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***  kgd_test  ***

elNémo ID: 20120115465378288

Job options:

ID        	=	 20120115465378288
JOBID     	=	 kgd_test
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER kgd_test

HEADER    POLYKETIDE SYNTHASE                     22-JUN-98   1BI5              
TITLE     CHALCONE SYNTHASE FROM ALFALFA                                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CHALCONE SYNTHASE;                                         
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: CHS;                                                        
COMPND   5 EC: 2.3.1.74;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MEDICAGO SATIVA;                                
SOURCE   3 ORGANISM_TAXID: 3879;                                                
SOURCE   4 TISSUE: 21 DAY OLD ROOT NODULE;                                      
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;                            
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PET28B                                    
KEYWDS    POLYKETIDE SYNTHASE, CHALCONE BIOSYNTHESIS                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.L.FERRER,J.M.JEZ,M.E.BOWMAN,R.A.DIXON,J.P.NOEL                      
REVDAT   5   04-APR-18 1BI5    1       REMARK                                   
REVDAT   4   13-JUL-11 1BI5    1       VERSN                                    
REVDAT   3   24-FEB-09 1BI5    1       VERSN                                    
REVDAT   2   28-JUN-05 1BI5    1       AUTHOR JRNL   REMARK                     
REVDAT   1   22-JUN-99 1BI5    0                                                
JRNL        AUTH   J.L.FERRER,J.M.JEZ,M.E.BOWMAN,R.A.DIXON,J.P.NOEL             
JRNL        TITL   STRUCTURE OF CHALCONE SYNTHASE AND THE MOLECULAR BASIS OF    
JRNL        TITL 2 PLANT POLYKETIDE BIOSYNTHESIS.                               
JRNL        REF    NAT.STRUCT.BIOL.              V.   6   775 1999              
JRNL        REFN                   ISSN 1072-8368                               
JRNL        PMID   10426957                                                     
JRNL        DOI    10.1038/11553                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.56 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : SHELXL-97                                            
REMARK   3   AUTHORS     : G.M.SHELDRICK                                        
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.56                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 91.3                           
REMARK   3   CROSS-VALIDATION METHOD           : RANDOM                         
REMARK   3   FREE R VALUE TEST SET SELECTION   : 0.05                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (NO CUTOFF).                         
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : 0.132                  
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.136                  
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.193                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.400                  
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : 2507                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 46763                  
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).                     
REMARK   3   R VALUE   (WORKING + TEST SET, F>4SIG(F)) : 0.128                  
REMARK   3   R VALUE          (WORKING SET, F>4SIG(F)) : 0.131                  
REMARK   3   FREE R VALUE                  (F>4SIG(F)) : 0.187                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 5.400                  
REMARK   3   FREE R VALUE TEST SET COUNT   (F>4SIG(F)) : 2347                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (F>4SIG(F)) : 43475                  
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS      : 2997                                          
REMARK   3   NUCLEIC ACID ATOMS : 0                                             
REMARK   3   HETEROGEN ATOMS    : 0                                             
REMARK   3   SOLVENT ATOMS      : 479                                           
REMARK   3                                                                      
REMARK   3  MODEL REFINEMENT.                                                   
REMARK   3   OCCUPANCY SUM OF NON-HYDROGEN ATOMS      : 3413.2                  
REMARK   3   OCCUPANCY SUM OF HYDROGEN ATOMS          : 0.00                    
REMARK   3   NUMBER OF DISCRETELY DISORDERED RESIDUES : 17                      
REMARK   3   NUMBER OF LEAST-SQUARES PARAMETERS       : 32565                   
REMARK   3   NUMBER OF RESTRAINTS                     : 41135                   
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.                        
REMARK   3   BOND LENGTHS                         (A) : 0.009                   
REMARK   3   ANGLE DISTANCES                      (A) : 0.026                   
REMARK   3   SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000                   
REMARK   3   DISTANCES FROM RESTRAINT PLANES      (A) : 0.026                   
REMARK   3   ZERO CHIRAL VOLUMES               (A**3) : 0.044                   
REMARK   3   NON-ZERO CHIRAL VOLUMES           (A**3) : 0.060                   
REMARK   3   ANTI-BUMPING DISTANCE RESTRAINTS     (A) : 0.027                   
REMARK   3   RIGID-BOND ADP COMPONENTS         (A**2) : 0.001                   
REMARK   3   SIMILAR ADP COMPONENTS            (A**2) : 0.029                   
REMARK   3   APPROXIMATELY ISOTROPIC ADPS      (A**2) : 0.028                   
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED: MOEWS & KRETSINGER                                    
REMARK   3                                                                      
REMARK   3  STEREOCHEMISTRY TARGET VALUES : ENGH AND HUBER                      
REMARK   3   SPECIAL CASE: NULL                                                 
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: 1ST STEP OF THE REFINEMENT PERFORMED      
REMARK   3  WITH REFMAC + ARP.                                                  
REMARK   4                                                                      
REMARK   4 1BI5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 100 THE DEPOSITION ID IS D_1000171785.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : MAY-98                             
REMARK 200  TEMPERATURE           (KELVIN) : 105                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : MACSCIENCE                         
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NI FILTER                          
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MAC SCIENCE DIP-2000               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 46763                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.560                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 25.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.3                               
REMARK 200  DATA REDUNDANCY                : 5.000                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.03900                            
REMARK 200   FOR THE DATA SET  : 38.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.56                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.60                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 62.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.00                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.16300                            
REMARK 200   FOR SHELL         : 4.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIRAS + SOLVENT FLIPPING     
REMARK 200 SOFTWARE USED: SHARP, SOLOMON                                        
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 42.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 6.5                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+1/3                                           
REMARK 290       6555   -X,-X+Y,-Z+2/3                                          
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       43.68000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       21.84000            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       21.84000            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       43.68000            
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 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: 6140 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 27150 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 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 -0.500000  0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.866025  0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      131.04000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 390  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 460  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 464  LIES ON A SPECIAL POSITION.                          
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A  67   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    ASN A  82   CA  -  CB  -  CG  ANGL. DEV. =  14.7 DEGREES          
REMARK 500    MET A 137   CG  -  SD  -  CE  ANGL. DEV. = -11.4 DEGREES          
REMARK 500    ARG A 151   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.2 DEGREES          
REMARK 500    VAL A 342   N   -  CA  -  CB  ANGL. DEV. = -15.2 DEGREES          
REMARK 500    ILE A 389   C   -  N   -  CA  ANGL. DEV. =  22.8 DEGREES          
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    SER A  90        1.09   -161.28                                   
REMARK 500    GLU A 231       -0.27     65.45                                   
REMARK 500    MET A 337       31.52    -95.86                                   
REMARK 500    SER A 338     -133.55     49.97                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: CYS                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: CATALYTIC SITE.                                    
DBREF  1BI5 A    1   389  UNP    P30074   CHS2_MEDSA       1    389             
SEQADV 1BI5 CSD A  164  UNP  P30074    CYS   164 MODIFIED                       
SEQRES   1 A  389  MET VAL SER VAL SER GLU ILE ARG LYS ALA GLN ARG ALA          
SEQRES   2 A  389  GLU GLY PRO ALA THR ILE LEU ALA ILE GLY THR ALA ASN          
SEQRES   3 A  389  PRO ALA ASN CYS VAL GLU GLN SER THR TYR PRO ASP PHE          
SEQRES   4 A  389  TYR PHE LYS ILE THR ASN SER GLU HIS LYS THR GLU LEU          
SEQRES   5 A  389  LYS GLU LYS PHE GLN ARG MET CYS ASP LYS SER MET ILE          
SEQRES   6 A  389  LYS ARG ARG TYR MET TYR LEU THR GLU GLU ILE LEU LYS          
SEQRES   7 A  389  GLU ASN PRO ASN VAL CYS GLU TYR MET ALA PRO SER LEU          
SEQRES   8 A  389  ASP ALA ARG GLN ASP MET VAL VAL VAL GLU VAL PRO ARG          
SEQRES   9 A  389  LEU GLY LYS GLU ALA ALA VAL LYS ALA ILE LYS GLU TRP          
SEQRES  10 A  389  GLY GLN PRO LYS SER LYS ILE THR HIS LEU ILE VAL CYS          
SEQRES  11 A  389  THR THR SER GLY VAL ASP MET PRO GLY ALA ASP TYR GLN          
SEQRES  12 A  389  LEU THR LYS LEU LEU GLY LEU ARG PRO TYR VAL LYS ARG          
SEQRES  13 A  389  TYR MET MET TYR GLN GLN GLY CSD PHE ALA GLY GLY THR          
SEQRES  14 A  389  VAL LEU ARG LEU ALA LYS ASP LEU ALA GLU ASN ASN LYS          
SEQRES  15 A  389  GLY ALA ARG VAL LEU VAL VAL CYS SER GLU VAL THR ALA          
SEQRES  16 A  389  VAL THR PHE ARG GLY PRO SER ASP THR HIS LEU ASP SER          
SEQRES  17 A  389  LEU VAL GLY GLN ALA LEU PHE GLY ASP GLY ALA ALA ALA          
SEQRES  18 A  389  LEU ILE VAL GLY SER ASP PRO VAL PRO GLU ILE GLU LYS          
SEQRES  19 A  389  PRO ILE PHE GLU MET VAL TRP THR ALA GLN THR ILE ALA          
SEQRES  20 A  389  PRO ASP SER GLU GLY ALA ILE ASP GLY HIS LEU ARG GLU          
SEQRES  21 A  389  ALA GLY LEU THR PHE HIS LEU LEU LYS ASP VAL PRO GLY          
SEQRES  22 A  389  ILE VAL SER LYS ASN ILE THR LYS ALA LEU VAL GLU ALA          
SEQRES  23 A  389  PHE GLU PRO LEU GLY ILE SER ASP TYR ASN SER ILE PHE          
SEQRES  24 A  389  TRP ILE ALA HIS PRO GLY GLY PRO ALA ILE LEU ASP GLN          
SEQRES  25 A  389  VAL GLU GLN LYS LEU ALA LEU LYS PRO GLU LYS MET ASN          
SEQRES  26 A  389  ALA THR ARG GLU VAL LEU SER GLU TYR GLY ASN MET SER          
SEQRES  27 A  389  SER ALA CYS VAL LEU PHE ILE LEU ASP GLU MET ARG LYS          
SEQRES  28 A  389  LYS SER THR GLN ASN GLY LEU LYS THR THR GLY GLU GLY          
SEQRES  29 A  389  LEU GLU TRP GLY VAL LEU PHE GLY PHE GLY PRO GLY LEU          
SEQRES  30 A  389  THR ILE GLU THR VAL VAL LEU ARG SER VAL ALA ILE              
MODRES 1BI5 CSD A  164  CYS  3-SULFINOALANINE                                   
HET    CSD  A 164       8                                                       
HETNAM     CSD 3-SULFINOALANINE                                                 
HETSYN     CSD S-CYSTEINESULFINIC ACID; S-SULFINOCYSTEINE                       
FORMUL   1  CSD    C3 H7 N O4 S                                                 
FORMUL   2  HOH   *479(H2 O)                                                    
HELIX    1   1 VAL A    4  GLN A   11  1                                   8    
HELIX    2   2 TYR A   36  ILE A   43  1                                   8    
HELIX    3   3 THR A   50  ASP A   61  1                                  12    
HELIX    4   4 GLU A   74  LYS A   78  1                                   5    
HELIX    5   5 PRO A   81  CYS A   84  1                                   4    
HELIX    6   6 LEU A   91  TRP A  117  1                                  27    
HELIX    7   7 LYS A  121  LYS A  123  5                                   3    
HELIX    8   8 ALA A  140  LEU A  148  1                                   9    
HELIX    9   9 ALA A  166  GLU A  179  1                                  14    
HELIX   10  10 THR A  194  VAL A  196  5                                   3    
HELIX   11  11 LEU A  206  LEU A  214  1                                   9    
HELIX   12  12 VAL A  271  LEU A  290  1                                  20    
HELIX   13  13 PRO A  307  LEU A  317  1                                  11    
HELIX   14  14 PRO A  321  TYR A  334  5                                  14    
HELIX   15  15 SER A  338  GLN A  355  5                                  18    
SHEET    1   A 2 CYS A  30  GLU A  32  0                                        
SHEET    2   A 2 ARG A  67  TYR A  69 -1  N  ARG A  68   O  VAL A  31           
SHEET    1   B 5 LYS A 155  TYR A 160  0                                        
SHEET    2   B 5 HIS A 126  THR A 131  1  N  LEU A 127   O  LYS A 155           
SHEET    3   B 5 ARG A 185  GLU A 192  1  N  LEU A 187   O  HIS A 126           
SHEET    4   B 5 GLY A 218  GLY A 225 -1  N  VAL A 224   O  VAL A 186           
SHEET    5   B 5 THR A  18  ALA A  25 -1  N  ALA A  25   O  ALA A 219           
SHEET    1   C 4 PHE A 299  ALA A 302  0                                        
SHEET    2   C 4 TRP A 367  GLY A 374  1  N  VAL A 369   O  PHE A 299           
SHEET    3   C 4 THR A 378  SER A 386 -1  N  LEU A 384   O  GLY A 368           
SHEET    4   C 4 PHE A 237  ILE A 246 -1  N  THR A 245   O  ILE A 379           
LINK         N   CSD A 164                 C   GLY A 163     1555   1555  1.34  
LINK         C   CSD A 164                 N   PHE A 165     1555   1555  1.31  
CISPEP   1 MET A  137    PRO A  138          0       -10.92                     
CISPEP   2 GLY A  376    LEU A  377          0        -3.73                     
SITE     1 CYS  1 CSD A 164                                                     
CRYST1   97.540   97.540   65.520  90.00  90.00 120.00 P 32 2 1      6          
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      0.010252  0.005919  0.000000        0.00000                         
SCALE2      0.000000  0.011838  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.015263        0.00000                         
ATOM      1  N   MET A   1      57.211  72.171  83.874  1.00 56.38           N  
ANISOU    1  N   MET A   1     8808   6777   5836  -1450  -1683   -464       N  
ATOM      2  CA  MET A   1      58.174  72.418  82.796  1.00 55.91           C  
ANISOU    2  CA  MET A   1     7831   7521   5892  -1304  -2172     22       C  
ATOM      3  C   MET A   1      57.512  72.502  81.423  1.00 55.72           C  
ANISOU    3  C   MET A   1     7934   7196   6041  -1491  -2298    490       C  
ATOM      4  O   MET A   1      57.538  73.570  80.807  1.00 69.11           O  
ANISOU    4  O   MET A   1    11161   8450   6648  -4226  -3022   1625       O  
ATOM      5  CB  MET A   1      59.253  71.329  82.810  1.00 57.53           C  
ANISOU    5  CB  MET A   1     7880   7952   6029  -1030  -2254    239       C  
ATOM      6  CG  MET A   1      60.038  71.162  81.517  1.00 59.24           C  
ANISOU    6  CG  MET A   1     7810   8302   6397   -962  -1989    189       C  
ATOM      7  SD  MET A   1      60.489  69.437  81.222  1.00118.30           S  
ANISOU    7  SD  MET A   1    20328  10145  14475   2561   4024  -1475       S  
ATOM      8  CE  MET A   1      60.883  69.445  79.469  1.00100.97           C  
ANISOU    8  CE  MET A   1     9257  15392  13716   1549   1086  -4728       C  
ATOM      9  N   VAL A   2      56.931  71.409  80.932  1.00 47.29           N  
ANISOU    9  N   VAL A   2     5443   6421   6102    -71  -2280    470       N  
ATOM     10  CA  VAL A   2      56.388  71.350  79.583  1.00 45.36           C  
ANISOU   10  CA  VAL A   2     5240   6150   5847   -246  -1896    604       C  
ATOM     11  C   VAL A   2      55.166  72.236  79.405  1.00 41.25           C  
ANISOU   11  C   VAL A   2     5077   5413   5184   -617  -1795    455       C  
ATOM     12  O   VAL A   2      54.381  72.339  80.359  1.00 41.81           O  
ANISOU   12  O   VAL A   2     4691   5964   5230   -731  -1807   1133       O  
ATOM     13  CB  VAL A   2      55.968  69.908  79.237  1.00 43.05           C  
ANISOU   13  CB  VAL A   2     4599   5929   5831    147  -2154    784       C  
ATOM     14  CG1 VAL A   2      55.361  69.860  77.835  1.00 39.09           C  
ANISOU   14  CG1 VAL A   2     4284   4764   5806   1084  -2102    787       C  
ATOM     15  CG2 VAL A   2      57.166  68.983  79.391  1.00 42.14           C  
ANISOU   15  CG2 VAL A   2     4262   6223   5527    -54  -2586   1212       C  
ATOM     16  N   SER A   3      55.029  72.814  78.223  1.00 38.43           N  
ANISOU   16  N   SER A   3     4670   4897   5034   -995  -1614    272       N  
ATOM     17  CA  SER A   3      53.924  73.695  77.857  1.00 35.05           C  
ANISOU   17  CA  SER A   3     4520   4303   4494  -1223  -1265    340       C  
ATOM     18  C   SER A   3      52.862  73.023  76.982  1.00 31.01           C  
ANISOU   18  C   SER A   3     4005   3927   3850   -810   -708     15       C  
ATOM     19  O   SER A   3      53.092  72.733  75.804  1.00 27.50           O  
ANISOU   19  O   SER A   3     3356   2915   4178    261   -456    -89       O  
ATOM     20  CB  SER A   3      54.489  74.932  77.133  1.00 37.52           C  
ANISOU   20  CB  SER A   3     5278   4235   4744  -1534   -839     69       C  
ATOM     21  OG  SER A   3      53.492  75.862  76.748  1.00 37.54           O  
ANISOU   21  OG  SER A   3     6409   3520   4333   -912    -93   -306       O  
ATOM     22  N   VAL A   4      51.676  72.794  77.563  1.00 26.94           N  
ANISOU   22  N   VAL A   4     3724   3344   3167    -84   -919     99       N  
ATOM     23  CA  VAL A   4      50.595  72.190  76.774  1.00 24.21           C  
ANISOU   23  CA  VAL A   4     3405   2804   2989    208   -760    103       C  
ATOM     24  C   VAL A   4      50.132  73.155  75.698  1.00 24.80           C  
ANISOU   24  C   VAL A   4     4187   2439   2795   -233   -897     27       C  
ATOM     25  O   VAL A   4      49.745  72.725  74.596  1.00 26.24           O  
ANISOU   25  O   VAL A   4     4952   2325   2694   -395   -822     57       O  
ATOM     26  CB  VAL A   4      49.423  71.742  77.660  1.00 22.94           C  
ANISOU   26  CB  VAL A   4     3382   2704   2629    448   -804    134       C  
ATOM     27  CG1 VAL A   4      48.211  71.283  76.842  1.00 21.87           C  
ANISOU   27  CG1 VAL A   4     3533   2555   2223     95   -578    205       C  
ATOM     28  CG2 VAL A   4      49.866  70.589  78.541  1.00 24.21           C  
ANISOU   28  CG2 VAL A   4     3372   2830   2997    752   -619    275       C  
ATOM     29  N  ASER A   5      50.156  74.459  75.967  0.38 24.12           N  
ANISOU   29  N  ASER A   5     3997   2489   2678   -213   -600   -107       N  
ATOM     30  N  BSER A   5      50.133  74.476  75.934  0.62 24.03           N  
ANISOU   30  N  BSER A   5     3969   2485   2676   -205   -570   -110       N  
ATOM     31  CA ASER A   5      49.764  75.416  74.936  0.38 23.81           C  
ANISOU   31  CA ASER A   5     3882   2382   2784    -80   -365    -60       C  
ATOM     32  CA BSER A   5      49.702  75.354  74.845  0.62 23.67           C  
ANISOU   32  CA BSER A   5     3849   2375   2770    -33   -350    -70       C  
ATOM     33  C  ASER A   5      50.658  75.294  73.706  0.38 23.37           C  
ANISOU   33  C  ASER A   5     3574   2395   2910    -83   -369     49       C  
ATOM     34  C  BSER A   5      50.663  75.250  73.661  0.62 23.41           C  
ANISOU   34  C  BSER A   5     3542   2428   2924    -92   -352     89       C  
ATOM     35  O  ASER A   5      50.168  75.350  72.585  0.38 21.65           O  
ANISOU   35  O  ASER A   5     3197   2188   2840   -386   -219     24       O  
ATOM     36  O  BSER A   5      50.212  75.290  72.527  0.62 22.08           O  
ANISOU   36  O  BSER A   5     3162   2376   2852   -344   -189     48       O  
ATOM     37  CB ASER A   5      49.822  76.840  75.489  0.38 25.33           C  
ANISOU   37  CB ASER A   5     4182   2437   3007   -214   -353   -156       C  
ATOM     38  CB BSER A   5      49.603  76.816  75.263  0.62 25.29           C  
ANISOU   38  CB BSER A   5     4165   2404   3041   -167   -417   -182       C  
ATOM     39  OG ASER A   5      49.074  76.920  76.701  0.38 29.50           O  
ANISOU   39  OG ASER A   5     5292   2667   3251   -471    178   -478       O  
ATOM     40  OG BSER A   5      50.761  77.278  75.924  0.62 29.00           O  
ANISOU   40  OG BSER A   5     4437   3142   3441   -868   -361   -259       O  
ATOM     41  N   GLU A   6      51.951  75.125  73.947  1.00 24.60           N  
ANISOU   41  N   GLU A   6     3580   2680   3086   -331   -541    182       N  
ATOM     42  CA  GLU A   6      52.935  74.967  72.885  1.00 23.79           C  
ANISOU   42  CA  GLU A   6     3195   2773   3071   -390   -684    438       C  
ATOM     43  C   GLU A   6      52.670  73.671  72.144  1.00 21.55           C  
ANISOU   43  C   GLU A   6     2454   2736   2998   -138   -535    401       C  
ATOM     44  O   GLU A   6      52.687  73.620  70.905  1.00 21.33           O  
ANISOU   44  O   GLU A   6     2400   2711   2994   -664   -398    514       O  
ATOM     45  CB  GLU A   6      54.370  75.030  73.440  1.00 27.87           C  
ANISOU   45  CB  GLU A   6     3340   3590   3660   -818   -958    330       C  
ATOM     46  CG  GLU A   6      54.664  76.470  73.864  1.00 37.31           C  
ANISOU   46  CG  GLU A   6     5264   4214   4699  -1757  -1197   -304       C  
ATOM     47  CD  GLU A   6      55.961  76.737  74.589  1.00 40.70           C  
ANISOU   47  CD  GLU A   6     5667   4869   4927  -1889  -1548   -508       C  
ATOM     48  OE1 GLU A   6      56.948  75.997  74.351  1.00 46.74           O  
ANISOU   48  OE1 GLU A   6     5318   6853   5590  -1295  -1141    241       O  
ATOM     49  OE2 GLU A   6      56.039  77.689  75.406  1.00 49.96           O  
ANISOU   49  OE2 GLU A   6     8314   4955   5716  -2734  -2160   -801       O  
ATOM     50  N   ILE A   7      52.413  72.606  72.894  1.00 21.44           N  
ANISOU   50  N   ILE A   7     2671   2923   2555   -713   -855    270       N  
ATOM     51  CA  ILE A   7      52.136  71.331  72.220  1.00 19.06           C  
ANISOU   51  CA  ILE A   7     2097   2764   2382   -206   -424    165       C  
ATOM     52  C   ILE A   7      50.897  71.422  71.341  1.00 17.52           C  
ANISOU   52  C   ILE A   7     1868   2574   2214   -431   -230     48       C  
ATOM     53  O   ILE A   7      50.854  70.932  70.215  1.00 18.39           O  
ANISOU   53  O   ILE A   7     2029   2816   2143   -779    -60     63       O  
ATOM     54  CB  ILE A   7      51.976  70.237  73.278  1.00 19.83           C  
ANISOU   54  CB  ILE A   7     2802   2757   1975   -488   -508    -66       C  
ATOM     55  CG1 ILE A   7      53.301  69.967  74.011  1.00 19.99           C  
ANISOU   55  CG1 ILE A   7     2870   2630   2095   -195   -451    101       C  
ATOM     56  CG2 ILE A   7      51.397  68.932  72.739  1.00 21.55           C  
ANISOU   56  CG2 ILE A   7     3622   2620   1948   -422   -663   -106       C  
ATOM     57  CD1 ILE A   7      53.116  69.133  75.240  1.00 23.62           C  
ANISOU   57  CD1 ILE A   7     3853   2467   2654    260   -309    515       C  
ATOM     58  N   ARG A   8      49.866  72.070  71.879  1.00 18.31           N  
ANISOU   58  N   ARG A   8     2019   2400   2539   -289   -252     44       N  
ATOM     59  CA  ARG A   8      48.585  72.118  71.160  1.00 17.98           C  
ANISOU   59  CA  ARG A   8     2090   2220   2521   -129   -298    228       C  
ATOM     60  C   ARG A   8      48.783  72.888  69.869  1.00 19.65           C  
ANISOU   60  C   ARG A   8     2507   2403   2555   -430   -282    274       C  
ATOM     61  O   ARG A   8      48.291  72.499  68.806  1.00 19.72           O  
ANISOU   61  O   ARG A   8     2492   2530   2471   -392   -177    243       O  
ATOM     62  CB  ARG A   8      47.517  72.736  72.055  1.00 17.43           C  
ANISOU   62  CB  ARG A   8     2076   2025   2521   -200   -394     49       C  
ATOM     63  CG  ARG A   8      46.105  72.746  71.488  1.00 16.23           C  
ANISOU   63  CG  ARG A   8     2004   1958   2204   -376   -232    128       C  
ATOM     64  CD  ARG A   8      45.397  71.395  71.616  1.00 16.89           C  
ANISOU   64  CD  ARG A   8     2531   1993   1894   -588   -103   -133       C  
ATOM     65  NE  ARG A   8      45.720  70.425  70.568  1.00 14.80           N  
ANISOU   65  NE  ARG A   8     1859   2021   1743   -304    -46     76       N  
ATOM     66  CZ  ARG A   8      45.185  70.393  69.345  1.00 14.76           C  
ANISOU   66  CZ  ARG A   8     1851   2155   1601   -262    132     72       C  
ATOM     67  NH1 ARG A   8      44.268  71.304  68.977  1.00 16.08           N  
ANISOU   67  NH1 ARG A   8     1732   2544   1832   -247     35    315       N  
ATOM     68  NH2 ARG A   8      45.517  69.472  68.434  1.00 15.76           N  
ANISOU   68  NH2 ARG A   8     2013   2207   1769   -716    535    -83       N  
ATOM     69  N  ALYS A   9      49.518  73.995  69.943  0.48 22.54           N  
ANISOU   69  N  ALYS A   9     3099   2692   2775   -833   -257    298       N  
ATOM     70  N  BLYS A   9      49.514  73.999  69.937  0.52 22.54           N  
ANISOU   70  N  BLYS A   9     3112   2674   2778   -827   -276    309       N  
ATOM     71  CA ALYS A   9      49.722  74.828  68.751  0.48 22.95           C  
ANISOU   71  CA ALYS A   9     3204   2696   2820   -920   -234    308       C  
ATOM     72  CA BLYS A   9      49.745  74.814  68.740  0.52 23.05           C  
ANISOU   72  CA BLYS A   9     3228   2718   2813   -905   -205    316       C  
ATOM     73  C  ALYS A   9      50.510  74.116  67.661  0.48 23.06           C  
ANISOU   73  C  ALYS A   9     3088   2870   2804   -912   -228    310       C  
ATOM     74  C  BLYS A   9      50.476  74.058  67.639  0.52 23.06           C  
ANISOU   74  C  BLYS A   9     3079   2855   2828   -896   -221    291       C  
ATOM     75  O  ALYS A   9      50.238  74.240  66.456  0.48 24.38           O  
ANISOU   75  O  ALYS A   9     3264   3248   2752   -966    -52    516       O  
ATOM     76  O  BLYS A   9      50.160  74.097  66.442  0.52 24.44           O  
ANISOU   76  O  BLYS A   9     3166   3357   2764   -829    -86    386       O  
ATOM     77  CB ALYS A   9      50.404  76.130  69.197  0.48 24.68           C  
ANISOU   77  CB ALYS A   9     3662   2769   2947  -1094   -337    304       C  
ATOM     78  CB BLYS A   9      50.555  76.057  69.134  0.52 23.64           C  
ANISOU   78  CB BLYS A   9     3392   2746   2843   -969   -315    363       C  
ATOM     79  CG ALYS A   9      49.471  77.072  69.946  0.48 27.24           C  
ANISOU   79  CG ALYS A   9     4047   2998   3303  -1043   -329   -165       C  
ATOM     80  CG BLYS A   9      51.092  76.836  67.938  0.52 24.96           C  
ANISOU   80  CG BLYS A   9     3907   2699   2879  -1111   -541    558       C  
ATOM     81  CD ALYS A   9      50.211  77.908  70.976  0.48 31.92           C  
ANISOU   81  CD ALYS A   9     5118   3365   3645  -1547   -423   -409       C  
ATOM     82  CD BLYS A   9      49.990  77.681  67.317  0.52 26.67           C  
ANISOU   82  CD BLYS A   9     4014   2843   3276   -818   -364    625       C  
ATOM     83  CE ALYS A   9      49.791  79.364  71.011  0.48 33.20           C  
ANISOU   83  CE ALYS A   9     5360   3370   3886  -1536   -221   -589       C  
ATOM     84  CE BLYS A   9      50.504  78.424  66.084  0.52 27.11           C  
ANISOU   84  CE BLYS A   9     4129   2939   3233   -695   -496    774       C  
ATOM     85  NZ ALYS A   9      48.417  79.601  70.507  0.48 37.04           N  
ANISOU   85  NZ ALYS A   9     5639   3757   4678  -1085   -530   -257       N  
ATOM     86  NZ BLYS A   9      49.409  78.795  65.146  0.52 26.95           N  
ANISOU   86  NZ BLYS A   9     4327   2629   3282   -307   -618    322       N  
ATOM     87  N   ALA A  10      51.517  73.336  68.033  1.00 23.57           N  
ANISOU   87  N   ALA A  10     2852   2995   3108   -979   -307    187       N  
ATOM     88  CA  ALA A  10      52.326  72.569  67.096  1.00 22.35           C  
ANISOU   88  CA  ALA A  10     2279   3526   2689  -1031   -364    375       C  
ATOM     89  C   ALA A  10      51.593  71.343  66.581  1.00 21.36           C  
ANISOU   89  C   ALA A  10     2267   3283   2568   -817      0    199       C  
ATOM     90  O   ALA A  10      51.927  70.795  65.538  1.00 25.06           O  
ANISOU   90  O   ALA A  10     2796   4002   2723  -1086    335    -70       O  
ATOM     91  CB  ALA A  10      53.624  72.126  67.787  1.00 22.48           C  
ANISOU   91  CB  ALA A  10     2661   3404   2476   -937   -456    766       C  
ATOM     92  N   GLN A  11      50.583  70.899  67.344  1.00 18.67           N  
ANISOU   92  N   GLN A  11     1933   2845   2315   -508   -261    363       N  
ATOM     93  CA  GLN A  11      49.928  69.648  66.993  1.00 18.80           C  
ANISOU   93  CA  GLN A  11     2379   2853   1911   -640   -214    404       C  
ATOM     94  C   GLN A  11      48.856  69.796  65.920  1.00 18.15           C  
ANISOU   94  C   GLN A  11     2476   2683   1738   -606   -190    297       C  
ATOM     95  O   GLN A  11      48.543  68.791  65.268  1.00 18.18           O  
ANISOU   95  O   GLN A  11     2067   2903   1936   -288     36   -116       O  
ATOM     96  CB  GLN A  11      49.258  69.067  68.248  1.00 17.11           C  
ANISOU   96  CB  GLN A  11     2002   2540   1961   -104   -176    532       C  
ATOM     97  CG  GLN A  11      48.974  67.567  68.201  1.00 18.10           C  
ANISOU   97  CG  GLN A  11     2010   2589   2279   -204     80    423       C  
ATOM     98  CD  GLN A  11      48.347  67.128  69.527  1.00 16.16           C  
ANISOU   98  CD  GLN A  11     1524   2398   2217   -103    -44    370       C  
ATOM     99  OE1 GLN A  11      47.170  67.420  69.721  1.00 16.41           O  
ANISOU   99  OE1 GLN A  11     1535   2474   2224    -58   -174    -41       O  
ATOM    100  NE2 GLN A  11      49.102  66.506  70.426  1.00 15.83           N  
ANISOU  100  NE2 GLN A  11     1514   2150   2349   -323   -201    367       N  
ATOM    101  N   ARG A  12      48.253  70.962  65.757  1.00 17.39           N  
ANISOU  101  N   ARG A  12     2399   2576   1633   -738   -194    303       N  
ATOM    102  CA  ARG A  12      47.056  71.080  64.940  1.00 17.60           C  
ANISOU  102  CA  ARG A  12     2523   2527   1637   -573   -290     50       C  
ATOM    103  C   ARG A  12      47.329  71.525  63.508  1.00 15.73           C  
ANISOU  103  C   ARG A  12     1990   2305   1682   -583   -270     39       C  
ATOM    104  O   ARG A  12      48.372  72.108  63.213  1.00 16.41           O  
ANISOU  104  O   ARG A  12     1771   2425   2038   -387    122   -409       O  
ATOM    105  CB  ARG A  12      46.113  72.052  65.664  1.00 19.24           C  
ANISOU  105  CB  ARG A  12     2433   3043   1835   -550    -11    -38       C  
ATOM    106  CG  ARG A  12      46.634  73.484  65.642  1.00 21.28           C  
ANISOU  106  CG  ARG A  12     3124   2886   2074   -475    150   -504       C  
ATOM    107  CD  ARG A  12      45.994  74.364  66.708  1.00 24.07           C  
ANISOU  107  CD  ARG A  12     3246   3717   2184   -691    449   -850       C  
ATOM    108  NE  ARG A  12      44.545  74.312  66.655  1.00 25.76           N  
ANISOU  108  NE  ARG A  12     3229   4133   2424   -526    476   -768       N  
ATOM    109  CZ  ARG A  12      43.656  74.620  67.584  1.00 25.37           C  
ANISOU  109  CZ  ARG A  12     3205   3926   2508   -215    274  -1138       C  
ATOM    110  NH1 ARG A  12      44.105  75.073  68.781  1.00 23.01           N  
ANISOU  110  NH1 ARG A  12     2996   3310   2435    674   -193   -755       N  
ATOM    111  NH2 ARG A  12      42.342  74.481  67.300  1.00 20.27           N  
ANISOU  111  NH2 ARG A  12     3268   2349   2086  -1050    597   -917       N  
ATOM    112  N   ALA A  13      46.387  71.242  62.599  1.00 15.99           N  
ANISOU  112  N   ALA A  13     2069   2244   1764   -429   -419    131       N  
ATOM    113  CA  ALA A  13      46.529  71.599  61.188  1.00 15.76           C  
ANISOU  113  CA  ALA A  13     2135   2118   1734   -248   -346     47       C  
ATOM    114  C   ALA A  13      46.062  73.038  60.991  1.00 16.85           C  
ANISOU  114  C   ALA A  13     2661   1942   1800   -432   -260     20       C  
ATOM    115  O   ALA A  13      45.571  73.672  61.943  1.00 18.39           O  
ANISOU  115  O   ALA A  13     2847   1868   2273   -485    331     76       O  
ATOM    116  CB  ALA A  13      45.735  70.692  60.254  1.00 13.58           C  
ANISOU  116  CB  ALA A  13     1785   1876   1500   -308    116     85       C  
ATOM    117  N  AGLU A  14      46.194  73.565  59.766  0.48 17.96           N  
ANISOU  117  N  AGLU A  14     2634   2337   1854   -257   -428    236       N  
ATOM    118  N  BGLU A  14      46.213  73.567  59.771  0.52 18.00           N  
ANISOU  118  N  BGLU A  14     2662   2327   1849   -269   -411    228       N  
ATOM    119  CA AGLU A  14      45.842  74.988  59.650  0.48 19.18           C  
ANISOU  119  CA AGLU A  14     2828   2317   2143   -326   -463    372       C  
ATOM    120  CA BGLU A  14      45.828  74.966  59.603  0.52 18.99           C  
ANISOU  120  CA BGLU A  14     2781   2353   2080   -265   -396    353       C  
ATOM    121  C  AGLU A  14      44.658  75.224  58.724  0.48 19.04           C  
ANISOU  121  C  AGLU A  14     2794   2330   2112   -239   -390    436       C  
ATOM    122  C  BGLU A  14      44.540  75.098  58.798  0.52 19.07           C  
ANISOU  122  C  BGLU A  14     2752   2337   2158   -249   -374    412       C  
ATOM    123  O  AGLU A  14      43.830  76.074  59.078  0.48 19.11           O  
ANISOU  123  O  AGLU A  14     2880   2209   2174   -243   -246    566       O  
ATOM    124  O  BGLU A  14      43.593  75.717  59.278  0.52 19.28           O  
ANISOU  124  O  BGLU A  14     2711   2639   1975   -267   -207    562       O  
ATOM    125  CB AGLU A  14      47.070  75.793  59.239  0.48 20.33           C  
ANISOU  125  CB AGLU A  14     2897   2477   2351   -435   -404    358       C  
ATOM    126  CB BGLU A  14      46.925  75.788  58.923  0.52 20.25           C  
ANISOU  126  CB BGLU A  14     2860   2499   2334   -439   -440    426       C  
ATOM    127  CG AGLU A  14      47.575  75.664  57.823  0.48 23.77           C  
ANISOU  127  CG AGLU A  14     3375   2951   2705   -684     83    116       C  
ATOM    128  CG BGLU A  14      46.505  77.231  58.651  0.52 21.16           C  
ANISOU  128  CG BGLU A  14     2974   2470   2596   -472   -426    468       C  
ATOM    129  CD AGLU A  14      48.846  76.449  57.552  0.48 28.43           C  
ANISOU  129  CD AGLU A  14     4148   3321   3333  -1259    585    -51       C  
ATOM    130  CD BGLU A  14      46.180  78.031  59.895  0.52 24.61           C  
ANISOU  130  CD BGLU A  14     2869   3087   3397    -57    -26    -66       C  
ATOM    131  OE1AGLU A  14      48.933  77.631  57.963  0.48 37.50           O  
ANISOU  131  OE1AGLU A  14     6791   3790   3668  -2390    580   -701       O  
ATOM    132  OE1BGLU A  14      47.073  78.225  60.755  0.52 29.27           O  
ANISOU  132  OE1BGLU A  14     3092   4443   3587     33     71  -1392       O  
ATOM    133  OE2AGLU A  14      49.781  75.916  56.921  0.48 34.30           O  
ANISOU  133  OE2AGLU A  14     3113   4752   5168   -375    322    615       O  
ATOM    134  OE2BGLU A  14      45.039  78.505  60.075  0.52 30.87           O  
ANISOU  134  OE2BGLU A  14     3125   3811   4793    399     40     40       O  
ATOM    135  N   GLY A  15      44.529  74.546  57.594  1.00 18.10           N  
ANISOU  135  N   GLY A  15     2389   2346   2142   -480   -304    426       N  
ATOM    136  CA  GLY A  15      43.467  74.779  56.636  1.00 17.39           C  
ANISOU  136  CA  GLY A  15     2220   2221   2166   -455   -223    422       C  
ATOM    137  C   GLY A  15      42.278  73.847  56.737  1.00 15.94           C  
ANISOU  137  C   GLY A  15     2009   1901   2148   -176      0    392       C  
ATOM    138  O   GLY A  15      42.255  72.947  57.582  1.00 15.22           O  
ANISOU  138  O   GLY A  15     2040   1946   1795    -15    222    251       O  
ATOM    139  N   PRO A  16      41.268  74.065  55.903  1.00 14.63           N  
ANISOU  139  N   PRO A  16     2022   1778   1758   -272    110    234       N  
ATOM    140  CA  PRO A  16      40.058  73.251  55.894  1.00 14.48           C  
ANISOU  140  CA  PRO A  16     2109   1717   1676   -315     89    242       C  
ATOM    141  C   PRO A  16      40.355  71.832  55.410  1.00 15.28           C  
ANISOU  141  C   PRO A  16     2027   1818   1961   -319    342    101       C  
ATOM    142  O   PRO A  16      41.172  71.605  54.507  1.00 14.35           O  
ANISOU  142  O   PRO A  16     1892   1952   1609   -118    115    376       O  
ATOM    143  CB  PRO A  16      39.140  73.935  54.876  1.00 15.08           C  
ANISOU  143  CB  PRO A  16     1895   2070   1763   -376    226    538       C  
ATOM    144  CG  PRO A  16      40.100  74.646  53.972  1.00 15.35           C  
ANISOU  144  CG  PRO A  16     1730   2205   1899   -390    185    563       C  
ATOM    145  CD  PRO A  16      41.186  75.171  54.911  1.00 14.60           C  
ANISOU  145  CD  PRO A  16     1788   1933   1825   -245    236    368       C  
ATOM    146  N   ALA A  17      39.655  70.887  56.047  1.00 12.05           N  
ANISOU  146  N   ALA A  17     1438   1664   1475   -176   -101     63       N  
ATOM    147  CA  ALA A  17      39.695  69.500  55.554  1.00 12.71           C  
ANISOU  147  CA  ALA A  17     1870   1737   1223   -178    420     10       C  
ATOM    148  C   ALA A  17      39.316  69.436  54.068  1.00 12.82           C  
ANISOU  148  C   ALA A  17     1992   1656   1223    -20    381     87       C  
ATOM    149  O   ALA A  17      38.285  70.004  53.677  1.00 14.47           O  
ANISOU  149  O   ALA A  17     1978   1902   1619    -32    152      3       O  
ATOM    150  CB  ALA A  17      38.775  68.624  56.400  1.00 13.80           C  
ANISOU  150  CB  ALA A  17     2086   1888   1268   -459    103    277       C  
ATOM    151  N   THR A  18      40.133  68.707  53.298  1.00 13.10           N  
ANISOU  151  N   THR A  18     1899   1771   1305   -228    418   -110       N  
ATOM    152  CA  THR A  18      40.004  68.658  51.843  1.00 11.85           C  
ANISOU  152  CA  THR A  18     1671   1501   1330   -117    371    -73       C  
ATOM    153  C   THR A  18      39.914  67.225  51.334  1.00 12.22           C  
ANISOU  153  C   THR A  18     1590   1523   1532     15    178   -153       C  
ATOM    154  O   THR A  18      40.693  66.364  51.775  1.00 14.64           O  
ANISOU  154  O   THR A  18     1965   1632   1967    186    218    133       O  
ATOM    155  CB  THR A  18      41.198  69.353  51.161  1.00 12.57           C  
ANISOU  155  CB  THR A  18     1600   1934   1244   -291    132    104       C  
ATOM    156  OG1 THR A  18      41.243  70.715  51.630  1.00 15.79           O  
ANISOU  156  OG1 THR A  18     2069   1803   2128   -464    298    134       O  
ATOM    157  CG2 THR A  18      41.019  69.416  49.666  1.00 17.30           C  
ANISOU  157  CG2 THR A  18     2207   3123   1244   -411    177    376       C  
ATOM    158  N   ILE A  19      38.986  66.964  50.420  1.00 13.29           N  
ANISOU  158  N   ILE A  19     1706   1896   1448   -328    248   -141       N  
ATOM    159  CA  ILE A  19      38.927  65.642  49.789  1.00 12.77           C  
ANISOU  159  CA  ILE A  19     1211   1905   1737   -232    225   -250       C  
ATOM    160  C   ILE A  19      39.967  65.617  48.678  1.00 12.55           C  
ANISOU  160  C   ILE A  19     1271   1837   1660    -23    211    -18       C  
ATOM    161  O   ILE A  19      39.906  66.488  47.795  1.00 14.00           O  
ANISOU  161  O   ILE A  19     1825   1764   1732    114    297    -33       O  
ATOM    162  CB  ILE A  19      37.518  65.334  49.237  1.00 12.23           C  
ANISOU  162  CB  ILE A  19     1220   1678   1750    -85     82     47       C  
ATOM    163  CG1 ILE A  19      36.460  65.303  50.340  1.00 13.16           C  
ANISOU  163  CG1 ILE A  19     1188   1784   2029    -90    209    322       C  
ATOM    164  CG2 ILE A  19      37.538  64.040  48.406  1.00 13.11           C  
ANISOU  164  CG2 ILE A  19     1791   1722   1467   -127   -369    114       C  
ATOM    165  CD1 ILE A  19      35.041  65.143  49.847  1.00 15.55           C  
ANISOU  165  CD1 ILE A  19     1228   2577   2102   -123    156    131       C  
ATOM    166  N   LEU A  20      40.896  64.671  48.733  1.00 13.04           N  
ANISOU  166  N   LEU A  20     1512   1720   1721     51    258   -124       N  
ATOM    167  CA  LEU A  20      42.046  64.605  47.848  1.00 12.97           C  
ANISOU  167  CA  LEU A  20     1361   1790   1777    -21    178   -267       C  
ATOM    168  C   LEU A  20      42.035  63.459  46.837  1.00 13.44           C  
ANISOU  168  C   LEU A  20     1566   1827   1714    -19    189   -264       C  
ATOM    169  O   LEU A  20      42.851  63.407  45.902  1.00 14.98           O  
ANISOU  169  O   LEU A  20     1599   2231   1861    -48    266   -445       O  
ATOM    170  CB  LEU A  20      43.323  64.471  48.708  1.00 12.98           C  
ANISOU  170  CB  LEU A  20     1498   1676   1759    -38     98   -103       C  
ATOM    171  CG  LEU A  20      43.510  65.655  49.666  1.00 13.86           C  
ANISOU  171  CG  LEU A  20     2111   1660   1495    -89    -94     35       C  
ATOM    172  CD1 LEU A  20      44.617  65.374  50.680  1.00 17.14           C  
ANISOU  172  CD1 LEU A  20     2324   2275   1915   -386   -456    244       C  
ATOM    173  CD2 LEU A  20      43.798  66.917  48.862  1.00 16.87           C  
ANISOU  173  CD2 LEU A  20     2770   1523   2117    110    100    174       C  
ATOM    174  N   ALA A  21      41.091  62.538  47.010  1.00 13.00           N  
ANISOU  174  N   ALA A  21     1782   1582   1575     -2     40    -61       N  
ATOM    175  CA  ALA A  21      40.959  61.364  46.163  1.00 13.05           C  
ANISOU  175  CA  ALA A  21     1327   1837   1795     79    214   -353       C  
ATOM    176  C   ALA A  21      39.617  60.696  46.429  1.00 13.58           C  
ANISOU  176  C   ALA A  21     1577   1788   1795   -142    -43    174       C  
ATOM    177  O   ALA A  21      39.162  60.779  47.568  1.00 12.75           O  
ANISOU  177  O   ALA A  21     1409   1584   1853   -198     -5    183       O  
ATOM    178  CB  ALA A  21      42.085  60.365  46.405  1.00 13.51           C  
ANISOU  178  CB  ALA A  21     1700   1901   1534    272    349    -18       C  
ATOM    179  N   ILE A  22      39.044  60.083  45.406  1.00 12.83           N  
ANISOU  179  N   ILE A  22     1447   1541   1888    101   -174    178       N  
ATOM    180  CA  ILE A  22      37.799  59.327  45.543  1.00 12.90           C  
ANISOU  180  CA  ILE A  22     1378   1574   1950    148     27   -128       C  
ATOM    181  C   ILE A  22      37.904  58.077  44.672  1.00 12.49           C  
ANISOU  181  C   ILE A  22     1576   1549   1621    147     29    -11       C  
ATOM    182  O   ILE A  22      38.266  58.157  43.484  1.00 15.84           O  
ANISOU  182  O   ILE A  22     2482   1985   1551   -248     37     -9       O  
ATOM    183  CB  ILE A  22      36.544  60.126  45.139  1.00 13.29           C  
ANISOU  183  CB  ILE A  22     1365   1646   2039    161    172     50       C  
ATOM    184  CG1 ILE A  22      36.493  61.519  45.759  1.00 13.02           C  
ANISOU  184  CG1 ILE A  22     1480   1547   1921    225    -82    164       C  
ATOM    185  CG2 ILE A  22      35.267  59.339  45.476  1.00 13.22           C  
ANISOU  185  CG2 ILE A  22     1378   1731   1913     78     35    102       C  
ATOM    186  CD1 ILE A  22      35.403  62.386  45.143  1.00 15.64           C  
ANISOU  186  CD1 ILE A  22     2259   1732   1950    459   -629     71       C  
ATOM    187  N   GLY A  23      37.615  56.916  45.230  1.00 12.03           N  
ANISOU  187  N   GLY A  23     1327   1533   1709    214     -1     16       N  
ATOM    188  CA  GLY A  23      37.602  55.678  44.449  1.00 12.77           C  
ANISOU  188  CA  GLY A  23     1242   1579   2030    119    212   -132       C  
ATOM    189  C   GLY A  23      36.349  54.895  44.821  1.00 12.74           C  
ANISOU  189  C   GLY A  23     1245   1828   1766     12     47    -38       C  
ATOM    190  O   GLY A  23      35.883  54.980  45.970  1.00 13.91           O  
ANISOU  190  O   GLY A  23     1650   1773   1862   -136    249    -95       O  
ATOM    191  N   THR A  24      35.801  54.144  43.872  1.00 14.07           N  
ANISOU  191  N   THR A  24     1576   1875   1895   -137     61   -136       N  
ATOM    192  CA  THR A  24      34.606  53.365  44.219  1.00 12.53           C  
ANISOU  192  CA  THR A  24     1478   1520   1762     61     37   -154       C  
ATOM    193  C   THR A  24      34.756  51.933  43.697  1.00 13.57           C  
ANISOU  193  C   THR A  24     1833   1516   1808    141    402   -101       C  
ATOM    194  O   THR A  24      35.617  51.689  42.842  1.00 14.53           O  
ANISOU  194  O   THR A  24     1816   1939   1768     69    358   -297       O  
ATOM    195  CB  THR A  24      33.314  53.976  43.638  1.00 13.48           C  
ANISOU  195  CB  THR A  24     1514   1823   1787    240    122   -120       C  
ATOM    196  OG1 THR A  24      33.357  53.918  42.192  1.00 14.26           O  
ANISOU  196  OG1 THR A  24     1808   1862   1749   -152    -80      1       O  
ATOM    197  CG2 THR A  24      33.129  55.451  44.000  1.00 14.37           C  
ANISOU  197  CG2 THR A  24     1628   1795   2038    316     95    -58       C  
ATOM    198  N   ALA A  25      33.902  51.057  44.215  1.00 13.42           N  
ANISOU  198  N   ALA A  25     1839   1418   1842    184    304      3       N  
ATOM    199  CA  ALA A  25      33.868  49.664  43.760  1.00 12.01           C  
ANISOU  199  CA  ALA A  25     1529   1442   1592    289    109      8       C  
ATOM    200  C   ALA A  25      32.509  49.053  43.983  1.00 12.68           C  
ANISOU  200  C   ALA A  25     1659   1676   1483     91     -2    124       C  
ATOM    201  O   ALA A  25      31.694  49.557  44.775  1.00 13.11           O  
ANISOU  201  O   ALA A  25     1653   1848   1480    -57    162    205       O  
ATOM    202  CB  ALA A  25      34.892  48.834  44.499  1.00 14.96           C  
ANISOU  202  CB  ALA A  25     1662   1803   2221    458    101    361       C  
ATOM    203  N   ASN A  26      32.165  47.977  43.300  1.00 14.13           N  
ANISOU  203  N   ASN A  26     1732   1839   1800     59   -197    -19       N  
ATOM    204  CA  ASN A  26      30.881  47.312  43.471  1.00 13.50           C  
ANISOU  204  CA  ASN A  26     1664   1654   1812    169   -195     65       C  
ATOM    205  C   ASN A  26      31.071  45.820  43.207  1.00 12.70           C  
ANISOU  205  C   ASN A  26     1477   1701   1649    252    -54     52       C  
ATOM    206  O   ASN A  26      32.005  45.501  42.451  1.00 14.51           O  
ANISOU  206  O   ASN A  26     1648   2090   1777    269    102    -19       O  
ATOM    207  CB  ASN A  26      29.850  47.835  42.475  1.00 14.30           C  
ANISOU  207  CB  ASN A  26     1619   1829   1984    310   -119    226       C  
ATOM    208  CG  ASN A  26      29.620  49.329  42.475  1.00 13.35           C  
ANISOU  208  CG  ASN A  26     1537   1812   1725    267     43    166       C  
ATOM    209  OD1 ASN A  26      30.390  50.039  41.823  1.00 13.13           O  
ANISOU  209  OD1 ASN A  26     1498   1815   1674    149     37    -18       O  
ATOM    210  ND2 ASN A  26      28.627  49.843  43.203  1.00 15.04           N  
ANISOU  210  ND2 ASN A  26     1874   1898   1941     72    379    -70       N  
ATOM    211  N   PRO A  27      30.234  44.958  43.767  1.00 13.41           N  
ANISOU  211  N   PRO A  27     1660   1667   1769     85     26   -132       N  
ATOM    212  CA  PRO A  27      30.244  43.530  43.389  1.00 15.25           C  
ANISOU  212  CA  PRO A  27     2177   1690   1927     91    -11   -244       C  
ATOM    213  C   PRO A  27      30.079  43.386  41.875  1.00 14.80           C  
ANISOU  213  C   PRO A  27     2156   1574   1894    272     66   -181       C  
ATOM    214  O   PRO A  27      29.477  44.231  41.203  1.00 15.74           O  
ANISOU  214  O   PRO A  27     1792   1976   2212    233   -148    -25       O  
ATOM    215  CB  PRO A  27      29.046  42.958  44.141  1.00 15.46           C  
ANISOU  215  CB  PRO A  27     2446   1624   1806    -86    -70    -34       C  
ATOM    216  CG  PRO A  27      28.972  43.841  45.369  1.00 15.20           C  
ANISOU  216  CG  PRO A  27     2364   1580   1833   -203     47    -37       C  
ATOM    217  CD  PRO A  27      29.215  45.237  44.800  1.00 13.80           C  
ANISOU  217  CD  PRO A  27     1868   1580   1796     39    173      8       C  
ATOM    218  N   ALA A  28      30.644  42.302  41.307  1.00 16.26           N  
ANISOU  218  N   ALA A  28     2283   1788   2108    271    531   -232       N  
ATOM    219  CA  ALA A  28      30.586  42.125  39.856  1.00 16.77           C  
ANISOU  219  CA  ALA A  28     2239   2031   2100    419    555   -253       C  
ATOM    220  C   ALA A  28      29.210  41.738  39.335  1.00 19.78           C  
ANISOU  220  C   ALA A  28     2638   2626   2251   -176    373   -210       C  
ATOM    221  O   ALA A  28      28.892  41.905  38.141  1.00 22.47           O  
ANISOU  221  O   ALA A  28     2745   3429   2364   -147    211    -39       O  
ATOM    222  CB  ALA A  28      31.616  41.079  39.431  1.00 19.04           C  
ANISOU  222  CB  ALA A  28     3343   1869   2020    993    198   -320       C  
ATOM    223  N   ASN A  29      28.295  41.253  40.157  1.00 18.31           N  
ANISOU  223  N   ASN A  29     2317   2214   2426    246    520   -353       N  
ATOM    224  CA  ASN A  29      26.986  40.836  39.648  1.00 16.84           C  
ANISOU  224  CA  ASN A  29     2530   2040   1827    101    374      1       C  
ATOM    225  C   ASN A  29      26.045  42.020  39.417  1.00 17.46           C  
ANISOU  225  C   ASN A  29     2559   2118   1958    142    226    -81       C  
ATOM    226  O   ASN A  29      25.555  42.645  40.354  1.00 16.70           O  
ANISOU  226  O   ASN A  29     2472   2083   1789    227   -142   -167       O  
ATOM    227  CB  ASN A  29      26.387  39.835  40.645  1.00 17.78           C  
ANISOU  227  CB  ASN A  29     3054   1999   1703    -97    448   -152       C  
ATOM    228  CG  ASN A  29      24.973  39.429  40.265  1.00 20.28           C  
ANISOU  228  CG  ASN A  29     3237   2558   1909   -588    565   -200       C  
ATOM    229  OD1 ASN A  29      24.662  39.314  39.064  1.00 21.60           O  
ANISOU  229  OD1 ASN A  29     3416   2795   1995  -1164    424   -144       O  
ATOM    230  ND2 ASN A  29      24.147  39.234  41.295  1.00 17.50           N  
ANISOU  230  ND2 ASN A  29     2892   1614   2145    560    709     94       N  
ATOM    231  N   CYS A  30      25.785  42.317  38.129  1.00 16.60           N  
ANISOU  231  N   CYS A  30     2136   2266   1906    252    249   -186       N  
ATOM    232  CA  CYS A  30      24.922  43.442  37.773  1.00 16.15           C  
ANISOU  232  CA  CYS A  30     1957   2243   1935    189    271   -216       C  
ATOM    233  C   CYS A  30      23.504  42.963  37.576  1.00 16.68           C  
ANISOU  233  C   CYS A  30     2059   2143   2136    145    180   -477       C  
ATOM    234  O   CYS A  30      23.259  42.059  36.766  1.00 20.17           O  
ANISOU  234  O   CYS A  30     2494   2636   2534    227   -101   -898       O  
ATOM    235  CB  CYS A  30      25.461  44.099  36.496  1.00 18.95           C  
ANISOU  235  CB  CYS A  30     2641   2419   2142   -121    197     82       C  
ATOM    236  SG  CYS A  30      24.482  45.515  35.924  1.00 21.84           S  
ANISOU  236  SG  CYS A  30     2825   2876   2597    175    377    466       S  
ATOM    237  N   VAL A  31      22.562  43.520  38.315  1.00 16.00           N  
ANISOU  237  N   VAL A  31     1934   2099   2045     59    279   -217       N  
ATOM    238  CA  VAL A  31      21.187  43.034  38.308  1.00 15.27           C  
ANISOU  238  CA  VAL A  31     1898   2019   1884    140   -110    -64       C  
ATOM    239  C   VAL A  31      20.244  44.059  37.687  1.00 14.82           C  
ANISOU  239  C   VAL A  31     2225   1702   1705     22   -188    -69       C  
ATOM    240  O   VAL A  31      20.025  45.136  38.249  1.00 15.04           O  
ANISOU  240  O   VAL A  31     2010   1922   1782    104    223   -178       O  
ATOM    241  CB  VAL A  31      20.780  42.724  39.762  1.00 16.19           C  
ANISOU  241  CB  VAL A  31     1631   2370   2148    241    -17    452       C  
ATOM    242  CG1 VAL A  31      19.320  42.273  39.801  1.00 19.51           C  
ANISOU  242  CG1 VAL A  31     1754   2985   2672    -80   -121    436       C  
ATOM    243  CG2 VAL A  31      21.718  41.707  40.428  1.00 17.13           C  
ANISOU  243  CG2 VAL A  31     2028   2103   2375    320   -194    292       C  
ATOM    244  N   GLU A  32      19.657  43.765  36.526  1.00 16.01           N  
ANISOU  244  N   GLU A  32     2143   2014   1924   -152   -360    -86       N  
ATOM    245  CA  GLU A  32      18.801  44.740  35.846  1.00 14.94           C  
ANISOU  245  CA  GLU A  32     2056   2068   1554    138   -213   -462       C  
ATOM    246  C   GLU A  32      17.506  44.949  36.591  1.00 15.03           C  
ANISOU  246  C   GLU A  32     2413   1777   1522      0    161   -233       C  
ATOM    247  O   GLU A  32      16.878  43.998  37.041  1.00 16.57           O  
ANISOU  247  O   GLU A  32     2613   1930   1752   -128    -86     56       O  
ATOM    248  CB  GLU A  32      18.427  44.262  34.427  1.00 18.05           C  
ANISOU  248  CB  GLU A  32     2776   2852   1230     -4    -38   -320       C  
ATOM    249  CG  GLU A  32      19.664  44.232  33.533  1.00 22.48           C  
ANISOU  249  CG  GLU A  32     3358   3340   1844   -163    568   -442       C  
ATOM    250  CD  GLU A  32      20.108  45.630  33.142  1.00 27.56           C  
ANISOU  250  CD  GLU A  32     3966   3808   2698   -890    700   -237       C  
ATOM    251  OE1 GLU A  32      19.262  46.413  32.642  1.00 32.16           O  
ANISOU  251  OE1 GLU A  32     5172   3405   3642   -590    588    270       O  
ATOM    252  OE2 GLU A  32      21.299  45.954  33.326  1.00 39.62           O  
ANISOU  252  OE2 GLU A  32     4732   5784   4536  -2167   -213    -79       O  
ATOM    253  N   GLN A  33      17.073  46.191  36.702  1.00 14.44           N  
ANISOU  253  N   GLN A  33     2363   1798   1328    -34    246   -339       N  
ATOM    254  CA  GLN A  33      15.839  46.421  37.444  1.00 14.95           C  
ANISOU  254  CA  GLN A  33     2229   1962   1490     18    203   -134       C  
ATOM    255  C   GLN A  33      14.634  45.992  36.635  1.00 16.79           C  
ANISOU  255  C   GLN A  33     2392   2292   1696   -236    134   -168       C  
ATOM    256  O   GLN A  33      13.666  45.583  37.242  1.00 18.29           O  
ANISOU  256  O   GLN A  33     2404   2764   1781   -334     27    149       O  
ATOM    257  CB  GLN A  33      15.761  47.906  37.755  1.00 14.19           C  
ANISOU  257  CB  GLN A  33     1761   1931   1700     73    312    -84       C  
ATOM    258  CG  GLN A  33      14.717  48.332  38.769  1.00 14.12           C  
ANISOU  258  CG  GLN A  33     1805   2043   1516    213    296    137       C  
ATOM    259  CD  GLN A  33      14.998  47.927  40.206  1.00 14.65           C  
ANISOU  259  CD  GLN A  33     1995   2030   1540     77     76     85       C  
ATOM    260  OE1 GLN A  33      15.591  46.877  40.469  1.00 14.27           O  
ANISOU  260  OE1 GLN A  33     1700   1956   1764   -145     39    256       O  
ATOM    261  NE2 GLN A  33      14.564  48.727  41.187  1.00 14.62           N  
ANISOU  261  NE2 GLN A  33     1950   2020   1586   -293   -179   -227       N  
ATOM    262  N   SER A  34      14.674  46.111  35.309  1.00 17.07           N  
ANISOU  262  N   SER A  34     2217   2552   1717   -233     14    -35       N  
ATOM    263  CA  SER A  34      13.489  45.842  34.486  1.00 21.45           C  
ANISOU  263  CA  SER A  34     2940   2874   2335   -583   -650    195       C  
ATOM    264  C   SER A  34      12.904  44.457  34.748  1.00 21.77           C  
ANISOU  264  C   SER A  34     3198   2867   2207   -722   -673     50       C  
ATOM    265  O   SER A  34      11.674  44.283  34.728  1.00 26.45           O  
ANISOU  265  O   SER A  34     3249   3291   3508   -899   -930    865       O  
ATOM    266  CB  SER A  34      13.795  45.957  32.990  1.00 23.13           C  
ANISOU  266  CB  SER A  34     3431   3125   2234   -665   -944    419       C  
ATOM    267  OG  SER A  34      14.904  45.119  32.648  1.00 24.60           O  
ANISOU  267  OG  SER A  34     3920   3076   2352   -715   -109    355       O  
ATOM    268  N   THR A  35      13.812  43.517  34.981  1.00 21.50           N  
ANISOU  268  N   THR A  35     3316   2735   2119   -655   -446    -75       N  
ATOM    269  CA  THR A  35      13.465  42.108  35.132  1.00 22.05           C  
ANISOU  269  CA  THR A  35     3499   2729   2149   -736   -515   -235       C  
ATOM    270  C   THR A  35      13.574  41.652  36.576  1.00 19.65           C  
ANISOU  270  C   THR A  35     2757   2572   2136   -536    -98   -192       C  
ATOM    271  O   THR A  35      13.423  40.475  36.899  1.00 20.88           O  
ANISOU  271  O   THR A  35     2794   2580   2559   -666  -1017    -69       O  
ATOM    272  CB  THR A  35      14.377  41.215  34.265  1.00 22.47           C  
ANISOU  272  CB  THR A  35     4041   2716   1780   -618   -263     28       C  
ATOM    273  OG1 THR A  35      15.743  41.476  34.591  1.00 27.81           O  
ANISOU  273  OG1 THR A  35     3636   3909   3021   -860    448    606       O  
ATOM    274  CG2 THR A  35      14.244  41.501  32.764  1.00 32.47           C  
ANISOU  274  CG2 THR A  35     6880   3812   1645  -2056   -101     24       C  
ATOM    275  N   TYR A  36      13.866  42.580  37.490  1.00 16.74           N  
ANISOU  275  N   TYR A  36     1959   2454   1947   -477    -56    -27       N  
ATOM    276  CA  TYR A  36      14.050  42.162  38.885  1.00 16.91           C  
ANISOU  276  CA  TYR A  36     1951   2448   2026   -285    -71     57       C  
ATOM    277  C   TYR A  36      12.792  41.626  39.551  1.00 16.90           C  
ANISOU  277  C   TYR A  36     1989   2326   2106   -138      6    223       C  
ATOM    278  O   TYR A  36      12.898  40.660  40.312  1.00 17.13           O  
ANISOU  278  O   TYR A  36     2359   2339   1810   -145    -40    106       O  
ATOM    279  CB  TYR A  36      14.646  43.330  39.718  1.00 16.90           C  
ANISOU  279  CB  TYR A  36     1916   2583   1923   -175    -97    -64       C  
ATOM    280  CG  TYR A  36      15.182  42.815  41.029  1.00 17.47           C  
ANISOU  280  CG  TYR A  36     2348   2315   1974   -236   -115     57       C  
ATOM    281  CD1 TYR A  36      16.237  41.892  41.063  1.00 17.41           C  
ANISOU  281  CD1 TYR A  36     2433   2552   1629    -73    -81     10       C  
ATOM    282  CD2 TYR A  36      14.641  43.230  42.252  1.00 16.04           C  
ANISOU  282  CD2 TYR A  36     2231   1936   1927   -135   -376    -58       C  
ATOM    283  CE1 TYR A  36      16.731  41.407  42.279  1.00 18.04           C  
ANISOU  283  CE1 TYR A  36     2716   2486   1653    -92   -258    -76       C  
ATOM    284  CE2 TYR A  36      15.123  42.756  43.469  1.00 16.26           C  
ANISOU  284  CE2 TYR A  36     2239   1982   1957   -265   -479    -39       C  
ATOM    285  CZ  TYR A  36      16.170  41.840  43.463  1.00 16.25           C  
ANISOU  285  CZ  TYR A  36     2215   2338   1623   -118   -338     47       C  
ATOM    286  OH  TYR A  36      16.657  41.380  44.676  1.00 15.97           O  
ANISOU  286  OH  TYR A  36     2352   2050   1667   -248    -24    442       O  
ATOM    287  N   PRO A  37      11.609  42.170  39.373  1.00 17.60           N  
ANISOU  287  N   PRO A  37     2023   2289   2377    -39    144     75       N  
ATOM    288  CA  PRO A  37      10.431  41.557  40.028  1.00 18.19           C  
ANISOU  288  CA  PRO A  37     2061   2168   2684    -28    279     14       C  
ATOM    289  C   PRO A  37      10.240  40.075  39.702  1.00 18.53           C  
ANISOU  289  C   PRO A  37     2302   2281   2459   -187    -23   -116       C  
ATOM    290  O   PRO A  37       9.882  39.321  40.601  1.00 19.30           O  
ANISOU  290  O   PRO A  37     2685   2159   2490   -110   -552    163       O  
ATOM    291  CB  PRO A  37       9.257  42.371  39.457  1.00 19.07           C  
ANISOU  291  CB  PRO A  37     2017   2415   2815   -164    138    266       C  
ATOM    292  CG  PRO A  37       9.887  43.722  39.210  1.00 17.57           C  
ANISOU  292  CG  PRO A  37     1702   2523   2450   -123    172    441       C  
ATOM    293  CD  PRO A  37      11.229  43.386  38.624  1.00 17.56           C  
ANISOU  293  CD  PRO A  37     1879   2244   2549     31    195     66       C  
ATOM    294  N   ASP A  38      10.466  39.667  38.463  1.00 19.88           N  
ANISOU  294  N   ASP A  38     2139   2831   2583     99    -66   -345       N  
ATOM    295  CA  ASP A  38      10.405  38.280  38.039  1.00 21.07           C  
ANISOU  295  CA  ASP A  38     2618   2923   2463   -126    214   -443       C  
ATOM    296  C   ASP A  38      11.474  37.463  38.739  1.00 20.63           C  
ANISOU  296  C   ASP A  38     2615   2487   2738   -121    450   -285       C  
ATOM    297  O   ASP A  38      11.208  36.389  39.280  1.00 22.97           O  
ANISOU  297  O   ASP A  38     3504   2857   2368   -909   -328   -139       O  
ATOM    298  CB  ASP A  38      10.650  38.226  36.532  1.00 27.48           C  
ANISOU  298  CB  ASP A  38     4116   3926   2399   -112    105   -646       C  
ATOM    299  CG  ASP A  38       9.416  37.796  35.793  1.00 34.42           C  
ANISOU  299  CG  ASP A  38     4585   5870   2623   -876    345  -1949       C  
ATOM    300  OD1 ASP A  38       8.297  38.041  36.291  1.00 45.40           O  
ANISOU  300  OD1 ASP A  38     4129   8126   4995   -488    272  -2206       O  
ATOM    301  OD2 ASP A  38       9.529  37.200  34.701  1.00 52.60           O  
ANISOU  301  OD2 ASP A  38     7903   7930   4153  -2933   1105  -4013       O  
ATOM    302  N   PHE A  39      12.700  38.000  38.737  1.00 19.46           N  
ANISOU  302  N   PHE A  39     2645   2722   2026   -205    233    -77       N  
ATOM    303  CA  PHE A  39      13.787  37.273  39.383  1.00 18.25           C  
ANISOU  303  CA  PHE A  39     2664   2316   1953     87    502   -425       C  
ATOM    304  C   PHE A  39      13.519  37.092  40.873  1.00 16.97           C  
