CNRS Nantes University UFIP UFIP
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***  TRANSCRIPTION 19-SEP-02 1IZ3  ***

elNémo ID: 210514094648106491

Job options:

ID        	=	 210514094648106491
JOBID     	=	 TRANSCRIPTION 19-SEP-02 1IZ3
USERID    	=	 unknown
PRIVAT    	=	 0

NMODES    	=	 5
DQMIN     	=	 -100
DQMAX     	=	 100
DQSTEP    	=	 20
DOGRAPHS  	=	 on

DOPROJMODS	=	 on
DORMSD    	=	 on

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


HEADER    TRANSCRIPTION                           19-SEP-02   1IZ3              
TITLE     DIMERIC STRUCTURE OF FIH (FACTOR INHIBITING HIF)                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: FIH;                                                       
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: FACTOR INHIBITING HIF1;                                     
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    DOUBLE BETA-SHEET HELIX, TRANSCRIPTION                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.LEE,S.-J.KIM,D.-G.JEONG,S.M.LEE,S.-E.RYU                            
REVDAT   3   13-JUL-11 1IZ3    1       VERSN                                    
REVDAT   2   24-FEB-09 1IZ3    1       VERSN                                    
REVDAT   1   10-JUN-03 1IZ3    0                                                
JRNL        AUTH   C.LEE,S.J.KIM,D.G.JEONG,S.M.LEE,S.E.RYU                      
JRNL        TITL   STRUCTURE OF HUMAN FIH-1 REVEALS A UNIQUE ACTIVE SITE POCKET 
JRNL        TITL 2 AND INTERACTION SITES FOR HIF-1 AND VON HIPPEL-LINDAU.       
JRNL        REF    J.BIOL.CHEM.                  V. 278  7558 2003              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   12482756                                                     
JRNL        DOI    10.1074/JBC.M210385200                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 0.9                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 95.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 24716                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.230                           
REMARK   3   FREE R VALUE                     : 0.277                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 1169                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 50.00                        
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2773                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 5                                       
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.009                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.47                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 24.20                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1IZ3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-SEP-02.                  
REMARK 100 THE RCSB ID CODE IS RCSB005427.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 09-JUL-02                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PAL/PLS                            
REMARK 200  BEAMLINE                       : 6B                                 
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979                              
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MACSCIENCE                         
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 24716                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 99.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.7                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 50.00                    
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SHARP                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 64.38                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.48                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.4M LITHIUM SULFATE, 20% PEG 4000, PH   
REMARK 280  8.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       71.71000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       43.44500            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       43.44500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       35.85500            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       43.44500            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       43.44500            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      107.56500            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       43.44500            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       43.44500            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       35.85500            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       43.44500            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       43.44500            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      107.56500            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       71.71000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: THE SECOND PART OF THE BIOLOGICAL ASSEMBLY IS GENERATED BY   
REMARK 300 THE TWO FOLD AXIS : -X, Y, -Z                                        
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 3450 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 31630 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -51.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      143.42000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     ALA A     3                                                      
REMARK 465     THR A     4                                                      
REMARK 465     ALA A     5                                                      
REMARK 465     ALA A     6                                                      
REMARK 465     GLU A     7                                                      
REMARK 465     ALA A     8                                                      
REMARK 465     VAL A     9                                                      
REMARK 465     THR A    10                                                      
REMARK 465     SER A    11                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OE2  GLU A   202     NH2  ARG A   238              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   CD1  ILE A   344     CD1  ILE A   344     7556     2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ALA A  22       41.47     37.05                                   
REMARK 500    SER A  36       39.30    -89.43                                   
REMARK 500    LEU A  74       -6.82    -55.94                                   
REMARK 500    ASN A  87      -70.10    -45.91                                   
REMARK 500    LYS A 106      -10.18    -48.96                                   
REMARK 500    GLN A 112      -17.74    -42.14                                   
REMARK 500    GLU A 130      -76.05    -54.22                                   
REMARK 500    GLU A 141      -95.67    -91.21                                   
REMARK 500    TYR A 145      101.34   -160.44                                   
REMARK 500    LEU A 150       50.89    -97.80                                   
REMARK 500    THR A 153       97.41    -61.80                                   
REMARK 500    TRP A 179      175.05    -58.23                                   
REMARK 500    GLN A 181      145.58    -35.46                                   
REMARK 500    HIS A 199     -179.21   -171.53                                   
REMARK 500    ILE A 210      -67.28   -131.83                                   
REMARK 500    TYR A 228       73.99     48.70                                   
REMARK 500    ARG A 238       -1.70     85.56                                   
REMARK 500    ASN A 246       67.41   -171.36                                   
REMARK 500    ASP A 248       78.63   -110.78                                   
REMARK 500    TYR A 249       -8.78    -55.18                                   
REMARK 500    PRO A 267      -62.12    -17.42                                   
REMARK 500    TYR A 276      -19.93     72.74                                   
REMARK 500    ASN A 332       97.19    163.10                                   
REMARK 500    PRO A 333      -19.22    -48.13                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 501                 
DBREF  1IZ3 A    1   349  UNP    Q9NWT6   HIF1N_HUMAN      1    349             
SEQADV 1IZ3 ASP A   28  UNP  Q9NWT6    HIS    28 CONFLICT                       
SEQADV 1IZ3 MSE A  108  UNP  Q9NWT6    MET   108 MODIFIED RESIDUE               
SEQADV 1IZ3 MSE A  123  UNP  Q9NWT6    MET   123 MODIFIED RESIDUE               
SEQADV 1IZ3 MSE A  160  UNP  Q9NWT6    MET   160 MODIFIED RESIDUE               
SEQADV 1IZ3 MSE A  191  UNP  Q9NWT6    MET   191 MODIFIED RESIDUE               
SEQADV 1IZ3 MSE A  275  UNP  Q9NWT6    MET   275 MODIFIED RESIDUE               
SEQADV 1IZ3 MSE A  319  UNP  Q9NWT6    MET   319 MODIFIED RESIDUE               
SEQADV 1IZ3 MSE A  325  UNP  Q9NWT6    MET   325 MODIFIED RESIDUE               
SEQADV 1IZ3 MSE A  343  UNP  Q9NWT6    MET   343 MODIFIED RESIDUE               
SEQRES   1 A  349  MET ALA ALA THR ALA ALA GLU ALA VAL THR SER GLY SER          
SEQRES   2 A  349  GLY GLU PRO ARG GLU GLU ALA GLY ALA LEU GLY PRO ALA          
SEQRES   3 A  349  TRP ASP GLU SER GLN LEU ARG SER TYR SER PHE PRO THR          
SEQRES   4 A  349  ARG PRO ILE PRO ARG LEU SER GLN SER ASP PRO ARG ALA          
SEQRES   5 A  349  GLU GLU LEU ILE GLU ASN GLU GLU PRO VAL VAL LEU THR          
SEQRES   6 A  349  ASP THR ASN LEU VAL TYR PRO ALA LEU LYS TRP ASP LEU          
SEQRES   7 A  349  GLU TYR LEU GLN GLU ASN ILE GLY ASN GLY ASP PHE SER          
SEQRES   8 A  349  VAL TYR SER ALA SER THR HIS LYS PHE LEU TYR TYR ASP          
SEQRES   9 A  349  GLU LYS LYS MSE ALA ASN PHE GLN ASN PHE LYS PRO ARG          
SEQRES  10 A  349  SER ASN ARG GLU GLU MSE LYS PHE HIS GLU PHE VAL GLU          
SEQRES  11 A  349  LYS LEU GLN ASP ILE GLN GLN ARG GLY GLY GLU GLU ARG          
SEQRES  12 A  349  LEU TYR LEU GLN GLN THR LEU ASN ASP THR VAL GLY GLY          
SEQRES  13 A  349  LYS ILE VAL MSE ASP PHE LEU GLY PHE ASN TRP ASN TRP          
SEQRES  14 A  349  ILE ASN LYS GLN GLN GLY LYS ARG GLY TRP GLY GLN LEU          
SEQRES  15 A  349  THR SER ASN LEU LEU LEU ILE GLY MSE GLU GLY ASN VAL          
SEQRES  16 A  349  THR PRO ALA HIS TYR ASP GLU GLN GLN ASN PHE PHE ALA          
SEQRES  17 A  349  GLN ILE LYS GLY TYR LYS ARG CYS ILE LEU PHE PRO PRO          
SEQRES  18 A  349  ASP GLN PHE GLU CYS LEU TYR PRO TYR PRO VAL HIS HIS          
SEQRES  19 A  349  PRO CYS ASP ARG GLN SER GLN VAL ASP PHE ASP ASN PRO          
SEQRES  20 A  349  ASP TYR GLU ARG PHE PRO ASN PHE GLN ASN VAL VAL GLY          
SEQRES  21 A  349  TYR GLU THR VAL VAL GLY PRO GLY ASP VAL LEU TYR ILE          
SEQRES  22 A  349  PRO MSE TYR TRP TRP HIS HIS ILE GLU SER LEU LEU ASN          
SEQRES  23 A  349  GLY GLY ILE THR ILE THR VAL ASN PHE TRP TYR LYS GLY          
SEQRES  24 A  349  ALA PRO THR PRO LYS ARG ILE GLU TYR PRO LEU LYS ALA          
SEQRES  25 A  349  HIS GLN LYS VAL ALA ILE MSE ARG ASN ILE GLU LYS MSE          
SEQRES  26 A  349  LEU GLY GLU ALA LEU GLY ASN PRO GLN GLU VAL GLY PRO          
SEQRES  27 A  349  LEU LEU ASN THR MSE ILE LYS GLY ARG TYR ASN                  
MODRES 1IZ3 MSE A  108  MET  SELENOMETHIONINE                                   
MODRES 1IZ3 MSE A  123  MET  SELENOMETHIONINE                                   
MODRES 1IZ3 MSE A  160  MET  SELENOMETHIONINE                                   
MODRES 1IZ3 MSE A  191  MET  SELENOMETHIONINE                                   
MODRES 1IZ3 MSE A  275  MET  SELENOMETHIONINE                                   
MODRES 1IZ3 MSE A  319  MET  SELENOMETHIONINE                                   
MODRES 1IZ3 MSE A  325  MET  SELENOMETHIONINE                                   
MODRES 1IZ3 MSE A  343  MET  SELENOMETHIONINE                                   
HET    MSE  A 108       8                                                       
HET    MSE  A 123       8                                                       
HET    MSE  A 160       8                                                       
HET    MSE  A 191       8                                                       
HET    MSE  A 275       8                                                       
HET    MSE  A 319       8                                                       
HET    MSE  A 325       8                                                       
HET    MSE  A 343       8                                                       
HET    SO4  A 501       5                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM     SO4 SULFATE ION                                                      
FORMUL   1  MSE    8(C5 H11 N O2 SE)                                            
FORMUL   2  SO4    O4 S 2-                                                      
HELIX    1   1 ASP A   28  LEU A   32  5                                   5    
HELIX    2   2 ASP A   49  ASN A   58  1                                  10    
HELIX    3   3 VAL A   70  TRP A   76  5                                   7    
HELIX    4   4 ASP A   77  ILE A   85  1                                   9    
HELIX    5   5 ASP A  104  GLN A  112  5                                   9    
HELIX    6   6 PHE A  125  GLY A  139  1                                  15    
HELIX    7   7 GLY A  155  PHE A  165  1                                  11    
HELIX    8   8 ASN A  166  ARG A  177  1                                  12    
HELIX    9   9 PRO A  220  ASP A  222  5                                   3    
HELIX   10  10 GLN A  223  TYR A  228  1                                   6    
HELIX   11  11 PHE A  252  VAL A  258  5                                   7    
HELIX   12  12 LYS A  311  GLY A  331  1                                  21    
HELIX   13  13 ASN A  332  GLN A  334  5                                   3    
HELIX   14  14 GLU A  335  LYS A  345  1                                  11    
SHEET    1   A 5 THR A  39  PRO A  41  0                                        
SHEET    2   A 5 GLY A 260  VAL A 265  1  O  GLU A 262   N  ARG A  40           
SHEET    3   A 5 LYS A 214  PHE A 219 -1  N  CYS A 216   O  THR A 263           
SHEET    4   A 5 TRP A 278  SER A 283 -1  O  GLU A 282   N  ARG A 215           
SHEET    5   A 5 VAL A 195  TYR A 200 -1  N  THR A 196   O  ILE A 281           
SHEET    1   B 9 ARG A  44  LEU A  45  0                                        
SHEET    2   B 9 VAL A  63  LEU A  64  1  O  VAL A  63   N  LEU A  45           
SHEET    3   B 9 VAL A 270  ILE A 273 -1  O  VAL A 270   N  LEU A  64           
SHEET    4   B 9 GLN A 204  LYS A 211 -1  N  ASN A 205   O  ILE A 273           
SHEET    5   B 9 THR A 290  TYR A 297 -1  O  VAL A 293   N  ALA A 208           
SHEET    6   B 9 LEU A 182  GLY A 190 -1  N  LEU A 188   O  THR A 292           
SHEET    7   B 9 ARG A 143  THR A 149 -1  N  GLN A 148   O  LEU A 187           
SHEET    8   B 9 ASP A  89  ALA A  95 -1  N  TYR A  93   O  TYR A 145           
SHEET    9   B 9 ASN A 119  LYS A 124 -1  O  ASN A 119   N  SER A  94           
LINK         C   LYS A 107                 N   MSE A 108     1555   1555  1.33  
LINK         C   MSE A 108                 N   ALA A 109     1555   1555  1.32  
LINK         C   GLU A 122                 N   MSE A 123     1555   1555  1.33  
LINK         C   MSE A 123                 N   LYS A 124     1555   1555  1.33  
LINK         C   VAL A 159                 N   MSE A 160     1555   1555  1.33  
LINK         C   MSE A 160                 N   ASP A 161     1555   1555  1.33  
LINK         C   GLY A 190                 N   MSE A 191     1555   1555  1.33  
LINK         C   MSE A 191                 N   GLU A 192     1555   1555  1.33  
LINK         C   PRO A 274                 N   MSE A 275     1555   1555  1.32  
LINK         C   MSE A 275                 N   TYR A 276     1555   1555  1.33  
LINK         C   ILE A 318                 N   MSE A 319     1555   1555  1.33  
LINK         C   MSE A 319                 N   ARG A 320     1555   1555  1.33  
LINK         C   LYS A 324                 N   MSE A 325     1555   1555  1.33  
LINK         C   MSE A 325                 N   LEU A 326     1555   1555  1.33  
LINK         C   THR A 342                 N   MSE A 343     1555   1555  1.33  
LINK         C   MSE A 343                 N   ILE A 344     1555   1555  1.33  
CISPEP   1 TYR A  308    PRO A  309          0        -0.40                     
SITE     1 AC1  4 LYS A 107  ARG A 238  ARG A 320  LYS A 324                    
CRYST1   86.890   86.890  143.420  90.00  90.00  90.00 P 41 21 2     8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.011509  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011509  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006973        0.00000                         
ATOM      1  N   GLY A  12     -31.931   6.512  94.153  1.00 69.50           N  
ATOM      2  CA  GLY A  12     -30.601   6.887  93.581  1.00 70.24           C  
ATOM      3  C   GLY A  12     -30.374   8.384  93.637  1.00 70.52           C  
ATOM      4  O   GLY A  12     -29.354   8.857  94.151  1.00 71.46           O  
ATOM      5  N   SER A  13     -31.330   9.135  93.100  1.00 70.10           N  
ATOM      6  CA  SER A  13     -31.260  10.594  93.097  1.00 68.60           C  
ATOM      7  C   SER A  13     -31.900  11.167  94.369  1.00 68.13           C  
ATOM      8  O   SER A  13     -31.992  12.385  94.534  1.00 69.64           O  
ATOM      9  CB  SER A  13     -31.959  11.144  91.847  1.00 67.85           C  
ATOM     10  OG  SER A  13     -33.165  10.440  91.584  1.00 67.47           O  
ATOM     11  N   GLY A  14     -32.334  10.276  95.263  1.00 66.65           N  
ATOM     12  CA  GLY A  14     -32.951  10.685  96.516  1.00 64.18           C  
ATOM     13  C   GLY A  14     -34.345  11.263  96.361  1.00 62.44           C  
ATOM     14  O   GLY A  14     -34.834  11.423  95.243  1.00 63.19           O  
ATOM     15  N   GLU A  15     -34.999  11.557  97.483  1.00 60.81           N  
ATOM     16  CA  GLU A  15     -36.334  12.148  97.447  1.00 58.35           C  
ATOM     17  C   GLU A  15     -36.213  13.619  97.058  1.00 54.22           C  
ATOM     18  O   GLU A  15     -35.304  14.321  97.509  1.00 54.89           O  
ATOM     19  CB  GLU A  15     -37.042  12.016  98.805  1.00 61.97           C  
ATOM     20  CG  GLU A  15     -36.135  11.924 100.031  1.00 68.26           C  
ATOM     21  CD  GLU A  15     -36.927  11.919 101.345  1.00 72.77           C  
ATOM     22  OE1 GLU A  15     -37.509  12.974 101.696  1.00 72.96           O  
ATOM     23  OE2 GLU A  15     -36.975  10.862 102.024  1.00 72.96           O  
ATOM     24  N   PRO A  16     -37.138  14.108  96.220  1.00 50.71           N  
ATOM     25  CA  PRO A  16     -37.099  15.506  95.779  1.00 47.76           C  
ATOM     26  C   PRO A  16     -36.876  16.481  96.930  1.00 46.60           C  
ATOM     27  O   PRO A  16     -37.272  16.226  98.064  1.00 45.98           O  
ATOM     28  CB  PRO A  16     -38.467  15.701  95.110  1.00 47.76           C  
ATOM     29  CG  PRO A  16     -38.831  14.307  94.646  1.00 47.11           C  
ATOM     30  CD  PRO A  16     -38.403  13.465  95.820  1.00 49.04           C  
ATOM     31  N   ARG A  17     -36.225  17.594  96.645  1.00 45.29           N  
ATOM     32  CA  ARG A  17     -36.010  18.586  97.678  1.00 44.68           C  
ATOM     33  C   ARG A  17     -37.288  19.430  97.711  1.00 44.34           C  
ATOM     34  O   ARG A  17     -37.935  19.607  96.674  1.00 44.85           O  
ATOM     35  CB  ARG A  17     -34.784  19.438  97.328  1.00 43.42           C  
ATOM     36  CG  ARG A  17     -33.493  18.629  97.244  1.00 43.91           C  
ATOM     37  CD  ARG A  17     -32.260  19.509  97.113  1.00 43.21           C  
ATOM     38  NE  ARG A  17     -32.131  20.122  95.792  1.00 44.70           N  
ATOM     39  CZ  ARG A  17     -31.851  19.457  94.672  1.00 44.97           C  
ATOM     40  NH1 ARG A  17     -31.672  18.142  94.696  1.00 44.33           N  
ATOM     41  NH2 ARG A  17     -31.733  20.114  93.525  1.00 45.92           N  
ATOM     42  N   GLU A  18     -37.671  19.922  98.892  1.00 44.34           N  
ATOM     43  CA  GLU A  18     -38.876  20.754  99.032  1.00 43.07           C  
ATOM     44  C   GLU A  18     -38.547  22.215  98.730  1.00 42.85           C  
ATOM     45  O   GLU A  18     -37.592  22.764  99.276  1.00 44.65           O  
ATOM     46  CB  GLU A  18     -39.438  20.672 100.459  1.00 41.69           C  
ATOM     47  CG  GLU A  18     -40.239  19.415 100.810  1.00 41.09           C  
ATOM     48  CD  GLU A  18     -41.509  19.268  99.986  1.00 42.86           C  
ATOM     49  OE1 GLU A  18     -42.166  20.292  99.685  1.00 44.12           O  
ATOM     50  OE2 GLU A  18     -41.860  18.122  99.643  1.00 43.04           O  
ATOM     51  N   GLU A  19     -39.340  22.846  97.868  1.00 43.14           N  
ATOM     52  CA  GLU A  19     -39.131  24.253  97.503  1.00 42.18           C  
ATOM     53  C   GLU A  19     -39.444  25.188  98.687  1.00 39.77           C  
ATOM     54  O   GLU A  19     -40.344  24.920  99.483  1.00 41.42           O  
ATOM     55  CB  GLU A  19     -40.027  24.604  96.312  1.00 46.83           C  
ATOM     56  CG  GLU A  19     -39.353  25.401  95.214  1.00 52.72           C  
ATOM     57  CD  GLU A  19     -38.213  24.644  94.571  1.00 57.58           C  
ATOM     58  OE1 GLU A  19     -37.918  24.913  93.387  1.00 59.43           O  
ATOM     59  OE2 GLU A  19     -37.603  23.788  95.249  1.00 60.54           O  
ATOM     60  N   ALA A  20     -38.717  26.292  98.803  1.00 36.44           N  
ATOM     61  CA  ALA A  20     -38.941  27.221  99.911  1.00 33.96           C  
ATOM     62  C   ALA A  20     -40.291  27.925  99.821  1.00 31.64           C  
ATOM     63  O   ALA A  20     -40.789  28.207  98.732  1.00 30.98           O  
ATOM     64  CB  ALA A  20     -37.823  28.248  99.967  1.00 31.58           C  
ATOM     65  N   GLY A  21     -40.879  28.220 100.973  1.00 31.16           N  
ATOM     66  CA  GLY A  21     -42.165  28.881 100.969  1.00 29.62           C  
ATOM     67  C   GLY A  21     -43.232  27.918 100.494  1.00 30.39           C  
ATOM     68  O   GLY A  21     -44.031  28.247  99.622  1.00 28.86           O  
ATOM     69  N   ALA A  22     -43.227  26.712 101.058  1.00 32.22           N  
ATOM     70  CA  ALA A  22     -44.212  25.688 100.717  1.00 33.89           C  
ATOM     71  C   ALA A  22     -44.631  25.640  99.239  1.00 35.58           C  
ATOM     72  O   ALA A  22     -45.816  25.459  98.935  1.00 34.69           O  
ATOM     73  CB  ALA A  22     -45.449  25.876 101.590  1.00 33.10           C  
ATOM     74  N   LEU A  23     -43.676  25.788  98.324  1.00 38.19           N  
ATOM     75  CA  LEU A  23     -44.009  25.757  96.904  1.00 41.48           C  
ATOM     76  C   LEU A  23     -44.090  24.338  96.369  1.00 43.52           C  
ATOM     77  O   LEU A  23     -44.293  24.136  95.172  1.00 44.65           O  
ATOM     78  CB  LEU A  23     -42.994  26.552  96.095  1.00 44.05           C  
ATOM     79  CG  LEU A  23     -43.017  28.058  96.370  1.00 46.27           C  
ATOM     80  CD1 LEU A  23     -41.908  28.740  95.586  1.00 44.69           C  
ATOM     81  CD2 LEU A  23     -44.380  28.630  95.995  1.00 45.85           C  
ATOM     82  N   GLY A  24     -43.921  23.356  97.254  1.00 44.29           N  
ATOM     83  CA  GLY A  24     -44.025  21.966  96.844  1.00 46.14           C  
ATOM     84  C   GLY A  24     -42.729  21.310  96.437  1.00 46.85           C  
ATOM     85  O   GLY A  24     -41.730  21.996  96.227  1.00 47.41           O  
ATOM     86  N   PRO A  25     -42.710  19.973  96.306  1.00 46.85           N  
ATOM     87  CA  PRO A  25     -41.480  19.281  95.914  1.00 45.94           C  
ATOM     88  C   PRO A  25     -40.895  19.875  94.638  1.00 43.32           C  
ATOM     89  O   PRO A  25     -41.618  20.172  93.690  1.00 42.71           O  
ATOM     90  CB  PRO A  25     -41.939  17.832  95.750  1.00 46.44           C  
ATOM     91  CG  PRO A  25     -43.357  17.979  95.314  1.00 46.73           C  
ATOM     92  CD  PRO A  25     -43.861  19.054  96.253  1.00 47.77           C  
ATOM     93  N   ALA A  26     -39.580  20.058  94.634  1.00 41.69           N  
ATOM     94  CA  ALA A  26     -38.869  20.637  93.499  1.00 39.90           C  
ATOM     95  C   ALA A  26     -39.203  19.951  92.183  1.00 39.19           C  
ATOM     96  O   ALA A  26     -39.551  20.606  91.198  1.00 38.71           O  
ATOM     97  CB  ALA A  26     -37.368  20.574  93.754  1.00 39.40           C  
ATOM     98  N   TRP A  27     -39.087  18.628  92.179  1.00 38.33           N  
ATOM     99  CA  TRP A  27     -39.358  17.815  91.003  1.00 38.84           C  
ATOM    100  C   TRP A  27     -39.972  16.536  91.562  1.00 40.90           C  
ATOM    101  O   TRP A  27     -40.072  16.387  92.782  1.00 40.66           O  
ATOM    102  CB  TRP A  27     -38.033  17.494  90.286  1.00 37.43           C  
ATOM    103  CG  TRP A  27     -37.233  16.386  90.940  1.00 37.10           C  
ATOM    104  CD1 TRP A  27     -37.389  15.033  90.750  1.00 35.87           C  
ATOM    105  CD2 TRP A  27     -36.229  16.527  91.957  1.00 37.47           C  
ATOM    106  NE1 TRP A  27     -36.551  14.331  91.586  1.00 35.02           N  
ATOM    107  CE2 TRP A  27     -35.828  15.218  92.338  1.00 36.86           C  
ATOM    108  CE3 TRP A  27     -35.632  17.626  92.585  1.00 38.55           C  
ATOM    109  CZ2 TRP A  27     -34.861  14.984  93.324  1.00 36.59           C  
ATOM    110  CZ3 TRP A  27     -34.667  17.391  93.571  1.00 40.43           C  
ATOM    111  CH2 TRP A  27     -34.295  16.077  93.927  1.00 39.60           C  
ATOM    112  N   ASP A  28     -40.389  15.618  90.695  1.00 43.32           N  
ATOM    113  CA  ASP A  28     -40.930  14.354  91.182  1.00 46.68           C  
ATOM    114  C   ASP A  28     -40.442  13.194  90.318  1.00 46.56           C  
ATOM    115  O   ASP A  28     -40.128  13.368  89.140  1.00 45.28           O  
ATOM    116  CB  ASP A  28     -42.455  14.388  91.228  1.00 50.61           C  
ATOM    117  CG  ASP A  28     -43.084  13.637  90.092  1.00 55.38           C  
ATOM    118  OD1 ASP A  28     -43.057  14.157  88.956  1.00 58.91           O  
ATOM    119  OD2 ASP A  28     -43.596  12.522  90.339  1.00 57.80           O  
ATOM    120  N   GLU A  29     -40.384  12.011  90.917  1.00 47.51           N  
ATOM    121  CA  GLU A  29     -39.891  10.813  90.245  1.00 48.52           C  
ATOM    122  C   GLU A  29     -40.334  10.540  88.804  1.00 47.40           C  
ATOM    123  O   GLU A  29     -39.521  10.112  87.986  1.00 48.58           O  
ATOM    124  CB  GLU A  29     -40.187   9.585  91.102  1.00 53.58           C  
ATOM    125  CG  GLU A  29     -39.762   8.281  90.459  1.00 62.10           C  
ATOM    126  CD  GLU A  29     -39.821   7.109  91.419  1.00 69.10           C  
ATOM    127  OE1 GLU A  29     -40.888   6.895  92.040  1.00 72.22           O  
ATOM    128  OE2 GLU A  29     -38.797   6.399  91.548  1.00 72.74           O  
ATOM    129  N   SER A  30     -41.600  10.771  88.480  1.00 45.80           N  
ATOM    130  CA  SER A  30     -42.062  10.515  87.120  1.00 45.50           C  
ATOM    131  C   SER A  30     -41.279  11.307  86.063  1.00 45.11           C  
ATOM    132  O   SER A  30     -41.334  10.994  84.873  1.00 44.47           O  
ATOM    133  CB  SER A  30     -43.556  10.834  86.999  1.00 44.81           C  
ATOM    134  OG  SER A  30     -43.807  12.228  87.057  1.00 45.52           O  
ATOM    135  N   GLN A  31     -40.545  12.329  86.493  1.00 45.10           N  
ATOM    136  CA  GLN A  31     -39.769  13.147  85.559  1.00 42.18           C  
ATOM    137  C   GLN A  31     -38.384  12.572  85.211  1.00 41.21           C  
ATOM    138  O   GLN A  31     -37.675  13.111  84.339  1.00 41.92           O  
ATOM    139  CB  GLN A  31     -39.624  14.564  86.116  1.00 41.74           C  
ATOM    140  CG  GLN A  31     -40.941  15.309  86.146  1.00 40.24           C  
ATOM    141  CD  GLN A  31     -40.841  16.646  86.833  1.00 36.47           C  
ATOM    142  OE1 GLN A  31     -40.730  16.724  88.059  1.00 34.23           O  
ATOM    143  NE2 GLN A  31     -40.874  17.715  86.046  1.00 36.41           N  
ATOM    144  N   LEU A  32     -38.010  11.481  85.889  1.00 37.61           N  
ATOM    145  CA  LEU A  32     -36.726  10.812  85.671  1.00 34.49           C  
ATOM    146  C   LEU A  32     -36.902   9.661  84.677  1.00 33.49           C  
ATOM    147  O   LEU A  32     -37.836   8.873  84.807  1.00 34.45           O  
ATOM    148  CB  LEU A  32     -36.182  10.249  86.995  1.00 30.86           C  
ATOM    149  CG  LEU A  32     -35.902  11.187  88.177  1.00 26.78           C  
ATOM    150  CD1 LEU A  32     -35.326  10.398  89.367  1.00 22.54           C  
ATOM    151  CD2 LEU A  32     -34.932  12.259  87.754  1.00 24.16           C  
ATOM    152  N   ARG A  33     -36.012   9.560  83.692  1.00 31.19           N  
ATOM    153  CA  ARG A  33     -36.101   8.487  82.717  1.00 30.66           C  
ATOM    154  C   ARG A  33     -35.687   7.145  83.340  1.00 32.45           C  
ATOM    155  O   ARG A  33     -34.993   7.110  84.358  1.00 33.89           O  
ATOM    156  CB  ARG A  33     -35.224   8.807  81.506  1.00 29.66           C  
ATOM    157  CG  ARG A  33     -35.830   9.834  80.559  1.00 28.00           C  
ATOM    158  CD  ARG A  33     -34.900  10.122  79.393  1.00 30.15           C  
ATOM    159  NE  ARG A  33     -35.254  11.364  78.704  1.00 33.66           N  
ATOM    160  CZ  ARG A  33     -36.154  11.457  77.732  1.00 35.21           C  
ATOM    161  NH1 ARG A  33     -36.801  10.379  77.315  1.00 35.67           N  
ATOM    162  NH2 ARG A  33     -36.418  12.633  77.186  1.00 38.38           N  
ATOM    163  N   SER A  34     -36.119   6.043  82.730  1.00 33.27           N  
ATOM    164  CA  SER A  34     -35.810   4.709  83.235  1.00 33.61           C  
ATOM    165  C   SER A  34     -34.504   4.137  82.685  1.00 34.78           C  
ATOM    166  O   SER A  34     -34.227   4.214  81.481  1.00 35.30           O  
ATOM    167  CB  SER A  34     -36.959   3.758  82.906  1.00 35.35           C  
ATOM    168  OG  SER A  34     -38.164   4.170  83.542  1.00 38.74           O  
ATOM    169  N   TYR A  35     -33.699   3.555  83.568  1.00 35.66           N  
ATOM    170  CA  TYR A  35     -32.430   2.970  83.150  1.00 35.62           C  
ATOM    171  C   TYR A  35     -32.194   1.607  83.789  1.00 36.48           C  
ATOM    172  O   TYR A  35     -32.762   1.290  84.837  1.00 34.69           O  
ATOM    173  CB  TYR A  35     -31.287   3.934  83.458  1.00 29.76           C  
ATOM    174  CG  TYR A  35     -31.408   5.218  82.670  1.00 28.43           C  
ATOM    175  CD1 TYR A  35     -31.346   6.459  83.309  1.00 26.25           C  
ATOM    176  CD2 TYR A  35     -31.603   5.197  81.284  1.00 26.39           C  
ATOM    177  CE1 TYR A  35     -31.476   7.644  82.597  1.00 25.93           C  
ATOM    178  CE2 TYR A  35     -31.735   6.382  80.558  1.00 26.52           C  
ATOM    179  CZ  TYR A  35     -31.676   7.604  81.226  1.00 25.82           C  
ATOM    180  OH  TYR A  35     -31.872   8.791  80.545  1.00 27.17           O  
ATOM    181  N   SER A  36     -31.346   0.811  83.142  1.00 38.15           N  
ATOM    182  CA  SER A  36     -31.044  -0.549  83.582  1.00 38.34           C  
ATOM    183  C   SER A  36     -29.888  -0.699  84.556  1.00 36.62           C  
ATOM    184  O   SER A  36     -29.122  -1.658  84.440  1.00 38.99           O  
ATOM    185  CB  SER A  36     -30.762  -1.413  82.349  1.00 43.63           C  
ATOM    186  OG  SER A  36     -29.796  -0.793  81.503  1.00 44.79           O  
ATOM    187  N   PHE A  37     -29.750   0.219  85.511  1.00 33.26           N  
ATOM    188  CA  PHE A  37     -28.636   0.124  86.459  1.00 31.43           C  
ATOM    189  C   PHE A  37     -28.799   0.944  87.738  1.00 29.19           C  
ATOM    190  O   PHE A  37     -29.471   1.976  87.759  1.00 28.06           O  
ATOM    191  CB  PHE A  37     -27.322   0.528  85.767  1.00 33.29           C  
ATOM    192  CG  PHE A  37     -27.339   1.926  85.205  1.00 33.52           C  
ATOM    193  CD1 PHE A  37     -27.220   3.034  86.046  1.00 33.32           C  
ATOM    194  CD2 PHE A  37     -27.548   2.140  83.842  1.00 34.01           C  
ATOM    195  CE1 PHE A  37     -27.316   4.329  85.538  1.00 34.18           C  
ATOM    196  CE2 PHE A  37     -27.647   3.438  83.321  1.00 33.50           C  
ATOM    197  CZ  PHE A  37     -27.533   4.529  84.167  1.00 34.11           C  
ATOM    198  N   PRO A  38     -28.176   0.483  88.832  1.00 26.77           N  
ATOM    199  CA  PRO A  38     -28.218   1.140  90.146  1.00 25.50           C  
ATOM    200  C   PRO A  38     -27.375   2.409  90.152  1.00 25.71           C  
ATOM    201  O   PRO A  38     -26.582   2.631  89.238  1.00 26.42           O  
ATOM    202  CB  PRO A  38     -27.645   0.079  91.073  1.00 23.66           C  
ATOM    203  CG  PRO A  38     -26.603  -0.576  90.181  1.00 25.15           C  
ATOM    204  CD  PRO A  38     -27.371  -0.753  88.885  1.00 24.48           C  
ATOM    205  N   THR A  39     -27.539   3.233  91.184  1.00 26.21           N  
ATOM    206  CA  THR A  39     -26.790   4.487  91.312  1.00 27.92           C  
ATOM    207  C   THR A  39     -26.755   4.932  92.757  1.00 31.96           C  
ATOM    208  O   THR A  39     -27.692   4.677  93.515  1.00 33.76           O  
ATOM    209  CB  THR A  39     -27.440   5.658  90.515  1.00 26.39           C  
ATOM    210  OG1 THR A  39     -28.836   5.730  90.832  1.00 24.84           O  
ATOM    211  CG2 THR A  39     -27.267   5.488  89.010  1.00 21.99           C  
ATOM    212  N   ARG A  40     -25.670   5.601  93.134  1.00 35.84           N  
ATOM    213  CA  ARG A  40     -25.517   6.142  94.484  1.00 39.41           C  
ATOM    214  C   ARG A  40     -25.637   7.653  94.362  1.00 38.62           C  
ATOM    215  O   ARG A  40     -25.411   8.219  93.295  1.00 39.22           O  
ATOM    216  CB  ARG A  40     -24.140   5.811  95.062  1.00 46.04           C  
ATOM    217  CG  ARG A  40     -23.988   4.403  95.622  1.00 57.01           C  
ATOM    218  CD  ARG A  40     -24.886   4.164  96.841  1.00 64.47           C  
ATOM    219  NE  ARG A  40     -26.308   4.097  96.493  1.00 69.45           N  
ATOM    220  CZ  ARG A  40     -27.279   3.783  97.351  1.00 71.53           C  
ATOM    221  NH1 ARG A  40     -26.990   3.502  98.617  1.00 70.92           N  
ATOM    222  NH2 ARG A  40     -28.545   3.754  96.941  1.00 72.06           N  
ATOM    223  N   PRO A  41     -26.005   8.332  95.451  1.00 37.59           N  
ATOM    224  CA  PRO A  41     -26.124   9.793  95.379  1.00 34.60           C  
ATOM    225  C   PRO A  41     -24.787  10.531  95.522  1.00 31.48           C  
ATOM    226  O   PRO A  41     -23.900  10.099  96.258  1.00 28.72           O  
ATOM    227  CB  PRO A  41     -27.073  10.111  96.531  1.00 35.00           C  
ATOM    228  CG  PRO A  41     -26.687   9.087  97.546  1.00 34.95           C  
ATOM    229  CD  PRO A  41     -26.598   7.823  96.701  1.00 35.95           C  
ATOM    230  N   ILE A  42     -24.639  11.635  94.799  1.00 28.84           N  
ATOM    231  CA  ILE A  42     -23.424  12.440  94.916  1.00 24.79           C  
ATOM    232  C   ILE A  42     -23.717  13.329  96.112  1.00 25.11           C  
ATOM    233  O   ILE A  42     -24.824  13.863  96.251  1.00 26.10           O  
ATOM    234  CB  ILE A  42     -23.199  13.341  93.695  1.00 23.86           C  
ATOM    235  CG1 ILE A  42     -23.241  12.501  92.417  1.00 22.43           C  
ATOM    236  CG2 ILE A  42     -21.863  14.060  93.839  1.00 20.36           C  
ATOM    237  CD1 ILE A  42     -23.177  13.306  91.160  1.00 21.39           C  
ATOM    238  N   PRO A  43     -22.749  13.485  97.005  1.00 23.76           N  
ATOM    239  CA  PRO A  43     -22.982  14.327  98.180  1.00 26.50           C  
ATOM    240  C   PRO A  43     -23.208  15.817  97.902  1.00 27.86           C  
ATOM    241  O   PRO A  43     -22.452  16.443  97.142  1.00 29.70           O  
ATOM    242  CB  PRO A  43     -21.743  14.059  99.044  1.00 25.66           C  
ATOM    243  CG  PRO A  43     -20.701  13.673  98.055  1.00 25.56           C  
ATOM    244  CD  PRO A  43     -21.462  12.785  97.099  1.00 24.37           C  
ATOM    245  N   ARG A  44     -24.262  16.377  98.509  1.00 28.38           N  
ATOM    246  CA  ARG A  44     -24.584  17.804  98.355  1.00 26.66           C  
ATOM    247  C   ARG A  44     -24.060  18.509  99.597  1.00 24.92           C  
ATOM    248  O   ARG A  44     -24.528  18.245 100.703  1.00 24.93           O  
ATOM    249  CB  ARG A  44     -26.105  18.031  98.231  1.00 27.51           C  
ATOM    250  CG  ARG A  44     -26.738  17.341  97.014  1.00 29.92           C  
ATOM    251  CD  ARG A  44     -28.211  17.734  96.773  1.00 32.47           C  
ATOM    252  NE  ARG A  44     -28.389  19.058  96.156  1.00 34.35           N  
ATOM    253  CZ  ARG A  44     -28.890  20.112  96.800  1.00 35.68           C  
ATOM    254  NH1 ARG A  44     -29.261  19.991  98.072  1.00 33.89           N  
ATOM    255  NH2 ARG A  44     -29.021  21.283  96.182  1.00 34.00           N  
ATOM    256  N   LEU A  45     -23.097  19.409  99.409  1.00 25.12           N  
ATOM    257  CA  LEU A  45     -22.492  20.126 100.528  1.00 26.42           C  
ATOM    258  C   LEU A  45     -22.339  21.639 100.352  1.00 26.89           C  
ATOM    259  O   LEU A  45     -22.732  22.220  99.328  1.00 28.55           O  
ATOM    260  CB  LEU A  45     -21.108  19.541 100.803  1.00 24.07           C  
ATOM    261  CG  LEU A  45     -21.059  18.028 100.993  1.00 21.70           C  
ATOM    262  CD1 LEU A  45     -19.604  17.611 101.142  1.00 18.44           C  
ATOM    263  CD2 LEU A  45     -21.892  17.634 102.208  1.00 15.92           C  
ATOM    264  N   SER A  46     -21.754  22.258 101.374  1.00 25.95           N  
ATOM    265  CA  SER A  46     -21.487  23.682 101.382  1.00 29.43           C  
ATOM    266  C   SER A  46     -19.999  23.904 101.073  1.00 33.39           C  
ATOM    267  O   SER A  46     -19.128  23.143 101.520  1.00 34.16           O  
ATOM    268  CB  SER A  46     -21.814  24.272 102.748  1.00 29.76           C  
ATOM    269  OG  SER A  46     -21.002  25.409 103.004  1.00 27.53           O  
ATOM    270  N   GLN A  47     -19.708  24.960 100.324  1.00 34.32           N  
ATOM    271  CA  GLN A  47     -18.343  25.269  99.936  1.00 36.26           C  
ATOM    272  C   GLN A  47     -17.404  25.428 101.132  1.00 36.81           C  
ATOM    273  O   GLN A  47     -16.184  25.299 100.999  1.00 37.80           O  
ATOM    274  CB  GLN A  47     -18.344  26.549  99.118  1.00 39.84           C  
ATOM    275  CG  GLN A  47     -18.804  27.740  99.931  1.00 44.70           C  
ATOM    276  CD  GLN A  47     -17.812  28.877  99.869  1.00 47.88           C  
ATOM    277  OE1 GLN A  47     -17.858  29.711  98.952  1.00 50.30           O  
ATOM    278  NE2 GLN A  47     -16.889  28.911 100.833  1.00 48.15           N  
ATOM    279  N   SER A  48     -17.967  25.711 102.300  1.00 37.99           N  
ATOM    280  CA  SER A  48     -17.160  25.898 103.512  1.00 40.27           C  
ATOM    281  C   SER A  48     -16.897  24.567 104.203  1.00 40.52           C  
ATOM    282  O   SER A  48     -16.058  24.468 105.106  1.00 39.26           O  
ATOM    283  CB  SER A  48     -17.884  26.801 104.494  1.00 41.87           C  
ATOM    284  OG  SER A  48     -19.006  26.111 105.019  1.00 45.91           O  
ATOM    285  N   ASP A  49     -17.636  23.546 103.792  1.00 40.23           N  
ATOM    286  CA  ASP A  49     -17.462  22.235 104.376  1.00 39.40           C  
ATOM    287  C   ASP A  49     -16.129  21.634 103.917  1.00 38.72           C  
ATOM    288  O   ASP A  49     -15.870  21.504 102.717  1.00 40.05           O  
ATOM    289  CB  ASP A  49     -18.625  21.341 103.970  1.00 36.78           C  
ATOM    290  CG  ASP A  49     -18.584  20.007 104.653  1.00 37.41           C  
ATOM    291  OD1 ASP A  49     -19.670  19.434 104.882  1.00 37.93           O  
ATOM    292  OD2 ASP A  49     -17.469  19.525 104.953  1.00 38.15           O  
ATOM    293  N   PRO A  50     -15.261  21.272 104.873  1.00 38.84           N  
ATOM    294  CA  PRO A  50     -13.954  20.687 104.571  1.00 39.22           C  
ATOM    295  C   PRO A  50     -14.046  19.459 103.677  1.00 41.39           C  
ATOM    296  O   PRO A  50     -13.176  19.245 102.826  1.00 42.62           O  
ATOM    297  CB  PRO A  50     -13.410  20.336 105.949  1.00 39.27           C  
ATOM    298  CG  PRO A  50     -13.999  21.395 106.811  1.00 38.26           C  
ATOM    299  CD  PRO A  50     -15.430  21.426 106.327  1.00 39.42           C  
ATOM    300  N   ARG A  51     -15.097  18.661 103.863  1.00 42.64           N  
ATOM    301  CA  ARG A  51     -15.276  17.436 103.080  1.00 45.29           C  
ATOM    302  C   ARG A  51     -15.425  17.713 101.583  1.00 43.99           C  
ATOM    303  O   ARG A  51     -15.077  16.873 100.746  1.00 44.11           O  
ATOM    304  CB  ARG A  51     -16.494  16.657 103.581  1.00 48.87           C  
ATOM    305  CG  ARG A  51     -16.562  15.210 103.089  1.00 54.03           C  
ATOM    306  CD  ARG A  51     -17.943  14.606 103.384  1.00 61.26           C  
ATOM    307  NE  ARG A  51     -18.150  13.305 102.740  1.00 65.90           N  
ATOM    308  CZ  ARG A  51     -19.344  12.737 102.566  1.00 68.16           C  
ATOM    309  NH1 ARG A  51     -20.446  13.357 102.985  1.00 68.33           N  
ATOM    310  NH2 ARG A  51     -19.436  11.548 101.977  1.00 69.84           N  
ATOM    311  N   ALA A  52     -15.939  18.891 101.250  1.00 42.70           N  
ATOM    312  CA  ALA A  52     -16.125  19.263  99.855  1.00 41.91           C  
ATOM    313  C   ALA A  52     -14.774  19.491  99.200  1.00 42.02           C  
ATOM    314  O   ALA A  52     -14.514  18.980  98.109  1.00 42.62           O  
ATOM    315  CB  ALA A  52     -16.974  20.518  99.752  1.00 41.69           C  
ATOM    316  N   GLU A  53     -13.917  20.268  99.854  1.00 43.57           N  
ATOM    317  CA  GLU A  53     -12.590  20.534  99.308  1.00 45.82           C  
ATOM    318  C   GLU A  53     -11.882  19.195  99.189  1.00 44.15           C  
ATOM    319  O   GLU A  53     -11.079  18.976  98.284  1.00 44.26           O  
ATOM    320  CB  GLU A  53     -11.797  21.464 100.232  1.00 47.03           C  
ATOM    321  CG  GLU A  53     -12.299  22.918 100.257  1.00 56.74           C  
ATOM    322  CD  GLU A  53     -11.802  23.746  99.076  1.00 62.32           C  
ATOM    323  OE1 GLU A  53     -10.573  23.946  98.965  1.00 65.56           O  
ATOM    324  OE2 GLU A  53     -12.635  24.199  98.259  1.00 65.38           O  
ATOM    325  N   GLU A  54     -12.203  18.287 100.100  1.00 44.01           N  
ATOM    326  CA  GLU A  54     -11.584  16.976 100.083  1.00 43.36           C  
ATOM    327  C   GLU A  54     -11.995  16.246  98.810  1.00 41.93           C  
ATOM    328  O   GLU A  54     -11.151  15.922  97.976  1.00 42.51           O  
ATOM    329  CB  GLU A  54     -12.017  16.174 101.304  1.00 48.91           C  
ATOM    330  CG  GLU A  54     -10.899  15.398 101.950  1.00 57.41           C  
ATOM    331  CD  GLU A  54     -11.418  14.391 102.959  1.00 64.08           C  
ATOM    332  OE1 GLU A  54     -12.096  13.425 102.538  1.00 69.59           O  
ATOM    333  OE2 GLU A  54     -11.156  14.565 104.170  1.00 68.51           O  
ATOM    334  N   LEU A  55     -13.292  15.993  98.657  1.00 38.14           N  
ATOM    335  CA  LEU A  55     -13.803  15.301  97.479  1.00 35.26           C  
ATOM    336  C   LEU A  55     -13.276  15.883  96.172  1.00 34.48           C  
ATOM    337  O   LEU A  55     -12.985  15.149  95.220  1.00 33.44           O  
ATOM    338  CB  LEU A  55     -15.320  15.344  97.477  1.00 30.88           C  
ATOM    339  CG  LEU A  55     -15.946  14.389  98.481  1.00 27.83           C  
ATOM    340  CD1 LEU A  55     -17.462  14.545  98.502  1.00 26.63           C  
ATOM    341  CD2 LEU A  55     -15.559  12.977  98.083  1.00 26.13           C  
ATOM    342  N   ILE A  56     -13.151  17.201  96.129  1.00 33.98           N  
ATOM    343  CA  ILE A  56     -12.658  17.864  94.934  1.00 36.26           C  
ATOM    344  C   ILE A  56     -11.193  17.548  94.724  1.00 40.23           C  
ATOM    345  O   ILE A  56     -10.724  17.449  93.590  1.00 41.26           O  
ATOM    346  CB  ILE A  56     -12.817  19.394  95.027  1.00 32.08           C  
ATOM    347  CG1 ILE A  56     -14.288  19.771  94.873  1.00 27.86           C  
ATOM    348  CG2 ILE A  56     -11.956  20.071  93.979  1.00 29.84           C  
ATOM    349  CD1 ILE A  56     -14.517  21.250  94.780  1.00 25.23           C  
ATOM    350  N   GLU A  57     -10.470  17.389  95.823  1.00 43.74           N  
ATOM    351  CA  GLU A  57      -9.052  17.092  95.750  1.00 49.36           C  
ATOM    352  C   GLU A  57      -8.801  15.637  95.376  1.00 48.95           C  
ATOM    353  O   GLU A  57      -7.832  15.333  94.688  1.00 52.37           O  
ATOM    354  CB  GLU A  57      -8.375  17.412  97.082  1.00 53.99           C  
ATOM    355  CG  GLU A  57      -6.863  17.297  97.045  1.00 63.38           C  
ATOM    356  CD  GLU A  57      -6.246  18.201  95.997  1.00 70.15           C  
ATOM    357  OE1 GLU A  57      -6.363  19.438  96.137  1.00 72.57           O  
ATOM    358  OE2 GLU A  57      -5.651  17.672  95.028  1.00 72.96           O  
ATOM    359  N   ASN A  58      -9.654  14.729  95.834  1.00 49.50           N  
ATOM    360  CA  ASN A  58      -9.465  13.327  95.484  1.00 48.59           C  
ATOM    361  C   ASN A  58     -10.209  13.100  94.186  1.00 48.33           C  
ATOM    362  O   ASN A  58     -10.566  11.974  93.844  1.00 47.34           O  
ATOM    363  CB  ASN A  58     -10.033  12.399  96.558  1.00 50.55           C  
ATOM    364  CG  ASN A  58      -9.631  12.814  97.948  1.00 51.19           C  
ATOM    365  OD1 ASN A  58      -8.460  13.107  98.205  1.00 50.38           O  
ATOM    366  ND2 ASN A  58     -10.600  12.839  98.867  1.00 50.14           N  
ATOM    367  N   GLU A  59     -10.443  14.184  93.463  1.00 46.26           N  
ATOM    368  CA  GLU A  59     -11.165  14.106  92.207  1.00 46.30           C  
ATOM    369  C   GLU A  59     -12.393  13.191  92.246  1.00 43.86           C  
ATOM    370  O   GLU A  59     -12.531  12.265  91.440  1.00 42.25           O  
ATOM    371  CB  GLU A  59     -10.217  13.700  91.090  1.00 47.76           C  
ATOM    372  CG  GLU A  59      -9.530  14.892  90.468  1.00 53.62           C  
ATOM    373  CD  GLU A  59      -8.232  14.521  89.806  1.00 58.80           C  
ATOM    374  OE1 GLU A  59      -7.243  14.279  90.532  1.00 60.51           O  
ATOM    375  OE2 GLU A  59      -8.200  14.459  88.562  1.00 62.00           O  
ATOM    376  N   GLU A  60     -13.270  13.469  93.210  1.00 40.73           N  
ATOM    377  CA  GLU A  60     -14.529  12.758  93.379  1.00 38.36           C  
ATOM    378  C   GLU A  60     -15.615  13.835  93.263  1.00 34.54           C  
ATOM    379  O   GLU A  60     -15.501  14.910  93.861  1.00 34.29           O  
ATOM    380  CB  GLU A  60     -14.598  12.108  94.750  1.00 41.96           C  
ATOM    381  CG  GLU A  60     -13.603  11.001  95.007  1.00 42.34           C  
ATOM    382  CD  GLU A  60     -14.031  10.173  96.201  1.00 45.61           C  
ATOM    383  OE1 GLU A  60     -15.071   9.481  96.084  1.00 44.42           O  
ATOM    384  OE2 GLU A  60     -13.351  10.230  97.257  1.00 47.82           O  
ATOM    385  N   PRO A  61     -16.698  13.555  92.523  1.00 31.87           N  
ATOM    386  CA  PRO A  61     -17.753  14.565  92.371  1.00 29.86           C  
ATOM    387  C   PRO A  61     -18.468  15.044  93.622  1.00 25.93           C  
ATOM    388  O   PRO A  61     -18.693  14.283  94.560  1.00 23.80           O  
ATOM    389  CB  PRO A  61     -18.710  13.924  91.359  1.00 28.06           C  
ATOM    390  CG  PRO A  61     -18.591  12.479  91.675  1.00 29.02           C  
ATOM    391  CD  PRO A  61     -17.090  12.288  91.882  1.00 31.67           C  
ATOM    392  N   VAL A  62     -18.806  16.334  93.613  1.00 24.79           N  
ATOM    393  CA  VAL A  62     -19.534  16.976  94.702  1.00 22.27           C  
ATOM    394  C   VAL A  62     -20.569  17.916  94.115  1.00 23.59           C  
ATOM    395  O   VAL A  62     -20.465  18.342  92.957  1.00 25.58           O  
ATOM    396  CB  VAL A  62     -18.684  17.902  95.560  1.00 19.17           C  
ATOM    397  CG1 VAL A  62     -19.080  17.731  96.998  1.00 17.83           C  
ATOM    398  CG2 VAL A  62     -17.226  17.670  95.341  1.00 18.94           C  
ATOM    399  N   VAL A  63     -21.573  18.244  94.916  1.00 20.94           N  
ATOM    400  CA  VAL A  63     -22.554  19.207  94.482  1.00 20.97           C  
ATOM    401  C   VAL A  63     -22.472  20.257  95.563  1.00 21.22           C  
ATOM    402  O   VAL A  63     -22.858  20.014  96.707  1.00 20.74           O  
ATOM    403  CB  VAL A  63     -23.955  18.611  94.406  1.00 20.90           C  
ATOM    404  CG1 VAL A  63     -24.994  19.720  94.476  1.00 20.45           C  
ATOM    405  CG2 VAL A  63     -24.110  17.862  93.086  1.00 18.92           C  
ATOM    406  N   LEU A  64     -21.897  21.404  95.208  1.00 23.28           N  
ATOM    407  CA  LEU A  64     -21.750  22.524  96.136  1.00 21.00           C  
ATOM    408  C   LEU A  64     -23.037  23.310  95.965  1.00 22.13           C  
ATOM    409  O   LEU A  64     -23.412  23.634  94.833  1.00 21.74           O  
ATOM    410  CB  LEU A  64     -20.537  23.356  95.740  1.00 16.20           C  
ATOM    411  CG  LEU A  64     -19.223  22.556  95.769  1.00 15.54           C  
ATOM    412  CD1 LEU A  64     -18.218  23.157  94.819  1.00 15.36           C  
ATOM    413  CD2 LEU A  64     -18.638  22.527  97.168  1.00 13.62           C  
ATOM    414  N   THR A  65     -23.721  23.580  97.078  1.00 25.24           N  
ATOM    415  CA  THR A  65     -24.997  24.307  97.064  1.00 29.68           C  
ATOM    416  C   THR A  65     -24.970  25.801  97.420  1.00 30.99           C  
ATOM    417  O   THR A  65     -25.982  26.486  97.251  1.00 33.94           O  
ATOM    418  CB  THR A  65     -26.002  23.680  98.037  1.00 27.23           C  
ATOM    419  OG1 THR A  65     -25.391  23.579  99.331  1.00 28.15           O  
ATOM    420  CG2 THR A  65     -26.442  22.306  97.558  1.00 26.12           C  
ATOM    421  N   ASP A  66     -23.846  26.319  97.904  1.00 31.39           N  
ATOM    422  CA  ASP A  66     -23.811  27.724  98.297  1.00 32.82           C  
ATOM    423  C   ASP A  66     -22.547  28.465  97.867  1.00 33.08           C  
ATOM    424  O   ASP A  66     -21.837  29.024  98.703  1.00 35.78           O  
ATOM    425  CB  ASP A  66     -23.957  27.807  99.813  1.00 35.06           C  
ATOM    426  CG  ASP A  66     -22.827  27.089 100.550  1.00 36.22           C  
ATOM    427  OD1 ASP A  66     -22.056  26.345  99.882  1.00 38.31           O  
ATOM    428  OD2 ASP A  66     -22.715  27.262 101.791  1.00 33.83           O  
ATOM    429  N   THR A  67     -22.265  28.483  96.570  1.00 31.91           N  
ATOM    430  CA  THR A  67     -21.071  29.146  96.074  1.00 29.62           C  
ATOM    431  C   THR A  67     -21.437  30.488  95.474  1.00 31.04           C  
ATOM    432  O   THR A  67     -20.575  31.352  95.285  1.00 32.01           O  
ATOM    433  CB  THR A  67     -20.404  28.332  94.964  1.00 27.51           C  
ATOM    434  OG1 THR A  67     -21.352  28.128  93.914  1.00 25.89           O  
ATOM    435  CG2 THR A  67     -19.922  26.988  95.474  1.00 23.52           C  
ATOM    436  N   ASN A  68     -22.713  30.663  95.153  1.00 30.05           N  
ATOM    437  CA  ASN A  68     -23.163  31.915  94.543  1.00 30.00           C  
ATOM    438  C   ASN A  68     -22.345  32.173  93.300  1.00 29.00           C  
ATOM    439  O   ASN A  68     -22.243  33.305  92.828  1.00 28.54           O  
ATOM    440  CB  ASN A  68     -22.976  33.073  95.515  1.00 27.59           C  
ATOM    441  CG  ASN A  68     -23.802  32.904  96.751  1.00 28.64           C  
ATOM    442  OD1 ASN A  68     -25.033  32.765  96.665  1.00 26.77           O  
ATOM    443  ND2 ASN A  68     -23.146  32.895  97.917  1.00 25.88           N  
ATOM    444  N   LEU A  69     -21.747  31.116  92.777  1.00 28.63           N  
ATOM    445  CA  LEU A  69     -20.934  31.254  91.589  1.00 29.15           C  
ATOM    446  C   LEU A  69     -21.690  31.994  90.488  1.00 30.53           C  
ATOM    447  O   LEU A  69     -21.133  32.829  89.778  1.00 30.79           O  
ATOM    448  CB  LEU A  69     -20.522  29.871  91.089  1.00 26.80           C  
ATOM    449  CG  LEU A  69     -19.743  29.863  89.778  1.00 25.81           C  
ATOM    450  CD1 LEU A  69     -18.554  30.821  89.889  1.00 22.94           C  
ATOM    451  CD2 LEU A  69     -19.278  28.430  89.481  1.00 25.99           C  
ATOM    452  N   VAL A  70     -22.977  31.707  90.385  1.00 33.09           N  
ATOM    453  CA  VAL A  70     -23.807  32.278  89.341  1.00 36.06           C  
ATOM    454  C   VAL A  70     -24.990  33.099  89.871  1.00 36.54           C  
ATOM    455  O   VAL A  70     -25.985  33.311  89.178  1.00 35.94           O  
ATOM    456  CB  VAL A  70     -24.275  31.104  88.445  1.00 37.48           C  
ATOM    457  CG1 VAL A  70     -25.251  31.551  87.391  1.00 39.40           C  
ATOM    458  CG2 VAL A  70     -23.052  30.483  87.793  1.00 39.02           C  
ATOM    459  N   TYR A  71     -24.860  33.588  91.099  1.00 39.03           N  
ATOM    460  CA  TYR A  71     -25.925  34.362  91.736  1.00 39.79           C  
ATOM    461  C   TYR A  71     -26.664  35.331  90.805  1.00 38.25           C  
ATOM    462  O   TYR A  71     -27.880  35.219  90.614  1.00 39.13           O  
ATOM    463  CB  TYR A  71     -25.369  35.138  92.939  1.00 42.35           C  
ATOM    464  CG  TYR A  71     -26.425  35.922  93.671  1.00 45.96           C  
ATOM    465  CD1 TYR A  71     -27.390  35.276  94.440  1.00 48.81           C  
ATOM    466  CD2 TYR A  71     -26.481  37.308  93.570  1.00 47.88           C  
ATOM    467  CE1 TYR A  71     -28.392  35.995  95.096  1.00 52.14           C  
ATOM    468  CE2 TYR A  71     -27.475  38.038  94.214  1.00 51.03           C  
ATOM    469  CZ  TYR A  71     -28.430  37.377  94.978  1.00 52.48           C  
ATOM    470  OH  TYR A  71     -29.420  38.097  95.621  1.00 54.03           O  
ATOM    471  N   PRO A  72     -25.946  36.298  90.212  1.00 37.28           N  
ATOM    472  CA  PRO A  72     -26.684  37.208  89.334  1.00 35.78           C  
ATOM    473  C   PRO A  72     -27.503  36.540  88.229  1.00 34.23           C  
ATOM    474  O   PRO A  72     -28.605  36.990  87.915  1.00 33.81           O  
ATOM    475  CB  PRO A  72     -25.596  38.147  88.797  1.00 38.47           C  
ATOM    476  CG  PRO A  72     -24.291  37.392  89.025  1.00 40.07           C  
ATOM    477  CD  PRO A  72     -24.527  36.688  90.323  1.00 39.72           C  
ATOM    478  N   ALA A  73     -26.997  35.450  87.659  1.00 33.03           N  
ATOM    479  CA  ALA A  73     -27.718  34.782  86.572  1.00 31.10           C  
ATOM    480  C   ALA A  73     -29.015  34.062  86.963  1.00 29.01           C  
ATOM    481  O   ALA A  73     -29.842  33.764  86.101  1.00 29.02           O  
ATOM    482  CB  ALA A  73     -26.788  33.815  85.861  1.00 28.48           C  
ATOM    483  N   LEU A  74     -29.210  33.795  88.251  1.00 28.55           N  
ATOM    484  CA  LEU A  74     -30.419  33.091  88.681  1.00 27.37           C  
ATOM    485  C   LEU A  74     -31.711  33.785  88.238  1.00 27.95           C  
ATOM    486  O   LEU A  74     -32.793  33.248  88.405  1.00 27.92           O  
ATOM    487  CB  LEU A  74     -30.423  32.890  90.210  1.00 25.22           C  
ATOM    488  CG  LEU A  74     -29.260  32.080  90.846  1.00 24.92           C  
ATOM    489  CD1 LEU A  74     -29.579  31.779  92.303  1.00 20.35           C  
ATOM    490  CD2 LEU A  74     -29.019  30.755  90.106  1.00 21.08           C  
ATOM    491  N   LYS A  75     -31.613  34.973  87.661  1.00 30.17           N  
ATOM    492  CA  LYS A  75     -32.822  35.670  87.234  1.00 33.53           C  
ATOM    493  C   LYS A  75     -33.043  35.457  85.747  1.00 33.98           C  
ATOM    494  O   LYS A  75     -34.143  35.664  85.246  1.00 34.66           O  
ATOM    495  CB  LYS A  75     -32.715  37.172  87.530  1.00 32.15           C  
ATOM    496  CG  LYS A  75     -31.543  37.860  86.858  1.00 31.73           C  
ATOM    497  CD  LYS A  75     -31.596  39.369  87.067  1.00 31.95           C  
ATOM    498  CE  LYS A  75     -30.431  40.088  86.364  1.00 33.39           C  
ATOM    499  NZ  LYS A  75     -29.111  39.864  87.033  1.00 33.13           N  
ATOM    500  N   TRP A  76     -31.995  35.042  85.042  1.00 34.40           N  
ATOM    501  CA  TRP A  76     -32.096  34.816  83.610  1.00 34.23           C  
ATOM    502  C   TRP A  76     -33.282  33.938  83.238  1.00 36.97           C  
ATOM    503  O   TRP A  76     -33.707  33.068  84.000  1.00 37.57           O  
ATOM    504  CB  TRP A  76     -30.826  34.156  83.071  1.00 35.26           C  
ATOM    505  CG  TRP A  76     -29.608  34.999  83.180  1.00 36.16           C  
ATOM    506  CD1 TRP A  76     -29.528  36.264  83.682  1.00 37.47           C  
ATOM    507  CD2 TRP A  76     -28.284  34.645  82.776  1.00 37.21           C  
ATOM    508  NE1 TRP A  76     -28.236  36.723  83.618  1.00 36.72           N  
ATOM    509  CE2 TRP A  76     -27.449  35.751  83.064  1.00 36.49           C  
ATOM    510  CE3 TRP A  76     -27.716  33.502  82.197  1.00 38.02           C  
ATOM    511  CZ2 TRP A  76     -26.074  35.748  82.792  1.00 36.38           C  
ATOM    512  CZ3 TRP A  76     -26.341  33.499  81.924  1.00 37.54           C  
ATOM    513  CH2 TRP A  76     -25.540  34.617  82.224  1.00 36.64           C  
ATOM    514  N   ASP A  77     -33.819  34.190  82.053  1.00 38.36           N  
ATOM    515  CA  ASP A  77     -34.919  33.417  81.498  1.00 40.17           C  
ATOM    516  C   ASP A  77     -34.990  33.870  80.043  1.00 41.47           C  
ATOM    517  O   ASP A  77     -34.349  34.858  79.670  1.00 42.31           O  
ATOM    518  CB  ASP A  77     -36.230  33.637  82.296  1.00 40.64           C  
ATOM    519  CG  ASP A  77     -36.943  34.945  81.975  1.00 42.49           C  
ATOM    520  OD1 ASP A  77     -36.398  35.793  81.227  1.00 44.35           O  
ATOM    521  OD2 ASP A  77     -38.075  35.118  82.494  1.00 43.14           O  
ATOM    522  N   LEU A  78     -35.720  33.146  79.210  1.00 43.72           N  
ATOM    523  CA  LEU A  78     -35.789  33.504  77.797  1.00 47.36           C  
ATOM    524  C   LEU A  78     -36.027  35.003  77.599  1.00 50.27           C  
ATOM    525  O   LEU A  78     -35.141  35.721  77.115  1.00 49.07           O  
ATOM    526  CB  LEU A  78     -36.884  32.691  77.103  1.00 48.63           C  
ATOM    527  CG  LEU A  78     -36.963  31.211  77.495  1.00 49.13           C  
ATOM    528  CD1 LEU A  78     -37.725  31.076  78.838  1.00 45.93           C  
ATOM    529  CD2 LEU A  78     -37.671  30.428  76.390  1.00 47.73           C  
ATOM    530  N   GLU A  79     -37.217  35.466  77.980  1.00 52.71           N  
ATOM    531  CA  GLU A  79     -37.584  36.875  77.860  1.00 54.77           C  
ATOM    532  C   GLU A  79     -36.399  37.779  78.160  1.00 53.33           C  
ATOM    533  O   GLU A  79     -35.921  38.508  77.283  1.00 54.34           O  
ATOM    534  CB  GLU A  79     -38.723  37.212  78.825  1.00 58.86           C  
ATOM    535  CG  GLU A  79     -38.970  38.709  78.986  1.00 65.40           C  
ATOM    536  CD  GLU A  79     -40.184  39.024  79.845  1.00 70.60           C  
ATOM    537  OE1 GLU A  79     -40.219  38.604  81.024  1.00 72.96           O  
ATOM    538  OE2 GLU A  79     -41.106  39.697  79.339  1.00 71.36           O  
ATOM    539  N   TYR A  80     -35.935  37.727  79.405  1.00 50.92           N  
ATOM    540  CA  TYR A  80     -34.799  38.529  79.840  1.00 49.79           C  
ATOM    541  C   TYR A  80     -33.643  38.415  78.856  1.00 51.55           C  
ATOM    542  O   TYR A  80     -33.197  39.410  78.288  1.00 51.83           O  
ATOM    543  CB  TYR A  80     -34.322  38.058  81.207  1.00 47.66           C  
ATOM    544  CG  TYR A  80     -33.223  38.901  81.809  1.00 44.32           C  
ATOM    545  CD1 TYR A  80     -33.525  39.963  82.672  1.00 42.80           C  
ATOM    546  CD2 TYR A  80     -31.877  38.620  81.550  1.00 41.21           C  
ATOM    547  CE1 TYR A  80     -32.511  40.720  83.269  1.00 42.83           C  
ATOM    548  CE2 TYR A  80     -30.855  39.368  82.139  1.00 41.01           C  
ATOM    549  CZ  TYR A  80     -31.179  40.412  82.999  1.00 42.78           C  
ATOM    550  OH  TYR A  80     -30.181  41.131  83.613  1.00 45.87           O  
ATOM    551  N   LEU A  81     -33.167  37.190  78.656  1.00 52.02           N  
ATOM    552  CA  LEU A  81     -32.051  36.928  77.756  1.00 53.44           C  
ATOM    553  C   LEU A  81     -32.178  37.492  76.339  1.00 54.18           C  
ATOM    554  O   LEU A  81     -31.247  38.138  75.851  1.00 54.55           O  
ATOM    555  CB  LEU A  81     -31.785  35.421  77.702  1.00 52.13           C  
ATOM    556  CG  LEU A  81     -31.099  34.882  78.964  1.00 52.36           C  
ATOM    557  CD1 LEU A  81     -31.293  33.383  79.098  1.00 51.27           C  
ATOM    558  CD2 LEU A  81     -29.628  35.242  78.904  1.00 52.21           C  
ATOM    559  N   GLN A  82     -33.305  37.257  75.669  1.00 56.74           N  
ATOM    560  CA  GLN A  82     -33.460  37.780  74.309  1.00 59.76           C  
ATOM    561  C   GLN A  82     -33.420  39.292  74.353  1.00 60.63           C  
ATOM    562  O   GLN A  82     -32.831  39.952  73.493  1.00 60.61           O  
ATOM    563  CB  GLN A  82     -34.789  37.364  73.680  1.00 60.13           C  
ATOM    564  CG  GLN A  82     -34.925  37.914  72.266  1.00 65.27           C  
ATOM    565  CD  GLN A  82     -36.278  37.651  71.636  1.00 69.13           C  
ATOM    566  OE1 GLN A  82     -36.755  36.514  71.604  1.00 70.44           O  
ATOM    567  NE2 GLN A  82     -36.898  38.704  71.112  1.00 70.48           N  
ATOM    568  N   GLU A  83     -34.066  39.822  75.379  1.00 61.67           N  
ATOM    569  CA  GLU A  83     -34.160  41.246  75.596  1.00 61.70           C  
ATOM    570  C   GLU A  83     -32.811  41.927  75.854  1.00 61.12           C  
ATOM    571  O   GLU A  83     -32.582  43.040  75.382  1.00 61.69           O  
ATOM    572  CB  GLU A  83     -35.103  41.488  76.771  1.00 64.38           C  
ATOM    573  CG  GLU A  83     -35.364  42.942  77.106  1.00 69.01           C  
ATOM    574  CD  GLU A  83     -36.128  43.092  78.416  1.00 72.64           C  
ATOM    575  OE1 GLU A  83     -35.530  42.850  79.495  1.00 71.90           O  
ATOM    576  OE2 GLU A  83     -37.330  43.439  78.362  1.00 72.96           O  
ATOM    577  N   ASN A  84     -31.908  41.263  76.571  1.00 60.34           N  
ATOM    578  CA  ASN A  84     -30.627  41.884  76.905  1.00 60.38           C  
ATOM    579  C   ASN A  84     -29.352  41.339  76.273  1.00 60.09           C  
ATOM    580  O   ASN A  84     -28.251  41.674  76.710  1.00 57.57           O  
ATOM    581  CB  ASN A  84     -30.464  41.903  78.422  1.00 61.55           C  
ATOM    582  CG  ASN A  84     -31.649  42.538  79.119  1.00 63.45           C  
ATOM    583  OD1 ASN A  84     -31.933  43.723  78.930  1.00 64.90           O  
ATOM    584  ND2 ASN A  84     -32.357  41.751  79.922  1.00 64.71           N  
ATOM    585  N   ILE A  85     -29.484  40.501  75.256  1.00 60.96           N  
ATOM    586  CA  ILE A  85     -28.303  39.972  74.594  1.00 62.40           C  
ATOM    587  C   ILE A  85     -28.206  40.519  73.175  1.00 64.74           C  
ATOM    588  O   ILE A  85     -29.214  40.628  72.464  1.00 64.55           O  
ATOM    589  CB  ILE A  85     -28.321  38.444  74.503  1.00 59.56           C  
ATOM    590  CG1 ILE A  85     -28.172  37.830  75.887  1.00 59.78           C  
ATOM    591  CG2 ILE A  85     -27.184  37.979  73.617  1.00 61.35           C  
ATOM    592  CD1 ILE A  85     -28.064  36.319  75.862  1.00 57.94           C  
ATOM    593  N   GLY A  86     -26.986  40.857  72.767  1.00 67.17           N  
ATOM    594  CA  GLY A  86     -26.777  41.381  71.432  1.00 69.79           C  
ATOM    595  C   GLY A  86     -27.244  40.388  70.386  1.00 71.41           C  
ATOM    596  O   GLY A  86     -27.562  39.240  70.704  1.00 71.30           O  
ATOM    597  N   ASN A  87     -27.299  40.842  69.137  1.00 72.96           N  
ATOM    598  CA  ASN A  87     -27.709  40.002  68.015  1.00 72.91           C  
ATOM    599  C   ASN A  87     -26.958  38.695  68.186  1.00 72.94           C  
ATOM    600  O   ASN A  87     -27.545  37.663  68.514  1.00 72.96           O  
ATOM    601  CB  ASN A  87     -27.283  40.653  66.701  1.00 72.55           C  
ATOM    602  CG  ASN A  87     -27.494  42.155  66.702  1.00 72.96           C  
ATOM    603  OD1 ASN A  87     -28.619  42.639  66.539  1.00 72.96           O  
ATOM    604  ND2 ASN A  87     -26.410  42.905  66.905  1.00 72.96           N  
ATOM    605  N   GLY A  88     -25.647  38.775  67.968  1.00 72.96           N  
ATOM    606  CA  GLY A  88     -24.757  37.636  68.102  1.00 72.05           C  
ATOM    607  C   GLY A  88     -25.229  36.331  67.500  1.00 71.26           C  
ATOM    608  O   GLY A  88     -26.425  36.071  67.370  1.00 72.13           O  
ATOM    609  N   ASP A  89     -24.278  35.500  67.107  1.00 70.67           N  
ATOM    610  CA  ASP A  89     -24.630  34.204  66.553  1.00 69.52           C  
ATOM    611  C   ASP A  89     -24.664  33.211  67.707  1.00 67.20           C  
ATOM    612  O   ASP A  89     -23.810  33.242  68.595  1.00 66.93           O  
ATOM    613  CB  ASP A  89     -23.605  33.757  65.505  1.00 71.55           C  
ATOM    614  CG  ASP A  89     -23.735  34.519  64.198  1.00 72.96           C  
ATOM    615  OD1 ASP A  89     -24.860  34.567  63.642  1.00 72.96           O  
ATOM    616  OD2 ASP A  89     -22.710  35.061  63.728  1.00 72.96           O  
ATOM    617  N   PHE A  90     -25.662  32.339  67.707  1.00 63.32           N  
ATOM    618  CA  PHE A  90     -25.776  31.347  68.764  1.00 59.28           C  
ATOM    619  C   PHE A  90     -25.910  29.930  68.216  1.00 57.34           C  
ATOM    620  O   PHE A  90     -26.948  29.567  67.660  1.00 56.87           O  
ATOM    621  CB  PHE A  90     -26.976  31.659  69.670  1.00 58.58           C  
ATOM    622  CG  PHE A  90     -26.825  32.925  70.464  1.00 54.43           C  
ATOM    623  CD1 PHE A  90     -27.412  34.110  70.033  1.00 52.78           C  
ATOM    624  CD2 PHE A  90     -26.068  32.942  71.630  1.00 53.09           C  
ATOM    625  CE1 PHE A  90     -27.245  35.291  70.755  1.00 49.84           C  
ATOM    626  CE2 PHE A  90     -25.895  34.121  72.356  1.00 49.74           C  
ATOM    627  CZ  PHE A  90     -26.483  35.292  71.915  1.00 48.86           C  
ATOM    628  N   SER A  91     -24.860  29.128  68.370  1.00 53.54           N  
ATOM    629  CA  SER A  91     -24.918  27.755  67.895  1.00 50.84           C  
ATOM    630  C   SER A  91     -26.131  27.091  68.531  1.00 48.31           C  
ATOM    631  O   SER A  91     -26.268  27.055  69.753  1.00 48.31           O  
ATOM    632  CB  SER A  91     -23.652  26.985  68.283  1.00 49.63           C  
ATOM    633  OG  SER A  91     -22.512  27.533  67.652  1.00 49.54           O  
ATOM    634  N   VAL A  92     -27.034  26.596  67.700  1.00 45.18           N  
ATOM    635  CA  VAL A  92     -28.203  25.927  68.222  1.00 43.19           C  
ATOM    636  C   VAL A  92     -28.234  24.519  67.654  1.00 45.19           C  
ATOM    637  O   VAL A  92     -28.501  24.309  66.467  1.00 44.63           O  
ATOM    638  CB  VAL A  92     -29.492  26.681  67.869  1.00 39.53           C  
ATOM    639  CG1 VAL A  92     -30.704  25.910  68.365  1.00 38.64           C  
ATOM    640  CG2 VAL A  92     -29.468  28.055  68.516  1.00 39.21           C  
ATOM    641  N   TYR A  93     -27.919  23.555  68.512  1.00 46.74           N  
ATOM    642  CA  TYR A  93     -27.909  22.162  68.109  1.00 47.94           C  
ATOM    643  C   TYR A  93     -29.340  21.657  68.120  1.00 49.08           C  
ATOM    644  O   TYR A  93     -30.143  22.059  68.966  1.00 49.54           O  
ATOM    645  CB  TYR A  93     -27.030  21.335  69.059  1.00 48.15           C  
ATOM    646  CG  TYR A  93     -25.569  21.740  69.027  1.00 50.27           C  
ATOM    647  CD1 TYR A  93     -25.137  22.920  69.636  1.00 49.93           C  
ATOM    648  CD2 TYR A  93     -24.631  20.978  68.328  1.00 50.98           C  
ATOM    649  CE1 TYR A  93     -23.807  23.336  69.545  1.00 53.57           C  
ATOM    650  CE2 TYR A  93     -23.297  21.385  68.229  1.00 53.62           C  
ATOM    651  CZ  TYR A  93     -22.894  22.564  68.835  1.00 54.40           C  
ATOM    652  OH  TYR A  93     -21.590  22.983  68.704  1.00 54.41           O  
ATOM    653  N   SER A  94     -29.658  20.791  67.164  1.00 50.89           N  
ATOM    654  CA  SER A  94     -30.993  20.227  67.057  1.00 52.52           C  
ATOM    655  C   SER A  94     -30.897  18.728  66.852  1.00 53.82           C  
ATOM    656  O   SER A  94     -29.967  18.236  66.207  1.00 53.73           O  
ATOM    657  CB  SER A  94     -31.739  20.859  65.885  1.00 52.39           C  
ATOM    658  OG  SER A  94     -31.028  20.661  64.678  1.00 53.15           O  
ATOM    659  N   ALA A  95     -31.868  18.017  67.414  1.00 55.06           N  
ATOM    660  CA  ALA A  95     -31.948  16.566  67.331  1.00 55.01           C  
ATOM    661  C   ALA A  95     -33.374  16.223  66.922  1.00 55.74           C  
ATOM    662  O   ALA A  95     -34.252  17.087  66.954  1.00 57.44           O  
ATOM    663  CB  ALA A  95     -31.633  15.953  68.686  1.00 54.22           C  
ATOM    664  N   SER A  96     -33.610  14.974  66.538  1.00 55.39           N  
ATOM    665  CA  SER A  96     -34.944  14.563  66.140  1.00 54.61           C  
ATOM    666  C   SER A  96     -35.666  13.906  67.316  1.00 53.39           C  
ATOM    667  O   SER A  96     -36.852  13.589  67.224  1.00 53.35           O  
ATOM    668  CB  SER A  96     -34.871  13.584  64.972  1.00 56.28           C  
ATOM    669  OG  SER A  96     -34.476  12.299  65.417  1.00 61.13           O  
ATOM    670  N   THR A  97     -34.942  13.690  68.412  1.00 51.12           N  
ATOM    671  CA  THR A  97     -35.506  13.082  69.618  1.00 48.55           C  
ATOM    672  C   THR A  97     -34.777  13.623  70.840  1.00 48.56           C  
ATOM    673  O   THR A  97     -33.996  14.562  70.732  1.00 49.74           O  
ATOM    674  CB  THR A  97     -35.361  11.551  69.621  1.00 49.70           C  
ATOM    675  OG1 THR A  97     -33.972  11.203  69.630  1.00 47.70           O  
ATOM    676  CG2 THR A  97     -36.032  10.949  68.394  1.00 48.11           C  
ATOM    677  N   HIS A  98     -35.016  13.019  71.998  1.00 47.57           N  
ATOM    678  CA  HIS A  98     -34.385  13.468  73.233  1.00 48.67           C  
ATOM    679  C   HIS A  98     -32.849  13.325  73.247  1.00 49.00           C  
ATOM    680  O   HIS A  98     -32.150  14.172  73.827  1.00 48.71           O  
ATOM    681  CB  HIS A  98     -34.987  12.713  74.423  1.00 49.22           C  
ATOM    682  CG  HIS A  98     -34.699  11.244  74.410  1.00 53.18           C  
ATOM    683  ND1 HIS A  98     -35.155  10.403  73.416  1.00 54.40           N  
ATOM    684  CD2 HIS A  98     -33.964  10.472  75.247  1.00 54.11           C  
ATOM    685  CE1 HIS A  98     -34.709   9.179  73.639  1.00 53.99           C  
ATOM    686  NE2 HIS A  98     -33.984   9.194  74.743  1.00 54.05           N  
ATOM    687  N   LYS A  99     -32.323  12.267  72.620  1.00 47.68           N  
ATOM    688  CA  LYS A  99     -30.872  12.036  72.589  1.00 46.47           C  
ATOM    689  C   LYS A  99     -30.137  12.968  71.648  1.00 44.17           C  
ATOM    690  O   LYS A  99     -30.403  12.975  70.453  1.00 45.13           O  
ATOM    691  CB  LYS A  99     -30.543  10.600  72.156  1.00 48.16           C  
ATOM    692  CG  LYS A  99     -30.324   9.587  73.272  1.00 51.33           C  
ATOM    693  CD  LYS A  99     -29.971   8.218  72.688  1.00 56.11           C  
ATOM    694  CE  LYS A  99     -31.056   7.741  71.711  1.00 60.99           C  
ATOM    695  NZ  LYS A  99     -30.685   6.521  70.929  1.00 63.13           N  
ATOM    696  N   PHE A 100     -29.208  13.748  72.184  1.00 43.43           N  
ATOM    697  CA  PHE A 100     -28.417  14.642  71.355  1.00 43.35           C  
ATOM    698  C   PHE A 100     -27.125  13.941  71.007  1.00 43.91           C  
ATOM    699  O   PHE A 100     -26.291  13.679  71.875  1.00 43.01           O  
ATOM    700  CB  PHE A 100     -28.124  15.950  72.079  1.00 44.27           C  
ATOM    701  CG  PHE A 100     -29.246  16.936  71.993  1.00 45.13           C  
ATOM    702  CD1 PHE A 100     -30.399  16.766  72.755  1.00 45.58           C  
ATOM    703  CD2 PHE A 100     -29.179  18.000  71.099  1.00 44.26           C  
ATOM    704  CE1 PHE A 100     -31.470  17.637  72.626  1.00 46.69           C  
ATOM    705  CE2 PHE A 100     -30.242  18.876  70.962  1.00 46.91           C  
ATOM    706  CZ  PHE A 100     -31.394  18.695  71.728  1.00 47.52           C  
ATOM    707  N   LEU A 101     -26.970  13.648  69.720  1.00 45.33           N  
ATOM    708  CA  LEU A 101     -25.804  12.936  69.204  1.00 46.09           C  
ATOM    709  C   LEU A 101     -24.712  13.857  68.657  1.00 45.63           C  
ATOM    710  O   LEU A 101     -24.567  13.984  67.439  1.00 44.91           O  
ATOM    711  CB  LEU A 101     -26.263  11.980  68.099  1.00 47.27           C  
ATOM    712  CG  LEU A 101     -27.445  11.063  68.456  1.00 52.94           C  
ATOM    713  CD1 LEU A 101     -28.062  10.484  67.183  1.00 56.00           C  
ATOM    714  CD2 LEU A 101     -26.983   9.954  69.398  1.00 54.32           C  
ATOM    715  N   TYR A 102     -23.935  14.484  69.539  1.00 45.80           N  
ATOM    716  CA  TYR A 102     -22.871  15.376  69.082  1.00 45.47           C  
ATOM    717  C   TYR A 102     -21.780  14.566  68.402  1.00 46.04           C  
ATOM    718  O   TYR A 102     -21.657  13.372  68.633  1.00 45.83           O  
ATOM    719  CB  TYR A 102     -22.244  16.146  70.242  1.00 48.15           C  
ATOM    720  CG  TYR A 102     -23.210  16.937  71.086  1.00 53.26           C  
ATOM    721  CD1 TYR A 102     -23.899  16.333  72.140  1.00 57.10           C  
ATOM    722  CD2 TYR A 102     -23.413  18.297  70.858  1.00 54.93           C  
ATOM    723  CE1 TYR A 102     -24.762  17.072  72.952  1.00 60.62           C  
ATOM    724  CE2 TYR A 102     -24.272  19.041  71.659  1.00 59.06           C  
ATOM    725  CZ  TYR A 102     -24.940  18.424  72.706  1.00 60.65           C  
ATOM    726  OH  TYR A 102     -25.763  19.162  73.525  1.00 64.63           O  
ATOM    727  N   TYR A 103     -20.982  15.221  67.567  1.00 47.35           N  
ATOM    728  CA  TYR A 103     -19.899  14.540  66.876  1.00 46.88           C  
ATOM    729  C   TYR A 103     -18.817  15.507  66.402  1.00 47.04           C  
ATOM    730  O   TYR A 103     -19.075  16.683  66.137  1.00 46.35           O  
ATOM    731  CB  TYR A 103     -20.452  13.756  65.694  1.00 50.26           C  
ATOM    732  CG  TYR A 103     -20.933  14.627  64.569  1.00 54.32           C  
ATOM    733  CD1 TYR A 103     -20.045  15.093  63.604  1.00 57.02           C  
ATOM    734  CD2 TYR A 103     -22.275  14.987  64.466  1.00 55.78           C  
ATOM    735  CE1 TYR A 103     -20.481  15.893  62.561  1.00 59.89           C  
ATOM    736  CE2 TYR A 103     -22.720  15.789  63.430  1.00 58.39           C  
ATOM    737  CZ  TYR A 103     -21.817  16.236  62.479  1.00 59.78           C  
ATOM    738  OH  TYR A 103     -22.242  17.024  61.437  1.00 61.73           O  
ATOM    739  N   ASP A 104     -17.599  14.987  66.311  1.00 45.90           N  
ATOM    740  CA  ASP A 104     -16.437  15.746  65.880  1.00 44.18           C  
ATOM    741  C   ASP A 104     -16.296  15.592  64.372  1.00 45.73           C  
ATOM    742  O   ASP A 104     -15.950  14.517  63.880  1.00 45.24           O  
ATOM    743  CB  ASP A 104     -15.197  15.197  66.584  1.00 43.26           C  
ATOM    744  CG  ASP A 104     -13.904  15.716  65.993  1.00 41.99           C  
ATOM    745  OD1 ASP A 104     -13.802  15.801  64.752  1.00 43.35           O  
ATOM    746  OD2 ASP A 104     -12.970  16.018  66.768  1.00 41.26           O  
ATOM    747  N   GLU A 105     -16.555  16.670  63.641  1.00 46.64           N  
ATOM    748  CA  GLU A 105     -16.453  16.646  62.184  1.00 48.81           C  
ATOM    749  C   GLU A 105     -15.060  16.252  61.687  1.00 45.50           C  
ATOM    750  O   GLU A 105     -14.929  15.443  60.770  1.00 46.94           O  
ATOM    751  CB  GLU A 105     -16.827  18.017  61.609  1.00 52.36           C  
ATOM    752  CG  GLU A 105     -18.239  18.466  61.961  1.00 59.74           C  
ATOM    753  CD  GLU A 105     -18.670  19.688  61.171  1.00 65.21           C  
ATOM    754  OE1 GLU A 105     -18.559  19.646  59.923  1.00 68.63           O  
ATOM    755  OE2 GLU A 105     -19.120  20.680  61.794  1.00 67.71           O  
ATOM    756  N   LYS A 106     -14.027  16.821  62.296  1.00 42.60           N  
ATOM    757  CA  LYS A 106     -12.652  16.538  61.899  1.00 41.33           C  
ATOM    758  C   LYS A 106     -12.302  15.063  61.759  1.00 40.74           C  
ATOM    759  O   LYS A 106     -11.223  14.740  61.257  1.00 39.93           O  
ATOM    760  CB  LYS A 106     -11.670  17.187  62.884  1.00 42.56           C  
ATOM    761  CG  LYS A 106     -11.722  18.692  62.860  1.00 44.13           C  
ATOM    762  CD  LYS A 106     -11.038  19.326  64.056  1.00 47.17           C  
ATOM    763  CE  LYS A 106     -11.344  20.833  64.081  1.00 49.77           C  
ATOM    764  NZ  LYS A 106     -11.118  21.473  62.737  1.00 51.31           N  
ATOM    765  N   LYS A 107     -13.186  14.169  62.201  1.00 39.26           N  
ATOM    766  CA  LYS A 107     -12.898  12.738  62.108  1.00 38.67           C  
ATOM    767  C   LYS A 107     -13.914  11.977  61.259  1.00 40.73           C  
ATOM    768  O   LYS A 107     -14.078  10.762  61.408  1.00 42.86           O  
ATOM    769  CB  LYS A 107     -12.839  12.108  63.510  1.00 34.16           C  
ATOM    770  CG  LYS A 107     -11.753  12.646  64.418  1.00 26.63           C  
ATOM    771  CD  LYS A 107     -11.745  11.932  65.762  1.00 21.97           C  
ATOM    772  CE  LYS A 107     -10.774  12.601  66.731  1.00 20.48           C  
ATOM    773  NZ  LYS A 107     -10.799  12.058  68.125  1.00 22.48           N  
HETATM  774  N   MSE A 108     -14.602  12.677  60.368  1.00 42.12           N  
HETATM  775  CA  MSE A 108     -15.582  12.004  59.530  1.00 44.69           C  
HETATM  776  C   MSE A 108     -14.917  11.290  58.365  1.00 44.42           C  
HETATM  777  O   MSE A 108     -15.493  10.383  57.768  1.00 45.30           O  
HETATM  778  CB  MSE A 108     -16.611  13.003  59.011  1.00 46.42           C  
HETATM  779  CG  MSE A 108     -17.539  13.531  60.087  1.00 48.44           C  
HETATM  780 SE   MSE A 108     -18.990  14.634  59.381  1.00 67.24          SE  
HETATM  781  CE  MSE A 108     -20.363  13.278  59.151  1.00 43.58           C  
ATOM    782  N   ALA A 109     -13.702  11.703  58.039  1.00 46.11           N  
ATOM    783  CA  ALA A 109     -12.980  11.079  56.944  1.00 48.69           C  
ATOM    784  C   ALA A 109     -12.701   9.615  57.283  1.00 49.67           C  
ATOM    785  O   ALA A 109     -12.900   8.731  56.451  1.00 50.85           O  
ATOM    786  CB  ALA A 109     -11.679  11.821  56.694  1.00 46.77           C  
ATOM    787  N   ASN A 110     -12.264   9.366  58.518  1.00 52.39           N  
ATOM    788  CA  ASN A 110     -11.939   8.010  58.984  1.00 53.51           C  
ATOM    789  C   ASN A 110     -13.107   7.020  58.992  1.00 53.78           C  
ATOM    790  O   ASN A 110     -12.894   5.802  59.040  1.00 53.59           O  
ATOM    791  CB  ASN A 110     -11.353   8.055  60.397  1.00 51.64           C  
ATOM    792  CG  ASN A 110     -10.248   9.065  60.531  1.00 51.48           C  
ATOM    793  OD1 ASN A 110      -9.409   9.200  59.637  1.00 53.80           O  
ATOM    794  ND2 ASN A 110     -10.229   9.780  61.655  1.00 49.77           N  
ATOM    795  N   PHE A 111     -14.332   7.531  58.975  1.00 54.50           N  
ATOM    796  CA  PHE A 111     -15.491   6.656  58.985  1.00 56.29           C  
ATOM    797  C   PHE A 111     -16.539   7.149  58.014  1.00 60.29           C  
ATOM    798  O   PHE A 111     -17.669   7.428  58.391  1.00 60.86           O  
ATOM    799  CB  PHE A 111     -16.072   6.566  60.395  1.00 52.25           C  
ATOM    800  CG  PHE A 111     -15.216   5.784  61.353  1.00 45.05           C  
ATOM    801  CD1 PHE A 111     -14.044   6.329  61.876  1.00 42.34           C  
ATOM    802  CD2 PHE A 111     -15.571   4.494  61.718  1.00 39.63           C  
ATOM    803  CE1 PHE A 111     -13.239   5.597  62.752  1.00 39.75           C  
ATOM    804  CE2 PHE A 111     -14.782   3.757  62.586  1.00 39.24           C  
ATOM    805  CZ  PHE A 111     -13.607   4.310  63.106  1.00 40.39           C  
ATOM    806  N   GLN A 112     -16.141   7.232  56.751  1.00 64.08           N  
ATOM    807  CA  GLN A 112     -16.985   7.714  55.663  1.00 67.43           C  
ATOM    808  C   GLN A 112     -18.442   7.253  55.627  1.00 67.73           C  
ATOM    809  O   GLN A 112     -19.269   7.873  54.959  1.00 68.64           O  
ATOM    810  CB  GLN A 112     -16.291   7.409  54.333  1.00 68.81           C  
ATOM    811  CG  GLN A 112     -15.043   8.267  54.129  1.00 71.62           C  
ATOM    812  CD  GLN A 112     -14.103   7.740  53.055  1.00 72.96           C  
ATOM    813  OE1 GLN A 112     -14.517   7.468  51.925  1.00 72.96           O  
ATOM    814  NE2 GLN A 112     -12.824   7.606  53.403  1.00 72.83           N  
ATOM    815  N   ASN A 113     -18.765   6.184  56.348  1.00 66.89           N  
ATOM    816  CA  ASN A 113     -20.138   5.693  56.377  1.00 66.29           C  
ATOM    817  C   ASN A 113     -20.888   6.172  57.618  1.00 64.81           C  
ATOM    818  O   ASN A 113     -21.974   5.682  57.939  1.00 63.52           O  
ATOM    819  CB  ASN A 113     -20.145   4.167  56.311  1.00 68.88           C  
ATOM    820  CG  ASN A 113     -19.754   3.648  54.940  1.00 72.14           C  
ATOM    821  OD1 ASN A 113     -20.527   3.739  53.983  1.00 72.96           O  
ATOM    822  ND2 ASN A 113     -18.542   3.111  54.834  1.00 72.96           N  
ATOM    823  N   PHE A 114     -20.296   7.136  58.314  1.00 62.03           N  
ATOM    824  CA  PHE A 114     -20.906   7.699  59.509  1.00 60.36           C  
ATOM    825  C   PHE A 114     -21.887   8.780  59.096  1.00 61.90           C  
ATOM    826  O   PHE A 114     -21.501   9.773  58.472  1.00 62.30           O  
ATOM    827  CB  PHE A 114     -19.839   8.310  60.422  1.00 55.19           C  
ATOM    828  CG  PHE A 114     -20.401   9.136  61.557  1.00 51.68           C  
ATOM    829  CD1 PHE A 114     -21.126   8.536  62.588  1.00 48.35           C  
ATOM    830  CD2 PHE A 114     -20.196  10.517  61.597  1.00 49.99           C  
ATOM    831  CE1 PHE A 114     -21.634   9.301  63.638  1.00 48.50           C  
ATOM    832  CE2 PHE A 114     -20.701  11.292  62.643  1.00 49.26           C  
ATOM    833  CZ  PHE A 114     -21.421  10.686  63.665  1.00 48.98           C  
ATOM    834  N   LYS A 115     -23.157   8.580  59.427  1.00 63.19           N  
ATOM    835  CA  LYS A 115     -24.163   9.578  59.104  1.00 64.14           C  
ATOM    836  C   LYS A 115     -24.567  10.328  60.377  1.00 64.34           C  
ATOM    837  O   LYS A 115     -25.085   9.740  61.334  1.00 63.28           O  
ATOM    838  CB  LYS A 115     -25.376   8.929  58.417  1.00 64.75           C  
ATOM    839  CG  LYS A 115     -25.124   8.633  56.936  1.00 69.20           C  
ATOM    840  CD  LYS A 115     -26.349   8.068  56.210  1.00 72.69           C  
ATOM    841  CE  LYS A 115     -26.459   6.548  56.335  1.00 72.96           C  
ATOM    842  NZ  LYS A 115     -27.603   5.998  55.530  1.00 72.96           N  
ATOM    843  N   PRO A 116     -24.299  11.645  60.407  1.00 65.78           N  
ATOM    844  CA  PRO A 116     -24.607  12.531  61.531  1.00 66.71           C  
ATOM    845  C   PRO A 116     -26.103  12.687  61.799  1.00 68.71           C  
ATOM    846  O   PRO A 116     -26.911  12.795  60.871  1.00 68.61           O  
ATOM    847  CB  PRO A 116     -23.942  13.842  61.121  1.00 67.13           C  
ATOM    848  CG  PRO A 116     -24.046  13.821  59.638  1.00 66.27           C  
ATOM    849  CD  PRO A 116     -23.662  12.400  59.314  1.00 66.44           C  
ATOM    850  N   ARG A 117     -26.455  12.702  63.082  1.00 69.83           N  
ATOM    851  CA  ARG A 117     -27.843  12.833  63.517  1.00 70.67           C  
ATOM    852  C   ARG A 117     -28.042  13.997  64.500  1.00 69.71           C  
ATOM    853  O   ARG A 117     -28.866  13.930  65.418  1.00 68.71           O  
ATOM    854  CB  ARG A 117     -28.298  11.507  64.138  1.00 71.36           C  
ATOM    855  CG  ARG A 117     -28.523  10.418  63.098  1.00 72.61           C  
ATOM    856  CD  ARG A 117     -28.355   9.017  63.670  1.00 72.96           C  
ATOM    857  NE  ARG A 117     -28.741   7.998  62.692  1.00 72.96           N  
ATOM    858  CZ  ARG A 117     -28.412   6.710  62.765  1.00 72.96           C  
ATOM    859  NH1 ARG A 117     -27.677   6.264  63.777  1.00 72.96           N  
ATOM    860  NH2 ARG A 117     -28.822   5.864  61.822  1.00 72.96           N  
ATOM    861  N   SER A 118     -27.285  15.068  64.285  1.00 69.08           N  
ATOM    862  CA  SER A 118     -27.362  16.248  65.136  1.00 68.31           C  
ATOM    863  C   SER A 118     -26.869  17.469  64.374  1.00 67.53           C  
ATOM    864  O   SER A 118     -25.680  17.785  64.391  1.00 68.48           O  
ATOM    865  CB  SER A 118     -26.501  16.062  66.386  1.00 68.89           C  
ATOM    866  OG  SER A 118     -25.123  16.032  66.050  1.00 69.30           O  
ATOM    867  N   ASN A 119     -27.783  18.160  63.708  1.00 66.29           N  
ATOM    868  CA  ASN A 119     -27.403  19.342  62.952  1.00 66.46           C  
ATOM    869  C   ASN A 119     -27.188  20.515  63.911  1.00 65.37           C  
ATOM    870  O   ASN A 119     -27.838  20.604  64.953  1.00 65.64           O  
ATOM    871  CB  ASN A 119     -28.500  19.691  61.932  1.00 66.29           C  
ATOM    872  CG  ASN A 119     -28.881  18.506  61.045  1.00 69.05           C  
ATOM    873  OD1 ASN A 119     -29.346  17.466  61.529  1.00 70.44           O  
ATOM    874  ND2 ASN A 119     -28.688  18.663  59.739  1.00 71.45           N  
ATOM    875  N   ARG A 120     -26.257  21.395  63.564  1.00 64.21           N  
ATOM    876  CA  ARG A 120     -25.975  22.579  64.362  1.00 63.12           C  
ATOM    877  C   ARG A 120     -26.225  23.789  63.473  1.00 63.84           C  
ATOM    878  O   ARG A 120     -25.573  23.949  62.443  1.00 63.42           O  
ATOM    879  CB  ARG A 120     -24.517  22.587  64.829  1.00 63.52           C  
ATOM    880  CG  ARG A 120     -23.916  23.983  64.922  1.00 66.83           C  
ATOM    881  CD  ARG A 120     -22.486  23.980  65.431  1.00 69.68           C  
ATOM    882  NE  ARG A 120     -21.795  25.213  65.055  1.00 72.96           N  
ATOM    883  CZ  ARG A 120     -21.263  25.437  63.853  1.00 72.96           C  
ATOM    884  NH1 ARG A 120     -21.334  24.505  62.911  1.00 72.87           N  
ATOM    885  NH2 ARG A 120     -20.672  26.597  63.586  1.00 72.96           N  
ATOM    886  N   GLU A 121     -27.170  24.638  63.848  1.00 64.26           N  
ATOM    887  CA  GLU A 121     -27.430  25.809  63.029  1.00 65.99           C  
ATOM    888  C   GLU A 121     -27.150  27.107  63.770  1.00 66.29           C  
ATOM    889  O   GLU A 121     -27.533  27.275  64.926  1.00 66.65           O  
ATOM    890  CB  GLU A 121     -28.871  25.814  62.518  1.00 66.55           C  
ATOM    891  CG  GLU A 121     -29.157  27.002  61.613  1.00 70.04           C  
ATOM    892  CD  GLU A 121     -30.595  27.060  61.133  1.00 72.88           C  
ATOM    893  OE1 GLU A 121     -30.940  28.029  60.415  1.00 72.96           O  
ATOM    894  OE2 GLU A 121     -31.378  26.141  61.472  1.00 72.96           O  
ATOM    895  N   GLU A 122     -26.465  28.021  63.094  1.00 66.73           N  
ATOM    896  CA  GLU A 122     -26.138  29.314  63.672  1.00 66.11           C  
ATOM    897  C   GLU A 122     -27.362  30.206  63.502  1.00 65.73           C  
ATOM    898  O   GLU A 122     -27.973  30.234  62.431  1.00 65.58           O  
ATOM    899  CB  GLU A 122     -24.947  29.923  62.935  1.00 67.36           C  
ATOM    900  CG  GLU A 122     -23.894  30.528  63.839  1.00 67.42           C  
ATOM    901  CD  GLU A 122     -23.460  29.570  64.931  1.00 67.60           C  
ATOM    902  OE1 GLU A 122     -23.389  28.347  64.668  1.00 68.25           O  
ATOM    903  OE2 GLU A 122     -23.182  30.043  66.053  1.00 68.54           O  
HETATM  904  N   MSE A 123     -27.734  30.923  64.555  1.00 64.62           N  
HETATM  905  CA  MSE A 123     -28.888  31.804  64.471  1.00 65.41           C  
HETATM  906  C   MSE A 123     -28.875  32.853  65.570  1.00 64.32           C  
HETATM  907  O   MSE A 123     -28.102  32.760  66.525  1.00 64.67           O  
HETATM  908  CB  MSE A 123     -30.190  30.990  64.513  1.00 66.52           C  
HETATM  909  CG  MSE A 123     -30.590  30.428  65.868  1.00 68.06           C  
HETATM  910 SE   MSE A 123     -32.017  29.096  65.697  1.00 72.95          SE  
HETATM  911  CE  MSE A 123     -33.158  30.017  64.424  1.00 69.73           C  
ATOM    912  N   LYS A 124     -29.723  33.863  65.422  1.00 63.48           N  
ATOM    913  CA  LYS A 124     -29.795  34.939  66.399  1.00 62.44           C  
ATOM    914  C   LYS A 124     -30.740  34.531  67.519  1.00 59.85           C  
ATOM    915  O   LYS A 124     -31.816  33.983  67.269  1.00 58.69           O  
ATOM    916  CB  LYS A 124     -30.247  36.226  65.701  1.00 64.66           C  
ATOM    917  CG  LYS A 124     -29.432  36.491  64.434  1.00 67.67           C  
ATOM    918  CD  LYS A 124     -29.651  37.871  63.869  1.00 70.35           C  
ATOM    919  CE  LYS A 124     -29.001  38.924  64.746  1.00 72.53           C  
ATOM    920  NZ  LYS A 124     -29.166  40.301  64.184  1.00 72.96           N  
ATOM    921  N   PHE A 125     -30.323  34.797  68.754  1.00 57.63           N  
ATOM    922  CA  PHE A 125     -31.095  34.413  69.928  1.00 56.07           C  
ATOM    923  C   PHE A 125     -32.614  34.363  69.772  1.00 57.68           C  
ATOM    924  O   PHE A 125     -33.229  33.325  70.040  1.00 57.95           O  
ATOM    925  CB  PHE A 125     -30.757  35.301  71.121  1.00 52.14           C  
ATOM    926  CG  PHE A 125     -31.164  34.704  72.428  1.00 48.55           C  
ATOM    927  CD1 PHE A 125     -30.266  33.927  73.162  1.00 46.83           C  
ATOM    928  CD2 PHE A 125     -32.472  34.840  72.895  1.00 47.34           C  
ATOM    929  CE1 PHE A 125     -30.663  33.286  74.345  1.00 44.74           C  
ATOM    930  CE2 PHE A 125     -32.882  34.203  74.078  1.00 46.59           C  
ATOM    931  CZ  PHE A 125     -31.972  33.423  74.803  1.00 45.19           C  
ATOM    932  N   HIS A 126     -33.224  35.469  69.353  1.00 58.12           N  
ATOM    933  CA  HIS A 126     -34.677  35.494  69.204  1.00 59.41           C  
ATOM    934  C   HIS A 126     -35.163  34.386  68.270  1.00 59.87           C  
ATOM    935  O   HIS A 126     -36.172  33.732  68.543  1.00 59.05           O  
ATOM    936  CB  HIS A 126     -35.150  36.872  68.706  1.00 60.11           C  
ATOM    937  CG  HIS A 126     -34.809  37.165  67.276  1.00 60.37           C  
ATOM    938  ND1 HIS A 126     -35.731  37.065  66.256  1.00 59.80           N  
ATOM    939  CD2 HIS A 126     -33.649  37.555  66.697  1.00 61.43           C  
ATOM    940  CE1 HIS A 126     -35.154  37.381  65.110  1.00 60.11           C  
ATOM    941  NE2 HIS A 126     -33.890  37.682  65.350  1.00 61.33           N  
ATOM    942  N   GLU A 127     -34.439  34.167  67.177  1.00 60.28           N  
ATOM    943  CA  GLU A 127     -34.814  33.131  66.225  1.00 61.05           C  
ATOM    944  C   GLU A 127     -34.912  31.805  66.978  1.00 61.01           C  
ATOM    945  O   GLU A 127     -35.840  31.013  66.752  1.00 60.57           O  
ATOM    946  CB  GLU A 127     -33.774  33.048  65.100  1.00 63.53           C  
ATOM    947  CG  GLU A 127     -33.692  34.309  64.242  1.00 67.13           C  
ATOM    948  CD  GLU A 127     -32.730  34.176  63.067  1.00 70.30           C  
ATOM    949  OE1 GLU A 127     -31.506  34.038  63.295  1.00 72.12           O  
ATOM    950  OE2 GLU A 127     -33.203  34.211  61.908  1.00 72.34           O  
ATOM    951  N   PHE A 128     -33.956  31.580  67.883  1.00 59.54           N  
ATOM    952  CA  PHE A 128     -33.926  30.368  68.701  1.00 57.50           C  
ATOM    953  C   PHE A 128     -35.232  30.253  69.481  1.00 57.70           C  
ATOM    954  O   PHE A 128     -35.968  29.278  69.342  1.00 57.56           O  
ATOM    955  CB  PHE A 128     -32.741  30.409  69.673  1.00 53.23           C  
ATOM    956  CG  PHE A 128     -32.842  29.407  70.798  1.00 50.54           C  
ATOM    957  CD1 PHE A 128     -33.116  28.061  70.538  1.00 48.72           C  
ATOM    958  CD2 PHE A 128     -32.669  29.810  72.124  1.00 48.80           C  
ATOM    959  CE1 PHE A 128     -33.222  27.128  71.584  1.00 47.16           C  
ATOM    960  CE2 PHE A 128     -32.773  28.887  73.177  1.00 47.12           C  
ATOM    961  CZ  PHE A 128     -33.051  27.542  72.905  1.00 45.70           C  
ATOM    962  N   VAL A 129     -35.514  31.260  70.300  1.00 58.44           N  
ATOM    963  CA  VAL A 129     -36.737  31.271  71.086  1.00 58.58           C  
ATOM    964  C   VAL A 129     -37.935  30.931  70.198  1.00 61.07           C  
ATOM    965  O   VAL A 129     -38.824  30.182  70.600  1.00 61.36           O  
ATOM    966  CB  VAL A 129     -36.963  32.645  71.721  1.00 56.90           C  
ATOM    967  CG1 VAL A 129     -38.185  32.599  72.625  1.00 55.55           C  
ATOM    968  CG2 VAL A 129     -35.720  33.071  72.493  1.00 54.15           C  
ATOM    969  N   GLU A 130     -37.955  31.478  68.986  1.00 63.45           N  
ATOM    970  CA  GLU A 130     -39.045  31.209  68.051  1.00 66.62           C  
ATOM    971  C   GLU A 130     -39.234  29.712  67.846  1.00 66.09           C  
ATOM    972  O   GLU A 130     -40.171  29.110  68.375  1.00 66.27           O  
ATOM    973  CB  GLU A 130     -38.767  31.843  66.688  1.00 68.41           C  
ATOM    974  CG  GLU A 130     -38.891  33.346  66.642  1.00 71.67           C  
ATOM    975  CD  GLU A 130     -39.480  33.811  65.328  1.00 72.67           C  
ATOM    976  OE1 GLU A 130     -38.888  33.517  64.264  1.00 71.44           O  
ATOM    977  OE2 GLU A 130     -40.545  34.462  65.363  1.00 72.96           O  
ATOM    978  N   LYS A 131     -38.331  29.124  67.064  1.00 65.01           N  
ATOM    979  CA  LYS A 131     -38.372  27.702  66.759  1.00 61.64           C  
ATOM    980  C   LYS A 131     -38.653  26.906  68.023  1.00 59.82           C  
ATOM    981  O   LYS A 131     -39.412  25.937  68.002  1.00 61.17           O  
ATOM    982  CB  LYS A 131     -37.041  27.269  66.147  1.00 63.38           C  
ATOM    983  CG  LYS A 131     -37.078  25.919  65.458  1.00 67.29           C  
ATOM    984  CD  LYS A 131     -35.873  25.747  64.540  1.00 70.64           C  
ATOM    985  CE  LYS A 131     -35.997  24.487  63.690  1.00 72.81           C  
ATOM    986  NZ  LYS A 131     -34.819  24.292  62.790  1.00 72.96           N  
ATOM    987  N   LEU A 132     -38.049  27.335  69.125  1.00 57.46           N  
ATOM    988  CA  LEU A 132     -38.219  26.674  70.411  1.00 55.65           C  
ATOM    989  C   LEU A 132     -39.680  26.623  70.839  1.00 55.74           C  
ATOM    990  O   LEU A 132     -40.160  25.599  71.332  1.00 53.68           O  
ATOM    991  CB  LEU A 132     -37.383  27.396  71.470  1.00 56.48           C  
ATOM    992  CG  LEU A 132     -37.658  27.131  72.955  1.00 58.85           C  
ATOM    993  CD1 LEU A 132     -37.798  25.650  73.207  1.00 59.65           C  
ATOM    994  CD2 LEU A 132     -36.520  27.713  73.794  1.00 59.87           C  
ATOM    995  N   GLN A 133     -40.392  27.727  70.649  1.00 56.96           N  
ATOM    996  CA  GLN A 133     -41.797  27.776  71.026  1.00 57.82           C  
ATOM    997  C   GLN A 133     -42.629  26.998  70.020  1.00 59.27           C  
ATOM    998  O   GLN A 133     -43.573  26.296  70.399  1.00 60.41           O  
ATOM    999  CB  GLN A 133     -42.258  29.225  71.105  1.00 57.48           C  
ATOM   1000  CG  GLN A 133     -41.254  30.099  71.825  1.00 62.27           C  
ATOM   1001  CD  GLN A 133     -41.885  31.264  72.549  1.00 65.43           C  
ATOM   1002  OE1 GLN A 133     -42.409  32.190  71.930  1.00 67.74           O  
ATOM   1003  NE2 GLN A 133     -41.840  31.223  73.877  1.00 67.08           N  
ATOM   1004  N   ASP A 134     -42.267  27.122  68.741  1.00 61.51           N  
ATOM   1005  CA  ASP A 134     -42.955  26.419  67.654  1.00 65.31           C  
ATOM   1006  C   ASP A 134     -43.155  24.963  68.040  1.00 67.21           C  
ATOM   1007  O   ASP A 134     -44.287  24.456  68.092  1.00 66.94           O  
ATOM   1008  CB  ASP A 134     -42.122  26.488  66.371  1.00 67.39           C  
ATOM   1009  CG  ASP A 134     -42.298  27.803  65.625  1.00 71.76           C  
ATOM   1010  OD1 ASP A 134     -42.539  28.839  66.289  1.00 72.96           O  
ATOM   1011  OD2 ASP A 134     -42.184  27.803  64.375  1.00 72.53           O  
ATOM   1012  N   ILE A 135     -42.034  24.301  68.310  1.00 68.06           N  
ATOM   1013  CA  ILE A 135     -42.025  22.897  68.719  1.00 69.59           C  
ATOM   1014  C   ILE A 135     -43.013  22.707  69.859  1.00 70.46           C  
ATOM   1015  O   ILE A 135     -43.790  21.761  69.881  1.00 71.39           O  
ATOM   1016  CB  ILE A 135     -40.592  22.479  69.156  1.00 68.47           C  
ATOM   1017  CG1 ILE A 135     -39.602  22.746  68.019  1.00 68.20           C  
ATOM   1018  CG2 ILE A 135     -40.555  21.004  69.532  1.00 68.24           C  
ATOM   1019  CD1 ILE A 135     -38.155  22.459  68.378  1.00 71.68           C  
ATOM   1020  N   GLN A 136     -42.963  23.626  70.813  1.00 71.73           N  
ATOM   1021  CA  GLN A 136     -43.887  23.588  71.937  1.00 72.56           C  
ATOM   1022  C   GLN A 136     -45.357  23.805  71.665  1.00 72.96           C  
ATOM   1023  O   GLN A 136     -46.191  23.604  72.511  1.00 72.96           O  
ATOM   1024  CB  GLN A 136     -43.417  24.534  73.025  1.00 72.22           C  
ATOM   1025  CG  GLN A 136     -42.266  24.004  73.826  1.00 72.96           C  
ATOM   1026  CD  GLN A 136     -41.743  25.006  74.796  1.00 72.96           C  
ATOM   1027  OE1 GLN A 136     -41.278  26.074  74.403  1.00 72.96           O  
ATOM   1028  NE2 GLN A 136     -41.802  24.672  76.083  1.00 72.96           N  
ATOM   1029  N   GLN A 137     -45.689  24.198  70.459  1.00 72.96           N  
ATOM   1030  CA  GLN A 137     -47.088  24.375  70.109  1.00 72.86           C  
ATOM   1031  C   GLN A 137     -47.540  23.195  69.220  1.00 72.96           C  
ATOM   1032  O   GLN A 137     -48.559  22.534  69.497  1.00 71.77           O  
ATOM   1033  CB  GLN A 137     -47.243  25.727  69.427  1.00 72.50           C  
ATOM   1034  CG  GLN A 137     -46.980  26.827  70.414  1.00 72.72           C  
ATOM   1035  CD  GLN A 137     -46.964  28.237  69.797  1.00 72.96           C  
ATOM   1036  OE1 GLN A 137     -47.060  28.437  68.565  1.00 72.96           O  
ATOM   1037  NE2 GLN A 137     -46.826  29.229  70.668  1.00 72.96           N  
ATOM   1038  N   ARG A 138     -46.804  22.942  68.132  1.00 72.96           N  
ATOM   1039  CA  ARG A 138     -47.140  21.779  67.276  1.00 72.96           C  
ATOM   1040  C   ARG A 138     -46.806  20.565  68.148  1.00 72.80           C  
ATOM   1041  O   ARG A 138     -47.696  19.808  68.525  1.00 72.83           O  
ATOM   1042  CB  ARG A 138     -46.313  21.654  65.986  1.00 72.77           C  
ATOM   1043  CG  ARG A 138     -45.507  22.835  65.605  1.00 72.96           C  
ATOM   1044  CD  ARG A 138     -44.489  22.428  64.554  1.00 72.96           C  
ATOM   1045  NE  ARG A 138     -43.173  22.127  65.134  1.00 72.96           N  
ATOM   1046  CZ  ARG A 138     -42.819  20.993  65.754  1.00 72.96           C  
ATOM   1047  NH1 ARG A 138     -43.673  19.981  65.906  1.00 72.96           N  
ATOM   1048  NH2 ARG A 138     -41.585  20.871  66.245  1.00 72.96           N  
ATOM   1049  N   GLY A 139     -45.526  20.363  68.465  1.00 72.82           N  
ATOM   1050  CA  GLY A 139     -45.210  19.257  69.361  1.00 72.96           C  
ATOM   1051  C   GLY A 139     -43.799  18.752  69.613  1.00 72.96           C  
ATOM   1052  O   GLY A 139     -42.831  19.209  69.008  1.00 72.52           O  
ATOM   1053  N   GLY A 140     -43.702  17.774  70.515  1.00 72.96           N  
ATOM   1054  CA  GLY A 140     -42.416  17.191  70.840  1.00 72.96           C  
ATOM   1055  C   GLY A 140     -41.793  16.483  69.655  1.00 72.96           C  
ATOM   1056  O   GLY A 140     -41.634  15.268  69.674  1.00 72.88           O  
ATOM   1057  N   GLU A 141     -41.478  17.229  68.602  1.00 72.96           N  
ATOM   1058  CA  GLU A 141     -40.817  16.641  67.449  1.00 72.00           C  
ATOM   1059  C   GLU A 141     -39.334  16.818  67.750  1.00 71.41           C  
ATOM   1060  O   GLU A 141     -38.748  16.015  68.477  1.00 72.00           O  
ATOM   1061  CB  GLU A 141     -41.206  17.368  66.165  1.00 72.29           C  
ATOM   1062  CG  GLU A 141     -40.637  16.701  64.941  1.00 72.07           C  
ATOM   1063  CD  GLU A 141     -41.121  17.316  63.653  1.00 72.96           C  
ATOM   1064  OE1 GLU A 141     -40.797  16.755  62.583  1.00 72.96           O  
ATOM   1065  OE2 GLU A 141     -41.819  18.356  63.699  1.00 72.96           O  
ATOM   1066  N   GLU A 142     -38.714  17.874  67.237  1.00 70.02           N  
ATOM   1067  CA  GLU A 142     -37.307  18.035  67.564  1.00 68.34           C  
ATOM   1068  C   GLU A 142     -37.114  18.493  69.010  1.00 65.79           C  
ATOM   1069  O   GLU A 142     -38.056  18.800  69.742  1.00 64.59           O  
ATOM   1070  CB  GLU A 142     -36.584  19.086  66.713  1.00 69.06           C  
ATOM   1071  CG  GLU A 142     -37.050  19.440  65.329  1.00 71.34           C  
ATOM   1072  CD  GLU A 142     -36.017  20.381  64.698  1.00 72.96           C  
ATOM   1073  OE1 GLU A 142     -34.886  19.910  64.438  1.00 72.48           O  
ATOM   1074  OE2 GLU A 142     -36.296  21.585  64.487  1.00 72.96           O  
ATOM   1075  N   ARG A 143     -35.849  18.551  69.393  1.00 63.22           N  
ATOM   1076  CA  ARG A 143     -35.440  19.027  70.699  1.00 59.65           C  
ATOM   1077  C   ARG A 143     -34.201  19.865  70.362  1.00 56.37           C  
ATOM   1078  O   ARG A 143     -33.308  19.407  69.651  1.00 56.21           O  
ATOM   1079  CB  ARG A 143     -35.145  17.847  71.626  1.00 59.84           C  
ATOM   1080  CG  ARG A 143     -36.405  17.274  72.273  1.00 60.63           C  
ATOM   1081  CD  ARG A 143     -36.846  18.144  73.444  1.00 63.40           C  
ATOM   1082  NE  ARG A 143     -38.168  18.758  73.285  1.00 65.67           N  
ATOM   1083  CZ  ARG A 143     -39.318  18.087  73.328  1.00 66.87           C  
ATOM   1084  NH1 ARG A 143     -39.311  16.775  73.519  1.00 68.65           N  
ATOM   1085  NH2 ARG A 143     -40.483  18.721  73.212  1.00 66.98           N  
ATOM   1086  N   LEU A 144     -34.181  21.115  70.817  1.00 53.42           N  
ATOM   1087  CA  LEU A 144     -33.070  22.025  70.517  1.00 49.90           C  
ATOM   1088  C   LEU A 144     -32.146  22.154  71.710  1.00 47.45           C  
ATOM   1089  O   LEU A 144     -32.501  21.735  72.807  1.00 47.90           O  
ATOM   1090  CB  LEU A 144     -33.615  23.405  70.157  1.00 48.88           C  
ATOM   1091  CG  LEU A 144     -34.836  23.314  69.235  1.00 48.18           C  
ATOM   1092  CD1 LEU A 144     -35.699  24.542  69.398  1.00 50.81           C  
ATOM   1093  CD2 LEU A 144     -34.404  23.126  67.789  1.00 48.86           C  
ATOM   1094  N   TYR A 145     -30.974  22.751  71.501  1.00 44.07           N  
ATOM   1095  CA  TYR A 145     -29.994  22.916  72.575  1.00 41.76           C  
ATOM   1096  C   TYR A 145     -29.001  24.018  72.208  1.00 41.49           C  
ATOM   1097  O   TYR A 145     -28.072  23.788  71.436  1.00 40.56           O  
ATOM   1098  CB  TYR A 145     -29.239  21.584  72.803  1.00 40.67           C  
ATOM   1099  CG  TYR A 145     -29.061  21.150  74.264  1.00 38.95           C  
ATOM   1100  CD1 TYR A 145     -28.962  19.788  74.597  1.00 35.30           C  
ATOM   1101  CD2 TYR A 145     -28.966  22.090  75.306  1.00 37.20           C  
ATOM   1102  CE1 TYR A 145     -28.774  19.370  75.914  1.00 33.57           C  
ATOM   1103  CE2 TYR A 145     -28.775  21.680  76.637  1.00 35.60           C  
ATOM   1104  CZ  TYR A 145     -28.679  20.316  76.930  1.00 35.75           C  
ATOM   1105  OH  TYR A 145     -28.490  19.895  78.233  1.00 35.46           O  
ATOM   1106  N   LEU A 146     -29.183  25.209  72.770  1.00 40.85           N  
ATOM   1107  CA  LEU A 146     -28.283  26.317  72.464  1.00 41.95           C  
ATOM   1108  C   LEU A 146     -27.052  26.305  73.359  1.00 43.34           C  
ATOM   1109  O   LEU A 146     -27.145  26.394  74.586  1.00 44.10           O  
ATOM   1110  CB  LEU A 146     -29.035  27.649  72.572  1.00 38.84           C  
ATOM   1111  CG  LEU A 146     -28.401  28.876  73.241  1.00 38.58           C  
ATOM   1112  CD1 LEU A 146     -26.973  29.126  72.764  1.00 39.64           C  
ATOM   1113  CD2 LEU A 146     -29.287  30.072  72.930  1.00 37.30           C  
ATOM   1114  N   GLN A 147     -25.892  26.190  72.728  1.00 45.72           N  
ATOM   1115  CA  GLN A 147     -24.635  26.155  73.446  1.00 48.51           C  
ATOM   1116  C   GLN A 147     -23.793  27.291  72.923  1.00 50.97           C  
ATOM   1117  O   GLN A 147     -23.416  27.288  71.758  1.00 51.14           O  
ATOM   1118  CB  GLN A 147     -23.903  24.837  73.185  1.00 49.83           C  
ATOM   1119  CG  GLN A 147     -24.811  23.631  72.965  1.00 53.62           C  
ATOM   1120  CD  GLN A 147     -24.515  22.476  73.915  1.00 56.37           C  
ATOM   1121  OE1 GLN A 147     -23.353  22.124  74.145  1.00 57.65           O  
ATOM   1122  NE2 GLN A 147     -25.572  21.871  74.460  1.00 58.04           N  
ATOM   1123  N   GLN A 148     -23.497  28.264  73.774  1.00 55.40           N  
ATOM   1124  CA  GLN A 148     -22.678  29.386  73.344  1.00 59.99           C  
ATOM   1125  C   GLN A 148     -21.745  29.895  74.425  1.00 62.86           C  
ATOM   1126  O   GLN A 148     -22.100  29.917  75.601  1.00 63.64           O  
ATOM   1127  CB  GLN A 148     -23.560  30.517  72.825  1.00 60.96           C  
ATOM   1128  CG  GLN A 148     -23.625  30.531  71.311  1.00 63.44           C  
ATOM   1129  CD  GLN A 148     -22.264  30.781  70.678  1.00 65.75           C  
ATOM   1130  OE1 GLN A 148     -22.043  30.459  69.507  1.00 66.71           O  
ATOM   1131  NE2 GLN A 148     -21.347  31.370  71.448  1.00 66.65           N  
ATOM   1132  N   THR A 149     -20.551  30.308  74.006  1.00 66.28           N  
ATOM   1133  CA  THR A 149     -19.510  30.802  74.903  1.00 69.97           C  
ATOM   1134  C   THR A 149     -19.817  32.138  75.568  1.00 71.13           C  
ATOM   1135  O   THR A 149     -20.635  32.909  75.066  1.00 72.25           O  
ATOM   1136  CB  THR A 149     -18.193  30.942  74.142  1.00 70.64           C  
ATOM   1137  OG1 THR A 149     -18.303  30.271  72.882  1.00 72.00           O  
ATOM   1138  CG2 THR A 149     -17.056  30.318  74.924  1.00 71.82           C  
ATOM   1139  N   LEU A 150     -19.155  32.424  76.688  1.00 71.71           N  
ATOM   1140  CA  LEU A 150     -19.403  33.680  77.391  1.00 71.76           C  
ATOM   1141  C   LEU A 150     -18.378  34.752  77.060  1.00 72.96           C  
ATOM   1142  O   LEU A 150     -17.797  35.374  77.958  1.00 72.96           O  
ATOM   1143  CB  LEU A 150     -19.441  33.457  78.907  1.00 70.09           C  
ATOM   1144  CG  LEU A 150     -20.828  33.040  79.409  1.00 68.07           C  
ATOM   1145  CD1 LEU A 150     -20.817  32.719  80.898  1.00 67.04           C  
ATOM   1146  CD2 LEU A 150     -21.813  34.178  79.128  1.00 68.11           C  
ATOM   1147  N   ASN A 151     -18.162  34.973  75.767  1.00 72.96           N  
