 -24.508 1.00 58.25 N ATOM 2 CA ASN B 483 22.326 -87.673 -24.018 1.00 58. 27 C ATOM 3 CB ASN B 483 23.466 -87.069 -24.846 1.00 58.41 C ATOM 4 CG ASN B 483 24.180 -85.936 -24.122 1.00 58.98 C ATOM 5 OD1 ASN B 483 24.148 -84.782 -24.560 1.00 58.96 0 ATOM 6 ND2 ASN B 483 24.828 -86.264 -23.005 1.00 59.69 N ATOM 7 C ASNB483 21.130-86.730-24.011 1.0057.99 C ATOM 8 0 ASNB483 20.749-86.219-22.971 1.0057.84 0 ATOM I N SER B 484 20.548 -86. 515 -25.185 1.00 57.91 N ATOM 2 CA SER B 484 19.395 -85.634 -25.365 1.00 57. 86 C ATOM 3 CB SERB 484 18.779-85.891 -26.746 1.00 57.83 C ATOM 4 00 SER B 484 17.367 -85.789 -26.726 1.00 58.63 0 ATOM 5 C SERB 484 18.351 -85.771 -24.249 1.00 57.69 C ATOM 6 0 SERB484 18.038-84.801 -23.542 1.00 57 89 0 ATOM I N VALB485 17.823-86.978-24.085 1.0057.50 N ATOM 2 CA VAL B 485 16.868 -87.246 -23.025 1.00 57.27 C ATOM 3 CB VAL B 485 16.534 -88.746 -22.933 1.00 57.16 C ATOM 4 CG1 VALB485 15.787-89.050-21.650 1.0056.97 C ATOM 5 CG2 VAL B 485 15.713 -89.173 -24.133 1.00 56.96 C ATOM 6 C VAL B 485 17.425 -86.756 -2 1.697 1.00 57.35 C ATOM 7 0 VAL B 485 16.803 -85. 944 -21.017 1.00 57.43 0 ATOM 1 N LEUB 486 18.613 -87.233 -21.341 1.00 57.54 N ATOM 2 CA LEU B 486 19.239 -86.843 -20.080 1.00 57.77 C ATOM 3 CB LEUB486 20.638-87.454-19.946 1.0057.88 C ATOM 4 CO LEU B 486 20.729 -88.972 -19.774 1.00 58.42 C ATOM 5 CDI LEU B 486 22.172 -89.447 -19.904 1.00 58.66 C ATOM 6 CD2 LEU B 486 20.138 -89.407 -18.439 1.00 58.90 C ATOM 7 C LEU B 486 19.303 -85.325 -19.908 1.00 57.80 C ATOM 8 0 LEU B 486 18.955 -84.808 -18.850 1.00 57.86 0 a. ATOM I N GLY B 487 19.749 -84.618 -20.945 1.00 57.71 N : ... ATOM 2 CA GLYB487 19.857-83.163 -20.904 1.00 57.64 C ATOM 3 C GLYB487 18.516-82.531-20.601 1.0057.70 C ATOM 4 0 GLYB487 18.406-81.638-19.741 1.0057.71 0 ATOM I N ARG B 488 17.488 -83.010 -21. 298 1.00 57.78 N ATOM 2 CA ARGB488 16.128-82.544-21.042 1.00 57.97 C ATOM 3 CB ARGB488 15.152-83.209-22.013 1.00 58.06 C ATOM 4 CG ARG B 488 13.971 -82.338 -22.415 1.00 59.39 C * S ATOM 5 CD ARG B 488 13.610 -82.573 -23.881 1.00 61.62 C * ** 50 ATOM 6 NE ARG B 488 13.092 -83.923 -24.122 1.00 63.12 N ATOM 7 CZ ARGB488 13.449-84.695-25.150 1.00 63.38 C ATOM 8 NH1 ARG B 488 12.920 -85.907 -25.285 1.00 63.40 N : ATOM 9 NH2ARGB488 14.347-84.266-26.033 1.0063.17 N ATOM 10 C ARGB488 15.727-82.814-19.583 1.0057.81 C ATOM 11 0 ARGB488 15.145-81.947-18.904 1.00 57.77 0 ATOM 1 N ILE B 489 16.064 -84.008 -19.099 1.00 57.58 N ATOM 2 CA ILE B 489 15.757 -84.377 -17.724 1.00 57.48 C ATOM 3 CB 1LEB489 16.163-85.815-17.413 1.00 57.33 C ATOM 4 CGI ILE B 489 15.256 -86.784 -18.167 1.00 57.24 C ATOM 5 CDI ILE B 489 15.547 -88.239 -17.903 1.00 57.50 C ATOM 6 CG2 ILE B 489 16.068 -86.066 -15.925 1.00 57.45 C ATOM 7 C 1LEB489 16.453-83.441-16.755 1.00 57.56 C ATOM 8 0 1LEB489 15.844-82.935-15.813 1.0057.63 0 ATOM I N TRPB49O 17.736-83.206-16.988 1.0057.67 N ATOM 2 CA TRP B 490 18.470 -82.265 -16.172 1.00 57.64 C ATOM 3 CB TRP B 490 19.867 -82.008 -16.731 1.00 57.40 C ATOM 4 CO TRP B 490 20.498 -80.874 -16.021 1.00 57.22 C ATOM 5 CDI TRP B 490 20.466 -79.563 -16.383 1.00 56.97 C ATOM 6 NE1 TRPB49O 21.128-78.800-15.453 1.00 57.04 N ATOM 7 CE2TRPB49O 21.592-79.619-14.458 1.0057.10 C ATOM 8 CD2 TRP B 490 21.204 -80.933 -14.780 1.00 57.28 C ATOM 9 CE3 TRY B 490 21.556 -81.974 -13.913 1.00 57.40 C ATOM 10 CZ3 TRP B 490 22.280 -81.672 -12.774 1.0057 15 C ATOM 11 CH2TRPB49O 22.654-80.354-12. 483 1.0057.10 C ATOM 12 CZ2 TRP B 490 22.320 -79.316 -13.310 1.00 57.08 C ATOM 13 C TRP B 490 17.708 -80.950 -16.129 1.00 57.62 C ATOM 14 0 TRPB49O 17.365-80.442-15.050 1.0057.65 0 ATOM I N LYS B 491 17.442 -80.409 -17. 