ANISOU  304  C   PHE A  39     2543   1954   1952    134    410   -299       C  
ATOM    305  O   PHE A  39      13.673  36.001  41.478  1.00 19.23           O  
ANISOU  305  O   PHE A  39     2999   2098   2211    108   -481   -200       O  
ATOM    306  CB  PHE A  39      15.119  38.019  39.130  1.00 19.19           C  
ANISOU  306  CB  PHE A  39     2563   2718   2011     97    493   -223       C  
ATOM    307  CG  PHE A  39      16.291  37.410  39.902  1.00 23.32           C  
ANISOU  307  CG  PHE A  39     2870   3197   2793    112    -75   -187       C  
ATOM    308  CD1 PHE A  39      16.986  36.333  39.387  1.00 25.28           C  
ANISOU  308  CD1 PHE A  39     2815   3561   3229    520   -273   -217       C  
ATOM    309  CD2 PHE A  39      16.686  37.917  41.134  1.00 25.11           C  
ANISOU  309  CD2 PHE A  39     3124   3496   2921   -153   -331   -147       C  
ATOM    310  CE1 PHE A  39      18.038  35.773  40.110  1.00 27.09           C  
ANISOU  310  CE1 PHE A  39     3003   3859   3430    451   -703   -407       C  
ATOM    311  CE2 PHE A  39      17.707  37.380  41.886  1.00 26.06           C  
ANISOU  311  CE2 PHE A  39     3093   3742   3069    -43   -350   -170       C  
ATOM    312  CZ  PHE A  39      18.381  36.298  41.347  1.00 28.06           C  
ANISOU  312  CZ  PHE A  39     3483   3819   3360    179   -609   -343       C  
ATOM    313  N   TYR A  40      13.132  38.173  41.538  1.00 16.89           N  
ANISOU  313  N   TYR A  40     2498   2027   1891   -128    233   -543       N  
ATOM    314  CA  TYR A  40      13.005  38.183  43.006  1.00 16.14           C  
ANISOU  314  CA  TYR A  40     2183   2083   1866    -64     29   -483       C  
ATOM    315  C   TYR A  40      11.833  37.332  43.477  1.00 16.26           C  
ANISOU  315  C   TYR A  40     2290   2071   1816    -64   -155    -84       C  
ATOM    316  O   TYR A  40      11.930  36.605  44.479  1.00 18.66           O  
ANISOU  316  O   TYR A  40     3031   2041   2017   -116   -406     20       O  
ATOM    317  CB  TYR A  40      12.875  39.639  43.474  1.00 15.31           C  
ANISOU  317  CB  TYR A  40     1938   2111   1767    -31     71   -498       C  
ATOM    318  CG  TYR A  40      12.476  39.827  44.924  1.00 15.30           C  
ANISOU  318  CG  TYR A  40     2005   2034   1773      6    152   -348       C  
ATOM    319  CD1 TYR A  40      13.413  39.654  45.938  1.00 15.53           C  
ANISOU  319  CD1 TYR A  40     2129   2039   1732    114    123   -475       C  
ATOM    320  CD2 TYR A  40      11.171  40.178  45.272  1.00 15.45           C  
ANISOU  320  CD2 TYR A  40     1962   2034   1874   -150    219   -356       C  
ATOM    321  CE1 TYR A  40      13.088  39.813  47.275  1.00 15.16           C  
ANISOU  321  CE1 TYR A  40     1859   2128   1771     99    171   -509       C  
ATOM    322  CE2 TYR A  40      10.814  40.342  46.600  1.00 15.16           C  
ANISOU  322  CE2 TYR A  40     1874   2046   1842     17    109   -359       C  
ATOM    323  CZ  TYR A  40      11.771  40.160  47.587  1.00 15.45           C  
ANISOU  323  CZ  TYR A  40     1706   2219   1946    -89     96   -459       C  
ATOM    324  OH  TYR A  40      11.380  40.339  48.885  1.00 13.81           O  
ANISOU  324  OH  TYR A  40     1490   1909   1850    327    135    186       O  
ATOM    325  N   PHE A  41      10.691  37.420  42.779  1.00 16.82           N  
ANISOU  325  N   PHE A  41     2175   2174   2044    -74   -132      0       N  
ATOM    326  CA  PHE A  41       9.559  36.623  43.248  1.00 19.14           C  
ANISOU  326  CA  PHE A  41     2324   2300   2648   -202   -193    279       C  
ATOM    327  C   PHE A  41       9.837  35.154  42.968  1.00 20.51           C  
ANISOU  327  C   PHE A  41     2789   2292   2713   -324   -219    112       C  
ATOM    328  O   PHE A  41       9.388  34.278  43.709  1.00 22.29           O  
ANISOU  328  O   PHE A  41     3551   2229   2689   -887   -222   -137       O  
ATOM    329  CB  PHE A  41       8.233  37.094  42.621  1.00 18.12           C  
ANISOU  329  CB  PHE A  41     2282   2447   2155   -485   -263    304       C  
ATOM    330  CG  PHE A  41       7.608  38.128  43.561  1.00 18.47           C  
ANISOU  330  CG  PHE A  41     2044   2383   2590   -335   -278    282       C  
ATOM    331  CD1 PHE A  41       8.159  39.397  43.594  1.00 20.51           C  
ANISOU  331  CD1 PHE A  41     2340   2568   2885   -594    -19      3       C  
ATOM    332  CD2 PHE A  41       6.539  37.857  44.388  1.00 19.27           C  
ANISOU  332  CD2 PHE A  41     2228   2348   2745   -347    -89    209       C  
ATOM    333  CE1 PHE A  41       7.647  40.352  44.447  1.00 19.72           C  
ANISOU  333  CE1 PHE A  41     2175   2528   2790   -508   -174     67       C  
ATOM    334  CE2 PHE A  41       6.007  38.809  45.236  1.00 18.89           C  
ANISOU  334  CE2 PHE A  41     2056   2406   2716   -419   -269     89       C  
ATOM    335  CZ  PHE A  41       6.565  40.083  45.266  1.00 19.64           C  
ANISOU  335  CZ  PHE A  41     2307   2510   2644   -587   -159     44       C  
ATOM    336  N  ALYS A  42      10.602  34.874  41.913  0.20 21.01           N  
ANISOU  336  N  ALYS A  42     2853   2459   2670   -258   -303    -47       N  
ATOM    337  N  BLYS A  42      10.592  34.868  41.899  0.80 20.59           N  
ANISOU  337  N  BLYS A  42     2704   2477   2642   -268   -371    -56       N  
ATOM    338  CA ALYS A  42      10.961  33.493  41.603  0.20 22.01           C  
ANISOU  338  CA ALYS A  42     3185   2470   2707   -231   -333   -103       C  
ATOM    339  CA BLYS A  42      10.927  33.461  41.680  0.80 22.08           C  
ANISOU  339  CA BLYS A  42     3149   2503   2738   -155   -346    -67       C  
ATOM    340  C  ALYS A  42      11.977  32.932  42.592  0.20 22.12           C  
ANISOU  340  C  ALYS A  42     3249   2358   2796   -194   -339    -34       C  
ATOM    341  C  BLYS A  42      11.932  32.943  42.703  0.80 22.09           C  
ANISOU  341  C  BLYS A  42     3259   2353   2783   -224   -387     57       C  
ATOM    342  O  ALYS A  42      11.822  31.797  43.060  0.20 23.46           O  
ANISOU  342  O  ALYS A  42     3842   2145   2926   -127   -442   -212       O  
ATOM    343  O  BLYS A  42      11.718  31.873  43.301  0.80 23.81           O  
ANISOU  343  O  BLYS A  42     3989   2096   2962   -228   -460    -53       O  
ATOM    344  CB ALYS A  42      11.492  33.396  40.171  0.20 23.09           C  
ANISOU  344  CB ALYS A  42     3561   2524   2689   -310   -307   -220       C  
ATOM    345  CB BLYS A  42      11.455  33.264  40.250  0.80 22.95           C  
ANISOU  345  CB BLYS A  42     3565   2456   2699   -194   -346   -144       C  
ATOM    346  CG ALYS A  42      12.586  32.365  39.971  0.20 23.54           C  
ANISOU  346  CG ALYS A  42     3596   2548   2800   -333   -153   -315       C  
ATOM    347  CG BLYS A  42      10.313  33.009  39.282  0.80 26.31           C  
ANISOU  347  CG BLYS A  42     4269   2785   2941   -778   -675   -204       C  
ATOM    348  CD ALYS A  42      12.842  32.109  38.494  0.20 26.17           C  
ANISOU  348  CD ALYS A  42     4115   2848   2982   -833    262   -595       C  
ATOM    349  CD BLYS A  42      10.515  33.615  37.918  0.80 30.52           C  
ANISOU  349  CD BLYS A  42     5046   3413   3138  -1451  -1307    188       C  
ATOM    350  CE ALYS A  42      14.285  32.438  38.134  0.20 26.36           C  
ANISOU  350  CE ALYS A  42     4017   2851   3146   -734    251   -824       C  
ATOM    351  CE BLYS A  42       9.676  32.977  36.833  0.80 29.30           C  
ANISOU  351  CE BLYS A  42     4434   3406   3294   -939  -1313    -30       C  
ATOM    352  NZ ALYS A  42      14.375  33.469  37.060  0.20 19.02           N  
ANISOU  352  NZ ALYS A  42     1846   2839   2543    436    547  -1135       N  
ATOM    353  NZ BLYS A  42       8.425  33.775  36.605  0.80 27.83           N  
ANISOU  353  NZ BLYS A  42     4063   3093   3419   -863   -705  -1221       N  
ATOM    354  N   ILE A  43      13.014  33.695  42.934  1.00 21.27           N  
ANISOU  354  N   ILE A  43     2918   2464   2699    -53   -149   -139       N  
ATOM    355  CA  ILE A  43      14.041  33.177  43.848  1.00 20.80           C  
ANISOU  355  CA  ILE A  43     2738   2279   2888     31      4     -7       C  
ATOM    356  C   ILE A  43      13.553  33.052  45.287  1.00 20.46           C  
ANISOU  356  C   ILE A  43     2594   2336   2845   -116   -128    125       C  
ATOM    357  O   ILE A  43      14.058  32.216  46.042  1.00 21.75           O  
ANISOU  357  O   ILE A  43     2523   2669   3073   -462   -722    271       O  
ATOM    358  CB  ILE A  43      15.319  34.040  43.790  1.00 20.30           C  
ANISOU  358  CB  ILE A  43     2848   2257   2609    -48    -89    212       C  
ATOM    359  CG1 ILE A  43      16.586  33.302  44.231  1.00 20.57           C  
ANISOU  359  CG1 ILE A  43     2695   2200   2918     36    167     64       C  
ATOM    360  CG2 ILE A  43      15.199  35.311  44.610  1.00 18.88           C  
ANISOU  360  CG2 ILE A  43     2377   2298   2497    101   -246    214       C  
ATOM    361  CD1 ILE A  43      16.812  32.028  43.456  1.00 25.95           C  
ANISOU  361  CD1 ILE A  43     3549   2840   3473    460   -169   -583       C  
ATOM    362  N   THR A  44      12.569  33.861  45.669  1.00 21.37           N  
ANISOU  362  N   THR A  44     2904   2281   2936   -193     37   -301       N  
ATOM    363  CA  THR A  44      11.992  33.765  47.004  1.00 22.08           C  
ANISOU  363  CA  THR A  44     3149   2294   2948   -198     75   -182       C  
ATOM    364  C   THR A  44      10.789  32.820  47.020  1.00 22.90           C  
ANISOU  364  C   THR A  44     3290   2695   2717   -426    -75     22       C  
ATOM    365  O   THR A  44      10.073  32.806  48.024  1.00 22.86           O  
ANISOU  365  O   THR A  44     3547   2454   2686   -345    -20    460       O  
ATOM    366  CB  THR A  44      11.562  35.137  47.568  1.00 21.11           C  
ANISOU  366  CB  THR A  44     2711   2439   2872     78     54    -95       C  
ATOM    367  OG1 THR A  44      10.565  35.703  46.708  1.00 18.69           O  
ANISOU  367  OG1 THR A  44     2663   2252   2187   -433     44   -144       O  
ATOM    368  CG2 THR A  44      12.774  36.064  47.602  1.00 20.74           C  
ANISOU  368  CG2 THR A  44     3062   2243   2576    -41   -731     46       C  
ATOM    369  N   ASN A  45      10.569  32.062  45.952  1.00 24.46           N  
ANISOU  369  N   ASN A  45     3591   2996   2707   -561   -443      9       N  
ATOM    370  CA  ASN A  45       9.466  31.115  45.959  1.00 25.73           C  
ANISOU  370  CA  ASN A  45     3553   3114   3108   -587   -869    236       C  
ATOM    371  C   ASN A  45       8.118  31.760  46.231  1.00 25.12           C  
ANISOU  371  C   ASN A  45     3642   2958   2944   -741   -470     41       C  
ATOM    372  O   ASN A  45       7.306  31.132  46.922  1.00 30.18           O  
ANISOU  372  O   ASN A  45     4089   3448   3931   -709    -99    692       O  
ATOM    373  CB  ASN A  45       9.744  30.085  47.059  1.00 33.68           C  
ANISOU  373  CB  ASN A  45     5428   2689   4680   -631  -1223    886       C  
ATOM    374  CG  ASN A  45       9.941  28.680  46.539  1.00 40.63           C  
ANISOU  374  CG  ASN A  45     7026   2895   5516   -661   -312    535       C  
ATOM    375  OD1 ASN A  45      10.818  28.433  45.692  1.00 52.14           O  
ANISOU  375  OD1 ASN A  45     8371   4694   6745    -44    673   -146       O  
ATOM    376  ND2 ASN A  45       9.128  27.772  47.073  1.00 51.36           N  
ANISOU  376  ND2 ASN A  45     8702   3547   7265  -2899   -214   -666       N  
ATOM    377  N   SER A  46       7.850  32.952  45.740  1.00 22.79           N  
ANISOU  377  N   SER A  46     3211   2883   2563   -776   -498   -143       N  
ATOM    378  CA  SER A  46       6.659  33.716  46.017  1.00 23.27           C  
ANISOU  378  CA  SER A  46     2799   3112   2932   -948   -496     97       C  
ATOM    379  C   SER A  46       5.772  33.996  44.808  1.00 25.53           C  
ANISOU  379  C   SER A  46     3041   3586   3072   -983   -667    180       C  
ATOM    380  O   SER A  46       4.983  34.951  44.821  1.00 26.28           O  
ANISOU  380  O   SER A  46     3650   2870   3463  -1147   -823    892       O  
ATOM    381  CB  SER A  46       7.064  35.089  46.603  1.00 22.94           C  
ANISOU  381  CB  SER A  46     2399   3078   3240   -590   -368   -171       C  
ATOM    382  OG  SER A  46       7.839  34.884  47.753  1.00 25.35           O  
ANISOU  382  OG  SER A  46     3258   2898   3476   -208   -856   -545       O  
ATOM    383  N   GLU A  47       5.880  33.190  43.761  1.00 29.03           N  
ANISOU  383  N   GLU A  47     3926   3979   3125  -1240   -833    -70       N  
ATOM    384  CA  GLU A  47       5.166  33.476  42.530  1.00 28.85           C  
ANISOU  384  CA  GLU A  47     3550   4085   3326   -304   -847   -465       C  
ATOM    385  C   GLU A  47       3.651  33.424  42.712  1.00 31.29           C  
ANISOU  385  C   GLU A  47     3629   4426   3833   -565   -555   -268       C  
ATOM    386  O   GLU A  47       2.932  34.015  41.898  1.00 31.46           O  
ANISOU  386  O   GLU A  47     3156   4866   3933   -900   -799   -303       O  
ATOM    387  CB  GLU A  47       5.589  32.497  41.437  1.00 30.93           C  
ANISOU  387  CB  GLU A  47     3974   4367   3411     87  -1091   -640       C  
ATOM    388  CG  GLU A  47       7.021  32.710  40.967  1.00 35.03           C  
ANISOU  388  CG  GLU A  47     4127   4904   4280    488   -517   -729       C  
ATOM    389  CD  GLU A  47       7.031  33.114  39.503  1.00 38.42           C  
ANISOU  389  CD  GLU A  47     5107   5159   4333    695    172   -649       C  
ATOM    390  OE1 GLU A  47       6.407  34.136  39.158  1.00 43.47           O  
ANISOU  390  OE1 GLU A  47     5562   5454   5500    292   -386    500       O  
ATOM    391  OE2 GLU A  47       7.652  32.412  38.680  1.00 52.58           O  
ANISOU  391  OE2 GLU A  47     7255   7239   5483    990   1667  -1445       O  
ATOM    392  N   HIS A  48       3.199  32.735  43.756  1.00 33.68           N  
ANISOU  392  N   HIS A  48     4399   4337   4061   -703   -230   -282       N  
ATOM    393  CA  HIS A  48       1.775  32.713  44.069  1.00 36.28           C  
ANISOU  393  CA  HIS A  48     4561   4474   4752   -890    185    -80       C  
ATOM    394  C   HIS A  48       1.306  34.009  44.717  1.00 34.22           C  
ANISOU  394  C   HIS A  48     3934   4605   4464   -775   -260   -145       C  
ATOM    395  O   HIS A  48       0.094  34.192  44.899  1.00 37.29           O  
ANISOU  395  O   HIS A  48     3844   5157   5167  -1267   -116  -1056       O  
ATOM    396  CB  HIS A  48       1.444  31.550  45.012  1.00 40.20           C  
ANISOU  396  CB  HIS A  48     5485   4612   5177  -1164    332    101       C  
ATOM    397  CG  HIS A  48       2.163  31.592  46.324  1.00 42.71           C  
ANISOU  397  CG  HIS A  48     6132   4799   5298  -1103     -1    557       C  
ATOM    398  ND1 HIS A  48       3.535  31.521  46.429  1.00 43.81           N  
ANISOU  398  ND1 HIS A  48     6182   4987   5478   -886   -289    539       N  
ATOM    399  CD2 HIS A  48       1.700  31.707  47.593  1.00 43.85           C  
ANISOU  399  CD2 HIS A  48     6495   5009   5156  -1282    -59    723       C  
ATOM    400  CE1 HIS A  48       3.877  31.584  47.709  1.00 45.20           C  
ANISOU  400  CE1 HIS A  48     6504   5175   5495  -1218   -326    493       C  
ATOM    401  NE2 HIS A  48       2.780  31.701  48.446  1.00 45.32           N  
ANISOU  401  NE2 HIS A  48     6607   5223   5388  -1380   -232    643       N  
ATOM    402  N   LYS A  49       2.220  34.905  45.096  1.00 31.02           N  
ANISOU  402  N   LYS A  49     3350   4368   4067   -493   -155    148       N  
ATOM    403  CA  LYS A  49       1.742  36.172  45.684  1.00 29.01           C  
ANISOU  403  CA  LYS A  49     3032   4383   3608   -445   -453    221       C  
ATOM    404  C   LYS A  49       1.551  37.188  44.567  1.00 28.20           C  
ANISOU  404  C   LYS A  49     3185   4257   3271   -761   -730    -20       C  
ATOM    405  O   LYS A  49       2.263  38.162  44.415  1.00 26.72           O  
ANISOU  405  O   LYS A  49     2995   4430   2727   -779   -323   -181       O  
ATOM    406  CB  LYS A  49       2.706  36.628  46.779  1.00 28.13           C  
ANISOU  406  CB  LYS A  49     2861   4339   3487   -328   -480    511       C  
ATOM    407  CG  LYS A  49       2.851  35.568  47.863  1.00 28.03           C  
ANISOU  407  CG  LYS A  49     2914   4202   3536    -79   -100    496       C  
ATOM    408  CD  LYS A  49       3.753  36.053  48.988  1.00 31.04           C  
ANISOU  408  CD  LYS A  49     3762   4666   3365   -486   -428    898       C  
ATOM    409  CE  LYS A  49       4.019  34.941  49.997  1.00 35.76           C  
ANISOU  409  CE  LYS A  49     4674   4905   4008   -584   -801   1286       C  
ATOM    410  NZ  LYS A  49       5.468  34.595  50.026  1.00 41.91           N  
ANISOU  410  NZ  LYS A  49     5016   5657   5250    167   -951   1691       N  
ATOM    411  N   THR A  50       0.551  36.947  43.728  1.00 27.28           N  
ANISOU  411  N   THR A  50     3089   4401   2874   -646   -438   -501       N  
ATOM    412  CA  THR A  50       0.297  37.681  42.501  1.00 29.60           C  
ANISOU  412  CA  THR A  50     3245   4621   3381   -684   -881   -142       C  
ATOM    413  C   THR A  50       0.102  39.163  42.731  1.00 27.20           C  
ANISOU  413  C   THR A  50     2528   4630   3175   -806   -746   -191       C  
ATOM    414  O   THR A  50       0.676  39.995  42.017  1.00 28.05           O  
ANISOU  414  O   THR A  50     3160   4631   2869  -1453   -498   -828       O  
ATOM    415  CB  THR A  50      -0.953  37.034  41.840  1.00 33.49           C  
ANISOU  415  CB  THR A  50     4182   4674   3869  -1023  -1521   -234       C  
ATOM    416  OG1 THR A  50      -0.531  35.885  41.077  1.00 38.98           O  
ANISOU  416  OG1 THR A  50     4871   4950   4989  -1139  -1163   -809       O  
ATOM    417  CG2 THR A  50      -1.659  37.923  40.851  1.00 39.50           C  
ANISOU  417  CG2 THR A  50     4574   5033   5402  -1515  -2561    401       C  
ATOM    418  N   GLU A  51      -0.727  39.511  43.714  1.00 27.53           N  
ANISOU  418  N   GLU A  51     2367   4798   3296   -806   -660    -12       N  
ATOM    419  CA  GLU A  51      -1.088  40.899  43.993  1.00 28.00           C  
ANISOU  419  CA  GLU A  51     2040   5000   3600   -309   -499    206       C  
ATOM    420  C   GLU A  51       0.177  41.622  44.427  1.00 24.74           C  
ANISOU  420  C   GLU A  51     2354   4153   2891   -213   -579    229       C  
ATOM    421  O   GLU A  51       0.513  42.724  44.003  1.00 25.30           O  
ANISOU  421  O   GLU A  51     2640   3983   2989      4   -884    299       O  
ATOM    422  CB  GLU A  51      -2.171  41.036  45.072  1.00 36.31           C  
ANISOU  422  CB  GLU A  51     2590   6270   4936   -259    408    -92       C  
ATOM    423  CG  GLU A  51      -3.595  41.202  44.564  1.00 42.34           C  
ANISOU  423  CG  GLU A  51     2437   7396   6256    123    518      9       C  
ATOM    424  CD  GLU A  51      -4.522  42.046  45.418  1.00 46.65           C  
ANISOU  424  CD  GLU A  51     2987   7881   6858    362   1086     46       C  
ATOM    425  OE1 GLU A  51      -4.782  41.698  46.600  1.00 55.66           O  
ANISOU  425  OE1 GLU A  51     6458   8247   6442   -364   1676   -844       O  
ATOM    426  OE2 GLU A  51      -5.037  43.085  44.922  1.00 55.84           O  
ANISOU  426  OE2 GLU A  51     4030   8180   9007   1225   1172    246       O  
ATOM    427  N   LEU A  52       0.894  40.925  45.304  1.00 22.00           N  
ANISOU  427  N   LEU A  52     2024   3688   2647   -218   -190    183       N  
ATOM    428  CA  LEU A  52       2.130  41.509  45.849  1.00 19.63           C  
ANISOU  428  CA  LEU A  52     1912   3117   2430    -58    -82    204       C  
ATOM    429  C   LEU A  52       3.188  41.731  44.773  1.00 19.33           C  
ANISOU  429  C   LEU A  52     2254   2816   2275   -270     -5     30       C  
ATOM    430  O   LEU A  52       3.887  42.759  44.722  1.00 18.39           O  
ANISOU  430  O   LEU A  52     2518   2957   1510   -471   -303     28       O  
ATOM    431  CB  LEU A  52       2.628  40.558  46.935  1.00 19.83           C  
ANISOU  431  CB  LEU A  52     2438   2937   2160   -306   -232     72       C  
ATOM    432  CG  LEU A  52       3.738  41.114  47.832  1.00 19.68           C  
ANISOU  432  CG  LEU A  52     2150   2733   2595    -43   -318    -34       C  
ATOM    433  CD1 LEU A  52       3.281  42.447  48.417  1.00 22.35           C  
ANISOU  433  CD1 LEU A  52     2001   2598   3895   -137   -574   -311       C  
ATOM    434  CD2 LEU A  52       4.117  40.121  48.920  1.00 20.27           C  
ANISOU  434  CD2 LEU A  52     1607   3089   3004    143   -368    223       C  
ATOM    435  N   LYS A  53       3.314  40.749  43.862  1.00 18.99           N  
ANISOU  435  N   LYS A  53     2317   2773   2124   -402   -205     67       N  
ATOM    436  CA  LYS A  53       4.246  40.888  42.753  1.00 18.89           C  
ANISOU  436  CA  LYS A  53     2157   2618   2404     37    -49     63       C  
ATOM    437  C   LYS A  53       3.906  42.077  41.854  1.00 17.95           C  
ANISOU  437  C   LYS A  53     1887   2844   2087     75     -4     75       C  
ATOM    438  O   LYS A  53       4.739  42.880  41.422  1.00 17.38           O  
ANISOU  438  O   LYS A  53     1922   2704   1977    -90   -382      1       O  
ATOM    439  CB  LYS A  53       4.248  39.601  41.927  1.00 20.53           C  
ANISOU  439  CB  LYS A  53     2577   2698   2526   -346     97    -31       C  
ATOM    440  CG  LYS A  53       5.332  39.615  40.873  1.00 20.41           C  
ANISOU  440  CG  LYS A  53     2268   2693   2795   -234     87   -316       C  
ATOM    441  CD  LYS A  53       5.485  38.299  40.162  1.00 21.20           C  
ANISOU  441  CD  LYS A  53     2373   2773   2910   -192   -223   -452       C  
ATOM    442  CE  LYS A  53       6.565  38.440  39.078  1.00 23.13           C  
ANISOU  442  CE  LYS A  53     2973   2855   2962   -418    116   -850       C  
ATOM    443  NZ  LYS A  53       6.649  37.191  38.258  1.00 30.64           N  
ANISOU  443  NZ  LYS A  53     4969   3807   2864  -1833    545  -1725       N  
ATOM    444  N   GLU A  54       2.604  42.247  41.562  1.00 19.22           N  
ANISOU  444  N   GLU A  54     1998   2903   2402   -282   -554    -98       N  
ATOM    445  CA  GLU A  54       2.184  43.447  40.847  1.00 20.43           C  
ANISOU  445  CA  GLU A  54     2086   2907   2770     35   -697   -217       C  
ATOM    446  C   GLU A  54       2.615  44.749  41.545  1.00 19.92           C  
ANISOU  446  C   GLU A  54     2106   2899   2562   -205   -620    -44       C  
ATOM    447  O   GLU A  54       3.089  45.706  40.882  1.00 20.16           O  
ANISOU  447  O   GLU A  54     2116   2877   2665     52   -855    299       O  
ATOM    448  CB  GLU A  54       0.658  43.424  40.676  1.00 23.89           C  
ANISOU  448  CB  GLU A  54     2178   3569   3331   -217  -1141   -138       C  
ATOM    449  CG  GLU A  54       0.186  42.390  39.665  1.00 32.45           C  
ANISOU  449  CG  GLU A  54     3664   4564   4100  -1141  -1577   -545       C  
ATOM    450  CD  GLU A  54      -1.313  42.310  39.500  1.00 37.13           C  
ANISOU  450  CD  GLU A  54     3790   5305   5015  -1157  -2246   -714       C  
ATOM    451  OE1 GLU A  54      -2.040  43.220  39.953  1.00 43.80           O  
ANISOU  451  OE1 GLU A  54     3659   7064   5921   -806  -1413  -1277       O  
ATOM    452  OE2 GLU A  54      -1.764  41.305  38.906  1.00 44.41           O  
ANISOU  452  OE2 GLU A  54     5083   5466   6326  -1663  -3410   -557       O  
ATOM    453  N   LYS A  55       2.460  44.822  42.872  1.00 19.12           N  
ANISOU  453  N   LYS A  55     1850   2803   2610    -48   -487    -92       N  
ATOM    454  CA  LYS A  55       2.880  46.007  43.636  1.00 19.53           C  
ANISOU  454  CA  LYS A  55     1879   2825   2715     27    -45   -329       C  
ATOM    455  C   LYS A  55       4.389  46.200  43.527  1.00 18.16           C  
ANISOU  455  C   LYS A  55     1888   2526   2487    -42   -202   -317       C  
ATOM    456  O   LYS A  55       4.911  47.307  43.349  1.00 19.01           O  
ANISOU  456  O   LYS A  55     2191   2391   2640   -103     73   -753       O  
ATOM    457  CB  LYS A  55       2.490  45.920  45.123  1.00 20.53           C  
ANISOU  457  CB  LYS A  55     1891   3246   2664     34   -123   -260       C  
ATOM    458  CG  LYS A  55       0.987  46.030  45.361  1.00 24.09           C  
ANISOU  458  CG  LYS A  55     2007   3781   3365     66    322     19       C  
ATOM    459  CD  LYS A  55       0.632  45.840  46.823  1.00 25.94           C  
ANISOU  459  CD  LYS A  55     2293   4036   3525    218    467    504       C  
ATOM    460  CE  LYS A  55      -0.877  45.546  46.976  1.00 28.90           C  
ANISOU  460  CE  LYS A  55     2199   4379   4401    680   1003    293       C  
ATOM    461  NZ  LYS A  55      -1.506  46.705  47.638  1.00 41.66           N  
ANISOU  461  NZ  LYS A  55     3353   5546   6932    883   1388  -1337       N  
ATOM    462  N   PHE A  56       5.118  45.092  43.620  1.00 17.11           N  
ANISOU  462  N   PHE A  56     1804   2486   2210   -114   -367   -412       N  
ATOM    463  CA  PHE A  56       6.581  45.208  43.495  1.00 15.81           C  
ANISOU  463  CA  PHE A  56     1843   2242   1921   -149   -112   -327       C  
ATOM    464  C   PHE A  56       6.997  45.661  42.107  1.00 16.21           C  
ANISOU  464  C   PHE A  56     1995   2190   1975    145   -412    116       C  
ATOM    465  O   PHE A  56       7.945  46.446  41.949  1.00 16.35           O  
ANISOU  465  O   PHE A  56     2541   2048   1623   -107   -240    -65       O  
ATOM    466  CB  PHE A  56       7.266  43.877  43.794  1.00 15.30           C  
ANISOU  466  CB  PHE A  56     1604   2386   1822   -368   -263    241       C  
ATOM    467  CG  PHE A  56       8.771  43.957  43.999  1.00 15.44           C  
ANISOU  467  CG  PHE A  56     1603   2515   1749   -452   -144    357       C  
ATOM    468  CD1 PHE A  56       9.278  44.762  45.019  1.00 15.19           C  
ANISOU  468  CD1 PHE A  56     1710   2142   1919   -414   -423    523       C  
ATOM    469  CD2 PHE A  56       9.631  43.223  43.195  1.00 16.62           C  
ANISOU  469  CD2 PHE A  56     1723   2471   2119    -77   -267    360       C  
ATOM    470  CE1 PHE A  56      10.639  44.806  45.242  1.00 13.97           C  
ANISOU  470  CE1 PHE A  56     1688   1852   1767   -201   -390    590       C  
ATOM    471  CE2 PHE A  56      11.011  43.297  43.420  1.00 16.31           C  
ANISOU  471  CE2 PHE A  56     1705   2368   2125   -226   -206    203       C  
ATOM    472  CZ  PHE A  56      11.508  44.080  44.446  1.00 16.47           C  
ANISOU  472  CZ  PHE A  56     1961   2211   2086   -104   -333    255       C  
ATOM    473  N   GLN A  57       6.313  45.157  41.072  1.00 17.37           N  
ANISOU  473  N   GLN A  57     1908   2765   1928    -75   -270     24       N  
ATOM    474  CA  GLN A  57       6.609  45.614  39.723  1.00 18.82           C  
ANISOU  474  CA  GLN A  57     2470   2703   1978   -321   -428    190       C  
ATOM    475  C   GLN A  57       6.439  47.131  39.658  1.00 18.77           C  
ANISOU  475  C   GLN A  57     2244   2754   2133    -63   -491     95       C  
ATOM    476  O   GLN A  57       7.298  47.836  39.107  1.00 18.18           O  
ANISOU  476  O   GLN A  57     2559   2345   2005    168   -169     46       O  
ATOM    477  CB  GLN A  57       5.711  44.914  38.703  1.00 19.75           C  
ANISOU  477  CB  GLN A  57     2696   2838   1971   -379   -536    224       C  
ATOM    478  CG  GLN A  57       6.080  45.311  37.263  1.00 23.73           C  
ANISOU  478  CG  GLN A  57     3934   3113   1968   -776   -623    375       C  
ATOM    479  CD  GLN A  57       7.377  44.690  36.792  1.00 25.05           C  
ANISOU  479  CD  GLN A  57     4495   3095   1929   -984    258    109       C  
ATOM    480  OE1 GLN A  57       7.524  43.466  36.774  1.00 26.50           O  
ANISOU  480  OE1 GLN A  57     5201   3144   1723   -792    349   -352       O  
ATOM    481  NE2 GLN A  57       8.350  45.501  36.404  1.00 28.25           N  
ANISOU  481  NE2 GLN A  57     4543   3910   2283  -1392    113    262       N  
ATOM    482  N   ARG A  58       5.333  47.639  40.237  1.00 20.22           N  
ANISOU  482  N   ARG A  58     1789   3235   2661   -110   -701    -45       N  
ATOM    483  CA  ARG A  58       5.182  49.097  40.180  1.00 21.49           C  
ANISOU  483  CA  ARG A  58     2158   3303   2702    286   -711   -198       C  
ATOM    484  C   ARG A  58       6.308  49.783  40.957  1.00 21.16           C  
ANISOU  484  C   ARG A  58     2543   2956   2542   -236   -653    290       C  
ATOM    485  O   ARG A  58       6.868  50.801  40.530  1.00 21.46           O  
ANISOU  485  O   ARG A  58     2751   2463   2939    234   -382    347       O  
ATOM    486  CB  ARG A  58       3.828  49.555  40.726  1.00 27.26           C  
ANISOU  486  CB  ARG A  58     2346   4261   3752    645   -454   -356       C  
ATOM    487  CG  ARG A  58       3.450  50.964  40.322  1.00 35.55           C  
ANISOU  487  CG  ARG A  58     3499   4691   5318   1621   -241   -104       C  
ATOM    488  CD  ARG A  58       2.056  51.430  40.683  1.00 42.63           C  
ANISOU  488  CD  ARG A  58     4205   5507   6487   2213    523   -586       C  
ATOM    489  NE  ARG A  58       2.070  52.361  41.812  1.00 52.99           N  
ANISOU  489  NE  ARG A  58     6511   6432   7191   1587   1682  -1397       N  
ATOM    490  CZ  ARG A  58       1.065  53.017  42.355  1.00 55.38           C  
ANISOU  490  CZ  ARG A  58     6659   6953   7431   1663   1791  -1744       C  
ATOM    491  NH1 ARG A  58      -0.181  52.894  41.889  1.00 61.62           N  
ANISOU  491  NH1 ARG A  58     6401   8431   8579   1558   1881  -1375       N  
ATOM    492  NH2 ARG A  58       1.273  53.833  43.395  1.00 60.99           N  
ANISOU  492  NH2 ARG A  58     8381   7243   7551   1332   2295  -2041       N  
ATOM    493  N   MET A  59       6.629  49.227  42.131  1.00 15.83           N  
ANISOU  493  N   MET A  59     1392   2408   2214    307   -113    -90       N  
ATOM    494  CA  MET A  59       7.715  49.811  42.911  1.00 17.02           C  
ANISOU  494  CA  MET A  59     1925   2613   1926   -265     -7    -76       C  
ATOM    495  C   MET A  59       9.006  49.928  42.107  1.00 16.09           C  
ANISOU  495  C   MET A  59     1583   2581   1951    -23   -252    -90       C  
ATOM    496  O   MET A  59       9.704  50.944  42.066  1.00 17.22           O  
ANISOU  496  O   MET A  59     1853   2371   2318     69    417   -167       O  
ATOM    497  CB  MET A  59       8.023  48.949  44.153  1.00 16.97           C  
ANISOU  497  CB  MET A  59     1610   2809   2029     72    -92    -57       C  
ATOM    498  CG  MET A  59       6.978  49.029  45.262  1.00 19.64           C  
ANISOU  498  CG  MET A  59     2022   3446   1995   -220    116     86       C  
ATOM    499  SD  MET A  59       7.419  47.968  46.664  1.00 23.46           S  
ANISOU  499  SD  MET A  59     3028   3555   2330   -140    110    380       S  
ATOM    500  CE  MET A  59       5.982  48.211  47.721  1.00 20.54           C  
ANISOU  500  CE  MET A  59     2793   3372   1641   -108   -330    302       C  
ATOM    501  N   CYS A  60       9.371  48.811  41.459  1.00 15.34           N  
ANISOU  501  N   CYS A  60     1574   2436   1817    -58   -381      8       N  
ATOM    502  CA  CYS A  60      10.589  48.834  40.640  1.00 16.01           C  
ANISOU  502  CA  CYS A  60     1893   2296   1894     97   -102    147       C  
ATOM    503  C   CYS A  60      10.423  49.746  39.429  1.00 17.72           C  
ANISOU  503  C   CYS A  60     2306   2452   1975   -204   -330    260       C  
ATOM    504  O   CYS A  60      11.396  50.439  39.090  1.00 17.47           O  
ANISOU  504  O   CYS A  60     2536   2302   1798   -285   -123      1       O  
ATOM    505  CB  CYS A  60      10.984  47.435  40.164  1.00 17.46           C  
ANISOU  505  CB  CYS A  60     2405   2302   1926    -39    107     16       C  
ATOM    506  SG  CYS A  60      11.512  46.362  41.539  1.00 18.14           S  
ANISOU  506  SG  CYS A  60     2046   2298   2548    147    -10    264       S  
ATOM    507  N   ASP A  61       9.243  49.726  38.798  1.00 17.89           N  
ANISOU  507  N   ASP A  61     2364   2407   2027     75   -423     95       N  
ATOM    508  CA  ASP A  61       9.114  50.614  37.636  1.00 20.11           C  
ANISOU  508  CA  ASP A  61     2759   2607   2276     23   -581    317       C  
ATOM    509  C   ASP A  61       9.242  52.090  37.991  1.00 21.33           C  
ANISOU  509  C   ASP A  61     2826   2548   2730   -144   -393    412       C  
ATOM    510  O   ASP A  61       9.691  52.911  37.163  1.00 23.74           O  
ANISOU  510  O   ASP A  61     2496   2892   3631    -40   -147    914       O  
ATOM    511  CB  ASP A  61       7.763  50.359  36.955  1.00 22.03           C  
ANISOU  511  CB  ASP A  61     3042   2941   2387   -333   -827    701       C  
ATOM    512  CG  ASP A  61       7.780  49.074  36.155  1.00 25.11           C  
ANISOU  512  CG  ASP A  61     3850   3495   2194   -893   -586    302       C  
ATOM    513  OD1 ASP A  61       8.883  48.539  35.881  1.00 28.77           O  
ANISOU  513  OD1 ASP A  61     4362   3231   3338   -564   -501   -285       O  
ATOM    514  OD2 ASP A  61       6.679  48.595  35.812  1.00 29.54           O  
ANISOU  514  OD2 ASP A  61     4385   4195   2643  -1186  -1343    385       O  
ATOM    515  N   LYS A  62       8.839  52.455  39.211  1.00 19.23           N  
ANISOU  515  N   LYS A  62     1850   2590   2865    163   -735     96       N  
ATOM    516  CA  LYS A  62       8.895  53.848  39.634  1.00 21.10           C  
ANISOU  516  CA  LYS A  62     1775   2593   3649    215   -643     -9       C  
ATOM    517  C   LYS A  62      10.180  54.203  40.378  1.00 18.98           C  
ANISOU  517  C   LYS A  62     2144   2194   2873    243   -801    224       C  
ATOM    518  O   LYS A  62      10.371  55.342  40.781  1.00 18.48           O  
ANISOU  518  O   LYS A  62     1546   2331   3146    256    -52   -117       O  
ATOM    519  CB  LYS A  62       7.749  54.176  40.593  1.00 26.37           C  
ANISOU  519  CB  LYS A  62     2263   3072   4686    385    -70   -434       C  
ATOM    520  CG  LYS A  62       6.352  54.052  39.997  1.00 30.13           C  
ANISOU  520  CG  LYS A  62     1979   4122   5347    442     88   -419       C  
ATOM    521  CD  LYS A  62       5.312  54.140  41.095  1.00 35.58           C  
ANISOU  521  CD  LYS A  62     2533   4973   6014    142    685   -943       C  
ATOM    522  CE  LYS A  62       5.644  55.153  42.175  1.00 40.79           C  
ANISOU  522  CE  LYS A  62     4021   5493   5982   -326   1074  -1231       C  
ATOM    523  NZ  LYS A  62       4.417  55.845  42.692  1.00 42.77           N  
ANISOU  523  NZ  LYS A  62     4794   5774   5682    551    884  -1231       N  
ATOM    524  N   SER A  63      11.055  53.227  40.560  1.00 16.59           N  
ANISOU  524  N   SER A  63     1784   2134   2384    117   -331    218       N  
ATOM    525  CA  SER A  63      12.220  53.445  41.394  1.00 14.30           C  
ANISOU  525  CA  SER A  63     1913   1608   1912    150   -275    386       C  
ATOM    526  C   SER A  63      13.251  54.372  40.739  1.00 13.93           C  
ANISOU  526  C   SER A  63     2073   1629   1590    -35   -288    147       C  
ATOM    527  O   SER A  63      14.093  54.908  41.475  1.00 14.56           O  
ANISOU  527  O   SER A  63     2047   1943   1540    -41   -219    -70       O  
ATOM    528  CB  SER A  63      12.914  52.119  41.738  1.00 14.81           C  
ANISOU  528  CB  SER A  63     2138   1520   1970    266   -157    198       C  
ATOM    529  OG  SER A  63      13.399  51.483  40.571  1.00 16.42           O  
ANISOU  529  OG  SER A  63     1993   2069   2177    230    125    100       O  
ATOM    530  N   MET A  64      13.207  54.522  39.411  1.00 13.53           N  
ANISOU  530  N   MET A  64     1775   1757   1609     89   -363    167       N  
ATOM    531  CA  MET A  64      14.224  55.319  38.710  1.00 13.75           C  
ANISOU  531  CA  MET A  64     1909   1603   1713    294   -130    249       C  
ATOM    532  C   MET A  64      15.621  54.737  38.836  1.00 12.99           C  
ANISOU  532  C   MET A  64     1904   1624   1410    328    -43     72       C  
ATOM    533  O   MET A  64      16.645  55.411  38.699  1.00 14.29           O  
ANISOU  533  O   MET A  64     1890   1497   2044    438     54    224       O  
ATOM    534  CB  MET A  64      14.177  56.766  39.215  1.00 15.45           C  
ANISOU  534  CB  MET A  64     2238   1461   2171    407      8    380       C  
ATOM    535  CG  MET A  64      12.756  57.340  39.093  1.00 16.98           C  
ANISOU  535  CG  MET A  64     2179   1912   2359    522    293    121       C  
ATOM    536  SD  MET A  64      12.135  57.242  37.378  1.00 25.19           S  
ANISOU  536  SD  MET A  64     3120   3286   3166    767   -972    -67       S  
ATOM    537  CE  MET A  64      11.151  55.759  37.475  1.00 74.82           C  
ANISOU  537  CE  MET A  64    14269  11163   2998  -8970    963  -2046       C  
ATOM    538  N   ILE A  65      15.681  53.448  39.118  1.00 12.75           N  
ANISOU  538  N   ILE A  65     1696   1629   1520    260   -181     70       N  
ATOM    539  CA  ILE A  65      16.888  52.625  39.103  1.00 12.61           C  
ANISOU  539  CA  ILE A  65     1785   1588   1419    297   -101    -64       C  
ATOM    540  C   ILE A  65      16.873  51.728  37.871  1.00 13.57           C  
ANISOU  540  C   ILE A  65     1793   1818   1547    -25     27   -219       C  
ATOM    541  O   ILE A  65      15.903  51.004  37.648  1.00 13.92           O  
ANISOU  541  O   ILE A  65     1794   1897   1599    -31   -197    -36       O  
ATOM    542  CB  ILE A  65      16.966  51.792  40.386  1.00 12.91           C  
ANISOU  542  CB  ILE A  65     1841   1505   1561    192   -370    -12       C  
ATOM    543  CG1 ILE A  65      16.991  52.652  41.657  1.00 12.91           C  
ANISOU  543  CG1 ILE A  65     1801   1698   1407     40   -168     36       C  
ATOM    544  CG2 ILE A  65      18.149  50.812  40.297  1.00 14.27           C  
ANISOU  544  CG2 ILE A  65     1980   1495   1946    254   -168     99       C  
ATOM    545  CD1 ILE A  65      16.667  51.835  42.908  1.00 13.53           C  
ANISOU  545  CD1 ILE A  65     1922   1598   1622   -282   -123     87       C  
ATOM    546  N   LYS A  66      17.949  51.785  37.090  1.00 14.12           N  
ANISOU  546  N   LYS A  66     1743   1839   1784    168    105   -345       N  
ATOM    547  CA  LYS A  66      18.142  50.909  35.936  1.00 13.27           C  
ANISOU  547  CA  LYS A  66     2016   1663   1362    262    -79    -40       C  
ATOM    548  C   LYS A  66      18.795  49.579  36.328  1.00 13.55           C  
ANISOU  548  C   LYS A  66     2007   1624   1517    241   -233   -112       C  
ATOM    549  O   LYS A  66      18.419  48.544  35.770  1.00 14.37           O  
ANISOU  549  O   LYS A  66     2035   1683   1742    190     85   -318       O  
ATOM    550  CB  LYS A  66      18.987  51.582  34.842  1.00 18.10           C  
ANISOU  550  CB  LYS A  66     3277   2189   1412   -166    163    150       C  
ATOM    551  CG  LYS A  66      18.196  52.679  34.133  1.00 23.98           C  
ANISOU  551  CG  LYS A  66     4201   2744   2165   -252   -364    900       C  
ATOM    552  CD  LYS A  66      18.894  53.131  32.860  1.00 34.14           C  
ANISOU  552  CD  LYS A  66     6731   3818   2423  -1422   -105   1477       C  
ATOM    553  CE  LYS A  66      18.484  54.534  32.443  1.00 38.31           C  
ANISOU  553  CE  LYS A  66     7612   3947   2996  -1456   -493   1811       C  
ATOM    554  NZ  LYS A  66      19.499  55.225  31.594  1.00 48.22           N  
ANISOU  554  NZ  LYS A  66     9512   5314   3497  -2676   -350   2671       N  
ATOM    555  N   ARG A  67      19.744  49.619  37.257  1.00 14.16           N  
ANISOU  555  N   ARG A  67     1892   1961   1526    142   -169    148       N  
ATOM    556  CA  ARG A  67      20.459  48.428  37.682  1.00 13.98           C  
ANISOU  556  CA  ARG A  67     1712   2042   1557    276   -108     -8       C  
ATOM    557  C   ARG A  67      21.117  48.678  39.051  1.00 14.07           C  
ANISOU  557  C   ARG A  67     1818   1820   1706    -63   -300    214       C  
ATOM    558  O   ARG A  67      21.303  49.818  39.480  1.00 13.81           O  
ANISOU  558  O   ARG A  67     1969   1784   1496     71   -134    201       O  
ATOM    559  CB  ARG A  67      21.494  47.954  36.655  1.00 18.58           C  
ANISOU  559  CB  ARG A  67     2342   2592   2126    383    432   -166       C  
ATOM    560  CG  ARG A  67      22.479  48.980  36.149  1.00 25.35           C  
ANISOU  560  CG  ARG A  67     3103   3476   3053   -338   1412   -698       C  
ATOM    561  CD  ARG A  67      22.999  48.660  34.721  1.00 33.12           C  
ANISOU  561  CD  ARG A  67     4835   4306   3441   -760   2311   -854       C  
ATOM    562  NE  ARG A  67      22.660  49.799  33.872  1.00 39.84           N  
ANISOU  562  NE  ARG A  67     6621   5125   3392  -1311   1931    -89       N  
ATOM    563  CZ  ARG A  67      21.762  49.905  32.903  1.00 40.81           C  
ANISOU  563  CZ  ARG A  67     6837   5318   3351  -1386   1821     81       C  
ATOM    564  NH1 ARG A  67      20.966  48.897  32.509  1.00 42.38           N  
ANISOU  564  NH1 ARG A  67     6103   5939   4061  -1496   2134   -420       N  
ATOM    565  NH2 ARG A  67      21.641  51.072  32.286  1.00 47.06           N  
ANISOU  565  NH2 ARG A  67     7842   5634   4403   -963   1494    505       N  
ATOM    566  N   ARG A  68      21.438  47.534  39.652  1.00 12.41           N  
ANISOU  566  N   ARG A  68     1380   1782   1553    170     68     90       N  
ATOM    567  CA  ARG A  68      22.150  47.495  40.923  1.00 11.99           C  
ANISOU  567  CA  ARG A  68     1219   1759   1578    193     87    151       C  
ATOM    568  C   ARG A  68      23.211  46.392  40.864  1.00 12.93           C  
ANISOU  568  C   ARG A  68     1232   1923   1760    257    -84   -272       C  
ATOM    569  O   ARG A  68      23.060  45.416  40.100  1.00 17.10           O  
ANISOU  569  O   ARG A  68     2170   1923   2404    345   -483   -515       O  
ATOM    570  CB  ARG A  68      21.203  47.217  42.086  1.00 12.22           C  
ANISOU  570  CB  ARG A  68     1425   1640   1578    132    194     47       C  
ATOM    571  CG  ARG A  68      20.293  48.389  42.460  1.00 12.83           C  
ANISOU  571  CG  ARG A  68     1825   1428   1621     66    461     57       C  
ATOM    572  CD  ARG A  68      19.291  47.956  43.531  1.00 13.10           C  
ANISOU  572  CD  ARG A  68     1832   1603   1542   -246    490   -332       C  
ATOM    573  NE  ARG A  68      18.193  47.168  42.942  1.00 11.42           N  
ANISOU  573  NE  ARG A  68     1478   1436   1424    203    -27    168       N  
ATOM    574  CZ  ARG A  68      17.274  46.562  43.697  1.00 13.05           C  
ANISOU  574  CZ  ARG A  68     1858   1603   1497   -290     16    -40       C  
ATOM    575  NH1 ARG A  68      17.331  46.631  45.029  1.00 13.58           N  
ANISOU  575  NH1 ARG A  68     1518   2159   1483   -124    199   -106       N  
ATOM    576  NH2 ARG A  68      16.291  45.881  43.106  1.00 13.42           N  
ANISOU  576  NH2 ARG A  68     1433   1765   1899     84   -301     48       N  
ATOM    577  N   TYR A  69      24.235  46.547  41.710  1.00 12.68           N  
ANISOU  577  N   TYR A  69     1162   2024   1631    149    -27     58       N  
ATOM    578  CA  TYR A  69      25.271  45.529  41.812  1.00 12.69           C  
ANISOU  578  CA  TYR A  69     1218   1892   1712    107     42    270       C  
ATOM    579  C   TYR A  69      25.009  44.783  43.117  1.00 13.32           C  
ANISOU  579  C   TYR A  69     1997   1507   1557    112    272    -30       C  
ATOM    580  O   TYR A  69      24.790  45.475  44.116  1.00 14.64           O  
ANISOU  580  O   TYR A  69     2202   1687   1674     72     92   -262       O  
ATOM    581  CB  TYR A  69      26.696  46.154  41.766  1.00 12.75           C  
ANISOU  581  CB  TYR A  69     1162   1919   1762    132    -96    114       C  
ATOM    582  CG  TYR A  69      26.864  46.756  40.372  1.00 13.43           C  
ANISOU  582  CG  TYR A  69     1226   2033   1843     77    265    111       C  
ATOM    583  CD1 TYR A  69      26.432  48.058  40.131  1.00 14.25           C  
ANISOU  583  CD1 TYR A  69     1590   1967   1859    -29    542    303       C  
ATOM    584  CD2 TYR A  69      27.403  46.004  39.328  1.00 15.38           C  
ANISOU  584  CD2 TYR A  69     1666   2184   1993    -41    355   -121       C  
ATOM    585  CE1 TYR A  69      26.547  48.647  38.884  1.00 15.84           C  
ANISOU  585  CE1 TYR A  69     2225   2092   1703    -21    570    177       C  
ATOM    586  CE2 TYR A  69      27.524  46.571  38.067  1.00 16.28           C  
ANISOU  586  CE2 TYR A  69     1906   2355   1925    -11    423   -163       C  
ATOM    587  CZ  TYR A  69      27.099  47.872  37.879  1.00 17.26           C  
ANISOU  587  CZ  TYR A  69     2358   2311   1887    -29    605    -38       C  
ATOM    588  OH  TYR A  69      27.215  48.435  36.635  1.00 21.19           O  
ANISOU  588  OH  TYR A  69     3789   2398   1865    245    950    -96       O  
ATOM    589  N   MET A  70      25.013  43.453  43.084  1.00 13.63           N  
ANISOU  589  N   MET A  70     2100   1504   1575    274   -128    -38       N  
ATOM    590  CA  MET A  70      24.697  42.710  44.294  1.00 15.04           C  
ANISOU  590  CA  MET A  70     2316   1615   1785    148   -395    255       C  
ATOM    591  C   MET A  70      25.688  41.575  44.536  1.00 15.53           C  
ANISOU  591  C   MET A  70     2572   1693   1636    335   -469      0       C  
ATOM    592  O   MET A  70      25.941  40.743  43.662  1.00 15.92           O  
ANISOU  592  O   MET A  70     2328   1998   1723    175   -152   -136       O  
ATOM    593  CB  MET A  70      23.276  42.116  44.236  1.00 17.78           C  
ANISOU  593  CB  MET A  70     2472   1948   2336   -107   -618    943       C  
ATOM    594  CG  MET A  70      22.179  43.201  44.218  1.00 21.34           C  
ANISOU  594  CG  MET A  70     2328   2700   3080    135  -1192   1974       C  
ATOM    595  SD  MET A  70      20.562  42.340  44.306  1.00 27.79           S  
ANISOU  595  SD  MET A  70     2528   3597   4435   -206    294     89       S  
ATOM    596  CE  MET A  70      19.540  43.829  44.308  1.00 32.68           C  
ANISOU  596  CE  MET A  70     2609   4415   5391    472   1144   1858       C  
ATOM    597  N   TYR A  71      26.212  41.566  45.771  1.00 14.38           N  
ANISOU  597  N   TYR A  71     1946   1848   1669    109   -394     58       N  
ATOM    598  CA  TYR A  71      26.970  40.405  46.218  1.00 14.02           C  
ANISOU  598  CA  TYR A  71     1766   1792   1768    -30   -473     61       C  
ATOM    599  C   TYR A  71      26.143  39.133  46.028  1.00 13.87           C  
ANISOU  599  C   TYR A  71     1642   1778   1849     57   -101   -268       C  
ATOM    600  O   TYR A  71      26.635  38.086  45.603  1.00 15.68           O  
ANISOU  600  O   TYR A  71     1825   1894   2237    143     51   -370       O  
ATOM    601  CB  TYR A  71      27.325  40.562  47.704  1.00 14.68           C  
ANISOU  601  CB  TYR A  71     2021   1809   1748   -201   -518    191       C  
ATOM    602  CG  TYR A  71      27.905  39.339  48.353  1.00 13.49           C  
ANISOU  602  CG  TYR A  71     2158   1617   1352     16   -151    -81       C  
ATOM    603  CD1 TYR A  71      29.268  39.091  48.252  1.00 14.83           C  
ANISOU  603  CD1 TYR A  71     2355   1562   1717    346    287   -264       C  
ATOM    604  CD2 TYR A  71      27.097  38.470  49.075  1.00 14.64           C  
ANISOU  604  CD2 TYR A  71     2390   1652   1520    -22    -21    -26       C  
ATOM    605  CE1 TYR A  71      29.801  37.957  48.864  1.00 15.77           C  
ANISOU  605  CE1 TYR A  71     2560   1600   1834    520    326   -277       C  
ATOM    606  CE2 TYR A  71      27.605  37.353  49.668  1.00 16.77           C  
ANISOU  606  CE2 TYR A  71     2655   1795   1923     49     22    225       C  
ATOM    607  CZ  TYR A  71      28.957  37.111  49.552  1.00 17.15           C  
ANISOU  607  CZ  TYR A  71     2859   1713   1946    450    311    -38       C  
ATOM    608  OH  TYR A  71      29.428  35.974  50.187  1.00 21.35           O  
ANISOU  608  OH  TYR A  71     3012   2202   2898    241   -333    570       O  
ATOM    609  N   LEU A  72      24.888  39.211  46.484  1.00 14.40           N  
ANISOU  609  N   LEU A  72     1749   1712   2011     91    111    -72       N  
ATOM    610  CA  LEU A  72      24.030  38.028  46.371  1.00 12.78           C  
ANISOU  610  CA  LEU A  72     1705   1588   1561    180    146    -98       C  
ATOM    611  C   LEU A  72      23.799  37.651  44.925  1.00 15.07           C  
ANISOU  611  C   LEU A  72     2491   1766   1470      6    246    -28       C  
ATOM    612  O   LEU A  72      23.464  38.488  44.072  1.00 19.89           O  
ANISOU  612  O   LEU A  72     3368   2241   1950     65   -711    112       O  
ATOM    613  CB  LEU A  72      22.687  38.311  47.052  1.00 13.88           C  
ANISOU  613  CB  LEU A  72     1682   1887   1705    122    147   -210       C  
ATOM    614  CG  LEU A  72      22.723  38.423  48.578  1.00 13.17           C  
ANISOU  614  CG  LEU A  72     1445   1868   1692    329    158   -119       C  
ATOM    615  CD1 LEU A  72      21.338  38.879  49.055  1.00 15.67           C  
ANISOU  615  CD1 LEU A  72     1270   2532   2154      2    305   -477       C  
ATOM    616  CD2 LEU A  72      23.138  37.085  49.178  1.00 16.39           C  
ANISOU  616  CD2 LEU A  72     2318   1812   2096    104    188    143       C  
ATOM    617  N   THR A  73      23.964  36.376  44.629  1.00 16.08           N  
ANISOU  617  N   THR A  73     2672   1828   1610   -181    530   -243       N  
ATOM    618  CA  THR A  73      23.706  35.800  43.323  1.00 15.84           C  
ANISOU  618  CA  THR A  73     2327   1974   1715     86    155   -259       C  
ATOM    619  C   THR A  73      22.636  34.726  43.450  1.00 16.76           C  
ANISOU  619  C   THR A  73     2432   2168   1769    -58    -23   -118       C  
ATOM    620  O   THR A  73      22.289  34.307  44.548  1.00 16.51           O  
ANISOU  620  O   THR A  73     2334   2193   1746   -142    -82   -149       O  
ATOM    621  CB  THR A  73      24.981  35.168  42.745  1.00 15.42           C  
ANISOU  621  CB  THR A  73     2567   1701   1592    151    284   -186       C  
ATOM    622  OG1 THR A  73      25.395  34.118  43.650  1.00 16.25           O  
ANISOU  622  OG1 THR A  73     2763   1858   1555    245    345   -104       O  
ATOM    623  CG2 THR A  73      26.108  36.185  42.619  1.00 15.78           C  
ANISOU  623  CG2 THR A  73     2466   1954   1577    101    378   -142       C  
ATOM    624  N   GLU A  74      22.127  34.278  42.309  1.00 16.53           N  
ANISOU  624  N   GLU A  74     2384   2181   1716    -12    166   -304       N  
ATOM    625  CA  GLU A  74      21.182  33.172  42.304  1.00 18.51           C  
ANISOU  625  CA  GLU A  74     2674   2434   1926   -274    -73   -162       C  
ATOM    626  C   GLU A  74      21.786  31.978  43.030  1.00 18.00           C  
ANISOU  626  C   GLU A  74     2746   2123   1971    -33    373   -382       C  
ATOM    627  O   GLU A  74      21.155  31.299  43.834  1.00 19.51           O  
ANISOU  627  O   GLU A  74     2948   2036   2430   -205    364   -199       O  
ATOM    628  CB  GLU A  74      20.780  32.829  40.865  1.00 20.59           C  
ANISOU  628  CB  GLU A  74     2950   2685   2187     21   -237   -692       C  
ATOM    629  CG  GLU A  74      19.808  31.662  40.792  1.00 26.93           C  
ANISOU  629  CG  GLU A  74     3975   3586   2672   -921   -126  -1007       C  
ATOM    630  CD  GLU A  74      19.025  31.663  39.486  1.00 34.33           C  
ANISOU  630  CD  GLU A  74     4893   4695   3454  -1696  -1057   -721       C  
ATOM    631  OE1 GLU A  74      19.634  31.969  38.434  1.00 36.76           O  
ANISOU  631  OE1 GLU A  74     5426   5566   2976  -1608  -1421   -318       O  
ATOM    632  OE2 GLU A  74      17.811  31.362  39.505  1.00 42.74           O  
ANISOU  632  OE2 GLU A  74     4900   6460   4881  -1897  -1512     27       O  
ATOM    633  N   GLU A  75      23.074  31.720  42.766  1.00 17.94           N  
ANISOU  633  N   GLU A  75     2675   2403   1740    -58    137   -773       N  
ATOM    634  CA  GLU A  75      23.614  30.518  43.362  1.00 19.63           C  
ANISOU  634  CA  GLU A  75     2602   2574   2284     25     -3   -635       C  
ATOM    635  C   GLU A  75      23.695  30.663  44.873  1.00 18.19           C  
ANISOU  635  C   GLU A  75     2562   2109   2239   -174     97   -354       C  
ATOM    636  O   GLU A  75      23.381  29.706  45.571  1.00 18.30           O  
ANISOU  636  O   GLU A  75     2169   2080   2706   -137    272   -260       O  
ATOM    637  CB  GLU A  75      24.989  30.161  42.771  1.00 23.44           C  
ANISOU  637  CB  GLU A  75     3048   3225   2633    507    431   -387       C  
ATOM    638  CG  GLU A  75      25.464  28.835  43.377  1.00 30.74           C  
ANISOU  638  CG  GLU A  75     3841   3596   4244   1163      9   -164       C  
ATOM    639  CD  GLU A  75      26.866  28.488  42.925  1.00 34.75           C  
ANISOU  639  CD  GLU A  75     3869   4191   5142   1358     49   -294       C  
ATOM    640  OE1 GLU A  75      27.802  29.283  43.171  1.00 44.04           O  
ANISOU  640  OE1 GLU A  75     4087   6300   6347    254    -58   -189       O  
ATOM    641  OE2 GLU A  75      27.058  27.417  42.313  1.00 42.94           O  
ANISOU  641  OE2 GLU A  75     5801   4680   5836   1897   1315   -575       O  
ATOM    642  N   ILE A  76      24.131  31.837  45.353  1.00 16.17           N  
ANISOU  642  N   ILE A  76     2155   1960   2031     24    389   -384       N  
ATOM    643  CA  ILE A  76      24.224  32.019  46.815  1.00 16.50           C  
ANISOU  643  CA  ILE A  76     2349   1913   2010    -26    207   -191       C  
ATOM    644  C   ILE A  76      22.851  31.901  47.449  1.00 15.91           C  
ANISOU  644  C   ILE A  76     2424   1808   1815    131    286   -368       C  
ATOM    645  O   ILE A  76      22.632  31.274  48.495  1.00 16.85           O  
ANISOU  645  O   ILE A  76     2424   1890   2086    -58    237   -135       O  
ATOM    646  CB  ILE A  76      24.910  33.367  47.137  1.00 15.79           C  
ANISOU  646  CB  ILE A  76     2412   1667   1920    227    448   -345       C  
ATOM    647  CG1 ILE A  76      26.363  33.406  46.650  1.00 16.36           C  
ANISOU  647  CG1 ILE A  76     2395   1862   1960    -20    386    -31       C  
ATOM    648  CG2 ILE A  76      24.798  33.708  48.611  1.00 15.14           C  
ANISOU  648  CG2 ILE A  76     1875   2139   1740    424    -57   -176       C  
ATOM    649  CD1 ILE A  76      27.102  34.715  46.806  1.00 16.95           C  
ANISOU  649  CD1 ILE A  76     2327   1954   2159     62    -45   -511       C  
ATOM    650  N   LEU A  77      21.849  32.516  46.794  1.00 16.55           N  
ANISOU  650  N   LEU A  77     2328   2026   1934    -60    170   -239       N  
ATOM    651  CA  LEU A  77      20.495  32.489  47.331  1.00 15.85           C  
ANISOU  651  CA  LEU A  77     2317   1858   1849    -67    157   -221       C  
ATOM    652  C   LEU A  77      19.924  31.063  47.355  1.00 15.79           C  
ANISOU  652  C   LEU A  77     2548   1825   1625    -62    288   -227       C  
ATOM    653  O   LEU A  77      19.238  30.687  48.285  1.00 16.96           O  
ANISOU  653  O   LEU A  77     2186   2369   1888   -340    270   -223       O  
ATOM    654  CB  LEU A  77      19.630  33.463  46.532  1.00 16.76           C  
ANISOU  654  CB  LEU A  77     2445   1828   2094     30    182   -172       C  
ATOM    655  CG  LEU A  77      19.901  34.947  46.883  1.00 19.26           C  
ANISOU  655  CG  LEU A  77     3460   1800   2057   -104    301   -106       C  
ATOM    656  CD1 LEU A  77      19.145  35.848  45.915  1.00 20.49           C  
ANISOU  656  CD1 LEU A  77     3226   1835   2725    475    170   -367       C  
ATOM    657  CD2 LEU A  77      19.545  35.232  48.342  1.00 17.39           C  
ANISOU  657  CD2 LEU A  77     2147   1973   2486     48    782   -417       C  
ATOM    658  N   LYS A  78      20.193  30.254  46.353  1.00 18.15           N  
ANISOU  658  N   LYS A  78     2917   2131   1849    -49    187   -547       N  
ATOM    659  CA  LYS A  78      19.747  28.864  46.295  1.00 22.03           C  
ANISOU  659  CA  LYS A  78     4121   2307   1942   -456   -420   -671       C  
ATOM    660  C   LYS A  78      20.362  28.045  47.416  1.00 21.67           C  
ANISOU  660  C   LYS A  78     3430   2174   2629   -219   -148   -320       C  
ATOM    661  O   LYS A  78      19.760  27.073  47.872  1.00 21.49           O  
ANISOU  661  O   LYS A  78     3322   2348   2494   -272     49   -405       O  
ATOM    662  CB  LYS A  78      20.068  28.312  44.884  1.00 28.61           C  
ANISOU  662  CB  LYS A  78     5509   2968   2394   -365    -82  -1273       C  
ATOM    663  CG  LYS A  78      20.886  27.030  44.961  1.00 36.98           C  
ANISOU  663  CG  LYS A  78     6190   3859   4003    601    640  -1462       C  
ATOM    664  CD  LYS A  78      22.353  27.268  44.598  1.00 42.16           C  
ANISOU  664  CD  LYS A  78     5991   5092   4935    545    256  -1377       C  
ATOM    665  CE  LYS A  78      23.224  26.046  44.813  1.00 44.24           C  
ANISOU  665  CE  LYS A  78     6092   5411   5307    832    308  -1394       C  
ATOM    666  NZ  LYS A  78      22.517  24.958  45.548  1.00 60.27           N  
ANISOU  666  NZ  LYS A  78    10590   5571   6738   -627   -518   -288       N  
ATOM    667  N   GLU A  79      21.552  28.423  47.889  1.00 18.47           N  
ANISOU  667  N   GLU A  79     2936   1957   2126    129    376   -496       N  
ATOM    668  CA  GLU A  79      22.161  27.715  49.005  1.00 19.57           C  
ANISOU  668  CA  GLU A  79     2922   2090   2426    -40    284   -210       C  
ATOM    669  C   GLU A  79      21.683  28.248  50.348  1.00 18.43           C  
ANISOU  669  C   GLU A  79     3065   1716   2221     61    162     47       C  
ATOM    670  O   GLU A  79      22.082  27.699  51.396  1.00 20.31           O  
ANISOU  670  O   GLU A  79     3518   1794   2406    203   -147     31       O  
ATOM    671  CB  GLU A  79      23.675  27.875  48.956  1.00 20.68           C  
ANISOU  671  CB  GLU A  79     2933   2411   2514   -138    179   -264       C  
ATOM    672  CG  GLU A  79      24.261  27.362  47.653  1.00 22.33           C  
ANISOU  672  CG  GLU A  79     3013   2659   2814    -15    504   -274       C  
ATOM    673  CD  GLU A  79      25.736  27.651  47.472  1.00 23.99           C  
ANISOU  673  CD  GLU A  79     2794   2966   3354    404    341     73       C  
ATOM    674  OE1 GLU A  79      26.313  28.371  48.310  1.00 30.25           O  
ANISOU  674  OE1 GLU A  79     2743   4549   4200   -257    657   -873       O  
ATOM    675  OE2 GLU A  79      26.307  27.134  46.475  1.00 26.98           O  
ANISOU  675  OE2 GLU A  79     2733   3695   3822    555    465   -305       O  
ATOM    676  N   ASN A  80      20.881  29.307  50.349  1.00 16.92           N  
ANISOU  676  N   ASN A  80     2757   1506   2167   -176    149     73       N  
ATOM    677  CA  ASN A  80      20.498  29.908  51.626  1.00 18.38           C  
ANISOU  677  CA  ASN A  80     2981   1668   2334   -179    406     13       C  
ATOM    678  C   ASN A  80      19.022  30.211  51.628  1.00 17.03           C  
ANISOU  678  C   ASN A  80     3004   1498   1970   -127    199     35       C  
ATOM    679  O   ASN A  80      18.576  31.364  51.624  1.00 19.31           O  
ANISOU  679  O   ASN A  80     3248   1500   2589    -75   -174     37       O  
ATOM    680  CB  ASN A  80      21.244  31.224  51.887  1.00 19.12           C  
ANISOU  680  CB  ASN A  80     2810   1691   2762    -48    658   -420       C  
ATOM    681  CG  ASN A  80      22.692  31.038  52.270  1.00 19.28           C  
ANISOU  681  CG  ASN A  80     2895   1974   2457   -144    502   -311       C  
ATOM    682  OD1 ASN A  80      23.001  30.870  53.450  1.00 23.54           O  
ANISOU  682  OD1 ASN A  80     3105   3343   2496  -1025    461    133       O  
ATOM    683  ND2 ASN A  80      23.573  31.069  51.269  1.00 17.90           N  
ANISOU  683  ND2 ASN A  80     2664   1807   2330     -9    334   -380       N  
ATOM    684  N   PRO A  81      18.192  29.182  51.641  1.00 17.54           N  
ANISOU  684  N   PRO A  81     2949   1524   2192   -119     -6   -136       N  
ATOM    685  CA  PRO A  81      16.754  29.426  51.606  1.00 17.93           C  
ANISOU  685  CA  PRO A  81     2952   1622   2238    -82     79     31       C  
ATOM    686  C   PRO A  81      16.319  30.231  52.815  1.00 18.40           C  
ANISOU  686  C   PRO A  81     2893   1827   2272   -161    178    -16       C  
ATOM    687  O   PRO A  81      15.297  30.932  52.719  1.00 18.34           O  
ANISOU  687  O   PRO A  81     2736   1966   2266   -204    210    -99       O  
ATOM    688  CB  PRO A  81      16.184  28.009  51.595  1.00 19.14           C  
ANISOU  688  CB  PRO A  81     2879   1652   2743   -104    111     18       C  
ATOM    689  CG  PRO A  81      17.261  27.150  52.182  1.00 18.13           C  
ANISOU  689  CG  PRO A  81     2734   1524   2633    -16    337   -154       C  
ATOM    690  CD  PRO A  81      18.545  27.739  51.667  1.00 18.01           C  
ANISOU  690  CD  PRO A  81     2864   1509   2470   -169    314   -239       C  
ATOM    691  N  AASN A  82      17.026  30.163  53.940  0.50 17.44           N  
ANISOU  691  N  AASN A  82     2897   1576   2153   -162    282     73       N  
ATOM    692  N  BASN A  82      17.080  30.141  53.905  0.50 17.55           N  
ANISOU  692  N  BASN A  82     2883   1625   2160   -181    271     65       N  
ATOM    693  CA AASN A  82      16.518  30.965  55.057  0.50 16.35           C  
ANISOU  693  CA AASN A  82     2644   1464   2103     -5    296    251       C  
ATOM    694  CA BASN A  82      16.843  30.871  55.147  0.50 17.84           C  
ANISOU  694  CA BASN A  82     3151   1530   2098   -211    389    157       C  
ATOM    695  C  AASN A  82      16.680  32.452  54.766  0.50 16.18           C  
ANISOU  695  C  AASN A  82     2719   1499   1928   -111    315    236       C  
ATOM    696  C  BASN A  82      16.861  32.382  54.898  0.50 17.04           C  
ANISOU  696  C  BASN A  82     2948   1549   1976   -250    335    176       C  
ATOM    697  O  AASN A  82      15.898  33.261  55.278  0.50 15.96           O  
ANISOU  697  O  AASN A  82     2828   1389   1848   -106    349    293       O  
ATOM    698  O  BASN A  82      16.133  33.131  55.561  0.50 17.38           O  
ANISOU  698  O  BASN A  82     3047   1519   2037   -149    447    347       O  
ATOM    699  CB AASN A  82      17.216  30.591  56.357  0.50 16.30           C  
ANISOU  699  CB AASN A  82     2620   1479   2094    152    341    190       C  
ATOM    700  CB BASN A  82      17.808  30.481  56.253  0.50 17.97           C  
ANISOU  700  CB BASN A  82     3280   1529   2019   -155    408    183       C  
ATOM    701  CG AASN A  82      16.774  29.291  56.981  0.50 20.21           C  
ANISOU  701  CG AASN A  82     3979   1724   1977   -127    465    321       C  
ATOM    702  CG BASN A  82      19.298  30.626  56.272  0.50 17.10           C  
ANISOU  702  CG BASN A  82     3213   1882   1403     33    559    252       C  
ATOM    703  OD1AASN A  82      15.891  28.608  56.443  0.50 30.73           O  
ANISOU  703  OD1AASN A  82     6161   2386   3130  -1217  -1111   1126       O  
ATOM    704  OD1BASN A  82      20.006  30.821  55.247  0.50 17.87           O  
ANISOU  704  OD1BASN A  82     3370   2335   1084    379    460    315       O  
ATOM    705  ND2AASN A  82      17.345  28.900  58.114  0.50 19.97           N  
ANISOU  705  ND2AASN A  82     4483   1585   1520   -621    443    799       N  
ATOM    706  ND2BASN A  82      19.901  30.486  57.472  0.50 13.55           N  
ANISOU  706  ND2BASN A  82     3023    901   1226   -217    839    551       N  
ATOM    707  N   VAL A  83      17.655  32.837  53.963  1.00 15.16           N  