ATOM   1148  CA  ASN A 151     -17.215  35.985  75.320  1.00 72.96           C  
ATOM   1149  C   ASN A 151     -17.814  36.779  74.140  1.00 72.96           C  
ATOM   1150  O   ASN A 151     -17.172  37.683  73.566  1.00 72.96           O  
ATOM   1151  CB  ASN A 151     -15.891  35.314  74.950  1.00 72.96           C  
ATOM   1152  CG  ASN A 151     -14.698  35.995  75.598  1.00 72.96           C  
ATOM   1153  OD1 ASN A 151     -14.797  37.142  76.055  1.00 72.96           O  
ATOM   1154  ND2 ASN A 151     -13.557  35.303  75.627  1.00 72.96           N  
ATOM   1155  N   ASP A 152     -19.054  36.420  73.795  1.00 72.96           N  
ATOM   1156  CA  ASP A 152     -19.806  37.105  72.756  1.00 72.96           C  
ATOM   1157  C   ASP A 152     -20.104  38.424  73.447  1.00 72.96           C  
ATOM   1158  O   ASP A 152     -20.743  38.451  74.507  1.00 72.96           O  
ATOM   1159  CB  ASP A 152     -21.133  36.378  72.439  1.00 72.96           C  
ATOM   1160  CG  ASP A 152     -21.057  35.561  71.158  1.00 72.96           C  
ATOM   1161  OD1 ASP A 152     -22.093  35.198  70.554  1.00 72.39           O  
ATOM   1162  OD2 ASP A 152     -19.920  35.265  70.753  1.00 72.96           O  
ATOM   1163  N   THR A 153     -19.608  39.514  72.890  1.00 71.99           N  
ATOM   1164  CA  THR A 153     -19.891  40.785  73.505  1.00 71.46           C  
ATOM   1165  C   THR A 153     -21.408  40.880  73.416  1.00 70.58           C  
ATOM   1166  O   THR A 153     -21.964  41.235  72.375  1.00 71.31           O  
ATOM   1167  CB  THR A 153     -19.233  41.896  72.732  1.00 71.87           C  
ATOM   1168  OG1 THR A 153     -19.515  41.719  71.340  1.00 72.88           O  
ATOM   1169  CG2 THR A 153     -17.724  41.864  72.954  1.00 72.78           C  
ATOM   1170  N   VAL A 154     -22.078  40.523  74.504  1.00 69.44           N  
ATOM   1171  CA  VAL A 154     -23.528  40.539  74.531  1.00 66.95           C  
ATOM   1172  C   VAL A 154     -24.061  41.723  75.320  1.00 65.58           C  
ATOM   1173  O   VAL A 154     -23.298  42.455  75.948  1.00 64.65           O  
ATOM   1174  CB  VAL A 154     -24.056  39.267  75.161  1.00 66.52           C  
ATOM   1175  CG1 VAL A 154     -23.862  38.101  74.204  1.00 66.83           C  
ATOM   1176  CG2 VAL A 154     -23.311  39.006  76.459  1.00 65.07           C  
ATOM   1177  N   GLY A 155     -25.378  41.897  75.292  1.00 64.40           N  
ATOM   1178  CA  GLY A 155     -26.009  42.997  76.002  1.00 62.84           C  
ATOM   1179  C   GLY A 155     -25.341  43.418  77.302  1.00 62.45           C  
ATOM   1180  O   GLY A 155     -25.021  42.580  78.157  1.00 62.80           O  
ATOM   1181  N   GLY A 156     -25.136  44.727  77.450  1.00 60.81           N  
ATOM   1182  CA  GLY A 156     -24.508  45.266  78.645  1.00 57.43           C  
ATOM   1183  C   GLY A 156     -25.097  44.671  79.909  1.00 56.05           C  
ATOM   1184  O   GLY A 156     -24.380  44.413  80.876  1.00 56.71           O  
ATOM   1185  N   LYS A 157     -26.406  44.449  79.903  1.00 54.48           N  
ATOM   1186  CA  LYS A 157     -27.070  43.881  81.063  1.00 55.08           C  
ATOM   1187  C   LYS A 157     -26.368  42.567  81.417  1.00 54.61           C  
ATOM   1188  O   LYS A 157     -25.963  42.353  82.561  1.00 54.56           O  
ATOM   1189  CB  LYS A 157     -28.548  43.620  80.747  1.00 56.77           C  
ATOM   1190  CG  LYS A 157     -29.480  43.793  81.937  1.00 58.84           C  
ATOM   1191  CD  LYS A 157     -29.792  45.263  82.186  1.00 60.27           C  
ATOM   1192  CE  LYS A 157     -31.155  45.637  81.626  1.00 61.97           C  
ATOM   1193  NZ  LYS A 157     -32.247  44.877  82.299  1.00 63.51           N  
ATOM   1194  N   ILE A 158     -26.208  41.700  80.419  1.00 53.19           N  
ATOM   1195  CA  ILE A 158     -25.565  40.405  80.614  1.00 52.03           C  
ATOM   1196  C   ILE A 158     -24.129  40.505  81.126  1.00 51.69           C  
ATOM   1197  O   ILE A 158     -23.765  39.835  82.092  1.00 52.30           O  
ATOM   1198  CB  ILE A 158     -25.554  39.591  79.305  1.00 50.78           C  
ATOM   1199  CG1 ILE A 158     -26.985  39.427  78.776  1.00 48.88           C  
ATOM   1200  CG2 ILE A 158     -24.880  38.243  79.539  1.00 48.06           C  
ATOM   1201  CD1 ILE A 158     -27.921  38.754  79.733  1.00 49.41           C  
ATOM   1202  N   VAL A 159     -23.313  41.323  80.470  1.00 51.83           N  
ATOM   1203  CA  VAL A 159     -21.915  41.502  80.870  1.00 52.52           C  
ATOM   1204  C   VAL A 159     -21.822  41.808  82.360  1.00 51.59           C  
ATOM   1205  O   VAL A 159     -20.894  41.371  83.047  1.00 51.41           O  
ATOM   1206  CB  VAL A 159     -21.262  42.665  80.090  1.00 53.76           C  
ATOM   1207  CG1 VAL A 159     -19.931  43.032  80.720  1.00 53.39           C  
ATOM   1208  CG2 VAL A 159     -21.068  42.267  78.625  1.00 54.63           C  
HETATM 1209  N   MSE A 160     -22.792  42.579  82.845  1.00 51.68           N  
HETATM 1210  CA  MSE A 160     -22.851  42.943  84.251  1.00 51.30           C  
HETATM 1211  C   MSE A 160     -23.000  41.668  85.054  1.00 49.60           C  
HETATM 1212  O   MSE A 160     -22.226  41.402  85.970  1.00 50.47           O  
HETATM 1213  CB  MSE A 160     -24.050  43.863  84.522  1.00 53.25           C  
HETATM 1214  CG  MSE A 160     -23.849  45.320  84.105  1.00 53.28           C  
HETATM 1215 SE   MSE A 160     -22.338  46.195  85.028  1.00 72.90          SE  
HETATM 1216  CE  MSE A 160     -23.281  46.798  86.642  1.00 51.19           C  
ATOM   1217  N   ASP A 161     -24.004  40.877  84.694  1.00 48.01           N  
ATOM   1218  CA  ASP A 161     -24.261  39.621  85.372  1.00 46.34           C  
ATOM   1219  C   ASP A 161     -23.025  38.716  85.284  1.00 46.81           C  
ATOM   1220  O   ASP A 161     -22.584  38.157  86.286  1.00 46.16           O  
ATOM   1221  CB  ASP A 161     -25.500  38.952  84.758  1.00 44.40           C  
ATOM   1222  CG  ASP A 161     -26.774  39.810  84.916  1.00 43.00           C  
ATOM   1223  OD1 ASP A 161     -26.859  40.572  85.907  1.00 40.33           O  
ATOM   1224  OD2 ASP A 161     -27.696  39.719  84.068  1.00 39.03           O  
ATOM   1225  N   PHE A 162     -22.453  38.593  84.092  1.00 47.12           N  
ATOM   1226  CA  PHE A 162     -21.266  37.771  83.900  1.00 48.84           C  
ATOM   1227  C   PHE A 162     -20.198  38.225  84.890  1.00 47.12           C  
ATOM   1228  O   PHE A 162     -19.388  37.428  85.357  1.00 48.80           O  
ATOM   1229  CB  PHE A 162     -20.761  37.920  82.458  1.00 55.52           C  
ATOM   1230  CG  PHE A 162     -19.604  37.018  82.114  1.00 63.95           C  
ATOM   1231  CD1 PHE A 162     -19.780  35.643  81.999  1.00 68.63           C  
ATOM   1232  CD2 PHE A 162     -18.328  37.547  81.916  1.00 68.91           C  
ATOM   1233  CE1 PHE A 162     -18.694  34.807  81.693  1.00 72.30           C  
ATOM   1234  CE2 PHE A 162     -17.240  36.719  81.610  1.00 72.34           C  
ATOM   1235  CZ  PHE A 162     -17.425  35.346  81.498  1.00 72.96           C  
ATOM   1236  N   LEU A 163     -20.196  39.514  85.207  1.00 45.88           N  
ATOM   1237  CA  LEU A 163     -19.235  40.066  86.158  1.00 43.10           C  
ATOM   1238  C   LEU A 163     -19.656  39.710  87.584  1.00 41.67           C  
ATOM   1239  O   LEU A 163     -18.822  39.479  88.458  1.00 41.19           O  
ATOM   1240  CB  LEU A 163     -19.163  41.586  86.010  1.00 45.72           C  
ATOM   1241  CG  LEU A 163     -18.400  42.118  84.795  1.00 46.72           C  
ATOM   1242  CD1 LEU A 163     -18.525  43.640  84.715  1.00 48.00           C  
ATOM   1243  CD2 LEU A 163     -16.935  41.701  84.913  1.00 47.73           C  
ATOM   1244  N   GLY A 164     -20.963  39.666  87.808  1.00 39.56           N  
ATOM   1245  CA  GLY A 164     -21.478  39.334  89.119  1.00 35.59           C  
ATOM   1246  C   GLY A 164     -21.130  37.932  89.585  1.00 34.12           C  
ATOM   1247  O   GLY A 164     -21.286  37.637  90.770  1.00 35.46           O  
ATOM   1248  N   PHE A 165     -20.671  37.065  88.680  1.00 30.93           N  
ATOM   1249  CA  PHE A 165     -20.310  35.695  89.060  1.00 28.96           C  
ATOM   1250  C   PHE A 165     -19.228  35.721  90.144  1.00 28.33           C  
ATOM   1251  O   PHE A 165     -18.416  36.650  90.196  1.00 30.15           O  
ATOM   1252  CB  PHE A 165     -19.818  34.906  87.841  1.00 23.31           C  
ATOM   1253  CG  PHE A 165     -20.894  34.597  86.836  1.00 18.59           C  
ATOM   1254  CD1 PHE A 165     -20.570  33.996  85.618  1.00 19.00           C  
ATOM   1255  CD2 PHE A 165     -22.220  34.912  87.094  1.00 18.14           C  
ATOM   1256  CE1 PHE A 165     -21.564  33.713  84.660  1.00 20.14           C  
ATOM   1257  CE2 PHE A 165     -23.234  34.637  86.150  1.00 19.01           C  
ATOM   1258  CZ  PHE A 165     -22.905  34.037  84.929  1.00 19.19           C  
ATOM   1259  N   ASN A 166     -19.223  34.704  91.004  1.00 28.00           N  
ATOM   1260  CA  ASN A 166     -18.272  34.622  92.112  1.00 25.11           C  
ATOM   1261  C   ASN A 166     -16.904  34.179  91.645  1.00 26.77           C  
ATOM   1262  O   ASN A 166     -16.477  33.056  91.924  1.00 25.94           O  
ATOM   1263  CB  ASN A 166     -18.788  33.643  93.175  1.00 25.34           C  
ATOM   1264  CG  ASN A 166     -17.910  33.604  94.432  1.00 25.60           C  
ATOM   1265  OD1 ASN A 166     -16.685  33.803  94.377  1.00 25.40           O  
ATOM   1266  ND2 ASN A 166     -18.535  33.318  95.568  1.00 20.42           N  
ATOM   1267  N   TRP A 167     -16.196  35.057  90.950  1.00 26.62           N  
ATOM   1268  CA  TRP A 167     -14.877  34.684  90.472  1.00 30.12           C  
ATOM   1269  C   TRP A 167     -13.885  34.362  91.592  1.00 33.08           C  
ATOM   1270  O   TRP A 167     -13.132  33.396  91.485  1.00 35.12           O  
ATOM   1271  CB  TRP A 167     -14.340  35.770  89.552  1.00 26.92           C  
ATOM   1272  CG  TRP A 167     -15.224  35.951  88.355  1.00 25.84           C  
ATOM   1273  CD1 TRP A 167     -16.185  36.903  88.178  1.00 23.74           C  
ATOM   1274  CD2 TRP A 167     -15.292  35.093  87.204  1.00 24.60           C  
ATOM   1275  NE1 TRP A 167     -16.856  36.689  86.986  1.00 24.09           N  
ATOM   1276  CE2 TRP A 167     -16.324  35.585  86.373  1.00 24.57           C  
ATOM   1277  CE3 TRP A 167     -14.584  33.951  86.800  1.00 24.55           C  
ATOM   1278  CZ2 TRP A 167     -16.665  34.976  85.160  1.00 25.72           C  
ATOM   1279  CZ3 TRP A 167     -14.922  33.341  85.591  1.00 24.49           C  
ATOM   1280  CH2 TRP A 167     -15.954  33.857  84.786  1.00 25.80           C  
ATOM   1281  N   ASN A 168     -13.894  35.139  92.673  1.00 35.94           N  
ATOM   1282  CA  ASN A 168     -12.981  34.882  93.782  1.00 38.48           C  
ATOM   1283  C   ASN A 168     -12.951  33.379  94.065  1.00 39.65           C  
ATOM   1284  O   ASN A 168     -11.894  32.755  93.996  1.00 40.13           O  
ATOM   1285  CB  ASN A 168     -13.429  35.631  95.048  1.00 41.96           C  
ATOM   1286  CG  ASN A 168     -12.433  35.481  96.209  1.00 46.18           C  
ATOM   1287  OD1 ASN A 168     -12.803  35.598  97.387  1.00 47.65           O  
ATOM   1288  ND2 ASN A 168     -11.163  35.229  95.878  1.00 46.26           N  
ATOM   1289  N   TRP A 169     -14.116  32.804  94.359  1.00 40.40           N  
ATOM   1290  CA  TRP A 169     -14.236  31.369  94.659  1.00 41.67           C  
ATOM   1291  C   TRP A 169     -13.667  30.435  93.595  1.00 42.60           C  
ATOM   1292  O   TRP A 169     -12.721  29.683  93.848  1.00 42.36           O  
ATOM   1293  CB  TRP A 169     -15.701  30.977  94.849  1.00 37.81           C  
ATOM   1294  CG  TRP A 169     -15.849  29.568  95.292  1.00 33.56           C  
ATOM   1295  CD1 TRP A 169     -15.702  29.090  96.564  1.00 34.01           C  
ATOM   1296  CD2 TRP A 169     -16.110  28.434  94.465  1.00 32.34           C  
ATOM   1297  NE1 TRP A 169     -15.855  27.721  96.578  1.00 33.20           N  
ATOM   1298  CE2 TRP A 169     -16.105  27.295  95.301  1.00 32.10           C  
ATOM   1299  CE3 TRP A 169     -16.346  28.265  93.097  1.00 32.55           C  
ATOM   1300  CZ2 TRP A 169     -16.327  26.009  94.810  1.00 30.76           C  
ATOM   1301  CZ3 TRP A 169     -16.567  26.981  92.611  1.00 27.82           C  
ATOM   1302  CH2 TRP A 169     -16.556  25.876  93.464  1.00 28.26           C  
ATOM   1303  N   ILE A 170     -14.280  30.474  92.415  1.00 43.77           N  
ATOM   1304  CA  ILE A 170     -13.874  29.626  91.305  1.00 45.71           C  
ATOM   1305  C   ILE A 170     -12.387  29.709  91.035  1.00 48.10           C  
ATOM   1306  O   ILE A 170     -11.777  28.729  90.610  1.00 49.25           O  
ATOM   1307  CB  ILE A 170     -14.641  29.983  90.021  1.00 45.82           C  
ATOM   1308  CG1 ILE A 170     -14.671  28.770  89.095  1.00 43.94           C  
ATOM   1309  CG2 ILE A 170     -13.982  31.158  89.315  1.00 43.02           C  
ATOM   1310  CD1 ILE A 170     -15.545  28.972  87.878  1.00 45.61           C  
ATOM   1311  N   ASN A 171     -11.800  30.876  91.279  1.00 51.75           N  
ATOM   1312  CA  ASN A 171     -10.366  31.046  91.066  1.00 54.77           C  
ATOM   1313  C   ASN A 171      -9.619  30.363  92.200  1.00 53.73           C  
ATOM   1314  O   ASN A 171      -8.588  29.724  91.975  1.00 53.32           O  
ATOM   1315  CB  ASN A 171      -9.994  32.529  91.004  1.00 58.23           C  
ATOM   1316  CG  ASN A 171     -10.637  33.237  89.831  1.00 61.85           C  
ATOM   1317  OD1 ASN A 171     -10.889  32.630  88.793  1.00 64.52           O  
ATOM   1318  ND2 ASN A 171     -10.897  34.525  89.985  1.00 66.21           N  
ATOM   1319  N   LYS A 172     -10.146  30.496  93.415  1.00 52.03           N  
ATOM   1320  CA  LYS A 172      -9.535  29.863  94.574  1.00 50.47           C  
ATOM   1321  C   LYS A 172      -9.351  28.392  94.216  1.00 48.96           C  
ATOM   1322  O   LYS A 172      -8.414  27.743  94.671  1.00 49.70           O  
ATOM   1323  CB  LYS A 172     -10.438  29.987  95.814  1.00 55.33           C  
ATOM   1324  CG  LYS A 172      -9.803  30.746  96.993  1.00 56.51           C  
ATOM   1325  CD  LYS A 172     -10.684  30.745  98.263  1.00 58.13           C  
ATOM   1326  CE  LYS A 172     -11.992  31.535  98.086  1.00 60.60           C  
ATOM   1327  NZ  LYS A 172     -12.796  31.625  99.350  1.00 58.10           N  
ATOM   1328  N   GLN A 173     -10.250  27.867  93.392  1.00 45.18           N  
ATOM   1329  CA  GLN A 173     -10.155  26.477  92.973  1.00 42.54           C  
ATOM   1330  C   GLN A 173      -9.028  26.307  91.960  1.00 40.77           C  
ATOM   1331  O   GLN A 173      -8.071  25.556  92.195  1.00 40.38           O  
ATOM   1332  CB  GLN A 173     -11.485  26.013  92.373  1.00 45.20           C  
ATOM   1333  CG  GLN A 173     -12.591  25.879  93.397  1.00 44.60           C  
ATOM   1334  CD  GLN A 173     -12.105  25.167  94.639  1.00 45.80           C  
ATOM   1335  OE1 GLN A 173     -11.200  25.647  95.316  1.00 48.28           O  
ATOM   1336  NE2 GLN A 173     -12.694  24.017  94.941  1.00 44.78           N  
ATOM   1337  N   GLN A 174      -9.136  27.018  90.840  1.00 38.04           N  
ATOM   1338  CA  GLN A 174      -8.121  26.959  89.788  1.00 37.80           C  
ATOM   1339  C   GLN A 174      -6.694  26.998  90.325  1.00 37.85           C  
ATOM   1340  O   GLN A 174      -5.778  26.479  89.689  1.00 37.59           O  
ATOM   1341  CB  GLN A 174      -8.300  28.121  88.811  1.00 39.45           C  
ATOM   1342  CG  GLN A 174      -7.361  28.089  87.616  1.00 39.78           C  
ATOM   1343  CD  GLN A 174      -7.711  29.161  86.599  1.00 42.97           C  
ATOM   1344  OE1 GLN A 174      -7.284  29.109  85.438  1.00 41.70           O  
ATOM   1345  NE2 GLN A 174      -8.494  30.148  87.031  1.00 42.76           N  
ATOM   1346  N   GLY A 175      -6.504  27.622  91.485  1.00 38.93           N  
ATOM   1347  CA  GLY A 175      -5.174  27.714  92.054  1.00 40.41           C  
ATOM   1348  C   GLY A 175      -4.947  26.726  93.174  1.00 42.29           C  
ATOM   1349  O   GLY A 175      -3.967  25.982  93.170  1.00 44.68           O  
ATOM   1350  N   LYS A 176      -5.850  26.721  94.143  1.00 44.84           N  
ATOM   1351  CA  LYS A 176      -5.740  25.819  95.280  1.00 47.35           C  
ATOM   1352  C   LYS A 176      -5.612  24.369  94.802  1.00 49.65           C  
ATOM   1353  O   LYS A 176      -4.933  23.556  95.437  1.00 49.85           O  
ATOM   1354  CB  LYS A 176      -6.980  25.960  96.163  1.00 49.49           C  
ATOM   1355  CG  LYS A 176      -6.846  25.400  97.567  1.00 51.78           C  
ATOM   1356  CD  LYS A 176      -8.202  25.374  98.279  1.00 53.26           C  
ATOM   1357  CE  LYS A 176      -8.900  26.738  98.269  1.00 53.62           C  
ATOM   1358  NZ  LYS A 176     -10.311  26.651  98.769  1.00 54.46           N  
ATOM   1359  N   ARG A 177      -6.263  24.049  93.682  1.00 50.15           N  
ATOM   1360  CA  ARG A 177      -6.227  22.689  93.141  1.00 51.05           C  
ATOM   1361  C   ARG A 177      -4.995  22.469  92.254  1.00 51.23           C  
ATOM   1362  O   ARG A 177      -4.584  21.326  92.016  1.00 50.97           O  
ATOM   1363  CB  ARG A 177      -7.496  22.399  92.321  1.00 53.29           C  
ATOM   1364  CG  ARG A 177      -8.845  22.701  93.001  1.00 52.45           C  
ATOM   1365  CD  ARG A 177      -9.098  21.839  94.234  1.00 51.31           C  
ATOM   1366  NE  ARG A 177      -8.357  22.330  95.395  1.00 53.42           N  
ATOM   1367  CZ  ARG A 177      -8.260  21.684  96.556  1.00 53.07           C  
ATOM   1368  NH1 ARG A 177      -8.865  20.508  96.710  1.00 52.17           N  
ATOM   1369  NH2 ARG A 177      -7.555  22.210  97.557  1.00 50.63           N  
ATOM   1370  N   GLY A 178      -4.419  23.563  91.758  1.00 49.42           N  
ATOM   1371  CA  GLY A 178      -3.246  23.467  90.907  1.00 47.47           C  
ATOM   1372  C   GLY A 178      -3.565  23.312  89.427  1.00 47.02           C  
ATOM   1373  O   GLY A 178      -2.657  23.148  88.604  1.00 46.53           O  
ATOM   1374  N   TRP A 179      -4.849  23.364  89.076  1.00 45.49           N  
ATOM   1375  CA  TRP A 179      -5.253  23.228  87.680  1.00 43.43           C  
ATOM   1376  C   TRP A 179      -4.610  24.285  86.815  1.00 43.99           C  
ATOM   1377  O   TRP A 179      -3.934  25.180  87.306  1.00 44.37           O  
ATOM   1378  CB  TRP A 179      -6.761  23.355  87.538  1.00 42.25           C  
ATOM   1379  CG  TRP A 179      -7.521  22.434  88.408  1.00 40.08           C  
ATOM   1380  CD1 TRP A 179      -7.035  21.357  89.087  1.00 38.84           C  
ATOM   1381  CD2 TRP A 179      -8.928  22.477  88.667  1.00 39.49           C  
ATOM   1382  NE1 TRP A 179      -8.055  20.721  89.751  1.00 39.70           N  
ATOM   1383  CE2 TRP A 179      -9.228  21.387  89.513  1.00 38.77           C  
ATOM   1384  CE3 TRP A 179      -9.968  23.332  88.264  1.00 39.11           C  
ATOM   1385  CZ2 TRP A 179     -10.528  21.124  89.968  1.00 37.35           C  
ATOM   1386  CZ3 TRP A 179     -11.260  23.072  88.716  1.00 37.56           C  
ATOM   1387  CH2 TRP A 179     -11.525  21.973  89.561  1.00 36.78           C  
ATOM   1388  N   GLY A 180      -4.838  24.178  85.517  1.00 45.52           N  
ATOM   1389  CA  GLY A 180      -4.281  25.141  84.596  1.00 48.90           C  
ATOM   1390  C   GLY A 180      -5.392  25.955  83.973  1.00 51.14           C  
ATOM   1391  O   GLY A 180      -6.527  25.941  84.446  1.00 50.89           O  
ATOM   1392  N   GLN A 181      -5.051  26.652  82.898  1.00 52.42           N  
ATOM   1393  CA  GLN A 181      -5.967  27.512  82.156  1.00 55.15           C  
ATOM   1394  C   GLN A 181      -7.425  27.053  82.044  1.00 53.74           C  
ATOM   1395  O   GLN A 181      -7.710  25.859  81.947  1.00 53.20           O  
ATOM   1396  CB  GLN A 181      -5.413  27.723  80.744  1.00 59.87           C  
ATOM   1397  CG  GLN A 181      -6.338  28.507  79.826  1.00 66.06           C  
ATOM   1398  CD  GLN A 181      -5.958  28.363  78.370  1.00 69.07           C  
ATOM   1399  OE1 GLN A 181      -5.907  27.246  77.840  1.00 69.90           O  
ATOM   1400  NE2 GLN A 181      -5.690  29.490  77.709  1.00 69.44           N  
ATOM   1401  N   LEU A 182      -8.338  28.022  82.044  1.00 52.05           N  
ATOM   1402  CA  LEU A 182      -9.758  27.743  81.900  1.00 50.04           C  
ATOM   1403  C   LEU A 182     -10.011  27.516  80.407  1.00 49.04           C  
ATOM   1404  O   LEU A 182     -10.205  28.458  79.648  1.00 50.00           O  
ATOM   1405  CB  LEU A 182     -10.579  28.931  82.406  1.00 49.00           C  
ATOM   1406  CG  LEU A 182     -12.069  28.995  82.036  1.00 48.99           C  
ATOM   1407  CD1 LEU A 182     -12.788  27.718  82.445  1.00 47.90           C  
ATOM   1408  CD2 LEU A 182     -12.692  30.202  82.716  1.00 48.63           C  
ATOM   1409  N   THR A 183     -10.008  26.257  79.989  1.00 49.13           N  
ATOM   1410  CA  THR A 183     -10.207  25.927  78.582  1.00 48.61           C  
ATOM   1411  C   THR A 183     -11.489  26.463  77.959  1.00 47.93           C  
ATOM   1412  O   THR A 183     -11.447  27.058  76.891  1.00 46.88           O  
ATOM   1413  CB  THR A 183     -10.167  24.404  78.351  1.00 50.03           C  
ATOM   1414  OG1 THR A 183     -11.452  23.830  78.639  1.00 50.47           O  
ATOM   1415  CG2 THR A 183      -9.126  23.777  79.256  1.00 51.05           C  
ATOM   1416  N   SER A 184     -12.631  26.260  78.605  1.00 47.52           N  
ATOM   1417  CA  SER A 184     -13.878  26.733  78.011  1.00 46.93           C  
ATOM   1418  C   SER A 184     -14.916  27.231  79.017  1.00 44.47           C  
ATOM   1419  O   SER A 184     -14.781  27.032  80.224  1.00 46.42           O  
ATOM   1420  CB  SER A 184     -14.479  25.617  77.148  1.00 45.98           C  
ATOM   1421  OG  SER A 184     -15.526  26.114  76.333  1.00 47.24           O  
ATOM   1422  N   ASN A 185     -15.949  27.893  78.509  1.00 42.30           N  
ATOM   1423  CA  ASN A 185     -17.015  28.411  79.358  1.00 40.59           C  
ATOM   1424  C   ASN A 185     -18.278  28.606  78.532  1.00 39.57           C  
ATOM   1425  O   ASN A 185     -18.435  29.608  77.834  1.00 38.89           O  
ATOM   1426  CB  ASN A 185     -16.600  29.735  79.991  1.00 42.12           C  
ATOM   1427  CG  ASN A 185     -17.676  30.308  80.897  1.00 43.49           C  
ATOM   1428  OD1 ASN A 185     -18.092  29.682  81.885  1.00 42.99           O  
ATOM   1429  ND2 ASN A 185     -18.137  31.508  80.565  1.00 44.35           N  
ATOM   1430  N   LEU A 186     -19.192  27.653  78.627  1.00 37.86           N  
ATOM   1431  CA  LEU A 186     -20.402  27.733  77.837  1.00 36.42           C  
ATOM   1432  C   LEU A 186     -21.708  27.916  78.567  1.00 34.56           C  
ATOM   1433  O   LEU A 186     -21.882  27.493  79.716  1.00 36.59           O  
ATOM   1434  CB  LEU A 186     -20.536  26.492  76.961  1.00 37.47           C  
ATOM   1435  CG  LEU A 186     -19.542  26.280  75.829  1.00 36.44           C  
ATOM   1436  CD1 LEU A 186     -20.185  25.303  74.858  1.00 35.31           C  
ATOM   1437  CD2 LEU A 186     -19.221  27.593  75.115  1.00 34.69           C  
ATOM   1438  N   LEU A 187     -22.638  28.527  77.845  1.00 31.77           N  
ATOM   1439  CA  LEU A 187     -23.982  28.777  78.321  1.00 31.06           C  
ATOM   1440  C   LEU A 187     -24.881  27.752  77.634  1.00 31.61           C  
ATOM   1441  O   LEU A 187     -24.757  27.528  76.428  1.00 31.19           O  
ATOM   1442  CB  LEU A 187     -24.410  30.190  77.929  1.00 26.82           C  
ATOM   1443  CG  LEU A 187     -25.922  30.386  77.825  1.00 25.28           C  
ATOM   1444  CD1 LEU A 187     -26.578  30.052  79.170  1.00 23.05           C  
ATOM   1445  CD2 LEU A 187     -26.227  31.826  77.387  1.00 22.47           C  
ATOM   1446  N   LEU A 188     -25.779  27.129  78.391  1.00 31.70           N  
ATOM   1447  CA  LEU A 188     -26.678  26.134  77.815  1.00 31.56           C  
ATOM   1448  C   LEU A 188     -28.137  26.303  78.190  1.00 33.14           C  
ATOM   1449  O   LEU A 188     -28.479  26.463  79.368  1.00 34.83           O  
ATOM   1450  CB  LEU A 188     -26.257  24.735  78.222  1.00 31.02           C  
ATOM   1451  CG  LEU A 188     -24.994  24.163  77.601  1.00 31.98           C  
ATOM   1452  CD1 LEU A 188     -23.756  24.885  78.128  1.00 32.01           C  
ATOM   1453  CD2 LEU A 188     -24.950  22.687  77.940  1.00 31.32           C  
ATOM   1454  N   ILE A 189     -28.998  26.250  77.181  1.00 33.64           N  
ATOM   1455  CA  ILE A 189     -30.432  26.364  77.394  1.00 34.28           C  
ATOM   1456  C   ILE A 189     -31.047  25.217  76.617  1.00 37.30           C  
ATOM   1457  O   ILE A 189     -30.885  25.147  75.397  1.00 38.83           O  
ATOM   1458  CB  ILE A 189     -30.989  27.676  76.831  1.00 33.44           C  
ATOM   1459  CG1 ILE A 189     -30.326  28.864  77.518  1.00 31.87           C  
ATOM   1460  CG2 ILE A 189     -32.494  27.733  77.047  1.00 31.92           C  
ATOM   1461  CD1 ILE A 189     -30.710  30.192  76.906  1.00 28.25           C  
ATOM   1462  N   GLY A 190     -31.731  24.315  77.319  1.00 39.45           N  
ATOM   1463  CA  GLY A 190     -32.348  23.174  76.663  1.00 40.13           C  
ATOM   1464  C   GLY A 190     -33.811  23.038  77.029  1.00 41.16           C  
ATOM   1465  O   GLY A 190     -34.313  23.774  77.885  1.00 41.30           O  
HETATM 1466  N   MSE A 191     -34.497  22.101  76.384  1.00 42.37           N  
HETATM 1467  CA  MSE A 191     -35.913  21.874  76.635  1.00 47.20           C  
HETATM 1468  C   MSE A 191     -36.079  20.612  77.454  1.00 46.61           C  
HETATM 1469  O   MSE A 191     -35.108  19.917  77.720  1.00 48.54           O  
HETATM 1470  CB  MSE A 191     -36.660  21.724  75.311  1.00 50.06           C  
HETATM 1471  CG  MSE A 191     -36.478  22.898  74.349  1.00 53.00           C  
HETATM 1472 SE   MSE A 191     -36.930  22.460  72.484  1.00 58.84          SE  
HETATM 1473  CE  MSE A 191     -38.877  22.361  72.676  1.00 52.07           C  
ATOM   1474  N   GLU A 192     -37.312  20.312  77.844  1.00 47.67           N  
ATOM   1475  CA  GLU A 192     -37.595  19.122  78.635  1.00 49.08           C  
ATOM   1476  C   GLU A 192     -37.068  17.879  77.925  1.00 47.50           C  
ATOM   1477  O   GLU A 192     -36.881  17.888  76.709  1.00 47.25           O  
ATOM   1478  CB  GLU A 192     -39.101  18.991  78.846  1.00 53.31           C  
ATOM   1479  CG  GLU A 192     -39.755  20.292  79.284  1.00 62.70           C  
ATOM   1480  CD  GLU A 192     -41.251  20.159  79.518  1.00 69.27           C  
ATOM   1481  OE1 GLU A 192     -41.939  19.567  78.657  1.00 72.89           O  
ATOM   1482  OE2 GLU A 192     -41.739  20.658  80.557  1.00 72.41           O  
ATOM   1483  N   GLY A 193     -36.813  16.825  78.698  1.00 45.59           N  
ATOM   1484  CA  GLY A 193     -36.333  15.574  78.140  1.00 42.61           C  
ATOM   1485  C   GLY A 193     -35.008  15.577  77.395  1.00 41.35           C  
ATOM   1486  O   GLY A 193     -34.551  14.520  76.965  1.00 41.90           O  
ATOM   1487  N   ASN A 194     -34.375  16.732  77.216  1.00 39.76           N  
ATOM   1488  CA  ASN A 194     -33.095  16.738  76.505  1.00 37.95           C  
ATOM   1489  C   ASN A 194     -32.095  15.830  77.199  1.00 36.47           C  
ATOM   1490  O   ASN A 194     -31.891  15.931  78.407  1.00 36.99           O  
ATOM   1491  CB  ASN A 194     -32.493  18.144  76.421  1.00 37.14           C  
ATOM   1492  CG  ASN A 194     -33.143  18.995  75.351  1.00 38.76           C  
ATOM   1493  OD1 ASN A 194     -33.686  18.479  74.370  1.00 40.71           O  
ATOM   1494  ND2 ASN A 194     -33.074  20.310  75.521  1.00 41.32           N  
ATOM   1495  N   VAL A 195     -31.466  14.944  76.437  1.00 34.25           N  
ATOM   1496  CA  VAL A 195     -30.472  14.045  77.008  1.00 29.88           C  
ATOM   1497  C   VAL A 195     -29.189  14.075  76.179  1.00 30.33           C  
ATOM   1498  O   VAL A 195     -29.236  14.036  74.948  1.00 30.87           O  
ATOM   1499  CB  VAL A 195     -30.977  12.580  77.037  1.00 29.68           C  
ATOM   1500  CG1 VAL A 195     -30.040  11.723  77.860  1.00 28.01           C  
ATOM   1501  CG2 VAL A 195     -32.383  12.517  77.594  1.00 29.77           C  
ATOM   1502  N   THR A 196     -28.050  14.178  76.853  1.00 29.57           N  
ATOM   1503  CA  THR A 196     -26.745  14.135  76.185  1.00 26.51           C  
ATOM   1504  C   THR A 196     -26.176  12.809  76.685  1.00 23.48           C  
ATOM   1505  O   THR A 196     -25.770  12.707  77.843  1.00 25.36           O  
ATOM   1506  CB  THR A 196     -25.796  15.242  76.673  1.00 27.64           C  
ATOM   1507  OG1 THR A 196     -25.953  15.387  78.092  1.00 28.15           O  
ATOM   1508  CG2 THR A 196     -26.079  16.557  75.974  1.00 28.18           C  
ATOM   1509  N   PRO A 197     -26.162  11.777  75.833  1.00 22.25           N  
ATOM   1510  CA  PRO A 197     -25.648  10.452  76.193  1.00 20.29           C  
ATOM   1511  C   PRO A 197     -24.311  10.520  76.932  1.00 20.16           C  
ATOM   1512  O   PRO A 197     -23.491  11.428  76.702  1.00 21.25           O  
ATOM   1513  CB  PRO A 197     -25.512   9.763  74.843  1.00 20.17           C  
ATOM   1514  CG  PRO A 197     -26.613  10.360  74.047  1.00 18.96           C  
ATOM   1515  CD  PRO A 197     -26.497  11.830  74.400  1.00 21.40           C  
ATOM   1516  N   ALA A 198     -24.098   9.558  77.825  1.00 20.32           N  
ATOM   1517  CA  ALA A 198     -22.870   9.490  78.605  1.00 22.59           C  
ATOM   1518  C   ALA A 198     -21.622   9.669  77.724  1.00 22.57           C  
ATOM   1519  O   ALA A 198     -21.609   9.231  76.574  1.00 22.46           O  
ATOM   1520  CB  ALA A 198     -22.803   8.143  79.339  1.00 20.89           C  
ATOM   1521  N   HIS A 199     -20.592  10.316  78.278  1.00 22.22           N  
ATOM   1522  CA  HIS A 199     -19.318  10.552  77.593  1.00 24.50           C  
ATOM   1523  C   HIS A 199     -18.312  11.131  78.610  1.00 24.85           C  
ATOM   1524  O   HIS A 199     -18.650  11.293  79.786  1.00 25.83           O  
ATOM   1525  CB  HIS A 199     -19.500  11.524  76.425  1.00 29.22           C  
ATOM   1526  CG  HIS A 199     -19.592  12.961  76.841  1.00 35.08           C  
ATOM   1527  ND1 HIS A 199     -20.710  13.496  77.447  1.00 36.80           N  
ATOM   1528  CD2 HIS A 199     -18.688  13.967  76.764  1.00 36.79           C  
ATOM   1529  CE1 HIS A 199     -20.492  14.768  77.726  1.00 36.55           C  
ATOM   1530  NE2 HIS A 199     -19.272  15.078  77.323  1.00 39.62           N  
ATOM   1531  N   TYR A 200     -17.085  11.435  78.185  1.00 23.80           N  
ATOM   1532  CA  TYR A 200     -16.110  11.978  79.126  1.00 24.70           C  
ATOM   1533  C   TYR A 200     -15.128  13.037  78.581  1.00 28.37           C  
ATOM   1534  O   TYR A 200     -14.697  12.955  77.430  1.00 29.20           O  
ATOM   1535  CB  TYR A 200     -15.324  10.827  79.762  1.00 23.97           C  
ATOM   1536  CG  TYR A 200     -14.285  10.168  78.872  1.00 24.16           C  
ATOM   1537  CD1 TYR A 200     -12.934  10.503  78.980  1.00 24.28           C  
ATOM   1538  CD2 TYR A 200     -14.648   9.188  77.931  1.00 25.60           C  
ATOM   1539  CE1 TYR A 200     -11.952   9.874  78.170  1.00 25.25           C  
ATOM   1540  CE2 TYR A 200     -13.677   8.552  77.114  1.00 23.85           C  
ATOM   1541  CZ  TYR A 200     -12.331   8.902  77.241  1.00 24.63           C  
ATOM   1542  OH  TYR A 200     -11.364   8.300  76.443  1.00 22.80           O  
ATOM   1543  N   ASP A 201     -14.805  14.040  79.410  1.00 29.86           N  
ATOM   1544  CA  ASP A 201     -13.839  15.080  79.043  1.00 30.36           C  
ATOM   1545  C   ASP A 201     -12.569  14.659  79.756  1.00 30.89           C  
ATOM   1546  O   ASP A 201     -12.592  13.768  80.603  1.00 30.29           O  
ATOM   1547  CB  ASP A 201     -14.182  16.468  79.614  1.00 32.21           C  
ATOM   1548  CG  ASP A 201     -15.639  16.829  79.482  1.00 37.97           C  
ATOM   1549  OD1 ASP A 201     -16.169  16.837  78.350  1.00 40.25           O  
ATOM   1550  OD2 ASP A 201     -16.258  17.122  80.530  1.00 42.52           O  
ATOM   1551  N   GLU A 202     -11.467  15.316  79.428  1.00 32.63           N  
ATOM   1552  CA  GLU A 202     -10.207  15.040  80.089  1.00 33.81           C  
ATOM   1553  C   GLU A 202      -9.896  16.314  80.862  1.00 36.46           C  
ATOM   1554  O   GLU A 202      -8.732  16.691  81.001  1.00 36.54           O  
ATOM   1555  CB  GLU A 202      -9.104  14.791  79.067  1.00 35.65           C  
ATOM   1556  CG  GLU A 202      -9.485  13.849  77.935  1.00 37.87           C  
ATOM   1557  CD  GLU A 202      -8.273  13.229  77.256  1.00 38.17           C  
ATOM   1558  OE1 GLU A 202      -7.626  12.340  77.857  1.00 40.28           O  
ATOM   1559  OE2 GLU A 202      -7.961  13.635  76.125  1.00 38.00           O  
ATOM   1560  N   GLN A 203     -10.943  16.978  81.359  1.00 38.98           N  
ATOM   1561  CA  GLN A 203     -10.774  18.240  82.082  1.00 41.95           C  
ATOM   1562  C   GLN A 203     -11.704  18.377  83.280  1.00 39.52           C  
ATOM   1563  O   GLN A 203     -12.786  17.792  83.301  1.00 41.10           O  
ATOM   1564  CB  GLN A 203     -11.039  19.408  81.131  1.00 47.12           C  
ATOM   1565  CG  GLN A 203     -10.318  19.309  79.800  1.00 58.16           C  
ATOM   1566  CD  GLN A 203     -10.900  20.251  78.768  1.00 65.90           C  
ATOM   1567  OE1 GLN A 203     -12.079  20.144  78.405  1.00 71.41           O  
ATOM   1568  NE2 GLN A 203     -10.082  21.184  78.288  1.00 69.06           N  
ATOM   1569  N   GLN A 204     -11.286  19.166  84.268  1.00 35.85           N  
ATOM   1570  CA  GLN A 204     -12.095  19.399  85.461  1.00 34.03           C  
ATOM   1571  C   GLN A 204     -13.359  20.145  85.033  1.00 32.82           C  
ATOM   1572  O   GLN A 204     -13.287  21.062  84.226  1.00 34.57           O  
ATOM   1573  CB  GLN A 204     -11.326  20.254  86.457  1.00 33.66           C  
ATOM   1574  CG  GLN A 204      -9.888  19.830  86.661  1.00 35.05           C  
ATOM   1575  CD  GLN A 204      -9.761  18.440  87.244  1.00 36.46           C  
ATOM   1576  OE1 GLN A 204     -10.751  17.814  87.635  1.00 37.11           O  
ATOM   1577  NE2 GLN A 204      -8.529  17.948  87.315  1.00 37.04           N  
ATOM   1578  N   ASN A 205     -14.507  19.768  85.582  1.00 31.57           N  
ATOM   1579  CA  ASN A 205     -15.772  20.402  85.220  1.00 31.79           C  
ATOM   1580  C   ASN A 205     -16.538  20.974  86.393  1.00 30.66           C  
ATOM   1581  O   ASN A 205     -16.567  20.385  87.476  1.00 31.04           O  
ATOM   1582  CB  ASN A 205     -16.696  19.387  84.554  1.00 33.20           C  
ATOM   1583  CG  ASN A 205     -16.332  19.115  83.123  1.00 36.54           C  
ATOM   1584  OD1 ASN A 205     -16.630  19.921  82.252  1.00 37.44           O  
ATOM   1585  ND2 ASN A 205     -15.681  17.971  82.865  1.00 36.93           N  
ATOM   1586  N   PHE A 206     -17.190  22.107  86.157  1.00 29.62           N  
ATOM   1587  CA  PHE A 206     -18.032  22.758  87.164  1.00 26.70           C  
ATOM   1588  C   PHE A 206     -19.301  23.154  86.434  1.00 26.93           C  
ATOM   1589  O   PHE A 206     -19.256  23.971  85.527  1.00 28.28           O  
ATOM   1590  CB  PHE A 206     -17.361  24.007  87.726  1.00 23.75           C  
ATOM   1591  CG  PHE A 206     -16.437  23.738  88.881  1.00 20.51           C  
ATOM   1592  CD1 PHE A 206     -15.090  24.038  88.792  1.00 19.75           C  
ATOM   1593  CD2 PHE A 206     -16.921  23.202  90.064  1.00 19.92           C  
ATOM   1594  CE1 PHE A 206     -14.231  23.807  89.868  1.00 21.47           C  
ATOM   1595  CE2 PHE A 206     -16.073  22.967  91.143  1.00 21.48           C  
ATOM   1596  CZ  PHE A 206     -14.725  23.270  91.046  1.00 20.73           C  
ATOM   1597  N   PHE A 207     -20.432  22.571  86.797  1.00 26.23           N  
ATOM   1598  CA  PHE A 207     -21.669  22.916  86.112  1.00 27.27           C  
ATOM   1599  C   PHE A 207     -22.553  23.764  87.002  1.00 25.71           C  
ATOM   1600  O   PHE A 207     -23.018  23.323  88.045  1.00 27.65           O  
ATOM   1601  CB  PHE A 207     -22.374  21.642  85.649  1.00 30.48           C  
ATOM   1602  CG  PHE A 207     -21.689  20.976  84.490  1.00 36.58           C  
ATOM   1603  CD1 PHE A 207     -20.399  21.375  84.102  1.00 40.21           C  
ATOM   1604  CD2 PHE A 207     -22.308  19.948  83.792  1.00 38.51           C  
ATOM   1605  CE1 PHE A 207     -19.740  20.757  83.036  1.00 42.32           C  
ATOM   1606  CE2 PHE A 207     -21.652  19.319  82.718  1.00 42.01           C  
ATOM   1607  CZ  PHE A 207     -20.369  19.724  82.342  1.00 42.62           C  
ATOM   1608  N   ALA A 208     -22.761  25.000  86.582  1.00 23.99           N  
ATOM   1609  CA  ALA A 208     -23.546  25.940  87.353  1.00 24.00           C  
ATOM   1610  C   ALA A 208     -24.991  25.998  86.872  1.00 25.67           C  
ATOM   1611  O   ALA A 208     -25.317  26.717  85.912  1.00 23.67           O  
ATOM   1612  CB  ALA A 208     -22.901  27.306  87.268  1.00 24.13           C  
ATOM   1613  N   GLN A 209     -25.855  25.239  87.547  1.00 26.86           N  
ATOM   1614  CA  GLN A 209     -27.269  25.189  87.179  1.00 28.47           C  
ATOM   1615  C   GLN A 209     -27.865  26.550  87.436  1.00 29.37           C  
ATOM   1616  O   GLN A 209     -27.417  27.260  88.336  1.00 30.46           O  
ATOM   1617  CB  GLN A 209     -28.007  24.127  87.994  1.00 24.80           C  
ATOM   1618  CG  GLN A 209     -29.420  23.829  87.509  1.00 24.68           C  
ATOM   1619  CD  GLN A 209     -29.491  23.594  86.005  1.00 26.99           C  
ATOM   1620  OE1 GLN A 209     -28.575  23.027  85.405  1.00 25.53           O  
ATOM   1621  NE2 GLN A 209     -30.593  24.025  85.390  1.00 27.33           N  
ATOM   1622  N   ILE A 210     -28.865  26.921  86.645  1.00 31.21           N  
ATOM   1623  CA  ILE A 210     -29.478  28.223  86.801  1.00 32.13           C  
ATOM   1624  C   ILE A 210     -30.984  28.145  86.835  1.00 33.20           C  
ATOM   1625  O   ILE A 210     -31.607  28.438  87.859  1.00 33.79           O  
ATOM   1626  CB  ILE A 210     -29.063  29.157  85.664  1.00 32.49           C  
ATOM   1627  CG1 ILE A 210     -27.558  29.405  85.737  1.00 31.37           C  
ATOM   1628  CG2 ILE A 210     -29.845  30.465  85.757  1.00 32.69           C  
ATOM   1629  CD1 ILE A 210     -27.069  30.476  84.799  1.00 28.00           C  
ATOM   1630  N   LYS A 211     -31.568  27.773  85.701  1.00 32.89           N  
ATOM   1631  CA  LYS A 211     -33.013  27.644  85.605  1.00 32.98           C  
ATOM   1632  C   LYS A 211     -33.319  26.186  85.292  1.00 32.32           C  
ATOM   1633  O   LYS A 211     -32.580  25.538  84.547  1.00 34.69           O  
ATOM   1634  CB  LYS A 211     -33.564  28.544  84.502  1.00 31.44           C  
ATOM   1635  CG  LYS A 211     -35.071  28.465  84.377  1.00 32.88           C  
ATOM   1636  CD  LYS A 211     -35.598  29.334  83.247  1.00 33.28           C  
ATOM   1637  CE  LYS A 211     -37.119  29.260  83.154  1.00 34.98           C  
ATOM   1638  NZ  LYS A 211     -37.790  29.635  84.432  1.00 34.13           N  
ATOM   1639  N   GLY A 212     -34.394  25.668  85.874  1.00 30.76           N  
ATOM   1640  CA  GLY A 212     -34.759  24.284  85.632  1.00 28.95           C  
ATOM   1641  C   GLY A 212     -33.913  23.320  86.443  1.00 26.90           C  
ATOM   1642  O   GLY A 212     -33.004  23.744  87.161  1.00 24.34           O  
ATOM   1643  N   TYR A 213     -34.215  22.024  86.335  1.00 26.36           N  
ATOM   1644  CA  TYR A 213     -33.467  20.995  87.061  1.00 25.31           C  
ATOM   1645  C   TYR A 213     -32.848  20.010  86.087  1.00 24.01           C  
ATOM   1646  O   TYR A 213     -33.487  19.622  85.110  1.00 23.71           O  
ATOM   1647  CB  TYR A 213     -34.379  20.227  88.029  1.00 24.32           C  
ATOM   1648  CG  TYR A 213     -34.782  21.030  89.246  1.00 27.22           C  
ATOM   1649  CD1 TYR A 213     -35.876  21.911  89.194  1.00 26.87           C  
ATOM   1650  CD2 TYR A 213     -34.017  20.981  90.425  1.00 24.54           C  
ATOM   1651  CE1 TYR A 213     -36.193  22.736  90.274  1.00 27.36           C  
ATOM   1652  CE2 TYR A 213     -34.324  21.800  91.518  1.00 27.95           C  
ATOM   1653  CZ  TYR A 213     -35.414  22.687  91.435  1.00 30.30           C  
ATOM   1654  OH  TYR A 213     -35.694  23.562  92.481  1.00 29.98           O  
ATOM   1655  N   LYS A 214     -31.603  19.614  86.346  1.00 22.67           N  
ATOM   1656  CA  LYS A 214     -30.919  18.658  85.484  1.00 22.08           C  
ATOM   1657  C   LYS A 214     -30.468  17.414  86.246  1.00 22.87           C  
ATOM   1658  O   LYS A 214     -29.890  17.505  87.336  1.00 22.04           O  
ATOM   1659  CB  LYS A 214     -29.718  19.310  84.811  1.00 19.62           C  
ATOM   1660  CG  LYS A 214     -30.070  19.961  83.504  1.00 21.91           C  
ATOM   1661  CD  LYS A 214     -28.828  20.395  82.753  1.00 24.70           C  
ATOM   1662  CE  LYS A 214     -29.162  20.736  81.313  1.00 24.16           C  
ATOM   1663  NZ  LYS A 214     -27.951  21.266  80.649  1.00 27.89           N  
ATOM   1664  N   ARG A 215     -30.750  16.249  85.670  1.00 23.32           N  
ATOM   1665  CA  ARG A 215     -30.363  14.990  86.283  1.00 24.57           C  
ATOM   1666  C   ARG A 215     -28.989  14.643  85.772  1.00 24.00           C  
ATOM   1667  O   ARG A 215     -28.781  14.529  84.559  1.00 24.65           O  
ATOM   1668  CB  ARG A 215     -31.327  13.879  85.894  1.00 26.24           C  
ATOM   1669  CG  ARG A 215     -30.882  12.525  86.398  1.00 28.40           C  
ATOM   1670  CD  ARG A 215     -31.782  11.429  85.880  1.00 31.90           C  
ATOM   1671  NE  ARG A 215     -31.485  10.167  86.537  1.00 37.51           N  
ATOM   1672  CZ  ARG A 215     -32.272   9.102  86.481  1.00 40.35           C  
ATOM   1673  NH1 ARG A 215     -33.407   9.150  85.796  1.00 42.95           N  
ATOM   1674  NH2 ARG A 215     -31.923   7.994  87.117  1.00 43.06           N  
ATOM   1675  N   CYS A 216     -28.053  14.454  86.691  1.00 23.97           N  
ATOM   1676  CA  CYS A 216     -26.694  14.135  86.297  1.00 23.36           C  
ATOM   1677  C   CYS A 216     -26.294  12.756  86.753  1.00 25.03           C  
ATOM   1678  O   CYS A 216     -26.463  12.416  87.930  1.00 27.41           O  
ATOM   1679  CB  CYS A 216     -25.749  15.167  86.888  1.00 23.83           C  
ATOM   1680  SG  CYS A 216     -26.250  16.833  86.440  1.00 26.88           S  
ATOM   1681  N   ILE A 217     -25.757  11.964  85.825  1.00 25.41           N  
ATOM   1682  CA  ILE A 217     -25.306  10.600  86.133  1.00 23.55           C  
ATOM   1683  C   ILE A 217     -23.822  10.428  85.737  1.00 21.61           C  
ATOM   1684  O   ILE A 217     -23.440  10.646  84.573  1.00 21.44           O  
ATOM   1685  CB  ILE A 217     -26.176   9.568  85.394  1.00 24.42           C  
ATOM   1686  CG1 ILE A 217     -27.658   9.828  85.700  1.00 23.53           C  
ATOM   1687  CG2 ILE A 217     -25.805   8.165  85.821  1.00 22.94           C  
ATOM   1688  CD1 ILE A 217     -28.591   8.768  85.130  1.00 23.59           C  
ATOM   1689  N   LEU A 218     -22.998  10.042  86.713  1.00 18.56           N  
ATOM   1690  CA  LEU A 218     -21.567   9.879  86.501  1.00 18.61           C  
ATOM   1691  C   LEU A 218     -21.024   8.483  86.813  1.00 22.21           C  
ATOM   1692  O   LEU A 218     -21.476   7.813  87.755  1.00 22.84           O  
ATOM   1693  CB  LEU A 218     -20.798  10.871  87.373  1.00 17.96           C  
ATOM   1694  CG  LEU A 218     -21.390  12.271  87.577  1.00 19.36           C  
ATOM   1695  CD1 LEU A 218     -20.435  13.071  88.446  1.00 17.29           C  
ATOM   1696  CD2 LEU A 218     -21.620  12.973  86.250  1.00 15.64           C  
ATOM   1697  N   PHE A 219     -20.025   8.067  86.037  1.00 22.69           N  
ATOM   1698  CA  PHE A 219     -19.382   6.782  86.238  1.00 22.92           C  
ATOM   1699  C   PHE A 219     -17.875   7.040  86.355  1.00 20.21           C  
ATOM   1700  O   PHE A 219     -17.301   7.745  85.535  1.00 20.89           O  
ATOM   1701  CB  PHE A 219     -19.680   5.853  85.059  1.00 24.28           C  
ATOM   1702  CG  PHE A 219     -21.142   5.719  84.749  1.00 25.85           C  
ATOM   1703  CD1 PHE A 219     -21.730   6.495  83.753  1.00 27.81           C  
ATOM   1704  CD2 PHE A 219     -21.937   4.813  85.450  1.00 27.74           C  
ATOM   1705  CE1 PHE A 219     -23.093   6.372  83.451  1.00 26.63           C  
ATOM   1706  CE2 PHE A 219     -23.302   4.679  85.161  1.00 27.41           C  
ATOM   1707  CZ  PHE A 219     -23.881   5.460  84.158  1.00 26.66           C  
ATOM   1708  N   PRO A 220     -17.214   6.460  87.369  1.00 20.07           N  
ATOM   1709  CA  PRO A 220     -15.771   6.672  87.546  1.00 20.85           C  
ATOM   1710  C   PRO A 220     -14.981   6.144  86.354  1.00 22.17           C  
ATOM   1711  O   PRO A 220     -15.417   5.223  85.658  1.00 20.12           O  
ATOM   1712  CB  PRO A 220     -15.453   5.897  88.825  1.00 17.28           C  
ATOM   1713  CG  PRO A 220     -16.820   5.764  89.516  1.00 18.42           C  
ATOM   1714  CD  PRO A 220     -17.717   5.481  88.344  1.00 16.98           C  
ATOM   1715  N   PRO A 221     -13.800   6.721  86.100  1.00 21.71           N  
ATOM   1716  CA  PRO A 221     -13.047   6.215  84.954  1.00 25.07           C  
ATOM   1717  C   PRO A 221     -12.849   4.700  84.954  1.00 26.76           C  
ATOM   1718  O   PRO A 221     -12.848   4.086  83.885  1.00 28.94           O  
ATOM   1719  CB  PRO A 221     -11.739   7.021  85.009  1.00 23.68           C  
ATOM   1720  CG  PRO A 221     -11.676   7.528  86.436  1.00 21.77           C  
ATOM   1721  CD  PRO A 221     -13.105   7.847  86.745  1.00 20.25           C  
ATOM   1722  N   ASP A 222     -12.723   4.085  86.130  1.00 27.64           N  
ATOM   1723  CA  ASP A 222     -12.525   2.628  86.191  1.00 28.07           C  
ATOM   1724  C   ASP A 222     -13.685   1.811  85.613  1.00 27.61           C  
ATOM   1725  O   ASP A 222     -13.620   0.577  85.571  1.00 28.11           O  
ATOM   1726  CB  ASP A 222     -12.272   2.154  87.630  1.00 35.25           C  
ATOM   1727  CG  ASP A 222     -13.544   2.101  88.474  1.00 41.48           C  
ATOM   1728  OD1 ASP A 222     -14.653   1.905  87.913  1.00 42.10           O  
ATOM   1729  OD2 ASP A 222     -13.433   2.234  89.716  1.00 41.62           O  
ATOM   1730  N   GLN A 223     -14.745   2.493  85.183  1.00 23.53           N  
ATOM   1731  CA  GLN A 223     -15.926   1.842  84.611  1.00 21.59           C  
ATOM   1732  C   GLN A 223     -15.777   1.748  83.084  1.00 20.44           C  
ATOM   1733  O   GLN A 223     -16.746   1.502  82.342  1.00 19.56           O  
ATOM   1734  CB  GLN A 223     -17.156   2.673  84.932  1.00 23.67           C  
ATOM   1735  CG  GLN A 223     -18.400   1.885  85.200  1.00 23.36           C  
ATOM   1736  CD  GLN A 223     -18.668   1.784  86.673  1.00 24.83           C  
ATOM   1737  OE1 GLN A 223     -19.810   1.633  87.091  1.00 25.81           O  
ATOM   1738  NE2 GLN A 223     -17.611   1.863  87.477  1.00 25.65           N  
ATOM   1739  N   PHE A 224     -14.555   1.963  82.621  1.00 18.78           N  
ATOM   1740  CA  PHE A 224     -14.249   1.925  81.204  1.00 19.87           C  
ATOM   1741  C   PHE A 224     -14.725   0.649  80.509  1.00 23.04           C  
ATOM   1742  O   PHE A 224     -15.339   0.709  79.441  1.00 24.66           O  
ATOM   1743  CB  PHE A 224     -12.746   2.051  81.015  1.00 15.17           C  
ATOM   1744  CG  PHE A 224     -12.336   2.203  79.600  1.00 13.14           C  
ATOM   1745  CD1 PHE A 224     -12.237   3.466  79.026  1.00 15.63           C  
ATOM   1746  CD2 PHE A 224     -12.035   1.086  78.827  1.00 12.44           C  
ATOM   1747  CE1 PHE A 224     -11.835   3.626  77.690  1.00 14.18           C  
ATOM   1748  CE2 PHE A 224     -11.633   1.230  77.489  1.00 12.13           C  
ATOM   1749  CZ  PHE A 224     -11.531   2.508  76.918  1.00 10.68           C  
ATOM   1750  N   GLU A 225     -14.434  -0.504  81.107  1.00 24.61           N  
ATOM   1751  CA  GLU A 225     -14.805  -1.779  80.508  1.00 25.79           C  
ATOM   1752  C   GLU A 225     -16.298  -2.030  80.418  1.00 26.51           C  
ATOM   1753  O   GLU A 225     -16.719  -2.984  79.752  1.00 28.07           O  
ATOM   1754  CB  GLU A 225     -14.170  -2.950  81.272  1.00 33.66           C  
ATOM   1755  CG  GLU A 225     -12.786  -2.680  81.820  1.00 40.79           C  
ATOM   1756  CD  GLU A 225     -12.855  -2.138  83.226  1.00 47.91           C  
ATOM   1757  OE1 GLU A 225     -13.202  -2.938  84.127  1.00 51.41           O  
ATOM   1758  OE2 GLU A 225     -12.581  -0.921  83.425  1.00 48.16           O  
ATOM   1759  N   CYS A 226     -17.106  -1.211  81.085  1.00 25.67           N  
ATOM   1760  CA  CYS A 226     -18.557  -1.423  81.051  1.00 25.86           C  
ATOM   1761  C   CYS A 226     -19.255  -0.405  80.163  1.00 26.77           C  
ATOM   1762  O   CYS A 226     -20.426  -0.586  79.810  1.00 26.79           O  
ATOM   1763  CB  CYS A 226     -19.173  -1.306  82.453  1.00 27.02           C  
ATOM   1764  SG  CYS A 226     -18.331  -2.161  83.788  1.00 28.65           S  
ATOM   1765  N   LEU A 227     -18.545   0.672  79.829  1.00 25.09           N  
ATOM   1766  CA  LEU A 227     -19.113   1.735  79.021  1.00 22.49           C  
ATOM   1767  C   LEU A 227     -18.768   1.711  77.542  1.00 22.05           C  
ATOM   1768  O   LEU A 227     -19.463   2.322  76.736  1.00 21.06           O  
ATOM   1769  CB  LEU A 227     -18.766   3.072  79.660  1.00 24.29           C  
ATOM   1770  CG  LEU A 227     -19.720   3.216  80.857  1.00 24.44           C  
ATOM   1771  CD1 LEU A 227     -19.108   4.099  81.956  1.00 24.90           C  
ATOM   1772  CD2 LEU A 227     -21.067   3.774  80.327  1.00 20.14           C  
ATOM   1773  N   TYR A 228     -17.695   1.014  77.188  1.00 22.18           N  
ATOM   1774  CA  TYR A 228     -17.318   0.855  75.792  1.00 21.17           C  
ATOM   1775  C   TYR A 228     -17.283   2.130  74.951  1.00 20.92           C  
ATOM   1776  O   TYR A 228     -18.160   2.360  74.107  1.00 21.54           O  
ATOM   1777  CB  TYR A 228     -18.276  -0.143  75.123  1.00 22.97           C  
ATOM   1778  CG  TYR A 228     -18.382  -1.469  75.837  1.00 23.49           C  
ATOM   1779  CD1 TYR A 228     -19.183  -1.615  76.968  1.00 24.39           C  
ATOM   1780  CD2 TYR A 228     -17.662  -2.580  75.394  1.00 23.72           C  
ATOM   1781  CE1 TYR A 228     -19.265  -2.838  77.641  1.00 25.24           C  
ATOM   1782  CE2 TYR A 228     -17.732  -3.796  76.055  1.00 24.72           C  
ATOM   1783  CZ  TYR A 228     -18.534  -3.920  77.177  1.00 26.37           C  
ATOM   1784  OH  TYR A 228     -18.588  -5.132  77.834  1.00 31.21           O  
ATOM   1785  N   PRO A 229     -16.264   2.972  75.152  1.00 23.01           N  
ATOM   1786  CA  PRO A 229     -16.147   4.219  74.380  1.00 20.09           C  
ATOM   1787  C   PRO A 229     -16.002   3.869  72.888  1.00 19.59           C  
ATOM   1788  O   PRO A 229     -15.697   2.726  72.550  1.00 25.07           O  
ATOM   1789  CB  PRO A 229     -14.861   4.830  74.911  1.00 21.88           C  
ATOM   1790  CG  PRO A 229     -14.678   4.190  76.271  1.00 20.04           C  
ATOM   1791  CD  PRO A 229     -15.120   2.793  76.057  1.00 21.73           C  
ATOM   1792  N   TYR A 230     -16.231   4.825  71.995  1.00 19.72           N  
ATOM   1793  CA  TYR A 230     -16.037   4.559  70.567  1.00 20.01           C  
ATOM   1794  C   TYR A 230     -14.522   4.530  70.321  1.00 17.63           C  
ATOM   1795  O   TYR A 230     -13.735   4.942  71.182  1.00 19.89           O  
ATOM   1796  CB  TYR A 230     -16.595   5.691  69.704  1.00 19.06           C  
ATOM   1797  CG  TYR A 230     -18.061   5.616  69.389  1.00 16.89           C  
ATOM   1798  CD1 TYR A 230     -19.018   6.087  70.282  1.00 16.07           C  
ATOM   1799  CD2 TYR A 230     -18.498   5.066  68.183  1.00 17.13           C  
ATOM   1800  CE1 TYR A 230     -20.382   6.009  69.979  1.00 16.48           C  
ATOM   1801  CE2 TYR A 230     -19.861   4.984  67.871  1.00 15.71           C  
ATOM   1802  CZ  TYR A 230     -20.792   5.455  68.770  1.00 16.11           C  
ATOM   1803  OH  TYR A 230     -22.133   5.368  68.455  1.00 18.42           O  
ATOM   1804  N   PRO A 231     -14.093   4.039  69.145  1.00 19.42           N  
ATOM   1805  CA  PRO A 231     -12.657   4.001  68.841  1.00 22.11           C  
ATOM   1806  C   PRO A 231     -12.159   5.451  68.862  1.00 20.57           C  
ATOM   1807  O   PRO A 231     -12.906   6.375  68.504  1.00 20.38           O  
ATOM   1808  CB  PRO A 231     -12.622   3.406  67.434  1.00 19.36           C  
ATOM   1809  CG  PRO A 231     -13.806   2.464  67.441  1.00 19.26           C  
ATOM   1810  CD  PRO A 231     -14.868   3.299  68.129  1.00 21.00           C  
ATOM   1811  N   VAL A 232     -10.917   5.668  69.280  1.00 21.37           N  
ATOM   1812  CA  VAL A 232     -10.388   7.026  69.325  1.00 20.78           C  
ATOM   1813  C   VAL A 232     -10.585   7.822  68.033  1.00 23.85           C  
ATOM   1814  O   VAL A 232     -10.934   9.010  68.082  1.00 26.87           O  
ATOM   1815  CB  VAL A 232      -8.895   7.029  69.645  1.00 19.85           C  
ATOM   1816  CG1 VAL A 232      -8.283   8.351  69.205  1.00 18.26           C  
ATOM   1817  CG2 VAL A 232      -8.688   6.825  71.142  1.00 20.55           C  
ATOM   1818  N   HIS A 233     -10.360   7.184  66.884  1.00 23.98           N  
ATOM   1819  CA  HIS A 233     -10.493   7.872  65.605  1.00 26.73           C  
ATOM   1820  C   HIS A 233     -11.922   8.049  65.103  1.00 27.57           C  
ATOM   1821  O   HIS A 233     -12.133   8.555  64.001  1.00 30.40           O  
ATOM   1822  CB  HIS A 233      -9.691   7.148  64.524  1.00 32.29           C  
ATOM   1823  CG  HIS A 233      -8.225   7.063  64.807  1.00 36.63           C  
ATOM   1824  ND1 HIS A 233      -7.673   6.068  65.582  1.00 40.77           N  
ATOM   1825  CD2 HIS A 233      -7.194   7.845  64.410  1.00 40.20           C  
ATOM   1826  CE1 HIS A 233      -6.365   6.238  65.651  1.00 43.68           C  
ATOM   1827  NE2 HIS A 233      -6.048   7.311  64.947  1.00 44.34           N  
ATOM   1828  N   HIS A 234     -12.910   7.659  65.892  1.00 27.19           N  
ATOM   1829  CA  HIS A 234     -14.291   7.788  65.430  1.00 23.66           C  
ATOM   1830  C   HIS A 234     -14.928   9.139  65.762  1.00 22.01           C  
ATOM   1831  O   HIS A 234     -14.747   9.667  66.864  1.00 20.89           O  
ATOM   1832  CB  HIS A 234     -15.151   6.669  66.029  1.00 28.52           C  
ATOM   1833  CG  HIS A 234     -16.539   6.610  65.473  1.00 30.41           C  
ATOM   1834  ND1 HIS A 234     -17.394   7.690  65.496  1.00 32.16           N  
ATOM   1835  CD2 HIS A 234     -17.218   5.605  64.870  1.00 30.91           C  
ATOM   1836  CE1 HIS A 234     -18.540   7.353  64.931  1.00 31.70           C  
ATOM   1837  NE2 HIS A 234     -18.460   6.094  64.542  1.00 30.55           N  
ATOM   1838  N   PRO A 235     -15.694   9.710  64.812  1.00 23.26           N  
ATOM   1839  CA  PRO A 235     -16.335  10.999  65.068  1.00 22.55           C  
ATOM   1840  C   PRO A 235     -16.880  11.094  66.495  1.00 21.41           C  
ATOM   1841  O   PRO A 235     -16.777  12.159  67.125  1.00 24.03           O  
ATOM   1842  CB  PRO A 235     -17.450  11.038  64.022  1.00 20.95           C  
ATOM   1843  CG  PRO A 235     -16.804  10.387  62.854  1.00 21.03           C  
ATOM   1844  CD  PRO A 235     -16.094   9.190  63.492  1.00 23.68           C  
ATOM   1845  N   CYS A 236     -17.438   9.989  67.009  1.00 20.75           N  
ATOM   1846  CA  CYS A 236     -18.020   9.982  68.355  1.00 20.11           C  
ATOM   1847  C   CYS A 236     -17.064   9.621  69.481  1.00 19.46           C  
ATOM   1848  O   CYS A 236     -17.473   9.252  70.584  1.00 19.13           O  
ATOM   1849  CB  CYS A 236     -19.221   9.047  68.390  1.00 21.86           C  
ATOM   1850  SG  CYS A 236     -20.588   9.618  67.358  1.00 27.00           S  
ATOM   1851  N   ASP A 237     -15.782   9.732  69.201  1.00 19.33           N  
ATOM   1852  CA  ASP A 237     -14.756   9.426  70.187  1.00 19.63           C  
ATOM   1853  C   ASP A 237     -15.100  10.031  71.550  1.00 19.50           C  
ATOM   1854  O   ASP A 237     -15.604  11.143  71.617  1.00 24.71           O  
ATOM   1855  CB  ASP A 237     -13.413   9.946  69.654  1.00 20.88           C  
ATOM   1856  CG  ASP A 237     -12.370  10.064  70.717  1.00 23.10           C  
ATOM   1857  OD1 ASP A 237     -12.391   9.262  71.683  1.00 28.15           O  
ATOM   1858  OD2 ASP A 237     -11.516  10.962  70.568  1.00 22.50           O  
ATOM   1859  N   ARG A 238     -14.849   9.284  72.620  1.00 21.60           N  
ATOM   1860  CA  ARG A 238     -15.118   9.716  73.994  1.00 23.93           C  
ATOM   1861  C   ARG A 238     -16.537   9.462  74.483  1.00 25.51           C  
ATOM   1862  O   ARG A 238     -16.860   9.750  75.640  1.00 25.60           O  
ATOM   1863  CB  ARG A 238     -14.803  11.191  74.170  1.00 27.47           C  
ATOM   1864  CG  ARG A 238     -13.355  11.524  73.957  1.00 35.53           C  
ATOM   1865  CD  ARG A 238     -13.043  12.961  74.385  1.00 38.14           C  
ATOM   1866  NE  ARG A 238     -11.647  13.051  74.809  1.00 39.04           N  
ATOM   1867  CZ  ARG A 238     -10.631  13.358  74.005  1.00 41.81           C  
ATOM   1868  NH1 ARG A 238     -10.844  13.627  72.714  1.00 44.36           N  
ATOM   1869  NH2 ARG A 238      -9.395  13.368  74.486  1.00 40.24           N  
ATOM   1870  N   GLN A 239     -17.385   8.916  73.619  1.00 26.71           N  
ATOM   1871  CA  GLN A 239     -18.768   8.630  74.005  1.00 26.97           C  
ATOM   1872  C   GLN A 239     -19.084   7.141  74.136  1.00 26.38           C  
ATOM   1873  O   GLN A 239     -18.615   6.322  73.343  1.00 26.31           O  
ATOM   1874  CB  GLN A 239     -19.717   9.191  72.974  1.00 29.00           C  
ATOM   1875  CG  GLN A 239     -19.533  10.622  72.688  1.00 36.57           C  
ATOM   1876  CD  GLN A 239     -20.390  11.032  71.537  1.00 39.99           C  
ATOM   1877  OE1 GLN A 239     -21.586  10.741  71.509  1.00 41.42           O  
ATOM   1878  NE2 GLN A 239     -19.792  11.709  70.569  1.00 44.30           N  
ATOM   1879  N   SER A 240     -19.900   6.786  75.125  1.00 25.84           N  
ATOM   1880  CA  SER A 240     -20.287   5.392  75.290  1.00 24.84           C  
ATOM   1881  C   SER A 240     -21.039   4.985  74.017  1.00 24.29           C  
ATOM   1882  O   SER A 240     -21.755   5.808  73.440  1.00 21.39           O  
ATOM   1883  CB  SER A 240     -21.206   5.241  76.495  1.00 26.59           C  
ATOM   1884  OG  SER A 240     -21.775   3.938  76.522  1.00 29.98           O  
ATOM   1885  N   GLN A 241     -20.876   3.731  73.581  1.00 21.85           N  
ATOM   1886  CA  GLN A 241     -21.552   3.249  72.369  1.00 19.83           C  
ATOM   1887  C   GLN A 241     -22.865   2.617  72.744  1.00 17.77           C  
ATOM   1888  O   GLN A 241     -23.676   2.263  71.876  1.00 16.64           O  
ATOM   1889  CB  GLN A 241     -20.746   2.162  71.666  1.00 17.14           C  
ATOM   1890  CG  GLN A 241     -19.304   2.464  71.412  1.00 21.09           C  
ATOM   1891  CD  GLN A 241     -18.624   1.284  70.765  1.00 24.84           C  
ATOM   1892  OE1 GLN A 241     -18.944   0.919  69.629  1.00 26.87           O  
ATOM   1893  NE2 GLN A 241     -17.692   0.661  71.489  1.00 23.04           N  
ATOM   1894  N   VAL A 242     -23.064   2.458  74.045  1.00 18.55           N  
ATOM   1895  CA  VAL A 242     -24.260   1.797  74.546  1.00 19.24           C  
ATOM   1896  C   VAL A 242     -25.485   2.665  74.616  1.00 20.22           C  
ATOM   1897  O   VAL A 242     -25.477   3.691  75.287  1.00 24.44           O  
ATOM   1898  CB  VAL A 242     -24.027   1.232  75.949  1.00 18.34           C  
ATOM   1899  CG1 VAL A 242     -25.136   0.278  76.293  1.00 16.79           C  
ATOM   1900  CG2 VAL A 242     -22.664   0.564  76.026  1.00 16.26           C  
ATOM   1901  N   ASP A 243     -26.541   2.257  73.926  1.00 20.48           N  
ATOM   1902  CA  ASP A 243     -27.792   3.000  73.962  1.00 24.58           C  
ATOM   1903  C   ASP A 243     -28.348   2.750  75.362  1.00 25.25           C  
ATOM   1904  O   ASP A 243     -28.850   1.662  75.644  1.00 27.72           O  
ATOM   1905  CB  ASP A 243     -28.775   2.447  72.936  1.00 25.69           C  
ATOM   1906  CG  ASP A 243     -30.051   3.270  72.851  1.00 29.95           C  
ATOM   1907  OD1 ASP A 243     -30.455   3.881  73.875  1.00 32.44           O  
ATOM   1908  OD2 ASP A 243     -30.660   3.298  71.755  1.00 31.33           O  
ATOM   1909  N   PHE A 244     -28.259   3.731  76.248  1.00 24.02           N  
ATOM   1910  CA  PHE A 244     -28.773   3.519  77.589  1.00 24.97           C  
ATOM   1911  C   PHE A 244     -30.273   3.221  77.622  1.00 27.30           C  
ATOM   1912  O   PHE A 244     -30.774   2.657  78.599  1.00 28.31           O  
ATOM   1913  CB  PHE A 244     -28.466   4.726  78.465  1.00 22.74           C  
ATOM   1914  CG  PHE A 244     -27.058   4.745  78.997  1.00 19.02           C  
ATOM   1915  CD1 PHE A 244     -26.003   4.261  78.227  1.00 17.33           C  
ATOM   1916  CD2 PHE A 244     -26.780   5.301  80.243  1.00 14.82           C  
ATOM   1917  CE1 PHE A 244     -24.703   4.335  78.681  1.00 14.68           C  
ATOM   1918  CE2 PHE A 244     -25.483   5.377  80.705  1.00 13.65           C  
ATOM   1919  CZ  PHE A 244     -24.441   4.893  79.920  1.00 16.87           C  
ATOM   1920  N   ASP A 245     -30.984   3.581  76.556  1.00 29.24           N  
ATOM   1921  CA  ASP A 245     -32.429   3.349  76.486  1.00 31.70           C  
ATOM   1922  C   ASP A 245     -32.780   1.945  76.027  1.00 32.79           C  
ATOM   1923  O   ASP A 245     -33.949   1.569  76.025  1.00 31.84           O  
ATOM   1924  CB  ASP A 245     -33.078   4.346  75.529  1.00 35.77           C  
ATOM   1925  CG  ASP A 245     -33.098   5.746  76.079  1.00 40.83           C  
ATOM   1926  OD1 ASP A 245     -32.838   6.692  75.302  1.00 44.56           O  
ATOM   1927  OD2 ASP A 245     -33.380   5.899  77.288  1.00 42.85           O  
ATOM   1928  N   ASN A 246     -31.769   1.176  75.622  1.00 34.00           N  
ATOM   1929  CA  ASN A 246     -31.984  -0.190  75.134  1.00 31.97           C  
ATOM   1930  C   ASN A 246     -30.622  -0.848  74.964  1.00 27.98           C  
ATOM   1931  O   ASN A 246     -30.203  -1.165  73.836  1.00 28.03           O  
ATOM   1932  CB  ASN A 246     -32.706  -0.155  73.782  1.00 34.42           C  
ATOM   1933  CG  ASN A 246     -33.181  -1.530  73.330  1.00 37.63           C  
ATOM   1934  OD1 ASN A 246     -33.526  -1.714  72.161  1.00 38.61           O  
ATOM   1935  ND2 ASN A 246     -33.214  -2.501  74.257  1.00 40.23           N  
ATOM   1936  N   PRO A 247     -29.923  -1.088  76.089  1.00 25.59           N  
ATOM   1937  CA  PRO A 247     -28.595  -1.709  76.022  1.00 26.33           C  
ATOM   1938  C   PRO A 247     -28.618  -3.018  75.246  1.00 27.01           C  
ATOM   1939  O   PRO A 247     -29.615  -3.755  75.260  1.00 27.47           O  
ATOM   1940  CB  PRO A 247     -28.210  -1.944  77.483  1.00 24.02           C  
ATOM   1941  CG  PRO A 247     -29.303  -1.271  78.310  1.00 25.29           C  
ATOM   1942  CD  PRO A 247     -30.517  -1.234  77.428  1.00 25.48           C  
ATOM   1943  N   ASP A 248     -27.505  -3.298  74.578  1.00 27.20           N  
ATOM   1944  CA  ASP A 248     -27.360  -4.504  73.790  1.00 27.50           C  
ATOM   1945  C   ASP A 248     -26.350  -5.371  74.514  1.00 28.29           C  
ATOM   1946  O   ASP A 248     -25.176  -5.437  74.138  1.00 28.56           O  
ATOM   1947  CB  ASP A 248     -26.838  -4.157  72.404  1.00 28.69           C  
ATOM   1948  CG  ASP A 248     -26.740  -5.360  71.513  1.00 30.42           C  
ATOM   1949  OD1 ASP A 248     -26.741  -6.498  72.049  1.00 30.45           O  
ATOM   1950  OD2 ASP A 248     -26.649  -5.166  70.283  1.00 29.11           O  
ATOM   1951  N   TYR A 249     -26.816  -6.034  75.562  1.00 28.93           N  
ATOM   1952  CA  TYR A 249     -25.958  -6.887  76.368  1.00 30.27           C  
ATOM   1953  C   TYR A 249     -25.217  -7.968  75.577  1.00 30.66           C  
ATOM   1954  O   TYR A 249     -24.338  -8.643  76.118  1.00 31.49           O  
ATOM   1955  CB  TYR A 249     -26.789  -7.510  77.487  1.00 31.30           C  
ATOM   1956  CG  TYR A 249     -27.477  -6.475  78.345  1.00 31.11           C  
ATOM   1957  CD1 TYR A 249     -28.850  -6.267  78.264  1.00 31.44           C  
ATOM   1958  CD2 TYR A 249     -26.751  -5.702  79.244  1.00 32.16           C  
ATOM   1959  CE1 TYR A 249     -29.483  -5.313  79.069  1.00 32.82           C  
ATOM   1960  CE2 TYR A 249     -27.369  -4.754  80.048  1.00 32.81           C  
ATOM   1961  CZ  TYR A 249     -28.728  -4.568  79.960  1.00 33.48           C  
ATOM   1962  OH  TYR A 249     -29.333  -3.655  80.792  1.00 38.10           O  
ATOM   1963  N   GLU A 250     -25.560  -8.134  74.303  1.00 30.54           N  
ATOM   1964  CA  GLU A 250     -24.881  -9.129  73.472  1.00 33.76           C  
ATOM   1965  C   GLU A 250     -23.510  -8.598  73.026  1.00 31.21           C  
ATOM   1966  O   GLU A 250     -22.544  -9.358  72.920  1.00 30.16           O  
ATOM   1967  CB  GLU A 250     -25.722  -9.462  72.232  1.00 38.93           C  
ATOM   1968  CG  GLU A 250     -27.138  -9.960  72.536  1.00 49.63           C  
ATOM   1969  CD  GLU A 250     -27.155 -11.149  73.498  1.00 56.74           C  
ATOM   1970  OE1 GLU A 250     -26.286 -12.043  73.358  1.00 58.97           O  
ATOM   1971  OE2 GLU A 250     -28.044 -11.195  74.386  1.00 58.77           O  
ATOM   1972  N   ARG A 251     -23.444  -7.288  72.772  1.00 30.66           N  
ATOM   1973  CA  ARG A 251     -22.220  -6.618  72.334  1.00 27.67           C  
ATOM   1974  C   ARG A 251     -21.516  -5.884  73.478  1.00 27.16           C  
ATOM   1975  O   ARG A 251     -20.296  -5.707  73.456  1.00 26.03           O  
ATOM   1976  CB  ARG A 251     -22.546  -5.595  71.253  1.00 28.83           C  
ATOM   1977  CG  ARG A 251     -23.417  -6.120  70.118  1.00 31.53           C  
ATOM   1978  CD  ARG A 251     -23.760  -4.996  69.160  1.00 30.93           C  
ATOM   1979  NE  ARG A 251     -22.559  -4.250  68.791  1.00 34.33           N  
ATOM   1980  CZ  ARG A 251     -22.544  -2.947  68.527  1.00 36.57           C  
ATOM   1981  NH1 ARG A 251     -23.665  -2.242  68.587  1.00 37.51           N  
ATOM   1982  NH2 ARG A 251     -21.404  -2.345  68.221  1.00 39.89           N  
ATOM   1983  N   PHE A 252     -22.284  -5.450  74.474  1.00 24.23           N  
ATOM   1984  CA  PHE A 252     -21.713  -4.714  75.595  1.00 21.38           C  
ATOM   1985  C   PHE A 252     -22.150  -5.376  76.885  1.00 22.15           C  
ATOM   1986  O   PHE A 252     -22.771  -4.759  77.750  1.00 26.33           O  
ATOM   1987  CB  PHE A 252     -22.193  -3.268  75.521  1.00 20.07           C  
ATOM   1988  CG  PHE A 252     -22.044  -2.669  74.151  1.00 15.26           C  
ATOM   1989  CD1 PHE A 252     -23.152  -2.205  73.452  1.00 11.83           C  
ATOM   1990  CD2 PHE A 252     -20.790  -2.604  73.543  1.00 13.50           C  
ATOM   1991  CE1 PHE A 252     -23.021  -1.674  72.141  1.00 11.63           C  
ATOM   1992  CE2 PHE A 252     -20.641  -2.075  72.233  1.00 12.42           C  
ATOM   1993  CZ  PHE A 252     -21.769  -1.610  71.532  1.00  9.11           C  
ATOM   1994  N   PRO A 253     -21.807  -6.656  77.037  1.00 22.87           N  
ATOM   1995  CA  PRO A 253     -22.181  -7.411  78.228  1.00 22.16           C  
ATOM   1996  C   PRO A 253     -21.848  -6.765  79.567  1.00 23.16           C  
ATOM   1997  O   PRO A 253     -22.644  -6.837  80.517  1.00 23.98           O  
ATOM   1998  CB  PRO A 253     -21.470  -8.753  78.024  1.00 20.31           C  
ATOM   1999  CG  PRO A 253     -20.267  -8.385  77.220  1.00 20.00           C  
ATOM   2000  CD  PRO A 253     -20.841  -7.408  76.218  1.00 22.50           C  
ATOM   2001  N   ASN A 254     -20.696  -6.120  79.662  1.00 23.90           N  
ATOM   2002  CA  ASN A 254     -20.326  -5.552  80.944  1.00 26.94           C  
ATOM   2003  C   ASN A 254     -21.108  -4.320  81.344  1.00 27.11           C  
ATOM   2004  O   ASN A 254     -20.877  -3.732  82.406  1.00 26.48           O  
ATOM   2005  CB  ASN A 254     -18.820  -5.317  80.976  1.00 26.12           C  
ATOM   2006  CG  ASN A 254     -18.053  -6.631  81.028  1.00 29.89           C  
ATOM   2007  OD1 ASN A 254     -18.107  -7.343  82.034  1.00 34.57           O  
ATOM   2008  ND2 ASN A 254     -17.366  -6.977  79.941  1.00 28.90           N  
ATOM   2009  N   PHE A 255     -22.058  -3.941  80.500  1.00 29.31           N  
ATOM   2010  CA  PHE A 255     -22.871  -2.790  80.816  1.00 31.08           C  
ATOM   2011  C   PHE A 255     -23.782  -3.190  81.965  1.00 29.92           C  
ATOM   2012  O   PHE A 255     -24.360  -2.344  82.632  1.00 29.64           O  
ATOM   2013  CB  PHE A 255     -23.708  -2.344  79.619  1.00 34.91           C  
ATOM   2014  CG  PHE A 255     -24.564  -1.146  79.914  1.00 41.96           C  
ATOM   2015  CD1 PHE A 255     -23.990   0.030  80.383  1.00 44.22           C  
ATOM   2016  CD2 PHE A 255     -25.949  -1.206  79.794  1.00 44.22           C  
ATOM   2017  CE1 PHE A 255     -24.783   1.123  80.735  1.00 45.63           C  
ATOM   2018  CE2 PHE A 255     -26.748  -0.114  80.143  1.00 44.30           C  
ATOM   2019  CZ  PHE A 255     -26.164   1.047  80.616  1.00 44.33           C  
ATOM   2020  N   GLN A 256     -23.889  -4.492  82.201  1.00 29.38           N  
ATOM   2021  CA  GLN A 256     -24.731  -5.009  83.275  1.00 29.98           C  
ATOM   2022  C   GLN A 256     -24.041  -4.886  84.611  1.00 27.31           C  
ATOM   2023  O   GLN A 256     -24.626  -5.204  85.633  1.00 30.08           O  
ATOM   2024  CB  GLN A 256     -25.075  -6.482  83.056  1.00 32.28           C  
ATOM   2025  CG  GLN A 256     -25.486  -6.817  81.655  1.00 38.71           C  
ATOM   2026  CD  GLN A 256     -26.534  -7.907  81.600  1.00 44.14           C  
ATOM   2027  OE1 GLN A 256     -26.253  -9.075  81.891  1.00 45.38           O  
ATOM   2028  NE2 GLN A 256     -27.762  -7.530  81.233  1.00 44.44           N  
ATOM   2029  N   ASN A 257     -22.790  -4.455  84.602  1.00 28.30           N  
ATOM   2030  CA  ASN A 257     -22.040  -4.287  85.839  1.00 28.43           C  
ATOM   2031  C   ASN A 257     -21.834  -2.783  86.112  1.00 29.75           C  
ATOM   2032  O   ASN A 257     -21.201  -2.391  87.099  1.00 30.31           O  
ATOM   2033  CB  ASN A 257     -20.688  -4.994  85.725  1.00 24.19           C  
ATOM   2034  CG  ASN A 257     -20.832  -6.498  85.521  1.00 28.05           C  
ATOM   2035  OD1 ASN A 257     -21.379  -7.200  86.376  1.00 28.50           O  
ATOM   2036  ND2 ASN A 257     -20.335  -7.004  84.389  1.00 29.16           N  
ATOM   2037  N   VAL A 258     -22.375  -1.933  85.244  1.00 30.72           N  
ATOM   2038  CA  VAL A 258     -22.187  -0.502  85.433  1.00 31.86           C  
ATOM   2039  C   VAL A 258     -22.925  -0.016  86.671  1.00 32.78           C  
ATOM   2040  O   VAL A 258     -23.969  -0.535  87.038  1.00 34.32           O  
ATOM   2041  CB  VAL A 258     -22.642   0.309  84.195  1.00 30.09           C  
ATOM   2042  CG1 VAL A 258     -24.128   0.598  84.249  1.00 27.35           C  
ATOM   2043  CG2 VAL A 258     -21.852   1.573  84.122  1.00 29.29           C  
ATOM   2044  N   VAL A 259     -22.364   0.988  87.317  1.00 34.94           N  
ATOM   2045  CA  VAL A 259     -22.934   1.544  88.531  1.00 36.38           C  
ATOM   2046  C   VAL A 259     -22.401   2.958  88.640  1.00 36.51           C  
ATOM   2047  O   VAL A 259     -21.189   3.157  88.701  1.00 37.28           O  
ATOM   2048  CB  VAL A 259     -22.470   0.746  89.774  1.00 37.34           C  
ATOM   2049  CG1 VAL A 259     -22.729   1.558  91.040  1.00 36.95           C  
ATOM   2050  CG2 VAL A 259     -23.199  -0.600  89.840  1.00 35.42           C  
ATOM   2051  N   GLY A 260     -23.290   3.940  88.667  1.00 36.03           N  
ATOM   2052  CA  GLY A 260     -22.822   5.308  88.767  1.00 38.22           C  
ATOM   2053  C   GLY A 260     -23.414   6.129  89.896  1.00 36.76           C  
ATOM   2054  O   GLY A 260     -24.323   5.687  90.601  1.00 37.03           O  
ATOM   2055  N   TYR A 261     -22.876   7.332  90.070  1.00 36.01           N  
ATOM   2056  CA  TYR A 261     -23.355   8.242  91.091  1.00 33.25           C  
ATOM   2057  C   TYR A 261     -24.319   9.148  90.376  1.00 32.37           C  
ATOM   2058  O   TYR A 261     -24.117   9.447  89.206  1.00 34.47           O  
ATOM   2059  CB  TYR A 261     -22.198   9.063  91.650  1.00 32.88           C  
ATOM   2060  CG  TYR A 261     -21.078   8.198  92.159  1.00 34.79           C  
ATOM   2061  CD1 TYR A 261     -20.265   7.498  91.271  1.00 36.33           C  
ATOM   2062  CD2 TYR A 261     -20.878   8.012  93.527  1.00 35.29           C  
ATOM   2063  CE1 TYR A 261     -19.283   6.630  91.729  1.00 37.47           C  
ATOM   2064  CE2 TYR A 261     -19.901   7.142  93.998  1.00 35.35           C  
ATOM   2065  CZ  TYR A 261     -19.107   6.454  93.092  1.00 37.47           C  
ATOM   2066  OH  TYR A 261     -18.136   5.579  93.534  1.00 38.88           O  
ATOM   2067  N   GLU A 262     -25.386   9.566  91.043  1.00 32.23           N  
ATOM   2068  CA  GLU A 262     -26.317  10.471  90.387  1.00 33.30           C  
ATOM   2069  C   GLU A 262     -26.867  11.537  91.318  1.00 32.30           C  
ATOM   2070  O   GLU A 262     -26.840  11.400  92.541  1.00 30.61           O  
ATOM   2071  CB  GLU A 262     -27.473   9.709  89.735  1.00 31.79           C  
ATOM   2072  CG  GLU A 262     -28.571   9.263  90.660  1.00 34.36           C  
ATOM   2073  CD  GLU A 262     -29.796   8.793  89.889  1.00 38.18           C  
ATOM   2074  OE1 GLU A 262     -30.496   9.640  89.284  1.00 37.92           O  
ATOM   2075  OE2 GLU A 262     -30.053   7.571  89.872  1.00 40.85           O  
ATOM   2076  N   THR A 263     -27.357  12.610  90.715  1.00 32.35           N  
ATOM   2077  CA  THR A 263     -27.917  13.705  91.469  1.00 31.45           C  
ATOM   2078  C   THR A 263     -28.726  14.609  90.558  1.00 32.17           C  
ATOM   2079  O   THR A 263     -28.598  14.571  89.326  1.00 32.10           O  
ATOM   2080  CB  THR A 263     -26.816  14.540  92.116  1.00 32.11           C  
ATOM   2081  OG1 THR A 263     -27.271  15.015  93.387  1.00 34.68           O  
ATOM   2082  CG2 THR A 263     -26.463  15.726  91.231  1.00 33.04           C  
ATOM   2083  N   VAL A 264     -29.565  15.424  91.178  1.00 31.06           N  
ATOM   2084  CA  VAL A 264     -30.384  16.362  90.441  1.00 31.05           C  
ATOM   2085  C   VAL A 264     -29.957  17.759  90.867  1.00 31.91           C  
ATOM   2086  O   VAL A 264     -29.996  18.103  92.053  1.00 31.76           O  
ATOM   2087  CB  VAL A 264     -31.863  16.140  90.745  1.00 29.78           C  
ATOM   2088  CG1 VAL A 264     -32.700  17.222  90.098  1.00 31.00           C  
ATOM   2089  CG2 VAL A 264     -32.272  14.783  90.227  1.00 30.46           C  
ATOM   2090  N   VAL A 265     -29.529  18.557  89.900  1.00 30.68           N  
ATOM   2091  CA  VAL A 265     -29.091  19.909  90.195  1.00 29.89           C  
ATOM   2092  C   VAL A 265     -30.185  20.923  89.912  1.00 29.84           C  
ATOM   2093  O   VAL A 265     -30.884  20.836  88.894  1.00 27.34           O  
ATOM   2094  CB  VAL A 265     -27.861  20.294  89.360  1.00 29.79           C  
ATOM   2095  CG1 VAL A 265     -26.730  19.336  89.637  1.00 29.49           C  
ATOM   2096  CG2 VAL A 265     -28.222  20.289  87.877  1.00 30.62           C  
ATOM   2097  N   GLY A 266     -30.321  21.880  90.825  1.00 30.35           N  
ATOM   2098  CA  GLY A 266     -31.306  22.939  90.673  1.00 30.70           C  
ATOM   2099  C   GLY A 266     -30.632  24.300  90.680  1.00 30.89           C  
ATOM   2100  O   GLY A 266     -29.439  24.386  90.956  1.00 31.59           O  
ATOM   2101  N   PRO A 267     -31.372  25.383  90.417  1.00 31.06           N  
ATOM   2102  CA  PRO A 267     -30.903  26.766  90.371  1.00 32.63           C  
ATOM   2103  C   PRO A 267     -29.579  27.190  90.996  1.00 35.14           C  
ATOM   2104  O   PRO A 267     -28.688  27.647  90.277  1.00 36.57           O  
ATOM   2105  CB  PRO A 267     -32.092  27.523  90.910  1.00 32.75           C  
ATOM   2106  CG  PRO A 267     -33.192  26.856  90.151  1.00 32.13           C  
ATOM   2107  CD  PRO A 267     -32.842  25.360  90.302  1.00 33.14           C  
ATOM   2108  N   GLY A 268     -29.396  27.057  92.298  1.00 34.15           N  
ATOM   2109  CA  GLY A 268     -28.116  27.512  92.820  1.00 35.66           C  
ATOM   2110  C   GLY A 268     -26.989  26.506  92.995  1.00 36.75           C  
ATOM   2111  O   GLY A 268     -25.982  26.818  93.649  1.00 37.81           O  
ATOM   2112  N   ASP A 269     -27.122  25.320  92.399  1.00 36.04           N  
ATOM   2113  CA  ASP A 269     -26.123  24.265  92.579  1.00 33.21           C  
ATOM   2114  C   ASP A 269     -24.995  24.224  91.574  1.00 31.93           C  
ATOM   2115  O   ASP A 269     -25.178  24.561  90.410  1.00 34.43           O  
ATOM   2116  CB  ASP A 269     -26.806  22.890  92.591  1.00 31.60           C  
ATOM   2117  CG  ASP A 269     -27.933  22.792  93.611  1.00 30.95           C  
ATOM   2118  OD1 ASP A 269     -27.787  23.349  94.725  1.00 31.31           O  
ATOM   2119  OD2 ASP A 269     -28.965  22.146  93.304  1.00 31.32           O  
ATOM   2120  N   VAL A 270     -23.823  23.804  92.037  1.00 31.95           N  
ATOM   2121  CA  VAL A 270     -22.643  23.651  91.184  1.00 31.25           C  
ATOM   2122  C   VAL A 270     -22.107  22.230  91.383  1.00 31.16           C  
ATOM   2123  O   VAL A 270     -21.744  21.831  92.500  1.00 32.01           O  
ATOM   2124  CB  VAL A 270     -21.523  24.626  91.556  1.00 31.43           C  
ATOM   2125  CG1 VAL A 270     -20.294  24.323  90.728  1.00 32.06           C  
ATOM   2126  CG2 VAL A 270     -21.971  26.056  91.327  1.00 32.36           C  
ATOM   2127  N   LEU A 271     -22.073  21.458  90.306  1.00 27.87           N  
ATOM   2128  CA  LEU A 271     -21.580  20.100  90.392  1.00 26.85           C  
ATOM   2129  C   LEU A 271     -20.173  19.976  89.839  1.00 25.60           C  
ATOM   2130  O   LEU A 271     -19.884  20.435  88.733  1.00 25.01           O  
ATOM   2131  CB  LEU A 271     -22.496  19.162  89.614  1.00 25.80           C  
ATOM   2132  CG  LEU A 271     -21.875  17.808  89.246  1.00 24.75           C  
ATOM   2133  CD1 LEU A 271     -21.588  16.989  90.512  1.00 22.78           C  
ATOM   2134  CD2 LEU A 271     -22.824  17.073  88.318  1.00 22.91           C  
ATOM   2135  N   TYR A 272     -19.295  19.358  90.613  1.00 24.23           N  
ATOM   2136  CA  TYR A 272     -17.930  19.138  90.169  1.00 24.32           C  
ATOM   2137  C   TYR A 272     -17.965  17.821  89.423  1.00 25.22           C  
ATOM   2138  O   TYR A 272     -18.589  16.855  89.895  1.00 28.63           O  
ATOM   2139  CB  TYR A 272     -16.988  18.995  91.361  1.00 21.62           C  
ATOM   2140  CG  TYR A 272     -15.583  18.519  91.024  1.00 18.41           C  
ATOM   2141  CD1 TYR A 272     -14.929  17.595  91.842  1.00 18.60           C  
ATOM   2142  CD2 TYR A 272     -14.887  19.029  89.931  1.00 18.19           C  
ATOM   2143  CE1 TYR A 272     -13.614  17.185  91.581  1.00 17.61           C  
ATOM   2144  CE2 TYR A 272     -13.569  18.633  89.660  1.00 17.74           C  
ATOM   2145  CZ  TYR A 272     -12.945  17.706  90.490  1.00 18.10           C  
ATOM   2146  OH  TYR A 272     -11.665  17.273  90.219  1.00 20.78           O  
ATOM   2147  N   ILE A 273     -17.325  17.776  88.258  1.00 25.10           N  
ATOM   2148  CA  ILE A 273     -17.253  16.538  87.491  1.00 24.76           C  
ATOM   2149  C   ILE A 273     -15.769  16.312  87.219  1.00 24.68           C  
ATOM   2150  O   ILE A 273     -15.225  16.818  86.231  1.00 26.58           O  
ATOM   2151  CB  ILE A 273     -18.003  16.639  86.162  1.00 20.22           C  
ATOM   2152  CG1 ILE A 273     -19.425  17.127  86.405  1.00 21.11           C  
ATOM   2153  CG2 ILE A 273     -18.067  15.279  85.520  1.00 19.91           C  
ATOM   2154  CD1 ILE A 273     -20.268  17.252  85.134  1.00 21.36           C  
ATOM   2155  N   PRO A 274     -15.086  15.564  88.105  1.00 24.44           N  
ATOM   2156  CA  PRO A 274     -13.652  15.301  87.919  1.00 25.62           C  
ATOM   2157  C   PRO A 274     -13.328  14.856  86.501  1.00 24.41           C  
ATOM   2158  O   PRO A 274     -14.096  14.143  85.862  1.00 26.36           O  
ATOM   2159  CB  PRO A 274     -13.346  14.229  88.979  1.00 22.93           C  
ATOM   2160  CG  PRO A 274     -14.697  13.593  89.250  1.00 21.50           C  
ATOM   2161  CD  PRO A 274     -15.632  14.766  89.217  1.00 23.75           C  
HETATM 2162  N   MSE A 275     -12.189  15.306  86.006  1.00 26.50           N  
HETATM 2163  CA  MSE A 275     -11.767  14.975  84.665  1.00 29.87           C  
HETATM 2164  C   MSE A 275     -11.835  13.466  84.438  1.00 28.98           C  
HETATM 2165  O   MSE A 275     -11.742  12.673  85.390  1.00 28.10           O  
HETATM 2166  CB  MSE A 275     -10.343  15.461  84.460  1.00 35.33           C  
HETATM 2167  CG  MSE A 275      -9.358  14.773  85.389  1.00 43.50           C  
HETATM 2168 SE   MSE A 275      -7.512  15.404  85.222  1.00 54.92          SE  
HETATM 2169  CE  MSE A 275      -7.478  15.633  83.270  1.00 45.47           C  
ATOM   2170  N   TYR A 276     -12.010  13.079  83.174  1.00 26.31           N  
ATOM   2171  CA  TYR A 276     -12.067  11.673  82.787  1.00 25.82           C  
ATOM   2172  C   TYR A 276     -13.325  10.900  83.164  1.00 24.44           C  
ATOM   2173  O   TYR A 276     -13.608   9.846  82.573  1.00 24.14           O  
ATOM   2174  CB  TYR A 276     -10.850  10.951  83.335  1.00 24.46           C  
ATOM   2175  CG  TYR A 276      -9.637  11.161  82.478  1.00 27.75           C  
ATOM   2176  CD1 TYR A 276      -8.483  11.741  82.998  1.00 31.94           C  
ATOM   2177  CD2 TYR A 276      -9.633  10.769  81.137  1.00 27.74           C  
ATOM   2178  CE1 TYR A 276      -7.348  11.922  82.205  1.00 33.14           C  
ATOM   2179  CE2 TYR A 276      -8.511  10.946  80.341  1.00 28.85           C  
ATOM   2180  CZ  TYR A 276      -7.372  11.521  80.880  1.00 31.75           C  
ATOM   2181  OH  TYR A 276      -6.246  11.680  80.100  1.00 34.08           O  
ATOM   2182  N   TRP A 277     -14.072  11.413  84.140  1.00 19.59           N  
ATOM   2183  CA  TRP A 277     -15.294  10.752  84.573  1.00 18.37           C  
ATOM   2184  C   TRP A 277     -16.294  10.737  83.455  1.00 19.41           C  
ATOM   2185  O   TRP A 277     -16.158  11.480  82.489  1.00 23.33           O  
ATOM   2186  CB  TRP A 277     -15.900  11.471  85.771  1.00 16.78           C  
ATOM   2187  CG  TRP A 277     -15.295  11.046  87.060  1.00  9.96           C  
ATOM   2188  CD1 TRP A 277     -13.963  11.092  87.412  1.00  9.19           C  
ATOM   2189  CD2 TRP A 277     -15.982  10.461  88.155  1.00  6.12           C  
ATOM   2190  NE1 TRP A 277     -13.789  10.557  88.673  1.00  7.75           N  
ATOM   2191  CE2 TRP A 277     -15.015  10.163  89.151  1.00  7.27           C  
ATOM   2192  CE3 TRP A 277     -17.326  10.153  88.399  1.00  6.67           C  
ATOM   2193  CZ2 TRP A 277     -15.355   9.572  90.372  1.00  5.19           C  
ATOM   2194  CZ3 TRP A 277     -17.666   9.566  89.616  1.00  6.27           C  
ATOM   2195  CH2 TRP A 277     -16.684   9.281  90.584  1.00  6.76           C  
ATOM   2196  N   TRP A 278     -17.314   9.907  83.591  1.00 18.75           N  
ATOM   2197  CA  TRP A 278     -18.335   9.808  82.561  1.00 19.04           C  
ATOM   2198  C   TRP A 278     -19.579  10.538  83.007  1.00 18.64           C  
ATOM   2199  O   TRP A 278     -20.132  10.203  84.054  1.00 18.40           O  
ATOM   2200  CB  TRP A 278     -18.735   8.335  82.314  1.00 18.40           C  
ATOM   2201  CG  TRP A 278     -17.657   7.442  81.743  1.00 17.47           C  
ATOM   2202  CD1 TRP A 278     -16.618   6.878  82.414  1.00 17.04           C  
ATOM   2203  CD2 TRP A 278     -17.529   7.021  80.376  1.00 16.35           C  
ATOM   2204  NE1 TRP A 278     -15.843   6.125  81.549  1.00 19.08           N  
ATOM   2205  CE2 TRP A 278     -16.383   6.199  80.295  1.00 16.36           C  
ATOM   2206  CE3 TRP A 278     -18.269   7.264  79.215  1.00 16.24           C  
ATOM   2207  CZ2 TRP A 278     -15.961   5.617  79.098  1.00 16.09           C  
ATOM   2208  CZ3 TRP A 278     -17.852   6.687  78.027  1.00 18.29           C  
ATOM   2209  CH2 TRP A 278     -16.707   5.872  77.976  1.00 15.72           C  
ATOM   2210  N   HIS A 279     -20.041  11.528  82.252  1.00 18.78           N  
ATOM   2211  CA  HIS A 279     -21.282  12.138  82.674  1.00 20.04           C  
ATOM   2212  C   HIS A 279     -22.394  11.970  81.663  1.00 19.67           C  
ATOM   2213  O   HIS A 279     -22.160  11.903  80.463  1.00 19.63           O  
ATOM   2214  CB  HIS A 279     -21.122  13.617  83.090  1.00 24.98           C  
ATOM   2215  CG  HIS A 279     -20.487  14.513  82.069  1.00 28.87           C  
ATOM   2216  ND1 HIS A 279     -19.133  14.495  81.793  1.00 30.41           N  
ATOM   2217  CD2 HIS A 279     -21.001  15.547  81.356  1.00 29.47           C  
ATOM   2218  CE1 HIS A 279     -18.842  15.480  80.963  1.00 30.41           C  
ATOM   2219  NE2 HIS A 279     -19.957  16.135  80.683  1.00 31.91           N  
ATOM   2220  N   HIS A 280     -23.613  11.867  82.183  1.00 19.82           N  
ATOM   2221  CA  HIS A 280     -24.825  11.692  81.389  1.00 20.77           C  
ATOM   2222  C   HIS A 280     -25.795  12.751  81.922  1.00 21.02           C  
ATOM   2223  O   HIS A 280     -26.182  12.688  83.084  1.00 22.19           O  
ATOM   2224  CB  HIS A 280     -25.356  10.273  81.640  1.00 21.97           C  
ATOM   2225  CG  HIS A 280     -26.724  10.011  81.092  1.00 21.52           C  
ATOM   2226  ND1 HIS A 280     -27.853  10.640  81.573  1.00 21.79           N  
ATOM   2227  CD2 HIS A 280     -27.148   9.176  80.111  1.00 20.23           C  
ATOM   2228  CE1 HIS A 280     -28.914  10.206  80.912  1.00 20.90           C  
ATOM   2229  NE2 HIS A 280     -28.513   9.319  80.019  1.00 19.06           N  
ATOM   2230  N   ILE A 281     -26.164  13.730  81.092  1.00 20.44           N  
ATOM   2231  CA  ILE A 281     -27.072  14.816  81.511  1.00 17.94           C  
ATOM   2232  C   ILE A 281     -28.459  14.808  80.847  1.00 19.01           C  
ATOM   2233  O   ILE A 281     -28.564  14.668  79.624  1.00 18.59           O  
ATOM   2234  CB  ILE A 281     -26.463  16.209  81.202  1.00 17.99           C  
ATOM   2235  CG1 ILE A 281     -25.061  16.332  81.796  1.00 17.91           C  
ATOM   2236  CG2 ILE A 281     -27.372  17.302  81.764  1.00 14.98           C  
ATOM   2237  CD1 ILE A 281     -25.029  16.323  83.324  1.00 22.96           C  
ATOM   2238  N   GLU A 282     -29.515  14.978  81.639  1.00 20.85           N  
ATOM   2239  CA  GLU A 282     -30.872  15.029  81.089  1.00 23.64           C  
ATOM   2240  C   GLU A 282     -31.734  16.057  81.808  1.00 24.03           C  
ATOM   2241  O   GLU A 282     -31.758  16.113  83.038  1.00 26.07           O  
ATOM   2242  CB  GLU A 282     -31.566  13.661  81.157  1.00 25.32           C  
ATOM   2243  CG  GLU A 282     -31.703  13.088  82.545  1.00 31.88           C  
ATOM   2244  CD  GLU A 282     -32.608  11.860  82.583  1.00 37.88           C  
ATOM   2245  OE1 GLU A 282     -33.849  12.013  82.424  1.00 38.81           O  
ATOM   2246  OE2 GLU A 282     -32.075  10.743  82.770  1.00 38.75           O  
ATOM   2247  N   SER A 283     -32.430  16.881  81.034  1.00 25.17           N  
ATOM   2248  CA  SER A 283     -33.296  17.899  81.602  1.00 25.45           C  
ATOM   2249  C   SER A 283     -34.592  17.203  81.970  1.00 27.63           C  
ATOM   2250  O   SER A 283     -35.250  16.628  81.101  1.00 31.20           O  
ATOM   2251  CB  SER A 283     -33.556  19.010  80.576  1.00 26.94           C  
ATOM   2252  OG  SER A 283     -32.388  19.794  80.330  1.00 25.36           O  
ATOM   2253  N   LEU A 284     -34.960  17.242  83.248  1.00 28.95           N  
ATOM   2254  CA  LEU A 284     -36.183  16.579  83.700  1.00 31.38           C  
ATOM   2255  C   LEU A 284     -37.379  16.734  82.770  1.00 33.78           C  
ATOM   2256  O   LEU A 284     -37.608  17.793  82.190  1.00 33.97           O  
ATOM   2257  CB  LEU A 284     -36.583  17.054  85.104  1.00 29.76           C  
ATOM   2258  CG  LEU A 284     -35.576  16.788  86.234  1.00 29.47           C  
ATOM   2259  CD1 LEU A 284     -36.262  16.955  87.588  1.00 26.40           C  
ATOM   2260  CD2 LEU A 284     -35.014  15.377  86.118  1.00 29.73           C  
ATOM   2261  N   LEU A 285     -38.131  15.649  82.627  1.00 36.92           N  
ATOM   2262  CA  LEU A 285     -39.332  15.635  81.800  1.00 37.97           C  
ATOM   2263  C   LEU A 285     -40.338  16.587  82.440  1.00 40.60           C  
ATOM   2264  O   LEU A 285     -40.472  16.623  83.672  1.00 39.66           O  
ATOM   2265  CB  LEU A 285     -39.913  14.218  81.751  1.00 32.80           C  
ATOM   2266  CG  LEU A 285     -39.016  13.228  81.011  1.00 30.45           C  
ATOM   2267  CD1 LEU A 285     -39.464  11.797  81.249  1.00 28.54           C  
ATOM   2268  CD2 LEU A 285     -39.045  13.565  79.528  1.00 29.58           C  
ATOM   2269  N   ASN A 286     -41.026  17.364  81.608  1.00 41.97           N  
ATOM   2270  CA  ASN A 286     -42.022  18.313  82.096  1.00 44.07           C  
ATOM   2271  C   ASN A 286     -41.419  19.320  83.070  1.00 43.62           C  
ATOM   2272  O   ASN A 286     -42.128  19.867  83.913  1.00 45.04           O  
ATOM   2273  CB  ASN A 286     -43.171  17.583  82.810  1.00 47.52           C  
ATOM   2274  CG  ASN A 286     -43.811  16.508  81.954  1.00 52.15           C  
ATOM   2275  OD1 ASN A 286     -44.193  16.759  80.803  1.00 54.44           O  
ATOM   2276  ND2 ASN A 286     -43.947  15.301  82.515  1.00 52.62           N  
ATOM   2277  N   GLY A 287     -40.119  19.561  82.977  1.00 43.07           N  
ATOM   2278  CA  GLY A 287     -39.508  20.506  83.892  1.00 41.33           C  
ATOM   2279  C   GLY A 287     -39.310  21.875  83.269  1.00 41.26           C  
ATOM   2280  O   GLY A 287     -38.730  22.773  83.887  1.00 42.30           O  
ATOM   2281  N   GLY A 288     -39.802  22.044  82.045  1.00 39.96           N  
ATOM   2282  CA  GLY A 288     -39.636  23.313  81.365  1.00 36.97           C  
ATOM   2283  C   GLY A 288     -38.198  23.445  80.905  1.00 35.16           C  
ATOM   2284  O   GLY A 288     -37.431  22.474  80.938  1.00 36.23           O  
ATOM   2285  N   ILE A 289     -37.814  24.646  80.492  1.00 32.35           N  
ATOM   2286  CA  ILE A 289     -36.463  24.870  80.008  1.00 30.91           C  
ATOM   2287  C   ILE A 289     -35.412  24.873  81.112  1.00 30.90           C  
ATOM   2288  O   ILE A 289     -35.719  25.146  82.283  1.00 29.72           O  
ATOM   2289  CB  ILE A 289     -36.358  26.203  79.269  1.00 30.19           C  
ATOM   2290  CG1 ILE A 289     -36.755  27.339  80.205  1.00 29.23           C  
ATOM   2291  CG2 ILE A 289     -37.247  26.193  78.040  1.00 27.95           C  
ATOM   2292  CD1 ILE A 289     -35.956  28.614  79.940  1.00 29.14           C  
ATOM   2293  N   THR A 290     -34.168  24.580  80.729  1.00 28.88           N  
ATOM   2294  CA  THR A 290     -33.065  24.571  81.681  1.00 27.92           C  
ATOM   2295  C   THR A 290     -31.958  25.479  81.191  1.00 26.76           C  
ATOM   2296  O   THR A 290     -31.636  25.514  80.013  1.00 29.29           O  
ATOM   2297  CB  THR A 290     -32.474  23.168  81.867  1.00 26.69           C  
ATOM   2298  OG1 THR A 290     -31.805  22.762  80.665  1.00 27.50           O  
ATOM   2299  CG2 THR A 290     -33.576  22.177  82.195  1.00 25.76           C  
ATOM   2300  N   ILE A 291     -31.381  26.234  82.101  1.00 27.21           N  
ATOM   2301  CA  ILE A 291     -30.296  27.115  81.731  1.00 28.04           C  
ATOM   2302  C   ILE A 291     -29.192  26.721  82.679  1.00 28.00           C  
ATOM   2303  O   ILE A 291     -29.457  26.455  83.869  1.00 27.30           O  
ATOM   2304  CB  ILE A 291     -30.639  28.595  81.991  1.00 32.50           C  
ATOM   2305  CG1 ILE A 291     -32.023  28.916  81.437  1.00 34.55           C  
ATOM   2306  CG2 ILE A 291     -29.588  29.496  81.352  1.00 30.65           C  
ATOM   2307  CD1 ILE A 291     -32.446  30.349  81.687  1.00 40.43           C  
ATOM   2308  N   THR A 292     -27.970  26.678  82.160  1.00 26.54           N  
ATOM   2309  CA  THR A 292     -26.812  26.329  82.969  1.00 25.11           C  
ATOM   2310  C   THR A 292     -25.563  26.858  82.271  1.00 28.05           C  
ATOM   2311  O   THR A 292     -25.525  26.961  81.042  1.00 28.53           O  
ATOM   2312  CB  THR A 292     -26.708  24.789  83.160  1.00 22.11           C  
ATOM   2313  OG1 THR A 292     -25.571  24.478  83.966  1.00 19.71           O  
ATOM   2314  CG2 THR A 292     -26.559  24.085  81.829  1.00 18.37           C  
ATOM   2315  N   VAL A 293     -24.561  27.233  83.056  1.00 29.99           N  
ATOM   2316  CA  VAL A 293     -23.304  27.733  82.509  1.00 30.65           C  
ATOM   2317  C   VAL A 293     -22.228  26.783  82.995  1.00 33.75           C  
ATOM   2318  O   VAL A 293     -22.135  26.522  84.201  1.00 34.78           O  
ATOM   2319  CB  VAL A 293     -22.980  29.153  83.031  1.00 32.94           C  
ATOM   2320  CG1 VAL A 293     -21.514  29.484  82.769  1.00 30.85           C  
ATOM   2321  CG2 VAL A 293     -23.880  30.170  82.354  1.00 30.45           C  
ATOM   2322  N   ASN A 294     -21.414  26.259  82.082  1.00 33.84           N  
ATOM   2323  CA  ASN A 294     -20.383  25.331  82.513  1.00 35.69           C  
ATOM   2324  C   ASN A 294     -18.983  25.837  82.300  1.00 36.00           C  
ATOM   2325  O   ASN A 294     -18.708  26.550  81.335  1.00 37.73           O  
ATOM   2326  CB  ASN A 294     -20.545  23.975  81.822  1.00 38.48           C  
ATOM   2327  CG  ASN A 294     -21.919  23.376  82.045  1.00 40.16           C  
ATOM   2328  OD1 ASN A 294     -22.518  23.541  83.115  1.00 41.17           O  
ATOM   2329  ND2 ASN A 294     -22.427  22.669  81.041  1.00 41.51           N  
ATOM   2330  N   PHE A 295     -18.102  25.444  83.214  1.00 36.96           N  
ATOM   2331  CA  PHE A 295     -16.708  25.827  83.180  1.00 37.02           C  
ATOM   2332  C   PHE A 295     -15.837  24.584  83.022  1.00 38.48           C  
ATOM   2333  O   PHE A 295     -16.090  23.555  83.642  1.00 39.09           O  
ATOM   2334  CB  PHE A 295     -16.353  26.553  84.467  1.00 37.70           C  
ATOM   2335  CG  PHE A 295     -17.265  27.696  84.780  1.00 39.21           C  
ATOM   2336  CD1 PHE A 295     -18.565  27.463  85.212  1.00 40.92           C  
ATOM   2337  CD2 PHE A 295     -16.825  29.013  84.648  1.00 39.39           C  
ATOM   2338  CE1 PHE A 295     -19.416  28.532  85.513  1.00 43.37           C  
ATOM   2339  CE2 PHE A 295     -17.658  30.082  84.944  1.00 39.03           C  
ATOM   2340  CZ  PHE A 295     -18.956  29.849  85.378  1.00 41.65           C  
ATOM   2341  N   TRP A 296     -14.806  24.699  82.192  1.00 39.27           N  
ATOM   2342  CA  TRP A 296     -13.882  23.609  81.900  1.00 39.17           C  
ATOM   2343  C   TRP A 296     -12.440  24.054  82.133  1.00 39.83           C  
ATOM   2344  O   TRP A 296     -11.906  24.861  81.371  1.00 41.29           O  
ATOM   2345  CB  TRP A 296     -14.035  23.203  80.434  1.00 37.73           C  
ATOM   2346  CG  TRP A 296     -15.136  22.225  80.155  1.00 38.74           C  
ATOM   2347  CD1 TRP A 296     -15.044  20.866  80.179  1.00 38.36           C  
ATOM   2348  CD2 TRP A 296     -16.485  22.529  79.764  1.00 39.03           C  
ATOM   2349  NE1 TRP A 296     -16.250  20.302  79.821  1.00 39.03           N  
ATOM   2350  CE2 TRP A 296     -17.151  21.300  79.566  1.00 38.16           C  
ATOM   2351  CE3 TRP A 296     -17.194  23.721  79.562  1.00 40.31           C  
ATOM   2352  CZ2 TRP A 296     -18.492  21.226  79.178  1.00 39.37           C  
ATOM   2353  CZ3 TRP A 296     -18.533  23.646  79.172  1.00 41.11           C  
ATOM   2354  CH2 TRP A 296     -19.164  22.407  78.987  1.00 39.76           C  
ATOM   2355  N   TYR A 297     -11.800  23.533  83.170  1.00 41.53           N  
ATOM   2356  CA  TYR A 297     -10.419  23.910  83.440  1.00 43.05           C  
ATOM   2357  C   TYR A 297      -9.478  22.792  83.036  1.00 43.41           C  
ATOM   2358  O   TYR A 297      -9.742  21.627  83.332  1.00 43.17           O  
ATOM   2359  CB  TYR A 297     -10.213  24.216  84.933  1.00 47.67           C  
ATOM   2360  CG  TYR A 297     -10.808  25.531  85.388  1.00 51.74           C  
ATOM   2361  CD1 TYR A 297     -12.174  25.651  85.643  1.00 53.66           C  
ATOM   2362  CD2 TYR A 297     -10.011  26.673  85.510  1.00 53.73           C  
ATOM   2363  CE1 TYR A 297     -12.738  26.876  86.003  1.00 57.95           C  
ATOM   2364  CE2 TYR A 297     -10.562  27.902  85.871  1.00 58.40           C  
ATOM   2365  CZ  TYR A 297     -11.929  27.997  86.113  1.00 60.00           C  
ATOM   2366  OH  TYR A 297     -12.492  29.208  86.447  1.00 60.59           O  
ATOM   2367  N   LYS A 298      -8.392  23.135  82.349  1.00 43.61           N  
ATOM   2368  CA  LYS A 298      -7.413  22.127  81.965  1.00 46.29           C  
ATOM   2369  C   LYS A 298      -6.895  21.573  83.283  1.00 46.16           C  
ATOM   2370  O   LYS A 298      -6.804  22.305  84.268  1.00 45.92           O  
ATOM   2371  CB  LYS A 298      -6.255  22.743  81.169  1.00 50.69           C  
ATOM   2372  CG  LYS A 298      -5.056  21.813  81.042  1.00 54.71           C  
ATOM   2373  CD  LYS A 298      -3.864  22.461  80.359  1.00 61.25           C  
ATOM   2374  CE  LYS A 298      -2.586  21.652  80.610  1.00 66.35           C  
ATOM   2375  NZ  LYS A 298      -2.709  20.209  80.233  1.00 68.08           N  
ATOM   2376  N   GLY A 299      -6.557  20.289  83.308  1.00 46.34           N  
ATOM   2377  CA  GLY A 299      -6.085  19.684  84.543  1.00 46.92           C  
ATOM   2378  C   GLY A 299      -4.724  20.120  85.045  1.00 47.59           C  
ATOM   2379  O   GLY A 299      -3.964  20.779  84.341  1.00 46.37           O  
ATOM   2380  N   ALA A 300      -4.423  19.743  86.282  1.00 50.76           N  
ATOM   2381  CA  ALA A 300      -3.144  20.067  86.893  1.00 55.37           C  
ATOM   2382  C   ALA A 300      -2.078  19.247  86.181  1.00 59.84           C  
ATOM   2383  O   ALA A 300      -2.207  18.029  86.056  1.00 58.42           O  
ATOM   2384  CB  ALA A 300      -3.169  19.719  88.378  1.00 56.11           C  
ATOM   2385  N   PRO A 301      -1.010  19.904  85.697  1.00 63.92           N  
ATOM   2386  CA  PRO A 301       0.059  19.181  85.000  1.00 67.85           C  
ATOM   2387  C   PRO A 301       0.495  17.942  85.777  1.00 69.38           C  
ATOM   2388  O   PRO A 301       0.727  17.995  86.990  1.00 69.43           O  
ATOM   2389  CB  PRO A 301       1.165  20.232  84.870  1.00 68.14           C  
ATOM   2390  CG  PRO A 301       0.895  21.172  86.010  1.00 68.55           C  
ATOM   2391  CD  PRO A 301      -0.607  21.294  85.967  1.00 66.55           C  
ATOM   2392  N   THR A 302       0.592  16.829  85.059  1.00 70.37           N  
ATOM   2393  CA  THR A 302       0.958  15.538  85.634  1.00 71.67           C  
ATOM   2394  C   THR A 302       2.348  15.486  86.264  1.00 72.48           C  
ATOM   2395  O   THR A 302       3.308  16.029  85.718  1.00 72.96           O  
ATOM   2396  CB  THR A 302       0.866  14.436  84.559  1.00 72.85           C  
ATOM   2397  OG1 THR A 302       1.874  14.648  83.562  1.00 72.79           O  
ATOM   2398  CG2 THR A 302      -0.497  14.476  83.879  1.00 72.96           C  
ATOM   2399  N   PRO A 303       2.474  14.829  87.432  1.00 72.35           N  
ATOM   2400  CA  PRO A 303       3.780  14.732  88.093  1.00 72.84           C  
ATOM   2401  C   PRO A 303       4.723  13.813  87.321  1.00 72.96           C  
ATOM   2402  O   PRO A 303       4.308  12.763  86.828  1.00 72.96           O  
ATOM   2403  CB  PRO A 303       3.430  14.182  89.475  1.00 72.62           C  
ATOM   2404  CG  PRO A 303       2.222  13.355  89.209  1.00 71.50           C  
ATOM   2405  CD  PRO A 303       1.422  14.230  88.271  1.00 72.06           C  
ATOM   2406  N   LYS A 304       5.989  14.213  87.214  1.00 72.96           N  
ATOM   2407  CA  LYS A 304       6.982  13.417  86.495  1.00 72.96           C  
ATOM   2408  C   LYS A 304       7.239  12.114  87.256  1.00 72.96           C  
ATOM   2409  O   LYS A 304       7.740  11.142  86.689  1.00 72.96           O  
ATOM   2410  CB  LYS A 304       8.284  14.212  86.336  1.00 72.96           C  
ATOM   2411  CG  LYS A 304       9.158  13.785  85.153  1.00 72.96           C  
ATOM   2412  CD  LYS A 304       9.103  14.803  84.013  1.00 72.68           C  
ATOM   2413  CE  LYS A 304      10.136  14.494  82.925  1.00 72.96           C  
ATOM   2414  NZ  LYS A 304      11.559  14.534  83.404  1.00 72.96           N  
ATOM   2415  N   ARG A 305       6.896  12.105  88.544  1.00 72.90           N  
ATOM   2416  CA  ARG A 305       7.054  10.910  89.371  1.00 72.96           C  
ATOM   2417  C   ARG A 305       5.752  10.102  89.317  1.00 72.96           C  
ATOM   2418  O   ARG A 305       4.753  10.475  89.941  1.00 72.96           O  
ATOM   2419  CB  ARG A 305       7.370  11.285  90.829  1.00 72.96           C  
ATOM   2420  CG  ARG A 305       6.332  12.168  91.537  1.00 72.96           C  
ATOM   2421  CD  ARG A 305       6.433  11.985  93.055  1.00 72.96           C  
ATOM   2422  NE  ARG A 305       6.018  13.167  93.818  1.00 72.96           N  
ATOM   2423  CZ  ARG A 305       6.061  13.256  95.150  1.00 72.96           C  
ATOM   2424  NH1 ARG A 305       6.499  12.232  95.876  1.00 72.96           N  
ATOM   2425  NH2 ARG A 305       5.673  14.374  95.760  1.00 72.96           N  
ATOM   2426  N   ILE A 306       5.766   8.997  88.574  1.00 72.38           N  
ATOM   2427  CA  ILE A 306       4.576   8.157  88.432  1.00 72.13           C  
ATOM   2428  C   ILE A 306       4.529   7.008  89.449  1.00 71.81           C  
ATOM   2429  O   ILE A 306       5.358   6.099  89.409  1.00 72.19           O  
ATOM   2430  CB  ILE A 306       4.493   7.552  87.004  1.00 72.96           C  
ATOM   2431  CG1 ILE A 306       4.909   8.597  85.963  1.00 72.96           C  
ATOM   2432  CG2 ILE A 306       3.068   7.095  86.719  1.00 72.96           C  
ATOM   2433  CD1 ILE A 306       4.918   8.074  84.538  1.00 72.96           C  
ATOM   2434  N   GLU A 307       3.559   7.048  90.358  1.00 71.10           N  
ATOM   2435  CA  GLU A 307       3.425   5.997  91.367  1.00 70.30           C  
ATOM   2436  C   GLU A 307       2.598   4.842  90.818  1.00 68.19           C  
ATOM   2437  O   GLU A 307       1.678   5.053  90.027  1.00 69.39           O  
ATOM   2438  CB  GLU A 307       2.757   6.548  92.632  1.00 70.73           C  
ATOM   2439  CG  GLU A 307       3.584   7.587  93.382  1.00 71.37           C  
ATOM   2440  CD  GLU A 307       2.776   8.297  94.455  1.00 72.96           C  
ATOM   2441  OE1 GLU A 307       3.094   8.134  95.654  1.00 72.96           O  
ATOM   2442  OE2 GLU A 307       1.817   9.016  94.093  1.00 72.96           O  
ATOM   2443  N   TYR A 308       2.925   3.625  91.240  1.00 66.38           N  
ATOM   2444  CA  TYR A 308       2.212   2.443  90.776  1.00 65.15           C  
ATOM   2445  C   TYR A 308       1.498   1.726  91.902  1.00 66.03           C  
ATOM   2446  O   TYR A 308       1.922   1.794  93.053  1.00 66.94           O  
ATOM   2447  CB  TYR A 308       3.172   1.463  90.102  1.00 63.87           C  
ATOM   2448  CG  TYR A 308       3.861   2.039  88.894  1.00 62.72           C  
ATOM   2449  CD1 TYR A 308       4.917   2.941  89.032  1.00 61.40           C  
ATOM   2450  CD2 TYR A 308       3.418   1.732  87.607  1.00 62.30           C  
ATOM   2451  CE1 TYR A 308       5.513   3.528  87.919  1.00 62.13           C  
ATOM   2452  CE2 TYR A 308       4.005   2.313  86.485  1.00 62.62           C  
ATOM   2453  CZ  TYR A 308       5.048   3.212  86.649  1.00 62.81           C  
ATOM   2454  OH  TYR A 308       5.607   3.815  85.547  1.00 64.70           O  
ATOM   2455  N   PRO A 309       0.378   1.048  91.587  1.00 65.71           N  
ATOM   2456  CA  PRO A 309      -0.170   0.986  90.225  1.00 63.63           C  
ATOM   2457  C   PRO A 309      -0.787   2.322  89.796  1.00 59.14           C  
ATOM   2458  O   PRO A 309      -0.926   3.247  90.600  1.00 58.26           O  
ATOM   2459  CB  PRO A 309      -1.197  -0.148  90.310  1.00 63.88           C  
ATOM   2460  CG  PRO A 309      -1.638  -0.106  91.747  1.00 66.62           C  
ATOM   2461  CD  PRO A 309      -0.331   0.113  92.482  1.00 66.01           C  
ATOM   2462  N   LEU A 310      -1.144   2.413  88.523  1.00 55.28           N  
ATOM   2463  CA  LEU A 310      -1.717   3.631  87.965  1.00 50.47           C  
ATOM   2464  C   LEU A 310      -3.210   3.815  88.237  1.00 48.82           C  
ATOM   2465  O   LEU A 310      -3.944   2.852  88.433  1.00 48.04           O  
ATOM   2466  CB  LEU A 310      -1.489   3.652  86.452  1.00 49.61           C  
ATOM   2467  CG  LEU A 310      -0.071   3.377  85.962  1.00 45.61           C  
ATOM   2468  CD1 LEU A 310      -0.036   3.452  84.443  1.00 44.51           C  
ATOM   2469  CD2 LEU A 310       0.874   4.385  86.575  1.00 45.74           C  
ATOM   2470  N   LYS A 311      -3.657   5.063  88.248  1.00 46.86           N  
ATOM   2471  CA  LYS A 311      -5.066   5.342  88.457  1.00 45.54           C  
ATOM   2472  C   LYS A 311      -5.745   4.994  87.128  1.00 42.53           C  
ATOM   2473  O   LYS A 311      -5.100   4.994  86.070  1.00 41.34           O  
ATOM   2474  CB  LYS A 311      -5.279   6.823  88.784  1.00 49.32           C  
ATOM   2475  CG  LYS A 311      -4.587   7.303  90.050  1.00 55.00           C  
ATOM   2476  CD  LYS A 311      -4.741   8.812  90.198  1.00 63.16           C  
ATOM   2477  CE  LYS A 311      -3.872   9.364  91.326  1.00 68.29           C  
ATOM   2478  NZ  LYS A 311      -3.798  10.864  91.308  1.00 70.56           N  
ATOM   2479  N   ALA A 312      -7.040   4.708  87.180  1.00 37.16           N  
ATOM   2480  CA  ALA A 312      -7.761   4.347  85.982  1.00 31.79           C  
ATOM   2481  C   ALA A 312      -7.533   5.320  84.835  1.00 33.12           C  
ATOM   2482  O   ALA A 312      -7.248   4.896  83.713  1.00 32.38           O  
ATOM   2483  CB  ALA A 312      -9.234   4.240  86.281  1.00 30.97           C  
ATOM   2484  N   HIS A 313      -7.631   6.622  85.095  1.00 32.90           N  
ATOM   2485  CA  HIS A 313      -7.475   7.572  83.997  1.00 34.47           C  
ATOM   2486  C   HIS A 313      -6.108   7.502  83.326  1.00 31.74           C  
ATOM   2487  O   HIS A 313      -5.964   7.835  82.154  1.00 32.95           O  
ATOM   2488  CB  HIS A 313      -7.791   9.015  84.447  1.00 35.64           C  
ATOM   2489  CG  HIS A 313      -6.665   9.701  85.150  1.00 39.62           C  
ATOM   2490  ND1 HIS A 313      -6.498   9.649  86.518  1.00 42.81           N  
ATOM   2491  CD2 HIS A 313      -5.614  10.410  84.668  1.00 40.12           C  
ATOM   2492  CE1 HIS A 313      -5.391  10.291  86.848  1.00 43.41           C  
ATOM   2493  NE2 HIS A 313      -4.836  10.762  85.744  1.00 41.50           N  
ATOM   2494  N   GLN A 314      -5.107   7.051  84.062  1.00 31.80           N  
ATOM   2495  CA  GLN A 314      -3.768   6.948  83.503  1.00 30.90           C  
ATOM   2496  C   GLN A 314      -3.787   5.854  82.452  1.00 30.76           C  
ATOM   2497  O   GLN A 314      -3.129   5.958  81.413  1.00 31.63           O  
ATOM   2498  CB  GLN A 314      -2.773   6.614  84.604  1.00 33.97           C  
ATOM   2499  CG  GLN A 314      -2.961   7.499  85.826  1.00 36.98           C  
ATOM   2500  CD  GLN A 314      -1.720   7.573  86.676  1.00 38.12           C  
ATOM   2501  OE1 GLN A 314      -1.580   6.847  87.664  1.00 40.37           O  
ATOM   2502  NE2 GLN A 314      -0.796   8.447  86.287  1.00 35.22           N  
ATOM   2503  N   LYS A 315      -4.536   4.791  82.718  1.00 28.52           N  
ATOM   2504  CA  LYS A 315      -4.637   3.730  81.732  1.00 26.51           C  
ATOM   2505  C   LYS A 315      -5.385   4.313  80.528  1.00 26.51           C  