315 1.00 57.68 N ATOM 2 CA LYS B 491 16.802 -79.103 -17.398 1.00 57.74 C ATOM 3 CB LYS B 491 16.559 -78.684 -18.847 1.00 57.75 C ATOM 4 CO LYS B 491 15.983 -77.286 -18.974 1.00 58.40 C ATOM 5 CD LYSB491 16.464-76.592-20. 236 1.0060.09 C ATOM 6 CE LYS B 491 17.902 -76.107 -20.079 1.00 61.13 C ATOM 7 NZ LYS B 491 17.986 -75.022 -19.050 1.00 62.38 N ATOM 8 C LYSB49I 15.509-79.077-16.602 1.0057.58 C ATOM 9 0 LYS B 491 15.215 -78.090 -15. 925 1.00 57.50 0 ATOM I N LEU B 492 14.746 -80.166 -16.680 1.00 57.51 N ATOM 2 CA LEU B 492 13.5 18 -80.287 -15.895 1.00 57.34 C ATOM 3 CB LEUB492 12.727-81.513-16.345 1.00 57.12 C ATOM 4 CG LEU B 492 11.442 -81.329 -17.148 1.00 56.50 C ATOM 5 CD1 LEU B 492 11.487 -80.090 -18.020 1.00 56.61 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 1.00 57.59 C ATOM 8 0 LEUB492 13.029-79.801 -13.582 1.00 57.53 0 ATOM 1 N SERB 493 14.847-81.051 -13.998 1.00 57.77 N ATOM 2 CA SERB493 15.079-81.357-12.595 1.0058.08 C ATOM 3 CB SER B 493 15.893 -82.641 -12.456 1.00 58.12 C ATOM 4 00 SERB493 15.156-83.746-12. 947 1.0058.62 0 ATOM 5 C SERB493 15.738 -80.231 -11.812 1.00 58.20 C * ATOM 6 0 SERB493 15.432-80.036-10.634 1.0058.25 0 ** ATOM 1 N ASP B 494 16.650 -79.499 -12.443 1.00 58.27 N ATOM 2 CA ASP B 494 17.297 -78.397 -11.735 1.00 58.62 C * * 45 ATOM 3 CB ASPB494 18.562-77.935-12.449 1.0058.56 C *.. ATOM 4 CG ASPB494 19.324-76.894-11.657 1.00 58.70 C ATOM 5 ODI ASP B 494 18.970 -76.661 -10.478 1.00 58.46 0 ATOM 6 0D2 ASP B 494 20.277 -76.308 -12.215 1.00 59.37 0 ATOM 7 C ASPB494 16.321-77.238-11.581 1.00 58.87 C * *. 50 ATOM 8 0 ASP B 494 16.383 -76.250 -12 315 1.00 58.88 0 ATOM 1 N VALB495 15.422-77.368-10.614 1.0059.15 N * ATOM 2 CA VALB49S 14.318-76.438-10.477 1.0059.38 C *. .: ATOM 3 CB VALB495 13.281 -76.921 -9.444 1.00 59.37 C ATOM 4 CGI VAL B 495 12.186 -75.883 -9.265 1.00 59.25 C ATOM S CG2 VAL B 495 12.681 -78.234 -9.894 1.00 59.21 C ATOM 6 C VAL B 495 14.779 -75.025 -10.155 1.00 59.65 C ATOM 7 0 VAL B 495 14.327 -74.077 -10.794 1.00 60.04 0 ATOM 1 N ASP B 496 15.671 -74.869 -9.180 1.00 59.85 N ATOM 2 CA ASPB496 16.168-73.525 -8.852 1.0060.04 C ATOM 3 CB ASP B 496 16.633 -73.422.7.395 1.00 60.09 C ATOM 4 CG ASPB496 17.676-74.455 -7.036 1.0060.31 C ATOM 5 ODI ASP B 496 17.844 -75.432 -7.801 1.00 60.71 0 ATOM 6 0D2 ASP B 496 18.325 -74.289 -5.979 1.00 60.45 0 ATOM 7 C ASP B 496 17. 271 -73.111 -9.817 1.00 60.06 C ATOM 8 0 ASP B 496 17.873 -72.046 -9.673 1.00 59.85 0 ATOM I N ARGB497 17.499-73.980-10.802 1.0060.35 N ATOM 2 CA AR0B497 18.462-73.785 -11.891 1.006065 C ATOM 3 CB ARGB497 17 785-73.166-13 129 1.00 60.76 C ATOM 4 CO ARGB497 17.801-71.656-13.234 1.0062.10 C ATOM 5 CD ARGB497 16.567-71.162-13.975 1.00 64.37 C ATOM 6 NE ARGB497 15.450-70.975-13.051 1.00 66.05 N ATOM 7 CZ ARG B 497 15 155 -69.817 -12.463 1.00 67.08 C ATOM 8 NH1 ARGB497 14.125-69.738-11.628 1.0067.52 N ATOM 9 NH2 ARG B 497 15.885 -68.733 -12.713 1.00 67.06 N ATOM 10 C ARGB497 19.771 -73.097-11.481 1.00 60.58 C ATOM 11 0 ARGB497 20.138-72.036-11.994 1.0060.38 0 ATOM 1 N ASPB498 20.476-73.740-10.552 1.0060.75 N ATOM 2 CA ASP B 498 21.748 -73.227 -10.062 1.00 60.92 C ATOM 3 CB ASP B 498 21.779 -73.207 -8.525 1.00 60.94 C ATOM 4 CO ASP B 498 21. 