ANISOU  707  N   VAL A  83     2165   1705   1889    -93    -63    368       N  
ATOM    708  CA  VAL A  83      17.802  34.246  53.577  1.00 15.64           C  
ANISOU  708  CA  VAL A  83     2061   1797   2083   -322   -183    455       C  
ATOM    709  C   VAL A  83      16.687  34.669  52.623  1.00 14.80           C  
ANISOU  709  C   VAL A  83     1906   1731   1987   -105     24    423       C  
ATOM    710  O   VAL A  83      16.322  35.861  52.576  1.00 18.09           O  
ANISOU  710  O   VAL A  83     2391   1973   2510    396    299    316       O  
ATOM    711  CB  VAL A  83      19.180  34.429  52.924  1.00 15.37           C  
ANISOU  711  CB  VAL A  83     1951   1833   2055   -170   -255    439       C  
ATOM    712  CG1 VAL A  83      19.278  35.764  52.195  1.00 16.42           C  
ANISOU  712  CG1 VAL A  83     2050   1949   2239     90    316    564       C  
ATOM    713  CG2 VAL A  83      20.275  34.295  53.985  1.00 15.14           C  
ANISOU  713  CG2 VAL A  83     2043   2091   1619     43   -125    -34       C  
ATOM    714  N   CYS A  84      16.129  33.713  51.885  1.00 17.38           N  
ANISOU  714  N   CYS A  84     2422   2146   2036   -269   -332    354       N  
ATOM    715  CA  CYS A  84      15.073  33.967  50.896  1.00 16.00           C  
ANISOU  715  CA  CYS A  84     2312   1877   1891     87   -125    224       C  
ATOM    716  C   CYS A  84      13.692  34.060  51.521  1.00 17.40           C  
ANISOU  716  C   CYS A  84     2354   2035   2221    -82      4    148       C  
ATOM    717  O   CYS A  84      12.749  34.570  50.930  1.00 18.93           O  
ANISOU  717  O   CYS A  84     2323   2258   2613    153    235    489       O  
ATOM    718  CB  CYS A  84      15.079  32.849  49.842  1.00 18.01           C  
ANISOU  718  CB  CYS A  84     2629   2310   1904   -319     29    -13       C  
ATOM    719  SG  CYS A  84      16.561  32.931  48.788  1.00 20.00           S  
ANISOU  719  SG  CYS A  84     2652   2709   2238   -244    175   -315       S  
ATOM    720  N  AGLU A  85      13.563  33.536  52.745  0.63 17.12           N  
ANISOU  720  N  AGLU A  85     2460   1909   2134   -106     91      5       N  
ATOM    721  N  BGLU A  85      13.581  33.552  52.748  0.37 17.17           N  
ANISOU  721  N  BGLU A  85     2455   1922   2147    -90     99     17       N  
ATOM    722  CA AGLU A  85      12.279  33.695  53.411  0.63 17.76           C  
ANISOU  722  CA AGLU A  85     2488   1975   2285    -68    151    -21       C  
ATOM    723  CA BGLU A  85      12.327  33.689  53.472  0.37 17.48           C  
ANISOU  723  CA BGLU A  85     2431   1933   2278    -34    116     34       C  
ATOM    724  C  AGLU A  85      12.112  35.124  53.909  0.63 17.14           C  
ANISOU  724  C  AGLU A  85     2216   1945   2353    -26     13     17       C  
ATOM    725  C  BGLU A  85      12.120  35.123  53.934  0.37 17.02           C  
ANISOU  725  C  BGLU A  85     2201   1926   2339     -8     -6     42       C  
ATOM    726  O  AGLU A  85      13.098  35.854  54.090  0.63 17.35           O  
ANISOU  726  O  AGLU A  85     2184   1971   2438    -51     78     53       O  
ATOM    727  O  BGLU A  85      13.086  35.879  54.100  0.37 17.34           O  
ANISOU  727  O  BGLU A  85     2184   1969   2434    -45    120     20       O  
ATOM    728  CB AGLU A  85      12.172  32.734  54.596  0.63 17.48           C  
ANISOU  728  CB AGLU A  85     2345   1955   2342    142    292      7       C  
ATOM    729  CB BGLU A  85      12.330  32.757  54.686  0.37 17.56           C  
ANISOU  729  CB BGLU A  85     2370   1969   2334    135    265     82       C  
ATOM    730  CG AGLU A  85      11.964  31.279  54.193  0.63 19.08           C  
ANISOU  730  CG AGLU A  85     2515   1933   2800     46     53     55       C  
ATOM    731  CG BGLU A  85      12.428  31.281  54.322  0.37 18.76           C  
ANISOU  731  CG BGLU A  85     2530   1932   2667     72     48     99       C  
ATOM    732  CD AGLU A  85      11.642  30.433  55.410  0.63 19.44           C  
ANISOU  732  CD AGLU A  85     2551   1977   2857     75    -70    178       C  
ATOM    733  CD BGLU A  85      11.191  30.530  54.772  0.37 20.11           C  
ANISOU  733  CD BGLU A  85     2576   2106   2957    -51     17    169       C  
ATOM    734  OE1AGLU A  85      10.736  30.859  56.158  0.63 18.95           O  
ANISOU  734  OE1AGLU A  85     2053   2433   2714     89   -279    431       O  
ATOM    735  OE1BGLU A  85      10.141  31.189  54.903  0.37 22.23           O  
ANISOU  735  OE1BGLU A  85     2591   2389   3466    -16    243   -176       O  
ATOM    736  OE2AGLU A  85      12.281  29.368  55.606  0.63 22.46           O  
ANISOU  736  OE2AGLU A  85     2945   2374   3216    471    -62    391       O  
ATOM    737  OE2BGLU A  85      11.272  29.302  54.992  0.37 23.96           O  
ANISOU  737  OE2BGLU A  85     3006   2243   3856   -150     33    604       O  
ATOM    738  N   TYR A  86      10.867  35.509  54.184  1.00 15.95           N  
ANISOU  738  N   TYR A  86     2068   1826   2165    165   -569    354       N  
ATOM    739  CA  TYR A  86      10.683  36.834  54.785  1.00 15.57           C  
ANISOU  739  CA  TYR A  86     1732   2069   2114   -100    -49    117       C  
ATOM    740  C   TYR A  86      11.277  36.867  56.187  1.00 15.72           C  
ANISOU  740  C   TYR A  86     1635   2152   2184    -18    -87    117       C  
ATOM    741  O   TYR A  86      11.915  37.849  56.570  1.00 15.59           O  
ANISOU  741  O   TYR A  86     1484   2115   2325    108   -195     55       O  
ATOM    742  CB  TYR A  86       9.203  37.199  54.808  1.00 16.31           C  
ANISOU  742  CB  TYR A  86     1778   2246   2173     32   -159    217       C  
ATOM    743  CG  TYR A  86       8.956  38.413  55.690  1.00 16.60           C  
ANISOU  743  CG  TYR A  86     1739   2479   2090    190   -229    121       C  
ATOM    744  CD1 TYR A  86       9.337  39.681  55.285  1.00 16.67           C  
ANISOU  744  CD1 TYR A  86     1868   2346   2120    142   -410    -51       C  
ATOM    745  CD2 TYR A  86       8.345  38.213  56.924  1.00 19.82           C  
ANISOU  745  CD2 TYR A  86     2506   3040   1985     55   -148     97       C  
ATOM    746  CE1 TYR A  86       9.103  40.779  56.123  1.00 18.73           C  
ANISOU  746  CE1 TYR A  86     2031   2531   2555    449    -92   -175       C  
ATOM    747  CE2 TYR A  86       8.112  39.290  57.743  1.00 19.18           C  
ANISOU  747  CE2 TYR A  86     2018   3288   1982    430   -343     19       C  
ATOM    748  CZ  TYR A  86       8.484  40.548  57.348  1.00 20.68           C  
ANISOU  748  CZ  TYR A  86     2153   3173   2532    187    -26   -391       C  
ATOM    749  OH  TYR A  86       8.217  41.570  58.223  1.00 24.00           O  
ANISOU  749  OH  TYR A  86     2919   3714   2486   -119   -196   -871       O  
ATOM    750  N   MET A  87      11.086  35.851  57.016  1.00 14.80           N  
ANISOU  750  N   MET A  87     1685   1932   2008    296     61    -44       N  
ATOM    751  CA  MET A  87      11.595  35.982  58.377  1.00 15.11           C  
ANISOU  751  CA  MET A  87     1687   2017   2036    306     28    -97       C  
ATOM    752  C   MET A  87      12.046  34.641  58.918  1.00 14.35           C  
ANISOU  752  C   MET A  87     1591   1982   1879    160     79    -70       C  
ATOM    753  O   MET A  87      11.295  33.930  59.598  1.00 18.64           O  
ANISOU  753  O   MET A  87     1703   2219   3159     74    396    287       O  
ATOM    754  CB  MET A  87      10.506  36.536  59.286  1.00 16.40           C  
ANISOU  754  CB  MET A  87     1993   2253   1987    510    152     32       C  
ATOM    755  CG  MET A  87      11.032  37.092  60.607  1.00 21.70           C  
ANISOU  755  CG  MET A  87     3308   3037   1901    119    277   -243       C  
ATOM    756  SD  MET A  87      12.118  38.525  60.377  1.00 24.78           S  
ANISOU  756  SD  MET A  87     2842   2972   3604    136   -344   -620       S  
ATOM    757  CE  MET A  87      10.978  39.718  59.681  1.00 22.27           C  
ANISOU  757  CE  MET A  87     3121   2426   2916    250     19   -924       C  
ATOM    758  N   ALA A  88      13.286  34.273  58.629  1.00 12.96           N  
ANISOU  758  N   ALA A  88     1602   1877   1445    197     -5   -169       N  
ATOM    759  CA  ALA A  88      13.793  32.979  59.117  1.00 13.46           C  
ANISOU  759  CA  ALA A  88     1670   1958   1488    164      2     10       C  
ATOM    760  C   ALA A  88      15.173  33.177  59.740  1.00 12.62           C  
ANISOU  760  C   ALA A  88     1600   1862   1334     74    122    193       C  
ATOM    761  O   ALA A  88      15.928  34.032  59.251  1.00 14.31           O  
ANISOU  761  O   ALA A  88     2192   1822   1423   -322   -128    212       O  
ATOM    762  CB  ALA A  88      13.871  31.969  57.993  1.00 14.99           C  
ANISOU  762  CB  ALA A  88     2160   1541   1996   -292    103   -103       C  
ATOM    763  N   PRO A  89      15.512  32.405  60.777  1.00 13.43           N  
ANISOU  763  N   PRO A  89     1709   1857   1537     -4     17    319       N  
ATOM    764  CA  PRO A  89      16.839  32.521  61.371  1.00 12.67           C  
ANISOU  764  CA  PRO A  89     1589   1571   1653    199     80    313       C  
ATOM    765  C   PRO A  89      17.927  32.401  60.310  1.00 13.60           C  
ANISOU  765  C   PRO A  89     1768   1593   1806    -29    221    -40       C  
ATOM    766  O   PRO A  89      18.012  31.415  59.578  1.00 14.09           O  
ANISOU  766  O   PRO A  89     1650   1817   1888    -45    -10   -249       O  
ATOM    767  CB  PRO A  89      16.897  31.314  62.322  1.00 16.03           C  
ANISOU  767  CB  PRO A  89     1848   1969   2274    -90   -135    826       C  
ATOM    768  CG  PRO A  89      15.471  30.953  62.612  1.00 17.32           C  
ANISOU  768  CG  PRO A  89     1852   2394   2334   -277   -334   1053       C  
ATOM    769  CD  PRO A  89      14.643  31.392  61.439  1.00 15.52           C  
ANISOU  769  CD  PRO A  89     2011   2054   1832   -343   -287    546       C  
ATOM    770  N   SER A  90      18.769  33.437  60.210  1.00 14.02           N  
ANISOU  770  N   SER A  90     1955   1551   1820    -80    359     14       N  
ATOM    771  CA  SER A  90      19.710  33.529  59.101  1.00 12.10           C  
ANISOU  771  CA  SER A  90     1455   1841   1301    -90   -154    -87       C  
ATOM    772  C   SER A  90      20.862  34.481  59.363  1.00 12.36           C  
ANISOU  772  C   SER A  90     1470   1836   1389    -98   -141   -177       C  
ATOM    773  O   SER A  90      21.697  34.639  58.452  1.00 13.30           O  
ANISOU  773  O   SER A  90     2019   1784   1249   -411    -77    177       O  
ATOM    774  CB  SER A  90      18.983  34.026  57.826  1.00 12.75           C  
ANISOU  774  CB  SER A  90     1402   1829   1615    195   -305   -103       C  
ATOM    775  OG  SER A  90      18.168  35.150  58.091  1.00 12.98           O  
ANISOU  775  OG  SER A  90     1384   1580   1968    -27     37    -23       O  
ATOM    776  N   LEU A  91      20.911  35.102  60.552  1.00 12.73           N  
ANISOU  776  N   LEU A  91     1599   1793   1445    -63   -172   -189       N  
ATOM    777  CA  LEU A  91      21.983  36.059  60.822  1.00 11.84           C  
ANISOU  777  CA  LEU A  91     1449   1515   1536    189   -123   -325       C  
ATOM    778  C   LEU A  91      23.370  35.446  60.704  1.00 12.03           C  
ANISOU  778  C   LEU A  91     1486   1507   1578    233    -32     56       C  
ATOM    779  O   LEU A  91      24.293  36.126  60.198  1.00 12.44           O  
ANISOU  779  O   LEU A  91     1538   1517   1672    139     32    -69       O  
ATOM    780  CB  LEU A  91      21.793  36.687  62.214  1.00 10.76           C  
ANISOU  780  CB  LEU A  91     1202   1726   1162     73   -227     -8       C  
ATOM    781  CG  LEU A  91      22.940  37.647  62.597  1.00 12.21           C  
ANISOU  781  CG  LEU A  91     1614   1930   1095   -384    306   -237       C  
ATOM    782  CD1 LEU A  91      22.951  38.876  61.693  1.00 15.10           C  
ANISOU  782  CD1 LEU A  91     2584   1951   1202   -533     40   -191       C  
ATOM    783  CD2 LEU A  91      22.836  38.009  64.067  1.00 12.72           C  
ANISOU  783  CD2 LEU A  91     1682   2051   1102   -221    113   -299       C  
ATOM    784  N   ASP A  92      23.544  34.197  61.141  1.00 12.27           N  
ANISOU  784  N   ASP A  92     1666   1557   1438    229   -164     84       N  
ATOM    785  CA  ASP A  92      24.901  33.619  61.105  1.00 12.27           C  
ANISOU  785  CA  ASP A  92     1699   1499   1465    275   -267      2       C  
ATOM    786  C   ASP A  92      25.360  33.518  59.657  1.00 11.77           C  
ANISOU  786  C   ASP A  92     1561   1424   1487    266   -232     68       C  
ATOM    787  O   ASP A  92      26.498  33.897  59.348  1.00 13.45           O  
ANISOU  787  O   ASP A  92     1810   1461   1841    -33    -57    -69       O  
ATOM    788  CB  ASP A  92      24.956  32.239  61.770  1.00 12.64           C  
ANISOU  788  CB  ASP A  92     1471   1766   1565    120   -512    298       C  
ATOM    789  CG  ASP A  92      24.839  32.332  63.276  1.00 14.23           C  
ANISOU  789  CG  ASP A  92     1878   1918   1611    -73   -307    239       C  
ATOM    790  OD1 ASP A  92      24.800  33.462  63.815  1.00 15.03           O  
ANISOU  790  OD1 ASP A  92     1965   2024   1723     39   -173    111       O  
ATOM    791  OD2 ASP A  92      24.768  31.279  63.953  1.00 15.22           O  
ANISOU  791  OD2 ASP A  92     2099   2052   1633    162   -143    362       O  
ATOM    792  N   ALA A  93      24.496  33.030  58.755  1.00 12.23           N  
ANISOU  792  N   ALA A  93     1878   1387   1383      4   -238    175       N  
ATOM    793  CA  ALA A  93      24.846  32.963  57.333  1.00 11.60           C  
ANISOU  793  CA  ALA A  93     1807   1157   1445    131   -158    110       C  
ATOM    794  C   ALA A  93      25.124  34.348  56.725  1.00 11.65           C  
ANISOU  794  C   ALA A  93     1671   1128   1626    226    325     64       C  
ATOM    795  O   ALA A  93      26.072  34.523  55.955  1.00 14.15           O  
ANISOU  795  O   ALA A  93     1727   1673   1979     79    482     55       O  
ATOM    796  CB  ALA A  93      23.716  32.303  56.537  1.00 11.70           C  
ANISOU  796  CB  ALA A  93     1700   1514   1233    -39      2    176       C  
ATOM    797  N   ARG A  94      24.272  35.326  57.035  1.00 12.16           N  
ANISOU  797  N   ARG A  94     1571   1245   1805    347     70    119       N  
ATOM    798  CA  ARG A  94      24.465  36.686  56.554  1.00 11.96           C  
ANISOU  798  CA  ARG A  94     1144   1329   2071    461   -116    318       C  
ATOM    799  C   ARG A  94      25.756  37.314  57.072  1.00 11.54           C  
ANISOU  799  C   ARG A  94     1110   1508   1767    342    138    163       C  
ATOM    800  O   ARG A  94      26.499  37.921  56.290  1.00 12.78           O  
ANISOU  800  O   ARG A  94     1604   1700   1553      3    160     24       O  
ATOM    801  CB  ARG A  94      23.267  37.536  57.009  1.00 11.64           C  
ANISOU  801  CB  ARG A  94     1103   1349   1969    335    -72     74       C  
ATOM    802  CG  ARG A  94      21.942  37.038  56.396  1.00 11.48           C  
ANISOU  802  CG  ARG A  94     1075   1414   1872    273     62    -81       C  
ATOM    803  CD  ARG A  94      20.804  37.731  57.153  1.00 11.08           C  
ANISOU  803  CD  ARG A  94     1094   1486   1630    174    135    -23       C  
ATOM    804  NE  ARG A  94      19.451  37.391  56.784  1.00 11.33           N  
ANISOU  804  NE  ARG A  94     1074   1619   1614    151    137    103       N  
ATOM    805  CZ  ARG A  94      18.773  37.812  55.717  1.00 12.64           C  
ANISOU  805  CZ  ARG A  94     1332   1615   1856     66   -102    207       C  
ATOM    806  NH1 ARG A  94      19.365  38.623  54.853  1.00 11.18           N  
ANISOU  806  NH1 ARG A  94     1637   1262   1350    293    185   -202       N  
ATOM    807  NH2 ARG A  94      17.507  37.415  55.516  1.00 13.33           N  
ANISOU  807  NH2 ARG A  94     1295   1580   2191    211   -212    -72       N  
ATOM    808  N   GLN A  95      26.046  37.191  58.373  1.00 11.98           N  
ANISOU  808  N   GLN A  95     1313   1534   1704     84    171    158       N  
ATOM    809  CA  GLN A  95      27.305  37.660  58.946  1.00 12.77           C  
ANISOU  809  CA  GLN A  95     1341   1730   1780    142    144   -125       C  
ATOM    810  C   GLN A  95      28.518  37.040  58.247  1.00 12.67           C  
ANISOU  810  C   GLN A  95     1324   1648   1840     90    206   -113       C  
ATOM    811  O   GLN A  95      29.505  37.711  57.901  1.00 12.61           O  
ANISOU  811  O   GLN A  95     1391   1656   1745     22    164   -121       O  
ATOM    812  CB  GLN A  95      27.408  37.319  60.441  1.00 13.94           C  
ANISOU  812  CB  GLN A  95     1756   1876   1665      3    112   -354       C  
ATOM    813  CG  GLN A  95      26.508  38.172  61.339  1.00 15.25           C  
ANISOU  813  CG  GLN A  95     2290   1697   1807    202    110   -436       C  
ATOM    814  CD  GLN A  95      27.226  39.475  61.721  1.00 14.53           C  
ANISOU  814  CD  GLN A  95     2269   1570   1681    150     71    -76       C  
ATOM    815  OE1 GLN A  95      27.495  40.318  60.863  1.00 16.26           O  
ANISOU  815  OE1 GLN A  95     2232   2057   1888    154    -56    323       O  
ATOM    816  NE2 GLN A  95      27.526  39.671  63.013  1.00 13.30           N  
ANISOU  816  NE2 GLN A  95     1758   1542   1752     43    -76      7       N  
ATOM    817  N   ASP A  96      28.489  35.724  58.031  1.00 12.58           N  
ANISOU  817  N   ASP A  96     1301   1571   1908    156    152     75       N  
ATOM    818  CA  ASP A  96      29.587  35.070  57.330  1.00 13.39           C  
ANISOU  818  CA  ASP A  96     1613   1606   1869    400    176    151       C  
ATOM    819  C   ASP A  96      29.799  35.710  55.961  1.00 13.42           C  
ANISOU  819  C   ASP A  96     1575   1765   1758    109    134     44       C  
ATOM    820  O   ASP A  96      30.964  35.862  55.540  1.00 15.79           O  
ANISOU  820  O   ASP A  96     1642   2219   2140    196    332    139       O  
ATOM    821  CB  ASP A  96      29.306  33.571  57.192  1.00 14.53           C  
ANISOU  821  CB  ASP A  96     2021   1590   1910    426    -61    119       C  
ATOM    822  CG  ASP A  96      29.362  32.858  58.542  1.00 16.45           C  
ANISOU  822  CG  ASP A  96     2285   1808   2158    258   -106    413       C  
ATOM    823  OD1 ASP A  96      29.782  33.443  59.568  1.00 20.18           O  
ANISOU  823  OD1 ASP A  96     3033   2572   2064   -103   -498    594       O  
ATOM    824  OD2 ASP A  96      28.971  31.673  58.564  1.00 18.62           O  
ANISOU  824  OD2 ASP A  96     2358   1831   2885    235    205    546       O  
ATOM    825  N   MET A  97      28.737  36.116  55.270  1.00 12.42           N  
ANISOU  825  N   MET A  97     1665   1382   1673   -133    -21    -15       N  
ATOM    826  CA  MET A  97      28.911  36.811  54.000  1.00 12.74           C  
ANISOU  826  CA  MET A  97     1799   1427   1615     -4    106    -94       C  
ATOM    827  C   MET A  97      29.578  38.178  54.169  1.00 12.32           C  
ANISOU  827  C   MET A  97     1720   1271   1692    139    204     20       C  
ATOM    828  O   MET A  97      30.590  38.476  53.528  1.00 13.00           O  
ANISOU  828  O   MET A  97     1669   1615   1655    -26    164   -141       O  
ATOM    829  CB  MET A  97      27.557  37.026  53.304  1.00 12.51           C  
ANISOU  829  CB  MET A  97     1849   1223   1682    118     92     34       C  
ATOM    830  CG  MET A  97      26.964  35.686  52.857  1.00 14.17           C  
ANISOU  830  CG  MET A  97     2167   1452   1763    132   -317   -227       C  
ATOM    831  SD  MET A  97      25.253  35.937  52.339  1.00 15.84           S  
ANISOU  831  SD  MET A  97     2101   1824   2094      2   -293    -23       S  
ATOM    832  CE  MET A  97      24.690  34.246  52.270  1.00 18.25           C  
ANISOU  832  CE  MET A  97     2875   1954   2104   -278  -1015   -353       C  
ATOM    833  N   VAL A  98      28.961  39.007  55.027  1.00 11.25           N  
ANISOU  833  N   VAL A  98     1806   1294   1174    144     40    140       N  
ATOM    834  CA  VAL A  98      29.347  40.415  54.979  1.00 11.10           C  
ANISOU  834  CA  VAL A  98     1348   1318   1551    156    140    -33       C  
ATOM    835  C   VAL A  98      30.560  40.728  55.835  1.00 11.90           C  
ANISOU  835  C   VAL A  98     1247   1597   1679    170    142     50       C  
ATOM    836  O   VAL A  98      31.181  41.775  55.622  1.00 12.68           O  
ANISOU  836  O   VAL A  98     1576   1687   1554    -64     15    -66       O  
ATOM    837  CB  VAL A  98      28.154  41.314  55.401  1.00 10.90           C  
ANISOU  837  CB  VAL A  98     1284   1429   1426    193    102     48       C  
ATOM    838  CG1 VAL A  98      27.023  41.125  54.410  1.00 15.88           C  
ANISOU  838  CG1 VAL A  98     1831   1905   2299    286   -720    575       C  
ATOM    839  CG2 VAL A  98      27.689  41.019  56.826  1.00 13.36           C  
ANISOU  839  CG2 VAL A  98     2191   1363   1523      5    515   -165       C  
ATOM    840  N   VAL A  99      30.912  39.872  56.818  1.00 12.44           N  
ANISOU  840  N   VAL A  99     1532   1690   1505    203     75    -33       N  
ATOM    841  CA  VAL A  99      32.140  40.179  57.572  1.00 13.12           C  
ANISOU  841  CA  VAL A  99     1544   1982   1458     62     89    115       C  
ATOM    842  C   VAL A  99      33.343  40.098  56.651  1.00 12.90           C  
ANISOU  842  C   VAL A  99     1536   1781   1583    164    105     87       C  
ATOM    843  O   VAL A  99      34.364  40.761  56.902  1.00 14.44           O  
ANISOU  843  O   VAL A  99     1699   1838   1950    -59    324      0       O  
ATOM    844  CB  VAL A  99      32.235  39.228  58.779  1.00 16.22           C  
ANISOU  844  CB  VAL A  99     1788   2678   1696   -172    -74    546       C  
ATOM    845  CG1 VAL A  99      33.625  39.235  59.391  1.00 21.03           C  
ANISOU  845  CG1 VAL A  99     2144   3025   2823     76   -733    752       C  
ATOM    846  CG2 VAL A  99      31.192  39.615  59.846  1.00 17.14           C  
ANISOU  846  CG2 VAL A  99     2298   2614   1601   -898    223    106       C  
ATOM    847  N   VAL A 100      33.212  39.297  55.583  1.00 12.39           N  
ANISOU  847  N   VAL A 100     1746   1425   1536    328    111    229       N  
ATOM    848  CA  VAL A 100      34.249  39.178  54.570  1.00 12.52           C  
ANISOU  848  CA  VAL A 100     1551   1630   1575    350     22    128       C  
ATOM    849  C   VAL A 100      34.025  40.184  53.444  1.00 11.91           C  
ANISOU  849  C   VAL A 100     1692   1648   1183    -74   -176    -43       C  
ATOM    850  O   VAL A 100      34.950  40.896  53.022  1.00 13.87           O  
ANISOU  850  O   VAL A 100     1700   1947   1622     38    210    109       O  
ATOM    851  CB  VAL A 100      34.282  37.760  53.980  1.00 14.18           C  
ANISOU  851  CB  VAL A 100     2118   1672   1596     73    486     72       C  
ATOM    852  CG1 VAL A 100      35.289  37.687  52.840  1.00 15.33           C  
ANISOU  852  CG1 VAL A 100     2019   1809   1998     78    665    -11       C  
ATOM    853  CG2 VAL A 100      34.641  36.746  55.066  1.00 16.00           C  
ANISOU  853  CG2 VAL A 100     2507   1620   1952    504    547    143       C  
ATOM    854  N   GLU A 101      32.796  40.265  52.911  1.00 11.77           N  
ANISOU  854  N   GLU A 101     1727   1430   1315    136   -206   -134       N  
ATOM    855  CA  GLU A 101      32.621  41.124  51.742  1.00 11.07           C  
ANISOU  855  CA  GLU A 101     1220   1472   1514    243     64     34       C  
ATOM    856  C   GLU A 101      32.768  42.610  52.057  1.00 11.41           C  
ANISOU  856  C   GLU A 101     1384   1534   1418    -29    238     45       C  
ATOM    857  O   GLU A 101      33.272  43.356  51.176  1.00 13.53           O  
ANISOU  857  O   GLU A 101     1826   1690   1624     60    373    290       O  
ATOM    858  CB  GLU A 101      31.263  40.821  51.072  1.00 12.16           C  
ANISOU  858  CB  GLU A 101     1506   1554   1559     39   -190    173       C  
ATOM    859  CG  GLU A 101      31.009  41.680  49.837  1.00 13.74           C  
ANISOU  859  CG  GLU A 101     1564   2022   1635    271    -41    384       C  
ATOM    860  CD  GLU A 101      31.828  41.285  48.616  1.00 15.24           C  
ANISOU  860  CD  GLU A 101     1785   2261   1744    326    135    444       C  
ATOM    861  OE1 GLU A 101      32.716  40.400  48.727  1.00 16.21           O  
ANISOU  861  OE1 GLU A 101     2363   1701   2096    400    257    161       O  
ATOM    862  OE2 GLU A 101      31.578  41.873  47.518  1.00 16.39           O  
ANISOU  862  OE2 GLU A 101     2126   2416   1684     96     66    475       O  
ATOM    863  N   VAL A 102      32.328  43.090  53.221  1.00 11.06           N  
ANISOU  863  N   VAL A 102     1127   1541   1533     91    221    -29       N  
ATOM    864  CA  VAL A 102      32.444  44.542  53.451  1.00 11.65           C  
ANISOU  864  CA  VAL A 102     1220   1591   1615    -72    254    -68       C  
ATOM    865  C   VAL A 102      33.897  44.981  53.350  1.00 11.69           C  
ANISOU  865  C   VAL A 102     1225   1748   1468    -87    192    133       C  
ATOM    866  O   VAL A 102      34.161  45.913  52.584  1.00 12.03           O  
ANISOU  866  O   VAL A 102     1369   1439   1761    -13    348     55       O  
ATOM    867  CB  VAL A 102      31.774  44.929  54.786  1.00 11.16           C  
ANISOU  867  CB  VAL A 102     1059   1609   1572    -41    114   -171       C  
ATOM    868  CG1 VAL A 102      32.218  46.295  55.274  1.00 12.41           C  
ANISOU  868  CG1 VAL A 102     1602   1668   1447   -342    127    -52       C  
ATOM    869  CG2 VAL A 102      30.269  44.891  54.610  1.00 12.67           C  
ANISOU  869  CG2 VAL A 102     1056   2129   1628   -133    120    -72       C  
ATOM    870  N  APRO A 103      34.847  44.393  54.073  0.46 12.06           N  
ANISOU  870  N  APRO A 103     1361   1816   1405   -112      0    -29       N  
ATOM    871  N  BPRO A 103      34.840  44.388  54.074  0.54 12.05           N  
ANISOU  871  N  BPRO A 103     1364   1786   1431    -98     -3    -33       N  
ATOM    872  CA APRO A 103      36.242  44.786  53.870  0.46 12.24           C  
ANISOU  872  CA APRO A 103     1297   1840   1515     12     41    -10       C  
ATOM    873  CA BPRO A 103      36.234  44.792  53.874  0.54 12.22           C  
ANISOU  873  CA BPRO A 103     1298   1821   1525     22     37     -9       C  
ATOM    874  C  APRO A 103      36.792  44.446  52.486  0.46 12.66           C  
ANISOU  874  C  APRO A 103     1421   1867   1521    -68     89    -22       C  
ATOM    875  C  BPRO A 103      36.793  44.437  52.498  0.54 12.63           C  
ANISOU  875  C  BPRO A 103     1414   1855   1530    -38     70    -24       C  
ATOM    876  O  APRO A 103      37.636  45.198  51.971  0.46 13.05           O  
ANISOU  876  O  APRO A 103     1291   2062   1606    -12     55    163       O  
ATOM    877  O  BPRO A 103      37.649  45.185  51.990  0.54 13.53           O  
ANISOU  877  O  BPRO A 103     1558   1979   1604    -48    137    120       O  
ATOM    878  CB APRO A 103      37.006  44.009  54.944  0.46 12.93           C  
ANISOU  878  CB APRO A 103     1351   1975   1585    -89     -2    135       C  
ATOM    879  CB BPRO A 103      36.971  44.059  54.999  0.54 12.91           C  
ANISOU  879  CB BPRO A 103     1356   1966   1582   -106      0    123       C  
ATOM    880  CG APRO A 103      36.008  43.394  55.845  0.46 12.15           C  
ANISOU  880  CG APRO A 103     1231   1848   1537    -49    -14      6       C  
ATOM    881  CG BPRO A 103      36.079  42.961  55.443  0.54 12.69           C  
ANISOU  881  CG BPRO A 103     1272   1949   1602    -81      4     83       C  
ATOM    882  CD APRO A 103      34.674  43.403  55.149  0.46 12.48           C  
ANISOU  882  CD APRO A 103     1352   1853   1538    -99   -120     80       C  
ATOM    883  CD BPRO A 103      34.663  43.391  55.145  0.54 12.44           C  
ANISOU  883  CD BPRO A 103     1335   1842   1550    -81   -120     73       C  
ATOM    884  N   ARG A 104      36.386  43.359  51.846  1.00 13.74           N  
ANISOU  884  N   ARG A 104     1719   1814   1688     53     52   -123       N  
ATOM    885  CA  ARG A 104      36.918  43.017  50.518  1.00 13.94           C  
ANISOU  885  CA  ARG A 104     1804   1694   1798    406     79   -124       C  
ATOM    886  C   ARG A 104      36.560  44.106  49.502  1.00 13.40           C  
ANISOU  886  C   ARG A 104     1432   1870   1789    315    171     19       C  
ATOM    887  O   ARG A 104      37.375  44.612  48.728  1.00 15.61           O  
ANISOU  887  O   ARG A 104     1334   2284   2314    223    203    317       O  
ATOM    888  CB  ARG A 104      36.400  41.657  50.053  1.00 13.62           C  
ANISOU  888  CB  ARG A 104     1485   1742   1948    394    245   -220       C  
ATOM    889  CG  ARG A 104      37.077  41.257  48.728  1.00 16.06           C  
ANISOU  889  CG  ARG A 104     1914   2107   2081    240    398   -463       C  
ATOM    890  CD  ARG A 104      36.206  40.277  47.948  1.00 17.12           C  
ANISOU  890  CD  ARG A 104     2181   2172   2152    420    -32   -480       C  
ATOM    891  NE  ARG A 104      35.095  40.992  47.335  1.00 17.34           N  
ANISOU  891  NE  ARG A 104     2012   2394   2181    373    218   -103       N  
ATOM    892  CZ  ARG A 104      35.083  41.756  46.259  1.00 17.81           C  
ANISOU  892  CZ  ARG A 104     1950   2635   2181    319    283    -15       C  
ATOM    893  NH1 ARG A 104      36.173  41.982  45.530  1.00 21.30           N  
ANISOU  893  NH1 ARG A 104     2013   3377   2703    -58    353    235       N  
ATOM    894  NH2 ARG A 104      33.933  42.318  45.891  1.00 18.49           N  
ANISOU  894  NH2 ARG A 104     2075   2996   1954    358     42    -48       N  
ATOM    895  N   LEU A 105      35.280  44.511  49.515  1.00 12.88           N  
ANISOU  895  N   LEU A 105     1385   1855   1655    263    166    -78       N  
ATOM    896  CA  LEU A 105      34.815  45.557  48.619  1.00 13.58           C  
ANISOU  896  CA  LEU A 105     1434   1962   1763    268    -68    -78       C  
ATOM    897  C   LEU A 105      35.389  46.909  48.964  1.00 13.17           C  
ANISOU  897  C   LEU A 105     1317   1802   1885    453    138   -109       C  
ATOM    898  O   LEU A 105      35.758  47.720  48.103  1.00 15.48           O  
ANISOU  898  O   LEU A 105     2198   1771   1913    346    416   -195       O  
ATOM    899  CB  LEU A 105      33.277  45.556  48.712  1.00 14.29           C  
ANISOU  899  CB  LEU A 105     1439   2102   1888    275     31     21       C  
ATOM    900  CG  LEU A 105      32.523  46.369  47.678  1.00 14.46           C  
ANISOU  900  CG  LEU A 105     1325   2416   1752    345    126     55       C  
ATOM    901  CD1 LEU A 105      32.743  45.878  46.248  1.00 15.18           C  
ANISOU  901  CD1 LEU A 105     1776   2283   1710    -18    441    188       C  
ATOM    902  CD2 LEU A 105      31.051  46.330  48.086  1.00 15.22           C  
ANISOU  902  CD2 LEU A 105     1314   2380   2091    397    197   -340       C  
ATOM    903  N   GLY A 106      35.495  47.188  50.275  1.00 13.84           N  
ANISOU  903  N   GLY A 106     1622   1741   1896    254    119   -129       N  
ATOM    904  CA  GLY A 106      36.088  48.426  50.748  1.00 13.06           C  
ANISOU  904  CA  GLY A 106     1630   1541   1793    254    526    -68       C  
ATOM    905  C   GLY A 106      37.549  48.524  50.311  1.00 13.86           C  
ANISOU  905  C   GLY A 106     1665   1715   1888    202    552     84       C  
ATOM    906  O   GLY A 106      38.007  49.618  49.959  1.00 13.70           O  
ANISOU  906  O   GLY A 106     1925   1864   1417    -10    464     96       O  
ATOM    907  N   LYS A 107      38.272  47.412  50.335  1.00 14.03           N  
ANISOU  907  N   LYS A 107     1433   1977   1920    327    274    236       N  
ATOM    908  CA  LYS A 107      39.673  47.401  49.892  1.00 13.37           C  
ANISOU  908  CA  LYS A 107     1322   2006   1752    224     28    410       C  
ATOM    909  C   LYS A 107      39.757  47.807  48.421  1.00 13.47           C  
ANISOU  909  C   LYS A 107     1705   1845   1567    -56    143      2       C  
ATOM    910  O   LYS A 107      40.633  48.594  48.069  1.00 12.46           O  
ANISOU  910  O   LYS A 107     1633   1689   1412     16    144   -101       O  
ATOM    911  CB  LYS A 107      40.360  46.054  50.163  1.00 14.89           C  
ANISOU  911  CB  LYS A 107     1424   1928   2305    300    361    331       C  
ATOM    912  CG  LYS A 107      41.814  46.089  49.671  1.00 15.78           C  
ANISOU  912  CG  LYS A 107     1506   1902   2589    250    531    340       C  
ATOM    913  CD  LYS A 107      42.338  44.688  49.404  1.00 18.39           C  
ANISOU  913  CD  LYS A 107     2051   2101   2835    349   1011    -14       C  
ATOM    914  CE  LYS A 107      43.711  44.686  48.781  1.00 20.50           C  
ANISOU  914  CE  LYS A 107     2025   2555   3209    467   1070     47       C  
ATOM    915  NZ  LYS A 107      44.607  43.549  49.134  1.00 25.00           N  
ANISOU  915  NZ  LYS A 107     2195   2975   4329    798    546   -178       N  
ATOM    916  N  AGLU A 108      38.873  47.301  47.561  0.57 12.65           N  
ANISOU  916  N  AGLU A 108     1479   1698   1630     71    228    -83       N  
ATOM    917  N  BGLU A 108      38.847  47.306  47.595  0.43 13.03           N  
ANISOU  917  N  BGLU A 108     1614   1723   1616    -32    201    -63       N  
ATOM    918  CA AGLU A 108      38.979  47.661  46.144  0.57 12.65           C  
ANISOU  918  CA AGLU A 108     1387   1807   1611    196    131    -77       C  
ATOM    919  CA BGLU A 108      38.792  47.598  46.174  0.43 12.72           C  
ANISOU  919  CA BGLU A 108     1437   1787   1610    160    159   -105       C  
ATOM    920  C  AGLU A 108      38.799  49.167  45.993  0.57 12.50           C  
ANISOU  920  C  AGLU A 108     1311   1808   1628    158    310    -19       C  
ATOM    921  C  BGLU A 108      38.682  49.094  45.906  0.43 12.40           C  
ANISOU  921  C  BGLU A 108     1339   1808   1564    122    312    -56       C  
ATOM    922  O  AGLU A 108      39.566  49.846  45.302  0.57 15.78           O  
ANISOU  922  O  AGLU A 108     2017   2023   1956   -219    709   -143       O  
ATOM    923  O  BGLU A 108      39.371  49.666  45.060  0.43 14.36           O  
ANISOU  923  O  BGLU A 108     1649   2109   1697   -165    383    -24       O  
ATOM    924  CB AGLU A 108      37.950  46.914  45.292  0.57 13.84           C  
ANISOU  924  CB AGLU A 108     1549   2105   1606    -58    324   -285       C  
ATOM    925  CB BGLU A 108      37.577  46.910  45.521  0.43 14.49           C  
ANISOU  925  CB BGLU A 108     1768   2077   1662   -188    167   -160       C  
ATOM    926  CG AGLU A 108      38.166  45.405  45.292  0.57 13.41           C  
ANISOU  926  CG AGLU A 108     1470   2114   1510    -45    499   -388       C  
ATOM    927  CG BGLU A 108      37.898  46.386  44.141  0.43 15.17           C  
ANISOU  927  CG BGLU A 108     1795   2222   1748    -16    112   -295       C  
ATOM    928  CD AGLU A 108      37.200  44.736  44.330  0.57 16.63           C  
ANISOU  928  CD AGLU A 108     2086   2284   1949   -140     30   -458       C  
ATOM    929  CD BGLU A 108      36.711  45.842  43.380  0.43 16.92           C  
ANISOU  929  CD BGLU A 108     2090   2350   1990   -192     -2   -451       C  
ATOM    930  OE1AGLU A 108      36.237  45.450  43.973  0.57 18.09           O  
ANISOU  930  OE1AGLU A 108     2331   2348   2195   -129   -375   -455       O  
ATOM    931  OE1BGLU A 108      36.058  44.896  43.878  0.43 18.78           O  
ANISOU  931  OE1BGLU A 108     2426   2536   2171   -462   -206   -319       O  
ATOM    932  OE2AGLU A 108      37.386  43.560  43.948  0.57 17.63           O  
ANISOU  932  OE2AGLU A 108     2813   2504   1381    161   -127   -627       O  
ATOM    933  OE2BGLU A 108      36.467  46.381  42.270  0.43 14.03           O  
ANISOU  933  OE2BGLU A 108     1401   2082   1849    123    206   -684       O  
ATOM    934  N   ALA A 109      37.768  49.718  46.648  1.00 12.49           N  
ANISOU  934  N   ALA A 109     1306   1902   1536    186    133   -270       N  
ATOM    935  CA  ALA A 109      37.580  51.168  46.511  1.00 11.77           C  
ANISOU  935  CA  ALA A 109     1045   1965   1462    265    114    -10       C  
ATOM    936  C   ALA A 109      38.795  51.914  47.064  1.00 11.49           C  
ANISOU  936  C   ALA A 109     1164   1850   1351    116    171    140       C  
ATOM    937  O   ALA A 109      39.312  52.880  46.480  1.00 13.90           O  
ANISOU  937  O   ALA A 109     1790   1678   1814     47     22    317       O  
ATOM    938  CB  ALA A 109      36.312  51.562  47.257  1.00 11.89           C  
ANISOU  938  CB  ALA A 109     1206   1779   1533    -11    296   -354       C  
ATOM    939  N   ALA A 110      39.273  51.476  48.242  1.00 11.97           N  
ANISOU  939  N   ALA A 110     1146   1944   1459    145     62    192       N  
ATOM    940  CA  ALA A 110      40.403  52.151  48.901  1.00 12.87           C  
ANISOU  940  CA  ALA A 110     1443   2137   1312     22    119   -141       C  
ATOM    941  C   ALA A 110      41.668  52.144  48.048  1.00 12.61           C  
ANISOU  941  C   ALA A 110     1254   1772   1767      0    156      3       C  
ATOM    942  O   ALA A 110      42.402  53.134  47.929  1.00 14.23           O  
ANISOU  942  O   ALA A 110     1697   1953   1755   -295    -64    168       O  
ATOM    943  CB  ALA A 110      40.704  51.524  50.262  1.00 14.45           C  
ANISOU  943  CB  ALA A 110     1807   2312   1369   -106    -87    -85       C  
ATOM    944  N   VAL A 111      41.988  51.005  47.402  1.00 13.17           N  
ANISOU  944  N   VAL A 111     1287   1955   1762     34    206   -131       N  
ATOM    945  CA  VAL A 111      43.185  50.967  46.557  1.00 14.04           C  
ANISOU  945  CA  VAL A 111     1361   1941   2031    312    347    245       C  
ATOM    946  C   VAL A 111      43.118  51.986  45.430  1.00 14.43           C  
ANISOU  946  C   VAL A 111     1569   2009   1906    127    164    211       C  
ATOM    947  O   VAL A 111      44.090  52.646  45.070  1.00 15.69           O  
ANISOU  947  O   VAL A 111     1855   2311   1793   -193    115    237       O  
ATOM    948  CB  VAL A 111      43.311  49.531  45.992  1.00 16.45           C  
ANISOU  948  CB  VAL A 111     1879   1994   2378    456    757    193       C  
ATOM    949  CG1 VAL A 111      44.164  49.500  44.750  1.00 22.72           C  
ANISOU  949  CG1 VAL A 111     2966   2920   2745    354   1376   -173       C  
ATOM    950  CG2 VAL A 111      43.821  48.625  47.127  1.00 18.42           C  
ANISOU  950  CG2 VAL A 111     2204   1985   2810    656    330    167       C  
ATOM    951  N   LYS A 112      41.901  52.129  44.870  1.00 14.31           N  
ANISOU  951  N   LYS A 112     1655   1974   1807    292    107    -53       N  
ATOM    952  CA  LYS A 112      41.718  53.100  43.797  1.00 14.33           C  
ANISOU  952  CA  LYS A 112     1595   1960   1888    339    100    -36       C  
ATOM    953  C   LYS A 112      41.924  54.529  44.296  1.00 15.39           C  
ANISOU  953  C   LYS A 112     2009   1980   1858    201    209    -35       C  
ATOM    954  O   LYS A 112      42.580  55.345  43.634  1.00 16.59           O  
ANISOU  954  O   LYS A 112     2169   2118   2015     29    397   -142       O  
ATOM    955  CB  LYS A 112      40.323  52.980  43.162  1.00 15.65           C  
ANISOU  955  CB  LYS A 112     1616   2452   1879    228     62     51       C  
ATOM    956  CG  LYS A 112      40.147  51.777  42.258  1.00 19.24           C  
ANISOU  956  CG  LYS A 112     1973   3118   2220   -290    209   -439       C  
ATOM    957  CD  LYS A 112      38.761  51.875  41.608  1.00 22.20           C  
ANISOU  957  CD  LYS A 112     1960   4033   2443   -426    132   -568       C  
ATOM    958  CE  LYS A 112      38.250  50.530  41.137  1.00 26.45           C  
ANISOU  958  CE  LYS A 112     2664   4550   2836  -1007    -46   -806       C  
ATOM    959  NZ  LYS A 112      36.851  50.634  40.655  1.00 26.46           N  
ANISOU  959  NZ  LYS A 112     2358   5221   2474   -932    392  -1324       N  
ATOM    960  N   ALA A 113      41.360  54.834  45.474  1.00 14.23           N  
ANISOU  960  N   ALA A 113     1794   2005   1606     66    -74    -27       N  
ATOM    961  CA  ALA A 113      41.530  56.172  46.054  1.00 13.53           C  
ANISOU  961  CA  ALA A 113     1536   1969   1637    157   -126      9       C  
ATOM    962  C   ALA A 113      43.009  56.447  46.348  1.00 13.56           C  
ANISOU  962  C   ALA A 113     1490   1885   1780    137     21     66       C  
ATOM    963  O   ALA A 113      43.507  57.540  46.061  1.00 14.21           O  
ANISOU  963  O   ALA A 113     1736   1999   1665     -4    139     72       O  
ATOM    964  CB  ALA A 113      40.699  56.366  47.321  1.00 13.86           C  
ANISOU  964  CB  ALA A 113     1487   1894   1884     63     48    -83       C  
ATOM    965  N   ILE A 114      43.697  55.466  46.952  1.00 13.86           N  
ANISOU  965  N   ILE A 114     1493   1970   1804    210   -107     -1       N  
ATOM    966  CA  ILE A 114      45.111  55.667  47.279  1.00 14.58           C  
ANISOU  966  CA  ILE A 114     1451   2202   1887     87     38    286       C  
ATOM    967  C   ILE A 114      45.921  55.842  45.997  1.00 16.60           C  
ANISOU  967  C   ILE A 114     1947   2328   2033   -150    302    202       C  
ATOM    968  O   ILE A 114      46.837  56.688  45.919  1.00 17.31           O  
ANISOU  968  O   ILE A 114     1714   2598   2268   -158    291    206       O  
ATOM    969  CB  ILE A 114      45.607  54.487  48.154  1.00 14.18           C  
ANISOU  969  CB  ILE A 114     1101   2187   2098    333    298    271       C  
ATOM    970  CG1 ILE A 114      44.880  54.473  49.519  1.00 14.30           C  
ANISOU  970  CG1 ILE A 114     1608   1835   1990    312    346    263       C  
ATOM    971  CG2 ILE A 114      47.097  54.497  48.342  1.00 14.82           C  
ANISOU  971  CG2 ILE A 114     1151   2038   2443    263     56   -363       C  
ATOM    972  CD1 ILE A 114      45.075  53.176  50.284  1.00 16.96           C  
ANISOU  972  CD1 ILE A 114     2444   1768   2234     27     45    331       C  
ATOM    973  N   LYS A 115      45.597  55.073  44.959  1.00 17.79           N  
ANISOU  973  N   LYS A 115     2104   2569   2088   -178    412     20       N  
ATOM    974  CA  LYS A 115      46.323  55.225  43.686  1.00 17.01           C  
ANISOU  974  CA  LYS A 115     1723   2571   2168    257    404     70       C  
ATOM    975  C   LYS A 115      46.152  56.631  43.138  1.00 17.03           C  
ANISOU  975  C   LYS A 115     1760   2649   2062    112    229    179       C  
ATOM    976  O   LYS A 115      47.140  57.251  42.704  1.00 18.06           O  
ANISOU  976  O   LYS A 115     1748   2837   2278   -125    -11    214       O  
ATOM    977  CB  LYS A 115      45.870  54.182  42.681  1.00 19.51           C  
ANISOU  977  CB  LYS A 115     2563   2718   2132     65    487    -26       C  
ATOM    978  CG  LYS A 115      46.548  54.308  41.319  1.00 25.42           C  
ANISOU  978  CG  LYS A 115     3849   3320   2490   -525   1178   -408       C  
ATOM    979  CD  LYS A 115      46.179  53.117  40.452  1.00 31.12           C  
ANISOU  979  CD  LYS A 115     5209   3988   2625   -925   1157   -841       C  
ATOM    980  CE  LYS A 115      45.600  53.566  39.113  1.00 39.19           C  
ANISOU  980  CE  LYS A 115     6848   4641   3402  -1724   -207   -540       C  
ATOM    981  NZ  LYS A 115      44.119  53.328  39.082  1.00 49.35           N  
ANISOU  981  NZ  LYS A 115     6820   6360   5572  -1533  -1118   -550       N  
ATOM    982  N   GLU A 116      44.933  57.159  43.151  1.00 16.14           N  
ANISOU  982  N   GLU A 116     1776   2456   1900     79     93    136       N  
ATOM    983  CA  GLU A 116      44.672  58.527  42.703  1.00 15.54           C  
ANISOU  983  CA  GLU A 116     1690   2574   1639    -83   -161    285       C  
ATOM    984  C   GLU A 116      45.401  59.575  43.541  1.00 16.55           C  
ANISOU  984  C   GLU A 116     2134   2517   1640   -324   -214    432       C  
ATOM    985  O   GLU A 116      45.992  60.538  43.026  1.00 17.64           O  
ANISOU  985  O   GLU A 116     2408   2346   1948   -209     -1    450       O  
ATOM    986  CB  GLU A 116      43.159  58.850  42.733  1.00 15.75           C  
ANISOU  986  CB  GLU A 116     1718   2399   1866    -25    101    361       C  
ATOM    987  CG  GLU A 116      42.949  60.317  42.343  1.00 17.11           C  
ANISOU  987  CG  GLU A 116     1731   2464   2307   -189   -128    610       C  
ATOM    988  CD  GLU A 116      41.532  60.806  42.528  1.00 16.97           C  
ANISOU  988  CD  GLU A 116     1723   2456   2271    -59   -528    513       C  
ATOM    989  OE1 GLU A 116      40.630  60.020  42.865  1.00 17.01           O  
ANISOU  989  OE1 GLU A 116     1599   2169   2697    112   -159    105       O  
ATOM    990  OE2 GLU A 116      41.298  62.024  42.323  1.00 21.66           O  
ANISOU  990  OE2 GLU A 116     2204   2424   3602      8     92    612       O  
ATOM    991  N   TRP A 117      45.376  59.406  44.846  1.00 14.40           N  
ANISOU  991  N   TRP A 117     1872   2021   1578    266     28    157       N  
ATOM    992  CA  TRP A 117      46.096  60.306  45.746  1.00 14.84           C  
ANISOU  992  CA  TRP A 117     2070   2086   1484    -45    543    -43       C  
ATOM    993  C   TRP A 117      47.574  60.340  45.440  1.00 17.12           C  
ANISOU  993  C   TRP A 117     2006   2799   1699   -208    386   -168       C  
ATOM    994  O   TRP A 117      48.165  61.423  45.379  1.00 19.01           O  
ANISOU  994  O   TRP A 117     1958   2956   2308   -290     38    409       O  
ATOM    995  CB  TRP A 117      45.859  59.858  47.202  1.00 15.84           C  
ANISOU  995  CB  TRP A 117     2672   1897   1451    -84    566   -105       C  
ATOM    996  CG  TRP A 117      46.475  60.664  48.273  1.00 14.53           C  
ANISOU  996  CG  TRP A 117     2042   1989   1490    -82    618    -91       C  
ATOM    997  CD1 TRP A 117      46.600  62.024  48.423  1.00 13.99           C  
ANISOU  997  CD1 TRP A 117     1435   1977   1903    259    278   -275       C  
ATOM    998  CD2 TRP A 117      47.094  60.088  49.449  1.00 14.25           C  
ANISOU  998  CD2 TRP A 117     1549   2025   1840    166    493   -133       C  
ATOM    999  NE1 TRP A 117      47.255  62.315  49.616  1.00 15.11           N  
ANISOU  999  NE1 TRP A 117     1888   2044   1811     57    212   -133       N  
ATOM   1000  CE2 TRP A 117      47.565  61.139  50.248  1.00 15.34           C  
ANISOU 1000  CE2 TRP A 117     1797   2094   1936    -35    231    -16       C  
ATOM   1001  CE3 TRP A 117      47.281  58.768  49.875  1.00 16.63           C  
ANISOU 1001  CE3 TRP A 117     2207   2071   2040    -96    264     65       C  
ATOM   1002  CZ2 TRP A 117      48.222  60.911  51.467  1.00 15.38           C  
ANISOU 1002  CZ2 TRP A 117     1583   2111   2149    -74    128     76       C  
ATOM   1003  CZ3 TRP A 117      47.931  58.561  51.077  1.00 16.49           C  
ANISOU 1003  CZ3 TRP A 117     2162   2095   2009   -149    333    147       C  
ATOM   1004  CH2 TRP A 117      48.399  59.618  51.869  1.00 15.04           C  
ANISOU 1004  CH2 TRP A 117     1527   2129   2059    -37    365    101       C  
ATOM   1005  N   GLY A 118      48.144  59.153  45.244  1.00 17.40           N  
ANISOU 1005  N   GLY A 118     1697   3035   1880   -101    400   -321       N  
ATOM   1006  CA  GLY A 118      49.507  59.033  44.721  1.00 19.02           C  
ANISOU 1006  CA  GLY A 118     1743   3438   2047   -206    533   -139       C  
ATOM   1007  C   GLY A 118      50.584  59.067  45.785  1.00 18.53           C  
ANISOU 1007  C   GLY A 118     1606   3238   2197   -249    549   -243       C  
ATOM   1008  O   GLY A 118      51.774  58.942  45.444  1.00 21.07           O  
ANISOU 1008  O   GLY A 118     1689   3700   2615    127    611   -168       O  
ATOM   1009  N  AGLN A 119      50.222  59.230  47.054  0.54 17.67           N  
ANISOU 1009  N  AGLN A 119     1789   2831   2094    -61    430    -95       N  
ATOM   1010  N  BGLN A 119      50.213  59.227  47.051  0.46 17.58           N  
ANISOU 1010  N  BGLN A 119     1802   2784   2093    -57    429    -95       N  
ATOM   1011  CA AGLN A 119      51.231  59.320  48.106  0.54 17.45           C  
ANISOU 1011  CA AGLN A 119     1692   2696   2241     38    397   -162       C  
ATOM   1012  CA BGLN A 119      51.165  59.315  48.147  0.46 17.54           C  
ANISOU 1012  CA BGLN A 119     1752   2666   2247    -13    380   -155       C  
ATOM   1013  C  AGLN A 119      51.368  57.985  48.823  0.54 17.77           C  
ANISOU 1013  C  AGLN A 119     1649   2710   2395    118    380   -114       C  
ATOM   1014  C  BGLN A 119      51.376  57.958  48.806  0.46 17.77           C  
ANISOU 1014  C  BGLN A 119     1677   2695   2378     79    369   -114       C  
ATOM   1015  O  AGLN A 119      50.488  57.145  48.634  0.54 17.75           O  
ANISOU 1015  O  AGLN A 119     1517   2568   2661    266    187     -1       O  
ATOM   1016  O  BGLN A 119      50.562  57.066  48.564  0.46 19.48           O  
ANISOU 1016  O  BGLN A 119     2146   2717   2540    -82   -259    187       O  
ATOM   1017  CB AGLN A 119      50.837  60.435  49.081  0.54 17.88           C  
ANISOU 1017  CB AGLN A 119     1821   2650   2324    -35    391   -219       C  
ATOM   1018  CB BGLN A 119      50.655  60.307  49.195  0.46 17.88           C  
ANISOU 1018  CB BGLN A 119     1975   2576   2242    -78    392   -169       C  
ATOM   1019  CG AGLN A 119      50.395  61.697  48.346  0.54 19.01           C  
ANISOU 1019  CG AGLN A 119     2187   2488   2546   -183    448   -157       C  
ATOM   1020  CG BGLN A 119      50.765  61.760  48.770  0.46 19.02           C  
ANISOU 1020  CG BGLN A 119     2033   2567   2627   -138    221   -127       C  
ATOM   1021  CD AGLN A 119      51.410  62.111  47.297  0.54 20.08           C  
ANISOU 1021  CD AGLN A 119     2216   2617   2798   -350    531   -132       C  
ATOM   1022  CD BGLN A 119      52.205  62.187  48.558  0.46 18.73           C  
ANISOU 1022  CD BGLN A 119     1993   2465   2658     13    315     36       C  
ATOM   1023  OE1AGLN A 119      52.594  62.259  47.619  0.54 20.85           O  
ANISOU 1023  OE1AGLN A 119     2182   2720   3019   -215    467     -4       O  
ATOM   1024  OE1BGLN A 119      52.615  62.590  47.468  0.46 23.20           O  
ANISOU 1024  OE1BGLN A 119     3081   2833   2900   -750    600     67       O  
ATOM   1025  NE2AGLN A 119      50.957  62.303  46.061  0.54 21.99           N  
ANISOU 1025  NE2AGLN A 119     2468   3162   2725  -1582    445    -34       N  
ATOM   1026  NE2BGLN A 119      52.984  62.105  49.626  0.46 20.85           N  
ANISOU 1026  NE2BGLN A 119     2080   2380   3461    206   -209    425       N  
ATOM   1027  N   PRO A 120      52.428  57.764  49.598  1.00 18.19           N  
ANISOU 1027  N   PRO A 120     1889   2777   2244   -186    216    -29       N  
ATOM   1028  CA  PRO A 120      52.619  56.492  50.304  1.00 18.72           C  
ANISOU 1028  CA  PRO A 120     1879   2921   2315   -306     69    103       C  
ATOM   1029  C   PRO A 120      51.504  56.179  51.298  1.00 18.12           C  
ANISOU 1029  C   PRO A 120     1948   2683   2254   -192    134      5       C  
ATOM   1030  O   PRO A 120      51.071  57.011  52.089  1.00 19.54           O  
ANISOU 1030  O   PRO A 120     2468   2608   2351   -466    298   -128       O  
ATOM   1031  CB  PRO A 120      53.942  56.659  51.076  1.00 21.23           C  
ANISOU 1031  CB  PRO A 120     1931   3073   3064   -334   -196    199       C  
ATOM   1032  CG  PRO A 120      54.626  57.800  50.386  1.00 22.10           C  
ANISOU 1032  CG  PRO A 120     2141   3052   3206   -532   -260    119       C  
ATOM   1033  CD  PRO A 120      53.538  58.701  49.836  1.00 20.88           C  
ANISOU 1033  CD  PRO A 120     2364   2806   2763   -400   -131    -51       C  
ATOM   1034  N   LYS A 121      51.046  54.920  51.241  1.00 17.17           N  
ANISOU 1034  N   LYS A 121     1840   2532   2152     38    337    -16       N  
ATOM   1035  CA  LYS A 121      49.960  54.580  52.165  1.00 16.61           C  
ANISOU 1035  CA  LYS A 121     1777   2288   2245     74    411   -261       C  
ATOM   1036  C   LYS A 121      50.422  54.651  53.614  1.00 16.16           C  
ANISOU 1036  C   LYS A 121     1312   2602   2226    283    509   -208       C  
ATOM   1037  O   LYS A 121      49.558  54.700  54.491  1.00 16.05           O  
ANISOU 1037  O   LYS A 121     1545   2226   2328    130    691   -186       O  
ATOM   1038  CB  LYS A 121      49.429  53.204  51.782  1.00 18.88           C  
ANISOU 1038  CB  LYS A 121     1988   2336   2848    -39    396   -356       C  
ATOM   1039  CG  LYS A 121      50.432  52.064  51.904  1.00 20.50           C  
ANISOU 1039  CG  LYS A 121     2722   2162   2903     53   -519    -93       C  
ATOM   1040  CD  LYS A 121      49.756  50.750  51.499  1.00 23.84           C  
ANISOU 1040  CD  LYS A 121     3945   2233   2880   -135   -752   -294       C  
ATOM   1041  CE  LYS A 121      50.755  49.617  51.342  1.00 26.28           C  
ANISOU 1041  CE  LYS A 121     4407   2360   3217     39   -334   -611       C  
ATOM   1042  NZ  LYS A 121      51.554  49.362  52.582  1.00 28.65           N  
ANISOU 1042  NZ  LYS A 121     3868   3050   3966    523   -552   -248       N  
ATOM   1043  N   SER A 122      51.725  54.678  53.883  1.00 17.31           N  
ANISOU 1043  N   SER A 122     1347   2529   2703     10    400   -147       N  
ATOM   1044  CA  SER A 122      52.255  54.793  55.243  1.00 17.57           C  
ANISOU 1044  CA  SER A 122     1551   2236   2890    233     53    150       C  
ATOM   1045  C   SER A 122      52.014  56.177  55.845  1.00 16.35           C  
ANISOU 1045  C   SER A 122     1379   2364   2470    155    188     88       C  
ATOM   1046  O   SER A 122      52.214  56.395  57.043  1.00 18.18           O  
ANISOU 1046  O   SER A 122     1580   2822   2504    -97     28     98       O  
ATOM   1047  CB  SER A 122      53.769  54.510  55.243  1.00 19.11           C  
ANISOU 1047  CB  SER A 122     1626   2315   3321    440     74    341       C  
ATOM   1048  OG  SER A 122      54.456  55.538  54.518  1.00 20.88           O  
ANISOU 1048  OG  SER A 122     1724   2870   3341    203    423    298       O  
ATOM   1049  N   LYS A 123      51.598  57.112  54.982  1.00 15.63           N  
ANISOU 1049  N   LYS A 123     1382   2202   2353    219    491     50       N  
ATOM   1050  CA  LYS A 123      51.246  58.459  55.420  1.00 16.06           C  
ANISOU 1050  CA  LYS A 123     1291   2192   2620     66    569    -67       C  
ATOM   1051  C   LYS A 123      49.775  58.573  55.828  1.00 14.02           C  
ANISOU 1051  C   LYS A 123     1254   2086   1986     31    370   -118       C  
ATOM   1052  O   LYS A 123      49.301  59.620  56.264  1.00 13.83           O  
ANISOU 1052  O   LYS A 123     1403   2101   1752    179    424     68       O  
ATOM   1053  CB  LYS A 123      51.556  59.461  54.305  1.00 18.42           C  
ANISOU 1053  CB  LYS A 123     1804   2174   3023    511   1328     66       C  
ATOM   1054  CG  LYS A 123      53.034  59.609  53.957  1.00 23.88           C  
ANISOU 1054  CG  LYS A 123     1944   3231   3898   -151   1477     37       C  
ATOM   1055  CD  LYS A 123      53.616  60.879  54.523  1.00 31.77           C  
ANISOU 1055  CD  LYS A 123     3260   4155   4655  -1174   1156   -273       C  
ATOM   1056  CE  LYS A 123      54.456  61.640  53.530  1.00 31.39           C  
ANISOU 1056  CE  LYS A 123     3453   3632   4841  -1108    929     49       C  
ATOM   1057  NZ  LYS A 123      54.337  63.106  53.697  1.00 26.35           N  
ANISOU 1057  NZ  LYS A 123     2681   3759   3572   -558   -141   -151       N  
ATOM   1058  N   ILE A 124      49.024  57.485  55.701  1.00 13.04           N  
ANISOU 1058  N   ILE A 124     1358   2125   1474    -75    227    211       N  
ATOM   1059  CA  ILE A 124      47.645  57.535  56.212  1.00 12.79           C  
ANISOU 1059  CA  ILE A 124     1413   1976   1469    -95    301   -117       C  
ATOM   1060  C   ILE A 124      47.696  57.369  57.729  1.00 11.71           C  
ANISOU 1060  C   ILE A 124     1286   1670   1494    110    264    -97       C  
ATOM   1061  O   ILE A 124      48.198  56.341  58.234  1.00 13.72           O  
ANISOU 1061  O   ILE A 124     1603   1887   1721    444    180   -123       O  
ATOM   1062  CB  ILE A 124      46.794  56.461  55.528  1.00 13.52           C  
ANISOU 1062  CB  ILE A 124     1651   2194   1291   -462    613   -140       C  
ATOM   1063  CG1 ILE A 124      46.679  56.668  53.997  1.00 11.68           C  
ANISOU 1063  CG1 ILE A 124     1190   1884   1364     87    394   -127       C  
ATOM   1064  CG2 ILE A 124      45.411  56.333  56.157  1.00 13.63           C  
ANISOU 1064  CG2 ILE A 124     1254   2667   1257   -125    207    237       C  
ATOM   1065  CD1 ILE A 124      46.097  55.468  53.281  1.00 13.83           C  
ANISOU 1065  CD1 ILE A 124     1881   1956   1420     44    689   -458       C  
ATOM   1066  N   THR A 125      47.184  58.382  58.425  1.00 11.43           N  
ANISOU 1066  N   THR A 125     1166   1617   1557     27    274   -128       N  
ATOM   1067  CA  THR A 125      47.267  58.434  59.880  1.00 11.77           C  
ANISOU 1067  CA  THR A 125     1144   1760   1568     11    249   -203       C  
ATOM   1068  C   THR A 125      45.996  58.011  60.623  1.00 11.55           C  
ANISOU 1068  C   THR A 125     1142   1753   1495    -91    176   -124       C  
ATOM   1069  O   THR A 125      46.083  57.643  61.812  1.00 12.12           O  
ANISOU 1069  O   THR A 125     1498   1660   1447   -113    180   -214       O  
ATOM   1070  CB  THR A 125      47.577  59.875  60.372  1.00 12.03           C  
ANISOU 1070  CB  THR A 125     1050   1823   1699   -141    -33   -169       C  
ATOM   1071  OG1 THR A 125      46.628  60.767  59.769  1.00 12.22           O  
ANISOU 1071  OG1 THR A 125     1324   1756   1562     36    133   -166       O  
ATOM   1072  CG2 THR A 125      48.963  60.302  59.923  1.00 12.73           C  
ANISOU 1072  CG2 THR A 125     1317   1541   1978     47    401    445       C  
ATOM   1073  N   HIS A 126      44.869  58.090  59.929  1.00 11.67           N  
ANISOU 1073  N   HIS A 126     1120   1554   1760     80    145   -101       N  
ATOM   1074  CA  HIS A 126      43.550  57.824  60.469  1.00 10.53           C  
ANISOU 1074  CA  HIS A 126     1117   1346   1538     50     54    -52       C  
ATOM   1075  C   HIS A 126      42.744  57.005  59.452  1.00 10.80           C  
ANISOU 1075  C   HIS A 126     1297   1343   1463      4     38    -14       C  
ATOM   1076  O   HIS A 126      42.902  57.241  58.238  1.00 12.27           O  
ANISOU 1076  O   HIS A 126     1429   1775   1459   -147    150    -60       O  
ATOM   1077  CB  HIS A 126      42.767  59.112  60.740  1.00 10.82           C  
ANISOU 1077  CB  HIS A 126     1195   1392   1524    100    136    -72       C  
ATOM   1078  CG  HIS A 126      43.370  60.026  61.766  1.00 12.67           C  
ANISOU 1078  CG  HIS A 126     1806   1305   1702   -142    102    -80       C  
ATOM   1079  ND1 HIS A 126      44.525  60.762  61.562  1.00 13.40           N  
ANISOU 1079  ND1 HIS A 126     1800   1644   1647   -277    -85     11       N  
ATOM   1080  CD2 HIS A 126      42.970  60.326  63.036  1.00 11.83           C  
ANISOU 1080  CD2 HIS A 126     1466   1296   1735     80    -57   -209       C  
ATOM   1081  CE1 HIS A 126      44.803  61.469  62.651  1.00 13.28           C  
ANISOU 1081  CE1 HIS A 126     1714   1642   1690   -185      4    -90       C  
ATOM   1082  NE2 HIS A 126      43.874  61.221  63.574  1.00 12.60           N  
ANISOU 1082  NE2 HIS A 126     1386   1603   1798    -73    -77   -164       N  
ATOM   1083  N   LEU A 127      41.903  56.128  59.973  1.00  9.83           N  
ANISOU 1083  N   LEU A 127     1231   1033   1473    156   -198    151       N  
ATOM   1084  CA  LEU A 127      41.044  55.313  59.119  1.00 10.26           C  
ANISOU 1084  CA  LEU A 127     1052   1401   1443    119     -1    -93       C  
ATOM   1085  C   LEU A 127      39.636  55.325  59.698  1.00 11.16           C  
ANISOU 1085  C   LEU A 127     1107   1631   1501    129     53    161       C  
ATOM   1086  O   LEU A 127      39.487  54.949  60.857  1.00 10.94           O  
ANISOU 1086  O   LEU A 127     1188   1483   1486    153     43    116       O  
ATOM   1087  CB  LEU A 127      41.562  53.870  59.059  1.00 11.29           C  
ANISOU 1087  CB  LEU A 127     1500   1364   1425     89    133   -297       C  
ATOM   1088  CG  LEU A 127      40.647  52.847  58.351  1.00 10.69           C  
ANISOU 1088  CG  LEU A 127     1379   1370   1313    160   -106    -65       C  
ATOM   1089  CD1 LEU A 127      40.529  53.188  56.863  1.00 12.58           C  
ANISOU 1089  CD1 LEU A 127     1971   1559   1251   -340    138    -47       C  
ATOM   1090  CD2 LEU A 127      41.170  51.456  58.588  1.00 11.87           C  
ANISOU 1090  CD2 LEU A 127     1178   1270   2063     38     34    -33       C  
ATOM   1091  N   ILE A 128      38.680  55.734  58.880  1.00 10.18           N  
ANISOU 1091  N   ILE A 128     1044   1437   1389    164     92     -4       N  
ATOM   1092  CA  ILE A 128      37.261  55.654  59.215  1.00 10.41           C  
ANISOU 1092  CA  ILE A 128     1070   1521   1366     60     98    -19       C  
ATOM   1093  C   ILE A 128      36.637  54.573  58.348  1.00 10.53           C  
ANISOU 1093  C   ILE A 128     1182   1477   1342     87    -60     71       C  
ATOM   1094  O   ILE A 128      36.758  54.692  57.111  1.00 11.36           O  
ANISOU 1094  O   ILE A 128     1347   1635   1336   -113    -68    105       O  
ATOM   1095  CB  ILE A 128      36.532  56.990  58.981  1.00 10.66           C  
ANISOU 1095  CB  ILE A 128      942   1569   1537    117    167   -119       C  
ATOM   1096  CG1 ILE A 128      37.123  58.174  59.745  1.00 12.73           C  
ANISOU 1096  CG1 ILE A 128     1597   1487   1754   -113    100    -49       C  
ATOM   1097  CG2 ILE A 128      35.042  56.839  59.309  1.00 12.69           C  
ANISOU 1097  CG2 ILE A 128      920   2289   1611    105    134    111       C  
ATOM   1098  CD1 ILE A 128      36.575  59.543  59.311  1.00 13.31           C  
ANISOU 1098  CD1 ILE A 128     1668   1604   1784    140    -25   -202       C  
ATOM   1099  N   VAL A 129      36.023  53.580  58.979  1.00  9.85           N  
ANISOU 1099  N   VAL A 129     1019   1467   1256    121     67    -44       N  
ATOM   1100  CA  VAL A 129      35.288  52.579  58.201  1.00 10.66           C  
ANISOU 1100  CA  VAL A 129     1056   1644   1350     29    132   -163       C  
ATOM   1101  C   VAL A 129      33.829  52.642  58.661  1.00 10.63           C  
ANISOU 1101  C   VAL A 129     1066   1857   1115    -18    112   -176       C  
ATOM   1102  O   VAL A 129      33.563  52.725  59.842  1.00 11.03           O  
ANISOU 1102  O   VAL A 129     1415   1635   1140    -92    229   -182       O  
ATOM   1103  CB  VAL A 129      35.807  51.159  58.369  1.00 10.92           C  
ANISOU 1103  CB  VAL A 129     1236   1558   1354    -37    200   -206       C  
ATOM   1104  CG1 VAL A 129      35.030  50.151  57.512  1.00 11.37           C  
ANISOU 1104  CG1 VAL A 129     1395   1639   1286    -19    -63    -88       C  
ATOM   1105  CG2 VAL A 129      37.292  51.137  57.998  1.00 12.57           C  
ANISOU 1105  CG2 VAL A 129     1126   1991   1659    210      9   -317       C  
ATOM   1106  N   CYS A 130      32.949  52.606  57.664  1.00 10.33           N  
ANISOU 1106  N   CYS A 130     1154   1466   1305    278    -51    -71       N  
ATOM   1107  CA  CYS A 130      31.535  52.770  57.932  1.00 10.60           C  
ANISOU 1107  CA  CYS A 130     1120   1452   1454     81      1     54       C  
ATOM   1108  C   CYS A 130      30.735  51.725  57.189  1.00 10.65           C  
ANISOU 1108  C   CYS A 130     1277   1437   1332     22    147      4       C  
ATOM   1109  O   CYS A 130      30.912  51.557  55.966  1.00 11.64           O  
ANISOU 1109  O   CYS A 130     1520   1552   1352   -159    285     13       O  
ATOM   1110  CB  CYS A 130      31.103  54.172  57.468  1.00 11.98           C  
ANISOU 1110  CB  CYS A 130     1373   1386   1791    384    -37   -232       C  