ATOM   2506  O   LYS A 315      -4.868   4.310  79.409  1.00 27.78           O  
ATOM   2507  CB  LYS A 315      -5.376   2.526  82.315  1.00 25.01           C  
ATOM   2508  CG  LYS A 315      -4.579   1.828  83.400  1.00 23.03           C  
ATOM   2509  CD  LYS A 315      -5.404   0.844  84.176  1.00 23.07           C  
ATOM   2510  CE  LYS A 315      -4.593   0.290  85.336  1.00 28.47           C  
ATOM   2511  NZ  LYS A 315      -5.311  -0.799  86.088  1.00 32.81           N  
ATOM   2512  N   VAL A 316      -6.586   4.839  80.753  1.00 24.44           N  
ATOM   2513  CA  VAL A 316      -7.341   5.434  79.653  1.00 22.76           C  
ATOM   2514  C   VAL A 316      -6.432   6.307  78.773  1.00 24.25           C  
ATOM   2515  O   VAL A 316      -6.573   6.341  77.549  1.00 24.73           O  
ATOM   2516  CB  VAL A 316      -8.489   6.301  80.164  1.00 19.95           C  
ATOM   2517  CG1 VAL A 316      -9.341   6.747  78.990  1.00 16.15           C  
ATOM   2518  CG2 VAL A 316      -9.315   5.519  81.173  1.00 17.73           C  
ATOM   2519  N   ALA A 317      -5.502   7.012  79.404  1.00 25.31           N  
ATOM   2520  CA  ALA A 317      -4.564   7.860  78.678  1.00 26.20           C  
ATOM   2521  C   ALA A 317      -3.744   6.960  77.757  1.00 27.02           C  
ATOM   2522  O   ALA A 317      -3.658   7.158  76.538  1.00 28.95           O  
ATOM   2523  CB  ALA A 317      -3.649   8.562  79.664  1.00 27.16           C  
ATOM   2524  N   ILE A 318      -3.136   5.964  78.376  1.00 28.48           N  
ATOM   2525  CA  ILE A 318      -2.332   4.981  77.678  1.00 28.18           C  
ATOM   2526  C   ILE A 318      -3.091   4.404  76.477  1.00 25.63           C  
ATOM   2527  O   ILE A 318      -2.638   4.493  75.327  1.00 27.94           O  
ATOM   2528  CB  ILE A 318      -1.973   3.853  78.651  1.00 27.70           C  
ATOM   2529  CG1 ILE A 318      -1.137   4.451  79.798  1.00 26.97           C  
ATOM   2530  CG2 ILE A 318      -1.299   2.696  77.902  1.00 28.33           C  
ATOM   2531  CD1 ILE A 318      -0.574   3.451  80.796  1.00 27.23           C  
HETATM 2532  N   MSE A 319      -4.254   3.828  76.747  1.00 27.24           N  
HETATM 2533  CA  MSE A 319      -5.052   3.233  75.692  1.00 33.36           C  
HETATM 2534  C   MSE A 319      -5.283   4.262  74.596  1.00 27.93           C  
HETATM 2535  O   MSE A 319      -4.991   4.014  73.413  1.00 27.59           O  
HETATM 2536  CB  MSE A 319      -6.381   2.731  76.256  1.00 32.98           C  
HETATM 2537  CG  MSE A 319      -6.222   1.811  77.466  1.00 37.81           C  
HETATM 2538 SE   MSE A 319      -7.743   0.604  77.704  1.00 49.23          SE  
HETATM 2539  CE  MSE A 319      -8.644   1.428  79.231  1.00 36.89           C  
ATOM   2540  N   ARG A 320      -5.786   5.431  74.986  1.00 26.29           N  
ATOM   2541  CA  ARG A 320      -6.031   6.471  74.001  1.00 28.26           C  
ATOM   2542  C   ARG A 320      -4.819   6.642  73.108  1.00 27.63           C  
ATOM   2543  O   ARG A 320      -4.940   6.556  71.885  1.00 27.05           O  
ATOM   2544  CB  ARG A 320      -6.346   7.808  74.661  1.00 24.69           C  
ATOM   2545  CG  ARG A 320      -7.750   7.926  75.236  1.00 26.97           C  
ATOM   2546  CD  ARG A 320      -8.141   9.406  75.389  1.00 26.36           C  
ATOM   2547  NE  ARG A 320      -8.447  10.010  74.096  1.00 26.52           N  
ATOM   2548  CZ  ARG A 320      -9.606   9.842  73.464  1.00 26.90           C  
ATOM   2549  NH1 ARG A 320     -10.553   9.096  74.021  1.00 24.74           N  
ATOM   2550  NH2 ARG A 320      -9.820  10.411  72.281  1.00 24.71           N  
ATOM   2551  N   ASN A 321      -3.648   6.854  73.712  1.00 27.49           N  
ATOM   2552  CA  ASN A 321      -2.437   7.080  72.926  1.00 29.28           C  
ATOM   2553  C   ASN A 321      -2.087   5.967  71.984  1.00 28.15           C  
ATOM   2554  O   ASN A 321      -1.853   6.208  70.800  1.00 28.28           O  
ATOM   2555  CB  ASN A 321      -1.231   7.348  73.817  1.00 36.04           C  
ATOM   2556  CG  ASN A 321      -1.402   8.584  74.676  1.00 43.79           C  
ATOM   2557  OD1 ASN A 321      -2.054   9.565  74.274  1.00 46.82           O  
ATOM   2558  ND2 ASN A 321      -0.801   8.554  75.868  1.00 46.75           N  
ATOM   2559  N   ILE A 322      -2.044   4.744  72.498  1.00 25.73           N  
ATOM   2560  CA  ILE A 322      -1.691   3.615  71.656  1.00 22.25           C  
ATOM   2561  C   ILE A 322      -2.560   3.579  70.416  1.00 23.01           C  
ATOM   2562  O   ILE A 322      -2.067   3.307  69.322  1.00 24.49           O  
ATOM   2563  CB  ILE A 322      -1.801   2.286  72.424  1.00 22.23           C  
ATOM   2564  CG1 ILE A 322      -0.640   2.197  73.417  1.00 20.53           C  
ATOM   2565  CG2 ILE A 322      -1.801   1.101  71.445  1.00 15.52           C  
ATOM   2566  CD1 ILE A 322      -0.544   0.905  74.149  1.00 20.52           C  
ATOM   2567  N   GLU A 323      -3.847   3.867  70.578  1.00 22.12           N  
ATOM   2568  CA  GLU A 323      -4.742   3.863  69.434  1.00 25.52           C  
ATOM   2569  C   GLU A 323      -4.277   4.921  68.445  1.00 29.25           C  
ATOM   2570  O   GLU A 323      -4.079   4.632  67.269  1.00 30.23           O  
ATOM   2571  CB  GLU A 323      -6.192   4.135  69.867  1.00 26.05           C  
ATOM   2572  CG  GLU A 323      -6.835   2.980  70.637  1.00 25.48           C  
ATOM   2573  CD  GLU A 323      -8.302   3.210  70.969  1.00 26.58           C  
ATOM   2574  OE1 GLU A 323      -9.102   3.447  70.039  1.00 26.31           O  
ATOM   2575  OE2 GLU A 323      -8.660   3.144  72.166  1.00 29.35           O  
ATOM   2576  N   LYS A 324      -4.088   6.143  68.920  1.00 30.71           N  
ATOM   2577  CA  LYS A 324      -3.642   7.217  68.043  1.00 33.56           C  
ATOM   2578  C   LYS A 324      -2.317   6.822  67.413  1.00 34.59           C  
ATOM   2579  O   LYS A 324      -2.065   7.089  66.239  1.00 35.77           O  
ATOM   2580  CB  LYS A 324      -3.443   8.523  68.829  1.00 35.11           C  
ATOM   2581  CG  LYS A 324      -4.701   9.177  69.352  1.00 35.27           C  
ATOM   2582  CD  LYS A 324      -4.399  10.580  69.842  1.00 39.86           C  
ATOM   2583  CE  LYS A 324      -4.757  10.744  71.318  1.00 44.90           C  
ATOM   2584  NZ  LYS A 324      -4.649  12.156  71.774  1.00 45.94           N  
HETATM 2585  N   MSE A 325      -1.476   6.187  68.217  1.00 36.31           N  
HETATM 2586  CA  MSE A 325      -0.151   5.753  67.790  1.00 39.76           C  
HETATM 2587  C   MSE A 325      -0.235   4.800  66.600  1.00 39.53           C  
HETATM 2588  O   MSE A 325       0.556   4.889  65.664  1.00 38.11           O  
HETATM 2589  CB  MSE A 325       0.540   5.063  68.963  1.00 45.68           C  
HETATM 2590  CG  MSE A 325       2.029   5.299  69.091  1.00 55.82           C  
HETATM 2591 SE   MSE A 325       2.597   5.101  70.986  1.00 72.96          SE  
HETATM 2592  CE  MSE A 325       2.731   6.993  71.480  1.00 68.16           C  
ATOM   2593  N   LEU A 326      -1.189   3.876  66.642  1.00 38.42           N  
ATOM   2594  CA  LEU A 326      -1.337   2.936  65.547  1.00 37.96           C  
ATOM   2595  C   LEU A 326      -1.950   3.680  64.374  1.00 39.73           C  
ATOM   2596  O   LEU A 326      -1.748   3.313  63.215  1.00 41.74           O  
ATOM   2597  CB  LEU A 326      -2.216   1.757  65.965  1.00 36.11           C  
ATOM   2598  CG  LEU A 326      -1.543   0.843  66.990  1.00 32.13           C  
ATOM   2599  CD1 LEU A 326      -2.527  -0.193  67.502  1.00 30.48           C  
ATOM   2600  CD2 LEU A 326      -0.345   0.173  66.351  1.00 27.68           C  
ATOM   2601  N   GLY A 327      -2.696   4.736  64.677  1.00 40.13           N  
ATOM   2602  CA  GLY A 327      -3.298   5.518  63.617  1.00 42.07           C  
ATOM   2603  C   GLY A 327      -2.181   6.065  62.756  1.00 42.47           C  
ATOM   2604  O   GLY A 327      -2.242   5.988  61.531  1.00 41.66           O  
ATOM   2605  N   GLU A 328      -1.153   6.610  63.405  1.00 43.55           N  
ATOM   2606  CA  GLU A 328       0.002   7.168  62.703  1.00 44.80           C  
ATOM   2607  C   GLU A 328       0.711   6.064  61.940  1.00 42.63           C  
ATOM   2608  O   GLU A 328       0.713   6.025  60.705  1.00 41.20           O  
ATOM   2609  CB  GLU A 328       1.014   7.755  63.689  1.00 50.11           C  
ATOM   2610  CG  GLU A 328       1.120   9.266  63.700  1.00 59.81           C  
ATOM   2611  CD  GLU A 328       0.321   9.888  64.826  1.00 65.70           C  
ATOM   2612  OE1 GLU A 328      -0.694  10.556  64.538  1.00 67.62           O  
ATOM   2613  OE2 GLU A 328       0.708   9.699  66.003  1.00 69.98           O  
ATOM   2614  N   ALA A 329       1.320   5.176  62.717  1.00 40.14           N  
ATOM   2615  CA  ALA A 329       2.082   4.049  62.210  1.00 37.73           C  
ATOM   2616  C   ALA A 329       1.495   3.382  60.973  1.00 36.26           C  
ATOM   2617  O   ALA A 329       2.072   3.456  59.891  1.00 37.55           O  
ATOM   2618  CB  ALA A 329       2.258   3.023  63.314  1.00 37.83           C  
ATOM   2619  N   LEU A 330       0.347   2.738  61.134  1.00 34.74           N  
ATOM   2620  CA  LEU A 330      -0.286   2.025  60.033  1.00 34.25           C  
ATOM   2621  C   LEU A 330      -0.756   2.923  58.898  1.00 35.60           C  
ATOM   2622  O   LEU A 330      -1.102   2.433  57.818  1.00 34.99           O  
ATOM   2623  CB  LEU A 330      -1.476   1.225  60.558  1.00 33.07           C  
ATOM   2624  CG  LEU A 330      -1.253   0.319  61.769  1.00 29.15           C  
ATOM   2625  CD1 LEU A 330      -2.545  -0.448  62.038  1.00 29.23           C  
ATOM   2626  CD2 LEU A 330      -0.103  -0.654  61.507  1.00 28.06           C  
ATOM   2627  N   GLY A 331      -0.768   4.231  59.141  1.00 35.74           N  
ATOM   2628  CA  GLY A 331      -1.227   5.165  58.131  1.00 35.25           C  
ATOM   2629  C   GLY A 331      -2.649   4.874  57.674  1.00 36.69           C  
ATOM   2630  O   GLY A 331      -2.899   4.780  56.479  1.00 38.71           O  
ATOM   2631  N   ASN A 332      -3.581   4.724  58.614  1.00 37.73           N  
ATOM   2632  CA  ASN A 332      -4.985   4.442  58.293  1.00 36.53           C  
ATOM   2633  C   ASN A 332      -5.705   3.917  59.534  1.00 36.16           C  
ATOM   2634  O   ASN A 332      -5.648   2.722  59.838  1.00 36.88           O  
ATOM   2635  CB  ASN A 332      -5.098   3.401  57.177  1.00 40.91           C  
ATOM   2636  CG  ASN A 332      -6.530   2.959  56.945  1.00 45.58           C  
ATOM   2637  OD1 ASN A 332      -7.473   3.649  57.351  1.00 49.32           O  
ATOM   2638  ND2 ASN A 332      -6.707   1.815  56.283  1.00 47.67           N  
ATOM   2639  N   PRO A 333      -6.413   4.801  60.256  1.00 36.01           N  
ATOM   2640  CA  PRO A 333      -7.132   4.401  61.470  1.00 33.69           C  
ATOM   2641  C   PRO A 333      -8.013   3.147  61.387  1.00 33.74           C  
ATOM   2642  O   PRO A 333      -8.338   2.551  62.416  1.00 34.48           O  
ATOM   2643  CB  PRO A 333      -7.916   5.670  61.835  1.00 34.44           C  
ATOM   2644  CG  PRO A 333      -8.098   6.363  60.512  1.00 30.68           C  
ATOM   2645  CD  PRO A 333      -6.710   6.206  59.928  1.00 34.70           C  
ATOM   2646  N   GLN A 334      -8.380   2.741  60.176  1.00 34.02           N  
ATOM   2647  CA  GLN A 334      -9.204   1.551  59.984  1.00 37.47           C  
ATOM   2648  C   GLN A 334      -8.443   0.271  60.346  1.00 35.48           C  
ATOM   2649  O   GLN A 334      -8.998  -0.643  60.959  1.00 35.31           O  
ATOM   2650  CB  GLN A 334      -9.669   1.491  58.534  1.00 42.05           C  
ATOM   2651  CG  GLN A 334     -10.264   2.816  58.059  1.00 53.02           C  
ATOM   2652  CD  GLN A 334     -11.573   2.639  57.313  1.00 60.94           C  
ATOM   2653  OE1 GLN A 334     -11.601   2.073  56.214  1.00 65.98           O  
ATOM   2654  NE2 GLN A 334     -12.671   3.117  57.910  1.00 62.97           N  
ATOM   2655  N   GLU A 335      -7.166   0.212  59.975  1.00 35.31           N  
ATOM   2656  CA  GLU A 335      -6.341  -0.951  60.278  1.00 34.48           C  
ATOM   2657  C   GLU A 335      -6.065  -1.156  61.781  1.00 31.73           C  
ATOM   2658  O   GLU A 335      -5.642  -2.245  62.206  1.00 33.31           O  
ATOM   2659  CB  GLU A 335      -5.022  -0.861  59.517  1.00 39.43           C  
ATOM   2660  CG  GLU A 335      -5.188  -1.020  58.016  1.00 47.30           C  
ATOM   2661  CD  GLU A 335      -3.885  -1.357  57.331  1.00 52.69           C  
ATOM   2662  OE1 GLU A 335      -3.223  -2.326  57.775  1.00 56.33           O  
ATOM   2663  OE2 GLU A 335      -3.525  -0.663  56.354  1.00 54.56           O  
ATOM   2664  N   VAL A 336      -6.309  -0.119  62.581  1.00 27.02           N  
ATOM   2665  CA  VAL A 336      -6.101  -0.194  64.029  1.00 22.83           C  
ATOM   2666  C   VAL A 336      -6.709  -1.474  64.611  1.00 23.04           C  
ATOM   2667  O   VAL A 336      -6.007  -2.298  65.203  1.00 20.37           O  
ATOM   2668  CB  VAL A 336      -6.747   1.022  64.741  1.00 22.98           C  
ATOM   2669  CG1 VAL A 336      -6.711   0.825  66.272  1.00 20.13           C  
ATOM   2670  CG2 VAL A 336      -6.033   2.305  64.331  1.00 16.68           C  
ATOM   2671  N   GLY A 337      -8.019  -1.635  64.437  1.00 21.34           N  
ATOM   2672  CA  GLY A 337      -8.684  -2.816  64.958  1.00 21.71           C  
ATOM   2673  C   GLY A 337      -8.003  -4.123  64.575  1.00 21.10           C  
ATOM   2674  O   GLY A 337      -7.458  -4.836  65.435  1.00 20.47           O  
ATOM   2675  N   PRO A 338      -7.994  -4.453  63.277  1.00 20.01           N  
ATOM   2676  CA  PRO A 338      -7.368  -5.695  62.810  1.00 18.98           C  
ATOM   2677  C   PRO A 338      -6.003  -5.961  63.449  1.00 20.89           C  
ATOM   2678  O   PRO A 338      -5.684  -7.112  63.750  1.00 21.93           O  
ATOM   2679  CB  PRO A 338      -7.270  -5.493  61.296  1.00 19.77           C  
ATOM   2680  CG  PRO A 338      -8.441  -4.591  60.992  1.00 20.64           C  
ATOM   2681  CD  PRO A 338      -8.346  -3.586  62.137  1.00 20.19           C  
ATOM   2682  N   LEU A 339      -5.198  -4.922  63.668  1.00 20.21           N  
ATOM   2683  CA  LEU A 339      -3.888  -5.150  64.277  1.00 20.58           C  
ATOM   2684  C   LEU A 339      -4.025  -5.617  65.723  1.00 21.55           C  
ATOM   2685  O   LEU A 339      -3.495  -6.674  66.098  1.00 26.24           O  
ATOM   2686  CB  LEU A 339      -3.030  -3.890  64.266  1.00 23.02           C  
ATOM   2687  CG  LEU A 339      -1.575  -4.254  64.596  1.00 24.83           C  
ATOM   2688  CD1 LEU A 339      -0.879  -4.669  63.306  1.00 23.46           C  
ATOM   2689  CD2 LEU A 339      -0.832  -3.080  65.237  1.00 25.57           C  
ATOM   2690  N   LEU A 340      -4.739  -4.836  66.533  1.00 21.53           N  
ATOM   2691  CA  LEU A 340      -4.933  -5.179  67.936  1.00 23.35           C  
ATOM   2692  C   LEU A 340      -5.406  -6.620  68.095  1.00 22.02           C  
ATOM   2693  O   LEU A 340      -4.982  -7.340  69.003  1.00 22.38           O  
ATOM   2694  CB  LEU A 340      -5.949  -4.234  68.567  1.00 27.03           C  
ATOM   2695  CG  LEU A 340      -5.603  -2.740  68.598  1.00 30.71           C  
ATOM   2696  CD1 LEU A 340      -6.758  -1.956  69.211  1.00 31.94           C  
ATOM   2697  CD2 LEU A 340      -4.340  -2.521  69.400  1.00 29.52           C  
ATOM   2698  N   ASN A 341      -6.286  -7.048  67.202  1.00 21.48           N  
ATOM   2699  CA  ASN A 341      -6.802  -8.401  67.278  1.00 21.78           C  
ATOM   2700  C   ASN A 341      -5.752  -9.468  66.996  1.00 23.77           C  
ATOM   2701  O   ASN A 341      -5.610 -10.423  67.782  1.00 21.38           O  
ATOM   2702  CB  ASN A 341      -7.986  -8.565  66.324  1.00 25.21           C  
ATOM   2703  CG  ASN A 341      -9.210  -7.814  66.801  1.00 26.40           C  
ATOM   2704  OD1 ASN A 341      -9.857  -8.222  67.763  1.00 28.34           O  
ATOM   2705  ND2 ASN A 341      -9.519  -6.696  66.148  1.00 29.57           N  
ATOM   2706  N   THR A 342      -5.004  -9.329  65.900  1.00 21.78           N  
ATOM   2707  CA  THR A 342      -4.022 -10.367  65.616  1.00 21.52           C  
ATOM   2708  C   THR A 342      -2.994 -10.402  66.751  1.00 23.28           C  
ATOM   2709  O   THR A 342      -2.503 -11.471  67.116  1.00 25.45           O  
ATOM   2710  CB  THR A 342      -3.320 -10.175  64.242  1.00 21.43           C  
ATOM   2711  OG1 THR A 342      -2.008  -9.647  64.442  1.00 24.01           O  
ATOM   2712  CG2 THR A 342      -4.111  -9.229  63.359  1.00 20.41           C  
HETATM 2713  N   MSE A 343      -2.710  -9.238  67.331  1.00 24.46           N  
HETATM 2714  CA  MSE A 343      -1.750  -9.121  68.436  1.00 28.03           C  
HETATM 2715  C   MSE A 343      -2.252  -9.862  69.679  1.00 23.11           C  
HETATM 2716  O   MSE A 343      -1.463 -10.403  70.444  1.00 24.04           O  
HETATM 2717  CB  MSE A 343      -1.526  -7.627  68.765  1.00 29.45           C  
HETATM 2718  CG  MSE A 343      -0.509  -7.289  69.880  1.00 35.74           C  
HETATM 2719 SE   MSE A 343      -0.271  -5.298  70.174  1.00 47.61          SE  
HETATM 2720  CE  MSE A 343      -1.036  -4.709  68.475  1.00 36.65           C  
ATOM   2721  N   ILE A 344      -3.567  -9.919  69.856  1.00 23.11           N  
ATOM   2722  CA  ILE A 344      -4.151 -10.562  71.033  1.00 25.02           C  
ATOM   2723  C   ILE A 344      -4.656 -11.987  70.834  1.00 23.80           C  
ATOM   2724  O   ILE A 344      -4.363 -12.883  71.634  1.00 23.63           O  
ATOM   2725  CB  ILE A 344      -5.320  -9.726  71.557  1.00 27.67           C  
ATOM   2726  CG1 ILE A 344      -4.818  -8.335  71.929  1.00 29.67           C  
ATOM   2727  CG2 ILE A 344      -5.972 -10.409  72.744  1.00 29.02           C  
ATOM   2728  CD1 ILE A 344      -5.927  -7.339  72.137  1.00 35.14           C  
ATOM   2729  N   LYS A 345      -5.444 -12.192  69.785  1.00 21.79           N  
ATOM   2730  CA  LYS A 345      -5.984 -13.510  69.519  1.00 20.30           C  
ATOM   2731  C   LYS A 345      -4.923 -14.584  69.684  1.00 20.94           C  
ATOM   2732  O   LYS A 345      -3.868 -14.533  69.046  1.00 21.95           O  
ATOM   2733  CB  LYS A 345      -6.526 -13.597  68.099  1.00 20.74           C  
ATOM   2734  CG  LYS A 345      -7.858 -12.920  67.826  1.00 20.70           C  
ATOM   2735  CD  LYS A 345      -8.175 -13.166  66.358  1.00 26.10           C  
ATOM   2736  CE  LYS A 345      -9.434 -12.499  65.882  1.00 28.98           C  
ATOM   2737  NZ  LYS A 345      -9.489 -12.608  64.392  1.00 33.11           N  
ATOM   2738  N   GLY A 346      -5.214 -15.554  70.540  1.00 20.90           N  
ATOM   2739  CA  GLY A 346      -4.307 -16.662  70.758  1.00 21.84           C  
ATOM   2740  C   GLY A 346      -3.093 -16.318  71.587  1.00 23.33           C  
ATOM   2741  O   GLY A 346      -2.292 -17.201  71.911  1.00 24.22           O  
ATOM   2742  N   ARG A 347      -2.952 -15.046  71.941  1.00 23.87           N  
ATOM   2743  CA  ARG A 347      -1.812 -14.620  72.731  1.00 23.39           C  
ATOM   2744  C   ARG A 347      -2.187 -14.050  74.099  1.00 24.68           C  
ATOM   2745  O   ARG A 347      -1.632 -14.477  75.108  1.00 28.01           O  
ATOM   2746  CB  ARG A 347      -0.981 -13.620  71.927  1.00 22.94           C  
ATOM   2747  CG  ARG A 347      -0.338 -14.245  70.696  1.00 20.01           C  
ATOM   2748  CD  ARG A 347       0.480 -13.227  69.909  1.00 21.19           C  
ATOM   2749  NE  ARG A 347       1.744 -12.883  70.557  1.00 21.93           N  
ATOM   2750  CZ  ARG A 347       2.133 -11.635  70.783  1.00 26.00           C  
ATOM   2751  NH1 ARG A 347       1.361 -10.629  70.417  1.00 26.47           N  
ATOM   2752  NH2 ARG A 347       3.292 -11.388  71.376  1.00 31.51           N  
ATOM   2753  N   TYR A 348      -3.105 -13.091  74.158  1.00 24.47           N  
ATOM   2754  CA  TYR A 348      -3.504 -12.559  75.454  1.00 29.08           C  
ATOM   2755  C   TYR A 348      -4.989 -12.787  75.696  1.00 34.39           C  
ATOM   2756  O   TYR A 348      -5.558 -12.254  76.649  1.00 34.93           O  
ATOM   2757  CB  TYR A 348      -3.221 -11.068  75.551  1.00 26.20           C  
ATOM   2758  CG  TYR A 348      -1.760 -10.693  75.491  1.00 22.23           C  
ATOM   2759  CD1 TYR A 348      -1.134 -10.393  74.270  1.00 18.40           C  
ATOM   2760  CD2 TYR A 348      -1.004 -10.619  76.655  1.00 20.12           C  
ATOM   2761  CE1 TYR A 348       0.212 -10.028  74.221  1.00 18.32           C  
ATOM   2762  CE2 TYR A 348       0.340 -10.253  76.619  1.00 20.34           C  
ATOM   2763  CZ  TYR A 348       0.944  -9.959  75.406  1.00 20.68           C  
ATOM   2764  OH  TYR A 348       2.280  -9.592  75.402  1.00 25.55           O  
ATOM   2765  N   ASN A 349      -5.602 -13.570  74.812  1.00 39.97           N  
ATOM   2766  CA  ASN A 349      -7.021 -13.924  74.855  1.00 44.56           C  
ATOM   2767  C   ASN A 349      -7.602 -14.181  76.226  1.00 48.77           C  
ATOM   2768  O   ASN A 349      -7.767 -15.382  76.548  1.00 48.71           O  
ATOM   2769  CB  ASN A 349      -7.253 -15.161  74.016  1.00 46.85           C  
ATOM   2770  CG  ASN A 349      -7.514 -14.829  72.593  1.00 50.59           C  
ATOM   2771  OD1 ASN A 349      -7.306 -15.652  71.710  1.00 51.17           O  
ATOM   2772  ND2 ASN A 349      -7.997 -13.614  72.349  1.00 54.55           N  
ATOM   2773  OXT ASN A 349      -7.887 -13.201  76.951  1.00 58.62           O  
TER    2774      ASN A 349                                                      
HETATM 2775  S   SO4 A 501      -7.773  13.820  70.437  1.00 58.94           S  
HETATM 2776  O1  SO4 A 501      -6.505  14.359  69.895  1.00 54.88           O  
HETATM 2777  O2  SO4 A 501      -8.463  14.855  71.239  1.00 57.26           O  
HETATM 2778  O3  SO4 A 501      -8.649  13.417  69.310  1.00 56.16           O  
HETATM 2779  O4  SO4 A 501      -7.472  12.651  71.300  1.00 56.46           O  
CONECT  767  774                                                                
CONECT  774  767  775                                                           
CONECT  775  774  776  778                                                      
CONECT  776  775  777  782                                                      
CONECT  777  776                                                                
CONECT  778  775  779                                                           
CONECT  779  778  780                                                           
CONECT  780  779  781                                                           
CONECT  781  780                                                                
CONECT  782  776                                                                
CONECT  897  904                                                                
CONECT  904  897  905                                                           
CONECT  905  904  906  908                                                      
CONECT  906  905  907  912                                                      
CONECT  907  906                                                                
CONECT  908  905  909                                                           
CONECT  909  908  910                                                           
CONECT  910  909  911                                                           
CONECT  911  910                                                                
CONECT  912  906                                                                
CONECT 1204 1209                                                                
CONECT 1209 1204 1210                                                           
CONECT 1210 1209 1211 1213                                                      
CONECT 1211 1210 1212 1217                                                      
CONECT 1212 1211                                                                
CONECT 1213 1210 1214                                                           
CONECT 1214 1213 1215                                                           
CONECT 1215 1214 1216                                                           
CONECT 1216 1215                                                                
CONECT 1217 1211                                                                
CONECT 1464 1466                                                                
CONECT 1466 1464 1467                                                           
CONECT 1467 1466 1468 1470                                                      
CONECT 1468 1467 1469 1474                                                      
CONECT 1469 1468                                                                
CONECT 1470 1467 1471                                                           
CONECT 1471 1470 1472                                                           
CONECT 1472 1471 1473                                                           
CONECT 1473 1472                                                                
CONECT 1474 1468                                                                
CONECT 2157 2162                                                                
CONECT 2162 2157 2163                                                           
CONECT 2163 2162 2164 2166                                                      
CONECT 2164 2163 2165 2170                                                      
CONECT 2165 2164                                                                
CONECT 2166 2163 2167                                                           
CONECT 2167 2166 2168                                                           
CONECT 2168 2167 2169                                                           
CONECT 2169 2168                                                                
CONECT 2170 2164                                                                
CONECT 2526 2532                                                                
CONECT 2532 2526 2533                                                           
CONECT 2533 2532 2534 2536                                                      
CONECT 2534 2533 2535 2540                                                      
CONECT 2535 2534                                                                
CONECT 2536 2533 2537                                                           
CONECT 2537 2536 2538                                                           
CONECT 2538 2537 2539                                                           
CONECT 2539 2538                                                                
CONECT 2540 2534                                                                
CONECT 2578 2585                                                                
CONECT 2585 2578 2586                                                           
CONECT 2586 2585 2587 2589                                                      
CONECT 2587 2586 2588 2593                                                      
CONECT 2588 2587                                                                
CONECT 2589 2586 2590                                                           
CONECT 2590 2589 2591                                                           
CONECT 2591 2590 2592                                                           
CONECT 2592 2591                                                                
CONECT 2593 2587                                                                
CONECT 2708 2713                                                                
CONECT 2713 2708 2714                                                           
CONECT 2714 2713 2715 2717                                                      
CONECT 2715 2714 2716 2721                                                      
CONECT 2716 2715                                                                
CONECT 2717 2714 2718                                                           
CONECT 2718 2717 2719                                                           
CONECT 2719 2718 2720                                                           
CONECT 2720 2719                                                                
CONECT 2721 2715                                                                
CONECT 2775 2776 2777 2778 2779                                                 
CONECT 2776 2775                                                                
CONECT 2777 2775                                                                
CONECT 2778 2775                                                                
CONECT 2779 2775                                                                
MASTER      327    0    9   14   14    0    1    6 2778    1   85   27          
END                                                                             


A second structure was input as follows:


HELIX    1   1 GLU A   29  GLN A   31  1                                   3
HELIX    2   2 PRO A   50  GLU A   57  1                                   8
HELIX    3   3 TYR A   71  LYS A   75  1                                   5
HELIX    4   4 LEU A   78  ASN A   84  1                                   7
HELIX    5   5 GLU A  105  MET A  108  1                                   4
HELIX    6   6 PHE A  125  GLY A  139  1                                  15
HELIX    7   7 ARG A  156  LEU A  163  1                                   8
HELIX    8   8 TRP A  167  LYS A  176  1                                  10
HELIX    9   9 PRO A  221  CYS A  226  1                                   6
HELIX   10  10 PRO A  253  ASN A  257  1                                   5
HELIX   11  11 ALA A  312  ALA A  329  1                                  18
HELIX   12  12 PRO A  333  ILE A  344  1                                  12
SHEET    1   1 1 THR A  39  PRO A  41  0
SHEET    2   2 1 VAL A  62  LEU A  64  0
SHEET    3   3 1 PHE A  90  ALA A  95  0
SHEET    4   4 1 ARG A 120  MET A 123  0
SHEET    5   5 1 ARG A 143  THR A 149  0
SHEET    6   6 1 LEU A 182  GLY A 190  0
SHEET    7   7 1 GLN A 204  LYS A 211  0
SHEET    8   8 1 LYS A 214  PHE A 219  0
SHEET    9   9 1 GLY A 260  VAL A 265  0
SHEET   10  10 1 VAL A 270  ILE A 273  0
SHEET   11  11 1 TRP A 278  SER A 283  0
SHEET   12  12 1 THR A 290  TYR A 297  0
ATOM      1  N   GLU A  15      -9.951  35.008 -24.969  1.00106.40           N
ANISOU    1  N   GLU A  15    11421  15136  13870   -351   -914   3591       N
ATOM      2  CA  GLU A  15     -10.801  35.229 -26.165  1.00108.02           C
ANISOU    2  CA  GLU A  15    11613  15354  14073   -320  -1006   3692       C
ATOM      3  C   GLU A  15     -12.268  35.343 -25.739  1.00109.04           C
ANISOU    3  C   GLU A  15    11804  15231  14397   -234  -1063   3486       C
ATOM      4  O   GLU A  15     -13.044  34.403 -25.956  1.00108.13           O
ANISOU    4  O   GLU A  15    11708  15170  14208   -115   -992   3315       O
ATOM      5  CB  GLU A  15     -10.651  34.147 -27.266  1.00  0.00           C
ATOM      6  CG  GLU A  15      -9.239  33.915 -27.824  1.00  0.00           C
ATOM      7  CD  GLU A  15      -8.343  33.051 -26.927  1.00  0.00           C
ATOM      8  OE1 GLU A  15      -8.778  32.797 -25.775  1.00  0.00           O
ATOM      9  OE2 GLU A  15      -7.152  32.938 -27.260  1.00  0.00           O
ATOM     10  H1  GLU A  15     -10.031  35.769 -24.302  1.00  0.00           H
ATOM     11  H2  GLU A  15     -10.191  34.120 -24.545  1.00  0.00           H
ATOM     12  H3  GLU A  15      -8.983  34.895 -25.247  1.00  0.00           H
ATOM     13  HA  GLU A  15     -10.520  36.183 -26.610  1.00  0.00           H
ATOM     14  HB2 GLU A  15     -11.271  34.467 -28.106  1.00  0.00           H
ATOM     15  HB3 GLU A  15     -11.054  33.192 -26.924  1.00  0.00           H
ATOM     16  HG2 GLU A  15      -9.345  33.407 -28.785  1.00  0.00           H
ATOM     17  HG3 GLU A  15      -8.771  34.883 -28.008  1.00  0.00           H
ATOM     18  N   PRO A  16     -12.668  36.471 -25.124  1.00109.16           N
ANISOU   18  N   PRO A  16    11847  14966  14662   -292  -1191   3503       N
ATOM     19  CA  PRO A  16     -14.046  36.708 -24.709  1.00107.64           C
ANISOU   19  CA  PRO A  16    11713  14520  14666   -206  -1240   3309       C
ATOM     20  C   PRO A  16     -15.027  36.558 -25.875  1.00104.08           C
ANISOU   20  C   PRO A  16    11244  14114  14188   -141  -1302   3350       C
ATOM     21  O   PRO A  16     -14.622  36.482 -27.056  1.00106.93           O
ANISOU   21  O   PRO A  16    11561  14567  14500   -199  -1395   3589       O
ATOM     22  CB  PRO A  16     -14.053  38.092 -24.044  1.00109.42           C
ANISOU   22  CB  PRO A  16    11967  14464  15143   -302  -1379   3384       C
ATOM     23  CG  PRO A  16     -12.849  38.808 -24.654  1.00110.53           C
ANISOU   23  CG  PRO A  16    12048  14727  15223   -444  -1443   3677       C
ATOM     24  CD  PRO A  16     -11.865  37.660 -24.862  1.00109.87           C
ANISOU   24  CD  PRO A  16    11917  14954  14873   -438  -1297   3701       C
ATOM     25  HA  PRO A  16     -14.323  35.981 -23.951  1.00129.17           H
ATOM     26  HB2 PRO A  16     -14.980  38.647 -24.200  1.00131.30           H
ATOM     27  HB3 PRO A  16     -13.870  37.969 -22.974  1.00131.30           H
ATOM     28  HG2 PRO A  16     -13.123  39.250 -25.612  1.00132.64           H
ATOM     29  HG3 PRO A  16     -12.440  39.565 -23.979  1.00132.64           H
ATOM     30  HD2 PRO A  16     -11.188  37.898 -25.683  1.00131.84           H
ATOM     31  HD3 PRO A  16     -11.309  37.504 -23.939  1.00131.84           H
ATOM     32  N   ARG A  17     -16.233  36.124 -25.546  1.00 98.04           N
ANISOU   32  N   ARG A  17    10512  13281  13459    -15  -1250   3117       N
ATOM     33  CA  ARG A  17     -17.302  35.876 -26.517  1.00 98.49           C
ANISOU   33  CA  ARG A  17    10551  13382  13490     58  -1305   3124       C
ATOM     34  C   ARG A  17     -18.190  37.117 -26.578  1.00 93.42           C
ANISOU   34  C   ARG A  17     9923  12484  13089     38  -1474   3195       C
ATOM     35  O   ARG A  17     -18.406  37.776 -25.566  1.00 95.58           O
ANISOU   35  O   ARG A  17    10240  12501  13576     12  -1519   3136       O
ATOM     36  H   ARG A  17     -16.524  36.306 -24.587  1.00117.65           H
ATOM     37  CB  ARG A  17     -18.086  34.595 -26.177  1.00  0.00           C
ATOM     38  CG  ARG A  17     -17.285  33.274 -26.245  1.00  0.00           C
ATOM     39  CD  ARG A  17     -16.690  32.919 -27.622  1.00  0.00           C
ATOM     40  NE  ARG A  17     -15.451  33.666 -27.916  1.00  0.00           N
ATOM     41  CZ  ARG A  17     -14.924  33.925 -29.095  1.00  0.00           C
ATOM     42  NH1 ARG A  17     -15.398  33.431 -30.207  1.00  0.00           N
ATOM     43  NH2 ARG A  17     -13.917  34.738 -29.172  1.00  0.00           N
ATOM     44  HA  ARG A  17     -16.877  35.768 -27.507  1.00  0.00           H
ATOM     45  HB2 ARG A  17     -18.498  34.691 -25.169  1.00  0.00           H
ATOM     46  HB3 ARG A  17     -18.934  34.515 -26.864  1.00  0.00           H
ATOM     47  HG2 ARG A  17     -17.971  32.469 -25.974  1.00  0.00           H
ATOM     48  HG3 ARG A  17     -16.489  33.284 -25.501  1.00  0.00           H
ATOM     49  HD2 ARG A  17     -16.454  31.852 -27.626  1.00  0.00           H
ATOM     50  HD3 ARG A  17     -17.445  33.105 -28.389  1.00  0.00           H
ATOM     51  HE  ARG A  17     -14.961  34.081 -27.128  1.00  0.00           H
ATOM     52 HH11 ARG A  17     -16.239  32.887 -30.166  1.00  0.00           H
ATOM     53 HH12 ARG A  17     -14.998  33.695 -31.087  1.00  0.00           H
ATOM     54 HH21 ARG A  17     -13.776  35.330 -28.355  1.00  0.00           H
ATOM     55 HH22 ARG A  17     -13.534  35.013 -30.054  1.00  0.00           H
ATOM     56  N   GLU A  18     -18.548  37.483 -27.802  1.00 83.88           N
ANISOU   56  N   GLU A  18     8682  11349  11840     57  -1567   3323       N
ATOM     57  CA  GLU A  18     -19.499  38.561 -28.072  1.00 78.06           C
ANISOU   57  CA  GLU A  18     7950  10399  11309     46  -1728   3410       C
ATOM     58  C   GLU A  18     -20.914  38.001 -27.905  0.50 75.41           C
ANISOU   58  C   GLU A  18     7632   9946  11074    175  -1728   3193       C
ATOM     59  O   GLU A  18     -21.208  36.927 -28.446  0.50 68.11           O
ANISOU   59  O   GLU A  18     6681   9194  10003    254  -1689   3131       O
ATOM     60  CB  GLU A  18     -19.266  39.084 -29.500  0.50 87.27           C
ANISOU   60  CB  GLU A  18     9069  11714  12375     -8  -1835   3695       C
ATOM     61  CG  GLU A  18     -20.080  40.338 -29.855  0.50 97.07           C
ANISOU   61  CG  GLU A  18    10315  12744  13824    -27  -2005   3816       C
ATOM     62  CD  GLU A  18     -19.763  41.564 -28.985  0.50103.04           C
ANISOU   62  CD  GLU A  18    11101  13258  14792   -131  -2075   3895       C
ATOM     63  OE1 GLU A  18     -18.668  41.585 -28.374  0.50103.73           O
ANISOU   63  OE1 GLU A  18    11195  13375  14843   -205  -2007   3904       O
ATOM     64  OE2 GLU A  18     -20.544  42.538 -29.077  0.50105.28           O
ANISOU   64  OE2 GLU A  18    11403  13319  15278   -137  -2200   3949       O
ATOM     65  H   GLU A  18     -18.400  36.836 -28.553  1.00100.66           H
ATOM     66  HA  GLU A  18     -19.347  39.374 -27.358  1.00 93.67           H
ATOM     67  HB2 GLU A  18     -18.203  39.300 -29.634  0.50104.72           H
ATOM     68  HB3 GLU A  18     -19.520  38.293 -30.210  0.50104.72           H
ATOM     69  HG2 GLU A  18     -19.871  40.585 -30.898  0.50116.49           H
ATOM     70  HG3 GLU A  18     -21.141  40.098 -29.783  0.50116.49           H
ATOM     71  N   GLU A  19     -21.748  38.653 -27.103  1.00 87.67           N
ANISOU   71  N   GLU A  19     9229  11205  12878    197  -1772   3079       N
ATOM     72  CA  GLU A  19     -23.131  38.225 -26.883  1.00 91.62           C
ANISOU   72  CA  GLU A  19     9740  11570  13501    318  -1770   2878       C
ATOM     73  C   GLU A  19     -24.049  38.592 -28.071  1.00 91.16           C
ANISOU   73  C   GLU A  19     9643  11528  13465    344  -1906   3003       C
ATOM     74  O   GLU A  19     -23.862  39.599 -28.765  1.00 95.73           O
ANISOU   74  O   GLU A  19    10208  12092  14073    266  -2031   3237       O
ATOM     75  H   GLU A  19     -21.449  39.526 -26.673  1.00105.21           H
ATOM     76  CB  GLU A  19     -23.645  38.779 -25.540  1.00  0.00           C
ATOM     77  CG  GLU A  19     -22.995  38.128 -24.312  1.00  0.00           C
ATOM     78  CD  GLU A  19     -23.274  36.620 -24.150  1.00  0.00           C
ATOM     79  OE2 GLU A  19     -22.612  35.992 -23.283  1.00  0.00           O
ATOM     80  OE1 GLU A  19     -24.089  36.051 -24.919  1.00  0.00           O
ATOM     81  HA  GLU A  19     -23.138  37.138 -26.818  1.00  0.00           H
ATOM     82  HB2 GLU A  19     -23.429  39.852 -25.507  1.00  0.00           H
ATOM     83  HB3 GLU A  19     -24.730  38.655 -25.481  1.00  0.00           H
ATOM     84  HG2 GLU A  19     -23.341  38.641 -23.422  1.00  0.00           H
ATOM     85  HG3 GLU A  19     -21.927  38.276 -24.387  1.00  0.00           H
ATOM     86  N   ALA A  20     -25.062  37.760 -28.334  1.00 82.51           N
ANISOU   86  N   ALA A  20     8528  10463  12359    455  -1882   2845       N
ATOM     87  CA  ALA A  20     -26.006  37.982 -29.434  1.00 81.88           C
ANISOU   87  CA  ALA A  20     8409  10413  12288    493  -2009   2939       C
ATOM     88  C   ALA A  20     -26.787  39.302 -29.265  1.00 81.95           C
ANISOU   88  C   ALA A  20     8434  10146  12556    476  -2151   3024       C
ATOM     89  O   ALA A  20     -27.065  39.730 -28.148  1.00 85.61           O
ANISOU   89  O   ALA A  20     8945  10375  13206    456  -2142   2965       O
ATOM     90  CB  ALA A  20     -26.944  36.774 -29.548  1.00 78.87           C
ANISOU   90  CB  ALA A  20     8003  10085  11877    617  -1955   2723       C
ATOM     91  H   ALA A  20     -25.216  36.989 -27.698  1.00 99.01           H
ATOM     92  HA  ALA A  20     -25.429  38.053 -30.357  1.00 98.26           H
ATOM     93  HB1 ALA A  20     -27.620  36.905 -30.394  1.00 94.64           H
ATOM     94  HB2 ALA A  20     -26.361  35.864 -29.698  1.00 94.64           H
ATOM     95  HB3 ALA A  20     -27.533  36.678 -28.634  1.00 94.64           H
ATOM     96  N   GLY A  21     -27.228  39.923 -30.366  1.00 78.31           N
ANISOU   96  N   GLY A  21     7938   9715  12101    491  -2284   3164       N
ATOM     97  CA  GLY A  21     -27.931  41.215 -30.313  1.00 80.08           C
ANISOU   97  CA  GLY A  21     8175   9699  12554    476  -2424   3272       C
ATOM     98  C   GLY A  21     -27.022  42.446 -30.177  1.00 86.88           C
ANISOU   98  C   GLY A  21     9064  10477  13468    351  -2482   3484       C
ATOM     99  O   GLY A  21     -27.547  43.539 -29.984  1.00 86.87           O
ANISOU   99  O   GLY A  21     9093  10227  13687    332  -2574   3538       O
ATOM    100  H   GLY A  21     -27.035  39.514 -31.266  1.00 93.97           H
ATOM    101  HA2 GLY A  21     -28.528  41.342 -31.214  1.00 96.10           H
ATOM    102  HA3 GLY A  21     -28.612  41.218 -29.460  1.00 96.10           H
ATOM    103  N   ALA A  22     -25.703  42.290 -30.357  1.00 92.84           N
ANISOU  103  N   ALA A  22     9810  11432  14033    265  -2430   3607       N
ATOM    104  CA  ALA A  22     -24.685  43.336 -30.169  1.00 92.65           C
ANISOU  104  CA  ALA A  22     9803  11346  14054    136  -2480   3816       C
ATOM    105  C   ALA A  22     -24.676  43.919 -28.739  1.00 93.02           C
ANISOU  105  C   ALA A  22     9914  11111  14318    107  -2460   3698       C
ATOM    106  O   ALA A  22     -24.531  45.125 -28.543  1.00 90.49           O
ANISOU  106  O   ALA A  22     9619  10626  14137     19  -2548   3845       O
ATOM    107  CB  ALA A  22     -24.767  44.386 -31.293  1.00 91.21           C
ANISOU  107  CB  ALA A  22     9599  11126  13931     96  -2640   4074       C
ATOM    108  H   ALA A  22     -25.357  41.348 -30.449  1.00111.41           H
ATOM    109  HA  ALA A  22     -23.716  42.846 -30.277  1.00111.18           H
ATOM    110  HB1 ALA A  22     -23.905  45.051 -31.228  1.00109.45           H
ATOM    111  HB2 ALA A  22     -24.766  43.898 -32.266  1.00109.45           H
ATOM    112  HB3 ALA A  22     -25.673  44.984 -31.183  1.00109.45           H
ATOM    113  N   LEU A  23     -24.893  43.055 -27.739  1.00 99.37           N
ANISOU  113  N   LEU A  23    10747  11858  15150    184  -2343   3432       N
ATOM    114  CA  LEU A  23     -24.912  43.421 -26.316  1.00101.16           C
ANISOU  114  CA  LEU A  23    11043  11819  15572    180  -2314   3295       C
ATOM    115  C   LEU A  23     -23.502  43.702 -25.740  1.00100.58           C
ANISOU  115  C   LEU A  23    10996  11762  15459     60  -2282   3374       C
ATOM    116  O   LEU A  23     -23.400  44.164 -24.605  1.00101.03           O
ANISOU  116  O   LEU A  23    11118  11603  15667     50  -2266   3267       O
ATOM    117  H   LEU A  23     -24.956  42.072 -27.967  1.00119.24           H
ATOM    118  CB  LEU A  23     -25.663  42.325 -25.527  1.00  0.00           C
ATOM    119  CG  LEU A  23     -27.156  42.154 -25.886  1.00  0.00           C
ATOM    120  CD2 LEU A  23     -28.014  43.365 -25.509  1.00  0.00           C
ATOM    121  CD1 LEU A  23     -27.736  40.940 -25.156  1.00  0.00           C
ATOM    122  HA  LEU A  23     -25.462  44.356 -26.212  1.00  0.00           H
ATOM    123  HB2 LEU A  23     -25.157  41.377 -25.705  1.00  0.00           H
ATOM    124  HB3 LEU A  23     -25.587  42.542 -24.460  1.00  0.00           H
ATOM    125  HG  LEU A  23     -27.258  41.992 -26.957  1.00  0.00           H
ATOM    126 HD21 LEU A  23     -29.062  43.149 -25.716  1.00  0.00           H
ATOM    127 HD22 LEU A  23     -27.719  44.225 -26.109  1.00  0.00           H
ATOM    128 HD23 LEU A  23     -27.892  43.596 -24.451  1.00  0.00           H
ATOM    129 HD11 LEU A  23     -28.768  40.781 -25.466  1.00  0.00           H
ATOM    130 HD12 LEU A  23     -27.161  40.051 -25.420  1.00  0.00           H
ATOM    131 HD13 LEU A  23     -27.692  41.088 -24.078  1.00  0.00           H
ATOM    132  N   GLY A  24     -22.445  43.534 -26.546  1.00 99.96           N
ANISOU  132  N   GLY A  24    10869  11929  15184    -26  -2275   3558       N
ATOM    133  CA  GLY A  24     -21.042  43.741 -26.190  1.00100.15           C
ANISOU  133  CA  GLY A  24    10903  11979  15172   -146  -2253   3655       C
ATOM    134  C   GLY A  24     -20.317  42.463 -25.730  1.00 97.27           C
ANISOU  134  C   GLY A  24    10539  11778  14643   -123  -2089   3490       C
ATOM    135  O   GLY A  24     -20.893  41.365 -25.734  1.00 96.73           O
ANISOU  135  O   GLY A  24    10469  11787  14497    -11  -1986   3290       O
ATOM    136  H   GLY A  24     -22.603  43.159 -27.468  1.00119.96           H
ATOM    137  HA2 GLY A  24     -20.520  44.125 -27.066  1.00120.19           H
ATOM    138  HA3 GLY A  24     -20.968  44.489 -25.401  1.00120.19           H
ATOM    139  N   PRO A  25     -19.077  42.612 -25.223  1.00 84.32           N
ANISOU  139  N   PRO A  25     8898  10193  12949   -229  -2061   3573       N
ATOM    140  CA  PRO A  25     -18.345  41.537 -24.562  1.00 80.78           C
ANISOU  140  CA  PRO A  25     8450   9901  12342   -208  -1902   3425       C
ATOM    141  C   PRO A  25     -19.050  41.147 -23.251  1.00 81.94           C
ANISOU  141  C   PRO A  25     8669   9853  12613   -111  -1823   3133       C
ATOM    142  O   PRO A  25     -19.216  41.989 -22.370  1.00 81.95           O
ANISOU  142  O   PRO A  25     8732   9581  12825   -126  -1888   3084       O
ATOM    143  CB  PRO A  25     -16.926  42.086 -24.315  1.00 78.84           C
ANISOU  143  CB  PRO A  25     8189   9700  12068   -354  -1924   3599       C
ATOM    144  CG  PRO A  25     -16.821  43.304 -25.235  1.00 80.85           C
ANISOU  144  CG  PRO A  25     8413   9901  12405   -449  -2079   3875       C
ATOM    145  CD  PRO A  25     -18.257  43.811 -25.281  1.00 81.58           C
ANISOU  145  CD  PRO A  25     8543   9770  12683   -374  -2172   3813       C
ATOM    146  HA  PRO A  25     -18.291  40.679 -25.234  1.00 96.94           H
ATOM    147  HB2 PRO A  25     -16.815  42.418 -23.281  1.00 94.61           H
ATOM    148  HB3 PRO A  25     -16.160  41.347 -24.550  1.00 94.61           H
ATOM    149  HG2 PRO A  25     -16.139  44.058 -24.839  1.00 97.02           H
ATOM    150  HG3 PRO A  25     -16.512  42.991 -26.234  1.00 97.02           H
ATOM    151  HD2 PRO A  25     -18.460  44.429 -24.405  1.00 97.89           H
ATOM    152  HD3 PRO A  25     -18.422  44.381 -26.196  1.00 97.89           H
ATOM    153  N   ALA A  26     -19.328  39.855 -23.044  1.00 89.55           N
ANISOU  153  N   ALA A  26     9627  10956  13442     -7  -1679   2939       N
ATOM    154  CA  ALA A  26     -19.931  39.351 -21.795  1.00 86.98           C
ANISOU  154  CA  ALA A  26     9365  10465  13218     96  -1583   2661       C
ATOM    155  C   ALA A  26     -19.092  39.612 -20.529  1.00 83.43           C
ANISOU  155  C   ALA A  26     8967   9926  12808     39  -1543   2609       C
ATOM    156  O   ALA A  26     -19.597  39.502 -19.407  1.00 82.91           O
ANISOU  156  O   ALA A  26     8974   9620  12907     95  -1530   2441       O
ATOM    157  CB  ALA A  26     -20.074  37.835 -21.930  1.00 86.12           C
ANISOU  157  CB  ALA A  26     9233  10546  12944    211  -1429   2481       C
ATOM    158  H   ALA A  26     -19.235  39.217 -23.822  1.00107.46           H
ATOM    159  HA  ALA A  26     -20.913  39.805 -21.656  1.00104.38           H
ATOM    160  HB1 ALA A  26     -20.476  37.441 -21.001  1.00103.35           H
ATOM    161  HB2 ALA A  26     -20.745  37.584 -22.740  1.00103.35           H
ATOM    162  HB3 ALA A  26     -19.100  37.386 -22.122  1.00103.35           H
ATOM    163  N   TRP A  27     -17.777  39.633 -20.725  1.00 75.83           N
ANISOU  163  N   TRP A  27     7966   9153  11694    -66  -1524   2752       N
ATOM    164  CA  TRP A  27     -16.724  39.739 -19.724  1.00 71.59           C
ANISOU  164  CA  TRP A  27     7467   8555  11180   -130  -1495   2718       C
ATOM    165  C   TRP A  27     -15.412  40.121 -20.421  1.00 71.79           C
ANISOU  165  C   TRP A  27     7425   8773  11078   -276  -1536   2972       C
ATOM    166  O   TRP A  27     -15.235  39.823 -21.606  1.00 72.31           O
ANISOU  166  O   TRP A  27     7420   9061  10992   -301  -1539   3134       O
ATOM    167  CB  TRP A  27     -16.570  38.411 -18.952  1.00 71.48           C
ANISOU  167  CB  TRP A  27     7483   8616  11062    -29  -1314   2471       C
ATOM    168  CG  TRP A  27     -16.285  37.170 -19.750  1.00 68.74           C
ANISOU  168  CG  TRP A  27     7072   8585  10462     14  -1187   2466       C
ATOM    169  CD1 TRP A  27     -17.221  36.303 -20.194  1.00 66.83           C
ANISOU  169  CD1 TRP A  27     6815   8420  10155    132  -1111   2341       C
ATOM    170  CD2 TRP A  27     -15.003  36.649 -20.225  1.00 65.56           C
ANISOU  170  CD2 TRP A  27     6611   8459   9839    -61  -1123   2595       C
ATOM    171  NE1 TRP A  27     -16.619  35.302 -20.931  1.00 66.45           N
ANISOU  171  NE1 TRP A  27     6713   8678   9856    138  -1005   2378       N
ATOM    172  CE2 TRP A  27     -15.249  35.465 -20.984  1.00 66.79           C
ANISOU  172  CE2 TRP A  27     6730   8852   9797     24  -1006   2536       C
ATOM    173  CE3 TRP A  27     -13.656  37.046 -20.087  1.00 67.59           C
ANISOU  173  CE3 TRP A  27     6844   8788  10052   -190  -1153   2756       C
ATOM    174  CZ2 TRP A  27     -14.216  34.727 -21.586  1.00 65.49           C
ANISOU  174  CZ2 TRP A  27     6510   8988   9386    -10   -914   2633       C
ATOM    175  CZ3 TRP A  27     -12.610  36.320 -20.690  1.00 70.07           C
ANISOU  175  CZ3 TRP A  27     7093   9404  10126   -225  -1060   2858       C
ATOM    176  CH2 TRP A  27     -12.886  35.160 -21.435  1.00 67.38           C
ANISOU  176  CH2 TRP A  27     6723   9294   9585   -132   -940   2796       C
ATOM    177  H   TRP A  27     -17.464  39.676 -21.684  1.00 91.00           H
ATOM    178  HA  TRP A  27     -16.988  40.538 -19.032  1.00 85.91           H
ATOM    179  HB2 TRP A  27     -15.752  38.524 -18.240  1.00 85.78           H
ATOM    180  HB3 TRP A  27     -17.474  38.246 -18.365  1.00 85.78           H
ATOM    181  HD1 TRP A  27     -18.286  36.418 -20.016  1.00 80.19           H
ATOM    182  HE1 TRP A  27     -17.145  34.570 -21.383  1.00 79.74           H
ATOM    183  HE3 TRP A  27     -13.435  37.936 -19.517  1.00 81.11           H
ATOM    184  HZ2 TRP A  27     -14.441  33.836 -22.150  1.00 78.59           H
ATOM    185  HZ3 TRP A  27     -11.592  36.671 -20.582  1.00 84.09           H
ATOM    186  HH2 TRP A  27     -12.075  34.606 -21.882  1.00 80.86           H
ATOM    187  N   ASP A  28     -14.450  40.642 -19.661  1.00 72.48           N
ANISOU  187  N   ASP A  28     7537   8771  11231   -370  -1569   3006       N
ATOM    188  CA  ASP A  28     -13.078  40.900 -20.118  1.00 75.62           C
ANISOU  188  CA  ASP A  28     7868   9342  11522   -512  -1596   3235       C
ATOM    189  C   ASP A  28     -12.032  40.291 -19.163  1.00 73.88           C
ANISOU  189  C   ASP A  28     7661   9195  11216   -524  -1488   3121       C
ATOM    190  O   ASP A  28     -12.347  39.796 -18.074  1.00 74.05           O
ANISOU  190  O   ASP A  28     7756   9080  11298   -436  -1422   2881       O
ATOM    191  CB  ASP A  28     -12.863  42.408 -20.325  1.00 77.62           C
ANISOU  191  CB  ASP A  28     8119   9412  11960   -648  -1779   3449       C
ATOM    192  CG  ASP A  28     -12.794  43.175 -19.004  1.00 77.14           C
ANISOU  192  CG  ASP A  28     8148   9049  12113   -670  -1845   3326       C
ATOM    193  OD1 ASP A  28     -11.727  43.100 -18.351  1.00 77.70           O
ANISOU  193  OD1 ASP A  28     8222   9138  12163   -740  -1826   3317       O
ATOM    194  OD2 ASP A  28     -13.798  43.805 -18.618  1.00 78.88           O
ANISOU  194  OD2 ASP A  28     8438   9014  12521   -614  -1919   3240       O
ATOM    195  H   ASP A  28     -14.679  40.876 -18.700  1.00 86.97           H
ATOM    196  HA  ASP A  28     -12.930  40.419 -21.085  1.00 90.75           H
ATOM    197  HB2 ASP A  28     -11.926  42.550 -20.864  1.00 93.14           H
ATOM    198  HB3 ASP A  28     -13.663  42.802 -20.953  1.00 93.14           H
ATOM    199  N   GLU A  29     -10.773  40.228 -19.605  1.00 71.09           N
ANISOU  199  N   GLU A  29     7232   9060  10717   -628  -1470   3304       N
ATOM    200  CA  GLU A  29      -9.720  39.524 -18.875  1.00 70.37           C
ANISOU  200  CA  GLU A  29     7137   9093  10508   -638  -1356   3218       C
ATOM    201  C   GLU A  29      -9.359  40.153 -17.502  1.00 69.29           C
ANISOU  201  C   GLU A  29     7070   8710  10548   -682  -1419   3118       C
ATOM    202  O   GLU A  29      -8.833  39.432 -16.651  1.00 70.76           O
ANISOU  202  O   GLU A  29     7273   8956  10656   -658  -1320   2986       O
ATOM    203  H   GLU A  29     -10.552  40.579 -20.538  1.00 85.30           H
ATOM    204  CB  GLU A  29      -8.472  39.330 -19.765  1.00  0.00           C
ATOM    205  CG  GLU A  29      -8.639  38.414 -21.001  1.00  0.00           C
ATOM    206  CD  GLU A  29      -9.171  39.042 -22.301  1.00  0.00           C
ATOM    207  OE2 GLU A  29      -9.168  38.295 -23.316  1.00  0.00           O
ATOM    208  OE1 GLU A  29      -9.728  40.161 -22.249  1.00  0.00           O
ATOM    209  HA  GLU A  29     -10.103  38.533 -18.642  1.00  0.00           H
ATOM    210  HB2 GLU A  29      -7.727  38.841 -19.133  1.00  0.00           H
ATOM    211  HB3 GLU A  29      -8.058  40.299 -20.051  1.00  0.00           H
ATOM    212  HG2 GLU A  29      -7.651  38.019 -21.231  1.00  0.00           H
ATOM    213  HG3 GLU A  29      -9.266  37.567 -20.735  1.00  0.00           H
ATOM    214  N   SER A  30      -9.750  41.403 -17.195  1.00 69.83           N
ANISOU  214  N   SER A  30     7183   8503  10846   -741  -1581   3172       N
ATOM    215  CA  SER A  30      -9.532  42.037 -15.875  1.00 66.88           C
ANISOU  215  CA  SER A  30     6888   7883  10641   -778  -1650   3069       C
ATOM    216  C   SER A  30     -10.332  41.380 -14.741  1.00 65.02           C
ANISOU  216  C   SER A  30     6754   7510  10439   -619  -1550   2752       C
ATOM    217  O   SER A  30      -9.916  41.403 -13.579  1.00 64.16           O
ANISOU  217  O   SER A  30     6713   7263  10403   -621  -1559   2627       O
ATOM    218  CB  SER A  30      -9.861  43.537 -15.933  1.00 66.23           C
ANISOU  218  CB  SER A  30     6838   7529  10799   -868  -1845   3198       C
ATOM    219  OG  SER A  30     -11.251  43.784 -15.921  1.00 67.69           O
ANISOU  219  OG  SER A  30     7096   7509  11114   -755  -1870   3069       O
ATOM    220  H   SER A  30     -10.333  41.907 -17.865  1.00 83.79           H
ATOM    221  HA  SER A  30      -8.478  41.941 -15.618  1.00 80.26           H
ATOM    222  HB2 SER A  30      -9.421  44.032 -15.067  1.00 79.48           H
ATOM    223  HB3 SER A  30      -9.428  43.972 -16.835  1.00 79.48           H
ATOM    224  HG  SER A  30     -11.583  43.601 -16.841  1.00 81.23           H
ATOM    225  N   GLN A  31     -11.422  40.687 -15.082  1.00 66.97           N
ANISOU  225  N   GLN A  31     7015   7791  10639   -479  -1457   2622       N
ATOM    226  CA  GLN A  31     -12.245  39.932 -14.139  1.00 65.84           C
ANISOU  226  CA  GLN A  31     6959   7534  10522   -318  -1342   2329       C
ATOM    227  C   GLN A  31     -11.643  38.563 -13.755  1.00 69.25           C
ANISOU  227  C   GLN A  31     7371   8198  10741   -252  -1156   2199       C
ATOM    228  O   GLN A  31     -12.145  37.910 -12.829  1.00 66.88           O
ANISOU  228  O   GLN A  31     7144   7815  10453   -121  -1047   1956       O
ATOM    229  CB  GLN A  31     -13.650  39.741 -14.722  1.00 64.18           C
ANISOU  229  CB  GLN A  31     6763   7257  10366   -198  -1322   2248       C
ATOM    230  CG  GLN A  31     -14.322  41.028 -15.225  1.00 69.25           C
ANISOU  230  CG  GLN A  31     7411   7705  11195   -255  -1498   2396       C
ATOM    231  CD  GLN A  31     -15.739  40.751 -15.705  1.00 68.35           C
ANISOU  231  CD  GLN A  31     7295   7557  11118   -139  -1478   2329       C
ATOM    232  OE1 GLN A  31     -15.996  40.647 -16.886  1.00 67.86           O
ANISOU  232  OE1 GLN A  31     7165   7603  11015   -177  -1536   2498       O
ATOM    233  NE2 GLN A  31     -16.655  40.367 -14.845  1.00 69.04           N
ANISOU  233  NE2 GLN A  31     7455   7494  11284      7  -1395   2084       N
ATOM    234  H   GLN A  31     -11.712  40.724 -16.055  1.00 80.36           H
ATOM    235  HA  GLN A  31     -12.332  40.524 -13.230  1.00 79.01           H
ATOM    236  HB2 GLN A  31     -13.600  39.026 -15.546  1.00 77.02           H
ATOM    237  HB3 GLN A  31     -14.269  39.321 -13.933  1.00 77.02           H
ATOM    238  HG2 GLN A  31     -14.354  41.768 -14.426  1.00 83.10           H
ATOM    239  HG3 GLN A  31     -13.758  41.442 -16.063  1.00 83.10           H
ATOM    240 HE21 GLN A  31     -16.487  40.510 -13.856  1.00 82.85           H
ATOM    241 HE22 GLN A  31     -17.568  40.238 -15.238  1.00 82.85           H
ATOM    242  N   LEU A  32     -10.635  38.088 -14.501  1.00 71.44           N
ANISOU  242  N   LEU A  32     7555   8761  10828   -333  -1112   2359       N
ATOM    243  CA  LEU A  32      -9.904  36.842 -14.253  1.00 69.75           C
ANISOU  243  CA  LEU A  32     7317   8783  10402   -277   -935   2259       C
ATOM    244  C   LEU A  32      -8.745  37.085 -13.274  1.00 70.70           C
ANISOU  244  C   LEU A  32     7450   8888  10525   -357   -954   2262       C
ATOM    245  O   LEU A  32      -8.008  38.062 -13.388  1.00 76.96           O
ANISOU  245  O   LEU A  32     8211   9633  11398   -506  -1095   2452       O
ATOM    246  CB  LEU A  32      -9.374  36.246 -15.579  1.00 66.71           C
ANISOU  246  CB  LEU A  32     6826   8725   9794   -312   -869   2430       C
ATOM    247  CG  LEU A  32     -10.390  36.110 -16.733  1.00 67.22           C
ANISOU  247  CG  LEU A  32     6864   8840   9838   -257   -877   2474       C
ATOM    248  CD1 LEU A  32      -9.759  35.373 -17.917  1.00 67.14           C
ANISOU  248  CD1 LEU A  32     6759   9165   9585   -286   -805   2637       C
ATOM    249  CD2 LEU A  32     -11.636  35.322 -16.339  1.00 66.20           C
ANISOU  249  CD2 LEU A  32     6800   8612   9742    -86   -774   2207       C
ATOM    250  H   LEU A  32     -10.241  38.715 -15.198  1.00 85.73           H
ATOM    251  HA  LEU A  32     -10.585  36.121 -13.800  1.00 83.70           H
ATOM    252  HB2 LEU A  32      -8.557  36.878 -15.932  1.00 80.05           H
ATOM    253  HB3 LEU A  32      -8.953  35.265 -15.364  1.00 80.05           H
ATOM    254  HG  LEU A  32     -10.699  37.101 -17.060  1.00 80.67           H
ATOM    255 HD11 LEU A  32      -8.896  35.932 -18.279  1.00  0.00           H
ATOM    256 HD12 LEU A  32     -10.485  35.295 -18.726  1.00  0.00           H
ATOM    257 HD13 LEU A  32      -9.443  34.371 -17.624  1.00  0.00           H
ATOM    258 HD21 LEU A  32     -12.128  35.831 -15.516  1.00  0.00           H
ATOM    259 HD22 LEU A  32     -11.367  34.310 -16.059  1.00  0.00           H
ATOM    260 HD23 LEU A  32     -12.326  35.297 -17.183  1.00  0.00           H
ATOM    261  N   ARG A  33      -8.480  36.140 -12.365  1.00 64.02           N
ANISOU  261  N   ARG A  33     6649   8080   9595   -256   -811   2053       N
ATOM    262  CA  ARG A  33      -7.293  36.214 -11.491  1.00 63.69           C
ANISOU  262  CA  ARG A  33     6611   8067   9520   -320   -810   2048       C
ATOM    263  C   ARG A  33      -6.026  35.847 -12.273  1.00 64.27           C
ANISOU  263  C   ARG A  33     6567   8467   9384   -412   -754   2240       C
ATOM    264  O   ARG A  33      -6.039  34.889 -13.045  1.00 64.20           O
ANISOU  264  O   ARG A  33     6500   8687   9207   -371   -648   2289       O
ATOM    265  CB  ARG A  33      -7.494  35.321 -10.262  1.00 65.29           C
ANISOU  265  CB  ARG A  33     6903   8214   9691   -169   -667   1762       C
ATOM    266  CG  ARG A  33      -8.684  35.806  -9.420  1.00 64.95           C
ANISOU  266  CG  ARG A  33     6978   7849   9849    -62   -707   1569       C
ATOM    267  CD  ARG A  33      -8.900  34.929  -8.182  1.00 63.63           C
ANISOU  267  CD  ARG A  33     6898   7636   9642     98   -552   1295       C
ATOM    268  NE  ARG A  33     -10.038  35.405  -7.380  1.00 68.17           N
ANISOU  268  NE  ARG A  33     7588   7903  10412    210   -583   1119       N
ATOM    269  CZ  ARG A  33     -10.039  36.442  -6.574  1.00 69.10           C
ANISOU  269  CZ  ARG A  33     7798   7757  10699    192   -703   1066       C
ATOM    270  NH1 ARG A  33      -8.960  37.128  -6.324  1.00 68.55           N
ANISOU  270  NH1 ARG A  33     7719   7688  10638     61   -813   1168       N
ATOM    271  NH2 ARG A  33     -11.142  36.796  -5.986  1.00 66.86           N
ANISOU  271  NH2 ARG A  33     7618   7205  10580    309   -714    909       N
ATOM    272  H   ARG A  33      -9.047  35.301 -12.354  1.00 76.82           H
ATOM    273  HA  ARG A  33      -7.171  37.248 -11.162  1.00 76.43           H
ATOM    274  HB2 ARG A  33      -7.674  34.301 -10.595  1.00 78.35           H
ATOM    275  HB3 ARG A  33      -6.589  35.338  -9.650  1.00 78.35           H
ATOM    276  HG2 ARG A  33      -8.499  36.834  -9.106  1.00 77.94           H
ATOM    277  HG3 ARG A  33      -9.596  35.785 -10.019  1.00 77.94           H
ATOM    278  HD2 ARG A  33      -9.134  33.921  -8.511  1.00 76.35           H
ATOM    279  HD3 ARG A  33      -7.983  34.875  -7.589  1.00 76.35           H
ATOM    280  HE  ARG A  33     -10.927  34.976  -7.581  1.00 81.81           H
ATOM    281 HH11 ARG A  33      -8.096  36.822  -6.749  1.00 82.26           H
ATOM    282 HH12 ARG A  33      -8.993  37.998  -5.831  1.00 82.26           H
ATOM    283 HH21 ARG A  33     -11.975  36.220  -6.085  1.00 80.23           H
ATOM    284 HH22 ARG A  33     -11.210  37.697  -5.556  1.00 80.23           H
ATOM    285  N   SER A  34      -4.910  36.533 -12.050  1.00 66.78           N
ANISOU  285  N   SER A  34     6853   8804   9717   -539   -830   2354       N
ATOM    286  CA  SER A  34      -3.620  36.113 -12.611  1.00 69.74           C
ANISOU  286  CA  SER A  34     7111   9474   9912   -637   -786   2555       C
ATOM    287  C   SER A  34      -3.025  34.946 -11.804  1.00 65.07           C
ANISOU  287  C   SER A  34     6524   9045   9153   -565   -624   2411       C
ATOM    288  O   SER A  34      -3.200  34.874 -10.590  1.00 66.05           O
ANISOU  288  O   SER A  34     6731   9014   9351   -512   -620   2221       O
ATOM    289  CB  SER A  34      -2.674  37.314 -12.732  1.00 71.68           C
ANISOU  289  CB  SER A  34     7300   9656  10278   -829   -968   2792       C
ATOM    290  OG  SER A  34      -2.528  37.998 -11.502  1.00 74.48           O
ANISOU  290  OG  SER A  34     7731   9777  10790   -855  -1060   2672       O
ATOM    291  H   SER A  34      -4.892  37.255 -11.346  1.00 80.14           H
ATOM    292  HA  SER A  34      -3.792  35.754 -13.626  1.00 83.69           H
ATOM    293  HB2 SER A  34      -1.699  36.974 -13.082  1.00 86.01           H
ATOM    294  HB3 SER A  34      -3.083  38.007 -13.470  1.00 86.01           H
ATOM    295  HG  SER A  34      -1.863  38.685 -11.607  1.00 89.37           H
ATOM    296  N   TYR A  35      -2.359  34.008 -12.487  1.00 60.14           N
ANISOU  296  N   TYR A  35     5814   8735   8299   -556   -490   2502       N
ATOM    297  CA  TYR A  35      -1.669  32.847 -11.902  1.00 57.72           C
ANISOU  297  CA  TYR A  35     5503   8615   7811   -481   -319   2381       C
ATOM    298  C   TYR A  35      -0.360  32.566 -12.664  1.00 56.52           C
ANISOU  298  C   TYR A  35     5226   8764   7484   -586   -283   2620       C
ATOM    299  O   TYR A  35      -0.176  33.054 -13.778  1.00 55.76           O
ANISOU  299  O   TYR A  35     5050   8745   7392   -696   -369   2869       O
ATOM    300  CB  TYR A  35      -2.578  31.598 -11.899  1.00 55.78           C
ANISOU  300  CB  TYR A  35     5310   8443   7442   -295   -129   2164       C
ATOM    301  CG  TYR A  35      -3.881  31.713 -11.124  1.00 56.50           C
ANISOU  301  CG  TYR A  35     5521   8243   7703   -179   -144   1920       C
ATOM    302  CD1 TYR A  35      -3.841  31.930  -9.734  1.00 55.75           C
ANISOU  302  CD1 TYR A  35     5512   7961   7710   -138   -158   1744       C
ATOM    303  CD2 TYR A  35      -5.128  31.613 -11.780  1.00 56.92           C
ANISOU  303  CD2 TYR A  35     5602   8209   7815   -106   -144   1869       C
ATOM    304  CE1 TYR A  35      -5.026  32.076  -9.000  1.00 56.52           C
ANISOU  304  CE1 TYR A  35     5722   7792   7961    -22   -163   1528       C
ATOM    305  CE2 TYR A  35      -6.324  31.769 -11.048  1.00 56.23           C
ANISOU  305  CE2 TYR A  35     5619   7857   7890      4   -152   1655       C
ATOM    306  CZ  TYR A  35      -6.260  32.020  -9.658  1.00 56.17           C
ANISOU  306  CZ  TYR A  35     5696   7666   7978     48   -157   1487       C
ATOM    307  OH  TYR A  35      -7.380  32.187  -8.911  1.00 60.56           O
ANISOU  307  OH  TYR A  35     6358   7958   8693    166   -157   1281       O
ATOM    308  H   TYR A  35      -2.215  34.145 -13.478  1.00 72.16           H
ATOM    309  HA  TYR A  35      -1.406  33.079 -10.869  1.00 69.26           H
ATOM    310  HB2 TYR A  35      -2.796  31.316 -12.931  1.00 66.94           H
ATOM    311  HB3 TYR A  35      -2.012  30.779 -11.454  1.00 66.94           H
ATOM    312  HD1 TYR A  35      -2.894  32.053  -9.231  1.00 66.90           H
ATOM    313  HD2 TYR A  35      -5.159  31.460 -12.850  1.00 68.30           H
ATOM    314  HE1 TYR A  35      -4.996  32.299  -7.941  1.00 67.83           H
ATOM    315  HE2 TYR A  35      -7.277  31.745 -11.555  1.00 67.48           H
ATOM    316  HH  TYR A  35      -8.176  32.356  -9.459  1.00 72.67           H
ATOM    317  N   SER A  36       0.565  31.810 -12.064  1.00 61.50           N
ANISOU  317  N   SER A  36     5842   9568   7959   -542   -147   2547       N
ATOM    318  CA  SER A  36       1.921  31.571 -12.598  1.00 64.60           C
ANISOU  318  CA  SER A  36     6116  10232   8199   -642   -113   2765       C
ATOM    319  C   SER A  36       2.015  30.565 -13.758  1.00 62.38           C
ANISOU  319  C   SER A  36     5771  10253   7675   -585     44   2859       C
ATOM    320  O   SER A  36       3.041  30.521 -14.434  1.00 66.36           O
ANISOU  320  O   SER A  36     6170  10985   8060   -675     59   3089       O
ATOM    321  CB  SER A  36       2.818  31.094 -11.455  1.00 61.48           C
ANISOU  321  CB  SER A  36     5728   9892   7741   -621    -42   2652       C
ATOM    322  OG  SER A  36       2.299  29.921 -10.850  1.00 57.62           O
ANISOU  322  OG  SER A  36     5302   9487   7104   -443    159   2415       O
ATOM    323  H   SER A  36       0.373  31.437 -11.145  1.00 73.81           H
ATOM    324  HA  SER A  36       2.324  32.515 -12.967  1.00 77.53           H
ATOM    325  HB2 SER A  36       3.816  30.884 -11.843  1.00 73.78           H
ATOM    326  HB3 SER A  36       2.898  31.878 -10.702  1.00 73.78           H
ATOM    327  HG  SER A  36       3.039  29.483 -10.407  1.00 69.14           H
ATOM    328  N   PHE A  37       1.006  29.712 -13.953  1.00 57.68           N
ANISOU  328  N   PHE A  37     5239   9668   7011   -440    159   2691       N
ATOM    329  CA  PHE A  37       1.027  28.599 -14.910  1.00 58.11           C
ANISOU  329  CA  PHE A  37     5250  10011   6819   -367    324   2738       C
ATOM    330  C   PHE A  37       0.338  28.935 -16.251  1.00 57.55           C
ANISOU  330  C   PHE A  37     5154   9959   6752   -388    258   2883       C
ATOM    331  O   PHE A  37      -0.694  29.612 -16.258  1.00 57.32           O
ANISOU  331  O   PHE A  37     5167   9696   6917   -412    118   2866       O
ATOM    332  CB  PHE A  37       0.407  27.366 -14.239  1.00 54.06           C
ANISOU  332  CB  PHE A  37     4817   9520   6201   -183    513   2450       C
ATOM    333  CG  PHE A  37      -1.015  27.539 -13.731  1.00 52.07           C
ANISOU  333  CG  PHE A  37     4668   8989   6126    -93    472   2230       C
ATOM    334  CD1 PHE A  37      -2.102  27.447 -14.619  1.00 51.43           C
ANISOU  334  CD1 PHE A  37     4604   8884   6052    -37    470   2212       C
ATOM    335  CD2 PHE A  37      -1.248  27.846 -12.377  1.00 51.09           C
ANISOU  335  CD2 PHE A  37     4624   8627   6161    -61    435   2044       C
ATOM    336  CE1 PHE A  37      -3.402  27.737 -14.175  1.00 53.39           C
ANISOU  336  CE1 PHE A  37     4939   8877   6471     46    435   2018       C
ATOM    337  CE2 PHE A  37      -2.554  28.100 -11.924  1.00 49.90           C
ANISOU  337  CE2 PHE A  37     4566   8219   6174     29    405   1850       C
ATOM    338  CZ  PHE A  37      -3.631  28.069 -12.828  1.00 53.23           C
ANISOU  338  CZ  PHE A  37     4997   8620   6610     81    406   1839       C
ATOM    339  H   PHE A  37       0.197  29.801 -13.361  1.00 69.22           H
ATOM    340  HA  PHE A  37       2.067  28.356 -15.122  1.00 69.73           H
ATOM    341  HB2 PHE A  37       0.430  26.533 -14.942  1.00 64.87           H
ATOM    342  HB3 PHE A  37       1.047  27.106 -13.396  1.00 64.87           H
ATOM    343  HD1 PHE A  37      -1.928  27.220 -15.661  1.00 61.71           H
ATOM    344  HD2 PHE A  37      -0.414  27.913 -11.690  1.00 61.31           H
ATOM    345  HE1 PHE A  37      -4.212  27.744 -14.887  1.00 64.07           H
ATOM    346  HE2 PHE A  37      -2.718  28.368 -10.891  1.00 59.88           H
ATOM    347  HZ  PHE A  37      -4.625  28.323 -12.493  1.00 63.88           H
ATOM    348  N   PRO A  38       0.797  28.375 -17.388  1.00 57.39           N
ANISOU  348  N   PRO A  38     5071  10219   6517   -376    354   3029       N
ATOM    349  CA  PRO A  38       0.110  28.509 -18.667  1.00 54.88           C
ANISOU  349  CA  PRO A  38     4738   9940   6176   -376    303   3152       C
ATOM    350  C   PRO A  38      -1.121  27.591 -18.737  1.00 53.91           C
ANISOU  350  C   PRO A  38     4689   9807   5988   -215    411   2926       C
ATOM    351  O   PRO A  38      -1.157  26.503 -18.152  1.00 53.74           O
ANISOU  351  O   PRO A  38     4721   9796   5902   -100    554   2695       O
ATOM    352  CB  PRO A  38       1.163  28.147 -19.717  1.00 55.58           C
ANISOU  352  CB  PRO A  38     4727  10346   6046   -429    368   3412       C
ATOM    353  CG  PRO A  38       1.975  27.063 -19.009  1.00 56.16           C
ANISOU  353  CG  PRO A  38     4794  10594   5952   -368    544   3309       C
ATOM    354  CD  PRO A  38       1.948  27.491 -17.538  1.00 50.09           C
ANISOU  354  CD  PRO A  38     4081   9594   5357   -370    504   3113       C
ATOM    355  HA  PRO A  38      -0.208  29.543 -18.818  1.00 65.86           H
ATOM    356  HB2 PRO A  38       0.722  27.785 -20.647  1.00 66.70           H
ATOM    357  HB3 PRO A  38       1.802  29.012 -19.911  1.00 66.70           H
ATOM    358  HG2 PRO A  38       1.467  26.107 -19.124  1.00 67.40           H
ATOM    359  HG3 PRO A  38       2.993  27.003 -19.395  1.00 67.40           H
ATOM    360  HD2 PRO A  38       1.845  26.610 -16.903  1.00 60.11           H
ATOM    361  HD3 PRO A  38       2.865  28.028 -17.292  1.00 60.11           H
ATOM    362  N   THR A  39      -2.052  27.929 -19.628  1.00 52.56           N
ANISOU  362  N   THR A  39     4519   9612   5839   -209    337   2999       N
ATOM    363  CA  THR A  39      -3.226  27.105 -19.954  1.00 53.57           C
ANISOU  363  CA  THR A  39     4707   9726   5920    -68    417   2804       C
ATOM    364  C   THR A  39      -3.452  27.002 -21.465  1.00 56.42           C
ANISOU  364  C   THR A  39     5031  10234   6171    -72    380   2975       C
ATOM    365  O   THR A  39      -2.901  27.788 -22.249  1.00 60.52           O
ANISOU  365  O   THR A  39     5495  10767   6731   -183    251   3225       O
ATOM    366  CB  THR A  39      -4.490  27.632 -19.253  1.00 52.76           C
ANISOU  366  CB  THR A  39     4682   9298   6065    -24    330   2602       C
ATOM    367  OG1 THR A  39      -4.741  28.962 -19.638  1.00 54.10           O
ANISOU  367  OG1 THR A  39     4835   9293   6427   -136    127   2766       O
ATOM    368  CG2 THR A  39      -4.382  27.602 -17.730  1.00 53.35           C
ANISOU  368  CG2 THR A  39     4811   9228   6233     10    384   2400       C
ATOM    369  H   THR A  39      -2.024  28.853 -20.033  1.00 63.07           H
ATOM    370  HA  THR A  39      -3.043  26.099 -19.591  1.00 64.28           H
ATOM    371  HB  THR A  39      -5.335  27.011 -19.550  1.00 63.31           H
ATOM    372  HG1 THR A  39      -5.357  29.357 -18.978  1.00 64.92           H
ATOM    373 HG21 THR A  39      -5.337  27.880 -17.289  1.00 64.03           H
ATOM    374 HG22 THR A  39      -4.120  26.601 -17.401  1.00 64.03           H
ATOM    375 HG23 THR A  39      -3.622  28.306 -17.390  1.00 64.03           H
ATOM    376  N   ARG A  40      -4.193  25.979 -21.912  1.00 53.91           N
ANISOU  376  N   ARG A  40     4747  10024   5712     55    496   2838       N
ATOM    377  CA  ARG A  40      -4.764  25.844 -23.274  1.00 56.46           C
ANISOU  377  CA  ARG A  40     5058  10447   5948     80    454   2939       C
ATOM    378  C   ARG A  40      -6.305  25.854 -23.197  1.00 52.77           C
ANISOU  378  C   ARG A  40     4653   9767   5631    165    404   2734       C
ATOM    379  O   ARG A  40      -6.832  25.503 -22.144  1.00 47.57           O
ANISOU  379  O   ARG A  40     4049   8958   5066    241    471   2485       O
ATOM    380  H   ARG A  40      -4.558  25.344 -21.201  1.00 64.69           H
ATOM    381  CB  ARG A  40      -4.225  24.568 -23.961  1.00  0.00           C
ATOM    382  CG  ARG A  40      -2.724  24.556 -24.327  1.00  0.00           C
ATOM    383  CD  ARG A  40      -2.281  25.595 -25.377  1.00  0.00           C
ATOM    384  NE  ARG A  40      -2.192  26.946 -24.796  1.00  0.00           N
ATOM    385  CZ  ARG A  40      -2.175  28.126 -25.382  1.00  0.00           C
ATOM    386  NH1 ARG A  40      -2.134  28.281 -26.675  1.00  0.00           N
ATOM    387  NH2 ARG A  40      -2.245  29.187 -24.634  1.00  0.00           N
ATOM    388  HA  ARG A  40      -4.495  26.717 -23.857  1.00  0.00           H
ATOM    389  HB2 ARG A  40      -4.415  23.718 -23.301  1.00  0.00           H
ATOM    390  HB3 ARG A  40      -4.794  24.389 -24.875  1.00  0.00           H
ATOM    391  HG2 ARG A  40      -2.498  23.568 -24.733  1.00  0.00           H
ATOM    392  HG3 ARG A  40      -2.125  24.675 -23.423  1.00  0.00           H
ATOM    393  HD2 ARG A  40      -1.291  25.309 -25.743  1.00  0.00           H
ATOM    394  HD3 ARG A  40      -2.978  25.578 -26.217  1.00  0.00           H
ATOM    395  HE  ARG A  40      -2.250  26.994 -23.784  1.00  0.00           H
ATOM    396 HH11 ARG A  40      -2.102  27.469 -27.261  1.00  0.00           H
ATOM    397 HH12 ARG A  40      -2.171  29.203 -27.070  1.00  0.00           H
ATOM    398 HH21 ARG A  40      -2.413  29.050 -23.640  1.00  0.00           H
ATOM    399 HH22 ARG A  40      -2.267  30.111 -25.023  1.00  0.00           H
ATOM    400  N   PRO A  41      -7.049  26.300 -24.229  1.00 57.73           N
ANISOU  400  N   PRO A  41     5273  10376   6287    159    290   2833       N
ATOM    401  CA  PRO A  41      -8.504  26.439 -24.132  1.00 58.61           C
ANISOU  401  CA  PRO A  41     5434  10265   6570    229    223   2653       C
ATOM    402  C   PRO A  41      -9.201  25.066 -24.174  1.00 54.86           C
ANISOU  402  C   PRO A  41     4996   9881   5967    372    364   2433       C
ATOM    403  O   PRO A  41      -8.873  24.244 -25.029  1.00 57.58           O
ANISOU  403  O   PRO A  41     5325  10482   6070    413    464   2480       O
ATOM    404  CB  PRO A  41      -8.936  27.338 -25.302  1.00 59.65           C
ANISOU  404  CB  PRO A  41     5534  10376   6756    166     49   2867       C
ATOM    405  CG  PRO A  41      -7.650  27.688 -26.059  1.00 63.33           C
ANISOU  405  CG  PRO A  41     5935  11077   7049     75     45   3158       C
ATOM    406  CD  PRO A  41      -6.610  26.686 -25.559  1.00 61.68           C
ANISOU  406  CD  PRO A  41     5719  11068   6648    103    227   3106       C
ATOM    407  HA  PRO A  41      -8.746  26.948 -23.202  1.00 70.33           H
ATOM    408  HB2 PRO A  41      -9.628  26.812 -25.961  1.00 71.58           H
ATOM    409  HB3 PRO A  41      -9.408  28.249 -24.931  1.00 71.58           H
ATOM    410  HG2 PRO A  41      -7.790  27.604 -27.137  1.00 75.99           H
ATOM    411  HG3 PRO A  41      -7.335  28.699 -25.798  1.00 75.99           H
ATOM    412  HD2 PRO A  41      -6.621  25.802 -26.200  1.00 74.01           H
ATOM    413  HD3 PRO A  41      -5.622  27.143 -25.565  1.00 74.01           H
ATOM    414  N   ILE A  42     -10.237  24.848 -23.355  1.00 49.83           N
ANISOU  414  N   ILE A  42     4408   9025   5499    450    374   2191       N
ATOM    415  CA  ILE A  42     -11.158  23.702 -23.512  1.00 45.73           C
ANISOU  415  CA  ILE A  42     3921   8544   4909    583    482   1976       C
ATOM    416  C   ILE A  42     -12.013  23.924 -24.778  1.00 48.81           C
ANISOU  416  C   ILE A  42     4295   8950   5298    593    361   2055       C
ATOM    417  O   ILE A  42     -12.531  25.034 -24.949  1.00 47.96           O
ANISOU  417  O   ILE A  42     4177   8681   5366    531    191   2161       O
ATOM    418  CB  ILE A  42     -12.037  23.485 -22.251  1.00 47.11           C
ANISOU  418  CB  ILE A  42     4148   8471   5282    664    535   1703       C
ATOM    419  CG1 ILE A  42     -11.149  23.147 -21.035  1.00 45.29           C
ANISOU  419  CG1 ILE A  42     3937   8235   5035    662    656   1626       C
ATOM    420  CG2 ILE A  42     -13.071  22.364 -22.446  1.00 43.47           C
ANISOU  420  CG2 ILE A  42     3711   8037   4770    796    639   1489       C
ATOM    421  CD1 ILE A  42     -11.829  23.169 -19.662  1.00 43.13           C
ANISOU  421  CD1 ILE A  42     3721   7703   4963    739    703   1379       C
ATOM    422  H   ILE A  42     -10.475  25.580 -22.692  1.00 59.79           H
ATOM    423  HA  ILE A  42     -10.550  22.810 -23.644  1.00 54.87           H
ATOM    424  HB  ILE A  42     -12.584  24.401 -22.054  1.00 56.54           H
ATOM    425 HG12 ILE A  42     -10.728  22.153 -21.189  1.00 54.34           H
ATOM    426 HG13 ILE A  42     -10.332  23.864 -20.984  1.00 54.34           H
ATOM    427 HG21 ILE A  42     -13.687  22.242 -21.557  1.00 52.17           H
ATOM    428 HG22 ILE A  42     -13.737  22.585 -23.280  1.00 52.17           H
ATOM    429 HG23 ILE A  42     -12.550  21.429 -22.644  1.00 52.17           H
ATOM    430 HD11 ILE A  42     -11.076  23.014 -18.890  1.00 51.75           H
ATOM    431 HD12 ILE A  42     -12.304  24.132 -19.496  1.00 51.75           H
ATOM    432 HD13 ILE A  42     -12.566  22.374 -19.585  1.00 51.75           H
ATOM    433  N   PRO A  43     -12.256  22.910 -25.636  1.00 51.34           N
ANISOU  433  N   PRO A  43     4619   9457   5430    673    436   2006       N
ATOM    434  CA  PRO A  43     -13.059  23.095 -26.844  1.00 49.25           C
ANISOU  434  CA  PRO A  43     4341   9219   5153    683    308   2088       C
ATOM    435  C   PRO A  43     -14.509  23.468 -26.495  1.00 52.28           C
ANISOU  435  C   PRO A  43     4744   9340   5781    733    220   1921       C
ATOM    436  O   PRO A  43     -15.164  22.768 -25.721  1.00 50.19           O
ANISOU  436  O   PRO A  43     4509   8957   5604    816    317   1676       O
ATOM    437  CB  PRO A  43     -12.964  21.778 -27.632  1.00 48.05           C
ANISOU  437  CB  PRO A  43     4200   9329   4729    768    432   2038       C
ATOM    438  CG  PRO A  43     -11.739  21.078 -27.043  1.00 47.75           C
ANISOU  438  CG  PRO A  43     4170   9429   4543    781    618   1991       C
ATOM    439  CD  PRO A  43     -11.751  21.543 -25.591  1.00 49.86           C
ANISOU  439  CD  PRO A  43     4451   9469   5026    758    635   1877       C
ATOM    440  HA  PRO A  43     -12.608  23.891 -27.437  1.00 59.10           H
ATOM    441  HB2 PRO A  43     -13.845  21.160 -27.456  1.00 57.66           H
ATOM    442  HB3 PRO A  43     -12.839  21.959 -28.700  1.00 57.66           H
ATOM    443  HG2 PRO A  43     -11.812  19.995 -27.117  1.00 57.30           H
ATOM    444  HG3 PRO A  43     -10.833  21.434 -27.534  1.00 57.30           H
ATOM    445  HD2 PRO A  43     -12.444  20.923 -25.018  1.00 59.84           H
ATOM    446  HD3 PRO A  43     -10.747  21.471 -25.177  1.00 59.84           H
ATOM    447  N   ARG A  44     -15.024  24.545 -27.105  1.00 49.76           N
ANISOU  447  N   ARG A  44     4404   8929   5574    685     37   2062       N
ATOM    448  CA  ARG A  44     -16.457  24.885 -27.123  1.00 52.12           C
ANISOU  448  CA  ARG A  44     4710   9004   6088    733    -65   1938       C
ATOM    449  C   ARG A  44     -17.073  24.299 -28.395  1.00 51.72           C
ANISOU  449  C   ARG A  44     4649   9098   5903    795   -104   1939       C
ATOM    450  O   ARG A  44     -16.689  24.714 -29.486  1.00 51.27           O
ANISOU  450  O   ARG A  44     4570   9160   5752    750   -215   2152       O
ATOM    451  CB  ARG A  44     -16.675  26.412 -27.048  1.00 55.43           C
ANISOU  451  CB  ARG A  44     5117   9215   6728    645   -244   2087       C
ATOM    452  CG  ARG A  44     -16.196  27.051 -25.728  1.00 57.86           C
ANISOU  452  CG  ARG A  44     5444   9353   7188    584   -226   2074       C
ATOM    453  CD  ARG A  44     -16.379  28.582 -25.689  1.00 60.77           C
ANISOU  453  CD  ARG A  44     5803   9522   7763    493   -410   2237       C
ATOM    454  NE  ARG A  44     -17.792  28.995 -25.761  1.00 68.89           N
ANISOU  454  NE  ARG A  44     6838  10357   8981    545   -520   2157       N
ATOM    455  CZ  ARG A  44     -18.661  29.035 -24.769  1.00 68.93           C
ANISOU  455  CZ  ARG A  44     6876  10104   9209    599   -516   1967       C
ATOM    456  NH1 ARG A  44     -18.357  28.862 -23.521  1.00 68.61           N
ANISOU  456  NH1 ARG A  44     6873   9964   9232    613   -409   1829       N
ATOM    457  NH2 ARG A  44     -19.909  29.230 -25.045  1.00 69.34           N
ANISOU  457  NH2 ARG A  44     6925  10001   9422    646   -618   1918       N
ATOM    458  H   ARG A  44     -14.428  25.028 -27.761  1.00 59.71           H
ATOM    459  HA  ARG A  44     -16.955  24.423 -26.272  1.00 62.54           H
ATOM    460  HB2 ARG A  44     -16.158  26.889 -27.882  1.00 66.52           H
ATOM    461  HB3 ARG A  44     -17.743  26.604 -27.157  1.00 66.52           H
ATOM    462  HG2 ARG A  44     -16.742  26.612 -24.895  1.00 69.44           H
ATOM    463  HG3 ARG A  44     -15.135  26.838 -25.594  1.00 69.44           H
ATOM    464  HD2 ARG A  44     -15.930  28.967 -24.771  1.00 72.92           H
ATOM    465  HD3 ARG A  44     -15.841  29.022 -26.534  1.00 72.92           H
ATOM    466  HE  ARG A  44     -18.191  29.129 -26.669  1.00 82.67           H
ATOM    467 HH11 ARG A  44     -17.422  28.926 -23.174  1.00 82.33           H
ATOM    468 HH12 ARG A  44     -19.129  28.926 -22.845  1.00 82.33           H
ATOM    469 HH21 ARG A  44     -20.268  29.389 -25.964  1.00 83.21           H
ATOM    470 HH22 ARG A  44     -20.557  28.908 -24.317  1.00 83.21           H
ATOM    471  N   LEU A  45     -17.933  23.292 -28.259  1.00 50.18           N
ANISOU  471  N   LEU A  45     4472   8893   5700    900    -12   1702       N
ATOM    472  CA  LEU A  45     -18.499  22.495 -29.355  1.00 55.67           C
ANISOU  472  CA  LEU A  45     5163   9741   6248    967    -31   1670       C
ATOM    473  C   LEU A  45     -20.029  22.355 -29.210  1.00 64.23           C
ANISOU  473  C   LEU A  45     6243  10624   7535   1040    -89   1475       C
ATOM    474  O   LEU A  45     -20.576  22.506 -28.119  1.00 54.03           O
ANISOU  474  O   LEU A  45     4957   9089   6484   1052    -84   1348       O
ATOM    475  CB  LEU A  45     -17.807  21.114 -29.393  1.00 59.69           C
ANISOU  475  CB  LEU A  45     5695  10485   6499   1028    154   1576       C
ATOM    476  CG  LEU A  45     -16.280  21.106 -29.632  1.00 61.58           C
ANISOU  476  CG  LEU A  45     5934  10954   6510    969    231   1765       C
ATOM    477  CD1 LEU A  45     -15.764  19.667 -29.613  1.00 61.50           C
ANISOU  477  CD1 LEU A  45     5951  11146   6269   1045    427   1637       C
ATOM    478  CD2 LEU A  45     -15.861  21.692 -30.982  1.00 62.87           C
ANISOU  478  CD2 LEU A  45     6075  11271   6543    913     96   2038       C
ATOM    479  H   LEU A  45     -18.202  23.025 -27.316  1.00 60.21           H
ATOM    480  HA  LEU A  45     -18.314  22.998 -30.305  1.00 66.81           H
ATOM    481  HB2 LEU A  45     -17.998  20.625 -28.436  1.00 71.63           H
ATOM    482  HB3 LEU A  45     -18.278  20.510 -30.171  1.00 71.63           H
ATOM    483  HG  LEU A  45     -15.783  21.660 -28.838  1.00 73.90           H
ATOM    484 HD11 LEU A  45     -15.966  19.214 -28.645  1.00  0.00           H
ATOM    485 HD12 LEU A  45     -14.688  19.645 -29.788  1.00  0.00           H
ATOM    486 HD13 LEU A  45     -16.266  19.090 -30.387  1.00  0.00           H
ATOM    487 HD21 LEU A  45     -16.128  22.745 -31.036  1.00  0.00           H
ATOM    488 HD22 LEU A  45     -14.782  21.602 -31.102  1.00  0.00           H
ATOM    489 HD23 LEU A  45     -16.358  21.152 -31.786  1.00  0.00           H
ATOM    490  N   SER A  46     -20.715  22.006 -30.301  1.00 60.88           N
ANISOU  490  N   SER A  46     5811  10309   7011   1093   -146   1455       N
ATOM    491  CA  SER A  46     -22.116  21.560 -30.264  1.00 57.93           C
ANISOU  491  CA  SER A  46     5425   9781   6805   1167   -200   1270       C
ATOM    492  C   SER A  46     -22.226  20.134 -29.700  1.00 56.18           C
ANISOU  492  C   SER A  46     5221   9608   6516   1261    -29   1018       C
ATOM    493  O   SER A  46     -21.401  19.279 -30.016  1.00 56.05           O
ANISOU  493  O   SER A  46     5229   9816   6253   1281     92   1014       O
ATOM    494  CB  SER A  46     -22.715  21.648 -31.678  1.00 59.47           C
ANISOU  494  CB  SER A  46     5598  10057   6940   1173   -373   1383       C
ATOM    495  OG  SER A  46     -23.991  21.046 -31.759  1.00 58.13           O
ANISOU  495  OG  SER A  46     5412   9787   6886   1254   -406   1186       O
ATOM    496  H   SER A  46     -20.196  21.821 -31.144  1.00 73.06           H
ATOM    497  HA  SER A  46     -22.686  22.229 -29.617  1.00 69.51           H
ATOM    498  HB2 SER A  46     -22.812  22.698 -31.959  1.00 71.36           H
ATOM    499  HB3 SER A  46     -22.050  21.154 -32.387  1.00 71.36           H
ATOM    500  HG  SER A  46     -24.610  21.676 -31.278  1.00 69.75           H
ATOM    501  N   GLN A  47     -23.364  19.809 -29.080  1.00 62.83           N
ANISOU  501  N   GLN A  47     6052  10236   7586   1322    -15    810       N
ATOM    502  CA  GLN A  47     -23.848  18.451 -28.789  1.00 65.47           C
ANISOU  502  CA  GLN A  47     6397  10589   7891   1414    141    564       C
ATOM    503  C   GLN A  47     -23.942  17.554 -30.035  1.00 65.44           C
ANISOU  503  C   GLN A  47     6398  10819   7648   1454    133    554       C
ATOM    504  O   GLN A  47     -24.005  16.328 -29.898  1.00 67.45           O
ANISOU  504  O   GLN A  47     6677  11194   7757   1510    291    417       O
ATOM    505  CB  GLN A  47     -25.219  18.612 -28.091  1.00 67.73           C
ANISOU  505  CB  GLN A  47     6656  10603   8476   1472    119    374       C
ATOM    506  CG  GLN A  47     -26.184  17.411 -28.132  1.00 69.07           C
ANISOU  506  CG  GLN A  47     6814  10783   8646   1567    197    145       C
ATOM    507  CD  GLN A  47     -26.938  17.236 -29.452  1.00 70.46           C
ANISOU  507  CD  GLN A  47     6956  11018   8796   1580     28    173       C
ATOM    508  OE1 GLN A  47     -27.382  18.167 -30.091  1.00 70.48           O
ANISOU  508  OE1 GLN A  47     6937  10986   8856   1531   -155    337       O
ATOM    509  NE2 GLN A  47     -27.253  16.028 -29.863  1.00 74.57           N
ANISOU  509  NE2 GLN A  47     7475  11626   9233   1648     88     10       N
ATOM    510  H   GLN A  47     -24.013  20.576 -28.901  1.00 75.40           H
ATOM    511  HA  GLN A  47     -23.150  17.963 -28.109  1.00 78.57           H
ATOM    512  HB2 GLN A  47     -25.020  18.854 -27.045  1.00 81.28           H
ATOM    513  HB3 GLN A  47     -25.745  19.464 -28.520  1.00 81.28           H
ATOM    514  HG2 GLN A  47     -25.637  16.500 -27.896  1.00 82.88           H
ATOM    515  HG3 GLN A  47     -26.938  17.568 -27.362  1.00 82.88           H
ATOM    516 HE21 GLN A  47     -26.709  15.250 -29.546  1.00 89.49           H
ATOM    517 HE22 GLN A  47     -27.706  16.035 -30.761  1.00 89.49           H
ATOM    518  N   SER A  48     -24.104  18.148 -31.216  1.00 61.34           N
ANISOU  518  N   SER A  48     5859  10367   7079   1430    -49    699       N
ATOM    519  CA  SER A  48     -24.167  17.446 -32.500  1.00 61.71           C
ANISOU  519  CA  SER A  48     5919  10634   6894   1471    -78    699       C
ATOM    520  C   SER A  48     -22.792  17.158 -33.120  1.00 63.41           C
ANISOU  520  C   SER A  48     6174  11130   6791   1444     -7    863       C
ATOM    521  O   SER A  48     -22.703  16.295 -33.992  1.00 63.79           O
ANISOU  521  O   SER A  48     6247  11377   6612   1491      7    846       O
ATOM    522  CB  SER A  48     -25.054  18.230 -33.474  1.00 65.99           C
ANISOU  522  CB  SER A  48     6429  11146   7497   1464   -305    798       C
ATOM    523  OG  SER A  48     -24.476  19.455 -33.880  1.00 67.50           O
ANISOU  523  OG  SER A  48     6617  11368   7663   1384   -422   1063       O
ATOM    524  H   SER A  48     -24.119  19.163 -31.230  1.00 73.60           H
ATOM    525  HA  SER A  48     -24.640  16.479 -32.339  1.00 74.05           H
ATOM    526  HB2 SER A  48     -25.216  17.622 -34.364  1.00 79.18           H
ATOM    527  HB3 SER A  48     -26.022  18.422 -33.005  1.00 79.18           H
ATOM    528  HG  SER A  48     -24.433  20.065 -33.116  1.00 81.00           H
ATOM    529  N   ASP A  49     -21.715  17.797 -32.649  1.00 65.97           N
ANISOU  529  N   ASP A  49     6503  11471   7092   1373     36   1020       N
ATOM    530  CA  ASP A  49     -20.359  17.589 -33.164  1.00 64.48           C
ANISOU  530  CA  ASP A  49     6342  11545   6614   1342     99   1201       C
ATOM    531  C   ASP A  49     -19.756  16.260 -32.652  1.00 65.15           C
ANISOU  531  C   ASP A  49     6463  11758   6534   1397    322   1051       C
ATOM    532  O   ASP A  49     -19.537  16.122 -31.443  1.00 64.48           O
ANISOU  532  O   ASP A  49     6380  11553   6568   1398    449    933       O
ATOM    533  CB  ASP A  49     -19.501  18.806 -32.794  1.00 64.78           C
ANISOU  533  CB  ASP A  49     6363  11545   6706   1242     64   1420       C
ATOM    534  CG  ASP A  49     -18.161  18.864 -33.521  1.00 64.53           C
ANISOU  534  CG  ASP A  49     6344  11781   6392   1203     94   1652       C
ATOM    535  OD1 ASP A  49     -17.575  17.821 -33.887  1.00 66.46           O
ANISOU  535  OD1 ASP A  49     6622  12240   6391   1260    209   1607       O
ATOM    536  OD2 ASP A  49     -17.630  19.985 -33.634  1.00 66.31           O
ANISOU  536  OD2 ASP A  49     6547  12002   6646   1117      4   1883       O
ATOM    537  H   ASP A  49     -21.817  18.414 -31.852  1.00 79.16           H
ATOM    538  HA  ASP A  49     -20.414  17.573 -34.250  1.00 77.38           H
ATOM    539  HB2 ASP A  49     -20.057  19.711 -33.047  1.00 77.74           H
ATOM    540  HB3 ASP A  49     -19.314  18.817 -31.720  1.00 77.74           H
ATOM    541  N   PRO A  50     -19.373  15.310 -33.534  1.00 73.78           N
ANISOU  541  N   PRO A  50     8810  12613   6609    206   -419    635       N
ATOM    542  CA  PRO A  50     -18.760  14.046 -33.120  1.00 72.02           C
ANISOU  542  CA  PRO A  50     8654  12299   6410    303   -361    405       C
ATOM    543  C   PRO A  50     -17.463  14.215 -32.316  1.00 67.27           C
ANISOU  543  C   PRO A  50     7971  11669   5917    428   -194    345       C
ATOM    544  O   PRO A  50     -17.209  13.396 -31.435  1.00 63.99           O
ANISOU  544  O   PRO A  50     7559  11124   5629    517   -169    220       O
ATOM    545  CB  PRO A  50     -18.515  13.253 -34.410  1.00 72.78           C
ANISOU  545  CB  PRO A  50     8905  12509   6239    259   -359    249       C
ATOM    546  CG  PRO A  50     -19.523  13.841 -35.394  1.00 74.22           C
ANISOU  546  CG  PRO A  50     9117  12802   6280    108   -480    407       C
ATOM    547  CD  PRO A  50     -19.597  15.305 -34.972  1.00 73.86           C
ANISOU  547  CD  PRO A  50     8920  12784   6360     91   -466    642       C
ATOM    548  HA  PRO A  50     -19.477  13.504 -32.503  1.00 86.42           H
ATOM    549  HB2 PRO A  50     -17.503  13.432 -34.779  1.00 87.34           H
ATOM    550  HB3 PRO A  50     -18.679  12.185 -34.260  1.00 87.34           H
ATOM    551  HG2 PRO A  50     -19.191  13.736 -36.427  1.00 89.06           H
ATOM    552  HG3 PRO A  50     -20.497  13.369 -35.252  1.00 89.06           H
ATOM    553  HD2 PRO A  50     -18.805  15.875 -35.460  1.00 88.64           H
ATOM    554  HD3 PRO A  50     -20.573  15.708 -35.236  1.00 88.64           H
ATOM    555  N   ARG A  51     -16.773  15.359 -32.456  1.00 71.31           N
ANISOU  555  N   ARG A  51     8411  12300   6383    428    -90    442       N
ATOM    556  CA  ARG A  51     -15.589  15.715 -31.656  1.00 73.84           C
ANISOU  556  CA  ARG A  51     8646  12601   6809    531     59    411       C
ATOM    557  C   ARG A  51     -15.912  15.883 -30.172  1.00 68.94           C
ANISOU  557  C   ARG A  51     7946  11796   6451    586     33    463       C
ATOM    558  O   ARG A  51     -15.127  15.499 -29.312  1.00 68.52           O
ANISOU  558  O   ARG A  51     7867  11658   6507    680    110    359       O
ATOM    559  CB  ARG A  51     -14.947  16.989 -32.206  1.00 73.30           C
ANISOU  559  CB  ARG A  51     8507  12683   6660    490    140    556       C
ATOM    560  CG  ARG A  51     -14.420  16.786 -33.635  1.00 79.18           C
ANISOU  560  CG  ARG A  51     9319  13634   7131    442    200    491       C
ATOM    561  CD  ARG A  51     -13.795  18.076 -34.167  1.00 80.71           C
ANISOU  561  CD  ARG A  51     9434  13982   7250    383    268    657       C
ATOM    562  NE  ARG A  51     -14.806  19.141 -34.327  1.00 81.13           N
ANISOU  562  NE  ARG A  51     9461  14029   7336    275    141    882       N
ATOM    563  CZ  ARG A  51     -14.588  20.396 -34.666  1.00 78.58           C
ANISOU  563  CZ  ARG A  51     9078  13810   6970    202    153   1064       C
ATOM    564  NH1 ARG A  51     -13.395  20.847 -34.933  1.00 78.98           N
ANISOU  564  NH1 ARG A  51     9083  13993   6932    215    288   1057       N
ATOM    565  NH2 ARG A  51     -15.568  21.239 -34.743  1.00 77.70           N
ANISOU  565  NH2 ARG A  51     8946  13669   6907    116     23   1263       N
ATOM    566  H   ARG A  51     -17.127  16.055 -33.112  1.00 85.57           H
ATOM    567  HA  ARG A  51     -14.848  14.923 -31.740  1.00 88.61           H
ATOM    568  HB2 ARG A  51     -15.678  17.796 -32.185  1.00 87.96           H
ATOM    569  HB3 ARG A  51     -14.111  17.268 -31.562  1.00 87.96           H
ATOM    570  HG2 ARG A  51     -13.666  15.998 -33.629  1.00 95.02           H
ATOM    571  HG3 ARG A  51     -15.228  16.485 -34.303  1.00 95.02           H
ATOM    572  HD2 ARG A  51     -13.017  18.395 -33.470  1.00 96.85           H
ATOM    573  HD3 ARG A  51     -13.335  17.860 -35.133  1.00 96.85           H
ATOM    574  HE  ARG A  51     -15.780  18.884 -34.142  1.00 97.36           H
ATOM    575 HH11 ARG A  51     -12.626  20.208 -34.861  1.00 94.77           H
ATOM    576 HH12 ARG A  51     -13.272  21.803 -35.197  1.00 94.77           H
ATOM    577 HH21 ARG A  51     -16.473  20.886 -34.409  1.00 93.24           H
ATOM    578 HH22 ARG A  51     -15.445  22.209 -34.925  1.00 93.24           H
ATOM    579  N   ALA A  52     -17.101  16.381 -29.843  1.00 63.13           N
ANISOU  579  N   ALA A  52     7168  11001   5819    530    -74    627       N
ATOM    580  CA  ALA A  52     -17.553  16.454 -28.458  1.00 58.86           C
ANISOU  580  CA  ALA A  52     6559  10295   5512    578    -99    670       C
ATOM    581  C   ALA A  52     -17.951  15.072 -27.901  1.00 59.07           C
ANISOU  581  C   ALA A  52     6642  10203   5597    606   -161    523       C
ATOM    582  O   ALA A  52     -17.731  14.786 -26.724  1.00 56.94           O
ANISOU  582  O   ALA A  52     6332   9806   5497    665   -141    492       O
ATOM    583  CB  ALA A  52     -18.714  17.445 -28.395  1.00 53.64           C
ANISOU  583  CB  ALA A  52     5836   9608   4936    521   -194    873       C
ATOM    584  H   ALA A  52     -17.770  16.564 -30.581  1.00 75.76           H
ATOM    585  HA  ALA A  52     -16.737  16.838 -27.844  1.00 70.64           H
ATOM    586  HB1 ALA A  52     -18.938  17.645 -27.352  1.00 64.37           H
ATOM    587  HB2 ALA A  52     -18.443  18.378 -28.881  1.00 64.37           H
ATOM    588  HB3 ALA A  52     -19.596  17.035 -28.889  1.00 64.37           H
ATOM    589  N   GLU A  53     -18.503  14.201 -28.752  1.00 66.03           N
ANISOU  589  N   GLU A  53     7628  11123   6337    554   -246    436       N
ATOM    590  CA  GLU A  53     -18.911  12.832 -28.397  1.00 68.38           C
ANISOU  590  CA  GLU A  53     7997  11303   6682    565   -331    304       C
ATOM    591  C   GLU A  53     -17.688  11.915 -28.143  1.00 73.34           C
ANISOU  591  C   GLU A  53     8663  11877   7327    669   -232    108       C
ATOM    592  O   GLU A  53     -17.728  11.134 -27.188  1.00 67.65           O
ANISOU  592  O   GLU A  53     7944  11014   6745    709   -267     36       O
ATOM    593  CB  GLU A  53     -19.851  12.292 -29.501  1.00 70.87           C
ANISOU  593  CB  GLU A  53     8430  11672   6825    469   -460    270       C
ATOM    594  CG  GLU A  53     -20.706  11.066 -29.187  1.00 73.43           C
ANISOU  594  CG  GLU A  53     8813  11869   7217    434   -605    214       C
ATOM    595  CD  GLU A  53     -22.011  11.473 -28.483  1.00 73.60           C
ANISOU  595  CD  GLU A  53     8728  11836   7400    381   -703    402       C
ATOM    596  OE1 GLU A  53     -22.005  11.935 -27.308  1.00 73.36           O
ANISOU  596  OE1 GLU A  53     8575  11820   7477    412   -633    539       O
ATOM    597  OE2 GLU A  53     -23.043  10.895 -28.884  1.00 73.77           O
ANISOU  597  OE2 GLU A  53     8788  11803   7438    308   -852    414       O
ATOM    598  H   GLU A  53     -18.602  14.490 -29.716  1.00 79.24           H
ATOM    599  HA  GLU A  53     -19.467  12.885 -27.463  1.00 82.06           H
ATOM    600  HB2 GLU A  53     -20.518  13.099 -29.821  1.00 85.04           H
ATOM    601  HB3 GLU A  53     -19.234  12.033 -30.363  1.00 85.04           H
ATOM    602  HG2 GLU A  53     -20.994  10.591 -30.116  1.00 88.11           H
ATOM    603  HG3 GLU A  53     -20.163  10.345 -28.608  1.00 88.11           H
ATOM    604  N   GLU A  54     -16.574  12.087 -28.879  1.00 80.98           N
ANISOU  604  N   GLU A  54     9652  12960   8156    713   -110     27       N
ATOM    605  CA  GLU A  54     -15.284  11.421 -28.600  1.00 84.70           C
ANISOU  605  CA  GLU A  54    10139  13393   8651    827     -4   -150       C
ATOM    606  C   GLU A  54     -14.512  12.030 -27.414  1.00 81.75           C
ANISOU  606  C   GLU A  54     9640  12958   8464    894     90    -86       C
ATOM    607  O   GLU A  54     -13.975  11.255 -26.625  1.00 85.08           O
ANISOU  607  O   GLU A  54    10056  13279   8993    978    126   -200       O
ATOM    608  CB  GLU A  54     -14.384  11.310 -29.854  1.00 84.92           C
ANISOU  608  CB  GLU A  54    10219  13586   8461    856    107   -255       C
ATOM    609  CG  GLU A  54     -13.854  12.650 -30.382  1.00 85.46           C
ANISOU  609  CG  GLU A  54    10199  13824   8447    818    203   -104       C
ATOM    610  CD  GLU A  54     -12.995  12.549 -31.655  1.00 89.26           C
ANISOU  610  CD  GLU A  54    10715  14485   8713    851    332   -212       C
ATOM    611  OE1 GLU A  54     -12.373  11.483 -31.871  1.00 90.12           O
ANISOU  611  OE1 GLU A  54    10883  14572   8788    949    393   -414       O
ATOM    612  OE2 GLU A  54     -12.973  13.549 -32.412  1.00 90.97           O
ANISOU  612  OE2 GLU A  54    10901  14870   8796    779    372    -92       O
ATOM    613  H   GLU A  54     -16.621  12.702 -29.689  1.00 97.17           H
ATOM    614  HA  GLU A  54     -15.505  10.395 -28.305  1.00101.64           H
ATOM    615  HB2 GLU A  54     -13.532  10.676 -29.600  1.00101.90           H
ATOM    616  HB3 GLU A  54     -14.946  10.811 -30.645  1.00101.90           H
ATOM    617  HG2 GLU A  54     -14.728  13.253 -30.590  1.00102.55           H
ATOM    618  HG3 GLU A  54     -13.272  13.145 -29.604  1.00102.55           H
ATOM    619  N   LEU A  55     -14.574  13.345 -27.150  1.00 62.96           N
ANISOU  619  N   LEU A  55     7165  10631   6125    855    123     97       N
ATOM    620  CA  LEU A  55     -13.973  13.927 -25.931  1.00 55.95           C
ANISOU  620  CA  LEU A  55     6175   9671   5414    902    194    167       C
ATOM    621  C   LEU A  55     -14.619  13.364 -24.648  1.00 56.17           C
ANISOU  621  C   LEU A  55     6195   9518   5632    911    112    158       C
ATOM    622  O   LEU A  55     -13.909  12.920 -23.744  1.00 55.87           O
ANISOU  622  O   LEU A  55     6121   9388   5721    971    159    106       O
ATOM    623  CB  LEU A  55     -14.057  15.469 -25.962  1.00 60.02           C
ANISOU  623  CB  LEU A  55     6616  10255   5936    848    217    367       C
ATOM    624  CG  LEU A  55     -13.079  16.143 -26.947  1.00 65.24           C
ANISOU  624  CG  LEU A  55     7253  11091   6445    838    322    405       C
ATOM    625  CD1 LEU A  55     -13.465  17.611 -27.153  1.00 66.93           C
ANISOU  625  CD1 LEU A  55     7415  11350   6666    766    300    615       C
ATOM    626  CD2 LEU A  55     -11.628  16.121 -26.465  1.00 65.13           C
ANISOU  626  CD2 LEU A  55     7182  11087   6478    918    451    339       C
ATOM    627  H   LEU A  55     -14.959  13.968 -27.853  1.00 75.55           H
ATOM    628  HA  LEU A  55     -12.921  13.642 -25.891  1.00 67.14           H
ATOM    629  HB2 LEU A  55     -15.079  15.750 -26.218  1.00 72.03           H
ATOM    630  HB3 LEU A  55     -13.851  15.855 -24.961  1.00 72.03           H
ATOM    631  HG  LEU A  55     -13.116  15.638 -27.907  1.00 78.29           H
ATOM    632 HD11 LEU A  55     -14.506  17.676 -27.459  1.00  0.00           H
ATOM    633 HD12 LEU A  55     -12.845  18.033 -27.943  1.00  0.00           H
ATOM    634 HD13 LEU A  55     -13.314  18.169 -26.228  1.00  0.00           H
ATOM    635 HD21 LEU A  55     -11.266  15.094 -26.409  1.00  0.00           H
ATOM    636 HD22 LEU A  55     -10.995  16.654 -27.173  1.00  0.00           H
ATOM    637 HD23 LEU A  55     -11.540  16.587 -25.484  1.00  0.00           H
ATOM    638  N   ILE A  56     -15.951  13.199 -24.632  1.00 56.11           N
ANISOU  638  N   ILE A  56     6212   9465   5642    844    -14    218       N
ATOM    639  CA  ILE A  56     -16.656  12.574 -23.497  1.00 55.90           C
ANISOU  639  CA  ILE A  56     6176   9287   5777    839    -97    212       C
ATOM    640  C   ILE A  56     -16.316  11.076 -23.364  1.00 56.08           C
ANISOU  640  C   ILE A  56     6279   9225   5803    880   -134     27       C
ATOM    641  O   ILE A  56     -16.193  10.580 -22.244  1.00 57.24           O
ANISOU  641  O   ILE A  56     6406   9247   6097    910   -145    -13       O
ATOM    642  CB  ILE A  56     -18.185  12.831 -23.564  1.00 58.80           C
ANISOU  642  CB  ILE A  56     6538   9651   6153    755   -222    331       C
ATOM    643  CG1 ILE A  56     -18.501  14.344 -23.501  1.00 62.12           C
ANISOU  643  CG1 ILE A  56     6874  10131   6597    734   -187    515       C
ATOM    644  CG2 ILE A  56     -18.939  12.138 -22.408  1.00 59.51           C
ANISOU  644  CG2 ILE A  56     6612   9605   6395    741   -307    328       C
ATOM    645  CD1 ILE A  56     -19.924  14.705 -23.945  1.00 63.69           C
ANISOU  645  CD1 ILE A  56     7055  10356   6790    662   -301    645       C
ATOM    646  H   ILE A  56     -16.483  13.556 -25.419  1.00 67.33           H
ATOM    647  HA  ILE A  56     -16.289  13.049 -22.591  1.00 67.08           H
ATOM    648  HB  ILE A  56     -18.553  12.430 -24.510  1.00 70.56           H
ATOM    649 HG12 ILE A  56     -18.340  14.715 -22.488  1.00 74.54           H
ATOM    650 HG13 ILE A  56     -17.819  14.884 -24.152  1.00 74.54           H
ATOM    651 HG21 ILE A  56     -20.012  12.293 -22.500  1.00 71.42           H
ATOM    652 HG22 ILE A  56     -18.746  11.069 -22.415  1.00 71.42           H
ATOM    653 HG23 ILE A  56     -18.595  12.538 -21.452  1.00 71.42           H
ATOM    654 HD11 ILE A  56     -19.994  15.788 -24.030  1.00 76.43           H
ATOM    655 HD12 ILE A  56     -20.136  14.263 -24.918  1.00 76.43           H
ATOM    656 HD13 ILE A  56     -20.656  14.361 -23.216  1.00 76.43           H
ATOM    657  N   GLU A  57     -16.150  10.345 -24.473  1.00 67.77           N
ANISOU  657  N   GLU A  57     7861  10768   7123    878   -159    -91       N
ATOM    658  CA  GLU A  57     -15.766   8.920 -24.460  1.00 71.64           C
ANISOU  658  CA  GLU A  57     8445  11164   7610    927   -198   -281       C
ATOM    659  C   GLU A  57     -14.316   8.680 -23.992  1.00 71.26           C
ANISOU  659  C   GLU A  57     8356  11087   7632   1042    -72   -378       C
ATOM    660  O   GLU A  57     -14.079   7.816 -23.147  1.00 75.38           O
ANISOU  660  O   GLU A  57     8896  11471   8274   1087   -109   -471       O
ATOM    661  CB  GLU A  57     -16.006   8.317 -25.859  1.00 73.57           C
ANISOU  661  CB  GLU A  57     8821  11487   7646    904   -241   -392       C
ATOM    662  CG  GLU A  57     -15.847   6.787 -25.956  1.00 76.46           C
ANISOU  662  CG  GLU A  57     9311  11743   7996    961   -293   -603       C
ATOM    663  CD  GLU A  57     -16.747   5.985 -25.003  1.00 79.79           C
ANISOU  663  CD  GLU A  57     9765  11993   8558    909   -455   -599       C
ATOM    664  OE1 GLU A  57     -17.835   6.514 -24.653  1.00 79.38           O
ANISOU  664  OE1 GLU A  57     9665  11940   8558    808   -547   -442       O
ATOM    665  OE2 GLU A  57     -16.522   4.767 -24.862  1.00 83.54           O
ANISOU  665  OE2 GLU A  57    10309  12337   9094    968   -493   -748       O
ATOM    666  H   GLU A  57     -16.242  10.805 -25.371  1.00 81.33           H
ATOM    667  HA  GLU A  57     -16.407   8.401 -23.748  1.00 85.96           H
ATOM    668  HB2 GLU A  57     -17.014   8.581 -26.181  1.00 88.29           H
ATOM    669  HB3 GLU A  57     -15.319   8.784 -26.566  1.00 88.29           H
ATOM    670  HG2 GLU A  57     -16.083   6.499 -26.982  1.00 91.75           H
ATOM    671  HG3 GLU A  57     -14.803   6.534 -25.780  1.00 91.75           H
ATOM    672  N   ASN A  58     -13.377   9.530 -24.418  1.00 62.85           N
ANISOU  672  N   ASN A  58     7230  10154   6498   1083     70   -347       N
ATOM    673  CA  ASN A  58     -11.966   9.491 -24.013  1.00 57.14           C
ANISOU  673  CA  ASN A  58     6441   9424   5844   1185    195   -409       C
ATOM    674  C   ASN A  58     -11.704  10.022 -22.577  1.00 59.44           C
ANISOU  674  C   ASN A  58     6622   9638   6322   1176    219   -279       C
ATOM    675  O   ASN A  58     -10.605   9.830 -22.049  1.00 59.15           O
ANISOU  675  O   ASN A  58     6512   9616   6344   1239    323   -283       O
ATOM    676  H   ASN A  58     -13.642  10.222 -25.113  1.00 75.42           H
ATOM    677  CB  ASN A  58     -11.133  10.197 -25.105  1.00  0.00           C
ATOM    678  CG  ASN A  58     -11.066   9.388 -26.396  1.00  0.00           C
ATOM    679  OD1 ASN A  58     -10.654   8.237 -26.411  1.00  0.00           O
ATOM    680  ND2 ASN A  58     -11.482   9.936 -27.514  1.00  0.00           N
ATOM    681  HA  ASN A  58     -11.653   8.447 -23.993  1.00  0.00           H
ATOM    682  HB2 ASN A  58     -11.538  11.188 -25.305  1.00  0.00           H
ATOM    683  HB3 ASN A  58     -10.107  10.329 -24.761  1.00  0.00           H
ATOM    684 HD21 ASN A  58     -11.386   9.408 -28.361  1.00  0.00           H
ATOM    685 HD22 ASN A  58     -11.900  10.851 -27.494  1.00  0.00           H
ATOM    686  N   GLU A  59     -12.741  10.481 -21.865  1.00 62.93           N
ANISOU  686  N   GLU A  59     7051  10004   6854   1098    127   -163       N
ATOM    687  CA  GLU A  59     -12.685  11.093 -20.522  1.00 64.43           C