636 -74.597 -7.922 1.00 60.96 C ATOM 5 ODI ASP B 498 21.077 -75.493 -8.593 1.00 61.07 0 ATOM 6 0D2 ASP B 498 22.078 -74.792 -6.768 1.00 60.82 0 ATOM 7 C ASPB498 22.935-74.025-10.610 1.0061.06 C ATOM 8 0 ASP B 498 24.084 -73.496 -10.694 1.00 61.39 0 ATOM 1 N GLY B 499 22.672 -75.293 -10.981 1.00 61.04 N ATOM 2 CA GLY B 499 23.746-76.100-11.553 1.00 61.21 C ATOM 3 C GLYB499 24.043-77.366-10.775 1.0061.37 C ATOM 4 0 GLYB499 24.801 -78.229-11.235 1.0061.52 0 ATOM 1 N METB 500 23.448 -77.476 -9.592 1.00 61.28 N ATOM 2 CA METB 500 23.592-78.669 -8.778 1.00 61.23 C ATOM 3 CB METB 500 24.169 -78.304 -7.416 1.00 61.21 C ATOM 4 CO MET B 500 25.572 -77.74 1 -7.473 1.00 61.10 C ATOM 5 SD MET B 500 26.097 -77.079 -5.879 1.00 61.13 S ATOM 6 CE METB 500 27.861 -76.890 -6.152 1.00 61.68 C ATOM 7 C METB500 22.237-79.338 -8.606 1.0061.33 C ATOM 8 0 METB 500 21.221 -78.816 -9.063 1.00 61.29 0 ATOM 1 N LEU B 501 22.227 -80.500 -7.956 1.00 61.45 N ATOM 2 CA LEU B 501 20.977 -81.158 -7.585 1.00 61.49 C : ATOM 3 CB LEU B 501 20.759 -82.432 -8.408 1.00 61.41 C 4,. ATOM 4 CO LEUB 501 20.599-82.291.9.924 1.00 61.24 C ATOM 5 CD1LEUB5OI 20.682-83.646-10.611 1.0060.96 C ATOM 6 CD2LEUB5O1 19.292-81.603-10.266 1.0061.45 C ATOM 7 C LEUB5OI 20.980-81.494 -6.095 1.0061.59 C ATOM 8 0 LEUB5OI 21.852-82.220 -5.619 1.0061.52 0 ATOM I N ASPB5O2 20.015-80.952 -5.358 1.0061.72 N * S ATOM 2 CA ASP B 502 19.853 -8 1.329 -3.964 1.00 61.94 C ATOM 3 CB ASP B 502 19.236 -80.192 -3.144 1.00 62.06 C : .. 50 ATOM 4 CO ASP B 502 17.815 -79.857 -3.568 1.00 62.72 C ATOM 5 OD1 ASP B 502 17.039 -80.784 -3.890 1.00 63.46 0 ". : ATOM 6 OD2ASPB5O2 17.466-78.655 -3.557 1.0063.58 0 * ATOM 7 C ASP B 502 19.005 -82.590 -3.902 1.00 61.99 C ATOM 8 0 ASPB5O2 18.595-83.111.4.937 1.0062.07 0 ATOM 1 N ASP B 503 18.742 -83.079 -2.695 1.00 62.08 N ATOM 2 CA ASP B 503 18.016 -84.337 -2.521 1.00 62.21 C ATOM 3 CB ASP B 503 17.778 -84.611 -1.039 1.0062 34 C ATOM 4 CG ASPB5O3 17014-83.495 -0.358 1.0062.98 C ATOM 5 ODI ASPB5O3 17.226-82.315 -0.718 1.00 63.16 0 ATOM 6 0D2 ASP B 503 16.203 -83.803 0.542 1.00 64.06 0 ATOM 7 C ASP B 503 16.693 -84.407 -3.290 1.00 62.12 C ATOM 8 0 ASP B 503 16.455 -85.360 -4.040 1.00 62.04 0 ATOM I N GLU B 504 15.837 -83.405 -3.104 1.00 62.02 N ATOM 2 CA GLU B 504 14.53 1 -83 400 -3.757 1.00 6212 C ATOM 3 CB GLU B 504 13.687 -82.201 -3.309 1.00 62.02 C ATOM 4 CG GLU B 504 13.660 -81.992 -1.794 1.00 62.68 C ATOM 5 CD GLUB5O4 12.496-81.120 -1.327 1.0062.81 C ATOM 6 OE1 GLU B 504 12.703 -79.905 -1.092 1.00 63.40 0 ATOM 7 0E2 GLU B 504 11.370 -81.652 -1.189 1.00 63.95 0 ATOM 8 C GLUB 504 14.707-83.410 -5.269 1.0061.85 C ATOM 9 0 GLU B 504 14.2 14 -84.308 -5. 956 1.00 61.84 0 ATOM 1 N GLUB 505 15.431 -82.420 -5.781 1.00 61.64 N ATOM 2 CA GLUB5O5 15.704-82.340 -7.206 1.0061.43 C ATOM 3 CB GLU B 505 16.701 -81.228 -7.493 1.00 61.18 C ATOM 4 CG GLU B 505 16.088 -79.85 1 -7.502 1.00 60.83 C ATOM 5 CD GLU B 505 17.131 -78.753 -7.597 1.00 60.55 C ATOM 6 OEI GLU B 505 18.127 -78.807 -6.840 1.00 60.25 0 ATOM 7 OE2GLUB5O5 16.957-77.832 -8.427 1.0060.26 0 ATOM 8 C GLU B 505 16.235 -83.667 -7.734 1.00 61.67 C ATOM 9 0 GLUB 505 15.857-84.106 -8.827 1.00 61.83 0 ATOM 1 N PHEB5O6 17.104-84.309 -6.956 1.0061.68 N ATOM 2 CA PHE B 506 17.680 -85.586 -7.362 1.00 61.63 C ATOM 3 CB PHE B 506 18.794 -86.020 -6.409 1. 00 61.56 C ATOM 4 CG PHE B 506 19.485 -87.290 -6.827 1.00 61.67 C ATOM 5 CD1 PHE B 506 18.970 -88.528 -6.469 1.00 61.62 C ATOM 6 CE1 PilE B 506 19.598 -89.695 -6.859 1.00 61.32 C ATOM 7 CZ PHE B 506 20.757 -89.633 -7.610 1. 00 61.44 C ATOM 8 CE2PHEB 506 21.281 -88.409 -7.971 1.00 61.14 C ATOM 9 CD2 PHE B 506 20.647 -87.247 -7.584 1.00 61.51 C ATOM 10 C PHE B 506 16.602 -86.658 -7.440 1.00 61.66 C ATOM 11 0 PHE B 506 16.548 -87.430 -8.401 1. 00 61.70 0 ATOM 1 N ALAB 507 15.745 -86.705 -6.425 1.00 61.76 N ATOM 2 CA ALA B 507 14.624 -87.636 -6.436 1.00 61.66 C ATOM 3 CB ALAB5O7 13.794-87.488 -5.177 1.0061.65 C ATOM 4 C ALA B 507 13.768 -87.405 -7.679 1.00 61.68 C ATOM 5 0 ALA B 507 13.344 -88.361 -8.332 1.00 61.70 0 ATOM 1 N LEUB5O8 13.531-86.133 -8.005 1.0061.60 N ATOM 2 CA LEU B 508 12.805 -85.767 -9. 