ATOM   1111  SG  CYS A 130      29.314  54.474  57.622  1.00 13.06           S  
ANISOU 1111  SG  CYS A 130     1358   1710   1893    327     89    143       S  
ATOM   1112  N   THR A 131      29.848  51.059  57.908  1.00 10.15           N  
ANISOU 1112  N   THR A 131     1418   1399   1042    -38    -54    144       N  
ATOM   1113  CA  THR A 131      28.963  50.110  57.247  1.00 10.64           C  
ANISOU 1113  CA  THR A 131     1354   1428   1262    -18    -15     -8       C  
ATOM   1114  C   THR A 131      27.679  49.963  58.057  1.00 11.67           C  
ANISOU 1114  C   THR A 131     1427   1767   1241   -128      7     25       C  
ATOM   1115  O   THR A 131      27.681  50.262  59.266  1.00 15.45           O  
ANISOU 1115  O   THR A 131     1625   2945   1300   -672    148   -185       O  
ATOM   1116  CB  THR A 131      29.613  48.720  57.090  1.00 10.75           C  
ANISOU 1116  CB  THR A 131     1394   1346   1346    -13   -215    175       C  
ATOM   1117  OG1 THR A 131      28.762  47.879  56.276  1.00 10.72           O  
ANISOU 1117  OG1 THR A 131     1102   1471   1499    -10     81   -106       O  
ATOM   1118  CG2 THR A 131      29.796  48.048  58.435  1.00 12.92           C  
ANISOU 1118  CG2 THR A 131     1673   1776   1461   -139   -112    440       C  
ATOM   1119  N   THR A 132      26.630  49.518  57.387  1.00 11.48           N  
ANISOU 1119  N   THR A 132     1284   1585   1493     80     32   -275       N  
ATOM   1120  CA  THR A 132      25.385  49.143  58.022  1.00 12.73           C  
ANISOU 1120  CA  THR A 132     1263   1741   1834    131    184   -414       C  
ATOM   1121  C   THR A 132      25.147  47.641  57.890  1.00 12.92           C  
ANISOU 1121  C   THR A 132     1629   1671   1610     83    378     -6       C  
ATOM   1122  O   THR A 132      24.083  47.167  58.254  1.00 13.96           O  
ANISOU 1122  O   THR A 132     1677   1910   1719    -70    426   -279       O  
ATOM   1123  CB  THR A 132      24.223  49.924  57.372  1.00 13.60           C  
ANISOU 1123  CB  THR A 132     1329   1747   2092    209    337   -134       C  
ATOM   1124  OG1 THR A 132      24.651  51.302  57.339  1.00 16.19           O  
ANISOU 1124  OG1 THR A 132     1996   1832   2323    -28     91     69       O  
ATOM   1125  CG2 THR A 132      22.936  49.855  58.173  1.00 14.99           C  
ANISOU 1125  CG2 THR A 132     1371   2098   2225    334    439   -167       C  
ATOM   1126  N   SER A 133      26.129  46.910  57.357  1.00 12.16           N  
ANISOU 1126  N   SER A 133     1589   1461   1571    106    267     41       N  
ATOM   1127  CA  SER A 133      25.937  45.473  57.143  1.00 13.39           C  
ANISOU 1127  CA  SER A 133     1950   1459   1678    104   -222     42       C  
ATOM   1128  C   SER A 133      26.984  44.650  57.879  1.00 13.62           C  
ANISOU 1128  C   SER A 133     1733   1544   1899    112     -9    193       C  
ATOM   1129  O   SER A 133      28.135  44.517  57.431  1.00 14.63           O  
ANISOU 1129  O   SER A 133     1893   1858   1808    244    106    -12       O  
ATOM   1130  CB  SER A 133      25.974  45.087  55.680  1.00 17.55           C  
ANISOU 1130  CB  SER A 133     3086   1843   1738   -357   -379   -144       C  
ATOM   1131  OG  SER A 133      26.923  45.842  54.993  1.00 21.92           O  
ANISOU 1131  OG  SER A 133     3961   2160   2209   -375   1059   -857       O  
ATOM   1132  N   GLY A 134      26.502  44.071  58.989  1.00 12.75           N  
ANISOU 1132  N   GLY A 134     1666   1546   1632     68   -187     70       N  
ATOM   1133  CA  GLY A 134      27.349  43.206  59.770  1.00 13.61           C  
ANISOU 1133  CA  GLY A 134     1634   1693   1846    -35   -382    154       C  
ATOM   1134  C   GLY A 134      28.125  43.955  60.826  1.00 12.39           C  
ANISOU 1134  C   GLY A 134     1299   1788   1619      0    -31     33       C  
ATOM   1135  O   GLY A 134      28.355  45.165  60.746  1.00 13.28           O  
ANISOU 1135  O   GLY A 134     1659   1755   1630     16    -23   -100       O  
ATOM   1136  N   VAL A 135      28.528  43.182  61.840  1.00 13.12           N  
ANISOU 1136  N   VAL A 135     1392   2049   1544   -205    -51    162       N  
ATOM   1137  CA  VAL A 135      29.443  43.683  62.862  1.00 12.28           C  
ANISOU 1137  CA  VAL A 135     1379   1651   1634    208    -82   -157       C  
ATOM   1138  C   VAL A 135      30.371  42.540  63.257  1.00 13.45           C  
ANISOU 1138  C   VAL A 135     1442   1589   2082    201   -188   -162       C  
ATOM   1139  O   VAL A 135      29.963  41.392  63.136  1.00 14.62           O  
ANISOU 1139  O   VAL A 135     2058   1604   1894     58   -560    -13       O  
ATOM   1140  CB  VAL A 135      28.751  44.188  64.144  1.00 12.99           C  
ANISOU 1140  CB  VAL A 135     1573   1604   1759     57    214    -72       C  
ATOM   1141  CG1 VAL A 135      27.744  45.295  63.813  1.00 14.96           C  
ANISOU 1141  CG1 VAL A 135     1919   1461   2306    238    396   -137       C  
ATOM   1142  CG2 VAL A 135      28.112  43.044  64.906  1.00 16.55           C  
ANISOU 1142  CG2 VAL A 135     2435   2154   1699   -193   -100    493       C  
ATOM   1143  N   ASP A 136      31.556  42.863  63.764  1.00 13.80           N  
ANISOU 1143  N   ASP A 136     1238   1650   2356    293    -22   -247       N  
ATOM   1144  CA  ASP A 136      32.479  41.823  64.221  1.00 11.91           C  
ANISOU 1144  CA  ASP A 136     1348   1470   1709    217    -33   -334       C  
ATOM   1145  C   ASP A 136      33.555  42.420  65.124  1.00 12.74           C  
ANISOU 1145  C   ASP A 136     1638   1677   1524   -141   -119      3       C  
ATOM   1146  O   ASP A 136      33.738  43.644  65.036  1.00 11.91           O  
ANISOU 1146  O   ASP A 136     1423   1680   1421   -142     67    -51       O  
ATOM   1147  CB  ASP A 136      33.128  41.142  62.993  1.00 12.71           C  
ANISOU 1147  CB  ASP A 136     1853   1307   1671    243    172   -182       C  
ATOM   1148  CG  ASP A 136      33.810  39.821  63.371  1.00 13.44           C  
ANISOU 1148  CG  ASP A 136     1862   1464   1781    395    430    -40       C  
ATOM   1149  OD1 ASP A 136      33.334  39.121  64.288  1.00 14.51           O  
ANISOU 1149  OD1 ASP A 136     1863   1531   2120     24    211    188       O  
ATOM   1150  OD2 ASP A 136      34.838  39.500  62.728  1.00 14.72           O  
ANISOU 1150  OD2 ASP A 136     1642   1790   2161    315    341   -343       O  
ATOM   1151  N   MET A 137      34.234  41.600  65.896  1.00 11.70           N  
ANISOU 1151  N   MET A 137     1213   1755   1477    -17    145    -15       N  
ATOM   1152  CA  MET A 137      35.330  42.087  66.726  1.00 12.92           C  
ANISOU 1152  CA  MET A 137     1415   1813   1683    -15    -55    -61       C  
ATOM   1153  C   MET A 137      36.580  41.244  66.508  1.00 12.44           C  
ANISOU 1153  C   MET A 137     1444   1572   1711     11   -252     98       C  
ATOM   1154  O   MET A 137      36.514  40.021  66.715  1.00 15.63           O  
ANISOU 1154  O   MET A 137     2183   1608   2149     18     87    248       O  
ATOM   1155  CB  MET A 137      34.994  42.161  68.226  1.00 12.27           C  
ANISOU 1155  CB  MET A 137     1538   1600   1526    214   -259    346       C  
ATOM   1156  CG  MET A 137      34.029  43.355  68.402  1.00 16.05           C  
ANISOU 1156  CG  MET A 137     1827   2054   2219    503    206     16       C  
ATOM   1157  SD  MET A 137      33.905  43.792  70.189  1.00 23.28           S  
ANISOU 1157  SD  MET A 137     3692   2626   2528   -218    956   -487       S  
ATOM   1158  CE  MET A 137      33.101  42.193  70.485  1.00 17.33           C  
ANISOU 1158  CE  MET A 137     2149   2053   2382    747   1163   -457       C  
ATOM   1159  N   PRO A 138      37.747  41.754  66.126  1.00 13.12           N  
ANISOU 1159  N   PRO A 138     1563   1645   1778    141    142     -2       N  
ATOM   1160  CA  PRO A 138      38.026  43.098  65.640  1.00 12.43           C  
ANISOU 1160  CA  PRO A 138     1269   1797   1659    133     87    180       C  
ATOM   1161  C   PRO A 138      37.155  43.438  64.418  1.00 12.90           C  
ANISOU 1161  C   PRO A 138     1230   1720   1951    133   -152     14       C  
ATOM   1162  O   PRO A 138      36.680  42.493  63.789  1.00 13.45           O  
ANISOU 1162  O   PRO A 138     1526   1493   2090    -45   -254    278       O  
ATOM   1163  CB  PRO A 138      39.493  43.073  65.203  1.00 12.93           C  
ANISOU 1163  CB  PRO A 138     1218   1797   1897    391     43    295       C  
ATOM   1164  CG  PRO A 138      40.076  41.879  65.845  1.00 14.06           C  
ANISOU 1164  CG  PRO A 138     1565   1492   2286    301    215    348       C  
ATOM   1165  CD  PRO A 138      38.969  40.901  66.151  1.00 14.31           C  
ANISOU 1165  CD  PRO A 138     1483   1770   2185    106   -117    211       C  
ATOM   1166  N   GLY A 139      36.903  44.719  64.204  1.00 10.92           N  
ANISOU 1166  N   GLY A 139     1213   1621   1316   -130    -49     22       N  
ATOM   1167  CA  GLY A 139      36.002  45.120  63.162  1.00 11.24           C  
ANISOU 1167  CA  GLY A 139     1233   1755   1284   -103      6    120       C  
ATOM   1168  C   GLY A 139      36.623  45.165  61.766  1.00 11.39           C  
ANISOU 1168  C   GLY A 139     1175   1814   1338    239     51    163       C  
ATOM   1169  O   GLY A 139      37.768  44.794  61.511  1.00 12.74           O  
ANISOU 1169  O   GLY A 139     1201   1894   1744    164     50   -524       O  
ATOM   1170  N   ALA A 140      35.791  45.664  60.845  1.00 12.49           N  
ANISOU 1170  N   ALA A 140     1695   1667   1385    131   -226    206       N  
ATOM   1171  CA  ALA A 140      36.176  45.820  59.440  1.00 11.71           C  
ANISOU 1171  CA  ALA A 140     1368   1711   1371     13   -268     73       C  
ATOM   1172  C   ALA A 140      37.345  46.793  59.307  1.00 12.24           C  
ANISOU 1172  C   ALA A 140     1290   1699   1662     71    -31   -189       C  
ATOM   1173  O   ALA A 140      38.060  46.753  58.306  1.00 12.73           O  
ANISOU 1173  O   ALA A 140     1441   1837   1560    -17    -42   -122       O  
ATOM   1174  CB  ALA A 140      34.975  46.283  58.611  1.00 10.58           C  
ANISOU 1174  CB  ALA A 140     1451   1241   1328    147   -291   -131       C  
ATOM   1175  N   ASP A 141      37.500  47.663  60.309  1.00 11.55           N  
ANISOU 1175  N   ASP A 141     1331   1480   1577    160   -123    -49       N  
ATOM   1176  CA  ASP A 141      38.611  48.615  60.363  1.00 10.72           C  
ANISOU 1176  CA  ASP A 141     1313   1082   1679    333     41    -30       C  
ATOM   1177  C   ASP A 141      39.939  47.887  60.514  1.00 11.72           C  
ANISOU 1177  C   ASP A 141     1253   1328   1870    324    132    208       C  
ATOM   1178  O   ASP A 141      40.926  48.139  59.830  1.00 13.77           O  
ANISOU 1178  O   ASP A 141     1241   1834   2159    190    200    237       O  
ATOM   1179  CB  ASP A 141      38.433  49.653  61.478  1.00 11.89           C  
ANISOU 1179  CB  ASP A 141     1612   1273   1632    274     14   -100       C  
ATOM   1180  CG  ASP A 141      38.285  49.058  62.854  1.00 12.02           C  
ANISOU 1180  CG  ASP A 141     1408   1543   1615    154   -101    -63       C  
ATOM   1181  OD1 ASP A 141      37.603  48.036  63.039  1.00 13.56           O  
ANISOU 1181  OD1 ASP A 141     1725   1818   1608   -112    255   -136       O  
ATOM   1182  OD2 ASP A 141      38.889  49.631  63.796  1.00 13.56           O  
ANISOU 1182  OD2 ASP A 141     1639   1887   1625    154     58   -443       O  
ATOM   1183  N   TYR A 142      39.947  46.939  61.438  1.00 12.05           N  
ANISOU 1183  N   TYR A 142     1484   1318   1775    389    -29    159       N  
ATOM   1184  CA  TYR A 142      41.110  46.077  61.623  1.00 11.29           C  
ANISOU 1184  CA  TYR A 142     1320   1392   1579    320     -5    102       C  
ATOM   1185  C   TYR A 142      41.362  45.324  60.308  1.00 12.25           C  
ANISOU 1185  C   TYR A 142     1622   1349   1682    276     63     28       C  
ATOM   1186  O   TYR A 142      42.490  45.210  59.825  1.00 14.46           O  
ANISOU 1186  O   TYR A 142     1797   1874   1824    143    320   -164       O  
ATOM   1187  CB  TYR A 142      40.868  45.150  62.831  1.00 11.28           C  
ANISOU 1187  CB  TYR A 142     1261   1320   1707    348     42    163       C  
ATOM   1188  CG  TYR A 142      41.922  44.034  62.885  1.00 11.28           C  
ANISOU 1188  CG  TYR A 142     1244   1287   1756    323     15     56       C  
ATOM   1189  CD1 TYR A 142      43.138  44.269  63.547  1.00 11.09           C  
ANISOU 1189  CD1 TYR A 142     1160   1579   1473    309    138    154       C  
ATOM   1190  CD2 TYR A 142      41.723  42.787  62.310  1.00 12.16           C  
ANISOU 1190  CD2 TYR A 142     1619   1193   1807    222     68    151       C  
ATOM   1191  CE1 TYR A 142      44.099  43.275  63.610  1.00 11.46           C  
ANISOU 1191  CE1 TYR A 142     1042   1646   1665    301    259     49       C  
ATOM   1192  CE2 TYR A 142      42.684  41.790  62.352  1.00 13.52           C  
ANISOU 1192  CE2 TYR A 142     1515   1329   2292    260    183   -148       C  
ATOM   1193  CZ  TYR A 142      43.869  42.058  63.016  1.00 13.70           C  
ANISOU 1193  CZ  TYR A 142     1548   1488   2169    277    114    114       C  
ATOM   1194  OH  TYR A 142      44.849  41.104  63.091  1.00 15.66           O  
ANISOU 1194  OH  TYR A 142     1933   1574   2443    515   -169     85       O  
ATOM   1195  N   GLN A 143      40.288  44.752  59.751  1.00 12.14           N  
ANISOU 1195  N   GLN A 143     1783   1273   1556    279   -123    176       N  
ATOM   1196  CA  GLN A 143      40.485  43.962  58.525  1.00 13.08           C  
ANISOU 1196  CA  GLN A 143     1724   1601   1645    153     21     21       C  
ATOM   1197  C   GLN A 143      41.080  44.792  57.391  1.00 12.27           C  
ANISOU 1197  C   GLN A 143     1489   1536   1635    173    -49     -3       C  
ATOM   1198  O   GLN A 143      41.977  44.354  56.661  1.00 14.03           O  
ANISOU 1198  O   GLN A 143     1499   1700   2131    171    228     80       O  
ATOM   1199  CB  GLN A 143      39.181  43.320  58.019  1.00 14.04           C  
ANISOU 1199  CB  GLN A 143     1825   1886   1623   -104    200   -114       C  
ATOM   1200  CG  GLN A 143      38.526  42.335  58.944  1.00 15.55           C  
ANISOU 1200  CG  GLN A 143     2006   1792   2110     10    498    -23       C  
ATOM   1201  CD  GLN A 143      39.393  41.147  59.322  1.00 18.26           C  
ANISOU 1201  CD  GLN A 143     2469   2121   2349    123    -16    263       C  
ATOM   1202  OE1 GLN A 143      40.364  40.805  58.642  1.00 20.01           O  
ANISOU 1202  OE1 GLN A 143     2047   2113   3443    373    -24    362       O  
ATOM   1203  NE2 GLN A 143      39.006  40.522  60.451  1.00 23.09           N  
ANISOU 1203  NE2 GLN A 143     3502   2687   2585   -408   -252    710       N  
ATOM   1204  N   LEU A 144      40.582  46.009  57.181  1.00 12.87           N  
ANISOU 1204  N   LEU A 144     1624   1454   1813    112    -54    -22       N  
ATOM   1205  CA  LEU A 144      41.118  46.811  56.070  1.00 13.25           C  
ANISOU 1205  CA  LEU A 144     1682   1588   1766    135   -159     86       C  
ATOM   1206  C   LEU A 144      42.533  47.259  56.371  1.00 12.60           C  
ANISOU 1206  C   LEU A 144     1595   1600   1592    193   -107    229       C  
ATOM   1207  O   LEU A 144      43.349  47.353  55.446  1.00 15.30           O  
ANISOU 1207  O   LEU A 144     1968   2227   1618   -222     25    334       O  
ATOM   1208  CB  LEU A 144      40.236  48.034  55.826  1.00 14.04           C  
ANISOU 1208  CB  LEU A 144     1591   1846   1898    261   -103    244       C  
ATOM   1209  CG  LEU A 144      39.045  47.739  54.919  1.00 15.12           C  
ANISOU 1209  CG  LEU A 144     1688   2032   2026    411   -182   -129       C  
ATOM   1210  CD1 LEU A 144      37.953  48.772  55.167  1.00 18.59           C  
ANISOU 1210  CD1 LEU A 144     2285   1971   2806    876   -889   -177       C  
ATOM   1211  CD2 LEU A 144      39.524  47.697  53.466  1.00 18.28           C  
ANISOU 1211  CD2 LEU A 144     3023   2062   1859    -95   -169    184       C  
ATOM   1212  N   THR A 145      42.825  47.514  57.667  1.00 13.01           N  
ANISOU 1212  N   THR A 145     1624   1635   1685    164    -42    -86       N  
ATOM   1213  CA  THR A 145      44.229  47.788  57.992  1.00 13.21           C  
ANISOU 1213  CA  THR A 145     1615   1662   1742    218    -22   -399       C  
ATOM   1214  C   THR A 145      45.137  46.674  57.492  1.00 13.74           C  
ANISOU 1214  C   THR A 145     1653   1661   1906    136    296   -352       C  
ATOM   1215  O   THR A 145      46.180  46.912  56.827  1.00 16.03           O  
ANISOU 1215  O   THR A 145     1772   2085   2235    182    472   -110       O  
ATOM   1216  CB  THR A 145      44.382  47.980  59.517  1.00 13.52           C  
ANISOU 1216  CB  THR A 145     1422   1983   1734    168     96   -407       C  
ATOM   1217  OG1 THR A 145      43.601  49.129  59.870  1.00 13.08           O  
ANISOU 1217  OG1 THR A 145     1370   1890   1710     29    486   -267       O  
ATOM   1218  CG2 THR A 145      45.830  48.252  59.914  1.00 14.89           C  
ANISOU 1218  CG2 THR A 145     1477   2312   1870    214   -120   -219       C  
ATOM   1219  N   LYS A 146      44.756  45.443  57.826  1.00 13.63           N  
ANISOU 1219  N   LYS A 146     1823   1646   1710    238    213   -225       N  
ATOM   1220  CA  LYS A 146      45.537  44.260  57.442  1.00 14.47           C  
ANISOU 1220  CA  LYS A 146     2021   1703   1774    346    441    -60       C  
ATOM   1221  C   LYS A 146      45.544  44.106  55.930  1.00 14.63           C  
ANISOU 1221  C   LYS A 146     1805   1931   1824    315    347   -291       C  
ATOM   1222  O   LYS A 146      46.590  43.938  55.275  1.00 15.41           O  
ANISOU 1222  O   LYS A 146     1742   2438   1674    382    263   -130       O  
ATOM   1223  CB  LYS A 146      44.936  43.038  58.164  1.00 17.28           C  
ANISOU 1223  CB  LYS A 146     2642   1691   2231    156    406     57       C  
ATOM   1224  CG  LYS A 146      45.432  41.702  57.662  1.00 18.77           C  
ANISOU 1224  CG  LYS A 146     2617   1717   2797    418     95     75       C  
ATOM   1225  CD  LYS A 146      44.850  40.545  58.480  1.00 22.12           C  
ANISOU 1225  CD  LYS A 146     3716   1750   2939    312   -174    411       C  
ATOM   1226  CE  LYS A 146      45.424  39.219  58.010  1.00 26.54           C  
ANISOU 1226  CE  LYS A 146     4925   1672   3488      5    257    -64       C  
ATOM   1227  NZ  LYS A 146      44.459  38.102  58.074  1.00 27.56           N  
ANISOU 1227  NZ  LYS A 146     5266   2135   3071   -396    975   -400       N  
ATOM   1228  N   LEU A 147      44.366  44.166  55.309  1.00 14.25           N  
ANISOU 1228  N   LEU A 147     1680   1795   1939     26    415   -413       N  
ATOM   1229  CA  LEU A 147      44.284  43.965  53.872  1.00 14.38           C  
ANISOU 1229  CA  LEU A 147     1738   1806   1919    146    291   -265       C  
ATOM   1230  C   LEU A 147      45.047  45.016  53.069  1.00 13.81           C  
ANISOU 1230  C   LEU A 147     1494   1850   1904    206    176   -208       C  
ATOM   1231  O   LEU A 147      45.609  44.647  51.998  1.00 16.19           O  
ANISOU 1231  O   LEU A 147     1604   2227   2321     30    587   -396       O  
ATOM   1232  CB  LEU A 147      42.831  43.965  53.403  1.00 15.16           C  
ANISOU 1232  CB  LEU A 147     1702   2030   2029      8    307    -62       C  
ATOM   1233  CG  LEU A 147      41.930  42.794  53.753  1.00 17.89           C  
ANISOU 1233  CG  LEU A 147     2147   2000   2652   -283    108   -203       C  
ATOM   1234  CD1 LEU A 147      40.520  43.058  53.252  1.00 23.41           C  
ANISOU 1234  CD1 LEU A 147     1712   3225   3958   -302    461     23       C  
ATOM   1235  CD2 LEU A 147      42.472  41.503  53.148  1.00 21.32           C  
ANISOU 1235  CD2 LEU A 147     2480   2093   3530   -301   1009   -191       C  
ATOM   1236  N   LEU A 148      45.056  46.252  53.533  1.00 13.39           N  
ANISOU 1236  N   LEU A 148     1636   1757   1695    232   -210    -52       N  
ATOM   1237  CA  LEU A 148      45.734  47.293  52.765  1.00 14.26           C  
ANISOU 1237  CA  LEU A 148     1777   1883   1759    138    -62    -91       C  
ATOM   1238  C   LEU A 148      47.207  47.439  53.097  1.00 14.86           C  
ANISOU 1238  C   LEU A 148     1725   2131   1792    105     74   -246       C  
ATOM   1239  O   LEU A 148      47.967  48.163  52.426  1.00 17.04           O  
ANISOU 1239  O   LEU A 148     1821   2463   2189    160    483   -201       O  
ATOM   1240  CB  LEU A 148      45.053  48.642  53.036  1.00 14.67           C  
ANISOU 1240  CB  LEU A 148     1964   1787   1825    181   -257     48       C  
ATOM   1241  CG  LEU A 148      43.660  48.841  52.416  1.00 14.89           C  
ANISOU 1241  CG  LEU A 148     1967   2010   1679    275   -218      0       C  
ATOM   1242  CD1 LEU A 148      43.034  50.110  52.984  1.00 15.44           C  
ANISOU 1242  CD1 LEU A 148     1855   2013   1998    187   -109    -85       C  
ATOM   1243  CD2 LEU A 148      43.729  48.941  50.895  1.00 16.72           C  
ANISOU 1243  CD2 LEU A 148     2255   2399   1698    518   -183    101       C  
ATOM   1244  N   GLY A 149      47.634  46.805  54.181  1.00 14.80           N  
ANISOU 1244  N   GLY A 149     1698   1868   2059    395    -93   -332       N  
ATOM   1245  CA  GLY A 149      48.995  47.060  54.629  1.00 14.25           C  
ANISOU 1245  CA  GLY A 149     1466   1823   2126    544    171   -351       C  
ATOM   1246  C   GLY A 149      49.166  48.458  55.184  1.00 14.12           C  
ANISOU 1246  C   GLY A 149     1509   1886   1971    235    298   -312       C  
ATOM   1247  O   GLY A 149      50.197  49.102  54.977  1.00 18.04           O  
ANISOU 1247  O   GLY A 149     1586   2522   2747    -92    220   -379       O  
ATOM   1248  N   LEU A 150      48.191  49.016  55.902  1.00 13.80           N  
ANISOU 1248  N   LEU A 150     1637   1806   1799    420    123   -363       N  
ATOM   1249  CA  LEU A 150      48.364  50.310  56.527  1.00 12.27           C  
ANISOU 1249  CA  LEU A 150     1106   1720   1837    180    163   -193       C  
ATOM   1250  C   LEU A 150      49.277  50.116  57.749  1.00 12.83           C  
ANISOU 1250  C   LEU A 150     1239   1773   1861    231    106   -164       C  
ATOM   1251  O   LEU A 150      49.474  48.982  58.219  1.00 15.22           O  
ANISOU 1251  O   LEU A 150     2132   1899   1753     98     49     48       O  
ATOM   1252  CB  LEU A 150      47.032  50.917  56.993  1.00 11.80           C  
ANISOU 1252  CB  LEU A 150     1194   1529   1761    178    185   -194       C  
ATOM   1253  CG  LEU A 150      45.955  51.090  55.918  1.00 12.26           C  
ANISOU 1253  CG  LEU A 150     1047   1895   1716    231    330     17       C  
ATOM   1254  CD1 LEU A 150      44.717  51.754  56.528  1.00 13.88           C  
ANISOU 1254  CD1 LEU A 150     1154   2261   1860    331    362   -223       C  
ATOM   1255  CD2 LEU A 150      46.506  51.892  54.730  1.00 13.66           C  
ANISOU 1255  CD2 LEU A 150     1501   2065   1626    -15    370    -68       C  
ATOM   1256  N   ARG A 151      49.796  51.208  58.285  1.00 13.71           N  
ANISOU 1256  N   ARG A 151     1513   1940   1756     46     88   -181       N  
ATOM   1257  CA  ARG A 151      50.588  51.121  59.525  1.00 14.07           C  
ANISOU 1257  CA  ARG A 151     1764   1951   1630    120    118   -193       C  
ATOM   1258  C   ARG A 151      49.763  50.604  60.698  1.00 12.99           C  
ANISOU 1258  C   ARG A 151     1623   1551   1761    596    337   -212       C  
ATOM   1259  O   ARG A 151      48.586  50.944  60.795  1.00 14.29           O  
ANISOU 1259  O   ARG A 151     1538   1822   2068    526    147   -361       O  
ATOM   1260  CB  ARG A 151      51.176  52.491  59.850  1.00 17.93           C  
ANISOU 1260  CB  ARG A 151     2215   2519   2078   -544    104   -429       C  
ATOM   1261  CG  ARG A 151      52.155  52.977  58.793  1.00 20.18           C  
ANISOU 1261  CG  ARG A 151     2274   2927   2468   -501    -30    448       C  
ATOM   1262  CD  ARG A 151      53.518  52.366  59.168  1.00 25.42           C  
ANISOU 1262  CD  ARG A 151     2279   3838   3541     55    343    293       C  
ATOM   1263  NE  ARG A 151      53.678  51.171  58.318  1.00 30.78           N  
ANISOU 1263  NE  ARG A 151     3226   4304   4165    462    343   -180       N  
ATOM   1264  CZ  ARG A 151      54.605  51.237  57.356  1.00 34.55           C  
ANISOU 1264  CZ  ARG A 151     4124   4447   4555    211    989   -506       C  
ATOM   1265  NH1 ARG A 151      55.285  52.373  57.279  1.00 38.16           N  
ANISOU 1265  NH1 ARG A 151     5643   4395   4461    -61    913    886       N  
ATOM   1266  NH2 ARG A 151      54.810  50.211  56.547  1.00 41.14           N  
ANISOU 1266  NH2 ARG A 151     5056   5006   5570   1209   1066  -1028       N  
ATOM   1267  N  APRO A 152      50.339  49.778  61.568  0.65 14.05           N  
ANISOU 1267  N  APRO A 152     1645   1830   1862    431    150    -24       N  
ATOM   1268  N  BPRO A 152      50.342  49.765  61.547  0.35 14.08           N  
ANISOU 1268  N  BPRO A 152     1656   1821   1874    462    177    -22       N  
ATOM   1269  CA APRO A 152      49.587  49.250  62.709  0.65 14.56           C  
ANISOU 1269  CA APRO A 152     1793   1769   1971    405    224     13       C  
ATOM   1270  CA BPRO A 152      49.620  49.230  62.703  0.35 14.51           C  
ANISOU 1270  CA BPRO A 152     1772   1772   1969    419    227     11       C  
ATOM   1271  C  APRO A 152      49.047  50.320  63.650  0.65 13.55           C  
ANISOU 1271  C  APRO A 152     1552   1750   1847    336    163     35       C  
ATOM   1272  C  BPRO A 152      49.070  50.304  63.639  0.35 13.59           C  
ANISOU 1272  C  BPRO A 152     1550   1767   1849    327    177     12       C  
ATOM   1273  O  APRO A 152      48.085  50.063  64.366  0.65 13.58           O  
ANISOU 1273  O  APRO A 152     1397   2143   1619    272    -26     34       O  
ATOM   1274  O  BPRO A 152      48.101  50.055  64.355  0.35 13.95           O  
ANISOU 1274  O  BPRO A 152     1484   2156   1662    237     59    -10       O  
ATOM   1275  CB APRO A 152      50.614  48.433  63.520  0.65 15.44           C  
ANISOU 1275  CB APRO A 152     1909   1869   2089    553    326    173       C  
ATOM   1276  CB BPRO A 152      50.687  48.424  63.464  0.35 15.26           C  
ANISOU 1276  CB BPRO A 152     1862   1867   2070    521    303    162       C  
ATOM   1277  CG APRO A 152      51.948  48.842  62.982  0.65 15.58           C  
ANISOU 1277  CG APRO A 152     1835   2036   2050    440    121    313       C  
ATOM   1278  CG BPRO A 152      51.744  48.125  62.452  0.35 15.18           C  
ANISOU 1278  CG BPRO A 152     1825   1865   2077    513    295    213       C  
ATOM   1279  CD APRO A 152      51.718  49.252  61.535  0.65 14.61           C  
ANISOU 1279  CD APRO A 152     1748   1844   1960    556    180    143       C  
ATOM   1280  CD BPRO A 152      51.715  49.239  61.439  0.35 14.44           C  
ANISOU 1280  CD BPRO A 152     1711   1861   1914    546    156    124       C  
ATOM   1281  N   TYR A 153      49.682  51.470  63.632  1.00 13.32           N  
ANISOU 1281  N   TYR A 153     1411   1890   1758    254   -155    -69       N  
ATOM   1282  CA  TYR A 153      49.349  52.602  64.489  1.00 13.19           C  
ANISOU 1282  CA  TYR A 153     1268   1897   1847    216    -11    -92       C  
ATOM   1283  C   TYR A 153      48.442  53.585  63.776  1.00 12.09           C  
ANISOU 1283  C   TYR A 153     1279   1779   1535    118     85    -91       C  
ATOM   1284  O   TYR A 153      48.307  54.724  64.261  1.00 12.27           O  
ANISOU 1284  O   TYR A 153     1423   1738   1501     94     46    -52       O  
ATOM   1285  CB  TYR A 153      50.615  53.319  64.970  1.00 14.31           C  
ANISOU 1285  CB  TYR A 153     1357   1940   2139    212   -131   -213       C  
ATOM   1286  CG  TYR A 153      51.646  53.625  63.921  1.00 16.22           C  
ANISOU 1286  CG  TYR A 153     1433   2208   2522    -67    -35    -14       C  
ATOM   1287  CD1 TYR A 153      51.559  54.759  63.135  1.00 18.20           C  
ANISOU 1287  CD1 TYR A 153     1733   2734   2450   -225   -440    332       C  
ATOM   1288  CD2 TYR A 153      52.736  52.779  63.721  1.00 18.33           C  
ANISOU 1288  CD2 TYR A 153     1582   2529   2854     34    408    -80       C  
ATOM   1289  CE1 TYR A 153      52.485  55.091  62.162  1.00 20.55           C  
ANISOU 1289  CE1 TYR A 153     2133   3145   2529   -621   -338    389       C  
ATOM   1290  CE2 TYR A 153      53.686  53.075  62.746  1.00 19.89           C  
ANISOU 1290  CE2 TYR A 153     1872   2974   2711   -276    467   -273       C  
ATOM   1291  CZ  TYR A 153      53.536  54.225  61.987  1.00 21.77           C  
ANISOU 1291  CZ  TYR A 153     2255   3367   2649   -632    218     39       C  
ATOM   1292  OH  TYR A 153      54.475  54.536  61.022  1.00 25.21           O  
ANISOU 1292  OH  TYR A 153     2339   4607   2633  -1000    121    281       O  
ATOM   1293  N   VAL A 154      47.810  53.160  62.677  1.00 11.03           N  
ANISOU 1293  N   VAL A 154      760   1909   1520    138    316   -215       N  
ATOM   1294  CA  VAL A 154      46.736  54.019  62.130  1.00 11.66           C  
ANISOU 1294  CA  VAL A 154     1173   1754   1502    238    153   -225       C  
ATOM   1295  C   VAL A 154      45.652  54.211  63.181  1.00 11.01           C  
ANISOU 1295  C   VAL A 154      878   1723   1583    372     80     58       C  
ATOM   1296  O   VAL A 154      45.313  53.291  63.938  1.00 12.63           O  
ANISOU 1296  O   VAL A 154     1416   1490   1894    126    380   -142       O  
ATOM   1297  CB  VAL A 154      46.220  53.374  60.820  1.00 12.48           C  
ANISOU 1297  CB  VAL A 154     1533   1584   1624    214    -65   -167       C  
ATOM   1298  CG1 VAL A 154      45.506  52.039  61.048  1.00 14.00           C  
ANISOU 1298  CG1 VAL A 154     2099   1586   1635     74      4   -162       C  
ATOM   1299  CG2 VAL A 154      45.308  54.340  60.086  1.00 15.09           C  
ANISOU 1299  CG2 VAL A 154     1814   1826   2093     65   -441    164       C  
ATOM   1300  N   LYS A 155      45.086  55.410  63.324  1.00 11.43           N  
ANISOU 1300  N   LYS A 155     1036   1649   1659    268    227     20       N  
ATOM   1301  CA  LYS A 155      44.033  55.669  64.299  1.00 10.79           C  
ANISOU 1301  CA  LYS A 155      995   1555   1548    177    137   -135       C  
ATOM   1302  C   LYS A 155      42.672  55.351  63.687  1.00 10.99           C  
ANISOU 1302  C   LYS A 155     1022   1663   1492     88    106     22       C  
ATOM   1303  O   LYS A 155      42.296  56.028  62.705  1.00 11.31           O  
ANISOU 1303  O   LYS A 155     1365   1532   1400    -69    -28    -72       O  
ATOM   1304  CB  LYS A 155      44.060  57.105  64.806  1.00 10.61           C  
ANISOU 1304  CB  LYS A 155     1083   1408   1541    332   -126     52       C  
ATOM   1305  CG  LYS A 155      45.319  57.371  65.666  1.00 13.53           C  
ANISOU 1305  CG  LYS A 155     1654   1637   1851    303   -642    -54       C  
ATOM   1306  CD  LYS A 155      45.515  58.890  65.778  1.00 18.55           C  
ANISOU 1306  CD  LYS A 155     2226   1760   3061   -103   -833   -170       C  
ATOM   1307  CE  LYS A 155      46.740  59.223  66.626  1.00 22.90           C  
ANISOU 1307  CE  LYS A 155     2298   2527   3874   -404   -984   -461       C  
ATOM   1308  NZ  LYS A 155      48.010  59.103  65.845  1.00 29.15           N  
ANISOU 1308  NZ  LYS A 155     2179   3489   5406    -38   -562    238       N  
ATOM   1309  N   ARG A 156      41.989  54.365  64.272  1.00 10.35           N  
ANISOU 1309  N   ARG A 156     1120   1541   1273     79    165   -151       N  
ATOM   1310  CA  ARG A 156      40.782  53.823  63.662  1.00 10.24           C  
ANISOU 1310  CA  ARG A 156     1131   1384   1375    138    236   -400       C  
ATOM   1311  C   ARG A 156      39.498  54.271  64.335  1.00 10.08           C  
ANISOU 1311  C   ARG A 156     1102   1439   1289    185    244   -149       C  
ATOM   1312  O   ARG A 156      39.432  54.557  65.535  1.00 11.75           O  
ANISOU 1312  O   ARG A 156     1026   2049   1390     87    278   -421       O  
ATOM   1313  CB  ARG A 156      40.845  52.276  63.671  1.00 11.99           C  
ANISOU 1313  CB  ARG A 156     1744   1377   1432    179    314   -460       C  
ATOM   1314  CG  ARG A 156      41.977  51.763  62.755  1.00 11.30           C  
ANISOU 1314  CG  ARG A 156     1410   1266   1619    416    213    -94       C  
ATOM   1315  CD  ARG A 156      42.209  50.274  62.929  1.00 11.26           C  
ANISOU 1315  CD  ARG A 156     1369   1322   1588    461   -224     -4       C  
ATOM   1316  NE  ARG A 156      42.903  49.951  64.173  1.00 11.77           N  
ANISOU 1316  NE  ARG A 156     1274   1704   1494     74   -168    152       N  
ATOM   1317  CZ  ARG A 156      42.502  49.142  65.133  1.00 12.52           C  
ANISOU 1317  CZ  ARG A 156     1675   1705   1376   -185   -140     -3       C  
ATOM   1318  NH1 ARG A 156      41.340  48.504  65.050  1.00 12.72           N  
ANISOU 1318  NH1 ARG A 156     1353   2110   1370    -53    308   -203       N  
ATOM   1319  NH2 ARG A 156      43.284  48.946  66.208  1.00 11.73           N  
ANISOU 1319  NH2 ARG A 156     1488   1481   1490    328    -21    110       N  
ATOM   1320  N   TYR A 157      38.467  54.426  63.484  1.00 10.28           N  
ANISOU 1320  N   TYR A 157     1109   1380   1417     19    184    -59       N  
ATOM   1321  CA  TYR A 157      37.111  54.882  63.815  1.00 10.77           C  
ANISOU 1321  CA  TYR A 157     1093   1427   1571     76     99    -41       C  
ATOM   1322  C   TYR A 157      36.179  53.870  63.148  1.00  9.79           C  
ANISOU 1322  C   TYR A 157     1049   1432   1238     84    287    -71       C  
ATOM   1323  O   TYR A 157      36.011  53.928  61.937  1.00 11.43           O  
ANISOU 1323  O   TYR A 157     1472   1593   1279     92    128     29       O  
ATOM   1324  CB  TYR A 157      36.831  56.351  63.374  1.00 11.70           C  
ANISOU 1324  CB  TYR A 157     1265   1449   1732     81   -469    -56       C  
ATOM   1325  CG  TYR A 157      37.867  57.242  64.048  1.00 11.24           C  
ANISOU 1325  CG  TYR A 157     1253   1560   1459   -106   -201    -38       C  
ATOM   1326  CD1 TYR A 157      39.136  57.365  63.484  1.00 12.96           C  
ANISOU 1326  CD1 TYR A 157     1669   1705   1550   -505    212    154       C  
ATOM   1327  CD2 TYR A 157      37.602  57.931  65.222  1.00 11.53           C  
ANISOU 1327  CD2 TYR A 157     1308   1530   1542      8   -215    -79       C  
ATOM   1328  CE1 TYR A 157      40.124  58.136  64.043  1.00 12.82           C  
ANISOU 1328  CE1 TYR A 157     1311   1715   1844   -192    237   -134       C  
ATOM   1329  CE2 TYR A 157      38.596  58.723  65.819  1.00 11.37           C  
ANISOU 1329  CE2 TYR A 157     1349   1375   1594   -109     40   -158       C  
ATOM   1330  CZ  TYR A 157      39.821  58.821  65.212  1.00 12.03           C  
ANISOU 1330  CZ  TYR A 157     1320   1525   1725     16     71     11       C  
ATOM   1331  OH  TYR A 157      40.838  59.563  65.765  1.00 12.32           O  
ANISOU 1331  OH  TYR A 157     1267   1640   1773    -36    239   -106       O  
ATOM   1332  N   MET A 158      35.625  52.925  63.918  1.00 10.06           N  
ANISOU 1332  N   MET A 158     1242   1183   1396    173    196      3       N  
ATOM   1333  CA  MET A 158      34.796  51.850  63.345  1.00 11.34           C  
ANISOU 1333  CA  MET A 158     1444   1380   1483     -9    317   -150       C  
ATOM   1334  C   MET A 158      33.336  52.233  63.535  1.00 11.36           C  
ANISOU 1334  C   MET A 158     1369   1609   1339   -112    242    -96       C  
ATOM   1335  O   MET A 158      32.841  52.126  64.677  1.00 12.83           O  
ANISOU 1335  O   MET A 158     1390   2017   1467   -236    362     79       O  
ATOM   1336  CB  MET A 158      35.102  50.518  64.014  1.00 12.13           C  
ANISOU 1336  CB  MET A 158     1620   1274   1714   -148     94   -172       C  
ATOM   1337  CG  MET A 158      34.373  49.283  63.461  1.00 13.20           C  
ANISOU 1337  CG  MET A 158     1901   1359   1757    -59    231   -613       C  
ATOM   1338  SD  MET A 158      34.657  49.017  61.686  1.00 13.25           S  
ANISOU 1338  SD  MET A 158     1762   1710   1563     24     42   -196       S  
ATOM   1339  CE  MET A 158      33.087  49.650  61.037  1.00 17.04           C  
ANISOU 1339  CE  MET A 158     1825   2279   2371     66    -98    179       C  
ATOM   1340  N   MET A 159      32.704  52.678  62.458  1.00 12.19           N  
ANISOU 1340  N   MET A 159     1509   1738   1383    -73    149   -133       N  
ATOM   1341  CA  MET A 159      31.315  53.139  62.499  1.00 12.58           C  
ANISOU 1341  CA  MET A 159     1536   1657   1589    -58    103     63       C  
ATOM   1342  C   MET A 159      30.400  52.020  62.007  1.00 11.79           C  
ANISOU 1342  C   MET A 159     1425   1552   1505     72    131     20       C  
ATOM   1343  O   MET A 159      30.332  51.790  60.791  1.00 13.03           O  
ANISOU 1343  O   MET A 159     1748   1725   1480    -61     92     64       O  
ATOM   1344  CB  MET A 159      31.155  54.411  61.672  1.00 14.01           C  
ANISOU 1344  CB  MET A 159     1869   1600   1854    -16    259    136       C  
ATOM   1345  CG  MET A 159      32.219  55.461  61.947  1.00 14.38           C  
ANISOU 1345  CG  MET A 159     2125   1445   1896    -15    330   -194       C  
ATOM   1346  SD  MET A 159      32.340  55.932  63.687  1.00 16.84           S  
ANISOU 1346  SD  MET A 159     2391   2123   1883     24    271   -230       S  
ATOM   1347  CE  MET A 159      30.809  56.825  63.935  1.00 17.09           C  
ANISOU 1347  CE  MET A 159     2374   2144   1977    -92    705   -238       C  
ATOM   1348  N   TYR A 160      29.750  51.337  62.957  1.00 12.98           N  
ANISOU 1348  N   TYR A 160     1861   1603   1468   -183     66     51       N  
ATOM   1349  CA  TYR A 160      28.910  50.186  62.628  1.00 11.70           C  
ANISOU 1349  CA  TYR A 160     1642   1540   1266    -33    -26     44       C  
ATOM   1350  C   TYR A 160      27.427  50.506  62.820  1.00 12.74           C  
ANISOU 1350  C   TYR A 160     1697   1564   1580     94    -50    -81       C  
ATOM   1351  O   TYR A 160      27.049  51.341  63.653  1.00 13.64           O  
ANISOU 1351  O   TYR A 160     1966   1720   1495   -113    460     -9       O  
ATOM   1352  CB  TYR A 160      29.182  48.992  63.543  1.00 12.35           C  
ANISOU 1352  CB  TYR A 160     1866   1400   1424    149     78    -18       C  
ATOM   1353  CG  TYR A 160      30.223  47.998  63.149  1.00 12.78           C  
ANISOU 1353  CG  TYR A 160     1674   1630   1554    137    170    -32       C  
ATOM   1354  CD1 TYR A 160      30.161  47.411  61.889  1.00 12.24           C  
ANISOU 1354  CD1 TYR A 160     1435   1668   1548    101    282    -44       C  
ATOM   1355  CD2 TYR A 160      31.257  47.624  64.014  1.00 12.35           C  
ANISOU 1355  CD2 TYR A 160     1522   1638   1532     15    266     71       C  
ATOM   1356  CE1 TYR A 160      31.103  46.478  61.482  1.00 12.11           C  
ANISOU 1356  CE1 TYR A 160     1461   1508   1632     87    340     89       C  
ATOM   1357  CE2 TYR A 160      32.205  46.690  63.614  1.00 12.50           C  
ANISOU 1357  CE2 TYR A 160     1416   1665   1667    -24    317    103       C  
ATOM   1358  CZ  TYR A 160      32.120  46.120  62.349  1.00 12.29           C  
ANISOU 1358  CZ  TYR A 160     1475   1533   1661     77    331    117       C  
ATOM   1359  OH  TYR A 160      33.030  45.196  61.902  1.00 13.32           O  
ANISOU 1359  OH  TYR A 160     1765   1466   1831    266    301    197       O  
ATOM   1360  N   GLN A 161      26.581  49.833  62.047  1.00 13.90           N  
ANISOU 1360  N   GLN A 161     1626   2071   1583   -230     55    -52       N  
ATOM   1361  CA  GLN A 161      25.144  49.882  62.129  1.00 13.29           C  
ANISOU 1361  CA  GLN A 161     1632   1904   1512     70     74      6       C  
ATOM   1362  C   GLN A 161      24.615  51.309  62.040  1.00 14.76           C  
ANISOU 1362  C   GLN A 161     2161   1807   1638     26    294    109       C  
ATOM   1363  O   GLN A 161      23.696  51.708  62.757  1.00 17.61           O  
ANISOU 1363  O   GLN A 161     2478   1904   2311    284    586     11       O  
ATOM   1364  CB  GLN A 161      24.671  49.276  63.451  1.00 12.77           C  
ANISOU 1364  CB  GLN A 161     1603   1688   1562    159    159    -10       C  
ATOM   1365  CG  GLN A 161      23.300  48.612  63.313  1.00 15.07           C  
ANISOU 1365  CG  GLN A 161     1841   2241   1645   -208    138    -72       C  
ATOM   1366  CD  GLN A 161      23.318  47.605  62.185  1.00 16.83           C  
ANISOU 1366  CD  GLN A 161     2312   2160   1922   -181    -87   -193       C  
ATOM   1367  OE1 GLN A 161      24.095  46.659  62.150  1.00 17.36           O  
ANISOU 1367  OE1 GLN A 161     2992   1673   1931   -200    405    272       O  
ATOM   1368  NE2 GLN A 161      22.477  47.821  61.185  1.00 24.12           N  
ANISOU 1368  NE2 GLN A 161     2836   3367   2961    103  -1105  -1064       N  
ATOM   1369  N   GLN A 162      25.204  52.060  61.131  1.00 15.71           N  
ANISOU 1369  N   GLN A 162     2274   2169   1525   -406   -122    271       N  
ATOM   1370  CA  GLN A 162      25.023  53.483  61.077  1.00 17.61           C  
ANISOU 1370  CA  GLN A 162     2699   2120   1874   -607   -292    374       C  
ATOM   1371  C   GLN A 162      23.780  53.916  60.333  1.00 16.48           C  
ANISOU 1371  C   GLN A 162     2316   1942   2004   -282     90     79       C  
ATOM   1372  O   GLN A 162      23.065  54.774  60.853  1.00 19.96           O  
ANISOU 1372  O   GLN A 162     2913   2285   2385   -188    552   -153       O  
ATOM   1373  CB  GLN A 162      26.269  54.109  60.392  1.00 18.97           C  
ANISOU 1373  CB  GLN A 162     2382   2374   2452   -543   -509    762       C  
ATOM   1374  CG  GLN A 162      27.535  53.810  61.197  1.00 18.76           C  
ANISOU 1374  CG  GLN A 162     2597   2468   2064   -159   -537    281       C  
ATOM   1375  CD  GLN A 162      27.689  54.688  62.417  1.00 20.21           C  
ANISOU 1375  CD  GLN A 162     2894   2311   2473    -41   -542     38       C  
ATOM   1376  OE1 GLN A 162      27.632  55.914  62.284  1.00 23.68           O  
ANISOU 1376  OE1 GLN A 162     3649   2326   3022    -46   -520    157       O  
ATOM   1377  NE2 GLN A 162      27.890  54.103  63.605  1.00 17.30           N  
ANISOU 1377  NE2 GLN A 162     2283   2157   2132     87   -286   -303       N  
ATOM   1378  N   GLY A 163      23.523  53.370  59.143  1.00 14.74           N  
ANISOU 1378  N   GLY A 163     2140   1639   1822    130    -85    363       N  
ATOM   1379  CA  GLY A 163      22.361  53.759  58.350  1.00 14.54           C  
ANISOU 1379  CA  GLY A 163     1804   1814   1908    327    249    443       C  
ATOM   1380  C   GLY A 163      22.666  54.789  57.266  1.00 13.70           C  
ANISOU 1380  C   GLY A 163     1620   1721   1863     93    -26    395       C  
ATOM   1381  O   GLY A 163      23.792  55.276  57.072  1.00 13.05           O  
ANISOU 1381  O   GLY A 163     1593   2028   1339     70     82     83       O  
HETATM 1382  N   CSD A 164      21.611  55.112  56.508  1.00 12.35           N  
ANISOU 1382  N   CSD A 164     1506   1397   1790    353    110     76       N  
HETATM 1383  CA  CSD A 164      21.810  55.783  55.235  1.00 13.72           C  
ANISOU 1383  CA  CSD A 164     2154   1724   1335   -343   -456   -223       C  
HETATM 1384  CB  CSD A 164      20.508  55.951  54.458  1.00 11.69           C  
ANISOU 1384  CB  CSD A 164     1945    981   1515    140   -246   -586       C  
HETATM 1385  SG  CSD A 164      19.948  54.402  53.750  1.00  2.75           S  
ANISOU 1385  SG  CSD A 164     -220    353    913    303    931   -106       S  
HETATM 1386  C   CSD A 164      22.369  57.191  55.334  1.00 11.59           C  
ANISOU 1386  C   CSD A 164     1551   1650   1202   -153     51   -150       C  
HETATM 1387  O   CSD A 164      22.863  57.670  54.301  1.00 17.60           O  
ANISOU 1387  O   CSD A 164     2796   2523   1369   -526    321    111       O  
HETATM 1388  OD1 CSD A 164      19.538  53.648  54.921  1.00 22.42           O  
ANISOU 1388  OD1 CSD A 164     3334   3043   2141  -1485    350   1590       O  
HETATM 1389  OD2 CSD A 164      18.832  54.807  52.840  1.00 15.39           O  
ANISOU 1389  OD2 CSD A 164     1465   2352   2029    -16   -748    -69       O  
ATOM   1390  N   PHE A 165      22.286  57.843  56.471  1.00 12.15           N  
ANISOU 1390  N   PHE A 165     1743   1544   1332   -156    -13   -243       N  
ATOM   1391  CA  PHE A 165      22.781  59.202  56.590  1.00 10.37           C  
ANISOU 1391  CA  PHE A 165     1161   1289   1491    239    316   -120       C  
ATOM   1392  C   PHE A 165      24.309  59.213  56.768  1.00 11.63           C  
ANISOU 1392  C   PHE A 165     1217   1336   1865    217     98    -24       C  
ATOM   1393  O   PHE A 165      24.889  60.314  56.767  1.00 10.94           O  
ANISOU 1393  O   PHE A 165     1314   1363   1479    135     19    -50       O  
ATOM   1394  CB  PHE A 165      22.132  59.934  57.784  1.00 10.11           C  
ANISOU 1394  CB  PHE A 165     1369   1434   1039    180    118    -28       C  
ATOM   1395  CG  PHE A 165      22.337  59.307  59.149  1.00 12.14           C  
ANISOU 1395  CG  PHE A 165     1774   1576   1262   -185   -172    229       C  
ATOM   1396  CD1 PHE A 165      23.495  59.432  59.915  1.00 12.03           C  
ANISOU 1396  CD1 PHE A 165     1788   1429   1355   -122   -225    301       C  
ATOM   1397  CD2 PHE A 165      21.301  58.554  59.721  1.00 11.95           C  
ANISOU 1397  CD2 PHE A 165     1679   1531   1330    -34   -117    294       C  
ATOM   1398  CE1 PHE A 165      23.665  58.846  61.155  1.00 12.06           C  
ANISOU 1398  CE1 PHE A 165     1847   1412   1323   -118   -195    292       C  
ATOM   1399  CE2 PHE A 165      21.445  57.934  60.948  1.00 11.84           C  
ANISOU 1399  CE2 PHE A 165     1570   1532   1398    142    -53    357       C  
ATOM   1400  CZ  PHE A 165      22.622  58.086  61.672  1.00 12.46           C  
ANISOU 1400  CZ  PHE A 165     1627   1653   1454     51   -117    446       C  
ATOM   1401  N   ALA A 166      24.933  58.060  57.027  1.00 10.82           N  
ANISOU 1401  N   ALA A 166     1260   1388   1464    220     29     65       N  
ATOM   1402  CA  ALA A 166      26.322  58.124  57.517  1.00 10.28           C  
ANISOU 1402  CA  ALA A 166     1298   1356   1252    153     25     43       C  
ATOM   1403  C   ALA A 166      27.383  58.452  56.493  1.00 10.10           C  
ANISOU 1403  C   ALA A 166     1330   1133   1373     98     80     -3       C  
ATOM   1404  O   ALA A 166      28.576  58.607  56.846  1.00 11.52           O  
ANISOU 1404  O   ALA A 166     1372   1553   1454    -20     30    222       O  
ATOM   1405  CB  ALA A 166      26.642  56.798  58.228  1.00 12.94           C  
ANISOU 1405  CB  ALA A 166     1371   1762   1782    230     89    560       C  
ATOM   1406  N   GLY A 167      27.053  58.588  55.206  1.00 10.62           N  
ANISOU 1406  N   GLY A 167     1102   1566   1368    207    186     50       N  
ATOM   1407  CA  GLY A 167      28.020  59.205  54.294  1.00 11.18           C  
ANISOU 1407  CA  GLY A 167     1330   1564   1354     65    341   -174       C  
ATOM   1408  C   GLY A 167      28.271  60.635  54.751  1.00 11.49           C  
ANISOU 1408  C   GLY A 167     1434   1558   1373     42     87    -92       C  
ATOM   1409  O   GLY A 167      29.383  61.176  54.687  1.00 12.70           O  
ANISOU 1409  O   GLY A 167     1483   1728   1614    -63     20   -123       O  
ATOM   1410  N   GLY A 168      27.235  61.336  55.221  1.00 10.32           N  
ANISOU 1410  N   GLY A 168     1589   1327   1006     96     95     37       N  
ATOM   1411  CA  GLY A 168      27.564  62.644  55.815  1.00 10.44           C  
ANISOU 1411  CA  GLY A 168     1477   1286   1202     17   -108    131       C  
ATOM   1412  C   GLY A 168      28.313  62.509  57.139  1.00 10.40           C  
ANISOU 1412  C   GLY A 168     1274   1384   1295     60   -136    102       C  
ATOM   1413  O   GLY A 168      29.215  63.282  57.426  1.00 12.25           O  
ANISOU 1413  O   GLY A 168     1601   1655   1399   -155    -88   -250       O  
ATOM   1414  N   THR A 169      27.953  61.554  57.989  1.00 10.01           N  
ANISOU 1414  N   THR A 169     1322   1418   1063    321    127     36       N  
ATOM   1415  CA  THR A 169      28.610  61.349  59.276  1.00 10.39           C  
ANISOU 1415  CA  THR A 169     1301   1439   1209     75    -40     54       C  
ATOM   1416  C   THR A 169      30.111  61.172  59.084  1.00 10.68           C  
ANISOU 1416  C   THR A 169     1284   1371   1402     31    -51    -65       C  
ATOM   1417  O   THR A 169      30.912  61.754  59.809  1.00 11.49           O  
ANISOU 1417  O   THR A 169     1375   1453   1539    -27    -94   -129       O  
ATOM   1418  CB  THR A 169      28.076  60.099  59.976  1.00 11.02           C  
ANISOU 1418  CB  THR A 169     1339   1626   1224     48    -92    230       C  
ATOM   1419  OG1 THR A 169      26.624  60.135  60.009  1.00 11.26           O  
ANISOU 1419  OG1 THR A 169     1341   1428   1508     56    136   -112       O  
ATOM   1420  CG2 THR A 169      28.560  60.013  61.424  1.00 13.97           C  
ANISOU 1420  CG2 THR A 169     2539   1313   1457   -253   -673    220       C  
ATOM   1421  N   VAL A 170      30.503  60.345  58.116  1.00 10.63           N  
ANISOU 1421  N   VAL A 170     1307   1371   1362   -176    159    -25       N  
ATOM   1422  CA  VAL A 170      31.949  60.121  58.002  1.00  9.94           C  
ANISOU 1422  CA  VAL A 170     1331   1337   1110    -27     82    148       C  
ATOM   1423  C   VAL A 170      32.690  61.362  57.522  1.00  9.95           C  
ANISOU 1423  C   VAL A 170     1097   1413   1272     54     23    296       C  
ATOM   1424  O   VAL A 170      33.856  61.569  57.896  1.00 10.64           O  
ANISOU 1424  O   VAL A 170      975   1467   1601    139    144    198       O  
ATOM   1425  CB  VAL A 170      32.300  58.954  57.068  1.00 11.05           C  
ANISOU 1425  CB  VAL A 170     1592   1459   1148    128     32     76       C  
ATOM   1426  CG1 VAL A 170      31.739  57.629  57.594  1.00 13.49           C  
ANISOU 1426  CG1 VAL A 170     2071   1288   1768    231    227    143       C  
ATOM   1427  CG2 VAL A 170      31.836  59.219  55.633  1.00 11.39           C  
ANISOU 1427  CG2 VAL A 170     1780   1199   1347    369   -377   -106       C  
ATOM   1428  N   LEU A 171      32.017  62.205  56.735  1.00 10.01           N  
ANISOU 1428  N   LEU A 171     1383   1259   1162    173    -25    127       N  
ATOM   1429  CA  LEU A 171      32.672  63.455  56.338  1.00 10.46           C  
ANISOU 1429  CA  LEU A 171     1654   1234   1087    140     95     79       C  
ATOM   1430  C   LEU A 171      32.795  64.389  57.539  1.00  9.96           C  
ANISOU 1430  C   LEU A 171     1254   1347   1182    199     34    -16       C  
ATOM   1431  O   LEU A 171      33.814  65.024  57.766  1.00 11.93           O  
ANISOU 1431  O   LEU A 171     1453   1851   1228   -133    189   -112       O  
ATOM   1432  CB  LEU A 171      31.837  64.097  55.224  1.00 10.90           C  
ANISOU 1432  CB  LEU A 171     1927   1115   1098    203     -6      3       C  
ATOM   1433  CG  LEU A 171      32.003  63.440  53.855  1.00 11.51           C  
ANISOU 1433  CG  LEU A 171     1516   1742   1115     49     60   -148       C  
ATOM   1434  CD1 LEU A 171      30.969  63.958  52.857  1.00 13.87           C  
ANISOU 1434  CD1 LEU A 171     1674   2457   1137      0    -13    122       C  
ATOM   1435  CD2 LEU A 171      33.425  63.665  53.341  1.00 14.65           C  
ANISOU 1435  CD2 LEU A 171     1552   2167   1847    169    302    -78       C  
ATOM   1436  N   ARG A 172      31.719  64.496  58.334  1.00 10.84           N  
ANISOU 1436  N   ARG A 172     1381   1475   1264     21    167    -97       N  
ATOM   1437  CA  ARG A 172      31.669  65.303  59.526  1.00  9.84           C  
ANISOU 1437  CA  ARG A 172     1087   1426   1228    187     42    -36       C  
ATOM   1438  C   ARG A 172      32.787  64.868  60.479  1.00 10.86           C  
ANISOU 1438  C   ARG A 172     1230   1500   1395    178    -45    108       C  
ATOM   1439  O   ARG A 172      33.477  65.684  61.087  1.00 10.89           O  
ANISOU 1439  O   ARG A 172     1138   1565   1437     67    -96    257       O  
ATOM   1440  CB  ARG A 172      30.284  65.164  60.169  1.00 11.13           C  
ANISOU 1440  CB  ARG A 172     1159   1630   1438     91    164   -132       C  
ATOM   1441  CG  ARG A 172      30.170  65.758  61.566  1.00 11.69           C  
ANISOU 1441  CG  ARG A 172     1250   1657   1534     41    287   -212       C  
ATOM   1442  CD  ARG A 172      28.725  65.947  61.979  1.00 12.38           C  
ANISOU 1442  CD  ARG A 172     1283   1764   1656    -11    382   -165       C  
ATOM   1443  NE  ARG A 172      27.881  64.771  62.079  1.00 11.54           N  
ANISOU 1443  NE  ARG A 172     1212   1671   1500     55    172    -79       N  
ATOM   1444  CZ  ARG A 172      27.802  63.897  63.079  1.00 12.73           C  
ANISOU 1444  CZ  ARG A 172     1670   1415   1753    124   -145    -19       C  
ATOM   1445  NH1 ARG A 172      28.569  64.023  64.165  1.00 10.96           N  
ANISOU 1445  NH1 ARG A 172     1448   1226   1490    425    127   -295       N  
ATOM   1446  NH2 ARG A 172      26.950  62.873  63.017  1.00 12.40           N  
ANISOU 1446  NH2 ARG A 172     1602   1398   1710    151    -26    -26       N  
ATOM   1447  N   LEU A 173      33.007  63.568  60.597  1.00 11.31           N  
ANISOU 1447  N   LEU A 173     1383   1513   1403    109    -66    270       N  
ATOM   1448  CA  LEU A 173      34.066  63.051  61.470  1.00 10.95           C  
ANISOU 1448  CA  LEU A 173     1290   1433   1438     43    -31    282       C  
ATOM   1449  C   LEU A 173      35.437  63.336  60.843  1.00 10.67           C  
ANISOU 1449  C   LEU A 173     1331   1178   1547    170    174    -95       C  
ATOM   1450  O   LEU A 173      36.347  63.858  61.509  1.00 11.08           O  
ANISOU 1450  O   LEU A 173     1337   1465   1409     -8    282   -115       O  
ATOM   1451  CB  LEU A 173      33.841  61.560  61.706  1.00 10.51           C  
ANISOU 1451  CB  LEU A 173     1383   1366   1244     92    -54    117       C  
ATOM   1452  CG  LEU A 173      34.952  60.811  62.463  1.00 10.79           C  
ANISOU 1452  CG  LEU A 173     1367   1378   1354    212     11     88       C  
ATOM   1453  CD1 LEU A 173      35.260  61.472  63.793  1.00 12.73           C  
ANISOU 1453  CD1 LEU A 173     1784   1735   1317    118   -239    152       C  
ATOM   1454  CD2 LEU A 173      34.540  59.352  62.625  1.00 13.80           C  
ANISOU 1454  CD2 LEU A 173     1996   1420   1828     86   -242    318       C  
ATOM   1455  N   ALA A 174      35.618  62.997  59.571  1.00 11.19           N  
ANISOU 1455  N   ALA A 174     1519   1247   1487     25     86    -45       N  
ATOM   1456  CA  ALA A 174      36.931  63.219  58.932  1.00 11.91           C  
ANISOU 1456  CA  ALA A 174     1641   1240   1645    168    355   -403       C  
ATOM   1457  C   ALA A 174      37.382  64.662  58.977  1.00 10.41           C  
ANISOU 1457  C   ALA A 174     1280   1295   1381    145    179    -87       C  
ATOM   1458  O   ALA A 174      38.574  64.964  59.076  1.00 12.81           O  
ANISOU 1458  O   ALA A 174     1323   1761   1782     33    -68    120       O  
ATOM   1459  CB  ALA A 174      36.880  62.760  57.479  1.00 11.53           C  
ANISOU 1459  CB  ALA A 174     1371   1525   1486   -169     45   -139       C  
ATOM   1460  N   LYS A 175      36.416  65.581  58.882  1.00 11.29           N  
ANISOU 1460  N   LYS A 175     1451   1273   1568    166   -238    139       N  
ATOM   1461  CA  LYS A 175      36.763  66.993  58.966  1.00 11.14           C  
ANISOU 1461  CA  LYS A 175     1481   1271   1482    137     -8    225       C  
ATOM   1462  C   LYS A 175      37.503  67.320  60.260  1.00 12.03           C  
ANISOU 1462  C   LYS A 175     1777   1307   1488    -73     53     57       C  
ATOM   1463  O   LYS A 175      38.531  68.032  60.188  1.00 12.39           O  
ANISOU 1463  O   LYS A 175     1417   1701   1590     42     69     87       O  
ATOM   1464  CB  LYS A 175      35.499  67.857  58.827  1.00 12.38           C  
ANISOU 1464  CB  LYS A 175     1438   1281   1985    199    145   -262       C  
ATOM   1465  CG  LYS A 175      35.685  69.361  58.950  1.00 12.84           C  
ANISOU 1465  CG  LYS A 175     1722   1278   1876    199    369   -331       C  
ATOM   1466  CD  LYS A 175      34.318  70.046  58.843  1.00 13.31           C  
ANISOU 1466  CD  LYS A 175     1897   1284   1875    326     91   -272       C  
ATOM   1467  CE  LYS A 175      34.401  71.576  58.836  1.00 13.79           C  
ANISOU 1467  CE  LYS A 175     2086   1295   1857    251   -558   -267       C  
ATOM   1468  NZ  LYS A 175      35.063  72.086  60.086  1.00 13.15           N  
ANISOU 1468  NZ  LYS A 175     1591   1717   1689     37   -297   -217       N  
ATOM   1469  N   ASP A 176      37.016  66.839  61.417  1.00 11.42           N  
ANISOU 1469  N   ASP A 176     1699   1212   1427     24     -2     49       N  
ATOM   1470  CA  ASP A 176      37.669  67.196  62.690  1.00 11.32           C  
ANISOU 1470  CA  ASP A 176     1351   1471   1480     -6     68     -5       C  
ATOM   1471  C   ASP A 176      39.011  66.483  62.843  1.00 12.28           C  
ANISOU 1471  C   ASP A 176     1454   1388   1823     51    -16   -141       C  
ATOM   1472  O   ASP A 176      39.962  67.041  63.389  1.00 12.05           O  
ANISOU 1472  O   ASP A 176     1513   1480   1586    134   -200    -39       O  
ATOM   1473  CB  ASP A 176      36.754  66.867  63.897  1.00 12.64           C  
ANISOU 1473  CB  ASP A 176     1894   1405   1503    103    360   -123       C  
ATOM   1474  CG  ASP A 176      35.645  67.885  64.076  1.00 13.30           C  
ANISOU 1474  CG  ASP A 176     1794   1454   1807     61    419   -152       C  
ATOM   1475  OD1 ASP A 176      35.744  69.044  63.626  1.00 13.15           O  
ANISOU 1475  OD1 ASP A 176     1561   1641   1796    168     22    157       O  
ATOM   1476  OD2 ASP A 176      34.607  67.591  64.685  1.00 13.97           O  
ANISOU 1476  OD2 ASP A 176     1700   1777   1830      0    312    -80       O  
ATOM   1477  N   LEU A 177      39.067  65.232  62.348  1.00 12.30           N  
ANISOU 1477  N   LEU A 177     1583   1462   1628     -9    360   -202       N  
ATOM   1478  CA  LEU A 177      40.305  64.488  62.451  1.00 11.63           C  
ANISOU 1478  CA  LEU A 177     1564   1303   1553    -67    382   -145       C  
ATOM   1479  C   LEU A 177      41.410  65.192  61.651  1.00 12.12           C  
ANISOU 1479  C   LEU A 177     1520   1430   1657    -51    289     83       C  
ATOM   1480  O   LEU A 177      42.529  65.336  62.129  1.00 13.20           O  
ANISOU 1480  O   LEU A 177     1546   1622   1848   -123    220    128       O  
ATOM   1481  CB  LEU A 177      40.160  63.080  61.889  1.00 10.86           C  
ANISOU 1481  CB  LEU A 177     1253   1415   1457    -56    -20   -211       C  
ATOM   1482  CG  LEU A 177      39.109  62.197  62.572  1.00 11.61           C  
ANISOU 1482  CG  LEU A 177     1731   1316   1364   -148     47   -109       C  
ATOM   1483  CD1 LEU A 177      39.123  60.827  61.899  1.00 10.88           C  
ANISOU 1483  CD1 LEU A 177     1302   1254   1579    107     57   -110       C  
ATOM   1484  CD2 LEU A 177      39.351  62.157  64.065  1.00 13.63           C  
ANISOU 1484  CD2 LEU A 177     1929   1859   1392   -232    -64    -88       C  
ATOM   1485  N   ALA A 178      41.061  65.580  60.433  1.00 12.12           N  
ANISOU 1485  N   ALA A 178     1634   1490   1482     30    384   -104       N  
ATOM   1486  CA  ALA A 178      42.046  66.205  59.554  1.00 11.86           C  
ANISOU 1486  CA  ALA A 178     1510   1637   1360    -58    280   -170       C  
ATOM   1487  C   ALA A 178      42.462  67.589  60.056  1.00 12.91           C  
ANISOU 1487  C   ALA A 178     1340   1666   1901    -80    226   -239       C  
ATOM   1488  O   ALA A 178      43.648  67.948  60.059  1.00 14.26           O  
ANISOU 1488  O   ALA A 178     1366   2001   2051   -200    222   -174       O  
ATOM   1489  CB  ALA A 178      41.475  66.302  58.133  1.00 11.74           C  
ANISOU 1489  CB  ALA A 178     1176   1782   1503    -22    213     41       C  
ATOM   1490  N   GLU A 179      41.499  68.397  60.472  1.00 11.45           N  
ANISOU 1490  N   GLU A 179     1415   1489   1444     -8    103    -15       N  
ATOM   1491  CA  GLU A 179      41.731  69.797  60.820  1.00 12.45           C  
ANISOU 1491  CA  GLU A 179     1714   1427   1589     64   -195     86       C  
ATOM   1492  C   GLU A 179      42.460  69.974  62.144  1.00 12.14           C  
ANISOU 1492  C   GLU A 179     1651   1469   1493     85    -60    -27       C  
ATOM   1493  O   GLU A 179      43.182  70.954  62.344  1.00 15.06           O  
ANISOU 1493  O   GLU A 179     2031   2108   1584   -503   -119     75       O  
ATOM   1494  CB  GLU A 179      40.371  70.523  60.869  1.00 12.23           C  
ANISOU 1494  CB  GLU A 179     1748   1404   1496    103    -66    201       C  
ATOM   1495  CG  GLU A 179      39.902  70.837  59.446  1.00 12.59           C  
ANISOU 1495  CG  GLU A 179     1679   1642   1464    170    -89     65       C  
ATOM   1496  CD  GLU A 179      38.502  71.397  59.377  1.00 12.19           C  
ANISOU 1496  CD  GLU A 179     1622   1651   1359    117    -30     34       C  
ATOM   1497  OE1 GLU A 179      37.850  71.635  60.433  1.00 12.81           O  
ANISOU 1497  OE1 GLU A 179     1838   1539   1489     13    186     63       O  
ATOM   1498  OE2 GLU A 179      38.065  71.610  58.226  1.00 12.67           O  
ANISOU 1498  OE2 GLU A 179     1552   1832   1430    -12   -107     90       O  
ATOM   1499  N   ASN A 180      42.285  69.012  63.066  1.00 12.17           N  
ANISOU 1499  N   ASN A 180     1407   1735   1483    130     13    106       N  
ATOM   1500  CA  ASN A 180      42.892  69.185  64.398  1.00 12.31           C  
ANISOU 1500  CA  ASN A 180     1477   1596   1605     46   -121    106       C  
ATOM   1501  C   ASN A 180      44.261  68.525  64.516  1.00 12.42           C  
ANISOU 1501  C   ASN A 180     1398   1656   1666      1   -111    -17       C  
ATOM   1502  O   ASN A 180      44.842  68.575  65.603  1.00 13.11           O  
ANISOU 1502  O   ASN A 180     1413   1800   1769    -96   -202    113       O  
ATOM   1503  CB  ASN A 180      41.962  68.593  65.471  1.00 12.14           C  
ANISOU 1503  CB  ASN A 180     1476   1753   1383     76    -95    -85       C  
ATOM   1504  CG  ASN A 180      42.339  69.101  66.856  1.00 12.28           C  
ANISOU 1504  CG  ASN A 180     1560   1598   1508     61   -305    -91       C  
ATOM   1505  OD1 ASN A 180      42.496  70.314  67.008  1.00 13.85           O  
ANISOU 1505  OD1 ASN A 180     1805   1612   1844     60    -49   -232       O  
ATOM   1506  ND2 ASN A 180      42.462  68.220  67.829  1.00 13.04           N  
ANISOU 1506  ND2 ASN A 180     1491   1950   1515   -318   -305    124       N  
ATOM   1507  N   ASN A 181      44.753  67.910  63.438  1.00 13.52           N  
ANISOU 1507  N   ASN A 181     1681   1521   1937    -84    114   -147       N  
ATOM   1508  CA  ASN A 181      45.985  67.126  63.539  1.00 13.95           C  
ANISOU 1508  CA  ASN A 181     1712   1745   1843      5    228    -78       C  
ATOM   1509  C   ASN A 181      46.874  67.393  62.335  1.00 14.31           C  
ANISOU 1509  C   ASN A 181     1739   1852   1848   -104    202    -16       C  
ATOM   1510  O   ASN A 181      46.605  66.940  61.227  1.00 13.67           O  
ANISOU 1510  O   ASN A 181     1595   1952   1647   -246    -12    388       O  
ATOM   1511  CB  ASN A 181      45.658  65.623  63.645  1.00 13.19           C  
ANISOU 1511  CB  ASN A 181     1898   1690   1422    150    287    -38       C  
ATOM   1512  CG  ASN A 181      44.918  65.297  64.945  1.00 14.38           C  
ANISOU 1512  CG  ASN A 181     1734   2272   1457   -143    197     22       C  
ATOM   1513  OD1 ASN A 181      45.549  65.235  66.016  1.00 14.54           O  
ANISOU 1513  OD1 ASN A 181     1897   2135   1494     65    142    280       O  