ANISOU  687  CA  GLU A  59     7157  10112   7211   1082    142    -49       C
ATOM    688  C   GLU A  59     -11.886  12.427 -20.494  1.00 61.59           C
ANISOU  688  C   GLU A  59     6715   9846   6839   1097    267     50       C
ATOM    689  O   GLU A  59     -11.203  12.721 -19.505  1.00 59.64           O
ANISOU  689  O   GLU A  59     6412   9560   6691   1134    331     55       O
ATOM    690  CB  GLU A  59     -12.276  10.090 -19.401  1.00 63.33           C
ANISOU  690  CB  GLU A  59     7019   9823   7220   1122    109   -138       C
ATOM    691  CG  GLU A  59     -13.113   8.804 -19.250  1.00 60.53           C
ANISOU  691  CG  GLU A  59     6742   9358   6898   1084    -38   -205       C
ATOM    692  CD  GLU A  59     -12.708   7.993 -17.988  1.00 57.26           C
ANISOU  692  CD  GLU A  59     6315   8787   6656   1089    -91   -235       C
ATOM    693  OE1 GLU A  59     -11.808   7.090 -17.999  1.00 62.29           O
ANISOU  693  OE1 GLU A  59     6999   9349   7318   1149   -117   -373       O
ATOM    694  OE2 GLU A  59     -13.354   8.210 -16.937  1.00 55.31           O
ANISOU  694  OE2 GLU A  59     6013   8487   6515   1033   -107   -122       O
ATOM    695  H   GLU A  59     -13.616  10.560 -22.370  1.00 75.51           H
ATOM    696  HA  GLU A  59     -13.710  11.388 -20.299  1.00 77.32           H
ATOM    697  HB2 GLU A  59     -11.233   9.804 -19.530  1.00 75.99           H
ATOM    698  HB3 GLU A  59     -12.346  10.621 -18.449  1.00 75.99           H
ATOM    699  HG2 GLU A  59     -14.162   9.100 -19.152  1.00 72.64           H
ATOM    700  HG3 GLU A  59     -13.028   8.188 -20.143  1.00 72.64           H
ATOM    701  N   GLU A  60     -12.011  13.254 -21.543  1.00 63.78           N
ANISOU  701  N   GLU A  60     6989  10250   6994   1056    289    140       N
ATOM    702  CA  GLU A  60     -11.440  14.610 -21.699  1.00 58.07           C
ANISOU  702  CA  GLU A  60     6198   9616   6250   1043    382    264       C
ATOM    703  C   GLU A  60     -12.496  15.736 -21.548  1.00 52.69           C
ANISOU  703  C   GLU A  60     5503   8930   5585    973    331    427       C
ATOM    704  O   GLU A  60     -13.666  15.534 -21.880  1.00 49.06           O
ANISOU  704  O   GLU A  60     5084   8476   5081    933    244    441       O
ATOM    705  CB  GLU A  60     -10.772  14.740 -23.079  1.00 63.24           C
ANISOU  705  CB  GLU A  60     6855  10449   6726   1063    467    227       C
ATOM    706  CG  GLU A  60      -9.563  13.808 -23.234  1.00 63.80           C
ANISOU  706  CG  GLU A  60     6918  10540   6781   1155    545     72       C
ATOM    707  CD  GLU A  60      -8.720  14.181 -24.458  1.00 67.98           C
ANISOU  707  CD  GLU A  60     7436  11268   7125   1175    649     43       C
ATOM    708  OE1 GLU A  60      -8.595  13.319 -25.355  1.00 71.02           O
ANISOU  708  OE1 GLU A  60     7890  11706   7386   1218    657   -107       O
ATOM    709  OE2 GLU A  60      -8.111  15.278 -24.420  1.00 67.22           O
ANISOU  709  OE2 GLU A  60     7266  11276   6998   1141    721    173       O
ATOM    710  H   GLU A  60     -12.578  12.935 -22.326  1.00 76.54           H
ATOM    711  HA  GLU A  60     -10.671  14.760 -20.943  1.00 69.68           H
ATOM    712  HB2 GLU A  60     -11.500  14.521 -23.862  1.00 75.89           H
ATOM    713  HB3 GLU A  60     -10.442  15.773 -23.207  1.00 75.89           H
ATOM    714  HG2 GLU A  60      -8.940  13.895 -22.341  1.00 76.55           H
ATOM    715  HG3 GLU A  60      -9.912  12.776 -23.306  1.00 76.55           H
ATOM    716  N   PRO A  61     -12.141  16.946 -21.059  1.00 48.58           N
ANISOU  716  N   PRO A  61     4929   8398   5131    956    379    554       N
ATOM    717  CA  PRO A  61     -13.096  18.043 -20.893  1.00 42.36           C
ANISOU  717  CA  PRO A  61     4132   7583   4379    907    331    702       C
ATOM    718  C   PRO A  61     -13.565  18.647 -22.224  1.00 43.86           C
ANISOU  718  C   PRO A  61     4337   7905   4422    864    307    773       C
ATOM    719  O   PRO A  61     -12.761  18.988 -23.092  1.00 43.99           O
ANISOU  719  O   PRO A  61     4359   8057   4300    859    359    750       O
ATOM    720  CB  PRO A  61     -12.380  19.075 -20.025  1.00 43.88           C
ANISOU  720  CB  PRO A  61     4283   7732   4657    902    394    802       C
ATOM    721  CG  PRO A  61     -10.907  18.871 -20.376  1.00 46.62           C
ANISOU  721  CG  PRO A  61     4603   8162   4947    927    480    747       C
ATOM    722  CD  PRO A  61     -10.830  17.356 -20.575  1.00 45.34           C
ANISOU  722  CD  PRO A  61     4466   7997   4765    979    472    575       C
ATOM    723  HA  PRO A  61     -13.970  17.681 -20.354  1.00 50.83           H
ATOM    724  HB2 PRO A  61     -12.712  20.094 -20.224  1.00 52.65           H
ATOM    725  HB3 PRO A  61     -12.547  18.813 -18.983  1.00 52.65           H
ATOM    726  HG2 PRO A  61     -10.672  19.382 -21.311  1.00 55.94           H
ATOM    727  HG3 PRO A  61     -10.247  19.216 -19.578  1.00 55.94           H
ATOM    728  HD2 PRO A  61     -10.038  17.109 -21.283  1.00 54.41           H
ATOM    729  HD3 PRO A  61     -10.646  16.876 -19.613  1.00 54.41           H
ATOM    730  N   VAL A  62     -14.841  19.033 -22.259  1.00 48.00           N
ANISOU  730  N   VAL A  62     4864   8396   4977    831    226    867       N
ATOM    731  CA  VAL A  62     -15.486  19.734 -23.381  1.00 44.77           C
ANISOU  731  CA  VAL A  62     4463   8096   4451    779    181    966       C
ATOM    732  C   VAL A  62     -16.577  20.673 -22.860  1.00 41.73           C
ANISOU  732  C   VAL A  62     4048   7631   4177    767    118   1107       C
ATOM    733  O   VAL A  62     -17.263  20.342 -21.891  1.00 42.00           O
ANISOU  733  O   VAL A  62     4068   7552   4340    793     90   1090       O
ATOM    734  CB  VAL A  62     -16.015  18.720 -24.421  1.00 46.65           C
ANISOU  734  CB  VAL A  62     4757   8414   4553    754    119    871       C
ATOM    735  CG1 VAL A  62     -17.106  17.775 -23.897  1.00 44.70           C
ANISOU  735  CG1 VAL A  62     4527   8062   4397    758     29    818       C
ATOM    736  CG2 VAL A  62     -16.561  19.416 -25.672  1.00 44.83           C
ANISOU  736  CG2 VAL A  62     4538   8307   4188    684     67    984       C
ATOM    737  H   VAL A  62     -15.422  18.805 -21.465  1.00 57.60           H
ATOM    738  HA  VAL A  62     -14.737  20.347 -23.884  1.00 53.72           H
ATOM    739  HB  VAL A  62     -15.176  18.101 -24.734  1.00 55.98           H
ATOM    740 HG11 VAL A  62     -17.421  17.109 -24.701  1.00 53.65           H
ATOM    741 HG12 VAL A  62     -16.706  17.163 -23.090  1.00 53.65           H
ATOM    742 HG13 VAL A  62     -17.971  18.335 -23.543  1.00 53.65           H
ATOM    743 HG21 VAL A  62     -16.792  18.665 -26.424  1.00 53.79           H
ATOM    744 HG22 VAL A  62     -17.470  19.973 -25.444  1.00 53.79           H
ATOM    745 HG23 VAL A  62     -15.807  20.090 -26.077  1.00 53.79           H
ATOM    746  N   VAL A  63     -16.721  21.858 -23.461  1.00 41.97           N
ANISOU  746  N   VAL A  63     4065   7722   4159    730     99   1248       N
ATOM    747  CA  VAL A  63     -17.865  22.753 -23.226  1.00 48.67           C
ANISOU  747  CA  VAL A  63     4883   8504   5105    730     34   1388       C
ATOM    748  C   VAL A  63     -18.883  22.557 -24.342  1.00 44.90           C
ANISOU  748  C   VAL A  63     4410   8116   4536    678    -67   1442       C
ATOM    749  O   VAL A  63     -18.590  22.827 -25.505  1.00 44.05           O
ANISOU  749  O   VAL A  63     4323   8132   4284    621    -83   1489       O
ATOM    750  CB  VAL A  63     -17.439  24.228 -23.113  1.00 48.32           C
ANISOU  750  CB  VAL A  63     4827   8438   5096    725     65   1525       C
ATOM    751  CG1 VAL A  63     -18.644  25.164 -22.942  1.00 44.24           C
ANISOU  751  CG1 VAL A  63     4280   7857   4672    736     -9   1670       C
ATOM    752  CG2 VAL A  63     -16.537  24.439 -21.895  1.00 45.66           C
ANISOU  752  CG2 VAL A  63     4491   7996   4860    764    148   1484       C
ATOM    753  H   VAL A  63     -16.147  22.053 -24.278  1.00 50.36           H
ATOM    754  HA  VAL A  63     -18.350  22.488 -22.288  1.00 58.40           H
ATOM    755  HB  VAL A  63     -16.887  24.519 -24.004  1.00 57.99           H
ATOM    756 HG11 VAL A  63     -18.309  26.184 -22.758  1.00 53.09           H
ATOM    757 HG12 VAL A  63     -19.261  25.172 -23.840  1.00 53.09           H
ATOM    758 HG13 VAL A  63     -19.250  24.836 -22.098  1.00 53.09           H
ATOM    759 HG21 VAL A  63     -16.276  25.492 -21.812  1.00 54.79           H
ATOM    760 HG22 VAL A  63     -17.064  24.132 -20.993  1.00 54.79           H
ATOM    761 HG23 VAL A  63     -15.626  23.853 -22.001  1.00 54.79           H
ATOM    762  N   LEU A  64     -20.072  22.085 -23.982  1.00 47.39           N
ANISOU  762  N   LEU A  64     4701   8376   4927    688   -140   1444       N
ATOM    763  CA  LEU A  64     -21.213  21.946 -24.880  1.00 48.58           C
ANISOU  763  CA  LEU A  64     4845   8600   5013    632   -254   1518       C
ATOM    764  C   LEU A  64     -22.096  23.196 -24.799  1.00 46.45           C
ANISOU  764  C   LEU A  64     4511   8294   4843    645   -301   1703       C
ATOM    765  O   LEU A  64     -22.561  23.543 -23.713  1.00 49.45           O
ANISOU  765  O   LEU A  64     4843   8562   5385    712   -278   1737       O
ATOM    766  CB  LEU A  64     -22.011  20.698 -24.495  1.00 48.97           C
ANISOU  766  CB  LEU A  64     4895   8618   5093    625   -320   1435       C
ATOM    767  CG  LEU A  64     -21.228  19.378 -24.505  1.00 49.57           C
ANISOU  767  CG  LEU A  64     5043   8702   5088    623   -286   1244       C
ATOM    768  CD1 LEU A  64     -22.086  18.322 -23.820  1.00 51.81           C
ANISOU  768  CD1 LEU A  64     5324   8911   5449    623   -349   1174       C
ATOM    769  CD2 LEU A  64     -20.939  18.898 -25.922  1.00 52.15           C
ANISOU  769  CD2 LEU A  64     5444   9161   5209    558   -316   1198       C
ATOM    770  H   LEU A  64     -20.233  21.904 -22.997  1.00 56.86           H
ATOM    771  HA  LEU A  64     -20.861  21.825 -25.900  1.00 58.29           H
ATOM    772  HB2 LEU A  64     -22.407  20.857 -23.492  1.00 58.76           H
ATOM    773  HB3 LEU A  64     -22.848  20.611 -25.188  1.00 58.76           H
ATOM    774  HG  LEU A  64     -20.293  19.469 -23.952  1.00 59.48           H
ATOM    775 HD11 LEU A  64     -22.252  18.604 -22.780  1.00  0.00           H
ATOM    776 HD12 LEU A  64     -21.577  17.362 -23.845  1.00  0.00           H
ATOM    777 HD13 LEU A  64     -23.042  18.248 -24.337  1.00  0.00           H
ATOM    778 HD21 LEU A  64     -20.223  19.566 -26.401  1.00  0.00           H
ATOM    779 HD22 LEU A  64     -21.853  18.883 -26.511  1.00  0.00           H
ATOM    780 HD23 LEU A  64     -20.521  17.894 -25.882  1.00  0.00           H
ATOM    781  N   THR A  65     -22.365  23.840 -25.932  1.00 48.20           N
ANISOU  781  N   THR A  65     4736   8610   4967    582   -368   1822       N
ATOM    782  CA  THR A  65     -23.002  25.173 -25.982  1.00 49.45           C
ANISOU  782  CA  THR A  65     4839   8731   5217    597   -417   2007       C
ATOM    783  C   THR A  65     -24.524  25.161 -26.212  1.00 50.61           C
ANISOU  783  C   THR A  65     4921   8887   5420    583   -537   2116       C
ATOM    784  O   THR A  65     -25.167  26.192 -26.041  1.00 55.00           O
ANISOU  784  O   THR A  65     5417   9394   6087    619   -579   2269       O
ATOM    785  CB  THR A  65     -22.307  26.021 -27.058  1.00 54.05           C
ANISOU  785  CB  THR A  65     5455   9407   5673    527   -430   2105       C
ATOM    786  OG1 THR A  65     -22.323  25.350 -28.299  1.00 54.52           O
ANISOU  786  OG1 THR A  65     5559   9617   5540    428   -489   2077       O
ATOM    787  CG2 THR A  65     -20.837  26.284 -26.722  1.00 51.99           C
ANISOU  787  CG2 THR A  65     5234   9133   5388    545   -314   2042       C
ATOM    788  H   THR A  65     -21.925  23.515 -26.789  1.00 57.84           H
ATOM    789  HA  THR A  65     -22.853  25.680 -25.027  1.00 59.34           H
ATOM    790  HB  THR A  65     -22.824  26.976 -27.156  1.00 64.86           H
ATOM    791  HG1 THR A  65     -22.219  25.999 -28.995  1.00 65.43           H
ATOM    792 HG21 THR A  65     -20.402  26.948 -27.466  1.00 62.39           H
ATOM    793 HG22 THR A  65     -20.773  26.746 -25.737  1.00 62.39           H
ATOM    794 HG23 THR A  65     -20.276  25.348 -26.704  1.00 62.39           H
ATOM    795  N   ASP A  66     -25.121  24.017 -26.557  1.00 50.50           N
ANISOU  795  N   ASP A  66     4918   8932   5338    532   -601   2050       N
ATOM    796  CA  ASP A  66     -26.481  23.930 -27.129  1.00 53.01           C
ANISOU  796  CA  ASP A  66     5173   9287   5682    490   -735   2177       C
ATOM    797  C   ASP A  66     -27.299  22.733 -26.587  1.00 55.74           C
ANISOU  797  C   ASP A  66     5506   9623   6050    478   -776   2087       C
ATOM    798  O   ASP A  66     -28.361  22.389 -27.122  1.00 54.99           O
ANISOU  798  O   ASP A  66     5424   9606   5864    386   -893   2112       O
ATOM    799  CB  ASP A  66     -26.351  23.899 -28.661  1.00 54.72           C
ANISOU  799  CB  ASP A  66     5435   9636   5722    372   -833   2261       C
ATOM    800  CG  ASP A  66     -25.518  22.731 -29.192  1.00 56.59           C
ANISOU  800  CG  ASP A  66     5785   9966   5750    294   -818   2098       C
ATOM    801  OD1 ASP A  66     -24.945  21.957 -28.387  1.00 51.91           O
ANISOU  801  OD1 ASP A  66     5234   9326   5162    343   -723   1925       O
ATOM    802  OD2 ASP A  66     -25.326  22.669 -30.424  1.00 59.69           O
ANISOU  802  OD2 ASP A  66     6229  10477   5973    185   -900   2143       O
ATOM    803  H   ASP A  66     -24.504  23.263 -26.841  1.00 60.60           H
ATOM    804  HA  ASP A  66     -27.040  24.827 -26.866  1.00 63.62           H
ATOM    805  HB2 ASP A  66     -27.341  23.866 -29.117  1.00 65.67           H
ATOM    806  HB3 ASP A  66     -25.874  24.827 -28.980  1.00 65.67           H
ATOM    807  N   THR A  67     -26.908  22.150 -25.452  1.00 54.81           N
ANISOU  807  N   THR A  67     5365   9407   6051    557   -692   1991       N
ATOM    808  CA  THR A  67     -27.568  20.968 -24.849  1.00 52.83           C
ANISOU  808  CA  THR A  67     5097   9142   5836    539   -739   1922       C
ATOM    809  C   THR A  67     -29.024  21.204 -24.426  1.00 52.19           C
ANISOU  809  C   THR A  67     4883   9048   5897    563   -807   2068       C
ATOM    810  O   THR A  67     -29.738  20.236 -24.144  1.00 55.68           O
ANISOU  810  O   THR A  67     5297   9519   6338    507   -895   2068       O
ATOM    811  CB  THR A  67     -26.835  20.467 -23.594  1.00 52.16           C
ANISOU  811  CB  THR A  67     5042   8966   5812    599   -629   1762       C
ATOM    812  OG1 THR A  67     -26.814  21.468 -22.598  1.00 49.27           O
ANISOU  812  OG1 THR A  67     4616   8510   5595    699   -532   1808       O
ATOM    813  CG2 THR A  67     -25.398  20.036 -23.844  1.00 50.38           C
ANISOU  813  CG2 THR A  67     4932   8759   5452    581   -565   1611       C
ATOM    814  H   THR A  67     -26.063  22.515 -25.034  1.00 65.77           H
ATOM    815  HA  THR A  67     -27.578  20.166 -25.587  1.00 63.40           H
ATOM    816  HB  THR A  67     -27.374  19.609 -23.195  1.00 62.60           H
ATOM    817  HG1 THR A  67     -26.009  21.986 -22.711  1.00 59.13           H
ATOM    818 HG21 THR A  67     -24.969  19.642 -22.922  1.00 60.46           H
ATOM    819 HG22 THR A  67     -25.383  19.252 -24.600  1.00 60.46           H
ATOM    820 HG23 THR A  67     -24.816  20.887 -24.185  1.00 60.46           H
ATOM    821  N   ASN A  68     -29.414  22.461 -24.194  1.00 54.15           N
ANISOU  821  N   ASN A  68     5048   9255   6271    646   -770   2195       N
ATOM    822  CA  ASN A  68     -30.631  22.863 -23.477  1.00 53.40           C
ANISOU  822  CA  ASN A  68     4811   9143   6336    703   -803   2324       C
ATOM    823  C   ASN A  68     -30.773  22.230 -22.071  1.00 51.34           C
ANISOU  823  C   ASN A  68     4513   8832   6162    740   -745   2228       C
ATOM    824  O   ASN A  68     -31.875  22.223 -21.517  1.00 56.30           O
ANISOU  824  O   ASN A  68     5026   9486   6879    746   -794   2309       O
ATOM    825  CB  ASN A  68     -31.862  22.687 -24.395  1.00 53.85           C
ANISOU  825  CB  ASN A  68     4804   9303   6355    612   -965   2468       C
ATOM    826  CG  ASN A  68     -31.777  23.596 -25.608  1.00 56.57           C
ANISOU  826  CG  ASN A  68     5166   9697   6633    573  -1035   2599       C
ATOM    827  OD1 ASN A  68     -31.685  24.801 -25.476  1.00 56.04           O
ANISOU  827  OD1 ASN A  68     5058   9575   6659    658   -991   2689       O
ATOM    828  ND2 ASN A  68     -31.718  23.072 -26.809  1.00 56.39           N
ANISOU  828  ND2 ASN A  68     5212   9774   6441    437  -1150   2609       N
ATOM    829  H   ASN A  68     -28.786  23.193 -24.495  1.00 64.98           H
ATOM    830  HA  ASN A  68     -30.537  23.935 -23.291  1.00 64.08           H
ATOM    831  HB2 ASN A  68     -31.966  21.648 -24.704  1.00 64.63           H
ATOM    832  HB3 ASN A  68     -32.767  22.966 -23.855  1.00 64.63           H
ATOM    833 HD21 ASN A  68     -31.481  23.723 -27.538  1.00 67.67           H
ATOM    834 HD22 ASN A  68     -31.602  22.086 -26.935  1.00 67.67           H
ATOM    835  N   LEU A  69     -29.696  21.698 -21.471  1.00 46.70           N
ANISOU  835  N   LEU A  69     4015   8179   5549    759   -644   2064       N
ATOM    836  CA  LEU A  69     -29.777  20.779 -20.323  1.00 51.58           C
ANISOU  836  CA  LEU A  69     4617   8755   6225    768   -605   1966       C
ATOM    837  C   LEU A  69     -30.548  21.353 -19.134  1.00 52.24           C
ANISOU  837  C   LEU A  69     4577   8796   6476    865   -541   2042       C
ATOM    838  O   LEU A  69     -31.405  20.667 -18.591  1.00 57.12           O
ANISOU  838  O   LEU A  69     5108   9446   7151    847   -577   2070       O
ATOM    839  CB  LEU A  69     -28.367  20.339 -19.890  1.00 47.47           C
ANISOU  839  CB  LEU A  69     4211   8166   5659    776   -509   1793       C
ATOM    840  CG  LEU A  69     -28.348  19.403 -18.662  1.00 48.50           C
ANISOU  840  CG  LEU A  69     4341   8243   5842    771   -477   1686       C
ATOM    841  CD1 LEU A  69     -29.072  18.083 -18.932  1.00 50.39           C
ANISOU  841  CD1 LEU A  69     4574   8541   6031    671   -606   1674       C
ATOM    842  CD2 LEU A  69     -26.902  19.104 -18.274  1.00 49.09           C
ANISOU  842  CD2 LEU A  69     4523   8250   5879    781   -391   1534       C
ATOM    843  H   LEU A  69     -28.811  21.737 -21.970  1.00 56.04           H
ATOM    844  HA  LEU A  69     -30.319  19.898 -20.646  1.00 61.89           H
ATOM    845  HB2 LEU A  69     -27.880  19.833 -20.723  1.00 56.96           H
ATOM    846  HB3 LEU A  69     -27.790  21.233 -19.647  1.00 56.96           H
ATOM    847  HG  LEU A  69     -28.820  19.892 -17.812  1.00 58.19           H
ATOM    848 HD11 LEU A  69     -30.139  18.258 -19.066  1.00  0.00           H
ATOM    849 HD12 LEU A  69     -28.953  17.418 -18.077  1.00  0.00           H
ATOM    850 HD13 LEU A  69     -28.668  17.615 -19.826  1.00  0.00           H
ATOM    851 HD21 LEU A  69     -26.371  20.038 -18.101  1.00  0.00           H
ATOM    852 HD22 LEU A  69     -26.886  18.526 -17.351  1.00  0.00           H
ATOM    853 HD23 LEU A  69     -26.403  18.553 -19.068  1.00  0.00           H
ATOM    854  N   VAL A  70     -30.321  22.626 -18.820  1.00 49.32           N
ANISOU  854  N   VAL A  70     4202   8356   6183    968   -447   2077       N
ATOM    855  CA  VAL A  70     -31.005  23.377 -17.756  1.00 49.43           C
ANISOU  855  CA  VAL A  70     4112   8320   6349   1079   -370   2135       C
ATOM    856  C   VAL A  70     -31.788  24.571 -18.324  1.00 51.51           C
ANISOU  856  C   VAL A  70     4297   8589   6685   1151   -402   2299       C
ATOM    857  O   VAL A  70     -31.960  25.578 -17.646  1.00 53.47           O
ANISOU  857  O   VAL A  70     4518   8754   7043   1271   -316   2331       O
ATOM    858  CB  VAL A  70     -30.028  23.752 -16.619  1.00 48.96           C
ANISOU  858  CB  VAL A  70     4126   8143   6331   1148   -228   2020       C
ATOM    859  CG1 VAL A  70     -29.464  22.500 -15.938  1.00 49.48           C
ANISOU  859  CG1 VAL A  70     4253   8203   6346   1077   -208   1875       C
ATOM    860  CG2 VAL A  70     -28.861  24.627 -17.097  1.00 47.16           C
ANISOU  860  CG2 VAL A  70     4005   7855   6060   1166   -193   2009       C
ATOM    861  H   VAL A  70     -29.614  23.111 -19.353  1.00 59.19           H
ATOM    862  HA  VAL A  70     -31.759  22.729 -17.310  1.00 59.32           H
ATOM    863  HB  VAL A  70     -30.575  24.296 -15.852  1.00 58.75           H
ATOM    864 HG11 VAL A  70     -28.894  22.790 -15.056  1.00 59.38           H
ATOM    865 HG12 VAL A  70     -30.288  21.859 -15.626  1.00 59.38           H
ATOM    866 HG13 VAL A  70     -28.816  21.952 -16.620  1.00 59.38           H
ATOM    867 HG21 VAL A  70     -28.173  24.802 -16.272  1.00 56.60           H
ATOM    868 HG22 VAL A  70     -28.316  24.144 -17.906  1.00 56.60           H
ATOM    869 HG23 VAL A  70     -29.235  25.591 -17.445  1.00 56.60           H
ATOM    870  N   TYR A  71     -32.287  24.473 -19.563  1.00 55.20           N
ANISOU  870  N   TYR A  71     4733   9148   7090   1075   -534   2404       N
ATOM    871  CA  TYR A  71     -32.971  25.569 -20.274  1.00 59.73           C
ANISOU  871  CA  TYR A  71     5233   9732   7729   1126   -592   2577       C
ATOM    872  C   TYR A  71     -34.088  26.296 -19.470  1.00 62.73           C
ANISOU  872  C   TYR A  71     5464  10078   8291   1265   -540   2672       C
ATOM    873  O   TYR A  71     -34.003  27.519 -19.344  1.00 63.73           O
ANISOU  873  O   TYR A  71     5582  10124   8509   1373   -502   2741       O
ATOM    874  CB  TYR A  71     -33.450  25.059 -21.647  1.00 65.38           C
ANISOU  874  CB  TYR A  71     5922  10570   8348    999   -758   2682       C
ATOM    875  CG  TYR A  71     -34.335  26.030 -22.404  1.00 68.42           C
ANISOU  875  CG  TYR A  71     6207  10981   8811   1035   -846   2886       C
ATOM    876  CD1 TYR A  71     -33.758  27.140 -23.051  1.00 70.66           C
ANISOU  876  CD1 TYR A  71     6552  11215   9082   1057   -852   2945       C
ATOM    877  CD2 TYR A  71     -35.732  25.845 -22.434  1.00 71.74           C
ANISOU  877  CD2 TYR A  71     6463  11476   9320   1038   -932   3034       C
ATOM    878  CE1 TYR A  71     -34.578  28.084 -23.697  1.00 72.87           C
ANISOU  878  CE1 TYR A  71     6741  11507   9440   1087   -947   3141       C
ATOM    879  CE2 TYR A  71     -36.555  26.784 -23.088  1.00 73.83           C
ANISOU  879  CE2 TYR A  71     6624  11759   9667   1073  -1021   3232       C
ATOM    880  CZ  TYR A  71     -35.976  27.912 -23.713  1.00 76.33           C
ANISOU  880  CZ  TYR A  71     7013  12014   9975   1099  -1031   3282       C
ATOM    881  OH  TYR A  71     -36.762  28.831 -24.334  1.00 87.07           O
ANISOU  881  OH  TYR A  71     8303  13358  11422   1113  -1113   3451       O
ATOM    882  H   TYR A  71     -32.135  23.609 -20.074  1.00 66.23           H
ATOM    883  HA  TYR A  71     -32.221  26.332 -20.482  1.00 71.68           H
ATOM    884  HB2 TYR A  71     -32.572  24.856 -22.261  1.00 78.45           H
ATOM    885  HB3 TYR A  71     -33.983  24.115 -21.533  1.00 78.45           H
ATOM    886  HD1 TYR A  71     -32.684  27.272 -23.053  1.00 84.80           H
ATOM    887  HD2 TYR A  71     -36.174  24.983 -21.954  1.00 86.09           H
ATOM    888  HE1 TYR A  71     -34.144  28.945 -24.184  1.00 87.45           H
ATOM    889  HE2 TYR A  71     -37.624  26.647 -23.105  1.00 88.59           H
ATOM    890  HH  TYR A  71     -37.678  28.561 -24.372  1.00104.49           H
ATOM    891  N   PRO A  72     -34.978  25.612 -18.713  1.00 61.45           N
ANISOU  891  N   PRO A  72     5184   9974   8190   1272   -534   2683       N
ATOM    892  CA  PRO A  72     -35.981  26.270 -17.856  1.00 59.96           C
ANISOU  892  CA  PRO A  72     4844   9765   8173   1421   -463   2768       C
ATOM    893  C   PRO A  72     -35.410  26.986 -16.622  1.00 57.50           C
ANISOU  893  C   PRO A  72     4596   9319   7932   1553   -295   2659       C
ATOM    894  O   PRO A  72     -36.133  27.743 -15.969  1.00 58.55           O
ANISOU  894  O   PRO A  72     4641   9403   8203   1703   -227   2723       O
ATOM    895  CB  PRO A  72     -36.930  25.165 -17.386  1.00 60.65           C
ANISOU  895  CB  PRO A  72     4806   9965   8274   1365   -492   2787       C
ATOM    896  CG  PRO A  72     -36.637  23.979 -18.292  1.00 59.00           C
ANISOU  896  CG  PRO A  72     4676   9831   7910   1181   -624   2754       C
ATOM    897  CD  PRO A  72     -35.182  24.176 -18.686  1.00 58.52           C
ANISOU  897  CD  PRO A  72     4809   9690   7735   1146   -595   2624       C
ATOM    898  HA  PRO A  72     -36.535  26.994 -18.454  1.00 71.95           H
ATOM    899  HB2 PRO A  72     -36.688  24.884 -16.362  1.00 72.78           H
ATOM    900  HB3 PRO A  72     -37.975  25.473 -17.453  1.00 72.78           H
ATOM    901  HG2 PRO A  72     -36.763  23.050 -17.747  1.00 70.80           H
ATOM    902  HG3 PRO A  72     -37.273  24.011 -19.177  1.00 70.80           H
ATOM    903  HD2 PRO A  72     -34.533  23.747 -17.924  1.00 70.22           H
ATOM    904  HD3 PRO A  72     -34.994  23.706 -19.650  1.00 70.22           H
ATOM    905  N   ALA A  73     -34.170  26.679 -16.237  1.00 56.18           N
ANISOU  905  N   ALA A  73     4581   9090   7677   1503   -228   2496       N
ATOM    906  CA  ALA A  73     -33.474  27.335 -15.137  1.00 52.34           C
ANISOU  906  CA  ALA A  73     4171   8474   7242   1605    -79   2390       C
ATOM    907  C   ALA A  73     -32.776  28.639 -15.556  1.00 54.62           C
ANISOU  907  C   ALA A  73     4560   8643   7549   1670    -63   2414       C
ATOM    908  O   ALA A  73     -32.481  29.451 -14.690  1.00 58.21           O
ANISOU  908  O   ALA A  73     5085   8975   8058   1763     49   2346       O
ATOM    909  CB  ALA A  73     -32.480  26.355 -14.506  1.00 50.35           C
ANISOU  909  CB  ALA A  73     4033   8203   6894   1514    -28   2223       C
ATOM    910  H   ALA A  73     -33.613  26.080 -16.834  1.00 67.42           H
ATOM    911  HA  ALA A  73     -34.203  27.597 -14.373  1.00 62.81           H
ATOM    912  HB1 ALA A  73     -32.048  26.809 -13.618  1.00 60.42           H
ATOM    913  HB2 ALA A  73     -32.987  25.441 -14.208  1.00 60.42           H
ATOM    914  HB3 ALA A  73     -31.673  26.134 -15.200  1.00 60.42           H
ATOM    915  N   LEU A  74     -32.589  28.923 -16.852  1.00 49.59           N
ANISOU  915  N   LEU A  74     3941   8038   6863   1614   -177   2512       N
ATOM    916  CA  LEU A  74     -31.886  30.137 -17.319  1.00 53.57           C
ANISOU  916  CA  LEU A  74     4546   8435   7374   1652   -179   2546       C
ATOM    917  C   LEU A  74     -32.587  31.468 -16.949  1.00 56.09           C
ANISOU  917  C   LEU A  74     4804   8650   7857   1821   -143   2637       C
ATOM    918  O   LEU A  74     -31.934  32.504 -16.890  1.00 58.08           O
ANISOU  918  O   LEU A  74     5154   8778   8134   1868   -132   2653       O
ATOM    919  CB  LEU A  74     -31.630  30.035 -18.836  1.00 54.26           C
ANISOU  919  CB  LEU A  74     4660   8603   7355   1535   -317   2640       C
ATOM    920  CG  LEU A  74     -30.786  28.823 -19.284  1.00 55.28           C
ANISOU  920  CG  LEU A  74     4875   8820   7309   1381   -345   2534       C
ATOM    921  CD1 LEU A  74     -30.610  28.841 -20.802  1.00 56.50           C
ANISOU  921  CD1 LEU A  74     5053   9065   7350   1271   -474   2630       C
ATOM    922  CD2 LEU A  74     -29.397  28.796 -18.648  1.00 45.67           C
ANISOU  922  CD2 LEU A  74     3797   7519   6037   1370   -241   2386       C
ATOM    923  H   LEU A  74     -32.834  28.221 -17.542  1.00 59.51           H
ATOM    924  HA  LEU A  74     -30.918  30.187 -16.823  1.00 64.29           H
ATOM    925  HB2 LEU A  74     -32.591  29.999 -19.351  1.00 65.12           H
ATOM    926  HB3 LEU A  74     -31.117  30.944 -19.155  1.00 65.12           H
ATOM    927  HG  LEU A  74     -31.299  27.902 -19.014  1.00 66.34           H
ATOM    928 HD11 LEU A  74     -31.588  28.820 -21.284  1.00  0.00           H
ATOM    929 HD12 LEU A  74     -30.037  27.972 -21.124  1.00  0.00           H
ATOM    930 HD13 LEU A  74     -30.082  29.746 -21.105  1.00  0.00           H
ATOM    931 HD21 LEU A  74     -29.490  28.641 -17.576  1.00  0.00           H
ATOM    932 HD22 LEU A  74     -28.881  29.738 -18.837  1.00  0.00           H
ATOM    933 HD23 LEU A  74     -28.815  27.973 -19.061  1.00  0.00           H
ATOM    934  N   LYS A  75     -33.868  31.419 -16.558  1.00 64.42           N
ANISOU  934  N   LYS A  75     5699   9751   9026   1914   -125   2699       N
ATOM    935  CA  LYS A  75     -34.633  32.522 -15.934  1.00 62.37           C
ANISOU  935  CA  LYS A  75     5373   9390   8934   2102    -68   2765       C
ATOM    936  C   LYS A  75     -34.481  32.636 -14.398  1.00 62.08           C
ANISOU  936  C   LYS A  75     5382   9257   8948   2211    103   2622       C
ATOM    937  O   LYS A  75     -35.314  33.286 -13.773  1.00 64.83           O
ANISOU  937  O   LYS A  75     5693   9508   9430   2383    174   2645       O
ATOM    938  CB  LYS A  75     -36.114  32.414 -16.355  1.00 61.07           C
ANISOU  938  CB  LYS A  75     5032   9315   8856   2125   -125   2881       C
ATOM    939  CG  LYS A  75     -36.755  31.110 -15.851  1.00 60.85           C
ANISOU  939  CG  LYS A  75     4904   9423   8794   2056    -96   2832       C
ATOM    940  CD  LYS A  75     -38.239  31.003 -16.222  1.00 58.11           C
ANISOU  940  CD  LYS A  75     4408   9156   8514   2040   -164   2949       C
ATOM    941  CE  LYS A  75     -38.724  29.548 -16.164  1.00 55.64           C
ANISOU  941  CE  LYS A  75     4015   9004   8123   1901   -211   2947       C
ATOM    942  NZ  LYS A  75     -38.521  28.937 -14.836  1.00 54.72           N
ANISOU  942  NZ  LYS A  75     3891   8903   7996   1924    -80   2816       N
ATOM    943  H   LYS A  75     -34.306  30.515 -16.607  1.00 77.30           H
ATOM    944  HA  LYS A  75     -34.249  33.466 -16.326  1.00 74.84           H
ATOM    945  HB2 LYS A  75     -36.671  33.269 -15.964  1.00 73.28           H
ATOM    946  HB3 LYS A  75     -36.178  32.448 -17.444  1.00 73.28           H
ATOM    947  HG2 LYS A  75     -36.221  30.273 -16.298  1.00 73.02           H
ATOM    948  HG3 LYS A  75     -36.660  31.047 -14.766  1.00 73.02           H
ATOM    949  HD2 LYS A  75     -38.828  31.626 -15.547  1.00 69.73           H
ATOM    950  HD3 LYS A  75     -38.383  31.364 -17.241  1.00 69.73           H
ATOM    951  HE2 LYS A  75     -39.781  29.511 -16.434  1.00 66.77           H
ATOM    952  HE3 LYS A  75     -38.161  28.965 -16.899  1.00 66.77           H
ATOM    953  HZ1 LYS A  75     -38.916  27.993 -14.792  1.00 65.66           H
ATOM    954  HZ2 LYS A  75     -37.537  28.785 -14.646  1.00 65.66           H
ATOM    955  HZ3 LYS A  75     -38.945  29.455 -14.078  1.00 65.66           H
ATOM    956  N   TRP A  76     -33.646  31.817 -13.754  1.00 65.79           N
ANISOU  956  N   TRP A  76     5937   9746   9313   2116    167   2475       N
ATOM    957  CA  TRP A  76     -33.462  31.833 -12.296  1.00 67.30           C
ANISOU  957  CA  TRP A  76     6173   9861   9535   2195    322   2343       C
ATOM    958  C   TRP A  76     -32.540  32.971 -11.849  1.00 73.48           C
ANISOU  958  C   TRP A  76     7120  10449  10352   2281    385   2290       C
ATOM    959  O   TRP A  76     -31.381  33.052 -12.269  1.00 72.12           O
ANISOU  959  O   TRP A  76     7070  10207  10126   2216    316   2309       O
ATOM    960  CB  TRP A  76     -32.893  30.510 -11.750  1.00 63.80           C
ANISOU  960  CB  TRP A  76     5793   9478   8970   2053    352   2211       C
ATOM    961  CG  TRP A  76     -33.720  29.257 -11.805  1.00 63.35           C
ANISOU  961  CG  TRP A  76     5590   9591   8890   1978    309   2241       C
ATOM    962  CD1 TRP A  76     -35.007  29.146 -12.204  1.00 64.39           C
ANISOU  962  CD1 TRP A  76     5537   9835   9092   2015    249   2376       C
ATOM    963  CD2 TRP A  76     -33.317  27.908 -11.407  1.00 58.32           C
ANISOU  963  CD2 TRP A  76     4979   9025   8156   1843    309   2143       C
ATOM    964  NE1 TRP A  76     -35.424  27.833 -12.075  1.00 64.21           N
ANISOU  964  NE1 TRP A  76     5430   9951   9014   1903    208   2369       N
ATOM    965  CE2 TRP A  76     -34.420  27.024 -11.597  1.00 56.29           C
ANISOU  965  CE2 TRP A  76     4557   8919   7910   1799    242   2224       C
ATOM    966  CE3 TRP A  76     -32.123  27.344 -10.906  1.00 58.14           C
ANISOU  966  CE3 TRP A  76     5099   8948   8044   1754    349   2003       C
ATOM    967  CZ2 TRP A  76     -34.342  25.650 -11.320  1.00 56.71           C
ANISOU  967  CZ2 TRP A  76     4599   9060   7886   1666    210   2165       C
ATOM    968  CZ3 TRP A  76     -32.030  25.965 -10.629  1.00 55.77           C
ANISOU  968  CZ3 TRP A  76     4780   8734   7676   1633    321   1943       C
ATOM    969  CH2 TRP A  76     -33.135  25.119 -10.835  1.00 59.66           C
ANISOU  969  CH2 TRP A  76     5121   9368   8180   1589    250   2022       C
ATOM    970  H   TRP A  76     -33.035  31.221 -14.300  1.00 78.94           H
ATOM    971  HA  TRP A  76     -34.430  32.002 -11.826  1.00 80.75           H
ATOM    972  HB2 TRP A  76     -31.942  30.308 -12.246  1.00 76.56           H
ATOM    973  HB3 TRP A  76     -32.664  30.669 -10.696  1.00 76.56           H
ATOM    974  HD1 TRP A  76     -35.615  29.974 -12.549  1.00 77.27           H
ATOM    975  HE1 TRP A  76     -36.373  27.520 -12.291  1.00 77.05           H
ATOM    976  HE3 TRP A  76     -31.272  27.989 -10.746  1.00 69.77           H
ATOM    977  HZ2 TRP A  76     -35.197  25.014 -11.483  1.00 68.05           H
ATOM    978  HZ3 TRP A  76     -31.103  25.555 -10.258  1.00 66.92           H
ATOM    979  HH2 TRP A  76     -33.057  24.063 -10.617  1.00 71.59           H
ATOM    980  N   ASP A  77     -32.938  33.606 -10.759  1.00 74.69           N
ANISOU  980  N   ASP A  77     7275  10516  10588   2423    516   2225       N
ATOM    981  CA  ASP A  77     -32.197  34.592  -9.976  1.00 74.98           C
ANISOU  981  CA  ASP A  77     7491  10356  10642   2495    592   2141       C
ATOM    982  C   ASP A  77     -32.631  34.495  -8.497  1.00 73.99           C
ANISOU  982  C   ASP A  77     7362  10205  10545   2588    755   2021       C
ATOM    983  O   ASP A  77     -33.260  33.515  -8.093  1.00 75.79           O
ANISOU  983  O   ASP A  77     7442  10577  10777   2589    803   2015       O
ATOM    984  CB  ASP A  77     -32.443  35.980 -10.589  1.00 73.91           C
ANISOU  984  CB  ASP A  77     7378  10087  10618   2623    536   2249       C
ATOM    985  CG  ASP A  77     -33.920  36.346 -10.724  1.00 76.89           C
ANISOU  985  CG  ASP A  77     7562  10508  11145   2796    550   2350       C
ATOM    986  OD1 ASP A  77     -34.709  35.911  -9.844  1.00 75.32           O
ANISOU  986  OD1 ASP A  77     7251  10387  10981   2870    663   2298       O
ATOM    987  OD2 ASP A  77     -34.196  37.143 -11.635  1.00 77.71           O
ANISOU  987  OD2 ASP A  77     7620  10573  11334   2854    446   2490       O
ATOM    988  H   ASP A  77     -33.893  33.467 -10.453  1.00 89.63           H
ATOM    989  HA  ASP A  77     -31.132  34.374 -10.023  1.00 89.98           H
ATOM    990  HB2 ASP A  77     -31.941  36.740  -9.987  1.00 88.69           H
ATOM    991  HB3 ASP A  77     -31.984  35.997 -11.578  1.00 88.69           H
ATOM    992  N   LEU A  78     -32.165  35.414  -7.643  1.00 74.40           N
ANISOU  992  N   LEU A  78     7444  10949   9877   2835    198  -1888       N
ATOM    993  CA  LEU A  78     -32.452  35.367  -6.202  1.00 75.57           C
ANISOU  993  CA  LEU A  78     7535  11433   9745   2721    307  -1981       C
ATOM    994  C   LEU A  78     -33.938  35.575  -5.890  1.00 79.36           C
ANISOU  994  C   LEU A  78     7754  12292  10107   2741    447  -2209       C
ATOM    995  O   LEU A  78     -34.426  34.973  -4.940  1.00 79.12           O
ANISOU  995  O   LEU A  78     7639  12581   9844   2546    580  -2194       O
ATOM    996  CB  LEU A  78     -31.615  36.424  -5.458  1.00 79.66           C
ANISOU  996  CB  LEU A  78     8156  11869  10240   2877    229  -2119       C
ATOM    997  CG  LEU A  78     -30.097  36.225  -5.578  1.00 81.05           C
ANISOU  997  CG  LEU A  78     8594  11700  10500   2842     99  -1901       C
ATOM    998  CD1 LEU A  78     -29.353  37.444  -5.035  1.00 81.67           C
ANISOU  998  CD1 LEU A  78     8753  11673  10605   3044     11  -2077       C
ATOM    999  CD2 LEU A  78     -29.575  34.982  -4.849  1.00 81.01           C
ANISOU  999  CD2 LEU A  78     8691  11793  10294   2543    156  -1654       C
ATOM   1000  H   LEU A  78     -31.738  36.244  -8.019  1.00 89.28           H
ATOM   1001  HA  LEU A  78     -32.196  34.378  -5.824  1.00 90.68           H
ATOM   1002  HB2 LEU A  78     -31.874  37.405  -5.860  1.00 95.59           H
ATOM   1003  HB3 LEU A  78     -31.890  36.419  -4.402  1.00 95.59           H
ATOM   1004  HG  LEU A  78     -29.860  36.135  -6.634  1.00 97.25           H
ATOM   1005 HD11 LEU A  78     -29.621  38.326  -5.617  1.00  0.00           H
ATOM   1006 HD12 LEU A  78     -28.277  37.293  -5.108  1.00  0.00           H
ATOM   1007 HD13 LEU A  78     -29.619  37.613  -3.992  1.00  0.00           H
ATOM   1008 HD21 LEU A  78     -30.038  34.083  -5.253  1.00  0.00           H
ATOM   1009 HD22 LEU A  78     -29.793  35.056  -3.785  1.00  0.00           H
ATOM   1010 HD23 LEU A  78     -28.496  34.905  -4.975  1.00  0.00           H
ATOM   1011  N   GLU A  79     -34.645  36.382  -6.685  1.00 87.65           N
ANISOU 1011  N   GLU A  79     8673  13315  11316   2975    421  -2421       N
ATOM   1012  CA  GLU A  79     -36.069  36.685  -6.508  1.00 92.04           C
ANISOU 1012  CA  GLU A  79     8976  14223  11772   3013    548  -2656       C
ATOM   1013  C   GLU A  79     -36.938  35.479  -6.889  1.00 87.71           C
ANISOU 1013  C   GLU A  79     8316  13834  11177   2802    655  -2518       C
ATOM   1014  O   GLU A  79     -37.519  34.842  -6.008  1.00 94.28           O
ANISOU 1014  O   GLU A  79     9021  15012  11790   2638    798  -2555       O
ATOM   1015  CB  GLU A  79     -36.414  37.949  -7.322  1.00 91.26           C
ANISOU 1015  CB  GLU A  79     8970  13865  11841   3089    436  -2710       C
ATOM   1016  CG  GLU A  79     -37.868  38.411  -7.124  1.00 95.14           C
ANISOU 1016  CG  GLU A  79     9285  14633  12231   3076    525  -2898       C
ATOM   1017  CD  GLU A  79     -38.218  39.717  -7.861  1.00 95.77           C
ANISOU 1017  CD  GLU A  79     9461  14473  12455   3149    418  -2938       C
ATOM   1018  OE1 GLU A  79     -37.332  40.290  -8.537  1.00 94.89           O
ANISOU 1018  OE1 GLU A  79     9546  13985  12521   3175    295  -2790       O
ATOM   1019  OE2 GLU A  79     -39.386  40.148  -7.727  1.00 98.21           O
ANISOU 1019  OE2 GLU A  79     9647  14980  12687   3163    464  -3105       O
ATOM   1020  H   GLU A  79     -34.224  36.713  -7.542  1.00105.18           H
ATOM   1021  HA  GLU A  79     -36.260  36.903  -5.457  1.00110.44           H
ATOM   1022  HB2 GLU A  79     -35.742  38.750  -7.008  1.00109.52           H
ATOM   1023  HB3 GLU A  79     -36.239  37.752  -8.381  1.00109.52           H
ATOM   1024  HG2 GLU A  79     -38.536  37.620  -7.467  1.00114.16           H
ATOM   1025  HG3 GLU A  79     -38.033  38.554  -6.055  1.00114.16           H
ATOM   1026  N   TYR A  80     -36.801  34.985  -8.126  1.00 74.51           N
ANISOU 1026  N   TYR A  80     6687  11911   9710   2803    590  -2358       N
ATOM   1027  CA  TYR A  80     -37.537  33.815  -8.617  1.00 69.20           C
ANISOU 1027  CA  TYR A  80     5906  11371   9018   2613    684  -2230       C
ATOM   1028  C   TYR A  80     -37.295  32.554  -7.779  1.00 70.33           C
ANISOU 1028  C   TYR A  80     6109  11675   8940   2299    779  -2018       C
ATOM   1029  O   TYR A  80     -38.228  31.765  -7.567  1.00 73.89           O
ANISOU 1029  O   TYR A  80     6404  12430   9242   2136    922  -2030       O
ATOM   1030  CB  TYR A  80     -37.144  33.542 -10.074  1.00 67.18           C
ANISOU 1030  CB  TYR A  80     5727  10776   9021   2658    579  -2061       C
ATOM   1031  CG  TYR A  80     -37.837  32.322 -10.660  1.00 70.45           C
ANISOU 1031  CG  TYR A  80     6044  11291   9434   2460    663  -1913       C
ATOM   1032  CD1 TYR A  80     -37.248  31.048 -10.541  1.00 69.38           C
ANISOU 1032  CD1 TYR A  80     6028  11101   9233   2191    684  -1619       C
ATOM   1033  CD2 TYR A  80     -39.105  32.454 -11.258  1.00 69.38           C
ANISOU 1033  CD2 TYR A  80     5694  11303   9366   2543    722  -2068       C
ATOM   1034  CE1 TYR A  80     -37.919  29.915 -11.034  1.00 69.22           C
ANISOU 1034  CE1 TYR A  80     5915  11167   9217   2009    761  -1485       C
ATOM   1035  CE2 TYR A  80     -39.773  31.322 -11.762  1.00 68.61           C
ANISOU 1035  CE2 TYR A  80     5501  11297   9272   2363    800  -1939       C
ATOM   1036  CZ  TYR A  80     -39.172  30.052 -11.658  1.00 70.46           C
ANISOU 1036  CZ  TYR A  80     5856  11471   9443   2095    820  -1647       C
ATOM   1037  OH  TYR A  80     -39.777  28.975 -12.221  1.00 71.27           O
ANISOU 1037  OH  TYR A  80     5862  11660   9556   1915    897  -1521       O
ATOM   1038  H   TYR A  80     -36.209  35.497  -8.786  1.00 89.41           H
ATOM   1039  HA  TYR A  80     -38.603  34.038  -8.575  1.00 83.05           H
ATOM   1040  HB2 TYR A  80     -37.380  34.418 -10.680  1.00 80.61           H
ATOM   1041  HB3 TYR A  80     -36.064  33.390 -10.126  1.00 80.61           H
ATOM   1042  HD1 TYR A  80     -36.290  30.939 -10.047  1.00 83.26           H
ATOM   1043  HD2 TYR A  80     -39.557  33.435 -11.327  1.00 83.26           H
ATOM   1044  HE1 TYR A  80     -37.473  28.942 -10.931  1.00 83.06           H
ATOM   1045  HE2 TYR A  80     -40.739  31.420 -12.227  1.00 82.33           H
ATOM   1046  HH  TYR A  80     -39.150  28.217 -12.303  1.00 85.52           H
ATOM   1047  N   LEU A  81     -36.044  32.335  -7.348  1.00 76.79           N
ANISOU 1047  N   LEU A  81     7150  12292   9734   2212    703  -1822       N
ATOM   1048  CA  LEU A  81     -35.711  31.247  -6.436  1.00 78.64           C
ANISOU 1048  CA  LEU A  81     7459  12657   9765   1916    784  -1603       C
ATOM   1049  C   LEU A  81     -36.324  31.483  -5.053  1.00 82.87           C
ANISOU 1049  C   LEU A  81     7878  13589  10020   1844    920  -1763       C
ATOM   1050  O   LEU A  81     -37.083  30.626  -4.628  1.00 85.47           O
ANISOU 1050  O   LEU A  81     8108  14190  10177   1626   1059  -1697       O
ATOM   1051  CB  LEU A  81     -34.192  31.011  -6.356  1.00 74.51           C
ANISOU 1051  CB  LEU A  81     7204  11824   9283   1865    661  -1379       C
ATOM   1052  CG  LEU A  81     -33.572  30.415  -7.637  1.00 73.45           C
ANISOU 1052  CG  LEU A  81     7202  11320   9385   1846    549  -1143       C
ATOM   1053  CD1 LEU A  81     -32.046  30.417  -7.534  1.00 71.26           C
ANISOU 1053  CD1 LEU A  81     7185  10727   9166   1850    414   -976       C
ATOM   1054  CD2 LEU A  81     -33.984  28.956  -7.850  1.00 72.53           C
ANISOU 1054  CD2 LEU A  81     7042  11294   9221   1580    639   -922       C
ATOM   1055  H   LEU A  81     -35.337  33.036  -7.551  1.00 92.15           H
ATOM   1056  HA  LEU A  81     -36.177  30.337  -6.811  1.00 94.37           H
ATOM   1057  HB2 LEU A  81     -33.706  31.958  -6.120  1.00 89.41           H
ATOM   1058  HB3 LEU A  81     -33.991  30.328  -5.530  1.00 89.41           H
ATOM   1059  HG  LEU A  81     -33.870  30.994  -8.510  1.00 88.14           H
ATOM   1060 HD11 LEU A  81     -31.694  31.442  -7.418  1.00  0.00           H
ATOM   1061 HD12 LEU A  81     -31.615  29.999  -8.443  1.00  0.00           H
ATOM   1062 HD13 LEU A  81     -31.741  29.825  -6.675  1.00  0.00           H
ATOM   1063 HD21 LEU A  81     -35.056  28.893  -8.013  1.00  0.00           H
ATOM   1064 HD22 LEU A  81     -33.483  28.559  -8.730  1.00  0.00           H
ATOM   1065 HD23 LEU A  81     -33.706  28.359  -6.984  1.00  0.00           H
ATOM   1066  N   GLN A  82     -36.163  32.643  -4.412  1.00 84.84           N
ANISOU 1066  N   GLN A  82     8138  13879  10219   2022    884  -1974       N
ATOM   1067  CA  GLN A  82     -36.736  32.893  -3.079  1.00 91.28           C
ANISOU 1067  CA  GLN A  82     8837  15075  10771   1974   1008  -2148       C
ATOM   1068  C   GLN A  82     -38.266  32.693  -3.025  1.00 94.26           C
ANISOU 1068  C   GLN A  82     8955  15788  11072   1935   1157  -2298       C
ATOM   1069  O   GLN A  82     -38.737  31.918  -2.188  1.00 98.74           O
ANISOU 1069  O   GLN A  82     9430  16685  11401   1754   1299  -2302       O
ATOM   1070  CB  GLN A  82     -36.313  34.299  -2.628  1.00 90.28           C
ANISOU 1070  CB  GLN A  82     8727  14923  10652   2222    937  -2397       C
ATOM   1071  CG  GLN A  82     -36.823  34.688  -1.234  1.00 92.52           C
ANISOU 1071  CG  GLN A  82     8917  15579  10659   2179   1050  -2571       C
ATOM   1072  CD  GLN A  82     -36.343  36.074  -0.811  1.00 91.64           C
ANISOU 1072  CD  GLN A  82     8842  15418  10559   2416    968  -2800       C
ATOM   1073  OE1 GLN A  82     -35.742  36.235   0.236  1.00 90.75           O
ANISOU 1073  OE1 GLN A  82     8788  15438  10253   2365    991  -2830       O
ATOM   1074  NE2 GLN A  82     -36.428  37.081  -1.650  1.00 90.44           N
ANISOU 1074  NE2 GLN A  82     8654  15077  10634   2678    874  -2967       N
ATOM   1075  H   GLN A  82     -35.643  33.395  -4.853  1.00101.81           H
ATOM   1076  HA  GLN A  82     -36.300  32.174  -2.386  1.00109.54           H
ATOM   1077  HB2 GLN A  82     -35.224  34.337  -2.603  1.00108.34           H
ATOM   1078  HB3 GLN A  82     -36.671  35.026  -3.358  1.00108.34           H
ATOM   1079  HG2 GLN A  82     -37.912  34.685  -1.225  1.00111.03           H
ATOM   1080  HG3 GLN A  82     -36.459  33.958  -0.511  1.00111.03           H
ATOM   1081 HE21 GLN A  82     -36.954  36.987  -2.504  1.00108.53           H
ATOM   1082 HE22 GLN A  82     -36.089  37.967  -1.323  1.00108.53           H
ATOM   1083  N   GLU A  83     -38.985  33.157  -4.048  1.00 89.42           N
ANISOU 1083  N   GLU A  83     8221  15097  10658   2102   1126  -2421       N
ATOM   1084  CA  GLU A  83     -40.441  32.997  -4.213  1.00 88.66           C
ANISOU 1084  CA  GLU A  83     7870  15313  10505   2088   1260  -2586       C
ATOM   1085  C   GLU A  83     -40.917  31.545  -4.423  1.00 88.89           C
ANISOU 1085  C   GLU A  83     7855  15453  10465   1806   1366  -2364       C
ATOM   1086  O   GLU A  83     -42.076  31.221  -4.145  1.00 91.39           O
ANISOU 1086  O   GLU A  83     7998  16119  10606   1679   1521  -2443       O
ATOM   1087  CB  GLU A  83     -40.871  33.824  -5.440  1.00 84.58           C
ANISOU 1087  CB  GLU A  83     7246  14662  10228   2348   1189  -2767       C
ATOM   1088  CG  GLU A  83     -40.790  35.341  -5.221  0.50 81.42           C
ANISOU 1088  CG  GLU A  83     6863  14188   9886   2618   1099  -3015       C
ATOM   1089  CD  GLU A  83     -41.593  35.783  -3.994  0.50 82.31           C
ANISOU 1089  CD  GLU A  83     6868  14631   9773   2596   1192  -3223       C
ATOM   1090  OE1 GLU A  83     -42.766  35.330  -3.905  0.50 82.53           O
ANISOU 1090  OE1 GLU A  83     6732  14956   9672   2461   1325  -3269       O
ATOM   1091  OE2 GLU A  83     -40.944  36.229  -3.022  0.50 81.98           O
ANISOU 1091  OE2 GLU A  83     6913  14545   9690   2707   1128  -3335       O
ATOM   1092  H   GLU A  83     -38.521  33.807  -4.681  1.00107.31           H
ATOM   1093  HA  GLU A  83     -40.954  33.375  -3.327  1.00106.40           H
ATOM   1094  HB2 GLU A  83     -40.249  33.547  -6.295  1.00101.49           H
ATOM   1095  HB3 GLU A  83     -41.901  33.564  -5.699  1.00101.49           H
ATOM   1096  HG2 GLU A  83     -39.748  35.631  -5.104  0.50 97.71           H
ATOM   1097  HG3 GLU A  83     -41.172  35.836  -6.111  0.50 97.71           H
ATOM   1098  N   ASN A  84     -40.104  30.677  -5.035  1.00 84.30           N
ANISOU 1098  N   ASN A  84     7427  14580  10023   1704   1288  -2088       N
ATOM   1099  CA  ASN A  84     -40.556  29.358  -5.506  1.00 85.94           C
ANISOU 1099  CA  ASN A  84     7585  14847  10221   1466   1372  -1885       C
ATOM   1100  C   ASN A  84     -39.728  28.163  -5.022  0.80 81.41           C
ANISOU 1100  C   ASN A  84     7193  14201   9537   1199   1382  -1572       C
ATOM   1101  O   ASN A  84     -40.178  27.032  -5.198  0.80 68.34           O
ANISOU 1101  O   ASN A  84     5502  12603   7860    981   1458  -1390       O
ATOM   1102  CB  ASN A  84     -40.681  29.364  -7.037  0.80 89.18           C
ANISOU 1102  CB  ASN A  84     7982  14993  10911   1568   1283  -1830       C
ATOM   1103  CG  ASN A  84     -41.779  30.296  -7.511  0.80 96.37           C
ANISOU 1103  CG  ASN A  84     8669  16036  11912   1778   1310  -2116       C
ATOM   1104  OD1 ASN A  84     -42.952  29.929  -7.594  0.80 98.73           O
ANISOU 1104  OD1 ASN A  84     8769  16604  12139   1687   1439  -2189       O
ATOM   1105  ND2 ASN A  84     -41.396  31.413  -8.075  0.80 97.37           N
ANISOU 1105  ND2 ASN A  84     8826  15971  12200   2060   1189  -2278       N
ATOM   1106  H   ASN A  84     -39.174  31.007  -5.278  1.00101.16           H
ATOM   1107  HA  ASN A  84     -41.553  29.165  -5.106  1.00103.13           H
ATOM   1108  HB2 ASN A  84     -39.725  29.657  -7.473  0.80107.02           H
ATOM   1109  HB3 ASN A  84     -40.909  28.357  -7.378  0.80107.02           H
ATOM   1110 HD21 ASN A  84     -42.063  32.160  -8.097  0.80116.85           H
ATOM   1111 HD22 ASN A  84     -40.405  31.642  -8.024  0.80116.85           H
ATOM   1112  N   ILE A  85     -38.568  28.367  -4.400  1.00 94.18           N
ANISOU 1112  N   ILE A  85     9001  15696  11085   1206   1307  -1503       N
ATOM   1113  CA  ILE A  85     -37.734  27.303  -3.828  1.00 96.12           C
ANISOU 1113  CA  ILE A  85     9426  15868  11228    955   1312  -1202       C
ATOM   1114  C   ILE A  85     -38.357  26.703  -2.564  1.00 93.78           C
ANISOU 1114  C   ILE A  85     9042  15951  10638    724   1485  -1181       C
ATOM   1115  O   ILE A  85     -38.203  25.509  -2.355  1.00 96.22           O
ANISOU 1115  O   ILE A  85     9438  16260  10861    473   1531   -922       O
ATOM   1116  CB  ILE A  85     -36.288  27.808  -3.612  1.00 95.05           C
ANISOU 1116  CB  ILE A  85     9530  15465  11122   1037   1170  -1127       C
ATOM   1117  CG1 ILE A  85     -35.253  26.672  -3.507  1.00 92.39           C
ANISOU 1117  CG1 ILE A  85     9396  14953  10757    800   1138   -783       C
ATOM   1118  CG2 ILE A  85     -36.177  28.696  -2.366  1.00 98.68           C
ANISOU 1118  CG2 ILE A  85     9974  16147  11373   1108   1208  -1323       C
ATOM   1119  CD1 ILE A  85     -34.963  25.980  -4.843  1.00 88.51           C
ANISOU 1119  CD1 ILE A  85     8967  14158  10502    763   1058   -579       C
ATOM   1120  H   ILE A  85     -38.234  29.323  -4.310  1.00113.01           H
ATOM   1121  HA  ILE A  85     -37.699  26.493  -4.552  1.00115.35           H
ATOM   1122  HB  ILE A  85     -36.000  28.404  -4.479  1.00114.06           H
ATOM   1123 HG12 ILE A  85     -34.309  27.083  -3.142  1.00110.87           H
ATOM   1124 HG13 ILE A  85     -35.608  25.926  -2.799  1.00110.87           H
ATOM   1125 HG21 ILE A  85     -35.234  29.231  -2.410  1.00118.42           H
ATOM   1126 HG22 ILE A  85     -36.976  29.435  -2.341  1.00118.42           H
ATOM   1127 HG23 ILE A  85     -36.213  28.098  -1.455  1.00118.42           H
ATOM   1128 HD11 ILE A  85     -34.167  25.248  -4.709  1.00106.21           H
ATOM   1129 HD12 ILE A  85     -35.856  25.466  -5.187  1.00106.21           H
ATOM   1130 HD13 ILE A  85     -34.650  26.714  -5.585  1.00106.21           H
ATOM   1131  N   GLY A  86     -39.280  27.412  -1.905  1.00 86.73           N
ANISOU 1131  N   GLY A  86     7982  15382   9592    802   1583  -1445       N
ATOM   1132  CA  GLY A  86     -40.009  26.905  -0.740  1.00 86.74           C
ANISOU 1132  CA  GLY A  86     7880  15762   9313    594   1757  -1445       C
ATOM   1133  C   GLY A  86     -39.218  27.042   0.565  1.00 90.09           C
ANISOU 1133  C   GLY A  86     8436  16273   9521    544   1759  -1424       C
ATOM   1134  O   GLY A  86     -38.100  27.562   0.596  1.00 86.00           O
ANISOU 1134  O   GLY A  86     8093  15518   9065    667   1624  -1409       O
ATOM   1135  H   GLY A  86     -39.351  28.396  -2.122  1.00104.08           H
ATOM   1136  HA2 GLY A  86     -40.954  27.438  -0.644  1.00104.08           H
ATOM   1137  HA3 GLY A  86     -40.235  25.846  -0.885  1.00104.08           H
ATOM   1138  N   ASN A  87     -39.805  26.605   1.679  0.80 98.19           N
ANISOU 1138  N   ASN A  87     9372  17653  10284    359   1919  -1425       N
ATOM   1139  CA  ASN A  87     -39.087  26.505   2.947  0.80100.72           C
ANISOU 1139  CA  ASN A  87     9795  18114  10362    288   1946  -1407       C
ATOM   1140  C   ASN A  87     -38.228  25.226   2.990  0.80 98.70           C
ANISOU 1140  C   ASN A  87     9720  17752  10028     24   1951  -1057       C
ATOM   1141  O   ASN A  87     -38.772  24.124   3.063  0.80101.96           O
ANISOU 1141  O   ASN A  87    10064  18340  10335   -210   2081   -913       O
ATOM   1142  H   ASN A  87     -40.725  26.189   1.621  0.80117.83           H
ATOM   1143  CB  ASN A  87     -40.087  26.610   4.118  1.00  0.00           C
ATOM   1144  CG  ASN A  87     -41.258  25.655   4.077  1.00  0.00           C
ATOM   1145  ND2 ASN A  87     -41.090  24.427   4.438  1.00  0.00           N
ATOM   1146  OD1 ASN A  87     -42.361  26.050   3.747  1.00  0.00           O
ATOM   1147  HA  ASN A  87     -38.401  27.360   3.016  0.80  0.00           H
ATOM   1148  HB2 ASN A  87     -40.478  27.639   4.123  1.00  0.00           H
ATOM   1149  HB3 ASN A  87     -39.542  26.476   5.058  1.00  0.00           H
ATOM   1150 HD21 ASN A  87     -41.918  23.865   4.468  1.00  0.00           H
ATOM   1151 HD22 ASN A  87     -40.187  24.004   4.208  1.00  0.00           H
ATOM   1152  N   GLY A  88     -36.924  25.367   3.209  1.00 94.67           N
ANISOU 1152  N   GLY A  88     9441  16955   9573     61   1809   -922       N
ATOM   1153  CA  GLY A  88     -36.016  24.233   3.372  1.00 90.25           C
ANISOU 1153  CA  GLY A  88     9072  16271   8949   -172   1796   -593       C
ATOM   1154  C   GLY A  88     -34.609  24.697   3.716  1.00 86.32           C
ANISOU 1154  C   GLY A  88     8801  15551   8447    -89   1655   -539       C
ATOM   1155  O   GLY A  88     -34.282  25.862   3.482  1.00 81.19           O
ANISOU 1155  O   GLY A  88     8172  14783   7895    157   1551   -736       O
ATOM   1156  H   GLY A  88     -36.490  26.279   3.139  1.00113.60           H
ATOM   1157  HA2 GLY A  88     -36.378  23.583   4.169  1.00108.30           H
ATOM   1158  HA3 GLY A  88     -35.978  23.655   2.447  1.00108.30           H
ATOM   1159  N   ASP A  89     -33.894  23.878   4.479  1.00 95.63           N
ANISOU 1159  N   ASP A  89    10151  16672   9512   -297   1654   -267       N
ATOM   1160  CA  ASP A  89     -32.519  24.150   4.898  1.00 97.75           C
ANISOU 1160  CA  ASP A  89    10645  16743   9754   -251   1529   -189       C
ATOM   1161  C   ASP A  89     -31.533  24.020   3.726  1.00 91.11           C
ANISOU 1161  C   ASP A  89     9976  15449   9193   -181   1354    -29       C
ATOM   1162  O   ASP A  89     -31.520  23.032   2.982  1.00 91.42           O
ANISOU 1162  O   ASP A  89    10055  15342   9339   -331   1352    201       O
ATOM   1163  CB  ASP A  89     -32.167  23.265   6.105  1.00 98.90           C
ANISOU 1163  CB  ASP A  89    10898  17039   9640   -503   1606     29       C
ATOM   1164  CG  ASP A  89     -33.086  23.575   7.293  1.00103.39           C
ANISOU 1164  CG  ASP A  89    11334  18036   9913   -539   1754   -145       C
ATOM   1165  OD1 ASP A  89     -33.297  24.790   7.531  1.00104.76           O
ANISOU 1165  OD1 ASP A  89    11442  18306  10055   -331   1731   -419       O
ATOM   1166  OD2 ASP A  89     -33.945  22.725   7.613  1.00105.90           O
ANISOU 1166  OD2 ASP A  89    11612  18594  10031   -775   1896     -6       O
ATOM   1167  H   ASP A  89     -34.282  22.989   4.761  1.00114.76           H
ATOM   1168  HA  ASP A  89     -32.467  25.184   5.240  1.00117.30           H
ATOM   1169  HB2 ASP A  89     -32.249  22.212   5.831  1.00118.68           H
ATOM   1170  HB3 ASP A  89     -31.137  23.461   6.404  1.00118.68           H
ATOM   1171  N   PHE A  90     -30.793  25.103   3.494  1.00 83.79           N
ANISOU 1171  N   PHE A  90     9146  14303   8386     48   1210   -155       N
ATOM   1172  CA  PHE A  90     -29.710  25.200   2.524  1.00 78.64           C
ANISOU 1172  CA  PHE A  90     8668  13215   7994    137   1036    -23       C
ATOM   1173  C   PHE A  90     -28.378  25.245   3.273  1.00 78.24           C
ANISOU 1173  C   PHE A  90     8844  13008   7876    140    931     72       C
ATOM   1174  O   PHE A  90     -28.148  26.191   4.032  1.00 79.06           O
ANISOU 1174  O   PHE A  90     8946  13242   7853    257    927   -116       O
ATOM   1175  CB  PHE A  90     -29.920  26.446   1.636  1.00 78.98           C
ANISOU 1175  CB  PHE A  90     8631  13100   8279    424    947   -256       C
ATOM   1176  CG  PHE A  90     -31.135  26.328   0.732  1.00 83.20           C
ANISOU 1176  CG  PHE A  90     8968  13715   8929    434   1020   -322       C
ATOM   1177  CD1 PHE A  90     -31.009  25.704  -0.520  1.00 81.43           C
ANISOU 1177  CD1 PHE A  90     8787  13231   8921    384    962   -136       C
ATOM   1178  CD2 PHE A  90     -32.409  26.699   1.194  1.00 85.26           C
ANISOU 1178  CD2 PHE A  90     8998  14313   9084    494   1145   -573       C
ATOM   1179  CE1 PHE A  90     -32.148  25.339  -1.257  1.00 83.07           C
ANISOU 1179  CE1 PHE A  90     8811  13516   9236    397   1027   -200       C
ATOM   1180  CE2 PHE A  90     -33.554  26.339   0.459  1.00 84.80           C
ANISOU 1180  CE2 PHE A  90     8756  14330   9133    506   1211   -638       C
ATOM   1181  CZ  PHE A  90     -33.423  25.620  -0.739  1.00 84.25           C
ANISOU 1181  CZ  PHE A  90     8731  14001   9278    457   1152   -452       C
ATOM   1182  H   PHE A  90     -30.915  25.901   4.109  1.00100.55           H
ATOM   1183  HA  PHE A  90     -29.713  24.318   1.886  1.00 94.36           H
ATOM   1184  HB2 PHE A  90     -30.019  27.333   2.265  1.00 94.78           H
ATOM   1185  HB3 PHE A  90     -29.032  26.581   1.020  1.00 94.78           H
ATOM   1186  HD1 PHE A  90     -30.032  25.437  -0.876  1.00 97.71           H
ATOM   1187  HD2 PHE A  90     -32.508  27.169   2.161  1.00102.31           H
ATOM   1188  HE1 PHE A  90     -32.047  24.792  -2.181  1.00 99.68           H
ATOM   1189  HE2 PHE A  90     -34.538  26.545   0.855  1.00101.76           H
ATOM   1190  HZ  PHE A  90     -34.304  25.256  -1.243  1.00101.10           H
ATOM   1191  N   SER A  91     -27.433  24.383   2.883  1.00 80.06           N
ANISOU 1191  N   SER A  91     9266  12961   8191     13    846    358       N
ATOM   1192  CA  SER A  91     -26.051  24.494   3.364  1.00 80.98           C
ANISOU 1192  CA  SER A  91     9608  12897   8262     10    736    468       C
ATOM   1193  C   SER A  91     -25.392  25.743   2.772  1.00 77.44           C
ANISOU 1193  C   SER A  91     9238  12154   8033    285    573    317       C
ATOM   1194  O   SER A  91     -25.157  25.817   1.557  1.00 73.91           O
ANISOU 1194  O   SER A  91     8810  11426   7848    382    483    351       O
ATOM   1195  CB  SER A  91     -25.196  23.267   3.009  1.00 79.42           C
ANISOU 1195  CB  SER A  91     9585  12492   8099   -212    696    821       C
ATOM   1196  OG  SER A  91     -25.831  22.027   3.284  1.00 81.12           O
ANISOU 1196  OG  SER A  91     9712  12953   8156   -461    848    965       O
ATOM   1197  H   SER A  91     -27.689  23.587   2.313  1.00 96.07           H
ATOM   1198  HA  SER A  91     -26.068  24.598   4.448  1.00 97.17           H
ATOM   1199  HB2 SER A  91     -24.952  23.295   1.954  1.00 95.30           H
ATOM   1200  HB3 SER A  91     -24.272  23.313   3.575  1.00 95.30           H
ATOM   1201  HG  SER A  91     -26.754  22.212   3.507  1.00 97.34           H
ATOM   1202  N   VAL A  92     -25.013  26.702   3.619  1.00 74.82           N
ANISOU 1202  N   VAL A  92     8948  11884   7595    412    537    149       N
ATOM   1203  CA  VAL A  92     -24.275  27.913   3.229  1.00 72.43           C
ANISOU 1203  CA  VAL A  92     8714  11327   7480    678    391    -16       C
ATOM   1204  C   VAL A  92     -22.876  27.871   3.835  1.00 73.28           C
ANISOU 1204  C   VAL A  92     9047  11268   7529    657    286     96       C
ATOM   1205  O   VAL A  92     -22.707  27.651   5.029  1.00 75.70           O
ANISOU 1205  O   VAL A  92     9380  11802   7579    550    349    105       O
ATOM   1206  CB  VAL A  92     -25.031  29.196   3.628  1.00 76.89           C
ANISOU 1206  CB  VAL A  92     9097  12123   7995    888    440   -371       C
ATOM   1207  CG1 VAL A  92     -24.315  30.464   3.137  1.00 75.20           C
ANISOU 1207  CG1 VAL A  92     8947  11624   8002   1167    289   -538       C
ATOM   1208  CG2 VAL A  92     -26.441  29.217   3.024  1.00 78.48           C
ANISOU 1208  CG2 VAL A  92     9065  12533   8221    886    560   -480       C
ATOM   1209  H   VAL A  92     -25.265  26.602   4.604  1.00 89.78           H
ATOM   1210  HA  VAL A  92     -24.165  27.930   2.147  1.00 86.92           H
ATOM   1211  HB  VAL A  92     -25.113  29.245   4.715  1.00 92.27           H
ATOM   1212 HG11 VAL A  92     -24.871  31.340   3.474  1.00 90.24           H
ATOM   1213 HG12 VAL A  92     -23.313  30.529   3.560  1.00 90.24           H
ATOM   1214 HG13 VAL A  92     -24.259  30.468   2.049  1.00 90.24           H
ATOM   1215 HG21 VAL A  92     -26.915  30.176   3.219  1.00 94.18           H
ATOM   1216 HG22 VAL A  92     -26.402  29.039   1.951  1.00 94.18           H
ATOM   1217 HG23 VAL A  92     -27.050  28.447   3.495  1.00 94.18           H
ATOM   1218  N   TYR A  93     -21.846  28.104   3.026  1.00 70.53           N
ANISOU 1218  N   TYR A  93     8858  10524   7416    761    127    178       N
ATOM   1219  CA  TYR A  93     -20.461  28.182   3.495  1.00 71.16           C
ANISOU 1219  CA  TYR A  93     9161  10398   7477    750     11    294       C
ATOM   1220  C   TYR A  93     -20.010  29.643   3.559  1.00 70.42           C
ANISOU 1220  C   TYR A  93     9097  10159   7503   1026    -99     51       C
ATOM   1221  O   TYR A  93     -20.251  30.392   2.608  1.00 66.68           O
ANISOU 1221  O   TYR A  93     8571   9497   7266   1217   -163    -70       O
ATOM   1222  CB  TYR A  93     -19.563  27.307   2.613  1.00 66.98           C
ANISOU 1222  CB  TYR A  93     8810   9515   7124    639    -89    596       C
ATOM   1223  CG  TYR A  93     -19.937  25.826   2.638  1.00 64.51           C
ANISOU 1223  CG  TYR A  93     8487   9321   6702    357     11    855       C
ATOM   1224  CD1 TYR A  93     -20.996  25.342   1.841  1.00 65.89           C
ANISOU 1224  CD1 TYR A  93     8507   9572   6955    304     94    873       C
ATOM   1225  CD2 TYR A  93     -19.250  24.943   3.494  1.00 64.63           C
ANISOU 1225  CD2 TYR A  93     8647   9371   6538    146     22   1079       C
ATOM   1226  CE1 TYR A  93     -21.352  23.983   1.878  1.00 66.52           C
ANISOU 1226  CE1 TYR A  93     8574   9757   6943     46    187   1106       C
ATOM   1227  CE2 TYR A  93     -19.585  23.575   3.518  1.00 66.39           C
ANISOU 1227  CE2 TYR A  93     8861   9697   6666   -112    114   1317       C
ATOM   1228  CZ  TYR A  93     -20.629  23.089   2.701  1.00 67.93           C
ANISOU 1228  CZ  TYR A  93     8899   9964   6947   -162    198   1329       C
ATOM   1229  OH  TYR A  93     -20.944  21.769   2.708  1.00 67.21           O
ANISOU 1229  OH  TYR A  93     8796   9973   6769   -420    292   1564       O
ATOM   1230  H   TYR A  93     -22.027  28.262   2.042  1.00 84.64           H
ATOM   1231  HA  TYR A  93     -20.397  27.782   4.504  1.00 85.39           H
ATOM   1232  HB2 TYR A  93     -19.600  27.665   1.584  1.00 80.37           H
ATOM   1233  HB3 TYR A  93     -18.534  27.413   2.959  1.00 80.37           H
ATOM   1234  HD1 TYR A  93     -21.567  26.026   1.224  1.00 79.06           H
ATOM   1235  HD2 TYR A  93     -18.478  25.329   4.146  1.00 77.56           H
ATOM   1236  HE1 TYR A  93     -22.192  23.615   1.308  1.00 79.82           H
ATOM   1237  HE2 TYR A  93     -19.060  22.894   4.166  1.00 79.66           H
ATOM   1238  HH  TYR A  93     -20.934  21.400   3.592  1.00 80.65           H
ATOM   1239  N   SER A  94     -19.309  30.033   4.628  1.00 73.44           N
ANISOU 1239  N   SER A  94     9559  10626   7720   1046   -121    -20       N
ATOM   1240  CA  SER A  94     -18.695  31.361   4.777  1.00 72.34           C
ANISOU 1240  CA  SER A  94     9452  10363   7672   1296   -223   -251       C
ATOM   1241  C   SER A  94     -17.180  31.334   4.552  1.00 71.57           C
ANISOU 1241  C   SER A  94     9597   9903   7695   1311   -381    -95       C
ATOM   1242  O   SER A  94     -16.502  30.325   4.762  1.00 68.47           O
ANISOU 1242  O   SER A  94     9350   9440   7225   1113   -397    167       O
ATOM   1243  H   SER A  94     -19.108  29.350   5.352  1.00 88.13           H
ATOM   1244  CB  SER A  94     -19.068  32.009   6.122  1.00  0.00           C
ATOM   1245  OG  SER A  94     -18.508  31.330   7.233  1.00  0.00           O
ATOM   1246  HA  SER A  94     -19.099  32.009   4.006  1.00  0.00           H
ATOM   1247  HB2 SER A  94     -20.153  32.013   6.229  1.00  0.00           H
ATOM   1248  HB3 SER A  94     -18.727  33.046   6.131  1.00  0.00           H
ATOM   1249  HG  SER A  94     -18.911  31.717   8.019  1.00  0.00           H
ATOM   1250  N   ALA A  95     -16.631  32.460   4.096  1.00 72.68           N
ANISOU 1250  N   ALA A  95     9778   9809   8028   1551   -499   -263       N
ATOM   1251  CA  ALA A  95     -15.196  32.681   3.972  1.00 69.44           C
ANISOU 1251  CA  ALA A  95     9588   9045   7752   1597   -654   -152       C
ATOM   1252  C   ALA A  95     -14.853  34.166   4.185  1.00 68.26           C
ANISOU 1252  C   ALA A  95     9432   8804   7702   1865   -737   -430       C
ATOM   1253  O   ALA A  95     -15.335  35.039   3.466  1.00 68.73           O
ANISOU 1253  O   ALA A  95     9351   8872   7892   2053   -726   -644       O
ATOM   1254  CB  ALA A  95     -14.717  32.156   2.609  1.00 67.71           C
ANISOU 1254  CB  ALA A  95     9469   8458   7800   1575   -744     63       C
ATOM   1255  H   ALA A  95     -17.251  33.206   3.791  1.00 87.22           H
ATOM   1256  HA  ALA A  95     -14.695  32.105   4.750  1.00 83.33           H
ATOM   1257  HB1 ALA A  95     -13.639  32.277   2.515  1.00 81.25           H
ATOM   1258  HB2 ALA A  95     -14.965  31.098   2.515  1.00 81.25           H
ATOM   1259  HB3 ALA A  95     -15.210  32.706   1.805  1.00 81.25           H
ATOM   1260  N   SER A  96     -13.840  34.431   5.014  1.00 95.41           N
ANISOU 1260  N   SER A  96    11441  14409  10400   -231  -1425    430       N
ATOM   1261  CA  SER A  96     -13.278  35.771   5.269  1.00 97.36           C
ANISOU 1261  CA  SER A  96    11911  14452  10631   -186  -1765    347       C
ATOM   1262  C   SER A  96     -12.565  36.414   4.071  1.00 95.06           C
ANISOU 1262  C   SER A  96    11371  14035  10714   -249  -1895    403       C
ATOM   1263  O   SER A  96     -12.040  37.514   4.216  1.00 97.76           O
ANISOU 1263  O   SER A  96    11859  14230  11055   -191  -2127    310       O
ATOM   1264  CB  SER A  96     -12.287  35.668   6.437  1.00 99.26           C
ANISOU 1264  CB  SER A  96    12436  14503  10773   -262  -2121    435       C
ATOM   1265  OG  SER A  96     -11.284  34.687   6.181  1.00 99.92           O
ANISOU 1265  OG  SER A  96    12334  14526  11105   -446  -2200    663       O
ATOM   1266  H   SER A  96     -13.454  33.674   5.553  1.00114.49           H
ATOM   1267  HA  SER A  96     -14.084  36.446   5.561  1.00116.84           H
ATOM   1268  HB2 SER A  96     -11.813  36.638   6.602  1.00119.11           H
ATOM   1269  HB3 SER A  96     -12.826  35.398   7.346  1.00119.11           H
ATOM   1270  HG  SER A  96     -10.618  34.793   6.869  1.00119.90           H
ATOM   1271  N   THR A  97     -12.377  35.685   2.968  1.00 91.37           N
ANISOU 1271  N   THR A  97    10538  13617  10562   -365  -1754    551       N
ATOM   1272  CA  THR A  97     -11.704  36.133   1.737  1.00 89.61           C
ANISOU 1272  CA  THR A  97    10061  13280  10706   -430  -1859    617       C
ATOM   1273  C   THR A  97     -12.121  35.248   0.556  1.00 86.84           C
ANISOU 1273  C   THR A  97     9333  13123  10538   -434  -1489    640       C
ATOM   1274  O   THR A  97     -12.662  34.149   0.746  1.00 87.64           O
ANISOU 1274  O   THR A  97     9389  13440  10469   -375  -1164    588       O
ATOM   1275  CB  THR A  97     -10.158  36.149   1.821  1.00 89.73           C
ANISOU 1275  CB  THR A  97    10029  13076  10988   -613  -2190    828       C
ATOM   1276  OG1 THR A  97      -9.578  34.860   1.719  1.00 89.78           O
ANISOU 1276  OG1 THR A  97     9873  13168  11073   -736  -2057    998       O
ATOM   1277  CG2 THR A  97      -9.472  36.761   3.037  1.00 93.12           C
ANISOU 1277  CG2 THR A  97    10839  13311  11233   -604  -2563    799       C
ATOM   1278  H   THR A  97     -13.000  34.887   2.870  1.00109.65           H
ATOM   1279  HA  THR A  97     -12.039  37.147   1.526  1.00107.53           H
ATOM   1280  HB  THR A  97      -9.811  36.717   0.958  1.00107.68           H
ATOM   1281  HG1 THR A  97      -8.631  35.032   1.628  1.00107.74           H
ATOM   1282 HG21 THR A  97      -8.386  36.707   2.932  1.00111.75           H
ATOM   1283 HG22 THR A  97      -9.748  37.813   3.117  1.00111.75           H
ATOM   1284 HG23 THR A  97      -9.762  36.240   3.950  1.00111.75           H
ATOM   1285  N   HIS A  98     -11.729  35.608  -0.664  1.00 83.61           N
ANISOU 1285  N   HIS A  98     8653  12634  10482   -504  -1539    719       N
ATOM   1286  CA  HIS A  98     -12.075  34.896  -1.907  1.00 80.66           C
ANISOU 1286  CA  HIS A  98     7907  12426  10315   -519  -1212    758       C
ATOM   1287  C   HIS A  98     -11.737  33.395  -1.942  1.00 81.41           C
ANISOU 1287  C   HIS A  98     7808  12600  10526   -660  -1084    949       C
ATOM   1288  O   HIS A  98     -12.448  32.655  -2.617  1.00 82.38           O
ANISOU 1288  O   HIS A  98     7712  12927  10661   -641   -740    947       O
ATOM   1289  CB  HIS A  98     -11.434  35.608  -3.102  1.00 77.12           C
ANISOU 1289  CB  HIS A  98     7231  11856  10214   -559  -1318    800       C
ATOM   1290  CG  HIS A  98      -9.929  35.713  -3.067  1.00 78.73           C
ANISOU 1290  CG  HIS A  98     7411  11820  10684   -720  -1672    985       C
ATOM   1291  ND1 HIS A  98      -9.159  36.768  -2.588  1.00 78.19           N
ANISOU 1291  ND1 HIS A  98     7582  11529  10598   -715  -2037    954       N
ATOM   1292  CD2 HIS A  98      -9.082  34.747  -3.531  1.00 77.59           C
ANISOU 1292  CD2 HIS A  98     7032  11620  10830   -891  -1718   1203       C
ATOM   1293  CE1 HIS A  98      -7.863  36.436  -2.770  1.00 79.90           C
ANISOU 1293  CE1 HIS A  98     7709  11562  11087   -876  -2292   1144       C
ATOM   1294  NE2 HIS A  98      -7.810  35.221  -3.340  1.00 78.73           N
ANISOU 1294  NE2 HIS A  98     7275  11511  11129   -985  -2105   1299       N
ATOM   1295  H   HIS A  98     -11.331  36.535  -0.745  1.00100.34           H
ATOM   1296  HA  HIS A  98     -13.153  34.938  -2.042  1.00 96.79           H
ATOM   1297  HB2 HIS A  98     -11.693  35.036  -3.993  1.00 92.54           H
ATOM   1298  HB3 HIS A  98     -11.872  36.602  -3.210  1.00 92.54           H
ATOM   1299  HD2 HIS A  98      -9.344  33.792  -3.970  1.00 93.11           H
ATOM   1300  HE1 HIS A  98      -6.987  37.030  -2.520  1.00 95.88           H
ATOM   1301  HE2 HIS A  98      -6.940  34.716  -3.579  1.00 94.48           H
ATOM   1302  HD1 HIS A  98      -9.499  37.652  -2.214  1.00  0.00           H
ATOM   1303  N   LYS A  99     -10.642  32.944  -1.306  1.00 79.10           N
ANISOU 1303  N   LYS A  99     7591  12146  10317   -799  -1357   1113       N
ATOM   1304  CA  LYS A  99     -10.342  31.508  -1.151  1.00 76.10           C
ANISOU 1304  CA  LYS A  99     7030  11820  10064   -944  -1268   1306       C
ATOM   1305  C   LYS A  99     -11.361  30.880  -0.197  1.00 75.62           C
ANISOU 1305  C   LYS A  99     7124  11941   9667   -884  -1048   1249       C
ATOM   1306  O   LYS A  99     -11.354  31.162   1.007  1.00 77.48           O
ANISOU 1306  O   LYS A  99     7669  12110   9659   -873  -1220   1231       O
ATOM   1307  H   LYS A  99     -10.115  33.606  -0.759  1.00 94.92           H
ATOM   1308  CB  LYS A  99      -8.855  31.261  -0.776  1.00  0.00           C
ATOM   1309  CG  LYS A  99      -8.393  31.773   0.602  1.00  0.00           C
ATOM   1310  CD  LYS A  99      -8.451  30.749   1.754  1.00  0.00           C
ATOM   1311  CE  LYS A  99      -8.683  31.414   3.123  1.00  0.00           C
ATOM   1312  NZ  LYS A  99      -9.976  32.149   3.186  1.00  0.00           N
ATOM   1313  HA  LYS A  99     -10.493  31.023  -2.118  1.00  0.00           H
ATOM   1314  HB2 LYS A  99      -8.244  31.764  -1.530  1.00  0.00           H
ATOM   1315  HB3 LYS A  99      -8.634  30.196  -0.855  1.00  0.00           H
ATOM   1316  HG2 LYS A  99      -7.361  32.118   0.520  1.00  0.00           H
ATOM   1317  HG3 LYS A  99      -8.997  32.637   0.843  1.00  0.00           H
ATOM   1318  HD2 LYS A  99      -7.499  30.208   1.781  1.00  0.00           H
ATOM   1319  HD3 LYS A  99      -9.227  30.004   1.577  1.00  0.00           H
ATOM   1320  HE2 LYS A  99      -8.673  30.629   3.880  1.00  0.00           H
ATOM   1321  HE3 LYS A  99      -7.854  32.093   3.336  1.00  0.00           H
ATOM   1322  HZ1 LYS A  99     -10.462  31.999   4.058  1.00  0.00           H
ATOM   1323  HZ2 LYS A  99      -9.857  33.147   3.035  1.00  0.00           H
ATOM   1324  HZ3 LYS A  99     -10.588  31.839   2.432  1.00  0.00           H
ATOM   1325  N   PHE A 100     -12.218  30.020  -0.719  1.00 74.41           N
ANISOU 1325  N   PHE A 100     6758  12017   9499   -841   -665   1218       N
ATOM   1326  CA  PHE A 100     -12.966  29.062   0.096  1.00 71.88           C
ANISOU 1326  CA  PHE A 100     6528  11877   8905   -804   -427   1192       C
ATOM   1327  C   PHE A 100     -12.039  27.886   0.434  1.00 75.71           C
ANISOU 1327  C   PHE A 100     6898  12345   9524   -975   -459   1413       C
ATOM   1328  O   PHE A 100     -11.027  27.690  -0.237  1.00 73.27           O
ANISOU 1328  O   PHE A 100     6389  11912   9539  -1118   -613   1583       O
ATOM   1329  CB  PHE A 100     -14.230  28.620  -0.661  1.00 72.05           C
ANISOU 1329  CB  PHE A 100     6353  12147   8874   -696     -5   1078       C
ATOM   1330  CG  PHE A 100     -15.356  29.627  -0.529  1.00 72.40           C
ANISOU 1330  CG  PHE A 100     6600  12265   8645   -502     88    836       C
ATOM   1331  CD1 PHE A 100     -15.284  30.875  -1.182  1.00 70.26           C
ANISOU 1331  CD1 PHE A 100     6346  11890   8458   -432    -48    731       C
ATOM   1332  CD2 PHE A 100     -16.415  29.366   0.362  1.00 70.51           C
ANISOU 1332  CD2 PHE A 100     6530  12197   8064   -390    317    713       C
ATOM   1333  CE1 PHE A 100     -16.243  31.867  -0.916  1.00 68.04           C
ANISOU 1333  CE1 PHE A 100     6251  11677   7925   -254     38    507       C
ATOM   1334  CE2 PHE A 100     -17.373  30.358   0.623  1.00 72.11           C
ANISOU 1334  CE2 PHE A 100     6917  12468   8015   -211    406    490       C
ATOM   1335  CZ  PHE A 100     -17.284  31.605  -0.011  1.00 71.35           C
ANISOU 1335  CZ  PHE A 100     6837  12268   8005   -143    266    386       C
ATOM   1336  H   PHE A 100     -12.108  29.796  -1.703  1.00 89.30           H
ATOM   1337  HA  PHE A 100     -13.278  29.532   1.032  1.00 86.25           H
ATOM   1338  HB2 PHE A 100     -14.002  28.456  -1.715  1.00 86.45           H
ATOM   1339  HB3 PHE A 100     -14.574  27.668  -0.253  1.00 86.45           H
ATOM   1340  HD1 PHE A 100     -14.461  31.097  -1.845  1.00 84.31           H
ATOM   1341  HD2 PHE A 100     -16.477  28.425   0.890  1.00 84.61           H
ATOM   1342  HE1 PHE A 100     -16.163  32.847  -1.365  1.00 81.65           H
ATOM   1343  HE2 PHE A 100     -18.156  30.176   1.343  1.00 86.54           H
ATOM   1344  HZ  PHE A 100     -18.005  32.372   0.218  1.00 85.62           H
ATOM   1345  N   LEU A 101     -12.396  27.047   1.408  1.00 78.94           N
ANISOU 1345  N   LEU A 101     7437  12879   9678   -960   -311   1412       N
ATOM   1346  CA  LEU A 101     -11.762  25.734   1.578  1.00 78.92           C
ANISOU 1346  CA  LEU A 101     7321  12886   9777  -1112   -300   1612       C
ATOM   1347  C   LEU A 101     -12.718  24.769   2.282  1.00 77.76           C
ANISOU 1347  C   LEU A 101     7269  12944   9331  -1049    -15   1561       C
ATOM   1348  O   LEU A 101     -13.357  25.141   3.264  1.00 83.39           O
ANISOU 1348  O   LEU A 101     8271  13708   9707   -915     18   1400       O
ATOM   1349  CB  LEU A 101     -10.433  25.880   2.352  1.00 80.17           C
ANISOU 1349  CB  LEU A 101     7672  12809   9979  -1230   -707   1741       C
ATOM   1350  CG  LEU A 101      -9.509  24.650   2.249  1.00 79.82           C
ANISOU 1350  CG  LEU A 101     7434  12720  10172  -1420   -763   1982       C
ATOM   1351  CD1 LEU A 101      -8.922  24.476   0.845  1.00 76.10           C
ANISOU 1351  CD1 LEU A 101     6577  12219  10120  -1519   -730   2100       C
ATOM   1352  CD2 LEU A 101      -8.326  24.800   3.203  1.00 82.81           C
ANISOU 1352  CD2 LEU A 101     8064  12879  10523  -1514  -1157   2083       C
ATOM   1353  H   LEU A 101     -13.232  27.238   1.949  1.00 94.73           H
ATOM   1354  HA  LEU A 101     -11.553  25.343   0.583  1.00 94.70           H
ATOM   1355  HB2 LEU A 101      -9.885  26.750   1.985  1.00 96.20           H
ATOM   1356  HB3 LEU A 101     -10.669  26.060   3.402  1.00 96.20           H
ATOM   1357  HG  LEU A 101     -10.059  23.749   2.520  1.00 95.78           H
ATOM   1358 HD11 LEU A 101      -9.709  24.274   0.123  1.00  0.00           H
ATOM   1359 HD12 LEU A 101      -8.222  23.641   0.835  1.00  0.00           H
ATOM   1360 HD13 LEU A 101      -8.391  25.383   0.551  1.00  0.00           H
ATOM   1361 HD21 LEU A 101      -8.685  24.859   4.229  1.00  0.00           H
ATOM   1362 HD22 LEU A 101      -7.660  23.942   3.111  1.00  0.00           H
ATOM   1363 HD23 LEU A 101      -7.769  25.707   2.964  1.00  0.00           H
ATOM   1364  N   TYR A 102     -12.819  23.530   1.806  1.00 72.23           N
ANISOU 1364  N   TYR A 102     6325  12360   8760  -1149    188   1701       N
ATOM   1365  CA  TYR A 102     -13.643  22.508   2.454  1.00 72.98           C
ANISOU 1365  CA  TYR A 102     6446  12665   8619  -1101    499   1671       C
ATOM   1366  C   TYR A 102     -12.876  21.714   3.532  1.00 71.90           C
ANISOU 1366  C   TYR A 102     6442  12472   8404  -1217    368   1824       C
ATOM   1367  O   TYR A 102     -11.693  21.389   3.372  1.00 70.28           O
ANISOU 1367  O   TYR A 102     6135  12124   8444  -1373    151   2006       O
ATOM   1368  CB  TYR A 102     -14.287  21.626   1.378  1.00 72.05           C
ANISOU 1368  CB  TYR A 102     5944  12742   8692  -1117    864   1705       C
ATOM   1369  CG  TYR A 102     -15.108  20.477   1.924  1.00 74.71           C
ANISOU 1369  CG  TYR A 102     6262  13287   8839  -1098   1180   1711       C
ATOM   1370  CD1 TYR A 102     -16.377  20.712   2.491  1.00 75.25           C
ANISOU 1370  CD1 TYR A 102     6511  13509   8572   -936   1403   1526       C
ATOM   1371  CD2 TYR A 102     -14.582  19.171   1.883  1.00 73.36           C
ANISOU 1371  CD2 TYR A 102     5984  13057   8833  -1207   1219   1854       C
ATOM   1372  CE1 TYR A 102     -17.121  19.637   3.016  1.00 76.12           C
ANISOU 1372  CE1 TYR A 102     6603  13807   8512   -919   1696   1532       C
ATOM   1373  CE2 TYR A 102     -15.331  18.095   2.390  1.00 73.74           C
ANISOU 1373  CE2 TYR A 102     6174  13104   8742  -1133   1423   1774       C
ATOM   1374  CZ  TYR A 102     -16.602  18.327   2.961  1.00 74.81           C
ANISOU 1374  CZ  TYR A 102     6427  13437   8560  -1000   1656   1626       C
ATOM   1375  OH  TYR A 102     -17.327  17.278   3.429  1.00 76.33           O
ANISOU 1375  OH  TYR A 102     6769  13576   8657   -930   1830   1542       O
ATOM   1376  H   TYR A 102     -12.300  23.273   0.970  1.00 86.68           H
ATOM   1377  HA  TYR A 102     -14.463  23.011   2.966  1.00 87.58           H
ATOM   1378  HB2 TYR A 102     -14.935  22.251   0.760  1.00 86.47           H
ATOM   1379  HB3 TYR A 102     -13.509  21.223   0.730  1.00 86.47           H
ATOM   1380  HD1 TYR A 102     -16.793  21.712   2.514  1.00 90.30           H
ATOM   1381  HD2 TYR A 102     -13.606  18.996   1.453  1.00 88.03           H
ATOM   1382  HE1 TYR A 102     -18.097  19.802   3.450  1.00 91.34           H
ATOM   1383  HE2 TYR A 102     -14.932  17.097   2.344  1.00 88.49           H
ATOM   1384  HH  TYR A 102     -16.917  16.443   3.217  1.00 91.60           H
ATOM   1385  N   TYR A 103     -13.602  21.271   4.560  1.00 75.40           N
ANISOU 1385  N   TYR A 103     7114  13030   8506  -1138    505   1748       N
ATOM   1386  CA  TYR A 103     -13.126  20.406   5.640  1.00 79.47           C
ANISOU 1386  CA  TYR A 103     7786  13511   8896  -1228    409   1874       C
ATOM   1387  C   TYR A 103     -14.132  19.258   5.829  1.00 77.94           C
ANISOU 1387  C   TYR A 103     7505  13556   8551  -1196    794   1869       C
ATOM   1388  O   TYR A 103     -15.263  19.490   6.242  1.00 80.68           O
ANISOU 1388  O   TYR A 103     8028  14035   8592  -1050    988   1706       O
ATOM   1389  CB  TYR A 103     -12.950  21.222   6.939  1.00 82.98           C
ANISOU 1389  CB  TYR A 103     8669  13824   9036  -1160    136   1788       C
ATOM   1390  CG  TYR A 103     -12.121  22.492   6.809  1.00 83.31           C
ANISOU 1390  CG  TYR A 103     8821  13635   9196  -1169   -237   1766       C
ATOM   1391  CD1 TYR A 103     -10.727  22.477   7.022  1.00 85.58           C
ANISOU 1391  CD1 TYR A 103     9125  13711   9681  -1318   -584   1933       C
ATOM   1392  CD2 TYR A 103     -12.759  23.703   6.477  1.00 84.54           C
ANISOU 1392  CD2 TYR A 103     9065  13783   9272  -1027   -243   1577       C
ATOM   1393  CE1 TYR A 103      -9.979  23.664   6.875  1.00 86.00           C
ANISOU 1393  CE1 TYR A 103     9277  13549   9850  -1328   -926   1914       C
ATOM   1394  CE2 TYR A 103     -12.018  24.889   6.325  1.00 86.36           C
ANISOU 1394  CE2 TYR A 103     9397  13801   9614  -1035   -583   1557       C
ATOM   1395  CZ  TYR A 103     -10.623  24.869   6.520  1.00 87.84           C
ANISOU 1395  CZ  TYR A 103     9596  13778   9999  -1186   -923   1726       C
ATOM   1396  OH  TYR A 103      -9.902  26.011   6.383  1.00 89.66           O
ANISOU 1396  OH  TYR A 103     9924  13794  10348  -1194  -1261   1707       O
ATOM   1397  H   TYR A 103     -14.583  21.512   4.584  1.00 90.48           H
ATOM   1398  HA  TYR A 103     -12.161  19.978   5.372  1.00 95.36           H
ATOM   1399  HB2 TYR A 103     -13.936  21.508   7.310  1.00 99.58           H
ATOM   1400  HB3 TYR A 103     -12.504  20.583   7.701  1.00 99.58           H
ATOM   1401  HD1 TYR A 103     -10.233  21.560   7.300  1.00102.70           H
ATOM   1402  HD2 TYR A 103     -13.828  23.728   6.332  1.00101.45           H
ATOM   1403  HE1 TYR A 103      -8.911  23.673   7.029  1.00103.20           H
ATOM   1404  HE2 TYR A 103     -12.526  25.804   6.049  1.00103.63           H
ATOM   1405  HH  TYR A 103     -10.466  26.755   6.166  1.00107.59           H
ATOM   1406  N   ASP A 104     -13.746  18.016   5.515  1.00 71.01           N
ANISOU 1406  N   ASP A 104     6356  12733   7889  -1333    907   2046       N
ATOM   1407  CA  ASP A 104     -14.580  16.837   5.766  1.00 67.40           C
ANISOU 1407  CA  ASP A 104     5819  12488   7300  -1321   1250   2065       C
ATOM   1408  C   ASP A 104     -14.750  16.620   7.282  1.00 71.69           C
ANISOU 1408  C   ASP A 104     6737  13033   7469  -1270   1196   2025       C
ATOM   1409  O   ASP A 104     -13.838  16.115   7.940  1.00 70.81           O
ANISOU 1409  O   ASP A 104     6770  12786   7348  -1375    946   2154       O
ATOM   1410  CB  ASP A 104     -13.957  15.629   5.042  1.00 69.64           C
ANISOU 1410  CB  ASP A 104     5786  12793   7881  -1495   1311   2284       C
ATOM   1411  CG  ASP A 104     -14.714  14.321   5.267  1.00 69.97           C
ANISOU 1411  CG  ASP A 104     5937  12754   7895  -1363   1544   2130       C
ATOM   1412  OD1 ASP A 104     -15.832  14.359   5.826  1.00 70.21           O
ANISOU 1412  OD1 ASP A 104     6107  12986   7583  -1310   1722   2092       O
ATOM   1413  OD2 ASP A 104     -14.307  13.276   4.706  1.00 72.97           O
ANISOU 1413  OD2 ASP A 104     6319  12821   8587  -1304   1533   2019       O
ATOM   1414  H   ASP A 104     -12.849  17.871   5.067  1.00 85.21           H
ATOM   1415  HA  ASP A 104     -15.574  17.011   5.354  1.00 80.87           H
ATOM   1416  HB2 ASP A 104     -13.933  15.829   3.975  1.00 83.57           H
ATOM   1417  HB3 ASP A 104     -12.936  15.499   5.381  1.00 83.57           H
ATOM   1418  N   GLU A 105     -15.922  16.970   7.824  1.00 75.28           N
ANISOU 1418  N   GLU A 105     7352  13637   7614  -1108   1428   1844       N
ATOM   1419  CA  GLU A 105     -16.263  16.962   9.260  1.00 75.35           C
ANISOU 1419  CA  GLU A 105     7734  13649   7247  -1042   1385   1789       C
ATOM   1420  C   GLU A 105     -15.928  15.626   9.955  1.00 76.19           C
ANISOU 1420  C   GLU A 105     7822  13791   7335  -1161   1432   1963       C
ATOM   1421  O   GLU A 105     -15.245  15.612  10.978  1.00 75.60           O
ANISOU 1421  O   GLU A 105     8037  13612   7078  -1188   1218   2009       O
ATOM   1422  H   GLU A 105     -16.533  17.525   7.236  1.00 90.34           H
ATOM   1423  CB  GLU A 105     -17.759  17.319   9.428  1.00  0.00           C
ATOM   1424  CG  GLU A 105     -18.063  18.766   8.974  1.00  0.00           C
ATOM   1425  CD  GLU A 105     -19.559  19.148   8.942  1.00  0.00           C
ATOM   1426  OE2 GLU A 105     -19.888  20.259   8.458  1.00  0.00           O
ATOM   1427  OE1 GLU A 105     -20.414  18.292   9.247  1.00  0.00           O
ATOM   1428  HA  GLU A 105     -15.690  17.736   9.765  1.00  0.00           H
ATOM   1429  HB2 GLU A 105     -18.035  17.209  10.479  1.00  0.00           H
ATOM   1430  HB3 GLU A 105     -18.354  16.612   8.845  1.00  0.00           H
ATOM   1431  HG2 GLU A 105     -17.530  19.446   9.639  1.00  0.00           H
ATOM   1432  HG3 GLU A 105     -17.668  18.905   7.969  1.00  0.00           H
ATOM   1433  N   LYS A 106     -16.105  14.502   9.248  1.00 75.54           N
ANISOU 1433  N   LYS A 106     7404  13854   7443  -1234   1706   2062       N
ATOM   1434  CA  LYS A 106     -15.759  13.152   9.732  1.00 77.78           C
ANISOU 1434  CA  LYS A 106     7652  14186   7713  -1345   1777   2226       C
ATOM   1435  C   LYS A 106     -14.247  12.922   9.893  1.00 78.50           C
ANISOU 1435  C   LYS A 106     7779  14064   7982  -1512   1408   2415       C
ATOM   1436  O   LYS A 106     -13.825  12.083  10.682  1.00 81.87           O
ANISOU 1436  O   LYS A 106     8375  14460   8273  -1573   1326   2512       O
ATOM   1437  H   LYS A 106     -16.464  14.615   8.310  1.00 90.65           H
ATOM   1438  CB  LYS A 106     -16.369  12.098   8.789  1.00  0.00           C
ATOM   1439  CG  LYS A 106     -17.913  12.053   8.794  1.00  0.00           C
ATOM   1440  CD  LYS A 106     -18.693  12.982   7.839  1.00  0.00           C
ATOM   1441  CE  LYS A 106     -18.881  12.421   6.421  1.00  0.00           C
ATOM   1442  NZ  LYS A 106     -17.693  12.622   5.563  1.00  0.00           N
ATOM   1443  HA  LYS A 106     -16.175  13.021  10.734  1.00  0.00           H
ATOM   1444  HB2 LYS A 106     -16.022  11.122   9.140  1.00  0.00           H
ATOM   1445  HB3 LYS A 106     -15.987  12.237   7.778  1.00  0.00           H
ATOM   1446  HG2 LYS A 106     -18.248  12.259   9.812  1.00  0.00           H
ATOM   1447  HG3 LYS A 106     -18.214  11.029   8.571  1.00  0.00           H
ATOM   1448  HD2 LYS A 106     -19.696  13.088   8.260  1.00  0.00           H
ATOM   1449  HD3 LYS A 106     -18.264  13.985   7.807  1.00  0.00           H
ATOM   1450  HE2 LYS A 106     -19.738  12.927   5.966  1.00  0.00           H
ATOM   1451  HE3 LYS A 106     -19.119  11.357   6.491  1.00  0.00           H
ATOM   1452  HZ1 LYS A 106     -17.800  12.258   4.630  1.00  0.00           H
ATOM   1453  HZ2 LYS A 106     -17.449  13.613   5.492  1.00  0.00           H
ATOM   1454  HZ3 LYS A 106     -16.842  12.267   5.979  1.00  0.00           H
ATOM   1455  N   LYS A 107     -13.420  13.626   9.120  1.00 72.96           N
ANISOU 1455  N   LYS A 107     6923  13215   7584  -1586   1183   2471       N
ATOM   1456  CA  LYS A 107     -11.949  13.559   9.149  1.00 72.54           C
ANISOU 1456  CA  LYS A 107     6870  12954   7738  -1750    834   2654       C
ATOM   1457  C   LYS A 107     -11.315  14.588  10.088  1.00 78.85           C
ANISOU 1457  C   LYS A 107     8045  13544   8369  -1720    448   2606       C
ATOM   1458  O   LYS A 107     -10.104  14.519  10.290  1.00 77.17           O
ANISOU 1458  O   LYS A 107     7868  13144   8308  -1849    131   2749       O
ATOM   1459  CB  LYS A 107     -11.416  13.710   7.722  1.00 70.26           C
ANISOU 1459  CB  LYS A 107     6223  12602   7873  -1850    779   2748       C
ATOM   1460  CG  LYS A 107     -11.796  12.506   6.857  1.00 62.69           C
ANISOU 1460  CG  LYS A 107     4969  11714   7136  -1846   1066   2754       C
ATOM   1461  CD  LYS A 107     -11.261  12.719   5.446  1.00 59.68           C
ANISOU 1461  CD  LYS A 107     4490  11042   7144  -1770    940   2635       C
ATOM   1462  CE  LYS A 107     -11.733  11.588   4.545  1.00 60.00           C
ANISOU 1462  CE  LYS A 107     4604  10811   7383  -1597   1075   2397       C
ATOM   1463  NZ  LYS A 107     -11.256  11.865   3.184  1.00 78.92           N
ANISOU 1463  NZ  LYS A 107     6991  12924  10070  -1514    997   2249       N
ATOM   1464  H   LYS A 107     -13.845  14.355   8.555  1.00 87.55           H
ATOM   1465  HA  LYS A 107     -11.640  12.586   9.533  1.00 87.05           H
ATOM   1466  HB2 LYS A 107     -11.834  14.611   7.281  1.00 84.32           H
ATOM   1467  HB3 LYS A 107     -10.330  13.806   7.738  1.00 84.32           H
ATOM   1468  HG2 LYS A 107     -11.366  11.596   7.276  1.00 75.22           H
ATOM   1469  HG3 LYS A 107     -12.881  12.404   6.818  1.00 75.22           H
ATOM   1470  HD2 LYS A 107     -11.637  13.664   5.052  1.00 71.62           H
ATOM   1471  HD3 LYS A 107     -10.172  12.753   5.462  1.00 71.62           H
ATOM   1472  HE2 LYS A 107     -11.338  10.639   4.912  1.00 72.00           H
ATOM   1473  HE3 LYS A 107     -12.828  11.553   4.565  1.00 72.00           H
ATOM   1474  HZ1 LYS A 107     -11.501  11.164   2.502  1.00 94.70           H
ATOM   1475  HZ2 LYS A 107     -11.619  12.747   2.850  1.00 94.70           H
ATOM   1476  HZ3 LYS A 107     -10.239  11.930   3.164  1.00 94.70           H
ATOM   1477  N   MET A 108     -12.103  15.478  10.700  1.00 91.44           N
ANISOU 1477  N   MET A 108     9919  15164   9659  -1554    465   2407       N
ATOM   1478  CA  MET A 108     -11.628  16.442  11.707  1.00100.08           C
ANISOU 1478  CA  MET A 108    11391  16067  10566  -1517    107   2353       C
ATOM   1479  C   MET A 108     -10.939  15.744  12.895  1.00100.84           C
ANISOU 1479  C   MET A 108    11705  16087  10523  -1602    -60   2479       C
ATOM   1480  O   MET A 108      -9.800  16.096  13.210  1.00103.48           O
ANISOU 1480  O   MET A 108    12260  16213  10846  -1647   -432   2521       O
ATOM   1481  CB  MET A 108     -12.802  17.314  12.184  1.00104.03           C
ANISOU 1481  CB  MET A 108    12159  16643  10723  -1316    212   2117       C
ATOM   1482  CG  MET A 108     -13.344  18.243  11.084  1.00102.75           C
ANISOU 1482  CG  MET A 108    11832  16538  10672  -1217    339   1972       C
ATOM   1483  SD  MET A 108     -12.434  19.797  10.878  1.00105.41           S
ANISOU 1483  SD  MET A 108    12320  16620  11110  -1199    -84   1906       S
ATOM   1484  CE  MET A 108     -13.109  20.680  12.314  1.00108.31           C
ANISOU 1484  CE  MET A 108    13202  16953  10996  -1035   -201   1724       C
ATOM   1485  H   MET A 108     -13.090  15.484  10.470  1.00109.73           H
ATOM   1486  HA  MET A 108     -10.889  17.101  11.254  1.00120.09           H
ATOM   1487  HB2 MET A 108     -13.607  16.672  12.538  1.00124.83           H
ATOM   1488  HB3 MET A 108     -12.482  17.922  13.030  1.00124.83           H
ATOM   1489  HG2 MET A 108     -13.364  17.717  10.129  1.00123.30           H
ATOM   1490  HG3 MET A 108     -14.375  18.501  11.333  1.00123.30           H
ATOM   1491  HE1 MET A 108     -12.686  21.679  12.361  1.00129.97           H
ATOM   1492  HE2 MET A 108     -14.193  20.756  12.224  1.00129.97           H
ATOM   1493  HE3 MET A 108     -12.861  20.149  13.232  1.00129.97           H
ATOM   1494  N   ALA A 109     -11.477  14.605  13.341  1.00 87.95           N
ANISOU 1494  N   ALA A 109    10014  14617   8786  -1623    207   2542       N
ATOM   1495  CA  ALA A 109     -10.931  13.788  14.434  1.00 91.11           C
ANISOU 1495  CA  ALA A 109    10623  14958   9036  -1697     73   2659       C
ATOM   1496  C   ALA A 109      -9.505  13.249  14.164  1.00 96.29           C
ANISOU 1496  C   ALA A 109    11136  15439  10010  -1891   -211   2874       C
ATOM   1497  O   ALA A 109      -8.652  13.271  15.047  1.00 98.44           O
ANISOU 1497  O   ALA A 109    11654  15539  10211  -1946   -532   2942       O
ATOM   1498  CB  ALA A 109     -11.908  12.626  14.666  1.00 91.17           C
ANISOU 1498  CB  ALA A 109    10566  15189   8885  -1678    448   2680       C
ATOM   1499  H   ALA A 109     -12.380  14.336  12.978  1.00105.54           H
ATOM   1500  HA  ALA A 109     -10.887  14.393  15.342  1.00109.33           H
ATOM   1501  HB1 ALA A 109     -11.572  12.028  15.515  1.00109.40           H
ATOM   1502  HB2 ALA A 109     -12.907  13.007  14.881  1.00109.40           H
ATOM   1503  HB3 ALA A 109     -11.952  11.984  13.783  1.00109.40           H
ATOM   1504  N   ASN A 110      -9.205  12.878  12.913  0.50 99.76           N
ANISOU 1504  N   ASN A 110    11178  15920  10806  -1996    -97   2984       N
ATOM   1505  CA  ASN A 110      -7.888  12.356  12.514  0.50102.03           C
ANISOU 1505  CA  ASN A 110    11301  16053  11413  -2184   -340   3196       C
ATOM   1506  C   ASN A 110      -6.756  13.401  12.631  0.50108.29           C
ANISOU 1506  C   ASN A 110    12294  16584  12267  -2214   -789   3201       C
ATOM   1507  O   ASN A 110      -5.583  13.009  12.523  0.50107.36           O
ANISOU 1507  O   ASN A 110    12301  16309  12181  -2323  -1071   3332       O
ATOM   1508  H   ASN A 110      -9.942  12.895  12.234  0.50119.71           H
ATOM   1509  CB  ASN A 110      -7.938  11.895  11.046  1.00  0.00           C
ATOM   1510  CG  ASN A 110      -8.927  10.804  10.705  1.00  0.00           C
ATOM   1511  OD1 ASN A 110      -9.400  10.038  11.517  1.00  0.00           O
ATOM   1512  ND2 ASN A 110      -9.235  10.656   9.437  1.00  0.00           N
ATOM   1513  HA  ASN A 110      -7.635  11.510  13.158  0.50  0.00           H
ATOM   1514  HB2 ASN A 110      -8.177  12.760  10.433  1.00  0.00           H
ATOM   1515  HB3 ASN A 110      -6.949  11.541  10.760  1.00  0.00           H
ATOM   1516 HD21 ASN A 110      -8.960  11.390   8.800  1.00  0.00           H
ATOM   1517 HD22 ASN A 110     -10.003  10.024   9.291  1.00  0.00           H
ATOM   1518  N   PHE A 111      -7.052  14.696  12.577  1.00120.97           N
ANISOU 1518  N   PHE A 111    13934  18137  13892  -2118   -863   3058       N
ATOM   1519  CA  PHE A 111      -6.076  15.794  12.530  1.00120.07           C
ANISOU 1519  CA  PHE A 111    14001  17777  13844  -2134  -1278   3045       C
ATOM   1520  C   PHE A 111      -6.446  16.911  13.517  1.00124.35           C
ANISOU 1520  C   PHE A 111    14952  18299  13995  -1968  -1358   2853       C
ATOM   1521  O   PHE A 111      -6.576  18.086  13.133  1.00125.50           O
ANISOU 1521  O   PHE A 111    15126  18526  14034  -1828  -1218   2676       O
ATOM   1522  CB  PHE A 111      -5.888  16.304  11.084  1.00113.21           C
ANISOU 1522  CB  PHE A 111    12861  16846  13307  -2156  -1323   3036       C
ATOM   1523  CG  PHE A 111      -4.986  15.484  10.182  1.00107.10           C
ANISOU 1523  CG  PHE A 111    11718  16037  12939  -2333  -1332   3240       C
ATOM   1524  CD1 PHE A 111      -5.507  14.388   9.473  1.00103.68           C
ANISOU 1524  CD1 PHE A 111    10992  15798  12604  -2379   -990   3318       C
ATOM   1525  CD2 PHE A 111      -3.630  15.839  10.011  1.00104.15           C
ANISOU 1525  CD2 PHE A 111    11287  15435  12849  -2451  -1682   3354       C
ATOM   1526  CE1 PHE A 111      -4.681  13.651   8.605  1.00100.16           C
ANISOU 1526  CE1 PHE A 111    10208  15320  12529  -2539   -996   3505       C
ATOM   1527  CE2 PHE A 111      -2.801  15.089   9.153  1.00100.44           C
ANISOU 1527  CE2 PHE A 111    10478  14932  12752  -2612  -1687   3543       C
ATOM   1528  CZ  PHE A 111      -3.328  13.998   8.444  1.00 99.25           C
ANISOU 1528  CZ  PHE A 111    10041  14977  12692  -2655  -1344   3618       C
ATOM   1529  H   PHE A 111      -8.043  14.938  12.629  1.00145.16           H
ATOM   1530  HA  PHE A 111      -5.116  15.414  12.869  1.00144.08           H
ATOM   1531  HB2 PHE A 111      -6.865  16.427  10.605  1.00135.85           H
ATOM   1532  HB3 PHE A 111      -5.440  17.296  11.117  1.00135.85           H
ATOM   1533  HD1 PHE A 111      -6.543  14.113   9.607  1.00124.42           H
ATOM   1534  HD2 PHE A 111      -3.216  16.685  10.544  1.00124.98           H
ATOM   1535  HE1 PHE A 111      -5.079  12.801   8.078  1.00120.19           H
ATOM   1536  HE2 PHE A 111      -1.752  15.337   9.058  1.00120.53           H
ATOM   1537  HZ  PHE A 111      -2.689  13.410   7.797  1.00119.10           H
ATOM   1538  N   GLN A 112      -6.412  16.608  14.813  1.00128.81           N
ANISOU 1538  N   GLN A 112    15838  18755  14348  -1985  -1587   2888       N
ATOM   1539  CA  GLN A 112      -6.892  17.469  15.906  1.00132.61           C
ANISOU 1539  CA  GLN A 112    16729  19212  14445  -1830  -1675   2714       C
ATOM   1540  C   GLN A 112      -6.338  18.911  15.923  1.00129.92           C
ANISOU 1540  C   GLN A 112    16535  18668  14162  -1791  -2013   2628       C
ATOM   1541  O   GLN A 112      -7.002  19.820  16.423  1.00135.76           O
ANISOU 1541  O   GLN A 112    17490  19428  14664  -1634  -1997   2438       O
ATOM   1542  CB  GLN A 112      -6.567  16.789  17.252  1.00133.68           C
ANISOU 1542  CB  GLN A 112    17160  19297  14333  -1860  -1808   2784       C
ATOM   1543  CG  GLN A 112      -7.472  17.275  18.402  1.00135.24           C
ANISOU 1543  CG  GLN A 112    17743  19563  14078  -1687  -1738   2607       C
ATOM   1544  CD  GLN A 112      -8.931  16.839  18.243  1.00134.41           C
ANISOU 1544  CD  GLN A 112    17545  19732  13794  -1582  -1271   2513       C
ATOM   1545  OE1 GLN A 112      -9.304  16.091  17.357  1.00132.33           O
ANISOU 1545  OE1 GLN A 112    16947  19610  13725  -1652  -1002   2603       O
ATOM   1546  NE2 GLN A 112      -9.846  17.356  19.026  1.00136.33           N
ANISOU 1546  NE2 GLN A 112    18081  20048  13668  -1411  -1173   2332       N
ATOM   1547  H   GLN A 112      -6.327  15.620  15.031  1.00154.57           H
ATOM   1548  HA  GLN A 112      -7.970  17.536  15.794  1.00159.13           H
ATOM   1549  HB2 GLN A 112      -6.673  15.707  17.168  1.00160.41           H
ATOM   1550  HB3 GLN A 112      -5.525  16.995  17.514  1.00160.41           H
ATOM   1551  HG2 GLN A 112      -7.093  16.873  19.343  1.00162.28           H
ATOM   1552  HG3 GLN A 112      -7.431  18.362  18.477  1.00162.28           H
ATOM   1553 HE21 GLN A 112      -9.606  17.958  19.790  1.00163.59           H
ATOM   1554 HE22 GLN A 112     -10.772  16.994  18.884  1.00163.59           H
ATOM   1555  N   ASN A 113      -5.117  19.151  15.426  0.80116.90           N
ANISOU 1555  N   ASN A 113    14768  16819  12830  -1931  -2321   2765       N
ATOM   1556  CA  ASN A 113      -4.508  20.490  15.412  0.80115.68           C
ANISOU 1556  CA  ASN A 113    14774  16448  12732  -1906  -2681   2700       C
ATOM   1557  C   ASN A 113      -5.283  21.475  14.519  0.80115.66           C
ANISOU 1557  C   ASN A 113    14661  16507  12779  -1790  -2546   2537       C
ATOM   1558  O   ASN A 113      -5.511  22.605  14.955  0.80117.09           O
ANISOU 1558  O   ASN A 113    15082  16588  12820  -1684  -2728   2394       O
ATOM   1559  H   ASN A 113      -4.599  18.376  15.038  0.80140.28           H
ATOM   1560  CB  ASN A 113      -3.036  20.370  14.974  1.00  0.00           C
ATOM   1561  CG  ASN A 113      -2.170  21.625  15.074  1.00  0.00           C
ATOM   1562  OD1 ASN A 113      -1.011  21.581  14.719  1.00  0.00           O
ATOM   1563  ND2 ASN A 113      -2.633  22.762  15.536  1.00  0.00           N
ATOM   1564  HA  ASN A 113      -4.534  20.877  16.431  0.80  0.00           H
ATOM   1565  HB2 ASN A 113      -2.553  19.619  15.601  1.00  0.00           H
ATOM   1566  HB3 ASN A 113      -2.994  20.025  13.940  1.00  0.00           H
ATOM   1567 HD21 ASN A 113      -3.611  22.922  15.706  1.00  0.00           H
ATOM   1568 HD22 ASN A 113      -1.952  23.503  15.585  1.00  0.00           H
ATOM   1569  N   PHE A 114      -5.755  21.029  13.347  0.80113.32           N
ANISOU 1569  N   PHE A 114    14005  16372  12681  -1806  -2231   2557       N
ATOM   1570  CA  PHE A 114      -6.422  21.869  12.344  0.80111.32           C
ANISOU 1570  CA  PHE A 114    13616  16172  12509  -1707  -2105   2416       C
ATOM   1571  C   PHE A 114      -7.696  22.524  12.902  0.80109.27           C
ANISOU 1571  C   PHE A 114    13631  16025  11863  -1506  -1957   2187       C
ATOM   1572  O   PHE A 114      -8.363  21.986  13.790  0.80108.88           O
ANISOU 1572  O   PHE A 114    13764  16099  11506  -1441  -1792   2143       O
ATOM   1573  H   PHE A 114      -5.718  20.033  13.172  0.80135.99           H
ATOM   1574  CB  PHE A 114      -6.682  21.062  11.048  1.00  0.00           C
ATOM   1575  CG  PHE A 114      -5.423  20.805  10.213  1.00  0.00           C
ATOM   1576  CD1 PHE A 114      -4.466  19.865  10.640  1.00  0.00           C
ATOM   1577  CD2 PHE A 114      -5.149  21.598   9.076  1.00  0.00           C
ATOM   1578  CE2 PHE A 114      -3.911  21.476   8.406  1.00  0.00           C
ATOM   1579  CZ  PHE A 114      -2.952  20.555   8.859  1.00  0.00           C
ATOM   1580  CE1 PHE A 114      -3.233  19.740   9.969  1.00  0.00           C
ATOM   1581  HA  PHE A 114      -5.741  22.682  12.084  0.80  0.00           H
ATOM   1582  HB2 PHE A 114      -7.391  21.611  10.426  1.00  0.00           H
ATOM   1583  HB3 PHE A 114      -7.148  20.106  11.297  1.00  0.00           H
ATOM   1584  HD1 PHE A 114      -4.642  19.286  11.538  1.00  0.00           H
ATOM   1585  HD2 PHE A 114      -5.854  22.359   8.758  1.00  0.00           H
ATOM   1586  HE2 PHE A 114      -3.669  22.154   7.595  1.00  0.00           H
ATOM   1587  HZ  PHE A 114      -1.970  20.526   8.405  1.00  0.00           H
ATOM   1588  HE1 PHE A 114      -2.473  19.077  10.358  1.00  0.00           H
ATOM   1589  N   LYS A 115      -7.971  23.745  12.434  0.80106.89           N
ANISOU 1589  N   LYS A 115    13360  15676  11579  -1407  -2018   2042       N
ATOM   1590  CA  LYS A 115      -9.130  24.574  12.794  0.80102.93           C
ANISOU 1590  CA  LYS A 115    13088  15277  10745  -1213  -1877   1816       C
ATOM   1591  C   LYS A 115      -9.681  25.231  11.511  0.80 97.68           C
ANISOU 1591  C   LYS A 115    12191  14680  10244  -1142  -1716   1707       C
ATOM   1592  O   LYS A 115      -8.866  25.629  10.676  0.80 92.09           O
ANISOU 1592  O   LYS A 115    11329  13826   9834  -1210  -1915   1759       O
ATOM   1593  H   LYS A 115      -7.369  24.132  11.717  0.80128.27           H
ATOM   1594  CB  LYS A 115      -8.741  25.626  13.860  1.00  0.00           C
ATOM   1595  CG  LYS A 115      -8.296  25.050  15.221  1.00  0.00           C
ATOM   1596  CD  LYS A 115      -9.366  24.225  15.966  1.00  0.00           C
ATOM   1597  CE  LYS A 115      -8.791  23.474  17.176  1.00  0.00           C
ATOM   1598  NZ  LYS A 115      -7.824  22.426  16.761  1.00  0.00           N
ATOM   1599  HA  LYS A 115      -9.897  23.933  13.211  0.80  0.00           H
ATOM   1600  HB2 LYS A 115      -7.919  26.231  13.467  1.00  0.00           H
ATOM   1601  HB3 LYS A 115      -9.585  26.298  14.025  1.00  0.00           H
ATOM   1602  HG2 LYS A 115      -7.408  24.443  15.061  1.00  0.00           H
ATOM   1603  HG3 LYS A 115      -8.003  25.881  15.866  1.00  0.00           H
ATOM   1604  HD2 LYS A 115      -9.825  23.495  15.302  1.00  0.00           H
ATOM   1605  HD3 LYS A 115     -10.152  24.900  16.310  1.00  0.00           H
ATOM   1606  HE2 LYS A 115      -9.619  23.012  17.722  1.00  0.00           H
ATOM   1607  HE3 LYS A 115      -8.312  24.194  17.847  1.00  0.00           H
ATOM   1608  HZ1 LYS A 115      -7.434  21.924  17.548  1.00  0.00           H
ATOM   1609  HZ2 LYS A 115      -7.061  22.809  16.209  1.00  0.00           H
ATOM   1610  HZ3 LYS A 115      -8.254  21.725  16.162  1.00  0.00           H
ATOM   1611  N   PRO A 116     -10.999  25.171  11.250  0.80101.02           N
ANISOU 1611  N   PRO A 116    12580  15319  10483  -1003  -1358   1557       N
ATOM   1612  CA  PRO A 116     -11.631  25.822  10.107  0.80 99.24           C
ANISOU 1612  CA  PRO A 116    12134  15160  10413   -932  -1202   1450       C
ATOM   1613  C   PRO A 116     -11.937  27.301  10.409  0.80 99.88           C
ANISOU 1613  C   PRO A 116    12473  15156  10322   -786  -1360   1254       C
ATOM   1614  O   PRO A 116     -11.742  27.763  11.535  0.80101.06           O
ANISOU 1614  O   PRO A 116    12985  15255  10159   -706  -1495   1168       O
ATOM   1615  CB  PRO A 116     -12.895  25.002   9.863  0.80 98.25           C
ANISOU 1615  CB  PRO A 116    11852  15310  10170   -857   -740   1387       C
ATOM   1616  CG  PRO A 116     -13.310  24.514  11.250  0.80100.83           C
ANISOU 1616  CG  PRO A 116    12467  15706  10138   -813   -679   1370       C
ATOM   1617  CD  PRO A 116     -12.022  24.549  12.077  0.80103.57           C
ANISOU 1617  CD  PRO A 116    13074  15830  10449   -900  -1084   1470       C
ATOM   1618  HA  PRO A 116     -10.997  25.779   9.223  0.80119.09           H
ATOM   1619  HB2 PRO A 116     -13.680  25.587   9.388  0.80117.90           H
ATOM   1620  HB3 PRO A 116     -12.647  24.140   9.243  0.80117.90           H
ATOM   1621  HG2 PRO A 116     -14.048  25.188  11.685  0.80121.00           H
ATOM   1622  HG3 PRO A 116     -13.712  23.501  11.194  0.80121.00           H
ATOM   1623  HD2 PRO A 116     -12.178  25.142  12.980  0.80124.29           H
ATOM   1624  HD3 PRO A 116     -11.728  23.534  12.337  0.80124.29           H
ATOM   1625  N   ASN A 119     -17.676  27.508   9.733  1.00101.01           N
ANISOU 1625  N   ASN A 119    12577  16158   9646   -132     69    518       N
ATOM   1626  CA  ASN A 119     -17.354  27.498   8.300  1.00 98.78           C
ANISOU 1626  CA  ASN A 119    11893  15895   9744   -212    159    596       C
ATOM   1627  C   ASN A 119     -18.581  27.228   7.421  1.00 99.25           C
ANISOU 1627  C   ASN A 119    11750  16184   9775    -97    568    465       C
ATOM   1628  O   ASN A 119     -18.622  27.640   6.261  1.00 98.75           O
ANISOU 1628  O   ASN A 119    11555  16122   9844    -36    601    369       O
ATOM   1629  CB  ASN A 119     -16.307  26.397   8.091  1.00 96.08           C
ANISOU 1629  CB  ASN A 119    11315  15535   9655   -401    147    833       C
ATOM   1630  CG  ASN A 119     -15.878  26.218   6.646  1.00 92.18           C
ANISOU 1630  CG  ASN A 119    10425  15027   9574   -497    183    930       C
ATOM   1631  OD1 ASN A 119     -15.017  26.946   6.150  1.00 90.73           O
ANISOU 1631  OD1 ASN A 119    10188  14755   9530   -460     65    860       O
ATOM   1632  ND2 ASN A 119     -16.089  25.074   6.058  1.00 89.39           N