222 1.00 61.54 C ATOM 3 CB LEU B 508 12.722 -84.247 -9.353 1.00 61.44 C ATOM 4 CG LEU B 508 11.482 -83.623 -9.997 1.00 61.08 C ATOM 5 CD! LEUB 508 11.788-82.195-10.402 1.0060.85 C ATOM 6 CD2 LEU B 508 10.995 -84.417 -11.192 1.00 60.65 C ATOM 7 C LEU B 508 13.509 -86.346 -10.450 1.00 61.70 C ATOM 8 0 LEUB 508 12.905-87.063-11.262 1.0061.61 0 ATOM I N ALAB 509 14.792-86.026-10.582 1.00 61.77 N ATOM 2 CA ALAB 509 15.593-86.572-11.662 1.00 61.78 C ATOM 3 CB ALAB5O9 17.060-86.243-11.449 1.0061.77 C ATOM 4 C ALA B 509 15.378 -88.082 -11.768 1.00 61.87 C ATOM 5 0 ALAB5O9 14.950-88.585-12.810 1.0061.97 0 . : ATOM I N SERB5IO 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 SER B 510 15.749 -90.793 -9.249 1.00 62.00 C ATOM 4 OG SERB 510 16.993 -90.333 -8.748 1.00 62.65 0 ATOM 5 C SERB 510 14.110-90.673-11.135 1.00 61.79 C ATOM 6 0 SERB 510 13.978-91.562-11.987 1.00 61.78 0 ATOM I N HIS B 511 13.084 -90.030 -10.579 1.00 61.62 N ATOM 2 CA HIS B 511 11.707-90.302 -10.970 1.0061.40 C ATOM 3 CB HIS B 511 10.742 -89.312 -10.307 1.00 61.24 C ATOM 4 CC HIS B 511 9.317 -89.470 -10.744 1.00 60.84 C ATOM 5 ND! HISB5II 8.390-90.185-10.016 1.0060.78 N ATOM 6 CE1 HIS B 511 7.225 -90 155 -10.639 1.0060.24 C ATOM 7 NE2 HIS B 511 7.363 -89.449.11.747 1.00 60.07 N ATOM 8 CD2 HIS B 511 8.662 -89.009 -11.836 1.00 60.36 C ATOM 9 C I-HSB 511 11.594-90.212-12.479 1.0061.38 C ATOM 10 0 HISB 511 11.092-91.124-13.132 1.00 61.56 0 ATOM 1 N LEUB 512 12.083-89.109-13.031 1.00 61.36 N ATOM 2 CA LEUB5I2 12.001-88.881-14.464 1.0061.37 C ATOM 3 CB LEU B 512 12.489 -87.469 -14.786 1.00 61.22 C ATOM 4 CC LEU B 512 11.466 -86.435 -14.3 10 1.00 60.86 C ATOM 5 CD1LEUB5I2 12.018-85.018-14.367 10060.51 C ATOM 6 CD2 LEU B 512 10.185 -86.565 -15.123 1.00 59.84 C ATOM 7 C LEUB 512 12.751 -89.938-15.278 1.00 61.48 C ATOM 8 0 LEU B 512 12.264-90.422-16.309 1.00 61.48 0 ATOM I N ILE B 513 13.929 -90,309 -14.793 1.00 61.74 N ATOM 2 CA ILEB5I3 14.709-91.371-15.415 1.0061.83 C ATOM 3 CB ILEB 513 16.079-91.518-14.728 1.00 61.81 C ATOM 4 CC! ILEB 513 16.825-90.181-14. 799 1.0061.73 C ATOM 5 CD! ILEB 513 18.282-90.257-14.427 1.0062.12 C ATOM 6 CG2 ILE B 513 16.882 -92.645 -15.365 1.00 61.68 C ATOM 7 C ILEB 513 13.946-92.705 -15.439 1.00 61.89 C ATOM 8 0 ILEB 513 13.817-93.333-16.492 1.0061.85 0 ATOM 1 N GLU B 514 13.429 -93.124 -14.285 1.00 61.92 N ATOM 2 CA GLUB5I4 12.589-94.317-14.223 1.0062.03 C ATOM 3 CB GLUB514 12.044-94.519-12.814 1.0062.08 C ATOM 4 CG GLUB 514 13.104-94.778-11.765 1.00 62.83 C ATOM 5 CD GLUB 514 12.556-95.511 -10.550 1.00 63.54 C ATOM 6 OEL GLUB 514 11.502-96.181 -10.667 1.00 63.39 0 ATOM 7 0E2 GLU B 514 13.190 -95.420 -9.476 1.00 64.11 0 ATOM 8 C CLUB 514 11.423-94.201-15.194 1.0062.07 C ATOM 9 0 GLUB 514 11.155-95.108-15.989 1.0062.33 0 ATOM I N ALAB5I5 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 ALA B 515 10.023 -93.091 -17.457 1.00 61.91 C ATOM 5 0 ALAB 515 9.366-93.878-18.137 1.00 61.89 0 ATOM 1 N LYSB516 11.111-92.472-17.911 1.0061.87 N ATOM 2 CA LYS B 516 11.554 -92.658 -19.291 1.00 61.79 C : ,,. ATOM 3 CB LYSB 516 12.747-91.760-19.625 1.00 61.68 C ATOM 4 CC LYS B 516 12.626 -91.054 -20.968 1.00 61.28 C ATOM 5 CD LYSB516 12.641-92.024-22.133 1.0061.20 C ATOM 6 CE LYS B 516 11.698 -91.567 -23.236 1.00 61.34 C **** ATOM 7 NZ LYSB 516 11.813-90.108-23.506 1.0061.19 N ATOM 8 C LYSB 516 11.902-94.113-19.547 1.00 61.88 C ATOM 9 0 LYS B 516 11.602 -94.645 -20.614 1.00 62.04 0 * ATOM I N LEUB517 12.525-94.761.18.568 1.00 61.97 N ATOM 2 CA LEUB5I7 12.857-96.176.18.705 1.0062.25 C : .. ATOM 3 CB LEUB 517 13.632-96690-17.487 1.00 62.24 C S... ATOM 4 CC LEUB5I7 15.064-96.164.17.332 1.0062.30 C **. : ATOM 5 CD1LEUB517 15.725-96.729-16.083 1.0062.24 C * ATOM 6 CD2 LEU B 517 15.895 -96.473 -18.570 1.00 62.23 C ATOM 7 C LEUB 517 11.607-97.019-18.948 1.00 62.46 C ATOM 8 0 LEUB517 11.629-97.939-19.760 1.0062.42 0 ATOM I N GLU B 518 10.517 -96.698 -18.255 1.00 62.79 N ATOM 2 CA GLU B 518 9.248 -97.404 -18.465 1.00 63.31 C ATOM 3 CB GLU B 518 8.186 -96.944 -17.462 1.00 63.45 C ATOM 4 cci GLUB518 7.762-98.010-16.464 1.0063.87 C ATOM 5 CD GLUB 518 8.718-98.127-15.302 1.0064.37 C ATOM 6 OE1 GLU B 518 9.452 -99.135 -15. 