ATOM   1514  ND2 ASN A 181      43.599  65.084  64.821  1.00 14.31           N  
ANISOU 1514  ND2 ASN A 181     1686   1768   1985     31    182     96       N  
ATOM   1515  N   LYS A 182      47.961  68.132  62.582  1.00 16.41           N  
ANISOU 1515  N   LYS A 182     2013   2350   1872   -452    364   -365       N  
ATOM   1516  CA  LYS A 182      48.925  68.487  61.558  1.00 16.60           C  
ANISOU 1516  CA  LYS A 182     1752   2415   2140   -217    445   -300       C  
ATOM   1517  C   LYS A 182      49.430  67.257  60.818  1.00 15.21           C  
ANISOU 1517  C   LYS A 182     1467   2348   1964    -98    124   -201       C  
ATOM   1518  O   LYS A 182      49.946  66.309  61.429  1.00 16.90           O  
ANISOU 1518  O   LYS A 182     1909   2203   2310   -333   -154    -30       O  
ATOM   1519  CB  LYS A 182      50.101  69.243  62.199  1.00 18.28           C  
ANISOU 1519  CB  LYS A 182     1822   2580   2545   -328    578   -642       C  
ATOM   1520  CG  LYS A 182      51.117  69.672  61.143  1.00 19.64           C  
ANISOU 1520  CG  LYS A 182     1921   2873   2671   -483    611   -499       C  
ATOM   1521  CD  LYS A 182      52.249  70.469  61.765  1.00 24.06           C  
ANISOU 1521  CD  LYS A 182     1945   4003   3193   -874    228   -188       C  
ATOM   1522  CE  LYS A 182      52.951  69.709  62.887  1.00 31.35           C  
ANISOU 1522  CE  LYS A 182     3490   4806   3616  -1046   -647    122       C  
ATOM   1523  NZ  LYS A 182      54.238  70.331  63.329  1.00 39.04           N  
ANISOU 1523  NZ  LYS A 182     3632   6151   5052  -1208  -1548    583       N  
ATOM   1524  N   GLY A 183      49.309  67.270  59.477  1.00 14.88           N  
ANISOU 1524  N   GLY A 183     1430   2288   1933   -352    271   -159       N  
ATOM   1525  CA  GLY A 183      49.869  66.126  58.771  1.00 16.87           C  
ANISOU 1525  CA  GLY A 183     2053   2265   2091   -459    748   -165       C  
ATOM   1526  C   GLY A 183      48.867  64.995  58.622  1.00 14.66           C  
ANISOU 1526  C   GLY A 183     1538   2010   2021    -34    233      3       C  
ATOM   1527  O   GLY A 183      49.164  64.072  57.840  1.00 15.85           O  
ANISOU 1527  O   GLY A 183     1471   2460   2091    -19      7   -368       O  
ATOM   1528  N   ALA A 184      47.733  65.037  59.326  1.00 14.00           N  
ANISOU 1528  N   ALA A 184     1305   1970   2045     54     42     59       N  
ATOM   1529  CA  ALA A 184      46.823  63.890  59.267  1.00 12.65           C  
ANISOU 1529  CA  ALA A 184     1363   1750   1695    186    228    -46       C  
ATOM   1530  C   ALA A 184      46.268  63.676  57.862  1.00 12.79           C  
ANISOU 1530  C   ALA A 184     1499   1680   1682    210    244    -89       C  
ATOM   1531  O   ALA A 184      45.877  64.633  57.215  1.00 12.55           O  
ANISOU 1531  O   ALA A 184     1599   1609   1559   -124    313     74       O  
ATOM   1532  CB  ALA A 184      45.656  64.078  60.238  1.00 13.53           C  
ANISOU 1532  CB  ALA A 184     1598   1767   1775    110    414   -176       C  
ATOM   1533  N   ARG A 185      46.189  62.449  57.416  1.00 13.04           N  
ANISOU 1533  N   ARG A 185     1431   1642   1883     63    137    -48       N  
ATOM   1534  CA  ARG A 185      45.604  61.995  56.159  1.00 12.47           C  
ANISOU 1534  CA  ARG A 185     1267   1672   1798     28    300    -77       C  
ATOM   1535  C   ARG A 185      44.664  60.849  56.533  1.00 12.12           C  
ANISOU 1535  C   ARG A 185     1319   1527   1759    107    399   -154       C  
ATOM   1536  O   ARG A 185      45.096  59.827  57.064  1.00 12.50           O  
ANISOU 1536  O   ARG A 185     1307   1605   1838    -21     68   -104       O  
ATOM   1537  CB  ARG A 185      46.681  61.565  55.158  1.00 13.38           C  
ANISOU 1537  CB  ARG A 185     1288   1831   1965     73    417    -19       C  
ATOM   1538  CG  ARG A 185      47.554  62.770  54.738  1.00 14.94           C  
ANISOU 1538  CG  ARG A 185     1752   2073   1853   -112    497    211       C  
ATOM   1539  CD  ARG A 185      46.720  63.746  53.936  1.00 16.65           C  
ANISOU 1539  CD  ARG A 185     2390   2082   1854   -290   -142    171       C  
ATOM   1540  NE  ARG A 185      47.430  64.850  53.272  1.00 15.19           N  
ANISOU 1540  NE  ARG A 185     2009   2109   1653    -43     59    127       N  
ATOM   1541  CZ  ARG A 185      47.479  66.073  53.789  1.00 15.77           C  
ANISOU 1541  CZ  ARG A 185     1774   2322   1894   -610    142   -116       C  
ATOM   1542  NH1 ARG A 185      46.889  66.291  54.971  1.00 13.33           N  
ANISOU 1542  NH1 ARG A 185     1352   1993   1719     67   -173    132       N  
ATOM   1543  NH2 ARG A 185      48.108  67.061  53.160  1.00 15.48           N  
ANISOU 1543  NH2 ARG A 185     1805   2095   1984     87    -96    590       N  
ATOM   1544  N   VAL A 186      43.392  61.099  56.286  1.00 11.03           N  
ANISOU 1544  N   VAL A 186     1355   1459   1378    -57    185    -81       N  
ATOM   1545  CA  VAL A 186      42.336  60.200  56.699  1.00 11.32           C  
ANISOU 1545  CA  VAL A 186     1427   1409   1467    -83    279   -165       C  
ATOM   1546  C   VAL A 186      41.846  59.369  55.524  1.00 10.76           C  
ANISOU 1546  C   VAL A 186     1228   1403   1459     59    171   -117       C  
ATOM   1547  O   VAL A 186      41.401  59.940  54.523  1.00 12.98           O  
ANISOU 1547  O   VAL A 186     1528   1675   1730    247   -110    -54       O  
ATOM   1548  CB  VAL A 186      41.159  61.006  57.271  1.00 11.14           C  
ANISOU 1548  CB  VAL A 186     1390   1298   1546   -100    253   -156       C  
ATOM   1549  CG1 VAL A 186      40.186  60.065  57.983  1.00 11.30           C  
ANISOU 1549  CG1 VAL A 186     1311   1571   1410      1    141    176       C  
ATOM   1550  CG2 VAL A 186      41.644  62.066  58.247  1.00 11.38           C  
ANISOU 1550  CG2 VAL A 186     1449   1428   1447    137    -46   -174       C  
ATOM   1551  N   LEU A 187      41.951  58.047  55.645  1.00 11.32           N  
ANISOU 1551  N   LEU A 187     1424   1366   1512    -10    248   -165       N  
ATOM   1552  CA  LEU A 187      41.318  57.178  54.637  1.00 11.32           C  
ANISOU 1552  CA  LEU A 187     1215   1396   1691    104      8   -127       C  
ATOM   1553  C   LEU A 187      39.886  56.924  55.121  1.00 11.75           C  
ANISOU 1553  C   LEU A 187     1245   1439   1783    125     37    174       C  
ATOM   1554  O   LEU A 187      39.711  56.478  56.256  1.00 12.12           O  
ANISOU 1554  O   LEU A 187     1252   1608   1747     74    -86    209       O  
ATOM   1555  CB  LEU A 187      42.093  55.887  54.437  1.00 12.02           C  
ANISOU 1555  CB  LEU A 187     1453   1498   1614    205     15   -311       C  
ATOM   1556  CG  LEU A 187      41.463  54.780  53.574  1.00 10.92           C  
ANISOU 1556  CG  LEU A 187     1359   1364   1425    284   -277    -25       C  
ATOM   1557  CD1 LEU A 187      41.226  55.270  52.144  1.00 12.66           C  
ANISOU 1557  CD1 LEU A 187     1747   1668   1397     68    -64    136       C  
ATOM   1558  CD2 LEU A 187      42.351  53.550  53.557  1.00 12.35           C  
ANISOU 1558  CD2 LEU A 187     1429   1536   1726    410   -359   -353       C  
ATOM   1559  N   VAL A 188      38.898  57.233  54.299  1.00 10.71           N  
ANISOU 1559  N   VAL A 188     1187   1462   1420   -134     80     23       N  
ATOM   1560  CA  VAL A 188      37.485  57.093  54.682  1.00 11.83           C  
ANISOU 1560  CA  VAL A 188     1178   1709   1607   -111     72    -89       C  
ATOM   1561  C   VAL A 188      36.919  55.980  53.805  1.00 10.89           C  
ANISOU 1561  C   VAL A 188     1224   1680   1235   -140   -286    258       C  
ATOM   1562  O   VAL A 188      37.075  56.106  52.579  1.00 13.48           O  
ANISOU 1562  O   VAL A 188     1666   2161   1296   -614    -28    247       O  
ATOM   1563  CB  VAL A 188      36.677  58.386  54.535  1.00 12.20           C  
ANISOU 1563  CB  VAL A 188     1092   1784   1759   -112    -14     58       C  
ATOM   1564  CG1 VAL A 188      35.233  58.193  55.023  1.00 14.86           C  
ANISOU 1564  CG1 VAL A 188     1240   2329   2079    130    313    550       C  
ATOM   1565  CG2 VAL A 188      37.283  59.538  55.293  1.00 12.74           C  
ANISOU 1565  CG2 VAL A 188     1651   1832   1358    143     56   -216       C  
ATOM   1566  N   VAL A 189      36.330  54.953  54.405  1.00 11.73           N  
ANISOU 1566  N   VAL A 189     1542   1757   1157   -283    155     10       N  
ATOM   1567  CA  VAL A 189      35.732  53.901  53.570  1.00 12.09           C  
ANISOU 1567  CA  VAL A 189     1273   1639   1681    -84    104   -170       C  
ATOM   1568  C   VAL A 189      34.301  53.610  54.020  1.00 11.55           C  
ANISOU 1568  C   VAL A 189     1240   1612   1536     13     54     -2       C  
ATOM   1569  O   VAL A 189      34.102  53.235  55.177  1.00 13.74           O  
ANISOU 1569  O   VAL A 189     1351   2254   1613   -149    -32    230       O  
ATOM   1570  CB  VAL A 189      36.552  52.599  53.598  1.00 13.50           C  
ANISOU 1570  CB  VAL A 189     1275   1775   2080     11    222    -88       C  
ATOM   1571  CG1 VAL A 189      35.958  51.521  52.679  1.00 15.45           C  
ANISOU 1571  CG1 VAL A 189     1530   1443   2898    174   -322   -102       C  
ATOM   1572  CG2 VAL A 189      37.992  52.841  53.192  1.00 14.21           C  
ANISOU 1572  CG2 VAL A 189     1121   2054   2225     60    -67    594       C  
ATOM   1573  N   CYS A 190      33.347  53.772  53.100  1.00 11.15           N  
ANISOU 1573  N   CYS A 190     1351   1436   1449   -166    -31   -191       N  
ATOM   1574  CA  CYS A 190      31.970  53.352  53.332  1.00 11.67           C  
ANISOU 1574  CA  CYS A 190     1300   1669   1466    -89     38   -271       C  
ATOM   1575  C   CYS A 190      31.714  52.113  52.476  1.00 10.70           C  
ANISOU 1575  C   CYS A 190     1164   1646   1254   -214    104   -163       C  
ATOM   1576  O   CYS A 190      32.006  52.176  51.286  1.00 12.89           O  
ANISOU 1576  O   CYS A 190     1764   1898   1237   -176    147   -134       O  
ATOM   1577  CB  CYS A 190      30.933  54.406  52.964  1.00 13.03           C  
ANISOU 1577  CB  CYS A 190     1467   1878   1607    127     26   -335       C  
ATOM   1578  SG  CYS A 190      31.031  55.864  54.036  1.00 12.94           S  
ANISOU 1578  SG  CYS A 190     1878   1559   1480     17    -12    -67       S  
ATOM   1579  N   SER A 191      31.225  51.018  53.046  1.00 10.96           N  
ANISOU 1579  N   SER A 191     1248   1486   1429     78    -97     81       N  
ATOM   1580  CA  SER A 191      31.101  49.790  52.272  1.00 12.09           C  
ANISOU 1580  CA  SER A 191     1316   1493   1784      6    265    -67       C  
ATOM   1581  C   SER A 191      29.798  49.123  52.728  1.00 12.22           C  
ANISOU 1581  C   SER A 191     1405   1659   1577   -128    172     43       C  
ATOM   1582  O   SER A 191      29.665  48.796  53.913  1.00 12.57           O  
ANISOU 1582  O   SER A 191     1718   1568   1489   -197    210   -130       O  
ATOM   1583  CB  SER A 191      32.310  48.875  52.490  1.00 11.87           C  
ANISOU 1583  CB  SER A 191     1421   1459   1628     14     79    -12       C  
ATOM   1584  OG  SER A 191      32.138  47.640  51.782  1.00 12.79           O  
ANISOU 1584  OG  SER A 191     1779   1466   1617    109    155    -61       O  
ATOM   1585  N   GLU A 192      28.878  48.966  51.786  1.00 11.15           N  
ANISOU 1585  N   GLU A 192     1251   1399   1587    146    208    -12       N  
ATOM   1586  CA  GLU A 192      27.513  48.567  52.075  1.00 11.14           C  
ANISOU 1586  CA  GLU A 192     1308   1268   1656     49    291   -221       C  
ATOM   1587  C   GLU A 192      27.113  47.361  51.226  1.00 11.33           C  
ANISOU 1587  C   GLU A 192     1638   1297   1371     12    296   -154       C  
ATOM   1588  O   GLU A 192      27.260  47.394  50.018  1.00 11.67           O  
ANISOU 1588  O   GLU A 192     1234   1879   1322    -71     34    -24       O  
ATOM   1589  CB  GLU A 192      26.516  49.723  51.881  1.00 11.03           C  
ANISOU 1589  CB  GLU A 192     1249   1417   1525    112    272   -288       C  
ATOM   1590  CG  GLU A 192      26.860  50.921  52.782  1.00 10.78           C  
ANISOU 1590  CG  GLU A 192     1425   1197   1475    -24    441   -109       C  
ATOM   1591  CD  GLU A 192      26.464  50.724  54.243  1.00 10.69           C  
ANISOU 1591  CD  GLU A 192     1450   1353   1260    232     13      2       C  
ATOM   1592  OE1 GLU A 192      26.151  49.579  54.660  1.00 11.32           O  
ANISOU 1592  OE1 GLU A 192     1510   1525   1266     16     70     87       O  
ATOM   1593  OE2 GLU A 192      26.454  51.749  54.970  1.00 13.24           O  
ANISOU 1593  OE2 GLU A 192     2073   1614   1342    -21     54   -225       O  
ATOM   1594  N   VAL A 193      26.630  46.315  51.897  1.00 11.19           N  
ANISOU 1594  N   VAL A 193     1608   1167   1475    109    188   -103       N  
ATOM   1595  CA  VAL A 193      26.300  45.045  51.250  1.00 10.77           C  
ANISOU 1595  CA  VAL A 193     1233   1271   1590    110    164   -217       C  
ATOM   1596  C   VAL A 193      24.934  44.580  51.701  1.00 10.71           C  
ANISOU 1596  C   VAL A 193     1194   1482   1393    171    148   -131       C  
ATOM   1597  O   VAL A 193      24.755  44.342  52.918  1.00 13.09           O  
ANISOU 1597  O   VAL A 193     1697   1862   1413    150    303   -121       O  
ATOM   1598  CB  VAL A 193      27.394  43.998  51.550  1.00 11.84           C  
ANISOU 1598  CB  VAL A 193     1186   1272   2041    140    223   -295       C  
ATOM   1599  CG1 VAL A 193      27.060  42.661  50.884  1.00 12.30           C  
ANISOU 1599  CG1 VAL A 193     1544   1183   1945    116    -84   -117       C  
ATOM   1600  CG2 VAL A 193      28.768  44.455  51.051  1.00 13.43           C  
ANISOU 1600  CG2 VAL A 193     1271   1431   2398     96    440   -484       C  
ATOM   1601  N   THR A 194      23.984  44.436  50.772  1.00 12.27           N  
ANISOU 1601  N   THR A 194     1327   1646   1688    -12    -27   -159       N  
ATOM   1602  CA  THR A 194      22.589  44.171  51.115  1.00 13.18           C  
ANISOU 1602  CA  THR A 194     1247   1755   2005    140    -65     32       C  
ATOM   1603  C   THR A 194      22.311  42.745  51.539  1.00 13.02           C  
ANISOU 1603  C   THR A 194     1106   1809   2033      0   -190     57       C  
ATOM   1604  O   THR A 194      21.153  42.371  51.793  1.00 12.56           O  
ANISOU 1604  O   THR A 194     1099   2064   1610    -38   -201    -43       O  
ATOM   1605  CB  THR A 194      21.663  44.517  49.921  1.00 13.08           C  
ANISOU 1605  CB  THR A 194     1359   1635   1978    267    -92   -105       C  
ATOM   1606  OG1 THR A 194      22.112  43.826  48.745  1.00 15.51           O  
ANISOU 1606  OG1 THR A 194     1695   2176   2021    -19    106   -334       O  
ATOM   1607  CG2 THR A 194      21.690  46.013  49.601  1.00 15.75           C  
ANISOU 1607  CG2 THR A 194     2373   1771   1841     49    -23    208       C  
ATOM   1608  N   ALA A 195      23.334  41.900  51.682  1.00 12.50           N  
ANISOU 1608  N   ALA A 195     1190   1670   1891     52    191     32       N  
ATOM   1609  CA  ALA A 195      23.086  40.530  52.155  1.00 14.07           C  
ANISOU 1609  CA  ALA A 195     1776   1656   1913     31    267     27       C  
ATOM   1610  C   ALA A 195      22.496  40.488  53.565  1.00 13.05           C  
ANISOU 1610  C   ALA A 195     1695   1542   1721     83     42     38       C  
ATOM   1611  O   ALA A 195      21.870  39.459  53.902  1.00 14.03           O  
ANISOU 1611  O   ALA A 195     1987   1687   1656   -126    117    -41       O  
ATOM   1612  CB  ALA A 195      24.348  39.689  52.140  1.00 15.05           C  
ANISOU 1612  CB  ALA A 195     2005   1521   2193    153    356    -31       C  
ATOM   1613  N   VAL A 196      22.663  41.511  54.394  1.00 13.62           N  
ANISOU 1613  N   VAL A 196     1807   1645   1724     20   -279     12       N  
ATOM   1614  CA  VAL A 196      22.054  41.400  55.743  1.00 14.98           C  
ANISOU 1614  CA  VAL A 196     2174   1874   1644    237   -270    -91       C  
ATOM   1615  C   VAL A 196      20.585  41.789  55.728  1.00 14.40           C  
ANISOU 1615  C   VAL A 196     2177   1630   1663    224    -72    -88       C  
ATOM   1616  O   VAL A 196      19.835  41.399  56.620  1.00 15.44           O  
ANISOU 1616  O   VAL A 196     2265   1793   1807    -33   -139     71       O  
ATOM   1617  CB  VAL A 196      22.815  42.226  56.786  1.00 19.32           C  
ANISOU 1617  CB  VAL A 196     2424   2977   1938   -228   -178   -549       C  
ATOM   1618  CG1 VAL A 196      22.481  41.772  58.201  1.00 26.71           C  
ANISOU 1618  CG1 VAL A 196     5161   3287   1701   -891    178  -1085       C  
ATOM   1619  CG2 VAL A 196      24.311  42.085  56.564  1.00 26.35           C  
ANISOU 1619  CG2 VAL A 196     2313   4237   3461   -258   -464   -694       C  
ATOM   1620  N   THR A 197      20.148  42.569  54.734  1.00 13.55           N  
ANISOU 1620  N   THR A 197     1869   1686   1595    -39   -249   -132       N  
ATOM   1621  CA  THR A 197      18.757  42.960  54.700  1.00 13.79           C  
ANISOU 1621  CA  THR A 197     1849   1592   1797    -75   -138    -88       C  
ATOM   1622  C   THR A 197      17.921  42.237  53.644  1.00 12.66           C  
ANISOU 1622  C   THR A 197     1536   1631   1644    -60     88   -100       C  
ATOM   1623  O   THR A 197      16.697  42.313  53.738  1.00 14.88           O  
ANISOU 1623  O   THR A 197     1528   1928   2197    130    -44   -243       O  
ATOM   1624  CB  THR A 197      18.593  44.461  54.338  1.00 15.18           C  
ANISOU 1624  CB  THR A 197     2288   1558   1920     63   -208   -151       C  
ATOM   1625  OG1 THR A 197      19.266  44.698  53.066  1.00 15.94           O  
ANISOU 1625  OG1 THR A 197     2371   1635   2049    106   -135    129       O  
ATOM   1626  CG2 THR A 197      19.204  45.397  55.348  1.00 17.68           C  
ANISOU 1626  CG2 THR A 197     2914   1639   2166   -186   -505   -120       C  
ATOM   1627  N   PHE A 198      18.491  41.591  52.651  1.00 12.35           N  
ANISOU 1627  N   PHE A 198     1855   1235   1601    -64    219     85       N  
ATOM   1628  CA  PHE A 198      17.693  40.864  51.669  1.00 13.88           C  
ANISOU 1628  CA  PHE A 198     1892   1804   1578   -304    408   -138       C  
ATOM   1629  C   PHE A 198      16.756  39.881  52.367  1.00 12.41           C  
ANISOU 1629  C   PHE A 198     1479   1600   1637    -45    205     23       C  
ATOM   1630  O   PHE A 198      17.218  39.094  53.210  1.00 13.23           O  
ANISOU 1630  O   PHE A 198     1744   1531   1750     -9      5    -30       O  
ATOM   1631  CB  PHE A 198      18.618  40.091  50.715  1.00 12.86           C  
ANISOU 1631  CB  PHE A 198     1525   1944   1418   -168    134    -91       C  
ATOM   1632  CG  PHE A 198      17.871  39.322  49.612  1.00 14.27           C  
ANISOU 1632  CG  PHE A 198     2002   1925   1494   -240     10   -152       C  
ATOM   1633  CD1 PHE A 198      17.360  38.036  49.760  1.00 15.35           C  
ANISOU 1633  CD1 PHE A 198     2502   1746   1585   -152    137   -333       C  
ATOM   1634  CD2 PHE A 198      17.670  39.951  48.390  1.00 13.81           C  
ANISOU 1634  CD2 PHE A 198     1563   1891   1794     84   -339    -38       C  
ATOM   1635  CE1 PHE A 198      16.638  37.383  48.787  1.00 15.44           C  
ANISOU 1635  CE1 PHE A 198     2284   1631   1951    -79   -248   -120       C  
ATOM   1636  CE2 PHE A 198      16.977  39.283  47.388  1.00 14.77           C  
ANISOU 1636  CE2 PHE A 198     2171   1626   1814    112   -428    -98       C  
ATOM   1637  CZ  PHE A 198      16.458  38.012  47.556  1.00 14.28           C  
ANISOU 1637  CZ  PHE A 198     1987   1594   1845    194    -89   -224       C  
ATOM   1638  N   ARG A 199      15.491  39.871  51.957  1.00 12.78           N  
ANISOU 1638  N   ARG A 199     1695   1535   1626   -190   -116   -211       N  
ATOM   1639  CA  ARG A 199      14.585  38.851  52.528  1.00 12.73           C  
ANISOU 1639  CA  ARG A 199     1489   1750   1599   -165   -125   -133       C  
ATOM   1640  C   ARG A 199      13.393  38.737  51.580  1.00 11.17           C  
ANISOU 1640  C   ARG A 199     1328   1521   1395    116     32   -268       C  
ATOM   1641  O   ARG A 199      13.237  39.582  50.692  1.00 13.43           O  
ANISOU 1641  O   ARG A 199     1729   1797   1578     69    -40    -28       O  
ATOM   1642  CB  ARG A 199      14.135  39.160  53.951  1.00 12.31           C  
ANISOU 1642  CB  ARG A 199     1562   1626   1490    -18   -271    -61       C  
ATOM   1643  CG  ARG A 199      13.353  40.448  54.147  1.00 13.02           C  
ANISOU 1643  CG  ARG A 199     1812   1659   1477     79   -253    -42       C  
ATOM   1644  CD  ARG A 199      13.092  40.763  55.639  1.00 13.07           C  
ANISOU 1644  CD  ARG A 199     1792   1674   1499      8   -157    -47       C  
ATOM   1645  NE  ARG A 199      14.386  41.021  56.294  1.00 13.60           N  
ANISOU 1645  NE  ARG A 199     2004   1595   1566   -111   -335    -48       N  
ATOM   1646  CZ  ARG A 199      15.050  40.157  57.067  1.00 13.91           C  
ANISOU 1646  CZ  ARG A 199     2082   1591   1611   -130   -460    -77       C  
ATOM   1647  NH1 ARG A 199      14.574  38.950  57.350  1.00 12.88           N  
ANISOU 1647  NH1 ARG A 199     1502   1649   1744    136    227     46       N  
ATOM   1648  NH2 ARG A 199      16.232  40.527  57.584  1.00 14.06           N  
ANISOU 1648  NH2 ARG A 199     1545   1647   2148    224   -138   -326       N  
ATOM   1649  N   GLY A 200      12.595  37.702  51.775  1.00 13.30           N  
ANISOU 1649  N   GLY A 200     1677   1865   1511   -276   -223   -149       N  
ATOM   1650  CA  GLY A 200      11.471  37.507  50.863  1.00 13.20           C  
ANISOU 1650  CA  GLY A 200     1743   1710   1561   -168   -360     27       C  
ATOM   1651  C   GLY A 200      10.353  38.488  51.183  1.00 14.32           C  
ANISOU 1651  C   GLY A 200     1878   1831   1732    -69   -221    116       C  
ATOM   1652  O   GLY A 200      10.413  39.226  52.180  1.00 14.17           O  
ANISOU 1652  O   GLY A 200     1714   2005   1665    -15    -80     91       O  
ATOM   1653  N   PRO A 201       9.337  38.503  50.328  1.00 14.42           N  
ANISOU 1653  N   PRO A 201     1750   2044   1684     22   -139    102       N  
ATOM   1654  CA  PRO A 201       8.230  39.455  50.410  1.00 15.79           C  
ANISOU 1654  CA  PRO A 201     1703   2416   1879    142    107    145       C  
ATOM   1655  C   PRO A 201       7.089  38.966  51.312  1.00 17.35           C  
ANISOU 1655  C   PRO A 201     1923   2326   2341     10    264    330       C  
ATOM   1656  O   PRO A 201       6.795  37.778  51.385  1.00 20.12           O  
ANISOU 1656  O   PRO A 201     2060   2405   3180   -178   -266    582       O  
ATOM   1657  CB  PRO A 201       7.725  39.558  48.963  1.00 15.52           C  
ANISOU 1657  CB  PRO A 201     1481   2324   2092      0   -151    241       C  
ATOM   1658  CG  PRO A 201       8.030  38.225  48.380  1.00 15.67           C  
ANISOU 1658  CG  PRO A 201     1944   2052   1960   -307   -413    316       C  
ATOM   1659  CD  PRO A 201       9.204  37.632  49.148  1.00 15.63           C  
ANISOU 1659  CD  PRO A 201     1831   1956   2153   -100   -429   -118       C  
ATOM   1660  N   SER A 202       6.451  39.927  51.985  1.00 18.56           N  
ANISOU 1660  N   SER A 202     2385   2885   1783    -71    494     64       N  
ATOM   1661  CA  SER A 202       5.269  39.651  52.781  1.00 19.71           C  
ANISOU 1661  CA  SER A 202     2297   3204   1987     37    460    460       C  
ATOM   1662  C   SER A 202       4.241  40.752  52.571  1.00 20.65           C  
ANISOU 1662  C   SER A 202     2066   3180   2599   -106    220    338       C  
ATOM   1663  O   SER A 202       4.553  41.945  52.601  1.00 18.08           O  
ANISOU 1663  O   SER A 202     1859   3176   1834    -69    163    338       O  
ATOM   1664  CB  SER A 202       5.655  39.538  54.260  1.00 22.59           C  
ANISOU 1664  CB  SER A 202     2785   3874   1925    111    565    653       C  
ATOM   1665  OG  SER A 202       4.566  39.901  55.111  1.00 28.38           O  
ANISOU 1665  OG  SER A 202     2738   5859   2185   -367   1003    694       O  
ATOM   1666  N   ASP A 203       2.979  40.369  52.352  1.00 22.27           N  
ANISOU 1666  N   ASP A 203     2291   3293   2876   -297   -194    375       N  
ATOM   1667  CA  ASP A 203       2.079  41.455  51.942  1.00 23.69           C  
ANISOU 1667  CA  ASP A 203     2460   3614   2929    -99   -646    171       C  
ATOM   1668  C   ASP A 203       1.653  42.329  53.106  1.00 23.87           C  
ANISOU 1668  C   ASP A 203     2114   3838   3117     -6   -128    291       C  
ATOM   1669  O   ASP A 203       1.006  43.363  52.908  1.00 26.59           O  
ANISOU 1669  O   ASP A 203     2428   4032   3642    259   -355    145       O  
ATOM   1670  CB  ASP A 203       0.892  40.894  51.168  1.00 29.20           C  
ANISOU 1670  CB  ASP A 203     3122   4209   3764   -600  -1317    471       C  
ATOM   1671  CG  ASP A 203       0.084  39.868  51.929  1.00 34.90           C  
ANISOU 1671  CG  ASP A 203     4149   4720   4390  -1581  -1759    769       C  
ATOM   1672  OD1 ASP A 203       0.316  39.757  53.157  1.00 38.32           O  
ANISOU 1672  OD1 ASP A 203     5143   5441   3977  -2298   -925    453       O  
ATOM   1673  OD2 ASP A 203      -0.759  39.199  51.282  1.00 46.12           O  
ANISOU 1673  OD2 ASP A 203     5567   6369   5588  -2944  -2758   1199       O  
ATOM   1674  N   THR A 204       2.007  42.033  54.357  1.00 22.95           N  
ANISOU 1674  N   THR A 204     2033   3777   2909   -252    178    279       N  
ATOM   1675  CA  THR A 204       1.672  43.016  55.393  1.00 23.55           C  
ANISOU 1675  CA  THR A 204     2238   3622   3086   -156    405    354       C  
ATOM   1676  C   THR A 204       2.923  43.757  55.826  1.00 23.19           C  
ANISOU 1676  C   THR A 204     2190   3616   3007    -49    537    -16       C  
ATOM   1677  O   THR A 204       2.962  44.326  56.917  1.00 24.61           O  
ANISOU 1677  O   THR A 204     2526   3675   3152    -67    693   -180       O  
ATOM   1678  CB  THR A 204       1.074  42.365  56.647  1.00 25.23           C  
ANISOU 1678  CB  THR A 204     2867   3707   3011   -441    473    248       C  
ATOM   1679  OG1 THR A 204       1.998  41.338  57.047  1.00 26.10           O  
ANISOU 1679  OG1 THR A 204     3033   4580   2302   -168     55    414       O  
ATOM   1680  CG2 THR A 204      -0.231  41.699  56.321  1.00 25.45           C  
ANISOU 1680  CG2 THR A 204     2324   3481   3865    -74    909    100       C  
ATOM   1681  N   HIS A 205       3.984  43.737  55.018  1.00 22.03           N  
ANISOU 1681  N   HIS A 205     1976   3413   2980    224    386      7       N  
ATOM   1682  CA  HIS A 205       5.189  44.527  55.294  1.00 19.61           C  
ANISOU 1682  CA  HIS A 205     1941   3182   2327    330    280    302       C  
ATOM   1683  C   HIS A 205       5.712  45.128  53.991  1.00 18.72           C  
ANISOU 1683  C   HIS A 205     2241   2785   2087    412    133    161       C  
ATOM   1684  O   HIS A 205       6.793  44.800  53.491  1.00 16.12           O  
ANISOU 1684  O   HIS A 205     2141   2205   1780    122     64     98       O  
ATOM   1685  CB  HIS A 205       6.268  43.716  56.023  1.00 22.94           C  
ANISOU 1685  CB  HIS A 205     2700   3515   2502    267   -315    603       C  
ATOM   1686  CG  HIS A 205       5.772  43.072  57.284  1.00 24.01           C  
ANISOU 1686  CG  HIS A 205     2967   3649   2509    133   -183    526       C  
ATOM   1687  ND1 HIS A 205       5.259  41.794  57.287  1.00 26.15           N  
ANISOU 1687  ND1 HIS A 205     3320   3994   2621   -365    261    308       N  
ATOM   1688  CD2 HIS A 205       5.670  43.524  58.554  1.00 23.90           C  
ANISOU 1688  CD2 HIS A 205     2874   3681   2525    223   -208    495       C  
ATOM   1689  CE1 HIS A 205       4.881  41.465  58.525  1.00 27.53           C  
ANISOU 1689  CE1 HIS A 205     3568   4318   2573   -714    204    266       C  
ATOM   1690  NE2 HIS A 205       5.121  42.507  59.299  1.00 27.71           N  
ANISOU 1690  NE2 HIS A 205     3683   4245   2601   -566    189    261       N  
ATOM   1691  N   LEU A 206       4.910  46.038  53.442  1.00 18.41           N  
ANISOU 1691  N   LEU A 206     2063   2862   2069    281   -260    -63       N  
ATOM   1692  CA  LEU A 206       5.221  46.689  52.158  1.00 19.51           C  
ANISOU 1692  CA  LEU A 206     2371   2841   2202    -94   -632    151       C  
ATOM   1693  C   LEU A 206       6.430  47.603  52.286  1.00 19.99           C  
ANISOU 1693  C   LEU A 206     2411   3036   2147   -191   -423   -150       C  
ATOM   1694  O   LEU A 206       7.122  47.862  51.285  1.00 19.82           O  
ANISOU 1694  O   LEU A 206     2122   3370   2038   -129   -539   -214       O  
ATOM   1695  CB  LEU A 206       4.002  47.466  51.655  1.00 20.14           C  
ANISOU 1695  CB  LEU A 206     2362   2971   2317     75   -445    179       C  
ATOM   1696  CG  LEU A 206       2.837  46.549  51.269  1.00 20.15           C  
ANISOU 1696  CG  LEU A 206     1925   2901   2830    177   -213    433       C  
ATOM   1697  CD1 LEU A 206       1.684  47.407  50.762  1.00 23.20           C  
ANISOU 1697  CD1 LEU A 206     2354   3461   2999    300   -605    829       C  
ATOM   1698  CD2 LEU A 206       3.214  45.506  50.224  1.00 21.53           C  
ANISOU 1698  CD2 LEU A 206     3252   2440   2487   -148   -513    525       C  
ATOM   1699  N   ASP A 207       6.625  48.054  53.530  1.00 18.12           N  
ANISOU 1699  N   ASP A 207     2198   2548   2139    158   -334   -168       N  
ATOM   1700  CA  ASP A 207       7.836  48.870  53.758  1.00 17.22           C  
ANISOU 1700  CA  ASP A 207     2354   2217   1973    154   -271   -157       C  
ATOM   1701  C   ASP A 207       9.092  48.027  53.597  1.00 17.58           C  
ANISOU 1701  C   ASP A 207     2195   2237   2248     83   -246    212       C  
ATOM   1702  O   ASP A 207      10.058  48.474  52.960  1.00 18.36           O  
ANISOU 1702  O   ASP A 207     1991   1984   3001   -146   -380    255       O  
ATOM   1703  CB  ASP A 207       7.838  49.523  55.133  1.00 19.01           C  
ANISOU 1703  CB  ASP A 207     3000   2371   1851    304   -632    -57       C  
ATOM   1704  CG  ASP A 207       7.535  48.614  56.293  1.00 19.72           C  
ANISOU 1704  CG  ASP A 207     2718   2699   2075     70    238   -167       C  
ATOM   1705  OD1 ASP A 207       7.146  47.442  56.116  1.00 20.57           O  
ANISOU 1705  OD1 ASP A 207     2779   2846   2193   -170   -325     67       O  
ATOM   1706  OD2 ASP A 207       7.702  49.107  57.438  1.00 17.18           O  
ANISOU 1706  OD2 ASP A 207     1831   2735   1962    240     45     14       O  
ATOM   1707  N   SER A 208       9.084  46.819  54.160  1.00 17.12           N  
ANISOU 1707  N   SER A 208     2215   1996   2293    -72   -142    -29       N  
ATOM   1708  CA  SER A 208      10.241  45.967  53.932  1.00 15.92           C  
ANISOU 1708  CA  SER A 208     1849   2017   2181   -218   -349    178       C  
ATOM   1709  C   SER A 208      10.435  45.749  52.442  1.00 14.99           C  
ANISOU 1709  C   SER A 208     1601   1905   2191     20   -264    302       C  
ATOM   1710  O   SER A 208      11.571  45.716  51.949  1.00 16.37           O  
ANISOU 1710  O   SER A 208     1652   1971   2595    265   -147    376       O  
ATOM   1711  CB  SER A 208      10.031  44.637  54.667  1.00 16.29           C  
ANISOU 1711  CB  SER A 208     1719   2226   2247   -154   -190    388       C  
ATOM   1712  OG  SER A 208      11.175  43.814  54.577  1.00 19.99           O  
ANISOU 1712  OG  SER A 208     2138   2326   3130    138   -108    487       O  
ATOM   1713  N   LEU A 209       9.359  45.591  51.673  1.00 15.53           N  
ANISOU 1713  N   LEU A 209     1729   2042   2131     26   -315    185       N  
ATOM   1714  CA  LEU A 209       9.443  45.264  50.242  1.00 17.64           C  
ANISOU 1714  CA  LEU A 209     2145   2407   2152    -20   -271    113       C  
ATOM   1715  C   LEU A 209      10.052  46.435  49.482  1.00 16.11           C  
ANISOU 1715  C   LEU A 209     1671   2404   2045    262   -326    222       C  
ATOM   1716  O   LEU A 209      10.808  46.260  48.521  1.00 17.61           O  
ANISOU 1716  O   LEU A 209     1745   2880   2065   -111   -283   -108       O  
ATOM   1717  CB  LEU A 209       8.045  44.898  49.736  1.00 18.84           C  
ANISOU 1717  CB  LEU A 209     2381   2714   2065   -347   -344     12       C  
ATOM   1718  CG  LEU A 209       7.906  44.379  48.314  1.00 19.60           C  
ANISOU 1718  CG  LEU A 209     2369   2906   2173   -266   -114   -246       C  
ATOM   1719  CD1 LEU A 209       8.546  43.009  48.164  1.00 23.98           C  
ANISOU 1719  CD1 LEU A 209     3879   2649   2586   -141   -354   -153       C  
ATOM   1720  CD2 LEU A 209       6.447  44.287  47.907  1.00 22.77           C  
ANISOU 1720  CD2 LEU A 209     2548   3906   2197   -825   -331   -195       C  
ATOM   1721  N   VAL A 210       9.738  47.660  49.915  1.00 17.96           N  
ANISOU 1721  N   VAL A 210     1939   2362   2523    148   -244    100       N  
ATOM   1722  CA  VAL A 210      10.337  48.842  49.281  1.00 19.42           C  
ANISOU 1722  CA  VAL A 210     2088   2388   2903    198    233     58       C  
ATOM   1723  C   VAL A 210      11.852  48.762  49.315  1.00 17.24           C  
ANISOU 1723  C   VAL A 210     2092   2091   2367    266    196   -117       C  
ATOM   1724  O   VAL A 210      12.552  49.063  48.336  1.00 16.27           O  
ANISOU 1724  O   VAL A 210     2001   2101   2082    205    -11   -217       O  
ATOM   1725  CB  VAL A 210       9.799  50.086  50.036  1.00 22.49           C  
ANISOU 1725  CB  VAL A 210     2405   2317   3825    799    309    248       C  
ATOM   1726  CG1 VAL A 210      10.559  51.349  49.734  1.00 27.04           C  
ANISOU 1726  CG1 VAL A 210     3303   2096   4875    685     84    424       C  
ATOM   1727  CG2 VAL A 210       8.316  50.224  49.696  1.00 25.21           C  
ANISOU 1727  CG2 VAL A 210     2673   3115   3790   1076   -186    286       C  
ATOM   1728  N   GLY A 211      12.388  48.336  50.462  1.00 16.24           N  
ANISOU 1728  N   GLY A 211     2213   1774   2185    159    280   -198       N  
ATOM   1729  CA  GLY A 211      13.837  48.151  50.588  1.00 15.71           C  
ANISOU 1729  CA  GLY A 211     2124   2019   1827   -337     78    -66       C  
ATOM   1730  C   GLY A 211      14.403  47.247  49.503  1.00 13.04           C  
ANISOU 1730  C   GLY A 211     1408   1786   1762     12   -332     94       C  
ATOM   1731  O   GLY A 211      15.487  47.461  48.926  1.00 13.85           O  
ANISOU 1731  O   GLY A 211     1687   2143   1430   -133   -247    368       O  
ATOM   1732  N   GLN A 212      13.670  46.179  49.185  1.00 14.19           N  
ANISOU 1732  N   GLN A 212     1743   1911   1737   -163   -383     72       N  
ATOM   1733  CA  GLN A 212      14.120  45.196  48.198  1.00 14.43           C  
ANISOU 1733  CA  GLN A 212     1909   1766   1807    -84   -451    102       C  
ATOM   1734  C   GLN A 212      14.158  45.795  46.795  1.00 14.29           C  
ANISOU 1734  C   GLN A 212     1920   1695   1816    112   -201     79       C  
ATOM   1735  O   GLN A 212      14.926  45.338  45.919  1.00 15.15           O  
ANISOU 1735  O   GLN A 212     1870   1840   2047     53    -82    -21       O  
ATOM   1736  CB  GLN A 212      13.187  43.985  48.294  1.00 16.60           C  
ANISOU 1736  CB  GLN A 212     2336   1942   2029   -362    -18    -26       C  
ATOM   1737  CG  GLN A 212      12.958  43.434  49.715  1.00 17.40           C  
ANISOU 1737  CG  GLN A 212     2234   2280   2096   -397   -273    225       C  
ATOM   1738  CD  GLN A 212      14.241  42.976  50.371  1.00 18.82           C  
ANISOU 1738  CD  GLN A 212     2345   2264   2542    171    -79    246       C  
ATOM   1739  OE1 GLN A 212      15.157  42.496  49.671  1.00 23.15           O  
ANISOU 1739  OE1 GLN A 212     2691   2790   3314    228    319   -101       O  
ATOM   1740  NE2 GLN A 212      14.421  43.089  51.666  1.00 18.51           N  
ANISOU 1740  NE2 GLN A 212     2177   2268   2588    313   -390    472       N  
ATOM   1741  N   ALA A 213      13.357  46.834  46.539  1.00 13.60           N  
ANISOU 1741  N   ALA A 213     1525   1842   1800      8   -287    148       N  
ATOM   1742  CA  ALA A 213      13.378  47.502  45.235  1.00 13.77           C  
ANISOU 1742  CA  ALA A 213     1636   1756   1839   -141   -352    150       C  
ATOM   1743  C   ALA A 213      14.498  48.523  45.101  1.00 13.74           C  
ANISOU 1743  C   ALA A 213     1450   2049   1722   -174   -267     64       C  
ATOM   1744  O   ALA A 213      14.873  48.869  43.974  1.00 15.35           O  
ANISOU 1744  O   ALA A 213     2068   1940   1824   -237    150   -147       O  
ATOM   1745  CB  ALA A 213      12.059  48.233  44.972  1.00 16.95           C  
ANISOU 1745  CB  ALA A 213     1510   2126   2804   -375   -634    846       C  
ATOM   1746  N   LEU A 214      14.995  49.044  46.231  1.00 13.72           N  
ANISOU 1746  N   LEU A 214     1591   1757   1865      0   -475     66       N  
ATOM   1747  CA  LEU A 214      15.856  50.230  46.213  1.00 12.07           C  
ANISOU 1747  CA  LEU A 214     1296   1578   1713    230   -162    -63       C  
ATOM   1748  C   LEU A 214      17.323  49.980  46.562  1.00 12.16           C  
ANISOU 1748  C   LEU A 214     1219   1784   1618    278     36     51       C  
ATOM   1749  O   LEU A 214      18.191  50.644  45.958  1.00 15.06           O  
ANISOU 1749  O   LEU A 214     1472   2786   1464   -404   -329    273       O  
ATOM   1750  CB  LEU A 214      15.339  51.307  47.197  1.00 12.13           C  
ANISOU 1750  CB  LEU A 214     1432   1549   1629    438    -50    142       C  
ATOM   1751  CG  LEU A 214      13.923  51.839  46.919  1.00 13.96           C  
ANISOU 1751  CG  LEU A 214     1639   1845   1820    655   -361    -53       C  
ATOM   1752  CD1 LEU A 214      13.471  52.833  47.998  1.00 14.95           C  
ANISOU 1752  CD1 LEU A 214     1367   2139   2176    518    -40   -284       C  
ATOM   1753  CD2 LEU A 214      13.870  52.502  45.545  1.00 15.71           C  
ANISOU 1753  CD2 LEU A 214     1965   2087   1916    636   -514     95       C  
ATOM   1754  N   PHE A 215      17.634  49.084  47.510  1.00 12.86           N  
ANISOU 1754  N   PHE A 215     1285   1860   1741    290    -90    108       N  
ATOM   1755  CA  PHE A 215      18.993  49.032  48.044  1.00 11.76           C  
ANISOU 1755  CA  PHE A 215     1153   1794   1523    211    125    168       C  
ATOM   1756  C   PHE A 215      19.904  48.144  47.200  1.00 11.68           C  
ANISOU 1756  C   PHE A 215     1233   1666   1538    113     73     40       C  
ATOM   1757  O   PHE A 215      19.560  47.034  46.783  1.00 12.26           O  
ANISOU 1757  O   PHE A 215     1422   1740   1496     38   -136     39       O  
ATOM   1758  CB  PHE A 215      18.956  48.542  49.488  1.00 12.87           C  
ANISOU 1758  CB  PHE A 215     1446   1992   1453    212     47    126       C  
ATOM   1759  CG  PHE A 215      18.446  49.583  50.478  1.00 16.17           C  
ANISOU 1759  CG  PHE A 215     2088   2376   1681    158    342   -133       C  
ATOM   1760  CD1 PHE A 215      17.102  49.789  50.655  1.00 19.20           C  
ANISOU 1760  CD1 PHE A 215     2196   2977   2122   -111   1009   -715       C  
ATOM   1761  CD2 PHE A 215      19.309  50.361  51.224  1.00 17.39           C  
ANISOU 1761  CD2 PHE A 215     2466   2119   2022    189    186   -263       C  
ATOM   1762  CE1 PHE A 215      16.606  50.728  51.543  1.00 19.75           C  
ANISOU 1762  CE1 PHE A 215     2212   2682   2608   -153    568  -1062       C  
ATOM   1763  CE2 PHE A 215      18.842  51.279  52.146  1.00 17.57           C  
ANISOU 1763  CE2 PHE A 215     2133   1892   2652    468     45   -357       C  
ATOM   1764  CZ  PHE A 215      17.480  51.466  52.328  1.00 18.92           C  
ANISOU 1764  CZ  PHE A 215     2023   2298   2866   -256    397   -572       C  
ATOM   1765  N   GLY A 216      21.108  48.670  46.967  1.00 11.25           N  
ANISOU 1765  N   GLY A 216     1161   1687   1426    176     92    -17       N  
ATOM   1766  CA  GLY A 216      22.120  47.917  46.222  1.00 11.33           C  
ANISOU 1766  CA  GLY A 216     1216   1598   1492    290    -26    -99       C  
ATOM   1767  C   GLY A 216      23.479  48.070  46.875  1.00 11.01           C  
ANISOU 1767  C   GLY A 216     1234   1542   1407    299     14   -265       C  
ATOM   1768  O   GLY A 216      23.635  48.762  47.896  1.00 12.02           O  
ANISOU 1768  O   GLY A 216     1632   1655   1280    180     15   -210       O  
ATOM   1769  N   ASP A 217      24.495  47.408  46.307  1.00 10.52           N  
ANISOU 1769  N   ASP A 217     1164   1586   1247    235    287    130       N  
ATOM   1770  CA  ASP A 217      25.756  47.315  47.028  1.00 11.45           C  
ANISOU 1770  CA  ASP A 217     1145   1369   1839    125    105     19       C  
ATOM   1771  C   ASP A 217      26.839  48.192  46.429  1.00 12.06           C  
ANISOU 1771  C   ASP A 217     1503   1517   1561   -205    -99     66       C  
ATOM   1772  O   ASP A 217      26.864  48.411  45.208  1.00 12.02           O  
ANISOU 1772  O   ASP A 217     1217   1838   1511    -27     -9    -49       O  
ATOM   1773  CB  ASP A 217      26.301  45.877  46.998  1.00 11.85           C  
ANISOU 1773  CB  ASP A 217     1302   1365   1837    182     73     70       C  
ATOM   1774  CG  ASP A 217      25.370  44.851  47.623  1.00 12.96           C  
ANISOU 1774  CG  ASP A 217     1753   1532   1639     54     35    310       C  
ATOM   1775  OD1 ASP A 217      24.319  45.223  48.184  1.00 13.00           O  
ANISOU 1775  OD1 ASP A 217     1519   1723   1697   -197    -17    169       O  
ATOM   1776  OD2 ASP A 217      25.688  43.640  47.536  1.00 13.89           O  
ANISOU 1776  OD2 ASP A 217     2018   1523   1739     99   -178    449       O  
ATOM   1777  N   GLY A 218      27.747  48.627  47.289  1.00 10.65           N  
ANISOU 1777  N   GLY A 218     1225   1282   1538    117    -66     23       N  
ATOM   1778  CA  GLY A 218      28.820  49.488  46.762  1.00 14.20           C  
ANISOU 1778  CA  GLY A 218     1840   1976   1578   -601   -142    -45       C  
ATOM   1779  C   GLY A 218      29.755  49.913  47.893  1.00 13.10           C  
ANISOU 1779  C   GLY A 218     1613   1835   1530   -336   -160     52       C  
ATOM   1780  O   GLY A 218      29.357  49.932  49.061  1.00 11.75           O  
ANISOU 1780  O   GLY A 218     1339   1608   1516      0   -225    175       O  
ATOM   1781  N   ALA A 219      30.976  50.289  47.536  1.00 11.83           N  
ANISOU 1781  N   ALA A 219     1531   1513   1450   -132   -195    226       N  
ATOM   1782  CA  ALA A 219      31.881  50.935  48.477  1.00 11.31           C  
ANISOU 1782  CA  ALA A 219     1354   1436   1508    -31    -77     53       C  
ATOM   1783  C   ALA A 219      32.516  52.168  47.839  1.00 11.71           C  
ANISOU 1783  C   ALA A 219     1541   1432   1474    -70   -153     87       C  
ATOM   1784  O   ALA A 219      32.772  52.185  46.625  1.00 11.73           O  
ANISOU 1784  O   ALA A 219     1547   1414   1494    -34    -72     32       O  
ATOM   1785  CB  ALA A 219      32.981  49.977  48.921  1.00 13.50           C  
ANISOU 1785  CB  ALA A 219     1526   1756   1847    -21   -272    451       C  
ATOM   1786  N   ALA A 220      32.798  53.163  48.690  1.00 10.99           N  
ANISOU 1786  N   ALA A 220     1383   1340   1453     68    -45     89       N  
ATOM   1787  CA  ALA A 220      33.491  54.363  48.225  1.00 10.80           C  
ANISOU 1787  CA  ALA A 220     1111   1220   1771    218   -201    169       C  
ATOM   1788  C   ALA A 220      34.548  54.699  49.261  1.00 10.73           C  
ANISOU 1788  C   ALA A 220     1128   1510   1439    161     63   -126       C  
ATOM   1789  O   ALA A 220      34.301  54.519  50.463  1.00 13.03           O  
ANISOU 1789  O   ALA A 220     1811   1671   1468     21    143    -37       O  
ATOM   1790  CB  ALA A 220      32.563  55.538  48.007  1.00 11.74           C  
ANISOU 1790  CB  ALA A 220     1158   1228   2074    349     27    -95       C  
ATOM   1791  N   ALA A 221      35.698  55.148  48.754  1.00 11.83           N  
ANISOU 1791  N   ALA A 221     1240   1577   1680   -115     12   -117       N  
ATOM   1792  CA  ALA A 221      36.794  55.540  49.634  1.00 10.68           C  
ANISOU 1792  CA  ALA A 221     1248   1456   1354     13    114   -227       C  
ATOM   1793  C   ALA A 221      37.258  56.957  49.290  1.00 10.26           C  
ANISOU 1793  C   ALA A 221     1012   1503   1384     28     98   -149       C  
ATOM   1794  O   ALA A 221      37.263  57.323  48.104  1.00 13.64           O  
ANISOU 1794  O   ALA A 221     1688   2031   1464   -400     22     70       O  
ATOM   1795  CB  ALA A 221      37.944  54.571  49.483  1.00 12.37           C  
ANISOU 1795  CB  ALA A 221     1345   1516   1841    123    -32   -280       C  
ATOM   1796  N   LEU A 222      37.671  57.716  50.301  1.00 11.57           N  
ANISOU 1796  N   LEU A 222     1357   1459   1579    -14    -47   -193       N  
ATOM   1797  CA  LEU A 222      38.202  59.054  50.174  1.00 10.95           C  
ANISOU 1797  CA  LEU A 222      956   1466   1739     65    202   -267       C  
ATOM   1798  C   LEU A 222      39.555  59.118  50.887  1.00 10.33           C  
ANISOU 1798  C   LEU A 222      825   1349   1753    195    303   -109       C  
ATOM   1799  O   LEU A 222      39.767  58.376  51.848  1.00 12.52           O  
ANISOU 1799  O   LEU A 222     1155   1654   1948    191    205    122       O  
ATOM   1800  CB  LEU A 222      37.360  60.121  50.891  1.00 12.28           C  
ANISOU 1800  CB  LEU A 222      994   1496   2174    418    127    -86       C  
ATOM   1801  CG  LEU A 222      35.838  60.002  50.823  1.00 12.11           C  
ANISOU 1801  CG  LEU A 222      993   1851   1757    536   -147    127       C  
ATOM   1802  CD1 LEU A 222      35.160  61.019  51.738  1.00 16.74           C  
ANISOU 1802  CD1 LEU A 222     1125   2494   2742    210    732   -347       C  
ATOM   1803  CD2 LEU A 222      35.409  60.119  49.361  1.00 17.74           C  
ANISOU 1803  CD2 LEU A 222     2128   2770   1841     76   -446    431       C  
ATOM   1804  N   ILE A 223      40.383  60.031  50.393  1.00 11.84           N  
ANISOU 1804  N   ILE A 223     1048   1652   1800   -105    228    -82       N  
ATOM   1805  CA  ILE A 223      41.474  60.584  51.209  1.00 12.25           C  
ANISOU 1805  CA  ILE A 223     1019   1644   1991    -16    174   -173       C  
ATOM   1806  C   ILE A 223      41.106  62.013  51.601  1.00 10.83           C  
ANISOU 1806  C   ILE A 223      872   1616   1627     31    187    -33       C  
ATOM   1807  O   ILE A 223      40.768  62.831  50.728  1.00 12.67           O  
ANISOU 1807  O   ILE A 223     1605   1715   1493     35     36    -45       O  
ATOM   1808  CB  ILE A 223      42.799  60.562  50.444  1.00 11.81           C  
ANISOU 1808  CB  ILE A 223      922   1634   1930    192     56   -135       C  
ATOM   1809  CG1 ILE A 223      43.227  59.130  50.114  1.00 13.08           C  
ANISOU 1809  CG1 ILE A 223     1491   1652   1826    251    108   -207       C  
ATOM   1810  CG2 ILE A 223      43.834  61.326  51.268  1.00 12.02           C  
ANISOU 1810  CG2 ILE A 223     1134   1876   1555   -236    358   -126       C  
ATOM   1811  CD1 ILE A 223      43.674  58.352  51.367  1.00 18.08           C  
ANISOU 1811  CD1 ILE A 223     1761   2122   2988    221   -298    663       C  
ATOM   1812  N   VAL A 224      41.161  62.287  52.885  1.00 11.96           N  
ANISOU 1812  N   VAL A 224     1458   1476   1610    209    -55     85       N  
ATOM   1813  CA  VAL A 224      40.839  63.597  53.413  1.00 11.93           C  
ANISOU 1813  CA  VAL A 224     1425   1494   1613     97    -91    -26       C  
ATOM   1814  C   VAL A 224      42.020  64.170  54.179  1.00 13.17           C  
ANISOU 1814  C   VAL A 224     1493   1663   1850    -23   -201     87       C  
ATOM   1815  O   VAL A 224      42.582  63.496  55.057  1.00 13.00           O  
ANISOU 1815  O   VAL A 224     1767   1645   1527    178   -227   -207       O  
ATOM   1816  CB  VAL A 224      39.585  63.544  54.315  1.00 12.21           C  
ANISOU 1816  CB  VAL A 224     1447   1585   1608     59    -92   -162       C  
ATOM   1817  CG1 VAL A 224      39.326  64.911  54.947  1.00 14.75           C  
ANISOU 1817  CG1 VAL A 224     1978   1618   2009   -239    458   -323       C  
ATOM   1818  CG2 VAL A 224      38.396  63.059  53.488  1.00 13.16           C  
ANISOU 1818  CG2 VAL A 224     1441   1613   1946     26   -250    -13       C  
ATOM   1819  N   GLY A 225      42.403  65.425  53.866  1.00 13.40           N  
ANISOU 1819  N   GLY A 225     1600   1653   1836   -101     -1    -50       N  
ATOM   1820  CA  GLY A 225      43.475  66.006  54.667  1.00 13.31           C  
ANISOU 1820  CA  GLY A 225     1551   1707   1800    -57     54   -143       C  
ATOM   1821  C   GLY A 225      43.386  67.527  54.624  1.00 12.91           C  
ANISOU 1821  C   GLY A 225     1588   1711   1606   -117   -135     -5       C  
ATOM   1822  O   GLY A 225      42.814  68.089  53.689  1.00 14.49           O  
ANISOU 1822  O   GLY A 225     1903   1962   1641   -149   -261    100       O  
ATOM   1823  N   SER A 226      43.931  68.165  55.653  1.00 13.37           N  
ANISOU 1823  N   SER A 226     1721   1702   1659    -96   -213    -32       N  
ATOM   1824  CA  SER A 226      44.138  69.610  55.643  1.00 13.68           C  
ANISOU 1824  CA  SER A 226     1698   1689   1812    -74    253   -218       C  
ATOM   1825  C   SER A 226      45.543  69.911  55.105  1.00 14.19           C  
ANISOU 1825  C   SER A 226     1815   1692   1886     27    464   -161       C  
ATOM   1826  O   SER A 226      46.437  69.039  55.101  1.00 15.66           O  
ANISOU 1826  O   SER A 226     1796   1711   2442     30    526    193       O  
ATOM   1827  CB  SER A 226      43.955  70.234  57.026  1.00 14.91           C  
ANISOU 1827  CB  SER A 226     1722   2038   1904   -283    461   -369       C  
ATOM   1828  OG  SER A 226      42.593  70.203  57.436  1.00 13.89           O  
ANISOU 1828  OG  SER A 226     1594   1813   1869     46    258   -108       O  
ATOM   1829  N   ASP A 227      45.718  71.162  54.671  1.00 13.87           N  
ANISOU 1829  N   ASP A 227     1419   1858   1992     74     64    183       N  
ATOM   1830  CA  ASP A 227      47.012  71.627  54.183  1.00 15.25           C  
ANISOU 1830  CA  ASP A 227     1558   2124   2111    -99    176    133       C  
ATOM   1831  C   ASP A 227      47.584  70.769  53.063  1.00 15.76           C  
ANISOU 1831  C   ASP A 227     1651   2240   2097    -16    253    157       C  
ATOM   1832  O   ASP A 227      48.678  70.184  53.192  1.00 17.12           O  
ANISOU 1832  O   ASP A 227     1521   2482   2503    -37    260    -27       O  
ATOM   1833  CB  ASP A 227      48.003  71.693  55.376  1.00 15.85           C  
ANISOU 1833  CB  ASP A 227     1493   2247   2281   -165     96     37       C  
ATOM   1834  CG  ASP A 227      47.362  72.417  56.548  1.00 16.23           C  
ANISOU 1834  CG  ASP A 227     1556   2557   2055   -157    146    162       C  
ATOM   1835  OD1 ASP A 227      46.707  73.457  56.336  1.00 17.52           O  
ANISOU 1835  OD1 ASP A 227     1802   2601   2253     47    326     26       O  
ATOM   1836  OD2 ASP A 227      47.491  71.941  57.700  1.00 19.20           O  
ANISOU 1836  OD2 ASP A 227     2248   2974   2074   -423   -155    227       O  
ATOM   1837  N  APRO A 228      46.895  70.668  51.933  0.59 16.48           N  
ANISOU 1837  N  APRO A 228     1921   2234   2106    -90    150    122       N  
ATOM   1838  N  BPRO A 228      46.902  70.671  51.929  0.41 16.58           N  
ANISOU 1838  N  BPRO A 228     1904   2269   2127    -75    148     94       N  
ATOM   1839  CA APRO A 228      47.396  69.798  50.861  0.59 17.13           C  
ANISOU 1839  CA APRO A 228     1862   2493   2154   -141    276     37       C  
ATOM   1840  CA BPRO A 228      47.406  69.799  50.860  0.41 17.14           C  
ANISOU 1840  CA BPRO A 228     1853   2483   2175   -136    267     17       C  
ATOM   1841  C  APRO A 228      48.733  70.290  50.332  0.59 18.26           C  
ANISOU 1841  C  APRO A 228     1885   2575   2476   -272    292    -45       C  
ATOM   1842  C  BPRO A 228      48.739  70.301  50.328  0.41 18.36           C  
ANISOU 1842  C  BPRO A 228     1904   2598   2474   -267    312    -47       C  
ATOM   1843  O  APRO A 228      48.936  71.507  50.277  0.59 22.87           O  
ANISOU 1843  O  APRO A 228     2635   2646   3407   -608    629   -183       O  
ATOM   1844  O  BPRO A 228      48.948  71.515  50.272  0.41 22.12           O  
ANISOU 1844  O  BPRO A 228     2529   2670   3207   -552    535    -95       O  
ATOM   1845  CB APRO A 228      46.347  69.934  49.744  0.59 17.64           C  
ANISOU 1845  CB APRO A 228     1908   2599   2196   -159    223   -100       C  
ATOM   1846  CB BPRO A 228      46.354  69.920  49.749  0.41 17.65           C  
ANISOU 1846  CB BPRO A 228     1939   2573   2192   -159    211    -79       C  
ATOM   1847  CG APRO A 228      45.149  70.540  50.407  0.59 17.58           C  
ANISOU 1847  CG APRO A 228     1924   2549   2208    -87    120   -199       C  
ATOM   1848  CG BPRO A 228      45.618  71.181  50.060  0.41 17.58           C  
ANISOU 1848  CG BPRO A 228     2099   2485   2096   -113     54     19       C  
ATOM   1849  CD APRO A 228      45.651  71.353  51.574  0.59 16.85           C  
ANISOU 1849  CD APRO A 228     1941   2414   2046    -43     11      4       C  
ATOM   1850  CD BPRO A 228      45.664  71.363  51.555  0.41 16.89           C  
ANISOU 1850  CD BPRO A 228     1923   2393   2102    -56      5     -6       C  
ATOM   1851  N   VAL A 229      49.628  69.407  49.922  1.00 20.36           N  
ANISOU 1851  N   VAL A 229     1942   3010   2786   -130    474   -132       N  
ATOM   1852  CA  VAL A 229      50.914  69.830  49.375  1.00 25.61           C  
ANISOU 1852  CA  VAL A 229     2214   3752   3763   -217   1008    -51       C  
ATOM   1853  C   VAL A 229      50.722  70.278  47.939  1.00 28.79           C  
ANISOU 1853  C   VAL A 229     3283   3926   3728   -285   1539    178       C  
ATOM   1854  O   VAL A 229      50.448  69.464  47.059  1.00 29.39           O  
ANISOU 1854  O   VAL A 229     3908   4023   3234   -447   1880    301       O  
ATOM   1855  CB  VAL A 229      51.908  68.665  49.450  1.00 26.67           C  
ANISOU 1855  CB  VAL A 229     2111   3934   4089   -121   1182   -388       C  
ATOM   1856  CG1 VAL A 229      53.255  69.162  48.963  1.00 30.92           C  
ANISOU 1856  CG1 VAL A 229     2474   4358   4915   -353   1908  -1057       C  
ATOM   1857  CG2 VAL A 229      51.982  68.130  50.866  1.00 26.87           C  
ANISOU 1857  CG2 VAL A 229     1701   4108   4400   -196    477    -34       C  
ATOM   1858  N   PRO A 230      50.816  71.569  47.647  1.00 35.62           N  
ANISOU 1858  N   PRO A 230     5283   4071   4182   -861   1449    368       N  
ATOM   1859  CA  PRO A 230      50.512  72.058  46.302  1.00 36.82           C  
ANISOU 1859  CA  PRO A 230     5887   3918   4185   -659   1605    450       C  
ATOM   1860  C   PRO A 230      51.338  71.369  45.214  1.00 39.38           C  
ANISOU 1860  C   PRO A 230     6154   4475   4334   -759   1847    291       C  
ATOM   1861  O   PRO A 230      52.509  71.028  45.391  1.00 41.84           O  
ANISOU 1861  O   PRO A 230     5380   5575   4944  -1513   2312   -184       O  
ATOM   1862  CB  PRO A 230      50.914  73.538  46.332  1.00 40.77           C  
ANISOU 1862  CB  PRO A 230     6983   4059   4451  -1077   1462    433       C  
ATOM   1863  CG  PRO A 230      51.151  73.886  47.754  1.00 41.66           C  
ANISOU 1863  CG  PRO A 230     7255   4132   4443  -1285   1525    403       C  
ATOM   1864  CD  PRO A 230      51.235  72.628  48.560  1.00 38.86           C  
ANISOU 1864  CD  PRO A 230     6481   4038   4247  -1028   1655    227       C  
ATOM   1865  N   GLU A 231      50.712  71.153  44.060  1.00 40.95           N  
ANISOU 1865  N   GLU A 231     6699   4785   4076   -879   1904    465       N  
ATOM   1866  CA  GLU A 231      51.345  70.515  42.912  1.00 45.88           C  
ANISOU 1866  CA  GLU A 231     7736   5317   4380  -1217   2398     48       C  
ATOM   1867  C   GLU A 231      51.716  69.062  43.160  1.00 42.15           C  
ANISOU 1867  C   GLU A 231     6192   5545   4280   -854   2283   -173       C  
ATOM   1868  O   GLU A 231      52.254  68.434  42.241  1.00 46.66           O  
ANISOU 1868  O   GLU A 231     6062   6598   5068   -253   3378    203       O  
ATOM   1869  CB  GLU A 231      52.588  71.325  42.491  1.00 54.22           C  
ANISOU 1869  CB  GLU A 231     9494   6244   4863  -2362   3831   -642       C  
ATOM   1870  CG  GLU A 231      52.215  72.767  42.145  1.00 59.02           C  
ANISOU 1870  CG  GLU A 231    11005   5952   5468  -2824   3847   -501       C  
ATOM   1871  CD  GLU A 231      53.389  73.703  42.030  1.00 62.42           C  
ANISOU 1871  CD  GLU A 231    11193   6469   6053  -3134   4405  -1058       C  
ATOM   1872  OE1 GLU A 231      54.043  73.698  40.949  1.00 70.91           O  
ANISOU 1872  OE1 GLU A 231    10601   8853   7489  -3329   4961  -2528       O  
ATOM   1873  OE2 GLU A 231      53.666  74.475  42.969  1.00 64.26           O  
ANISOU 1873  OE2 GLU A 231    10147   7675   6595  -2987   3964  -1807       O  
ATOM   1874  N   ILE A 232      51.458  68.508  44.339  1.00 35.83           N  
ANISOU 1874  N   ILE A 232     4461   5007   4147   -866   1790   -295       N  
ATOM   1875  CA  ILE A 232      51.738  67.108  44.636  1.00 30.86           C  
ANISOU 1875  CA  ILE A 232     2812   5160   3754   -436   1475   -630       C  
ATOM   1876  C   ILE A 232      50.421  66.414  44.986  1.00 27.04           C  
ANISOU 1876  C   ILE A 232     2613   4522   3140   -195   1081   -503       C  
ATOM   1877  O   ILE A 232      50.127  65.362  44.422  1.00 27.05           O  
ANISOU 1877  O   ILE A 232     3087   4469   2721   -203   1497   -482       O  
ATOM   1878  CB  ILE A 232      52.796  66.952  45.731  1.00 34.97           C  
ANISOU 1878  CB  ILE A 232     2997   6000   4292  -1318    969   -525       C  
ATOM   1879  CG1 ILE A 232      54.230  67.026  45.194  1.00 38.37           C  
ANISOU 1879  CG1 ILE A 232     2935   6699   4943  -1199    981   -516       C  
ATOM   1880  CG2 ILE A 232      52.639  65.656  46.505  1.00 30.67           C  
ANISOU 1880  CG2 ILE A 232     1940   5329   4386     27   1032   -793       C  
ATOM   1881  CD1 ILE A 232      54.632  68.282  44.461  1.00 44.80           C  
ANISOU 1881  CD1 ILE A 232     4947   7726   4348  -2709   1708   -689       C  
ATOM   1882  N   GLU A 233      49.661  67.039  45.872  1.00 19.99           N  
ANISOU 1882  N   GLU A 233     1857   3284   2454    110    298    114       N  
ATOM   1883  CA  GLU A 233      48.307  66.545  46.134  1.00 17.85           C  
ANISOU 1883  CA  GLU A 233     2002   2657   2123     15    246    124       C  
ATOM   1884  C   GLU A 233      47.298  67.375  45.360  1.00 17.95           C  
ANISOU 1884  C   GLU A 233     1819   2652   2348   -118    301    324       C  
ATOM   1885  O   GLU A 233      47.614  68.510  44.976  1.00 21.96           O  
ANISOU 1885  O   GLU A 233     2178   2855   3311   -366   -140    746       O  
ATOM   1886  CB  GLU A 233      48.023  66.588  47.627  1.00 16.81           C  
ANISOU 1886  CB  GLU A 233     2137   2131   2119    -46    229   -117       C  
ATOM   1887  CG  GLU A 233      48.907  65.626  48.423  1.00 16.78           C  
ANISOU 1887  CG  GLU A 233     2107   2272   1998    -31    354    -22       C  
ATOM   1888  CD  GLU A 233      48.645  65.706  49.922  1.00 17.00           C  
ANISOU 1888  CD  GLU A 233     2019   2408   2031   -129    420    -43       C  
ATOM   1889  OE1 GLU A 233      48.787  66.827  50.481  1.00 17.54           O  
ANISOU 1889  OE1 GLU A 233     2226   2479   1961   -333    481    -56       O  
ATOM   1890  OE2 GLU A 233      48.314  64.667  50.542  1.00 16.57           O  
ANISOU 1890  OE2 GLU A 233     1885   2411   2001   -148    385    -46       O  
ATOM   1891  N   LYS A 234      46.082  66.875  45.117  1.00 18.10           N  
ANISOU 1891  N   LYS A 234     1836   2671   2369   -125    327    171       N  
ATOM   1892  CA  LYS A 234      45.149  67.600  44.263  1.00 17.87           C  
ANISOU 1892  CA  LYS A 234     1822   2675   2292    -66    289     -5       C  
ATOM   1893  C   LYS A 234      43.771  67.677  44.902  1.00 17.48           C  
ANISOU 1893  C   LYS A 234     1839   2400   2403   -141    327      7       C  
ATOM   1894  O   LYS A 234      43.026  66.708  44.862  1.00 16.42           O  
ANISOU 1894  O   LYS A 234     1915   2140   2183    -18    191    376       O  
ATOM   1895  CB  LYS A 234      45.107  66.885  42.916  1.00 19.56           C  
ANISOU 1895  CB  LYS A 234     2116   2889   2428    223    215   -193       C  
ATOM   1896  CG  LYS A 234      44.160  67.422  41.876  1.00 22.33           C  
ANISOU 1896  CG  LYS A 234     2357   3429   2698    120   -276   -372       C  
ATOM   1897  CD  LYS A 234      44.108  66.510  40.656  1.00 28.97           C  
ANISOU 1897  CD  LYS A 234     3895   4337   2775   -550   -257   -727       C  
ATOM   1898  CE  LYS A 234      43.592  67.270  39.449  1.00 34.11           C  
ANISOU 1898  CE  LYS A 234     5204   5033   2725  -1239   -558   -362       C  
ATOM   1899  NZ  LYS A 234      43.719  66.460  38.212  1.00 47.41           N  
ANISOU 1899  NZ  LYS A 234     8028   7320   2664  -3374     87  -1260       N  
ATOM   1900  N   PRO A 235      43.497  68.831  45.482  1.00 16.96           N  
ANISOU 1900  N   PRO A 235     1798   2320   2326    -99    272    110       N  
ATOM   1901  CA  PRO A 235      42.169  69.119  46.046  1.00 16.28           C  
ANISOU 1901  CA  PRO A 235     1753   2317   2116    -98    170    114       C  
ATOM   1902  C   PRO A 235      41.037  68.905  45.042  1.00 15.78           C  
ANISOU 1902  C   PRO A 235     1812   2363   1821    -59    292    -49       C  
ATOM   1903  O   PRO A 235      41.184  69.249  43.864  1.00 17.05           O  
ANISOU 1903  O   PRO A 235     1922   2448   2108    -62    192    493       O  
ATOM   1904  CB  PRO A 235      42.295  70.605  46.416  1.00 17.34           C  
ANISOU 1904  CB  PRO A 235     1808   2436   2346   -116    136   -136       C  
ATOM   1905  CG  PRO A 235      43.748  70.725  46.796  1.00 17.78           C  
ANISOU 1905  CG  PRO A 235     1803   2509   2446   -180    142    -30       C  
ATOM   1906  CD  PRO A 235      44.445  69.946  45.686  1.00 16.98           C  
ANISOU 1906  CD  PRO A 235     1752   2317   2381    -84    132    164       C  
ATOM   1907  N   ILE A 236      39.929  68.337  45.541  1.00 14.20           N  
ANISOU 1907  N   ILE A 236     1773   2063   1560    -31    255   -268       N  
ATOM   1908  CA  ILE A 236      38.714  68.127  44.772  1.00 12.94           C  
ANISOU 1908  CA  ILE A 236     1818   1813   1287     85    259   -213       C  
ATOM   1909  C   ILE A 236      37.539  68.903  45.342  1.00 13.74           C  
ANISOU 1909  C   ILE A 236     1867   1930   1426    168    317   -142       C  
ATOM   1910  O   ILE A 236      36.840  69.626  44.624  1.00 14.54           O  
ANISOU 1910  O   ILE A 236     1593   2293   1639    115    240     -7       O  
ATOM   1911  CB  ILE A 236      38.376  66.617  44.695  1.00 13.91           C  
ANISOU 1911  CB  ILE A 236     1692   1836   1757     55    220   -156       C  
ATOM   1912  CG1 ILE A 236      39.563  65.730  44.285  1.00 14.67           C  
ANISOU 1912  CG1 ILE A 236     1951   1868   1755    205    203   -280       C  
ATOM   1913  CG2 ILE A 236      37.200  66.445  43.751  1.00 15.27           C  
ANISOU 1913  CG2 ILE A 236     1525   2265   2013   -500    264    260       C  
ATOM   1914  CD1 ILE A 236      39.265  64.255  44.394  1.00 15.33           C  
ANISOU 1914  CD1 ILE A 236     2118   1856   1850    281   -274     26       C  
ATOM   1915  N   PHE A 237      37.327  68.785  46.652  1.00 13.56           N  
ANISOU 1915  N   PHE A 237     1823   1808   1521     24    522    -46       N  
ATOM   1916  CA  PHE A 237      36.345  69.547  47.383  1.00 13.73           C  
ANISOU 1916  CA  PHE A 237     1647   2025   1546     -5    387   -196       C  