ANISOU 1632  ND2 ASN A 119     9791  14759   9416   -619    348   1092       N
ATOM   1633  HA  ASN A 119     -16.943  28.472   8.028  1.00118.53           H
ATOM   1634  HB2 ASN A 119     -15.428  26.655   8.671  1.00115.29           H
ATOM   1635  HB3 ASN A 119     -16.705  25.452   8.456  1.00115.29           H
ATOM   1636 HD21 ASN A 119     -15.731  24.992   5.130  1.00107.27           H
ATOM   1637 HD22 ASN A 119     -16.719  24.408   6.482  1.00107.27           H
ATOM   1638  H   ASN A 119     -18.451  28.093  10.060  1.00  0.00           H
ATOM   1639  N   ARG A 120     -19.496  26.405   7.926  1.00 99.33           N
ANISOU 1639  N   ARG A 120    11740  16387   9614    -68    878    461       N
ATOM   1640  CA  ARG A 120     -20.808  26.105   7.348  1.00 98.78           C
ANISOU 1640  CA  ARG A 120    11484  16547   9500     39   1285    343       C
ATOM   1641  C   ARG A 120     -21.871  26.593   8.323  1.00100.65           C
ANISOU 1641  C   ARG A 120    12029  16885   9330    220   1421    141       C
ATOM   1642  O   ARG A 120     -21.700  26.405   9.525  1.00109.35           O
ANISOU 1642  O   ARG A 120    13462  17923  10165    244   1273    128       O
ATOM   1643  CB  ARG A 120     -20.937  24.594   7.072  1.00 96.52           C
ANISOU 1643  CB  ARG A 120    10921  16418   9334    -57   1567    483       C
ATOM   1644  CG  ARG A 120     -22.303  24.189   6.478  1.00 92.23           C
ANISOU 1644  CG  ARG A 120    10179  16118   8744     48   2000    369       C
ATOM   1645  CD  ARG A 120     -22.362  22.702   6.086  1.00 88.14           C
ANISOU 1645  CD  ARG A 120     9348  15735   8405    -64   2249    525       C
ATOM   1646  NE  ARG A 120     -22.147  21.788   7.226  1.00 87.06           N
ANISOU 1646  NE  ARG A 120     9369  15608   8102   -132   2236    635       N
ATOM   1647  CZ  ARG A 120     -23.054  21.327   8.066  1.00 88.28           C
ANISOU 1647  CZ  ARG A 120     9670  15915   7957    -45   2475    562       C
ATOM   1648  NH1 ARG A 120     -24.329  21.573   7.980  1.00 87.84           N
ANISOU 1648  NH1 ARG A 120     9665  15900   7811    112   2695    366       N
ATOM   1649  NH2 ARG A 120     -22.643  20.555   9.023  1.00 87.51           N
ANISOU 1649  NH2 ARG A 120     9711  15809   7728   -117   2439    677       N
ATOM   1650  H   ARG A 120     -19.392  26.174   8.907  1.00119.20           H
ATOM   1651  HA  ARG A 120     -20.934  26.653   6.417  1.00118.53           H
ATOM   1652  HB2 ARG A 120     -20.150  24.301   6.377  1.00115.82           H
ATOM   1653  HB3 ARG A 120     -20.787  24.051   8.008  1.00115.82           H
ATOM   1654  HG2 ARG A 120     -23.099  24.388   7.196  1.00110.67           H
ATOM   1655  HG3 ARG A 120     -22.490  24.787   5.584  1.00110.67           H
ATOM   1656  HD2 ARG A 120     -23.331  22.503   5.621  1.00105.77           H
ATOM   1657  HD3 ARG A 120     -21.592  22.516   5.340  1.00105.77           H
ATOM   1658  HE  ARG A 120     -21.202  21.496   7.456  1.00104.47           H
ATOM   1659 HH11 ARG A 120     -24.704  22.182   7.235  1.00105.41           H
ATOM   1660 HH12 ARG A 120     -24.966  21.333   8.704  1.00105.41           H
ATOM   1661 HH21 ARG A 120     -21.662  20.257   9.008  1.00105.01           H
ATOM   1662 HH22 ARG A 120     -23.285  20.135   9.660  1.00105.01           H
ATOM   1663  N   GLU A 121     -22.965  27.103   7.785  1.00 91.19           N
ANISOU 1663  N   GLU A 121    10717  15844   8087    351   1706    -19       N
ATOM   1664  CA  GLU A 121     -24.196  27.412   8.503  1.00 88.89           C
ANISOU 1664  CA  GLU A 121    10686  15663   7427    532   1869   -222       C
ATOM   1665  C   GLU A 121     -25.406  26.855   7.731  1.00 87.37           C
ANISOU 1665  C   GLU A 121    10247  15701   7249    625   2289   -327       C
ATOM   1666  O   GLU A 121     -25.355  26.749   6.499  1.00 83.04           O
ANISOU 1666  O   GLU A 121     9422  15174   6955    621   2360   -344       O
ATOM   1667  H   GLU A 121     -23.008  27.200   6.775  1.00109.43           H
ATOM   1668  CB  GLU A 121     -24.265  28.936   8.731  1.00  0.00           C
ATOM   1669  CG  GLU A 121     -25.441  29.430   9.585  1.00  0.00           C
ATOM   1670  CD  GLU A 121     -25.464  28.762  10.969  1.00  0.00           C
ATOM   1671  OE2 GLU A 121     -25.813  27.560  11.014  1.00  0.00           O
ATOM   1672  OE1 GLU A 121     -24.815  29.337  11.874  1.00  0.00           O
ATOM   1673  HA  GLU A 121     -24.160  26.915   9.471  1.00  0.00           H
ATOM   1674  HB2 GLU A 121     -24.304  29.439   7.761  1.00  0.00           H
ATOM   1675  HB3 GLU A 121     -23.340  29.253   9.220  1.00  0.00           H
ATOM   1676  HG2 GLU A 121     -25.350  30.513   9.697  1.00  0.00           H
ATOM   1677  HG3 GLU A 121     -26.376  29.237   9.057  1.00  0.00           H
ATOM   1678  N   GLU A 122     -26.468  26.457   8.428  1.00 97.20           N
ANISOU 1678  N   GLU A 122    11594  17115   8223    710   2565   -396       N
ATOM   1679  CA  GLU A 122     -27.737  26.039   7.810  1.00 97.19           C
ANISOU 1679  CA  GLU A 122    11499  16919   8510    740   2786   -475       C
ATOM   1680  C   GLU A 122     -28.790  27.141   7.936  1.00 96.93           C
ANISOU 1680  C   GLU A 122    11683  16812   8334    895   2798   -687       C
ATOM   1681  O   GLU A 122     -29.025  27.663   9.029  1.00 99.33           O
ANISOU 1681  O   GLU A 122    12284  17213   8242   1001   2701   -790       O
ATOM   1682  CB  GLU A 122     -28.271  24.729   8.421  1.00 98.39           C
ANISOU 1682  CB  GLU A 122    11721  16950   8711    685   2939   -410       C
ATOM   1683  CG  GLU A 122     -27.400  23.504   8.123  1.00 97.45           C
ANISOU 1683  CG  GLU A 122    11410  16873   8742    531   2925   -201       C
ATOM   1684  CD  GLU A 122     -27.034  23.353   6.654  1.00 96.90           C
ANISOU 1684  CD  GLU A 122    11017  16643   9158    430   2926   -115       C
ATOM   1685  OE1 GLU A 122     -27.953  23.147   5.832  1.00 96.49           O
ANISOU 1685  OE1 GLU A 122    10930  16371   9363    470   2994   -212       O
ATOM   1686  OE2 GLU A 122     -25.822  23.128   6.406  1.00 96.41           O
ANISOU 1686  OE2 GLU A 122    10762  16649   9222    302   2843     55       O
ATOM   1687  H   GLU A 122     -26.482  26.693   9.427  1.00116.64           H
ATOM   1688  HA  GLU A 122     -27.588  25.875   6.744  1.00116.63           H
ATOM   1689  HB2 GLU A 122     -28.384  24.852   9.506  1.00118.07           H
ATOM   1690  HB3 GLU A 122     -29.275  24.553   8.013  1.00118.07           H
ATOM   1691  HG2 GLU A 122     -26.509  23.570   8.726  1.00116.94           H
ATOM   1692  HG3 GLU A 122     -27.941  22.621   8.456  1.00116.94           H
ATOM   1693  N   MET A 123     -29.492  27.452   6.847  1.00 93.36           N
ANISOU 1693  N   MET A 123    11107  16153   8212    901   2895   -745       N
ATOM   1694  CA  MET A 123     -30.519  28.496   6.860  1.00 91.86           C
ANISOU 1694  CA  MET A 123    11087  15876   7938   1023   2910   -925       C
ATOM   1695  C   MET A 123     -31.558  28.335   5.745  1.00 89.17           C
ANISOU 1695  C   MET A 123    10599  15274   8007    982   3029   -929       C
ATOM   1696  O   MET A 123     -31.323  27.660   4.740  1.00 87.96           O
ANISOU 1696  O   MET A 123    10217  15012   8193    879   3047   -810       O
ATOM   1697  CB  MET A 123     -29.837  29.873   6.811  1.00 91.85           C
ANISOU 1697  CB  MET A 123    11135  16037   7728   1121   2718  -1025       C
ATOM   1698  CG  MET A 123     -28.988  30.105   5.550  1.00 90.10           C
ANISOU 1698  CG  MET A 123    10597  15867   7772   1055   2635   -947       C
ATOM   1699  SD  MET A 123     -28.096  31.687   5.499  1.00 92.10           S
ANISOU 1699  SD  MET A 123    10922  16318   7755   1171   2393  -1076       S
ATOM   1700  CE  MET A 123     -26.895  31.428   6.834  1.00 92.10           C
ANISOU 1700  CE  MET A 123    11244  16164   7587   1075   2057   -945       C
ATOM   1701  H   MET A 123     -29.253  27.008   5.965  1.00112.03           H
ATOM   1702  HA  MET A 123     -31.057  28.431   7.806  1.00110.23           H
ATOM   1703  HB2 MET A 123     -30.605  30.637   6.878  1.00110.22           H
ATOM   1704  HB3 MET A 123     -29.205  29.981   7.692  1.00110.22           H
ATOM   1705  HG2 MET A 123     -28.252  29.305   5.471  1.00108.12           H
ATOM   1706  HG3 MET A 123     -29.638  30.050   4.676  1.00108.12           H
ATOM   1707  HE1 MET A 123     -26.201  32.267   6.867  1.00110.52           H
ATOM   1708  HE2 MET A 123     -27.411  31.358   7.791  1.00110.52           H
ATOM   1709  HE3 MET A 123     -26.340  30.506   6.657  1.00110.52           H
ATOM   1710  N   LYS A 124     -32.706  29.009   5.877  1.00 85.95           N
ANISOU 1710  N   LYS A 124    10354  14745   7559   1058   3095  -1062       N
ATOM   1711  CA  LYS A 124     -33.703  29.125   4.802  1.00 82.03           C
ANISOU 1711  CA  LYS A 124     9767  14001   7401   1030   3181  -1072       C
ATOM   1712  C   LYS A 124     -33.183  30.028   3.688  1.00 79.94           C
ANISOU 1712  C   LYS A 124     9339  13756   7277   1054   3053  -1091       C
ATOM   1713  O   LYS A 124     -32.522  31.030   3.954  1.00 80.96           O
ANISOU 1713  O   LYS A 124     9465  14096   7200   1118   2907  -1141       O
ATOM   1714  H   LYS A 124     -32.811  29.628   6.688  1.00103.14           H
ATOM   1715  CB  LYS A 124     -35.041  29.641   5.368  1.00  0.00           C
ATOM   1716  CG  LYS A 124     -35.663  28.758   6.472  1.00  0.00           C
ATOM   1717  CD  LYS A 124     -35.904  27.313   6.002  1.00  0.00           C
ATOM   1718  CE  LYS A 124     -36.529  26.390   7.055  1.00  0.00           C
ATOM   1719  NZ  LYS A 124     -35.553  26.022   8.108  1.00  0.00           N
ATOM   1720  HA  LYS A 124     -33.839  28.139   4.364  1.00  0.00           H
ATOM   1721  HB2 LYS A 124     -34.888  30.643   5.771  1.00  0.00           H
ATOM   1722  HB3 LYS A 124     -35.755  29.735   4.550  1.00  0.00           H
ATOM   1723  HG2 LYS A 124     -36.617  29.200   6.764  1.00  0.00           H
ATOM   1724  HG3 LYS A 124     -35.013  28.752   7.347  1.00  0.00           H
ATOM   1725  HD2 LYS A 124     -34.956  26.870   5.701  1.00  0.00           H
ATOM   1726  HD3 LYS A 124     -36.564  27.348   5.136  1.00  0.00           H
ATOM   1727  HE2 LYS A 124     -36.849  25.475   6.546  1.00  0.00           H
ATOM   1728  HE3 LYS A 124     -37.410  26.869   7.489  1.00  0.00           H
ATOM   1729  HZ1 LYS A 124     -35.910  25.345   8.765  1.00  0.00           H
ATOM   1730  HZ2 LYS A 124     -35.164  26.820   8.588  1.00  0.00           H
ATOM   1731  HZ3 LYS A 124     -34.741  25.549   7.695  1.00  0.00           H
ATOM   1732  N   PHE A 125     -33.688  29.838   2.469  1.00 94.50           N
ANISOU 1732  N   PHE A 125     8890  18796   8218   2094   2226   -697       N
ATOM   1733  CA  PHE A 125     -33.224  30.597   1.297  1.00 88.82           C
ANISOU 1733  CA  PHE A 125     8223  17721   7803   2221   2210   -759       C
ATOM   1734  C   PHE A 125     -33.311  32.128   1.464  1.00 89.13           C
ANISOU 1734  C   PHE A 125     8353  17734   7779   2597   2173  -1115       C
ATOM   1735  O   PHE A 125     -32.351  32.820   1.143  1.00 83.72           O
ANISOU 1735  O   PHE A 125     7751  16811   7249   2747   2122  -1244       O
ATOM   1736  CB  PHE A 125     -34.000  30.153   0.051  1.00 89.15           C
ANISOU 1736  CB  PHE A 125     8214  17560   8099   2121   2239   -596       C
ATOM   1737  CG  PHE A 125     -33.263  30.458  -1.239  1.00 88.01           C
ANISOU 1737  CG  PHE A 125     8119  17003   8317   2135   2223   -541       C
ATOM   1738  CD1 PHE A 125     -33.357  31.728  -1.841  1.00 86.68           C
ANISOU 1738  CD1 PHE A 125     8017  16629   8290   2419   2201   -767       C
ATOM   1739  CD2 PHE A 125     -32.489  29.452  -1.850  1.00 85.59           C
ANISOU 1739  CD2 PHE A 125     7807  16486   8226   1864   2219   -257       C
ATOM   1740  CE1 PHE A 125     -32.676  31.992  -3.042  1.00 83.52           C
ANISOU 1740  CE1 PHE A 125     7663  15825   8245   2438   2180   -708       C
ATOM   1741  CE2 PHE A 125     -31.817  29.712  -3.056  1.00 80.78           C
ANISOU 1741  CE2 PHE A 125     7244  15485   7962   1885   2205   -192       C
ATOM   1742  CZ  PHE A 125     -31.906  30.985  -3.648  1.00 80.61           C
ANISOU 1742  CZ  PHE A 125     7276  15266   8084   2176   2189   -416       C
ATOM   1743  H   PHE A 125     -34.186  28.975   2.305  1.00113.40           H
ATOM   1744  HA  PHE A 125     -32.173  30.352   1.140  1.00106.58           H
ATOM   1745  HB2 PHE A 125     -34.174  29.079   0.097  1.00106.98           H
ATOM   1746  HB3 PHE A 125     -34.979  30.637   0.032  1.00106.98           H
ATOM   1747  HD1 PHE A 125     -33.944  32.510  -1.380  1.00104.02           H
ATOM   1748  HD2 PHE A 125     -32.422  28.472  -1.397  1.00102.71           H
ATOM   1749  HE1 PHE A 125     -32.752  32.970  -3.499  1.00100.22           H
ATOM   1750  HE2 PHE A 125     -31.235  28.932  -3.524  1.00 96.93           H
ATOM   1751  HZ  PHE A 125     -31.393  31.192  -4.576  1.00 96.73           H
ATOM   1752  N   HIS A 126     -34.373  32.646   2.103  1.00 97.27           N
ANISOU 1752  N   HIS A 126     9374  18982   8603   2761   2185  -1276       N
ATOM   1753  CA  HIS A 126     -34.516  34.089   2.375  1.00 98.43           C
ANISOU 1753  CA  HIS A 126     9628  19069   8702   3111   2129  -1609       C
ATOM   1754  C   HIS A 126     -33.407  34.657   3.281  1.00101.07           C
ANISOU 1754  C   HIS A 126    10093  19438   8872   3260   2046  -1823       C
ATOM   1755  O   HIS A 126     -32.834  35.682   2.945  1.00100.49           O
ANISOU 1755  O   HIS A 126    10147  19142   8892   3525   1957  -2079       O
ATOM   1756  CB  HIS A 126     -35.936  34.415   2.895  1.00100.02           C
ANISOU 1756  CB  HIS A 126     9787  19527   8689   3237   2164  -1708       C
ATOM   1757  CG  HIS A 126     -36.186  34.125   4.360  1.00106.40           C
ANISOU 1757  CG  HIS A 126    10577  20714   9136   3213   2177  -1729       C
ATOM   1758  ND1 HIS A 126     -35.841  34.957   5.409  1.00110.01           N
ANISOU 1758  ND1 HIS A 126    11159  21288   9350   3446   2112  -1998       N
ATOM   1759  CD2 HIS A 126     -36.673  32.965   4.903  1.00108.42           C
ANISOU 1759  CD2 HIS A 126    10716  21235   9243   2988   2238  -1516       C
ATOM   1760  CE1 HIS A 126     -36.071  34.312   6.564  1.00111.62           C
ANISOU 1760  CE1 HIS A 126    11323  21822   9264   3364   2143  -1942       C
ATOM   1761  NE2 HIS A 126     -36.575  33.093   6.283  1.00110.01           N
ANISOU 1761  NE2 HIS A 126    10965  21714   9118   3086   2221  -1649       N
ATOM   1762  H   HIS A 126     -35.131  32.030   2.338  1.00116.73           H
ATOM   1763  HA  HIS A 126     -34.394  34.609   1.425  1.00118.12           H
ATOM   1764  HB2 HIS A 126     -36.100  35.486   2.747  1.00120.02           H
ATOM   1765  HB3 HIS A 126     -36.679  33.902   2.280  1.00120.02           H
ATOM   1766  HD1 HIS A 126     -35.442  35.907   5.327  1.00132.01           H
ATOM   1767  HD2 HIS A 126     -37.011  32.101   4.349  1.00130.10           H
ATOM   1768  HE1 HIS A 126     -35.749  34.672   7.540  1.00133.94           H
ATOM   1769  HE2 HIS A 126     -36.678  32.349   6.967  1.00  0.00           H
ATOM   1770  N   GLU A 127     -32.934  33.891   4.265  1.00104.82           N
ANISOU 1770  N   GLU A 127    10556  20161   9110   3089   2055  -1726       N
ATOM   1771  CA  GLU A 127     -31.818  34.262   5.151  1.00106.80           C
ANISOU 1771  CA  GLU A 127    10957  20437   9185   3205   1962  -1924       C
ATOM   1772  C   GLU A 127     -30.481  34.322   4.385  1.00101.19           C
ANISOU 1772  C   GLU A 127    10377  19167   8906   3104   1802  -1842       C
ATOM   1773  O   GLU A 127     -29.745  35.297   4.515  1.00103.84           O
ANISOU 1773  O   GLU A 127    10932  19151   9373   3241   1590  -2034       O
ATOM   1774  CB  GLU A 127     -31.737  33.262   6.325  1.00107.05           C
ANISOU 1774  CB  GLU A 127    10967  20790   8918   2968   1982  -1773       C
ATOM   1775  CG  GLU A 127     -33.058  33.169   7.109  1.00109.41           C
ANISOU 1775  CG  GLU A 127    11203  21416   8951   2984   2029  -1776       C
ATOM   1776  CD  GLU A 127     -33.101  32.069   8.181  1.00110.75           C
ANISOU 1776  CD  GLU A 127    11334  21858   8886   2723   2049  -1586       C
ATOM   1777  OE1 GLU A 127     -33.418  30.933   7.757  1.00108.74           O
ANISOU 1777  OE1 GLU A 127    10955  21594   8767   2405   2104  -1269       O
ATOM   1778  OE2 GLU A 127     -33.426  32.446   9.328  1.00114.36           O
ANISOU 1778  OE2 GLU A 127    11903  22512   9037   2837   1994  -1753       O
ATOM   1779  H   GLU A 127     -33.323  32.970   4.393  1.00125.79           H
ATOM   1780  HA  GLU A 127     -32.001  35.256   5.569  1.00128.16           H
ATOM   1781  HB2 GLU A 127     -31.500  32.287   5.913  1.00128.46           H
ATOM   1782  HB3 GLU A 127     -30.934  33.557   7.002  1.00128.46           H
ATOM   1783  HG2 GLU A 127     -33.271  34.141   7.556  1.00131.29           H
ATOM   1784  HG3 GLU A 127     -33.853  32.940   6.405  1.00131.29           H
ATOM   1785  N   PHE A 128     -30.262  33.425   3.413  1.00 92.24           N
ANISOU 1785  N   PHE A 128     9131  17875   8040   2835   1866  -1527       N
ATOM   1786  CA  PHE A 128     -29.122  33.527   2.487  1.00 89.14           C
ANISOU 1786  CA  PHE A 128     8868  16884   8117   2714   1703  -1398       C
ATOM   1787  C   PHE A 128     -29.196  34.767   1.574  1.00 89.19           C
ANISOU 1787  C   PHE A 128     8946  16558   8384   3014   1645  -1615       C
ATOM   1788  O   PHE A 128     -28.182  35.446   1.395  1.00 89.75           O
ANISOU 1788  O   PHE A 128     9207  16153   8740   3060   1438  -1684       O
ATOM   1789  CB  PHE A 128     -28.980  32.235   1.664  1.00 84.91           C
ANISOU 1789  CB  PHE A 128     8189  16291   7783   2396   1811  -1021       C
ATOM   1790  CG  PHE A 128     -27.945  32.330   0.553  1.00 81.78           C
ANISOU 1790  CG  PHE A 128     7893  15300   7879   2308   1690   -873       C
ATOM   1791  CD1 PHE A 128     -26.574  32.385   0.866  1.00 81.24           C
ANISOU 1791  CD1 PHE A 128     8012  14835   8019   2159   1478   -795       C
ATOM   1792  CD2 PHE A 128     -28.354  32.443  -0.791  1.00 79.81           C
ANISOU 1792  CD2 PHE A 128     7549  14891   7885   2376   1791   -802       C
ATOM   1793  CE1 PHE A 128     -25.617  32.543  -0.153  1.00 78.38           C
ANISOU 1793  CE1 PHE A 128     7734  13933   8115   2085   1376   -641       C
ATOM   1794  CE2 PHE A 128     -27.397  32.601  -1.811  1.00 75.10           C
ANISOU 1794  CE2 PHE A 128     7047  13754   7735   2309   1691   -656       C
ATOM   1795  CZ  PHE A 128     -26.028  32.650  -1.494  1.00 74.73           C
ANISOU 1795  CZ  PHE A 128     7179  13320   7894   2165   1488   -571       C
ATOM   1796  H   PHE A 128     -30.914  32.659   3.313  1.00110.69           H
ATOM   1797  HA  PHE A 128     -28.215  33.638   3.083  1.00106.97           H
ATOM   1798  HB2 PHE A 128     -28.708  31.419   2.334  1.00101.89           H
ATOM   1799  HB3 PHE A 128     -29.942  31.980   1.223  1.00101.89           H
ATOM   1800  HD1 PHE A 128     -26.262  32.338   1.899  1.00 97.48           H
ATOM   1801  HD2 PHE A 128     -29.407  32.431  -1.037  1.00 95.77           H
ATOM   1802  HE1 PHE A 128     -24.569  32.606   0.097  1.00 94.06           H
ATOM   1803  HE2 PHE A 128     -27.721  32.711  -2.835  1.00 90.12           H
ATOM   1804  HZ  PHE A 128     -25.295  32.790  -2.275  1.00 89.67           H
ATOM   1805  N   VAL A 129     -30.383  35.121   1.063  1.00 90.01           N
ANISOU 1805  N   VAL A 129     8895  16907   8398   3221   1824  -1721       N
ATOM   1806  CA  VAL A 129     -30.587  36.349   0.265  1.00 91.04           C
ANISOU 1806  CA  VAL A 129     9084  16758   8751   3523   1783  -1940       C
ATOM   1807  C   VAL A 129     -30.394  37.614   1.117  1.00 93.79           C
ANISOU 1807  C   VAL A 129     9625  17045   8965   3803   1618  -2292       C
ATOM   1808  O   VAL A 129     -29.614  38.482   0.726  1.00 89.44           O
ANISOU 1808  O   VAL A 129     9219  16072   8692   3977   1468  -2444       O
ATOM   1809  CB  VAL A 129     -31.960  36.354  -0.451  1.00 95.04           C
ANISOU 1809  CB  VAL A 129     9470  17392   9249   3544   1915  -1897       C
ATOM   1810  CG1 VAL A 129     -32.160  37.605  -1.320  1.00 96.83           C
ANISOU 1810  CG1 VAL A 129     9801  17246   9745   3774   1835  -2072       C
ATOM   1811  CG2 VAL A 129     -32.119  35.163  -1.407  1.00 92.38           C
ANISOU 1811  CG2 VAL A 129     9004  17020   9076   3222   2016  -1533       C
ATOM   1812  H   VAL A 129     -31.186  34.538   1.276  1.00108.02           H
ATOM   1813  HA  VAL A 129     -29.819  36.377  -0.506  1.00109.25           H
ATOM   1814  HB  VAL A 129     -32.756  36.314   0.291  1.00114.05           H
ATOM   1815 HG11 VAL A 129     -33.121  37.547  -1.832  1.00116.20           H
ATOM   1816 HG12 VAL A 129     -32.164  38.502  -0.701  1.00116.20           H
ATOM   1817 HG13 VAL A 129     -31.365  37.682  -2.061  1.00116.20           H
ATOM   1818 HG21 VAL A 129     -33.099  35.204  -1.883  1.00110.86           H
ATOM   1819 HG22 VAL A 129     -31.349  35.190  -2.172  1.00110.86           H
ATOM   1820 HG23 VAL A 129     -32.043  34.226  -0.864  1.00110.86           H
ATOM   1821  N   GLU A 130     -30.897  37.635   2.355  1.00102.15           N
ANISOU 1821  N   GLU A 130    10694  18521   9598   3857   1642  -2425       N
ATOM   1822  CA  GLU A 130     -30.668  38.700   3.345  1.00110.51           C
ANISOU 1822  CA  GLU A 130    11957  19532  10500   4119   1473  -2759       C
ATOM   1823  C   GLU A 130     -29.185  38.853   3.713  1.00109.02           C
ANISOU 1823  C   GLU A 130    12006  18856  10562   3985   1190  -2727       C
ATOM   1824  O   GLU A 130     -28.700  39.978   3.813  1.00111.54           O
ANISOU 1824  O   GLU A 130    12509  18831  11039   4194    998  -2953       O
ATOM   1825  CB  GLU A 130     -31.476  38.430   4.630  1.00115.66           C
ANISOU 1825  CB  GLU A 130    12566  20756  10623   4196   1574  -2878       C
ATOM   1826  CG  GLU A 130     -32.997  38.591   4.467  1.00118.13           C
ANISOU 1826  CG  GLU A 130    12745  21296  10845   4221   1702  -2829       C
ATOM   1827  CD  GLU A 130     -33.813  37.843   5.538  1.00120.08           C
ANISOU 1827  CD  GLU A 130    12917  21994  10713   4116   1782  -2751       C
ATOM   1828  OE1 GLU A 130     -33.250  37.436   6.580  1.00121.19           O
ANISOU 1828  OE1 GLU A 130    13163  22300  10585   4138   1720  -2853       O
ATOM   1829  OE2 GLU A 130     -34.971  37.478   5.237  1.00119.71           O
ANISOU 1829  OE2 GLU A 130    12718  22118  10649   4012   1897  -2586       O
ATOM   1830  H   GLU A 130     -31.528  36.883   2.622  1.00122.58           H
ATOM   1831  HA  GLU A 130     -30.994  39.654   2.929  1.00132.61           H
ATOM   1832  HB2 GLU A 130     -31.248  37.419   4.965  1.00138.79           H
ATOM   1833  HB3 GLU A 130     -31.147  39.121   5.410  1.00138.79           H
ATOM   1834  HG2 GLU A 130     -33.243  39.654   4.497  1.00141.76           H
ATOM   1835  HG3 GLU A 130     -33.295  38.218   3.487  1.00141.76           H
ATOM   1836  N   LYS A 131     -28.425  37.755   3.836  1.00100.92           N
ANISOU 1836  N   LYS A 131    10975  17792   9580   3637   1156  -2444       N
ATOM   1837  CA  LYS A 131     -26.978  37.799   4.110  1.00 93.01           C
ANISOU 1837  CA  LYS A 131    10182  16321   8835   3485    890  -2381       C
ATOM   1838  C   LYS A 131     -26.152  38.247   2.904  1.00 93.59           C
ANISOU 1838  C   LYS A 131    10310  15818   9430   3493    786  -2306       C
ATOM   1839  O   LYS A 131     -25.302  39.121   3.073  1.00 88.93           O
ANISOU 1839  O   LYS A 131     9918  14811   9061   3595    549  -2441       O
ATOM   1840  H   LYS A 131     -28.889  36.850   3.764  1.00121.11           H
ATOM   1841  CB  LYS A 131     -26.486  36.460   4.683  1.00  0.00           C
ATOM   1842  CG  LYS A 131     -26.971  36.089   6.101  1.00  0.00           C
ATOM   1843  CD  LYS A 131     -26.434  36.941   7.263  1.00  0.00           C
ATOM   1844  CE  LYS A 131     -27.182  38.263   7.451  1.00  0.00           C
ATOM   1845  NZ  LYS A 131     -26.567  39.071   8.519  1.00  0.00           N
ATOM   1846  HA  LYS A 131     -26.785  38.580   4.828  1.00  0.00           H
ATOM   1847  HB2 LYS A 131     -26.780  35.660   4.001  1.00  0.00           H
ATOM   1848  HB3 LYS A 131     -25.400  36.487   4.709  1.00  0.00           H
ATOM   1849  HG2 LYS A 131     -26.641  35.066   6.286  1.00  0.00           H
ATOM   1850  HG3 LYS A 131     -28.057  36.093   6.144  1.00  0.00           H
ATOM   1851  HD2 LYS A 131     -26.564  36.368   8.183  1.00  0.00           H
ATOM   1852  HD3 LYS A 131     -25.367  37.121   7.123  1.00  0.00           H
ATOM   1853  HE2 LYS A 131     -27.136  38.849   6.534  1.00  0.00           H
ATOM   1854  HE3 LYS A 131     -28.237  38.077   7.665  1.00  0.00           H
ATOM   1855  HZ1 LYS A 131     -26.969  40.005   8.489  1.00  0.00           H
ATOM   1856  HZ2 LYS A 131     -26.581  38.686   9.448  1.00  0.00           H
ATOM   1857  HZ3 LYS A 131     -25.637  39.357   8.238  1.00  0.00           H
ATOM   1858  N   LEU A 132     -26.490  37.816   1.689  1.00102.62           N
ANISOU 1858  N   LEU A 132    11283  16928  10780   3391    956  -2087       N
ATOM   1859  CA  LEU A 132     -25.876  38.350   0.469  1.00106.70           C
ANISOU 1859  CA  LEU A 132    11841  16917  11785   3413    883  -2002       C
ATOM   1860  C   LEU A 132     -26.186  39.854   0.287  1.00106.96           C
ANISOU 1860  C   LEU A 132    11956  16793  11890   3791    815  -2334       C
ATOM   1861  O   LEU A 132     -25.259  40.632   0.064  1.00111.81           O
ANISOU 1861  O   LEU A 132    12701  16903  12878   3861    642  -2363       O
ATOM   1862  H   LEU A 132     -27.221  37.114   1.608  1.00123.14           H
ATOM   1863  CB  LEU A 132     -26.276  37.435  -0.707  1.00  0.00           C
ATOM   1864  CG  LEU A 132     -25.602  37.767  -2.054  1.00  0.00           C
ATOM   1865  CD2 LEU A 132     -26.312  38.899  -2.806  1.00  0.00           C
ATOM   1866  CD1 LEU A 132     -25.564  36.516  -2.940  1.00  0.00           C
ATOM   1867  HA  LEU A 132     -24.793  38.276   0.581  1.00  0.00           H
ATOM   1868  HB2 LEU A 132     -25.978  36.422  -0.426  1.00  0.00           H
ATOM   1869  HB3 LEU A 132     -27.360  37.423  -0.826  1.00  0.00           H
ATOM   1870  HG  LEU A 132     -24.567  38.058  -1.878  1.00  0.00           H
ATOM   1871 HD21 LEU A 132     -26.197  38.787  -3.884  1.00  0.00           H
ATOM   1872 HD22 LEU A 132     -27.375  38.919  -2.567  1.00  0.00           H
ATOM   1873 HD23 LEU A 132     -25.869  39.853  -2.521  1.00  0.00           H
ATOM   1874 HD11 LEU A 132     -24.997  36.735  -3.841  1.00  0.00           H
ATOM   1875 HD12 LEU A 132     -26.575  36.203  -3.200  1.00  0.00           H
ATOM   1876 HD13 LEU A 132     -25.057  35.706  -2.414  1.00  0.00           H
ATOM   1877  N   GLN A 133     -27.403  40.307   0.605  1.00 99.50           N
ANISOU 1877  N   GLN A 133    10934  16274  10598   4042    950  -2581       N
ATOM   1878  CA  GLN A 133     -27.814  41.718   0.522  1.00103.27           C
ANISOU 1878  CA  GLN A 133    11499  16638  11099   4415    883  -2919       C
ATOM   1879  C   GLN A 133     -27.254  42.634   1.647  1.00110.33           C
ANISOU 1879  C   GLN A 133    12632  17401  11889   4544    630  -3170       C
ATOM   1880  O   GLN A 133     -26.926  43.792   1.377  1.00109.62           O
ANISOU 1880  O   GLN A 133    12689  16945  12016   4758    456  -3368       O
ATOM   1881  H   GLN A 133     -28.137  39.619   0.762  1.00119.40           H
ATOM   1882  CB  GLN A 133     -29.349  41.769   0.437  1.00  0.00           C
ATOM   1883  CG  GLN A 133     -29.944  43.152   0.126  1.00  0.00           C
ATOM   1884  CD  GLN A 133     -29.455  43.706  -1.206  1.00  0.00           C
ATOM   1885  NE2 GLN A 133     -28.359  44.429  -1.225  1.00  0.00           N
ATOM   1886  OE1 GLN A 133     -29.950  43.385  -2.269  1.00  0.00           O
ATOM   1887  HA  GLN A 133     -27.410  42.106  -0.404  1.00  0.00           H
ATOM   1888  HB2 GLN A 133     -29.667  41.091  -0.355  1.00  0.00           H
ATOM   1889  HB3 GLN A 133     -29.775  41.409   1.375  1.00  0.00           H
ATOM   1890  HG2 GLN A 133     -31.030  43.063   0.079  1.00  0.00           H
ATOM   1891  HG3 GLN A 133     -29.702  43.853   0.925  1.00  0.00           H
ATOM   1892 HE21 GLN A 133     -27.991  44.594  -2.144  1.00  0.00           H
ATOM   1893 HE22 GLN A 133     -27.821  44.525  -0.373  1.00  0.00           H
ATOM   1894  N   ASP A 134     -27.043  42.112   2.868  1.00118.88           N
ANISOU 1894  N   ASP A 134    13758  18772  12639   4419    599  -3162       N
ATOM   1895  CA  ASP A 134     -26.342  42.719   4.004  1.00123.22           C
ANISOU 1895  CA  ASP A 134    14548  19190  13081   4519    342  -3383       C
ATOM   1896  C   ASP A 134     -24.850  42.963   3.666  1.00124.84           C
ANISOU 1896  C   ASP A 134    14922  18769  13742   4381     71  -3272       C
ATOM   1897  O   ASP A 134     -24.359  44.090   3.796  1.00125.41           O
ANISOU 1897  O   ASP A 134    15186  18518  13948   4578   -157  -3498       O
ATOM   1898  CB  ASP A 134     -26.609  41.764   5.182  1.00123.70           C
ANISOU 1898  CB  ASP A 134    14612  19670  12717   4370    372  -3344       C
ATOM   1899  CG  ASP A 134     -25.816  42.037   6.479  1.00126.72           C
ANISOU 1899  CG  ASP A 134    15258  19875  13014   4418     85  -3522       C
ATOM   1900  OD1 ASP A 134     -25.077  43.090   6.568  1.00128.67           O
ANISOU 1900  OD1 ASP A 134    15673  19881  13335   4695    -90  -3806       O
ATOM   1901  OD2 ASP A 134     -25.992  41.290   7.470  1.00128.25           O
ANISOU 1901  OD2 ASP A 134    15494  20164  13069   4178     26  -3379       O
ATOM   1902  H   ASP A 134     -27.441  41.184   3.041  1.00142.66           H
ATOM   1903  HA  ASP A 134     -26.767  43.705   4.224  1.00147.87           H
ATOM   1904  HB2 ASP A 134     -27.634  41.869   5.489  1.00148.43           H
ATOM   1905  HB3 ASP A 134     -26.367  40.758   4.892  1.00148.43           H
ATOM   1906  N   ILE A 135     -24.170  41.958   3.097  1.00127.22           N
ANISOU 1906  N   ILE A 135    15154  18891  14292   4042     91  -2916       N
ATOM   1907  CA  ILE A 135     -22.761  42.031   2.663  1.00126.14           C
ANISOU 1907  CA  ILE A 135    15157  18162  14608   3895   -148  -2768       C
ATOM   1908  C   ILE A 135     -22.578  42.832   1.349  1.00128.08           C
ANISOU 1908  C   ILE A 135    15405  17992  15267   4074   -177  -2811       C
ATOM   1909  O   ILE A 135     -21.512  43.416   1.135  1.00124.40           O
ANISOU 1909  O   ILE A 135    15093  17023  15148   4097   -417  -2827       O
ATOM   1910  CB  ILE A 135     -22.158  40.602   2.561  1.00121.55           C
ANISOU 1910  CB  ILE A 135    14491  17526  14165   3493    -95  -2365       C
ATOM   1911  CG1 ILE A 135     -22.240  39.778   3.876  1.00122.93           C
ANISOU 1911  CG1 ILE A 135    14662  18123  13922   3319    -66  -2326       C
ATOM   1912  CG2 ILE A 135     -20.678  40.659   2.148  1.00119.22           C
ANISOU 1912  CG2 ILE A 135    14337  16622  14341   3342   -340  -2197       C
ATOM   1913  CD1 ILE A 135     -22.057  38.267   3.645  1.00120.53           C
ANISOU 1913  CD1 ILE A 135    14223  17911  13662   2945     63  -1940       C
ATOM   1914  H   ILE A 135     -24.654  41.072   2.986  1.00152.66           H
ATOM   1915  HA  ILE A 135     -22.203  42.578   3.422  1.00151.37           H
ATOM   1916  HB  ILE A 135     -22.712  40.067   1.788  1.00145.85           H
ATOM   1917 HG12 ILE A 135     -21.484  40.122   4.583  1.00147.51           H
ATOM   1918 HG13 ILE A 135     -23.211  39.914   4.348  1.00147.51           H
ATOM   1919 HG21 ILE A 135     -20.254  39.662   2.117  1.00143.07           H
ATOM   1920 HG22 ILE A 135     -20.562  41.080   1.151  1.00143.07           H
ATOM   1921 HG23 ILE A 135     -20.106  41.258   2.854  1.00143.07           H
ATOM   1922 HD11 ILE A 135     -22.245  37.728   4.574  1.00144.64           H
ATOM   1923 HD12 ILE A 135     -22.757  37.919   2.885  1.00144.64           H
ATOM   1924 HD13 ILE A 135     -21.041  38.038   3.325  1.00144.64           H
ATOM   1925  N   GLN A 136     -23.621  42.955   0.515  1.00135.55           N
ANISOU 1925  N   GLN A 136    16178  19132  16191   4200     61  -2821       N
ATOM   1926  CA  GLN A 136     -23.631  43.845  -0.659  1.00136.41           C
ANISOU 1926  CA  GLN A 136    16291  18888  16651   4410     45  -2898       C
ATOM   1927  C   GLN A 136     -23.578  45.323  -0.254  1.00135.55           C
ANISOU 1927  C   GLN A 136    16379  18558  16564   4707   -187  -3245       C
ATOM   1928  O   GLN A 136     -22.949  46.134  -0.943  1.00134.92           O
ANISOU 1928  O   GLN A 136    16418  17959  16886   4747   -384  -3238       O
ATOM   1929  H   GLN A 136     -24.431  42.372   0.682  1.00162.65           H
ATOM   1930  CB  GLN A 136     -24.899  43.587  -1.496  1.00  0.00           C
ATOM   1931  CG  GLN A 136     -25.021  44.439  -2.772  1.00  0.00           C
ATOM   1932  CD  GLN A 136     -23.971  44.062  -3.806  1.00  0.00           C
ATOM   1933  NE2 GLN A 136     -22.796  44.650  -3.765  1.00  0.00           N
ATOM   1934  OE1 GLN A 136     -24.164  43.166  -4.607  1.00  0.00           O
ATOM   1935  HA  GLN A 136     -22.751  43.624  -1.263  1.00  0.00           H
ATOM   1936  HB2 GLN A 136     -24.942  42.535  -1.779  1.00  0.00           H
ATOM   1937  HB3 GLN A 136     -25.763  43.804  -0.875  1.00  0.00           H
ATOM   1938  HG2 GLN A 136     -26.004  44.269  -3.213  1.00  0.00           H
ATOM   1939  HG3 GLN A 136     -24.952  45.503  -2.543  1.00  0.00           H
ATOM   1940 HE21 GLN A 136     -22.112  44.322  -4.429  1.00  0.00           H
ATOM   1941 HE22 GLN A 136     -22.587  45.341  -3.059  1.00  0.00           H
ATOM   1942  N   GLN A 137     -24.306  45.691   0.799  1.00117.52           N
ANISOU 1942  N   GLN A 137    14134  16665  13853   4924   -166  -3547       N
ATOM   1943  CA  GLN A 137     -24.107  46.951   1.511  1.00117.84           C
ANISOU 1943  CA  GLN A 137    14394  16527  13852   5176   -417  -3875       C
ATOM   1944  C   GLN A 137     -22.858  46.862   2.393  1.00128.66           C
ANISOU 1944  C   GLN A 137    15946  17677  15260   4976   -682  -3805       C
ATOM   1945  O   GLN A 137     -22.250  45.793   2.511  1.00127.37           O
ANISOU 1945  O   GLN A 137    15732  17685  14977   4687   -631  -3576       O
ATOM   1946  H   GLN A 137     -24.738  44.938   1.329  1.00141.02           H
ATOM   1947  CB  GLN A 137     -25.378  47.294   2.315  1.00  0.00           C
ATOM   1948  CG  GLN A 137     -26.562  47.675   1.405  1.00  0.00           C
ATOM   1949  CD  GLN A 137     -26.219  48.841   0.480  1.00  0.00           C
ATOM   1950  NE2 GLN A 137     -26.382  48.703  -0.817  1.00  0.00           N
ATOM   1951  OE1 GLN A 137     -25.652  49.839   0.893  1.00  0.00           O
ATOM   1952  HA  GLN A 137     -23.917  47.743   0.790  1.00  0.00           H
ATOM   1953  HB2 GLN A 137     -25.666  46.443   2.937  1.00  0.00           H
ATOM   1954  HB3 GLN A 137     -25.172  48.138   2.976  1.00  0.00           H
ATOM   1955  HG2 GLN A 137     -27.410  47.971   2.026  1.00  0.00           H
ATOM   1956  HG3 GLN A 137     -26.869  46.809   0.816  1.00  0.00           H
ATOM   1957 HE21 GLN A 137     -26.758  47.857  -1.204  1.00  0.00           H
ATOM   1958 HE22 GLN A 137     -26.030  49.451  -1.386  1.00  0.00           H
ATOM   1959  N   ARG A 138     -22.360  47.973   2.938  1.00142.95           N
ANISOU 1959  N   ARG A 138    17971  19098  17246   5129   -974  -4002       N
ATOM   1960  CA  ARG A 138     -21.095  48.038   3.716  1.00143.44           C
ANISOU 1960  CA  ARG A 138    18233  18873  17393   4983  -1277  -3975       C
ATOM   1961  C   ARG A 138     -19.812  47.653   2.939  0.50101.94           C
ANISOU 1961  C   ARG A 138    12971  13102  12660   4705  -1391  -3634       C
ATOM   1962  O   ARG A 138     -18.736  47.955   3.440  0.50 91.70           O
ANISOU 1962  O   ARG A 138    11841  11473  11530   4591  -1670  -3595       O
ATOM   1963  CB  ARG A 138     -21.206  47.177   5.004  1.00106.81           C
ANISOU 1963  CB  ARG A 138    13614  14651  12317   4815  -1249  -3944       C
ATOM   1964  CG  ARG A 138     -22.537  47.264   5.782  0.50 98.60           C
ANISOU 1964  CG  ARG A 138    12564  14173  10726   5066  -1107  -4238       C
ATOM   1965  CD  ARG A 138     -22.627  46.275   6.961  0.50 99.48           C
ANISOU 1965  CD  ARG A 138    12692  14683  10423   4892  -1075  -4181       C
ATOM   1966  NE  ARG A 138     -22.818  44.863   6.546  0.50 96.93           N
ANISOU 1966  NE  ARG A 138    12143  14626  10062   4590   -819  -3843       N
ATOM   1967  CZ  ARG A 138     -21.897  43.911   6.382  0.50 94.55           C
ANISOU 1967  CZ  ARG A 138    11814  14104  10005   4237   -870  -3510       C
ATOM   1968  NH1 ARG A 138     -20.621  44.080   6.533  0.50 94.31           N
ANISOU 1968  NH1 ARG A 138    11960  13581  10291   4127  -1165  -3454       N
ATOM   1969  NH2 ARG A 138     -22.276  42.679   6.126  0.50 92.43           N
ANISOU 1969  NH2 ARG A 138    11340  14110   9669   3991   -626  -3226       N
ATOM   1970  H   ARG A 138     -22.877  48.835   2.792  0.50171.54           H
ATOM   1971  HA  ARG A 138     -20.931  49.071   4.021  0.50172.12           H
ATOM   1972  HB2 ARG A 138     -21.045  46.137   4.725  0.50128.17           H
ATOM   1973  HB3 ARG A 138     -20.393  47.461   5.676  0.50128.17           H
ATOM   1974  HG2 ARG A 138     -22.644  48.282   6.165  0.50118.32           H
ATOM   1975  HG3 ARG A 138     -23.380  47.063   5.123  0.50118.32           H
ATOM   1976  HD2 ARG A 138     -21.749  46.378   7.598  0.50119.38           H
ATOM   1977  HD3 ARG A 138     -23.495  46.565   7.556  0.50119.38           H
ATOM   1978  HE  ARG A 138     -23.792  44.546   6.414  0.50116.32           H
ATOM   1979 HH11 ARG A 138     -20.289  45.014   6.623  0.50113.17           H
ATOM   1980 HH12 ARG A 138     -20.071  43.260   6.388  0.50113.17           H
ATOM   1981 HH21 ARG A 138     -23.291  42.575   6.148  0.50110.91           H
ATOM   1982 HH22 ARG A 138     -21.678  41.839   6.106  0.50110.91           H
ATOM   1983  N   GLY A 139     -19.898  47.014   1.766  0.50 92.64           N
ANISOU 1983  N   GLY A 139    11613  11841  11747   4599  -1191  -3381       N
ATOM   1984  CA  GLY A 139     -18.755  46.495   1.002  0.50102.99           C
ANISOU 1984  CA  GLY A 139    12913  12693  13526   4329  -1276  -3031       C
ATOM   1985  C   GLY A 139     -17.953  45.432   1.762  0.50113.27           C
ANISOU 1985  C   GLY A 139    14254  14036  14746   3999  -1360  -2809       C
ATOM   1986  O   GLY A 139     -16.738  45.563   1.885  0.50106.65           O
ANISOU 1986  O   GLY A 139    13509  12754  14259   3825  -1571  -2625       O
ATOM   1987  H   GLY A 139     -20.810  46.655   1.514  0.50111.17           H
ATOM   1988  HA2 GLY A 139     -19.126  46.040   0.082  0.50123.59           H
ATOM   1989  HA3 GLY A 139     -18.091  47.317   0.742  0.50123.59           H
ATOM   1990  N   GLY A 140     -18.634  44.531   2.481  1.00132.36           N
ANISOU 1990  N   GLY A 140    16599  16982  16710   3910  -1197  -2817       N
ATOM   1991  CA  GLY A 140     -17.968  43.588   3.387  1.00133.97           C
ANISOU 1991  CA  GLY A 140    16848  17260  16793   3609  -1278  -2632       C
ATOM   1992  C   GLY A 140     -17.071  42.585   2.640  1.00123.32           C
ANISOU 1992  C   GLY A 140    15413  15622  15822   3282  -1242  -2210       C
ATOM   1993  O   GLY A 140     -17.538  41.927   1.720  1.00120.56           O
ANISOU 1993  O   GLY A 140    14895  15295  15617   3230  -1018  -2020       O
ATOM   1994  H   GLY A 140     -19.625  44.419   2.293  1.00158.83           H
ATOM   1995  HA2 GLY A 140     -17.371  44.153   4.103  1.00160.76           H
ATOM   1996  HA3 GLY A 140     -18.728  43.033   3.935  1.00160.76           H
ATOM   1997  N   GLU A 141     -15.835  42.344   3.104  1.00114.81           N
ANISOU 1997  N   GLU A 141    14457  14263  14901   3063  -1469  -2060       N
ATOM   1998  CA  GLU A 141     -14.882  41.399   2.450  1.00109.04           C
ANISOU 1998  CA  GLU A 141    13661  13249  14519   2744  -1453  -1651       C
ATOM   1999  C   GLU A 141     -15.308  39.915   2.574  1.00107.60           C
ANISOU 1999  C   GLU A 141    13316  13488  14081   2489  -1197  -1413       C
ATOM   2000  O   GLU A 141     -14.788  39.039   1.870  1.00103.78           O
ANISOU 2000  O   GLU A 141    12748  12822  13862   2243  -1124  -1065       O
ATOM   2001  H   GLU A 141     -15.471  42.957   3.817  1.00137.77           H
ATOM   2002  CB  GLU A 141     -13.469  41.600   3.046  1.00  0.00           C
ATOM   2003  CG  GLU A 141     -12.274  40.829   2.423  1.00  0.00           C
ATOM   2004  CD  GLU A 141     -12.069  40.932   0.900  1.00  0.00           C
ATOM   2005  OE2 GLU A 141     -11.644  39.910   0.280  1.00  0.00           O
ATOM   2006  OE1 GLU A 141     -12.494  41.912   0.264  1.00  0.00           O
ATOM   2007  HA  GLU A 141     -14.847  41.646   1.389  1.00  0.00           H
ATOM   2008  HB2 GLU A 141     -13.242  42.669   3.031  1.00  0.00           H
ATOM   2009  HB3 GLU A 141     -13.525  41.314   4.102  1.00  0.00           H
ATOM   2010  HG2 GLU A 141     -11.372  41.192   2.917  1.00  0.00           H
ATOM   2011  HG3 GLU A 141     -12.372  39.782   2.693  1.00  0.00           H
ATOM   2012  N   GLU A 142     -16.232  39.626   3.505  1.00109.66           N
ANISOU 2012  N   GLU A 142    13528  14298  13839   2546  -1060  -1584       N
ATOM   2013  CA  GLU A 142     -16.863  38.313   3.677  1.00105.53           C
ANISOU 2013  CA  GLU A 142    12845  14193  13058   2306   -824  -1363       C
ATOM   2014  C   GLU A 142     -17.492  37.837   2.364  1.00104.16           C
ANISOU 2014  C   GLU A 142    12472  14092  13012   2302   -551  -1195       C
ATOM   2015  O   GLU A 142     -18.094  38.606   1.618  1.00100.91           O
ANISOU 2015  O   GLU A 142    12025  13611  12706   2556   -487  -1351       O
ATOM   2016  CB  GLU A 142     -17.915  38.333   4.811  1.00106.74           C
ANISOU 2016  CB  GLU A 142    12990  14923  12645   2404   -740  -1600       C
ATOM   2017  CG  GLU A 142     -18.450  36.917   5.110  1.00104.34           C
ANISOU 2017  CG  GLU A 142    12525  15069  12050   2147   -516  -1375       C
ATOM   2018  CD  GLU A 142     -19.378  36.809   6.319  1.00108.03           C
ANISOU 2018  CD  GLU A 142    12973  16112  11960   2268   -420  -1605       C
ATOM   2019  OE1 GLU A 142     -19.844  37.861   6.818  1.00110.48           O
ANISOU 2019  OE1 GLU A 142    13384  16494  12100   2577   -496  -1948       O
ATOM   2020  OE2 GLU A 142     -19.579  35.647   6.747  1.00107.53           O
ANISOU 2020  OE2 GLU A 142    12796  16430  11631   2059   -266  -1438       O
ATOM   2021  H   GLU A 142     -16.689  40.412   3.932  1.00131.59           H
ATOM   2022  HA  GLU A 142     -16.084  37.602   3.953  1.00126.63           H
ATOM   2023  HB2 GLU A 142     -17.449  38.738   5.712  1.00128.09           H
ATOM   2024  HB3 GLU A 142     -18.742  38.989   4.526  1.00128.09           H
ATOM   2025  HG2 GLU A 142     -18.985  36.548   4.235  1.00125.20           H
ATOM   2026  HG3 GLU A 142     -17.588  36.268   5.268  1.00125.20           H
ATOM   2027  N   ARG A 143     -17.392  36.539   2.085  1.00112.42           N
ANISOU 2027  N   ARG A 143    13392  15276  14045   2009   -396   -874       N
ATOM   2028  CA  ARG A 143     -18.072  35.918   0.954  1.00114.45           C
ANISOU 2028  CA  ARG A 143    13462  15631  14390   1969   -138   -687       C
ATOM   2029  C   ARG A 143     -18.805  34.672   1.405  1.00113.00           C
ANISOU 2029  C   ARG A 143    13131  15965  13840   1762     70   -543       C
ATOM   2030  O   ARG A 143     -18.285  33.889   2.200  1.00117.25           O
ANISOU 2030  O   ARG A 143    13711  16635  14203   1548      3   -450       O
ATOM   2031  CB  ARG A 143     -17.077  35.641  -0.172  1.00105.60           C
ANISOU 2031  CB  ARG A 143    12346  14002  13775   1808   -175   -365       C
ATOM   2032  CG  ARG A 143     -16.595  36.943  -0.826  1.00103.95           C
ANISOU 2032  CG  ARG A 143    12249  13279  13970   2023   -343   -474       C
ATOM   2033  CD  ARG A 143     -15.508  36.644  -1.855  1.00102.50           C
ANISOU 2033  CD  ARG A 143    12072  12602  14273   1849   -380   -126       C
ATOM   2034  NE  ARG A 143     -14.941  37.890  -2.411  1.00102.18           N
ANISOU 2034  NE  ARG A 143    12124  12059  14639   2050   -533   -203       N
ATOM   2035  CZ  ARG A 143     -14.033  38.637  -1.799  1.00102.89           C
ANISOU 2035  CZ  ARG A 143    12373  11770  14951   2062   -811   -252       C
ATOM   2036  NH1 ARG A 143     -13.568  38.311  -0.635  1.00104.64           N
ANISOU 2036  NH1 ARG A 143    12688  12048  15023   1888   -973   -242       N
ATOM   2037  NH2 ARG A 143     -13.491  39.684  -2.351  1.00101.77           N
ANISOU 2037  NH2 ARG A 143    12296  11184  15187   2250   -932   -309       N
ATOM   2038  H   ARG A 143     -16.883  35.941   2.730  1.00134.90           H
ATOM   2039  HA  ARG A 143     -18.831  36.606   0.577  1.00137.34           H
ATOM   2040  HB2 ARG A 143     -16.226  35.084   0.225  1.00126.72           H
ATOM   2041  HB3 ARG A 143     -17.573  35.038  -0.925  1.00126.72           H
ATOM   2042  HG2 ARG A 143     -17.429  37.453  -1.311  1.00124.74           H
ATOM   2043  HG3 ARG A 143     -16.178  37.602  -0.067  1.00124.74           H
ATOM   2044  HD2 ARG A 143     -14.727  36.075  -1.353  1.00123.01           H
ATOM   2045  HD3 ARG A 143     -15.923  36.023  -2.654  1.00123.01           H
ATOM   2046  HE  ARG A 143     -15.358  38.226  -3.268  1.00122.61           H
ATOM   2047 HH11 ARG A 143     -14.274  38.070   0.051  1.00125.57           H
ATOM   2048 HH12 ARG A 143     -12.878  38.953  -0.238  1.00125.57           H
ATOM   2049 HH21 ARG A 143     -13.963  40.126  -3.117  1.00122.12           H
ATOM   2050 HH22 ARG A 143     -12.940  40.277  -1.729  1.00122.12           H
ATOM   2051  N   LEU A 144     -19.942  34.424   0.766  1.00100.77           N
ANISOU 2051  N   LEU A 144    11406  14703  12178   1827    317   -523       N
ATOM   2052  CA  LEU A 144     -20.803  33.276   1.012  1.00 96.21           C
ANISOU 2052  CA  LEU A 144    10664  14629  11261   1652    529   -388       C
ATOM   2053  C   LEU A 144     -20.959  32.418  -0.245  1.00 72.91           C
ANISOU 2053  C   LEU A 144     7569  11604   8531   1503    707    -87       C
ATOM   2054  O   LEU A 144     -20.847  32.895  -1.383  1.00 64.38           O
ANISOU 2054  O   LEU A 144     6507  10138   7818   1591    695    -29       O
ATOM   2055  H   LEU A 144     -20.263  35.113   0.098  1.00120.92           H
ATOM   2056  CB  LEU A 144     -22.164  33.745   1.562  1.00  0.00           C
ATOM   2057  CG  LEU A 144     -22.115  34.550   2.877  1.00  0.00           C
ATOM   2058  CD2 LEU A 144     -21.563  33.743   4.050  1.00  0.00           C
ATOM   2059  CD1 LEU A 144     -23.527  34.991   3.244  1.00  0.00           C
ATOM   2060  HA  LEU A 144     -20.339  32.651   1.773  1.00  0.00           H
ATOM   2061  HB2 LEU A 144     -22.647  34.363   0.802  1.00  0.00           H
ATOM   2062  HB3 LEU A 144     -22.789  32.867   1.727  1.00  0.00           H
ATOM   2063  HG  LEU A 144     -21.500  35.439   2.743  1.00  0.00           H
ATOM   2064 HD21 LEU A 144     -21.642  34.326   4.971  1.00  0.00           H
ATOM   2065 HD22 LEU A 144     -20.510  33.550   3.885  1.00  0.00           H
ATOM   2066 HD23 LEU A 144     -22.109  32.808   4.169  1.00  0.00           H
ATOM   2067 HD11 LEU A 144     -23.481  35.554   4.174  1.00  0.00           H
ATOM   2068 HD12 LEU A 144     -23.931  35.635   2.461  1.00  0.00           H
ATOM   2069 HD13 LEU A 144     -24.177  34.126   3.379  1.00  0.00           H
ATOM   2070  N   TYR A 145     -21.206  31.128  -0.039  1.00 65.11           N
ANISOU 2070  N   TYR A 145     6439  10990   7309   1279    872    108       N
ATOM   2071  CA  TYR A 145     -21.451  30.160  -1.106  1.00 63.34           C
ANISOU 2071  CA  TYR A 145     6088  10711   7266   1107   1030    415       C
ATOM   2072  C   TYR A 145     -22.517  29.157  -0.649  1.00 71.64           C
ANISOU 2072  C   TYR A 145     6956  12331   7933    976   1234    494       C
ATOM   2073  O   TYR A 145     -22.240  28.280   0.168  1.00 93.06           O
ANISOU 2073  O   TYR A 145     9661  15240  10458    732   1222    634       O
ATOM   2074  CB  TYR A 145     -20.103  29.505  -1.467  1.00 64.98           C
ANISOU 2074  CB  TYR A 145     6384  10500   7803    833    918    734       C
ATOM   2075  CG  TYR A 145     -19.900  28.961  -2.874  1.00 62.02           C
ANISOU 2075  CG  TYR A 145     5954   9844   7768    757   1018   1004       C
ATOM   2076  CD1 TYR A 145     -20.969  28.684  -3.751  1.00 61.54           C
ANISOU 2076  CD1 TYR A 145     5740  10006   7638    842   1221   1016       C
ATOM   2077  CD2 TYR A 145     -18.576  28.835  -3.336  1.00 60.57           C
ANISOU 2077  CD2 TYR A 145     5874   9166   7974    608    904   1253       C
ATOM   2078  CE1 TYR A 145     -20.708  28.347  -5.094  1.00 54.67           C
ANISOU 2078  CE1 TYR A 145     4835   8869   7068    783   1304   1258       C
ATOM   2079  CE2 TYR A 145     -18.312  28.462  -4.666  1.00 57.79           C
ANISOU 2079  CE2 TYR A 145     5484   8552   7921    554    997   1503       C
ATOM   2080  CZ  TYR A 145     -19.380  28.225  -5.555  1.00 55.25           C
ANISOU 2080  CZ  TYR A 145     5022   8455   7514    645   1194   1500       C
ATOM   2081  OH  TYR A 145     -19.109  27.903  -6.850  1.00 54.54           O
ANISOU 2081  OH  TYR A 145     4911   8098   7714    601   1280   1745       O
ATOM   2082  H   TYR A 145     -21.121  30.781   0.916  1.00 78.13           H
ATOM   2083  HA  TYR A 145     -21.829  30.689  -1.979  1.00 76.00           H
ATOM   2084  HB2 TYR A 145     -19.340  30.275  -1.357  1.00 77.97           H
ATOM   2085  HB3 TYR A 145     -19.860  28.724  -0.744  1.00 77.97           H
ATOM   2086  HD1 TYR A 145     -21.995  28.769  -3.417  1.00 73.85           H
ATOM   2087  HD2 TYR A 145     -17.757  29.060  -2.662  1.00 72.69           H
ATOM   2088  HE1 TYR A 145     -21.533  28.230  -5.773  1.00 65.60           H
ATOM   2089  HE2 TYR A 145     -17.289  28.395  -5.004  1.00 69.35           H
ATOM   2090  HH  TYR A 145     -18.164  28.003  -6.997  1.00 65.45           H
ATOM   2091  N   LEU A 146     -23.739  29.283  -1.170  1.00 74.67           N
ANISOU 2091  N   LEU A 146     7192  12971   8209   1138   1414    409       N
ATOM   2092  CA  LEU A 146     -24.786  28.271  -1.005  1.00 74.35           C
ANISOU 2092  CA  LEU A 146     6957  13457   7836   1022   1612    500       C
ATOM   2093  C   LEU A 146     -24.420  27.038  -1.846  1.00 76.40           C
ANISOU 2093  C   LEU A 146     7134  13619   8274    735   1699    875       C
ATOM   2094  O   LEU A 146     -24.160  27.175  -3.047  1.00 72.35           O
ANISOU 2094  O   LEU A 146     6634  12761   8093    766   1714    989       O
ATOM   2095  CB  LEU A 146     -26.140  28.895  -1.400  1.00 68.75           C
ANISOU 2095  CB  LEU A 146     6115  13052   6957   1306   1765    275       C
ATOM   2096  CG  LEU A 146     -27.378  28.011  -1.147  1.00 66.72           C
ANISOU 2096  CG  LEU A 146     5640  13378   6332   1229   1970    334       C
ATOM   2097  CD1 LEU A 146     -28.608  28.893  -0.918  1.00 68.11           C
ANISOU 2097  CD1 LEU A 146     5735  13899   6245   1556   2064     16       C
ATOM   2098  CD2 LEU A 146     -27.707  27.091  -2.329  1.00 64.25           C
ANISOU 2098  CD2 LEU A 146     5184  13057   6170   1056   2109    624       C
ATOM   2099  H   LEU A 146     -23.887  29.987  -1.885  1.00 89.61           H
ATOM   2100  HA  LEU A 146     -24.841  27.981   0.045  1.00 89.22           H
ATOM   2101  HB2 LEU A 146     -26.252  29.811  -0.819  1.00 82.50           H
ATOM   2102  HB3 LEU A 146     -26.110  29.177  -2.449  1.00 82.50           H
ATOM   2103  HG  LEU A 146     -27.213  27.410  -0.254  1.00 80.06           H
ATOM   2104 HD11 LEU A 146     -28.453  29.516  -0.037  1.00  0.00           H
ATOM   2105 HD12 LEU A 146     -28.786  29.535  -1.780  1.00  0.00           H
ATOM   2106 HD13 LEU A 146     -29.490  28.278  -0.743  1.00  0.00           H
ATOM   2107 HD21 LEU A 146     -26.901  26.385  -2.508  1.00  0.00           H
ATOM   2108 HD22 LEU A 146     -27.886  27.680  -3.227  1.00  0.00           H
ATOM   2109 HD23 LEU A 146     -28.606  26.524  -2.103  1.00  0.00           H
ATOM   2110  N   GLN A 147     -24.434  25.842  -1.250  1.00 77.20           N
ANISOU 2110  N   GLN A 147     7156  14027   8149    463   1757   1067       N
ATOM   2111  CA  GLN A 147     -24.278  24.568  -1.967  1.00 72.56           C
ANISOU 2111  CA  GLN A 147     6486  13403   7682    178   1843   1424       C
ATOM   2112  C   GLN A 147     -25.209  23.500  -1.385  1.00 73.78           C
ANISOU 2112  C   GLN A 147     6564  13957   7512     27   1901   1453       C
ATOM   2113  O   GLN A 147     -24.839  22.815  -0.435  1.00 77.92           O
ANISOU 2113  O   GLN A 147     7091  14716   7798   -112   1868   1472       O
ATOM   2114  CB  GLN A 147     -22.815  24.076  -1.968  1.00 69.04           C
ANISOU 2114  CB  GLN A 147     6185  12561   7486    -72   1697   1663       C
ATOM   2115  CG  GLN A 147     -21.867  25.037  -2.698  1.00 68.36           C
ANISOU 2115  CG  GLN A 147     6268  11894   7813     64   1550   1624       C
ATOM   2116  CD  GLN A 147     -20.485  24.471  -3.005  1.00 67.98           C
ANISOU 2116  CD  GLN A 147     6330  11444   8055   -196   1443   1927       C
ATOM   2117  OE1 GLN A 147     -20.244  23.280  -3.149  1.00 68.22           O
ANISOU 2117  OE1 GLN A 147     6313  11621   7988   -483   1485   2175       O
ATOM   2118  NE2 GLN A 147     -19.535  25.326  -3.308  1.00 63.52           N
ANISOU 2118  NE2 GLN A 147     5910  10369   7854    -95   1304   1916       N
ATOM   2119  H   GLN A 147     -24.661  25.803  -0.256  1.00 92.64           H
ATOM   2120  HA  GLN A 147     -24.568  24.720  -3.001  1.00 87.08           H
ATOM   2121  HB2 GLN A 147     -22.467  23.936  -0.944  1.00 82.85           H
ATOM   2122  HB3 GLN A 147     -22.794  23.107  -2.469  1.00 82.85           H
ATOM   2123  HG2 GLN A 147     -22.317  25.330  -3.644  1.00 82.04           H
ATOM   2124  HG3 GLN A 147     -21.741  25.928  -2.083  1.00 82.04           H
ATOM   2125 HE21 GLN A 147     -19.718  26.312  -3.211  1.00 76.22           H
ATOM   2126 HE22 GLN A 147     -18.621  24.941  -3.400  1.00 76.22           H
ATOM   2127  N   GLN A 148     -26.349  23.254  -2.034  1.00 70.23           N
ANISOU 2127  N   GLN A 148     6132  13438   7115     60   1908   1420       N
ATOM   2128  CA  GLN A 148     -27.381  22.339  -1.533  1.00 73.17           C
ANISOU 2128  CA  GLN A 148     6497  14021   7281    -45   1882   1410       C
ATOM   2129  C   GLN A 148     -27.816  21.322  -2.592  1.00 73.07           C
ANISOU 2129  C   GLN A 148     6569  13703   7492   -150   1828   1526       C
ATOM   2130  O   GLN A 148     -27.996  21.658  -3.766  1.00 66.97           O
ANISOU 2130  O   GLN A 148     5815  12720   6910    -30   1858   1495       O
ATOM   2131  CB  GLN A 148     -28.561  23.159  -0.981  1.00 78.69           C
ANISOU 2131  CB  GLN A 148     7083  15125   7690    193   1967   1159       C
ATOM   2132  CG  GLN A 148     -29.689  22.329  -0.337  1.00 83.51           C
ANISOU 2132  CG  GLN A 148     7656  15963   8111    102   1947   1170       C
ATOM   2133  CD  GLN A 148     -29.202  21.452   0.812  1.00 87.85           C
ANISOU 2133  CD  GLN A 148     8228  16631   8521   -123   1879   1289       C
ATOM   2134  OE1 GLN A 148     -28.267  21.786   1.513  1.00 90.58           O
ANISOU 2134  OE1 GLN A 148     8586  17073   8758   -148   1874   1275       O
ATOM   2135  NE2 GLN A 148     -29.625  20.208   0.876  1.00 88.26           N
ANISOU 2135  NE2 GLN A 148     8286  16672   8577   -281   1821   1401       N
ATOM   2136  H   GLN A 148     -26.528  23.753  -2.899  1.00 84.28           H
ATOM   2137  HA  GLN A 148     -26.962  21.771  -0.700  1.00 87.80           H
ATOM   2138  HB2 GLN A 148     -28.179  23.859  -0.235  1.00 94.43           H
ATOM   2139  HB3 GLN A 148     -28.987  23.737  -1.802  1.00 94.43           H
ATOM   2140  HG2 GLN A 148     -30.445  23.002   0.067  1.00100.21           H
ATOM   2141  HG3 GLN A 148     -30.172  21.716  -1.096  1.00100.21           H
ATOM   2142 HE21 GLN A 148     -30.437  19.942   0.351  1.00105.92           H
ATOM   2143 HE22 GLN A 148     -29.368  19.747   1.734  1.00105.92           H
ATOM   2144  N   THR A 149     -27.979  20.057  -2.192  1.00 83.76           N
ANISOU 2144  N   THR A 149     7978  15032   8814   -354   1743   1640       N
ATOM   2145  CA  THR A 149     -28.536  19.022  -3.078  1.00 87.37           C
ANISOU 2145  CA  THR A 149     8514  15250   9433   -428   1685   1711       C
ATOM   2146  C   THR A 149     -30.046  19.221  -3.209  1.00 88.28           C
ANISOU 2146  C   THR A 149     8523  15610   9410   -302   1748   1599       C
ATOM   2147  O   THR A 149     -30.753  19.300  -2.196  1.00 93.19           O
ANISOU 2147  O   THR A 149     9028  16611   9768   -246   1792   1510       O
ATOM   2148  CB  THR A 149     -28.220  17.598  -2.602  1.00 87.00           C
ANISOU 2148  CB  THR A 149     8551  15115   9390   -644   1572   1834       C
ATOM   2149  OG1 THR A 149     -26.823  17.383  -2.542  1.00 86.55           O
ANISOU 2149  OG1 THR A 149     8595  14840   9449   -756   1508   1926       O
ATOM   2150  CG2 THR A 149     -28.742  16.533  -3.561  1.00 85.34           C
ANISOU 2150  CG2 THR A 149     8439  14633   9355   -696   1504   1885       C
ATOM   2151  H   THR A 149     -27.857  19.843  -1.212  1.00100.51           H
ATOM   2152  HA  THR A 149     -28.088  19.140  -4.062  1.00104.84           H
ATOM   2153  HB  THR A 149     -28.646  17.435  -1.613  1.00104.40           H
ATOM   2154  HG1 THR A 149     -26.662  16.824  -1.781  1.00103.85           H
ATOM   2155 HG21 THR A 149     -28.422  15.543  -3.239  1.00102.41           H
ATOM   2156 HG22 THR A 149     -29.828  16.546  -3.585  1.00102.41           H
ATOM   2157 HG23 THR A 149     -28.372  16.740  -4.564  1.00102.41           H
ATOM   2158  N   LEU A 150     -30.546  19.239  -4.449  1.00 83.96           N
ANISOU 2158  N   LEU A 150     8020  14841   9039   -253   1746   1602       N
ATOM   2159  CA  LEU A 150     -31.981  19.295  -4.739  1.00 87.50           C
ANISOU 2159  CA  LEU A 150     8376  15482   9387   -145   1794   1515       C
ATOM   2160  C   LEU A 150     -32.703  18.071  -4.145  1.00 90.88           C
ANISOU 2160  C   LEU A 150     8769  16082   9681   -279   1739   1584       C
ATOM   2161  O   LEU A 150     -32.221  16.943  -4.236  1.00 89.15           O
ANISOU 2161  O   LEU A 150     8645  15667   9562   -445   1644   1705       O
ATOM   2162  CB  LEU A 150     -32.235  19.413  -6.256  1.00 88.18           C
ANISOU 2162  CB  LEU A 150     8532  15271   9702    -84   1792   1515       C
ATOM   2163  CG  LEU A 150     -31.530  20.585  -6.971  1.00 87.42           C
ANISOU 2163  CG  LEU A 150     8475  14959   9782     54   1838   1458       C
ATOM   2164  CD1 LEU A 150     -31.905  20.594  -8.454  1.00 84.39           C
ANISOU 2164  CD1 LEU A 150     8161  14300   9605    105   1826   1458       C
ATOM   2165  CD2 LEU A 150     -31.914  21.948  -6.396  1.00 89.39           C
ANISOU 2165  CD2 LEU A 150     8601  15489   9873    271   1939   1280       C
ATOM   2166  H   LEU A 150     -29.905  19.113  -5.225  1.00100.75           H
ATOM   2167  HA  LEU A 150     -32.387  20.184  -4.253  1.00104.99           H
ATOM   2168  HB2 LEU A 150     -31.924  18.480  -6.730  1.00105.82           H
ATOM   2169  HB3 LEU A 150     -33.312  19.513  -6.408  1.00105.82           H
ATOM   2170  HG  LEU A 150     -30.450  20.461  -6.899  1.00104.91           H
ATOM   2171 HD11 LEU A 150     -31.652  19.636  -8.901  1.00  0.00           H
ATOM   2172 HD12 LEU A 150     -31.355  21.381  -8.971  1.00  0.00           H
ATOM   2173 HD13 LEU A 150     -32.976  20.769  -8.565  1.00  0.00           H
ATOM   2174 HD21 LEU A 150     -31.484  22.065  -5.402  1.00  0.00           H
ATOM   2175 HD22 LEU A 150     -32.998  22.040  -6.341  1.00  0.00           H
ATOM   2176 HD23 LEU A 150     -31.529  22.741  -7.035  1.00  0.00           H
ATOM   2177  N   ASN A 151     -33.847  18.318  -3.516  1.00 96.64           N
ANISOU 2177  N   ASN A 151     9359  17173  10186   -189   1797   1497       N
ATOM   2178  CA  ASN A 151     -34.653  17.346  -2.777  1.00 97.44           C
ANISOU 2178  CA  ASN A 151     9394  17488  10140   -296   1757   1560       C
ATOM   2179  C   ASN A 151     -36.153  17.659  -2.980  1.00 95.91           C
ANISOU 2179  C   ASN A 151     9086  17504   9853   -172   1814   1488       C
ATOM   2180  O   ASN A 151     -36.499  18.435  -3.867  1.00 98.33           O
ANISOU 2180  O   ASN A 151     9390  17726  10245    -27   1866   1403       O
ATOM   2181  CB  ASN A 151     -34.190  17.361  -1.305  1.00 98.41           C
ANISOU 2181  CB  ASN A 151     9456  17899  10035   -345   1761   1548       C
ATOM   2182  CG  ASN A 151     -34.365  18.716  -0.648  1.00101.38           C
ANISOU 2182  CG  ASN A 151     9732  18584  10202   -146   1864   1372       C
ATOM   2183  OD1 ASN A 151     -35.470  19.148  -0.379  1.00104.86           O
ANISOU 2183  OD1 ASN A 151    10060  19305  10478    -25   1921   1282       O
ATOM   2184  ND2 ASN A 151     -33.318  19.498  -0.522  1.00101.09           N
ANISOU 2184  ND2 ASN A 151     9741  18498  10172    -98   1885   1316       N
ATOM   2185  H   ASN A 151     -34.212  19.259  -3.539  1.00115.97           H
ATOM   2186  HA  ASN A 151     -34.481  16.345  -3.176  1.00116.93           H
ATOM   2187  HB2 ASN A 151     -34.759  16.631  -0.727  1.00118.09           H
ATOM   2188  HB3 ASN A 151     -33.141  17.073  -1.255  1.00118.09           H
ATOM   2189 HD21 ASN A 151     -33.485  20.397  -0.099  1.00121.31           H
ATOM   2190 HD22 ASN A 151     -32.429  19.232  -0.919  1.00121.31           H
ATOM   2191  N   ASP A 152     -37.045  16.978  -2.265  0.80 80.78           N
ANISOU 2191  N   ASP A 152     7068  15859   7764   -227   1802   1525       N
ATOM   2192  CA  ASP A 152     -38.504  17.070  -2.407  0.80 76.13           C
ANISOU 2192  CA  ASP A 152     6355  15488   7084   -135   1838   1496       C
ATOM   2193  C   ASP A 152     -39.124  18.362  -1.842  0.80 81.03           C
ANISOU 2193  C   ASP A 152     6874  16391   7524     77   1950   1317       C
ATOM   2194  O   ASP A 152     -40.182  18.772  -2.318  0.80 82.23           O
ANISOU 2194  O   ASP A 152     6947  16653   7643    190   1995   1263       O
ATOM   2195  H   ASP A 152     -36.735  16.434  -1.462  0.80 96.93           H
ATOM   2196  CB  ASP A 152     -39.151  15.857  -1.713  1.00  0.00           C
ATOM   2197  CG  ASP A 152     -38.821  15.729  -0.218  1.00  0.00           C
ATOM   2198  OD1 ASP A 152     -37.622  15.875   0.127  1.00  0.00           O
ATOM   2199  OD2 ASP A 152     -39.721  15.271   0.516  1.00  0.00           O
ATOM   2200  HA  ASP A 152     -38.758  17.036  -3.467  0.80  0.00           H
ATOM   2201  HB2 ASP A 152     -38.802  14.955  -2.217  1.00  0.00           H
ATOM   2202  HB3 ASP A 152     -40.231  15.910  -1.851  1.00  0.00           H
ATOM   2203  N   THR A 153     -38.455  19.052  -0.911  0.80 85.84           N
ANISOU 2203  N   THR A 153     7480  17136   8001    144   1987   1222       N
ATOM   2204  CA  THR A 153     -38.973  20.278  -0.258  0.80 90.13           C
ANISOU 2204  CA  THR A 153     7929  17982   8334    367   2079   1035       C
ATOM   2205  C   THR A 153     -39.084  21.491  -1.200  0.80 88.34           C
ANISOU 2205  C   THR A 153     7736  17611   8218    573   2132    886       C
ATOM   2206  O   THR A 153     -39.688  22.502  -0.829  0.80 85.13           O
ANISOU 2206  O   THR A 153     7281  17408   7656    786   2198    701       O
ATOM   2207  CB  THR A 153     -38.152  20.660   0.992  0.80 96.29           C
ANISOU 2207  CB  THR A 153     8710  18953   8924    384   2093    966       C
ATOM   2208  OG1 THR A 153     -36.870  21.132   0.654  0.80 94.65           O
ANISOU 2208  OG1 THR A 153     8615  18493   8855    380   2076    946       O
ATOM   2209  CG2 THR A 153     -37.953  19.504   1.979  0.80 98.66           C
ANISOU 2209  CG2 THR A 153     8984  19375   9126    176   2036   1113       C
ATOM   2210  H   THR A 153     -37.590  18.655  -0.563  0.80103.01           H
ATOM   2211  HA  THR A 153     -39.987  20.068   0.079  0.80108.16           H
ATOM   2212  HB  THR A 153     -38.678  21.460   1.516  0.80115.55           H
ATOM   2213  HG1 THR A 153     -36.365  20.369   0.318  0.80113.58           H
ATOM   2214 HG21 THR A 153     -37.406  19.863   2.851  0.80118.39           H
ATOM   2215 HG22 THR A 153     -38.920  19.120   2.301  0.80118.39           H
ATOM   2216 HG23 THR A 153     -37.386  18.692   1.521  0.80118.39           H
ATOM   2217  N   VAL A 154     -38.580  21.387  -2.437  1.00 90.57           N
ANISOU 2217  N   VAL A 154     8109  17541   8762    525   2101    951       N
ATOM   2218  CA  VAL A 154     -38.603  22.467  -3.436  1.00 86.65           C
ANISOU 2218  CA  VAL A 154     7652  16873   8398    714   2145    816       C
ATOM   2219  C   VAL A 154     -40.026  22.810  -3.918  1.00 87.84           C
ANISOU 2219  C   VAL A 154     7724  17128   8522    834   2184    753       C
ATOM   2220  O   VAL A 154     -40.814  21.937  -4.295  1.00 85.55           O
ANISOU 2220  O   VAL A 154     7379  16909   8215    724   2159    868       O
ATOM   2221  CB  VAL A 154     -37.649  22.213  -4.621  1.00 82.44           C
ANISOU 2221  CB  VAL A 154     7251  15912   8161    618   2098    916       C
ATOM   2222  CG1 VAL A 154     -36.186  22.089  -4.176  1.00 81.23           C
ANISOU 2222  CG1 VAL A 154     7170  15658   8037    522   2067    970       C
ATOM   2223  CG2 VAL A 154     -38.023  20.985  -5.452  1.00 79.05           C
ANISOU 2223  CG2 VAL A 154     6856  15315   7864    437   2033   1089       C
ATOM   2224  H   VAL A 154     -38.198  20.492  -2.704  1.00108.68           H
ATOM   2225  HA  VAL A 154     -38.214  23.334  -2.925  1.00103.98           H
ATOM   2226  HB  VAL A 154     -37.707  23.079  -5.281  1.00 98.93           H
ATOM   2227 HG11 VAL A 154     -35.545  21.980  -5.050  1.00 97.48           H
ATOM   2228 HG12 VAL A 154     -35.895  22.989  -3.633  1.00 97.48           H
ATOM   2229 HG13 VAL A 154     -36.060  21.222  -3.528  1.00 97.48           H
ATOM   2230 HG21 VAL A 154     -37.314  20.841  -6.266  1.00 94.86           H
ATOM   2231 HG22 VAL A 154     -38.048  20.096  -4.826  1.00 94.86           H
ATOM   2232 HG23 VAL A 154     -39.010  21.136  -5.867  1.00 94.86           H
ATOM   2233  N   GLY A 155     -40.344  24.099  -4.047  1.00 89.46           N
ANISOU 2233  N   GLY A 155     7927  17333   8731   1064   2240    567       N
ATOM   2234  CA  GLY A 155     -41.686  24.545  -4.443  1.00 90.35           C
ANISOU 2234  CA  GLY A 155     7967  17556   8807   1199   2280    487       C
ATOM   2235  C   GLY A 155     -42.066  24.293  -5.914  1.00 88.36           C
ANISOU 2235  C   GLY A 155     7749  17050   8774   1111   2251    597       C
ATOM   2236  O   GLY A 155     -41.234  24.034  -6.791  1.00 87.73           O
ANISOU 2236  O   GLY A 155     7764  16681   8888    964   2198    723       O
ATOM   2237  H   GLY A 155     -39.683  24.785  -3.697  1.00107.35           H
ATOM   2238  HA2 GLY A 155     -42.402  24.006  -3.824  1.00108.42           H
ATOM   2239  HA3 GLY A 155     -41.809  25.602  -4.208  1.00108.42           H
ATOM   2240  N   ARG A 156     -43.379  24.340  -6.206  1.00 85.37           N
ANISOU 2240  N   ARG A 156     6112  17881   8445   1219    910   2005       N
ATOM   2241  CA  ARG A 156     -44.007  23.735  -7.412  1.00 83.37           C
ANISOU 2241  CA  ARG A 156     5845  17514   8320   1025    862   2173       C
ATOM   2242  C   ARG A 156     -43.324  24.100  -8.733  1.00 78.63           C
ANISOU 2242  C   ARG A 156     5415  16446   8014   1083    852   2050       C
ATOM   2243  O   ARG A 156     -43.227  23.225  -9.593  1.00 76.05           O
ANISOU 2243  O   ARG A 156     5165  15857   7872    833    797   2200       O
ATOM   2244  H   ARG A 156     -43.984  24.546  -5.421  1.00102.45           H
ATOM   2245  CB  ARG A 156     -45.506  24.109  -7.481  1.00  0.00           C
ATOM   2246  CG  ARG A 156     -46.330  23.484  -8.635  1.00  0.00           C
ATOM   2247  CD  ARG A 156     -46.603  21.972  -8.540  1.00  0.00           C
ATOM   2248  NE  ARG A 156     -45.417  21.123  -8.788  1.00  0.00           N
ATOM   2249  CZ  ARG A 156     -45.280  19.861  -8.407  1.00  0.00           C
ATOM   2250  NH1 ARG A 156     -46.187  19.239  -7.706  1.00  0.00           N
ATOM   2251  NH2 ARG A 156     -44.225  19.169  -8.719  1.00  0.00           N
ATOM   2252  HA  ARG A 156     -43.912  22.657  -7.307  1.00  0.00           H
ATOM   2253  HB2 ARG A 156     -45.576  25.194  -7.589  1.00  0.00           H
ATOM   2254  HB3 ARG A 156     -45.984  23.848  -6.537  1.00  0.00           H
ATOM   2255  HG2 ARG A 156     -47.306  23.974  -8.626  1.00  0.00           H
ATOM   2256  HG3 ARG A 156     -45.879  23.714  -9.601  1.00  0.00           H
ATOM   2257  HD2 ARG A 156     -47.360  21.721  -9.287  1.00  0.00           H
ATOM   2258  HD3 ARG A 156     -47.023  21.763  -7.555  1.00  0.00           H
ATOM   2259  HE  ARG A 156     -44.663  21.533  -9.327  1.00  0.00           H
ATOM   2260 HH11 ARG A 156     -47.019  19.729  -7.436  1.00  0.00           H
ATOM   2261 HH12 ARG A 156     -46.037  18.294  -7.404  1.00  0.00           H
ATOM   2262 HH21 ARG A 156     -44.108  18.236  -8.366  1.00  0.00           H
ATOM   2263 HH22 ARG A 156     -43.490  19.585  -9.263  1.00  0.00           H
ATOM   2264  N   LYS A 157     -42.986  25.383  -8.928  1.00 78.30           N
ANISOU 2264  N   LYS A 157     5433  16297   8019   1418    885   1780       N
ATOM   2265  CA  LYS A 157     -42.371  25.915 -10.161  1.00 78.80           C
ANISOU 2265  CA  LYS A 157     5640  15949   8351   1487    862   1686       C
ATOM   2266  C   LYS A 157     -40.928  25.425 -10.355  1.00 75.88           C
ANISOU 2266  C   LYS A 157     5421  15232   8177   1313    844   1737       C
ATOM   2267  O   LYS A 157     -40.622  24.966 -11.447  1.00 72.85           O
ANISOU 2267  O   LYS A 157     5131  14549   8000   1219    804   1786       O
ATOM   2268  H   LYS A 157     -43.068  25.998  -8.132  1.00 93.96           H
ATOM   2269  CB  LYS A 157     -42.440  27.459 -10.196  1.00  0.00           C
ATOM   2270  CG  LYS A 157     -43.871  28.030 -10.298  1.00  0.00           C
ATOM   2271  CD  LYS A 157     -43.879  29.533 -10.646  1.00  0.00           C
ATOM   2272  CE  LYS A 157     -45.250  30.218 -10.513  1.00  0.00           C
ATOM   2273  NZ  LYS A 157     -45.826  30.112  -9.145  1.00  0.00           N
ATOM   2274  HA  LYS A 157     -42.918  25.540 -11.026  1.00  0.00           H
ATOM   2275  HB2 LYS A 157     -41.960  27.861  -9.305  1.00  0.00           H
ATOM   2276  HB3 LYS A 157     -41.872  27.804 -11.061  1.00  0.00           H
ATOM   2277  HG2 LYS A 157     -44.373  27.868  -9.344  1.00  0.00           H
ATOM   2278  HG3 LYS A 157     -44.418  27.496 -11.076  1.00  0.00           H
ATOM   2279  HD2 LYS A 157     -43.158  30.066 -10.029  1.00  0.00           H
ATOM   2280  HD3 LYS A 157     -43.538  29.650 -11.676  1.00  0.00           H
ATOM   2281  HE2 LYS A 157     -45.128  31.277 -10.764  1.00  0.00           H
ATOM   2282  HE3 LYS A 157     -45.931  29.786 -11.250  1.00  0.00           H
ATOM   2283  HZ1 LYS A 157     -46.709  30.609  -9.084  1.00  0.00           H
ATOM   2284  HZ2 LYS A 157     -45.981  29.146  -8.895  1.00  0.00           H
ATOM   2285  HZ3 LYS A 157     -45.187  30.501  -8.453  1.00  0.00           H
ATOM   2286  N   ILE A 158     -40.167  25.215  -9.279  1.00 76.15           N
ANISOU 2286  N   ILE A 158     5477  15320   8138   1275    870   1728       N
ATOM   2287  CA  ILE A 158     -38.817  24.627  -9.348  1.00 77.51           C
ANISOU 2287  CA  ILE A 158     5789  15179   8483   1125    854   1768       C
ATOM   2288  C   ILE A 158     -38.846  23.152  -9.767  1.00 76.25           C
ANISOU 2288  C   ILE A 158     5635  14949   8388    756    792   2033       C
ATOM   2289  O   ILE A 158     -38.097  22.778 -10.664  1.00 72.22           O
ANISOU 2289  O   ILE A 158     5243  14126   8072    628    748   2078       O
ATOM   2290  CB  ILE A 158     -38.063  24.827  -8.015  1.00 73.99           C
ANISOU 2290  CB  ILE A 158     5361  14824   7929   1204    895   1672       C
ATOM   2291  CG1 ILE A 158     -38.048  26.310  -7.581  1.00 75.88           C
ANISOU 2291  CG1 ILE A 158     5606  15108   8117   1593    921   1376       C
ATOM   2292  CG2 ILE A 158     -36.634  24.258  -8.086  1.00 73.02           C
ANISOU 2292  CG2 ILE A 158     5377  14391   7976   1052    878   1715       C
ATOM   2293  CD1 ILE A 158     -37.482  27.320  -8.582  1.00 72.82           C
ANISOU 2293  CD1 ILE A 158     5342  14354   7972   1781    886   1222       C
ATOM   2294  H   ILE A 158     -40.514  25.481  -8.368  1.00 91.38           H
ATOM   2295  HA  ILE A 158     -38.257  25.150 -10.124  1.00 93.02           H
ATOM   2296  HB  ILE A 158     -38.591  24.272  -7.239  1.00 88.79           H
ATOM   2297 HG12 ILE A 158     -39.069  26.611  -7.364  1.00 91.06           H
ATOM   2298 HG13 ILE A 158     -37.479  26.399  -6.660  1.00 91.06           H
ATOM   2299 HG21 ILE A 158     -36.105  24.462  -7.158  1.00 87.62           H
ATOM   2300 HG22 ILE A 158     -36.661  23.176  -8.217  1.00 87.62           H
ATOM   2301 HG23 ILE A 158     -36.082  24.706  -8.913  1.00 87.62           H
ATOM   2302 HD11 ILE A 158     -37.518  28.316  -8.139  1.00 87.38           H
ATOM   2303 HD12 ILE A 158     -36.449  27.076  -8.827  1.00 87.38           H
ATOM   2304 HD13 ILE A 158     -38.087  27.323  -9.487  1.00 87.38           H
ATOM   2305  N   VAL A 159     -39.838  22.363  -9.326  1.00 76.06           N
ANISOU 2305  N   VAL A 159     5480  15218   8201    585    768   2215       N
ATOM   2306  CA  VAL A 159     -40.039  21.002  -9.876  1.00 76.91           C
ANISOU 2306  CA  VAL A 159     5590  15245   8388    240    671   2468       C
ATOM   2307  C   VAL A 159     -40.447  21.027 -11.356  1.00 78.88           C
ANISOU 2307  C   VAL A 159     5873  15295   8804    214    618   2475       C
ATOM   2308  O   VAL A 159     -40.012  20.166 -12.113  1.00 75.27           O
ANISOU 2308  O   VAL A 159     5499  14585   8515     12    530   2576       O
ATOM   2309  CB  VAL A 159     -41.068  20.167  -9.087  1.00 83.18           C
ANISOU 2309  CB  VAL A 159     6221  16414   8969     70    638   2678       C
ATOM   2310  CG1 VAL A 159     -41.125  18.717  -9.600  1.00 82.90           C
ANISOU 2310  CG1 VAL A 159     6191  16266   9039   -290    502   2943       C
ATOM   2311  CG2 VAL A 159     -40.794  20.107  -7.587  1.00 82.66           C
ANISOU 2311  CG2 VAL A 159     6122  16556   8730     87    679   2687       C
ATOM   2312  H   VAL A 159     -40.396  22.685  -8.543  1.00 91.27           H
ATOM   2313  HA  VAL A 159     -39.083  20.481  -9.819  1.00 92.29           H
ATOM   2314  HB  VAL A 159     -42.049  20.621  -9.222  1.00 99.82           H
ATOM   2315 HG11 VAL A 159     -41.623  18.063  -8.885  1.00 99.48           H
ATOM   2316 HG12 VAL A 159     -41.655  18.672 -10.552  1.00 99.48           H
ATOM   2317 HG13 VAL A 159     -40.111  18.338  -9.751  1.00 99.48           H
ATOM   2318 HG21 VAL A 159     -41.541  19.495  -7.082  1.00 99.19           H
ATOM   2319 HG22 VAL A 159     -39.811  19.669  -7.408  1.00 99.19           H
ATOM   2320 HG23 VAL A 159     -40.840  21.106  -7.152  1.00 99.19           H
ATOM   2321  N   MET A 160     -41.270  21.989 -11.792  1.00 84.42           N
ANISOU 2321  N   MET A 160     6505  16116   9453    428    660   2363       N
ATOM   2322  CA  MET A 160     -41.615  22.139 -13.218  1.00 84.84           C
ANISOU 2322  CA  MET A 160     6589  15995   9653    431    613   2359       C
ATOM   2323  C   MET A 160     -40.383  22.493 -14.068  1.00 74.96           C
ANISOU 2323  C   MET A 160     5502  14361   8619    496    600   2254       C
ATOM   2324  O   MET A 160     -40.145  21.847 -15.085  1.00 73.92           O
ANISOU 2324  O   MET A 160     5427  14026   8632    353    520   2330       O
ATOM   2325  CB  MET A 160     -42.724  23.189 -13.412  1.00 87.50           C
ANISOU 2325  CB  MET A 160     6829  16528   9890    683    662   2242       C
ATOM   2326  CG  MET A 160     -44.077  22.774 -12.816  1.00 94.18           C
ANISOU 2326  CG  MET A 160     7492  17781  10512    611    662   2368       C
ATOM   2327  SD  MET A 160     -44.926  21.379 -13.609  1.00 98.84           S
ANISOU 2327  SD  MET A 160     8014  18390  11151    258    544   2638       S
ATOM   2328  CE  MET A 160     -45.291  22.076 -15.246  1.00 93.63           C
ANISOU 2328  CE  MET A 160     7389  17558  10628    426    534   2518       C
ATOM   2329  H   MET A 160     -41.530  22.727 -11.152  1.00101.30           H
ATOM   2330  HA  MET A 160     -41.983  21.184 -13.594  1.00101.81           H
ATOM   2331  HB2 MET A 160     -42.422  24.127 -12.952  1.00105.00           H
ATOM   2332  HB3 MET A 160     -42.852  23.382 -14.476  1.00105.00           H
ATOM   2333  HG2 MET A 160     -43.931  22.511 -11.772  1.00113.02           H
ATOM   2334  HG3 MET A 160     -44.743  23.637 -12.846  1.00113.02           H
ATOM   2335  HE1 MET A 160     -45.850  21.348 -15.833  1.00112.35           H
ATOM   2336  HE2 MET A 160     -45.885  22.983 -15.140  1.00112.35           H
ATOM   2337  HE3 MET A 160     -44.363  22.308 -15.769  1.00112.35           H
ATOM   2338  N   ASP A 161     -39.508  23.360 -13.552  1.00 64.03           N
ANISOU 2338  N   ASP A 161     4188  12887   7254    716    665   2081       N
ATOM   2339  CA  ASP A 161     -38.230  23.707 -14.182  1.00 67.63           C
ANISOU 2339  CA  ASP A 161     4791  13000   7904    764    647   2010       C
ATOM   2340  C   ASP A 161     -37.261  22.513 -14.240  1.00 61.07           C
ANISOU 2340  C   ASP A 161     4033  12017   7155    496    587   2143       C
ATOM   2341  O   ASP A 161     -36.740  22.204 -15.308  1.00 58.45           O
ANISOU 2341  O   ASP A 161     3843  11399   6968    413    510   2156       O
ATOM   2342  CB  ASP A 161     -37.588  24.896 -13.448  1.00 65.18           C
ANISOU 2342  CB  ASP A 161     4532  12638   7596   1029    709   1818       C
ATOM   2343  CG  ASP A 161     -38.454  26.155 -13.416  1.00 71.25           C
ANISOU 2343  CG  ASP A 161     5237  13539   8294   1322    737   1664       C
ATOM   2344  OD1 ASP A 161     -39.260  26.370 -14.351  1.00 68.12           O
ANISOU 2344  OD1 ASP A 161     4795  13180   7910   1344    713   1696       O
ATOM   2345  OD2 ASP A 161     -38.050  27.110 -12.716  1.00 71.86           O
ANISOU 2345  OD2 ASP A 161     5313  13684   8306   1539    771   1501       O
ATOM   2346  H   ASP A 161     -39.775  23.869 -12.717  1.00 76.83           H
ATOM   2347  HA  ASP A 161     -38.432  24.013 -15.208  1.00 81.15           H
ATOM   2348  HB2 ASP A 161     -37.370  24.609 -12.420  1.00 78.22           H
ATOM   2349  HB3 ASP A 161     -36.641  25.143 -13.929  1.00 78.22           H
ATOM   2350  N   PHE A 162     -37.174  21.735 -13.156  1.00 64.04           N
ANISOU 2350  N   PHE A 162     4376  12533   7422    361    599   2220       N
ATOM   2351  CA  PHE A 162     -36.369  20.514 -13.047  1.00 65.49           C
ANISOU 2351  CA  PHE A 162     4653  12550   7679    104    517   2345       C
ATOM   2352  C   PHE A 162     -36.834  19.401 -14.000  1.00 62.37           C
ANISOU 2352  C   PHE A 162     4252  12066   7379   -118    388   2494       C
ATOM   2353  O   PHE A 162     -36.018  18.764 -14.663  1.00 64.26           O
ANISOU 2353  O   PHE A 162     4685  11978   7754   -208    284   2477       O
ATOM   2354  CB  PHE A 162     -36.427  20.040 -11.585  1.00 67.86           C
ANISOU 2354  CB  PHE A 162     4871  13090   7824    -17    541   2450       C
ATOM   2355  CG  PHE A 162     -35.553  18.843 -11.271  1.00 68.60           C
ANISOU 2355  CG  PHE A 162     5083  12989   7992   -257    448   2567       C
ATOM   2356  CD1 PHE A 162     -34.200  19.041 -10.943  1.00 64.07           C
ANISOU 2356  CD1 PHE A 162     4714  12163   7467   -184    460   2433       C
ATOM   2357  CD2 PHE A 162     -36.079  17.536 -11.312  1.00 71.32           C
ANISOU 2357  CD2 PHE A 162     5367  13370   8360   -555    321   2800       C
ATOM   2358  CE1 PHE A 162     -33.373  17.938 -10.670  1.00 66.96           C
ANISOU 2358  CE1 PHE A 162     5219  12329   7894   -381    360   2520       C
ATOM   2359  CE2 PHE A 162     -35.250  16.434 -11.033  1.00 69.55           C
ANISOU 2359  CE2 PHE A 162     5298  12915   8214   -757    199   2888       C
ATOM   2360  CZ  PHE A 162     -33.896  16.635 -10.712  1.00 67.12           C
ANISOU 2360  CZ  PHE A 162     5190  12369   7942   -659    225   2743       C
ATOM   2361  H   PHE A 162     -37.649  22.056 -12.319  1.00 76.84           H
ATOM   2362  HA  PHE A 162     -35.333  20.747 -13.299  1.00 78.58           H
ATOM   2363  HB2 PHE A 162     -36.127  20.863 -10.936  1.00 81.43           H
ATOM   2364  HB3 PHE A 162     -37.458  19.791 -11.335  1.00 81.43           H
ATOM   2365  HD1 PHE A 162     -33.793  20.041 -10.913  1.00 76.89           H
ATOM   2366  HD2 PHE A 162     -37.115  17.376 -11.570  1.00 85.58           H
ATOM   2367  HE1 PHE A 162     -32.329  18.085 -10.445  1.00 80.35           H
ATOM   2368  HE2 PHE A 162     -35.645  15.429 -11.087  1.00 83.46           H
ATOM   2369  HZ  PHE A 162     -33.249  15.790 -10.522  1.00 80.54           H
ATOM   2370  N   LEU A 163     -38.146  19.196 -14.147  1.00 64.86           N
ANISOU 2370  N   LEU A 163     4421  12617   7607   -190    367   2600       N
ATOM   2371  CA  LEU A 163     -38.720  18.254 -15.119  1.00 64.23           C
ANISOU 2371  CA  LEU A 163     4322  12463   7621   -394    226   2731       C
ATOM   2372  C   LEU A 163     -38.539  18.714 -16.575  1.00 58.44           C
ANISOU 2372  C   LEU A 163     3649  11529   7026   -262    203   2620       C
ATOM   2373  O   LEU A 163     -38.408  17.871 -17.459  1.00 60.03           O
ANISOU 2373  O   LEU A 163     3938  11533   7337   -404     58   2661       O
ATOM   2374  CB  LEU A 163     -40.214  18.063 -14.812  1.00 68.14           C
ANISOU 2374  CB  LEU A 163     4666  13249   7976   -478    211   2854       C
ATOM   2375  CG  LEU A 163     -40.517  17.290 -13.515  1.00 68.56           C
ANISOU 2375  CG  LEU A 163     4645  13519   7887   -667    190   3030       C
ATOM   2376  CD1 LEU A 163     -42.020  17.366 -13.238  1.00 71.00           C
ANISOU 2376  CD1 LEU A 163     4783  14175   8018   -679    206   3127       C
ATOM   2377  CD2 LEU A 163     -40.123  15.814 -13.595  1.00 66.13           C
ANISOU 2377  CD2 LEU A 163     4400  13021   7706   -992      9   3218       C
ATOM   2378  H   LEU A 163     -38.779  19.758 -13.587  1.00 77.83           H
ATOM   2379  HA  LEU A 163     -38.210  17.294 -15.036  1.00 77.08           H
ATOM   2380  HB2 LEU A 163     -40.673  19.052 -14.754  1.00 81.77           H
ATOM   2381  HB3 LEU A 163     -40.679  17.533 -15.645  1.00 81.77           H
ATOM   2382  HG  LEU A 163     -39.985  17.733 -12.676  1.00 82.27           H
ATOM   2383 HD11 LEU A 163     -42.315  18.411 -13.140  1.00  0.00           H
ATOM   2384 HD12 LEU A 163     -42.570  16.914 -14.063  1.00  0.00           H
ATOM   2385 HD13 LEU A 163     -42.252  16.841 -12.313  1.00  0.00           H
ATOM   2386 HD21 LEU A 163     -39.043  15.723 -13.697  1.00  0.00           H
ATOM   2387 HD22 LEU A 163     -40.608  15.341 -14.448  1.00  0.00           H
ATOM   2388 HD23 LEU A 163     -40.422  15.306 -12.679  1.00  0.00           H
ATOM   2389  N   GLY A 164     -38.445  20.024 -16.813  1.00 58.26           N
ANISOU 2389  N   GLY A 164     3650  11496   6990     17    316   2456       N
ATOM   2390  CA  GLY A 164     -38.150  20.610 -18.122  1.00 59.02           C
ANISOU 2390  CA  GLY A 164     3853  11376   7198    151    290   2353       C
ATOM   2391  C   GLY A 164     -36.678  20.528 -18.562  1.00 55.55           C
ANISOU 2391  C   GLY A 164     3664  10572   6871    156    240   2263       C
ATOM   2392  O   GLY A 164     -36.352  21.015 -19.644  1.00 58.82           O
ANISOU 2392  O   GLY A 164     4164  10824   7360    264    218   2193       O
ATOM   2393  H   GLY A 164     -38.591  20.662 -16.037  1.00 69.91           H
ATOM   2394  HA2 GLY A 164     -38.756  20.113 -18.880  1.00 70.83           H
ATOM   2395  HA3 GLY A 164     -38.443  21.659 -18.096  1.00 70.83           H
ATOM   2396  N   PHE A 165     -35.771  20.002 -17.730  1.00 50.81           N
ANISOU 2396  N   PHE A 165     3170   9863   6272     48    221   2271       N
ATOM   2397  CA  PHE A 165     -34.366  19.765 -18.101  1.00 50.61           C
ANISOU 2397  CA  PHE A 165     3365   9524   6340     48    164   2191       C
ATOM   2398  C   PHE A 165     -34.259  18.729 -19.244  1.00 50.20           C
ANISOU 2398  C   PHE A 165     3373   9339   6363    -75      7   2227       C
ATOM   2399  O   PHE A 165     -35.105  17.840 -19.365  1.00 48.80           O
ANISOU 2399  O   PHE A 165     3088   9275   6179   -222    -83   2334       O
ATOM   2400  CB  PHE A 165     -33.566  19.324 -16.853  1.00 53.39           C
ANISOU 2400  CB  PHE A 165     3804   9811   6669    -43    165   2198       C
ATOM   2401  CG  PHE A 165     -33.299  20.343 -15.745  1.00 54.01           C
ANISOU 2401  CG  PHE A 165     3860   9986   6677    106    302   2119       C
ATOM   2402  CD1 PHE A 165     -33.778  21.666 -15.807  1.00 52.90           C
ANISOU 2402  CD1 PHE A 165     3641   9947   6511    320    395   2033       C
ATOM   2403  CD2 PHE A 165     -32.551  19.948 -14.617  1.00 49.41           C
ANISOU 2403  CD2 PHE A 165     3340   9380   6054     44    316   2118       C
ATOM   2404  CE1 PHE A 165     -33.512  22.576 -14.770  1.00 48.63           C
ANISOU 2404  CE1 PHE A 165     3093   9475   5912    477    486   1930       C
ATOM   2405  CE2 PHE A 165     -32.267  20.862 -13.583  1.00 49.03           C
ANISOU 2405  CE2 PHE A 165     3272   9423   5933    193    424   2023       C
ATOM   2406  CZ  PHE A 165     -32.746  22.181 -13.661  1.00 53.28           C
ANISOU 2406  CZ  PHE A 165     3739  10052   6451    414    502   1919       C
ATOM   2407  H   PHE A 165     -36.087  19.659 -16.834  1.00 60.97           H
ATOM   2408  HA  PHE A 165     -33.942  20.697 -18.473  1.00 60.73           H
ATOM   2409  HB2 PHE A 165     -34.085  18.486 -16.402  1.00 64.06           H
ATOM   2410  HB3 PHE A 165     -32.601  18.937 -17.177  1.00 64.06           H
ATOM   2411  HD1 PHE A 165     -34.390  21.989 -16.632  1.00 63.48           H
ATOM   2412  HD2 PHE A 165     -32.197  18.930 -14.542  1.00 59.29           H
ATOM   2413  HE1 PHE A 165     -33.928  23.570 -14.822  1.00 58.36           H
ATOM   2414  HE2 PHE A 165     -31.693  20.545 -12.725  1.00 58.83           H
ATOM   2415  HZ  PHE A 165     -32.544  22.886 -12.867  1.00 63.93           H
ATOM   2416  N   ASN A 166     -33.196  18.773 -20.064  1.00 50.99           N
ANISOU 2416  N   ASN A 166     3637   9209   6527     -7    -37   2132       N
ATOM   2417  CA  ASN A 166     -32.978  17.813 -21.170  1.00 49.29           C
ANISOU 2417  CA  ASN A 166     3488   8874   6365    -68   -196   2120       C
ATOM   2418  C   ASN A 166     -32.521  16.417 -20.678  1.00 51.07           C
ANISOU 2418  C   ASN A 166     3813   8967   6623   -249   -345   2153       C
ATOM   2419  O   ASN A 166     -31.441  15.919 -21.022  1.00 52.77           O
ANISOU 2419  O   ASN A 166     4183   8996   6869   -222   -413   2069       O
ATOM   2420  CB  ASN A 166     -32.072  18.406 -22.273  1.00 47.94           C
ANISOU 2420  CB  ASN A 166     3420   8577   6218    100   -181   2012       C
ATOM   2421  CG  ASN A 166     -32.155  17.640 -23.591  1.00 50.00           C
ANISOU 2421  CG  ASN A 166     3712   8787   6500     91   -335   1977       C
ATOM   2422  OD1 ASN A 166     -32.701  16.548 -23.703  1.00 46.14           O
ANISOU 2422  OD1 ASN A 166     3210   8287   6033    -54   -486   2014       O
ATOM   2423  ND2 ASN A 166     -31.583  18.175 -24.641  1.00 44.43           N
ANISOU 2423  ND2 ASN A 166     3041   8057   5785    245   -314   1911       N
ATOM   2424  H   ASN A 166     -32.528  19.522 -19.917  1.00 61.18           H
ATOM   2425  HA  ASN A 166     -33.954  17.659 -21.635  1.00 59.14           H
ATOM   2426  HB2 ASN A 166     -32.370  19.437 -22.467  1.00 57.53           H
ATOM   2427  HB3 ASN A 166     -31.033  18.399 -21.952  1.00 57.53           H
ATOM   2428 HD21 ASN A 166     -31.638  17.688 -25.514  1.00 53.32           H
ATOM   2429 HD22 ASN A 166     -31.024  19.019 -24.532  1.00 53.32           H
ATOM   2430  N   TRP A 167     -33.397  15.742 -19.930  1.00 55.41           N
ANISOU 2430  N   TRP A 167     4260   9632   7162   -439   -408   2290       N
ATOM   2431  CA  TRP A 167     -33.220  14.374 -19.441  1.00 54.57           C
ANISOU 2431  CA  TRP A 167     4241   9389   7103   -639   -582   2359       C
ATOM   2432  C   TRP A 167     -32.985  13.368 -20.577  1.00 56.10           C
ANISOU 2432  C   TRP A 167     4549   9382   7384   -673   -812   2293       C
ATOM   2433  O   TRP A 167     -32.137  12.493 -20.437  1.00 56.27           O
ANISOU 2433  O   TRP A 167     4719   9199   7463   -746   -975   2267       O
ATOM   2434  CB  TRP A 167     -34.427  13.984 -18.575  1.00 53.30           C
ANISOU 2434  CB  TRP A 167     3913   9431   6907   -857   -605   2565       C
ATOM   2435  CG  TRP A 167     -34.586  14.805 -17.332  1.00 54.16           C
ANISOU 2435  CG  TRP A 167     3903   9775   6902   -797   -392   2607       C
ATOM   2436  CD1 TRP A 167     -35.560  15.719 -17.109  1.00 58.36           C
ANISOU 2436  CD1 TRP A 167     4237  10598   7341   -711   -242   2639       C
ATOM   2437  CD2 TRP A 167     -33.700  14.877 -16.164  1.00 53.51           C
ANISOU 2437  CD2 TRP A 167     3889   9666   6776   -789   -318   2599       C
ATOM   2438  NE1 TRP A 167     -35.351  16.328 -15.890  1.00 58.74           N
ANISOU 2438  NE1 TRP A 167     4229  10805   7286   -638    -86   2636       N
ATOM   2439  CE2 TRP A 167     -34.204  15.879 -15.284  1.00 54.22           C
ANISOU 2439  CE2 TRP A 167     3817  10043   6742   -693   -127   2616       C
ATOM   2440  CE3 TRP A 167     -32.494  14.245 -15.778  1.00 52.53           C
ANISOU 2440  CE3 TRP A 167     3946   9314   6699   -841   -402   2569       C
ATOM   2441  CZ2 TRP A 167     -33.547  16.260 -14.108  1.00 59.12           C
ANISOU 2441  CZ2 TRP A 167     4451  10731   7282   -650    -22   2598       C
ATOM   2442  CZ3 TRP A 167     -31.830  14.610 -14.588  1.00 51.62           C
ANISOU 2442  CZ3 TRP A 167     3841   9262   6508   -813   -289   2570       C
ATOM   2443  CH2 TRP A 167     -32.354  15.614 -13.752  1.00 56.40           C
ANISOU 2443  CH2 TRP A 167     4284  10157   6988   -721   -101   2582       C
ATOM   2444  H   TRP A 167     -34.216  16.254 -19.608  1.00 66.49           H
ATOM   2445  HA  TRP A 167     -32.349  14.353 -18.794  1.00 65.48           H
ATOM   2446  HB2 TRP A 167     -35.339  14.058 -19.170  1.00 63.96           H
ATOM   2447  HB3 TRP A 167     -34.319  12.943 -18.269  1.00 63.96           H
ATOM   2448  HD1 TRP A 167     -36.353  15.986 -17.802  1.00 70.04           H
ATOM   2449  HE1 TRP A 167     -35.848  17.164 -15.585  1.00 70.49           H
ATOM   2450  HE3 TRP A 167     -32.068  13.483 -16.413  1.00 63.03           H
ATOM   2451  HZ2 TRP A 167     -33.961  17.047 -13.492  1.00 70.95           H
ATOM   2452  HZ3 TRP A 167     -30.904  14.125 -14.317  1.00 61.94           H
ATOM   2453  HH2 TRP A 167     -31.842  15.892 -12.840  1.00 67.68           H
ATOM   2454  N   ASN A 168     -33.586  13.577 -21.756  1.00 60.85           N
ANISOU 2454  N   ASN A 168     5087  10043   7991   -601   -841   2250       N
ATOM   2455  CA  ASN A 168     -33.350  12.756 -22.951  1.00 65.32           C
ANISOU 2455  CA  ASN A 168     5756  10442   8619   -592  -1066   2151       C
ATOM   2456  C   ASN A 168     -31.863  12.718 -23.356  1.00 65.01           C
ANISOU 2456  C   ASN A 168     5898  10223   8578   -429  -1089   1981       C
ATOM   2457  O   ASN A 168     -31.269  11.640 -23.435  1.00 66.94           O
ANISOU 2457  O   ASN A 168     6281  10275   8879   -466  -1307   1910       O
ATOM   2458  CB  ASN A 168     -34.241  13.282 -24.094  1.00 68.82           C
ANISOU 2458  CB  ASN A 168     6089  11019   9039   -496  -1053   2117       C
ATOM   2459  CG  ASN A 168     -34.068  12.481 -25.375  1.00 71.33           C
ANISOU 2459  CG  ASN A 168     6502  11200   9402   -463  -1295   1992       C
ATOM   2460  OD1 ASN A 168     -34.014  11.265 -25.374  1.00 75.56           O
ANISOU 2460  OD1 ASN A 168     7125  11566  10018   -610  -1541   1995       O
ATOM   2461  ND2 ASN A 168     -33.906  13.129 -26.504  1.00 68.90           N
ANISOU 2461  ND2 ASN A 168     6175  10964   9039   -261  -1242   1881       N
ATOM   2462  H   ASN A 168     -34.200  14.373 -21.834  1.00 73.02           H
ATOM   2463  HA  ASN A 168     -33.642  11.726 -22.737  1.00 78.38           H
ATOM   2464  HB2 ASN A 168     -35.288  13.223 -23.801  1.00 82.58           H
ATOM   2465  HB3 ASN A 168     -34.001  14.327 -24.290  1.00 82.58           H
ATOM   2466 HD21 ASN A 168     -33.813  12.564 -27.329  1.00 82.68           H
ATOM   2467 HD22 ASN A 168     -33.960  14.132 -26.536  1.00 82.68           H
ATOM   2468  N   TRP A 169     -31.220  13.884 -23.483  1.00 59.15           N
ANISOU 2468  N   TRP A 169     5154   9546   7774   -247   -881   1919       N
ATOM   2469  CA  TRP A 169     -29.796  13.962 -23.812  1.00 54.23           C
ANISOU 2469  CA  TRP A 169     4665   8809   7130    -88   -890   1776       C
ATOM   2470  C   TRP A 169     -28.886  13.385 -22.712  1.00 57.17           C
ANISOU 2470  C   TRP A 169     5162   9036   7525   -155   -928   1771       C
ATOM   2471  O   TRP A 169     -28.075  12.501 -23.004  1.00 56.69           O
ANISOU 2471  O   TRP A 169     5232   8828   7481   -113  -1089   1665       O
ATOM   2472  CB  TRP A 169     -29.425  15.404 -24.183  1.00 52.51           C
ANISOU 2472  CB  TRP A 169     4396   8701   6852     90   -675   1752       C
ATOM   2473  CG  TRP A 169     -27.966  15.597 -24.445  1.00 55.38           C
ANISOU 2473  CG  TRP A 169     4867   8994   7182    224   -661   1648       C
ATOM   2474  CD1 TRP A 169     -27.342  15.398 -25.628  1.00 54.66           C
ANISOU 2474  CD1 TRP A 169     4807   8920   7041    366   -742   1541       C
ATOM   2475  CD2 TRP A 169     -26.914  15.932 -23.490  1.00 55.33           C
ANISOU 2475  CD2 TRP A 169     4930   8922   7170    232   -565   1643       C
ATOM   2476  NE1 TRP A 169     -25.978  15.551 -25.463  1.00 54.61           N
ANISOU 2476  NE1 TRP A 169     4874   8881   6995    458   -696   1483       N
ATOM   2477  CE2 TRP A 169     -25.658  15.843 -24.157  1.00 55.45           C
ANISOU 2477  CE2 TRP A 169     5011   8921   7137    371   -591   1544       C
ATOM   2478  CE3 TRP A 169     -26.897  16.294 -22.127  1.00 53.58           C
ANISOU 2478  CE3 TRP A 169     4710   8681   6966    144   -463   1710       C
ATOM   2479  CZ2 TRP A 169     -24.443  16.045 -23.495  1.00 55.73           C
ANISOU 2479  CZ2 TRP A 169     5113   8907   7155    407   -522   1520       C
ATOM   2480  CZ3 TRP A 169     -25.682  16.517 -21.453  1.00 58.45           C
ANISOU 2480  CZ3 TRP A 169     5407   9232   7569    187   -399   1671       C
ATOM   2481  CH2 TRP A 169     -24.460  16.389 -22.134  1.00 57.66           C
ANISOU 2481  CH2 TRP A 169     5371   9101   7434    309   -429   1581       C
ATOM   2482  H   TRP A 169     -31.739  14.750 -23.363  1.00 70.98           H
ATOM   2483  HA  TRP A 169     -29.618  13.350 -24.696  1.00 65.07           H
ATOM   2484  HB2 TRP A 169     -29.986  15.698 -25.072  1.00 63.01           H
ATOM   2485  HB3 TRP A 169     -29.715  16.069 -23.369  1.00 63.01           H
ATOM   2486  HD1 TRP A 169     -27.843  15.147 -26.555  1.00 65.59           H
ATOM   2487  HE1 TRP A 169     -25.322  15.584 -26.234  1.00 65.53           H
ATOM   2488  HE3 TRP A 169     -27.834  16.411 -21.606  1.00 64.29           H
ATOM   2489  HZ2 TRP A 169     -23.508  15.949 -24.026  1.00 66.87           H
ATOM   2490  HZ3 TRP A 169     -25.681  16.793 -20.408  1.00 70.14           H
ATOM   2491  HH2 TRP A 169     -23.534  16.574 -21.612  1.00 69.19           H
ATOM   2492  N   ILE A 170     -29.067  13.772 -21.442  1.00 54.28           N
ANISOU 2492  N   ILE A 170     4752   8724   7148   -239   -787   1874       N
ATOM   2493  CA  ILE A 170     -28.134  13.357 -20.373  1.00 53.39           C
ANISOU 2493  CA  ILE A 170     4749   8495   7042   -285   -802   1872       C
ATOM   2494  C   ILE A 170     -28.285  11.880 -19.966  1.00 54.09           C
ANISOU 2494  C   ILE A 170     4915   8436   7202   -465  -1047   1927       C
ATOM   2495  O   ILE A 170     -27.278  11.178 -19.859  1.00 55.83           O
ANISOU 2495  O   ILE A 170     5277   8488   7448   -455  -1166   1864       O
ATOM   2496  CB  ILE A 170     -28.213  14.318 -19.169  1.00 54.93           C
ANISOU 2496  CB  ILE A 170     4867   8813   7192   -313   -595   1956       C
ATOM   2497  CG1 ILE A 170     -26.902  14.242 -18.358  1.00 55.69           C
ANISOU 2497  CG1 ILE A 170     5081   8803   7275   -288   -568   1909       C
ATOM   2498  CG2 ILE A 170     -29.457  14.068 -18.304  1.00 56.43           C
ANISOU 2498  CG2 ILE A 170     4937   9127   7378   -507   -614   2125       C
ATOM   2499  CD1 ILE A 170     -26.821  15.327 -17.283  1.00 56.20           C
ANISOU 2499  CD1 ILE A 170     5086   8981   7284   -253   -365   1935       C
ATOM   2500  H   ILE A 170     -29.765  14.483 -21.242  1.00 65.14           H
ATOM   2501  HA  ILE A 170     -27.129  13.456 -20.788  1.00 64.07           H
ATOM   2502  HB  ILE A 170     -28.284  15.328 -19.567  1.00 65.92           H
ATOM   2503 HG12 ILE A 170     -26.800  13.261 -17.896  1.00 66.83           H
ATOM   2504 HG13 ILE A 170     -26.057  14.383 -19.035  1.00 66.83           H
ATOM   2505 HG21 ILE A 170     -29.627  14.909 -17.632  1.00 67.72           H
ATOM   2506 HG22 ILE A 170     -30.321  13.967 -18.949  1.00 67.72           H
ATOM   2507 HG23 ILE A 170     -29.345  13.160 -17.711  1.00 67.72           H
ATOM   2508 HD11 ILE A 170     -25.860  15.287 -16.778  1.00 67.44           H
ATOM   2509 HD12 ILE A 170     -26.920  16.303 -17.750  1.00 67.44           H
ATOM   2510 HD13 ILE A 170     -27.606  15.186 -16.544  1.00 67.44           H
ATOM   2511  N   ASN A 171     -29.505  11.332 -20.005  1.00 61.51           N
ANISOU 2511  N   ASN A 171     5760   9431   8182   -636  -1144   2055       N
ATOM   2512  CA  ASN A 171     -29.739   9.893 -19.852  1.00 66.02           C
ANISOU 2512  CA  ASN A 171     6406   9831   8846   -833  -1421   2132       C
ATOM   2513  C   ASN A 171     -29.183   9.103 -21.055  1.00 64.77           C
ANISOU 2513  C   ASN A 171     6404   9459   8748   -724  -1666   1949       C
ATOM   2514  O   ASN A 171     -28.651   8.000 -20.881  1.00 68.38           O
ANISOU 2514  O   ASN A 171     7009   9694   9279   -784  -1895   1925       O
ATOM   2515  CB  ASN A 171     -31.243   9.624 -19.638  1.00 66.99           C
ANISOU 2515  CB  ASN A 171     6371  10085   8999  -1051  -1484   2324       C
ATOM   2516  CG  ASN A 171     -31.835  10.303 -18.407  1.00 66.88           C
ANISOU 2516  CG  ASN A 171     6194  10312   8906  -1166  -1282   2513       C
ATOM   2517  OD1 ASN A 171     -31.155  10.682 -17.468  1.00 71.54           O
ANISOU 2517  OD1 ASN A 171     6824  10909   9450  -1148  -1172   2528       O
ATOM   2518  ND2 ASN A 171     -33.139  10.446 -18.350  1.00 71.63           N
ANISOU 2518  ND2 ASN A 171     6599  11138   9477  -1271  -1236   2651       N
ATOM   2519  H   ASN A 171     -30.310  11.938 -20.130  1.00 73.82           H
ATOM   2520  HA  ASN A 171     -29.210   9.545 -18.961  1.00 79.22           H
ATOM   2521  HB2 ASN A 171     -31.792   9.951 -20.521  1.00 80.39           H
ATOM   2522  HB3 ASN A 171     -31.402   8.553 -19.524  1.00 80.39           H
ATOM   2523 HD21 ASN A 171     -33.495  10.916 -17.537  1.00 85.95           H
ATOM   2524 HD22 ASN A 171     -33.704  10.243 -19.152  1.00 85.95           H
ATOM   2525  N   LYS A 172     -29.159   9.690 -22.269  1.00 63.42           N
ANISOU 2525  N   LYS A 172     6200   9361   8536   -547  -1633   1814       N
ATOM   2526  CA  LYS A 172     -28.494   9.052 -23.418  1.00 64.51           C
ANISOU 2526  CA  LYS A 172     6468   9354   8689   -389  -1846   1607       C
ATOM   2527  C   LYS A 172     -26.971   9.043 -23.282  1.00 67.05           C
ANISOU 2527  C   LYS A 172     6918   9595   8963   -220  -1813   1472       C
ATOM   2528  O   LYS A 172     -26.369   8.052 -23.702  1.00 68.66           O
ANISOU 2528  O   LYS A 172     7266   9623   9199   -140  -2052   1328       O
ATOM   2529  H   LYS A 172     -29.597  10.601 -22.386  1.00 76.11           H
ATOM   2530  CB  LYS A 172     -28.930   9.653 -24.766  1.00  0.00           C
ATOM   2531  CG  LYS A 172     -28.495   8.834 -26.007  1.00  0.00           C
ATOM   2532  CD  LYS A 172     -29.163   7.448 -26.180  1.00  0.00           C
ATOM   2533  CE  LYS A 172     -28.621   6.267 -25.343  1.00  0.00           C
ATOM   2534  NZ  LYS A 172     -27.429   5.595 -25.921  1.00  0.00           N
ATOM   2535  HA  LYS A 172     -28.825   8.024 -23.380  1.00  0.00           H
ATOM   2536  HB2 LYS A 172     -28.512  10.658 -24.853  1.00  0.00           H
ATOM   2537  HB3 LYS A 172     -30.016   9.749 -24.782  1.00  0.00           H
ATOM   2538  HG2 LYS A 172     -28.775   9.429 -26.878  1.00  0.00           H
ATOM   2539  HG3 LYS A 172     -27.411   8.731 -26.038  1.00  0.00           H
ATOM   2540  HD2 LYS A 172     -29.122   7.175 -27.237  1.00  0.00           H
ATOM   2541  HD3 LYS A 172     -30.219   7.572 -25.936  1.00  0.00           H
ATOM   2542  HE2 LYS A 172     -29.427   5.532 -25.242  1.00  0.00           H
ATOM   2543  HE3 LYS A 172     -28.377   6.607 -24.338  1.00  0.00           H
ATOM   2544  HZ1 LYS A 172     -27.694   4.749 -26.412  1.00  0.00           H
ATOM   2545  HZ2 LYS A 172     -26.784   5.338 -25.180  1.00  0.00           H
ATOM   2546  HZ3 LYS A 172     -26.937   6.205 -26.556  1.00  0.00           H
ATOM   2547  N   GLN A 173     -26.366  10.089 -22.707  1.00 66.40           N
ANISOU 2547  N   GLN A 173     6784   9640   8804   -156  -1537   1509       N
ATOM   2548  CA  GLN A 173     -24.943  10.112 -22.337  1.00 63.43           C
ANISOU 2548  CA  GLN A 173     6511   9206   8383    -26  -1498   1409       C
ATOM   2549  C   GLN A 173     -24.602   9.075 -21.262  1.00 63.43           C
ANISOU 2549  C   GLN A 173     6630   9014   8456   -166  -1649   1464       C
ATOM   2550  O   GLN A 173     -23.838   8.158 -21.565  1.00 66.88           O
ANISOU 2550  O   GLN A 173     7199   9320   8891    -59  -1785   1337       O
ATOM   2551  CB  GLN A 173     -24.503  11.521 -21.892  1.00 60.34           C
ANISOU 2551  CB  GLN A 173     6033   8977   7915     42  -1191   1454       C
ATOM   2552  CG  GLN A 173     -24.414  12.524 -23.050  1.00 60.91           C
ANISOU 2552  CG  GLN A 173     6018   9214   7911    217  -1064   1391       C
ATOM   2553  CD  GLN A 173     -23.399  12.162 -24.128  1.00 61.94           C
ANISOU 2553  CD  GLN A 173     6211   9356   7968    421  -1146   1224       C
ATOM   2554  OE1 GLN A 173     -22.595  11.241 -24.014  1.00 60.98           O
ANISOU 2554  OE1 GLN A 173     6193   9140   7837    463  -1222   1151       O
ATOM   2555  NE2 GLN A 173     -23.568  12.712 -25.295  1.00 60.91           N
ANISOU 2555  NE2 GLN A 173     6004   9371   7768    560  -1131   1167       N
ATOM   2556  H   GLN A 173     -26.939  10.890 -22.460  1.00 79.68           H
ATOM   2557  HA  GLN A 173     -24.364   9.836 -23.215  1.00 76.11           H
ATOM   2558  HB2 GLN A 173     -25.200  11.909 -21.147  1.00 72.40           H
ATOM   2559  HB3 GLN A 173     -23.519  11.459 -21.421  1.00 72.40           H
ATOM   2560  HG2 GLN A 173     -25.400  12.622 -23.508  1.00 73.09           H
ATOM   2561  HG3 GLN A 173     -24.144  13.497 -22.639  1.00 73.09           H
ATOM   2562 HE21 GLN A 173     -24.119  13.541 -25.373  1.00 73.09           H
ATOM   2563 HE22 GLN A 173     -22.893  12.477 -26.032  1.00 73.09           H
ATOM   2564  N   GLN A 174     -25.352   9.034 -20.156  1.00 60.65           N
ANISOU 2564  N   GLN A 174     6222   8664   8158   -400  -1634   1663       N
ATOM   2565  CA  GLN A 174     -25.206   8.036 -19.083  1.00 60.86           C
ANISOU 2565  CA  GLN A 174     6348   8524   8253   -562  -1787   1761       C
ATOM   2566  C   GLN A 174     -25.151   6.591 -19.617  1.00 66.27           C
ANISOU 2566  C   GLN A 174     7187   8947   9044   -572  -2156   1671       C
ATOM   2567  O   GLN A 174     -24.182   5.874 -19.365  1.00 67.51           O
ANISOU 2567  O   GLN A 174     7494   8923   9234   -529  -2309   1605       O
ATOM   2568  CB  GLN A 174     -26.367   8.204 -18.080  1.00 62.51           C
ANISOU 2568  CB  GLN A 174     6428   8843   8481   -821  -1719   2016       C
ATOM   2569  CG  GLN A 174     -26.269   7.247 -16.875  1.00 65.68           C
ANISOU 2569  CG  GLN A 174     6903   9111   8941  -1020  -1869   2173       C
ATOM   2570  CD  GLN A 174     -27.506   7.251 -15.981  1.00 63.05           C
ANISOU 2570  CD  GLN A 174     6404   8958   8592  -1277  -1796   2448       C
ATOM   2571  OE1 GLN A 174     -28.556   7.780 -16.295  1.00 64.80           O
ANISOU 2571  OE1 GLN A 174     6459   9388   8773  -1307  -1667   2510       O
ATOM   2572  NE2 GLN A 174     -27.452   6.605 -14.844  1.00 66.89           N
ANISOU 2572  NE2 GLN A 174     6921   9394   9100  -1456  -1881   2622       N
ATOM   2573  H   GLN A 174     -25.979   9.819 -19.986  1.00 72.78           H
ATOM   2574  HA  GLN A 174     -24.271   8.227 -18.557  1.00 73.04           H
ATOM   2575  HB2 GLN A 174     -26.387   9.232 -17.715  1.00 75.01           H
ATOM   2576  HB3 GLN A 174     -27.306   8.013 -18.601  1.00 75.01           H
ATOM   2577  HG2 GLN A 174     -26.138   6.222 -17.220  1.00 78.82           H
ATOM   2578  HG3 GLN A 174     -25.398   7.514 -16.277  1.00 78.82           H
ATOM   2579 HE21 GLN A 174     -26.568   6.211 -14.540  1.00 80.27           H
ATOM   2580 HE22 GLN A 174     -28.320   6.521 -14.353  1.00 80.27           H
ATOM   2581  N   GLY A 175     -26.099   6.225 -20.490  1.00 66.02           N
ANISOU 2581  N   GLY A 175     7126   8885   9073   -619  -2323   1659       N
ATOM   2582  CA  GLY A 175     -26.111   4.918 -21.155  1.00 64.18           C
ANISOU 2582  CA  GLY A 175     7050   8381   8955   -616  -2713   1549       C
ATOM   2583  C   GLY A 175     -25.041   4.732 -22.242  1.00 69.86           C
ANISOU 2583  C   GLY A 175     7885   9047   9609   -292  -2797   1247       C
ATOM   2584  O   GLY A 175     -24.570   3.611 -22.410  1.00 71.55           O
ANISOU 2584  O   GLY A 175     8272   9025   9887   -222  -3075   1125       O
ATOM   2585  H   GLY A 175     -26.890   6.848 -20.619  1.00 79.22           H
ATOM   2586  HA2 GLY A 175     -25.969   4.138 -20.406  1.00 77.02           H
ATOM   2587  HA3 GLY A 175     -27.085   4.770 -21.616  1.00 77.02           H
ATOM   2588  N   LYS A 176     -24.640   5.778 -22.982  1.00 72.35           N
ANISOU 2588  N   LYS A 176     8100   9600   9790    -84  -2569   1130       N
ATOM   2589  CA  LYS A 176     -23.514   5.718 -23.942  1.00 74.40           C
ANISOU 2589  CA  LYS A 176     8426   9891   9950    231  -2629    862       C
ATOM   2590  C   LYS A 176     -22.188   5.387 -23.258  1.00 74.92           C
ANISOU 2590  C   LYS A 176     8603   9879   9983    338  -2631    791       C
ATOM   2591  O   LYS A 176     -21.485   4.505 -23.733  1.00 77.13           O
ANISOU 2591  O   LYS A 176     8991  10087  10227    564  -2828    566       O
ATOM   2592  CB  LYS A 176     -23.355   7.037 -24.734  1.00 72.81           C
ANISOU 2592  CB  LYS A 176     8069   9996   9601    394  -2344    823       C
ATOM   2593  CG  LYS A 176     -24.013   6.966 -26.118  1.00 73.46           C
ANISOU 2593  CG  LYS A 176     8099  10159   9655    499  -2466    705       C
ATOM   2594  CD  LYS A 176     -23.710   8.192 -26.995  1.00 73.72           C
ANISOU 2594  CD  LYS A 176     7985  10499   9525    687  -2203    669       C
ATOM   2595  CE  LYS A 176     -24.432   9.473 -26.545  1.00 73.14           C
ANISOU 2595  CE  LYS A 176     7762  10567   9459    529  -1913    890       C
ATOM   2596  NZ  LYS A 176     -25.204  10.082 -27.648  1.00 76.75           N
ANISOU 2596  NZ  LYS A 176     8112  11136   9915    514  -1933    910       N