238 1.006442 0 ATOM 7 OE2 GLU B 518 8.741 -97.205 -14.457 1.00 64.82 0 ATOM 8 C GLU B 518 8 701 -97.252 -19.882 1.00 63.54 C ATOM 9 0 GLU B 518 7.929 -98.091 -20.351 1.00 63.50 0 ATOM I N GLY B 519 9.094 -96.175 -20,554 1. 00 63.92 N ATOM 2 CA GLY B 519 8.584 -95.872 -21.888 1.0064.42 C ATOM 3 C GLY B 519 7.591 -94.725 -21.875 1.00 64.74 C ATOM 4 0 GLY B 519 6.488 -94.834 -22.4 15 1.0064.74 0 ATOM 1 N HISB52O 7.987-93.620-21.250 1.0065.16 N ATOM 2 CA HIS B 520 7.139 -92.438 -21.167 1.00 65.57 C ATOM 3 CB HIS B 520 6.765 -92.143 -19.7 14 1.00 65.67 C ATOM 4 CG HISB 520 5.660-93003-19.192 1.00 66.10 C ATOM 5 ND1 HISB52O 4.337-92.796-19.526 1.00 66.58 N ATOM 6 CEI HIS B 520 3.589 -93.707 -18.928 1.00 66.72 C ATOM 7 NE2 HIS B 520 4.379 -94.495 -18.2 17 1.00 66.89 N ATOM 8 CD2 HIS B 520 5.680 -94.077 -18.366 1.00 66.36 C ATOM 9 C HIS B 520 7.822 -91.219 -21.757 1.00 65.70 C ATOM 10 0 HIS B 520 8.924 -90.855 -21.345 1.00 65.77 0 ATOM I N GLY B 521 7.165 -90.583 -22.720 1.00 65.86 N ATOM 2 CA GLY B 521 7.633 -89.296 -23.205 1.00 66.01 C ATOM 3 C GLY B 521 7.785 -88.376 -22.0 10 1.00 66.07 C ATOM 4 0 GLYB52I 6.976-88.416-21.081 1.0066.13 0 ATOM I N LEU B 522 8.837 -87.569 -22.009 1.00 66.10 N ATOM 2 CA LEU B 522 9.017 -86.582 -20.954 1.00 66.04 C ATOM 3 CB LEU B 522 10.48 1 -86.174 -20.840 1.00 66.08 C ATOM 4 CG LEUB 522 11.321 -86.795-19.726 1.00 66.47 C ATOM 5 CD1 LEU B 522 10.858 -88.202 -19.364 1.00 66.89 C ATOM 6 CD2 LEU B 522 12.776 -86.798 -20.163 1.00 66.94 C ATOM 7 C LEUB 522 8.178-85.351-21.244 1.0065.97 C ATOM 8 0 LEU B 522 7.966 -84.999 -22.405 1.00 65.87 0 ATOM I N PRO B 523 7.692 -84.690 -20.184 1.00 65.92 N ATOM 2 CA PRO B 523 7.027 -83.409 -20.367 1.00 65.84 C ATOM 3 CB PRO B 523 6.65 1 -82.993 -18.940 1.00 65.78 C ATOM 4 CG PRO B 523 6.708 -84.24 1 -18.133 1.00 65.95 C ATOM 5 CD PRO B 523 7.749 -85.097 -18.770 1.00 65.96 C ATOM 6 C PRO B 523 8. 024 -82.4 14 -20.944 1.00 65.77 C ATOM 7 0 PRO B 523 9.228 -82.685 -20.982 1.00 65.97 0 ATOM I N THR B 524 7.535 -8 1.272 -21.399 1.00 65.48 N ATOM 2 CA THR B 524 8.435 -80.238 -21.863 1.00 65.17 C ATOM 3 CB THRB 524 8.019-79.717-23.260 1.00 65.20 C S. ATOM 4 OG1 THRB 524 8.323 -78.323 -23.369 1.00 65.65 0 ATOM 5 CG2 THR B 524 6.526 -79.937 -23.494 1.00 65. 23 C ATOM 6 C THRB524 8.548-79.137-20.799 1.0064.84 C ATOM 7 0 THR B 524 9.526 -78.392 -20.76 1 1.00 64.93 0 ATOM 1 N ASNB525 7.554-79.070-19.917 1.0064.41 N ATOM 2 CA ASN B 525 7.559 -78.137 -18.788 1.00 63.87 C ATOM 3 CB ASN B 525 6.682 -76.920 -19.078 1.00 63.88 C ATOM 4 CO ASNB 525 7.333 -75.948 -20.029 1.00 63.78 C . : ATOM 5 OD1 ASN B 525 6.763 -75.603 -21.063 1.00 63.84 0 ATOM 6 ND2ASNB 525 8.539-75.502-19.689 1.0063.55 N ATOM 7 C ASNB525 7.078-78.805-17.509 1.0063.51 C ATOM 8 0 ASN B 525 5.970 -79.340 -17.455 1.00 63.55 0 ATOM 1 N LEU B 526 7.917 -78.761 -16.482 1. 