ATOM   1917  C   PHE A 237      36.893  69.878  48.779  1.00 14.20           C  
ANISOU 1917  C   PHE A 237     1719   2045   1632    215    243   -276       C  
ATOM   1918  O   PHE A 237      37.618  69.074  49.375  1.00 16.06           O  
ANISOU 1918  O   PHE A 237     2054   2094   1955    249     -3   -188       O  
ATOM   1919  CB  PHE A 237      35.016  68.814  47.594  1.00 13.26           C  
ANISOU 1919  CB  PHE A 237     1621   1843   1573     75    270    148       C  
ATOM   1920  CG  PHE A 237      34.257  68.417  46.343  1.00 13.62           C  
ANISOU 1920  CG  PHE A 237     1570   1975   1631     37    225    163       C  
ATOM   1921  CD1 PHE A 237      33.493  69.349  45.638  1.00 14.92           C  
ANISOU 1921  CD1 PHE A 237     1958   2009   1703    -22     87    336       C  
ATOM   1922  CD2 PHE A 237      34.274  67.110  45.874  1.00 13.78           C  
ANISOU 1922  CD2 PHE A 237     1781   1976   1477    -59    217    197       C  
ATOM   1923  CE1 PHE A 237      32.777  68.985  44.512  1.00 15.92           C  
ANISOU 1923  CE1 PHE A 237     2144   1944   1962   -178   -159    426       C  
ATOM   1924  CE2 PHE A 237      33.580  66.765  44.721  1.00 14.85           C  
ANISOU 1924  CE2 PHE A 237     1807   1995   1841   -136   -101    254       C  
ATOM   1925  CZ  PHE A 237      32.825  67.693  44.023  1.00 15.74           C  
ANISOU 1925  CZ  PHE A 237     1884   2000   2098   -130   -195    322       C  
ATOM   1926  N   GLU A 238      36.493  71.033  49.294  1.00 14.86           N  
ANISOU 1926  N   GLU A 238     2148   1869   1631    104    298   -195       N  
ATOM   1927  CA  GLU A 238      36.814  71.388  50.670  1.00 15.44           C  
ANISOU 1927  CA  GLU A 238     2149   2144   1571    -49    528   -280       C  
ATOM   1928  C   GLU A 238      35.561  71.303  51.539  1.00 14.29           C  
ANISOU 1928  C   GLU A 238     1781   2027   1622    299    285     90       C  
ATOM   1929  O   GLU A 238      34.501  71.677  51.027  1.00 16.99           O  
ANISOU 1929  O   GLU A 238     2014   2372   2070    305    -67    225       O  
ATOM   1930  CB  GLU A 238      37.336  72.830  50.759  1.00 17.80           C  
ANISOU 1930  CB  GLU A 238     2650   2378   1736   -426    637   -473       C  
ATOM   1931  CG  GLU A 238      38.643  73.015  49.996  1.00 22.01           C  
ANISOU 1931  CG  GLU A 238     2609   2837   2916   -501    873    -43       C  
ATOM   1932  CD  GLU A 238      39.123  74.449  50.105  1.00 24.67           C  
ANISOU 1932  CD  GLU A 238     2694   2769   3910   -495    604    317       C  
ATOM   1933  OE1 GLU A 238      38.250  75.339  50.170  1.00 29.72           O  
ANISOU 1933  OE1 GLU A 238     3153   2834   5304   -188      6    523       O  
ATOM   1934  OE2 GLU A 238      40.368  74.631  50.116  1.00 28.22           O  
ANISOU 1934  OE2 GLU A 238     2779   3071   4872   -694    -63    793       O  
ATOM   1935  N   MET A 239      35.707  70.845  52.779  1.00 13.70           N  
ANISOU 1935  N   MET A 239     1686   1943   1575    187    300     37       N  
ATOM   1936  CA  MET A 239      34.629  70.943  53.743  1.00 14.94           C  
ANISOU 1936  CA  MET A 239     2006   1814   1856    110    609     21       C  
ATOM   1937  C   MET A 239      34.763  72.233  54.555  1.00 14.59           C  
ANISOU 1937  C   MET A 239     1667   1979   1897     66    530    -90       C  
ATOM   1938  O   MET A 239      35.855  72.669  54.898  1.00 16.97           O  
ANISOU 1938  O   MET A 239     1687   2090   2673    155    242   -133       O  
ATOM   1939  CB  MET A 239      34.601  69.735  54.703  1.00 14.64           C  
ANISOU 1939  CB  MET A 239     1995   1989   1578    200    388     39       C  
ATOM   1940  CG  MET A 239      34.177  68.459  53.967  1.00 15.03           C  
ANISOU 1940  CG  MET A 239     1694   1724   2293    375     34    104       C  
ATOM   1941  SD  MET A 239      34.022  67.092  55.144  1.00 17.24           S  
ANISOU 1941  SD  MET A 239     2071   2175   2305    -69   -109    319       S  
ATOM   1942  CE  MET A 239      35.722  66.479  55.158  1.00 14.95           C  
ANISOU 1942  CE  MET A 239     2088   1697   1894   -117   -211    605       C  
ATOM   1943  N   VAL A 240      33.606  72.844  54.851  1.00 13.22           N  
ANISOU 1943  N   VAL A 240     1698   1482   1842    202    241    267       N  
ATOM   1944  CA  VAL A 240      33.650  74.111  55.553  1.00 14.05           C  
ANISOU 1944  CA  VAL A 240     2015   1525   1800    105    433    235       C  
ATOM   1945  C   VAL A 240      32.833  74.081  56.837  1.00 13.70           C  
ANISOU 1945  C   VAL A 240     1974   1832   1400   -254     91    205       C  
ATOM   1946  O   VAL A 240      33.223  74.763  57.782  1.00 13.44           O  
ANISOU 1946  O   VAL A 240     1522   1822   1761     30    -46    -29       O  
ATOM   1947  CB  VAL A 240      33.085  75.193  54.605  1.00 14.65           C  
ANISOU 1947  CB  VAL A 240     2746   1352   1470    158    533    114       C  
ATOM   1948  CG1 VAL A 240      33.028  76.541  55.297  1.00 17.10           C  
ANISOU 1948  CG1 VAL A 240     3069   1608   1820    536     28   -224       C  
ATOM   1949  CG2 VAL A 240      33.907  75.241  53.312  1.00 18.20           C  
ANISOU 1949  CG2 VAL A 240     3366   2075   1476   -186    732    -18       C  
ATOM   1950  N   TRP A 241      31.706  73.337  56.851  1.00 11.88           N  
ANISOU 1950  N   TRP A 241     1835   1373   1305    -13     73    138       N  
ATOM   1951  CA  TRP A 241      30.791  73.385  57.997  1.00 13.27           C  
ANISOU 1951  CA  TRP A 241     1955   1414   1672     12    333     27       C  
ATOM   1952  C   TRP A 241      29.906  72.150  57.966  1.00 12.59           C  
ANISOU 1952  C   TRP A 241     1555   1763   1465    -90   -175    319       C  
ATOM   1953  O   TRP A 241      29.636  71.670  56.880  1.00 13.88           O  
ANISOU 1953  O   TRP A 241     2213   1553   1507    -59    187     61       O  
ATOM   1954  CB  TRP A 241      29.929  74.625  57.952  1.00 14.29           C  
ANISOU 1954  CB  TRP A 241     1722   1760   1947    184      0    -29       C  
ATOM   1955  CG  TRP A 241      28.905  74.892  59.007  1.00 16.39           C  
ANISOU 1955  CG  TRP A 241     1827   1957   2442    106    248   -369       C  
ATOM   1956  CD1 TRP A 241      29.085  75.625  60.142  1.00 18.47           C  
ANISOU 1956  CD1 TRP A 241     2111   2522   2385   -340    516   -508       C  
ATOM   1957  CD2 TRP A 241      27.536  74.448  59.053  1.00 16.56           C  
ANISOU 1957  CD2 TRP A 241     1735   2046   2511    210    155   -271       C  
ATOM   1958  NE1 TRP A 241      27.926  75.665  60.880  1.00 19.10           N  
ANISOU 1958  NE1 TRP A 241     2084   2725   2448   -264    515   -482       N  
ATOM   1959  CE2 TRP A 241      26.952  74.949  60.239  1.00 17.42           C  
ANISOU 1959  CE2 TRP A 241     1920   2369   2330    -18    293   -128       C  
ATOM   1960  CE3 TRP A 241      26.744  73.672  58.201  1.00 16.89           C  
ANISOU 1960  CE3 TRP A 241     2005   1930   2484    -94    171    -84       C  
ATOM   1961  CZ2 TRP A 241      25.620  74.711  60.613  1.00 16.82           C  
ANISOU 1961  CZ2 TRP A 241     1939   2109   2343     26    291     51       C  
ATOM   1962  CZ3 TRP A 241      25.421  73.434  58.566  1.00 15.66           C  
ANISOU 1962  CZ3 TRP A 241     1778   1757   2415    252    -63    143       C  
ATOM   1963  CH2 TRP A 241      24.851  73.939  59.750  1.00 15.11           C  
ANISOU 1963  CH2 TRP A 241     1767   1773   2201    360    -88    427       C  
ATOM   1964  N   THR A 242      29.534  71.656  59.146  1.00 12.28           N  
ANISOU 1964  N   THR A 242     1521   1631   1513     57    199    100       N  
ATOM   1965  CA  THR A 242      28.715  70.448  59.187  1.00 11.96           C  
ANISOU 1965  CA  THR A 242     1374   1537   1634    187    148    216       C  
ATOM   1966  C   THR A 242      27.661  70.571  60.278  1.00 11.48           C  
ANISOU 1966  C   THR A 242     1320   1442   1600     62    101    -85       C  
ATOM   1967  O   THR A 242      27.806  71.343  61.230  1.00 13.71           O  
ANISOU 1967  O   THR A 242     1766   1828   1617   -215     38   -208       O  
ATOM   1968  CB  THR A 242      29.538  69.167  59.487  1.00 12.04           C  
ANISOU 1968  CB  THR A 242     1427   1604   1544    294    -20    -16       C  
ATOM   1969  OG1 THR A 242      30.012  69.252  60.844  1.00 14.90           O  
ANISOU 1969  OG1 THR A 242     2351   1764   1547     59   -238    344       O  
ATOM   1970  CG2 THR A 242      30.733  69.031  58.567  1.00 12.52           C  
ANISOU 1970  CG2 THR A 242     1326   1530   1900    150    101    139       C  
ATOM   1971  N   ALA A 243      26.595  69.786  60.126  1.00 11.31           N  
ANISOU 1971  N   ALA A 243     1369   1450   1477     27     51      6       N  
ATOM   1972  CA  ALA A 243      25.557  69.711  61.130  1.00 11.72           C  
ANISOU 1972  CA  ALA A 243     1484   1378   1589    -19    177    -30       C  
ATOM   1973  C   ALA A 243      24.861  68.351  61.037  1.00 10.58           C  
ANISOU 1973  C   ALA A 243     1494   1185   1342    166     73    130       C  
ATOM   1974  O   ALA A 243      24.921  67.715  59.990  1.00 11.14           O  
ANISOU 1974  O   ALA A 243     1275   1406   1551    -49    359    -82       O  
ATOM   1975  CB  ALA A 243      24.507  70.798  60.946  1.00 14.46           C  
ANISOU 1975  CB  ALA A 243     2245   1230   2019    333    977    365       C  
ATOM   1976  N   GLN A 244      24.224  67.976  62.139  1.00 10.87           N  
ANISOU 1976  N   GLN A 244     1287   1467   1375     73     99     64       N  
ATOM   1977  CA  GLN A 244      23.381  66.797  62.178  1.00 10.56           C  
ANISOU 1977  CA  GLN A 244     1327   1312   1374    161    207    -22       C  
ATOM   1978  C   GLN A 244      22.139  67.188  62.985  1.00 11.53           C  
ANISOU 1978  C   GLN A 244     1370   1471   1539    143    323    -17       C  
ATOM   1979  O   GLN A 244      22.271  67.859  64.013  1.00 13.51           O  
ANISOU 1979  O   GLN A 244     1657   1907   1568    -98    616   -213       O  
ATOM   1980  CB  GLN A 244      24.035  65.613  62.867  1.00 11.95           C  
ANISOU 1980  CB  GLN A 244     1176   1480   1885     82    -41    150       C  
ATOM   1981  CG  GLN A 244      23.255  64.318  62.739  1.00 13.55           C  
ANISOU 1981  CG  GLN A 244     1643   1248   2256    136    270    -55       C  
ATOM   1982  CD  GLN A 244      23.743  63.260  63.707  1.00 12.81           C  
ANISOU 1982  CD  GLN A 244     1595   1385   1886     79    409    -49       C  
ATOM   1983  OE1 GLN A 244      23.950  63.522  64.896  1.00 13.87           O  
ANISOU 1983  OE1 GLN A 244     1465   1550   2252    213   -150   -444       O  
ATOM   1984  NE2 GLN A 244      23.911  62.047  63.195  1.00 11.38           N  
ANISOU 1984  NE2 GLN A 244     1388   1394   1544    202    166     19       N  
ATOM   1985  N   THR A 245      20.972  66.778  62.510  1.00 13.00           N  
ANISOU 1985  N   THR A 245     1331   1664   1943    171    223     24       N  
ATOM   1986  CA  THR A 245      19.784  67.029  63.308  1.00 13.21           C  
ANISOU 1986  CA  THR A 245     1325   1672   2023    220    233     87       C  
ATOM   1987  C   THR A 245      18.745  65.917  63.167  1.00 11.95           C  
ANISOU 1987  C   THR A 245     1119   1743   1677    309     -8     59       C  
ATOM   1988  O   THR A 245      18.847  65.091  62.258  1.00 14.94           O  
ANISOU 1988  O   THR A 245     1813   2161   1703    -81    329   -150       O  
ATOM   1989  CB  THR A 245      19.164  68.387  62.939  1.00 14.18           C  
ANISOU 1989  CB  THR A 245     1885   1652   1850    444    168   -150       C  
ATOM   1990  OG1 THR A 245      18.228  68.772  63.954  1.00 18.04           O  
ANISOU 1990  OG1 THR A 245     2470   1908   2477    532    688   -367       O  
ATOM   1991  CG2 THR A 245      18.419  68.263  61.627  1.00 16.75           C  
ANISOU 1991  CG2 THR A 245     2288   1968   2109    292   -222    130       C  
ATOM   1992  N   ILE A 246      17.781  65.922  64.071  1.00 10.91           N  
ANISOU 1992  N   ILE A 246     1467   1388   1290    185     -1    330       N  
ATOM   1993  CA  ILE A 246      16.696  64.971  64.105  1.00 11.59           C  
ANISOU 1993  CA  ILE A 246     1468   1381   1554    182    -81    504       C  
ATOM   1994  C   ILE A 246      15.423  65.750  63.782  1.00 11.43           C  
ANISOU 1994  C   ILE A 246     1482   1281   1578    212   -100    224       C  
ATOM   1995  O   ILE A 246      15.125  66.727  64.482  1.00 13.00           O  
ANISOU 1995  O   ILE A 246     1654   1607   1677    229    223     58       O  
ATOM   1996  CB  ILE A 246      16.578  64.272  65.474  1.00 11.92           C  
ANISOU 1996  CB  ILE A 246     1269   1726   1533    185    114    501       C  
ATOM   1997  CG1 ILE A 246      17.818  63.439  65.815  1.00 11.27           C  
ANISOU 1997  CG1 ILE A 246     1473   1423   1386    154    -92    465       C  
ATOM   1998  CG2 ILE A 246      15.283  63.457  65.524  1.00 12.10           C  
ANISOU 1998  CG2 ILE A 246     1404   1772   1422     54    187    243       C  
ATOM   1999  CD1 ILE A 246      17.967  63.123  67.295  1.00 11.64           C  
ANISOU 1999  CD1 ILE A 246     1481   1677   1266    338    202    359       C  
ATOM   2000  N   ALA A 247      14.746  65.354  62.721  1.00 11.75           N  
ANISOU 2000  N   ALA A 247     1176   1693   1593     37     13    201       N  
ATOM   2001  CA  ALA A 247      13.578  66.101  62.260  1.00 12.57           C  
ANISOU 2001  CA  ALA A 247     1228   1945   1601    214    -19    -27       C  
ATOM   2002  C   ALA A 247      12.446  65.950  63.295  1.00 13.37           C  
ANISOU 2002  C   ALA A 247     1379   1726   1974    218    231     24       C  
ATOM   2003  O   ALA A 247      12.245  64.876  63.872  1.00 14.10           O  
ANISOU 2003  O   ALA A 247     1166   1841   2350    158     99    224       O  
ATOM   2004  CB  ALA A 247      13.086  65.662  60.883  1.00 14.68           C  
ANISOU 2004  CB  ALA A 247     1322   2552   1705   -254   -195     46       C  
ATOM   2005  N   PRO A 248      11.700  67.015  63.541  1.00 15.06           N  
ANISOU 2005  N   PRO A 248     1486   1840   2395    348    363     74       N  
ATOM   2006  CA  PRO A 248      10.544  66.884  64.417  1.00 16.65           C  
ANISOU 2006  CA  PRO A 248     1649   1928   2751    322    628    -19       C  
ATOM   2007  C   PRO A 248       9.487  65.968  63.785  1.00 16.56           C  
ANISOU 2007  C   PRO A 248     1436   2063   2791    399    607    -25       C  
ATOM   2008  O   PRO A 248       9.406  65.770  62.580  1.00 17.52           O  
ANISOU 2008  O   PRO A 248     1465   2479   2713    274    156    418       O  
ATOM   2009  CB  PRO A 248       9.982  68.297  64.539  1.00 18.48           C  
ANISOU 2009  CB  PRO A 248     2014   1984   3023    435    837    -62       C  
ATOM   2010  CG  PRO A 248      10.519  69.002  63.327  1.00 17.06           C  
ANISOU 2010  CG  PRO A 248     1728   1943   2811    549    523     -2       C  
ATOM   2011  CD  PRO A 248      11.867  68.388  63.008  1.00 15.95           C  
ANISOU 2011  CD  PRO A 248     1546   1818   2695    424    408    136       C  
ATOM   2012  N   ASP A 249       8.662  65.377  64.654  1.00 17.28           N  
ANISOU 2012  N   ASP A 249     1292   2321   2950    392    680      8       N  
ATOM   2013  CA  ASP A 249       7.505  64.608  64.209  1.00 19.24           C  
ANISOU 2013  CA  ASP A 249     1451   2466   3393    246    491     84       C  
ATOM   2014  C   ASP A 249       7.935  63.466  63.308  1.00 19.02           C  
ANISOU 2014  C   ASP A 249     1796   2448   2982    258    207    113       C  
ATOM   2015  O   ASP A 249       7.232  63.099  62.368  1.00 22.22           O  
ANISOU 2015  O   ASP A 249     2160   2935   3346    586   -273      6       O  
ATOM   2016  CB  ASP A 249       6.496  65.493  63.465  1.00 20.73           C  
ANISOU 2016  CB  ASP A 249     1656   2842   3377    454    240    -97       C  
ATOM   2017  CG  ASP A 249       6.011  66.648  64.334  1.00 23.44           C  
ANISOU 2017  CG  ASP A 249     2159   2984   3762    824    608    -32       C  
ATOM   2018  OD1 ASP A 249       5.580  66.413  65.493  1.00 28.22           O  
ANISOU 2018  OD1 ASP A 249     2720   3820   4183    408   1397   -313       O  
ATOM   2019  OD2 ASP A 249       6.037  67.821  63.899  1.00 32.24           O  
ANISOU 2019  OD2 ASP A 249     4754   2824   4671    725    777    -91       O  
ATOM   2020  N   SER A 250       9.101  62.910  63.629  1.00 16.31           N  
ANISOU 2020  N   SER A 250     1766   2177   2254    208    325     17       N  
ATOM   2021  CA  SER A 250       9.598  61.816  62.797  1.00 14.39           C  
ANISOU 2021  CA  SER A 250     1636   2126   1704    -52    126     32       C  
ATOM   2022  C   SER A 250       9.908  60.537  63.563  1.00 14.81           C  
ANISOU 2022  C   SER A 250     1883   2011   1734      1    328    -10       C  
ATOM   2023  O   SER A 250      10.574  59.646  62.980  1.00 15.37           O  
ANISOU 2023  O   SER A 250     1715   2112   2014    -22    471    -55       O  
ATOM   2024  CB  SER A 250      10.869  62.292  62.077  1.00 13.91           C  
ANISOU 2024  CB  SER A 250     1672   2257   1357   -169     26     -8       C  
ATOM   2025  OG  SER A 250      11.980  62.362  62.961  1.00 13.90           O  
ANISOU 2025  OG  SER A 250     1556   2086   1638    161    -24     37       O  
ATOM   2026  N   GLU A 251       9.463  60.431  64.803  1.00 14.70           N  
ANISOU 2026  N   GLU A 251     1739   2095   1752     68    307     53       N  
ATOM   2027  CA  GLU A 251       9.820  59.260  65.593  1.00 17.28           C  
ANISOU 2027  CA  GLU A 251     2404   2208   1954     53    285    243       C  
ATOM   2028  C   GLU A 251       9.377  57.986  64.894  1.00 17.18           C  
ANISOU 2028  C   GLU A 251     2080   2108   2337    107     71    306       C  
ATOM   2029  O   GLU A 251       8.230  57.821  64.453  1.00 19.39           O  
ANISOU 2029  O   GLU A 251     2130   2135   3104     26   -146    577       O  
ATOM   2030  CB  GLU A 251       9.226  59.358  67.010  1.00 18.87           C  
ANISOU 2030  CB  GLU A 251     2569   2587   2013    196    417    448       C  
ATOM   2031  CG  GLU A 251       9.751  58.225  67.877  1.00 24.10           C  
ANISOU 2031  CG  GLU A 251     3838   2895   2422   -216   -194    942       C  
ATOM   2032  CD  GLU A 251       9.589  58.501  69.358  1.00 28.23           C  
ANISOU 2032  CD  GLU A 251     4913   3459   2355   -645   -127   1057       C  
ATOM   2033  OE1 GLU A 251       8.847  59.419  69.751  1.00 32.21           O  
ANISOU 2033  OE1 GLU A 251     5388   4104   2744   -673    725    491       O  
ATOM   2034  OE2 GLU A 251      10.233  57.772  70.152  1.00 35.11           O  
ANISOU 2034  OE2 GLU A 251     6046   4415   2878   -967  -1578   1177       O  
ATOM   2035  N   GLY A 252      10.325  57.061  64.748  1.00 17.81           N  
ANISOU 2035  N   GLY A 252     2192   2105   2468    174    -27    307       N  
ATOM   2036  CA  GLY A 252      10.006  55.809  64.083  1.00 17.60           C  
ANISOU 2036  CA  GLY A 252     2074   1985   2629    201   -189    414       C  
ATOM   2037  C   GLY A 252       9.920  55.819  62.579  1.00 17.03           C  
ANISOU 2037  C   GLY A 252     1852   1975   2642    196   -307    285       C  
ATOM   2038  O   GLY A 252       9.561  54.823  61.931  1.00 19.92           O  
ANISOU 2038  O   GLY A 252     2704   1995   2869    -36   -481    301       O  
ATOM   2039  N   ALA A 253      10.244  56.914  61.918  1.00 15.64           N  
ANISOU 2039  N   ALA A 253     1622   1972   2348    171   -158    122       N  
ATOM   2040  CA  ALA A 253      10.130  57.017  60.475  1.00 14.78           C  
ANISOU 2040  CA  ALA A 253     1567   1687   2362    305   -351    -27       C  
ATOM   2041  C   ALA A 253      10.926  55.964  59.708  1.00 16.25           C  
ANISOU 2041  C   ALA A 253     1816   1828   2532    435   -423   -187       C  
ATOM   2042  O   ALA A 253      10.418  55.383  58.742  1.00 19.24           O  
ANISOU 2042  O   ALA A 253     2587   2220   2503    491   -573   -377       O  
ATOM   2043  CB  ALA A 253      10.603  58.405  60.034  1.00 15.11           C  
ANISOU 2043  CB  ALA A 253     1814   1765   2162    192     -1   -104       C  
ATOM   2044  N   ILE A 254      12.171  55.727  60.099  1.00 16.96           N  
ANISOU 2044  N   ILE A 254     1705   2032   2709    529   -185     96       N  
ATOM   2045  CA  ILE A 254      13.026  54.714  59.488  1.00 17.50           C  
ANISOU 2045  CA  ILE A 254     1896   2123   2629    569   -259    -69       C  
ATOM   2046  C   ILE A 254      13.716  53.943  60.586  1.00 18.49           C  
ANISOU 2046  C   ILE A 254     1992   1983   3049    599   -613   -111       C  
ATOM   2047  O   ILE A 254      14.539  54.483  61.320  1.00 22.80           O  
ANISOU 2047  O   ILE A 254     2560   2155   3949    443  -1345      0       O  
ATOM   2048  CB  ILE A 254      14.093  55.341  58.574  1.00 19.54           C  
ANISOU 2048  CB  ILE A 254     1958   2523   2943    517     31   -195       C  
ATOM   2049  CG1 ILE A 254      13.495  56.257  57.492  1.00 19.78           C  
ANISOU 2049  CG1 ILE A 254     2117   2526   2871    195    141     47       C  
ATOM   2050  CG2 ILE A 254      14.988  54.295  57.936  1.00 20.35           C  
ANISOU 2050  CG2 ILE A 254     2146   2852   2734    553   -150   -625       C  
ATOM   2051  CD1 ILE A 254      14.551  57.206  56.951  1.00 22.17           C  
ANISOU 2051  CD1 ILE A 254     2386   2734   3303   -137    284   -144       C  
ATOM   2052  N  AASP A 255      13.357  52.668  60.764  0.47 18.82           N  
ANISOU 2052  N  AASP A 255     1974   2006   3172    600   -604    -58       N  
ATOM   2053  N  BASP A 255      13.368  52.664  60.719  0.54 18.88           N  
ANISOU 2053  N  BASP A 255     1984   2006   3183    594   -606    -67       N  
ATOM   2054  CA AASP A 255      13.985  51.837  61.791  0.47 18.66           C  
ANISOU 2054  CA AASP A 255     2031   2068   2989    614   -448    -27       C  
ATOM   2055  CA BASP A 255      14.016  51.841  61.742  0.54 18.73           C  
ANISOU 2055  CA BASP A 255     2052   2054   3012    612   -446    -18       C  
ATOM   2056  C  AASP A 255      14.605  50.579  61.181  0.47 17.97           C  
ANISOU 2056  C  AASP A 255     2032   1930   2864    538   -446     70       C  
ATOM   2057  C  BASP A 255      14.670  50.614  61.127  0.54 17.75           C  
ANISOU 2057  C  BASP A 255     2007   1930   2809    517   -461     57       C  
ATOM   2058  O  AASP A 255      14.203  50.101  60.119  0.47 17.04           O  
ANISOU 2058  O  AASP A 255     1285   2198   2994    612   -386    -86       O  
ATOM   2059  O  BASP A 255      14.355  50.204  60.008  0.54 16.16           O  
ANISOU 2059  O  BASP A 255     1324   2122   2693    410   -269    135       O  
ATOM   2060  CB AASP A 255      13.002  51.398  62.869  0.47 20.17           C  
ANISOU 2060  CB AASP A 255     2264   2317   3081    470   -263   -160       C  
ATOM   2061  CB BASP A 255      12.981  51.430  62.794  0.54 20.56           C  
ANISOU 2061  CB BASP A 255     2432   2338   3044    420   -193   -243       C  
ATOM   2062  CG AASP A 255      12.473  52.489  63.768  0.47 21.26           C  
ANISOU 2062  CG AASP A 255     2309   2424   3346    499   -146   -259       C  
ATOM   2063  CG BASP A 255      11.831  52.425  62.785  0.54 20.78           C  
ANISOU 2063  CG BASP A 255     2267   2493   3136    396   -147   -302       C  
ATOM   2064  OD1AASP A 255      12.882  53.660  63.598  0.47 21.37           O  
ANISOU 2064  OD1AASP A 255     1656   2427   4036    423   -745   -502       O  
ATOM   2065  OD1BASP A 255      12.049  53.524  63.367  0.54 24.66           O  
ANISOU 2065  OD1BASP A 255     2864   2476   4027    476    -93   -573       O  
ATOM   2066  OD2AASP A 255      11.631  52.180  64.652  0.47 27.89           O  
ANISOU 2066  OD2AASP A 255     3684   3213   3700    354    721   -328       O  
ATOM   2067  OD2BASP A 255      10.790  52.160  62.164  0.54 22.15           O  
ANISOU 2067  OD2BASP A 255     2527   2950   2941    257   -439    371       O  
ATOM   2068  N   GLY A 256      15.583  50.015  61.886  1.00 15.93           N  
ANISOU 2068  N   GLY A 256     1983   1688   2383    379   -269    152       N  
ATOM   2069  CA  GLY A 256      16.195  48.774  61.417  1.00 14.54           C  
ANISOU 2069  CA  GLY A 256     1749   1592   2186    220   -155    250       C  
ATOM   2070  C   GLY A 256      16.692  48.036  62.656  1.00 13.30           C  
ANISOU 2070  C   GLY A 256     1583   1491   1979    139   -102    112       C  
ATOM   2071  O   GLY A 256      17.445  48.601  63.467  1.00 16.01           O  
ANISOU 2071  O   GLY A 256     2332   1352   2399     88   -534     18       O  
ATOM   2072  N   HIS A 257      16.291  46.779  62.818  1.00 12.75           N  
ANISOU 2072  N   HIS A 257     1424   1446   1974    211   -209     67       N  
ATOM   2073  CA  HIS A 257      16.693  46.003  63.988  1.00 12.44           C  
ANISOU 2073  CA  HIS A 257     1227   1526   1972    321    -63    137       C  
ATOM   2074  C   HIS A 257      17.516  44.795  63.546  1.00 12.39           C  
ANISOU 2074  C   HIS A 257     1392   1524   1792    303   -127     15       C  
ATOM   2075  O   HIS A 257      17.109  44.143  62.570  1.00 15.05           O  
ANISOU 2075  O   HIS A 257     2306   1494   1920    226   -444     27       O  
ATOM   2076  CB  HIS A 257      15.459  45.530  64.772  1.00 15.36           C  
ANISOU 2076  CB  HIS A 257     1901   1732   2203     84    518   -137       C  
ATOM   2077  CG  HIS A 257      14.525  46.650  65.091  1.00 16.87           C  
ANISOU 2077  CG  HIS A 257     1707   2138   2564    183    522   -336       C  
ATOM   2078  ND1 HIS A 257      14.862  47.761  65.827  1.00 15.09           N  
ANISOU 2078  ND1 HIS A 257     1648   1874   2213    473    327    -99       N  
ATOM   2079  CD2 HIS A 257      13.209  46.813  64.772  1.00 18.58           C  
ANISOU 2079  CD2 HIS A 257     2059   2216   2784    364    -86   -236       C  
ATOM   2080  CE1 HIS A 257      13.812  48.576  65.941  1.00 15.74           C  
ANISOU 2080  CE1 HIS A 257     1570   2093   2319    563      0    -81       C  
ATOM   2081  NE2 HIS A 257      12.786  48.018  65.306  1.00 17.96           N  
ANISOU 2081  NE2 HIS A 257     1971   2097   2756    483   -355    -94       N  
ATOM   2082  N   LEU A 258      18.636  44.549  64.257  1.00 13.06           N  
ANISOU 2082  N   LEU A 258     1466   1411   2084    419   -212    104       N  
ATOM   2083  CA  LEU A 258      19.500  43.430  63.876  1.00 11.83           C  
ANISOU 2083  CA  LEU A 258     1340   1354   1801    227    -52    -29       C  
ATOM   2084  C   LEU A 258      19.062  42.243  64.752  1.00 12.89           C  
ANISOU 2084  C   LEU A 258     1709   1359   1829    239   -287    106       C  
ATOM   2085  O   LEU A 258      19.171  42.285  65.979  1.00 15.99           O  
ANISOU 2085  O   LEU A 258     2555   1636   1885   -159   -642    263       O  
ATOM   2086  CB  LEU A 258      20.982  43.721  64.031  1.00 12.58           C  
ANISOU 2086  CB  LEU A 258     1350   1682   1747    262   -162   -298       C  
ATOM   2087  CG  LEU A 258      21.939  42.658  63.500  1.00 13.62           C  
ANISOU 2087  CG  LEU A 258     1358   1980   1837    247     45   -460       C  
ATOM   2088  CD1 LEU A 258      21.865  42.626  61.989  1.00 19.14           C  
ANISOU 2088  CD1 LEU A 258     2807   2581   1885    -99   -101  -1038       C  
ATOM   2089  CD2 LEU A 258      23.381  42.928  63.922  1.00 16.37           C  
ANISOU 2089  CD2 LEU A 258     1300   2566   2354    257    124   -980       C  
ATOM   2090  N   ARG A 259      18.519  41.247  64.080  1.00 12.90           N  
ANISOU 2090  N   ARG A 259     1798   1317   1788    169    120    -55       N  
ATOM   2091  CA  ARG A 259      17.842  40.118  64.715  1.00 14.37           C  
ANISOU 2091  CA  ARG A 259     1731   1446   2285    152    483    -56       C  
ATOM   2092  C   ARG A 259      18.425  38.783  64.273  1.00 12.76           C  
ANISOU 2092  C   ARG A 259     1630   1342   1877     92    370     36       C  
ATOM   2093  O   ARG A 259      19.272  38.744  63.357  1.00 12.31           O  
ANISOU 2093  O   ARG A 259     1289   1535   1854     25    205    -60       O  
ATOM   2094  CB  ARG A 259      16.333  40.131  64.382  1.00 15.83           C  
ANISOU 2094  CB  ARG A 259     1748   1503   2764    250    373     28       C  
ATOM   2095  CG  ARG A 259      15.635  41.465  64.699  1.00 15.73           C  
ANISOU 2095  CG  ARG A 259     1898   1702   2377    343    630   -133       C  
ATOM   2096  CD  ARG A 259      15.617  41.830  66.168  1.00 18.28           C  
ANISOU 2096  CD  ARG A 259     2648   1955   2345   -122    536   -100       C  
ATOM   2097  NE  ARG A 259      14.644  41.153  67.022  1.00 16.41           N  
ANISOU 2097  NE  ARG A 259     2149   1982   2106    159    304      9       N  
ATOM   2098  CZ  ARG A 259      14.517  41.339  68.332  1.00 17.14           C  
ANISOU 2098  CZ  ARG A 259     2370   1999   2144     -6    310   -116       C  
ATOM   2099  NH1 ARG A 259      15.332  42.201  68.941  1.00 18.17           N  
ANISOU 2099  NH1 ARG A 259     2518   2163   2221   -247    309    -40       N  
ATOM   2100  NH2 ARG A 259      13.596  40.683  69.058  1.00 16.63           N  
ANISOU 2100  NH2 ARG A 259     2167   2350   1803   -153     17   -101       N  
ATOM   2101  N   GLU A 260      17.955  37.703  64.885  1.00 12.36           N  
ANISOU 2101  N   GLU A 260     1590   1515   1589    130    -64    326       N  
ATOM   2102  CA  GLU A 260      18.396  36.370  64.395  1.00 13.18           C  
ANISOU 2102  CA  GLU A 260     1941   1364   1702     88   -419    326       C  
ATOM   2103  C   GLU A 260      18.018  36.146  62.929  1.00 12.83           C  
ANISOU 2103  C   GLU A 260     1580   1625   1670     94   -259    226       C  
ATOM   2104  O   GLU A 260      18.690  35.325  62.290  1.00 13.54           O  
ANISOU 2104  O   GLU A 260     1547   1610   1987    -21   -236     28       O  
ATOM   2105  CB  GLU A 260      17.805  35.263  65.276  1.00 12.71           C  
ANISOU 2105  CB  GLU A 260     1657   1504   1670    -94   -396    218       C  
ATOM   2106  CG  GLU A 260      18.363  35.306  66.697  1.00 13.57           C  
ANISOU 2106  CG  GLU A 260     1891   1702   1564   -153   -311    245       C  
ATOM   2107  CD  GLU A 260      17.575  34.456  67.692  1.00 13.38           C  
ANISOU 2107  CD  GLU A 260     1659   1752   1672    -53   -203    215       C  
ATOM   2108  OE1 GLU A 260      17.204  33.319  67.327  1.00 13.94           O  
ANISOU 2108  OE1 GLU A 260     1918   1678   1701    -80   -105    252       O  
ATOM   2109  OE2 GLU A 260      17.325  34.976  68.799  1.00 13.58           O  
ANISOU 2109  OE2 GLU A 260     1705   1773   1682    -27   -196    209       O  
ATOM   2110  N   ALA A 261      17.017  36.846  62.413  1.00 12.88           N  
ANISOU 2110  N   ALA A 261     1354   1826   1715    -21   -282    290       N  
ATOM   2111  CA  ALA A 261      16.648  36.774  60.985  1.00 12.12           C  
ANISOU 2111  CA  ALA A 261     1261   1619   1724    -97   -263    189       C  
ATOM   2112  C   ALA A 261      17.325  37.854  60.145  1.00 12.20           C  
ANISOU 2112  C   ALA A 261     1470   1537   1630     31    178    -11       C  
ATOM   2113  O   ALA A 261      16.940  38.118  58.996  1.00 13.16           O  
ANISOU 2113  O   ALA A 261     1588   1610   1801    118     53    196       O  
ATOM   2114  CB  ALA A 261      15.129  36.877  60.812  1.00 15.15           C  
ANISOU 2114  CB  ALA A 261     1274   2368   2113   -335   -417    125       C  
ATOM   2115  N   GLY A 262      18.368  38.514  60.669  1.00 11.67           N  
ANISOU 2115  N   GLY A 262     1477   1388   1569    -20    355    -80       N  
ATOM   2116  CA  GLY A 262      19.026  39.529  59.841  1.00 11.48           C  
ANISOU 2116  CA  GLY A 262     1286   1367   1709    245    347    115       C  
ATOM   2117  C   GLY A 262      18.565  40.926  60.225  1.00 11.18           C  
ANISOU 2117  C   GLY A 262     1174   1367   1707    211    125     53       C  
ATOM   2118  O   GLY A 262      17.982  41.150  61.278  1.00 12.60           O  
ANISOU 2118  O   GLY A 262     1752   1291   1745    145    299    -67       O  
ATOM   2119  N   LEU A 263      18.868  41.874  59.328  1.00 11.82           N  
ANISOU 2119  N   LEU A 263     1754   1321   1416    143   -100    -18       N  
ATOM   2120  CA  LEU A 263      18.532  43.266  59.553  1.00 11.67           C  
ANISOU 2120  CA  LEU A 263     1512   1305   1618     80     52    -41       C  
ATOM   2121  C   LEU A 263      17.200  43.572  58.883  1.00 12.06           C  
ANISOU 2121  C   LEU A 263     1470   1444   1670    123    108     -2       C  
ATOM   2122  O   LEU A 263      17.045  43.433  57.676  1.00 12.79           O  
ANISOU 2122  O   LEU A 263     1510   1647   1702    -49     -3     -3       O  
ATOM   2123  CB  LEU A 263      19.622  44.174  58.969  1.00 11.28           C  
ANISOU 2123  CB  LEU A 263     1434   1312   1540    211    229   -123       C  
ATOM   2124  CG  LEU A 263      19.387  45.683  59.234  1.00 14.83           C  
ANISOU 2124  CG  LEU A 263     2461   1241   1932     11    567   -107       C  
ATOM   2125  CD1 LEU A 263      19.383  45.978  60.717  1.00 16.60           C  
ANISOU 2125  CD1 LEU A 263     2883   1366   2058   -435    738   -443       C  
ATOM   2126  CD2 LEU A 263      20.463  46.494  58.510  1.00 15.28           C  
ANISOU 2126  CD2 LEU A 263     2340   1525   1943   -143    316     63       C  
ATOM   2127  N   THR A 264      16.259  43.987  59.730  1.00 13.42           N  
ANISOU 2127  N   THR A 264     1538   1604   1955    107    295     -5       N  
ATOM   2128  CA  THR A 264      14.923  44.321  59.284  1.00 14.37           C  
ANISOU 2128  CA  THR A 264     1618   1753   2089    329    306     65       C  
ATOM   2129  C   THR A 264      14.899  45.790  58.855  1.00 17.67           C  
ANISOU 2129  C   THR A 264     2361   1865   2487    134   -391    309       C  
ATOM   2130  O   THR A 264      15.822  46.540  59.183  1.00 18.98           O  
ANISOU 2130  O   THR A 264     2679   1694   2837    155   -641    128       O  
ATOM   2131  CB  THR A 264      13.866  44.118  60.391  1.00 16.09           C  
ANISOU 2131  CB  THR A 264     1625   2259   2230    165    422   -238       C  
ATOM   2132  OG1 THR A 264      14.162  45.019  61.475  1.00 21.13           O  
ANISOU 2132  OG1 THR A 264     2650   3277   2101    185    181   -576       O  
ATOM   2133  CG2 THR A 264      13.912  42.712  60.961  1.00 24.88           C  
ANISOU 2133  CG2 THR A 264     3005   2762   3685   -674    747    752       C  
ATOM   2134  N   PHE A 265      13.881  46.183  58.125  1.00 16.18           N  
ANISOU 2134  N   PHE A 265     1900   1948   2300    454    100    144       N  
ATOM   2135  CA  PHE A 265      13.781  47.529  57.568  1.00 16.24           C  
ANISOU 2135  CA  PHE A 265     1903   1934   2336    340   -190    124       C  
ATOM   2136  C   PHE A 265      12.315  47.936  57.700  1.00 16.42           C  
ANISOU 2136  C   PHE A 265     1842   2001   2397    342   -518     72       C  
ATOM   2137  O   PHE A 265      11.438  47.202  57.215  1.00 17.27           O  
ANISOU 2137  O   PHE A 265     2001   2305   2256   -110    -84     -2       O  
ATOM   2138  CB  PHE A 265      14.256  47.537  56.112  1.00 18.04           C  
ANISOU 2138  CB  PHE A 265     2373   2158   2325    106   -133    254       C  
ATOM   2139  CG  PHE A 265      14.061  48.868  55.394  1.00 17.96           C  
ANISOU 2139  CG  PHE A 265     2599   1985   2241    464     79      7       C  
ATOM   2140  CD1 PHE A 265      14.810  49.983  55.751  1.00 19.40           C  
ANISOU 2140  CD1 PHE A 265     2740   2099   2530    202    113    207       C  
ATOM   2141  CD2 PHE A 265      13.118  48.980  54.372  1.00 17.51           C  
ANISOU 2141  CD2 PHE A 265     2477   1987   2191    748    189    -31       C  
ATOM   2142  CE1 PHE A 265      14.610  51.200  55.122  1.00 19.60           C  
ANISOU 2142  CE1 PHE A 265     2745   2093   2610    308     27    176       C  
ATOM   2143  CE2 PHE A 265      12.941  50.189  53.739  1.00 18.45           C  
ANISOU 2143  CE2 PHE A 265     2522   2015   2471    532    113    117       C  
ATOM   2144  CZ  PHE A 265      13.687  51.289  54.091  1.00 19.81           C  
ANISOU 2144  CZ  PHE A 265     2627   2090   2810    497    -24     29       C  
ATOM   2145  N   HIS A 266      12.074  49.055  58.377  1.00 16.97           N  
ANISOU 2145  N   HIS A 266     1623   2404   2419    367   -448   -236       N  
ATOM   2146  CA  HIS A 266      10.707  49.531  58.538  1.00 19.34           C  
ANISOU 2146  CA  HIS A 266     1773   2682   2893    597   -231    110       C  
ATOM   2147  C   HIS A 266      10.607  51.015  58.200  1.00 19.03           C  
ANISOU 2147  C   HIS A 266     1881   2583   2765    587   -198   -133       C  
ATOM   2148  O   HIS A 266      11.532  51.773  58.458  1.00 19.75           O  
ANISOU 2148  O   HIS A 266     1915   2723   2867    485   -208    -29       O  
ATOM   2149  CB  HIS A 266      10.256  49.376  59.984  1.00 22.01           C  
ANISOU 2149  CB  HIS A 266     2160   3040   3162    584    225    210       C  
ATOM   2150  CG  HIS A 266      10.705  48.109  60.635  1.00 24.28           C  
ANISOU 2150  CG  HIS A 266     2677   3302   3246    372   -160    561       C  
ATOM   2151  ND1 HIS A 266       9.867  47.032  60.776  1.00 23.68           N  
ANISOU 2151  ND1 HIS A 266     2319   3095   3585    679    411    378       N  
ATOM   2152  CD2 HIS A 266      11.899  47.743  61.183  1.00 26.03           C  
ANISOU 2152  CD2 HIS A 266     3223   3349   3320     72   -896    762       C  
ATOM   2153  CE1 HIS A 266      10.525  46.056  61.387  1.00 25.40           C  
ANISOU 2153  CE1 HIS A 266     2800   3370   3480    291   -274    698       C  
ATOM   2154  NE2 HIS A 266      11.764  46.460  61.642  1.00 26.46           N  
ANISOU 2154  NE2 HIS A 266     3260   3539   3255    -91   -875    977       N  
ATOM   2155  N   LEU A 267       9.486  51.408  57.627  1.00 18.63           N  
ANISOU 2155  N   LEU A 267     2129   2518   2431    422   -380    137       N  
ATOM   2156  CA  LEU A 267       9.169  52.784  57.324  1.00 18.66           C  
ANISOU 2156  CA  LEU A 267     2140   2478   2473    338   -316    158       C  
ATOM   2157  C   LEU A 267       7.787  53.048  57.909  1.00 18.98           C  
ANISOU 2157  C   LEU A 267     1941   2423   2847    303   -465    137       C  
ATOM   2158  O   LEU A 267       6.826  52.474  57.410  1.00 24.98           O  
ANISOU 2158  O   LEU A 267     2143   3224   4125    169   -680   -583       O  
ATOM   2159  CB  LEU A 267       9.119  53.063  55.819  1.00 19.79           C  
ANISOU 2159  CB  LEU A 267     2224   2746   2552   -140   -616    371       C  
ATOM   2160  CG  LEU A 267      10.413  52.873  55.035  1.00 21.93           C  
ANISOU 2160  CG  LEU A 267     2716   3275   2342   -622   -275   -417       C  
ATOM   2161  CD1 LEU A 267      10.125  52.797  53.541  1.00 25.70           C  
ANISOU 2161  CD1 LEU A 267     3475   3905   2384   -952   -542    -95       C  
ATOM   2162  CD2 LEU A 267      11.385  54.003  55.355  1.00 24.48           C  
ANISOU 2162  CD2 LEU A 267     2032   3603   3667   -386   -638   -714       C  
ATOM   2163  N   LEU A 268       7.689  53.870  58.929  1.00 17.19           N  
ANISOU 2163  N   LEU A 268     1845   2052   2633    470   -353    452       N  
ATOM   2164  CA  LEU A 268       6.419  54.100  59.578  1.00 17.72           C  
ANISOU 2164  CA  LEU A 268     1793   2279   2661    343   -296    658       C  
ATOM   2165  C   LEU A 268       5.835  55.476  59.311  1.00 17.62           C  
ANISOU 2165  C   LEU A 268     1676   2296   2722    429    -44    570       C  
ATOM   2166  O   LEU A 268       4.711  55.799  59.746  1.00 21.57           O  
ANISOU 2166  O   LEU A 268     1970   2635   3589    503    391    231       O  
ATOM   2167  CB  LEU A 268       6.616  53.965  61.093  1.00 20.83           C  
ANISOU 2167  CB  LEU A 268     2282   2982   2650    182   -175    937       C  
ATOM   2168  CG  LEU A 268       7.098  52.567  61.531  1.00 24.36           C  
ANISOU 2168  CG  LEU A 268     3445   2923   2889    -38   -580   1174       C  
ATOM   2169  CD1 LEU A 268       6.979  52.420  63.042  1.00 33.77           C  
ANISOU 2169  CD1 LEU A 268     5660   4345   2826  -1275  -1528   1618       C  
ATOM   2170  CD2 LEU A 268       6.321  51.521  60.751  1.00 26.71           C  
ANISOU 2170  CD2 LEU A 268     3925   3090   3132    210   -404    413       C  
ATOM   2171  N   LYS A 269       6.619  56.296  58.630  1.00 16.84           N  
ANISOU 2171  N   LYS A 269     1897   2120   2382    253   -196    393       N  
ATOM   2172  CA  LYS A 269       6.145  57.648  58.309  1.00 17.30           C  
ANISOU 2172  CA  LYS A 269     2086   2236   2251    435   -166    429       C  
ATOM   2173  C   LYS A 269       6.523  58.027  56.882  1.00 17.12           C  
ANISOU 2173  C   LYS A 269     2119   2113   2275    419    -42    334       C  
ATOM   2174  O   LYS A 269       7.271  57.283  56.226  1.00 18.09           O  
ANISOU 2174  O   LYS A 269     2421   2142   2309    548   -123    186       O  
ATOM   2175  CB  LYS A 269       6.702  58.640  59.343  1.00 19.75           C  
ANISOU 2175  CB  LYS A 269     2954   2237   2314    245    126    203       C  
ATOM   2176  CG  LYS A 269       6.154  58.416  60.746  1.00 21.90           C  
ANISOU 2176  CG  LYS A 269     3068   2890   2365    328    283    139       C  
ATOM   2177  CD  LYS A 269       6.542  59.397  61.821  1.00 25.50           C  
ANISOU 2177  CD  LYS A 269     3154   4062   2473     55    197   -316       C  
ATOM   2178  CE  LYS A 269       5.846  59.026  63.143  1.00 26.98           C  
ANISOU 2178  CE  LYS A 269     2702   4809   2739    351    635   -652       C  
ATOM   2179  NZ  LYS A 269       6.461  59.584  64.367  1.00 35.40           N  
ANISOU 2179  NZ  LYS A 269     4654   6305   2492   -437    290   -478       N  
ATOM   2180  N   ASP A 270       5.998  59.175  56.447  1.00 15.56           N  
ANISOU 2180  N   ASP A 270     1737   2029   2146    239    -20    312       N  
ATOM   2181  CA  ASP A 270       6.286  59.696  55.107  1.00 15.69           C  
ANISOU 2181  CA  ASP A 270     1666   2069   2225    156     67    335       C  
ATOM   2182  C   ASP A 270       7.670  60.330  55.056  1.00 15.78           C  
ANISOU 2182  C   ASP A 270     1677   2047   2271    152     41    151       C  
ATOM   2183  O   ASP A 270       7.844  61.494  55.414  1.00 16.56           O  
ANISOU 2183  O   ASP A 270     1804   2048   2439    105    316    107       O  
ATOM   2184  CB  ASP A 270       5.204  60.696  54.725  1.00 16.46           C  
ANISOU 2184  CB  ASP A 270     1706   2296   2251    208     35    519       C  
ATOM   2185  CG  ASP A 270       5.374  61.371  53.385  1.00 17.70           C  
ANISOU 2185  CG  ASP A 270     2161   2179   2385    224    211    587       C  
ATOM   2186  OD1 ASP A 270       6.311  61.009  52.634  1.00 19.00           O  
ANISOU 2186  OD1 ASP A 270     2475   2516   2227    121    285    227       O  
ATOM   2187  OD2 ASP A 270       4.560  62.260  53.039  1.00 20.02           O  
ANISOU 2187  OD2 ASP A 270     2242   2628   2737    290    -61    886       O  
ATOM   2188  N   VAL A 271       8.660  59.570  54.622  1.00 15.24           N  
ANISOU 2188  N   VAL A 271     1675   2074   2040     71     84     62       N  
ATOM   2189  CA  VAL A 271      10.039  60.069  54.605  1.00 14.03           C  
ANISOU 2189  CA  VAL A 271     1654   1646   2031    164    -68    279       C  
ATOM   2190  C   VAL A 271      10.246  61.170  53.581  1.00 13.69           C  
ANISOU 2190  C   VAL A 271     1785   1530   1886    312    -44    170       C  
ATOM   2191  O   VAL A 271      10.846  62.219  53.921  1.00 14.24           O  
ANISOU 2191  O   VAL A 271     1930   1621   1861    135    158    159       O  
ATOM   2192  CB  VAL A 271      11.029  58.891  54.414  1.00 13.52           C  
ANISOU 2192  CB  VAL A 271     1740   1596   1800    173     33    422       C  
ATOM   2193  CG1 VAL A 271      12.441  59.378  54.151  1.00 14.82           C  
ANISOU 2193  CG1 VAL A 271     1754   1933   1943    233    237    587       C  
ATOM   2194  CG2 VAL A 271      10.980  58.002  55.662  1.00 14.33           C  
ANISOU 2194  CG2 VAL A 271     1797   1731   1917    -53    -75    554       C  
ATOM   2195  N   PRO A 272       9.817  61.069  52.339  1.00 15.30           N  
ANISOU 2195  N   PRO A 272     2102   1973   1741     40    160    110       N  
ATOM   2196  CA  PRO A 272       9.914  62.224  51.416  1.00 14.36           C  
ANISOU 2196  CA  PRO A 272     1776   1947   1732    253    -20    120       C  
ATOM   2197  C   PRO A 272       9.251  63.462  51.992  1.00 14.13           C  
ANISOU 2197  C   PRO A 272     1735   1944   1688     37    121    -25       C  
ATOM   2198  O   PRO A 272       9.787  64.548  51.876  1.00 14.33           O  
ANISOU 2198  O   PRO A 272     1307   1878   2259    245    -74    274       O  
ATOM   2199  CB  PRO A 272       9.194  61.725  50.149  1.00 14.60           C  
ANISOU 2199  CB  PRO A 272     1933   1800   1816    221    -16    -28       C  
ATOM   2200  CG  PRO A 272       9.398  60.222  50.206  1.00 13.12           C  
ANISOU 2200  CG  PRO A 272     1586   1800   1598    152    238    271       C  
ATOM   2201  CD  PRO A 272       9.257  59.879  51.666  1.00 15.68           C  
ANISOU 2201  CD  PRO A 272     2349   2104   1506   -104    347     45       C  
ATOM   2202  N   GLY A 273       8.099  63.312  52.654  1.00 15.81           N  
ANISOU 2202  N   GLY A 273     2060   1978   1970    -23    474     21       N  
ATOM   2203  CA  GLY A 273       7.410  64.468  53.241  1.00 14.75           C  
ANISOU 2203  CA  GLY A 273     1801   2161   1641    204    110     59       C  
ATOM   2204  C   GLY A 273       8.201  65.098  54.377  1.00 14.92           C  
ANISOU 2204  C   GLY A 273     1780   1981   1908    293    -90     75       C  
ATOM   2205  O   GLY A 273       8.341  66.342  54.450  1.00 16.37           O  
ANISOU 2205  O   GLY A 273     2083   2015   2120     24   -402    359       O  
ATOM   2206  N   ILE A 274       8.732  64.241  55.262  1.00 13.33           N  
ANISOU 2206  N   ILE A 274     1459   1878   1729    189    164    105       N  
ATOM   2207  CA  ILE A 274       9.499  64.787  56.385  1.00 14.21           C  
ANISOU 2207  CA  ILE A 274     1669   2001   1730    -74     70    308       C  
ATOM   2208  C   ILE A 274      10.786  65.459  55.929  1.00 14.40           C  
ANISOU 2208  C   ILE A 274     1638   1900   1934    -19    125    273       C  
ATOM   2209  O   ILE A 274      11.171  66.543  56.385  1.00 15.37           O  
ANISOU 2209  O   ILE A 274     1772   2138   1931   -192     -4    164       O  
ATOM   2210  CB  ILE A 274       9.832  63.678  57.392  1.00 13.70           C  
ANISOU 2210  CB  ILE A 274     1356   1996   1853     84    146    322       C  
ATOM   2211  CG1 ILE A 274       8.531  63.113  57.993  1.00 16.27           C  
ANISOU 2211  CG1 ILE A 274     1616   2452   2114   -315    107    553       C  
ATOM   2212  CG2 ILE A 274      10.823  64.158  58.441  1.00 15.35           C  
ANISOU 2212  CG2 ILE A 274     1580   2049   2202    -68   -175    521       C  
ATOM   2213  CD1 ILE A 274       8.775  61.833  58.766  1.00 19.32           C  
ANISOU 2213  CD1 ILE A 274     2403   2385   2553   -329    279    688       C  
ATOM   2214  N   VAL A 275      11.497  64.802  55.004  1.00 13.91           N  
ANISOU 2214  N   VAL A 275     1635   2029   1621    137     19    442       N  
ATOM   2215  CA  VAL A 275      12.715  65.435  54.520  1.00 14.65           C  
ANISOU 2215  CA  VAL A 275     1677   1783   2108    177    212    282       C  
ATOM   2216  C   VAL A 275      12.385  66.754  53.844  1.00 14.24           C  
ANISOU 2216  C   VAL A 275     1524   1827   2061    158    207    302       C  
ATOM   2217  O   VAL A 275      13.004  67.791  54.111  1.00 15.91           O  
ANISOU 2217  O   VAL A 275     2213   1784   2047     80    -55    242       O  
ATOM   2218  CB  VAL A 275      13.448  64.516  53.514  1.00 14.75           C  
ANISOU 2218  CB  VAL A 275     2075   1618   1910     83    427    458       C  
ATOM   2219  CG1 VAL A 275      14.589  65.268  52.855  1.00 12.12           C  
ANISOU 2219  CG1 VAL A 275     1517   1835   1252   -156   -242    158       C  
ATOM   2220  CG2 VAL A 275      13.928  63.251  54.230  1.00 15.81           C  
ANISOU 2220  CG2 VAL A 275     2142   1784   2083    331    401    476       C  
ATOM   2221  N  ASER A 276      11.395  66.772  52.951  0.45 15.85           N  
ANISOU 2221  N  ASER A 276     1747   2061   2213    143     29    322       N  
ATOM   2222  N  BSER A 276      11.397  66.781  52.943  0.55 15.65           N  
ANISOU 2222  N  BSER A 276     1718   2034   2194    171     62    287       N  
ATOM   2223  CA ASER A 276      11.089  68.034  52.272  0.45 16.49           C  
ANISOU 2223  CA ASER A 276     1814   2068   2382    160   -155    347       C  
ATOM   2224  CA BSER A 276      11.179  68.065  52.255  0.55 16.44           C  
ANISOU 2224  CA BSER A 276     1828   2045   2373    181   -163    331       C  
ATOM   2225  C  ASER A 276      10.691  69.143  53.242  0.45 17.03           C  
ANISOU 2225  C  ASER A 276     1925   2065   2481    172    -93    308       C  
ATOM   2226  C  BSER A 276      10.643  69.137  53.205  0.55 17.01           C  
ANISOU 2226  C  BSER A 276     1974   1990   2500    148    -49    311       C  
ATOM   2227  O  ASER A 276      11.060  70.315  53.082  0.45 16.78           O  
ANISOU 2227  O  ASER A 276     1689   1840   2847    681     -2    590       O  
ATOM   2228  O  BSER A 276      10.902  70.339  52.992  0.55 18.53           O  
ANISOU 2228  O  BSER A 276     2371   2012   2659    108    -69    362       O  
ATOM   2229  CB ASER A 276       9.963  67.808  51.265  0.45 17.28           C  
ANISOU 2229  CB ASER A 276     1988   2196   2381    -55   -231    492       C  
ATOM   2230  CB BSER A 276      10.269  67.850  51.054  0.55 17.01           C  
ANISOU 2230  CB BSER A 276     1903   2172   2386    -35   -190    450       C  
ATOM   2231  OG ASER A 276      10.393  66.878  50.291  0.45 16.44           O  
ANISOU 2231  OG ASER A 276     1795   2344   2108    -11   -209    597       O  
ATOM   2232  OG BSER A 276       9.041  67.265  51.443  0.55 16.80           O  
ANISOU 2232  OG BSER A 276     1903   2310   2170     -4    -52    282       O  
ATOM   2233  N   LYS A 277       9.921  68.784  54.263  1.00 16.42           N  
ANISOU 2233  N   LYS A 277     1774   2128   2339    239   -222    349       N  
ATOM   2234  CA  LYS A 277       9.435  69.786  55.213  1.00 17.34           C  
ANISOU 2234  CA  LYS A 277     2004   2154   2429    348   -123    389       C  
ATOM   2235  C   LYS A 277      10.574  70.398  56.023  1.00 18.19           C  
ANISOU 2235  C   LYS A 277     2400   1942   2571    515   -486    287       C  
ATOM   2236  O   LYS A 277      10.451  71.520  56.517  1.00 20.01           O  
ANISOU 2236  O   LYS A 277     2167   2286   3150    607   -195   -174       O  
ATOM   2237  CB  LYS A 277       8.476  69.179  56.241  1.00 22.37           C  
ANISOU 2237  CB  LYS A 277     2792   3003   2703     53    440    324       C  
ATOM   2238  CG  LYS A 277       7.006  69.327  55.912  1.00 28.92           C  
ANISOU 2238  CG  LYS A 277     2492   4296   4202    411   1155    371       C  
ATOM   2239  CD  LYS A 277       6.179  69.025  57.146  1.00 33.83           C  
ANISOU 2239  CD  LYS A 277     3516   5055   4281    263   1716    -46       C  
ATOM   2240  CE  LYS A 277       6.745  69.793  58.340  1.00 42.25           C  
ANISOU 2240  CE  LYS A 277     5956   5759   4337   -493   1382   -152       C  
ATOM   2241  NZ  LYS A 277       5.698  70.224  59.325  1.00 50.51           N  
ANISOU 2241  NZ  LYS A 277     7604   6065   5524    773   1618  -1571       N  
ATOM   2242  N   ASN A 278      11.660  69.622  56.193  1.00 15.34           N  
ANISOU 2242  N   ASN A 278     1900   1758   2170    187     33    435       N  
ATOM   2243  CA  ASN A 278      12.739  70.072  57.047  1.00 14.04           C  
ANISOU 2243  CA  ASN A 278     1918   1808   1608    221    196    493       C  
ATOM   2244  C   ASN A 278      14.004  70.493  56.326  1.00 14.66           C  
ANISOU 2244  C   ASN A 278     1986   1840   1746     34    173    515       C  
ATOM   2245  O   ASN A 278      14.914  71.015  56.969  1.00 15.57           O  
ANISOU 2245  O   ASN A 278     1878   2038   1999    204    207     94       O  
ATOM   2246  CB  ASN A 278      13.071  68.901  58.006  1.00 15.53           C  
ANISOU 2246  CB  ASN A 278     2446   1822   1631    106    189    557       C  
ATOM   2247  CG  ASN A 278      11.964  68.803  59.046  1.00 13.35           C  
ANISOU 2247  CG  ASN A 278     2046   1607   1419    309    -99    492       C  
ATOM   2248  OD1 ASN A 278      12.016  69.566  60.009  1.00 19.36           O  
ANISOU 2248  OD1 ASN A 278     3113   2611   1633   -218    185    -43       O  
ATOM   2249  ND2 ASN A 278      11.009  67.910  58.859  1.00 15.48           N  
ANISOU 2249  ND2 ASN A 278     1907   1885   2091    254    -97    391       N  
ATOM   2250  N   ILE A 279      14.080  70.295  55.003  1.00 13.20           N  
ANISOU 2250  N   ILE A 279     1512   1610   1892    444    370    140       N  
ATOM   2251  CA  ILE A 279      15.303  70.636  54.285  1.00 14.10           C  
ANISOU 2251  CA  ILE A 279     1522   1658   2177    341    438      0       C  
ATOM   2252  C   ILE A 279      15.542  72.135  54.246  1.00 13.98           C  
ANISOU 2252  C   ILE A 279     1379   1673   2259    315    108    170       C  
ATOM   2253  O   ILE A 279      16.700  72.565  54.229  1.00 14.36           O  
ANISOU 2253  O   ILE A 279     1444   1948   2066    165    248     23       O  
ATOM   2254  CB  ILE A 279      15.283  70.066  52.838  1.00 13.85           C  
ANISOU 2254  CB  ILE A 279     1320   1808   2135    479    512     25       C  
ATOM   2255  CG1 ILE A 279      16.685  69.931  52.254  1.00 13.76           C  
ANISOU 2255  CG1 ILE A 279     1218   1945   2065    146    497    300       C  
ATOM   2256  CG2 ILE A 279      14.379  70.877  51.914  1.00 17.90           C  
ANISOU 2256  CG2 ILE A 279     1506   2617   2679    438   -210     26       C  
ATOM   2257  CD1 ILE A 279      17.443  68.750  52.816  1.00 19.11           C  
ANISOU 2257  CD1 ILE A 279     1441   2312   3508    729    867    569       C  
ATOM   2258  N   THR A 280      14.499  72.973  54.228  1.00 14.48           N  
ANISOU 2258  N   THR A 280     1533   1749   2222    435    137    519       N  
ATOM   2259  CA  THR A 280      14.797  74.418  54.203  1.00 16.60           C  
ANISOU 2259  CA  THR A 280     1873   1710   2725    478    159    177       C  
ATOM   2260  C   THR A 280      15.481  74.894  55.474  1.00 17.02           C  
ANISOU 2260  C   THR A 280     1893   1934   2640    421    281    103       C  
ATOM   2261  O   THR A 280      16.444  75.690  55.421  1.00 16.42           O  
ANISOU 2261  O   THR A 280     2413   1608   2216    254    158    313       O  
ATOM   2262  CB  THR A 280      13.526  75.263  53.961  1.00 19.50           C  
ANISOU 2262  CB  THR A 280     2193   1772   3444    663   -167    214       C  
ATOM   2263  OG1 THR A 280      12.836  74.795  52.804  1.00 20.38           O  
ANISOU 2263  OG1 THR A 280     1707   2750   3288    436     55    261       O  
ATOM   2264  CG2 THR A 280      13.915  76.706  53.659  1.00 26.88           C  
ANISOU 2264  CG2 THR A 280     3351   1922   4940    449  -1158    889       C  
ATOM   2265  N   LYS A 281      14.968  74.432  56.636  1.00 16.32           N  
ANISOU 2265  N   LYS A 281     1520   1988   2691    372    416    -55       N  
ATOM   2266  CA  LYS A 281      15.636  74.820  57.893  1.00 17.50           C  
ANISOU 2266  CA  LYS A 281     1819   2237   2594    391    517   -228       C  
ATOM   2267  C   LYS A 281      17.112  74.471  57.851  1.00 14.88           C  
ANISOU 2267  C   LYS A 281     1759   1804   2089    227    371    -90       C  
ATOM   2268  O   LYS A 281      17.970  75.208  58.326  1.00 14.85           O  
ANISOU 2268  O   LYS A 281     2093   1799   1749    -44    216    297       O  
ATOM   2269  CB  LYS A 281      14.930  74.119  59.053  1.00 20.68           C  
ANISOU 2269  CB  LYS A 281     2065   3154   2639    426    920   -224       C  
ATOM   2270  CG  LYS A 281      15.499  74.371  60.433  1.00 27.74           C  
ANISOU 2270  CG  LYS A 281     3606   4204   2731   -165    335    319       C  
ATOM   2271  CD  LYS A 281      14.870  73.446  61.470  1.00 30.82           C  
ANISOU 2271  CD  LYS A 281     4157   4716   2838   -100    980    318       C  
ATOM   2272  CE  LYS A 281      14.760  74.129  62.825  1.00 38.07           C  
ANISOU 2272  CE  LYS A 281     6147   5328   2990   -847   1202    -13       C  
ATOM   2273  NZ  LYS A 281      14.825  73.189  63.976  1.00 47.93           N  
ANISOU 2273  NZ  LYS A 281     8743   6588   2878  -1944   1409    584       N  
ATOM   2274  N   ALA A 282      17.419  73.303  57.272  1.00 14.42           N  
ANISOU 2274  N   ALA A 282     1879   1711   1890    279    486    112       N  
ATOM   2275  CA  ALA A 282      18.820  72.855  57.267  1.00 13.64           C  
ANISOU 2275  CA  ALA A 282     1908   1538   1736    271    364    149       C  
ATOM   2276  C   ALA A 282      19.660  73.752  56.378  1.00 12.60           C  
ANISOU 2276  C   ALA A 282     1699   1513   1575    187    175     39       C  
ATOM   2277  O   ALA A 282      20.797  74.079  56.707  1.00 14.96           O  
ANISOU 2277  O   ALA A 282     1711   1783   2190    177    -49    289       O  
ATOM   2278  CB  ALA A 282      18.849  71.413  56.807  1.00 12.96           C  
ANISOU 2278  CB  ALA A 282     1582   1541   1800    154     -7    100       C  
ATOM   2279  N   LEU A 283      19.066  74.108  55.236  1.00 13.53           N  
ANISOU 2279  N   LEU A 283     1764   1679   1695    219    131    198       N  
ATOM   2280  CA  LEU A 283      19.769  74.991  54.316  1.00 14.50           C  
ANISOU 2280  CA  LEU A 283     2057   1757   1695      8     37    226       C  
ATOM   2281  C   LEU A 283      19.944  76.369  54.926  1.00 14.79           C  
ANISOU 2281  C   LEU A 283     1882   1812   1925     -2    198     97       C  
ATOM   2282  O   LEU A 283      21.027  76.943  54.753  1.00 15.75           O  
ANISOU 2282  O   LEU A 283     1872   1734   2376     37    207    171       O  
ATOM   2283  CB  LEU A 283      18.982  75.117  53.013  1.00 13.74           C  
ANISOU 2283  CB  LEU A 283     1836   1645   1740    265    100    242       C  
ATOM   2284  CG  LEU A 283      19.034  73.867  52.132  1.00 12.65           C  
ANISOU 2284  CG  LEU A 283     1277   1656   1874    149    -27    157       C  
ATOM   2285  CD1 LEU A 283      17.965  73.934  51.073  1.00 12.93           C  
ANISOU 2285  CD1 LEU A 283     1464   1812   1636    113     19    505       C  
ATOM   2286  CD2 LEU A 283      20.390  73.706  51.447  1.00 13.11           C  
ANISOU 2286  CD2 LEU A 283     1432   1441   2107    290    180    431       C  
ATOM   2287  N   VAL A 284      18.929  76.901  55.630  1.00 15.74           N  
ANISOU 2287  N   VAL A 284     1986   1894   2102    213    289    249       N  
ATOM   2288  CA  VAL A 284      19.164  78.270  56.124  1.00 17.82           C  
ANISOU 2288  CA  VAL A 284     2049   2037   2684    313    282   -107       C  
ATOM   2289  C   VAL A 284      20.211  78.233  57.227  1.00 17.91           C  
ANISOU 2289  C   VAL A 284     2294   2044   2468    176    286   -124       C  
ATOM   2290  O   VAL A 284      21.022  79.160  57.312  1.00 17.96           O  
ANISOU 2290  O   VAL A 284     2114   2138   2571    175    195    219       O  
ATOM   2291  CB  VAL A 284      17.985  79.138  56.611  1.00 19.44           C  
ANISOU 2291  CB  VAL A 284     2102   2578   2708    288    449   -526       C  
ATOM   2292  CG1 VAL A 284      16.710  78.852  55.851  1.00 16.67           C  
ANISOU 2292  CG1 VAL A 284     1836   1874   2625    152    807   -726       C  
ATOM   2293  CG2 VAL A 284      17.769  79.055  58.093  1.00 21.89           C  
ANISOU 2293  CG2 VAL A 284     1535   3984   2798    263    513     65       C  
ATOM   2294  N   GLU A 285      20.215  77.196  58.062  1.00 17.22           N  
ANISOU 2294  N   GLU A 285     1902   2078   2564     91    333    -59       N  
ATOM   2295  CA  GLU A 285      21.287  77.145  59.064  1.00 18.02           C  
ANISOU 2295  CA  GLU A 285     2143   2265   2437    194    269   -165       C  
ATOM   2296  C   GLU A 285      22.663  77.116  58.410  1.00 17.91           C  
ANISOU 2296  C   GLU A 285     1955   2096   2754    372    119   -266       C  
ATOM   2297  O   GLU A 285      23.555  77.784  58.940  1.00 19.36           O  
ANISOU 2297  O   GLU A 285     2250   2563   2542    -59     80    -49       O  
ATOM   2298  CB  GLU A 285      21.108  75.938  60.003  1.00 21.98           C  
ANISOU 2298  CB  GLU A 285     2805   2738   2810    172    140    307       C  
ATOM   2299  CG  GLU A 285      22.256  75.845  61.001  1.00 26.29           C  
ANISOU 2299  CG  GLU A 285     3156   3473   3360    309   -255    652       C  
ATOM   2300  CD  GLU A 285      22.012  74.785  62.053  1.00 31.51           C  
ANISOU 2300  CD  GLU A 285     3842   4412   3720   -396   -770   1283       C  
ATOM   2301  OE1 GLU A 285      20.866  74.259  62.023  1.00 40.17           O  
ANISOU 2301  OE1 GLU A 285     4747   5984   4531  -1748  -1154   1890       O  
ATOM   2302  OE2 GLU A 285      22.932  74.500  62.856  1.00 37.23           O  
ANISOU 2302  OE2 GLU A 285     4805   5665   3677   -638  -1360   1600       O  
ATOM   2303  N   ALA A 286      22.783  76.373  57.314  1.00 16.99           N  
ANISOU 2303  N   ALA A 286     2000   1997   2458    266    254     13       N  
ATOM   2304  CA  ALA A 286      24.071  76.177  56.657  1.00 16.12           C  
ANISOU 2304  CA  ALA A 286     1883   1756   2488    330    115     61       C  
ATOM   2305  C   ALA A 286      24.475  77.411  55.845  1.00 16.81           C  
ANISOU 2305  C   ALA A 286     1897   1865   2624    234    148    131       C  
ATOM   2306  O   ALA A 286      25.651  77.759  55.838  1.00 19.62           O  
ANISOU 2306  O   ALA A 286     1951   2275   3229     81     74    367       O  
ATOM   2307  CB  ALA A 286      24.093  74.956  55.740  1.00 15.00           C  
ANISOU 2307  CB  ALA A 286     1863   1814   2024    378    -79    185       C  
ATOM   2308  N   PHE A 287      23.511  78.039  55.175  1.00 16.54           N  
ANISOU 2308  N   PHE A 287     2016   1962   2307    108     93    204       N  
ATOM   2309  CA  PHE A 287      23.924  79.046  54.221  1.00 15.36           C  
ANISOU 2309  CA  PHE A 287     1822   1920   2093    178    356    -13       C  
ATOM   2310  C   PHE A 287      23.574  80.482  54.556  1.00 16.51           C  
ANISOU 2310  C   PHE A 287     2226   1897   2150    250    328     50       C  
ATOM   2311  O   PHE A 287      24.193  81.404  53.983  1.00 20.75           O  
ANISOU 2311  O   PHE A 287     3462   1978   2445     -7    652    172       O  
ATOM   2312  CB  PHE A 287      23.307  78.654  52.866  1.00 15.83           C  
ANISOU 2312  CB  PHE A 287     1925   1832   2257    274     76     59       C  
ATOM   2313  CG  PHE A 287      23.993  77.428  52.268  1.00 15.00           C  
ANISOU 2313  CG  PHE A 287     2099   1727   1874    221    239    201       C  
ATOM   2314  CD1 PHE A 287      25.228  77.544  51.667  1.00 16.96           C  
ANISOU 2314  CD1 PHE A 287     2416   1671   2358    126    649    152       C  
ATOM   2315  CD2 PHE A 287      23.404  76.171  52.291  1.00 14.77           C  
ANISOU 2315  CD2 PHE A 287     2089   1783   1742    168    213    203       C  
ATOM   2316  CE1 PHE A 287      25.921  76.496  51.077  1.00 15.87           C  
ANISOU 2316  CE1 PHE A 287     2365   1718   1946    161    507    180       C  
ATOM   2317  CE2 PHE A 287      24.077  75.096  51.727  1.00 16.22           C  
ANISOU 2317  CE2 PHE A 287     2379   1763   2020     78    461     94       C  
ATOM   2318  CZ  PHE A 287      25.311  75.240  51.123  1.00 14.58           C  
ANISOU 2318  CZ  PHE A 287     1990   1697   1852    260     51    160       C  
ATOM   2319  N   GLU A 288      22.612  80.734  55.431  1.00 17.03           N  
ANISOU 2319  N   GLU A 288     2507   2111   1854    694    238    108       N  
ATOM   2320  CA  GLU A 288      22.388  82.151  55.734  1.00 21.91           C  