ATOM   2597  H   LYS A 176     -25.001   6.696 -22.736  1.00 86.82           H
ATOM   2598  HA  LYS A 176     -23.667   4.891 -24.636  1.00 89.28           H
ATOM   2599  HB2 LYS A 176     -23.755   7.878 -24.171  1.00 87.38           H
ATOM   2600  HB3 LYS A 176     -22.291   7.229 -24.891  1.00 87.38           H
ATOM   2601  HG2 LYS A 176     -23.623   6.084 -26.633  1.00 88.16           H
ATOM   2602  HG3 LYS A 176     -25.089   6.854 -26.006  1.00 88.16           H
ATOM   2603  HD2 LYS A 176     -22.633   8.378 -26.983  1.00 88.46           H
ATOM   2604  HD3 LYS A 176     -23.974   7.949 -28.025  1.00 88.46           H
ATOM   2605  HE2 LYS A 176     -25.068   9.273 -25.689  1.00 87.76           H
ATOM   2606  HE3 LYS A 176     -23.661  10.188 -26.237  1.00 87.76           H
ATOM   2607  HZ1 LYS A 176     -25.644  10.950 -27.389  1.00 92.10           H
ATOM   2608  HZ2 LYS A 176     -24.511  10.381 -28.335  1.00 92.10           H
ATOM   2609  HZ3 LYS A 176     -25.801   9.450 -28.147  1.00 92.10           H
ATOM   2610  N   ARG A 177     -21.908   6.005 -22.110  1.00 73.09           N
ANISOU 2610  N   ARG A 177     8340   9680   9751    198  -2420    965       N
ATOM   2611  CA  ARG A 177     -20.637   5.848 -21.379  1.00 73.62           C
ANISOU 2611  CA  ARG A 177     8499   9690   9783    283  -2404    916       C
ATOM   2612  C   ARG A 177     -20.639   4.707 -20.351  1.00 75.08           C
ANISOU 2612  C   ARG A 177     8818   9607  10102     93  -2628   1028       C
ATOM   2613  O   ARG A 177     -19.703   4.595 -19.565  1.00 76.99           O
ANISOU 2613  O   ARG A 177     9144   9782  10325    148  -2638   1000       O
ATOM   2614  CB  ARG A 177     -20.250   7.192 -20.735  1.00 70.98           C
ANISOU 2614  CB  ARG A 177     8047   9571   9351    276  -2035   1016       C
ATOM   2615  CG  ARG A 177     -20.322   8.440 -21.629  1.00 69.02           C
ANISOU 2615  CG  ARG A 177     7650   9578   8997    397  -1800    985       C
ATOM   2616  CD  ARG A 177     -19.572   8.300 -22.951  1.00 70.74           C
ANISOU 2616  CD  ARG A 177     7876   9889   9115    671  -1893    764       C
ATOM   2617  NE  ARG A 177     -20.087   9.264 -23.927  1.00 74.06           N
ANISOU 2617  NE  ARG A 177     8150  10531   9459    739  -1732    775       N
ATOM   2618  CZ  ARG A 177     -20.037   9.138 -25.231  1.00 74.64           C
ANISOU 2618  CZ  ARG A 177     8193  10715   9453    928  -1833    624       C
ATOM   2619  NH1 ARG A 177     -19.610   8.100 -25.876  1.00 74.16           N
ANISOU 2619  NH1 ARG A 177     8240  10563   9373   1092  -2106    420       N
ATOM   2620  NH2 ARG A 177     -20.590  10.048 -25.951  1.00 74.32           N
ANISOU 2620  NH2 ARG A 177     8011  10882   9344    968  -1674    671       N
ATOM   2621  H   ARG A 177     -22.561   6.714 -21.793  1.00 87.71           H
ATOM   2622  HA  ARG A 177     -19.851   5.577 -22.092  1.00 88.34           H
ATOM   2623  HB2 ARG A 177     -20.917   7.366 -19.891  1.00 85.18           H
ATOM   2624  HB3 ARG A 177     -19.227   7.103 -20.370  1.00 85.18           H
ATOM   2625  HG2 ARG A 177     -21.367   8.660 -21.839  1.00 82.82           H
ATOM   2626  HG3 ARG A 177     -19.912   9.292 -21.085  1.00 82.82           H
ATOM   2627  HD2 ARG A 177     -18.503   8.460 -22.798  1.00 84.89           H
ATOM   2628  HD3 ARG A 177     -19.721   7.301 -23.355  1.00 84.89           H
ATOM   2629  HE  ARG A 177     -20.501  10.118 -23.587  1.00 88.88           H
ATOM   2630 HH11 ARG A 177     -19.019   7.440 -25.349  1.00 88.99           H
ATOM   2631 HH12 ARG A 177     -19.427   8.191 -26.850  1.00 88.99           H
ATOM   2632 HH21 ARG A 177     -21.031  10.851 -25.535  1.00 89.18           H
ATOM   2633 HH22 ARG A 177     -20.463  10.053 -26.939  1.00 89.18           H
ATOM   2634  N   GLY A 178     -21.755   3.980 -20.214  1.00 70.25           N
ANISOU 2634  N   GLY A 178     8219   8849   9624   -139  -2817   1170       N
ATOM   2635  CA  GLY A 178     -21.952   2.940 -19.193  1.00 70.08           C
ANISOU 2635  CA  GLY A 178     8310   8580   9736   -356  -3045   1327       C
ATOM   2636  C   GLY A 178     -21.787   3.425 -17.744  1.00 68.11           C
ANISOU 2636  C   GLY A 178     8001   8434   9446   -512  -2810   1539       C
ATOM   2637  O   GLY A 178     -21.318   2.665 -16.895  1.00 69.18           O
ANISOU 2637  O   GLY A 178     8241   8389   9653   -628  -2973   1642       O
ATOM   2638  H   GLY A 178     -22.501   4.152 -20.869  1.00 84.30           H
ATOM   2639  HA2 GLY A 178     -22.966   2.553 -19.292  1.00 84.09           H
ATOM   2640  HA3 GLY A 178     -21.252   2.122 -19.367  1.00 84.09           H
ATOM   2641  N   TRP A 179     -22.038   4.713 -17.484  1.00 70.97           N
ANISOU 2641  N   TRP A 179     8196   9076   9692   -508  -2447   1603       N
ATOM   2642  CA  TRP A 179     -21.918   5.315 -16.153  1.00 69.54           C
ANISOU 2642  CA  TRP A 179     7948   9020   9454   -628  -2222   1774       C
ATOM   2643  C   TRP A 179     -22.951   4.722 -15.182  1.00 71.98           C
ANISOU 2643  C   TRP A 179     8217   9286   9845   -946  -2330   2059       C
ATOM   2644  O   TRP A 179     -24.047   4.312 -15.577  1.00 74.16           O
ANISOU 2644  O   TRP A 179     8484   9472  10224  -1101  -2535   2150       O
ATOM   2645  CB  TRP A 179     -22.059   6.846 -16.242  1.00 63.56           C
ANISOU 2645  CB  TRP A 179     7022   8550   8576   -558  -1856   1773       C
ATOM   2646  CG  TRP A 179     -20.970   7.639 -16.920  1.00 57.01           C
ANISOU 2646  CG  TRP A 179     6206   7799   7657   -288  -1723   1558       C
ATOM   2647  CD1 TRP A 179     -19.792   7.169 -17.398  1.00 57.70           C
ANISOU 2647  CD1 TRP A 179     6417   7780   7728    -96  -1857   1374       C
ATOM   2648  CD2 TRP A 179     -20.970   9.071 -17.234  1.00 52.76           C
ANISOU 2648  CD2 TRP A 179     5540   7478   7028   -183  -1442   1523       C
ATOM   2649  NE1 TRP A 179     -19.072   8.200 -17.978  1.00 54.11           N
ANISOU 2649  NE1 TRP A 179     5898   7496   7164    105  -1664   1246       N
ATOM   2650  CE2 TRP A 179     -19.778   9.381 -17.957  1.00 52.39           C
ANISOU 2650  CE2 TRP A 179     5536   7456   6913     45  -1417   1343       C
ATOM   2651  CE3 TRP A 179     -21.871  10.135 -17.012  1.00 49.76           C
ANISOU 2651  CE3 TRP A 179     5010   7277   6618   -253  -1225   1630       C
ATOM   2652  CZ2 TRP A 179     -19.515  10.658 -18.473  1.00 46.32           C
ANISOU 2652  CZ2 TRP A 179     4667   6872   6062    169  -1191   1299       C
ATOM   2653  CZ3 TRP A 179     -21.597  11.432 -17.486  1.00 49.05           C
ANISOU 2653  CZ3 TRP A 179     4842   7336   6459   -106  -1013   1559       C
ATOM   2654  CH2 TRP A 179     -20.437  11.691 -18.238  1.00 45.57           C
ANISOU 2654  CH2 TRP A 179     4448   6901   5965     86  -1002   1410       C
ATOM   2655  H   TRP A 179     -22.492   5.255 -18.211  1.00 85.16           H
ATOM   2656  HA  TRP A 179     -20.932   5.086 -15.753  1.00 83.45           H
ATOM   2657  HB2 TRP A 179     -23.000   7.072 -16.745  1.00 76.27           H
ATOM   2658  HB3 TRP A 179     -22.143   7.236 -15.228  1.00 76.27           H
ATOM   2659  HD1 TRP A 179     -19.493   6.128 -17.395  1.00 69.25           H
ATOM   2660  HE1 TRP A 179     -18.218   8.064 -18.508  1.00 64.93           H
ATOM   2661  HE3 TRP A 179     -22.788   9.949 -16.474  1.00 59.71           H
ATOM   2662  HZ2 TRP A 179     -18.614  10.845 -19.045  1.00 55.59           H
ATOM   2663  HZ3 TRP A 179     -22.293  12.234 -17.284  1.00 58.86           H
ATOM   2664  HH2 TRP A 179     -20.252  12.684 -18.630  1.00 54.69           H
ATOM   2665  N   GLY A 180     -22.635   4.741 -13.886  1.00 69.49           N
ANISOU 2665  N   GLY A 180     7865   9063   9475  -1049  -2193   2209       N
ATOM   2666  CA  GLY A 180     -23.595   4.428 -12.828  1.00 66.61           C
ANISOU 2666  CA  GLY A 180     7418   8750   9142  -1349  -2244   2513       C
ATOM   2667  C   GLY A 180     -24.714   5.467 -12.705  1.00 69.90           C
ANISOU 2667  C   GLY A 180     7608   9472   9479  -1448  -2008   2644       C
ATOM   2668  O   GLY A 180     -24.867   6.368 -13.531  1.00 66.32           O
ANISOU 2668  O   GLY A 180     7084   9116   8997  -1321  -1889   2515       O
ATOM   2669  H   GLY A 180     -21.767   5.200 -13.623  1.00 83.38           H
ATOM   2670  HA2 GLY A 180     -24.050   3.459 -13.034  1.00 79.94           H
ATOM   2671  HA3 GLY A 180     -23.071   4.358 -11.877  1.00 79.94           H
ATOM   2672  N   GLN A 181     -25.535   5.340 -11.665  1.00 83.83           N
ANISOU 2672  N   GLN A 181     9245  11414  11192  -1667  -1942   2908       N
ATOM   2673  CA  GLN A 181     -26.633   6.270 -11.389  1.00 89.02           C
ANISOU 2673  CA  GLN A 181     9665  12401  11757  -1762  -1738   3050       C
ATOM   2674  C   GLN A 181     -26.177   7.740 -11.289  1.00 83.80           C
ANISOU 2674  C   GLN A 181     8911  11987  10942  -1551  -1386   2910       C
ATOM   2675  O   GLN A 181     -25.083   8.019 -10.780  1.00 85.83           O
ANISOU 2675  O   GLN A 181     9243  12228  11142  -1433  -1287   2817       O
ATOM   2676  H   GLN A 181     -25.385   4.579 -11.010  1.00100.59           H
ATOM   2677  CB  GLN A 181     -27.418   5.809 -10.140  1.00  0.00           C
ATOM   2678  CG  GLN A 181     -26.766   5.964  -8.744  1.00  0.00           C
ATOM   2679  CD  GLN A 181     -25.825   4.838  -8.331  1.00  0.00           C
ATOM   2680  NE2 GLN A 181     -25.889   4.405  -7.086  1.00  0.00           N
ATOM   2681  OE1 GLN A 181     -25.104   4.231  -9.088  1.00  0.00           O
ATOM   2682  HA  GLN A 181     -27.321   6.209 -12.228  1.00  0.00           H
ATOM   2683  HB2 GLN A 181     -27.724   4.770 -10.275  1.00  0.00           H
ATOM   2684  HB3 GLN A 181     -28.337   6.407 -10.122  1.00  0.00           H
ATOM   2685  HG2 GLN A 181     -27.594   5.962  -8.032  1.00  0.00           H
ATOM   2686  HG3 GLN A 181     -26.281   6.937  -8.648  1.00  0.00           H
ATOM   2687 HE21 GLN A 181     -26.619   4.804  -6.522  1.00  0.00           H
ATOM   2688 HE22 GLN A 181     -25.706   3.422  -7.042  1.00  0.00           H
ATOM   2689  N   LEU A 182     -27.109   8.654 -11.594  1.00 71.95           N
ANISOU 2689  N   LEU A 182     7249  10707   9384  -1501  -1216   2893       N
ATOM   2690  CA  LEU A 182     -27.092  10.027 -11.078  1.00 66.44           C
ANISOU 2690  CA  LEU A 182     6443  10252   8550  -1326   -912   2793       C
ATOM   2691  C   LEU A 182     -27.136   9.937  -9.543  1.00 64.32           C
ANISOU 2691  C   LEU A 182     6080  10201   8158  -1417   -807   2944       C
ATOM   2692  O   LEU A 182     -27.985   9.224  -8.991  1.00 67.94           O
ANISOU 2692  O   LEU A 182     6360  10907   8548  -1591   -796   3166       O
ATOM   2693  CB  LEU A 182     -28.293  10.810 -11.662  1.00 69.98           C
ANISOU 2693  CB  LEU A 182     6717  10913   8959  -1285   -785   2792       C
ATOM   2694  CG  LEU A 182     -28.403  12.290 -11.227  1.00 70.89           C
ANISOU 2694  CG  LEU A 182     6713  11276   8946  -1099   -504   2694       C
ATOM   2695  CD1 LEU A 182     -27.410  13.209 -11.943  1.00 69.50           C
ANISOU 2695  CD1 LEU A 182     6665  10941   8802   -856   -417   2446       C
ATOM   2696  CD2 LEU A 182     -29.804  12.817 -11.545  1.00 71.84           C
ANISOU 2696  CD2 LEU A 182     6623  11661   9011  -1114   -416   2769       C
ATOM   2697  H   LEU A 182     -28.003   8.325 -11.927  1.00 86.35           H
ATOM   2698  HA  LEU A 182     -26.170  10.512 -11.390  1.00 79.73           H
ATOM   2699  HB2 LEU A 182     -28.256  10.775 -12.751  1.00 83.97           H
ATOM   2700  HB3 LEU A 182     -29.207  10.299 -11.353  1.00 83.97           H
ATOM   2701  HG  LEU A 182     -28.244  12.366 -10.153  1.00 85.07           H
ATOM   2702 HD11 LEU A 182     -26.397  12.827 -11.842  1.00  0.00           H
ATOM   2703 HD12 LEU A 182     -27.661  13.284 -13.000  1.00  0.00           H
ATOM   2704 HD13 LEU A 182     -27.459  14.203 -11.498  1.00  0.00           H
ATOM   2705 HD21 LEU A 182     -30.553  12.260 -10.983  1.00  0.00           H
ATOM   2706 HD22 LEU A 182     -30.013  12.727 -12.610  1.00  0.00           H
ATOM   2707 HD23 LEU A 182     -29.876  13.865 -11.259  1.00  0.00           H
ATOM   2708  N   THR A 183     -26.097  10.412  -8.868  1.00 65.33           N
ANISOU 2708  N   THR A 183     6309  10270   8242  -1298   -731   2833       N
ATOM   2709  CA  THR A 183     -25.959  10.338  -7.405  1.00 64.84           C
ANISOU 2709  CA  THR A 183     6170  10409   8055  -1378   -655   2969       C
ATOM   2710  C   THR A 183     -26.616  11.526  -6.713  1.00 66.69           C
ANISOU 2710  C   THR A 183     6196  11017   8125  -1286   -408   2958       C
ATOM   2711  O   THR A 183     -27.187  11.349  -5.638  1.00 70.95           O
ANISOU 2711  O   THR A 183     6568  11852   8536  -1412   -366   3153       O
ATOM   2712  CB  THR A 183     -24.501  10.250  -6.956  1.00 64.27           C
ANISOU 2712  CB  THR A 183     6266  10169   7983  -1269   -656   2838       C
ATOM   2713  OG1 THR A 183     -23.786  11.425  -7.261  1.00 67.11           O
ANISOU 2713  OG1 THR A 183     6657  10526   8316  -1024   -478   2589       O
ATOM   2714  CG2 THR A 183     -23.760   9.103  -7.623  1.00 66.30           C
ANISOU 2714  CG2 THR A 183     6730  10068   8394  -1314   -914   2817       C
ATOM   2715  H   THR A 183     -25.382  10.913  -9.390  1.00 78.39           H
ATOM   2716  HA  THR A 183     -26.473   9.445  -7.045  1.00 77.80           H
ATOM   2717  HB  THR A 183     -24.474  10.099  -5.880  1.00 77.12           H
ATOM   2718  HG1 THR A 183     -22.913  11.193  -7.613  1.00 80.54           H
ATOM   2719 HG21 THR A 183     -22.816   8.946  -7.111  1.00 79.56           H
ATOM   2720 HG22 THR A 183     -24.363   8.198  -7.566  1.00 79.56           H
ATOM   2721 HG23 THR A 183     -23.569   9.341  -8.669  1.00 79.56           H
ATOM   2722  N   SER A 184     -26.561  12.710  -7.331  1.00 65.59           N
ANISOU 2722  N   SER A 184     6058  10883   7981  -1061   -257   2737       N
ATOM   2723  CA  SER A 184     -27.206  13.930  -6.855  1.00 66.96           C
ANISOU 2723  CA  SER A 184     6057  11378   8008   -932    -50   2687       C
ATOM   2724  C   SER A 184     -27.249  15.017  -7.942  1.00 65.42           C
ANISOU 2724  C   SER A 184     5891  11098   7867   -711     49   2467       C
ATOM   2725  O   SER A 184     -26.412  15.042  -8.852  1.00 64.33           O
ANISOU 2725  O   SER A 184     5916  10681   7844   -631      0   2332       O
ATOM   2726  CB  SER A 184     -26.480  14.442  -5.600  1.00 67.16           C
ANISOU 2726  CB  SER A 184     6077  11537   7902   -859     51   2642       C
ATOM   2727  OG  SER A 184     -25.182  14.930  -5.867  1.00 64.18           O
ANISOU 2727  OG  SER A 184     5873  10923   7589   -691     82   2419       O
ATOM   2728  H   SER A 184     -25.983  12.787  -8.158  1.00 78.71           H
ATOM   2729  HA  SER A 184     -28.232  13.686  -6.576  1.00 80.36           H
ATOM   2730  HB2 SER A 184     -27.060  15.246  -5.166  1.00 80.59           H
ATOM   2731  HB3 SER A 184     -26.414  13.642  -4.863  1.00 80.59           H
ATOM   2732  HG  SER A 184     -24.785  15.195  -5.033  1.00 77.01           H
ATOM   2733  N   ASN A 185     -28.155  15.987  -7.775  1.00 65.39           N
ANISOU 2733  N   ASN A 185     5717  11359   7768   -608    181   2441       N
ATOM   2734  CA  ASN A 185     -28.062  17.305  -8.408  1.00 64.49           C
ANISOU 2734  CA  ASN A 185     5616  11202   7686   -377    285   2238       C
ATOM   2735  C   ASN A 185     -27.717  18.351  -7.347  1.00 63.41           C
ANISOU 2735  C   ASN A 185     5449  11207   7436   -201    411   2100       C
ATOM   2736  O   ASN A 185     -28.491  18.557  -6.414  1.00 68.43           O
ANISOU 2736  O   ASN A 185     5923  12167   7911   -201    477   2164       O
ATOM   2737  CB  ASN A 185     -29.374  17.666  -9.122  1.00 63.34           C
ANISOU 2737  CB  ASN A 185     5308  11233   7525   -352    317   2283       C
ATOM   2738  CG  ASN A 185     -29.557  16.926 -10.427  1.00 65.08           C
ANISOU 2738  CG  ASN A 185     5582  11269   7878   -473    186   2355       C
ATOM   2739  OD1 ASN A 185     -30.524  16.219 -10.631  1.00 69.45           O
ANISOU 2739  OD1 ASN A 185     6018  11953   8418   -642    114   2530       O
ATOM   2740  ND2 ASN A 185     -28.662  17.104 -11.367  1.00 63.20           N
ANISOU 2740  ND2 ASN A 185     5510  10744   7760   -386    145   2224       N
ATOM   2741  H   ASN A 185     -28.792  15.913  -6.995  1.00 78.47           H
ATOM   2742  HA  ASN A 185     -27.260  17.298  -9.141  1.00 77.39           H
ATOM   2743  HB2 ASN A 185     -30.227  17.466  -8.473  1.00 76.01           H
ATOM   2744  HB3 ASN A 185     -29.368  18.730  -9.358  1.00 76.01           H
ATOM   2745 HD21 ASN A 185     -28.886  16.726 -12.272  1.00 75.85           H
ATOM   2746 HD22 ASN A 185     -27.882  17.729 -11.236  1.00 75.85           H
ATOM   2747  N   LEU A 186     -26.563  19.004  -7.485  1.00 59.98           N
ANISOU 2747  N   LEU A 186     5160  10551   7080    -53    432   1915       N
ATOM   2748  CA  LEU A 186     -26.120  20.058  -6.567  1.00 61.02           C
ANISOU 2748  CA  LEU A 186     5298  10755   7134    113    513   1759       C
ATOM   2749  C   LEU A 186     -26.415  21.431  -7.181  1.00 62.01           C
ANISOU 2749  C   LEU A 186     5418  10830   7313    330    564   1589       C
ATOM   2750  O   LEU A 186     -25.884  21.725  -8.252  1.00 59.43           O
ANISOU 2750  O   LEU A 186     5196  10253   7130    358    526   1543       O
ATOM   2751  CB  LEU A 186     -24.622  19.844  -6.256  1.00 60.79           C
ANISOU 2751  CB  LEU A 186     5442  10501   7157     87    469   1698       C
ATOM   2752  CG  LEU A 186     -24.046  20.730  -5.133  1.00 63.50           C
ANISOU 2752  CG  LEU A 186     5794  10921   7411    224    527   1550       C
ATOM   2753  CD1 LEU A 186     -24.581  20.320  -3.765  1.00 62.30           C
ANISOU 2753  CD1 LEU A 186     5496  11116   7060    180    571   1641       C
ATOM   2754  CD2 LEU A 186     -22.524  20.567  -5.062  1.00 60.65           C
ANISOU 2754  CD2 LEU A 186     5609  10303   7132    205    476   1481       C
ATOM   2755  H   LEU A 186     -26.038  18.856  -8.338  1.00 71.98           H
ATOM   2756  HA  LEU A 186     -26.678  19.980  -5.635  1.00 73.23           H
ATOM   2757  HB2 LEU A 186     -24.469  18.799  -5.981  1.00 72.95           H
ATOM   2758  HB3 LEU A 186     -24.059  20.039  -7.168  1.00 72.95           H
ATOM   2759  HG  LEU A 186     -24.283  21.776  -5.327  1.00 76.20           H
ATOM   2760 HD11 LEU A 186     -25.657  20.431  -3.746  1.00  0.00           H
ATOM   2761 HD12 LEU A 186     -24.159  20.960  -2.989  1.00  0.00           H
ATOM   2762 HD13 LEU A 186     -24.335  19.281  -3.548  1.00  0.00           H
ATOM   2763 HD21 LEU A 186     -22.064  20.831  -6.008  1.00  0.00           H
ATOM   2764 HD22 LEU A 186     -22.269  19.539  -4.803  1.00  0.00           H
ATOM   2765 HD23 LEU A 186     -22.131  21.230  -4.288  1.00  0.00           H
ATOM   2766  N   LEU A 187     -27.203  22.267  -6.499  1.00 61.29           N
ANISOU 2766  N   LEU A 187     5199  10989   7098    491    636   1499       N
ATOM   2767  CA  LEU A 187     -27.312  23.704  -6.771  1.00 60.02           C
ANISOU 2767  CA  LEU A 187     5047  10765   6991    725    655   1315       C
ATOM   2768  C   LEU A 187     -26.152  24.435  -6.085  1.00 63.41           C
ANISOU 2768  C   LEU A 187     5603  11041   7449    851    637   1129       C
ATOM   2769  O   LEU A 187     -25.922  24.250  -4.891  1.00 64.64           O
ANISOU 2769  O   LEU A 187     5718  11378   7465    891    664   1074       O
ATOM   2770  CB  LEU A 187     -28.685  24.209  -6.278  1.00 63.55           C
ANISOU 2770  CB  LEU A 187     5288  11572   7288    871    718   1285       C
ATOM   2771  CG  LEU A 187     -28.934  25.728  -6.389  1.00 66.12           C
ANISOU 2771  CG  LEU A 187     5621  11848   7654   1156    713   1067       C
ATOM   2772  CD1 LEU A 187     -28.937  26.217  -7.839  1.00 63.13           C
ANISOU 2772  CD1 LEU A 187     5336  11178   7474   1161    664   1081       C
ATOM   2773  CD2 LEU A 187     -30.297  26.067  -5.783  1.00 68.89           C
ANISOU 2773  CD2 LEU A 187     5747  12619   7811   1328    775   1021       C
ATOM   2774  H   LEU A 187     -27.561  21.957  -5.599  1.00 73.54           H
ATOM   2775  HA  LEU A 187     -27.245  23.874  -7.847  1.00 72.02           H
ATOM   2776  HB2 LEU A 187     -29.459  23.690  -6.841  1.00 76.27           H
ATOM   2777  HB3 LEU A 187     -28.793  23.931  -5.228  1.00 76.27           H
ATOM   2778  HG  LEU A 187     -28.167  26.269  -5.834  1.00 79.34           H
ATOM   2779 HD11 LEU A 187     -27.952  26.100  -8.286  1.00  0.00           H
ATOM   2780 HD12 LEU A 187     -29.206  27.274  -7.865  1.00  0.00           H
ATOM   2781 HD13 LEU A 187     -29.671  25.657  -8.415  1.00  0.00           H
ATOM   2782 HD21 LEU A 187     -30.308  25.807  -4.724  1.00  0.00           H
ATOM   2783 HD22 LEU A 187     -30.495  27.134  -5.874  1.00  0.00           H
ATOM   2784 HD23 LEU A 187     -31.088  25.522  -6.298  1.00  0.00           H
ATOM   2785  N   LEU A 188     -25.450  25.287  -6.830  1.00 58.11           N
ANISOU 2785  N   LEU A 188     5076  10052   6953    905    582   1045       N
ATOM   2786  CA  LEU A 188     -24.384  26.159  -6.339  1.00 57.83           C
ANISOU 2786  CA  LEU A 188     5163   9832   6978   1007    536    879       C
ATOM   2787  C   LEU A 188     -24.763  27.614  -6.635  1.00 58.07           C
ANISOU 2787  C   LEU A 188     5211   9751   7102   1221    490    726       C
ATOM   2788  O   LEU A 188     -24.838  27.971  -7.813  1.00 55.68           O
ANISOU 2788  O   LEU A 188     4933   9293   6929   1219    461    781       O
ATOM   2789  CB  LEU A 188     -23.049  25.802  -7.028  1.00 58.97           C
ANISOU 2789  CB  LEU A 188     5462   9690   7256    864    484    936       C
ATOM   2790  CG  LEU A 188     -22.492  24.401  -6.729  1.00 57.49           C
ANISOU 2790  CG  LEU A 188     5295   9543   7004    673    492   1064       C
ATOM   2791  CD1 LEU A 188     -22.942  23.390  -7.781  1.00 60.20           C
ANISOU 2791  CD1 LEU A 188     5603   9901   7372    534    488   1234       C
ATOM   2792  CD2 LEU A 188     -20.959  24.412  -6.771  1.00 57.57           C
ANISOU 2792  CD2 LEU A 188     5448   9328   7099    618    440   1031       C
ATOM   2793  H   LEU A 188     -25.678  25.350  -7.819  1.00 69.74           H
ATOM   2794  HA  LEU A 188     -24.267  26.040  -5.261  1.00 69.40           H
ATOM   2795  HB2 LEU A 188     -23.157  25.927  -8.104  1.00 70.77           H
ATOM   2796  HB3 LEU A 188     -22.318  26.531  -6.700  1.00 70.77           H
ATOM   2797  HG  LEU A 188     -22.810  24.073  -5.740  1.00 68.98           H
ATOM   2798 HD11 LEU A 188     -24.026  23.345  -7.810  1.00  0.00           H
ATOM   2799 HD12 LEU A 188     -22.578  22.410  -7.505  1.00  0.00           H
ATOM   2800 HD13 LEU A 188     -22.583  23.671  -8.771  1.00  0.00           H
ATOM   2801 HD21 LEU A 188     -20.580  25.128  -6.041  1.00  0.00           H
ATOM   2802 HD22 LEU A 188     -20.582  23.425  -6.500  1.00  0.00           H
ATOM   2803 HD23 LEU A 188     -20.608  24.684  -7.766  1.00  0.00           H
ATOM   2804  N   ILE A 189     -24.830  28.471  -5.609  1.00 60.29           N
ANISOU 2804  N   ILE A 189     5483  10107   7316   1413    466    530       N
ATOM   2805  CA  ILE A 189     -25.020  29.925  -5.766  1.00 59.93           C
ANISOU 2805  CA  ILE A 189     5485   9908   7379   1639    376    350       C
ATOM   2806  C   ILE A 189     -23.889  30.662  -5.044  1.00 63.59           C
ANISOU 2806  C   ILE A 189     6084  10174   7904   1698    279    182       C
ATOM   2807  O   ILE A 189     -23.727  30.523  -3.831  1.00 65.34           O
ANISOU 2807  O   ILE A 189     6272  10584   7972   1753    302     77       O
ATOM   2808  CB  ILE A 189     -26.421  30.414  -5.322  1.00 62.04           C
ANISOU 2808  CB  ILE A 189     5593  10483   7494   1877    407    229       C
ATOM   2809  CG1 ILE A 189     -27.546  29.598  -6.000  1.00 63.71           C
ANISOU 2809  CG1 ILE A 189     5651  10921   7633   1785    503    418       C
ATOM   2810  CG2 ILE A 189     -26.560  31.924  -5.615  1.00 63.83           C
ANISOU 2810  CG2 ILE A 189     5894  10501   7859   2128    277     31       C
ATOM   2811  CD1 ILE A 189     -28.952  29.909  -5.481  1.00 65.79           C
ANISOU 2811  CD1 ILE A 189     5712  11580   7706   1997    555    335       C
ATOM   2812  H   ILE A 189     -24.696  28.112  -4.666  1.00 72.34           H
ATOM   2813  HA  ILE A 189     -24.943  30.161  -6.823  1.00 71.92           H
ATOM   2814  HB  ILE A 189     -26.514  30.280  -4.247  1.00 74.44           H
ATOM   2815 HG12 ILE A 189     -27.519  29.757  -7.075  1.00 76.45           H
ATOM   2816 HG13 ILE A 189     -27.382  28.537  -5.820  1.00 76.45           H
ATOM   2817 HG21 ILE A 189     -27.530  32.294  -5.286  1.00 76.60           H
ATOM   2818 HG22 ILE A 189     -25.803  32.492  -5.074  1.00 76.60           H
ATOM   2819 HG23 ILE A 189     -26.450  32.118  -6.682  1.00 76.60           H
ATOM   2820 HD11 ILE A 189     -29.658  29.244  -5.971  1.00 78.95           H
ATOM   2821 HD12 ILE A 189     -28.995  29.741  -4.405  1.00 78.95           H
ATOM   2822 HD13 ILE A 189     -29.235  30.936  -5.708  1.00 78.95           H
ATOM   2823  N   GLY A 190     -23.020  31.323  -5.811  1.00 63.59           N
ANISOU 2823  N   GLY A 190     6226   9811   8125   1676    163    172       N
ATOM   2824  CA  GLY A 190     -21.813  31.987  -5.311  1.00 61.69           C
ANISOU 2824  CA  GLY A 190     6117   9348   7973   1685     49     48       C
ATOM   2825  C   GLY A 190     -21.807  33.488  -5.586  1.00 65.10           C
ANISOU 2825  C   GLY A 190     6648   9486   8600   1846   -128    -91       C
ATOM   2826  O   GLY A 190     -22.305  33.931  -6.619  1.00 63.74           O
ANISOU 2826  O   GLY A 190     6460   9232   8525   1915   -163    -48       O
ATOM   2827  H   GLY A 190     -23.261  31.451  -6.792  1.00 76.31           H
ATOM   2828  HA2 GLY A 190     -21.711  31.833  -4.236  1.00 74.02           H
ATOM   2829  HA3 GLY A 190     -20.940  31.555  -5.797  1.00 74.02           H
ATOM   2830  N   MET A 191     -21.137  34.252  -4.728  1.00 68.46           N
ANISOU 2830  N   MET A 191     7180   9743   9090   1900   -260   -257       N
ATOM   2831  CA  MET A 191     -20.828  35.665  -4.963  1.00 71.53           C
ANISOU 2831  CA  MET A 191     7689   9794   9693   2031   -480   -393       C
ATOM   2832  C   MET A 191     -19.718  35.838  -6.015  1.00 70.55           C
ANISOU 2832  C   MET A 191     7674   9331   9800   1794   -575   -200       C
ATOM   2833  O   MET A 191     -18.986  34.895  -6.346  1.00 68.79           O
ANISOU 2833  O   MET A 191     7445   9145   9546   1568   -485    -34       O
ATOM   2834  CB  MET A 191     -20.460  36.339  -3.628  1.00 75.31           C
ANISOU 2834  CB  MET A 191     8225  10266  10122   2227   -607   -695       C
ATOM   2835  CG  MET A 191     -21.642  36.315  -2.644  1.00 76.15           C
ANISOU 2835  CG  MET A 191     8203  10749   9980   2509   -534   -909       C
ATOM   2836  SD  MET A 191     -21.266  36.822  -0.945  1.00 79.98           S
ANISOU 2836  SD  MET A 191     8729  11315  10344   2755   -664  -1279       S
ATOM   2837  CE  MET A 191     -20.723  38.535  -1.181  1.00 80.80           C
ANISOU 2837  CE  MET A 191     9055  10847  10797   2848  -1010  -1444       C
ATOM   2838  H   MET A 191     -20.715  33.816  -3.919  1.00 82.15           H
ATOM   2839  HA  MET A 191     -21.718  36.161  -5.352  1.00 85.83           H
ATOM   2840  HB2 MET A 191     -19.611  35.824  -3.180  1.00 90.37           H
ATOM   2841  HB3 MET A 191     -20.176  37.376  -3.809  1.00 90.37           H
ATOM   2842  HG2 MET A 191     -22.436  36.953  -3.034  1.00 91.37           H
ATOM   2843  HG3 MET A 191     -22.032  35.299  -2.584  1.00 91.37           H
ATOM   2844  HE1 MET A 191     -20.536  38.991  -0.209  1.00 96.96           H
ATOM   2845  HE2 MET A 191     -19.800  38.557  -1.759  1.00 96.96           H
ATOM   2846  HE3 MET A 191     -21.495  39.104  -1.700  1.00 96.96           H
ATOM   2847  N   GLU A 192     -19.587  37.058  -6.542  1.00 76.68           N
ANISOU 2847  N   GLU A 192     8542   9788  10804   1854   -772   -214       N
ATOM   2848  CA  GLU A 192     -18.489  37.461  -7.427  1.00 76.23           C
ANISOU 2848  CA  GLU A 192     8567   9430  10968   1626   -884     -5       C
ATOM   2849  C   GLU A 192     -17.121  37.354  -6.736  1.00 74.28           C
ANISOU 2849  C   GLU A 192     8389   9093  10742   1495   -950    -47       C
ATOM   2850  O   GLU A 192     -16.984  37.448  -5.507  1.00 75.88           O
ANISOU 2850  O   GLU A 192     8651   9255  10924   1642  -1060   -300       O
ATOM   2851  CB  GLU A 192     -18.744  38.866  -7.989  1.00 79.51           C
ANISOU 2851  CB  GLU A 192     9075   9502  11634   1722  -1125    -21       C
ATOM   2852  CG  GLU A 192     -18.756  40.017  -6.977  1.00 82.17           C
ANISOU 2852  CG  GLU A 192     9533   9614  12073   1925  -1371   -319       C
ATOM   2853  CD  GLU A 192     -19.264  41.314  -7.595  1.00 86.22           C
ANISOU 2853  CD  GLU A 192    10142   9784  12834   2058  -1629   -349       C
ATOM   2854  OE1 GLU A 192     -19.863  41.243  -8.700  1.00 85.47           O
ANISOU 2854  OE1 GLU A 192     9994   9701  12780   2047  -1577   -171       O
ATOM   2855  OE2 GLU A 192     -18.838  42.366  -7.085  1.00 90.39           O
ANISOU 2855  OE2 GLU A 192    10803  10018  13521   2176  -1901   -551       O
ATOM   2856  H   GLU A 192     -20.220  37.789  -6.259  1.00 92.01           H
ATOM   2857  HA  GLU A 192     -18.481  36.775  -8.284  1.00 91.48           H
ATOM   2858  HB2 GLU A 192     -17.988  39.081  -8.747  1.00 95.41           H
ATOM   2859  HB3 GLU A 192     -19.708  38.820  -8.492  1.00 95.41           H
ATOM   2860  HG2 GLU A 192     -19.383  39.735  -6.131  1.00 98.60           H
ATOM   2861  HG3 GLU A 192     -17.739  40.146  -6.610  1.00 98.60           H
ATOM   2862  N   GLY A 193     -16.099  36.979  -7.499  1.00 70.65           N
ANISOU 2862  N   GLY A 193     7912   8624  10309   1234   -888    192       N
ATOM   2863  CA  GLY A 193     -14.773  36.709  -6.957  1.00 70.22           C
ANISOU 2863  CA  GLY A 193     7901   8520  10260   1091   -933    185       C
ATOM   2864  C   GLY A 193     -14.635  35.475  -6.048  1.00 69.88           C
ANISOU 2864  C   GLY A 193     7793   8784   9975   1057   -736    151       C
ATOM   2865  O   GLY A 193     -13.498  35.218  -5.645  1.00 68.52           O
ANISOU 2865  O   GLY A 193     7638   8606   9791    911   -743    195       O
ATOM   2866  H   GLY A 193     -16.233  36.937  -8.508  1.00 84.78           H
ATOM   2867  HA2 GLY A 193     -14.082  36.589  -7.789  1.00 84.26           H
ATOM   2868  HA3 GLY A 193     -14.468  37.576  -6.373  1.00 84.26           H
ATOM   2869  N   ASN A 194     -15.688  34.690  -5.756  1.00 69.87           N
ANISOU 2869  N   ASN A 194     7712   9053   9784   1179   -574     90       N
ATOM   2870  CA  ASN A 194     -15.577  33.393  -5.056  1.00 66.24           C
ANISOU 2870  CA  ASN A 194     7189   8875   9104   1129   -406     93       C
ATOM   2871  C   ASN A 194     -14.605  32.448  -5.789  1.00 61.14           C
ANISOU 2871  C   ASN A 194     6525   8245   8459    897   -329    325       C
ATOM   2872  O   ASN A 194     -14.820  32.147  -6.964  1.00 60.54           O
ANISOU 2872  O   ASN A 194     6423   8117   8462    807   -309    508       O
ATOM   2873  CB  ASN A 194     -16.951  32.684  -4.928  1.00 61.78           C
ANISOU 2873  CB  ASN A 194     6520   8596   8359   1247   -255     71       C
ATOM   2874  CG  ASN A 194     -17.863  33.226  -3.843  1.00 63.04           C
ANISOU 2874  CG  ASN A 194     6658   8887   8407   1494   -289   -189       C
ATOM   2875  OD1 ASN A 194     -17.572  34.220  -3.211  1.00 64.95           O
ANISOU 2875  OD1 ASN A 194     6984   8946   8748   1618   -457   -380       O
ATOM   2876  ND2 ASN A 194     -18.828  32.444  -3.403  1.00 63.74           N
ANISOU 2876  ND2 ASN A 194     6625   9308   8283   1569   -144   -198       N
ATOM   2877  H   ASN A 194     -16.613  35.028  -6.001  1.00 83.85           H
ATOM   2878  HA  ASN A 194     -15.185  33.572  -4.053  1.00 79.49           H
ATOM   2879  HB2 ASN A 194     -17.476  32.723  -5.882  1.00 74.14           H
ATOM   2880  HB3 ASN A 194     -16.773  31.635  -4.693  1.00 74.14           H
ATOM   2881 HD21 ASN A 194     -19.334  32.754  -2.576  1.00 76.48           H
ATOM   2882 HD22 ASN A 194     -18.960  31.521  -3.770  1.00 76.48           H
ATOM   2883  N   VAL A 195     -13.687  31.807  -5.056  1.00 56.11           N
ANISOU 2883  N   VAL A 195     5897   7698   7724    817   -294    306       N
ATOM   2884  CA  VAL A 195     -12.737  30.810  -5.587  1.00 54.40           C
ANISOU 2884  CA  VAL A 195     5663   7521   7485    632   -235    488       C
ATOM   2885  C   VAL A 195     -12.902  29.466  -4.878  1.00 51.30           C
ANISOU 2885  C   VAL A 195     5227   7375   6888    623    -99    488       C
ATOM   2886  O   VAL A 195     -12.463  29.298  -3.737  1.00 53.81           O
ANISOU 2886  O   VAL A 195     5554   7793   7098    685    -95    352       O
ATOM   2887  CB  VAL A 195     -11.275  31.299  -5.486  1.00 56.05           C
ANISOU 2887  CB  VAL A 195     5926   7578   7795    523   -355    494       C
ATOM   2888  CG1 VAL A 195     -10.293  30.310  -6.127  1.00 53.26           C
ANISOU 2888  CG1 VAL A 195     5532   7311   7394    364   -291    673       C
ATOM   2889  CG2 VAL A 195     -11.071  32.648  -6.177  1.00 58.02           C
ANISOU 2889  CG2 VAL A 195     6220   7558   8268    508   -526    519       C
ATOM   2890  H   VAL A 195     -13.557  32.096  -4.090  1.00 67.33           H
ATOM   2891  HA  VAL A 195     -12.942  30.652  -6.645  1.00 65.28           H
ATOM   2892  HB  VAL A 195     -10.997  31.416  -4.438  1.00 67.27           H
ATOM   2893 HG11 VAL A 195      -9.277  30.699  -6.039  1.00 63.91           H
ATOM   2894 HG12 VAL A 195     -10.332  29.347  -5.620  1.00 63.91           H
ATOM   2895 HG13 VAL A 195     -10.539  30.180  -7.181  1.00 63.91           H
ATOM   2896 HG21 VAL A 195     -10.018  32.928  -6.133  1.00 69.63           H
ATOM   2897 HG22 VAL A 195     -11.379  32.581  -7.219  1.00 69.63           H
ATOM   2898 HG23 VAL A 195     -11.660  33.411  -5.678  1.00 69.63           H
ATOM   2899  N   THR A 196     -13.372  28.458  -5.616  1.00 46.81           N
ANISOU 2899  N   THR A 196     4612   6905   6269    546     -6    645       N
ATOM   2900  CA  THR A 196     -13.247  27.037  -5.259  1.00 47.32           C
ANISOU 2900  CA  THR A 196     4653   7151   6176    498     81    687       C
ATOM   2901  C   THR A 196     -11.826  26.560  -5.618  1.00 47.38           C
ANISOU 2901  C   THR A 196     4688   7121   6193    381     57    769       C
ATOM   2902  O   THR A 196     -11.520  26.476  -6.816  1.00 46.92           O
ANISOU 2902  O   THR A 196     4613   7020   6194    319     51    891       O
ATOM   2903  CB  THR A 196     -14.272  26.177  -6.023  1.00 47.81           C
ANISOU 2903  CB  THR A 196     4655   7324   6185    489    162    793       C
ATOM   2904  OG1 THR A 196     -15.596  26.642  -5.876  1.00 49.59           O
ANISOU 2904  OG1 THR A 196     4834   7613   6395    607    185    720       O
ATOM   2905  CG2 THR A 196     -14.304  24.730  -5.534  1.00 46.87           C
ANISOU 2905  CG2 THR A 196     4523   7359   5927    424    213    851       C
ATOM   2906  H   THR A 196     -13.635  28.671  -6.574  1.00 56.17           H
ATOM   2907  HA  THR A 196     -13.437  26.918  -4.194  1.00 56.78           H
ATOM   2908  HB  THR A 196     -14.026  26.178  -7.083  1.00 57.37           H
ATOM   2909  HG1 THR A 196     -16.183  25.950  -6.184  1.00 59.51           H
ATOM   2910 HG21 THR A 196     -15.099  24.185  -6.044  1.00 56.25           H
ATOM   2911 HG22 THR A 196     -13.349  24.252  -5.744  1.00 56.25           H
ATOM   2912 HG23 THR A 196     -14.491  24.708  -4.459  1.00 56.25           H
ATOM   2913  N   PRO A 197     -10.966  26.165  -4.651  1.00 48.61           N
ANISOU 2913  N   PRO A 197     4874   7317   6279    360     39    706       N
ATOM   2914  CA  PRO A 197      -9.586  25.763  -4.941  1.00 47.35           C
ANISOU 2914  CA  PRO A 197     4730   7129   6131    267      2    771       C
ATOM   2915  C   PRO A 197      -9.475  24.532  -5.849  1.00 47.15           C
ANISOU 2915  C   PRO A 197     4684   7184   6046    221     46    896       C
ATOM   2916  O   PRO A 197     -10.423  23.744  -6.002  1.00 44.50           O
ANISOU 2916  O   PRO A 197     4335   6922   5650    237     96    932       O
ATOM   2917  CB  PRO A 197      -8.904  25.522  -3.589  1.00 50.69           C
ANISOU 2917  CB  PRO A 197     5185   7613   6463    276    -17    665       C
ATOM   2918  CG  PRO A 197      -9.736  26.355  -2.624  1.00 53.68           C
ANISOU 2918  CG  PRO A 197     5567   8013   6816    383    -18    521       C
ATOM   2919  CD  PRO A 197     -11.145  26.256  -3.207  1.00 50.81           C
ANISOU 2919  CD  PRO A 197     5160   7695   6450    434     46    567       C
ATOM   2920  HA  PRO A 197      -9.089  26.603  -5.429  1.00 56.82           H
ATOM   2921  HB2 PRO A 197      -8.973  24.470  -3.309  1.00 60.83           H
ATOM   2922  HB3 PRO A 197      -7.862  25.846  -3.597  1.00 60.83           H
ATOM   2923  HG2 PRO A 197      -9.688  25.953  -1.613  1.00 64.42           H
ATOM   2924  HG3 PRO A 197      -9.400  27.394  -2.641  1.00 64.42           H
ATOM   2925  HD2 PRO A 197     -11.630  25.351  -2.842  1.00 60.97           H
ATOM   2926  HD3 PRO A 197     -11.718  27.132  -2.908  1.00 60.97           H
ATOM   2927  N   ALA A 198      -8.274  24.324  -6.400  1.00 46.38           N
ANISOU 2927  N   ALA A 198     4577   7081   5963    166      9    959       N
ATOM   2928  CA  ALA A 198      -7.974  23.157  -7.218  1.00 42.22           C
ANISOU 2928  CA  ALA A 198     4034   6631   5377    157     22   1045       C
ATOM   2929  C   ALA A 198      -8.195  21.866  -6.418  1.00 45.14           C
ANISOU 2929  C   ALA A 198     4446   7070   5635    168     33   1023       C
ATOM   2930  O   ALA A 198      -7.600  21.648  -5.364  1.00 41.16           O
ANISOU 2930  O   ALA A 198     3973   6594   5074    160     18    969       O
ATOM   2931  CB  ALA A 198      -6.547  23.259  -7.763  1.00 39.45           C
ANISOU 2931  CB  ALA A 198     3646   6315   5029    123    -23   1096       C
ATOM   2932  H   ALA A 198      -7.499  24.906  -6.115  1.00 55.66           H
ATOM   2933  HA  ALA A 198      -8.654  23.155  -8.070  1.00 50.67           H
ATOM   2934  HB1 ALA A 198      -6.318  22.390  -8.382  1.00 47.34           H
ATOM   2935  HB2 ALA A 198      -6.456  24.153  -8.374  1.00 47.34           H
ATOM   2936  HB3 ALA A 198      -5.825  23.309  -6.946  1.00 47.34           H
ATOM   2937  N   HIS A 199      -9.109  21.029  -6.905  1.00 44.15           N
ANISOU 2937  N   HIS A 199     4322   6968   5485    177     44   1076       N
ATOM   2938  CA  HIS A 199      -9.429  19.724  -6.322  1.00 40.11           C
ANISOU 2938  CA  HIS A 199     3850   6498   4891    162     25   1096       C
ATOM   2939  C   HIS A 199      -9.965  18.785  -7.397  1.00 42.09           C
ANISOU 2939  C   HIS A 199     4105   6735   5152    168    -13   1160       C
ATOM   2940  O   HIS A 199     -10.530  19.264  -8.383  1.00 49.54           O
ANISOU 2940  O   HIS A 199     5007   7665   6149    191      3   1180       O
ATOM   2941  CB  HIS A 199     -10.444  19.894  -5.182  1.00 46.03           C
ANISOU 2941  CB  HIS A 199     4588   7303   5599    148     74   1083       C
ATOM   2942  CG  HIS A 199     -11.834  20.239  -5.634  1.00 42.88           C
ANISOU 2942  CG  HIS A 199     4140   6917   5236    158    118   1116       C
ATOM   2943  ND1 HIS A 199     -12.275  21.465  -6.098  1.00 43.02           N
ANISOU 2943  ND1 HIS A 199     4121   6902   5324    206    156   1068       N
ATOM   2944  CD2 HIS A 199     -12.862  19.346  -5.735  1.00 42.04           C
ANISOU 2944  CD2 HIS A 199     4013   6847   5112    123    114   1199       C
ATOM   2945  CE1 HIS A 199     -13.573  21.317  -6.450  1.00 45.15           C
ANISOU 2945  CE1 HIS A 199     4345   7206   5605    215    188   1112       C
ATOM   2946  NE2 HIS A 199     -13.942  20.028  -6.238  1.00 46.57           N
ANISOU 2946  NE2 HIS A 199     4528   7435   5730    157    167   1194       N
ATOM   2947  H   HIS A 199      -9.636  21.320  -7.719  1.00 52.98           H
ATOM   2948  HA  HIS A 199      -8.514  19.289  -5.919  1.00 48.13           H
ATOM   2949  HB2 HIS A 199     -10.504  18.967  -4.611  1.00 55.24           H
ATOM   2950  HB3 HIS A 199     -10.098  20.678  -4.511  1.00 55.24           H
ATOM   2951  HD1 HIS A 199     -11.702  22.316  -6.163  1.00 51.62           H
ATOM   2952  HD2 HIS A 199     -12.840  18.284  -5.502  1.00 50.44           H
ATOM   2953  HE1 HIS A 199     -14.209  22.104  -6.837  1.00 54.18           H
ATOM   2954  HE2 HIS A 199     -14.812  19.549  -6.496  1.00  0.00           H
ATOM   2955  N   TYR A 200      -9.885  17.477  -7.175  1.00 41.70           N
ANISOU 2955  N   TYR A 200     4107   6682   5054    148    -82   1192       N
ATOM   2956  CA  TYR A 200     -10.513  16.474  -8.041  1.00 49.27           C
ANISOU 2956  CA  TYR A 200     5086   7603   6032    151   -155   1238       C
ATOM   2957  C   TYR A 200     -11.722  15.815  -7.360  1.00 51.78           C
ANISOU 2957  C   TYR A 200     5419   7921   6333     65   -182   1320       C
ATOM   2958  O   TYR A 200     -11.806  15.748  -6.131  1.00 52.65           O
ANISOU 2958  O   TYR A 200     5543   8073   6389     14   -177   1350       O
ATOM   2959  CB  TYR A 200      -9.462  15.467  -8.523  1.00 45.28           C
ANISOU 2959  CB  TYR A 200     4636   7067   5502    218   -271   1204       C
ATOM   2960  CG  TYR A 200      -8.885  14.560  -7.449  1.00 38.99           C
ANISOU 2960  CG  TYR A 200     3916   6241   4658    198   -356   1211       C
ATOM   2961  CD1 TYR A 200      -7.757  14.975  -6.715  1.00 45.73           C
ANISOU 2961  CD1 TYR A 200     4771   7141   5465    215   -329   1168       C
ATOM   2962  CD2 TYR A 200      -9.460  13.298  -7.196  1.00 39.49           C
ANISOU 2962  CD2 TYR A 200     4051   6223   4732    156   -482   1271       C
ATOM   2963  CE1 TYR A 200      -7.204  14.139  -5.729  1.00 40.84           C
ANISOU 2963  CE1 TYR A 200     4220   6502   4797    203   -410   1181       C
ATOM   2964  CE2 TYR A 200      -8.911  12.458  -6.209  1.00 42.65           C
ANISOU 2964  CE2 TYR A 200     4525   6584   5098    133   -578   1299       C
ATOM   2965  CZ  TYR A 200      -7.779  12.877  -5.472  1.00 44.08           C
ANISOU 2965  CZ  TYR A 200     4704   6826   5219    164   -535   1251       C
ATOM   2966  OH  TYR A 200      -7.234  12.059  -4.532  1.00 44.52           O
ANISOU 2966  OH  TYR A 200     4830   6850   5234    148   -633   1286       O
ATOM   2967  H   TYR A 200      -9.433  17.158  -6.325  1.00 50.04           H
ATOM   2968  HA  TYR A 200     -10.894  16.965  -8.936  1.00 59.13           H
ATOM   2969  HB2 TYR A 200      -9.915  14.851  -9.297  1.00 54.34           H
ATOM   2970  HB3 TYR A 200      -8.645  16.015  -8.997  1.00 54.34           H
ATOM   2971  HD1 TYR A 200      -7.298  15.934  -6.925  1.00 54.88           H
ATOM   2972  HD2 TYR A 200     -10.314  12.968  -7.775  1.00 47.39           H
ATOM   2973  HE1 TYR A 200      -6.334  14.468  -5.181  1.00 49.01           H
ATOM   2974  HE2 TYR A 200      -9.344  11.488  -6.021  1.00 51.19           H
ATOM   2975  HH  TYR A 200      -6.308  12.285  -4.396  1.00 53.42           H
ATOM   2976  N   ASP A 201     -12.672  15.323  -8.153  1.00 46.58           N
ANISOU 2976  N   ASP A 201     4744   7239   5717     42   -214   1370       N
ATOM   2977  CA  ASP A 201     -13.867  14.610  -7.675  1.00 46.31           C
ANISOU 2977  CA  ASP A 201     4705   7214   5677    -65   -263   1481       C
ATOM   2978  C   ASP A 201     -13.903  13.177  -8.269  1.00 49.79           C
ANISOU 2978  C   ASP A 201     5231   7529   6160    -80   -446   1511       C
ATOM   2979  O   ASP A 201     -13.351  12.927  -9.339  1.00 49.61           O
ANISOU 2979  O   ASP A 201     5246   7442   6160     22   -513   1424       O
ATOM   2980  CB  ASP A 201     -15.129  15.489  -7.883  1.00 39.96           C
ANISOU 2980  CB  ASP A 201     3805   6484   4893    -90   -178   1521       C
ATOM   2981  CG  ASP A 201     -15.150  16.775  -7.012  1.00 45.58           C
ANISOU 2981  CG  ASP A 201     4443   7300   5574    -43    -28   1466       C
ATOM   2982  OD1 ASP A 201     -14.781  16.673  -5.816  1.00 45.44           O
ANISOU 2982  OD1 ASP A 201     4422   7355   5488    -55      9   1455       O
ATOM   2983  OD2 ASP A 201     -15.223  17.906  -7.566  1.00 46.36           O
ANISOU 2983  OD2 ASP A 201     4492   7405   5717     15     35   1427       O
ATOM   2984  H   ASP A 201     -12.504  15.311  -9.153  1.00 55.90           H
ATOM   2985  HA  ASP A 201     -13.769  14.450  -6.606  1.00 55.57           H
ATOM   2986  HB2 ASP A 201     -15.193  15.800  -8.920  1.00 47.95           H
ATOM   2987  HB3 ASP A 201     -16.006  14.889  -7.655  1.00 47.95           H
ATOM   2988  N   GLU A 202     -14.353  12.175  -7.490  1.00 57.06           N
ANISOU 2988  N   GLU A 202     6172   8424   7084   -206   -543   1639       N
ATOM   2989  CA  GLU A 202     -14.273  10.730  -7.839  1.00 57.48           C
ANISOU 2989  CA  GLU A 202     6330   8314   7197   -235   -765   1674       C
ATOM   2990  C   GLU A 202     -15.479  10.268  -8.704  1.00 59.61           C
ANISOU 2990  C   GLU A 202     6578   8532   7538   -302   -853   1734       C
ATOM   2991  O   GLU A 202     -15.796   9.081  -8.763  1.00 59.99           O
ANISOU 2991  O   GLU A 202     6716   8422   7655   -348  -1072   1773       O
ATOM   2992  CB  GLU A 202     -14.051   9.851  -6.572  1.00 56.52           C
ANISOU 2992  CB  GLU A 202     6260   8162   7053   -355   -867   1805       C
ATOM   2993  CG  GLU A 202     -12.838  10.285  -5.714  1.00 53.68           C
ANISOU 2993  CG  GLU A 202     5923   7857   6615   -290   -796   1744       C
ATOM   2994  CD  GLU A 202     -12.354   9.235  -4.682  1.00 53.90           C
ANISOU 2994  CD  GLU A 202     6023   7832   6627   -387   -935   1872       C
ATOM   2995  OE1 GLU A 202     -12.329   9.556  -3.458  1.00 60.29           O
ANISOU 2995  OE1 GLU A 202     6758   8786   7364   -507   -861   2009       O
ATOM   2996  OE2 GLU A 202     -11.568   8.357  -5.097  1.00 52.26           O
ANISOU 2996  OE2 GLU A 202     5938   7449   6469   -333  -1129   1836       O
ATOM   2997  H   GLU A 202     -14.804  12.417  -6.625  1.00 68.47           H
ATOM   2998  HA  GLU A 202     -13.395  10.583  -8.473  1.00 68.98           H
ATOM   2999  HB2 GLU A 202     -14.951   9.875  -5.954  1.00 67.83           H
ATOM   3000  HB3 GLU A 202     -13.899   8.819  -6.894  1.00 67.83           H
ATOM   3001  HG2 GLU A 202     -12.008  10.483  -6.391  1.00 64.41           H
ATOM   3002  HG3 GLU A 202     -13.082  11.214  -5.205  1.00 64.41           H
ATOM   3003  N   GLN A 203     -16.237  11.217  -9.267  1.00 64.46           N
ANISOU 3003  N   GLN A 203     7081   9264   8147   -302   -708   1737       N
ATOM   3004  CA  GLN A 203     -17.460  11.022 -10.054  1.00 58.25           C
ANISOU 3004  CA  GLN A 203     6255   8457   7421   -366   -777   1795       C
ATOM   3005  C   GLN A 203     -17.428  11.902 -11.310  1.00 54.50           C
ANISOU 3005  C   GLN A 203     5737   8016   6956   -226   -691   1670       C
ATOM   3006  O   GLN A 203     -16.781  12.950 -11.313  1.00 51.10           O
ANISOU 3006  O   GLN A 203     5273   7657   6485   -119   -544   1584       O
ATOM   3007  CB  GLN A 203     -18.707  11.319  -9.196  1.00 58.97           C
ANISOU 3007  CB  GLN A 203     6221   8705   7480   -523   -692   1963       C
ATOM   3008  CG  GLN A 203     -18.805  10.368  -7.989  1.00 61.56           C
ANISOU 3008  CG  GLN A 203     6561   9052   7778   -685   -774   2134       C
ATOM   3009  CD  GLN A 203     -20.154  10.388  -7.279  1.00 65.59           C
ANISOU 3009  CD  GLN A 203     6917   9767   8239   -848   -714   2326       C
ATOM   3010  OE1 GLN A 203     -21.155  10.902  -7.740  1.00 64.07           O
ANISOU 3010  OE1 GLN A 203     6613   9695   8037   -827   -610   2315       O
ATOM   3011  NE2 GLN A 203     -20.260   9.754  -6.131  1.00 68.37           N
ANISOU 3011  NE2 GLN A 203     7248  10181   8549  -1011   -784   2517       N
ATOM   3012  H   GLN A 203     -15.890  12.165  -9.236  1.00 77.35           H
ATOM   3013  HA  GLN A 203     -17.516   9.986 -10.389  1.00 69.90           H
ATOM   3014  HB2 GLN A 203     -18.682  12.352  -8.845  1.00 70.77           H
ATOM   3015  HB3 GLN A 203     -19.596  11.204  -9.813  1.00 70.77           H
ATOM   3016  HG2 GLN A 203     -18.622   9.347  -8.322  1.00 73.88           H
ATOM   3017  HG3 GLN A 203     -18.035  10.638  -7.267  1.00 73.88           H
ATOM   3018 HE21 GLN A 203     -19.446   9.349  -5.712  1.00 82.05           H
ATOM   3019 HE22 GLN A 203     -21.104   9.954  -5.623  1.00 82.05           H
ATOM   3020  N   GLN A 204     -18.058  11.428 -12.384  1.00 52.77           N
ANISOU 3020  N   GLN A 204     5517   7740   6794   -236   -803   1672       N
ATOM   3021  CA  GLN A 204     -18.252  12.177 -13.626  1.00 49.08           C
ANISOU 3021  CA  GLN A 204     4990   7332   6327   -118   -727   1584       C
ATOM   3022  C   GLN A 204     -19.202  13.350 -13.341  1.00 47.09           C
ANISOU 3022  C   GLN A 204     4604   7234   6054   -157   -535   1651       C
ATOM   3023  O   GLN A 204     -20.137  13.191 -12.549  1.00 46.44           O
ANISOU 3023  O   GLN A 204     4459   7220   5968   -290   -519   1774       O
ATOM   3024  CB  GLN A 204     -18.854  11.239 -14.694  1.00 49.73           C
ANISOU 3024  CB  GLN A 204     5107   7321   6468   -114   -917   1558       C
ATOM   3025  CG  GLN A 204     -18.050   9.953 -14.986  1.00 51.80           C
ANISOU 3025  CG  GLN A 204     5513   7406   6761    -58  -1161   1473       C
ATOM   3026  CD  GLN A 204     -16.779  10.152 -15.810  1.00 52.25           C
ANISOU 3026  CD  GLN A 204     5602   7495   6755    163  -1150   1298       C
ATOM   3027  OE1 GLN A 204     -16.234  11.240 -15.904  1.00 49.38           O
ANISOU 3027  OE1 GLN A 204     5153   7277   6331    244   -958   1269       O
ATOM   3028  NE2 GLN A 204     -16.149   9.086 -16.251  1.00 50.59           N
ANISOU 3028  NE2 GLN A 204     5507   7158   6556    265  -1374   1185       N
ATOM   3029  H   GLN A 204     -18.696  10.653 -12.239  1.00 63.33           H
ATOM   3030  HA  GLN A 204     -17.297  12.569 -13.981  1.00 58.90           H
ATOM   3031  HB2 GLN A 204     -19.836  10.928 -14.340  1.00 59.68           H
ATOM   3032  HB3 GLN A 204     -19.008  11.790 -15.622  1.00 59.68           H
ATOM   3033  HG2 GLN A 204     -17.784   9.457 -14.056  1.00 62.16           H
ATOM   3034  HG3 GLN A 204     -18.702   9.267 -15.519  1.00 62.16           H
ATOM   3035 HE21 GLN A 204     -16.570   8.184 -16.214  1.00 60.70           H
ATOM   3036 HE22 GLN A 204     -15.218   9.186 -16.663  1.00 60.70           H
ATOM   3037  N   ASN A 205     -18.991  14.510 -13.966  1.00 47.82           N
ANISOU 3037  N   ASN A 205     4646   7394   6129    -36   -401   1576       N
ATOM   3038  CA  ASN A 205     -19.806  15.696 -13.702  1.00 49.89           C
ANISOU 3038  CA  ASN A 205     4801   7778   6378    -34   -235   1610       C
ATOM   3039  C   ASN A 205     -20.143  16.459 -14.992  1.00 48.88           C
ANISOU 3039  C   ASN A 205     4615   7684   6274     62   -190   1575       C
ATOM   3040  O   ASN A 205     -19.237  16.950 -15.666  1.00 44.83           O
ANISOU 3040  O   ASN A 205     4127   7148   5757    163   -194   1508       O
ATOM   3041  CB  ASN A 205     -19.060  16.563 -12.674  1.00 47.07           C
ANISOU 3041  CB  ASN A 205     4447   7451   5986      8   -115   1569       C
ATOM   3042  CG  ASN A 205     -19.849  17.782 -12.259  1.00 46.95           C
ANISOU 3042  CG  ASN A 205     4337   7533   5967     53     25   1565       C
ATOM   3043  OD1 ASN A 205     -21.068  17.786 -12.251  1.00 49.16           O
ANISOU 3043  OD1 ASN A 205     4535   7890   6254     37     49   1613       O
ATOM   3044  ND2 ASN A 205     -19.197  18.880 -11.972  1.00 46.94           N
ANISOU 3044  ND2 ASN A 205     4350   7525   5961    115    102   1501       N
ATOM   3045  H   ASN A 205     -18.160  14.634 -14.539  1.00 57.38           H
ATOM   3046  HA  ASN A 205     -20.754  15.395 -13.252  1.00 59.87           H
ATOM   3047  HB2 ASN A 205     -18.862  15.969 -11.785  1.00 56.48           H
ATOM   3048  HB3 ASN A 205     -18.107  16.872 -13.095  1.00 56.48           H
ATOM   3049 HD21 ASN A 205     -19.788  19.693 -11.834  1.00 56.33           H
ATOM   3050 HD22 ASN A 205     -18.210  18.929 -12.101  1.00 56.33           H
ATOM   3051  N   PHE A 206     -21.435  16.676 -15.256  1.00 47.72           N
ANISOU 3051  N   PHE A 206     4374   7619   6138     31   -148   1633       N
ATOM   3052  CA  PHE A 206     -21.878  17.739 -16.164  1.00 41.39           C
ANISOU 3052  CA  PHE A 206     3501   6870   5355    122    -79   1619       C
ATOM   3053  C   PHE A 206     -22.189  19.006 -15.352  1.00 42.31           C
ANISOU 3053  C   PHE A 206     3557   7053   5468    166     62   1618       C
ATOM   3054  O   PHE A 206     -23.098  19.029 -14.523  1.00 39.89           O
ANISOU 3054  O   PHE A 206     3183   6842   5132    120    107   1659       O
ATOM   3055  CB  PHE A 206     -23.048  17.275 -17.050  1.00 45.79           C
ANISOU 3055  CB  PHE A 206     3995   7475   5929     81   -144   1669       C
ATOM   3056  CG  PHE A 206     -22.675  16.272 -18.135  1.00 43.28           C
ANISOU 3056  CG  PHE A 206     3735   7086   5623    105   -295   1624       C
ATOM   3057  CD1 PHE A 206     -21.819  16.659 -19.186  1.00 42.38           C
ANISOU 3057  CD1 PHE A 206     3634   6977   5490    236   -290   1553       C
ATOM   3058  CD2 PHE A 206     -23.215  14.970 -18.136  1.00 49.51           C
ANISOU 3058  CD2 PHE A 206     4557   7817   6437      1   -457   1654       C
ATOM   3059  CE1 PHE A 206     -21.505  15.756 -20.218  1.00 44.36           C
ANISOU 3059  CE1 PHE A 206     3926   7205   5724    296   -433   1484       C
ATOM   3060  CE2 PHE A 206     -22.937  14.083 -19.193  1.00 47.76           C
ANISOU 3060  CE2 PHE A 206     4400   7519   6228     53   -625   1576       C
ATOM   3061  CZ  PHE A 206     -22.073  14.472 -20.230  1.00 45.60           C
ANISOU 3061  CZ  PHE A 206     4134   7280   5912    218   -607   1477       C
ATOM   3062  H   PHE A 206     -22.114  16.314 -14.594  1.00 57.26           H
ATOM   3063  HA  PHE A 206     -21.063  17.993 -16.843  1.00 49.67           H
ATOM   3064  HB2 PHE A 206     -23.839  16.863 -16.425  1.00 54.95           H
ATOM   3065  HB3 PHE A 206     -23.467  18.150 -17.547  1.00 54.95           H
ATOM   3066  HD1 PHE A 206     -21.405  17.657 -19.209  1.00 50.85           H
ATOM   3067  HD2 PHE A 206     -23.854  14.647 -17.330  1.00 59.41           H
ATOM   3068  HE1 PHE A 206     -20.852  16.060 -21.026  1.00 53.23           H
ATOM   3069  HE2 PHE A 206     -23.377  13.096 -19.203  1.00 57.31           H
ATOM   3070  HZ  PHE A 206     -21.847  13.788 -21.036  1.00 54.72           H
ATOM   3071  N   PHE A 207     -21.347  20.022 -15.535  1.00 42.19           N
ANISOU 3071  N   PHE A 207     3557   6997   5478    258    115   1573       N
ATOM   3072  CA  PHE A 207     -21.377  21.326 -14.876  1.00 41.77           C
ANISOU 3072  CA  PHE A 207     3483   6946   5442    315    205   1541       C
ATOM   3073  C   PHE A 207     -22.228  22.303 -15.708  1.00 41.07           C
ANISOU 3073  C   PHE A 207     3319   6891   5397    394    242   1563       C
ATOM   3074  O   PHE A 207     -21.734  22.862 -16.687  1.00 47.02           O
ANISOU 3074  O   PHE A 207     4074   7598   6194    444    230   1582       O
ATOM   3075  CB  PHE A 207     -19.904  21.769 -14.752  1.00 49.62           C
ANISOU 3075  CB  PHE A 207     4548   7849   6457    341    203   1500       C
ATOM   3076  CG  PHE A 207     -19.619  23.029 -13.961  1.00 44.62           C
ANISOU 3076  CG  PHE A 207     3920   7175   5858    391    254   1449       C
ATOM   3077  CD1 PHE A 207     -19.783  24.302 -14.542  1.00 47.34           C
ANISOU 3077  CD1 PHE A 207     4237   7469   6279    464    265   1456       C
ATOM   3078  CD2 PHE A 207     -19.115  22.923 -12.651  1.00 46.04           C
ANISOU 3078  CD2 PHE A 207     4139   7355   5998    370    268   1392       C
ATOM   3079  CE1 PHE A 207     -19.494  25.458 -13.796  1.00 51.59           C
ANISOU 3079  CE1 PHE A 207     4800   7932   6869    518    271   1392       C
ATOM   3080  CE2 PHE A 207     -18.813  24.075 -11.908  1.00 49.99           C
ANISOU 3080  CE2 PHE A 207     4653   7810   6530    431    289   1317       C
ATOM   3081  CZ  PHE A 207     -19.007  25.340 -12.485  1.00 50.67           C
ANISOU 3081  CZ  PHE A 207     4724   7819   6708    508    281   1309       C
ATOM   3082  H   PHE A 207     -20.605  19.895 -16.217  1.00 50.63           H
ATOM   3083  HA  PHE A 207     -21.809  21.236 -13.879  1.00 50.12           H
ATOM   3084  HB2 PHE A 207     -19.339  20.950 -14.303  1.00 59.55           H
ATOM   3085  HB3 PHE A 207     -19.497  21.911 -15.749  1.00 59.55           H
ATOM   3086  HD1 PHE A 207     -20.136  24.400 -15.560  1.00 56.80           H
ATOM   3087  HD2 PHE A 207     -18.963  21.947 -12.218  1.00 55.25           H
ATOM   3088  HE1 PHE A 207     -19.660  26.435 -14.228  1.00 61.90           H
ATOM   3089  HE2 PHE A 207     -18.445  23.987 -10.899  1.00 59.98           H
ATOM   3090  HZ  PHE A 207     -18.795  26.225 -11.920  1.00 60.80           H
ATOM   3091  N   ALA A 208     -23.534  22.385 -15.439  1.00 42.22           N
ANISOU 3091  N   ALA A 208     3384   7139   5519    407    282   1572       N
ATOM   3092  CA  ALA A 208     -24.466  23.230 -16.192  1.00 47.57           C
ANISOU 3092  CA  ALA A 208     3980   7866   6229    488    305   1594       C
ATOM   3093  C   ALA A 208     -24.519  24.658 -15.619  1.00 45.35           C
ANISOU 3093  C   ALA A 208     3691   7553   5987    609    348   1527       C
ATOM   3094  O   ALA A 208     -24.998  24.867 -14.498  1.00 43.10           O
ANISOU 3094  O   ALA A 208     3362   7365   5649    651    389   1473       O
ATOM   3095  CB  ALA A 208     -25.839  22.547 -16.190  1.00 45.24           C
ANISOU 3095  CB  ALA A 208     3581   7728   5878    438    306   1646       C
ATOM   3096  H   ALA A 208     -23.910  21.889 -14.638  1.00 50.66           H
ATOM   3097  HA  ALA A 208     -24.130  23.300 -17.226  1.00 57.08           H
ATOM   3098  HB1 ALA A 208     -26.499  23.065 -16.881  1.00 54.28           H
ATOM   3099  HB2 ALA A 208     -25.737  21.511 -16.506  1.00 54.28           H
ATOM   3100  HB3 ALA A 208     -26.275  22.574 -15.191  1.00 54.28           H
ATOM   3101  N   GLN A 209     -23.981  25.637 -16.350  1.00 43.29           N
ANISOU 3101  N   GLN A 209     3466   7167   5814    672    324   1536       N
ATOM   3102  CA  GLN A 209     -23.981  27.040 -15.932  1.00 46.98           C
ANISOU 3102  CA  GLN A 209     3951   7546   6354    788    318   1472       C
ATOM   3103  C   GLN A 209     -25.319  27.731 -16.270  1.00 50.53           C
ANISOU 3103  C   GLN A 209     4313   8071   6816    904    329   1469       C
ATOM   3104  O   GLN A 209     -25.895  27.515 -17.336  1.00 46.86           O
ANISOU 3104  O   GLN A 209     3790   7662   6351    894    326   1554       O
ATOM   3105  CB  GLN A 209     -22.748  27.738 -16.533  1.00 43.70           C
ANISOU 3105  CB  GLN A 209     3604   6955   6044    778    261   1520       C
ATOM   3106  CG  GLN A 209     -22.536  29.184 -16.055  1.00 46.78           C
ANISOU 3106  CG  GLN A 209     4042   7190   6542    876    207   1456       C
ATOM   3107  CD  GLN A 209     -22.172  29.324 -14.578  1.00 47.08           C
ANISOU 3107  CD  GLN A 209     4136   7202   6552    892    208   1320       C
ATOM   3108  OE1 GLN A 209     -22.071  28.375 -13.806  1.00 45.74           O
ANISOU 3108  OE1 GLN A 209     3971   7124   6283    812    255   1301       O
ATOM   3109  NE2 GLN A 209     -22.044  30.532 -14.097  1.00 48.27           N
ANISOU 3109  NE2 GLN A 209     4332   7218   6789   1002    138   1222       N
ATOM   3110  H   GLN A 209     -23.653  25.433 -17.293  1.00 51.94           H
ATOM   3111  HA  GLN A 209     -23.871  27.063 -14.850  1.00 56.38           H
ATOM   3112  HB2 GLN A 209     -21.856  27.159 -16.288  1.00 52.44           H
ATOM   3113  HB3 GLN A 209     -22.845  27.733 -17.618  1.00 52.44           H
ATOM   3114  HG2 GLN A 209     -21.732  29.625 -16.640  1.00 56.14           H
ATOM   3115  HG3 GLN A 209     -23.431  29.773 -16.255  1.00 56.14           H
ATOM   3116 HE21 GLN A 209     -22.244  31.321 -14.714  1.00 57.92           H
ATOM   3117 HE22 GLN A 209     -22.104  30.645 -13.109  1.00 57.92           H
ATOM   3118  N   ILE A 210     -25.856  28.509 -15.319  1.00 51.87           N
ANISOU 3118  N   ILE A 210     4468   8253   6986   1035    331   1358       N
ATOM   3119  CA  ILE A 210     -27.213  29.087 -15.394  1.00 56.89           C
ANISOU 3119  CA  ILE A 210     5007   9003   7607   1179    342   1326       C
ATOM   3120  C   ILE A 210     -27.188  30.616 -15.387  1.00 56.78           C
ANISOU 3120  C   ILE A 210     5050   8808   7715   1347    260   1245       C
ATOM   3121  O   ILE A 210     -27.765  31.238 -16.271  1.00 58.07           O
ANISOU 3121  O   ILE A 210     5196   8906   7962   1417    215   1304       O
ATOM   3122  CB  ILE A 210     -28.100  28.527 -14.255  1.00 58.44           C
ANISOU 3122  CB  ILE A 210     5097   9456   7651   1213    411   1257       C
ATOM   3123  CG1 ILE A 210     -28.391  27.031 -14.495  1.00 51.71           C
ANISOU 3123  CG1 ILE A 210     4179   8761   6706   1029    455   1377       C
ATOM   3124  CG2 ILE A 210     -29.423  29.297 -14.110  1.00 57.88           C
ANISOU 3124  CG2 ILE A 210     4913   9531   7548   1408    418   1189       C
ATOM   3125  CD1 ILE A 210     -28.886  26.297 -13.247  1.00 50.70           C
ANISOU 3125  CD1 ILE A 210     3956   8880   6429    995    511   1362       C
ATOM   3126  H   ILE A 210     -25.353  28.612 -14.446  1.00 62.24           H
ATOM   3127  HA  ILE A 210     -27.674  28.802 -16.339  1.00 68.27           H
ATOM   3128  HB  ILE A 210     -27.556  28.630 -13.318  1.00 70.13           H
ATOM   3129 HG12 ILE A 210     -29.128  26.927 -15.292  1.00 62.05           H
ATOM   3130 HG13 ILE A 210     -27.478  26.527 -14.811  1.00 62.05           H
ATOM   3131 HG21 ILE A 210     -30.050  28.867 -13.330  1.00 69.46           H
ATOM   3132 HG22 ILE A 210     -29.256  30.341 -13.845  1.00 69.46           H
ATOM   3133 HG23 ILE A 210     -29.964  29.264 -15.053  1.00 69.46           H
ATOM   3134 HD11 ILE A 210     -29.016  25.241 -13.483  1.00 60.84           H
ATOM   3135 HD12 ILE A 210     -28.150  26.402 -12.451  1.00 60.84           H
ATOM   3136 HD13 ILE A 210     -29.840  26.698 -12.911  1.00 60.84           H
ATOM   3137  N   LYS A 211     -26.499  31.225 -14.413  1.00 55.34           N
ANISOU 3137  N   LYS A 211     4938   8537   7550   1418    222   1108       N
ATOM   3138  CA  LYS A 211     -26.420  32.685 -14.236  1.00 52.97           C
ANISOU 3138  CA  LYS A 211     4714   8028   7383   1584    103   1004       C
ATOM   3139  C   LYS A 211     -24.985  33.103 -13.958  1.00 52.49           C
ANISOU 3139  C   LYS A 211     4790   7722   7432   1494     20    996       C
ATOM   3140  O   LYS A 211     -24.292  32.415 -13.204  1.00 50.60           O
ANISOU 3140  O   LYS A 211     4574   7535   7116   1390     69    971       O
ATOM   3141  CB  LYS A 211     -27.364  33.144 -13.109  1.00 54.57           C
ANISOU 3141  CB  LYS A 211     4862   8376   7497   1810    100    796       C
ATOM   3142  CG  LYS A 211     -27.556  34.671 -13.063  1.00 57.64           C
ANISOU 3142  CG  LYS A 211     5335   8534   8032   2026    -61    656       C
ATOM   3143  CD  LYS A 211     -28.545  35.089 -11.964  1.00 60.79           C
ANISOU 3143  CD  LYS A 211     5660   9130   8307   2295    -65    420       C
ATOM   3144  CE  LYS A 211     -29.093  36.514 -12.144  1.00 66.53           C
ANISOU 3144  CE  LYS A 211     6426   9686   9165   2553   -223    305       C
ATOM   3145  NZ  LYS A 211     -28.030  37.551 -12.191  1.00 67.30           N
ANISOU 3145  NZ  LYS A 211     6715   9359   9499   2557   -427    267       N
ATOM   3146  H   LYS A 211     -25.994  30.636 -13.762  1.00 66.40           H
ATOM   3147  HA  LYS A 211     -26.739  33.162 -15.165  1.00 63.56           H
ATOM   3148  HB2 LYS A 211     -28.339  32.674 -13.253  1.00 65.49           H
ATOM   3149  HB3 LYS A 211     -26.954  32.817 -12.156  1.00 65.49           H
ATOM   3150  HG2 LYS A 211     -26.600  35.156 -12.862  1.00 69.17           H
ATOM   3151  HG3 LYS A 211     -27.930  35.005 -14.031  1.00 69.17           H
ATOM   3152  HD2 LYS A 211     -29.397  34.416 -11.992  1.00 72.95           H
ATOM   3153  HD3 LYS A 211     -28.075  34.982 -10.987  1.00 72.95           H
ATOM   3154  HE2 LYS A 211     -29.681  36.538 -13.068  1.00 79.83           H
ATOM   3155  HE3 LYS A 211     -29.786  36.725 -11.323  1.00 79.83           H
ATOM   3156  HZ1 LYS A 211     -28.443  38.463 -12.350  1.00 80.77           H
ATOM   3157  HZ2 LYS A 211     -27.511  37.578 -11.323  1.00 80.77           H
ATOM   3158  HZ3 LYS A 211     -27.384  37.363 -12.946  1.00 80.77           H
ATOM   3159  N   GLY A 212     -24.601  34.280 -14.449  1.00 54.29           N
ANISOU 3159  N   GLY A 212     5101   7684   7844   1526   -118   1035       N
ATOM   3160  CA  GLY A 212     -23.241  34.800 -14.315  1.00 56.41           C
ANISOU 3160  CA  GLY A 212     5485   7716   8233   1423   -220   1054       C
ATOM   3161  C   GLY A 212     -22.218  33.919 -15.037  1.00 57.02           C
ANISOU 3161  C   GLY A 212     5552   7816   8295   1194   -163   1253       C
ATOM   3162  O   GLY A 212     -22.558  32.874 -15.599  1.00 54.41           O
ANISOU 3162  O   GLY A 212     5142   7654   7877   1126    -65   1369       O
ATOM   3163  H   GLY A 212     -25.216  34.743 -15.097  1.00 65.15           H
ATOM   3164  HA2 GLY A 212     -23.189  35.805 -14.736  1.00 67.69           H
ATOM   3165  HA3 GLY A 212     -22.977  34.864 -13.258  1.00 67.69           H
ATOM   3166  N   TYR A 213     -20.942  34.267 -14.911  1.00 54.51           N
ANISOU 3166  N   TYR A 213     5314   7338   8060   1086   -240   1280       N
ATOM   3167  CA  TYR A 213     -19.855  33.554 -15.582  1.00 54.07           C
ANISOU 3167  CA  TYR A 213     5242   7315   7986    892   -207   1458       C
ATOM   3168  C   TYR A 213     -18.904  32.914 -14.569  1.00 49.24           C
ANISOU 3168  C   TYR A 213     4676   6723   7311    812   -182   1374       C
ATOM   3169  O   TYR A 213     -18.628  33.469 -13.499  1.00 47.08           O
ANISOU 3169  O   TYR A 213     4475   6318   7094    863   -263   1233       O
ATOM   3170  CB  TYR A 213     -19.158  34.494 -16.578  1.00 56.44           C
ANISOU 3170  CB  TYR A 213     5562   7427   8456    808   -340   1647       C
ATOM   3171  CG  TYR A 213     -20.050  34.899 -17.746  1.00 61.16           C
ANISOU 3171  CG  TYR A 213     6104   8033   9101    865   -359   1775       C
ATOM   3172  CD1 TYR A 213     -20.963  35.958 -17.585  1.00 62.80           C
ANISOU 3172  CD1 TYR A 213     6349   8087   9424   1024   -463   1698       C
ATOM   3173  CD2 TYR A 213     -20.009  34.195 -18.970  1.00 60.19           C
ANISOU 3173  CD2 TYR A 213     5887   8084   8897    779   -281   1959       C
ATOM   3174  CE1 TYR A 213     -21.880  36.260 -18.602  1.00 62.86           C
ANISOU 3174  CE1 TYR A 213     6304   8106   9474   1082   -484   1820       C
ATOM   3175  CE2 TYR A 213     -20.898  34.533 -20.016  1.00 60.80           C
ANISOU 3175  CE2 TYR A 213     5906   8188   9006    834   -299   2078       C
ATOM   3176  CZ  TYR A 213     -21.865  35.546 -19.814  1.00 62.62           C
ANISOU 3176  CZ  TYR A 213     6176   8257   9359    978   -397   2017       C
ATOM   3177  OH  TYR A 213     -22.855  35.819 -20.702  1.00 66.96           O
ANISOU 3177  OH  TYR A 213     6667   8836   9940   1036   -419   2142       O
ATOM   3178  H   TYR A 213     -20.709  35.109 -14.403  1.00 65.41           H
ATOM   3179  HA  TYR A 213     -20.271  32.741 -16.174  1.00 64.88           H
ATOM   3180  HB2 TYR A 213     -18.840  35.395 -16.054  1.00 67.73           H
ATOM   3181  HB3 TYR A 213     -18.268  34.003 -16.968  1.00 67.73           H
ATOM   3182  HD1 TYR A 213     -20.978  36.543 -16.675  1.00 75.36           H
ATOM   3183  HD2 TYR A 213     -19.311  33.378 -19.098  1.00 72.22           H
ATOM   3184  HE1 TYR A 213     -22.602  37.052 -18.491  1.00 75.43           H
ATOM   3185  HE2 TYR A 213     -20.886  33.998 -20.954  1.00 72.96           H
ATOM   3186  HH  TYR A 213     -22.609  35.843 -21.659  1.00 80.35           H
ATOM   3187  N   LYS A 214     -18.390  31.728 -14.907  1.00 46.84           N
ANISOU 3187  N   LYS A 214     4329   6582   6887    700    -83   1450       N
ATOM   3188  CA  LYS A 214     -17.356  31.039 -14.126  1.00 50.00           C
ANISOU 3188  CA  LYS A 214     4764   7021   7214    622    -56   1391       C
ATOM   3189  C   LYS A 214     -16.189  30.674 -15.022  1.00 50.17           C
ANISOU 3189  C   LYS A 214     4757   7080   7225    483    -60   1554       C
ATOM   3190  O   LYS A 214     -16.348  29.944 -15.999  1.00 45.39           O
ANISOU 3190  O   LYS A 214     4084   6602   6561    459    -12   1668       O
ATOM   3191  CB  LYS A 214     -17.915  29.805 -13.404  1.00 49.09           C
ANISOU 3191  CB  LYS A 214     4623   7096   6934    648     58   1297       C
ATOM   3192  CG  LYS A 214     -18.722  30.184 -12.154  1.00 47.59           C
ANISOU 3192  CG  LYS A 214     4445   6932   6703    772     68   1119       C
ATOM   3193  CD  LYS A 214     -19.265  28.911 -11.499  1.00 44.44           C
ANISOU 3193  CD  LYS A 214     4002   6746   6136    753    172   1086       C
ATOM   3194  CE  LYS A 214     -19.917  29.184 -10.144  1.00 47.32           C
ANISOU 3194  CE  LYS A 214     4359   7199   6423    866    187    921       C
ATOM   3195  NZ  LYS A 214     -20.514  27.970  -9.549  1.00 52.39           N
ANISOU 3195  NZ  LYS A 214     4941   8065   6898    814    279    938       N
ATOM   3196  H   LYS A 214     -18.650  31.342 -15.814  1.00 56.21           H
ATOM   3197  HA  LYS A 214     -16.967  31.720 -13.369  1.00 60.00           H
ATOM   3198  HB2 LYS A 214     -18.533  29.224 -14.091  1.00 58.91           H
ATOM   3199  HB3 LYS A 214     -17.076  29.180 -13.090  1.00 58.91           H
ATOM   3200  HG2 LYS A 214     -18.069  30.703 -11.450  1.00 57.10           H
ATOM   3201  HG3 LYS A 214     -19.550  30.838 -12.430  1.00 57.10           H
ATOM   3202  HD2 LYS A 214     -19.993  28.460 -12.175  1.00 53.33           H
ATOM   3203  HD3 LYS A 214     -18.433  28.233 -11.351  1.00 53.33           H
ATOM   3204  HE2 LYS A 214     -19.183  29.632  -9.467  1.00 56.79           H
ATOM   3205  HE3 LYS A 214     -20.720  29.896 -10.316  1.00 56.79           H
ATOM   3206  HZ1 LYS A 214     -20.849  28.159  -8.614  1.00 62.86           H
ATOM   3207  HZ2 LYS A 214     -21.314  27.700 -10.121  1.00 62.86           H
ATOM   3208  HZ3 LYS A 214     -19.865  27.203  -9.536  1.00 62.86           H
ATOM   3209  N   ARG A 215     -14.994  31.067 -14.594  1.00 53.30           N
ANISOU 3209  N   ARG A 215     5193   7390   7669    402   -125   1557       N
ATOM   3210  CA  ARG A 215     -13.744  30.554 -15.139  1.00 47.90           C
ANISOU 3210  CA  ARG A 215     4462   6794   6944    280   -124   1697       C
ATOM   3211  C   ARG A 215     -13.451  29.193 -14.512  1.00 44.65           C
ANISOU 3211  C   ARG A 215     4058   6531   6378    273    -40   1607       C
ATOM   3212  O   ARG A 215     -13.374  29.062 -13.286  1.00 41.13           O
ANISOU 3212  O   ARG A 215     3673   6043   5912    286    -41   1471       O
ATOM   3213  CB  ARG A 215     -12.646  31.576 -14.872  1.00 51.07           C
ANISOU 3213  CB  ARG A 215     4887   7041   7477    181   -250   1765       C
ATOM   3214  CG  ARG A 215     -11.329  31.220 -15.566  1.00 51.98           C
ANISOU 3214  CG  ARG A 215     4921   7292   7538     52   -253   1930       C
ATOM   3215  CD  ARG A 215     -10.232  31.928 -14.785  1.00 54.66           C
ANISOU 3215  CD  ARG A 215     5294   7505   7968    -53   -362   1935       C
ATOM   3216  NE  ARG A 215      -8.973  31.950 -15.520  1.00 54.81           N
ANISOU 3216  NE  ARG A 215     5203   7660   7964   -192   -393   2150       N
ATOM   3217  CZ  ARG A 215      -7.856  32.499 -15.112  1.00 56.33           C
ANISOU 3217  CZ  ARG A 215     5386   7792   8227   -321   -493   2212       C
ATOM   3218  NH1 ARG A 215      -7.743  32.989 -13.916  1.00 58.04           N
ANISOU 3218  NH1 ARG A 215     5715   7789   8548   -319   -583   2054       N
ATOM   3219  NH2 ARG A 215      -6.841  32.523 -15.906  1.00 54.91           N
ANISOU 3219  NH2 ARG A 215     5071   7795   7999   -446   -511   2430       N
ATOM   3220  H   ARG A 215     -14.959  31.565 -13.709  1.00 63.96           H
ATOM   3221  HA  ARG A 215     -13.843  30.431 -16.217  1.00 57.48           H
ATOM   3222  HB2 ARG A 215     -12.960  32.555 -15.234  1.00 61.29           H
ATOM   3223  HB3 ARG A 215     -12.502  31.650 -13.796  1.00 61.29           H
ATOM   3224  HG2 ARG A 215     -11.138  30.147 -15.546  1.00 62.38           H
ATOM   3225  HG3 ARG A 215     -11.352  31.566 -16.601  1.00 62.38           H
ATOM   3226  HD2 ARG A 215     -10.535  32.955 -14.570  1.00 65.59           H
ATOM   3227  HD3 ARG A 215     -10.094  31.403 -13.839  1.00 65.59           H
ATOM   3228  HE  ARG A 215      -8.962  31.687 -16.507  1.00 65.78           H
ATOM   3229 HH11 ARG A 215      -8.557  32.995 -13.306  1.00 69.65           H
ATOM   3230 HH12 ARG A 215      -6.953  33.575 -13.666  1.00 69.65           H
ATOM   3231 HH21 ARG A 215      -6.980  32.091 -16.828  1.00 65.90           H
ATOM   3232 HH22 ARG A 215      -5.979  32.948 -15.639  1.00 65.90           H
ATOM   3233  N   CYS A 216     -13.232  28.195 -15.355  1.00 43.14           N
ANISOU 3233  N   CYS A 216     3806   6509   6076    262     16   1679       N
ATOM   3234  CA  CYS A 216     -12.926  26.826 -14.967  1.00 40.78           C
ANISOU 3234  CA  CYS A 216     3523   6328   5642    266     66   1602       C
ATOM   3235  C   CYS A 216     -11.541  26.454 -15.507  1.00 44.43           C
ANISOU 3235  C   CYS A 216     3935   6905   6042    214     45   1683       C
ATOM   3236  O   CYS A 216     -11.365  26.328 -16.716  1.00 44.79           O
ANISOU 3236  O   CYS A 216     3895   7066   6056    214     41   1804       O
ATOM   3237  CB  CYS A 216     -14.022  25.891 -15.504  1.00 42.51           C
ANISOU 3237  CB  CYS A 216     3725   6644   5784    322    116   1583       C
ATOM   3238  SG  CYS A 216     -15.672  26.397 -14.932  1.00 45.23           S
ANISOU 3238  SG  CYS A 216     4078   6924   6185    390    146   1523       S
ATOM   3239  H   CYS A 216     -13.286  28.402 -16.347  1.00 51.77           H
ATOM   3240  HA  CYS A 216     -12.905  26.745 -13.880  1.00 48.93           H
ATOM   3241  HB2 CYS A 216     -14.002  25.921 -16.594  1.00 51.02           H
ATOM   3242  HB3 CYS A 216     -13.820  24.869 -15.183  1.00 51.02           H
ATOM   3243  HG  CYS A 216     -16.380  25.590 -15.732  1.00 54.28           H
ATOM   3244  N   ILE A 217     -10.575  26.253 -14.606  1.00 46.23           N
ANISOU 3244  N   ILE A 217     4201   7129   6235    181     32   1618       N
ATOM   3245  CA  ILE A 217      -9.228  25.769 -14.933  1.00 41.67           C
ANISOU 3245  CA  ILE A 217     3567   6690   5575    149     13   1674       C
ATOM   3246  C   ILE A 217      -9.114  24.325 -14.450  1.00 38.75           C
ANISOU 3246  C   ILE A 217     3243   6400   5081    208     34   1563       C
ATOM   3247  O   ILE A 217      -9.209  24.056 -13.247  1.00 37.88           O
ANISOU 3247  O   ILE A 217     3214   6214   4965    204     39   1459       O
ATOM   3248  CB  ILE A 217      -8.124  26.642 -14.300  1.00 44.44           C
ANISOU 3248  CB  ILE A 217     3919   6974   5994     58    -42   1700       C
ATOM   3249  CG1 ILE A 217      -8.297  28.149 -14.599  1.00 48.15           C
ANISOU 3249  CG1 ILE A 217     4375   7294   6627     -8   -105   1802       C
ATOM   3250  CG2 ILE A 217      -6.741  26.130 -14.747  1.00 41.64           C
ANISOU 3250  CG2 ILE A 217     3468   6816   5537     28    -58   1783       C
ATOM   3251  CD1 ILE A 217      -7.311  29.022 -13.814  1.00 42.35           C
ANISOU 3251  CD1 ILE A 217     3655   6446   5992   -114   -199   1824       C
ATOM   3252  H   ILE A 217     -10.810  26.349 -13.626  1.00 55.47           H
ATOM   3253  HA  ILE A 217      -9.082  25.790 -16.014  1.00 50.01           H
ATOM   3254  HB  ILE A 217      -8.188  26.520 -13.221  1.00 53.33           H
ATOM   3255 HG12 ILE A 217      -8.176  28.335 -15.668  1.00 57.79           H
ATOM   3256 HG13 ILE A 217      -9.300  28.465 -14.312  1.00 57.79           H
ATOM   3257 HG21 ILE A 217      -5.967  26.593 -14.142  1.00 49.97           H
ATOM   3258 HG22 ILE A 217      -6.645  25.052 -14.616  1.00 49.97           H
ATOM   3259 HG23 ILE A 217      -6.573  26.368 -15.798  1.00 49.97           H
ATOM   3260 HD11 ILE A 217      -7.622  30.062 -13.875  1.00 50.83           H
ATOM   3261 HD12 ILE A 217      -7.296  28.726 -12.766  1.00 50.83           H
ATOM   3262 HD13 ILE A 217      -6.312  28.933 -14.238  1.00 50.83           H
ATOM   3263  N   LEU A 218      -9.034  23.392 -15.387  1.00 44.06           N
ANISOU 3263  N   LEU A 218     3864   7227   5650    270     29   1585       N
ATOM   3264  CA  LEU A 218      -8.895  21.962 -15.154  1.00 43.17           C
ANISOU 3264  CA  LEU A 218     3804   7162   5436    338      7   1483       C
ATOM   3265  C   LEU A 218      -7.423  21.533 -15.240  1.00 45.32           C
ANISOU 3265  C   LEU A 218     4027   7589   5605    374    -30   1479       C
ATOM   3266  O   LEU A 218      -6.658  22.136 -15.984  1.00 46.02           O
ANISOU 3266  O   LEU A 218     4000   7824   5663    365    -30   1580       O
ATOM   3267  CB  LEU A 218      -9.779  21.216 -16.170  1.00 44.49           C
ANISOU 3267  CB  LEU A 218     3964   7376   5562    413     -7   1469       C
ATOM   3268  CG  LEU A 218     -11.242  21.034 -15.725  1.00 49.07           C
ANISOU 3268  CG  LEU A 218     4608   7831   6204    392     13   1437       C
ATOM   3269  CD1 LEU A 218     -12.018  22.336 -15.509  1.00 44.68           C
ANISOU 3269  CD1 LEU A 218     4033   7189   5755    342     68   1490       C
ATOM   3270  CD2 LEU A 218     -11.981  20.220 -16.777  1.00 47.39           C
ANISOU 3270  CD2 LEU A 218     4379   7676   5951    457    -26   1427       C
ATOM   3271  H   LEU A 218      -8.972  23.705 -16.352  1.00 52.87           H
ATOM   3272  HA  LEU A 218      -9.240  21.740 -14.153  1.00 51.80           H
ATOM   3273  HB2 LEU A 218      -9.750  21.734 -17.130  1.00 53.38           H
ATOM   3274  HB3 LEU A 218      -9.357  20.226 -16.329  1.00 53.38           H
ATOM   3275  HG  LEU A 218     -11.260  20.465 -14.799  1.00 58.88           H
ATOM   3276 HD11 LEU A 218     -11.601  22.888 -14.670  1.00  0.00           H
ATOM   3277 HD12 LEU A 218     -13.059  22.108 -15.292  1.00  0.00           H
ATOM   3278 HD13 LEU A 218     -11.960  22.951 -16.409  1.00  0.00           H
ATOM   3279 HD21 LEU A 218     -11.482  19.259 -16.917  1.00  0.00           H
ATOM   3280 HD22 LEU A 218     -11.985  20.764 -17.721  1.00  0.00           H
ATOM   3281 HD23 LEU A 218     -13.008  20.036 -16.470  1.00  0.00           H
ATOM   3282  N   PHE A 219      -7.067  20.409 -14.614  1.00 39.60           N
ANISOU 3282  N   PHE A 219     3379   6848   4820    415    -68   1376       N
ATOM   3283  CA  PHE A 219      -5.779  19.733 -14.843  1.00 43.23           C
ANISOU 3283  CA  PHE A 219     3797   7464   5164    490   -118   1343       C
ATOM   3284  C   PHE A 219      -6.010  18.217 -14.970  1.00 47.42           C
ANISOU 3284  C   PHE A 219     4408   7987   5624    608   -200   1229       C
ATOM   3285  O   PHE A 219      -6.841  17.684 -14.216  1.00 44.21           O
ANISOU 3285  O   PHE A 219     4115   7414   5269    574   -221   1183       O
ATOM   3286  CB  PHE A 219      -4.735  20.069 -13.759  1.00 41.28           C
ANISOU 3286  CB  PHE A 219     3572   7187   4926    423   -117   1328       C
ATOM   3287  CG  PHE A 219      -4.588  21.547 -13.433  1.00 43.48           C
ANISOU 3287  CG  PHE A 219     3802   7411   5306    295    -77   1420       C
ATOM   3288  CD1 PHE A 219      -3.616  22.312 -14.099  1.00 40.40           C
ANISOU 3288  CD1 PHE A 219     3278   7176   4897    253    -83   1538       C
ATOM   3289  CD2 PHE A 219      -5.412  22.164 -12.469  1.00 44.81           C
ANISOU 3289  CD2 PHE A 219     4054   7384   5586    222    -51   1393       C
ATOM   3290  CE1 PHE A 219      -3.465  23.680 -13.808  1.00 43.12           C
ANISOU 3290  CE1 PHE A 219     3591   7431   5361    118    -86   1635       C
ATOM   3291  CE2 PHE A 219      -5.275  23.536 -12.189  1.00 43.53           C
ANISOU 3291  CE2 PHE A 219     3867   7139   5533    125    -53   1452       C
ATOM   3292  CZ  PHE A 219      -4.293  24.292 -12.855  1.00 45.38           C
ANISOU 3292  CZ  PHE A 219     3987   7480   5778     62    -81   1578       C
ATOM   3293  H   PHE A 219      -7.777  19.894 -14.108  1.00 47.52           H
ATOM   3294  HA  PHE A 219      -5.369  20.103 -15.779  1.00 51.88           H
ATOM   3295  HB2 PHE A 219      -4.951  19.523 -12.845  1.00 49.54           H
ATOM   3296  HB3 PHE A 219      -3.767  19.696 -14.101  1.00 49.54           H
ATOM   3297  HD1 PHE A 219      -2.968  21.842 -14.826  1.00 48.48           H
ATOM   3298  HD2 PHE A 219      -6.157  21.583 -11.953  1.00 53.77           H
ATOM   3299  HE1 PHE A 219      -2.701  24.259 -14.310  1.00 51.74           H
ATOM   3300  HE2 PHE A 219      -5.918  24.011 -11.465  1.00 52.24           H
ATOM   3301  HZ  PHE A 219      -4.164  25.343 -12.640  1.00 54.46           H
ATOM   3302  N   PRO A 220      -5.347  17.520 -15.913  1.00 46.35           N
ANISOU 3302  N   PRO A 220     4212   8034   5367    750   -263   1184       N
ATOM   3303  CA  PRO A 220      -5.528  16.082 -16.077  1.00 45.56           C
ANISOU 3303  CA  PRO A 220     4206   7889   5217    881   -386   1054       C
ATOM   3304  C   PRO A 220      -5.085  15.292 -14.823  1.00 47.96           C
ANISOU 3304  C   PRO A 220     4627   8067   5527    874   -453    984       C
ATOM   3305  O   PRO A 220      -4.318  15.797 -13.997  1.00 44.33           O
ANISOU 3305  O   PRO A 220     4150   7625   5067    807   -402   1015       O
ATOM   3306  CB  PRO A 220      -4.709  15.684 -17.301  1.00 46.21           C
ANISOU 3306  CB  PRO A 220     4171   8244   5144   1066   -441   1005       C
ATOM   3307  CG  PRO A 220      -4.438  16.979 -18.051  1.00 51.96           C
ANISOU 3307  CG  PRO A 220     4734   9153   5855   1001   -330   1151       C
ATOM   3308  CD  PRO A 220      -4.431  18.021 -16.934  1.00 52.03           C
ANISOU 3308  CD  PRO A 220     4760   9025   5982    808   -241   1254       C
ATOM   3309  HA  PRO A 220      -6.576  15.898 -16.294  1.00 54.68           H
ATOM   3310  HB2 PRO A 220      -3.771  15.300 -16.948  1.00 55.46           H
ATOM   3311  HB3 PRO A 220      -5.198  14.935 -17.924  1.00 55.46           H
ATOM   3312  HG2 PRO A 220      -3.483  16.949 -18.581  1.00 62.35           H
ATOM   3313  HG3 PRO A 220      -5.253  17.174 -18.745  1.00 62.35           H
ATOM   3314  HD2 PRO A 220      -3.431  18.099 -16.509  1.00 62.43           H
ATOM   3315  HD3 PRO A 220      -4.743  18.980 -17.345  1.00 62.43           H
ATOM   3316  N   PRO A 221      -5.513  14.025 -14.674  1.00 47.43           N
ANISOU 3316  N   PRO A 221     4684   7865   5472    936   -584    898       N
ATOM   3317  CA  PRO A 221      -5.116  13.173 -13.550  1.00 45.34           C
ANISOU 3317  CA  PRO A 221     4534   7483   5211    933   -670    851       C
ATOM   3318  C   PRO A 221      -3.620  12.817 -13.503  1.00 45.64           C
ANISOU 3318  C   PRO A 221     4523   7684   5133   1066   -713    781       C
ATOM   3319  O   PRO A 221      -3.213  12.179 -12.524  1.00 45.97           O
ANISOU 3319  O   PRO A 221     4620   7672   5176   1028   -727    778       O
ATOM   3320  CB  PRO A 221      -5.949  11.895 -13.692  1.00 47.54           C
ANISOU 3320  CB  PRO A 221     4941   7591   5532    985   -845    786       C
ATOM   3321  CG  PRO A 221      -7.137  12.305 -14.556  1.00 48.79           C
ANISOU 3321  CG  PRO A 221     5064   7730   5743    936   -803    830       C
ATOM   3322  CD  PRO A 221      -6.558  13.390 -15.454  1.00 46.28           C
ANISOU 3322  CD  PRO A 221     4588   7636   5359    980   -673    860       C
ATOM   3323  HA  PRO A 221      -5.376  13.680 -12.621  1.00 54.41           H
ATOM   3324  HB2 PRO A 221      -5.373  11.137 -14.221  1.00 57.05           H
ATOM   3325  HB3 PRO A 221      -6.264  11.519 -12.719  1.00 57.05           H
ATOM   3326  HG2 PRO A 221      -7.522  11.471 -15.143  1.00 58.55           H
ATOM   3327  HG3 PRO A 221      -7.919  12.730 -13.928  1.00 58.55           H
ATOM   3328  HD2 PRO A 221      -6.126  12.954 -16.357  1.00 55.53           H
ATOM   3329  HD3 PRO A 221      -7.350  14.091 -15.714  1.00 55.53           H
ATOM   3330  N   ASP A 222      -2.877  12.999 -14.594  1.00 53.94           N
ANISOU 3330  N   ASP A 222     5460   8966   6068   1230   -735    726       N
ATOM   3331  CA  ASP A 222      -1.434  12.737 -14.650  1.00 50.24           C
ANISOU 3331  CA  ASP A 222     4922   8703   5464   1381   -783    655       C
ATOM   3332  C   ASP A 222      -0.643  13.833 -13.916  1.00 47.35           C
ANISOU 3332  C   ASP A 222     4446   8460   5084   1254   -648    763       C
ATOM   3333  O   ASP A 222       0.145  13.437 -13.039  1.00 55.86           O
ANISOU 3333  O   ASP A 222     5459   9709   6055   1348   -680    722       O
ATOM   3334  CB  ASP A 222      -1.001  12.475 -16.107  1.00 49.76           C
ANISOU 3334  CB  ASP A 222     4734   8923   5249   1607   -838    570       C
ATOM   3335  CG  ASP A 222      -1.377  13.551 -17.122  1.00 54.51           C
ANISOU 3335  CG  ASP A 222     5150   9749   5814   1535   -689    705       C
ATOM   3336  OD1 ASP A 222      -1.602  14.690 -16.654  1.00 59.15           O
ANISOU 3336  OD1 ASP A 222     5665  10351   6457   1348   -556    855       O
ATOM   3337  OD2 ASP A 222      -1.770  13.149 -18.235  1.00 62.22           O
ANISOU 3337  OD2 ASP A 222     6051  10887   6704   1673   -723    662       O
ATOM   3338  H   ASP A 222      -3.246  13.545 -15.359  1.00 64.72           H
ATOM   3339  HA  ASP A 222      -1.224  11.821 -14.109  1.00 60.29           H
ATOM   3340  HB2 ASP A 222       0.076  12.324 -16.161  1.00 59.71           H
ATOM   3341  HB3 ASP A 222      -1.478  11.549 -16.425  1.00 59.71           H
ATOM   3342  N   GLN A 223      -1.092  15.080 -13.877  1.00 45.22           N
ANISOU 3342  N   GLN A 223     4151   8109   4921   1052   -517    891       N
ATOM   3343  CA  GLN A 223      -0.519  16.194 -13.092  1.00 45.68           C
ANISOU 3343  CA  GLN A 223     4134   8223   5001    913   -425    983       C
ATOM   3344  C   GLN A 223      -0.745  16.095 -11.557  1.00 41.63           C
ANISOU 3344  C   GLN A 223     3753   7495   4569    803   -424    966       C
ATOM   3345  O   GLN A 223      -0.691  17.094 -10.837  1.00 43.73           O
ANISOU 3345  O   GLN A 223     3992   7726   4897    660   -349   1032       O
ATOM   3346  CB  GLN A 223      -0.955  17.559 -13.662  1.00 47.53           C
ANISOU 3346  CB  GLN A 223     4268   8483   5310    774   -317   1122       C
ATOM   3347  CG  GLN A 223      -0.535  17.710 -15.137  1.00 51.36           C
ANISOU 3347  CG  GLN A 223     4575   9252   5687    859   -306   1186       C
ATOM   3348  CD  GLN A 223      -0.817  19.084 -15.727  1.00 59.95           C
ANISOU 3348  CD  GLN A 223     5555  10365   6857    696   -219   1361       C
ATOM   3349  OE1 GLN A 223      -0.924  20.091 -15.043  1.00 60.52           O
ANISOU 3349  OE1 GLN A 223     5648  10306   7041    533   -184   1430       O
ATOM   3350  NE2 GLN A 223      -1.019  19.171 -17.020  1.00 64.87           N
ANISOU 3350  NE2 GLN A 223     6070  11151   7428    747   -203   1432       N
ATOM   3351  H   GLN A 223      -1.750  15.324 -14.625  1.00 54.27           H
ATOM   3352  HA  GLN A 223       0.562  16.134 -13.227  1.00 54.82           H
ATOM   3353  HB2 GLN A 223      -2.039  17.678 -13.574  1.00 57.04           H
ATOM   3354  HB3 GLN A 223      -0.476  18.356 -13.086  1.00 57.04           H
ATOM   3355  HG2 GLN A 223       0.532  17.506 -15.229  1.00 61.63           H
ATOM   3356  HG3 GLN A 223      -1.073  16.977 -15.731  1.00 61.63           H
ATOM   3357 HE21 GLN A 223      -0.944  18.350 -17.598  1.00 77.85           H
ATOM   3358 HE22 GLN A 223      -1.367  20.059 -17.365  1.00 77.85           H
ATOM   3359  N   PHE A 224      -0.954  14.889 -11.017  1.00 42.71           N
ANISOU 3359  N   PHE A 224     4030   7492   4706    870   -523    883       N
ATOM   3360  CA  PHE A 224      -0.998  14.608  -9.579  1.00 41.97           C
ANISOU 3360  CA  PHE A 224     4043   7250   4652    781   -532    880       C
ATOM   3361  C   PHE A 224       0.284  15.063  -8.863  1.00 47.21           C
ANISOU 3361  C   PHE A 224     4636   8040   5260    760   -505    883       C
ATOM   3362  O   PHE A 224       0.201  15.679  -7.800  1.00 44.66           O
ANISOU 3362  O   PHE A 224     4336   7646   4986    632   -448    913       O
ATOM   3363  CB  PHE A 224      -1.242  13.101  -9.361  1.00 39.28           C
ANISOU 3363  CB  PHE A 224     3842   6781   4300    875   -683    812       C
ATOM   3364  CG  PHE A 224      -1.403  12.697  -7.901  1.00 40.65           C
ANISOU 3364  CG  PHE A 224     4122   6817   4507    776   -701    841       C
ATOM   3365  CD1 PHE A 224      -0.273  12.558  -7.070  1.00 40.24           C
ANISOU 3365  CD1 PHE A 224     4067   6831   4392    799   -721    816       C
ATOM   3366  CD2 PHE A 224      -2.685  12.465  -7.364  1.00 40.10           C
ANISOU 3366  CD2 PHE A 224     4138   6581   4515    662   -702    905       C
ATOM   3367  CE1 PHE A 224      -0.423  12.221  -5.714  1.00 39.58           C
ANISOU 3367  CE1 PHE A 224     4071   6647   4320    714   -740    852       C
ATOM   3368  CE2 PHE A 224      -2.832  12.087  -6.016  1.00 40.53           C
ANISOU 3368  CE2 PHE A 224     4267   6560   4574    571   -718    954       C
ATOM   3369  CZ  PHE A 224      -1.702  11.976  -5.187  1.00 39.40           C
ANISOU 3369  CZ  PHE A 224     4127   6480   4365    600   -736    925       C
ATOM   3370  H   PHE A 224      -0.813  14.105 -11.646  1.00 51.25           H
ATOM   3371  HA  PHE A 224      -1.826  15.165  -9.154  1.00 50.36           H
ATOM   3372  HB2 PHE A 224      -2.137  12.806  -9.910  1.00 47.13           H
ATOM   3373  HB3 PHE A 224      -0.409  12.536  -9.785  1.00 47.13           H
ATOM   3374  HD1 PHE A 224       0.719  12.727  -7.468  1.00 48.29           H
ATOM   3375  HD2 PHE A 224      -3.556  12.573  -7.993  1.00 48.11           H
ATOM   3376  HE1 PHE A 224       0.451  12.147  -5.080  1.00 47.50           H
ATOM   3377  HE2 PHE A 224      -3.813  11.905  -5.607  1.00 48.64           H
ATOM   3378  HZ  PHE A 224      -1.809  11.713  -4.143  1.00 47.28           H
ATOM   3379  N   GLU A 225       1.446  14.823  -9.481  1.00 56.39           N
ANISOU 3379  N   GLU A 225     5703   9414   6310    896   -552    843       N
ATOM   3380  CA  GLU A 225       2.779  15.172  -8.962  1.00 59.32           C
ANISOU 3380  CA  GLU A 225     5994   9931   6614    883   -545    847       C
ATOM   3381  C   GLU A 225       2.961  16.692  -8.796  1.00 56.01           C
ANISOU 3381  C   GLU A 225     5466   9558   6256    704   -439    952       C
ATOM   3382  O   GLU A 225       3.566  17.137  -7.823  1.00 52.68           O
ANISOU 3382  O   GLU A 225     5004   9191   5819    638   -436    963       O
ATOM   3383  CB  GLU A 225       3.850  14.594  -9.915  1.00 65.11           C
ANISOU 3383  CB  GLU A 225     6609  10936   7192   1082   -614    790       C
ATOM   3384  CG  GLU A 225       3.794  13.052 -10.032  1.00 70.13           C
ANISOU 3384  CG  GLU A 225     7356  11518   7771   1299   -761    657       C
ATOM   3385  CD  GLU A 225       4.291  12.491 -11.376  1.00 76.72           C
ANISOU 3385  CD  GLU A 225     8064  12616   8470   1514   -810    592       C
ATOM   3386  OE1 GLU A 225       4.820  11.352 -11.332  1.00 79.09           O
ANISOU 3386  OE1 GLU A 225     8332  13079   8637   1726   -917    481       O
ATOM   3387  OE2 GLU A 225       3.780  12.967 -12.410  1.00 80.68           O
ANISOU 3387  OE2 GLU A 225     8488  13183   8982   1485   -745    647       O
ATOM   3388  H   GLU A 225       1.427  14.331 -10.367  1.00 67.67           H
ATOM   3389  HA  GLU A 225       2.918  14.724  -7.977  1.00 71.18           H
ATOM   3390  HB2 GLU A 225       3.711  15.055 -10.893  1.00 78.13           H
ATOM   3391  HB3 GLU A 225       4.840  14.880  -9.554  1.00 78.13           H
ATOM   3392  HG2 GLU A 225       4.370  12.622  -9.212  1.00 84.15           H
ATOM   3393  HG3 GLU A 225       2.768  12.708  -9.914  1.00 84.15           H
ATOM   3394  N   CYS A 226       2.301  17.490  -9.639  1.00 54.28           N
ANISOU 3394  N   CYS A 226     5204   9307   6115    623   -373   1030       N
ATOM   3395  CA  CYS A 226       2.398  18.951  -9.662  1.00 48.07           C
ANISOU 3395  CA  CYS A 226     4318   8539   5406    458   -311   1141       C
ATOM   3396  C   CYS A 226       1.476  19.652  -8.649  1.00 47.09           C
ANISOU 3396  C   CYS A 226     4304   8164   5424    321   -272   1137       C
ATOM   3397  O   CYS A 226       1.697  20.817  -8.327  1.00 46.99           O
ANISOU 3397  O   CYS A 226     4242   8117   5493    189   -259   1196       O
ATOM   3398  CB  CYS A 226       2.083  19.428 -11.091  1.00 46.57           C
ANISOU 3398  CB  CYS A 226     3998   8484   5213    457   -278   1247       C
ATOM   3399  SG  CYS A 226       3.044  18.494 -12.323  1.00 50.54           S
ANISOU 3399  SG  CYS A 226     4349   9342   5510    667   -321   1230       S
ATOM   3400  H   CYS A 226       1.814  17.051 -10.407  1.00 65.14           H
ATOM   3401  HA  CYS A 226       3.418  19.240  -9.416  1.00 57.68           H
ATOM   3402  HB2 CYS A 226       1.019  19.298 -11.296  1.00 55.89           H
ATOM   3403  HB3 CYS A 226       2.329  20.489 -11.172  1.00 55.89           H
ATOM   3404  HG  CYS A 226       2.786  19.263 -13.387  1.00 60.65           H
ATOM   3405  N   LEU A 227       0.385  19.002  -8.222  1.00 43.81           N
ANISOU 3405  N   LEU A 227     4026   7583   5037    351   -268   1072       N
ATOM   3406  CA  LEU A 227      -0.709  19.631  -7.459  1.00 44.17           C
ANISOU 3406  CA  LEU A 227     4148   7446   5187    254   -223   1064       C
ATOM   3407  C   LEU A 227      -0.813  19.186  -5.996  1.00 44.36           C
ANISOU 3407  C   LEU A 227     4274   7394   5189    241   -236    991       C
ATOM   3408  O   LEU A 227      -1.627  19.754  -5.262  1.00 46.14           O
ANISOU 3408  O   LEU A 227     4542   7518   5473    179   -201    967       O
ATOM   3409  CB  LEU A 227      -2.032  19.408  -8.213  1.00 45.15           C
ANISOU 3409  CB  LEU A 227     4312   7486   5357    278   -193   1082       C
ATOM   3410  CG  LEU A 227      -2.133  20.254  -9.495  1.00 46.54           C
ANISOU 3410  CG  LEU A 227     4385   7723   5576    264   -166   1169       C
ATOM   3411  CD1 LEU A 227      -3.251  19.722 -10.380  1.00 45.27           C
ANISOU 3411  CD1 LEU A 227     4248   7536   5418    328   -157   1175       C
ATOM   3412  CD2 LEU A 227      -2.468  21.717  -9.184  1.00 44.89           C
ANISOU 3412  CD2 LEU A 227     4155   7413   5489    148   -137   1214       C
ATOM   3413  H   LEU A 227       0.241  18.069  -8.590  1.00 52.57           H
ATOM   3414  HA  LEU A 227      -0.528  20.705  -7.408  1.00 53.00           H
ATOM   3415  HB2 LEU A 227      -2.106  18.349  -8.465  1.00 54.18           H
ATOM   3416  HB3 LEU A 227      -2.876  19.655  -7.567  1.00 54.18           H
ATOM   3417  HG  LEU A 227      -1.200  20.205 -10.055  1.00 55.85           H
ATOM   3418 HD11 LEU A 227      -3.074  18.668 -10.598  1.00  0.00           H
ATOM   3419 HD12 LEU A 227      -4.211  19.844  -9.885  1.00  0.00           H
ATOM   3420 HD13 LEU A 227      -3.242  20.271 -11.319  1.00  0.00           H
ATOM   3421 HD21 LEU A 227      -1.655  22.173  -8.622  1.00  0.00           H
ATOM   3422 HD22 LEU A 227      -3.389  21.783  -8.609  1.00  0.00           H
ATOM   3423 HD23 LEU A 227      -2.587  22.265 -10.119  1.00  0.00           H
ATOM   3424  N   TYR A 228       0.007  18.231  -5.552  1.00 38.84           N
ANISOU 3424  N   TYR A 228     3607   6755   4396    312   -293    953       N
ATOM   3425  CA  TYR A 228       0.257  17.921  -4.135  1.00 40.57           C
ANISOU 3425  CA  TYR A 228     3895   6946   4573    293   -314    905       C
ATOM   3426  C   TYR A 228      -1.010  17.869  -3.249  1.00 46.35           C
ANISOU 3426  C   TYR A 228     4707   7569   5335    245   -275    900       C
ATOM   3427  O   TYR A 228      -1.144  18.691  -2.332  1.00 44.59           O
ANISOU 3427  O   TYR A 228     4482   7326   5133    187   -240    863       O
ATOM   3428  CB  TYR A 228       1.294  18.913  -3.582  1.00 45.38           C
ANISOU 3428  CB  TYR A 228     4441   7613   5188    227   -314    884       C
ATOM   3429  CG  TYR A 228       2.618  18.908  -4.322  1.00 43.10           C
ANISOU 3429  CG  TYR A 228     4041   7487   4849    259   -351    913       C
ATOM   3430  CD1 TYR A 228       3.636  18.020  -3.929  1.00 41.35           C
ANISOU 3430  CD1 TYR A 228     3815   7377   4519    341   -411    877       C
ATOM   3431  CD2 TYR A 228       2.839  19.808  -5.381  1.00 46.18           C
ANISOU 3431  CD2 TYR A 228     4314   7942   5289    209   -332    990       C
ATOM   3432  CE1 TYR A 228       4.878  18.034  -4.589  1.00 41.67           C
ANISOU 3432  CE1 TYR A 228     3727   7617   4490    387   -442    902       C
ATOM   3433  CE2 TYR A 228       4.076  19.822  -6.048  1.00 47.23           C
ANISOU 3433  CE2 TYR A 228     4310   8284   5350    233   -362   1040       C
ATOM   3434  CZ  TYR A 228       5.099  18.929  -5.658  1.00 46.94           C
ANISOU 3434  CZ  TYR A 228     4260   8382   5192    328   -412    989       C
ATOM   3435  OH  TYR A 228       6.300  18.965  -6.290  1.00 47.50           O
ANISOU 3435  OH  TYR A 228     4170   8708   5169    367   -438   1038       O
ATOM   3436  H   TYR A 228       0.674  17.863  -6.222  1.00 46.61           H
ATOM   3437  HA  TYR A 228       0.709  16.930  -4.094  1.00 48.68           H
ATOM   3438  HB2 TYR A 228       0.881  19.922  -3.609  1.00 54.46           H
ATOM   3439  HB3 TYR A 228       1.492  18.673  -2.536  1.00 54.46           H
ATOM   3440  HD1 TYR A 228       3.472  17.334  -3.111  1.00 49.62           H
ATOM   3441  HD2 TYR A 228       2.065  20.502  -5.686  1.00 55.41           H
ATOM   3442  HE1 TYR A 228       5.672  17.374  -4.277  1.00 50.01           H
ATOM   3443  HE2 TYR A 228       4.248  20.510  -6.860  1.00 56.67           H
ATOM   3444  HH  TYR A 228       6.644  18.078  -6.447  1.00 57.00           H
ATOM   3445  N   PRO A 229      -1.976  16.956  -3.490  1.00 43.22           N
ANISOU 3445  N   PRO A 229     4372   7118   4933    270   -293    934       N
ATOM   3446  CA  PRO A 229      -3.157  16.854  -2.634  1.00 45.51           C
ANISOU 3446  CA  PRO A 229     4708   7361   5224    216   -257    956       C
ATOM   3447  C   PRO A 229      -2.783  16.671  -1.157  1.00 43.94           C
ANISOU 3447  C   PRO A 229     4545   7210   4941    198   -278    942       C
ATOM   3448  O   PRO A 229      -1.794  16.013  -0.832  1.00 45.40           O
ANISOU 3448  O   PRO A 229     4752   7428   5070    236   -346    930       O
ATOM   3449  CB  PRO A 229      -3.988  15.670  -3.140  1.00 46.01           C
ANISOU 3449  CB  PRO A 229     4821   7362   5300    232   -310   1021       C
ATOM   3450  CG  PRO A 229      -3.029  14.889  -4.038  1.00 40.89           C
ANISOU 3450  CG  PRO A 229     4188   6720   4629    326   -406    998       C
ATOM   3451  CD  PRO A 229      -1.957  15.889  -4.480  1.00 39.75           C
ANISOU 3451  CD  PRO A 229     3953   6668   4483    352   -363    953       C
ATOM   3452  HA  PRO A 229      -3.730  17.768  -2.747  1.00 54.62           H
ATOM   3453  HB2 PRO A 229      -4.344  15.044  -2.319  1.00 55.22           H
ATOM   3454  HB3 PRO A 229      -4.842  16.030  -3.713  1.00 55.22           H
ATOM   3455  HG2 PRO A 229      -2.561  14.097  -3.453  1.00 49.07           H
ATOM   3456  HG3 PRO A 229      -3.556  14.472  -4.896  1.00 49.07           H
ATOM   3457  HD2 PRO A 229      -0.985  15.395  -4.518  1.00 47.70           H
ATOM   3458  HD3 PRO A 229      -2.200  16.290  -5.465  1.00 47.70           H
ATOM   3459  N   TYR A 230      -3.647  17.126  -0.249  1.00 45.94           N
ANISOU 3459  N   TYR A 230     4793   7492   5170    153   -220    940       N
ATOM   3460  CA  TYR A 230      -3.555  16.726   1.159  1.00 45.78           C
ANISOU 3460  CA  TYR A 230     4792   7557   5045    139   -233    941       C
ATOM   3461  C   TYR A 230      -3.666  15.187   1.320  1.00 44.03           C
ANISOU 3461  C   TYR A 230     4634   7317   4777    128   -322   1052       C
ATOM   3462  O   TYR A 230      -4.500  14.594   0.627  1.00 44.12           O
ANISOU 3462  O   TYR A 230     4679   7240   4846    128   -373   1116       O
ATOM   3463  CB  TYR A 230      -4.669  17.392   1.964  1.00 45.09           C
ANISOU 3463  CB  TYR A 230     4667   7553   4914    116   -156    926       C
ATOM   3464  CG  TYR A 230      -4.546  18.898   2.156  1.00 48.37           C
ANISOU 3464  CG  TYR A 230     5040   7970   5367    146   -110    788       C
ATOM   3465  CD1 TYR A 230      -5.190  19.779   1.269  1.00 46.08           C
ANISOU 3465  CD1 TYR A 230     4726   7593   5190    154    -75    760       C
ATOM   3466  CD2 TYR A 230      -3.835  19.409   3.258  1.00 51.75           C
ANISOU 3466  CD2 TYR A 230     5460   8475   5726    169   -123    684       C
ATOM   3467  CE1 TYR A 230      -5.149  21.163   1.486  1.00 48.43           C
ANISOU 3467  CE1 TYR A 230     5002   7853   5546    180    -71    638       C
ATOM   3468  CE2 TYR A 230      -3.797  20.792   3.494  1.00 49.76           C
ANISOU 3468  CE2 TYR A 230     5187   8190   5529    198   -121    545       C
ATOM   3469  CZ  TYR A 230      -4.449  21.678   2.609  1.00 49.55           C
ANISOU 3469  CZ  TYR A 230     5147   8049   5631    202   -103    525       C
ATOM   3470  OH  TYR A 230      -4.424  23.009   2.834  1.00 50.77           O
ANISOU 3470  OH  TYR A 230     5296   8131   5863    231   -138    391       O
ATOM   3471  H   TYR A 230      -4.440  17.671  -0.567  1.00 55.13           H
ATOM   3472  HA  TYR A 230      -2.589  17.062   1.534  1.00 54.94           H
ATOM   3473  HB2 TYR A 230      -5.625  17.168   1.495  1.00 54.11           H
ATOM   3474  HB3 TYR A 230      -4.684  16.944   2.952  1.00 54.11           H
ATOM   3475  HD1 TYR A 230      -5.720  19.392   0.406  1.00 55.30           H
ATOM   3476  HD2 TYR A 230      -3.300  18.738   3.918  1.00 62.10           H
ATOM   3477  HE1 TYR A 230      -5.611  21.851   0.795  1.00 58.11           H
ATOM   3478  HE2 TYR A 230      -3.249  21.200   4.326  1.00 59.71           H
ATOM   3479  HH  TYR A 230      -3.527  23.355   2.901  1.00 60.92           H
ATOM   3480  N   PRO A 231      -3.084  14.591   2.388  1.00 43.18           N
ANISOU 3480  N   PRO A 231     4550   7284   4572    121   -363   1076       N
ATOM   3481  CA  PRO A 231      -3.238  13.165   2.730  1.00 48.46           C
ANISOU 3481  CA  PRO A 231     5285   7919   5208     90   -470   1212       C
ATOM   3482  C   PRO A 231      -4.718  12.726   2.756  1.00 45.19           C
ANISOU 3482  C   PRO A 231     4861   7497   4811      4   -458   1343       C
ATOM   3483  O   PRO A 231      -5.519  13.419   3.385  1.00 47.82           O
ANISOU 3483  O   PRO A 231     5120   7925   5124    -25   -347   1330       O
ATOM   3484  CB  PRO A 231      -2.609  13.021   4.128  1.00 47.08           C
ANISOU 3484  CB  PRO A 231     5107   7873   4909     81   -483   1225       C
ATOM   3485  CG  PRO A 231      -1.614  14.177   4.236  1.00 46.06           C
ANISOU 3485  CG  PRO A 231     4934   7799   4768    139   -427   1062       C
ATOM   3486  CD  PRO A 231      -2.240  15.266   3.370  1.00 44.78           C
ANISOU 3486  CD  PRO A 231     4722   7595   4696    138   -336    984       C
ATOM   3487  HA  PRO A 231      -2.676  12.559   2.015  1.00 58.15           H
ATOM   3488  HB2 PRO A 231      -3.371  13.157   4.898  1.00 56.50           H
ATOM   3489  HB3 PRO A 231      -2.115  12.058   4.261  1.00 56.50           H
ATOM   3490  HG2 PRO A 231      -1.499  14.513   5.270  1.00 55.27           H
ATOM   3491  HG3 PRO A 231      -0.648  13.883   3.823  1.00 55.27           H
ATOM   3492  HD2 PRO A 231      -2.858  15.912   3.994  1.00 53.73           H
ATOM   3493  HD3 PRO A 231      -1.450  15.853   2.895  1.00 53.73           H
ATOM   3494  N   VAL A 232      -5.081  11.503   2.348  1.00 43.48           N
ANISOU 3494  N   VAL A 232     4717   7167   4636    -34   -592   1470       N
ATOM   3495  CA  VAL A 232      -6.493  11.042   2.254  1.00 47.77           C
ANISOU 3495  CA  VAL A 232     5246   7694   5209   -142   -609   1621       C
ATOM   3496  C   VAL A 232      -7.277  11.160   3.569  1.00 52.94           C
ANISOU 3496  C   VAL A 232     5814   8563   5738   -234   -530   1734       C
ATOM   3497  O   VAL A 232      -8.489  11.405   3.581  1.00 56.16           O
ANISOU 3497  O   VAL A 232     6137   9070   6130   -293   -447   1791       O
ATOM   3498  CB  VAL A 232      -6.555   9.581   1.754  1.00 52.13           C
ANISOU 3498  CB  VAL A 232     5909   8058   5840   -175   -817   1741       C
ATOM   3499  CG1 VAL A 232      -7.932   8.919   1.906  1.00 57.80           C
ANISOU 3499  CG1 VAL A 232     6604   8777   6581   -333   -864   1947       C
ATOM   3500  CG2 VAL A 232      -6.242   9.519   0.269  1.00 43.05           C
ANISOU 3500  CG2 VAL A 232     4817   6745   4796    -59   -882   1609       C
ATOM   3501  H   VAL A 232      -4.363  10.929   1.889  1.00 52.18           H
ATOM   3502  HA  VAL A 232      -6.997  11.670   1.522  1.00 57.32           H
ATOM   3503  HB  VAL A 232      -5.828   8.978   2.300  1.00 62.55           H
ATOM   3504 HG11 VAL A 232      -7.933   7.984   1.357  1.00 69.36           H
ATOM   3505 HG12 VAL A 232      -8.132   8.705   2.954  1.00 69.36           H
ATOM   3506 HG13 VAL A 232      -8.707   9.564   1.492  1.00 69.36           H
ATOM   3507 HG21 VAL A 232      -6.185   8.483  -0.055  1.00 51.66           H
ATOM   3508 HG22 VAL A 232      -6.979  10.061  -0.303  1.00 51.66           H
ATOM   3509 HG23 VAL A 232      -5.293  10.005   0.084  1.00 51.66           H
ATOM   3510  N   HIS A 233      -6.596  10.982   4.704  1.00 51.66           N
ANISOU 3510  N   HIS A 233     5656   8505   5466   -236   -555   1767       N
ATOM   3511  CA  HIS A 233      -7.175  11.094   6.051  1.00 53.11           C
ANISOU 3511  CA  HIS A 233     5740   8945   5493   -307   -485   1879       C
ATOM   3512  C   HIS A 233      -7.332  12.540   6.562  1.00 51.18           C
ANISOU 3512  C   HIS A 233     5396   8892   5158   -221   -317   1698       C
ATOM   3513  O   HIS A 233      -7.941  12.724   7.614  1.00 50.38           O
ANISOU 3513  O   HIS A 233     5190   9050   4904   -243   -245   1753       O
ATOM   3514  CB  HIS A 233      -6.328  10.255   7.015  1.00 58.04           C
ANISOU 3514  CB  HIS A 233     6406   9623   6024   -337   -588   1992       C
ATOM   3515  CG  HIS A 233      -6.328   8.771   6.716  1.00 64.42           C
ANISOU 3515  CG  HIS A 233     7317  10239   6920   -430   -789   2195       C
ATOM   3516  ND1 HIS A 233      -7.341   7.858   6.985  1.00 64.64           N
ANISOU 3516  ND1 HIS A 233     7481  10032   7049   -351   -941   2132       N
ATOM   3517  CD2 HIS A 233      -5.297   8.085   6.136  1.00 64.36           C
ANISOU 3517  CD2 HIS A 233     7296  10236   6923   -592   -887   2460       C
ATOM   3518  CE1 HIS A 233      -6.934   6.643   6.557  1.00 63.99           C
ANISOU 3518  CE1 HIS A 233     7484   9785   7045   -446  -1138   2330       C
ATOM   3519  NE2 HIS A 233      -5.695   6.767   6.045  1.00 65.01           N
ANISOU 3519  NE2 HIS A 233     7526  10045   7130   -612  -1114   2545       N
ATOM   3520  H   HIS A 233      -5.603  10.815   4.599  1.00 61.99           H
ATOM   3521  HA  HIS A 233      -8.182  10.678   6.032  1.00 63.73           H
ATOM   3522  HB2 HIS A 233      -5.296  10.613   6.989  1.00 69.65           H
ATOM   3523  HB3 HIS A 233      -6.700  10.404   8.031  1.00 69.65           H
ATOM   3524  HD1 HIS A 233      -8.181   8.038   7.524  1.00 77.57           H