00 62.99 N ATOM 2 CA LEU B 526 7.618 -79.378 -15.202 1.00 62.43 C ATOM 3 CB LEU B 526 8.806 -79.165 -14.268 1.00 62.46 C ATOM 4 CO LEUB 526 9.131 -80.239-13.233 1.00 62.26 C ATOM 5 CD1 LEU B 526 8.105 -80.225 -12.130 1.00 62.66 C ATOM 6 CD2 LEU B 526 9.197 -81.602 -13.887 1.00 62.13 C ATOM 7 C LEU B 526 6.354 -78.766 -14.597 1.00 62.24 C ATOM 8 0 LEU B 526 6.355 -77.599 -14.209 1.00 62.21 0 ATOM I N PR0B527 5.266-79.554-14.512 1.0061.99 N ATOM 2 CA PRO B 527 4.014 -79.062 -13.941 1.00 61.70 C ATOM 3 CB PR0B527 2.997-80.112-14.388 1.0061.70 C ATOM 4 CC PROB 527 3.778-81.364-14.488 1.0061.61 C ATOM 5 CD PRO B 527 5.160 -80.961 -14.942 1.00 61.99 C ATOM 6 C PRO B 527 4.083 -79.005 -12.417 1.00 61.51 C ATOM 7 0 PROB 527 4.849-79.751 -11.804 1.00 61.49 0 ATOM I N ARC B 528 3.279 -78 133-11.814 1.00 61.27 N ATOM 2 CA ARG B 528 3.346 -77.888 -10.373 1.00 61.10 C ATOM 3 CB ARG B 528 2.166 -77.024 -9.915 1.00 61.10 C ATOM 4 CG ARG B 528 2.137 -76.776 -8.411 1.00 61.06 C ATOM 5 CD ARC B 528 0.879 -76.043 -7.980 1.00 61.02 C ATOM 6 NE ARC B 528 0.850 -75.823 -6.536 1.00 60.86 N ATOM 7 CZ ARG B 528 1.2 18 -74.691 -5.938 1.00 60.65 C ATOM 8 NH! ARG B 528 1.157 -74.592 -4.616 1.00 60.39 N ATOM 9 NH2 ARG B 528 1.645 -73.658 -6.656 1.00 60.55 N ATOM 10 C ARC B 528 3.409 -79.163 -9.528 1.00 61.02 C ATOM 11 0 ARC B 528 4.218 -79.270 -8.606 1.00 60.96 0 ATOM 1 N ARGB529 2.552-80.125 -9.851 1.0060.92 N ATOM 2 CA ARC B 529 2.403 -81.325 -9.035 1.00 60.87 C ATOM 3 CB ARC B 529 1.251 -82.189 -9.555 1.00 61.05 C ATOM 4 CG ARGB 529 1.382-82.565-11.016 1.0061.92 C ATOM 5 CD ARGB 529 0.162-83.315-11.516 1.0063.40 C ATOM 6 NE ARC B 529 0.370 -83.798 -12.877 1.00 64.56 N ATOM 7 CZ ARGB 529 1047-84.901 -13.18! 1.00 65.44 C ATOM 8 NH! ARC B 529 1.189 -85.259 -14.45 1 1.00 65.89 N ATOM 9 NH2ARGB 529 1.584-85.646-12.218 1.0065.76 N ATOM 10 C ARC B 529 3.683 -82.142 -8.958 1.00 60.59 C ATOM II 0 ARC B 529 3.835 -82.979 -8.066 1.00 60.74 0 ATOM I N LEUB53O 4.599-81.907 -9.892 1.0060.16 N ATOM 2 CA LEU B 530 5.877 -82.605 -9.880 1.00 59.71 C ATOM 3 CB LEU B 530 6.291 -83.023 -11.292 1. 00 59.65 C ATOM 4 CC LEU B 530 5.799 -84.382 -11.791 1.00 59.14 C ATOM 5 CDI LEU B 530 6.397 -84.693 -13.153 1.00 58.59 C ATOM 6 CD2 LEU B 530 6.155 -85.472 -10.801 1.00 58.67 C ATOM 7 C LEU B 530 6.980 -81.784 -9.219 1.00 59.56 C : *... ATOM 8 0 LEUB53O 8.032-82.318 -8.874 1.0059.51 0 e**. ATOM I N VALB 531 6.744 -80.488 -9.043 1.00 59.45 N S..... ATOM 2 CA VAL B 531 7.716 -79.637 -8.364 1.00 59.44 C ATOM 3 CB VALB 531 7.333 -78.142 -8.445 1.00 59.28 C ATOM 4 CGI VALB 531 8.433-77.283 -7.859 1.00 58.89 C S..' ATOM 5 CG2VALB531 7.057-77.735 -9.877 1.0059.32 C ATOM 6 C VALB 531 7.815-80.033 -6.894 1.00 59.61 C * ATOM 7 0 VAL B 531 6.800 -80.081 -6. 198 1.00 59.64 0 ATOM I N PRO B 532 9.036 -80.329 -6.4 16 1.00 59.71 N : .. ATOM 2 CA PRO B 532 9.2 18 -80.580 -4.992 1.00 59.85 C ATOM 3 CB PRO B 532 10.724 -80.410 -4.804 1.00 59.82 C * * * ATOM 4 CC PROB 532 11.307-80.816 -6.117 1.00 59.65 C * S. ATOM 5 CD PROB532 10.297-80.447 -7.170 1.0059.60 C ATOM 6 C PR0B532 8.456-79.537 -4.176 1.0060.13 C ATOM 7 0 PRO B 532 8.415 -78.370 -4.561 1.00 60.15 0 ATOM I N PRO B 533 7.852 -79.960 -3.054 1.00 60.38 N ATOM 2 CA PRO B 533 6.965 -79.145 -2.224 1.00 60.52 C ATOM 3 CB PRO B 533 6.84 1 -79.97 1 -0.945 1.00 60.55 C ATOM 4 CG PRO B 533 6. 957 -8 1.366 -1.425 1.00 60.51 C ATOM 5 CD PRO B 533 8.002 -81.32 1 -2.510 1.00 60.41 C ATOM 6 C PRO B 533 7.469 -77.729 -1.918 1.00 60.72 C ATOM 7 0 PRO B 533 6.658 -76.825 -1.727 1.00 60.82 0 ATOM I N SERB 534 8.783 -77.532 -1.861 1.0061.01 N ATOM 2 CA SERB 534 9.324-76.176 -1.855 1.00 61.33 C ATOM 3 CB SERB 534 10.781 -76.179 -1.414 1.00 61.27 C ATOM 4 OG SERB 534 10.965 -77.089 -0.342 1.00 61.06 0 ATOM 5 C SER B 534 9.180 -75.634 -3.277 1.00 61.73 C ATOM 6 0 SERB534 10.158-75.532 -4.034 1.0061.49 0 ATOM I N LYS B 535 7.939 -75.302 -3.635 1.00 62.26 N ATOM 2 CA LYS B 535 7.591 -75.061 -5.034 1.00 62.66 C ATOM 3 CB LYSB 535 6.481 -76.020 -5.521 1.00 62.74 C ATOM 4 CG LYSB 535 5.237-76.121 -4.644 1.00 62.63 C ATOM 5 CD LYS B 535 4.224 -77.127 -5.215 1.00 62.53 C ATOM 6 CE LYS B 535 4.611 -78.574 -4.909 1.00 62.10 C ATOM 7 NZ LYS B 535 3.545 -79.555 -5.27 1 1.00 61.50 N ATOM 8 C LYS B 535 7.279 -73.624 -5.4 16 1. 