ANISOU 2320  CA  GLU A 288     3018   2190   3115    365    752   -372       C  
ATOM   2321  C   GLU A 288      23.638  82.806  56.311  1.00 23.43           C  
ANISOU 2321  C   GLU A 288     3307   2291   3303    227    437   -187       C  
ATOM   2322  O   GLU A 288      23.859  83.985  55.936  1.00 24.48           O  
ANISOU 2322  O   GLU A 288     3051   2292   3957    272    488    -68       O  
ATOM   2323  CB  GLU A 288      21.173  82.319  56.654  1.00 26.09           C  
ANISOU 2323  CB  GLU A 288     3449   2345   4120    436   1369   -671       C  
ATOM   2324  CG  GLU A 288      20.485  83.681  56.513  1.00 28.69           C  
ANISOU 2324  CG  GLU A 288     3158   2796   4947    685   1299   -123       C  
ATOM   2325  CD  GLU A 288      19.985  83.907  55.102  1.00 36.21           C  
ANISOU 2325  CD  GLU A 288     4799   3336   5624   -261    168    572       C  
ATOM   2326  OE1 GLU A 288      19.489  82.959  54.448  1.00 35.00           O  
ANISOU 2326  OE1 GLU A 288     5181   3087   5032    546    609     33       O  
ATOM   2327  OE2 GLU A 288      20.074  85.040  54.567  1.00 50.42           O  
ANISOU 2327  OE2 GLU A 288     7918   3977   7264  -1602  -1924   1601       O  
ATOM   2328  N   PRO A 289      24.474  82.186  57.129  1.00 24.29           N  
ANISOU 2328  N   PRO A 289     3483   2549   3196    180    371    -83       N  
ATOM   2329  CA  PRO A 289      25.756  82.822  57.490  1.00 23.93           C  
ANISOU 2329  CA  PRO A 289     3479   2406   3206    277    300   -159       C  
ATOM   2330  C   PRO A 289      26.727  83.052  56.344  1.00 22.13           C  
ANISOU 2330  C   PRO A 289     3116   2423   2869    330    -68    -98       C  
ATOM   2331  O   PRO A 289      27.660  83.875  56.491  1.00 26.81           O  
ANISOU 2331  O   PRO A 289     4108   3256   2824   -599    337   -548       O  
ATOM   2332  CB  PRO A 289      26.361  81.827  58.500  1.00 25.74           C  
ANISOU 2332  CB  PRO A 289     3707   2780   3292   -113    157    252       C  
ATOM   2333  CG  PRO A 289      25.152  81.154  59.094  1.00 25.75           C  
ANISOU 2333  CG  PRO A 289     3525   2922   3336    -80    146     93       C  
ATOM   2334  CD  PRO A 289      24.304  80.923  57.869  1.00 26.48           C  
ANISOU 2334  CD  PRO A 289     3770   2959   3331   -145     28    277       C  
ATOM   2335  N   LEU A 290      26.548  82.365  55.220  1.00 19.98           N  
ANISOU 2335  N   LEU A 290     2268   2367   2956    709   -333   -132       N  
ATOM   2336  CA  LEU A 290      27.425  82.606  54.069  1.00 22.70           C  
ANISOU 2336  CA  LEU A 290     2955   2594   3077     98      4   -562       C  
ATOM   2337  C   LEU A 290      26.829  83.603  53.088  1.00 22.06           C  
ANISOU 2337  C   LEU A 290     2985   2635   2762    -64    270   -442       C  
ATOM   2338  O   LEU A 290      27.434  83.892  52.054  1.00 25.10           O  
ANISOU 2338  O   LEU A 290     3782   2387   3367   -335    914   -413       O  
ATOM   2339  CB  LEU A 290      27.732  81.313  53.321  1.00 24.68           C  
ANISOU 2339  CB  LEU A 290     3317   2621   3439     42    343   -654       C  
ATOM   2340  CG  LEU A 290      28.434  80.231  54.140  1.00 25.60           C  
ANISOU 2340  CG  LEU A 290     2686   2838   4201    355    184   -754       C  
ATOM   2341  CD1 LEU A 290      28.658  79.000  53.265  1.00 28.85           C  
ANISOU 2341  CD1 LEU A 290     3316   3046   4599    567    177  -1007       C  
ATOM   2342  CD2 LEU A 290      29.742  80.728  54.733  1.00 33.58           C  
ANISOU 2342  CD2 LEU A 290     3618   3349   5792   -312   -820   -446       C  
ATOM   2343  N   GLY A 291      25.651  84.083  53.446  1.00 21.50           N  
ANISOU 2343  N   GLY A 291     2925   2386   2858    -45    143   -321       N  
ATOM   2344  CA  GLY A 291      24.944  85.076  52.684  1.00 22.57           C  
ANISOU 2344  CA  GLY A 291     3145   2348   3083   -144    306     29       C  
ATOM   2345  C   GLY A 291      24.339  84.463  51.455  1.00 22.83           C  
ANISOU 2345  C   GLY A 291     3369   2216   3087    -59      0    268       C  
ATOM   2346  O   GLY A 291      24.072  85.124  50.451  1.00 24.44           O  
ANISOU 2346  O   GLY A 291     3624   2136   3525    201   -315    400       O  
ATOM   2347  N   ILE A 292      24.092  83.138  51.470  1.00 22.31           N  
ANISOU 2347  N   ILE A 292     3160   2238   3080    -91   -407    397       N  
ATOM   2348  CA  ILE A 292      23.469  82.681  50.220  1.00 23.13           C  
ANISOU 2348  CA  ILE A 292     3325   2519   2944     43   -220    141       C  
ATOM   2349  C   ILE A 292      22.096  82.078  50.510  1.00 22.79           C  
ANISOU 2349  C   ILE A 292     3522   2380   2758   -227   -376    -20       C  
ATOM   2350  O   ILE A 292      21.894  81.327  51.477  1.00 21.96           O  
ANISOU 2350  O   ILE A 292     2899   2384   3063    435   -124    226       O  
ATOM   2351  CB  ILE A 292      24.343  81.706  49.408  1.00 26.28           C  
ANISOU 2351  CB  ILE A 292     3718   2761   3506    412   -183     11       C  
ATOM   2352  CG1 ILE A 292      23.655  80.340  49.306  1.00 23.95           C  
ANISOU 2352  CG1 ILE A 292     3238   2253   3610    941     43    579       C  
ATOM   2353  CG2 ILE A 292      25.805  81.585  49.809  1.00 25.19           C  
ANISOU 2353  CG2 ILE A 292     3677   2791   3104    460    -17    560       C  
ATOM   2354  CD1 ILE A 292      22.983  80.190  47.955  1.00 34.44           C  
ANISOU 2354  CD1 ILE A 292     5990   3224   3874  -1426   -714    868       C  
ATOM   2355  N   SER A 293      21.148  82.446  49.636  1.00 20.96           N  
ANISOU 2355  N   SER A 293     3326   2189   2451   -102    -83    -41       N  
ATOM   2356  CA  SER A 293      19.779  81.979  49.801  1.00 21.06           C  
ANISOU 2356  CA  SER A 293     3227   2331   2444     86    111    121       C  
ATOM   2357  C   SER A 293      19.175  81.478  48.502  1.00 18.53           C  
ANISOU 2357  C   SER A 293     2499   2120   2422    317    130    294       C  
ATOM   2358  O   SER A 293      18.028  81.022  48.525  1.00 21.75           O  
ANISOU 2358  O   SER A 293     2610   2675   2981     59    407   -127       O  
ATOM   2359  CB  SER A 293      18.861  83.070  50.379  1.00 24.58           C  
ANISOU 2359  CB  SER A 293     3734   2635   2971    185    383   -238       C  
ATOM   2360  OG  SER A 293      18.990  84.247  49.596  1.00 27.23           O  
ANISOU 2360  OG  SER A 293     4224   2712   3410    752   -478    141       O  
ATOM   2361  N   ASP A 294      19.904  81.552  47.400  1.00 17.37           N  
ANISOU 2361  N   ASP A 294     2412   1831   2356    496     61    385       N  
ATOM   2362  CA  ASP A 294      19.486  80.962  46.134  1.00 17.83           C  
ANISOU 2362  CA  ASP A 294     2676   1807   2291    158     20    556       C  
ATOM   2363  C   ASP A 294      19.987  79.529  46.041  1.00 16.80           C  
ANISOU 2363  C   ASP A 294     2168   1889   2325    139    -66    324       C  
ATOM   2364  O   ASP A 294      21.191  79.311  45.827  1.00 18.12           O  
ANISOU 2364  O   ASP A 294     2048   2265   2571    131   -267    603       O  
ATOM   2365  CB  ASP A 294      20.064  81.753  44.957  1.00 17.20           C  
ANISOU 2365  CB  ASP A 294     2325   1798   2410    477    707    241       C  
ATOM   2366  CG  ASP A 294      19.698  81.206  43.593  1.00 18.91           C  
ANISOU 2366  CG  ASP A 294     2610   2229   2346    215    457    442       C  
ATOM   2367  OD1 ASP A 294      18.989  80.177  43.512  1.00 19.11           O  
ANISOU 2367  OD1 ASP A 294     2284   2384   2594    241    -59    538       O  
ATOM   2368  OD2 ASP A 294      20.125  81.831  42.572  1.00 24.30           O  
ANISOU 2368  OD2 ASP A 294     3973   2847   2414   -173    100    979       O  
ATOM   2369  N   TYR A 295      19.113  78.547  46.212  1.00 16.02           N  
ANISOU 2369  N   TYR A 295     2050   1786   2249    223   -155    286       N  
ATOM   2370  CA  TYR A 295      19.621  77.182  46.343  1.00 15.87           C  
ANISOU 2370  CA  TYR A 295     1962   1876   2191    324    202    441       C  
ATOM   2371  C   TYR A 295      19.837  76.536  44.983  1.00 15.15           C  
ANISOU 2371  C   TYR A 295     1745   1875   2137    421    124    500       C  
ATOM   2372  O   TYR A 295      20.296  75.385  44.870  1.00 15.48           O  
ANISOU 2372  O   TYR A 295     1874   1730   2277    276   -203    325       O  
ATOM   2373  CB  TYR A 295      18.691  76.370  47.271  1.00 16.25           C  
ANISOU 2373  CB  TYR A 295     2043   2039   2093    180    144    438       C  
ATOM   2374  CG  TYR A 295      18.516  77.031  48.630  1.00 15.52           C  
ANISOU 2374  CG  TYR A 295     2061   1809   2026    364     32    556       C  
ATOM   2375  CD1 TYR A 295      19.611  77.471  49.356  1.00 17.36           C  
ANISOU 2375  CD1 TYR A 295     2285   2192   2118    188    -83    510       C  
ATOM   2376  CD2 TYR A 295      17.250  77.231  49.196  1.00 17.02           C  
ANISOU 2376  CD2 TYR A 295     2258   2018   2191     17    378    467       C  
ATOM   2377  CE1 TYR A 295      19.465  78.083  50.602  1.00 18.38           C  
ANISOU 2377  CE1 TYR A 295     2490   2150   2343    416   -236    288       C  
ATOM   2378  CE2 TYR A 295      17.086  77.837  50.427  1.00 18.44           C  
ANISOU 2378  CE2 TYR A 295     2463   2028   2516     68    434    161       C  
ATOM   2379  CZ  TYR A 295      18.190  78.263  51.135  1.00 20.01           C  
ANISOU 2379  CZ  TYR A 295     2746   2397   2459    138    160    144       C  
ATOM   2380  OH  TYR A 295      18.036  78.877  52.367  1.00 21.40           O  
ANISOU 2380  OH  TYR A 295     3133   2565   2433    537     -8    129       O  
ATOM   2381  N   ASN A 296      19.570  77.277  43.894  1.00 15.26           N  
ANISOU 2381  N   ASN A 296     1679   1918   2200    280     40    566       N  
ATOM   2382  CA  ASN A 296      20.025  76.833  42.575  1.00 15.39           C  
ANISOU 2382  CA  ASN A 296     1690   1978   2179    284    126    652       C  
ATOM   2383  C   ASN A 296      21.433  77.306  42.255  1.00 15.59           C  
ANISOU 2383  C   ASN A 296     1584   1960   2379    343     74    344       C  
ATOM   2384  O   ASN A 296      22.043  76.940  41.235  1.00 16.84           O  
ANISOU 2384  O   ASN A 296     1567   1952   2880    372    313     96       O  
ATOM   2385  CB  ASN A 296      19.090  77.365  41.484  1.00 15.87           C  
ANISOU 2385  CB  ASN A 296     1600   2258   2174    268    106    612       C  
ATOM   2386  CG  ASN A 296      17.810  76.549  41.404  1.00 16.92           C  
ANISOU 2386  CG  ASN A 296     1786   2229   2413    154     68    225       C  
ATOM   2387  OD1 ASN A 296      17.906  75.330  41.188  1.00 19.51           O  
ANISOU 2387  OD1 ASN A 296     2043   2148   3223    261    142    437       O  
ATOM   2388  ND2 ASN A 296      16.646  77.171  41.556  1.00 16.12           N  
ANISOU 2388  ND2 ASN A 296     1669   2172   2282    -53    311    -30       N  
ATOM   2389  N  ASER A 297      21.975  78.155  43.119  0.71 15.82           N  
ANISOU 2389  N  ASER A 297     1974   1809   2228    258   -166    621       N  
ATOM   2390  N  BSER A 297      22.016  78.154  43.100  0.29 15.95           N  
ANISOU 2390  N  BSER A 297     1930   1843   2289    265   -143    569       N  
ATOM   2391  CA ASER A 297      23.276  78.760  42.943  0.71 16.53           C  
ANISOU 2391  CA ASER A 297     2022   1881   2376    158   -213    537       C  
ATOM   2392  CA BSER A 297      23.344  78.661  42.772  0.29 16.28           C  
ANISOU 2392  CA BSER A 297     1950   1893   2343    175   -192    485       C  
ATOM   2393  C  ASER A 297      24.400  78.000  43.627  0.71 16.57           C  
ANISOU 2393  C  ASER A 297     1961   1950   2386    181   -190    505       C  
ATOM   2394  C  BSER A 297      24.456  77.825  43.382  0.29 16.15           C  
ANISOU 2394  C  BSER A 297     1901   1882   2355    205   -126    435       C  
ATOM   2395  O  ASER A 297      25.539  78.480  43.589  0.71 16.01           O  
ANISOU 2395  O  ASER A 297     2071   1720   2294    103   -307    496       O  
ATOM   2396  O  BSER A 297      25.625  78.082  43.084  0.29 15.57           O  
ANISOU 2396  O  BSER A 297     1943   1669   2303    215    -63    502       O  
ATOM   2397  CB ASER A 297      23.231  80.199  43.495  0.71 16.99           C  
ANISOU 2397  CB ASER A 297     2202   1898   2354    171   -328    509       C  
ATOM   2398  CB BSER A 297      23.468  80.114  43.251  0.29 16.68           C  
ANISOU 2398  CB BSER A 297     2034   1876   2429    217   -249    489       C  
ATOM   2399  OG ASER A 297      23.461  80.225  44.889  0.71 17.13           O  
ANISOU 2399  OG ASER A 297     2357   1815   2338    144   -306    605       O  
ATOM   2400  OG BSER A 297      22.392  80.864  42.714  0.29 18.15           O  
ANISOU 2400  OG BSER A 297     2733   1738   2425    110   -597   1107       O  
ATOM   2401  N   ILE A 298      24.049  76.877  44.209  1.00 14.81           N  
ANISOU 2401  N   ILE A 298     1546   1814   2267    343    -27    353       N  
ATOM   2402  CA  ILE A 298      24.964  75.926  44.851  1.00 13.37           C  
ANISOU 2402  CA  ILE A 298     1501   1694   1883    263   -123     99       C  
ATOM   2403  C   ILE A 298      24.892  74.580  44.128  1.00 13.54           C  
ANISOU 2403  C   ILE A 298     1474   1760   1909    223    -47     29       C  
ATOM   2404  O   ILE A 298      23.868  74.259  43.495  1.00 14.31           O  
ANISOU 2404  O   ILE A 298     1520   1982   1936    111    -56    -32       O  
ATOM   2405  CB  ILE A 298      24.675  75.736  46.358  1.00 14.66           C  
ANISOU 2405  CB  ILE A 298     2024   1651   1893    101    -43     41       C  
ATOM   2406  CG1 ILE A 298      23.323  75.111  46.659  1.00 16.43           C  
ANISOU 2406  CG1 ILE A 298     2329   1895   2018   -144    383   -323       C  
ATOM   2407  CG2 ILE A 298      24.820  77.068  47.092  1.00 14.12           C  
ANISOU 2407  CG2 ILE A 298     1831   1585   1948    230    -44     64       C  
ATOM   2408  CD1 ILE A 298      22.995  74.959  48.135  1.00 16.80           C  
ANISOU 2408  CD1 ILE A 298     2511   1890   1981    -96    150     76       C  
ATOM   2409  N   PHE A 299      25.975  73.784  44.243  1.00 12.64           N  
ANISOU 2409  N   PHE A 299     1497   1592   1712    180    188    305       N  
ATOM   2410  CA  PHE A 299      25.865  72.413  43.698  1.00 11.89           C  
ANISOU 2410  CA  PHE A 299     1313   1663   1541    167     24    268       C  
ATOM   2411  C   PHE A 299      25.307  71.481  44.762  1.00 12.55           C  
ANISOU 2411  C   PHE A 299     1689   1581   1498    111    -81    289       C  
ATOM   2412  O   PHE A 299      25.503  71.737  45.962  1.00 14.82           O  
ANISOU 2412  O   PHE A 299     2335   1811   1485     25   -161    320       O  
ATOM   2413  CB  PHE A 299      27.196  71.923  43.130  1.00 13.13           C  
ANISOU 2413  CB  PHE A 299     1342   1821   1825    316    -31    131       C  
ATOM   2414  CG  PHE A 299      28.379  71.910  44.080  1.00 13.04           C  
ANISOU 2414  CG  PHE A 299     1370   1741   1846    270    -53    123       C  
ATOM   2415  CD1 PHE A 299      29.176  73.044  44.239  1.00 13.25           C  
ANISOU 2415  CD1 PHE A 299     1705   1707   1624    218    -56    -75       C  
ATOM   2416  CD2 PHE A 299      28.663  70.746  44.802  1.00 13.76           C  
ANISOU 2416  CD2 PHE A 299     1872   1734   1623    223   -253     45       C  
ATOM   2417  CE1 PHE A 299      30.271  73.003  45.102  1.00 13.21           C  
ANISOU 2417  CE1 PHE A 299     1656   1687   1675    129    -45     40       C  
ATOM   2418  CE2 PHE A 299      29.770  70.722  45.649  1.00 13.26           C  
ANISOU 2418  CE2 PHE A 299     1710   1699   1629    167   -141    120       C  
ATOM   2419  CZ  PHE A 299      30.570  71.843  45.819  1.00 13.04           C  
ANISOU 2419  CZ  PHE A 299     1617   1655   1684    226     26    -13       C  
ATOM   2420  N   TRP A 300      24.632  70.428  44.326  1.00 13.03           N  
ANISOU 2420  N   TRP A 300     1844   1441   1666    150    -61    300       N  
ATOM   2421  CA  TRP A 300      23.879  69.539  45.176  1.00 12.33           C  
ANISOU 2421  CA  TRP A 300     1691   1375   1620    257   -270    472       C  
ATOM   2422  C   TRP A 300      24.299  68.075  45.140  1.00 11.48           C  
ANISOU 2422  C   TRP A 300     1744   1391   1226    297   -395    262       C  
ATOM   2423  O   TRP A 300      24.525  67.485  44.099  1.00 12.22           O  
ANISOU 2423  O   TRP A 300     1612   1694   1338    -63   -139    100       O  
ATOM   2424  CB  TRP A 300      22.404  69.544  44.731  1.00 13.39           C  
ANISOU 2424  CB  TRP A 300     1666   1579   1843    307   -257    547       C  
ATOM   2425  CG  TRP A 300      21.638  70.695  45.336  1.00 13.26           C  
ANISOU 2425  CG  TRP A 300     1611   1634   1795    234   -270    418       C  
ATOM   2426  CD1 TRP A 300      21.674  72.007  44.968  1.00 12.70           C  
ANISOU 2426  CD1 TRP A 300     1507   1600   1718    256   -314    353       C  
ATOM   2427  CD2 TRP A 300      20.721  70.570  46.424  1.00 14.62           C  
ANISOU 2427  CD2 TRP A 300     1754   1759   2041    201    -72    461       C  
ATOM   2428  NE1 TRP A 300      20.816  72.716  45.789  1.00 15.17           N  
ANISOU 2428  NE1 TRP A 300     1765   1674   2326    209    173    352       N  
ATOM   2429  CE2 TRP A 300      20.220  71.864  46.686  1.00 15.13           C  
ANISOU 2429  CE2 TRP A 300     1856   1817   2076    280     46    466       C  
ATOM   2430  CE3 TRP A 300      20.290  69.467  47.192  1.00 16.00           C  
ANISOU 2430  CE3 TRP A 300     2280   1765   2034    -35     48    359       C  
ATOM   2431  CZ2 TRP A 300      19.291  72.115  47.698  1.00 17.46           C  
ANISOU 2431  CZ2 TRP A 300     2411   1959   2264    170    401    313       C  
ATOM   2432  CZ3 TRP A 300      19.363  69.728  48.199  1.00 17.45           C  
ANISOU 2432  CZ3 TRP A 300     2694   1886   2052   -307    262    170       C  
ATOM   2433  CH2 TRP A 300      18.876  71.020  48.444  1.00 17.60           C  
ANISOU 2433  CH2 TRP A 300     2507   2079   2100    -46    336    260       C  
ATOM   2434  N   ILE A 301      24.353  67.511  46.357  1.00 11.09           N  
ANISOU 2434  N   ILE A 301     1524   1374   1314    323   -260    353       N  
ATOM   2435  CA  ILE A 301      24.462  66.056  46.512  1.00 11.39           C  
ANISOU 2435  CA  ILE A 301     1259   1392   1678    166     -5    485       C  
ATOM   2436  C   ILE A 301      23.436  65.659  47.565  1.00 11.81           C  
ANISOU 2436  C   ILE A 301     1265   1597   1626     30     70    168       C  
ATOM   2437  O   ILE A 301      23.540  66.162  48.701  1.00 13.23           O  
ANISOU 2437  O   ILE A 301     1569   1835   1624   -103    -28    128       O  
ATOM   2438  CB  ILE A 301      25.881  65.630  46.923  1.00 11.62           C  
ANISOU 2438  CB  ILE A 301     1248   1288   1878    256     80    449       C  
ATOM   2439  CG1 ILE A 301      26.954  66.003  45.896  1.00 11.33           C  
ANISOU 2439  CG1 ILE A 301     1251   1270   1784    -27    -28    392       C  
ATOM   2440  CG2 ILE A 301      25.923  64.132  47.249  1.00 13.32           C  
ANISOU 2440  CG2 ILE A 301     1595   1396   2070    436    550    684       C  
ATOM   2441  CD1 ILE A 301      27.606  67.339  46.215  1.00 13.43           C  
ANISOU 2441  CD1 ILE A 301     1719   1350   2033   -121    264      2       C  
ATOM   2442  N   ALA A 302      22.497  64.793  47.183  1.00 12.30           N  
ANISOU 2442  N   ALA A 302     1412   1689   1572   -106    110    162       N  
ATOM   2443  CA  ALA A 302      21.480  64.376  48.151  1.00 12.39           C  
ANISOU 2443  CA  ALA A 302     1240   1686   1782     89    143    312       C  
ATOM   2444  C   ALA A 302      21.394  62.863  48.220  1.00 12.14           C  
ANISOU 2444  C   ALA A 302     1320   1685   1605    -11    248    170       C  
ATOM   2445  O   ALA A 302      21.350  62.210  47.190  1.00 16.38           O  
ANISOU 2445  O   ALA A 302     2570   1996   1656   -401   -195     77       O  
ATOM   2446  CB  ALA A 302      20.130  64.977  47.765  1.00 13.86           C  
ANISOU 2446  CB  ALA A 302     1374   2075   1819    297    -24    104       C  
ATOM   2447  N   HIS A 303      21.384  62.294  49.426  1.00 13.14           N  
ANISOU 2447  N   HIS A 303     1735   1625   1631   -231    295    187       N  
ATOM   2448  CA  HIS A 303      21.234  60.851  49.486  1.00 12.11           C  
ANISOU 2448  CA  HIS A 303     1486   1554   1561     23   -108     95       C  
ATOM   2449  C   HIS A 303      19.924  60.436  48.824  1.00 11.47           C  
ANISOU 2449  C   HIS A 303     1415   1523   1420    152    -85     89       C  
ATOM   2450  O   HIS A 303      18.861  60.851  49.311  1.00 12.99           O  
ANISOU 2450  O   HIS A 303     1459   1713   1765     62     56   -118       O  
ATOM   2451  CB  HIS A 303      21.241  60.385  50.956  1.00 12.04           C  
ANISOU 2451  CB  HIS A 303     1475   1476   1623    251   -261    174       C  
ATOM   2452  CG  HIS A 303      21.099  58.879  50.964  1.00 13.78           C  
ANISOU 2452  CG  HIS A 303     1901   1499   1834     42   -380    185       C  
ATOM   2453  ND1 HIS A 303      22.082  58.070  50.457  1.00 16.94           N  
ANISOU 2453  ND1 HIS A 303     2370   1837   2229   -359    -81     30       N  
ATOM   2454  CD2 HIS A 303      20.119  58.059  51.457  1.00 12.60           C  
ANISOU 2454  CD2 HIS A 303     1733   1366   1686    176  -1025    174       C  
ATOM   2455  CE1 HIS A 303      21.715  56.789  50.609  1.00 15.44           C  
ANISOU 2455  CE1 HIS A 303     2122   1734   2009   -276  -1066    459       C  
ATOM   2456  NE2 HIS A 303      20.546  56.761  51.196  1.00 16.91           N  
ANISOU 2456  NE2 HIS A 303     2762   1502   2160   -207   -546     15       N  
ATOM   2457  N   PRO A 304      19.976  59.672  47.749  1.00 12.57           N  
ANISOU 2457  N   PRO A 304     1476   1663   1636     72    -43    -97       N  
ATOM   2458  CA  PRO A 304      18.775  59.275  47.006  1.00 11.98           C  
ANISOU 2458  CA  PRO A 304     1450   1797   1306     26     71     -2       C  
ATOM   2459  C   PRO A 304      18.153  58.069  47.676  1.00 11.97           C  
ANISOU 2459  C   PRO A 304     1498   1598   1450     81     43    -62       C  
ATOM   2460  O   PRO A 304      18.175  56.951  47.164  1.00 13.43           O  
ANISOU 2460  O   PRO A 304     1709   1644   1748    214   -195   -196       O  
ATOM   2461  CB  PRO A 304      19.377  58.952  45.625  1.00 11.43           C  
ANISOU 2461  CB  PRO A 304     1125   1664   1552    255    128   -128       C  
ATOM   2462  CG  PRO A 304      20.706  58.348  45.970  1.00 12.26           C  
ANISOU 2462  CG  PRO A 304     1222   1893   1543    189   -250   -130       C  
ATOM   2463  CD  PRO A 304      21.222  59.158  47.128  1.00 12.55           C  
ANISOU 2463  CD  PRO A 304     1479   1784   1507     31    -45   -162       C  
ATOM   2464  N   GLY A 305      17.564  58.287  48.880  1.00 11.46           N  
ANISOU 2464  N   GLY A 305     1282   1634   1438    145     37    126       N  
ATOM   2465  CA  GLY A 305      16.988  57.104  49.570  1.00 10.92           C  
ANISOU 2465  CA  GLY A 305     1193   1448   1508    296    -91    150       C  
ATOM   2466  C   GLY A 305      15.927  56.411  48.728  1.00 12.43           C  
ANISOU 2466  C   GLY A 305     1436   1568   1719    134   -102    -28       C  
ATOM   2467  O   GLY A 305      15.805  55.184  48.729  1.00 14.97           O  
ANISOU 2467  O   GLY A 305     1898   1564   2225      5    105   -152       O  
ATOM   2468  N   GLY A 306      15.184  57.242  47.998  1.00 12.97           N  
ANISOU 2468  N   GLY A 306     1216   1918   1794    167   -252    -60       N  
ATOM   2469  CA  GLY A 306      14.273  56.792  46.953  1.00 14.17           C  
ANISOU 2469  CA  GLY A 306     2055   1678   1652     14   -415   -127       C  
ATOM   2470  C   GLY A 306      14.013  58.018  46.065  1.00 13.82           C  
ANISOU 2470  C   GLY A 306     1832   1699   1721    172   -371   -119       C  
ATOM   2471  O   GLY A 306      14.285  59.139  46.516  1.00 13.11           O  
ANISOU 2471  O   GLY A 306     1522   1717   1742   -103    -12    -50       O  
ATOM   2472  N   PRO A 307      13.492  57.848  44.861  1.00 14.26           N  
ANISOU 2472  N   PRO A 307     1918   1889   1610    188   -260    -93       N  
ATOM   2473  CA  PRO A 307      13.278  58.976  43.970  1.00 14.50           C  
ANISOU 2473  CA  PRO A 307     1984   1971   1554    241   -199    -82       C  
ATOM   2474  C   PRO A 307      12.295  59.984  44.539  1.00 13.83           C  
ANISOU 2474  C   PRO A 307     1785   1889   1580    153   -160     16       C  
ATOM   2475  O   PRO A 307      12.385  61.177  44.218  1.00 15.34           O  
ANISOU 2475  O   PRO A 307     2175   1841   1813     99      0    -41       O  
ATOM   2476  CB  PRO A 307      12.698  58.318  42.695  1.00 16.55           C  
ANISOU 2476  CB  PRO A 307     2755   1963   1571    117   -332    -80       C  
ATOM   2477  CG  PRO A 307      12.134  57.004  43.165  1.00 15.78           C  
ANISOU 2477  CG  PRO A 307     2058   2146   1792     75   -490     51       C  
ATOM   2478  CD  PRO A 307      13.056  56.555  44.284  1.00 14.65           C  
ANISOU 2478  CD  PRO A 307     2033   1999   1534     75   -389    -99       C  
ATOM   2479  N   ALA A 308      11.369  59.588  45.396  1.00 14.75           N  
ANISOU 2479  N   ALA A 308     1653   2074   1875      3   -163     11       N  
ATOM   2480  CA  ALA A 308      10.351  60.567  45.836  1.00 15.02           C  
ANISOU 2480  CA  ALA A 308     1520   2259   1926     59   -121    134       C  
ATOM   2481  C   ALA A 308      10.970  61.570  46.772  1.00 14.16           C  
ANISOU 2481  C   ALA A 308     1438   1866   2077    238    -91    166       C  
ATOM   2482  O   ALA A 308      10.528  62.733  46.850  1.00 15.63           O  
ANISOU 2482  O   ALA A 308     1596   1930   2412    353    330    296       O  
ATOM   2483  CB  ALA A 308       9.203  59.816  46.483  1.00 17.93           C  
ANISOU 2483  CB  ALA A 308     1941   2561   2311   -337    284   -280       C  
ATOM   2484  N   ILE A 309      12.011  61.162  47.511  1.00 13.91           N  
ANISOU 2484  N   ILE A 309     1311   1921   2053     93    -81    147       N  
ATOM   2485  CA  ILE A 309      12.728  62.156  48.313  1.00 13.84           C  
ANISOU 2485  CA  ILE A 309     1723   1833   1703     97    -69    216       C  
ATOM   2486  C   ILE A 309      13.246  63.273  47.412  1.00 13.80           C  
ANISOU 2486  C   ILE A 309     1870   1582   1790    218    115     88       C  
ATOM   2487  O   ILE A 309      13.090  64.473  47.645  1.00 15.51           O  
ANISOU 2487  O   ILE A 309     2066   1617   2212    442      1     71       O  
ATOM   2488  CB  ILE A 309      13.906  61.538  49.068  1.00 13.97           C  
ANISOU 2488  CB  ILE A 309     1774   1641   1894     31   -261     82       C  
ATOM   2489  CG1 ILE A 309      13.463  60.484  50.088  1.00 13.24           C  
ANISOU 2489  CG1 ILE A 309     1403   1785   1843    329    -94    149       C  
ATOM   2490  CG2 ILE A 309      14.699  62.644  49.763  1.00 14.75           C  
ANISOU 2490  CG2 ILE A 309     1980   1554   2071    245   -315   -187       C  
ATOM   2491  CD1 ILE A 309      14.615  59.877  50.882  1.00 13.21           C  
ANISOU 2491  CD1 ILE A 309     1452   1787   1779    386   -188    -60       C  
ATOM   2492  N   LEU A 310      13.927  62.898  46.337  1.00 13.14           N  
ANISOU 2492  N   LEU A 310     1694   1764   1537    128   -105     59       N  
ATOM   2493  CA  LEU A 310      14.472  63.881  45.413  1.00 12.99           C  
ANISOU 2493  CA  LEU A 310     1559   1540   1836    368    136     52       C  
ATOM   2494  C   LEU A 310      13.381  64.697  44.733  1.00 13.77           C  
ANISOU 2494  C   LEU A 310     1553   1603   2077    360    142    203       C  
ATOM   2495  O   LEU A 310      13.581  65.925  44.628  1.00 16.20           O  
ANISOU 2495  O   LEU A 310     1893   1676   2587    218    -62    501       O  
ATOM   2496  CB  LEU A 310      15.340  63.209  44.328  1.00 14.64           C  
ANISOU 2496  CB  LEU A 310     1796   1851   1915    565    259     88       C  
ATOM   2497  CG  LEU A 310      16.342  62.164  44.845  1.00 13.93           C  
ANISOU 2497  CG  LEU A 310     1932   1704   1656    583    106   -194       C  
ATOM   2498  CD1 LEU A 310      17.092  61.553  43.671  1.00 14.10           C  
ANISOU 2498  CD1 LEU A 310     1733   1844   1782    389    277   -198       C  
ATOM   2499  CD2 LEU A 310      17.297  62.788  45.862  1.00 14.68           C  
ANISOU 2499  CD2 LEU A 310     2223   1688   1666    315      1    -20       C  
ATOM   2500  N   ASP A 311      12.304  64.061  44.289  1.00 13.50           N  
ANISOU 2500  N   ASP A 311     1496   1761   1872    313    203    289       N  
ATOM   2501  CA  ASP A 311      11.251  64.805  43.583  1.00 13.03           C  
ANISOU 2501  CA  ASP A 311     1771   1720   1461    335    108    191       C  
ATOM   2502  C   ASP A 311      10.628  65.855  44.502  1.00 13.82           C  
ANISOU 2502  C   ASP A 311     1568   1888   1795    382    288    111       C  
ATOM   2503  O   ASP A 311      10.413  66.999  44.126  1.00 15.89           O  
ANISOU 2503  O   ASP A 311     2024   1758   2254    315    618    113       O  
ATOM   2504  CB  ASP A 311      10.181  63.844  43.083  1.00 15.65           C  
ANISOU 2504  CB  ASP A 311     2097   2129   1721    159   -240    139       C  
ATOM   2505  CG  ASP A 311      10.663  62.909  41.979  1.00 17.29           C  
ANISOU 2505  CG  ASP A 311     2444   2055   2072     83   -248   -106       C  
ATOM   2506  OD1 ASP A 311      11.722  63.130  41.347  1.00 20.15           O  
ANISOU 2506  OD1 ASP A 311     3144   2055   2457    273    505    -17       O  
ATOM   2507  OD2 ASP A 311       9.965  61.902  41.761  1.00 22.10           O  
ANISOU 2507  OD2 ASP A 311     2873   2628   2897   -275   -708   -506       O  
ATOM   2508  N   GLN A 312      10.333  65.440  45.740  1.00 15.30           N  
ANISOU 2508  N   GLN A 312     2249   1929   1634    127    265   -116       N  
ATOM   2509  CA  GLN A 312       9.708  66.350  46.716  1.00 14.42           C  
ANISOU 2509  CA  GLN A 312     1692   1992   1794     84    258   -153       C  
ATOM   2510  C   GLN A 312      10.682  67.429  47.178  1.00 14.08           C  
ANISOU 2510  C   GLN A 312     1742   1936   1670    122    150   -104       C  
ATOM   2511  O   GLN A 312      10.246  68.581  47.383  1.00 15.86           O  
ANISOU 2511  O   GLN A 312     1962   1861   2201    143     65     -6       O  
ATOM   2512  CB  GLN A 312       9.113  65.541  47.872  1.00 14.30           C  
ANISOU 2512  CB  GLN A 312     1665   2021   1749     95    178   -124       C  
ATOM   2513  CG  GLN A 312       7.875  64.788  47.338  1.00 15.52           C  
ANISOU 2513  CG  GLN A 312     1664   2134   2098     16     39     68       C  
ATOM   2514  CD  GLN A 312       7.189  63.981  48.416  1.00 14.76           C  
ANISOU 2514  CD  GLN A 312     1406   2009   2192    267    -75    263       C  
ATOM   2515  OE1 GLN A 312       6.686  62.880  48.077  1.00 21.03           O  
ANISOU 2515  OE1 GLN A 312     2873   2689   2428   -771    179     82       O  
ATOM   2516  NE2 GLN A 312       7.179  64.507  49.630  1.00 14.74           N  
ANISOU 2516  NE2 GLN A 312     1277   2159   2164    265     79    254       N  
ATOM   2517  N   VAL A 313      11.965  67.153  47.316  1.00 13.23           N  
ANISOU 2517  N   VAL A 313     1820   1925   1283    106   -117    411       N  
ATOM   2518  CA  VAL A 313      12.882  68.257  47.618  1.00 14.37           C  
ANISOU 2518  CA  VAL A 313     1609   1798   2054    186    157    410       C  
ATOM   2519  C   VAL A 313      12.996  69.240  46.437  1.00 14.16           C  
ANISOU 2519  C   VAL A 313     1722   1633   2026    283    -91    382       C  
ATOM   2520  O   VAL A 313      13.009  70.464  46.607  1.00 15.16           O  
ANISOU 2520  O   VAL A 313     1720   1639   2400    389    490    330       O  
ATOM   2521  CB  VAL A 313      14.256  67.686  47.997  1.00 15.59           C  
ANISOU 2521  CB  VAL A 313     1814   1727   2381    112   -306    603       C  
ATOM   2522  CG1 VAL A 313      15.325  68.767  47.938  1.00 13.70           C  
ANISOU 2522  CG1 VAL A 313     1763   1484   1957    215   -361    -33       C  
ATOM   2523  CG2 VAL A 313      14.197  67.069  49.380  1.00 15.96           C  
ANISOU 2523  CG2 VAL A 313     2070   1832   2164    649    151    334       C  
ATOM   2524  N   GLU A 314      13.087  68.710  45.218  1.00 14.61           N  
ANISOU 2524  N   GLU A 314     1760   1768   2024    336     65    377       N  
ATOM   2525  CA  GLU A 314      13.130  69.568  44.027  1.00 16.08           C  
ANISOU 2525  CA  GLU A 314     1999   2081   2029    315    -78    486       C  
ATOM   2526  C   GLU A 314      11.907  70.470  44.000  1.00 16.49           C  
ANISOU 2526  C   GLU A 314     1948   2115   2202    280   -306    541       C  
ATOM   2527  O   GLU A 314      11.968  71.688  43.777  1.00 18.08           O  
ANISOU 2527  O   GLU A 314     1985   2059   2824    267   -356    452       O  
ATOM   2528  CB  GLU A 314      13.224  68.723  42.745  1.00 19.32           C  
ANISOU 2528  CB  GLU A 314     2932   2334   2076    128    357    394       C  
ATOM   2529  CG  GLU A 314      12.919  69.441  41.443  1.00 21.31           C  
ANISOU 2529  CG  GLU A 314     3060   3046   1992     47     80    406       C  
ATOM   2530  CD  GLU A 314      13.063  68.589  40.200  1.00 25.11           C  
ANISOU 2530  CD  GLU A 314     3772   3659   2110      0    367    145       C  
ATOM   2531  OE1 GLU A 314      13.862  67.616  40.255  1.00 31.70           O  
ANISOU 2531  OE1 GLU A 314     6151   2603   3289    413    988    421       O  
ATOM   2532  OE2 GLU A 314      12.403  68.891  39.175  1.00 32.96           O  
ANISOU 2532  OE2 GLU A 314     4482   5135   2906   -625  -1088   -627       O  
ATOM   2533  N   GLN A 315      10.734  69.859  44.224  1.00 16.65           N  
ANISOU 2533  N   GLN A 315     2053   2010   2263    318    307     19       N  
ATOM   2534  CA  GLN A 315       9.506  70.669  44.152  1.00 16.74           C  
ANISOU 2534  CA  GLN A 315     2005   2145   2209    322     95    -22       C  
ATOM   2535  C   GLN A 315       9.431  71.687  45.277  1.00 16.34           C  
ANISOU 2535  C   GLN A 315     2138   1863   2206    376    263    137       C  
ATOM   2536  O   GLN A 315       9.044  72.848  45.075  1.00 18.24           O  
ANISOU 2536  O   GLN A 315     1928   1836   3167    329     89    150       O  
ATOM   2537  CB  GLN A 315       8.283  69.740  44.201  1.00 20.92           C  
ANISOU 2537  CB  GLN A 315     2085   2790   3074     15     83   -423       C  
ATOM   2538  CG  GLN A 315       8.176  68.883  42.955  1.00 26.04           C  
ANISOU 2538  CG  GLN A 315     3095   3282   3516   -278   -222   -851       C  
ATOM   2539  CD  GLN A 315       7.425  67.587  43.195  1.00 32.12           C  
ANISOU 2539  CD  GLN A 315     4886   3872   3447  -1283    415  -1170       C  
ATOM   2540  OE1 GLN A 315       6.761  67.434  44.228  1.00 36.45           O  
ANISOU 2540  OE1 GLN A 315     4371   5980   3499  -1209     78     30       O  
ATOM   2541  NE2 GLN A 315       7.522  66.647  42.249  1.00 36.91           N  
ANISOU 2541  NE2 GLN A 315     6337   3381   4306   -272   -854  -1399       N  
ATOM   2542  N   LYS A 316       9.781  71.292  46.490  1.00 16.64           N  
ANISOU 2542  N   LYS A 316     2128   2126   2068    -16    356    146       N  
ATOM   2543  CA  LYS A 316       9.698  72.226  47.610  1.00 17.66           C  
ANISOU 2543  CA  LYS A 316     2402   2106   2202    -24    351     86       C  
ATOM   2544  C   LYS A 316      10.518  73.473  47.367  1.00 16.85           C  
ANISOU 2544  C   LYS A 316     2180   1977   2246    160    287    147       C  
ATOM   2545  O   LYS A 316      10.083  74.595  47.600  1.00 19.10           O  
ANISOU 2545  O   LYS A 316     2414   2021   2823    251    894    329       O  
ATOM   2546  CB  LYS A 316      10.252  71.531  48.868  1.00 19.37           C  
ANISOU 2546  CB  LYS A 316     3129   2174   2057   -170    310    136       C  
ATOM   2547  CG  LYS A 316      10.349  72.397  50.106  1.00 18.86           C  
ANISOU 2547  CG  LYS A 316     2631   2263   2271    295    205    -69       C  
ATOM   2548  CD  LYS A 316       8.990  72.568  50.765  1.00 20.91           C  
ANISOU 2548  CD  LYS A 316     2623   2525   2797    449    291    -62       C  
ATOM   2549  CE  LYS A 316       9.151  73.360  52.067  1.00 21.46           C  
ANISOU 2549  CE  LYS A 316     2696   2953   2504    687    427      3       C  
ATOM   2550  NZ  LYS A 316       7.838  73.546  52.744  1.00 25.08           N  
ANISOU 2550  NZ  LYS A 316     2915   4003   2611    553    750    286       N  
ATOM   2551  N   LEU A 317      11.748  73.244  46.927  1.00 15.30           N  
ANISOU 2551  N   LEU A 317     2043   1801   1969    198     17     93       N  
ATOM   2552  CA  LEU A 317      12.675  74.371  46.798  1.00 15.67           C  
ANISOU 2552  CA  LEU A 317     1902   1933   2117    172   -344    383       C  
ATOM   2553  C   LEU A 317      12.660  75.037  45.435  1.00 16.01           C  
ANISOU 2553  C   LEU A 317     2013   1882   2188    180   -468    459       C  
ATOM   2554  O   LEU A 317      13.360  76.042  45.290  1.00 17.76           O  
ANISOU 2554  O   LEU A 317     2738   2011   1999   -169   -367    309       O  
ATOM   2555  CB  LEU A 317      14.090  73.848  47.060  1.00 16.34           C  
ANISOU 2555  CB  LEU A 317     2020   2041   2147    297   -481    354       C  
ATOM   2556  CG  LEU A 317      14.334  73.284  48.465  1.00 16.34           C  
ANISOU 2556  CG  LEU A 317     1856   2150   2202    309   -239    519       C  
ATOM   2557  CD1 LEU A 317      15.721  72.658  48.511  1.00 21.39           C  
ANISOU 2557  CD1 LEU A 317     1912   2850   3365    476   -684    868       C  
ATOM   2558  CD2 LEU A 317      14.211  74.353  49.533  1.00 17.92           C  
ANISOU 2558  CD2 LEU A 317     2525   2217   2065   -438   -158    479       C  
ATOM   2559  N   ALA A 318      11.933  74.478  44.474  1.00 15.20           N  
ANISOU 2559  N   ALA A 318     1781   1794   2202    329   -438    428       N  
ATOM   2560  CA  ALA A 318      11.963  74.947  43.094  1.00 14.85           C  
ANISOU 2560  CA  ALA A 318     1998   1611   2034    684   -180    136       C  
ATOM   2561  C   ALA A 318      13.384  74.846  42.529  1.00 15.88           C  
ANISOU 2561  C   ALA A 318     1877   1774   2382    502   -208    263       C  
ATOM   2562  O   ALA A 318      13.882  75.753  41.856  1.00 16.29           O  
ANISOU 2562  O   ALA A 318     1888   1772   2530    219   -435    245       O  
ATOM   2563  CB  ALA A 318      11.510  76.397  42.892  1.00 14.80           C  
ANISOU 2563  CB  ALA A 318     2262   1524   1836    598   -308     87       C  
ATOM   2564  N   LEU A 319      14.017  73.708  42.809  1.00 15.68           N  
ANISOU 2564  N   LEU A 319     1559   1912   2485    483   -328    360       N  
ATOM   2565  CA  LEU A 319      15.287  73.409  42.163  1.00 14.68           C  
ANISOU 2565  CA  LEU A 319     1547   1917   2115    442   -375    534       C  
ATOM   2566  C   LEU A 319      15.068  73.216  40.659  1.00 15.76           C  
ANISOU 2566  C   LEU A 319     1847   2003   2137    310   -473    558       C  
ATOM   2567  O   LEU A 319      14.106  72.583  40.243  1.00 16.84           O  
ANISOU 2567  O   LEU A 319     2285   1880   2232     39   -160     14       O  
ATOM   2568  CB  LEU A 319      15.984  72.162  42.757  1.00 15.11           C  
ANISOU 2568  CB  LEU A 319     1484   2003   2253    478   -490    515       C  
ATOM   2569  CG  LEU A 319      16.302  72.209  44.259  1.00 14.78           C  
ANISOU 2569  CG  LEU A 319     1589   1746   2283    332   -582    523       C  
ATOM   2570  CD1 LEU A 319      16.981  70.915  44.734  1.00 15.17           C  
ANISOU 2570  CD1 LEU A 319     1858   1622   2283    216   -371    722       C  
ATOM   2571  CD2 LEU A 319      17.177  73.417  44.585  1.00 16.19           C  
ANISOU 2571  CD2 LEU A 319     2498   1625   2027    -13   -161    500       C  
ATOM   2572  N   LYS A 320      16.002  73.740  39.858  1.00 15.96           N  
ANISOU 2572  N   LYS A 320     2006   1974   2084    279   -303    360       N  
ATOM   2573  CA  LYS A 320      15.983  73.296  38.452  1.00 16.85           C  
ANISOU 2573  CA  LYS A 320     1975   2304   2123    327   -429    244       C  
ATOM   2574  C   LYS A 320      16.207  71.802  38.382  1.00 16.80           C  
ANISOU 2574  C   LYS A 320     1884   2297   2201    288   -226    133       C  
ATOM   2575  O   LYS A 320      16.954  71.215  39.177  1.00 16.36           O  
ANISOU 2575  O   LYS A 320     2025   2108   2085     96    -99    421       O  
ATOM   2576  CB  LYS A 320      17.050  74.069  37.673  1.00 16.76           C  
ANISOU 2576  CB  LYS A 320     2113   2263   1990    432   -344    317       C  
ATOM   2577  CG  LYS A 320      16.834  75.568  37.869  1.00 20.32           C  
ANISOU 2577  CG  LYS A 320     2899   2182   2638    351   -658    426       C  
ATOM   2578  CD  LYS A 320      17.844  76.396  37.096  1.00 25.74           C  
ANISOU 2578  CD  LYS A 320     4044   2631   3105   -539   -456    372       C  
ATOM   2579  CE  LYS A 320      17.739  77.836  37.625  1.00 33.34           C  
ANISOU 2579  CE  LYS A 320     5969   2704   3996   -955   -281     84       C  
ATOM   2580  NZ  LYS A 320      17.834  78.781  36.489  1.00 30.29           N  
ANISOU 2580  NZ  LYS A 320     5347   2380   3784    763  -1078   -271       N  
ATOM   2581  N   PRO A 321      15.577  71.091  37.456  1.00 18.96           N  
ANISOU 2581  N   PRO A 321     2228   2501   2477    300   -399    -62       N  
ATOM   2582  CA  PRO A 321      15.755  69.634  37.417  1.00 18.68           C  
ANISOU 2582  CA  PRO A 321     1924   2504   2669    274   -233   -196       C  
ATOM   2583  C   PRO A 321      17.210  69.193  37.283  1.00 19.49           C  
ANISOU 2583  C   PRO A 321     1922   2688   2796    300   -199    149       C  
ATOM   2584  O   PRO A 321      17.609  68.114  37.731  1.00 21.13           O  
ANISOU 2584  O   PRO A 321     2243   2309   3477    510    375    -74       O  
ATOM   2585  CB  PRO A 321      14.976  69.245  36.157  1.00 20.72           C  
ANISOU 2585  CB  PRO A 321     2213   2657   3002    316   -545   -324       C  
ATOM   2586  CG  PRO A 321      13.938  70.317  36.046  1.00 21.30           C  
ANISOU 2586  CG  PRO A 321     2476   2594   3023    370   -727   -254       C  
ATOM   2587  CD  PRO A 321      14.634  71.586  36.449  1.00 20.48           C  
ANISOU 2587  CD  PRO A 321     2484   2636   2662    358   -709   -249       C  
ATOM   2588  N   GLU A 322      18.024  70.061  36.687  1.00 18.98           N  
ANISOU 2588  N   GLU A 322     1995   2718   2499    269   -164     43       N  
ATOM   2589  CA  GLU A 322      19.435  69.685  36.508  1.00 19.15           C  
ANISOU 2589  CA  GLU A 322     1985   2864   2428    319   -173    228       C  
ATOM   2590  C   GLU A 322      20.199  69.631  37.823  1.00 17.66           C  
ANISOU 2590  C   GLU A 322     2122   2149   2438    352   -215    149       C  
ATOM   2591  O   GLU A 322      21.277  68.997  37.864  1.00 16.96           O  
ANISOU 2591  O   GLU A 322     2111   1993   2340    288   -184    220       O  
ATOM   2592  CB  GLU A 322      20.139  70.656  35.545  1.00 22.83           C  
ANISOU 2592  CB  GLU A 322     2681   3730   2263    268    392    339       C  
ATOM   2593  CG  GLU A 322      19.645  70.511  34.124  1.00 25.08           C  
ANISOU 2593  CG  GLU A 322     3146   4135   2247    612    389     71       C  
ATOM   2594  CD  GLU A 322      18.353  71.265  33.842  1.00 27.51           C  
ANISOU 2594  CD  GLU A 322     3369   4476   2606    733   -116      9       C  
ATOM   2595  OE1 GLU A 322      17.878  71.992  34.733  1.00 29.23           O  
ANISOU 2595  OE1 GLU A 322     3984   4383   2739   1571   -235    213       O  
ATOM   2596  OE2 GLU A 322      17.823  71.100  32.700  1.00 30.84           O  
ANISOU 2596  OE2 GLU A 322     4112   4697   2910    466   -585     27       O  
ATOM   2597  N   LYS A 323      19.701  70.277  38.875  1.00 17.00           N  
ANISOU 2597  N   LYS A 323     2034   1952   2472    172   -100    181       N  
ATOM   2598  CA  LYS A 323      20.476  70.252  40.110  1.00 15.07           C  
ANISOU 2598  CA  LYS A 323     1592   1698   2437    103     59    144       C  
ATOM   2599  C   LYS A 323      20.725  68.826  40.604  1.00 15.84           C  
ANISOU 2599  C   LYS A 323     2124   1598   2296    212    -53    -50       C  
ATOM   2600  O   LYS A 323      21.811  68.531  41.117  1.00 16.19           O  
ANISOU 2600  O   LYS A 323     2110   1560   2483    288     -8      2       O  
ATOM   2601  CB  LYS A 323      19.779  71.038  41.228  1.00 15.13           C  
ANISOU 2601  CB  LYS A 323     1639   1593   2517    246     -5    148       C  
ATOM   2602  CG  LYS A 323      19.550  72.511  40.865  1.00 14.16           C  
ANISOU 2602  CG  LYS A 323     1631   1652   2098    127     37    294       C  
ATOM   2603  CD  LYS A 323      20.772  73.202  40.279  1.00 13.06           C  
ANISOU 2603  CD  LYS A 323     1666   1979   1317     62     15    137       C  
ATOM   2604  CE  LYS A 323      21.843  73.408  41.332  1.00 14.69           C  
ANISOU 2604  CE  LYS A 323     1880   2184   1518   -150   -182    267       C  
ATOM   2605  NZ  LYS A 323      23.008  74.236  40.884  1.00 16.22           N  
ANISOU 2605  NZ  LYS A 323     1872   2132   2160   -179   -172    297       N  
ATOM   2606  N   MET A 324      19.741  67.961  40.450  1.00 16.41           N  
ANISOU 2606  N   MET A 324     2323   1711   2201     15   -167    314       N  
ATOM   2607  CA  MET A 324      19.835  66.591  40.929  1.00 14.96           C  
ANISOU 2607  CA  MET A 324     1888   1792   2006    153   -162    354       C  
ATOM   2608  C   MET A 324      20.434  65.646  39.896  1.00 14.83           C  
ANISOU 2608  C   MET A 324     1487   1946   2201    312   -136    349       C  
ATOM   2609  O   MET A 324      20.353  64.422  40.098  1.00 14.85           O  
ANISOU 2609  O   MET A 324     2019   1919   1705    150   -411    188       O  
ATOM   2610  CB  MET A 324      18.424  66.117  41.323  1.00 16.74           C  
ANISOU 2610  CB  MET A 324     2224   1906   2232    -21    416    -12       C  
ATOM   2611  CG  MET A 324      17.920  66.781  42.603  1.00 17.28           C  
ANISOU 2611  CG  MET A 324     2318   2071   2179    393     76   -121       C  
ATOM   2612  SD  MET A 324      18.757  66.218  44.122  1.00 20.23           S  
ANISOU 2612  SD  MET A 324     2799   2552   2335    132    -97    271       S  
ATOM   2613  CE  MET A 324      17.862  67.207  45.321  1.00 23.63           C  
ANISOU 2613  CE  MET A 324     3519   3380   2079   -356    630    110       C  
ATOM   2614  N   ASN A 325      21.003  66.163  38.797  1.00 15.56           N  
ANISOU 2614  N   ASN A 325     1854   1969   2091    364   -128    349       N  
ATOM   2615  CA  ASN A 325      21.490  65.240  37.751  1.00 15.65           C  
ANISOU 2615  CA  ASN A 325     1999   1915   2031    337   -188    344       C  
ATOM   2616  C   ASN A 325      22.475  64.189  38.279  1.00 14.49           C  
ANISOU 2616  C   ASN A 325     1908   1750   1848    198   -288    154       C  
ATOM   2617  O   ASN A 325      22.332  62.966  38.058  1.00 14.26           O  
ANISOU 2617  O   ASN A 325     2065   1711   1640     40   -307    347       O  
ATOM   2618  CB  ASN A 325      22.178  66.002  36.613  1.00 17.09           C  
ANISOU 2618  CB  ASN A 325     2361   2041   2091    432      0    423       C  
ATOM   2619  CG  ASN A 325      21.282  66.525  35.523  1.00 20.89           C  
ANISOU 2619  CG  ASN A 325     3038   2490   2407    245   -384    819       C  
ATOM   2620  OD1 ASN A 325      20.059  66.249  35.484  1.00 22.74           O  
ANISOU 2620  OD1 ASN A 325     3048   2803   2789    255   -852    532       O  
ATOM   2621  ND2 ASN A 325      21.877  67.293  34.592  1.00 24.82           N  
ANISOU 2621  ND2 ASN A 325     4338   2535   2558     14   -233    987       N  
ATOM   2622  N   ALA A 326      23.523  64.613  38.979  1.00 13.40           N  
ANISOU 2622  N   ALA A 326     1606   1808   1678    107     55    114       N  
ATOM   2623  CA  ALA A 326      24.551  63.657  39.432  1.00 13.38           C  
ANISOU 2623  CA  ALA A 326     1710   1863   1509     63    -37    286       C  
ATOM   2624  C   ALA A 326      23.964  62.633  40.402  1.00 13.89           C  
ANISOU 2624  C   ALA A 326     2032   1738   1506    -55    161     89       C  
ATOM   2625  O   ALA A 326      24.245  61.422  40.337  1.00 13.29           O  
ANISOU 2625  O   ALA A 326     2006   1794   1251     68    108    113       O  
ATOM   2626  CB  ALA A 326      25.689  64.424  40.073  1.00 15.26           C  
ANISOU 2626  CB  ALA A 326     1522   2273   2005    -85     26    290       C  
ATOM   2627  N   THR A 327      23.120  63.149  41.308  1.00 12.44           N  
ANISOU 2627  N   THR A 327     1636   1724   1365    179   -119    263       N  
ATOM   2628  CA  THR A 327      22.432  62.296  42.264  1.00 13.08           C  
ANISOU 2628  CA  THR A 327     1646   1735   1590    -84     50     44       C  
ATOM   2629  C   THR A 327      21.590  61.234  41.558  1.00 13.18           C  
ANISOU 2629  C   THR A 327     1654   1691   1661    123   -142    -31       C  
ATOM   2630  O   THR A 327      21.629  60.026  41.863  1.00 11.75           O  
ANISOU 2630  O   THR A 327     1350   1669   1447    164    -23    -95       O  
ATOM   2631  CB  THR A 327      21.557  63.171  43.197  1.00 14.64           C  
ANISOU 2631  CB  THR A 327     1778   1941   1843   -290    238   -254       C  
ATOM   2632  OG1 THR A 327      22.393  64.010  44.035  1.00 12.93           O  
ANISOU 2632  OG1 THR A 327     1720   1728   1465     69   -160     98       O  
ATOM   2633  CG2 THR A 327      20.700  62.299  44.100  1.00 15.43           C  
ANISOU 2633  CG2 THR A 327     2055   1810   1997   -121    455   -149       C  
ATOM   2634  N  AARG A 328      20.785  61.699  40.604  0.68 12.60           N  
ANISOU 2634  N  AARG A 328     1444   1796   1545    118     65    117       N  
ATOM   2635  N  BARG A 328      20.805  61.696  40.591  0.32 12.88           N  
ANISOU 2635  N  BARG A 328     1496   1767   1629    128      2     90       N  
ATOM   2636  CA AARG A 328      19.910  60.754  39.895  0.68 12.76           C  
ANISOU 2636  CA AARG A 328     1327   1698   1824    370   -144     41       C  
ATOM   2637  CA BARG A 328      19.917  60.793  39.860  0.32 12.77           C  
ANISOU 2637  CA BARG A 328     1366   1690   1794    331   -130     46       C  
ATOM   2638  C  AARG A 328      20.683  59.790  39.001  0.68 12.60           C  
ANISOU 2638  C  AARG A 328     1367   1574   1847    354    -89    115       C  
ATOM   2639  C  BARG A 328      20.665  59.816  38.966  0.32 12.72           C  
ANISOU 2639  C  BARG A 328     1418   1620   1796    309    -77     87       C  
ATOM   2640  O  AARG A 328      20.245  58.663  38.747  0.68 13.32           O  
ANISOU 2640  O  AARG A 328     1966   1715   1378     77    -54     88       O  
ATOM   2641  O  BARG A 328      20.187  58.711  38.694  0.32 14.52           O  
ANISOU 2641  O  BARG A 328     2186   1798   1532    -93    256    -42       O  
ATOM   2642  CB AARG A 328      18.866  61.528  39.073  0.68 13.06           C  
ANISOU 2642  CB AARG A 328     1390   1643   1931    415    -83    149       C  
ATOM   2643  CB BARG A 328      18.924  61.625  39.031  0.32 13.26           C  
ANISOU 2643  CB BARG A 328     1469   1652   1916    364   -105    138       C  
ATOM   2644  CG AARG A 328      17.699  62.076  39.897  0.68 13.48           C  
ANISOU 2644  CG AARG A 328     1417   1643   2060    426    -46    101       C  
ATOM   2645  CG BARG A 328      18.062  62.509  39.924  0.32 13.68           C  
ANISOU 2645  CG BARG A 328     1452   1694   2053    383    -62     98       C  
ATOM   2646  CD AARG A 328      16.834  62.966  39.024  0.68 13.91           C  
ANISOU 2646  CD AARG A 328     1387   1704   2193    446    -98    102       C  
ATOM   2647  CD BARG A 328      16.937  63.164  39.142  0.32 14.03           C  
ANISOU 2647  CD BARG A 328     1392   1798   2139    371    -51    133       C  
ATOM   2648  NE AARG A 328      15.861  63.763  39.752  0.68 14.03           N  
ANISOU 2648  NE AARG A 328     1337   1809   2184    453    -10    187       N  
ATOM   2649  NE BARG A 328      15.847  63.555  40.045  0.32 14.31           N  
ANISOU 2649  NE BARG A 328     1454   1850   2133    420    -36    102       N  
ATOM   2650  CZ AARG A 328      14.787  63.386  40.429  0.68 13.97           C  
ANISOU 2650  CZ AARG A 328     1454   1851   2003    372    -47    317       C  
ATOM   2651  CZ BARG A 328      15.366  64.792  40.107  0.32 14.25           C  
ANISOU 2651  CZ BARG A 328     1601   1735   2079    279    184    147       C  
ATOM   2652  NH1AARG A 328      14.441  62.112  40.543  0.68 15.11           N  
ANISOU 2652  NH1AARG A 328     1491   1891   2359    249   -169    199       N  
ATOM   2653  NH1BARG A 328      15.878  65.740  39.327  0.32 15.44           N  
ANISOU 2653  NH1BARG A 328      849   1960   3059    276    466    386       N  
ATOM   2654  NH2AARG A 328      14.035  64.330  41.014  0.68 14.47           N  
ANISOU 2654  NH2AARG A 328     1817   1858   1824    169    374    282       N  
ATOM   2655  NH2BARG A 328      14.377  65.072  40.948  0.32 12.19           N  
ANISOU 2655  NH2BARG A 328     1601   1265   1764     85     89    198       N  
ATOM   2656  N   GLU A 329      21.845  60.221  38.501  1.00 13.21           N  
ANISOU 2656  N   GLU A 329     1554   1836   1630    256     31    153       N  
ATOM   2657  CA  GLU A 329      22.654  59.313  37.673  1.00 13.62           C  
ANISOU 2657  CA  GLU A 329     1709   2019   1445    268     90    181       C  
ATOM   2658  C   GLU A 329      23.158  58.165  38.536  1.00 12.90           C  
ANISOU 2658  C   GLU A 329     1528   1868   1505    273    -63     -5       C  
ATOM   2659  O   GLU A 329      23.134  57.007  38.150  1.00 13.89           O  
ANISOU 2659  O   GLU A 329     1975   1863   1441     45     -8     43       O  
ATOM   2660  CB  GLU A 329      23.794  60.077  36.994  1.00 16.93           C  
ANISOU 2660  CB  GLU A 329     2055   2190   2188    235    571    262       C  
ATOM   2661  CG  GLU A 329      24.757  59.252  36.185  1.00 21.10           C  
ANISOU 2661  CG  GLU A 329     2642   2967   2407     71   1070   -285       C  
ATOM   2662  CD  GLU A 329      24.185  58.506  35.009  1.00 27.91           C  
ANISOU 2662  CD  GLU A 329     3994   3908   2703   -154    856   -796       C  
ATOM   2663  OE1 GLU A 329      23.037  58.738  34.579  1.00 32.63           O  
ANISOU 2663  OE1 GLU A 329     4099   5515   2785   -764    340   -528       O  
ATOM   2664  OE2 GLU A 329      24.919  57.637  34.462  1.00 34.91           O  
ANISOU 2664  OE2 GLU A 329     5897   4514   2851    306   1567  -1197       O  
ATOM   2665  N   VAL A 330      23.600  58.480  39.767  1.00 13.06           N  
ANISOU 2665  N   VAL A 330     1637   1759   1565     14   -180    119       N  
ATOM   2666  CA  VAL A 330      24.047  57.399  40.664  1.00 12.54           C  
ANISOU 2666  CA  VAL A 330     1519   1760   1487     10     70    190       C  
ATOM   2667  C   VAL A 330      22.867  56.512  41.043  1.00 13.21           C  
ANISOU 2667  C   VAL A 330     1425   1782   1811    -15    -20    123       C  
ATOM   2668  O   VAL A 330      22.994  55.276  41.047  1.00 12.79           O  
ANISOU 2668  O   VAL A 330     1392   1779   1690    -17    -73    144       O  
ATOM   2669  CB  VAL A 330      24.763  57.981  41.899  1.00 11.83           C  
ANISOU 2669  CB  VAL A 330     1430   1638   1427    -73     74    363       C  
ATOM   2670  CG1 VAL A 330      24.969  56.905  42.979  1.00 12.35           C  
ANISOU 2670  CG1 VAL A 330     2214   1176   1300    315    173     29       C  
ATOM   2671  CG2 VAL A 330      26.081  58.610  41.464  1.00 12.93           C  
ANISOU 2671  CG2 VAL A 330     1349   1577   1985     29    345     19       C  
ATOM   2672  N   LEU A 331      21.713  57.096  41.378  1.00 13.42           N  
ANISOU 2672  N   LEU A 331     1553   1736   1809    -52    186     48       N  
ATOM   2673  CA  LEU A 331      20.558  56.243  41.690  1.00 12.82           C  
ANISOU 2673  CA  LEU A 331     1560   1600   1712     21    240     59       C  
ATOM   2674  C   LEU A 331      20.258  55.305  40.528  1.00 12.33           C  
ANISOU 2674  C   LEU A 331     1360   1666   1657     99     44    145       C  
ATOM   2675  O   LEU A 331      19.989  54.121  40.707  1.00 12.55           O  
ANISOU 2675  O   LEU A 331     1730   1660   1380     66   -105    105       O  
ATOM   2676  CB  LEU A 331      19.354  57.126  41.999  1.00 13.54           C  
ANISOU 2676  CB  LEU A 331     1534   1606   2005     39    166     42       C  
ATOM   2677  CG  LEU A 331      18.049  56.370  42.301  1.00 12.54           C  
ANISOU 2677  CG  LEU A 331     1408   1569   1787    154    -78    450       C  
ATOM   2678  CD1 LEU A 331      18.161  55.521  43.568  1.00 14.01           C  
ANISOU 2678  CD1 LEU A 331     1875   1706   1743      7   -380    441       C  
ATOM   2679  CD2 LEU A 331      16.863  57.318  42.405  1.00 14.95           C  
ANISOU 2679  CD2 LEU A 331     1456   1804   2421    283   -134    432       C  
ATOM   2680  N   SER A 332      20.317  55.843  39.297  1.00 12.93           N  
ANISOU 2680  N   SER A 332     1547   1664   1703    135   -103    250       N  
ATOM   2681  CA  SER A 332      19.981  55.049  38.126  1.00 13.85           C  
ANISOU 2681  CA  SER A 332     1811   1722   1730    298   -244    195       C  
ATOM   2682  C   SER A 332      20.917  53.864  37.899  1.00 13.96           C  
ANISOU 2682  C   SER A 332     1771   1633   1898    213   -179    201       C  
ATOM   2683  O   SER A 332      20.461  52.764  37.557  1.00 14.00           O  
ANISOU 2683  O   SER A 332     1839   1748   1732     60    234     53       O  
ATOM   2684  CB  SER A 332      20.056  55.967  36.887  1.00 15.32           C  
ANISOU 2684  CB  SER A 332     2160   1898   1764    350   -451    287       C  
ATOM   2685  OG  SER A 332      19.699  55.283  35.724  1.00 18.97           O  
ANISOU 2685  OG  SER A 332     2698   2762   1748    113   -457     78       O  
ATOM   2686  N  AGLU A 333      22.213  54.114  38.080  0.66 13.42           N  
ANISOU 2686  N  AGLU A 333     1709   1747   1642    192    -23    265       N  
ATOM   2687  N  BGLU A 333      22.211  54.119  38.065  0.34 13.46           N  
ANISOU 2687  N  BGLU A 333     1714   1739   1662    199    -38    251       N  
ATOM   2688  CA AGLU A 333      23.251  53.152  37.734  0.66 14.18           C  
ANISOU 2688  CA AGLU A 333     1831   1958   1601    275    203    283       C  
ATOM   2689  CA BGLU A 333      23.271  53.172  37.754  0.34 14.21           C  
ANISOU 2689  CA BGLU A 333     1830   1973   1598    296    174    258       C  
ATOM   2690  C  AGLU A 333      23.614  52.216  38.883  0.66 13.15           C  
ANISOU 2690  C  AGLU A 333     1648   1787   1561    359    257    165       C  
ATOM   2691  C  BGLU A 333      23.510  52.163  38.874  0.34 13.11           C  
ANISOU 2691  C  BGLU A 333     1644   1797   1539    370    202    129       C  
ATOM   2692  O  AGLU A 333      24.254  51.182  38.661  0.66 13.59           O  
ANISOU 2692  O  AGLU A 333     1809   1582   1771    200    238     13       O  
ATOM   2693  O  BGLU A 333      23.954  51.041  38.615  0.34 13.42           O  
ANISOU 2693  O  BGLU A 333     1797   1580   1722     57    220     -3       O  
ATOM   2694  CB AGLU A 333      24.526  53.888  37.260  0.66 16.09           C  
ANISOU 2694  CB AGLU A 333     1935   2148   2032    283    365    513       C  
ATOM   2695  CB BGLU A 333      24.599  53.901  37.468  0.34 15.64           C  
ANISOU 2695  CB BGLU A 333     1850   2123   1970    310    232    476       C  
ATOM   2696  CG AGLU A 333      24.413  54.578  35.908  0.66 17.76           C  
ANISOU 2696  CG AGLU A 333     2322   2249   2177    351    498    697       C  
ATOM   2697  CG BGLU A 333      24.621  54.860  36.299  0.34 19.24           C  
ANISOU 2697  CG BGLU A 333     2889   2260   2160     53    397    637       C  
ATOM   2698  CD AGLU A 333      24.039  53.634  34.785  0.66 21.02           C  
ANISOU 2698  CD AGLU A 333     3554   2407   2025    236     98    849       C  
ATOM   2699  CD BGLU A 333      25.986  55.354  35.889  0.34 21.23           C  
ANISOU 2699  CD BGLU A 333     3189   2341   2535   -182    716    515       C  
ATOM   2700  OE1AGLU A 333      24.476  52.461  34.763  0.66 25.09           O  
ANISOU 2700  OE1AGLU A 333     5095   2127   2313    159    200    768       O  
ATOM   2701  OE1BGLU A 333      26.850  54.555  35.440  0.34 28.21           O  
ANISOU 2701  OE1BGLU A 333     3342   3746   3630    244   1182    215       O  
ATOM   2702  OE2AGLU A 333      23.275  54.023  33.871  0.66 27.47           O  
ANISOU 2702  OE2AGLU A 333     4033   3648   2757    214   -627    919       O  
ATOM   2703  OE2BGLU A 333      26.275  56.571  35.977  0.34 29.72           O  
ANISOU 2703  OE2BGLU A 333     4234   2603   4454   -814     99    453       O  
ATOM   2704  N   TYR A 334      23.238  52.551  40.119  1.00 13.10           N  
ANISOU 2704  N   TYR A 334     1717   1733   1526    284    210    120       N  
ATOM   2705  CA  TYR A 334      23.633  51.757  41.278  1.00 12.46           C  
ANISOU 2705  CA  TYR A 334     1509   1686   1538     37     67    106       C  
ATOM   2706  C   TYR A 334      22.600  51.533  42.365  1.00 12.27           C  
ANISOU 2706  C   TYR A 334     1593   1518   1550     66    111     98       C  
ATOM   2707  O   TYR A 334      22.852  50.758  43.306  1.00 13.15           O  
ANISOU 2707  O   TYR A 334     1651   1953   1393     82    -18    146       O  
ATOM   2708  CB  TYR A 334      24.775  52.523  41.976  1.00 13.53           C  
ANISOU 2708  CB  TYR A 334     1563   1750   1829    -18     84    -78       C  
ATOM   2709  CG  TYR A 334      26.001  52.755  41.121  1.00 13.21           C  
ANISOU 2709  CG  TYR A 334     1614   1829   1578   -134     39   -229       C  
ATOM   2710  CD1 TYR A 334      26.930  51.747  40.902  1.00 14.21           C  
ANISOU 2710  CD1 TYR A 334     1622   2029   1749    -42    125   -226       C  
ATOM   2711  CD2 TYR A 334      26.214  54.017  40.552  1.00 13.86           C  
ANISOU 2711  CD2 TYR A 334     1781   2017   1468   -171    -55    -37       C  
ATOM   2712  CE1 TYR A 334      28.052  51.983  40.121  1.00 15.11           C  
ANISOU 2712  CE1 TYR A 334     1544   2270   1927   -100    114   -184       C  
ATOM   2713  CE2 TYR A 334      27.333  54.250  39.770  1.00 15.91           C  
ANISOU 2713  CE2 TYR A 334     2011   2123   1911   -305    225    -81       C  
ATOM   2714  CZ  TYR A 334      28.236  53.223  39.561  1.00 16.27           C  
ANISOU 2714  CZ  TYR A 334     1908   2341   1933   -251    262   -169       C  
ATOM   2715  OH  TYR A 334      29.348  53.494  38.786  1.00 21.73           O  
ANISOU 2715  OH  TYR A 334     1998   3142   3116     77    654    728       O  
ATOM   2716  N   GLY A 335      21.437  52.185  42.328  1.00 12.16           N  
ANISOU 2716  N   GLY A 335     1547   1538   1536     16    120     59       N  
ATOM   2717  CA  GLY A 335      20.514  52.073  43.433  1.00 12.75           C  
ANISOU 2717  CA  GLY A 335     1507   1855   1482    -98     81     11       C  
ATOM   2718  C   GLY A 335      20.970  52.857  44.651  1.00 11.58           C  
ANISOU 2718  C   GLY A 335     1181   1656   1562    137     56     -6       C  
ATOM   2719  O   GLY A 335      21.958  53.578  44.646  1.00 12.86           O  
ANISOU 2719  O   GLY A 335     1234   1844   1807     35   -101     55       O  
ATOM   2720  N   ASN A 336      20.218  52.712  45.735  1.00 12.37           N  
ANISOU 2720  N   ASN A 336     1558   1761   1381    154     39    191       N  
ATOM   2721  CA  ASN A 336      20.522  53.303  47.032  1.00 12.12           C  
ANISOU 2721  CA  ASN A 336     1289   1787   1529    154     14     31       C  
ATOM   2722  C   ASN A 336      21.585  52.430  47.719  1.00 13.02           C  
ANISOU 2722  C   ASN A 336     1334   1896   1717     24   -136    256       C  
ATOM   2723  O   ASN A 336      21.263  51.347  48.244  1.00 12.95           O  