ATOM   3525  HD2 HIS A 233      -4.339   8.488   5.819  1.00 77.23           H
ATOM   3526  HE1 HIS A 233      -7.478   5.700   6.649  1.00 76.79           H
ATOM   3527  HE2 HIS A 233      -5.135   6.009   5.630  1.00  0.00           H
ATOM   3528  N   HIS A 234      -6.754  13.533   5.879  1.00 52.31           N
ANISOU 3528  N   HIS A 234     5564   8925   5387   -119   -270   1488       N
ATOM   3529  CA  HIS A 234      -6.845  14.972   6.170  1.00 53.69           C
ANISOU 3529  CA  HIS A 234     5664   9223   5510    -36   -153   1306       C
ATOM   3530  C   HIS A 234      -8.281  15.482   5.906  1.00 49.79           C
ANISOU 3530  C   HIS A 234     5091   8797   5031    -41    -66   1314       C
ATOM   3531  O   HIS A 234      -8.868  15.050   4.914  1.00 49.42           O
ANISOU 3531  O   HIS A 234     5065   8615   5098    -88    -85   1389       O
ATOM   3532  CB  HIS A 234      -5.780  15.697   5.308  1.00 54.24           C
ANISOU 3532  CB  HIS A 234     5783   9135   5691     42   -159   1120       C
ATOM   3533  CG  HIS A 234      -5.527  17.129   5.711  1.00 53.10           C
ANISOU 3533  CG  HIS A 234     5591   9079   5507    120    -97    929       C
ATOM   3534  ND1 HIS A 234      -6.115  18.250   5.154  1.00 50.67           N
ANISOU 3534  ND1 HIS A 234     5235   8773   5243    166    -30    828       N
ATOM   3535  CD2 HIS A 234      -4.804  17.538   6.801  1.00 54.87           C
ANISOU 3535  CD2 HIS A 234     5814   9376   5657    166   -117    811       C
ATOM   3536  CE1 HIS A 234      -5.803  19.313   5.923  1.00 52.15           C
ANISOU 3536  CE1 HIS A 234     5405   9012   5396    242    -26    648       C
ATOM   3537  NE2 HIS A 234      -5.013  18.898   6.944  1.00 54.80           N
ANISOU 3537  NE2 HIS A 234     5766   9396   5660    238    -77    634       N
ATOM   3538  H   HIS A 234      -6.337  13.288   4.986  1.00 62.77           H
ATOM   3539  HA  HIS A 234      -6.600  15.136   7.217  1.00 64.42           H
ATOM   3540  HB2 HIS A 234      -4.833  15.154   5.371  1.00 65.09           H
ATOM   3541  HB3 HIS A 234      -6.097  15.674   4.260  1.00 65.09           H
ATOM   3542  HD2 HIS A 234      -4.234  16.893   7.461  1.00 65.84           H
ATOM   3543  HE1 HIS A 234      -6.110  20.339   5.742  1.00 62.58           H
ATOM   3544  HE2 HIS A 234      -4.674  19.486   7.713  1.00 65.76           H
ATOM   3545  HD1 HIS A 234      -6.558  18.283   4.234  1.00  0.00           H
ATOM   3546  N   PRO A 235      -8.812  16.480   6.644  1.00 54.03           N
ANISOU 3546  N   PRO A 235     5530   9553   5446     23     22   1225       N
ATOM   3547  CA  PRO A 235     -10.125  17.077   6.343  1.00 52.57           C
ANISOU 3547  CA  PRO A 235     5256   9458   5260     43    102   1222       C
ATOM   3548  C   PRO A 235     -10.225  17.629   4.923  1.00 51.31           C
ANISOU 3548  C   PRO A 235     5143   9061   5291     70    109   1138       C
ATOM   3549  O   PRO A 235     -11.153  17.285   4.192  1.00 50.38           O
ANISOU 3549  O   PRO A 235     4978   8955   5211     42    143   1212       O
ATOM   3550  CB  PRO A 235     -10.339  18.163   7.405  1.00 55.85           C
ANISOU 3550  CB  PRO A 235     5582  10115   5523    174    169   1048       C
ATOM   3551  CG  PRO A 235      -9.534  17.641   8.592  1.00 56.18           C
ANISOU 3551  CG  PRO A 235     5628  10297   5421    164    133   1075       C
ATOM   3552  CD  PRO A 235      -8.341  16.938   7.944  1.00 56.26           C
ANISOU 3552  CD  PRO A 235     5769  10042   5564     95     41   1121       C
ATOM   3553  HA  PRO A 235     -10.892  16.318   6.469  1.00 63.08           H
ATOM   3554  HB2 PRO A 235      -9.923  19.114   7.073  1.00 67.02           H
ATOM   3555  HB3 PRO A 235     -11.396  18.273   7.657  1.00 67.02           H
ATOM   3556  HG2 PRO A 235      -9.222  18.444   9.261  1.00 67.42           H
ATOM   3557  HG3 PRO A 235     -10.134  16.910   9.128  1.00 67.42           H
ATOM   3558  HD2 PRO A 235      -7.521  17.644   7.816  1.00 67.51           H
ATOM   3559  HD3 PRO A 235      -8.031  16.099   8.571  1.00 67.51           H
ATOM   3560  N   CYS A 236      -9.162  18.272   4.454  1.00 54.87           N
ANISOU 3560  N   CYS A 236     5674   9318   5857    115     75   1003       N
ATOM   3561  CA  CYS A 236      -9.035  18.801   3.091  1.00 48.86           C
ANISOU 3561  CA  CYS A 236     4945   8355   5265    133     77    948       C
ATOM   3562  C   CYS A 236      -8.654  17.767   1.994  1.00 45.50           C
ANISOU 3562  C   CYS A 236     4584   7767   4936     65     12   1067       C
ATOM   3563  O   CYS A 236      -8.069  18.171   0.995  1.00 43.18           O
ANISOU 3563  O   CYS A 236     4323   7323   4759     87     -7   1016       O
ATOM   3564  CB  CYS A 236      -8.077  20.012   3.120  1.00 46.84           C
ANISOU 3564  CB  CYS A 236     4716   8001   5079    203     60    767       C
ATOM   3565  SG  CYS A 236      -8.454  21.103   4.520  1.00 55.36           S
ANISOU 3565  SG  CYS A 236     5738   9231   6065    323     93    573       S
ATOM   3566  H   CYS A 236      -8.571  18.699   5.157  1.00 65.85           H
ATOM   3567  HA  CYS A 236     -10.022  19.165   2.820  1.00 58.63           H
ATOM   3568  HB2 CYS A 236      -7.043  19.680   3.177  1.00 56.20           H
ATOM   3569  HB3 CYS A 236      -8.153  20.580   2.187  1.00 56.20           H
ATOM   3570  HG  CYS A 236      -9.619  21.588   4.045  1.00 66.43           H
ATOM   3571  N   ASP A 237      -8.886  16.460   2.190  1.00 50.99           N
ANISOU 3571  N   ASP A 237     5295   8498   5581    -14    -39   1227       N
ATOM   3572  CA  ASP A 237      -8.691  15.400   1.167  1.00 49.58           C
ANISOU 3572  CA  ASP A 237     5190   8155   5493    -56   -135   1319       C
ATOM   3573  C   ASP A 237      -9.178  15.831  -0.238  1.00 45.83           C
ANISOU 3573  C   ASP A 237     4705   7572   5137    -35   -112   1290       C
ATOM   3574  O   ASP A 237     -10.211  16.490  -0.375  1.00 44.16           O
ANISOU 3574  O   ASP A 237     4425   7423   4930    -40    -39   1299       O
ATOM   3575  CB  ASP A 237      -9.427  14.125   1.634  1.00 48.25           C
ANISOU 3575  CB  ASP A 237     5030   8028   5276   -164   -211   1515       C
ATOM   3576  CG  ASP A 237      -9.414  12.948   0.638  1.00 50.84           C
ANISOU 3576  CG  ASP A 237     5448   8157   5711   -195   -351   1592       C
ATOM   3577  OD1 ASP A 237      -8.462  12.800  -0.149  1.00 51.28           O
ANISOU 3577  OD1 ASP A 237     5571   8085   5827   -113   -405   1492       O
ATOM   3578  OD2 ASP A 237     -10.322  12.082   0.704  1.00 51.31           O
ANISOU 3578  OD2 ASP A 237     5506   8202   5790   -298   -421   1751       O
ATOM   3579  H   ASP A 237      -9.371  16.188   3.036  1.00 61.19           H
ATOM   3580  HA  ASP A 237      -7.624  15.167   1.102  1.00 59.50           H
ATOM   3581  HB2 ASP A 237      -8.972  13.793   2.566  1.00 57.90           H
ATOM   3582  HB3 ASP A 237     -10.464  14.386   1.853  1.00 57.90           H
ATOM   3583  N   ARG A 238      -8.467  15.408  -1.289  1.00 46.63           N
ANISOU 3583  N   ARG A 238     4863   7536   5320      4   -174   1254       N
ATOM   3584  CA  ARG A 238      -8.688  15.733  -2.718  1.00 45.33           C
ANISOU 3584  CA  ARG A 238     4691   7280   5254     33   -173   1237       C
ATOM   3585  C   ARG A 238      -8.508  17.199  -3.142  1.00 42.88           C
ANISOU 3585  C   ARG A 238     4329   6971   4991     85    -87   1133       C
ATOM   3586  O   ARG A 238      -8.516  17.452  -4.346  1.00 40.50           O
ANISOU 3586  O   ARG A 238     4010   6613   4763    112    -83   1127       O
ATOM   3587  CB  ARG A 238     -10.034  15.191  -3.244  1.00 47.79           C
ANISOU 3587  CB  ARG A 238     4974   7591   5592    -27   -171   1336       C
ATOM   3588  CG  ARG A 238     -10.510  13.852  -2.660  1.00 54.45           C
ANISOU 3588  CG  ARG A 238     5851   8441   6396   -123   -267   1480       C
ATOM   3589  CD  ARG A 238     -11.432  13.101  -3.627  1.00 54.25           C
ANISOU 3589  CD  ARG A 238     5854   8307   6450   -169   -368   1564       C
ATOM   3590  NE  ARG A 238     -12.575  13.925  -4.063  1.00 56.83           N
ANISOU 3590  NE  ARG A 238     6096   8687   6808   -184   -279   1576       N
ATOM   3591  CZ  ARG A 238     -13.764  13.975  -3.495  1.00 61.36           C
ANISOU 3591  CZ  ARG A 238     6586   9392   7337   -271   -230   1684       C
ATOM   3592  NH1 ARG A 238     -14.091  13.263  -2.469  1.00 63.74           N
ANISOU 3592  NH1 ARG A 238     6866   9800   7551   -365   -255   1807       N
ATOM   3593  NH2 ARG A 238     -14.697  14.747  -3.943  1.00 60.08           N
ANISOU 3593  NH2 ARG A 238     6345   9281   7203   -262   -154   1679       N
ATOM   3594  H   ARG A 238      -7.728  14.742  -1.077  1.00 55.96           H
ATOM   3595  HA  ARG A 238      -7.913  15.206  -3.273  1.00 54.40           H
ATOM   3596  HB2 ARG A 238     -10.814  15.933  -3.058  1.00 57.34           H
ATOM   3597  HB3 ARG A 238      -9.936  15.083  -4.326  1.00 57.34           H
ATOM   3598  HG2 ARG A 238      -9.648  13.221  -2.458  1.00 65.34           H
ATOM   3599  HG3 ARG A 238     -11.036  14.035  -1.721  1.00 65.34           H
ATOM   3600  HD2 ARG A 238     -10.850  12.812  -4.501  1.00 65.09           H
ATOM   3601  HD3 ARG A 238     -11.781  12.182  -3.155  1.00 65.09           H
ATOM   3602  HE  ARG A 238     -12.391  14.570  -4.834  1.00 68.19           H
ATOM   3603 HH11 ARG A 238     -13.386  12.668  -2.082  1.00 76.49           H
ATOM   3604 HH12 ARG A 238     -14.984  13.418  -2.052  1.00 76.49           H
ATOM   3605 HH21 ARG A 238     -14.442  15.431  -4.656  1.00 72.10           H
ATOM   3606 HH22 ARG A 238     -15.606  14.833  -3.529  1.00 72.10           H
ATOM   3607  N   GLN A 239      -8.339  18.152  -2.221  1.00 44.48           N
ANISOU 3607  N   GLN A 239     4509   7232   5158     99    -38   1055       N
ATOM   3608  CA  GLN A 239      -7.898  19.526  -2.528  1.00 43.96           C
ANISOU 3608  CA  GLN A 239     4411   7129   5163    135     -1    964       C
ATOM   3609  C   GLN A 239      -6.363  19.585  -2.631  1.00 47.52           C
ANISOU 3609  C   GLN A 239     4876   7555   5626    142    -48    920       C
ATOM   3610  O   GLN A 239      -5.674  18.814  -1.962  1.00 42.80           O
ANISOU 3610  O   GLN A 239     4309   6999   4955    140    -89    917       O
ATOM   3611  CB  GLN A 239      -8.448  20.536  -1.491  1.00 48.64           C
ANISOU 3611  CB  GLN A 239     4974   7787   5722    163     49    879       C
ATOM   3612  CG  GLN A 239      -9.993  20.539  -1.413  1.00 53.39           C
ANISOU 3612  CG  GLN A 239     5527   8461   6296    171    106    917       C
ATOM   3613  CD  GLN A 239     -10.571  21.350  -0.261  1.00 57.06           C
ANISOU 3613  CD  GLN A 239     5949   9035   6696    242    146    805       C
ATOM   3614  OE1 GLN A 239     -11.359  22.270  -0.434  1.00 64.05           O
ANISOU 3614  OE1 GLN A 239     6811   9878   7649    308    163    723       O
ATOM   3615  NE2 GLN A 239     -10.382  20.887   0.944  1.00 56.32           N
ANISOU 3615  NE2 GLN A 239     5842   9091   6464    243    151    795       N
ATOM   3616  H   GLN A 239      -8.320  17.866  -1.251  1.00 53.37           H
ATOM   3617  HA  GLN A 239      -8.288  19.815  -3.501  1.00 52.75           H
ATOM   3618  HB2 GLN A 239      -8.028  20.300  -0.514  1.00 58.37           H
ATOM   3619  HB3 GLN A 239      -8.112  21.540  -1.761  1.00 58.37           H
ATOM   3620  HG2 GLN A 239     -10.407  20.922  -2.342  1.00 64.06           H
ATOM   3621  HG3 GLN A 239     -10.343  19.516  -1.274  1.00 64.06           H
ATOM   3622 HE21 GLN A 239      -9.808  20.074   1.057  1.00 67.58           H
ATOM   3623 HE22 GLN A 239     -10.912  21.292   1.710  1.00 67.58           H
ATOM   3624  N   SER A 240      -5.837  20.474  -3.478  1.00 48.02           N
ANISOU 3624  N   SER A 240     4904   7561   5779    145    -48    904       N
ATOM   3625  CA  SER A 240      -4.408  20.807  -3.569  1.00 47.17           C
ANISOU 3625  CA  SER A 240     4777   7463   5683    133    -94    889       C
ATOM   3626  C   SER A 240      -3.929  21.517  -2.295  1.00 42.93           C
ANISOU 3626  C   SER A 240     4248   6926   5135    116   -113    796       C
ATOM   3627  O   SER A 240      -4.708  22.234  -1.663  1.00 41.11           O
ANISOU 3627  O   SER A 240     4025   6659   4937    128    -96    725       O
ATOM   3628  CB  SER A 240      -4.172  21.696  -4.800  1.00 46.62           C
ANISOU 3628  CB  SER A 240     4646   7357   5709    115    -97    941       C
ATOM   3629  OG  SER A 240      -2.821  22.087  -4.898  1.00 47.50           O
ANISOU 3629  OG  SER A 240     4711   7511   5828     81   -144    952       O
ATOM   3630  H   SER A 240      -6.472  21.076  -3.991  1.00 57.62           H
ATOM   3631  HA  SER A 240      -3.827  19.894  -3.698  1.00 56.61           H
ATOM   3632  HB2 SER A 240      -4.450  21.153  -5.706  1.00 55.94           H
ATOM   3633  HB3 SER A 240      -4.792  22.591  -4.726  1.00 55.94           H
ATOM   3634  HG  SER A 240      -2.293  21.307  -5.163  1.00 57.00           H
ATOM   3635  N   GLN A 241      -2.675  21.293  -1.892  1.00 41.94           N
ANISOU 3635  N   GLN A 241     4121   6856   4959    106   -159    783       N
ATOM   3636  CA  GLN A 241      -2.005  22.085  -0.849  1.00 43.54           C
ANISOU 3636  CA  GLN A 241     4325   7061   5156     85   -197    690       C
ATOM   3637  C   GLN A 241      -1.399  23.402  -1.361  1.00 44.43           C
ANISOU 3637  C   GLN A 241     4392   7093   5395     24   -249    686       C
ATOM   3638  O   GLN A 241      -0.958  24.203  -0.538  1.00 45.32           O
ANISOU 3638  O   GLN A 241     4516   7161   5541      2   -306    592       O
ATOM   3639  CB  GLN A 241      -0.881  21.256  -0.215  1.00 44.54           C
ANISOU 3639  CB  GLN A 241     4458   7286   5178     92   -236    685       C
ATOM   3640  CG  GLN A 241      -1.402  20.094   0.631  1.00 45.78           C
ANISOU 3640  CG  GLN A 241     4670   7508   5217    132   -220    698       C
ATOM   3641  CD  GLN A 241      -0.255  19.222   1.115  1.00 44.09           C
ANISOU 3641  CD  GLN A 241     4467   7375   4910    150   -276    699       C
ATOM   3642  OE1 GLN A 241       0.208  19.328   2.243  1.00 45.97           O
ANISOU 3642  OE1 GLN A 241     4711   7670   5083    147   -295    633       O
ATOM   3643  NE2 GLN A 241       0.260  18.361   0.270  1.00 46.42           N
ANISOU 3643  NE2 GLN A 241     4762   7686   5190    187   -312    760       N
ATOM   3644  H   GLN A 241      -2.105  20.641  -2.418  1.00 50.33           H
ATOM   3645  HA  GLN A 241      -2.726  22.353  -0.075  1.00 52.24           H
ATOM   3646  HB2 GLN A 241      -0.225  20.884  -1.005  1.00 53.44           H
ATOM   3647  HB3 GLN A 241      -0.290  21.895   0.441  1.00 53.44           H
ATOM   3648  HG2 GLN A 241      -1.931  20.496   1.491  1.00 54.94           H
ATOM   3649  HG3 GLN A 241      -2.091  19.486   0.048  1.00 54.94           H
ATOM   3650 HE21 GLN A 241      -0.131  18.298  -0.666  1.00 55.71           H
ATOM   3651 HE22 GLN A 241       1.049  17.815   0.559  1.00 55.71           H
ATOM   3652  N   VAL A 242      -1.261  23.565  -2.680  1.00 44.03           N
ANISOU 3652  N   VAL A 242     4287   7029   5413     -7   -246    792       N
ATOM   3653  CA  VAL A 242      -0.628  24.740  -3.288  1.00 46.60           C
ANISOU 3653  CA  VAL A 242     4550   7300   5858    -96   -312    846       C
ATOM   3654  C   VAL A 242      -1.573  25.934  -3.179  1.00 47.58           C
ANISOU 3654  C   VAL A 242     4711   7252   6115   -107   -340    797       C
ATOM   3655  O   VAL A 242      -2.701  25.875  -3.678  1.00 48.69           O
ANISOU 3655  O   VAL A 242     4874   7353   6273    -53   -282    804       O
ATOM   3656  CB  VAL A 242      -0.247  24.488  -4.762  1.00 46.13           C
ANISOU 3656  CB  VAL A 242     4397   7335   5797   -118   -296    996       C
ATOM   3657  CG1 VAL A 242       0.522  25.686  -5.327  1.00 43.63           C
ANISOU 3657  CG1 VAL A 242     3992   6989   5597   -240   -372   1101       C
ATOM   3658  CG2 VAL A 242       0.633  23.242  -4.931  1.00 42.43           C
ANISOU 3658  CG2 VAL A 242     3894   7043   5183    -61   -285   1011       C
ATOM   3659  H   VAL A 242      -1.712  22.913  -3.306  1.00 52.83           H
ATOM   3660  HA  VAL A 242       0.287  24.968  -2.739  1.00 55.93           H
ATOM   3661  HB  VAL A 242      -1.151  24.345  -5.355  1.00 55.36           H
ATOM   3662 HG11 VAL A 242       0.825  25.472  -6.346  1.00 52.36           H
ATOM   3663 HG12 VAL A 242      -0.106  26.575  -5.353  1.00 52.36           H
ATOM   3664 HG13 VAL A 242       1.412  25.884  -4.730  1.00 52.36           H
ATOM   3665 HG21 VAL A 242       0.913  23.125  -5.978  1.00 50.91           H
ATOM   3666 HG22 VAL A 242       1.536  23.354  -4.336  1.00 50.91           H
ATOM   3667 HG23 VAL A 242       0.101  22.347  -4.615  1.00 50.91           H
ATOM   3668  N   ASP A 243      -1.107  27.035  -2.590  1.00 52.26           N
ANISOU 3668  N   ASP A 243     5312   7737   6808   -170   -447    743       N
ATOM   3669  CA  ASP A 243      -1.787  28.319  -2.746  1.00 52.09           C
ANISOU 3669  CA  ASP A 243     5330   7519   6943   -174   -521    695       C
ATOM   3670  C   ASP A 243      -1.491  28.887  -4.139  1.00 51.99           C
ANISOU 3670  C   ASP A 243     5245   7448   7059   -280   -565    884       C
ATOM   3671  O   ASP A 243      -0.345  29.183  -4.472  1.00 50.50           O
ANISOU 3671  O   ASP A 243     4997   7244   6948   -410   -665    982       O
ATOM   3672  CB  ASP A 243      -1.431  29.290  -1.610  1.00 53.27           C
ANISOU 3672  CB  ASP A 243     5530   7552   7157   -191   -657    545       C
ATOM   3673  CG  ASP A 243      -2.348  30.524  -1.601  1.00 56.90           C
ANISOU 3673  CG  ASP A 243     6056   7789   7776   -149   -764    446       C
ATOM   3674  OD1 ASP A 243      -3.126  30.666  -2.584  1.00 57.43           O
ANISOU 3674  OD1 ASP A 243     6111   7773   7937   -154   -752    546       O
ATOM   3675  OD2 ASP A 243      -2.521  31.082  -0.499  1.00 59.60           O
ANISOU 3675  OD2 ASP A 243     6462   8039   8144    -96   -874    256       O
ATOM   3676  H   ASP A 243      -0.159  27.051  -2.246  1.00 62.71           H
ATOM   3677  HA  ASP A 243      -2.861  28.147  -2.675  1.00 62.51           H
ATOM   3678  HB2 ASP A 243      -1.538  28.766  -0.658  1.00 63.92           H
ATOM   3679  HB3 ASP A 243      -0.390  29.603  -1.702  1.00 63.92           H
ATOM   3680  N   PHE A 244      -2.500  28.914  -5.008  1.00 48.92           N
ANISOU 3680  N   PHE A 244     4849   7050   6690   -234   -493    954       N
ATOM   3681  CA  PHE A 244      -2.355  29.429  -6.372  1.00 48.98           C
ANISOU 3681  CA  PHE A 244     4775   7037   6797   -327   -526   1152       C
ATOM   3682  C   PHE A 244      -2.107  30.950  -6.384  1.00 53.30           C
ANISOU 3682  C   PHE A 244     5332   7373   7546   -443   -701   1193       C
ATOM   3683  O   PHE A 244      -1.498  31.434  -7.335  1.00 51.63           O
ANISOU 3683  O   PHE A 244     5024   7181   7411   -583   -766   1399       O
ATOM   3684  CB  PHE A 244      -3.604  29.095  -7.212  1.00 47.44           C
ANISOU 3684  CB  PHE A 244     4586   6836   6603   -244   -439   1188       C
ATOM   3685  CG  PHE A 244      -3.807  27.675  -7.738  1.00 48.55           C
ANISOU 3685  CG  PHE A 244     4687   7180   6581   -179   -310   1227       C
ATOM   3686  CD1 PHE A 244      -3.307  26.527  -7.085  1.00 48.70           C
ANISOU 3686  CD1 PHE A 244     4721   7325   6457   -137   -265   1152       C
ATOM   3687  CD2 PHE A 244      -4.491  27.519  -8.961  1.00 49.07           C
ANISOU 3687  CD2 PHE A 244     4705   7298   6644   -153   -255   1335       C
ATOM   3688  CE1 PHE A 244      -3.448  25.256  -7.676  1.00 44.21           C
ANISOU 3688  CE1 PHE A 244     4134   6901   5762    -70   -188   1177       C
ATOM   3689  CE2 PHE A 244      -4.612  26.255  -9.562  1.00 45.62           C
ANISOU 3689  CE2 PHE A 244     4242   7023   6069    -82   -171   1348       C
ATOM   3690  CZ  PHE A 244      -4.067  25.125  -8.931  1.00 43.46           C
ANISOU 3690  CZ  PHE A 244     3998   6844   5671    -40   -147   1266       C
ATOM   3691  H   PHE A 244      -3.417  28.691  -4.660  1.00 58.71           H
ATOM   3692  HA  PHE A 244      -1.481  28.971  -6.837  1.00 58.77           H
ATOM   3693  HB2 PHE A 244      -4.493  29.400  -6.661  1.00 56.93           H
ATOM   3694  HB3 PHE A 244      -3.546  29.730  -8.096  1.00 56.93           H
ATOM   3695  HD1 PHE A 244      -2.769  26.609  -6.153  1.00 58.44           H
ATOM   3696  HD2 PHE A 244      -4.856  28.394  -9.483  1.00 58.89           H
ATOM   3697  HE1 PHE A 244      -3.017  24.390  -7.188  1.00 53.05           H
ATOM   3698  HE2 PHE A 244      -5.059  26.165 -10.542  1.00 54.74           H
ATOM   3699  HZ  PHE A 244      -4.101  24.161  -9.419  1.00 52.15           H
ATOM   3700  N   ASP A 245      -2.539  31.694  -5.355  1.00 59.09           N
ANISOU 3700  N   ASP A 245     6175   7913   8366   -386   -795   1005       N
ATOM   3701  CA  ASP A 245      -2.259  33.135  -5.238  1.00 62.75           C
ANISOU 3701  CA  ASP A 245     6674   8122   9046   -484  -1006   1019       C
ATOM   3702  C   ASP A 245      -0.810  33.417  -4.769  1.00 66.29           C
ANISOU 3702  C   ASP A 245     7077   8584   9526   -641  -1125   1067       C
ATOM   3703  O   ASP A 245      -0.328  34.542  -4.926  1.00 68.83           O
ANISOU 3703  O   ASP A 245     7382   8736  10035   -799  -1312   1187       O
ATOM   3704  CB  ASP A 245      -3.235  33.806  -4.258  1.00 66.80           C
ANISOU 3704  CB  ASP A 245     7320   8435   9627   -332  -1090    761       C
ATOM   3705  CG  ASP A 245      -4.735  33.697  -4.545  1.00 63.30           C
ANISOU 3705  CG  ASP A 245     6904   7975   9174   -185   -998    727       C
ATOM   3706  OD1 ASP A 245      -5.189  33.564  -5.707  1.00 62.24           O
ANISOU 3706  OD1 ASP A 245     6716   7825   9108   -246   -978    924       O
ATOM   3707  OD2 ASP A 245      -5.490  34.082  -3.624  1.00 64.22           O
ANISOU 3707  OD2 ASP A 245     7080   8121   9200     -8   -946    511       O
ATOM   3708  H   ASP A 245      -2.933  31.237  -4.537  1.00 70.91           H
ATOM   3709  HA  ASP A 245      -2.378  33.602  -6.217  1.00 75.30           H
ATOM   3710  HB2 ASP A 245      -3.067  33.374  -3.276  1.00 80.16           H
ATOM   3711  HB3 ASP A 245      -2.984  34.862  -4.198  1.00 80.16           H
ATOM   3712  N   ASN A 246      -0.118  32.433  -4.163  1.00 67.32           N
ANISOU 3712  N   ASN A 246     7185   8911   9481   -609  -1036    987       N
ATOM   3713  CA  ASN A 246       1.283  32.528  -3.715  1.00 66.77           C
ANISOU 3713  CA  ASN A 246     7063   8889   9417   -745  -1140   1019       C
ATOM   3714  C   ASN A 246       1.953  31.132  -3.559  1.00 60.94           C
ANISOU 3714  C   ASN A 246     6256   8450   8449   -697   -982   1027       C
ATOM   3715  O   ASN A 246       1.983  30.599  -2.445  1.00 61.48           O
ANISOU 3715  O   ASN A 246     6379   8574   8406   -612   -955    851       O
ATOM   3716  CB  ASN A 246       1.326  33.339  -2.399  1.00 71.28           C
ANISOU 3716  CB  ASN A 246     7750   9259  10074   -713  -1304    785       C
ATOM   3717  CG  ASN A 246       2.750  33.619  -1.949  1.00 73.75           C
ANISOU 3717  CG  ASN A 246     8008   9588  10427   -878  -1447    827       C
ATOM   3718  OD1 ASN A 246       3.640  33.881  -2.737  1.00 73.04           O
ANISOU 3718  OD1 ASN A 246     7786   9590  10374  -1061  -1482   1073       O
ATOM   3719  ND2 ASN A 246       3.008  33.679  -0.663  1.00 76.06           N
ANISOU 3719  ND2 ASN A 246     8385   9818  10697   -812  -1534    589       N
ATOM   3720  H   ASN A 246      -0.577  31.537  -4.072  1.00 80.78           H
ATOM   3721  HA  ASN A 246       1.846  33.086  -4.464  1.00 80.12           H
ATOM   3722  HB2 ASN A 246       0.838  34.302  -2.542  1.00 85.54           H
ATOM   3723  HB3 ASN A 246       0.792  32.797  -1.619  1.00 85.54           H
ATOM   3724 HD21 ASN A 246       3.977  33.805  -0.433  1.00 91.27           H
ATOM   3725 HD22 ASN A 246       2.310  33.404  -0.001  1.00 91.27           H
ATOM   3726  N   PRO A 247       2.442  30.493  -4.646  1.00 54.56           N
ANISOU 3726  N   PRO A 247     5324   7848   7558   -736   -886   1224       N
ATOM   3727  CA  PRO A 247       2.948  29.119  -4.599  1.00 50.33           C
ANISOU 3727  CA  PRO A 247     4737   7579   6807   -652   -754   1211       C
ATOM   3728  C   PRO A 247       4.288  28.982  -3.856  1.00 52.06           C
ANISOU 3728  C   PRO A 247     4904   7903   6973   -724   -825   1189       C
ATOM   3729  O   PRO A 247       5.309  29.529  -4.271  1.00 52.54           O
ANISOU 3729  O   PRO A 247     4871   7964   7128   -893   -947   1319       O
ATOM   3730  CB  PRO A 247       3.064  28.643  -6.051  1.00 46.47           C
ANISOU 3730  CB  PRO A 247     4113   7280   6263   -673   -681   1421       C
ATOM   3731  CG  PRO A 247       2.175  29.610  -6.828  1.00 51.14           C
ANISOU 3731  CG  PRO A 247     4711   7697   7021   -737   -730   1528       C
ATOM   3732  CD  PRO A 247       2.295  30.906  -6.032  1.00 51.80           C
ANISOU 3732  CD  PRO A 247     4876   7509   7296   -835   -900   1460       C
ATOM   3733  HA  PRO A 247       2.205  28.500  -4.097  1.00 60.40           H
ATOM   3734  HB2 PRO A 247       4.090  28.738  -6.404  1.00 55.76           H
ATOM   3735  HB3 PRO A 247       2.727  27.613  -6.160  1.00 55.76           H
ATOM   3736  HG2 PRO A 247       2.519  29.737  -7.855  1.00 61.36           H
ATOM   3737  HG3 PRO A 247       1.142  29.260  -6.808  1.00 61.36           H
ATOM   3738  HD2 PRO A 247       3.191  31.448  -6.339  1.00 62.16           H
ATOM   3739  HD3 PRO A 247       1.407  31.517  -6.193  1.00 62.16           H
ATOM   3740  N   ASP A 248       4.326  28.076  -2.875  1.00 51.87           N
ANISOU 3740  N   ASP A 248     4934   7978   6797   -607   -757   1041       N
ATOM   3741  CA  ASP A 248       5.522  27.623  -2.148  1.00 56.69           C
ANISOU 3741  CA  ASP A 248     5493   8724   7324   -646   -808   1012       C
ATOM   3742  C   ASP A 248       6.287  26.598  -3.019  1.00 57.71           C
ANISOU 3742  C   ASP A 248     5486   9139   7302   -616   -732   1145       C
ATOM   3743  O   ASP A 248       5.948  25.412  -3.056  1.00 56.69           O
ANISOU 3743  O   ASP A 248     5389   9130   7020   -471   -642   1078       O
ATOM   3744  CB  ASP A 248       5.020  27.157  -0.774  1.00 54.12           C
ANISOU 3744  CB  ASP A 248     5288   8374   6903   -527   -784    799       C
ATOM   3745  CG  ASP A 248       6.115  26.707   0.198  1.00 56.29           C
ANISOU 3745  CG  ASP A 248     5515   8773   7099   -565   -850    757       C
ATOM   3746  OD1 ASP A 248       6.992  25.937  -0.255  1.00 56.86           O
ANISOU 3746  OD1 ASP A 248     5450   8988   7166   -670   -895    898       O
ATOM   3747  OD2 ASP A 248       5.770  26.686   1.404  1.00 58.21           O
ANISOU 3747  OD2 ASP A 248     5846   9000   7271   -488   -856    590       O
ATOM   3748  H   ASP A 248       3.451  27.655  -2.601  1.00 62.25           H
ATOM   3749  HA  ASP A 248       6.194  28.470  -2.000  1.00 68.03           H
ATOM   3750  HB2 ASP A 248       4.499  27.982  -0.307  1.00 64.95           H
ATOM   3751  HB3 ASP A 248       4.322  26.344  -0.906  1.00 64.95           H
ATOM   3752  N   TYR A 249       7.139  27.091  -3.926  1.00 55.85           N
ANISOU 3752  N   TYR A 249     5090   9027   7105   -751   -784   1341       N
ATOM   3753  CA  TYR A 249       7.885  26.273  -4.892  1.00 56.54           C
ANISOU 3753  CA  TYR A 249     5020   9434   7029   -696   -717   1462       C
ATOM   3754  C   TYR A 249       8.972  25.413  -4.225  1.00 54.66           C
ANISOU 3754  C   TYR A 249     4741   9393   6632   -627   -720   1385       C
ATOM   3755  O   TYR A 249       9.341  24.366  -4.751  1.00 58.70           O
ANISOU 3755  O   TYR A 249     5157  10168   6979   -508   -663   1419       O
ATOM   3756  CB  TYR A 249       8.495  27.180  -5.972  1.00 57.62           C
ANISOU 3756  CB  TYR A 249     4959   9711   7223   -869   -775   1715       C
ATOM   3757  CG  TYR A 249       7.496  27.914  -6.857  1.00 58.14           C
ANISOU 3757  CG  TYR A 249     5043   9625   7422   -923   -769   1827       C
ATOM   3758  CD1 TYR A 249       6.555  27.187  -7.612  1.00 53.52           C
ANISOU 3758  CD1 TYR A 249     4506   9061   6767   -764   -651   1794       C
ATOM   3759  CD2 TYR A 249       7.555  29.317  -6.982  1.00 59.49           C
ANISOU 3759  CD2 TYR A 249     5184   9623   7796  -1135   -902   1972       C
ATOM   3760  CE1 TYR A 249       5.710  27.851  -8.523  1.00 53.67           C
ANISOU 3760  CE1 TYR A 249     4535   8956   6901   -806   -646   1897       C
ATOM   3761  CE2 TYR A 249       6.684  29.990  -7.860  1.00 56.29           C
ANISOU 3761  CE2 TYR A 249     4797   9073   7516  -1177   -909   2083       C
ATOM   3762  CZ  TYR A 249       5.766  29.254  -8.637  1.00 55.46           C
ANISOU 3762  CZ  TYR A 249     4732   9018   7324  -1008   -771   2044       C
ATOM   3763  OH  TYR A 249       4.926  29.901  -9.486  1.00 57.95           O
ANISOU 3763  OH  TYR A 249     5060   9203   7757  -1044   -778   2155       O
ATOM   3764  H   TYR A 249       7.328  28.085  -3.901  1.00 67.03           H
ATOM   3765  HA  TYR A 249       7.193  25.581  -5.372  1.00 67.85           H
ATOM   3766  HB2 TYR A 249       9.150  27.906  -5.486  1.00 69.14           H
ATOM   3767  HB3 TYR A 249       9.121  26.571  -6.627  1.00 69.14           H
ATOM   3768  HD1 TYR A 249       6.505  26.112  -7.511  1.00 64.22           H
ATOM   3769  HD2 TYR A 249       8.268  29.880  -6.393  1.00 71.39           H
ATOM   3770  HE1 TYR A 249       5.031  27.298  -9.148  1.00 64.40           H
ATOM   3771  HE2 TYR A 249       6.727  31.065  -7.934  1.00 67.54           H
ATOM   3772  HH  TYR A 249       5.083  30.846  -9.430  1.00 69.54           H
ATOM   3773  N   GLU A 250       9.400  25.773  -3.016  1.00 52.44           N
ANISOU 3773  N   GLU A 250     4531   9000   6393   -680   -797   1269       N
ATOM   3774  CA  GLU A 250      10.305  25.011  -2.161  1.00 53.87           C
ANISOU 3774  CA  GLU A 250     4684   9361   6421   -604   -802   1189       C
ATOM   3775  C   GLU A 250       9.663  23.702  -1.636  1.00 54.38           C
ANISOU 3775  C   GLU A 250     4884   9421   6358   -391   -709   1048       C
ATOM   3776  O   GLU A 250      10.302  22.643  -1.668  1.00 54.31           O
ANISOU 3776  O   GLU A 250     4824   9620   6193   -262   -681   1043       O
ATOM   3777  H   GLU A 250       9.132  26.700  -2.685  1.00 62.93           H
ATOM   3778  CB  GLU A 250      10.772  25.913  -0.995  1.00  0.00           C
ATOM   3779  CG  GLU A 250      11.593  27.159  -1.386  1.00  0.00           C
ATOM   3780  CD  GLU A 250      10.804  28.434  -1.703  1.00  0.00           C
ATOM   3781  OE2 GLU A 250      11.428  29.507  -1.601  1.00  0.00           O
ATOM   3782  OE1 GLU A 250       9.613  28.325  -2.108  1.00  0.00           O
ATOM   3783  HA  GLU A 250      11.178  24.721  -2.742  1.00  0.00           H
ATOM   3784  HB2 GLU A 250      11.391  25.290  -0.347  1.00  0.00           H
ATOM   3785  HB3 GLU A 250       9.906  26.222  -0.402  1.00  0.00           H
ATOM   3786  HG2 GLU A 250      12.254  27.362  -0.549  1.00  0.00           H
ATOM   3787  HG3 GLU A 250      12.243  26.899  -2.226  1.00  0.00           H
ATOM   3788  N   ARG A 251       8.386  23.735  -1.214  1.00 58.35           N
ANISOU 3788  N   ARG A 251     5552   9692   6925   -349   -675    940       N
ATOM   3789  CA  ARG A 251       7.583  22.551  -0.847  1.00 57.08           C
ANISOU 3789  CA  ARG A 251     5512   9516   6660   -184   -602    847       C
ATOM   3790  C   ARG A 251       6.920  21.867  -2.044  1.00 53.29           C
ANISOU 3790  C   ARG A 251     5023   9072   6151    -90   -532    915       C
ATOM   3791  O   ARG A 251       6.610  20.675  -1.952  1.00 53.60           O
ANISOU 3791  O   ARG A 251     5113   9170   6082     50   -509    878       O
ATOM   3792  CB  ARG A 251       6.489  22.968   0.141  1.00 56.31           C
ANISOU 3792  CB  ARG A 251     5563   9214   6618   -177   -590    724       C
ATOM   3793  CG  ARG A 251       7.051  23.451   1.492  1.00 58.26           C
ANISOU 3793  CG  ARG A 251     5836   9422   6878   -235   -669    615       C
ATOM   3794  CD  ARG A 251       5.888  23.865   2.393  1.00 61.32           C
ANISOU 3794  CD  ARG A 251     6349   9660   7288   -190   -649    484       C
ATOM   3795  NE  ARG A 251       5.128  22.689   2.843  1.00 64.11           N
ANISOU 3795  NE  ARG A 251     6777  10065   7517    -70   -564    469       N
ATOM   3796  CZ  ARG A 251       3.845  22.684   3.136  1.00 66.84           C
ANISOU 3796  CZ  ARG A 251     7202  10339   7854    -18   -512    413       C
ATOM   3797  NH1 ARG A 251       3.165  23.791   3.237  1.00 63.96           N
ANISOU 3797  NH1 ARG A 251     6862   9849   7591    -41   -532    335       N
ATOM   3798  NH2 ARG A 251       3.230  21.547   3.313  1.00 70.18           N
ANISOU 3798  NH2 ARG A 251     7675  10822   8168     59   -454    441       N
ATOM   3799  H   ARG A 251       7.947  24.660  -1.122  1.00 70.01           H
ATOM   3800  HA  ARG A 251       8.223  21.802  -0.383  1.00 68.50           H
ATOM   3801  HB2 ARG A 251       5.870  23.740  -0.318  1.00 67.57           H
ATOM   3802  HB3 ARG A 251       5.822  22.121   0.306  1.00 67.57           H
ATOM   3803  HG2 ARG A 251       7.611  22.643   1.968  1.00 69.91           H
ATOM   3804  HG3 ARG A 251       7.717  24.308   1.363  1.00 69.91           H
ATOM   3805  HD2 ARG A 251       6.267  24.433   3.246  1.00 73.58           H
ATOM   3806  HD3 ARG A 251       5.225  24.509   1.817  1.00 73.58           H
ATOM   3807  HE  ARG A 251       5.589  21.809   2.704  1.00 76.93           H
ATOM   3808 HH11 ARG A 251       3.656  24.647   2.999  1.00 76.75           H
ATOM   3809 HH12 ARG A 251       2.181  23.804   3.402  1.00 76.75           H
ATOM   3810 HH21 ARG A 251       3.739  20.699   3.144  1.00 84.21           H
ATOM   3811 HH22 ARG A 251       2.234  21.524   3.414  1.00 84.21           H
ATOM   3812  N   PHE A 252       6.614  22.616  -3.104  1.00 51.34           N
ANISOU 3812  N   PHE A 252     4719   8783   6005   -164   -516   1014       N
ATOM   3813  CA  PHE A 252       5.795  22.169  -4.235  1.00 50.22           C
ANISOU 3813  CA  PHE A 252     4578   8655   5848    -80   -453   1065       C
ATOM   3814  C   PHE A 252       6.493  22.373  -5.609  1.00 49.55           C
ANISOU 3814  C   PHE A 252     4311   8777   5739   -114   -458   1217       C
ATOM   3815  O   PHE A 252       5.876  22.914  -6.533  1.00 52.75           O
ANISOU 3815  O   PHE A 252     4675   9136   6233   -181   -440   1317       O
ATOM   3816  CB  PHE A 252       4.403  22.832  -4.123  1.00 48.58           C
ANISOU 3816  CB  PHE A 252     4474   8216   5769   -116   -417   1044       C
ATOM   3817  CG  PHE A 252       3.719  22.750  -2.756  1.00 47.62           C
ANISOU 3817  CG  PHE A 252     4492   7944   5659    -98   -414    909       C
ATOM   3818  CD1 PHE A 252       3.508  21.507  -2.126  1.00 47.16           C
ANISOU 3818  CD1 PHE A 252     4515   7917   5488      8   -392    840       C
ATOM   3819  CD2 PHE A 252       3.276  23.922  -2.112  1.00 49.10           C
ANISOU 3819  CD2 PHE A 252     4722   7970   5964   -179   -450    855       C
ATOM   3820  CE1 PHE A 252       2.867  21.437  -0.874  1.00 50.15           C
ANISOU 3820  CE1 PHE A 252     4994   8212   5851     20   -384    744       C
ATOM   3821  CE2 PHE A 252       2.637  23.857  -0.860  1.00 49.50           C
ANISOU 3821  CE2 PHE A 252     4876   7939   5992   -136   -445    720       C
ATOM   3822  CZ  PHE A 252       2.433  22.614  -0.240  1.00 49.91           C
ANISOU 3822  CZ  PHE A 252     4987   8068   5910    -43   -402    676       C
ATOM   3823  H   PHE A 252       6.765  23.617  -3.014  1.00 61.61           H
ATOM   3824  HA  PHE A 252       5.643  21.096  -4.140  1.00 60.26           H
ATOM   3825  HB2 PHE A 252       4.498  23.880  -4.403  1.00 58.30           H
ATOM   3826  HB3 PHE A 252       3.741  22.384  -4.861  1.00 58.30           H
ATOM   3827  HD1 PHE A 252       3.867  20.606  -2.598  1.00 56.60           H
ATOM   3828  HD2 PHE A 252       3.447  24.884  -2.576  1.00 58.92           H
ATOM   3829  HE1 PHE A 252       2.719  20.477  -0.402  1.00 60.19           H
ATOM   3830  HE2 PHE A 252       2.314  24.769  -0.377  1.00 59.40           H
ATOM   3831  HZ  PHE A 252       1.943  22.571   0.719  1.00 59.90           H
ATOM   3832  N   PRO A 253       7.752  21.919  -5.811  1.00 52.89           N
ANISOU 3832  N   PRO A 253     4609   9461   6027    -60   -484   1243       N
ATOM   3833  CA  PRO A 253       8.598  22.284  -6.961  1.00 48.48           C
ANISOU 3833  CA  PRO A 253     3832   9172   5415   -104   -491   1409       C
ATOM   3834  C   PRO A 253       8.013  21.942  -8.338  1.00 49.72           C
ANISOU 3834  C   PRO A 253     3949   9409   5534     -8   -436   1466       C
ATOM   3835  O   PRO A 253       8.156  22.739  -9.269  1.00 46.77           O
ANISOU 3835  O   PRO A 253     3433   9143   5195   -113   -431   1635       O
ATOM   3836  CB  PRO A 253       9.940  21.572  -6.723  1.00 46.26           C
ANISOU 3836  CB  PRO A 253     3441   9181   4957      2   -522   1378       C
ATOM   3837  CG  PRO A 253       9.581  20.415  -5.792  1.00 45.16           C
ANISOU 3837  CG  PRO A 253     3487   8904   4767    158   -525   1194       C
ATOM   3838  CD  PRO A 253       8.511  21.056  -4.917  1.00 49.70           C
ANISOU 3838  CD  PRO A 253     4242   9146   5497     55   -512   1133       C
ATOM   3839  HA  PRO A 253       8.775  23.359  -6.949  1.00 58.17           H
ATOM   3840  HB2 PRO A 253      10.402  21.216  -7.646  1.00 55.52           H
ATOM   3841  HB3 PRO A 253      10.622  22.247  -6.203  1.00 55.52           H
ATOM   3842  HG2 PRO A 253       9.153  19.592  -6.367  1.00 54.19           H
ATOM   3843  HG3 PRO A 253      10.438  20.077  -5.207  1.00 54.19           H
ATOM   3844  HD2 PRO A 253       7.885  20.289  -4.460  1.00 59.64           H
ATOM   3845  HD3 PRO A 253       8.991  21.664  -4.147  1.00 59.64           H
ATOM   3846  N   ASN A 254       7.250  20.849  -8.455  1.00 54.43           N
ANISOU 3846  N   ASN A 254     4661   9961   6059    183   -409   1340       N
ATOM   3847  CA  ASN A 254       6.570  20.461  -9.694  1.00 54.32           C
ANISOU 3847  CA  ASN A 254     4607  10038   5996    293   -375   1371       C
ATOM   3848  C   ASN A 254       5.325  21.296 -10.029  1.00 51.94           C
ANISOU 3848  C   ASN A 254     4364   9521   5851    179   -333   1441       C
ATOM   3849  O   ASN A 254       4.860  21.227 -11.165  1.00 50.62           O
ANISOU 3849  O   ASN A 254     4149   9434   5649    251   -304   1484       O
ATOM   3850  CB  ASN A 254       6.250  18.957  -9.666  1.00 51.61           C
ANISOU 3850  CB  ASN A 254     4389   9662   5558    518   -397   1209       C
ATOM   3851  CG  ASN A 254       7.505  18.112  -9.689  1.00 56.78           C
ANISOU 3851  CG  ASN A 254     4949  10598   6027    697   -454   1144       C
ATOM   3852  OD1 ASN A 254       7.888  17.517  -8.693  1.00 57.35           O
ANISOU 3852  OD1 ASN A 254     5133  10594   6063    788   -508   1025       O
ATOM   3853  ND2 ASN A 254       8.270  18.179 -10.754  1.00 55.36           N
ANISOU 3853  ND2 ASN A 254     4549  10767   5717    754   -448   1230       N
ATOM   3854  H   ASN A 254       7.132  20.258  -7.641  1.00 65.32           H
ATOM   3855  HA  ASN A 254       7.258  20.638 -10.523  1.00 65.19           H
ATOM   3856  HB2 ASN A 254       5.668  18.710  -8.781  1.00 61.93           H
ATOM   3857  HB3 ASN A 254       5.657  18.691 -10.540  1.00 61.93           H
ATOM   3858 HD21 ASN A 254       9.119  17.652 -10.740  1.00 66.43           H
ATOM   3859 HD22 ASN A 254       8.025  18.782 -11.536  1.00 66.43           H
ATOM   3860  N   PHE A 255       4.863  22.199  -9.155  1.00 44.76           N
ANISOU 3860  N   PHE A 255     3550   8353   5103     24   -339   1442       N
ATOM   3861  CA  PHE A 255       3.832  23.172  -9.539  1.00 48.08           C
ANISOU 3861  CA  PHE A 255     4007   8588   5673    -74   -316   1513       C
ATOM   3862  C   PHE A 255       4.323  24.134 -10.644  1.00 49.39           C
ANISOU 3862  C   PHE A 255     3986   8914   5865   -192   -332   1725       C
ATOM   3863  O   PHE A 255       3.552  24.458 -11.542  1.00 47.36           O
ANISOU 3863  O   PHE A 255     3730   8562   5700   -238   -315   1811       O
ATOM   3864  CB  PHE A 255       3.298  23.911  -8.302  1.00 50.77           C
ANISOU 3864  CB  PHE A 255     4482   8640   6167   -183   -342   1441       C
ATOM   3865  CG  PHE A 255       2.074  24.765  -8.595  1.00 48.16           C
ANISOU 3865  CG  PHE A 255     4215   8097   5988   -239   -330   1473       C
ATOM   3866  CD1 PHE A 255       0.828  24.153  -8.833  1.00 51.83           C
ANISOU 3866  CD1 PHE A 255     4777   8471   6447   -135   -268   1403       C
ATOM   3867  CD2 PHE A 255       2.170  26.169  -8.636  1.00 49.81           C
ANISOU 3867  CD2 PHE A 255     4384   8190   6350   -398   -400   1577       C
ATOM   3868  CE1 PHE A 255      -0.306  24.936  -9.117  1.00 50.00           C
ANISOU 3868  CE1 PHE A 255     4591   8065   6343   -171   -257   1427       C
ATOM   3869  CE2 PHE A 255       1.040  26.952  -8.936  1.00 51.24           C
ANISOU 3869  CE2 PHE A 255     4629   8166   6673   -426   -405   1596       C
ATOM   3870  CZ  PHE A 255      -0.200  26.335  -9.174  1.00 51.15           C
ANISOU 3870  CZ  PHE A 255     4703   8094   6637   -304   -325   1516       C
ATOM   3871  H   PHE A 255       5.298  22.290  -8.242  1.00 53.71           H
ATOM   3872  HA  PHE A 255       2.995  22.615  -9.960  1.00 57.70           H
ATOM   3873  HB2 PHE A 255       3.022  23.175  -7.544  1.00 60.92           H
ATOM   3874  HB3 PHE A 255       4.087  24.534  -7.878  1.00 60.92           H
ATOM   3875  HD1 PHE A 255       0.744  23.078  -8.804  1.00 62.20           H
ATOM   3876  HD2 PHE A 255       3.109  26.651  -8.425  1.00 59.77           H
ATOM   3877  HE1 PHE A 255      -1.253  24.464  -9.320  1.00 60.00           H
ATOM   3878  HE2 PHE A 255       1.123  28.028  -8.987  1.00 61.48           H
ATOM   3879  HZ  PHE A 255      -1.067  26.936  -9.406  1.00 61.38           H
ATOM   3880  N   GLN A 256       5.642  24.326 -10.788  1.00 54.02           N
ANISOU 3880  N   GLN A 256     4400   9759   6366   -247   -370   1829       N
ATOM   3881  CA  GLN A 256       6.263  25.034 -11.926  1.00 60.61           C
ANISOU 3881  CA  GLN A 256     5018  10818   7191   -369   -389   2073       C
ATOM   3882  C   GLN A 256       6.132  24.299 -13.279  1.00 52.94           C
ANISOU 3882  C   GLN A 256     3923  10143   6049   -209   -329   2122       C
ATOM   3883  O   GLN A 256       6.446  24.866 -14.323  1.00 55.64           O
ANISOU 3883  O   GLN A 256     4066  10720   6355   -295   -333   2342       O
ATOM   3884  CB  GLN A 256       7.753  25.286 -11.634  1.00 63.60           C
ANISOU 3884  CB  GLN A 256     5225  11429   7511   -484   -451   2182       C
ATOM   3885  CG  GLN A 256       7.987  26.096 -10.353  1.00 63.78           C
ANISOU 3885  CG  GLN A 256     5354  11179   7702   -652   -537   2136       C
ATOM   3886  CD  GLN A 256       9.458  26.174  -9.980  1.00 70.05           C
ANISOU 3886  CD  GLN A 256     5977  12214   8425   -756   -605   2226       C
ATOM   3887  OE1 GLN A 256      10.141  27.154 -10.218  1.00 73.27           O
ANISOU 3887  OE1 GLN A 256     6272  12620   8948   -992   -701   2422       O
ATOM   3888  NE2 GLN A 256      10.034  25.093  -9.504  1.00 65.97           N
ANISOU 3888  NE2 GLN A 256     5441  11898   7724   -586   -571   2090       N
ATOM   3889  H   GLN A 256       6.259  23.933 -10.088  1.00 64.82           H
ATOM   3890  HA  GLN A 256       5.768  25.999 -12.042  1.00 72.73           H
ATOM   3891  HB2 GLN A 256       8.261  24.324 -11.552  1.00 76.32           H
ATOM   3892  HB3 GLN A 256       8.194  25.835 -12.467  1.00 76.32           H
ATOM   3893  HG2 GLN A 256       7.592  27.104 -10.480  1.00 76.54           H
ATOM   3894  HG3 GLN A 256       7.475  25.613  -9.526  1.00 76.54           H
ATOM   3895 HE21 GLN A 256       9.487  24.256  -9.351  1.00 79.16           H
ATOM   3896 HE22 GLN A 256      11.001  25.184  -9.258  1.00 79.16           H
ATOM   3897  N   ASN A 257       5.735  23.022 -13.274  1.00 50.00           N
ANISOU 3897  N   ASN A 257     3656   9774   5569     19   -290   1928       N
ATOM   3898  CA  ASN A 257       5.469  22.216 -14.470  1.00 50.67           C
ANISOU 3898  CA  ASN A 257     3651  10108   5492    206   -256   1922       C
ATOM   3899  C   ASN A 257       3.962  22.051 -14.765  1.00 45.34           C
ANISOU 3899  C   ASN A 257     3135   9186   4908    263   -223   1847       C
ATOM   3900  O   ASN A 257       3.607  21.302 -15.674  1.00 51.05           O
ANISOU 3900  O   ASN A 257     3821  10064   5510    435   -210   1801       O
ATOM   3901  CB  ASN A 257       6.154  20.841 -14.311  1.00 49.17           C
ANISOU 3901  CB  ASN A 257     3451  10129   5101    449   -279   1748       C
ATOM   3902  CG  ASN A 257       7.610  20.881 -13.883  1.00 48.96           C
ANISOU 3902  CG  ASN A 257     3281  10341   4980    411   -312   1793       C
ATOM   3903  OD1 ASN A 257       8.014  20.226 -12.932  1.00 52.89           O
ANISOU 3903  OD1 ASN A 257     3889  10730   5476    458   -345   1652       O
ATOM   3904  ND2 ASN A 257       8.440  21.668 -14.530  1.00 55.78           N
ANISOU 3904  ND2 ASN A 257     3884  11552   5758    319   -307   2007       N
ATOM   3905  H   ASN A 257       5.505  22.600 -12.382  1.00 60.00           H
ATOM   3906  HA  ASN A 257       5.894  22.717 -15.341  1.00 60.80           H
ATOM   3907  HB2 ASN A 257       5.605  20.261 -13.569  1.00 59.00           H
ATOM   3908  HB3 ASN A 257       6.095  20.309 -15.260  1.00 59.00           H
ATOM   3909 HD21 ASN A 257       9.372  21.737 -14.166  1.00 66.94           H
ATOM   3910 HD22 ASN A 257       8.100  22.270 -15.259  1.00 66.94           H
ATOM   3911  N   VAL A 258       3.069  22.615 -13.940  1.00 46.95           N
ANISOU 3911  N   VAL A 258     3503   9027   5309    136   -218   1825       N
ATOM   3912  CA  VAL A 258       1.612  22.463 -14.102  1.00 52.43           C
ANISOU 3912  CA  VAL A 258     4345   9493   6084    189   -187   1746       C
ATOM   3913  C   VAL A 258       1.123  23.180 -15.377  1.00 52.25           C
ANISOU 3913  C   VAL A 258     4214   9545   6093    139   -163   1913       C
ATOM   3914  O   VAL A 258       1.578  24.282 -15.687  1.00 50.31           O
ANISOU 3914  O   VAL A 258     3856   9335   5923    -27   -182   2105       O
ATOM   3915  CB  VAL A 258       0.887  22.903 -12.807  1.00 50.15           C
ANISOU 3915  CB  VAL A 258     4242   8848   5967     92   -188   1660       C
ATOM   3916  CG1 VAL A 258       0.589  24.399 -12.721  1.00 51.94           C
ANISOU 3916  CG1 VAL A 258     4443   8925   6365    -93   -208   1798       C
ATOM   3917  CG2 VAL A 258      -0.444  22.177 -12.634  1.00 53.75           C
ANISOU 3917  CG2 VAL A 258     4849   9127   6447    190   -159   1536       C
ATOM   3918  H   VAL A 258       3.402  23.241 -13.214  1.00 56.34           H
ATOM   3919  HA  VAL A 258       1.419  21.398 -14.234  1.00 62.92           H
ATOM   3920  HB  VAL A 258       1.507  22.632 -11.951  1.00 60.19           H
ATOM   3921 HG11 VAL A 258       0.276  24.657 -11.713  1.00 62.32           H
ATOM   3922 HG12 VAL A 258       1.493  24.958 -12.951  1.00 62.32           H
ATOM   3923 HG13 VAL A 258      -0.200  24.673 -13.419  1.00 62.32           H
ATOM   3924 HG21 VAL A 258      -0.962  22.559 -11.756  1.00 64.50           H
ATOM   3925 HG22 VAL A 258      -1.054  22.342 -13.515  1.00 64.50           H
ATOM   3926 HG23 VAL A 258      -0.274  21.107 -12.513  1.00 64.50           H
ATOM   3927  N   VAL A 259       0.181  22.584 -16.118  1.00 54.78           N
ANISOU 3927  N   VAL A 259     4569   9883   6362    275   -138   1851       N
ATOM   3928  CA  VAL A 259      -0.413  23.169 -17.343  1.00 53.51           C
ANISOU 3928  CA  VAL A 259     4318   9795   6219    252   -113   1993       C
ATOM   3929  C   VAL A 259      -1.908  22.871 -17.381  1.00 55.04           C
ANISOU 3929  C   VAL A 259     4674   9743   6496    313    -92   1877       C
ATOM   3930  O   VAL A 259      -2.311  21.707 -17.456  1.00 52.19           O
ANISOU 3930  O   VAL A 259     4399   9373   6058    463   -104   1712       O
ATOM   3931  CB  VAL A 259       0.250  22.665 -18.648  1.00 54.32           C
ANISOU 3931  CB  VAL A 259     4219  10316   6103    388   -110   2057       C
ATOM   3932  CG1 VAL A 259      -0.379  23.337 -19.883  1.00 53.97           C
ANISOU 3932  CG1 VAL A 259     4076  10359   6072    357    -85   2222       C
ATOM   3933  CG2 VAL A 259       1.759  22.927 -18.699  1.00 56.37           C
ANISOU 3933  CG2 VAL A 259     4288  10876   6254    332   -129   2182       C
ATOM   3934  H   VAL A 259      -0.181  21.690 -15.795  1.00 65.74           H
ATOM   3935  HA  VAL A 259      -0.284  24.250 -17.309  1.00 64.21           H
ATOM   3936  HB  VAL A 259       0.096  21.589 -18.735  1.00 65.18           H
ATOM   3937 HG11 VAL A 259       0.132  23.006 -20.787  1.00 64.77           H
ATOM   3938 HG12 VAL A 259      -1.430  23.062 -19.975  1.00 64.77           H
ATOM   3939 HG13 VAL A 259      -0.298  24.421 -19.802  1.00 64.77           H
ATOM   3940 HG21 VAL A 259       2.156  22.656 -19.678  1.00 67.64           H
ATOM   3941 HG22 VAL A 259       1.967  23.976 -18.499  1.00 67.64           H
ATOM   3942 HG23 VAL A 259       2.264  22.321 -17.947  1.00 67.64           H
ATOM   3943  N   GLY A 260      -2.737  23.912 -17.317  1.00 55.95           N
ANISOU 3943  N   GLY A 260     4828   9658   6771    198    -76   1966       N
ATOM   3944  CA  GLY A 260      -4.190  23.759 -17.236  1.00 55.88           C
ANISOU 3944  CA  GLY A 260     4955   9430   6845    239    -53   1870       C
ATOM   3945  C   GLY A 260      -4.912  23.695 -18.584  1.00 56.51           C
ANISOU 3945  C   GLY A 260     4960   9605   6904    284    -33   1960       C
ATOM   3946  O   GLY A 260      -4.453  24.235 -19.590  1.00 56.59           O
ANISOU 3946  O   GLY A 260     4810   9831   6859    257    -36   2130       O
ATOM   3947  H   GLY A 260      -2.335  24.844 -17.317  1.00 67.13           H
ATOM   3948  HA2 GLY A 260      -4.409  22.837 -16.698  1.00 67.05           H
ATOM   3949  HA3 GLY A 260      -4.618  24.571 -16.652  1.00 67.05           H
ATOM   3950  N   TYR A 261      -6.161  23.242 -18.530  1.00 55.21           N
ANISOU 3950  N   TYR A 261     4902   9301   6775    349    -18   1855       N
ATOM   3951  CA  TYR A 261      -7.171  23.428 -19.570  1.00 50.47           C
ANISOU 3951  CA  TYR A 261     4256   8734   6185    383     -1   1923       C
ATOM   3952  C   TYR A 261      -8.193  24.456 -19.079  1.00 48.59           C
ANISOU 3952  C   TYR A 261     4096   8236   6130    288     16   1961       C
ATOM   3953  O   TYR A 261      -8.800  24.268 -18.027  1.00 44.68           O
ANISOU 3953  O   TYR A 261     3728   7543   5706    278     25   1838       O
ATOM   3954  CB  TYR A 261      -7.835  22.092 -19.914  1.00 55.16           C
ANISOU 3954  CB  TYR A 261     4906   9364   6690    527    -17   1777       C
ATOM   3955  CG  TYR A 261      -6.917  21.090 -20.590  1.00 58.49           C
ANISOU 3955  CG  TYR A 261     5254  10044   6924    672    -63   1707       C
ATOM   3956  CD1 TYR A 261      -5.941  20.406 -19.841  1.00 60.95           C
ANISOU 3956  CD1 TYR A 261     5615  10366   7176    715   -102   1597       C
ATOM   3957  CD2 TYR A 261      -7.024  20.870 -21.978  1.00 61.58           C
ANISOU 3957  CD2 TYR A 261     5524  10685   7186    788    -78   1739       C
ATOM   3958  CE1 TYR A 261      -5.053  19.526 -20.482  1.00 60.72           C
ANISOU 3958  CE1 TYR A 261     5520  10579   6970    882   -161   1509       C
ATOM   3959  CE2 TYR A 261      -6.166  19.958 -22.615  1.00 62.46           C
ANISOU 3959  CE2 TYR A 261     5564  11061   7108    960   -134   1644       C
ATOM   3960  CZ  TYR A 261      -5.177  19.284 -21.869  1.00 62.19           C
ANISOU 3960  CZ  TYR A 261     5585  11021   7023   1014   -179   1524       C
ATOM   3961  OH  TYR A 261      -4.353  18.391 -22.467  1.00 63.30           O
ANISOU 3961  OH  TYR A 261     5653  11429   6969   1219   -251   1407       O
ATOM   3962  H   TYR A 261      -6.484  22.889 -17.636  1.00 66.25           H
ATOM   3963  HA  TYR A 261      -6.700  23.799 -20.477  1.00 60.56           H
ATOM   3964  HB2 TYR A 261      -8.263  21.644 -19.018  1.00 66.20           H
ATOM   3965  HB3 TYR A 261      -8.645  22.298 -20.603  1.00 66.20           H
ATOM   3966  HD1 TYR A 261      -5.857  20.576 -18.776  1.00 73.14           H
ATOM   3967  HD2 TYR A 261      -7.768  21.398 -22.560  1.00 73.89           H
ATOM   3968  HE1 TYR A 261      -4.275  19.025 -19.934  1.00 72.86           H
ATOM   3969  HE2 TYR A 261      -6.251  19.776 -23.676  1.00 74.95           H
ATOM   3970  HH  TYR A 261      -4.804  17.914 -23.170  1.00 75.96           H
ATOM   3971  N   GLU A 262      -8.324  25.581 -19.771  1.00 47.42           N
ANISOU 3971  N   GLU A 262     3864   8104   6048    227     11   2132       N
ATOM   3972  CA  GLU A 262      -9.063  26.759 -19.309  1.00 49.82           C
ANISOU 3972  CA  GLU A 262     4235   8157   6538    147     -4   2174       C
ATOM   3973  C   GLU A 262     -10.305  27.045 -20.161  1.00 50.89           C
ANISOU 3973  C   GLU A 262     4348   8278   6708    193     11   2230       C
ATOM   3974  O   GLU A 262     -10.291  26.917 -21.384  1.00 51.52           O
ANISOU 3974  O   GLU A 262     4321   8571   6684    243     22   2319       O
ATOM   3975  CB  GLU A 262      -8.092  27.947 -19.244  1.00 49.80           C
ANISOU 3975  CB  GLU A 262     4172   8114   6637      5    -69   2347       C
ATOM   3976  CG  GLU A 262      -8.739  29.240 -18.733  1.00 54.00           C
ANISOU 3976  CG  GLU A 262     4788   8353   7377    -58   -128   2371       C
ATOM   3977  CD  GLU A 262      -7.719  30.335 -18.389  1.00 50.75           C
ANISOU 3977  CD  GLU A 262     4350   7842   7091   -212   -233   2512       C
ATOM   3978  OE1 GLU A 262      -6.586  29.986 -17.981  1.00 55.76           O
ANISOU 3978  OE1 GLU A 262     4884   8664   7638   -283   -242   2605       O
ATOM   3979  OE2 GLU A 262      -8.194  31.440 -18.064  1.00 52.23           O
ANISOU 3979  OE2 GLU A 262     4615   7765   7466   -259   -321   2526       O
ATOM   3980  H   GLU A 262      -7.792  25.677 -20.632  1.00 56.90           H
ATOM   3981  HA  GLU A 262      -9.411  26.585 -18.293  1.00 59.79           H
ATOM   3982  HB2 GLU A 262      -7.298  27.655 -18.560  1.00 59.76           H
ATOM   3983  HB3 GLU A 262      -7.659  28.125 -20.231  1.00 59.76           H
ATOM   3984  HG2 GLU A 262      -9.423  29.621 -19.491  1.00 64.80           H
ATOM   3985  HG3 GLU A 262      -9.314  29.011 -17.835  1.00 64.80           H
ATOM   3986  N   THR A 263     -11.382  27.497 -19.525  1.00 47.36           N
ANISOU 3986  N   THR A 263     3997   7602   6396    192      8   2170       N
ATOM   3987  CA  THR A 263     -12.541  28.083 -20.208  1.00 47.20           C
ANISOU 3987  CA  THR A 263     3958   7542   6433    233     12   2228       C
ATOM   3988  C   THR A 263     -13.271  29.058 -19.293  1.00 42.90           C
ANISOU 3988  C   THR A 263     3517   6741   6044    237    -12   2147       C
ATOM   3989  O   THR A 263     -13.126  28.995 -18.068  1.00 46.27           O
ANISOU 3989  O   THR A 263     4031   7058   6492    235    -10   2005       O
ATOM   3990  CB  THR A 263     -13.465  26.980 -20.738  1.00 48.60           C
ANISOU 3990  CB  THR A 263     4122   7852   6490    336     63   2143       C
ATOM   3991  OG1 THR A 263     -14.425  27.514 -21.622  1.00 48.79           O
ANISOU 3991  OG1 THR A 263     4091   7898   6548    370     61   2241       O
ATOM   3992  CG2 THR A 263     -14.212  26.217 -19.643  1.00 44.93           C
ANISOU 3992  CG2 THR A 263     3766   7275   6030    373     93   1956       C
ATOM   3993  H   THR A 263     -11.375  27.523 -18.510  1.00 56.83           H
ATOM   3994  HA  THR A 263     -12.182  28.650 -21.069  1.00 56.64           H
ATOM   3995  HB  THR A 263     -12.854  26.284 -21.302  1.00 58.32           H
ATOM   3996  HG1 THR A 263     -14.652  26.815 -22.241  1.00 58.55           H
ATOM   3997 HG21 THR A 263     -14.603  25.287 -20.047  1.00 53.91           H
ATOM   3998 HG22 THR A 263     -13.530  25.979 -18.828  1.00 53.91           H
ATOM   3999 HG23 THR A 263     -15.030  26.823 -19.256  1.00 53.91           H
ATOM   4000  N   VAL A 264     -14.130  29.890 -19.873  1.00 45.25           N
ANISOU 4000  N   VAL A 264     3796   6962   6434    261    -41   2230       N
ATOM   4001  CA  VAL A 264     -15.174  30.612 -19.143  1.00 47.37           C
ANISOU 4001  CA  VAL A 264     4148   7019   6829    317    -70   2132       C
ATOM   4002  C   VAL A 264     -16.519  30.099 -19.651  1.00 45.01           C
ANISOU 4002  C   VAL A 264     3824   6799   6481    418    -11   2091       C
ATOM   4003  O   VAL A 264     -16.761  30.086 -20.862  1.00 46.55           O
ANISOU 4003  O   VAL A 264     3941   7083   6664    429    -15   2226       O
ATOM   4004  CB  VAL A 264     -15.016  32.141 -19.257  1.00 48.24           C
ANISOU 4004  CB  VAL A 264     4272   6933   7123    267   -195   2262       C
ATOM   4005  CG1 VAL A 264     -16.109  32.866 -18.465  1.00 49.30           C
ANISOU 4005  CG1 VAL A 264     4494   6861   7378    377   -243   2124       C
ATOM   4006  CG2 VAL A 264     -13.664  32.616 -18.703  1.00 48.30           C
ANISOU 4006  CG2 VAL A 264     4300   6862   7190    144   -273   2309       C
ATOM   4007  H   VAL A 264     -14.297  29.748 -20.864  1.00 54.30           H
ATOM   4008  HA  VAL A 264     -15.108  30.371 -18.087  1.00 56.84           H
ATOM   4009  HB  VAL A 264     -15.091  32.432 -20.305  1.00 57.88           H
ATOM   4010 HG11 VAL A 264     -15.945  33.942 -18.525  1.00 59.16           H
ATOM   4011 HG12 VAL A 264     -17.088  32.651 -18.890  1.00 59.16           H
ATOM   4012 HG13 VAL A 264     -16.086  32.561 -17.419  1.00 59.16           H
ATOM   4013 HG21 VAL A 264     -13.586  33.702 -18.794  1.00 57.96           H
ATOM   4014 HG22 VAL A 264     -13.570  32.344 -17.655  1.00 57.96           H
ATOM   4015 HG23 VAL A 264     -12.843  32.175 -19.268  1.00 57.96           H
ATOM   4016  N   VAL A 265     -17.301  29.510 -18.744  1.00 45.47           N
ANISOU 4016  N   VAL A 265     3930   6847   6498    484     42   1919       N
ATOM   4017  CA  VAL A 265     -18.685  29.091 -19.007  1.00 48.65           C
ANISOU 4017  CA  VAL A 265     4298   7337   6852    563     93   1880       C
ATOM   4018  C   VAL A 265     -19.656  30.211 -18.620  1.00 47.35           C
ANISOU 4018  C   VAL A 265     4153   7043   6795    655     59   1833       C
ATOM   4019  O   VAL A 265     -19.509  30.819 -17.553  1.00 45.89           O
ANISOU 4019  O   VAL A 265     4037   6714   6686    683     13   1738       O
ATOM   4020  CB  VAL A 265     -19.061  27.763 -18.314  1.00 40.83           C
ANISOU 4020  CB  VAL A 265     3323   6448   5743    563    158   1756       C
ATOM   4021  CG1 VAL A 265     -18.235  26.586 -18.842  1.00 45.88           C
ANISOU 4021  CG1 VAL A 265     3949   7203   6280    507    162   1786       C
ATOM   4022  CG2 VAL A 265     -18.926  27.755 -16.787  1.00 44.95           C
ANISOU 4022  CG2 VAL A 265     3914   6890   6276    569    164   1624       C
ATOM   4023  H   VAL A 265     -17.008  29.556 -17.773  1.00 54.56           H
ATOM   4024  HA  VAL A 265     -18.790  28.919 -20.078  1.00 58.39           H
ATOM   4025  HB  VAL A 265     -20.103  27.551 -18.544  1.00 49.00           H
ATOM   4026 HG11 VAL A 265     -18.610  25.665 -18.401  1.00 55.05           H
ATOM   4027 HG12 VAL A 265     -18.334  26.520 -19.925  1.00 55.05           H
ATOM   4028 HG13 VAL A 265     -17.187  26.714 -18.577  1.00 55.05           H
ATOM   4029 HG21 VAL A 265     -19.231  26.779 -16.413  1.00 53.95           H
ATOM   4030 HG22 VAL A 265     -17.896  27.943 -16.495  1.00 53.95           H
ATOM   4031 HG23 VAL A 265     -19.573  28.511 -16.349  1.00 53.95           H
ATOM   4032  N   GLY A 266     -20.660  30.444 -19.463  1.00 44.72           N
ANISOU 4032  N   GLY A 266     3760   6766   6464    721     68   1886       N
ATOM   4033  CA  GLY A 266     -21.801  31.338 -19.251  1.00 47.85           C
ANISOU 4033  CA  GLY A 266     4163   7072   6946    841     33   1830       C
ATOM   4034  C   GLY A 266     -23.163  30.624 -19.295  1.00 49.87           C
ANISOU 4034  C   GLY A 266     4347   7494   7106    913    108   1775       C
ATOM   4035  O   GLY A 266     -23.211  29.400 -19.425  1.00 49.64           O
ANISOU 4035  O   GLY A 266     4280   7620   6962    852    171   1777       O
ATOM   4036  H   GLY A 266     -20.669  29.913 -20.332  1.00 53.66           H
ATOM   4037  HA2 GLY A 266     -21.702  31.854 -18.297  1.00 57.42           H
ATOM   4038  HA3 GLY A 266     -21.805  32.080 -20.048  1.00 57.42           H
ATOM   4039  N   PRO A 267     -24.278  31.364 -19.154  1.00 46.97           N
ANISOU 4039  N   PRO A 267     3959   7099   6789   1045     84   1723       N
ATOM   4040  CA  PRO A 267     -25.644  30.830 -19.221  1.00 45.94           C
ANISOU 4040  CA  PRO A 267     3736   7157   6562   1111    152   1682       C
ATOM   4041  C   PRO A 267     -25.879  29.912 -20.435  1.00 48.11           C
ANISOU 4041  C   PRO A 267     3939   7568   6772   1038    183   1806       C
ATOM   4042  O   PRO A 267     -25.663  30.316 -21.573  1.00 48.46           O
ANISOU 4042  O   PRO A 267     3968   7577   6867   1032    139   1935       O
ATOM   4043  CB  PRO A 267     -26.542  32.076 -19.270  1.00 46.34           C
ANISOU 4043  CB  PRO A 267     3774   7133   6701   1284     92   1640       C
ATOM   4044  CG  PRO A 267     -25.740  33.105 -18.475  1.00 49.41           C
ANISOU 4044  CG  PRO A 267     4274   7288   7213   1324     -6   1570       C
ATOM   4045  CD  PRO A 267     -24.311  32.801 -18.915  1.00 47.43           C
ANISOU 4045  CD  PRO A 267     4078   6947   6996   1150    -26   1688       C
ATOM   4046  HA  PRO A 267     -25.853  30.279 -18.303  1.00 55.13           H
ATOM   4047  HB2 PRO A 267     -26.646  32.430 -20.297  1.00 55.61           H
ATOM   4048  HB3 PRO A 267     -27.524  31.896 -18.834  1.00 55.61           H
ATOM   4049  HG2 PRO A 267     -26.029  34.128 -18.719  1.00 59.29           H
ATOM   4050  HG3 PRO A 267     -25.845  32.915 -17.407  1.00 59.29           H
ATOM   4051  HD2 PRO A 267     -24.093  33.328 -19.846  1.00 56.92           H
ATOM   4052  HD3 PRO A 267     -23.607  33.102 -18.138  1.00 56.92           H
ATOM   4053  N   GLY A 268     -26.329  28.675 -20.203  1.00 47.76           N
ANISOU 4053  N   GLY A 268     3848   7686   6612    981    242   1771       N
ATOM   4054  CA  GLY A 268     -26.579  27.687 -21.266  1.00 46.94           C
ANISOU 4054  CA  GLY A 268     3684   7708   6441    922    246   1848       C
ATOM   4055  C   GLY A 268     -25.400  26.755 -21.592  1.00 50.02           C
ANISOU 4055  C   GLY A 268     4122   8103   6781    814    233   1868       C
ATOM   4056  O   GLY A 268     -25.648  25.596 -21.932  1.00 48.10           O
ANISOU 4056  O   GLY A 268     3843   7965   6466    772    218   1883       O
ATOM   4057  H   GLY A 268     -26.402  28.363 -19.242  1.00 57.31           H
ATOM   4058  HA2 GLY A 268     -27.435  27.073 -20.992  1.00 56.33           H
ATOM   4059  HA3 GLY A 268     -26.839  28.213 -22.186  1.00 56.33           H
ATOM   4060  N   ASP A 269     -24.153  27.148 -21.295  1.00 48.65           N
ANISOU 4060  N   ASP A 269     4026   7819   6641    778    222   1858       N
ATOM   4061  CA  ASP A 269     -22.982  26.262 -21.411  1.00 47.52           C
ANISOU 4061  CA  ASP A 269     3918   7698   6439    701    206   1867       C
ATOM   4062  C   ASP A 269     -23.030  25.090 -20.415  1.00 48.18           C
ANISOU 4062  C   ASP A 269     4045   7801   6460    638    219   1772       C
ATOM   4063  O   ASP A 269     -23.187  25.286 -19.201  1.00 49.84           O
ANISOU 4063  O   ASP A 269     4273   7984   6679    638    251   1707       O
ATOM   4064  CB  ASP A 269     -21.656  26.997 -21.170  1.00 48.19           C
ANISOU 4064  CB  ASP A 269     4049   7681   6580    677    184   1914       C
ATOM   4065  CG  ASP A 269     -21.372  28.100 -22.174  1.00 51.97           C
ANISOU 4065  CG  ASP A 269     4481   8141   7125    706    148   2056       C
ATOM   4066  OD1 ASP A 269     -21.396  27.714 -23.365  1.00 53.85           O
ANISOU 4066  OD1 ASP A 269     4644   8491   7323    743    145   2124       O
ATOM   4067  OD2 ASP A 269     -20.494  28.928 -21.841  1.00 54.21           O
ANISOU 4067  OD2 ASP A 269     4799   8296   7503    683    109   2111       O
ATOM   4068  H   ASP A 269     -24.018  28.077 -20.917  1.00 58.38           H
ATOM   4069  HA  ASP A 269     -22.976  25.857 -22.428  1.00 57.02           H
ATOM   4070  HB2 ASP A 269     -21.635  27.408 -20.168  1.00 57.83           H
ATOM   4071  HB3 ASP A 269     -20.847  26.278 -21.273  1.00 57.83           H
ATOM   4072  N   VAL A 270     -22.610  23.905 -20.874  1.00 43.65           N
ANISOU 4072  N   VAL A 270     3486   7284   5817    593    180   1764       N
ATOM   4073  CA  VAL A 270     -22.371  22.718 -20.036  1.00 42.14           C
ANISOU 4073  CA  VAL A 270     3348   7084   5578    522    158   1697       C
ATOM   4074  C   VAL A 270     -20.929  22.240 -20.196  1.00 44.75           C
ANISOU 4074  C   VAL A 270     3738   7392   5872    511    118   1675       C
ATOM   4075  O   VAL A 270     -20.581  21.628 -21.206  1.00 41.38           O
ANISOU 4075  O   VAL A 270     3289   7036   5399    550     70   1689       O
ATOM   4076  CB  VAL A 270     -23.379  21.595 -20.353  1.00 42.83           C
ANISOU 4076  CB  VAL A 270     3402   7243   5627    483    104   1694       C
ATOM   4077  CG1 VAL A 270     -23.133  20.329 -19.517  1.00 42.56           C
ANISOU 4077  CG1 VAL A 270     3436   7172   5562    392     45   1654       C
ATOM   4078  CG2 VAL A 270     -24.820  22.037 -20.081  1.00 46.76           C
ANISOU 4078  CG2 VAL A 270     3816   7808   6144    492    150   1724       C
ATOM   4079  H   VAL A 270     -22.481  23.818 -21.881  1.00 52.39           H
ATOM   4080  HA  VAL A 270     -22.514  22.993 -18.994  1.00 50.56           H
ATOM   4081  HB  VAL A 270     -23.301  21.328 -21.406  1.00 51.39           H
ATOM   4082 HG11 VAL A 270     -23.883  19.577 -19.762  1.00 51.07           H
ATOM   4083 HG12 VAL A 270     -22.153  19.911 -19.746  1.00 51.07           H
ATOM   4084 HG13 VAL A 270     -23.190  20.565 -18.454  1.00 51.07           H
ATOM   4085 HG21 VAL A 270     -25.499  21.210 -20.276  1.00 56.12           H
ATOM   4086 HG22 VAL A 270     -24.927  22.356 -19.048  1.00 56.12           H
ATOM   4087 HG23 VAL A 270     -25.084  22.870 -20.735  1.00 56.12           H
ATOM   4088  N   LEU A 271     -20.101  22.417 -19.164  1.00 45.97           N
ANISOU 4088  N   LEU A 271     3956   7476   6033    474    135   1635       N
ATOM   4089  CA  LEU A 271     -18.760  21.823 -19.104  1.00 39.39           C
ANISOU 4089  CA  LEU A 271     3173   6634   5158    467     97   1608       C
ATOM   4090  C   LEU A 271     -18.845  20.369 -18.608  1.00 40.14           C
ANISOU 4090  C   LEU A 271     3332   6712   5207    422     31   1546       C
ATOM   4091  O   LEU A 271     -19.240  20.116 -17.469  1.00 37.31           O
ANISOU 4091  O   LEU A 271     3000   6317   4860    359     46   1534       O
ATOM   4092  CB  LEU A 271     -17.840  22.727 -18.255  1.00 38.44           C
ANISOU 4092  CB  LEU A 271     3086   6442   5080    449    138   1606       C
ATOM   4093  CG  LEU A 271     -16.455  22.154 -17.896  1.00 38.61           C
ANISOU 4093  CG  LEU A 271     3154   6463   5052    432    106   1572       C
ATOM   4094  CD1 LEU A 271     -15.527  22.007 -19.099  1.00 40.83           C
ANISOU 4094  CD1 LEU A 271     3380   6859   5274    482     71   1616       C
ATOM   4095  CD2 LEU A 271     -15.761  23.089 -16.904  1.00 38.55           C
ANISOU 4095  CD2 LEU A 271     3178   6372   5095    399    137   1561       C
ATOM   4096  H   LEU A 271     -20.485  22.835 -18.323  1.00 55.16           H
ATOM   4097  HA  LEU A 271     -18.343  21.800 -20.111  1.00 47.26           H
ATOM   4098  HB2 LEU A 271     -17.689  23.658 -18.797  1.00 46.13           H
ATOM   4099  HB3 LEU A 271     -18.356  22.972 -17.328  1.00 46.13           H
ATOM   4100  HG  LEU A 271     -16.572  21.183 -17.422  1.00 46.33           H
ATOM   4101 HD11 LEU A 271     -15.978  21.355 -19.844  1.00  0.00           H
ATOM   4102 HD12 LEU A 271     -15.320  22.979 -19.544  1.00  0.00           H
ATOM   4103 HD13 LEU A 271     -14.593  21.546 -18.778  1.00  0.00           H
ATOM   4104 HD21 LEU A 271     -16.349  23.156 -15.989  1.00  0.00           H
ATOM   4105 HD22 LEU A 271     -15.654  24.080 -17.345  1.00  0.00           H
ATOM   4106 HD23 LEU A 271     -14.775  22.696 -16.669  1.00  0.00           H
ATOM   4107  N   TYR A 272     -18.363  19.414 -19.402  1.00 42.54           N
ANISOU 4107  N   TYR A 272     3655   7052   5454    463    -55   1509       N
ATOM   4108  CA  TYR A 272     -17.986  18.099 -18.881  1.00 43.10           C
ANISOU 4108  CA  TYR A 272     3809   7070   5498    434   -160   1446       C
ATOM   4109  C   TYR A 272     -16.682  18.219 -18.077  1.00 44.78           C
ANISOU 4109  C   TYR A 272     4078   7251   5685    436   -153   1410       C
ATOM   4110  O   TYR A 272     -15.659  18.675 -18.592  1.00 46.68           O
ANISOU 4110  O   TYR A 272     4297   7563   5878    510   -156   1393       O
ATOM   4111  CB  TYR A 272     -17.878  17.085 -20.031  1.00 40.61           C
ANISOU 4111  CB  TYR A 272     3499   6797   5135    511   -288   1388       C
ATOM   4112  CG  TYR A 272     -17.456  15.671 -19.637  1.00 39.60           C
ANISOU 4112  CG  TYR A 272     3475   6582   4990    510   -438   1305       C
ATOM   4113  CD1 TYR A 272     -18.053  14.997 -18.549  1.00 44.12           C
ANISOU 4113  CD1 TYR A 272     4113   7035   5615    385   -491   1335       C
ATOM   4114  CD2 TYR A 272     -16.463  15.016 -20.389  1.00 43.36           C
ANISOU 4114  CD2 TYR A 272     3977   7107   5391    641   -539   1205       C
ATOM   4115  CE1 TYR A 272     -17.607  13.712 -18.181  1.00 46.87           C
ANISOU 4115  CE1 TYR A 272     4568   7274   5967    375   -655   1280       C
ATOM   4116  CE2 TYR A 272     -16.032  13.725 -20.043  1.00 43.20           C
ANISOU 4116  CE2 TYR A 272     4066   6982   5365    663   -704   1116       C
ATOM   4117  CZ  TYR A 272     -16.586  13.075 -18.922  1.00 43.04           C
ANISOU 4117  CZ  TYR A 272     4128   6801   5424    522   -769   1160       C
ATOM   4118  OH  TYR A 272     -16.110  11.860 -18.551  1.00 41.51           O
ANISOU 4118  OH  TYR A 272     4054   6474   5244    535   -959   1090       O
ATOM   4119  H   TYR A 272     -18.024  19.683 -20.322  1.00 51.04           H
ATOM   4120  HA  TYR A 272     -18.770  17.754 -18.209  1.00 51.72           H
ATOM   4121  HB2 TYR A 272     -18.842  17.022 -20.531  1.00 48.73           H
ATOM   4122  HB3 TYR A 272     -17.163  17.471 -20.756  1.00 48.73           H
ATOM   4123  HD1 TYR A 272     -18.851  15.467 -17.991  1.00 52.94           H
ATOM   4124  HD2 TYR A 272     -16.015  15.505 -21.246  1.00 52.03           H
ATOM   4125  HE1 TYR A 272     -18.048  13.198 -17.344  1.00 56.24           H
ATOM   4126  HE2 TYR A 272     -15.257  13.236 -20.615  1.00 51.84           H
ATOM   4127  HH  TYR A 272     -16.108  11.746 -17.590  1.00 49.81           H
ATOM   4128  N   ILE A 273     -16.729  17.841 -16.799  1.00 43.92           N
ANISOU 4128  N   ILE A 273     4025   7068   5596    354   -143   1410       N
ATOM   4129  CA  ILE A 273     -15.550  17.619 -15.956  1.00 40.08           C
ANISOU 4129  CA  ILE A 273     3599   6549   5081    351   -152   1371       C
ATOM   4130  C   ILE A 273     -15.454  16.098 -15.741  1.00 45.34           C
ANISOU 4130  C   ILE A 273     4352   7148   5726    337   -295   1331       C
ATOM   4131  O   ILE A 273     -16.289  15.541 -15.013  1.00 46.68           O
ANISOU 4131  O   ILE A 273     4556   7259   5921    237   -328   1374       O
ATOM   4132  CB  ILE A 273     -15.629  18.405 -14.622  1.00 41.84           C
ANISOU 4132  CB  ILE A 273     3824   6745   5328    285    -57   1392       C
ATOM   4133  CG1 ILE A 273     -15.843  19.923 -14.842  1.00 41.77           C
ANISOU 4133  CG1 ILE A 273     3746   6758   5365    312     42   1419       C
ATOM   4134  CG2 ILE A 273     -14.358  18.144 -13.788  1.00 43.25           C
ANISOU 4134  CG2 ILE A 273     4061   6900   5473    284    -74   1350       C
ATOM   4135  CD1 ILE A 273     -15.990  20.775 -13.571  1.00 42.63           C
ANISOU 4135  CD1 ILE A 273     3859   6839   5499    284    113   1402       C
ATOM   4136  H   ILE A 273     -17.614  17.476 -16.456  1.00 52.71           H
ATOM   4137  HA  ILE A 273     -14.662  17.975 -16.475  1.00 48.10           H
ATOM   4138  HB  ILE A 273     -16.481  18.033 -14.057  1.00 50.21           H
ATOM   4139 HG12 ILE A 273     -15.018  20.323 -15.429  1.00 50.12           H
ATOM   4140 HG13 ILE A 273     -16.760  20.061 -15.414  1.00 50.12           H
ATOM   4141 HG21 ILE A 273     -14.459  18.616 -12.818  1.00 51.90           H
ATOM   4142 HG22 ILE A 273     -14.219  17.074 -13.624  1.00 51.90           H
ATOM   4143 HG23 ILE A 273     -13.480  18.537 -14.304  1.00 51.90           H
ATOM   4144 HD11 ILE A 273     -16.249  21.796 -13.853  1.00 51.16           H
ATOM   4145 HD12 ILE A 273     -16.785  20.376 -12.941  1.00 51.16           H
ATOM   4146 HD13 ILE A 273     -15.055  20.803 -13.014  1.00 51.16           H
ATOM   4147  N   PRO A 274     -14.486  15.403 -16.365  1.00 47.20           N
ANISOU 4147  N   PRO A 274     4622   7399   5914    438   -398   1255       N
ATOM   4148  CA  PRO A 274     -14.335  13.962 -16.190  1.00 43.71           C
ANISOU 4148  CA  PRO A 274     4284   6853   5471    442   -575   1203       C
ATOM   4149  C   PRO A 274     -13.903  13.609 -14.755  1.00 46.91           C
ANISOU 4149  C   PRO A 274     4758   7185   5880    365   -577   1226       C
ATOM   4150  O   PRO A 274     -13.247  14.398 -14.066  1.00 48.87           O
ANISOU 4150  O   PRO A 274     4980   7485   6104    359   -461   1234       O
ATOM   4151  CB  PRO A 274     -13.327  13.496 -17.248  1.00 42.57           C
ANISOU 4151  CB  PRO A 274     4142   6783   5250    619   -671   1087       C
ATOM   4152  CG  PRO A 274     -13.083  14.711 -18.150  1.00 41.12           C
ANISOU 4152  CG  PRO A 274     3832   6770   5021    681   -537   1114       C
ATOM   4153  CD  PRO A 274     -13.521  15.910 -17.330  1.00 40.02           C
ANISOU 4153  CD  PRO A 274     3650   6617   4939    560   -372   1218       C
ATOM   4154  HA  PRO A 274     -15.295  13.495 -16.400  1.00 52.45           H
ATOM   4155  HB2 PRO A 274     -12.405  13.178 -16.777  1.00 51.08           H
ATOM   4156  HB3 PRO A 274     -13.716  12.661 -17.828  1.00 51.08           H
ATOM   4157  HG2 PRO A 274     -12.037  14.819 -18.430  1.00 49.34           H
ATOM   4158  HG3 PRO A 274     -13.698  14.634 -19.045  1.00 49.34           H
ATOM   4159  HD2 PRO A 274     -12.661  16.324 -16.802  1.00 48.02           H
ATOM   4160  HD3 PRO A 274     -13.954  16.656 -17.997  1.00 48.02           H
ATOM   4161  N   MET A 275     -14.205  12.393 -14.293  1.00 51.22           N
ANISOU 4161  N   MET A 275     5395   7606   6461    298   -729   1245       N
ATOM   4162  CA  MET A 275     -13.783  11.936 -12.962  1.00 52.11           C
ANISOU 4162  CA  MET A 275     5571   7659   6571    215   -748   1292       C
ATOM   4163  C   MET A 275     -12.251  11.956 -12.810  1.00 45.37           C
ANISOU 4163  C   MET A 275     4748   6835   5655    331   -749   1200       C
ATOM   4164  O   MET A 275     -11.502  11.639 -13.732  1.00 45.53           O
ANISOU 4164  O   MET A 275     4779   6883   5636    481   -830   1094       O
ATOM   4165  CB  MET A 275     -14.374  10.561 -12.614  1.00 53.35           C
ANISOU 4165  CB  MET A 275     5824   7661   6785    124   -958   1347       C
ATOM   4166  CG  MET A 275     -13.879   9.416 -13.502  1.00 59.16           C
ANISOU 4166  CG  MET A 275     6653   8282   7542    252  -1187   1228       C
ATOM   4167  SD  MET A 275     -14.410   7.777 -12.930  1.00 66.64           S
ANISOU 4167  SD  MET A 275     7736   8989   8597    114  -1483   1315       S
ATOM   4168  CE  MET A 275     -13.956   6.810 -14.388  1.00 67.23           C
ANISOU 4168  CE  MET A 275     7921   8939   8686    343  -1756   1098       C
ATOM   4169  H   MET A 275     -14.761  11.783 -14.884  1.00 61.47           H
ATOM   4170  HA  MET A 275     -14.188  12.649 -12.241  1.00 62.54           H
ATOM   4171  HB2 MET A 275     -14.119  10.333 -11.578  1.00 64.02           H
ATOM   4172  HB3 MET A 275     -15.457  10.609 -12.690  1.00 64.02           H
ATOM   4173  HG2 MET A 275     -14.240   9.583 -14.515  1.00 70.99           H
ATOM   4174  HG3 MET A 275     -12.792   9.422 -13.537  1.00 70.99           H
ATOM   4175  HE1 MET A 275     -14.106   5.748 -14.208  1.00 80.68           H
ATOM   4176  HE2 MET A 275     -14.574   7.112 -15.231  1.00 80.68           H
ATOM   4177  HE3 MET A 275     -12.916   7.006 -14.645  1.00 80.68           H
ATOM   4178  N   TYR A 276     -11.786  12.274 -11.601  1.00 46.29           N
ANISOU 4178  N   TYR A 276     4865   6975   5747    270   -660   1238       N
ATOM   4179  CA  TYR A 276     -10.384  12.516 -11.238  1.00 46.46           C
ANISOU 4179  CA  TYR A 276     4907   7037   5710    350   -651   1172       C
ATOM   4180  C   TYR A 276      -9.681  13.689 -11.946  1.00 42.52           C
ANISOU 4180  C   TYR A 276     4312   6674   5171    439   -532   1122       C
ATOM   4181  O   TYR A 276      -8.586  14.038 -11.504  1.00 45.89           O
ANISOU 4181  O   TYR A 276     4730   7165   5543    502   -526   1075       O
ATOM   4182  CB  TYR A 276      -9.556  11.224 -11.296  1.00 45.02           C
ANISOU 4182  CB  TYR A 276     4826   6771   5510    454   -855   1095       C
ATOM   4183  CG  TYR A 276     -10.004  10.132 -10.331  1.00 51.21           C
ANISOU 4183  CG  TYR A 276     5716   7402   6338    347   -996   1173       C
ATOM   4184  CD1 TYR A 276      -9.471  10.106  -9.028  1.00 50.69           C
ANISOU 4184  CD1 TYR A 276     5676   7342   6241    283   -965   1225       C
ATOM   4185  CD2 TYR A 276     -10.945   9.156 -10.720  1.00 54.57           C
ANISOU 4185  CD2 TYR A 276     6211   7684   6840    297  -1174   1211       C
ATOM   4186  CE1 TYR A 276      -9.902   9.138  -8.100  1.00 54.96           C
ANISOU 4186  CE1 TYR A 276     6303   7765   6816    171  -1099   1332       C
ATOM   4187  CE2 TYR A 276     -11.371   8.178  -9.799  1.00 55.25           C
ANISOU 4187  CE2 TYR A 276     6387   7628   6978    169  -1324   1324       C
ATOM   4188  CZ  TYR A 276     -10.874   8.188  -8.475  1.00 55.63           C
ANISOU 4188  CZ  TYR A 276     6452   7700   6985    105  -1281   1394       C
ATOM   4189  OH  TYR A 276     -11.369   7.311  -7.561  1.00 59.43           O
ANISOU 4189  OH  TYR A 276     7011   8059   7511    -35  -1436   1539       O
ATOM   4190  H   TYR A 276     -12.475  12.489 -10.889  1.00 55.55           H
ATOM   4191  HA  TYR A 276     -10.399  12.808 -10.191  1.00 55.76           H
ATOM   4192  HB2 TYR A 276      -9.570  10.851 -12.317  1.00 54.03           H
ATOM   4193  HB3 TYR A 276      -8.518  11.464 -11.065  1.00 54.03           H
ATOM   4194  HD1 TYR A 276      -8.745  10.852  -8.736  1.00 60.82           H
ATOM   4195  HD2 TYR A 276     -11.368   9.186 -11.717  1.00 65.49           H
ATOM   4196  HE1 TYR A 276      -9.509   9.124  -7.097  1.00 65.95           H
ATOM   4197  HE2 TYR A 276     -12.119   7.449 -10.073  1.00 66.30           H
ATOM   4198  HH  TYR A 276     -11.410   7.698  -6.660  1.00 71.32           H
ATOM   4199  N   TRP A 277     -10.325  14.435 -12.851  1.00 45.95           N
ANISOU 4199  N   TRP A 277     4665   7163   5631    435   -446   1148       N
ATOM   4200  CA  TRP A 277      -9.784  15.725 -13.292  1.00 41.73           C
ANISOU 4200  CA  TRP A 277     4032   6748   5076    475   -336   1151       C
ATOM   4201  C   TRP A 277      -9.869  16.764 -12.172  1.00 43.46           C
ANISOU 4201  C   TRP A 277     4228   6951   5332    378   -215   1195       C
ATOM   4202  O   TRP A 277     -10.922  17.011 -11.562  1.00 39.27           O
ANISOU 4202  O   TRP A 277     3704   6371   4846    302   -166   1233       O
ATOM   4203  CB  TRP A 277     -10.437  16.218 -14.586  1.00 42.50           C
ANISOU 4203  CB  TRP A 277     4055   6905   5189    511   -308   1176       C
ATOM   4204  CG  TRP A 277      -9.976  15.505 -15.821  1.00 41.08           C
ANISOU 4204  CG  TRP A 277     3856   6816   4937    653   -410   1108       C
ATOM   4205  CD1 TRP A 277     -10.168  14.197 -16.106  1.00 42.46           C
ANISOU 4205  CD1 TRP A 277     4113   6926   5095    727   -570   1026       C
ATOM   4206  CD2 TRP A 277      -9.230  16.047 -16.954  1.00 40.44           C
ANISOU 4206  CD2 TRP A 277     3659   6924   4782    750   -375   1114       C
ATOM   4207  NE1 TRP A 277      -9.678  13.920 -17.369  1.00 47.20           N
ANISOU 4207  NE1 TRP A 277     4659   7670   5605    894   -638    946       N
ATOM   4208  CE2 TRP A 277      -9.044  15.010 -17.915  1.00 44.53           C
ANISOU 4208  CE2 TRP A 277     4186   7517   5216    907   -508   1010       C
ATOM   4209  CE3 TRP A 277      -8.708  17.317 -17.275  1.00 43.57           C
ANISOU 4209  CE3 TRP A 277     3940   7440   5174    715   -262   1208       C
ATOM   4210  CZ2 TRP A 277      -8.378  15.217 -19.128  1.00 39.35           C
ANISOU 4210  CZ2 TRP A 277     3408   7101   4442   1046   -509    992       C
ATOM   4211  CZ3 TRP A 277      -8.045  17.543 -18.497  1.00 42.53           C
ANISOU 4211  CZ3 TRP A 277     3686   7533   4942    819   -266   1227       C
ATOM   4212  CH2 TRP A 277      -7.875  16.495 -19.421  1.00 41.72           C
ANISOU 4212  CH2 TRP A 277     3576   7551   4726    990   -377   1117       C
ATOM   4213  H   TRP A 277     -11.241  14.160 -13.193  1.00 55.14           H
ATOM   4214  HA  TRP A 277      -8.725  15.592 -13.521  1.00 50.08           H
ATOM   4215  HB2 TRP A 277     -11.522  16.160 -14.511  1.00 51.00           H
ATOM   4216  HB3 TRP A 277     -10.188  17.274 -14.712  1.00 51.00           H
ATOM   4217  HD1 TRP A 277     -10.707  13.501 -15.478  1.00 50.95           H
ATOM   4218  HE1 TRP A 277     -10.002  13.137 -17.944  1.00 56.64           H
ATOM   4219  HE3 TRP A 277      -8.823  18.121 -16.570  1.00 52.28           H
ATOM   4220  HZ2 TRP A 277      -8.269  14.409 -19.840  1.00 47.22           H
ATOM   4221  HZ3 TRP A 277      -7.670  18.527 -18.742  1.00 51.04           H
ATOM   4222  HH2 TRP A 277      -7.374  16.676 -20.367  1.00 50.07           H
ATOM   4223  N   TRP A 278      -8.746  17.432 -11.938  1.00 41.50           N
ANISOU 4223  N   TRP A 278     3948   6762   5060    388   -179   1183       N
ATOM   4224  CA  TRP A 278      -8.673  18.607 -11.084  1.00 41.43           C
ANISOU 4224  CA  TRP A 278     3920   6724   5097    313    -93   1202       C
ATOM   4225  C   TRP A 278      -9.484  19.739 -11.694  1.00 39.25           C
ANISOU 4225  C   TRP A 278     3582   6437   4894    293    -27   1252       C
ATOM   4226  O   TRP A 278      -9.596  19.842 -12.910  1.00 39.56           O
ANISOU 4226  O   TRP A 278     3563   6534   4935    334    -32   1291       O
ATOM   4227  CB  TRP A 278      -7.221  19.039 -10.952  1.00 42.57           C
ANISOU 4227  CB  TRP A 278     4033   6930   5213    316    -95   1189       C
ATOM   4228  CG  TRP A 278      -6.327  18.038 -10.305  1.00 41.43           C
ANISOU 4228  CG  TRP A 278     3942   6809   4991    354   -164   1136       C
ATOM   4229  CD1 TRP A 278      -5.632  17.068 -10.940  1.00 40.99           C
ANISOU 4229  CD1 TRP A 278     3891   6820   4861    455   -249   1100       C
ATOM   4230  CD2 TRP A 278      -5.977  17.925  -8.897  1.00 40.06           C
ANISOU 4230  CD2 TRP A 278     3822   6599   4798    310   -166   1104       C
ATOM   4231  NE1 TRP A 278      -4.897  16.348 -10.020  1.00 43.20           N
ANISOU 4231  NE1 TRP A 278     4234   7089   5091    475   -309   1054       N
ATOM   4232  CE2 TRP A 278      -5.040  16.859  -8.747  1.00 42.29           C
ANISOU 4232  CE2 TRP A 278     4146   6916   5005    378   -254   1065       C
ATOM   4233  CE3 TRP A 278      -6.294  18.683  -7.751  1.00 40.94           C
ANISOU 4233  CE3 TRP A 278     3950   6665   4939    239   -111   1091       C
ATOM   4234  CZ2 TRP A 278      -4.442  16.564  -7.514  1.00 41.10           C
ANISOU 4234  CZ2 TRP A 278     4050   6751   4814    358   -282   1038       C
ATOM   4235  CZ3 TRP A 278      -5.687  18.407  -6.514  1.00 40.11           C
ANISOU 4235  CZ3 TRP A 278     3892   6567   4780    225   -135   1055       C
ATOM   4236  CH2 TRP A 278      -4.755  17.363  -6.400  1.00 40.49           C
ANISOU 4236  CH2 TRP A 278     3980   6647   4760    275   -216   1040       C
ATOM   4237  H   TRP A 278      -7.956  17.256 -12.553  1.00 49.80           H
ATOM   4238  HA  TRP A 278      -9.061  18.361 -10.100  1.00 49.71           H
ATOM   4239  HB2 TRP A 278      -6.848  19.260 -11.946  1.00 51.09           H
ATOM   4240  HB3 TRP A 278      -7.175  19.962 -10.371  1.00 51.09           H
ATOM   4241  HD1 TRP A 278      -5.621  16.905 -12.015  1.00 49.18           H
ATOM   4242  HE1 TRP A 278      -4.229  15.641 -10.302  1.00 51.84           H
ATOM   4243  HE3 TRP A 278      -6.943  19.535  -7.851  1.00 49.12           H
ATOM   4244  HZ2 TRP A 278      -3.702  15.780  -7.445  1.00 49.31           H
ATOM   4245  HZ3 TRP A 278      -5.891  19.033  -5.661  1.00 48.13           H
ATOM   4246  HH2 TRP A 278      -4.243  17.215  -5.465  1.00 48.59           H
ATOM   4247  N   HIS A 279     -10.054  20.598 -10.855  1.00 37.63           N
ANISOU 4247  N   HIS A 279     3386   6169   4742    247     27   1243       N
ATOM   4248  CA  HIS A 279     -10.757  21.801 -11.291  1.00 42.96           C
ANISOU 4248  CA  HIS A 279     4012   6811   5500    244     70   1278       C
ATOM   4249  C   HIS A 279     -10.687  22.885 -10.213  1.00 43.02           C
ANISOU 4249  C   HIS A 279     4035   6748   5561    220     87   1231       C
ATOM   4250  O   HIS A 279     -11.060  22.657  -9.062  1.00 42.35           O
ANISOU 4250  O   HIS A 279     3993   6662   5438    215     98   1164       O
ATOM   4251  CB  HIS A 279     -12.192  21.465 -11.752  1.00 40.98           C
ANISOU 4251  CB  HIS A 279     3750   6558   5263    258     95   1297       C
ATOM   4252  CG  HIS A 279     -12.952  20.441 -10.933  1.00 44.53           C
ANISOU 4252  CG  HIS A 279     4239   7019   5663    231     97   1272       C
ATOM   4253  ND1 HIS A 279     -12.690  19.080 -10.878  1.00 48.41           N
ANISOU 4253  ND1 HIS A 279     4775   7521   6097    213     34   1280       N
ATOM   4254  CD2 HIS A 279     -14.060  20.677 -10.161  1.00 38.18           C
ANISOU 4254  CD2 HIS A 279     3423   6234   4851    220    143   1255       C
ATOM   4255  CE1 HIS A 279     -13.608  18.507 -10.083  1.00 42.52           C
ANISOU 4255  CE1 HIS A 279     4043   6793   5320    163     39   1298       C
ATOM   4256  NE2 HIS A 279     -14.443  19.456  -9.628  1.00 37.73           N
ANISOU 4256  NE2 HIS A 279     3390   6219   4728    171    116   1282       N
ATOM   4257  H   HIS A 279     -10.051  20.373  -9.866  1.00 45.15           H
ATOM   4258  HA  HIS A 279     -10.235  22.189 -12.165  1.00 51.55           H
ATOM   4259  HB2 HIS A 279     -12.765  22.387 -11.822  1.00 49.18           H
ATOM   4260  HB3 HIS A 279     -12.128  21.070 -12.767  1.00 49.18           H
ATOM   4261  HD1 HIS A 279     -11.953  18.571 -11.375  1.00 58.09           H
ATOM   4262  HD2 HIS A 279     -14.544  21.637 -10.030  1.00 45.82           H
ATOM   4263  HE1 HIS A 279     -13.671  17.452  -9.843  1.00 51.03           H
ATOM   4264  HE2 HIS A 279     -15.176  19.253  -8.937  1.00  0.00           H
ATOM   4265  N   HIS A 280     -10.117  24.032 -10.590  1.00 45.26           N
ANISOU 4265  N   HIS A 280     4283   6981   5934    205     71   1272       N
ATOM   4266  CA  HIS A 280     -10.150  25.323  -9.899  1.00 45.89           C
ANISOU 4266  CA  HIS A 280     4386   6951   6100    194     47   1218       C
ATOM   4267  C   HIS A 280     -11.266  26.139 -10.561  1.00 45.67           C
ANISOU 4267  C   HIS A 280     4337   6849   6167    231     49   1243       C
ATOM   4268  O   HIS A 280     -11.256  26.272 -11.785  1.00 49.29           O
ANISOU 4268  O   HIS A 280     4745   7299   6682    211     30   1356       O
ATOM   4269  CB  HIS A 280      -8.760  25.979 -10.065  1.00 47.61           C
ANISOU 4269  CB  HIS A 280     4585   7141   6365    126    -16   1263       C
ATOM   4270  CG  HIS A 280      -8.666  27.432  -9.658  1.00 46.81           C
ANISOU 4270  CG  HIS A 280     4505   6882   6400    101    -89   1239       C
ATOM   4271  ND1 HIS A 280      -8.030  27.948  -8.537  1.00 47.92           N
ANISOU 4271  ND1 HIS A 280     4697   6951   6558     90   -141   1127       N
ATOM   4272  CD2 HIS A 280      -9.132  28.490 -10.390  1.00 48.45           C
ANISOU 4272  CD2 HIS A 280     4695   6973   6741     87   -143   1310       C
ATOM   4273  CE1 HIS A 280      -8.137  29.288  -8.576  1.00 48.95           C
ANISOU 4273  CE1 HIS A 280     4850   6912   6836     77   -237   1113       C
ATOM   4274  NE2 HIS A 280      -8.824  29.634  -9.683  1.00 49.50           N
ANISOU 4274  NE2 HIS A 280     4881   6942   6984     71   -244   1231       N
ATOM   4275  H   HIS A 280      -9.841  24.079 -11.570  1.00 54.32           H
ATOM   4276  HA  HIS A 280     -10.377  25.197  -8.839  1.00 55.07           H
ATOM   4277  HB2 HIS A 280      -8.025  25.403  -9.504  1.00 57.14           H
ATOM   4278  HB3 HIS A 280      -8.466  25.916 -11.114  1.00 57.14           H
ATOM   4279  HD2 HIS A 280      -9.614  28.449 -11.363  1.00 58.14           H
ATOM   4280  HE1 HIS A 280      -7.681  29.998  -7.887  1.00 58.74           H
ATOM   4281  HE2 HIS A 280      -9.042  30.602  -9.961  1.00 59.40           H
ATOM   4282  HD1 HIS A 280      -7.429  27.437  -7.902  1.00  0.00           H
ATOM   4283  N   ILE A 281     -12.290  26.530  -9.809  1.00 47.96           N
ANISOU 4283  N   ILE A 281     4652   7113   6457    297     71   1145       N
ATOM   4284  CA  ILE A 281     -13.453  27.266 -10.336  1.00 48.68           C
ANISOU 4284  CA  ILE A 281     4722   7155   6621    363     73   1148       C
ATOM   4285  C   ILE A 281     -13.457  28.643  -9.676  1.00 48.15           C
ANISOU 4285  C   ILE A 281     4697   6942   6655    417     -4   1043       C
ATOM   4286  O   ILE A 281     -13.428  28.704  -8.446  1.00 54.78           O
ANISOU 4286  O   ILE A 281     5574   7790   7448    452    -15    911       O
ATOM   4287  CB  ILE A 281     -14.782  26.511 -10.063  1.00 43.53           C
ANISOU 4287  CB  ILE A 281     4040   6625   5874    419    149   1114       C
ATOM   4288  CG1 ILE A 281     -14.802  25.016 -10.470  1.00 45.68           C
ANISOU 4288  CG1 ILE A 281     4297   7007   6053    359    185   1191       C
ATOM   4289  CG2 ILE A 281     -15.977  27.246 -10.693  1.00 48.20           C
ANISOU 4289  CG2 ILE A 281     4591   7189   6533    491    152   1135       C
ATOM   4290  CD1 ILE A 281     -14.648  24.724 -11.965  1.00 42.68           C
ANISOU 4290  CD1 ILE A 281     3881   6631   5704    337    170   1302       C
ATOM   4291  H   ILE A 281     -12.174  26.508  -8.799  1.00 57.55           H
ATOM   4292  HA  ILE A 281     -13.359  27.402 -11.413  1.00 58.42           H
ATOM   4293  HB  ILE A 281     -14.953  26.526  -8.989  1.00 52.23           H
ATOM   4294 HG12 ILE A 281     -14.018  24.486  -9.929  1.00 54.82           H
ATOM   4295 HG13 ILE A 281     -15.754  24.588 -10.152  1.00 54.82           H
ATOM   4296 HG21 ILE A 281     -16.885  26.662 -10.549  1.00 57.84           H
ATOM   4297 HG22 ILE A 281     -16.113  28.222 -10.223  1.00 57.84           H
ATOM   4298 HG23 ILE A 281     -15.814  27.396 -11.762  1.00 57.84           H
ATOM   4299 HD11 ILE A 281     -14.645  23.647 -12.128  1.00 51.21           H
ATOM   4300 HD12 ILE A 281     -15.495  25.138 -12.506  1.00 51.21           H
ATOM   4301 HD13 ILE A 281     -13.718  25.145 -12.343  1.00 51.21           H
ATOM   4302  N   GLU A 282     -13.565  29.725 -10.444  1.00 49.38           N
ANISOU 4302  N   GLU A 282     4849   6964   6949    431    -73   1099       N
ATOM   4303  CA  GLU A 282     -13.755  31.077  -9.892  1.00 55.09           C
ANISOU 4303  CA  GLU A 282     5630   7506   7798    501   -189    989       C
ATOM   4304  C   GLU A 282     -14.941  31.803 -10.558  1.00 56.20           C
ANISOU 4304  C   GLU A 282     5755   7567   8032    592   -222   1014       C
ATOM   4305  O   GLU A 282     -15.098  31.754 -11.779  1.00 56.42           O
ANISOU 4305  O   GLU A 282     5736   7600   8103    536   -211   1183       O
ATOM   4306  CB  GLU A 282     -12.427  31.862  -9.835  1.00 55.91           C
ANISOU 4306  CB  GLU A 282     5768   7446   8028    385   -317   1053       C
ATOM   4307  CG  GLU A 282     -11.731  32.155 -11.171  1.00 57.39           C
ANISOU 4307  CG  GLU A 282     5900   7606   8301    266   -349   1287       C
ATOM   4308  CD  GLU A 282     -10.312  32.681 -10.978  1.00 58.05           C
ANISOU 4308  CD  GLU A 282     5983   7601   8473    117   -461   1388       C
ATOM   4309  OE1 GLU A 282      -9.652  32.167 -10.035  1.00 58.30           O
ANISOU 4309  OE1 GLU A 282     6013   7723   8414     66   -430   1344       O
ATOM   4310  OE2 GLU A 282      -9.708  33.103 -11.986  1.00 59.42           O
ANISOU 4310  OE2 GLU A 282     6149   7619   8808     42   -589   1527       O
ATOM   4311  H   GLU A 282     -13.592  29.628 -11.458  1.00 59.26           H
ATOM   4312  HA  GLU A 282     -14.061  30.954  -8.850  1.00 66.11           H
ATOM   4313  HB2 GLU A 282     -12.605  32.803  -9.307  1.00 67.09           H
ATOM   4314  HB3 GLU A 282     -11.763  31.267  -9.201  1.00 67.09           H
ATOM   4315  HG2 GLU A 282     -11.646  31.240 -11.734  1.00 68.87           H
ATOM   4316  HG3 GLU A 282     -12.293  32.894 -11.720  1.00 68.87           H
ATOM   4317  N   SER A 283     -15.855  32.343  -9.736  1.00 53.63           N
ANISOU 4317  N   SER A 283     5460   7194   7723    750   -265    838       N
ATOM   4318  CA  SER A 283     -16.875  33.302 -10.191  1.00 52.79           C
ANISOU 4318  CA  SER A 283     5350   6987   7719    868   -327    832       C
ATOM   4319  C   SER A 283     -16.149  34.590 -10.569  1.00 59.81           C
ANISOU 4319  C   SER A 283     6317   7577   8833    832   -526    875       C
ATOM   4320  O   SER A 283     -15.299  35.037  -9.791  1.00 66.44           O
ANISOU 4320  O   SER A 283     7233   8270   9741    835   -649    756       O
ATOM   4321  CB  SER A 283     -17.877  33.658  -9.083  1.00 56.04           C
ANISOU 4321  CB  SER A 283     5752   7498   8043   1081   -307    612       C
ATOM   4322  OG  SER A 283     -18.620  32.549  -8.592  1.00 50.10           O
ANISOU 4322  OG  SER A 283     4910   7034   7092   1084   -137    620       O
ATOM   4323  H   SER A 283     -15.627  32.367  -8.748  1.00 64.36           H
ATOM   4324  HA  SER A 283     -17.406  32.916 -11.061  1.00 63.34           H
ATOM   4325  HB2 SER A 283     -17.340  34.096  -8.246  1.00 67.25           H
ATOM   4326  HB3 SER A 283     -18.574  34.406  -9.459  1.00 67.25           H
ATOM   4327  HG  SER A 283     -19.048  32.884  -7.789  1.00 60.12           H
ATOM   4328  N   LEU A 284     -16.447  35.175 -11.732  1.00 63.54           N
ANISOU 4328  N   LEU A 284     6766   7957   9421    789   -575   1055       N
ATOM   4329  CA  LEU A 284     -15.710  36.356 -12.203  1.00 65.55           C
ANISOU 4329  CA  LEU A 284     7077   7933   9896    697   -776   1174       C
ATOM   4330  C   LEU A 284     -15.827  37.542 -11.219  1.00 66.57           C
ANISOU 4330  C   LEU A 284     7323   7804  10168    843   -976    957       C
ATOM   4331  O   LEU A 284     -16.798  37.639 -10.462  1.00 65.36           O
ANISOU 4331  O   LEU A 284     7184   7681   9967   1066   -970    750       O
ATOM   4332  CB  LEU A 284     -16.134  36.732 -13.637  1.00 61.36           C
ANISOU 4332  CB  LEU A 284     6495   7367   9453    662   -798   1400       C
ATOM   4333  CG  LEU A 284     -16.035  35.626 -14.711  1.00 57.49           C
ANISOU 4333  CG  LEU A 284     5886   7136   8822    551   -626   1601       C
ATOM   4334  CD1 LEU A 284     -15.978  36.259 -16.101  1.00 58.25           C
ANISOU 4334  CD1 LEU A 284     5933   7166   9035    467   -705   1864       C
ATOM   4335  CD2 LEU A 284     -14.808  34.726 -14.574  1.00 56.48           C
ANISOU 4335  CD2 LEU A 284     5726   7149   8585    402   -550   1649       C
ATOM   4336  H   LEU A 284     -17.153  34.768 -12.335  1.00 76.25           H
ATOM   4337  HA  LEU A 284     -14.653  36.093 -12.234  1.00 78.66           H
ATOM   4338  HB2 LEU A 284     -17.160  37.109 -13.623  1.00 73.63           H
ATOM   4339  HB3 LEU A 284     -15.499  37.555 -13.951  1.00 73.63           H
ATOM   4340  HG  LEU A 284     -16.920  34.998 -14.656  1.00 68.99           H
ATOM   4341 HD11 LEU A 284     -16.839  36.911 -16.257  1.00  0.00           H
ATOM   4342 HD12 LEU A 284     -15.988  35.491 -16.871  1.00  0.00           H
ATOM   4343 HD13 LEU A 284     -15.069  36.853 -16.214  1.00  0.00           H
ATOM   4344 HD21 LEU A 284     -14.937  34.040 -13.740  1.00  0.00           H
ATOM   4345 HD22 LEU A 284     -13.931  35.344 -14.399  1.00  0.00           H
ATOM   4346 HD23 LEU A 284     -14.668  34.150 -15.488  1.00  0.00           H
ATOM   4347  N   LEU A 285     -14.776  38.360 -11.110  1.00 69.16           N
ANISOU 4347  N   LEU A 285     7723   7888  10665    721  -1168   1001       N
ATOM   4348  CA  LEU A 285     -14.796  39.597 -10.312  1.00 72.17           C
ANISOU 4348  CA  LEU A 285     8234   7973  11215    850  -1413    790       C
ATOM   4349  C   LEU A 285     -15.763  40.610 -10.941  1.00 72.06           C
ANISOU 4349  C   LEU A 285     8264   7744  11371    984  -1568    806       C
ATOM   4350  O   LEU A 285     -15.844  40.679 -12.165  1.00 69.04           O
ANISOU 4350  O   LEU A 285     7835   7318  11077    864  -1581   1079       O
ATOM   4351  CB  LEU A 285     -13.375  40.189 -10.216  1.00 72.12           C
ANISOU 4351  CB  LEU A 285     8289   7736  11378    645  -1610    882       C
ATOM   4352  CG  LEU A 285     -12.350  39.277  -9.518  1.00 72.73           C
ANISOU 4352  CG  LEU A 285     8326   8009  11299    519  -1484    862       C
ATOM   4353  CD1 LEU A 285     -10.909  39.697  -9.802  1.00 74.58           C
ANISOU 4353  CD1 LEU A 285     8558   8093  11685    249  -1636   1083       C
ATOM   4354  CD2 LEU A 285     -12.537  39.321  -8.002  1.00 75.60           C
ANISOU 4354  CD2 LEU A 285     8761   8394  11570    708  -1503    511       C
ATOM   4355  H   LEU A 285     -14.001  38.228 -11.753  1.00 82.99           H
ATOM   4356  HA  LEU A 285     -15.162  39.372  -9.309  1.00 86.61           H
ATOM   4357  HB2 LEU A 285     -13.029  40.392 -11.227  1.00 86.55           H
ATOM   4358  HB3 LEU A 285     -13.417  41.146  -9.693  1.00 86.55           H
ATOM   4359  HG  LEU A 285     -12.470  38.247  -9.855  1.00 87.27           H
ATOM   4360 HD11 LEU A 285     -10.728  39.674 -10.879  1.00  0.00           H
ATOM   4361 HD12 LEU A 285     -10.733  40.712  -9.444  1.00  0.00           H
ATOM   4362 HD13 LEU A 285     -10.214  39.010  -9.324  1.00  0.00           H
ATOM   4363 HD21 LEU A 285     -13.559  39.052  -7.753  1.00  0.00           H
ATOM   4364 HD22 LEU A 285     -11.843  38.627  -7.552  1.00  0.00           H
ATOM   4365 HD23 LEU A 285     -12.340  40.328  -7.633  1.00  0.00           H
ATOM   4366  N   ASN A 286     -16.517  41.357 -10.129  1.00 78.94           N
ANISOU 4366  N   ASN A 286     9220   8500  12275   1251  -1692    507       N
ATOM   4367  CA  ASN A 286     -17.514  42.347 -10.576  1.00 84.31           C
ANISOU 4367  CA  ASN A 286     9957   8961  13115   1433  -1867    467       C
ATOM   4368  C   ASN A 286     -18.613  41.775 -11.516  1.00 81.46           C
ANISOU 4368  C   ASN A 286     9477   8828  12644   1473  -1671    618       C
ATOM   4369  O   ASN A 286     -19.275  42.520 -12.235  1.00 85.04           O
ANISOU 4369  O   ASN A 286     9956   9106  13249   1540  -1802    709       O
ATOM   4370  CB  ASN A 286     -16.785  43.593 -11.127  1.00 86.17           C
ANISOU 4370  CB  ASN A 286    10299   8768  13674   1274  -2182    657       C
ATOM   4371  CG  ASN A 286     -15.616  44.068 -10.269  1.00 91.13           C
ANISOU 4371  CG  ASN A 286    11045   9147  14435   1204  -2407    526       C
ATOM   4372  OD1 ASN A 286     -15.562  43.910  -9.060  1.00 93.09           O
ANISOU 4372  OD1 ASN A 286    11351   9418  14600   1412  -2440    181       O
ATOM   4373  ND2 ASN A 286     -14.532  44.492 -10.871  1.00 93.52           N
ANISOU 4373  ND2 ASN A 286    11365   9235  14931    906  -2566    809       N
ATOM   4374  H   ASN A 286     -16.352  41.334  -9.133  1.00 94.73           H
ATOM   4375  HA  ASN A 286     -18.051  42.678  -9.683  1.00101.17           H
ATOM   4376  HB2 ASN A 286     -16.417  43.365 -12.127  1.00103.41           H
ATOM   4377  HB3 ASN A 286     -17.498  44.412 -11.219  1.00103.41           H
ATOM   4378 HD21 ASN A 286     -13.778  44.767 -10.272  1.00112.22           H
ATOM   4379 HD22 ASN A 286     -14.494  44.564 -11.872  1.00112.22           H
ATOM   4380  N   GLY A 287     -18.727  40.441 -11.612  1.00 73.71           N
ANISOU 4380  N   GLY A 287     8372   8225  11411   1431  -1378    649       N
ATOM   4381  CA  GLY A 287     -19.627  39.717 -12.520  1.00 65.76           C
ANISOU 4381  CA  GLY A 287     7248   7452  10288   1451  -1193    784       C
ATOM   4382  C   GLY A 287     -21.016  39.431 -11.937  1.00 67.66           C
ANISOU 4382  C   GLY A 287     7424   7937  10348   1712  -1070    556       C
ATOM   4383  O   GLY A 287     -21.761  38.626 -12.506  1.00 67.54           O
ANISOU 4383  O   GLY A 287     7295   8157  10209   1715   -900    659       O
ATOM   4384  H   GLY A 287     -18.156  39.894 -10.988  1.00 88.46           H
ATOM   4385  HA2 GLY A 287     -19.756  40.293 -13.437  1.00 78.92           H
ATOM   4386  HA3 GLY A 287     -19.170  38.763 -12.775  1.00 78.92           H
ATOM   4387  N   GLY A 288     -21.309  39.946 -10.742  1.00 71.96           N
ANISOU 4387  N   GLY A 288     8022   8459  10861   1934  -1157    253       N
ATOM   4388  CA  GLY A 288     -22.471  39.592  -9.940  1.00 72.28           C
ANISOU 4388  CA  GLY A 288     7970   8799  10696   2185  -1035     43       C
ATOM   4389  C   GLY A 288     -22.482  38.131  -9.471  1.00 72.27           C
ANISOU 4389  C   GLY A 288     7851   9176  10432   2086   -776     60       C
ATOM   4390  O   GLY A 288     -21.482  37.409  -9.495  1.00 71.67           O
ANISOU 4390  O   GLY A 288     7789   9109  10332   1861   -709    176       O
ATOM   4391  H   GLY A 288     -20.626  40.560 -10.294  1.00 86.35           H
ATOM   4392  HA2 GLY A 288     -22.492  40.239  -9.062  1.00 86.74           H
ATOM   4393  HA3 GLY A 288     -23.371  39.784 -10.526  1.00 86.74           H
ATOM   4394  N   ILE A 289     -23.642  37.677  -8.992  1.00 73.58           N
ANISOU 4394  N   ILE A 289     7891   9669  10396   2259   -640    -47       N
ATOM   4395  CA  ILE A 289     -23.806  36.293  -8.528  1.00 70.55           C
ANISOU 4395  CA  ILE A 289     7391   9647   9769   2161   -418    -11       C
ATOM   4396  C   ILE A 289     -23.630  35.285  -9.672  1.00 66.89           C
ANISOU 4396  C   ILE A 289     6865   9256   9292   1914   -277    276       C
ATOM   4397  O   ILE A 289     -24.122  35.500 -10.785  1.00 68.09           O
ANISOU 4397  O   ILE A 289     7014   9299   9559   1882   -307    423       O
ATOM   4398  CB  ILE A 289     -25.134  36.082  -7.771  1.00 72.64           C
ANISOU 4398  CB  ILE A 289     7514  10276   9810   2401   -326   -185       C
ATOM   4399  CG1 ILE A 289     -26.397  36.115  -8.666  1.00 75.45           C
ANISOU 4399  CG1 ILE A 289     7764  10746  10157   2482   -277    -94       C
ATOM   4400  CG2 ILE A 289     -25.225  37.089  -6.611  1.00 75.37           C
ANISOU 4400  CG2 ILE A 289     7917  10564  10156   2697   -487   -506       C
ATOM   4401  CD1 ILE A 289     -27.588  35.435  -7.995  1.00 74.76           C
ANISOU 4401  CD1 ILE A 289     7484  11114   9808   2618   -128   -164       C
ATOM   4402  H   ILE A 289     -24.422  38.309  -8.944  1.00 88.29           H
ATOM   4403  HA  ILE A 289     -23.002  36.103  -7.816  1.00 84.67           H
ATOM   4404  HB  ILE A 289     -25.076  35.085  -7.330  1.00 87.17           H
ATOM   4405 HG12 ILE A 289     -26.652  37.146  -8.916  1.00 90.54           H
ATOM   4406 HG13 ILE A 289     -26.231  35.572  -9.592  1.00 90.54           H
ATOM   4407 HG21 ILE A 289     -26.023  36.807  -5.927  1.00 90.44           H
ATOM   4408 HG22 ILE A 289     -24.285  37.094  -6.058  1.00 90.44           H
ATOM   4409 HG23 ILE A 289     -25.419  38.097  -6.975  1.00 90.44           H
ATOM   4410 HD11 ILE A 289     -28.483  35.564  -8.604  1.00 89.72           H
ATOM   4411 HD12 ILE A 289     -27.389  34.370  -7.870  1.00 89.72           H
ATOM   4412 HD13 ILE A 289     -27.746  35.883  -7.021  1.00 89.72           H
ATOM   4413  N   THR A 290     -23.162  34.080  -9.334  1.00 60.07           N
ANISOU 4413  N   THR A 290     5956   8585   8284   1750   -136    349       N
ATOM   4414  CA  THR A 290     -23.196  32.926 -10.244  1.00 54.33           C
ANISOU 4414  CA  THR A 290     5169   7961   7514   1545    -13    578       C
ATOM   4415  C   THR A 290     -24.140  31.839  -9.735  1.00 51.64           C
ANISOU 4415  C   THR A 290     4691   7973   6955   1545    138    583       C
ATOM   4416  O   THR A 290     -24.221  31.580  -8.532  1.00 51.20           O
ANISOU 4416  O   THR A 290     4597   8098   6758   1619    175    454       O
ATOM   4417  CB  THR A 290     -21.818  32.374 -10.594  1.00 53.06           C
ANISOU 4417  CB  THR A 290     5083   7683   7395   1327    -13    689       C
ATOM   4418  OG1 THR A 290     -21.173  31.809  -9.464  1.00 54.09           O
ANISOU 4418  OG1 THR A 290     5226   7921   7406   1318     22    574       O
ATOM   4419  CG2 THR A 290     -20.841  33.428 -11.092  1.00 56.03           C
ANISOU 4419  CG2 THR A 290     5568   7738   7982   1290   -170    727       C
ATOM   4420  H   THR A 290     -22.864  33.929  -8.374  1.00 72.09           H
ATOM   4421  HA  THR A 290     -23.610  33.271 -11.181  1.00 65.20           H
ATOM   4422  HB  THR A 290     -21.924  31.613 -11.357  1.00 63.67           H
ATOM   4423  HG1 THR A 290     -20.344  32.283  -9.379  1.00 64.91           H
ATOM   4424 HG21 THR A 290     -19.887  32.967 -11.330  1.00 67.23           H
ATOM   4425 HG22 THR A 290     -21.242  33.897 -11.991  1.00 67.23           H
ATOM   4426 HG23 THR A 290     -20.692  34.192 -10.332  1.00 67.23           H
ATOM   4427  N   ILE A 291     -24.824  31.164 -10.668  1.00 52.87           N
ANISOU 4427  N   ILE A 291     4767   8238   7084   1456    214    744       N
ATOM   4428  CA  ILE A 291     -25.691  30.005 -10.424  1.00 54.93           C
ANISOU 4428  CA  ILE A 291     4894   8814   7165   1406    333    800       C
ATOM   4429  C   ILE A 291     -25.241  28.866 -11.351  1.00 52.82           C
ANISOU 4429  C   ILE A 291     4633   8530   6906   1182    373    991       C
ATOM   4430  O   ILE A 291     -25.098  29.064 -12.560  1.00 51.77           O
ANISOU 4430  O   ILE A 291     4530   8258   6882   1137    339   1089       O
ATOM   4431  CB  ILE A 291     -27.201  30.344 -10.585  1.00 56.22           C
ANISOU 4431  CB  ILE A 291     4922   9170   7268   1566    359    772       C
ATOM   4432  CG1 ILE A 291     -27.631  31.540  -9.693  1.00 59.61           C
ANISOU 4432  CG1 ILE A 291     5350   9616   7683   1837    295    545       C
ATOM   4433  CG2 ILE A 291     -28.062  29.104 -10.271  1.00 55.98           C
ANISOU 4433  CG2 ILE A 291     4734   9485   7052   1477    470    864       C
ATOM   4434  CD1 ILE A 291     -29.084  32.001  -9.871  1.00 59.06           C
ANISOU 4434  CD1 ILE A 291     5152   9725   7562   2042    301    491       C
ATOM   4435  H   ILE A 291     -24.676  31.438 -11.635  1.00 63.45           H
ATOM   4436  HA  ILE A 291     -25.550  29.677  -9.396  1.00 65.92           H
ATOM   4437  HB  ILE A 291     -27.383  30.611 -11.626  1.00 67.46           H
ATOM   4438 HG12 ILE A 291     -27.477  31.287  -8.648  1.00 71.53           H
ATOM   4439 HG13 ILE A 291     -26.999  32.399  -9.912  1.00 71.53           H
ATOM   4440 HG21 ILE A 291     -29.117  29.324 -10.435  1.00 67.18           H
ATOM   4441 HG22 ILE A 291     -27.804  28.274 -10.925  1.00 67.18           H
ATOM   4442 HG23 ILE A 291     -27.917  28.801  -9.235  1.00 67.18           H