00 62.89 C ATOM 9 0 LYS B 535 8.077 -73.007 -6.120 1.00 63.20 0 ATOM 1 N ARG B 536 6.144 -73.086 -4.968 1.00 62.87 N ATOM 2 CA ARG B 536 5.680 -71.790 -5.472 1.00 62.96 C ATOM 3 CB ARG B 536 5.145 -71.935 -6.902 1.00 63.00 C ATOM 4 CG ARG B 536 5.911 -71.160 -7.963 1.00 62.88 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 1.00 62.80 N ATOM 7 CZ ARGB 536 5.838-67.741 -9.505 1.00 62.71 C ATOM 8 NHI ARG B 536 6.415 -67.202 -10.571 1.00 62.64 N ATOM 9 NH2 ARG B 536 5.115 -66.977 -8.697 1.00 62.73 N ATOM 10 C ARG B 536 4.593 -71.172 -4. 622 1.00 63.09 C ATOM 11 0 ARGB536 3.436-71.595 -4.688 1.00 63.09 0 ATOM I N ARG B 537 4.964 -70.154 -3.843 1.00 63.37 N ATOM 2 CA ARG B 537 3.993 -69.382 -3.075 1.00 63.60 C ATOM 3 CB ARG B 537 4.697 -68.242 -2.327 1.00 63.66 C ATOM 4 CG ARGB537 4.130-67.921 -0.934 1.0064.02 C ATOM 5 CD ARG B 537 2.685 -67.398 -0.982 1.00 64.23 C ATOM 6 NE ARG B 537 2.224 -66.952 0.333 1.00 64.87 N ATOM 7 CZ ARGB 537 1.914-65.692 0.633 1.00 65.30 C ATOM 8 N}11 ARU B 537 2.007 -64.746 -0.292 1.00 65.61 N ATOM 9 NH2 ARG B 537 1.502 -65.373 1.856 1.00 64.97 N :. ATOM 10 C ARG B 537 2.970 -68.8 16 -4.063 1.00 63.69 C * ATOM 11 0 ARGB537 3.298-68.553 -5.226 1.0063.76 0 ATOM I N GLN B 538 1.734 -68.641 -3.608 1.00 63.75 N ATOM 2 CA GLN B 538 0.666 -68.177 -4.489 1.00 63.87 C ATOM 3 CB GLN B 538 0.043 -69.363 -5. 225 1.00 63.84 C ** ATOM 4 CG GLN B 538 -0.406 -70.488 -4.301 1.00 63.92 C ATOM S CD GLN B 538 -0.796 -71.738 -5.066 1.0064.01 C ATOM 6 OE1GLNB 538 -0.803-71.751 -6.299 1.0064.15 0 ATOM 7 NE2 GLN B 538 -1.122 -72.802 -4.338 1.00 64.37 N * *. 50 ATOM 8 C GLNB538 -0409-67.416 -3.723 1.0063. 88 C ATOM 9 0 GLNB538 -1.543-67.243 -4.236 1.0063.92 0 * TER 9 GLNB538 HETATM 1 02A ANP B 600 3.973 -56.574 -52.078 1.0048.61 0 HETATM 2 PA ANP B 600 4. 052 -57 106 -50.670 1.00 48.08 P HETATM 3 O1A ANP B 600 2.9 10 -57.937 -50.141 1.00 48.41 0 HETATM 4 03A ANP B 600 4.279 -55.854 -49.694 1.00 49.01 0 HETATM 5 PB ANP B 600 3.622 -54.443 -50.096 1.00 49.55 P HETATM 6 O1B ANP B 600 3.428 -53.654 -48.825 1.00 49.44 0 HETATM 7 02B AN? B 600 2.4 12 -54.72 1 -50.957 1.00 49.32 0 HETATM 8 N3BANPB600 4.812-53.641 -51.080 1.0049.69 N HETATM 9 PG ANP B 600 4.339 -52.172 -5 1.877 1.0050. 29 P HETATM 10 03G ANP B 600 4.467 -51.114 -50.807 1.00 50.68 0 HETATM 11 02G ANP B 600 5.350 -52.031 -52 990 1.00 50.99 0 HETATM 12 OIGANPB600 2.921 -52.435-52.332 1.0049 88 0 HETATM 13 O5ANPB600 5.406-57.950-50.510 1.0048.33 0 HETATM 14 C5*ANPB600 6.435-57.592-49.597 1.0049.10 C HETATM 15 C4* ANP B 600 7.544 -58.626 -49.749 1.00 50.21 C HETATM 16 C3* ANP B 600 7.191 -59.661 -50.803 1.00 50.31 C HETATM 17 03* AN? B 600 8.395 -60.157 -51.392 1.00 50.26 0 HETATM 18 C2* ANP B 600 6.537 -60.782 -50.030 1.00 50.21 C HETATM 19 02 ANP B 600 6.795 -62.044 -50.644 1.00 50.10 0 HETATM 20 C1 AN? B 600 7.209 -60.692 -48.675 1.00 50.66 C HETATM 21 04*ANPB600 7.693-59.354-48.530 1.0050.80 0 HETATM 22 N9 ANP B 600 6.247 -60.938 -47.587 1.00 50.73 N HETATM 23 C4 AN? B 600 6.554 -61.536 -46.440 1.00 50.52 C HETATM 24 CS ANP B 600 5.320 -61.565 -45.655 1.00 50.67 C HETATM 25 N7 ANP B 600 4.370 -60.971 -46.403 1.00 51.15 N HETATM 26 CS ANP B 600 4.948 -60.592 -47.574 1.00 50.79 C HETATM 27 N3 ANP B 600 7.677 -62.07 1 -45.92 1 1.00 50.46 N HETATM 28 C2 AN? B 600 7.672 -62.625 -44.699 1.00 50.75 C HETATM 29 Ni AN? B 600 6.580 -62.692 -43.920 1.00 50.79 N HETATM 30 C6 AN? B 600 5.392 -62.188 -44.319 1.00 50.80 C HETATM 31 N6 AN? B 600 4.295 -62.253 -43.527 1.00 50.98 N HETATM 1 MG MG B 700 1.653 -53.618 -53.006 1.00 49.55 MG HETATM 1 CA CA B 701 19.587 -77.142 -8.004 1.00 46.71 CA U.