ATOM   4443 HD11 ILE A 291     -29.228  32.951  -9.356  1.00 70.87           H
ATOM   4444 HD12 ILE A 291     -29.307  32.133 -10.928  1.00 70.87           H
ATOM   4445 HD13 ILE A 291     -29.775  31.275  -9.445  1.00 70.87           H
ATOM   4446  N   THR A 292     -25.054  27.669 -10.791  1.00 48.36           N
ANISOU 4446  N   THR A 292     4039   8113   6223   1052    430   1040       N
ATOM   4447  CA  THR A 292     -24.678  26.431 -11.505  1.00 45.76           C
ANISOU 4447  CA  THR A 292     3729   7762   5897    861    438   1190       C
ATOM   4448  C   THR A 292     -25.500  25.268 -10.950  1.00 51.48           C
ANISOU 4448  C   THR A 292     4349   8733   6479    764    488   1266       C
ATOM   4449  O   THR A 292     -25.614  25.149  -9.727  1.00 53.38           O
ANISOU 4449  O   THR A 292     4523   9160   6599    806    528   1215       O
ATOM   4450  CB  THR A 292     -23.193  26.079 -11.297  1.00 50.09           C
ANISOU 4450  CB  THR A 292     4402   8139   6491    765    401   1189       C
ATOM   4451  OG1 THR A 292     -22.348  27.197 -11.436  1.00 52.85           O
ANISOU 4451  OG1 THR A 292     4832   8281   6968    839    341   1130       O
ATOM   4452  CG2 THR A 292     -22.632  25.018 -12.237  1.00 44.10           C
ANISOU 4452  CG2 THR A 292     3670   7338   5748    619    383   1314       C
ATOM   4453  H   THR A 292     -25.175  27.605  -9.784  1.00 58.03           H
ATOM   4454  HA  THR A 292     -24.870  26.538 -12.573  1.00 54.92           H
ATOM   4455  HB  THR A 292     -23.073  25.707 -10.282  1.00 60.11           H
ATOM   4456  HG1 THR A 292     -22.398  27.502 -12.369  1.00 63.42           H
ATOM   4457 HG21 THR A 292     -21.598  24.817 -11.972  1.00 52.92           H
ATOM   4458 HG22 THR A 292     -23.184  24.085 -12.150  1.00 52.92           H
ATOM   4459 HG23 THR A 292     -22.672  25.372 -13.268  1.00 52.92           H
ATOM   4460  N   VAL A 293     -25.864  24.298 -11.792  1.00 47.57           N
ANISOU 4460  N   VAL A 293     3833   8248   5995    632    472   1397       N
ATOM   4461  CA  VAL A 293     -26.313  22.963 -11.353  1.00 49.57           C
ANISOU 4461  CA  VAL A 293     4012   8673   6151    485    475   1509       C
ATOM   4462  C   VAL A 293     -25.316  21.901 -11.831  1.00 49.62           C
ANISOU 4462  C   VAL A 293     4128   8518   6209    335    402   1579       C
ATOM   4463  O   VAL A 293     -25.025  21.808 -13.020  1.00 50.54           O
ANISOU 4463  O   VAL A 293     4299   8495   6411    335    357   1590       O
ATOM   4464  CB  VAL A 293     -27.770  22.693 -11.791  1.00 53.11           C
ANISOU 4464  CB  VAL A 293     4313   9305   6563    474    489   1594       C
ATOM   4465  CG1 VAL A 293     -28.229  21.248 -11.551  1.00 50.82           C
ANISOU 4465  CG1 VAL A 293     3959   9143   6209    271    450   1750       C
ATOM   4466  CG2 VAL A 293     -28.743  23.579 -10.996  1.00 53.71           C
ANISOU 4466  CG2 VAL A 293     4258   9598   6551    645    559   1514       C
ATOM   4467  H   VAL A 293     -25.675  24.425 -12.786  1.00 57.09           H
ATOM   4468  HA  VAL A 293     -26.314  22.933 -10.267  1.00 59.49           H
ATOM   4469  HB  VAL A 293     -27.869  22.917 -12.853  1.00 63.74           H
ATOM   4470 HG11 VAL A 293     -29.264  21.139 -11.880  1.00 60.99           H
ATOM   4471 HG12 VAL A 293     -27.619  20.552 -12.125  1.00 60.99           H
ATOM   4472 HG13 VAL A 293     -28.162  21.002 -10.491  1.00 60.99           H
ATOM   4473 HG21 VAL A 293     -29.742  23.509 -11.428  1.00 64.45           H
ATOM   4474 HG22 VAL A 293     -28.777  23.266  -9.953  1.00 64.45           H
ATOM   4475 HG23 VAL A 293     -28.427  24.619 -11.028  1.00 64.45           H
ATOM   4476  N   ASN A 294     -24.741  21.121 -10.908  1.00 52.77           N
ANISOU 4476  N   ASN A 294     4554   8951   6546    224    381   1621       N
ATOM   4477  CA  ASN A 294     -23.963  19.924 -11.264  1.00 55.51           C
ANISOU 4477  CA  ASN A 294     5010   9146   6933    104    290   1670       C
ATOM   4478  C   ASN A 294     -24.879  18.693 -11.398  1.00 51.96           C
ANISOU 4478  C   ASN A 294     4508   8773   6460    -58    212   1813       C
ATOM   4479  O   ASN A 294     -25.822  18.528 -10.615  1.00 56.89           O
ANISOU 4479  O   ASN A 294     5011   9605   7000   -121    242   1902       O
ATOM   4480  CB  ASN A 294     -22.830  19.673 -10.249  1.00 59.09           C
ANISOU 4480  CB  ASN A 294     5550   9549   7353     87    288   1626       C
ATOM   4481  CG  ASN A 294     -21.671  20.645 -10.361  1.00 59.73           C
ANISOU 4481  CG  ASN A 294     5720   9481   7496    199    309   1505       C
ATOM   4482  OD1 ASN A 294     -21.088  20.874 -11.405  1.00 60.66           O
ANISOU 4482  OD1 ASN A 294     5872   9483   7694    241    287   1489       O
ATOM   4483  ND2 ASN A 294     -21.168  21.162  -9.270  1.00 63.51           N
ANISOU 4483  ND2 ASN A 294     6224   9977   7930    239    343   1430       N
ATOM   4484  H   ASN A 294     -25.069  21.223  -9.953  1.00 63.33           H
ATOM   4485  HA  ASN A 294     -23.496  20.077 -12.240  1.00 66.61           H
ATOM   4486  HB2 ASN A 294     -23.233  19.684  -9.243  1.00 70.91           H
ATOM   4487  HB3 ASN A 294     -22.421  18.679 -10.418  1.00 70.91           H
ATOM   4488 HD21 ASN A 294     -20.486  21.880  -9.412  1.00 76.22           H
ATOM   4489 HD22 ASN A 294     -21.647  21.029  -8.401  1.00 76.22           H
ATOM   4490  N   PHE A 295     -24.492  17.754 -12.265  1.00 50.70           N
ANISOU 4490  N   PHE A 295     4434   8457   6374   -121     96   1837       N
ATOM   4491  CA  PHE A 295     -25.115  16.437 -12.438  1.00 52.33           C
ANISOU 4491  CA  PHE A 295     4629   8661   6593   -286    -35   1963       C
ATOM   4492  C   PHE A 295     -24.057  15.350 -12.220  1.00 53.51           C
ANISOU 4492  C   PHE A 295     4921   8643   6768   -354   -156   1962       C
ATOM   4493  O   PHE A 295     -23.229  15.085 -13.097  1.00 54.23           O
ANISOU 4493  O   PHE A 295     5122   8572   6911   -278   -217   1866       O
ATOM   4494  CB  PHE A 295     -25.746  16.297 -13.834  1.00 55.04           C
ANISOU 4494  CB  PHE A 295     4956   8955   7003   -275   -107   1962       C
ATOM   4495  CG  PHE A 295     -26.887  17.236 -14.182  1.00 58.39           C
ANISOU 4495  CG  PHE A 295     5238   9544   7405   -203     -2   1970       C
ATOM   4496  CD1 PHE A 295     -26.645  18.605 -14.407  1.00 57.81           C
ANISOU 4496  CD1 PHE A 295     5153   9481   7330    -33    121   1868       C
ATOM   4497  CD2 PHE A 295     -28.191  16.726 -14.347  1.00 62.37           C
ANISOU 4497  CD2 PHE A 295     5619  10182   7897   -309    -45   2086       C
ATOM   4498  CE1 PHE A 295     -27.705  19.465 -14.737  1.00 59.73           C
ANISOU 4498  CE1 PHE A 295     5276   9861   7560     54    197   1867       C
ATOM   4499  CE2 PHE A 295     -29.250  17.586 -14.689  1.00 58.88           C
ANISOU 4499  CE2 PHE A 295     5038   9908   7425   -226     48   2087       C
ATOM   4500  CZ  PHE A 295     -29.007  18.957 -14.874  1.00 59.36           C
ANISOU 4500  CZ  PHE A 295     5100   9971   7485    -33    168   1971       C
ATOM   4501  H   PHE A 295     -23.689  17.969 -12.853  1.00 60.84           H
ATOM   4502  HA  PHE A 295     -25.902  16.294 -11.696  1.00 62.80           H
ATOM   4503  HB2 PHE A 295     -24.967  16.418 -14.584  1.00 66.05           H
ATOM   4504  HB3 PHE A 295     -26.116  15.276 -13.917  1.00 66.05           H
ATOM   4505  HD1 PHE A 295     -25.644  19.004 -14.337  1.00 69.37           H
ATOM   4506  HD2 PHE A 295     -28.384  15.669 -14.221  1.00 74.84           H
ATOM   4507  HE1 PHE A 295     -27.514  20.515 -14.897  1.00 71.68           H
ATOM   4508  HE2 PHE A 295     -30.249  17.194 -14.823  1.00 70.65           H
ATOM   4509  HZ  PHE A 295     -29.818  19.618 -15.143  1.00 71.24           H
ATOM   4510  N   TRP A 296     -24.032  14.784 -11.015  1.00 55.67           N
ANISOU 4510  N   TRP A 296     5181   8978   6995   -488   -194   2076       N
ATOM   4511  CA  TRP A 296     -23.006  13.836 -10.583  1.00 61.58           C
ANISOU 4511  CA  TRP A 296     6063   9572   7762   -547   -313   2086       C
ATOM   4512  C   TRP A 296     -23.367  12.403 -10.978  1.00 61.21           C
ANISOU 4512  C   TRP A 296     6066   9399   7791   -706   -535   2202       C
ATOM   4513  O   TRP A 296     -24.349  11.862 -10.473  1.00 62.96           O
ANISOU 4513  O   TRP A 296     6183   9735   8005   -866   -580   2370       O
ATOM   4514  CB  TRP A 296     -22.851  13.968  -9.066  1.00 65.09           C
ANISOU 4514  CB  TRP A 296     6470  10154   8107   -596   -239   2150       C
ATOM   4515  CG  TRP A 296     -22.390  15.313  -8.603  1.00 62.91           C
ANISOU 4515  CG  TRP A 296     6161   9975   7765   -436    -59   2015       C
ATOM   4516  CD1 TRP A 296     -23.175  16.260  -8.046  1.00 66.52           C
ANISOU 4516  CD1 TRP A 296     6479  10661   8134   -378     82   2009       C
ATOM   4517  CD2 TRP A 296     -21.052  15.892  -8.676  1.00 60.37           C
ANISOU 4517  CD2 TRP A 296     5948   9525   7467   -308    -24   1862       C
ATOM   4518  NE1 TRP A 296     -22.410  17.360  -7.712  1.00 66.09           N
ANISOU 4518  NE1 TRP A 296     6459  10591   8063   -220    182   1849       N
ATOM   4519  CE2 TRP A 296     -21.093  17.193  -8.090  1.00 61.47           C
ANISOU 4519  CE2 TRP A 296     6020   9788   7549   -193    122   1772       C
ATOM   4520  CE3 TRP A 296     -19.808  15.447  -9.175  1.00 58.93           C
ANISOU 4520  CE3 TRP A 296     5902   9149   7342   -273   -114   1791       C
ATOM   4521  CZ2 TRP A 296     -19.954  18.004  -7.987  1.00 60.09           C
ANISOU 4521  CZ2 TRP A 296     5917   9523   7393    -77    168   1633       C
ATOM   4522  CZ3 TRP A 296     -18.657  16.252  -9.075  1.00 57.00           C
ANISOU 4522  CZ3 TRP A 296     5706   8859   7094   -157    -44   1664       C
ATOM   4523  CH2 TRP A 296     -18.727  17.525  -8.480  1.00 58.83           C
ANISOU 4523  CH2 TRP A 296     5875   9190   7287    -75     90   1596       C
ATOM   4524  H   TRP A 296     -24.741  15.043 -10.338  1.00 66.81           H
ATOM   4525  HA  TRP A 296     -22.054  14.096 -11.045  1.00 73.89           H
ATOM   4526  HB2 TRP A 296     -23.810  13.751  -8.591  1.00 78.11           H
ATOM   4527  HB3 TRP A 296     -22.134  13.225  -8.719  1.00 78.11           H
ATOM   4528  HD1 TRP A 296     -24.240  16.144  -7.869  1.00 79.82           H
ATOM   4529  HE1 TRP A 296     -22.787  18.158  -7.226  1.00 79.31           H
ATOM   4530  HE3 TRP A 296     -19.755  14.482  -9.659  1.00 70.72           H
ATOM   4531  HZ2 TRP A 296     -20.024  18.983  -7.540  1.00 72.11           H
ATOM   4532  HZ3 TRP A 296     -17.721  15.895  -9.482  1.00 68.40           H
ATOM   4533  HH2 TRP A 296     -17.840  18.138  -8.412  1.00 70.59           H
ATOM   4534  N   TYR A 297     -22.498  11.714 -11.718  1.00 56.77           N
ANISOU 4534  N   TYR A 297     5658   8611   7302   -658   -688   2111       N
ATOM   4535  CA  TYR A 297     -22.658  10.294 -12.057  1.00 58.03           C
ANISOU 4535  CA  TYR A 297     5903   8590   7554   -777   -949   2178       C
ATOM   4536  C   TYR A 297     -21.477   9.470 -11.533  1.00 57.47           C
ANISOU 4536  C   TYR A 297     5992   8335   7510   -766  -1094   2145       C
ATOM   4537  O   TYR A 297     -20.312   9.816 -11.753  1.00 57.90           O
ANISOU 4537  O   TYR A 297     6122   8338   7538   -594  -1042   1982       O
ATOM   4538  CB  TYR A 297     -22.846  10.118 -13.572  1.00 57.09           C
ANISOU 4538  CB  TYR A 297     5817   8372   7501   -676  -1043   2055       C
ATOM   4539  CG  TYR A 297     -24.133  10.700 -14.129  1.00 59.34           C
ANISOU 4539  CG  TYR A 297     5953   8813   7780   -708   -955   2109       C
ATOM   4540  CD1 TYR A 297     -24.197  12.057 -14.502  1.00 57.63           C
ANISOU 4540  CD1 TYR A 297     5646   8746   7504   -564   -734   2027       C
ATOM   4541  CD2 TYR A 297     -25.263   9.875 -14.298  1.00 62.33           C
ANISOU 4541  CD2 TYR A 297     6281   9183   8219   -886  -1111   2249       C
ATOM   4542  CE1 TYR A 297     -25.392  12.589 -15.020  1.00 58.40           C
ANISOU 4542  CE1 TYR A 297     5608   8987   7594   -575   -661   2072       C
ATOM   4543  CE2 TYR A 297     -26.460  10.407 -14.818  1.00 58.81           C
ANISOU 4543  CE2 TYR A 297     5687   8901   7759   -910  -1032   2298       C
ATOM   4544  CZ  TYR A 297     -26.530  11.769 -15.171  1.00 57.40           C
ANISOU 4544  CZ  TYR A 297     5422   8876   7512   -743   -802   2203       C
ATOM   4545  OH  TYR A 297     -27.695  12.294 -15.632  1.00 61.42           O
ANISOU 4545  OH  TYR A 297     5784   9549   8006   -749   -730   2248       O
ATOM   4546  H   TYR A 297     -21.685  12.205 -12.082  1.00 68.13           H
ATOM   4547  HA  TYR A 297     -23.558   9.906 -11.584  1.00 69.63           H
ATOM   4548  HB2 TYR A 297     -22.007  10.577 -14.092  1.00 68.50           H
ATOM   4549  HB3 TYR A 297     -22.824   9.053 -13.802  1.00 68.50           H
ATOM   4550  HD1 TYR A 297     -23.332  12.697 -14.379  1.00 69.16           H
ATOM   4551  HD2 TYR A 297     -25.215   8.833 -14.019  1.00 74.80           H
ATOM   4552  HE1 TYR A 297     -25.449  13.628 -15.295  1.00 70.08           H
ATOM   4553  HE2 TYR A 297     -27.334   9.785 -14.930  1.00 70.58           H
ATOM   4554  HH  TYR A 297     -28.353  11.622 -15.830  1.00 73.71           H
ATOM   4555  N   LYS A 298     -21.742   8.300 -10.932  1.00 70.48           N
ANISOU 4555  N   LYS A 298     6782   9350  10646   -827  -2528    209       N
ATOM   4556  CA  LYS A 298     -20.664   7.324 -10.666  1.00 68.71           C
ANISOU 4556  CA  LYS A 298     6749   9061  10297   -840  -2491    187       C
ATOM   4557  C   LYS A 298     -20.021   6.922 -11.998  1.00 66.35           C
ANISOU 4557  C   LYS A 298     6663   8691   9856   -778  -2709     69       C
ATOM   4558  O   LYS A 298     -20.734   6.644 -12.959  1.00 70.71           O
ANISOU 4558  O   LYS A 298     7192   9178  10499   -803  -2942     12       O
ATOM   4559  H   LYS A 298     -22.714   8.017 -10.868  1.00 84.57           H
ATOM   4560  CB  LYS A 298     -21.165   6.090  -9.891  1.00  0.00           C
ATOM   4561  CG  LYS A 298     -21.574   6.456  -8.460  1.00  0.00           C
ATOM   4562  CD  LYS A 298     -21.970   5.252  -7.597  1.00  0.00           C
ATOM   4563  CE  LYS A 298     -22.522   5.768  -6.261  1.00  0.00           C
ATOM   4564  NZ  LYS A 298     -22.988   4.659  -5.393  1.00  0.00           N
ATOM   4565  HA  LYS A 298     -19.894   7.820 -10.075  1.00  0.00           H
ATOM   4566  HB2 LYS A 298     -22.019   5.657 -10.412  1.00  0.00           H
ATOM   4567  HB3 LYS A 298     -20.367   5.346  -9.852  1.00  0.00           H
ATOM   4568  HG2 LYS A 298     -20.754   6.985  -7.971  1.00  0.00           H
ATOM   4569  HG3 LYS A 298     -22.431   7.114  -8.533  1.00  0.00           H
ATOM   4570  HD2 LYS A 298     -21.100   4.615  -7.430  1.00  0.00           H
ATOM   4571  HD3 LYS A 298     -22.741   4.679  -8.114  1.00  0.00           H
ATOM   4572  HE2 LYS A 298     -21.749   6.355  -5.754  1.00  0.00           H
ATOM   4573  HE3 LYS A 298     -23.357   6.440  -6.480  1.00  0.00           H
ATOM   4574  HZ1 LYS A 298     -22.294   4.428  -4.693  1.00  0.00           H
ATOM   4575  HZ2 LYS A 298     -23.848   4.919  -4.924  1.00  0.00           H
ATOM   4576  HZ3 LYS A 298     -23.176   3.841  -5.956  1.00  0.00           H
ATOM   4577  N   GLY A 299     -18.689   6.861 -12.047  1.00 62.67           N
ANISOU 4577  N   GLY A 299     6408   8237   9167   -688  -2634     33       N
ATOM   4578  CA  GLY A 299     -17.970   6.440 -13.252  1.00 62.68           C
ANISOU 4578  CA  GLY A 299     6629   8185   9003   -599  -2805    -72       C
ATOM   4579  C   GLY A 299     -18.373   5.037 -13.716  1.00 72.64           C
ANISOU 4579  C   GLY A 299     7944   9294  10362   -694  -3012   -128       C
ATOM   4580  O   GLY A 299     -18.895   4.242 -12.929  1.00 76.50           O
ANISOU 4580  O   GLY A 299     8314   9706  11045   -837  -3004    -76       O
ATOM   4581  H   GLY A 299     -18.156   7.073 -11.221  1.00 75.20           H
ATOM   4582  HA2 GLY A 299     -18.176   7.147 -14.056  1.00 75.22           H
ATOM   4583  HA3 GLY A 299     -16.899   6.439 -13.060  1.00 75.22           H
ATOM   4584  N   ALA A 300     -18.090   4.716 -14.979  1.00 73.05           N
ANISOU 4584  N   ALA A 300     8182   9298  10277   -604  -3203   -236       N
ATOM   4585  CA  ALA A 300     -18.277   3.366 -15.507  1.00 71.90           C
ANISOU 4585  CA  ALA A 300     8125   8996  10198   -672  -3424   -316       C
ATOM   4586  C   ALA A 300     -17.530   2.315 -14.649  1.00 77.31           C
ANISOU 4586  C   ALA A 300     8898   9601  10875   -738  -3307   -286       C
ATOM   4587  O   ALA A 300     -16.421   2.587 -14.171  1.00 73.65           O
ANISOU 4587  O   ALA A 300     8546   9198  10242   -663  -3116   -254       O
ATOM   4588  CB  ALA A 300     -17.810   3.349 -16.966  1.00 71.71           C
ANISOU 4588  CB  ALA A 300     8324   8947   9974   -527  -3626   -444       C
ATOM   4589  H   ALA A 300     -17.662   5.397 -15.583  1.00 87.67           H
ATOM   4590  HA  ALA A 300     -19.345   3.150 -15.484  1.00 86.28           H
ATOM   4591  HB1 ALA A 300     -18.007   2.374 -17.411  1.00 86.05           H
ATOM   4592  HB2 ALA A 300     -18.354   4.101 -17.534  1.00 86.05           H
ATOM   4593  HB3 ALA A 300     -16.742   3.564 -17.026  1.00 86.05           H
ATOM   4594  N   PRO A 301     -18.105   1.119 -14.410  1.00 88.08           N
ANISOU 4594  N   PRO A 301    10211  10823  12432   -877  -3422   -290       N
ATOM   4595  CA  PRO A 301     -17.465   0.094 -13.589  1.00 89.46           C
ANISOU 4595  CA  PRO A 301    10455  10920  12616   -945  -3304   -247       C
ATOM   4596  C   PRO A 301     -16.163  -0.397 -14.237  1.00 90.36           C
ANISOU 4596  C   PRO A 301    10856  10990  12487   -827  -3334   -337       C
ATOM   4597  O   PRO A 301     -16.159  -0.773 -15.411  1.00 90.43           O
ANISOU 4597  O   PRO A 301    11018  10966  12375   -726  -3524   -455       O
ATOM   4598  CB  PRO A 301     -18.496  -1.032 -13.461  1.00 89.19           C
ANISOU 4598  CB  PRO A 301    10292  10726  12868  -1112  -3469   -239       C
ATOM   4599  CG  PRO A 301     -19.333  -0.889 -14.734  1.00 90.76           C
ANISOU 4599  CG  PRO A 301    10471  10881  13130  -1093  -3754   -344       C
ATOM   4600  CD  PRO A 301     -19.358   0.622 -14.964  1.00 91.67           C
ANISOU 4600  CD  PRO A 301    10545  11169  13118   -977  -3681   -334       C
ATOM   4601  HA  PRO A 301     -17.249   0.502 -12.601  1.00107.35           H
ATOM   4602  HB2 PRO A 301     -18.024  -2.014 -13.394  1.00107.02           H
ATOM   4603  HB3 PRO A 301     -19.127  -0.856 -12.588  1.00107.02           H
ATOM   4604  HG2 PRO A 301     -18.822  -1.375 -15.567  1.00108.91           H
ATOM   4605  HG3 PRO A 301     -20.336  -1.299 -14.610  1.00108.91           H
ATOM   4606  HD2 PRO A 301     -19.438   0.835 -16.030  1.00110.01           H
ATOM   4607  HD3 PRO A 301     -20.200   1.066 -14.429  1.00110.01           H
ATOM   4608  N   THR A 302     -15.127  -0.619 -13.422  1.00 93.38           N
ANISOU 4608  N   THR A 302    11311  11374  12796   -833  -3141   -275       N
ATOM   4609  CA  THR A 302     -13.798  -1.090 -13.864  1.00 96.96           C
ANISOU 4609  CA  THR A 302    12023  11789  13030   -719  -3132   -338       C
ATOM   4610  C   THR A 302     -13.872  -2.323 -14.803  1.00101.20           C
ANISOU 4610  C   THR A 302    12693  12154  13602   -739  -3381   -456       C
ATOM   4611  O   THR A 302     -14.649  -3.249 -14.515  1.00107.08           O
ANISOU 4611  O   THR A 302    13338  12776  14570   -889  -3470   -442       O
ATOM   4612  CB  THR A 302     -12.891  -1.337 -12.643  1.00 93.95           C
ANISOU 4612  CB  THR A 302    11668  11416  12611   -750  -2900   -241       C
ATOM   4613  OG1 THR A 302     -11.604  -1.718 -13.056  1.00 93.01           O
ANISOU 4613  OG1 THR A 302    11792  11236  12310   -650  -2906   -299       O
ATOM   4614  CG2 THR A 302     -13.363  -2.411 -11.659  1.00 95.83           C
ANISOU 4614  CG2 THR A 302    11765  11561  13086   -930  -2878   -164       C
ATOM   4615  H   THR A 302     -15.220  -0.305 -12.467  1.00112.06           H
ATOM   4616  HA  THR A 302     -13.345  -0.267 -14.408  1.00116.36           H
ATOM   4617  HB  THR A 302     -12.798  -0.403 -12.092  1.00112.74           H
ATOM   4618  HG1 THR A 302     -11.243  -2.306 -12.388  1.00111.61           H
ATOM   4619 HG21 THR A 302     -12.637  -2.516 -10.852  1.00115.00           H
ATOM   4620 HG22 THR A 302     -14.316  -2.116 -11.220  1.00115.00           H
ATOM   4621 HG23 THR A 302     -13.478  -3.371 -12.161  1.00115.00           H
ATOM   4622  N   PRO A 303     -13.180  -2.346 -15.968  1.00 95.84           N
ANISOU 4622  N   PRO A 303    12240  11458  12718   -586  -3499   -570       N
ATOM   4623  CA  PRO A 303     -13.210  -3.486 -16.895  1.00 94.93           C
ANISOU 4623  CA  PRO A 303    12273  11174  12622   -589  -3749   -701       C
ATOM   4624  C   PRO A 303     -12.690  -4.799 -16.266  1.00 97.09           C
ANISOU 4624  C   PRO A 303    12610  11313  12968   -678  -3700   -679       C
ATOM   4625  O   PRO A 303     -12.019  -4.796 -15.235  1.00 93.05           O
ANISOU 4625  O   PRO A 303    12081  10846  12427   -700  -3465   -572       O
ATOM   4626  CB  PRO A 303     -12.407  -3.056 -18.134  1.00 95.72           C
ANISOU 4626  CB  PRO A 303    12624  11317  12430   -369  -3807   -801       C
ATOM   4627  CG  PRO A 303     -12.454  -1.531 -18.090  1.00 94.66           C
ANISOU 4627  CG  PRO A 303    12408  11367  12193   -278  -3662   -730       C
ATOM   4628  CD  PRO A 303     -12.461  -1.236 -16.591  1.00 92.66           C
ANISOU 4628  CD  PRO A 303    11959  11183  12063   -395  -3420   -584       C
ATOM   4629  HA  PRO A 303     -14.244  -3.631 -17.206  1.00113.91           H
ATOM   4630  HB2 PRO A 303     -11.370  -3.382 -18.050  1.00114.87           H
ATOM   4631  HB3 PRO A 303     -12.852  -3.434 -19.056  1.00114.87           H
ATOM   4632  HG2 PRO A 303     -11.593  -1.082 -18.589  1.00113.60           H
ATOM   4633  HG3 PRO A 303     -13.382  -1.173 -18.539  1.00113.60           H
ATOM   4634  HD2 PRO A 303     -11.436  -1.208 -16.219  1.00111.19           H
ATOM   4635  HD3 PRO A 303     -12.954  -0.278 -16.426  1.00111.19           H
ATOM   4636  N   LYS A 304     -13.112  -5.958 -16.799  1.00107.62           N
ANISOU 4636  N   LYS A 304    14019  12470  14400   -726  -3938   -788       N
ATOM   4637  CA  LYS A 304     -12.713  -7.290 -16.263  1.00110.84           C
ANISOU 4637  CA  LYS A 304    14494  12727  14894   -808  -3921   -778       C
ATOM   4638  C   LYS A 304     -11.342  -7.747 -16.766  1.00111.46           C
ANISOU 4638  C   LYS A 304    14853  12789  14708   -647  -3855   -835       C
ATOM   4639  O   LYS A 304     -10.783  -8.720 -16.242  1.00108.88           O
ANISOU 4639  O   LYS A 304    14568  12422  14378   -681  -3696   -764       O
ATOM   4640  H   LYS A 304     -13.596  -5.919 -17.685  1.00129.14           H
ATOM   4641  CB  LYS A 304     -13.757  -8.364 -16.619  1.00  0.00           C
ATOM   4642  CG  LYS A 304     -15.030  -8.402 -15.755  1.00  0.00           C
ATOM   4643  CD  LYS A 304     -16.054  -7.272 -15.978  1.00  0.00           C
ATOM   4644  CE  LYS A 304     -15.898  -6.088 -15.012  1.00  0.00           C
ATOM   4645  NZ  LYS A 304     -16.666  -4.896 -15.459  1.00  0.00           N
ATOM   4646  HA  LYS A 304     -12.612  -7.233 -15.178  1.00  0.00           H
ATOM   4647  HB2 LYS A 304     -13.287  -9.342 -16.485  1.00  0.00           H
ATOM   4648  HB3 LYS A 304     -14.019  -8.289 -17.675  1.00  0.00           H
ATOM   4649  HG2 LYS A 304     -15.531  -9.341 -16.006  1.00  0.00           H
ATOM   4650  HG3 LYS A 304     -14.757  -8.462 -14.701  1.00  0.00           H
ATOM   4651  HD2 LYS A 304     -17.046  -7.703 -15.811  1.00  0.00           H
ATOM   4652  HD3 LYS A 304     -16.006  -6.944 -17.017  1.00  0.00           H
ATOM   4653  HE2 LYS A 304     -16.256  -6.407 -14.026  1.00  0.00           H
ATOM   4654  HE3 LYS A 304     -14.840  -5.824 -14.905  1.00  0.00           H
ATOM   4655  HZ1 LYS A 304     -17.602  -5.124 -15.761  1.00  0.00           H
ATOM   4656  HZ2 LYS A 304     -16.697  -4.212 -14.710  1.00  0.00           H
ATOM   4657  HZ3 LYS A 304     -16.179  -4.411 -16.198  1.00  0.00           H
ATOM   4658  N   ARG A 305     -10.891  -7.185 -17.877  1.00116.11           N
ANISOU 4658  N   ARG A 305    15634  13408  15073   -466  -3968   -954       N
ATOM   4659  CA  ARG A 305      -9.578  -7.348 -18.502  1.00116.32           C
ANISOU 4659  CA  ARG A 305    15930  13427  14838   -285  -3898  -1002       C
ATOM   4660  C   ARG A 305      -8.950  -5.962 -18.435  1.00111.00           C
ANISOU 4660  C   ARG A 305    15263  12947  13964   -148  -3672   -911       C
ATOM   4661  O   ARG A 305      -9.530  -5.050 -19.021  1.00111.07           O
ANISOU 4661  O   ARG A 305    15316  13051  13833    -15  -3732   -956       O
ATOM   4662  H   ARG A 305     -11.393  -6.359 -18.187  1.00139.33           H
ATOM   4663  CB  ARG A 305      -9.748  -7.864 -19.947  1.00  0.00           C
ATOM   4664  CG  ARG A 305     -10.327  -9.291 -20.080  1.00  0.00           C
ATOM   4665  CD  ARG A 305      -9.455 -10.416 -19.488  1.00  0.00           C
ATOM   4666  NE  ARG A 305      -9.492 -10.438 -18.014  1.00  0.00           N
ATOM   4667  CZ  ARG A 305      -8.645 -10.995 -17.172  1.00  0.00           C
ATOM   4668  NH1 ARG A 305      -7.631 -11.708 -17.567  1.00  0.00           N
ATOM   4669  NH2 ARG A 305      -8.799 -10.784 -15.897  1.00  0.00           N
ATOM   4670  HA  ARG A 305      -8.927  -8.012 -17.945  1.00  0.00           H
ATOM   4671  HB2 ARG A 305     -10.414  -7.186 -20.490  1.00  0.00           H
ATOM   4672  HB3 ARG A 305      -8.782  -7.834 -20.459  1.00  0.00           H
ATOM   4673  HG2 ARG A 305     -10.446  -9.498 -21.145  1.00  0.00           H
ATOM   4674  HG3 ARG A 305     -11.322  -9.327 -19.635  1.00  0.00           H
ATOM   4675  HD2 ARG A 305      -9.837 -11.371 -19.856  1.00  0.00           H
ATOM   4676  HD3 ARG A 305      -8.431 -10.290 -19.843  1.00  0.00           H
ATOM   4677  HE  ARG A 305     -10.210  -9.879 -17.573  1.00  0.00           H
ATOM   4678 HH11 ARG A 305      -7.486 -11.834 -18.553  1.00  0.00           H
ATOM   4679 HH12 ARG A 305      -6.974 -12.081 -16.907  1.00  0.00           H
ATOM   4680 HH21 ARG A 305      -9.530 -10.144 -15.605  1.00  0.00           H
ATOM   4681 HH22 ARG A 305      -8.196 -11.214 -15.221  1.00  0.00           H
ATOM   4682  N   ILE A 306      -8.169  -5.758 -17.381  1.00105.80           N
ANISOU 4682  N   ILE A 306    14559  12341  13299   -177  -3419   -781       N
ATOM   4683  CA  ILE A 306      -7.436  -4.510 -17.159  1.00103.35           C
ANISOU 4683  CA  ILE A 306    14235  12196  12836    -62  -3205   -686       C
ATOM   4684  C   ILE A 306      -6.351  -4.423 -18.229  1.00103.37           C
ANISOU 4684  C   ILE A 306    14489  12208  12581    165  -3194   -740       C
ATOM   4685  O   ILE A 306      -5.490  -5.296 -18.324  1.00108.79           O
ANISOU 4685  O   ILE A 306    15354  12785  13195    219  -3194   -778       O
ATOM   4686  H   ILE A 306      -7.858  -6.558 -16.857  1.00126.96           H
ATOM   4687  CB  ILE A 306      -6.815  -4.450 -15.743  1.00  0.00           C
ATOM   4688  CG2 ILE A 306      -5.929  -3.204 -15.589  1.00  0.00           C
ATOM   4689  CG1 ILE A 306      -7.901  -4.465 -14.641  1.00  0.00           C
ATOM   4690  CD1 ILE A 306      -7.354  -4.702 -13.224  1.00  0.00           C
ATOM   4691  HA  ILE A 306      -8.112  -3.658 -17.281  1.00  0.00           H
ATOM   4692  HB  ILE A 306      -6.180  -5.329 -15.613  1.00  0.00           H
ATOM   4693 HG21 ILE A 306      -5.491  -3.175 -14.596  1.00  0.00           H
ATOM   4694 HG22 ILE A 306      -6.505  -2.295 -15.769  1.00  0.00           H
ATOM   4695 HG23 ILE A 306      -5.100  -3.231 -16.298  1.00  0.00           H
ATOM   4696 HG12 ILE A 306      -8.610  -5.266 -14.846  1.00  0.00           H
ATOM   4697 HG13 ILE A 306      -8.448  -3.520 -14.659  1.00  0.00           H
ATOM   4698 HD11 ILE A 306      -8.190  -4.813 -12.533  1.00  0.00           H
ATOM   4699 HD12 ILE A 306      -6.754  -5.612 -13.202  1.00  0.00           H
ATOM   4700 HD13 ILE A 306      -6.747  -3.859 -12.895  1.00  0.00           H
ATOM   4701  N   GLU A 307      -6.451  -3.399 -19.059  1.00 94.11           N
ANISOU 4701  N   GLU A 307    13325  11163  11272    307  -3173   -734       N
ATOM   4702  CA  GLU A 307      -5.407  -2.919 -19.948  1.00 92.82           C
ANISOU 4702  CA  GLU A 307    13381  11026  10860    543  -3139   -760       C
ATOM   4703  C   GLU A 307      -4.227  -2.283 -19.173  1.00 91.50           C
ANISOU 4703  C   GLU A 307    13186  10954  10625    616  -2868   -616       C
ATOM   4704  O   GLU A 307      -4.425  -1.563 -18.193  1.00 88.14           O
ANISOU 4704  O   GLU A 307    12584  10647  10259    578  -2761   -528       O
ATOM   4705  H   GLU A 307      -7.282  -2.810 -18.990  1.00112.94           H
ATOM   4706  CB  GLU A 307      -6.075  -2.002 -21.001  1.00  0.00           C
ATOM   4707  CG  GLU A 307      -6.647  -0.608 -20.618  1.00  0.00           C
ATOM   4708  CD  GLU A 307      -7.885  -0.499 -19.685  1.00  0.00           C
ATOM   4709  OE1 GLU A 307      -8.415  -1.529 -19.207  1.00  0.00           O
ATOM   4710  OE2 GLU A 307      -8.314   0.651 -19.419  1.00  0.00           O
ATOM   4711  HA  GLU A 307      -5.011  -3.783 -20.483  1.00  0.00           H
ATOM   4712  HB2 GLU A 307      -5.315  -1.825 -21.764  1.00  0.00           H
ATOM   4713  HB3 GLU A 307      -6.864  -2.574 -21.495  1.00  0.00           H
ATOM   4714  HG2 GLU A 307      -6.929  -0.140 -21.566  1.00  0.00           H
ATOM   4715  HG3 GLU A 307      -5.835  -0.011 -20.202  1.00  0.00           H
ATOM   4716  N   TYR A 308      -2.980  -2.595 -19.561  1.00 94.59           N
ANISOU 4716  N   TYR A 308    13750  11286  10904    721  -2766   -593       N
ATOM   4717  CA  TYR A 308      -1.745  -2.016 -18.996  1.00 90.15           C
ANISOU 4717  CA  TYR A 308    13169  10791  10293    796  -2524   -454       C
ATOM   4718  C   TYR A 308      -0.930  -1.310 -20.101  1.00 90.59           C
ANISOU 4718  C   TYR A 308    13366  10911  10144   1047  -2467   -433       C
ATOM   4719  O   TYR A 308      -0.796  -1.893 -21.179  1.00 90.96           O
ANISOU 4719  O   TYR A 308    13593  10917  10049   1180  -2596   -532       O
ATOM   4720  CB  TYR A 308      -0.872  -3.079 -18.294  1.00 89.50           C
ANISOU 4720  CB  TYR A 308    13160  10601  10243    749  -2425   -414       C
ATOM   4721  CG  TYR A 308      -1.451  -3.652 -17.010  1.00 89.36           C
ANISOU 4721  CG  TYR A 308    12990  10535  10427    513  -2432   -394       C
ATOM   4722  CD1 TYR A 308      -2.370  -4.715 -17.073  1.00 90.87           C
ANISOU 4722  CD1 TYR A 308    13186  10616  10723    388  -2613   -494       C
ATOM   4723  CD2 TYR A 308      -1.076  -3.124 -15.755  1.00 87.13           C
ANISOU 4723  CD2 TYR A 308    12558  10314  10234    424  -2260   -271       C
ATOM   4724  CE1 TYR A 308      -2.949  -5.223 -15.896  1.00 90.53           C
ANISOU 4724  CE1 TYR A 308    12995  10529  10874    181  -2604   -454       C
ATOM   4725  CE2 TYR A 308      -1.649  -3.633 -14.572  1.00 85.80           C
ANISOU 4725  CE2 TYR A 308    12258  10111  10233    226  -2253   -241       C
ATOM   4726  CZ  TYR A 308      -2.600  -4.676 -14.644  1.00 88.01           C
ANISOU 4726  CZ  TYR A 308    12537  10285  10620    106  -2416   -324       C
ATOM   4727  OH  TYR A 308      -3.170  -5.163 -13.511  1.00 88.33           O
ANISOU 4727  OH  TYR A 308    12437  10289  10837    -83  -2393   -273       O
ATOM   4728  H   TYR A 308      -2.868  -3.149 -20.399  1.00113.51           H
ATOM   4729  HA  TYR A 308      -2.029  -1.291 -18.245  1.00108.18           H
ATOM   4730  HB2 TYR A 308      -0.664  -3.896 -18.986  1.00107.40           H
ATOM   4731  HB3 TYR A 308       0.093  -2.628 -18.050  1.00107.40           H
ATOM   4732  HD1 TYR A 308      -2.655  -5.125 -18.033  1.00109.04           H
ATOM   4733  HD2 TYR A 308      -0.349  -2.327 -15.701  1.00104.55           H
ATOM   4734  HE1 TYR A 308      -3.675  -6.017 -15.950  1.00108.64           H
ATOM   4735  HE2 TYR A 308      -1.377  -3.217 -13.616  1.00102.97           H
ATOM   4736  HH  TYR A 308      -2.665  -4.925 -12.734  1.00106.00           H
ATOM   4737  N   PRO A 309      -0.231  -0.191 -19.808  0.80 92.01           N
ANISOU 4737  N   PRO A 309    13465  11186  10309   1120  -2276   -300       N
ATOM   4738  CA  PRO A 309      -0.169   0.504 -18.517  0.80 90.27           C
ANISOU 4738  CA  PRO A 309    13039  11021  10239    984  -2137   -194       C
ATOM   4739  C   PRO A 309      -1.494   1.168 -18.107  0.80 86.89           C
ANISOU 4739  C   PRO A 309    12408  10677   9930    852  -2212   -215       C
ATOM   4740  O   PRO A 309      -2.225   1.687 -18.942  0.80 88.28           O
ANISOU 4740  O   PRO A 309    12587  10896  10059    904  -2342   -281       O
ATOM   4741  CB  PRO A 309       0.945   1.554 -18.655  0.80 88.41           C
ANISOU 4741  CB  PRO A 309    12809  10851   9931   1151  -1954    -68       C
ATOM   4742  CG  PRO A 309       1.759   1.087 -19.862  0.80 90.18           C
ANISOU 4742  CG  PRO A 309    13262  11025   9976   1360  -1957    -87       C
ATOM   4743  CD  PRO A 309       0.686   0.453 -20.739  0.80 93.56           C
ANISOU 4743  CD  PRO A 309    13791  11425  10332   1365  -2175   -239       C
ATOM   4744  HA  PRO A 309       0.128  -0.216 -17.755  0.80108.32           H
ATOM   4745  HB2 PRO A 309       0.514   2.533 -18.877  0.80106.09           H
ATOM   4746  HB3 PRO A 309       1.561   1.608 -17.757  0.80106.09           H
ATOM   4747  HG2 PRO A 309       2.257   1.918 -20.364  0.80108.21           H
ATOM   4748  HG3 PRO A 309       2.482   0.329 -19.555  0.80108.21           H
ATOM   4749  HD2 PRO A 309       0.151   1.229 -21.289  0.80112.27           H
ATOM   4750  HD3 PRO A 309       1.135  -0.256 -21.437  0.80112.27           H
ATOM   4751  N   LEU A 310      -1.752   1.233 -16.799  1.00 80.06           N
ANISOU 4751  N   LEU A 310    11372   9834   9213    691  -2131   -157       N
ATOM   4752  CA  LEU A 310      -2.971   1.827 -16.231  1.00 78.98           C
ANISOU 4752  CA  LEU A 310    11037   9767   9205    556  -2188   -171       C
ATOM   4753  C   LEU A 310      -3.083   3.337 -16.518  1.00 76.39           C
ANISOU 4753  C   LEU A 310    10612   9564   8847    656  -2140   -127       C
ATOM   4754  O   LEU A 310      -2.131   4.077 -16.218  1.00 76.48           O
ANISOU 4754  O   LEU A 310    10665   9615   8780    798  -2019    -53       O
ATOM   4755  CB  LEU A 310      -2.991   1.616 -14.706  1.00 77.76           C
ANISOU 4755  CB  LEU A 310    10742   9609   9195    384  -2088   -109       C
ATOM   4756  CG  LEU A 310      -2.828   0.175 -14.201  1.00 76.85           C
ANISOU 4756  CG  LEU A 310    10700   9370   9129    275  -2112   -128       C
ATOM   4757  CD1 LEU A 310      -2.799   0.187 -12.673  1.00 76.25           C
ANISOU 4757  CD1 LEU A 310    10496   9312   9165    142  -1981    -41       C
ATOM   4758  CD2 LEU A 310      -3.979  -0.722 -14.629  1.00 77.23           C
ANISOU 4758  CD2 LEU A 310    10752   9343   9249    182  -2309   -231       C
ATOM   4759  H   LEU A 310      -1.115   0.776 -16.170  1.00 96.07           H
ATOM   4760  HA  LEU A 310      -3.836   1.333 -16.677  1.00 94.78           H
ATOM   4761  HB2 LEU A 310      -2.193   2.217 -14.268  1.00 93.31           H
ATOM   4762  HB3 LEU A 310      -3.937   2.000 -14.330  1.00 93.31           H
ATOM   4763  HG  LEU A 310      -1.888  -0.243 -14.562  1.00 92.22           H
ATOM   4764 HD11 LEU A 310      -1.972   0.802 -12.321  1.00  0.00           H
ATOM   4765 HD12 LEU A 310      -2.667  -0.829 -12.301  1.00  0.00           H
ATOM   4766 HD13 LEU A 310      -3.738   0.589 -12.293  1.00  0.00           H
ATOM   4767 HD21 LEU A 310      -4.011  -0.795 -15.717  1.00  0.00           H
ATOM   4768 HD22 LEU A 310      -3.820  -1.720 -14.227  1.00  0.00           H
ATOM   4769 HD23 LEU A 310      -4.929  -0.325 -14.274  1.00  0.00           H
ATOM   4770  N   LYS A 311      -4.314   3.814 -16.764  1.00 71.16           N
ANISOU 4770  N   LYS A 311     9809   8960   8267    580  -2237   -165       N
ATOM   4771  CA  LYS A 311      -4.674   5.245 -16.862  1.00 70.44           C
ANISOU 4771  CA  LYS A 311     9593   8988   8183    647  -2188   -118       C
ATOM   4772  C   LYS A 311      -4.204   6.001 -15.612  1.00 67.55           C
ANISOU 4772  C   LYS A 311     9094   8673   7898    602  -2006    -21       C
ATOM   4773  O   LYS A 311      -4.412   5.520 -14.494  1.00 64.78           O
ANISOU 4773  O   LYS A 311     8708   8283   7621    481  -1942      1       O
ATOM   4774  CB  LYS A 311      -6.203   5.446 -17.041  1.00 72.01           C
ANISOU 4774  CB  LYS A 311     9653   9231   8479    557  -2328   -175       C
ATOM   4775  CG  LYS A 311      -6.892   4.718 -18.220  1.00 73.16           C
ANISOU 4775  CG  LYS A 311     9912   9323   8561    594  -2544   -284       C
ATOM   4776  CD  LYS A 311      -8.387   5.111 -18.331  1.00 76.34           C
ANISOU 4776  CD  LYS A 311    10148   9773   9085    505  -2678   -322       C
ATOM   4777  CE  LYS A 311      -9.139   4.362 -19.450  1.00 78.82           C
ANISOU 4777  CE  LYS A 311    10557  10009   9382    499  -2927   -443       C
ATOM   4778  NZ  LYS A 311     -10.539   4.858 -19.639  1.00 77.72           N
ANISOU 4778  NZ  LYS A 311    10229   9903   9396    394  -3061   -469       N
ATOM   4779  H   LYS A 311      -5.062   3.127 -16.839  1.00 85.39           H
ATOM   4780  HA  LYS A 311      -4.156   5.664 -17.725  1.00 84.53           H
ATOM   4781  HB2 LYS A 311      -6.702   5.140 -16.119  1.00 86.42           H
ATOM   4782  HB3 LYS A 311      -6.378   6.517 -17.167  1.00 86.42           H
ATOM   4783  HG2 LYS A 311      -6.384   4.982 -19.149  1.00 87.79           H
ATOM   4784  HG3 LYS A 311      -6.815   3.640 -18.072  1.00 87.79           H
ATOM   4785  HD2 LYS A 311      -8.876   4.902 -17.379  1.00 91.61           H
ATOM   4786  HD3 LYS A 311      -8.450   6.184 -18.528  1.00 91.61           H
ATOM   4787  HE2 LYS A 311      -8.585   4.491 -20.384  1.00 94.58           H
ATOM   4788  HE3 LYS A 311      -9.136   3.287 -19.226  1.00 94.58           H
ATOM   4789  HZ1 LYS A 311     -10.982   4.384 -20.416  1.00 93.26           H
ATOM   4790  HZ2 LYS A 311     -11.115   4.730 -18.820  1.00 93.26           H
ATOM   4791  HZ3 LYS A 311     -10.575   5.855 -19.837  1.00 93.26           H
ATOM   4792  N   ALA A 312      -3.825   7.271 -15.750  1.00 66.83           N
ANISOU 4792  N   ALA A 312     8931   8669   7794    707  -1928     38       N
ATOM   4793  CA  ALA A 312      -3.377   8.118 -14.634  1.00 50.92           C
ANISOU 4793  CA  ALA A 312     6794   6696   5857    680  -1776    117       C
ATOM   4794  C   ALA A 312      -4.353   8.151 -13.431  1.00 53.31           C
ANISOU 4794  C   ALA A 312     6936   7027   6294    504  -1771    102       C
ATOM   4795  O   ALA A 312      -3.986   7.729 -12.332  1.00 52.15           O
ANISOU 4795  O   ALA A 312     6754   6866   6194    431  -1672    140       O
ATOM   4796  CB  ALA A 312      -3.105   9.513 -15.201  1.00 47.01           C
ANISOU 4796  CB  ALA A 312     6227   6281   5353    815  -1719    175       C
ATOM   4797  H   ALA A 312      -3.654   7.611 -16.687  1.00 80.20           H
ATOM   4798  HA  ALA A 312      -2.429   7.729 -14.261  1.00 61.11           H
ATOM   4799  HB1 ALA A 312      -2.805  10.180 -14.394  1.00 56.41           H
ATOM   4800  HB2 ALA A 312      -2.290   9.462 -15.926  1.00 56.41           H
ATOM   4801  HB3 ALA A 312      -3.987   9.920 -15.697  1.00 56.41           H
ATOM   4802  N   HIS A 313      -5.664   8.271 -13.690  1.00 54.88           N
ANISOU 4802  N   HIS A 313     7034   7264   6554    440  -1876     53       N
ATOM   4803  CA  HIS A 313      -6.704   8.169 -12.646  1.00 57.06           C
ANISOU 4803  CA  HIS A 313     7144   7570   6966    286  -1855     54       C
ATOM   4804  C   HIS A 313      -6.802   6.815 -11.918  1.00 56.92           C
ANISOU 4804  C   HIS A 313     7165   7471   6992    150  -1869     41       C
ATOM   4805  O   HIS A 313      -7.408   6.751 -10.850  1.00 57.12           O
ANISOU 4805  O   HIS A 313     7075   7517   7113     38  -1796     73       O
ATOM   4806  CB  HIS A 313      -8.076   8.562 -13.222  1.00 61.35           C
ANISOU 4806  CB  HIS A 313     7561   8165   7583    255  -1968     15       C
ATOM   4807  CG  HIS A 313      -8.894   7.492 -13.921  1.00 62.91           C
ANISOU 4807  CG  HIS A 313     7812   8292   7797    192  -2145    -57       C
ATOM   4808  ND1 HIS A 313      -9.631   6.507 -13.284  1.00 67.43           N
ANISOU 4808  ND1 HIS A 313     8326   8806   8487     32  -2184    -70       N
ATOM   4809  CD2 HIS A 313      -9.276   7.504 -15.240  1.00 66.11           C
ANISOU 4809  CD2 HIS A 313     8324   8670   8123    272  -2303   -121       C
ATOM   4810  CE1 HIS A 313     -10.447   5.936 -14.205  1.00 70.10           C
ANISOU 4810  CE1 HIS A 313     8725   9074   8836      8  -2368   -143       C
ATOM   4811  NE2 HIS A 313     -10.259   6.547 -15.396  1.00 68.83           N
ANISOU 4811  NE2 HIS A 313     8673   8933   8546    155  -2449   -182       N
ATOM   4812  H   HIS A 313      -5.920   8.625 -14.602  1.00 65.86           H
ATOM   4813  HA  HIS A 313      -6.450   8.902 -11.878  1.00 68.47           H
ATOM   4814  HB2 HIS A 313      -8.670   8.871 -12.364  1.00 73.62           H
ATOM   4815  HB3 HIS A 313      -7.977   9.436 -13.869  1.00 73.62           H
ATOM   4816  HD1 HIS A 313      -9.696   6.406 -12.274  1.00 80.91           H
ATOM   4817  HD2 HIS A 313      -8.989   8.236 -15.982  1.00 79.33           H
ATOM   4818  HE1 HIS A 313     -11.233   5.224 -13.980  1.00 84.12           H
ATOM   4819  HE2 HIS A 313     -10.908   6.532 -16.207  1.00  0.00           H
ATOM   4820  N   GLN A 314      -6.371   5.709 -12.523  1.00 57.38           N
ANISOU 4820  N   GLN A 314     7384   7435   6983    166  -1954      0       N
ATOM   4821  CA  GLN A 314      -6.330   4.397 -11.861  1.00 57.90           C
ANISOU 4821  CA  GLN A 314     7492   7410   7096     45  -1957     -1       C
ATOM   4822  C   GLN A 314      -5.132   4.301 -10.905  1.00 58.10           C
ANISOU 4822  C   GLN A 314     7556   7427   7090     50  -1798     70       C
ATOM   4823  O   GLN A 314      -5.311   3.851  -9.778  1.00 58.58           O
ANISOU 4823  O   GLN A 314     7566   7469   7224    -67  -1739    105       O
ATOM   4824  CB  GLN A 314      -6.277   3.251 -12.885  1.00 57.93           C
ANISOU 4824  CB  GLN A 314     7666   7306   7037     73  -2099    -74       C
ATOM   4825  CG  GLN A 314      -7.536   3.073 -13.750  1.00 57.28           C
ANISOU 4825  CG  GLN A 314     7554   7211   6998     51  -2291   -156       C
ATOM   4826  CD  GLN A 314      -7.291   2.033 -14.843  1.00 58.86           C
ANISOU 4826  CD  GLN A 314     7938   7293   7133     82  -2446   -244       C
ATOM   4827  OE1 GLN A 314      -6.415   2.203 -15.667  1.00 61.57           O
ANISOU 4827  OE1 GLN A 314     8455   7620   7317    235  -2450   -267       O
ATOM   4828  NE2 GLN A 314      -8.010   0.934 -14.894  1.00 59.77           N
ANISOU 4828  NE2 GLN A 314     8015   7317   7379    -58  -2571   -289       N
ATOM   4829  H   GLN A 314      -5.816   5.820 -13.366  1.00 68.86           H
ATOM   4830  HA  GLN A 314      -7.231   4.270 -11.260  1.00 69.48           H
ATOM   4831  HB2 GLN A 314      -5.424   3.419 -13.538  1.00 69.51           H
ATOM   4832  HB3 GLN A 314      -6.107   2.315 -12.351  1.00 69.51           H
ATOM   4833  HG2 GLN A 314      -8.379   2.781 -13.124  1.00 68.73           H
ATOM   4834  HG3 GLN A 314      -7.781   4.017 -14.238  1.00 68.73           H
ATOM   4835 HE21 GLN A 314      -8.737   0.724 -14.240  1.00 71.73           H
ATOM   4836 HE22 GLN A 314      -7.820   0.337 -15.691  1.00 71.73           H
ATOM   4837  N   LYS A 315      -3.988   4.913 -11.248  1.00 53.86           N
ANISOU 4837  N   LYS A 315     7107   6904   6454    189  -1728    101       N
ATOM   4838  CA  LYS A 315      -2.862   5.103 -10.313  1.00 52.98           C
ANISOU 4838  CA  LYS A 315     7019   6783   6327    200  -1591    170       C
ATOM   4839  C   LYS A 315      -3.236   6.016  -9.135  1.00 50.02           C
ANISOU 4839  C   LYS A 315     6484   6495   6028    145  -1497    209       C
ATOM   4840  O   LYS A 315      -3.028   5.609  -7.996  1.00 47.10           O
ANISOU 4840  O   LYS A 315     6103   6114   5677     85  -1412    251       O
ATOM   4841  CB  LYS A 315      -1.620   5.632 -11.051  1.00 51.64           C
ANISOU 4841  CB  LYS A 315     6956   6602   6063    366  -1543    205       C
ATOM   4842  CG  LYS A 315      -1.090   4.667 -12.127  1.00 53.93           C
ANISOU 4842  CG  LYS A 315     7430   6801   6259    441  -1606    175       C
ATOM   4843  CD  LYS A 315       0.134   5.283 -12.820  1.00 55.82           C
ANISOU 4843  CD  LYS A 315     7759   7037   6415    621  -1535    232       C
ATOM   4844  CE  LYS A 315       0.718   4.352 -13.889  1.00 58.52           C
ANISOU 4844  CE  LYS A 315     8297   7290   6649    713  -1581    206       C
ATOM   4845  NZ  LYS A 315       1.875   4.990 -14.570  1.00 60.10           N
ANISOU 4845  NZ  LYS A 315     8576   7488   6773    902  -1495    280       N
ATOM   4846  H   LYS A 315      -3.926   5.337 -12.168  1.00 64.63           H
ATOM   4847  HA  LYS A 315      -2.606   4.139  -9.872  1.00 63.57           H
ATOM   4848  HB2 LYS A 315      -1.848   6.594 -11.510  1.00 61.97           H
ATOM   4849  HB3 LYS A 315      -0.829   5.794 -10.315  1.00 61.97           H
ATOM   4850  HG2 LYS A 315      -0.809   3.722 -11.658  1.00 64.71           H
ATOM   4851  HG3 LYS A 315      -1.864   4.477 -12.873  1.00 64.71           H
ATOM   4852  HD2 LYS A 315      -0.166   6.222 -13.290  1.00 66.99           H
ATOM   4853  HD3 LYS A 315       0.898   5.494 -12.069  1.00 66.99           H
ATOM   4854  HE2 LYS A 315       1.029   3.419 -13.407  1.00 70.22           H
ATOM   4855  HE3 LYS A 315      -0.067   4.113 -14.617  1.00 70.22           H
ATOM   4856  HZ1 LYS A 315       2.286   4.368 -15.254  1.00 72.12           H
ATOM   4857  HZ2 LYS A 315       1.583   5.833 -15.051  1.00 72.12           H
ATOM   4858  HZ3 LYS A 315       2.591   5.253 -13.902  1.00 72.12           H
ATOM   4859  N   VAL A 316      -4.020   7.076  -9.372  1.00 48.40           N
ANISOU 4859  N   VAL A 316     6157   6374   5858    174  -1511    194       N
ATOM   4860  CA  VAL A 316      -4.609   7.904  -8.293  1.00 49.43           C
ANISOU 4860  CA  VAL A 316     6135   6585   6060    126  -1427    218       C
ATOM   4861  C   VAL A 316      -5.546   7.092  -7.383  1.00 49.32           C
ANISOU 4861  C   VAL A 316     6052   6567   6122    -25  -1421    222       C
ATOM   4862  O   VAL A 316      -5.373   7.120  -6.166  1.00 51.55           O
ANISOU 4862  O   VAL A 316     6281   6879   6426    -71  -1320    260       O
ATOM   4863  CB  VAL A 316      -5.314   9.166  -8.844  1.00 45.99           C
ANISOU 4863  CB  VAL A 316     5581   6233   5660    184  -1454    200       C
ATOM   4864  CG1 VAL A 316      -5.895  10.044  -7.725  1.00 50.14           C
ANISOU 4864  CG1 VAL A 316     5952   6838   6260    142  -1366    216       C
ATOM   4865  CG2 VAL A 316      -4.347  10.050  -9.644  1.00 46.03           C
ANISOU 4865  CG2 VAL A 316     5647   6242   5602    341  -1444    219       C
ATOM   4866  H   VAL A 316      -4.102   7.387 -10.334  1.00 58.08           H
ATOM   4867  HA  VAL A 316      -3.794   8.246  -7.656  1.00 59.31           H
ATOM   4868  HB  VAL A 316      -6.130   8.863  -9.500  1.00 55.19           H
ATOM   4869 HG11 VAL A 316      -6.321  10.954  -8.150  1.00 60.16           H
ATOM   4870 HG12 VAL A 316      -6.683   9.515  -7.190  1.00 60.16           H
ATOM   4871 HG13 VAL A 316      -5.107  10.321  -7.025  1.00 60.16           H
ATOM   4872 HG21 VAL A 316      -4.858  10.943 -10.005  1.00 55.24           H
ATOM   4873 HG22 VAL A 316      -3.507  10.352  -9.019  1.00 55.24           H
ATOM   4874 HG23 VAL A 316      -3.955   9.522 -10.510  1.00 55.24           H
ATOM   4875  N   ALA A 317      -6.419   6.243  -7.941  1.00 49.33           N
ANISOU 4875  N   ALA A 317     6050   6523   6169    -98  -1530    186       N
ATOM   4876  CA  ALA A 317      -7.249   5.324  -7.152  1.00 49.37           C
ANISOU 4876  CA  ALA A 317     5981   6505   6273   -243  -1525    207       C
ATOM   4877  C   ALA A 317      -6.425   4.298  -6.335  1.00 49.12           C
ANISOU 4877  C   ALA A 317     6045   6410   6209   -288  -1454    252       C
ATOM   4878  O   ALA A 317      -6.736   4.079  -5.165  1.00 51.21           O
ANISOU 4878  O   ALA A 317     6237   6696   6523   -367  -1364    306       O
ATOM   4879  CB  ALA A 317      -8.262   4.643  -8.085  1.00 50.08           C
ANISOU 4879  CB  ALA A 317     6060   6532   6435   -308  -1683    157       C
ATOM   4880  H   ALA A 317      -6.559   6.270  -8.943  1.00 59.19           H
ATOM   4881  HA  ALA A 317      -7.816   5.915  -6.431  1.00 59.25           H
ATOM   4882  HB1 ALA A 317      -8.953   4.041  -7.494  1.00 60.09           H
ATOM   4883  HB2 ALA A 317      -8.834   5.398  -8.626  1.00 60.09           H
ATOM   4884  HB3 ALA A 317      -7.750   3.997  -8.797  1.00 60.09           H
ATOM   4885  N   ILE A 318      -5.320   3.763  -6.877  1.00 49.36           N
ANISOU 4885  N   ILE A 318     6238   6361   6155   -229  -1488    237       N
ATOM   4886  CA  ILE A 318      -4.380   2.895  -6.137  1.00 50.94           C
ANISOU 4886  CA  ILE A 318     6533   6495   6326   -262  -1423    284       C
ATOM   4887  C   ILE A 318      -3.740   3.648  -4.962  1.00 49.04           C
ANISOU 4887  C   ILE A 318     6260   6322   6051   -231  -1287    340       C
ATOM   4888  O   ILE A 318      -3.898   3.199  -3.829  1.00 51.41           O
ANISOU 4888  O   ILE A 318     6537   6624   6372   -305  -1212    393       O
ATOM   4889  CB  ILE A 318      -3.316   2.261  -7.074  1.00 52.92           C
ANISOU 4889  CB  ILE A 318     6964   6653   6492   -181  -1477    259       C
ATOM   4890  CG1 ILE A 318      -3.977   1.251  -8.042  1.00 53.97           C
ANISOU 4890  CG1 ILE A 318     7148   6701   6656   -222  -1624    192       C
ATOM   4891  CG2 ILE A 318      -2.195   1.551  -6.285  1.00 54.84           C
ANISOU 4891  CG2 ILE A 318     7300   6835   6702   -196  -1396    317       C
ATOM   4892  CD1 ILE A 318      -3.082   0.813  -9.210  1.00 53.69           C
ANISOU 4892  CD1 ILE A 318     7301   6580   6520   -117  -1684    152       C
ATOM   4893  H   ILE A 318      -5.116   3.976  -7.847  1.00 59.23           H
ATOM   4894  HA  ILE A 318      -4.950   2.077  -5.695  1.00 61.12           H
ATOM   4895  HB  ILE A 318      -2.856   3.056  -7.661  1.00 63.51           H
ATOM   4896 HG12 ILE A 318      -4.290   0.365  -7.487  1.00 64.76           H
ATOM   4897 HG13 ILE A 318      -4.872   1.694  -8.475  1.00 64.76           H
ATOM   4898 HG21 ILE A 318      -1.456   1.129  -6.965  1.00 65.81           H
ATOM   4899 HG22 ILE A 318      -1.664   2.254  -5.642  1.00 65.81           H
ATOM   4900 HG23 ILE A 318      -2.609   0.751  -5.670  1.00 65.81           H
ATOM   4901 HD11 ILE A 318      -3.668   0.199  -9.893  1.00 64.43           H
ATOM   4902 HD12 ILE A 318      -2.708   1.685  -9.747  1.00 64.43           H
ATOM   4903 HD13 ILE A 318      -2.242   0.216  -8.853  1.00 64.43           H
ATOM   4904  N   MET A 319      -3.160   4.835  -5.186  1.00 45.85           N
ANISOU 4904  N   MET A 319     5855   5970   5597   -117  -1260    332       N
ATOM   4905  CA  MET A 319      -2.537   5.654  -4.128  1.00 44.78           C
ANISOU 4905  CA  MET A 319     5692   5887   5437    -78  -1157    370       C
ATOM   4906  C   MET A 319      -3.508   5.956  -2.973  1.00 51.16           C
ANISOU 4906  C   MET A 319     6369   6775   6293   -153  -1090    387       C
ATOM   4907  O   MET A 319      -3.238   5.549  -1.839  1.00 57.09           O
ANISOU 4907  O   MET A 319     7130   7541   7019   -174  -1009    428       O
ATOM   4908  CB  MET A 319      -1.971   6.960  -4.720  1.00 43.90           C
ANISOU 4908  CB  MET A 319     5567   5811   5302     51  -1154    356       C
ATOM   4909  CG  MET A 319      -0.750   6.704  -5.614  1.00 44.81           C
ANISOU 4909  CG  MET A 319     5813   5849   5364    150  -1177    371       C
ATOM   4910  SD  MET A 319       0.154   8.183  -6.154  1.00 46.24           S
ANISOU 4910  SD  MET A 319     5961   6061   5548    304  -1148    390       S
ATOM   4911  CE  MET A 319      -1.022   8.990  -7.273  1.00 47.43           C
ANISOU 4911  CE  MET A 319     6032   6275   5716    341  -1218    342       C
ATOM   4912  H   MET A 319      -3.100   5.165  -6.145  1.00 55.02           H
ATOM   4913  HA  MET A 319      -1.705   5.095  -3.697  1.00 53.74           H
ATOM   4914  HB2 MET A 319      -2.743   7.476  -5.292  1.00 52.68           H
ATOM   4915  HB3 MET A 319      -1.660   7.611  -3.900  1.00 52.68           H
ATOM   4916  HG2 MET A 319      -0.044   6.095  -5.048  1.00 53.77           H
ATOM   4917  HG3 MET A 319      -1.050   6.137  -6.492  1.00 53.77           H
ATOM   4918  HE1 MET A 319      -0.566   9.896  -7.673  1.00 56.92           H
ATOM   4919  HE2 MET A 319      -1.268   8.326  -8.100  1.00 56.92           H
ATOM   4920  HE3 MET A 319      -1.923   9.264  -6.727  1.00 56.92           H
ATOM   4921  N   ARG A 320      -4.747   6.357  -3.304  1.00 56.31           N
ANISOU 4921  N   ARG A 320     6902   7481   7014   -186  -1122    360       N
ATOM   4922  CA  ARG A 320      -5.829   6.546  -2.318  1.00 56.15           C
ANISOU 4922  CA  ARG A 320     6751   7537   7048   -248  -1045    386       C
ATOM   4923  C   ARG A 320      -6.125   5.287  -1.500  1.00 58.21           C
ANISOU 4923  C   ARG A 320     7025   7759   7333   -356  -1000    446       C
ATOM   4924  O   ARG A 320      -6.432   5.402  -0.314  1.00 49.40           O
ANISOU 4924  O   ARG A 320     5875   6696   6199   -370   -893    493       O
ATOM   4925  CB  ARG A 320      -7.135   7.008  -2.995  1.00 47.43           C
ANISOU 4925  CB  ARG A 320     5510   6478   6035   -274  -1098    356       C
ATOM   4926  CG  ARG A 320      -7.098   8.434  -3.563  1.00 46.75           C
ANISOU 4926  CG  ARG A 320     5372   6453   5936   -168  -1112    313       C
ATOM   4927  CD  ARG A 320      -8.454   8.853  -4.172  1.00 48.63           C
ANISOU 4927  CD  ARG A 320     5455   6747   6274   -199  -1147    296       C
ATOM   4928  NE  ARG A 320      -9.504   9.154  -3.172  1.00 48.41           N
ANISOU 4928  NE  ARG A 320     5305   6780   6308   -261  -1044    338       N
ATOM   4929  CZ  ARG A 320      -9.431  10.003  -2.172  1.00 50.00           C
ANISOU 4929  CZ  ARG A 320     5444   7063   6491   -205   -940    341       C
ATOM   4930  NH1 ARG A 320      -8.486  10.895  -2.121  1.00 48.52           N
ANISOU 4930  NH1 ARG A 320     5292   6898   6247    -95   -937    303       N
ATOM   4931  NH2 ARG A 320     -10.325  10.055  -1.241  1.00 54.74           N
ANISOU 4931  NH2 ARG A 320     5944   7718   7136   -251   -838    385       N
ATOM   4932  H   ARG A 320      -4.914   6.611  -4.273  1.00 67.57           H
ATOM   4933  HA  ARG A 320      -5.487   7.297  -1.607  1.00 67.38           H
ATOM   4934  HB2 ARG A 320      -7.385   6.314  -3.798  1.00 56.92           H
ATOM   4935  HB3 ARG A 320      -7.933   6.968  -2.252  1.00 56.92           H
ATOM   4936  HG2 ARG A 320      -6.786   9.119  -2.775  1.00 56.10           H
ATOM   4937  HG3 ARG A 320      -6.341   8.492  -4.342  1.00 56.10           H
ATOM   4938  HD2 ARG A 320      -8.311   9.735  -4.785  1.00 58.35           H
ATOM   4939  HD3 ARG A 320      -8.802   8.049  -4.831  1.00 58.35           H
ATOM   4940  HE  ARG A 320     -10.447   8.840  -3.421  1.00 58.09           H
ATOM   4941 HH11 ARG A 320      -7.923  11.042  -2.940  1.00 58.23           H
ATOM   4942 HH12 ARG A 320      -8.419  11.540  -1.334  1.00 58.23           H
ATOM   4943 HH21 ARG A 320     -11.238   9.727  -1.509  1.00 65.69           H
ATOM   4944 HH22 ARG A 320     -10.210  10.774  -0.524  1.00 65.69           H
ATOM   4945  N   ASN A 321      -6.153   4.110  -2.124  1.00 62.17           N
ANISOU 4945  N   ASN A 321     7580   8167   7876   -424  -1082    446       N
ATOM   4946  CA  ASN A 321      -6.419   2.849  -1.427  1.00 66.56           C
ANISOU 4946  CA  ASN A 321     8134   8672   8483   -532  -1046    512       C
ATOM   4947  C   ASN A 321      -5.275   2.450  -0.476  1.00 63.30           C
ANISOU 4947  C   ASN A 321     7830   8243   7977   -509   -961    564       C
ATOM   4948  O   ASN A 321      -5.563   2.129   0.676  1.00 65.55           O
ANISOU 4948  O   ASN A 321     8081   8551   8272   -562   -867    638       O
ATOM   4949  CB  ASN A 321      -6.738   1.738  -2.442  1.00 66.88           C
ANISOU 4949  CB  ASN A 321     8219   8595   8596   -601  -1175    487       C
ATOM   4950  CG  ASN A 321      -7.996   1.997  -3.258  1.00 71.36           C
ANISOU 4950  CG  ASN A 321     8668   9169   9274   -640  -1276    443       C
ATOM   4951  OD1 ASN A 321      -8.928   2.677  -2.846  1.00 71.55           O
ANISOU 4951  OD1 ASN A 321     8542   9275   9368   -664  -1224    468       O
ATOM   4952  ND2 ASN A 321      -8.097   1.382  -4.415  1.00 72.69           N
ANISOU 4952  ND2 ASN A 321     8910   9250   9460   -641  -1426    375       N
ATOM   4953  H   ASN A 321      -5.927   4.086  -3.112  1.00 74.61           H
ATOM   4954  HA  ASN A 321      -7.303   2.980  -0.802  1.00 79.87           H
ATOM   4955  HB2 ASN A 321      -5.891   1.614  -3.115  1.00 80.25           H
ATOM   4956  HB3 ASN A 321      -6.882   0.799  -1.907  1.00 80.25           H
ATOM   4957 HD21 ASN A 321      -8.897   1.611  -4.971  1.00 87.23           H
ATOM   4958 HD22 ASN A 321      -7.317   0.861  -4.767  1.00 87.23           H
ATOM   4959  N   ILE A 322      -4.008   2.653  -0.865  1.00 52.77           N
ANISOU 4959  N   ILE A 322     6624   6870   6557   -426   -992    534       N
ATOM   4960  CA  ILE A 322      -2.834   2.401  -0.003  1.00 52.86           C
ANISOU 4960  CA  ILE A 322     6735   6859   6490   -400   -926    583       C
ATOM   4961  C   ILE A 322      -2.867   3.289   1.248  1.00 52.02           C
ANISOU 4961  C   ILE A 322     6571   6857   6338   -368   -822    611       C
ATOM   4962  O   ILE A 322      -2.792   2.776   2.365  1.00 52.79           O
ANISOU 4962  O   ILE A 322     6688   6965   6404   -402   -745    677       O
ATOM   4963  CB  ILE A 322      -1.505   2.604  -0.777  1.00 52.06           C
ANISOU 4963  CB  ILE A 322     6755   6701   6325   -301   -973    552       C
ATOM   4964  CG1 ILE A 322      -1.350   1.701  -2.024  1.00 52.34           C
ANISOU 4964  CG1 ILE A 322     6871   6633   6383   -314  -1070    520       C
ATOM   4965  CG2 ILE A 322      -0.273   2.437   0.133  1.00 47.10           C
ANISOU 4965  CG2 ILE A 322     6216   6046   5632   -273   -916    606       C
ATOM   4966  CD1 ILE A 322      -1.346   0.185  -1.789  1.00 55.34           C
ANISOU 4966  CD1 ILE A 322     7312   6918   6795   -406  -1078    562       C
ATOM   4967  H   ILE A 322      -3.848   3.017  -1.800  1.00 63.33           H
ATOM   4968  HA  ILE A 322      -2.878   1.369   0.347  1.00 63.43           H
ATOM   4969  HB  ILE A 322      -1.491   3.633  -1.137  1.00 62.47           H
ATOM   4970 HG12 ILE A 322      -2.151   1.921  -2.721  1.00 62.81           H
ATOM   4971 HG13 ILE A 322      -0.419   1.967  -2.526  1.00 62.81           H
ATOM   4972 HG21 ILE A 322       0.639   2.512  -0.459  1.00 56.52           H
ATOM   4973 HG22 ILE A 322      -0.243   3.228   0.883  1.00 56.52           H
ATOM   4974 HG23 ILE A 322      -0.294   1.471   0.639  1.00 56.52           H
ATOM   4975 HD11 ILE A 322      -1.274  -0.319  -2.754  1.00 66.40           H
ATOM   4976 HD12 ILE A 322      -0.489  -0.106  -1.182  1.00 66.40           H
ATOM   4977 HD13 ILE A 322      -2.270  -0.128  -1.303  1.00 66.40           H
ATOM   4978  N   GLU A 323      -3.130   4.592   1.092  1.00 46.68           N
ANISOU 4978  N   GLU A 323     5827   6258   5651   -294   -818    560       N
ATOM   4979  CA  GLU A 323      -3.263   5.494   2.243  1.00 46.70           C
ANISOU 4979  CA  GLU A 323     5784   6355   5603   -247   -730    568       C
ATOM   4980  C   GLU A 323      -4.444   5.114   3.149  1.00 47.69           C
ANISOU 4980  C   GLU A 323     5819   6540   5759   -320   -640    625       C
ATOM   4981  O   GLU A 323      -4.309   5.205   4.372  1.00 52.55           O
ANISOU 4981  O   GLU A 323     6459   7202   6306   -306   -551    671       O
ATOM   4982  CB  GLU A 323      -3.467   6.950   1.816  1.00 45.61           C
ANISOU 4982  CB  GLU A 323     5578   6277   5477   -160   -752    499       C
ATOM   4983  CG  GLU A 323      -2.316   7.612   1.056  1.00 49.39           C
ANISOU 4983  CG  GLU A 323     6130   6696   5940    -75   -824    463       C
ATOM   4984  CD  GLU A 323      -2.729   9.038   0.703  1.00 44.01           C
ANISOU 4984  CD  GLU A 323     5364   6064   5292      6   -848    408       C
ATOM   4985  OE1 GLU A 323      -3.034   9.786   1.682  1.00 44.13           O
ANISOU 4985  OE1 GLU A 323     5314   6152   5300     46   -799    386       O
ATOM   4986  OE2 GLU A 323      -3.150   9.221  -0.452  1.00 43.64           O
ANISOU 4986  OE2 GLU A 323     5321   5983   5276     37   -915    387       O
ATOM   4987  H   GLU A 323      -3.176   4.978   0.152  1.00 56.02           H
ATOM   4988  HA  GLU A 323      -2.356   5.431   2.849  1.00 56.03           H
ATOM   4989  HB2 GLU A 323      -4.373   7.010   1.210  1.00 54.74           H
ATOM   4990  HB3 GLU A 323      -3.638   7.524   2.730  1.00 54.74           H
ATOM   4991  HG2 GLU A 323      -1.425   7.638   1.677  1.00 59.27           H
ATOM   4992  HG3 GLU A 323      -2.096   7.056   0.146  1.00 59.27           H
ATOM   4993  N   LYS A 324      -5.600   4.719   2.587  1.00 53.41           N
ANISOU 4993  N   LYS A 324     6438   7264   6591   -394   -663    629       N
ATOM   4994  CA  LYS A 324      -6.775   4.272   3.363  1.00 55.27           C
ANISOU 4994  CA  LYS A 324     6565   7546   6888   -466   -571    703       C
ATOM   4995  C   LYS A 324      -6.434   3.050   4.215  1.00 58.79           C
ANISOU 4995  C   LYS A 324     7078   7944   7317   -529   -516    797       C
ATOM   4996  O   LYS A 324      -6.382   3.205   5.437  1.00 60.41           O
ANISOU 4996  O   LYS A 324     7256   8213   7485   -526   -393    873       O
ATOM   4997  CB  LYS A 324      -7.970   3.965   2.442  1.00 55.97           C
ANISOU 4997  CB  LYS A 324     6530   7611   7127   -545   -638    696       C
ATOM   4998  CG  LYS A 324      -8.680   5.230   1.946  1.00 57.67           C
ANISOU 4998  CG  LYS A 324     6642   7894   7375   -490   -665    628       C
ATOM   4999  CD  LYS A 324      -9.693   4.875   0.849  1.00 62.07           C
ANISOU 4999  CD  LYS A 324     7090   8412   8083   -570   -761    618       C
ATOM   5000  CE  LYS A 324     -10.465   6.098   0.341  1.00 62.97           C
ANISOU 5000  CE  LYS A 324     7076   8605   8246   -523   -769    573       C
ATOM   5001  NZ  LYS A 324     -11.490   5.678  -0.647  1.00 66.04           N
ANISOU 5001  NZ  LYS A 324     7352   8951   8788   -602   -877    566       N
ATOM   5002  H   LYS A 324      -5.627   4.640   1.574  1.00 64.09           H
ATOM   5003  HA  LYS A 324      -7.069   5.056   4.056  1.00 66.32           H
ATOM   5004  HB2 LYS A 324      -7.624   3.385   1.587  1.00 67.17           H
ATOM   5005  HB3 LYS A 324      -8.699   3.360   2.987  1.00 67.17           H
ATOM   5006  HG2 LYS A 324      -9.186   5.721   2.779  1.00 69.20           H
ATOM   5007  HG3 LYS A 324      -7.937   5.906   1.541  1.00 69.20           H
ATOM   5008  HD2 LYS A 324      -9.158   4.423   0.011  1.00 74.49           H
ATOM   5009  HD3 LYS A 324     -10.396   4.145   1.253  1.00 74.49           H
ATOM   5010  HE2 LYS A 324     -10.937   6.594   1.195  1.00 75.56           H
ATOM   5011  HE3 LYS A 324      -9.759   6.800  -0.115  1.00 75.56           H
ATOM   5012  HZ1 LYS A 324     -12.030   6.466  -0.980  1.00 79.24           H
ATOM   5013  HZ2 LYS A 324     -11.043   5.236  -1.444  1.00 79.24           H
ATOM   5014  HZ3 LYS A 324     -12.114   4.998  -0.230  1.00 79.24           H
ATOM   5015  N   MET A 325      -5.943   1.992   3.572  1.00 65.46           N
ANISOU 5015  N   MET A 325     8013   8675   8185   -576   -602    798       N
ATOM   5016  CA  MET A 325      -5.532   0.718   4.174  1.00 71.15           C
ANISOU 5016  CA  MET A 325     8789   9334   8910   -643   -558    892       C
ATOM   5017  C   MET A 325      -4.457   0.867   5.254  1.00 71.16           C
ANISOU 5017  C   MET A 325     8895   9377   8766   -572   -479    927       C
ATOM   5018  O   MET A 325      -4.639   0.333   6.340  1.00 72.32           O
ANISOU 5018  O   MET A 325     9037   9554   8888   -596   -376   1025       O
ATOM   5019  CB  MET A 325      -5.001  -0.212   3.071  1.00 74.36           C
ANISOU 5019  CB  MET A 325     9278   9602   9372   -697   -677    868       C
ATOM   5020  CG  MET A 325      -6.107  -0.976   2.332  1.00 80.93           C
ANISOU 5020  CG  MET A 325    10013  10363  10373   -810   -738    886       C
ATOM   5021  SD  MET A 325      -5.743  -1.365   0.592  1.00 89.88           S
ANISOU 5021  SD  MET A 325    11231  11365  11555   -821   -927    779       S
ATOM   5022  CE  MET A 325      -4.093  -2.108   0.728  1.00 84.64           C
ANISOU 5022  CE  MET A 325    10768  10634  10758   -754   -927    777       C
ATOM   5023  H   MET A 325      -5.927   2.040   2.558  1.00 78.56           H
ATOM   5024  HA  MET A 325      -6.396   0.248   4.651  1.00 85.38           H
ATOM   5025  HB2 MET A 325      -4.425   0.379   2.358  1.00 89.23           H
ATOM   5026  HB3 MET A 325      -4.325  -0.950   3.508  1.00 89.23           H
ATOM   5027  HG2 MET A 325      -6.296  -1.906   2.872  1.00 97.11           H
ATOM   5028  HG3 MET A 325      -7.027  -0.392   2.359  1.00 97.11           H
ATOM   5029  HE1 MET A 325      -3.808  -2.537  -0.232  1.00101.57           H
ATOM   5030  HE2 MET A 325      -3.370  -1.341   1.002  1.00101.57           H
ATOM   5031  HE3 MET A 325      -4.097  -2.891   1.487  1.00101.57           H
ATOM   5032  N   LEU A 326      -3.417   1.684   5.046  1.00 62.83           N
ANISOU 5032  N   LEU A 326     7933   8320   7620   -480   -530    855       N
ATOM   5033  CA  LEU A 326      -2.426   1.960   6.098  1.00 60.67           C
ANISOU 5033  CA  LEU A 326     7756   8077   7219   -408   -482    879       C
ATOM   5034  C   LEU A 326      -3.029   2.692   7.310  1.00 59.41           C
ANISOU 5034  C   LEU A 326     7540   8045   6990   -359   -371    901       C
ATOM   5035  O   LEU A 326      -2.595   2.462   8.432  1.00 62.29           O
ANISOU 5035  O   LEU A 326     7975   8442   7249   -322   -308    953       O
ATOM   5036  CB  LEU A 326      -1.246   2.757   5.514  1.00 62.36           C
ANISOU 5036  CB  LEU A 326     8049   8261   7385   -316   -564    799       C
ATOM   5037  CG  LEU A 326      -0.304   1.939   4.611  1.00 61.31           C
ANISOU 5037  CG  LEU A 326     8016   8003   7278   -330   -647    799       C
ATOM   5038  CD1 LEU A 326       0.749   2.873   4.014  1.00 60.51           C
ANISOU 5038  CD1 LEU A 326     7957   7879   7154   -229   -712    733       C
ATOM   5039  CD2 LEU A 326       0.423   0.836   5.384  1.00 62.45           C
ANISOU 5039  CD2 LEU A 326     8255   8092   7380   -362   -616    884       C
ATOM   5040  H   LEU A 326      -3.288   2.096   4.126  1.00 75.39           H
ATOM   5041  HA  LEU A 326      -2.053   1.013   6.486  1.00 72.80           H
ATOM   5042  HB2 LEU A 326      -1.642   3.604   4.951  1.00 74.84           H
ATOM   5043  HB3 LEU A 326      -0.654   3.154   6.341  1.00 74.84           H
ATOM   5044  HG  LEU A 326      -0.867   1.486   3.795  1.00 73.58           H
ATOM   5045 HD11 LEU A 326       0.257   3.638   3.413  1.00  0.00           H
ATOM   5046 HD12 LEU A 326       1.324   3.350   4.809  1.00  0.00           H
ATOM   5047 HD13 LEU A 326       1.422   2.305   3.372  1.00  0.00           H
ATOM   5048 HD21 LEU A 326      -0.268   0.027   5.618  1.00  0.00           H
ATOM   5049 HD22 LEU A 326       1.233   0.425   4.782  1.00  0.00           H
ATOM   5050 HD23 LEU A 326       0.832   1.232   6.314  1.00  0.00           H
ATOM   5051  N   GLY A 327      -4.084   3.489   7.122  1.00 57.76           N
ANISOU 5051  N   GLY A 327     7210   7908   6830   -349   -346    862       N
ATOM   5052  CA  GLY A 327      -4.815   4.104   8.233  1.00 59.44           C
ANISOU 5052  CA  GLY A 327     7367   8240   6978   -295   -226    886       C
ATOM   5053  C   GLY A 327      -5.614   3.114   9.085  1.00 61.07           C
ANISOU 5053  C   GLY A 327     7536   8469   7198   -358   -105   1019       C
ATOM   5054  O   GLY A 327      -5.791   3.365  10.272  1.00 61.40           O
ANISOU 5054  O   GLY A 327     7616   8590   7123   -295      2   1071       O
ATOM   5055  H   GLY A 327      -4.490   3.518   6.195  1.00 69.32           H
ATOM   5056  HA2 GLY A 327      -4.117   4.634   8.882  1.00 71.33           H
ATOM   5057  HA3 GLY A 327      -5.527   4.813   7.829  1.00 71.33           H
ATOM   5058  N   GLU A 328      -6.121   2.037   8.483  1.00 70.07           N
ANISOU 5058  N   GLU A 328     8603   9535   8484   -475   -122   1080       N
ATOM   5059  CA  GLU A 328      -6.820   0.943   9.176  1.00 76.65           C
ANISOU 5059  CA  GLU A 328     9386  10369   9367   -545    -10   1226       C
ATOM   5060  C   GLU A 328      -5.826  -0.058   9.798  1.00 72.52           C
ANISOU 5060  C   GLU A 328     8998   9788   8767   -555     -4   1295       C
ATOM   5061  O   GLU A 328      -5.878  -0.305  10.999  1.00 76.24           O
ANISOU 5061  O   GLU A 328     9490  10316   9163   -531    120   1404       O
ATOM   5062  CB  GLU A 328      -7.791   0.241   8.197  1.00 79.59           C
ANISOU 5062  CB  GLU A 328     9627  10662   9953   -671    -55   1263       C
ATOM   5063  CG  GLU A 328      -8.911   1.189   7.715  1.00 81.99           C
ANISOU 5063  CG  GLU A 328     9776  11021  10355   -671    -56   1218       C
ATOM   5064  CD  GLU A 328      -9.755   0.688   6.527  1.00 86.04           C
ANISOU 5064  CD  GLU A 328    10172  11436  11085   -795   -147   1233       C
ATOM   5065  OE1 GLU A 328      -9.456  -0.405   5.995  1.00 87.01           O
ANISOU 5065  OE1 GLU A 328    10335  11442  11281   -881   -208   1274       O
ATOM   5066  OE2 GLU A 328     -10.481   1.549   5.973  1.00 87.27           O
ANISOU 5066  OE2 GLU A 328    10194  11624  11343   -805   -168   1200       O
ATOM   5067  H   GLU A 328      -5.971   1.926   7.489  1.00 84.08           H
ATOM   5068  HA  GLU A 328      -7.409   1.350  10.001  1.00 91.98           H
ATOM   5069  HB2 GLU A 328      -7.220  -0.122   7.341  1.00 95.51           H
ATOM   5070  HB3 GLU A 328      -8.243  -0.617   8.698  1.00 95.51           H
ATOM   5071  HG2 GLU A 328      -9.567   1.402   8.561  1.00 98.38           H
ATOM   5072  HG3 GLU A 328      -8.464   2.134   7.404  1.00 98.38           H
ATOM   5073  N   ALA A 329      -4.806  -0.477   9.042  1.00 66.50           N
ANISOU 5073  N   ALA A 329     8331   8917   8020   -583   -132   1240       N
ATOM   5074  CA  ALA A 329      -3.798  -1.464   9.447  1.00 63.38           C
ANISOU 5074  CA  ALA A 329     8057   8452   7572   -600   -135   1308       C
ATOM   5075  C   ALA A 329      -2.900  -1.009  10.611  1.00 62.74           C
ANISOU 5075  C   ALA A 329     8079   8456   7301   -490    -72   1323       C
ATOM   5076  O   ALA A 329      -2.516  -1.830  11.442  1.00 66.27           O
ANISOU 5076  O   ALA A 329     8573   8917   7689   -492     12   1437       O
ATOM   5077  CB  ALA A 329      -2.942  -1.778   8.214  1.00 60.95           C
ANISOU 5077  CB  ALA A 329     7837   8019   7302   -621   -279   1231       C
ATOM   5078  H   ALA A 329      -4.806  -0.196   8.069  1.00 79.81           H
ATOM   5079  HA  ALA A 329      -4.306  -2.375   9.766  1.00 76.05           H
ATOM   5080  HB1 ALA A 329      -2.207  -2.544   8.465  1.00 73.14           H
ATOM   5081  HB2 ALA A 329      -3.575  -2.141   7.404  1.00 73.14           H
ATOM   5082  HB3 ALA A 329      -2.419  -0.878   7.889  1.00 73.14           H
ATOM   5083  N   LEU A 330      -2.550   0.279  10.661  1.00 58.57           N
ANISOU 5083  N   LEU A 330     7590   7982   6682   -389   -119   1210       N
ATOM   5084  CA  LEU A 330      -1.814   0.894  11.773  1.00 58.76           C
ANISOU 5084  CA  LEU A 330     7718   8076   6532   -276    -91   1201       C
ATOM   5085  C   LEU A 330      -2.747   1.384  12.900  1.00 62.30           C
ANISOU 5085  C   LEU A 330     8120   8664   6889   -210     47   1240       C
ATOM   5086  O   LEU A 330      -2.279   2.004  13.849  1.00 61.26           O
ANISOU 5086  O   LEU A 330     8084   8598   6593   -109     79   1241       O
ATOM   5087  CB  LEU A 330      -0.917   2.028  11.222  1.00 54.74           C
ANISOU 5087  CB  LEU A 330     7260   7553   5986   -193   -208   1064       C
ATOM   5088  CG  LEU A 330       0.036   1.602  10.083  1.00 56.16           C
ANISOU 5088  CG  LEU A 330     7491   7601   6245   -231   -332   1029       C
ATOM   5089  CD1 LEU A 330       0.796   2.808   9.524  1.00 54.00           C
ANISOU 5089  CD1 LEU A 330     7240   7318   5958   -142   -428    914       C
ATOM   5090  CD2 LEU A 330       1.043   0.546  10.542  1.00 54.01           C
ANISOU 5090  CD2 LEU A 330     7331   7255   5935   -255   -342   1113       C
ATOM   5091  H   LEU A 330      -2.840   0.883   9.903  1.00 70.28           H
ATOM   5092  HA  LEU A 330      -1.169   0.145  12.237  1.00 70.51           H
ATOM   5093  HB2 LEU A 330      -1.563   2.828  10.858  1.00 65.69           H
ATOM   5094  HB3 LEU A 330      -0.320   2.436  12.040  1.00 65.69           H
ATOM   5095  HG  LEU A 330      -0.538   1.176   9.262  1.00 67.39           H
ATOM   5096 HD11 LEU A 330       0.096   3.614   9.306  1.00  0.00           H
ATOM   5097 HD12 LEU A 330       1.308   2.529   8.607  1.00  0.00           H
ATOM   5098 HD13 LEU A 330       1.528   3.152  10.254  1.00  0.00           H
ATOM   5099 HD21 LEU A 330       0.521  -0.336  10.909  1.00  0.00           H
ATOM   5100 HD22 LEU A 330       1.667   0.950  11.342  1.00  0.00           H
ATOM   5101 HD23 LEU A 330       1.663   0.235   9.709  1.00  0.00           H
ATOM   5102  N   GLY A 331      -4.072   1.298  12.724  1.00 67.63           N
ANISOU 5102  N   GLY A 331     8651   9380   7664   -257    128   1275       N
ATOM   5103  CA  GLY A 331      -5.079   1.827  13.657  1.00 69.56           C
ANISOU 5103  CA  GLY A 331     8843   9757   7831   -185    278   1323       C
ATOM   5104  C   GLY A 331      -5.067   3.353  13.844  1.00 70.41           C
ANISOU 5104  C   GLY A 331     8981   9952   7818    -51    263   1196       C
ATOM   5105  O   GLY A 331      -5.882   3.884  14.606  1.00 72.83           O
ANISOU 5105  O   GLY A 331     9297  10371   8002     46    384   1223       O
ATOM   5106  H   GLY A 331      -4.416   0.761  11.938  1.00 81.15           H
ATOM   5107  HA2 GLY A 331      -6.065   1.543  13.290  1.00 83.48           H
ATOM   5108  HA3 GLY A 331      -4.931   1.359  14.630  1.00 83.48           H
ATOM   5109  N   ASN A 332      -4.196   4.080  13.143  1.00 70.12           N
ANISOU 5109  N   ASN A 332     8961   9865   7816    -35    122   1060       N
ATOM   5110  CA  ASN A 332      -3.947   5.509  13.308  1.00 71.59           C
ANISOU 5110  CA  ASN A 332     9170  10117   7915     89     91    934       C
ATOM   5111  C   ASN A 332      -3.524   6.166  11.969  1.00 70.34           C
ANISOU 5111  C   ASN A 332     8979   9884   7863     75    -54    817       C
ATOM   5112  O   ASN A 332      -2.398   5.966  11.504  1.00 70.13           O
ANISOU 5112  O   ASN A 332     9029   9762   7854     55   -166    794       O
ATOM   5113  CB  ASN A 332      -2.877   5.698  14.400  1.00 70.40           C
ANISOU 5113  CB  ASN A 332     9179   9991   7576    200     70    911       C
ATOM   5114  CG  ASN A 332      -2.586   7.155  14.712  1.00 70.83           C
ANISOU 5114  CG  ASN A 332     9261  10106   7545    335     31    776       C
ATOM   5115  OD1 ASN A 332      -3.131   8.080  14.124  1.00 71.24           O
ANISOU 5115  OD1 ASN A 332     9205  10201   7661    355     58    716       O
ATOM   5116  ND2 ASN A 332      -1.683   7.420  15.622  1.00 72.53           N
ANISOU 5116  ND2 ASN A 332     9618  10318   7623    431    -40    725       N
ATOM   5117  H   ASN A 332      -3.537   3.554  12.585  1.00 84.14           H
ATOM   5118  HA  ASN A 332      -4.859   5.974  13.675  1.00 85.91           H
ATOM   5119  HB2 ASN A 332      -3.219   5.228  15.321  1.00 84.48           H
ATOM   5120  HB3 ASN A 332      -1.949   5.209  14.101  1.00 84.48           H
ATOM   5121 HD21 ASN A 332      -1.513   8.377  15.852  1.00 87.04           H
ATOM   5122 HD22 ASN A 332      -1.178   6.657  16.053  1.00 87.04           H
ATOM   5123  N   PRO A 333      -4.296   7.143  11.452  1.00 68.28           N
ANISOU 5123  N   PRO A 333     8602   9664   7678     91    -48    751       N
ATOM   5124  CA  PRO A 333      -3.914   7.958  10.297  1.00 69.49           C
ANISOU 5124  CA  PRO A 333     8727   9754   7924     94   -179    648       C
ATOM   5125  C   PRO A 333      -2.621   8.771  10.419  1.00 68.55           C
ANISOU 5125  C   PRO A 333     8717   9594   7736    186   -284    564       C
ATOM   5126  O   PRO A 333      -2.122   9.238   9.392  1.00 65.34           O
ANISOU 5126  O   PRO A 333     8317   9101   7407    174   -394    522       O
ATOM   5127  CB  PRO A 333      -5.074   8.927  10.113  1.00 69.16           C
ANISOU 5127  CB  PRO A 333     8549   9788   7941    126   -130    600       C
ATOM   5128  CG  PRO A 333      -6.278   8.146  10.623  1.00 70.11           C
ANISOU 5128  CG  PRO A 333     8591   9974   8073     78     14    706       C
ATOM   5129  CD  PRO A 333      -5.679   7.415  11.817  1.00 69.93           C
ANISOU 5129  CD  PRO A 333     8687   9970   7912    101     84    785       C
ATOM   5130  HA  PRO A 333      -3.838   7.309   9.425  1.00 83.39           H
ATOM   5131  HB2 PRO A 333      -4.930   9.817  10.730  1.00 83.00           H
ATOM   5132  HB3 PRO A 333      -5.158   9.201   9.072  1.00 83.00           H
ATOM   5133  HG2 PRO A 333      -7.089   8.804  10.924  1.00 84.13           H
ATOM   5134  HG3 PRO A 333      -6.606   7.429   9.870  1.00 84.13           H
ATOM   5135  HD2 PRO A 333      -5.697   8.060  12.698  1.00 83.91           H
ATOM   5136  HD3 PRO A 333      -6.237   6.496  12.008  1.00 83.91           H
ATOM   5137  N   GLN A 334      -2.184   9.104  11.634  1.00 73.03           N
ANISOU 5137  N   GLN A 334     9368  10217   8164    285   -257    540       N
ATOM   5138  CA  GLN A 334      -0.953   9.858  11.880  1.00 76.84           C
ANISOU 5138  CA  GLN A 334     9942  10651   8602    375   -375    453       C
ATOM   5139  C   GLN A 334       0.310   9.019  11.576  1.00 75.15           C
ANISOU 5139  C   GLN A 334     9822  10328   8403    331   -466    497       C
ATOM   5140  O   GLN A 334       1.271   9.566  11.035  1.00 76.39           O
ANISOU 5140  O   GLN A 334    10019  10412   8593    382   -583    437       O
ATOM   5141  CB  GLN A 334      -0.959  10.419  13.322  1.00 81.74           C
ANISOU 5141  CB  GLN A 334    10648  11354   9057    495   -338    413       C
ATOM   5142  CG  GLN A 334      -2.179  11.284  13.729  1.00 86.61           C
ANISOU 5142  CG  GLN A 334    11185  12084   9641    560   -232    370       C
ATOM   5143  CD  GLN A 334      -2.259  12.643  13.030  1.00 89.15           C
ANISOU 5143  CD  GLN A 334    11433  12387  10053    621   -313    244       C
ATOM   5144  OE1 GLN A 334      -2.066  13.697  13.613  1.00 89.17           O
ANISOU 5144  OE1 GLN A 334    11484  12416   9980    741   -348    145       O
ATOM   5145  NE2 GLN A 334      -2.509  12.693  11.741  1.00 88.51           N
ANISOU 5145  NE2 GLN A 334    11238  12258  10133    544   -347    247       N
ATOM   5146  H   GLN A 334      -2.661   8.711  12.443  1.00 87.64           H
ATOM   5147  HA  GLN A 334      -0.918  10.705  11.197  1.00 92.21           H
ATOM   5148  HB2 GLN A 334      -0.903   9.579  14.014  1.00 98.09           H
ATOM   5149  HB3 GLN A 334      -0.058  11.014  13.472  1.00 98.09           H
ATOM   5150  HG2 GLN A 334      -3.107  10.740  13.550  1.00103.94           H
ATOM   5151  HG3 GLN A 334      -2.123  11.467  14.803  1.00103.94           H
ATOM   5152 HE21 GLN A 334      -2.797  11.861  11.267  1.00106.21           H
ATOM   5153 HE22 GLN A 334      -2.662  13.614  11.374  1.00106.21           H
ATOM   5154  N   GLU A 335       0.247   7.685  11.679  1.00 71.94           N
ANISOU 5154  N   GLU A 335     9443   9900   7990    241   -413    605       N
ATOM   5155  CA  GLU A 335       1.371   6.769  11.381  1.00 67.82           C
ANISOU 5155  CA  GLU A 335     9011   9273   7486    201   -487    654       C
ATOM   5156  C   GLU A 335       1.611   6.489   9.884  1.00 62.79           C
ANISOU 5156  C   GLU A 335     8326   8539   6993    129   -549    655       C
ATOM   5157  O   GLU A 335       2.719   6.106   9.498  1.00 64.42           O
ANISOU 5157  O   GLU A 335     8603   8648   7227    110   -613    688       O
ATOM   5158  CB  GLU A 335       1.180   5.442  12.129  1.00 71.03           C
ANISOU 5158  CB  GLU A 335     9475   9692   7821    142   -402    774       C
ATOM   5159  CG  GLU A 335       1.264   5.662  13.643  1.00 72.53           C
ANISOU 5159  CG  GLU A 335     9759   9960   7839    229   -357    793       C
ATOM   5160  CD  GLU A 335       1.447   4.370  14.437  1.00 76.68           C
ANISOU 5160  CD  GLU A 335    10360  10470   8307    176   -302    924       C
ATOM   5161  OE1 GLU A 335       2.319   3.568  14.029  1.00 76.14           O
ANISOU 5161  OE1 GLU A 335    10340  10293   8296    123   -375    961       O
ATOM   5162  OE2 GLU A 335       0.939   4.378  15.582  1.00 78.73           O
ANISOU 5162  OE2 GLU A 335    10625  10821   8466    194   -177    999       O
ATOM   5163  H   GLU A 335      -0.585   7.263  12.077  1.00 86.32           H
ATOM   5164  HA  GLU A 335       2.293   7.218  11.753  1.00 81.39           H
ATOM   5165  HB2 GLU A 335       0.219   4.996  11.862  1.00 85.24           H
ATOM   5166  HB3 GLU A 335       1.977   4.767  11.815  1.00 85.24           H
ATOM   5167  HG2 GLU A 335       2.117   6.307  13.852  1.00 87.04           H
ATOM   5168  HG3 GLU A 335       0.363   6.177  13.971  1.00 87.04           H
ATOM   5169  N   VAL A 336       0.649   6.823   9.012  1.00 56.92           N
ANISOU 5169  N   VAL A 336     7470   7819   6337     99   -532    622       N
ATOM   5170  CA  VAL A 336       0.754   6.595   7.557  1.00 54.53           C
ANISOU 5170  CA  VAL A 336     7136   7433   6150     44   -593    620       C
ATOM   5171  C   VAL A 336       1.973   7.312   6.957  1.00 50.03           C
ANISOU 5171  C   VAL A 336     6608   6782   5617    115   -695    575       C
ATOM   5172  O   VAL A 336       2.772   6.692   6.259  1.00 49.98           O
ANISOU 5172  O   VAL A 336     6655   6681   5655     92   -742    609       O
ATOM   5173  CB  VAL A 336      -0.545   7.012   6.829  1.00 56.16           C
ANISOU 5173  CB  VAL A 336     7214   7690   6436     14   -568    587       C
ATOM   5174  CG1 VAL A 336      -0.480   6.773   5.313  1.00 55.17           C
ANISOU 5174  CG1 VAL A 336     7073   7483   6409    -23   -643    575       C
ATOM   5175  CG2 VAL A 336      -1.770   6.248   7.349  1.00 57.77           C
ANISOU 5175  CG2 VAL A 336     7359   7955   6636    -63   -466    652       C
ATOM   5176  H   VAL A 336      -0.227   7.147   9.399  1.00 68.30           H
ATOM   5177  HA  VAL A 336       0.907   5.528   7.395  1.00 65.44           H
ATOM   5178  HB  VAL A 336      -0.716   8.077   6.995  1.00 67.40           H
ATOM   5179 HG11 VAL A 336      -1.433   7.027   4.850  1.00 66.21           H
ATOM   5180 HG12 VAL A 336       0.289   7.401   4.864  1.00 66.21           H
ATOM   5181 HG13 VAL A 336      -0.250   5.728   5.108  1.00 66.21           H
ATOM   5182 HG21 VAL A 336      -2.663   6.559   6.808  1.00 69.33           H
ATOM   5183 HG22 VAL A 336      -1.623   5.178   7.211  1.00 69.33           H
ATOM   5184 HG23 VAL A 336      -1.920   6.443   8.410  1.00 69.33           H
ATOM   5185  N   GLY A 337       2.197   8.583   7.311  1.00 51.30           N
ANISOU 5185  N   GLY A 337     6743   6976   5773    206   -727    503       N
ATOM   5186  CA  GLY A 337       3.355   9.357   6.844  1.00 49.45           C
ANISOU 5186  CA  GLY A 337     6524   6660   5604    277   -822    470       C
ATOM   5187  C   GLY A 337       4.713   8.779   7.285  1.00 48.98           C
ANISOU 5187  C   GLY A 337     6573   6513   5525    286   -871    522       C
ATOM   5188  O   GLY A 337       5.548   8.513   6.416  1.00 48.10           O
ANISOU 5188  O   GLY A 337     6485   6304   5486    282   -914    560       O
ATOM   5189  H   GLY A 337       1.569   9.002   7.982  1.00 61.56           H
ATOM   5190  HA2 GLY A 337       3.341   9.384   5.753  1.00 59.34           H
ATOM   5191  HA3 GLY A 337       3.274  10.381   7.210  1.00 59.34           H
ATOM   5192  N   PRO A 338       4.958   8.547   8.589  1.00 46.88           N
ANISOU 5192  N   PRO A 338     6378   6279   5156    308   -866    527       N
ATOM   5193  CA  PRO A 338       6.189   7.926   9.089  1.00 49.11           C
ANISOU 5193  CA  PRO A 338     6762   6476   5422    319   -924    580       C
ATOM   5194  C   PRO A 338       6.527   6.570   8.449  1.00 46.57           C
ANISOU 5194  C   PRO A 338     6482   6081   5130    237   -899    671       C
ATOM   5195  O   PRO A 338       7.669   6.367   8.021  1.00 45.15           O
ANISOU 5195  O   PRO A 338     6347   5797   5012    253   -959    710       O
ATOM   5196  CB  PRO A 338       5.982   7.790  10.602  1.00 50.39           C
ANISOU 5196  CB  PRO A 338     6994   6716   5436    346   -897    577       C
ATOM   5197  CG  PRO A 338       5.059   8.959  10.938  1.00 50.27           C
ANISOU 5197  CG  PRO A 338     6914   6803   5385    400   -866    489       C
ATOM   5198  CD  PRO A 338       4.174   9.069   9.700  1.00 47.71           C
ANISOU 5198  CD  PRO A 338     6476   6497   5153    347   -814    482       C
ATOM   5199  HA  PRO A 338       7.020   8.610   8.909  1.00 58.94           H
ATOM   5200  HB2 PRO A 338       5.472   6.852  10.832  1.00 60.47           H
ATOM   5201  HB3 PRO A 338       6.926   7.851  11.146  1.00 60.47           H
ATOM   5202  HG2 PRO A 338       4.470   8.762  11.835  1.00 60.33           H
ATOM   5203  HG3 PRO A 338       5.646   9.871  11.053  1.00 60.33           H
ATOM   5204  HD2 PRO A 338       3.284   8.465   9.837  1.00 57.25           H
ATOM   5205  HD3 PRO A 338       3.887  10.109   9.538  1.00 57.25           H
ATOM   5206  N   LEU A 339       5.533   5.693   8.258  1.00 46.05           N
ANISOU 5206  N   LEU A 339     6398   6060   5037    152   -815    708       N
ATOM   5207  CA  LEU A 339       5.748   4.391   7.620  1.00 51.16           C
ANISOU 5207  CA  LEU A 339     7092   6629   5719     74   -801    785       C
ATOM   5208  C   LEU A 339       6.070   4.510   6.122  1.00 50.90           C
ANISOU 5208  C   LEU A 339     7032   6515   5791     78   -842    770       C
ATOM   5209  O   LEU A 339       7.074   3.947   5.684  1.00 49.13           O
ANISOU 5209  O   LEU A 339     6872   6194   5603     62   -861    821       O
ATOM   5210  CB  LEU A 339       4.547   3.474   7.905  1.00 51.74           C
ANISOU 5210  CB  LEU A 339     7140   6758   5759    -19   -712    829       C
ATOM   5211  CG  LEU A 339       4.772   2.037   7.380  1.00 53.62           C
ANISOU 5211  CG  LEU A 339     7427   6905   6040   -103   -703    904       C
ATOM   5212  CD1 LEU A 339       4.182   1.000   8.329  1.00 56.64           C
ANISOU 5212  CD1 LEU A 339     7827   7327   6365   -169   -623    987       C
ATOM   5213  CD2 LEU A 339       4.106   1.814   6.021  1.00 54.62           C
ANISOU 5213  CD2 LEU A 339     7498   6999   6258   -151   -717    873       C
ATOM   5214  H   LEU A 339       4.618   5.890   8.657  1.00 55.26           H
ATOM   5215  HA  LEU A 339       6.620   3.934   8.091  1.00 61.40           H
ATOM   5216  HB2 LEU A 339       4.410   3.441   8.989  1.00 62.08           H
ATOM   5217  HB3 LEU A 339       3.638   3.900   7.475  1.00 62.08           H
ATOM   5218  HG  LEU A 339       5.840   1.836   7.295  1.00 64.34           H
ATOM   5219 HD11 LEU A 339       4.605   1.117   9.328  1.00  0.00           H
ATOM   5220 HD12 LEU A 339       4.407  -0.006   7.973  1.00  0.00           H
ATOM   5221 HD13 LEU A 339       3.106   1.130   8.378  1.00  0.00           H
ATOM   5222 HD21 LEU A 339       4.555   2.458   5.270  1.00  0.00           H
ATOM   5223 HD22 LEU A 339       3.042   2.032   6.093  1.00  0.00           H
ATOM   5224 HD23 LEU A 339       4.235   0.774   5.719  1.00  0.00           H
ATOM   5225  N   LEU A 340       5.336   5.324   5.355  1.00 51.45           N
ANISOU 5225  N   LEU A 340     7016   6627   5906    108   -850    704       N
ATOM   5226  CA  LEU A 340       5.629   5.563   3.931  1.00 48.14           C
ANISOU 5226  CA  LEU A 340     6579   6142   5569    132   -886    694       C
ATOM   5227  C   LEU A 340       7.042   6.130   3.705  1.00 51.37           C
ANISOU 5227  C   LEU A 340     7018   6464   6036    220   -942    713       C
ATOM   5228  O   LEU A 340       7.794   5.593   2.893  1.00 50.10           O
ANISOU 5228  O   LEU A 340     6898   6215   5925    239   -955    754       O
ATOM   5229  CB  LEU A 340       4.580   6.515   3.326  1.00 51.68           C
ANISOU 5229  CB  LEU A 340     6923   6663   6051    148   -881    627       C
ATOM   5230  CG  LEU A 340       3.168   5.925   3.148  1.00 54.71           C
ANISOU 5230  CG  LEU A 340     7256   7112   6421     59   -837    616       C
ATOM   5231  CD1 LEU A 340       2.240   7.007   2.597  1.00 55.29           C
ANISOU 5231  CD1 LEU A 340     7217   7258   6534     88   -841    552       C
ATOM   5232  CD2 LEU A 340       3.147   4.731   2.196  1.00 54.01           C
ANISOU 5232  CD2 LEU A 340     7217   6948   6356     -5   -850    649       C
ATOM   5233  H   LEU A 340       4.520   5.772   5.767  1.00 61.74           H
ATOM   5234  HA  LEU A 340       5.595   4.614   3.398  1.00 57.76           H
ATOM   5235  HB2 LEU A 340       4.516   7.404   3.958  1.00 62.02           H
ATOM   5236  HB3 LEU A 340       4.936   6.838   2.345  1.00 62.02           H
ATOM   5237  HG  LEU A 340       2.778   5.587   4.102  1.00 65.66           H
ATOM   5238 HD11 LEU A 340       2.248   7.870   3.264  1.00  0.00           H
ATOM   5239 HD12 LEU A 340       1.222   6.624   2.533  1.00  0.00           H
ATOM   5240 HD13 LEU A 340       2.572   7.317   1.605  1.00  0.00           H
ATOM   5241 HD21 LEU A 340       3.712   4.953   1.292  1.00  0.00           H
ATOM   5242 HD22 LEU A 340       2.120   4.487   1.930  1.00  0.00           H
ATOM   5243 HD23 LEU A 340       3.576   3.869   2.700  1.00  0.00           H
ATOM   5244  N   ASN A 341       7.471   7.081   4.540  1.00 53.32           N
ANISOU 5244  N   ASN A 341     7245   6729   6285    282   -978    685       N
ATOM   5245  CA  ASN A 341       8.841   7.601   4.527  1.00 50.69           C
ANISOU 5245  CA  ASN A 341     6924   6299   6036    361  -1042    713       C
ATOM   5246  C   ASN A 341       9.886   6.507   4.825  1.00 47.12           C
ANISOU 5246  C   ASN A 341     6568   5758   5576    340  -1052    795       C
ATOM   5247  O   ASN A 341      10.829   6.338   4.054  1.00 49.58           O
ANISOU 5247  O   ASN A 341     6899   5967   5974    380  -1071    852       O
ATOM   5248  CB  ASN A 341       8.941   8.767   5.522  1.00 52.22           C
ANISOU 5248  CB  ASN A 341     7078   6521   6243    427  -1100    655       C
ATOM   5249  CG  ASN A 341       8.376  10.056   4.962  1.00 53.45           C
ANISOU 5249  CG  ASN A 341     7127   6733   6450    470  -1101    584       C
ATOM   5250  OD1 ASN A 341       9.026  10.738   4.195  1.00 55.70           O
ANISOU 5250  OD1 ASN A 341     7356   6962   6847    525  -1122    598       O
ATOM   5251  ND2 ASN A 341       7.237  10.505   5.421  1.00 57.67           N
ANISOU 5251  ND2 ASN A 341     7631   7377   6906    453  -1069    516       N
ATOM   5252  H   ASN A 341       6.811   7.449   5.217  1.00 63.99           H
ATOM   5253  HA  ASN A 341       9.065   7.979   3.526  1.00 60.83           H
ATOM   5254  HB2 ASN A 341       8.452   8.509   6.462  1.00 62.67           H
ATOM   5255  HB3 ASN A 341       9.991   8.956   5.735  1.00 62.67           H
ATOM   5256 HD21 ASN A 341       6.907  11.364   5.022  1.00 69.21           H
ATOM   5257 HD22 ASN A 341       6.643   9.881   5.950  1.00 69.21           H
ATOM   5258  N   THR A 342       9.672   5.688   5.859  1.00 46.46           N
ANISOU 5258  N   THR A 342     6546   5713   5393    283  -1032    811       N
ATOM   5259  CA  THR A 342      10.531   4.529   6.198  1.00 44.61           C
ANISOU 5259  CA  THR A 342     6403   5398   5149    254  -1036    895       C
ATOM   5260  C   THR A 342      10.611   3.502   5.061  1.00 47.65           C
ANISOU 5260  C   THR A 342     6818   5709   5579    220   -999    945       C
ATOM   5261  O   THR A 342      11.651   2.885   4.836  1.00 45.49           O
ANISOU 5261  O   THR A 342     6602   5332   5350    233  -1012   1016       O
ATOM   5262  CB  THR A 342      10.001   3.846   7.472  1.00 46.68           C
ANISOU 5262  CB  THR A 342     6718   5730   5287    193   -998    914       C
ATOM   5263  OG1 THR A 342       9.952   4.782   8.528  1.00 51.60           O
ANISOU 5263  OG1 THR A 342     7337   6420   5848    247  -1038    863       O
ATOM   5264  CG2 THR A 342      10.841   2.665   7.956  1.00 44.53           C
ANISOU 5264  CG2 THR A 342     6537   5374   5009    160  -1000   1008       C
ATOM   5265  H   THR A 342       8.866   5.864   6.447  1.00 55.75           H
ATOM   5266  HA  THR A 342      11.547   4.876   6.390  1.00 53.53           H
ATOM   5267  HB  THR A 342       8.989   3.488   7.291  1.00 56.01           H
ATOM   5268  HG1 THR A 342       9.113   5.261   8.464  1.00 61.92           H
ATOM   5269 HG21 THR A 342      10.457   2.318   8.917  1.00 53.44           H
ATOM   5270 HG22 THR A 342      10.775   1.841   7.246  1.00 53.44           H
ATOM   5271 HG23 THR A 342      11.883   2.962   8.073  1.00 53.44           H
ATOM   5272  N   MET A 343       9.538   3.362   4.280  1.00 48.40           N
ANISOU 5272  N   MET A 343     6876   5851   5664    182   -958    905       N
ATOM   5273  CA  MET A 343       9.472   2.443   3.147  1.00 45.30           C
ANISOU 5273  CA  MET A 343     6526   5391   5295    151   -934    933       C
ATOM   5274  C   MET A 343      10.303   2.888   1.938  1.00 49.83           C
ANISOU 5274  C   MET A 343     7098   5887   5948    243   -952    947       C
ATOM   5275  O   MET A 343      10.838   2.009   1.259  1.00 48.41           O
ANISOU 5275  O   MET A 343     6988   5615   5790    253   -939    996       O
ATOM   5276  CB  MET A 343       8.008   2.272   2.734  1.00 45.72           C
ANISOU 5276  CB  MET A 343     6538   5517   5316     81   -905    880       C
ATOM   5277  CG  MET A 343       7.764   0.907   2.084  1.00 54.74           C
ANISOU 5277  CG  MET A 343     7741   6598   6458      8   -890    906       C
ATOM   5278  SD  MET A 343       6.156   0.733   1.266  1.00 55.67           S
ANISOU 5278  SD  MET A 343     7795   6777   6580    -66   -888    839       S
ATOM   5279  CE  MET A 343       5.062   1.354   2.569  1.00 56.43           C
ANISOU 5279  CE  MET A 343     7789   7015   6639    -98   -849    815       C
ATOM   5280  H   MET A 343       8.692   3.854   4.546  1.00 58.08           H
ATOM   5281  HA  MET A 343       9.857   1.479   3.483  1.00 54.36           H
ATOM   5282  HB2 MET A 343       7.374   2.348   3.616  1.00 54.86           H
ATOM   5283  HB3 MET A 343       7.729   3.061   2.035  1.00 54.86           H
ATOM   5284  HG2 MET A 343       8.534   0.724   1.335  1.00 65.68           H
ATOM   5285  HG3 MET A 343       7.850   0.141   2.856  1.00 65.68           H
ATOM   5286  HE1 MET A 343       4.021   1.205   2.282  1.00 67.72           H
ATOM   5287  HE2 MET A 343       5.265   0.831   3.502  1.00 67.72           H
ATOM   5288  HE3 MET A 343       5.243   2.419   2.708  1.00 67.72           H
ATOM   5289  N   ILE A 344      10.353   4.197   1.641  1.00 46.42           N
ANISOU 5289  N   ILE A 344     6588   5486   5564    318   -974    912       N
ATOM   5290  CA  ILE A 344      11.000   4.758   0.437  1.00 49.21           C
ANISOU 5290  CA  ILE A 344     6926   5777   5995    414   -974    938       C
ATOM   5291  C   ILE A 344      12.437   5.255   0.673  1.00 46.23           C
ANISOU 5291  C   ILE A 344     6533   5314   5718    495  -1003   1006       C
ATOM   5292  O   ILE A 344      13.280   5.006  -0.186  1.00 49.29           O
ANISOU 5292  O   ILE A 344     6940   5612   6177    570   -984   1076       O
ATOM   5293  CB  ILE A 344      10.117   5.830  -0.260  1.00 55.27           C
ANISOU 5293  CB  ILE A 344     7605   6624   6773    449   -975    873       C
ATOM   5294  CG1 ILE A 344       9.996   7.184   0.484  1.00 59.31           C
ANISOU 5294  CG1 ILE A 344     8022   7186   7327    482  -1009    836       C
ATOM   5295  CG2 ILE A 344       8.720   5.260  -0.573  1.00 54.15           C
ANISOU 5295  CG2 ILE A 344     7461   6562   6552    362   -960    808       C
ATOM   5296  CD1 ILE A 344      10.960   8.247  -0.062  1.00 58.75           C
ANISOU 5296  CD1 ILE A 344     7889   7054   7382    596  -1030    876       C
ATOM   5297  H   ILE A 344       9.813   4.826   2.225  1.00 55.70           H
ATOM   5298  HA  ILE A 344      11.099   3.954  -0.289  1.00 59.05           H
ATOM   5299  HB  ILE A 344      10.574   6.033  -1.230  1.00 66.33           H
ATOM   5300 HG12 ILE A 344       8.987   7.583   0.368  1.00 71.17           H
ATOM   5301 HG13 ILE A 344      10.172   7.047   1.550  1.00 71.17           H
ATOM   5302 HG21 ILE A 344       8.169   5.964  -1.198  1.00 64.98           H
ATOM   5303 HG22 ILE A 344       8.817   4.323  -1.121  1.00 64.98           H
ATOM   5304 HG23 ILE A 344       8.154   5.089   0.342  1.00 64.98           H
ATOM   5305 HD11 ILE A 344      10.881   9.159   0.532  1.00 70.51           H
ATOM   5306 HD12 ILE A 344      11.985   7.887  -0.019  1.00 70.51           H
ATOM   5307 HD13 ILE A 344      10.709   8.480  -1.098  1.00 70.51           H
ATOM   5308  N   LYS A 345      12.749   5.842   1.841  1.00 44.26           N
ANISOU 5308  N   LYS A 345     6249   5087   5480    489  -1052    987       N
ATOM   5309  CA  LYS A 345      14.012   6.566   2.112  1.00 39.51           C
ANISOU 5309  CA  LYS A 345     5613   4398   5000    565  -1108   1040       C
ATOM   5310  C   LYS A 345      15.256   5.676   1.949  1.00 44.03           C
ANISOU 5310  C   LYS A 345     6254   4849   5627    583  -1096   1148       C
ATOM   5311  O   LYS A 345      15.505   4.823   2.801  1.00 44.79           O
ANISOU 5311  O   LYS A 345     6427   4930   5663    521  -1101   1172       O
ATOM   5312  H   LYS A 345      12.013   5.913   2.535  1.00 53.11           H
ATOM   5313  CB  LYS A 345      13.973   7.201   3.516  1.00  0.00           C
ATOM   5314  CG  LYS A 345      13.118   8.482   3.592  1.00  0.00           C
ATOM   5315  CD  LYS A 345      12.951   8.989   5.037  1.00  0.00           C
ATOM   5316  CE  LYS A 345      14.259   9.588   5.579  1.00  0.00           C
ATOM   5317  NZ  LYS A 345      14.122  10.108   6.966  1.00  0.00           N
ATOM   5318  HA  LYS A 345      14.108   7.372   1.392  1.00  0.00           H
ATOM   5319  HB2 LYS A 345      14.992   7.457   3.806  1.00  0.00           H
ATOM   5320  HB3 LYS A 345      13.596   6.460   4.224  1.00  0.00           H
ATOM   5321  HG2 LYS A 345      12.131   8.289   3.174  1.00  0.00           H
ATOM   5322  HG3 LYS A 345      13.579   9.264   2.986  1.00  0.00           H
ATOM   5323  HD2 LYS A 345      12.175   9.757   5.041  1.00  0.00           H
ATOM   5324  HD3 LYS A 345      12.623   8.162   5.670  1.00  0.00           H
ATOM   5325  HE2 LYS A 345      15.037   8.821   5.547  1.00  0.00           H
ATOM   5326  HE3 LYS A 345      14.563  10.400   4.910  1.00  0.00           H
ATOM   5327  HZ1 LYS A 345      14.974  10.579   7.247  1.00  0.00           H
ATOM   5328  HZ2 LYS A 345      13.951   9.351   7.616  1.00  0.00           H
ATOM   5329  HZ3 LYS A 345      13.360  10.772   7.027  1.00  0.00           H
ATOM   5330  N   GLY A 346      16.101   5.972   0.959  1.00 46.09           N
ANISOU 5330  N   GLY A 346     6484   5021   6008    674  -1074   1223       N
ATOM   5331  CA  GLY A 346      17.302   5.184   0.640  1.00 40.25           C
ANISOU 5331  CA  GLY A 346     5798   4159   5337    708  -1050   1335       C
ATOM   5332  C   GLY A 346      16.997   3.809   0.029  1.00 44.16           C
ANISOU 5332  C   GLY A 346     6402   4643   5735    670   -978   1350       C
ATOM   5333  O   GLY A 346      17.776   2.874   0.227  1.00 42.98           O
ANISOU 5333  O   GLY A 346     6311   4394   5627    689   -954   1438       O
ATOM   5334  H   GLY A 346      15.802   6.657   0.267  1.00 55.31           H
ATOM   5335  HA2 GLY A 346      17.902   5.737  -0.084  1.00 48.30           H
ATOM   5336  HA3 GLY A 346      17.902   5.036   1.540  1.00 48.30           H
ATOM   5337  N   ARG A 347      15.785   3.617  -0.515  1.00 46.71           N
ANISOU 5337  N   ARG A 347     6749   5057   5942    620   -950   1265       N
ATOM   5338  CA  ARG A 347      15.291   2.329  -1.046  1.00 48.89           C
ANISOU 5338  CA  ARG A 347     7128   5315   6134    581   -902   1261       C
ATOM   5339  C   ARG A 347      14.526   2.436  -2.371  1.00 47.66           C
ANISOU 5339  C   ARG A 347     6978   5191   5939    634   -866   1218       C
ATOM   5340  O   ARG A 347      14.490   1.466  -3.117  1.00 44.39           O
ANISOU 5340  O   ARG A 347     6650   4715   5502    675   -825   1244       O
ATOM   5341  CB  ARG A 347      14.403   1.594  -0.025  1.00 47.86           C
ANISOU 5341  CB  ARG A 347     7034   5251   5901    449   -918   1202       C
ATOM   5342  CG  ARG A 347      14.800   1.689   1.461  1.00 46.68           C
ANISOU 5342  CG  ARG A 347     6869   5110   5757    405   -962   1224       C
ATOM   5343  CD  ARG A 347      14.302   0.492   2.285  1.00 47.35           C
ANISOU 5343  CD  ARG A 347     7020   5215   5756    295   -952   1225       C
ATOM   5344  NE  ARG A 347      12.890   0.179   2.004  1.00 52.63           N
ANISOU 5344  NE  ARG A 347     7682   5969   6346    219   -927   1151       N
ATOM   5345  CZ  ARG A 347      12.398  -0.872   1.379  1.00 44.65           C
ANISOU 5345  CZ  ARG A 347     6729   4924   5312    172   -900   1144       C
ATOM   5346  NH1 ARG A 347      13.143  -1.830   0.899  1.00 47.31           N
ANISOU 5346  NH1 ARG A 347     7147   5147   5681    198   -883   1200       N
ATOM   5347  NH2 ARG A 347      11.117  -0.946   1.183  1.00 43.64           N
ANISOU 5347  NH2 ARG A 347     6574   4869   5137    100   -895   1078       N
ATOM   5348  H   ARG A 347      15.178   4.430  -0.554  1.00 56.05           H
ATOM   5349  HA  ARG A 347      16.158   1.700  -1.259  1.00 58.67           H
ATOM   5350  HB2 ARG A 347      13.382   1.971  -0.115  1.00 57.44           H
ATOM   5351  HB3 ARG A 347      14.392   0.545  -0.324  1.00 57.44           H
ATOM   5352  HG2 ARG A 347      15.883   1.730   1.568  1.00 56.02           H
ATOM   5353  HG3 ARG A 347      14.372   2.603   1.876  1.00 56.02           H
ATOM   5354  HD2 ARG A 347      14.943  -0.366   2.081  1.00 56.82           H
ATOM   5355  HD3 ARG A 347      14.408   0.737   3.345  1.00 56.82           H
ATOM   5356  HE  ARG A 347      12.236   0.933   2.173  1.00 63.16           H
ATOM   5357 HH11 ARG A 347      14.139  -1.702   0.932  1.00 56.77           H
ATOM   5358 HH12 ARG A 347      12.751  -2.522   0.290  1.00 56.77           H
ATOM   5359 HH21 ARG A 347      10.584  -0.106   1.354  1.00 52.37           H
ATOM   5360 HH22 ARG A 347      10.705  -1.766   0.786  1.00 52.37           H
ATOM   5361  N   TYR A 348      13.859   3.561  -2.604  1.00 50.02           N
ANISOU 5361  N   TYR A 348     7193   5585   6228    641   -886   1150       N
ATOM   5362  CA  TYR A 348      13.116   3.917  -3.829  1.00 50.97           C
ANISOU 5362  CA  TYR A 348     7312   5743   6310    699   -864   1111       C
ATOM   5363  C   TYR A 348      13.342   5.374  -4.266  1.00 54.23           C
ANISOU 5363  C   TYR A 348     7622   6174   6811    807   -859   1139       C
ATOM   5364  O   TYR A 348      12.638   5.878  -5.126  1.00 48.79           O
ANISOU 5364  O   TYR A 348     6916   5532   6089    862   -845   1108       O
ATOM   5365  CB  TYR A 348      11.599   3.612  -3.632  1.00 50.87           C
ANISOU 5365  CB  TYR A 348     7292   5833   6204    597   -893   1002       C
ATOM   5366  CG  TYR A 348      11.223   2.148  -3.558  1.00 51.58           C
ANISOU 5366  CG  TYR A 348     7480   5893   6223    506   -896    978       C
ATOM   5367  CD1 TYR A 348      11.214   1.382  -4.737  1.00 41.90           C
ANISOU 5367  CD1 TYR A 348     6351   4614   4953    546   -887    967       C
ATOM   5368  CD2 TYR A 348      10.827   1.568  -2.341  1.00 44.42           C
ANISOU 5368  CD2 TYR A 348     6573   5010   5296    386   -909    966       C
ATOM   5369  CE1 TYR A 348      10.834   0.026  -4.699  1.00 41.49           C
ANISOU 5369  CE1 TYR A 348     6385   4520   4857    461   -902    939       C
ATOM   5370  CE2 TYR A 348      10.431   0.217  -2.297  1.00 44.23           C
ANISOU 5370  CE2 TYR A 348     6625   4948   5231    299   -911    955       C
ATOM   5371  CZ  TYR A 348      10.445  -0.561  -3.476  1.00 45.22           C
ANISOU 5371  CZ  TYR A 348     6840   5009   5333    333   -914    938       C
ATOM   5372  OH  TYR A 348      10.066  -1.866  -3.440  1.00 49.90           O
ANISOU 5372  OH  TYR A 348     7506   5550   5905    247   -928    921       O
ATOM   5373  H   TYR A 348      13.870   4.264  -1.876  1.00 60.03           H
ATOM   5374  HA  TYR A 348      13.480   3.281  -4.656  1.00 61.16           H
ATOM   5375  HB2 TYR A 348      11.266   4.138  -2.741  1.00 61.04           H
ATOM   5376  HB3 TYR A 348      11.061   4.043  -4.476  1.00 61.04           H
ATOM   5377  HD1 TYR A 348      11.506   1.833  -5.676  1.00 50.27           H
ATOM   5378  HD2 TYR A 348      10.822   2.156  -1.437  1.00 53.31           H
ATOM   5379  HE1 TYR A 348      10.837  -0.570  -5.599  1.00 49.78           H
ATOM   5380  HE2 TYR A 348      10.120  -0.223  -1.366  1.00 53.07           H
ATOM   5381  HH  TYR A 348       9.528  -2.061  -2.675  1.00 59.88           H
ATOM   5382  N   ASN A 349      14.334   6.096  -3.606  1.00 60.35           N
ANISOU 5382  N   ASN A 349     8323   6906   7702    839   -877   1197       N
ATOM   5383  CA  ASN A 349      14.791   7.424  -3.900  1.00 60.21           C
ANISOU 5383  CA  ASN A 349     8192   6882   7801    940   -877   1236       C
ATOM   5384  C   ASN A 349      16.282   7.559  -3.619  1.00 64.68           C
ANISOU 5384  C   ASN A 349     8729   7323   8523   1023   -865   1364       C
ATOM   5385  O   ASN A 349      16.774   6.631  -2.919  1.00 62.56           O
ANISOU 5385  O   ASN A 349     8513   6987   8271    983   -880   1405       O
ATOM   5386  CB  ASN A 349      13.939   8.447  -3.069  1.00 57.84           C
ANISOU 5386  CB  ASN A 349     7791   6667   7519    889   -940   1150       C
ATOM   5387  CG  ASN A 349      14.326   8.587  -1.598  1.00 59.45           C
ANISOU 5387  CG  ASN A 349     7985   6842   7762    830  -1003   1145       C
ATOM   5388  OD1 ASN A 349      14.559   7.641  -0.851  1.00 59.40           O
ANISOU 5388  OD1 ASN A 349     8052   6767   7749    803  -1003   1196       O
ATOM   5389  ND2 ASN A 349      14.094   9.739  -1.028  1.00 59.29           N
ANISOU 5389  ND2 ASN A 349     7879   6873   7776    818  -1061   1079       N
ATOM   5390  OXT ASN A 349      16.744   8.701  -3.867  1.00 70.22           O
ANISOU 5390  OXT ASN A 349     9347   7984   9350   1131   -842   1440       O
ATOM   5391  H   ASN A 349      14.929   5.560  -3.014  1.00 72.42           H
ATOM   5392  HA  ASN A 349      14.593   7.655  -4.941  1.00 72.25           H
ATOM   5393  HB2 ASN A 349      14.111   9.419  -3.506  1.00 69.41           H
ATOM   5394  HB3 ASN A 349      12.880   8.236  -3.116  1.00 69.41           H
ATOM   5395 HD21 ASN A 349      14.369   9.847  -0.066  1.00 71.15           H
ATOM   5396 HD22 ASN A 349      13.920  10.532  -1.626  1.00 71.15           H
END



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elNémo is maintained by Yves-Henri Sanejouand.
It was developed by Karsten Suhre.
Between 2003 and 2014, it was hosted by IGS (Marseille).
Last modification: October 18th, 2018.