I S *SS *... *

S

I..... * S *.

S *.*.

S * S S.

References 1. Praefcke, G. J. & McMahon, H. T. The dynamin superfamily: universal membrane tubulation and fission molecules? Nat. Rev. Mo!. Cell Biol. 5, 133-147 (2004).

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3. Grant, B. et al. Evidence that RME-1, a conserved C. elegaris EH-domain protein, functions in endocytic recycling. Nat. Cell Biol. 3, 573-579 (2001).

4. Caplan, S. et al. A tubular EHDI-containing compartment involved in the recycling of major histocompatibility complex class 1 molecules to the plasma membrane. EMBO.J 21, 2557-2567 (2002).

5. Sweitzer, S. M. & Hinshaw, J. E. Dynamin undergoes a GTP-dependent conformational change causing vesiculation. Cell 93, 1021-1029 (1998).

6. Sever, S., Muhlberg, A. B. & Schmid, S. L. Impairment of dynamin's GAP domain stimulates receptor-mediated endocytosis. Nature 398, 481-486 (1999).

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9. Lin, S. X., Grant, B., Hirsh, D. & Maxfield, F. R. Rrne-1 regulates the distribution and function of the endocytic recycling compartment in mammalian cells. Nat. Cell Biol. 3, 567-572 (2001).

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12. Jovic, M., Naslavsky, N., R.apaport, D., Horowitz, M. & Caplan, S. EHD1 regulates beta 1 integrin endosomal transport: effects on focal adhesions, cell spreading and migration. J. Cell Sci. 120, 802-8 14 (2007).

13. Blume, J. J., Halbach, A., Behrendt, D., Paulsson, M. & Plomann, M. El-ID proteins are associated with tubular and vesicular compartments and interact with specific phospholipids. Exp. Cell Res. 313, 219-231 (2007).

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16. Stowell, M. H., Marks, B., Wigge, P. & McMahon, H. T. Nucleotide-dependent conformational changes in dynamin: evidence for a mechanochemical molecular spring. Nat. Cell Biol. 1,27-32(1999).

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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. * * * *** **.. * * S... * . S... *.. * * * I. * . S S... S. S * S S * S.

Claims (46)

1. A method of identifying a modulator of an El-ID 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 El-ID family polypeptide.

2. A method according to claim I 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 I 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 EF[D 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 EFID 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 AlP hydrolysis.

8. A method according to any preceding claim further comprising the step of providing a further sample of El-ID family polypeptide, said further sample comprising an EHD family polypeptide bearing an Ii 57Q 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 nucleotidc 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 El-ID 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 * .. 30 bind to or to affect the structure of said EHD family polypeptide, wherein an expectation of binding or affecting the structure of said El-ID 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 identifying a candidate therapeutic agent, said method 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. S.. * * ****

20. Use of a candidate modulator of EHD family polypeptide activity identified * according to any of claims 12 to 18, wherein said END family polypeptide is EJ{D2, in the manufacture of a medicament for diabetes.

* ** 30

21. Use of the atomic coordinates as shown in Table A in the modelling of an El-ED 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 tubulation 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 membrarie-EHD family polypeptide complex with nucleotide in :: :::: 25 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 EI-[D family polypeptide to permit guanine nucleotide binding thereto, said method comprising mutating said EFID polypeptide at one or more amino acid residues within the region H192 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 EFID 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 1157 of said polypeptide. ***. S. *

* . 30

39. A method according to claim 37 or claim 38, wherein said 1157 is mutated toQ.

I

40. A method of inducing membrane fission, said method comprising contacting said membrane with an El-ID family polypeptide comprising an 1157Q mutation.

41. A method of modifying an EI-[D family polypeptide to reduce or abolish assembly stimulated ATP hydrolysis, said method comprising mutating said EHD polypeptide at E91, R167, K193, D198, F122, 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) 1157Q; and (iii) F322A.

44. 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.

:.

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 EI-1D2. * S. * . . *.SS S. S S 30