ANISOU 2723  O   ASN A 336     1726   1660   1535    -50   -240     -4       O  
ATOM   2724  CB  ASN A 336      19.254  53.403  47.873  1.00 12.97           C  
ANISOU 2724  CB  ASN A 336     1451   1845   1631     88    148    -57       C  
ATOM   2725  CG  ASN A 336      19.420  53.789  49.318  1.00 11.51           C  
ANISOU 2725  CG  ASN A 336     1344   1473   1556    232     76    142       C  
ATOM   2726  OD1 ASN A 336      20.535  53.949  49.799  1.00 12.57           O  
ANISOU 2726  OD1 ASN A 336     1423   1609   1745    215    -53    167       O  
ATOM   2727  ND2 ASN A 336      18.296  53.965  50.039  1.00 12.24           N  
ANISOU 2727  ND2 ASN A 336     1503   1433   1716     18    291     46       N  
ATOM   2728  N   MET A 337      22.813  52.928  47.723  1.00 13.98           N  
ANISOU 2728  N   MET A 337     1372   2218   1724    -75   -213    281       N  
ATOM   2729  CA  MET A 337      23.912  52.206  48.386  1.00 12.88           C  
ANISOU 2729  CA  MET A 337     1305   2149   1439    141    -72   -135       C  
ATOM   2730  C   MET A 337      24.178  52.687  49.814  1.00 11.99           C  
ANISOU 2730  C   MET A 337     1527   1597   1431    148    -60    -38       C  
ATOM   2731  O   MET A 337      25.315  52.638  50.317  1.00 11.27           O  
ANISOU 2731  O   MET A 337     1493   1491   1297    -54      3    -75       O  
ATOM   2732  CB  MET A 337      25.160  52.322  47.509  1.00 14.13           C  
ANISOU 2732  CB  MET A 337     1440   2336   1592    -77     48   -350       C  
ATOM   2733  CG  MET A 337      25.036  51.644  46.152  1.00 13.65           C  
ANISOU 2733  CG  MET A 337     1731   1998   1456   -269    149   -139       C  
ATOM   2734  SD  MET A 337      26.509  51.944  45.141  1.00 12.85           S  
ANISOU 2734  SD  MET A 337     1488   1755   1637    101    129    -65       S  
ATOM   2735  CE  MET A 337      26.331  53.696  44.813  1.00 12.88           C  
ANISOU 2735  CE  MET A 337     1969   1520   1405   -315    116   -463       C  
ATOM   2736  N   SER A 338      23.141  53.136  50.508  1.00 11.70           N  
ANISOU 2736  N   SER A 338     1574   1446   1425    145    -31     16       N  
ATOM   2737  CA  SER A 338      23.228  53.558  51.905  1.00 11.55           C  
ANISOU 2737  CA  SER A 338     1608   1254   1527    216    -93   -107       C  
ATOM   2738  C   SER A 338      24.372  54.528  52.105  1.00 10.92           C  
ANISOU 2738  C   SER A 338     1392   1457   1300    193    210   -121       C  
ATOM   2739  O   SER A 338      24.502  55.427  51.254  1.00 12.62           O  
ANISOU 2739  O   SER A 338     1708   1452   1636    160     66     53       O  
ATOM   2740  CB  SER A 338      23.320  52.331  52.823  1.00 13.31           C  
ANISOU 2740  CB  SER A 338     2227   1467   1363     57    195     10       C  
ATOM   2741  OG  SER A 338      23.373  52.724  54.202  1.00 14.88           O  
ANISOU 2741  OG  SER A 338     2146   2128   1378   -188    169    -97       O  
ATOM   2742  N   SER A 339      25.215  54.355  53.143  1.00 11.31           N  
ANISOU 2742  N   SER A 339     1350   1548   1399    123    167    -73       N  
ATOM   2743  CA  SER A 339      26.203  55.406  53.441  1.00 11.04           C  
ANISOU 2743  CA  SER A 339     1394   1368   1431    267    174   -262       C  
ATOM   2744  C   SER A 339      27.122  55.735  52.273  1.00 10.85           C  
ANISOU 2744  C   SER A 339     1019   1359   1746    347    197   -129       C  
ATOM   2745  O   SER A 339      27.586  56.881  52.168  1.00 13.31           O  
ANISOU 2745  O   SER A 339     1993   1273   1789    313    263     94       O  
ATOM   2746  CB  SER A 339      27.001  54.991  54.670  1.00 12.68           C  
ANISOU 2746  CB  SER A 339     1779   1453   1588    238   -120   -321       C  
ATOM   2747  OG  SER A 339      27.847  53.893  54.388  1.00 12.89           O  
ANISOU 2747  OG  SER A 339     1688   1498   1712    297     -5    -34       O  
ATOM   2748  N   ALA A 340      27.425  54.783  51.378  1.00 11.07           N  
ANISOU 2748  N   ALA A 340     1371   1549   1285     42    198   -122       N  
ATOM   2749  CA  ALA A 340      28.387  55.033  50.305  1.00 11.35           C  
ANISOU 2749  CA  ALA A 340     1455   1407   1451     51    292     -2       C  
ATOM   2750  C   ALA A 340      27.822  55.924  49.197  1.00 11.91           C  
ANISOU 2750  C   ALA A 340     1603   1463   1462   -152     99     33       C  
ATOM   2751  O   ALA A 340      28.566  56.521  48.400  1.00 12.54           O  
ANISOU 2751  O   ALA A 340     1613   1927   1227    -73    151     59       O  
ATOM   2752  CB  ALA A 340      28.809  53.735  49.637  1.00 12.24           C  
ANISOU 2752  CB  ALA A 340     1341   1606   1705    122    382   -173       C  
ATOM   2753  N   CYS A 341      26.499  56.029  49.115  1.00 11.44           N  
ANISOU 2753  N   CYS A 341     1601   1430   1315     57    224     -5       N  
ATOM   2754  CA  CYS A 341      25.905  56.617  47.905  1.00 12.61           C  
ANISOU 2754  CA  CYS A 341     1735   1520   1539    412    306    159       C  
ATOM   2755  C   CYS A 341      26.327  58.054  47.619  1.00 13.97           C  
ANISOU 2755  C   CYS A 341     2093   1665   1551    186    129    227       C  
ATOM   2756  O   CYS A 341      26.689  58.452  46.490  1.00 11.80           O  
ANISOU 2756  O   CYS A 341     1281   1629   1575    231     85    191       O  
ATOM   2757  CB  CYS A 341      24.384  56.478  48.085  1.00 14.71           C  
ANISOU 2757  CB  CYS A 341     1684   2027   1877    285    117    148       C  
ATOM   2758  SG  CYS A 341      23.463  56.492  46.544  1.00 18.04           S  
ANISOU 2758  SG  CYS A 341     2184   2606   2063    148   -173   -191       S  
ATOM   2759  N   VAL A 342      26.277  58.881  48.681  1.00 12.08           N  
ANISOU 2759  N   VAL A 342     1567   1587   1437     34   -122    299       N  
ATOM   2760  CA  VAL A 342      26.659  60.302  48.525  1.00 13.42           C  
ANISOU 2760  CA  VAL A 342     1332   1613   2154     32    -11    301       C  
ATOM   2761  C   VAL A 342      28.084  60.406  48.047  1.00 12.23           C  
ANISOU 2761  C   VAL A 342     1393   1498   1757    157      8    145       C  
ATOM   2762  O   VAL A 342      28.463  61.371  47.333  1.00 12.37           O  
ANISOU 2762  O   VAL A 342     1442   1464   1794    260    244     91       O  
ATOM   2763  CB  VAL A 342      26.280  60.739  49.969  1.00 19.26           C  
ANISOU 2763  CB  VAL A 342     1826   2331   3161     10    804   -847       C  
ATOM   2764  CG1 VAL A 342      27.372  61.332  50.788  1.00 22.12           C  
ANISOU 2764  CG1 VAL A 342     2186   3336   2884    469    398  -1361       C  
ATOM   2765  CG2 VAL A 342      24.966  61.514  49.890  1.00 14.78           C  
ANISOU 2765  CG2 VAL A 342     2843   1536   1236    470    -95    -14       C  
ATOM   2766  N   LEU A 343      28.946  59.462  48.424  1.00 11.88           N  
ANISOU 2766  N   LEU A 343     1507   1448   1560    260      3    -35       N  
ATOM   2767  CA  LEU A 343      30.357  59.558  48.019  1.00 11.56           C  
ANISOU 2767  CA  LEU A 343     1354   1750   1290    163   -343    174       C  
ATOM   2768  C   LEU A 343      30.484  59.210  46.535  1.00 10.90           C  
ANISOU 2768  C   LEU A 343     1236   1681   1226     67   -233    306       C  
ATOM   2769  O   LEU A 343      31.283  59.785  45.793  1.00 12.73           O  
ANISOU 2769  O   LEU A 343     1558   1559   1718     42    148    272       O  
ATOM   2770  CB  LEU A 343      31.279  58.671  48.880  1.00 10.77           C  
ANISOU 2770  CB  LEU A 343     1540   1425   1125    139   -167    226       C  
ATOM   2771  CG  LEU A 343      31.165  58.948  50.400  1.00 11.92           C  
ANISOU 2771  CG  LEU A 343     1837   1524   1166     58   -354     68       C  
ATOM   2772  CD1 LEU A 343      32.192  58.124  51.176  1.00 12.19           C  
ANISOU 2772  CD1 LEU A 343     1539   1911   1180    -67   -188    411       C  
ATOM   2773  CD2 LEU A 343      31.296  60.424  50.710  1.00 14.13           C  
ANISOU 2773  CD2 LEU A 343     2228   1578   1564    -58    -56    -84       C  
ATOM   2774  N   PHE A 344      29.686  58.270  46.041  1.00 11.85           N  
ANISOU 2774  N   PHE A 344     1356   1658   1486     45    234   -190       N  
ATOM   2775  CA  PHE A 344      29.601  57.987  44.616  1.00 10.79           C  
ANISOU 2775  CA  PHE A 344     1283   1328   1488    111    156   -113       C  
ATOM   2776  C   PHE A 344      29.110  59.229  43.870  1.00 12.26           C  
ANISOU 2776  C   PHE A 344     1613   1342   1703    156    305     36       C  
ATOM   2777  O   PHE A 344      29.554  59.491  42.735  1.00 13.12           O  
ANISOU 2777  O   PHE A 344     1298   1888   1800    -49    213    301       O  
ATOM   2778  CB  PHE A 344      28.606  56.881  44.264  1.00 11.91           C  
ANISOU 2778  CB  PHE A 344     1484   1405   1636    -43    100    -51       C  
ATOM   2779  CG  PHE A 344      29.175  55.469  44.332  1.00 12.87           C  
ANISOU 2779  CG  PHE A 344     1898   1342   1652    -28    251   -108       C  
ATOM   2780  CD1 PHE A 344      29.469  54.905  45.576  1.00 12.84           C  
ANISOU 2780  CD1 PHE A 344     1678   1440   1760    260     28   -180       C  
ATOM   2781  CD2 PHE A 344      29.399  54.738  43.174  1.00 12.70           C  
ANISOU 2781  CD2 PHE A 344     1497   1603   1725   -132    543   -164       C  
ATOM   2782  CE1 PHE A 344      29.961  53.606  45.648  1.00 11.18           C  
ANISOU 2782  CE1 PHE A 344     1084   1458   1708    201    230   -263       C  
ATOM   2783  CE2 PHE A 344      29.865  53.430  43.230  1.00 13.33           C  
ANISOU 2783  CE2 PHE A 344     1754   1623   1688    -49    488   -292       C  
ATOM   2784  CZ  PHE A 344      30.135  52.876  44.470  1.00 12.55           C  
ANISOU 2784  CZ  PHE A 344     1484   1559   1726    -34    415   -307       C  
ATOM   2785  N   ILE A 345      28.177  59.962  44.454  1.00 11.95           N  
ANISOU 2785  N   ILE A 345     1291   1478   1770    193     24    -16       N  
ATOM   2786  CA  ILE A 345      27.684  61.180  43.766  1.00 11.85           C  
ANISOU 2786  CA  ILE A 345     1101   1609   1795    156    -33     75       C  
ATOM   2787  C   ILE A 345      28.756  62.242  43.696  1.00 12.02           C  
ANISOU 2787  C   ILE A 345     1415   1673   1478    -49    -41     62       C  
ATOM   2788  O   ILE A 345      28.937  62.948  42.689  1.00 12.72           O  
ANISOU 2788  O   ILE A 345     1355   1897   1582     89     55    204       O  
ATOM   2789  CB  ILE A 345      26.400  61.684  44.450  1.00 12.09           C  
ANISOU 2789  CB  ILE A 345     1349   1484   1759    229    114     90       C  
ATOM   2790  CG1 ILE A 345      25.303  60.623  44.368  1.00 12.12           C  
ANISOU 2790  CG1 ILE A 345     1353   1749   1502     75    361    147       C  
ATOM   2791  CG2 ILE A 345      25.997  63.026  43.845  1.00 13.77           C  
ANISOU 2791  CG2 ILE A 345     1951   1426   1856    438    365     32       C  
ATOM   2792  CD1 ILE A 345      24.115  60.864  45.297  1.00 11.38           C  
ANISOU 2792  CD1 ILE A 345     1476   1420   1427    305    311     41       C  
ATOM   2793  N   LEU A 346      29.559  62.416  44.757  1.00 11.93           N  
ANISOU 2793  N   LEU A 346     1386   1633   1514    107    -45    -75       N  
ATOM   2794  CA  LEU A 346      30.654  63.362  44.662  1.00 13.07           C  
ANISOU 2794  CA  LEU A 346     1708   1908   1348   -200     45   -398       C  
ATOM   2795  C   LEU A 346      31.611  62.996  43.510  1.00 12.87           C  
ANISOU 2795  C   LEU A 346     1680   1704   1508     21    168    -66       C  
ATOM   2796  O   LEU A 346      32.104  63.846  42.770  1.00 13.44           O  
ANISOU 2796  O   LEU A 346     1444   1695   1967    -56    230     10       O  
ATOM   2797  CB  LEU A 346      31.449  63.401  45.969  1.00 11.85           C  
ANISOU 2797  CB  LEU A 346     1511   1437   1555    269   -109   -288       C  
ATOM   2798  CG  LEU A 346      30.807  64.084  47.181  1.00 11.21           C  
ANISOU 2798  CG  LEU A 346     1942   1179   1139    410   -183     68       C  
ATOM   2799  CD1 LEU A 346      31.642  63.796  48.425  1.00 15.03           C  
ANISOU 2799  CD1 LEU A 346     2350   1837   1525     27   -708    111       C  
ATOM   2800  CD2 LEU A 346      30.670  65.597  46.982  1.00 13.21           C  
ANISOU 2800  CD2 LEU A 346     1994   1132   1894    317    211     53       C  
ATOM   2801  N   ASP A 347      31.871  61.695  43.377  1.00 12.73           N  
ANISOU 2801  N   ASP A 347     1492   1695   1652     58    110      8       N  
ATOM   2802  CA  ASP A 347      32.754  61.220  42.313  1.00 12.87           C  
ANISOU 2802  CA  ASP A 347     1652   1761   1479    217    -27    -23       C  
ATOM   2803  C   ASP A 347      32.171  61.504  40.918  1.00 14.19           C  
ANISOU 2803  C   ASP A 347     1860   1973   1558   -142   -171    117       C  
ATOM   2804  O   ASP A 347      32.864  62.017  40.033  1.00 14.30           O  
ANISOU 2804  O   ASP A 347     1627   2262   1543     89    -99    147       O  
ATOM   2805  CB  ASP A 347      33.008  59.728  42.443  1.00 13.31           C  
ANISOU 2805  CB  ASP A 347     1864   1687   1505     52    377     81       C  
ATOM   2806  CG  ASP A 347      34.281  59.286  41.744  1.00 14.05           C  
ANISOU 2806  CG  ASP A 347     1891   1673   1776    147    398     16       C  
ATOM   2807  OD1 ASP A 347      35.208  60.126  41.569  1.00 15.65           O  
ANISOU 2807  OD1 ASP A 347     1699   2075   2170     15    315    -68       O  
ATOM   2808  OD2 ASP A 347      34.369  58.070  41.383  1.00 18.36           O  
ANISOU 2808  OD2 ASP A 347     2364   1844   2769    199    553   -392       O  
ATOM   2809  N   GLU A 348      30.889  61.196  40.748  1.00 12.79           N  
ANISOU 2809  N   GLU A 348     1787   1668   1402    -11    -78    -54       N  
ATOM   2810  CA  GLU A 348      30.183  61.475  39.498  1.00 12.42           C  
ANISOU 2810  CA  GLU A 348     1595   1714   1408     53     74    179       C  
ATOM   2811  C   GLU A 348      30.235  62.955  39.124  1.00 13.20           C  
ANISOU 2811  C   GLU A 348     1604   1701   1708    115    241    170       C  
ATOM   2812  O   GLU A 348      30.551  63.333  37.997  1.00 15.35           O  
ANISOU 2812  O   GLU A 348     2480   1804   1549    -90   -138    324       O  
ATOM   2813  CB  GLU A 348      28.717  61.033  39.619  1.00 13.24           C  
ANISOU 2813  CB  GLU A 348     1586   1846   1597     49     -2    368       C  
ATOM   2814  CG  GLU A 348      27.863  61.598  38.478  1.00 15.27           C  
ANISOU 2814  CG  GLU A 348     1828   2466   1510     54   -188    316       C  
ATOM   2815  CD  GLU A 348      28.070  60.962  37.123  1.00 17.90           C  
ANISOU 2815  CD  GLU A 348     2602   2538   1660    -34   -270    100       C  
ATOM   2816  OE1 GLU A 348      28.774  59.963  36.917  1.00 18.36           O  
ANISOU 2816  OE1 GLU A 348     2962   2599   1415    118   -214    129       O  
ATOM   2817  OE2 GLU A 348      27.479  61.477  36.149  1.00 18.73           O  
ANISOU 2817  OE2 GLU A 348     2807   2886   1423    315     21    172       O  
ATOM   2818  N   MET A 349      29.938  63.807  40.097  1.00 15.34           N  
ANISOU 2818  N   MET A 349     2161   1764   1901   -303    109   -156       N  
ATOM   2819  CA  MET A 349      29.917  65.249  39.875  1.00 13.11           C  
ANISOU 2819  CA  MET A 349     1452   1804   1724     28      1    -70       C  
ATOM   2820  C   MET A 349      31.291  65.786  39.488  1.00 12.35           C  
ANISOU 2820  C   MET A 349     1559   1698   1437     56    131    -20       C  
ATOM   2821  O   MET A 349      31.433  66.573  38.542  1.00 17.34           O  
ANISOU 2821  O   MET A 349     2250   2165   2172   -184    -22    632       O  
ATOM   2822  CB  MET A 349      29.423  65.976  41.140  1.00 12.79           C  
ANISOU 2822  CB  MET A 349     1541   1727   1589     13    197    182       C  
ATOM   2823  CG  MET A 349      29.494  67.500  40.931  1.00 14.53           C  
ANISOU 2823  CG  MET A 349     1948   1679   1895   -220    397    -20       C  
ATOM   2824  SD  MET A 349      28.861  68.409  42.378  1.00 15.79           S  
ANISOU 2824  SD  MET A 349     2101   2022   1877      1    119   -214       S  
ATOM   2825  CE  MET A 349      27.130  67.865  42.344  1.00 14.52           C  
ANISOU 2825  CE  MET A 349     2156   1710   1652    -76    500    135       C  
ATOM   2826  N   ARG A 350      32.339  65.397  40.214  1.00 13.26           N  
ANISOU 2826  N   ARG A 350     1368   1921   1748    155    207     45       N  
ATOM   2827  CA  ARG A 350      33.648  65.958  39.812  1.00 14.27           C  
ANISOU 2827  CA  ARG A 350     1518   2070   1834    -33    260     10       C  
ATOM   2828  C   ARG A 350      34.129  65.362  38.495  1.00 15.54           C  
ANISOU 2828  C   ARG A 350     1678   2220   2005    -76    509    -53       C  
ATOM   2829  O   ARG A 350      34.821  66.074  37.735  1.00 16.73           O  
ANISOU 2829  O   ARG A 350     2140   2438   1780    -80    357    272       O  
ATOM   2830  CB  ARG A 350      34.670  65.799  40.947  1.00 14.58           C  
ANISOU 2830  CB  ARG A 350     1415   2008   2117    -10    155    103       C  
ATOM   2831  CG  ARG A 350      35.002  64.369  41.334  1.00 14.67           C  
ANISOU 2831  CG  ARG A 350     1540   2002   2033     41    334     79       C  
ATOM   2832  CD  ARG A 350      36.291  63.884  40.674  1.00 16.54           C  
ANISOU 2832  CD  ARG A 350     1591   2105   2590     82    471     -5       C  
ATOM   2833  NE  ARG A 350      36.604  62.512  41.115  1.00 16.61           N  
ANISOU 2833  NE  ARG A 350     1730   2107   2473    140    484    -41       N  
ATOM   2834  CZ  ARG A 350      37.843  62.108  41.431  1.00 16.49           C  
ANISOU 2834  CZ  ARG A 350     1828   2183   2254    -40    163    194       C  
ATOM   2835  NH1 ARG A 350      38.878  62.949  41.365  1.00 16.50           N  
ANISOU 2835  NH1 ARG A 350     2000   2597   1672   -323     -3    218       N  
ATOM   2836  NH2 ARG A 350      38.054  60.853  41.820  1.00 15.91           N  
ANISOU 2836  NH2 ARG A 350     2212   2280   1551      2    -79    197       N  
ATOM   2837  N   LYS A 351      33.778  64.109  38.185  1.00 14.26           N  
ANISOU 2837  N   LYS A 351     1466   2059   1895    288    149      7       N  
ATOM   2838  CA  LYS A 351      34.248  63.514  36.934  1.00 16.55           C  
ANISOU 2838  CA  LYS A 351     2032   2232   2023    157    429    -61       C  
ATOM   2839  C   LYS A 351      33.562  64.157  35.737  1.00 16.26           C  
ANISOU 2839  C   LYS A 351     2118   2206   1855    -66    289   -197       C  
ATOM   2840  O   LYS A 351      34.227  64.388  34.716  1.00 17.72           O  
ANISOU 2840  O   LYS A 351     2118   2564   2052   -138    362     30       O  
ATOM   2841  CB  LYS A 351      34.032  61.999  36.948  1.00 19.03           C  
ANISOU 2841  CB  LYS A 351     2355   2112   2765    525    413   -210       C  
ATOM   2842  CG  LYS A 351      35.018  61.265  37.881  1.00 23.32           C  
ANISOU 2842  CG  LYS A 351     3211   2548   3101    209    -56    488       C  
ATOM   2843  CD  LYS A 351      34.699  59.772  37.904  1.00 23.82           C  
ANISOU 2843  CD  LYS A 351     3375   2340   3335    678    355    158       C  
ATOM   2844  CE  LYS A 351      35.964  58.948  38.076  1.00 24.44           C  
ANISOU 2844  CE  LYS A 351     3125   2820   3342    670    343   -146       C  
ATOM   2845  NZ  LYS A 351      36.666  59.260  39.337  1.00 26.65           N  
ANISOU 2845  NZ  LYS A 351     2963   2977   4186    232    -68   -597       N  
ATOM   2846  N   LYS A 352      32.265  64.447  35.879  1.00 15.47           N  
ANISOU 2846  N   LYS A 352     2223   1981   1675    107    323   -166       N  
ATOM   2847  CA  LYS A 352      31.557  65.088  34.766  1.00 16.83           C  
ANISOU 2847  CA  LYS A 352     2494   2029   1871    269    318      6       C  
ATOM   2848  C   LYS A 352      32.052  66.517  34.584  1.00 18.09           C  
ANISOU 2848  C   LYS A 352     2953   2134   1787     38    278      0       C  
ATOM   2849  O   LYS A 352      32.323  66.986  33.464  1.00 20.77           O  
ANISOU 2849  O   LYS A 352     3833   2236   1822    -41    275    131       O  
ATOM   2850  CB  LYS A 352      30.049  65.043  34.985  1.00 17.86           C  
ANISOU 2850  CB  LYS A 352     2414   2220   2150    296    127    -89       C  
ATOM   2851  CG  LYS A 352      29.434  63.647  34.853  1.00 22.26           C  
ANISOU 2851  CG  LYS A 352     3141   2742   2575   -441    655   -443       C  
ATOM   2852  CD  LYS A 352      29.980  62.969  33.597  1.00 29.08           C  
ANISOU 2852  CD  LYS A 352     4794   3225   3028   -970   1140  -1132       C  
ATOM   2853  CE  LYS A 352      28.874  62.371  32.748  1.00 28.82           C  
ANISOU 2853  CE  LYS A 352     4755   3148   3047   -780   1055  -1131       C  
ATOM   2854  NZ  LYS A 352      28.350  61.145  33.384  1.00 29.17           N  
ANISOU 2854  NZ  LYS A 352     5755   2368   2960   -765    214  -1341       N  
ATOM   2855  N   SER A 353      32.175  67.222  35.707  1.00 19.78           N  
ANISOU 2855  N   SER A 353     3224   2458   1832   -346     24    -53       N  
ATOM   2856  CA  SER A 353      32.630  68.621  35.655  1.00 19.10           C  
ANISOU 2856  CA  SER A 353     3143   2348   1768   -176    277    -89       C  
ATOM   2857  C   SER A 353      33.997  68.744  35.009  1.00 19.95           C  
ANISOU 2857  C   SER A 353     3433   2321   1824   -126    617      0       C  
ATOM   2858  O   SER A 353      34.313  69.650  34.224  1.00 22.71           O  
ANISOU 2858  O   SER A 353     3735   2705   2189   -559    356    317       O  
ATOM   2859  CB  SER A 353      32.638  69.171  37.088  1.00 17.60           C  
ANISOU 2859  CB  SER A 353     2830   2165   1694    -12    294     38       C  
ATOM   2860  OG  SER A 353      31.338  69.154  37.660  1.00 16.64           O  
ANISOU 2860  OG  SER A 353     2710   1916   1696     -1    156    296       O  
ATOM   2861  N  ATHR A 354      34.882  67.802  35.324  0.43 21.50           N  
ANISOU 2861  N  ATHR A 354     3251   2703   2215    -35    556     85       N  
ATOM   2862  N  BTHR A 354      34.914  67.816  35.297  0.57 21.53           N  
ANISOU 2862  N  BTHR A 354     3217   2737   2229    -53    525     93       N  
ATOM   2863  CA ATHR A 354      36.187  67.780  34.675  0.43 21.95           C  
ANISOU 2863  CA ATHR A 354     3342   2770   2226   -103    642    180       C  
ATOM   2864  CA BTHR A 354      36.226  67.871  34.635  0.57 21.84           C  
ANISOU 2864  CA BTHR A 354     3387   2685   2227    -89    676    199       C  
ATOM   2865  C  ATHR A 354      36.093  67.381  33.216  0.43 23.37           C  
ANISOU 2865  C  ATHR A 354     3758   2889   2233   -199    767    123       C  
ATOM   2866  C  BTHR A 354      36.153  67.340  33.220  0.57 23.40           C  
ANISOU 2866  C  BTHR A 354     3770   2892   2230   -198    751    156       C  
ATOM   2867  O  ATHR A 354      36.590  68.068  32.321  0.43 28.66           O  
ANISOU 2867  O  ATHR A 354     5281   3257   2353   -897   1310   -142       O  
ATOM   2868  O  BTHR A 354      36.720  67.928  32.285  0.57 27.86           O  
ANISOU 2868  O  BTHR A 354     4931   3198   2456   -740   1409   -204       O  
ATOM   2869  CB ATHR A 354      37.124  66.761  35.365  0.43 22.08           C  
ANISOU 2869  CB ATHR A 354     3225   2658   2505    -71    619     64       C  
ATOM   2870  CB BTHR A 354      37.287  67.101  35.448  0.57 21.94           C  
ANISOU 2870  CB BTHR A 354     3194   2655   2487    -87    624     62       C  
ATOM   2871  OG1ATHR A 354      37.408  67.202  36.689  0.43 23.06           O  
ANISOU 2871  OG1ATHR A 354     3834   2559   2370   -555    391    453       O  
ATOM   2872  OG1BTHR A 354      36.938  65.723  35.604  0.57 19.44           O  
ANISOU 2872  OG1BTHR A 354     2385   2641   2362     32    781     -2       O  
ATOM   2873  CG2ATHR A 354      38.409  66.686  34.562  0.43 23.93           C  
ANISOU 2873  CG2ATHR A 354     3112   2876   3105   -342    681     24       C  
ATOM   2874  CG2BTHR A 354      37.352  67.680  36.855  0.57 24.82           C  
ANISOU 2874  CG2BTHR A 354     4185   2845   2398   -859    238    243       C  
ATOM   2875  N   GLN A 355      35.464  66.243  32.962  1.00 25.34           N  
ANISOU 2875  N   GLN A 355     4310   3049   2271   -475   1174   -157       N  
ATOM   2876  CA  GLN A 355      35.382  65.762  31.583  1.00 27.99           C  
ANISOU 2876  CA  GLN A 355     4834   3400   2402   -397   1217   -427       C  
ATOM   2877  C   GLN A 355      34.720  66.789  30.682  1.00 28.79           C  
ANISOU 2877  C   GLN A 355     5365   3581   1992   -276   1246   -452       C  
ATOM   2878  O   GLN A 355      35.024  66.897  29.488  1.00 34.61           O  
ANISOU 2878  O   GLN A 355     7517   3527   2105   -381   1738   -455       O  
ATOM   2879  CB  GLN A 355      34.652  64.420  31.551  1.00 29.88           C  
ANISOU 2879  CB  GLN A 355     5093   3414   2846   -448    790   -570       C  
ATOM   2880  CG  GLN A 355      33.830  64.177  30.292  1.00 33.42           C  
ANISOU 2880  CG  GLN A 355     5543   3781   3375   -322    238   -613       C  
ATOM   2881  CD  GLN A 355      32.941  62.960  30.511  1.00 34.93           C  
ANISOU 2881  CD  GLN A 355     5531   4138   3602   -580   -278   -299       C  
ATOM   2882  OE1 GLN A 355      33.334  62.016  31.205  1.00 35.88           O  
ANISOU 2882  OE1 GLN A 355     5653   4024   3955   -434    -77   -212       O  
ATOM   2883  NE2 GLN A 355      31.747  63.005  29.927  1.00 40.22           N  
ANISOU 2883  NE2 GLN A 355     6789   5572   2919  -1491  -1382    -43       N  
ATOM   2884  N   ASN A 356      33.787  67.599  31.182  1.00 30.54           N  
ANISOU 2884  N   ASN A 356     5697   3307   2598    -88   1338   -310       N  
ATOM   2885  CA  ASN A 356      33.116  68.560  30.305  1.00 32.10           C  
ANISOU 2885  CA  ASN A 356     5665   3468   3063   -307   1004    -95       C  
ATOM   2886  C   ASN A 356      33.710  69.961  30.381  1.00 32.11           C  
ANISOU 2886  C   ASN A 356     5819   3297   3084   -140   1439   -266       C  
ATOM   2887  O   ASN A 356      33.106  70.924  29.899  1.00 35.83           O  
ANISOU 2887  O   ASN A 356     8098   3490   2027   -183    174   -120       O  
ATOM   2888  CB  ASN A 356      31.616  68.620  30.640  1.00 32.98           C  
ANISOU 2888  CB  ASN A 356     5577   3998   2956   -305    801   -323       C  
ATOM   2889  CG  ASN A 356      30.990  67.303  30.191  1.00 35.75           C  
ANISOU 2889  CG  ASN A 356     5885   4517   3180   -760    841   -594       C  
ATOM   2890  OD1 ASN A 356      29.937  66.925  30.697  1.00 37.70           O  
ANISOU 2890  OD1 ASN A 356     5278   5595   3450   -938     42     23       O  
ATOM   2891  ND2 ASN A 356      31.673  66.657  29.266  1.00 37.38           N  
ANISOU 2891  ND2 ASN A 356     6332   4725   3144    -24    231   -919       N  
ATOM   2892  N   GLY A 357      34.905  70.072  30.961  1.00 31.14           N  
ANISOU 2892  N   GLY A 357     5645   3233   2955   -346   1722   -525       N  
ATOM   2893  CA  GLY A 357      35.631  71.329  30.951  1.00 32.37           C  
ANISOU 2893  CA  GLY A 357     6102   3382   2816   -614   2197   -439       C  
ATOM   2894  C   GLY A 357      34.857  72.459  31.606  1.00 28.86           C  
ANISOU 2894  C   GLY A 357     5571   2988   2406   -535   1719      6       C  
ATOM   2895  O   GLY A 357      34.928  73.581  31.097  1.00 31.04           O  
ANISOU 2895  O   GLY A 357     6187   3046   2561  -1013   1289     88       O  
ATOM   2896  N   LEU A 358      34.140  72.187  32.705  1.00 25.68           N  
ANISOU 2896  N   LEU A 358     4281   3133   2342   -371   1283     53       N  
ATOM   2897  CA  LEU A 358      33.552  73.252  33.513  1.00 23.31           C  
ANISOU 2897  CA  LEU A 358     3753   2957   2146   -312    895    164       C  
ATOM   2898  C   LEU A 358      34.594  73.924  34.387  1.00 22.75           C  
ANISOU 2898  C   LEU A 358     3750   2851   2041   -144    637    472       C  
ATOM   2899  O   LEU A 358      35.743  73.474  34.498  1.00 26.50           O  
ANISOU 2899  O   LEU A 358     3855   3619   2595    204    582   -161       O  
ATOM   2900  CB  LEU A 358      32.411  72.704  34.382  1.00 24.28           C  
ANISOU 2900  CB  LEU A 358     4185   3027   2014   -592   1095   -103       C  
ATOM   2901  CG  LEU A 358      31.311  71.982  33.585  1.00 27.05           C  
ANISOU 2901  CG  LEU A 358     4474   3602   2202  -1122    787    433       C  
ATOM   2902  CD1 LEU A 358      30.138  71.597  34.473  1.00 29.92           C  
ANISOU 2902  CD1 LEU A 358     4829   4288   2251  -1558   1042    -26       C  
ATOM   2903  CD2 LEU A 358      30.831  72.830  32.414  1.00 30.97           C  
ANISOU 2903  CD2 LEU A 358     5867   3881   2020   -904    437    280       C  
ATOM   2904  N   LYS A 359      34.264  75.046  35.034  1.00 21.52           N  
ANISOU 2904  N   LYS A 359     3627   2710   1841    -28    184    596       N  
ATOM   2905  CA  LYS A 359      35.334  75.788  35.707  1.00 24.74           C  
ANISOU 2905  CA  LYS A 359     4304   2794   2301   -437   -291    887       C  
ATOM   2906  C   LYS A 359      35.629  75.315  37.112  1.00 20.94           C  
ANISOU 2906  C   LYS A 359     3489   2337   2131   -204     24    625       C  
ATOM   2907  O   LYS A 359      36.649  75.710  37.698  1.00 21.36           O  
ANISOU 2907  O   LYS A 359     3207   2756   2152   -490    194   1174       O  
ATOM   2908  CB  LYS A 359      34.963  77.282  35.754  1.00 27.93           C  
ANISOU 2908  CB  LYS A 359     4950   2760   2904   -403  -1273    978       C  
ATOM   2909  CG  LYS A 359      35.310  78.068  34.497  1.00 34.25           C  
ANISOU 2909  CG  LYS A 359     6267   3192   3554   -912  -1321   1591       C  
ATOM   2910  CD  LYS A 359      35.335  79.548  34.848  1.00 39.37           C  
ANISOU 2910  CD  LYS A 359     7599   3239   4122  -1332   -816   1447       C  
ATOM   2911  CE  LYS A 359      35.613  80.446  33.672  1.00 43.13           C  
ANISOU 2911  CE  LYS A 359     8296   3478   4611  -1401  -1366   2047       C  
ATOM   2912  NZ  LYS A 359      34.392  81.228  33.295  1.00 51.40           N  
ANISOU 2912  NZ  LYS A 359     8577   4831   6124   -994  -1576   2746       N  
ATOM   2913  N   THR A 360      34.778  74.496  37.719  1.00 17.11           N  
ANISOU 2913  N   THR A 360     2451   1954   2095    338    -90    500       N  
ATOM   2914  CA  THR A 360      35.060  73.954  39.050  1.00 15.89           C  
ANISOU 2914  CA  THR A 360     2522   1702   1815    119     39    208       C  
ATOM   2915  C   THR A 360      34.557  72.510  39.121  1.00 13.75           C  
ANISOU 2915  C   THR A 360     1902   1691   1633    219    233     92       C  
ATOM   2916  O   THR A 360      33.703  72.136  38.314  1.00 16.62           O  
ANISOU 2916  O   THR A 360     2844   2258   1215   -260    101     71       O  
ATOM   2917  CB  THR A 360      34.379  74.698  40.214  1.00 17.41           C  
ANISOU 2917  CB  THR A 360     2594   1709   2311   -279    324   -175       C  
ATOM   2918  OG1 THR A 360      32.972  74.343  40.266  1.00 17.36           O  
ANISOU 2918  OG1 THR A 360     2482   2069   2043   -114    182    433       O  
ATOM   2919  CG2 THR A 360      34.440  76.210  40.049  1.00 17.25           C  
ANISOU 2919  CG2 THR A 360     2081   1707   2766    187    -20     52       C  
ATOM   2920  N   THR A 361      35.064  71.752  40.088  1.00 14.77           N  
ANISOU 2920  N   THR A 361     1938   1837   1838     47    187    341       N  
ATOM   2921  CA  THR A 361      34.588  70.379  40.328  1.00 14.80           C  
ANISOU 2921  CA  THR A 361     1764   1809   2050     43   -152    336       C  
ATOM   2922  C   THR A 361      33.131  70.313  40.768  1.00 14.07           C  
ANISOU 2922  C   THR A 361     1821   1697   1828     63   -107    396       C  
ATOM   2923  O   THR A 361      32.533  69.221  40.766  1.00 14.93           O  
ANISOU 2923  O   THR A 361     1795   1642   2236    135    178    112       O  
ATOM   2924  CB  THR A 361      35.466  69.731  41.420  1.00 14.40           C  
ANISOU 2924  CB  THR A 361     1748   1872   1852     79    -35    305       C  
ATOM   2925  OG1 THR A 361      35.459  70.592  42.562  1.00 16.23           O  
ANISOU 2925  OG1 THR A 361     2121   2208   1838    130     81    189       O  
ATOM   2926  CG2 THR A 361      36.901  69.630  40.923  1.00 14.84           C  
ANISOU 2926  CG2 THR A 361     1757   2047   1833    145    -29    323       C  
ATOM   2927  N   GLY A 362      32.500  71.437  41.131  1.00 13.99           N  
ANISOU 2927  N   GLY A 362     1905   1609   1802   -144    132    260       N  
ATOM   2928  CA  GLY A 362      31.128  71.550  41.583  1.00 14.39           C  
ANISOU 2928  CA  GLY A 362     1828   1791   1847    -65    -14    186       C  
ATOM   2929  C   GLY A 362      30.234  72.120  40.490  1.00 15.57           C  
ANISOU 2929  C   GLY A 362     2158   1701   2055     26   -203    210       C  
ATOM   2930  O   GLY A 362      29.490  73.074  40.668  1.00 15.51           O  
ANISOU 2930  O   GLY A 362     1947   2051   1895    133     32    206       O  
ATOM   2931  N   GLU A 363      30.343  71.469  39.326  1.00 13.99           N  
ANISOU 2931  N   GLU A 363     1645   1780   1889    151    -80    376       N  
ATOM   2932  CA  GLU A 363      29.534  71.867  38.162  1.00 14.72           C  
ANISOU 2932  CA  GLU A 363     1617   1935   2039    -97   -205    529       C  
ATOM   2933  C   GLU A 363      29.729  73.334  37.804  1.00 14.99           C  
ANISOU 2933  C   GLU A 363     1933   1959   1804   -178   -326    524       C  
ATOM   2934  O   GLU A 363      28.815  74.010  37.319  1.00 16.48           O  
ANISOU 2934  O   GLU A 363     1929   2005   2330    164     42    574       O  
ATOM   2935  CB  GLU A 363      28.065  71.547  38.473  1.00 15.31           C  
ANISOU 2935  CB  GLU A 363     1585   1912   2321     66    -95    571       C  
ATOM   2936  CG  GLU A 363      27.937  70.060  38.826  1.00 16.08           C  
ANISOU 2936  CG  GLU A 363     1589   1876   2645     46    182    512       C  
ATOM   2937  CD  GLU A 363      26.532  69.597  39.091  1.00 16.96           C  
ANISOU 2937  CD  GLU A 363     1766   2138   2540    -74    583    271       C  
ATOM   2938  OE1 GLU A 363      25.608  70.411  39.352  1.00 18.60           O  
ANISOU 2938  OE1 GLU A 363     1807   2532   2727    133    660    432       O  
ATOM   2939  OE2 GLU A 363      26.300  68.365  39.038  1.00 18.54           O  
ANISOU 2939  OE2 GLU A 363     1937   2288   2820   -394    330   -122       O  
ATOM   2940  N   GLY A 364      30.919  73.879  38.053  1.00 14.62           N  
ANISOU 2940  N   GLY A 364     2101   2022   1432   -366   -150    119       N  
ATOM   2941  CA  GLY A 364      31.221  75.263  37.721  1.00 15.57           C  
ANISOU 2941  CA  GLY A 364     2251   1983   1681   -313    247     58       C  
ATOM   2942  C   GLY A 364      30.762  76.237  38.785  1.00 15.15           C  
ANISOU 2942  C   GLY A 364     1893   2004   1861    -21    376    179       C  
ATOM   2943  O   GLY A 364      30.935  77.460  38.607  1.00 17.95           O  
ANISOU 2943  O   GLY A 364     2635   1943   2242    110    587    178       O  
ATOM   2944  N   LEU A 365      30.197  75.745  39.894  1.00 15.72           N  
ANISOU 2944  N   LEU A 365     1913   2362   1697   -200    224    152       N  
ATOM   2945  CA  LEU A 365      29.733  76.631  40.961  1.00 15.57           C  
ANISOU 2945  CA  LEU A 365     2100   2249   1567   -183    197    249       C  
ATOM   2946  C   LEU A 365      30.748  76.583  42.085  1.00 16.20           C  
ANISOU 2946  C   LEU A 365     2142   2203   1810     -4     53     65       C  
ATOM   2947  O   LEU A 365      31.522  75.620  42.120  1.00 18.01           O  
ANISOU 2947  O   LEU A 365     2256   2434   2153    178    104    137       O  
ATOM   2948  CB  LEU A 365      28.340  76.203  41.434  1.00 14.98           C  
ANISOU 2948  CB  LEU A 365     1954   1938   1799    181    237    421       C  
ATOM   2949  CG  LEU A 365      27.279  76.193  40.319  1.00 16.38           C  
ANISOU 2949  CG  LEU A 365     2087   2019   2117    -30     18    407       C  
ATOM   2950  CD1 LEU A 365      25.961  75.637  40.814  1.00 15.22           C  
ANISOU 2950  CD1 LEU A 365     1985   1771   2028    203    229     80       C  
ATOM   2951  CD2 LEU A 365      27.121  77.609  39.791  1.00 21.93           C  
ANISOU 2951  CD2 LEU A 365     3132   2500   2698   -382   -657   1208       C  
ATOM   2952  N   GLU A 366      30.723  77.586  42.956  1.00 16.43           N  
ANISOU 2952  N   GLU A 366     2459   2151   1633   -308    222    161       N  
ATOM   2953  CA  GLU A 366      31.621  77.708  44.079  1.00 16.33           C  
ANISOU 2953  CA  GLU A 366     2431   2073   1703   -469    185    249       C  
ATOM   2954  C   GLU A 366      31.244  76.888  45.316  1.00 14.84           C  
ANISOU 2954  C   GLU A 366     1872   1939   1827    -90    215    362       C  
ATOM   2955  O   GLU A 366      32.087  76.160  45.837  1.00 14.31           O  
ANISOU 2955  O   GLU A 366     1882   1756   1798    115    354     37       O  
ATOM   2956  CB  GLU A 366      31.670  79.180  44.555  1.00 17.36           C  
ANISOU 2956  CB  GLU A 366     2877   2000   1719   -418    -62    362       C  
ATOM   2957  CG  GLU A 366      32.701  79.350  45.673  1.00 22.65           C  
ANISOU 2957  CG  GLU A 366     3631   2513   2461   -755   -720    169       C  
ATOM   2958  CD  GLU A 366      32.953  80.832  45.902  1.00 25.05           C  
ANISOU 2958  CD  GLU A 366     4199   2488   2831   -899  -1085    380       C  
ATOM   2959  OE1 GLU A 366      32.151  81.627  45.351  1.00 29.34           O  
ANISOU 2959  OE1 GLU A 366     4066   2949   4133    -40   -138    789       O  
ATOM   2960  OE2 GLU A 366      33.900  81.166  46.622  1.00 33.59           O  
ANISOU 2960  OE2 GLU A 366     5264   3539   3962  -2272  -1755    669       O  
ATOM   2961  N   TRP A 367      30.002  77.047  45.783  1.00 14.60           N  
ANISOU 2961  N   TRP A 367     1774   1932   1840      1     47    388       N  
ATOM   2962  CA  TRP A 367      29.548  76.451  47.045  1.00 13.98           C  
ANISOU 2962  CA  TRP A 367     1764   1783   1763    -44    200    140       C  
ATOM   2963  C   TRP A 367      28.569  75.307  46.801  1.00 13.41           C  
ANISOU 2963  C   TRP A 367     1619   1712   1766     72    -98    312       C  
ATOM   2964  O   TRP A 367      27.825  75.376  45.819  1.00 14.10           O  
ANISOU 2964  O   TRP A 367     1936   1757   1666    168   -150    257       O  
ATOM   2965  CB  TRP A 367      28.854  77.475  47.955  1.00 16.39           C  
ANISOU 2965  CB  TRP A 367     2111   2044   2074    166    119   -142       C  
ATOM   2966  CG  TRP A 367      29.789  78.547  48.443  1.00 16.03           C  
ANISOU 2966  CG  TRP A 367     1838   1966   2287    342    178   -239       C  
ATOM   2967  CD1 TRP A 367      29.979  79.784  47.903  1.00 19.26           C  
ANISOU 2967  CD1 TRP A 367     2784   2350   2183   -310    180    -27       C  
ATOM   2968  CD2 TRP A 367      30.660  78.443  49.575  1.00 18.13           C  
ANISOU 2968  CD2 TRP A 367     2539   2443   1905    -13    113   -342       C  
ATOM   2969  NE1 TRP A 367      30.918  80.464  48.632  1.00 23.32           N  
ANISOU 2969  NE1 TRP A 367     3555   2961   2346  -1047     12     80       N  
ATOM   2970  CE2 TRP A 367      31.353  79.658  49.664  1.00 22.25           C  
ANISOU 2970  CE2 TRP A 367     3184   2853   2416   -542   -164   -294       C  
ATOM   2971  CE3 TRP A 367      30.912  77.425  50.503  1.00 20.65           C  
ANISOU 2971  CE3 TRP A 367     2620   2716   2510    121   -427   -100       C  
ATOM   2972  CZ2 TRP A 367      32.298  79.891  50.676  1.00 24.62           C  
ANISOU 2972  CZ2 TRP A 367     2919   3212   3224   -430   -477   -375       C  
ATOM   2973  CZ3 TRP A 367      31.846  77.667  51.502  1.00 23.56           C  
ANISOU 2973  CZ3 TRP A 367     2472   3214   3267    125   -797    -24       C  
ATOM   2974  CH2 TRP A 367      32.532  78.890  51.588  1.00 25.16           C  
ANISOU 2974  CH2 TRP A 367     2710   3575   3275   -254   -643   -251       C  
ATOM   2975  N   GLY A 368      28.565  74.317  47.688  1.00 12.01           N  
ANISOU 2975  N   GLY A 368     1241   1713   1607    181     60    243       N  
ATOM   2976  CA  GLY A 368      27.703  73.170  47.478  1.00 13.88           C  
ANISOU 2976  CA  GLY A 368     1473   1835   1967    -32    500    154       C  
ATOM   2977  C   GLY A 368      27.264  72.614  48.829  1.00 14.31           C  
ANISOU 2977  C   GLY A 368     1754   1920   1763   -190    389      2       C  
ATOM   2978  O   GLY A 368      27.739  73.010  49.892  1.00 13.43           O  
ANISOU 2978  O   GLY A 368     1634   1486   1983    130     55     78       O  
ATOM   2979  N   VAL A 369      26.311  71.689  48.719  1.00 12.64           N  
ANISOU 2979  N   VAL A 369     1806   1512   1483    -21    206    200       N  
ATOM   2980  CA  VAL A 369      25.763  71.074  49.930  1.00 11.76           C  
ANISOU 2980  CA  VAL A 369     1636   1364   1469    273    262    204       C  
ATOM   2981  C   VAL A 369      25.637  69.578  49.673  1.00 10.69           C  
ANISOU 2981  C   VAL A 369     1289   1395   1377    204   -102    229       C  
ATOM   2982  O   VAL A 369      25.326  69.129  48.568  1.00 13.32           O  
ANISOU 2982  O   VAL A 369     2133   1539   1387    -73   -298    318       O  
ATOM   2983  CB  VAL A 369      24.409  71.680  50.336  1.00 11.34           C  
ANISOU 2983  CB  VAL A 369     1448   1451   1410    339    -41    335       C  
ATOM   2984  CG1 VAL A 369      23.372  71.260  49.308  1.00 16.28           C  
ANISOU 2984  CG1 VAL A 369     1795   2186   2206   -351   -324    170       C  
ATOM   2985  CG2 VAL A 369      23.973  71.266  51.743  1.00 13.65           C  
ANISOU 2985  CG2 VAL A 369     1903   1515   1767    301    560    350       C  
ATOM   2986  N   LEU A 370      25.890  68.817  50.723  1.00 10.31           N  
ANISOU 2986  N   LEU A 370     1227   1366   1327    208    -44    212       N  
ATOM   2987  CA  LEU A 370      25.746  67.363  50.693  1.00 10.77           C  
ANISOU 2987  CA  LEU A 370     1353   1353   1384    187    230    168       C  
ATOM   2988  C   LEU A 370      24.818  66.987  51.862  1.00 10.00           C  
ANISOU 2988  C   LEU A 370     1289   1381   1130     63     94    -25       C  
ATOM   2989  O   LEU A 370      25.096  67.438  52.975  1.00 11.97           O  
ANISOU 2989  O   LEU A 370     1637   1740   1171   -113   -114      9       O  
ATOM   2990  CB  LEU A 370      27.092  66.637  50.777  1.00 10.33           C  
ANISOU 2990  CB  LEU A 370     1384   1298   1244    225    154    -98       C  
ATOM   2991  CG  LEU A 370      27.073  65.112  50.811  1.00 11.08           C  
ANISOU 2991  CG  LEU A 370     1495   1300   1416    190    258     18       C  
ATOM   2992  CD1 LEU A 370      28.361  64.514  50.251  1.00 11.59           C  
ANISOU 2992  CD1 LEU A 370     1398   1308   1696    368     81    116       C  
ATOM   2993  CD2 LEU A 370      26.957  64.537  52.230  1.00 14.02           C  
ANISOU 2993  CD2 LEU A 370     1347   2157   1824     29    153    707       C  
ATOM   2994  N   PHE A 371      23.811  66.187  51.572  1.00 10.80           N  
ANISOU 2994  N   PHE A 371     1584   1306   1212    -95    243   -187       N  
ATOM   2995  CA  PHE A 371      22.860  65.749  52.583  1.00 10.38           C  
ANISOU 2995  CA  PHE A 371     1248   1379   1318    123     66    189       C  
ATOM   2996  C   PHE A 371      22.815  64.234  52.702  1.00 10.91           C  
ANISOU 2996  C   PHE A 371     1421   1368   1356    113    -10    160       C  
ATOM   2997  O   PHE A 371      22.737  63.543  51.679  1.00 10.83           O  
ANISOU 2997  O   PHE A 371     1308   1426   1382    165   -138    122       O  
ATOM   2998  CB  PHE A 371      21.427  66.174  52.247  1.00 12.95           C  
ANISOU 2998  CB  PHE A 371     1350   1583   1989    325    -73    -29       C  
ATOM   2999  CG  PHE A 371      21.161  67.659  52.446  1.00 13.14           C  
ANISOU 2999  CG  PHE A 371     1487   1558   1949    343    122     35       C  
ATOM   3000  CD1 PHE A 371      21.183  68.196  53.726  1.00 13.39           C  
ANISOU 3000  CD1 PHE A 371     1658   1486   1942    125    168     51       C  
ATOM   3001  CD2 PHE A 371      20.879  68.470  51.354  1.00 13.62           C  
ANISOU 3001  CD2 PHE A 371     1657   1570   1948    195    146     94       C  
ATOM   3002  CE1 PHE A 371      20.924  69.548  53.939  1.00 12.70           C  
ANISOU 3002  CE1 PHE A 371     1554   1523   1750    301    117    131       C  
ATOM   3003  CE2 PHE A 371      20.628  69.820  51.550  1.00 12.81           C  
ANISOU 3003  CE2 PHE A 371     1495   1630   1744    335     55     59       C  
ATOM   3004  CZ  PHE A 371      20.641  70.348  52.827  1.00 13.02           C  
ANISOU 3004  CZ  PHE A 371     1593   1641   1713    139   -142     97       C  
ATOM   3005  N   GLY A 372      22.857  63.768  53.950  1.00 10.52           N  
ANISOU 3005  N   GLY A 372     1363   1297   1337    295    219    140       N  
ATOM   3006  CA  GLY A 372      22.561  62.364  54.248  1.00 10.60           C  
ANISOU 3006  CA  GLY A 372     1355   1342   1329     91    -26    124       C  
ATOM   3007  C   GLY A 372      21.219  62.292  54.951  1.00 10.26           C  
ANISOU 3007  C   GLY A 372     1322   1364   1212     80    -99    111       C  
ATOM   3008  O   GLY A 372      20.884  63.179  55.763  1.00 11.47           O  
ANISOU 3008  O   GLY A 372     1427   1485   1445    102     15    -20       O  
ATOM   3009  N   PHE A 373      20.431  61.277  54.682  1.00 11.31           N  
ANISOU 3009  N   PHE A 373     1354   1543   1403    -25   -102     23       N  
ATOM   3010  CA  PHE A 373      19.132  61.102  55.326  1.00 11.74           C  
ANISOU 3010  CA  PHE A 373     1325   1564   1571     46    -87    245       C  
ATOM   3011  C   PHE A 373      19.024  59.660  55.810  1.00 10.95           C  
ANISOU 3011  C   PHE A 373     1387   1449   1327    119     15     30       C  
ATOM   3012  O   PHE A 373      19.454  58.784  55.072  1.00 14.91           O  
ANISOU 3012  O   PHE A 373     2242   1670   1753    143    492   -147       O  
ATOM   3013  CB  PHE A 373      17.971  61.350  54.357  1.00 12.45           C  
ANISOU 3013  CB  PHE A 373     1392   1577   1763     53   -236    179       C  
ATOM   3014  CG  PHE A 373      18.069  62.591  53.487  1.00 12.56           C  
ANISOU 3014  CG  PHE A 373     1381   1610   1782     99   -313    217       C  
ATOM   3015  CD1 PHE A 373      18.138  63.847  54.062  1.00 14.18           C  
ANISOU 3015  CD1 PHE A 373     1904   1589   1895    -17     67    217       C  
ATOM   3016  CD2 PHE A 373      18.074  62.514  52.099  1.00 12.73           C  
ANISOU 3016  CD2 PHE A 373     1308   1740   1789    155    -64    243       C  
ATOM   3017  CE1 PHE A 373      18.219  65.023  53.316  1.00 12.70           C  
ANISOU 3017  CE1 PHE A 373     1602   1623   1598     16    -32    171       C  
ATOM   3018  CE2 PHE A 373      18.160  63.672  51.350  1.00 12.41           C  
ANISOU 3018  CE2 PHE A 373     1419   1605   1690    145   -210    108       C  
ATOM   3019  CZ  PHE A 373      18.222  64.928  51.923  1.00 11.83           C  
ANISOU 3019  CZ  PHE A 373     1162   1709   1624    170     -5    -18       C  
ATOM   3020  N   GLY A 374      18.471  59.415  56.994  1.00 11.66           N  
ANISOU 3020  N   GLY A 374     1343   1486   1602    -51    280     37       N  
ATOM   3021  CA  GLY A 374      18.345  58.030  57.467  1.00 12.64           C  
ANISOU 3021  CA  GLY A 374     1592   1467   1745     29    453     46       C  
ATOM   3022  C   GLY A 374      17.644  57.959  58.817  1.00 11.83           C  
ANISOU 3022  C   GLY A 374     1424   1440   1633    196    285    147       C  
ATOM   3023  O   GLY A 374      16.987  58.935  59.212  1.00 11.63           O  
ANISOU 3023  O   GLY A 374     1372   1510   1538    205    122     12       O  
ATOM   3024  N   PRO A 375      17.785  56.845  59.519  1.00 13.08           N  
ANISOU 3024  N   PRO A 375     1804   1499   1666    182    117    201       N  
ATOM   3025  CA  PRO A 375      17.091  56.596  60.783  1.00 13.06           C  
ANISOU 3025  CA  PRO A 375     1931   1426   1606    134     69    212       C  
ATOM   3026  C   PRO A 375      17.189  57.745  61.774  1.00 12.65           C  
ANISOU 3026  C   PRO A 375     1681   1505   1618    104    -10    178       C  
ATOM   3027  O   PRO A 375      18.265  58.290  62.003  1.00 13.97           O  
ANISOU 3027  O   PRO A 375     1747   1956   1606    -14   -159    212       O  
ATOM   3028  CB  PRO A 375      17.830  55.349  61.330  1.00 13.08           C  
ANISOU 3028  CB  PRO A 375     1902   1514   1553    175   -137    142       C  
ATOM   3029  CG  PRO A 375      18.266  54.613  60.090  1.00 13.12           C  
ANISOU 3029  CG  PRO A 375     1817   1578   1592    236     63    259       C  
ATOM   3030  CD  PRO A 375      18.634  55.700  59.111  1.00 12.95           C  
ANISOU 3030  CD  PRO A 375     1642   1538   1742    274      1    331       C  
ATOM   3031  N   GLY A 376      16.046  58.134  62.364  1.00 13.84           N  
ANISOU 3031  N   GLY A 376     1852   1683   1723     37    220     49       N  
ATOM   3032  CA  GLY A 376      16.053  59.223  63.326  1.00 12.26           C  
ANISOU 3032  CA  GLY A 376     1430   1887   1343    106   -185     92       C  
ATOM   3033  C   GLY A 376      14.706  59.921  63.422  1.00 12.20           C  
ANISOU 3033  C   GLY A 376     1497   1749   1391    111    -40    167       C  
ATOM   3034  O   GLY A 376      14.101  59.858  64.506  1.00 12.66           O  
ANISOU 3034  O   GLY A 376     2015   1378   1417    374    141    114       O  
ATOM   3035  N   LEU A 377      14.185  60.552  62.377  1.00 12.00           N  
ANISOU 3035  N   LEU A 377     1276   1871   1410     40    -51    213       N  
ATOM   3036  CA  LEU A 377      14.842  60.718  61.088  1.00 10.89           C  
ANISOU 3036  CA  LEU A 377     1102   1625   1412     23    -87    174       C  
ATOM   3037  C   LEU A 377      15.972  61.741  61.217  1.00 10.72           C  
ANISOU 3037  C   LEU A 377     1107   1367   1600    174     92   -137       C  
ATOM   3038  O   LEU A 377      15.717  62.839  61.711  1.00 13.42           O  
ANISOU 3038  O   LEU A 377     1273   1493   2334    320    148   -346       O  
ATOM   3039  CB  LEU A 377      13.825  61.175  60.045  1.00 10.78           C  
ANISOU 3039  CB  LEU A 377     1199   1506   1391    237    -32    135       C  
ATOM   3040  CG  LEU A 377      14.272  61.371  58.598  1.00 13.34           C  
ANISOU 3040  CG  LEU A 377     1956   1788   1324      3    -35    138       C  
ATOM   3041  CD1 LEU A 377      13.114  61.111  57.620  1.00 14.15           C  
ANISOU 3041  CD1 LEU A 377     1848   2224   1305     -3     18    182       C  
ATOM   3042  CD2 LEU A 377      14.838  62.763  58.320  1.00 17.42           C  
ANISOU 3042  CD2 LEU A 377     2112   2325   2183   -425   -218    849       C  
ATOM   3043  N   THR A 378      17.166  61.342  60.787  1.00 10.94           N  
ANISOU 3043  N   THR A 378     1156   1400   1599    106    287   -120       N  
ATOM   3044  CA  THR A 378      18.353  62.171  60.848  1.00 10.91           C  
ANISOU 3044  CA  THR A 378     1206   1511   1428     26    178     64       C  
ATOM   3045  C   THR A 378      18.677  62.803  59.494  1.00 11.79           C  
ANISOU 3045  C   THR A 378     1511   1550   1420    -52     81     92       C  
ATOM   3046  O   THR A 378      18.610  62.165  58.445  1.00 12.03           O  
ANISOU 3046  O   THR A 378     1391   1786   1393   -200     86     49       O  
ATOM   3047  CB  THR A 378      19.565  61.305  61.252  1.00 11.67           C  
ANISOU 3047  CB  THR A 378     1312   1672   1450     50   -107    -32       C  
ATOM   3048  OG1 THR A 378      19.350  60.811  62.581  1.00 11.80           O  
ANISOU 3048  OG1 THR A 378     1304   1718   1460    -66   -146      0       O  
ATOM   3049  CG2 THR A 378      20.888  62.045  61.249  1.00 12.16           C  
ANISOU 3049  CG2 THR A 378     1276   1824   1520     38    -32     28       C  
ATOM   3050  N   ILE A 379      19.074  64.071  59.542  1.00 10.89           N  
ANISOU 3050  N   ILE A 379     1113   1410   1615    219    350     92       N  
ATOM   3051  CA  ILE A 379      19.596  64.800  58.401  1.00 10.62           C  
ANISOU 3051  CA  ILE A 379      995   1539   1500    189    181    141       C  
ATOM   3052  C   ILE A 379      21.019  65.233  58.725  1.00 10.46           C  
ANISOU 3052  C   ILE A 379     1078   1427   1469    104    248   -120       C  
ATOM   3053  O   ILE A 379      21.218  65.926  59.711  1.00 11.60           O  
ANISOU 3053  O   ILE A 379     1417   1361   1629    133    195   -209       O  
ATOM   3054  CB  ILE A 379      18.734  66.016  58.032  1.00 12.33           C  
ANISOU 3054  CB  ILE A 379     1298   1526   1859    203     15    216       C  
ATOM   3055  CG1 ILE A 379      17.275  65.628  57.732  1.00 13.02           C  
ANISOU 3055  CG1 ILE A 379     1181   1906   1860    387    -31    221       C  
ATOM   3056  CG2 ILE A 379      19.329  66.761  56.839  1.00 14.57           C  
ANISOU 3056  CG2 ILE A 379     1947   1496   2091   -208    -79    394       C  
ATOM   3057  CD1 ILE A 379      16.377  66.846  57.595  1.00 13.21           C  
ANISOU 3057  CD1 ILE A 379     1497   1501   2022    228   -514     12       C  
ATOM   3058  N   GLU A 380      21.986  64.798  57.923  1.00 10.46           N  
ANISOU 3058  N   GLU A 380     1028   1442   1502    103    287    -27       N  
ATOM   3059  CA  GLU A 380      23.363  65.286  57.973  1.00  9.63           C  
ANISOU 3059  CA  GLU A 380     1010   1299   1351    160     96    222       C  
ATOM   3060  C   GLU A 380      23.517  66.361  56.900  1.00 10.90           C  
ANISOU 3060  C   GLU A 380     1491   1243   1407    -42    -58    221       C  
ATOM   3061  O   GLU A 380      23.073  66.123  55.756  1.00 12.61           O  
ANISOU 3061  O   GLU A 380     2086   1337   1368   -227   -119    257       O  
ATOM   3062  CB  GLU A 380      24.359  64.151  57.690  1.00 10.12           C  
ANISOU 3062  CB  GLU A 380     1004   1305   1535    150     33     94       C  
ATOM   3063  CG  GLU A 380      24.292  63.060  58.782  1.00 12.43           C  
ANISOU 3063  CG  GLU A 380     1670   1316   1738    194   -294    230       C  
ATOM   3064  CD  GLU A 380      25.307  63.322  59.882  1.00 13.02           C  
ANISOU 3064  CD  GLU A 380     1635   1648   1663    284   -222    143       C  
ATOM   3065  OE1 GLU A 380      25.991  64.359  59.897  1.00 13.79           O  
ANISOU 3065  OE1 GLU A 380     1793   2060   1385    -84   -288    240       O  
ATOM   3066  OE2 GLU A 380      25.423  62.445  60.769  1.00 12.62           O  
ANISOU 3066  OE2 GLU A 380     1478   1894   1421    261     10    179       O  
ATOM   3067  N   THR A 381      24.114  67.485  57.264  1.00 11.78           N  
ANISOU 3067  N   THR A 381     1575   1413   1488   -223     92    129       N  
ATOM   3068  CA  THR A 381      24.471  68.538  56.327  1.00 11.01           C  
ANISOU 3068  CA  THR A 381     1421   1213   1547      1    159    109       C  
ATOM   3069  C   THR A 381      25.976  68.747  56.276  1.00 11.15           C  
ANISOU 3069  C   THR A 381     1403   1532   1300     42    226    172       C  
ATOM   3070  O   THR A 381      26.619  68.871  57.341  1.00 12.00           O  
ANISOU 3070  O   THR A 381     1440   1813   1307    -70    207    158       O  
ATOM   3071  CB  THR A 381      23.851  69.891  56.780  1.00 12.97           C  
ANISOU 3071  CB  THR A 381     1692   1425   1809    189    409     12       C  
ATOM   3072  OG1 THR A 381      22.439  69.755  56.996  1.00 13.87           O  
ANISOU 3072  OG1 THR A 381     1653   1478   2139    188    292     -9       O  
ATOM   3073  CG2 THR A 381      24.024  70.932  55.688  1.00 14.67           C  
ANISOU 3073  CG2 THR A 381     1835   1331   2409    308    349    301       C  
ATOM   3074  N   VAL A 382      26.564  68.809  55.082  1.00 11.83           N  
ANISOU 3074  N   VAL A 382     1598   1586   1312     30    288    -76       N  
ATOM   3075  CA  VAL A 382      27.977  69.142  54.906  1.00 11.65           C  
ANISOU 3075  CA  VAL A 382     1588   1435   1403    141    432    108       C  
ATOM   3076  C   VAL A 382      28.033  70.266  53.864  1.00 11.98           C  
ANISOU 3076  C   VAL A 382     1509   1437   1605     82     40    211       C  
ATOM   3077  O   VAL A 382      27.534  70.047  52.746  1.00 13.92           O  
ANISOU 3077  O   VAL A 382     1803   1881   1607   -299    -17    335       O  
ATOM   3078  CB  VAL A 382      28.825  67.958  54.421  1.00 12.20           C  
ANISOU 3078  CB  VAL A 382     1610   1424   1601    243     87     16       C  
ATOM   3079  CG1 VAL A 382      30.264  68.391  54.220  1.00 12.03           C  
ANISOU 3079  CG1 VAL A 382     1502   1511   1559    348     34   -182       C  
ATOM   3080  CG2 VAL A 382      28.711  66.801  55.421  1.00 13.80           C  
ANISOU 3080  CG2 VAL A 382     2311   1274   1657     -3   -174    -43       C  
ATOM   3081  N   VAL A 383      28.586  71.398  54.267  1.00 11.10           N  
ANISOU 3081  N   VAL A 383     1091   1323   1804    292    160    111       N  
ATOM   3082  CA  VAL A 383      28.802  72.509  53.332  1.00 12.11           C  
ANISOU 3082  CA  VAL A 383     1486   1352   1762    176    284     65       C  
ATOM   3083  C   VAL A 383      30.154  72.342  52.657  1.00 12.66           C  
ANISOU 3083  C   VAL A 383     1486   1635   1688    105    290     13       C  
ATOM   3084  O   VAL A 383      31.173  72.149  53.358  1.00 13.43           O  
ANISOU 3084  O   VAL A 383     1440   1746   1916     -1    220     31       O  
ATOM   3085  CB  VAL A 383      28.690  73.884  54.012  1.00 12.82           C  
ANISOU 3085  CB  VAL A 383     1523   1312   2036    115    304     41       C  
ATOM   3086  CG1 VAL A 383      29.132  74.975  53.048  1.00 13.97           C  
ANISOU 3086  CG1 VAL A 383     2167   1380   1763    150   -121    216       C  
ATOM   3087  CG2 VAL A 383      27.259  74.134  54.487  1.00 13.56           C  
ANISOU 3087  CG2 VAL A 383     1390   1552   2209    561    -81    -18       C  
ATOM   3088  N   LEU A 384      30.141  72.384  51.305  1.00 13.69           N  
ANISOU 3088  N   LEU A 384     1815   1695   1694    129    327    -49       N  
ATOM   3089  CA  LEU A 384      31.334  72.132  50.520  1.00 12.63           C  
ANISOU 3089  CA  LEU A 384     1825   1410   1565    160    277      0       C  
ATOM   3090  C   LEU A 384      31.729  73.361  49.707  1.00 12.80           C  
ANISOU 3090  C   LEU A 384     1711   1303   1849    149    277    -18       C  
ATOM   3091  O   LEU A 384      30.852  74.134  49.340  1.00 14.15           O  
ANISOU 3091  O   LEU A 384     1899   1474   2002    292    303    149       O  
ATOM   3092  CB  LEU A 384      31.134  70.957  49.549  1.00 12.26           C  
ANISOU 3092  CB  LEU A 384     1620   1220   1818    325     58     20       C  
ATOM   3093  CG  LEU A 384      30.783  69.603  50.171  1.00 13.79           C  
ANISOU 3093  CG  LEU A 384     2129   1350   1761    173   -649    291       C  
ATOM   3094  CD1 LEU A 384      30.216  68.676  49.093  1.00 14.80           C  
ANISOU 3094  CD1 LEU A 384     2339   1627   1656   -399   -453    378       C  
ATOM   3095  CD2 LEU A 384      31.996  68.984  50.849  1.00 14.99           C  
ANISOU 3095  CD2 LEU A 384     2040   1828   1827    378   -513    266       C  
ATOM   3096  N   ARG A 385      33.023  73.500  49.414  1.00 14.40           N  
ANISOU 3096  N   ARG A 385     1754   1728   1988     80    355     89       N  
ATOM   3097  CA  ARG A 385      33.447  74.460  48.387  1.00 14.05           C  
ANISOU 3097  CA  ARG A 385     1569   1884   1884    -14     86    174       C  
ATOM   3098  C   ARG A 385      34.118  73.646  47.282  1.00 14.84           C  
ANISOU 3098  C   ARG A 385     1760   2041   1839     40    199    244       C  
ATOM   3099  O   ARG A 385      34.852  72.701  47.584  1.00 15.75           O  
ANISOU 3099  O   ARG A 385     2337   1914   1733    213    397    280       O  
ATOM   3100  CB  ARG A 385      34.367  75.529  48.976  1.00 14.25           C  
ANISOU 3100  CB  ARG A 385     1586   1877   1952      0   -211    360       C  
ATOM   3101  CG  ARG A 385      34.638  76.680  48.016  1.00 18.86           C  
ANISOU 3101  CG  ARG A 385     3021   1875   2270   -394   -346    452       C  
ATOM   3102  CD  ARG A 385      35.331  77.833  48.740  1.00 19.81           C  
ANISOU 3102  CD  ARG A 385     2799   1709   3020   -112   -362    147       C  
ATOM   3103  NE  ARG A 385      36.685  77.505  49.152  1.00 22.66           N  
ANISOU 3103  NE  ARG A 385     2627   2464   3519   -124   -312   -256       N  
ATOM   3104  CZ  ARG A 385      37.609  78.410  49.517  1.00 22.14           C  
ANISOU 3104  CZ  ARG A 385     2755   1907   3751    119   -520   -189       C  
ATOM   3105  NH1 ARG A 385      37.269  79.716  49.509  1.00 23.83           N  
ANISOU 3105  NH1 ARG A 385     3359   1922   3773    255    570    423       N  
ATOM   3106  NH2 ARG A 385      38.838  78.028  49.880  1.00 20.32           N  
ANISOU 3106  NH2 ARG A 385     2144   2344   3234     79    363   -511       N  
ATOM   3107  N   SER A 386      33.887  73.959  46.019  1.00 14.54           N  
ANISOU 3107  N   SER A 386     1708   1974   1843   -126      9    146       N  
ATOM   3108  CA  SER A 386      34.520  73.284  44.896  1.00 14.81           C  
ANISOU 3108  CA  SER A 386     1901   1936   1788    -70    -12    164       C  
ATOM   3109  C   SER A 386      35.956  73.763  44.738  1.00 16.13           C  
ANISOU 3109  C   SER A 386     1970   1995   2164    -79    305     56       C  
ATOM   3110  O   SER A 386      36.416  74.651  45.475  1.00 15.56           O  
ANISOU 3110  O   SER A 386     1670   2088   2156   -127    388     36       O  
ATOM   3111  CB  SER A 386      33.784  73.603  43.578  1.00 16.61           C  
ANISOU 3111  CB  SER A 386     2622   1859   1829   -144   -225    267       C  
ATOM   3112  OG  SER A 386      33.849  75.015  43.381  1.00 13.88           O  
ANISOU 3112  OG  SER A 386     1659   1810   1804      9    276    151       O  
ATOM   3113  N   VAL A 387      36.614  73.165  43.756  1.00 15.70           N  
ANISOU 3113  N   VAL A 387     2192   1997   1777      1    265    291       N  
ATOM   3114  CA  VAL A 387      37.990  73.573  43.432  1.00 16.47           C  
ANISOU 3114  CA  VAL A 387     2208   2194   1857     86    397    521       C  
ATOM   3115  C   VAL A 387      38.064  73.961  41.967  1.00 15.92           C  
ANISOU 3115  C   VAL A 387     2135   2010   1902   -105     80    615       C  
ATOM   3116  O   VAL A 387      37.413  73.375  41.098  1.00 16.10           O  
ANISOU 3116  O   VAL A 387     1985   2175   1958    -39    300    287       O  
ATOM   3117  CB  VAL A 387      38.998  72.465  43.797  1.00 18.52           C  
ANISOU 3117  CB  VAL A 387     2267   2767   2005    244    239    945       C  
ATOM   3118  CG1 VAL A 387      40.430  72.770  43.376  1.00 23.98           C  
ANISOU 3118  CG1 VAL A 387     2333   3662   3118    508    675   1310       C  
ATOM   3119  CG2 VAL A 387      38.983  72.247  45.304  1.00 16.84           C  
ANISOU 3119  CG2 VAL A 387     1853   2761   1783    163   -116    169       C  
ATOM   3120  N   ALA A 388      38.840  74.997  41.663  1.00 17.83           N  
ANISOU 3120  N   ALA A 388     2395   2217   2163   -333    -35    819       N  
ATOM   3121  CA  ALA A 388      38.914  75.443  40.270  1.00 19.39           C  
ANISOU 3121  CA  ALA A 388     2428   2575   2365   -118    -35   1207       C  
ATOM   3122  C   ALA A 388      39.661  74.393  39.435  1.00 23.63           C  
ANISOU 3122  C   ALA A 388     3058   3396   2523   -316    582    688       C  
ATOM   3123  O   ALA A 388      40.679  73.876  39.905  1.00 20.81           O  
ANISOU 3123  O   ALA A 388     2628   3019   2260   -285    881    -45       O  
ATOM   3124  CB  ALA A 388      39.594  76.785  40.161  1.00 23.63           C  
ANISOU 3124  CB  ALA A 388     3287   3177   2514   -890    771   1007       C  
ATOM   3125  N   ILE A 389      39.072  74.185  38.305  1.00 26.46           N  
ANISOU 3125  N   ILE A 389     3611   3976   2469   -264    423    715       N  
ATOM   3126  CA  ILE A 389      39.074  73.379  37.115  1.00 34.50           C  
ANISOU 3126  CA  ILE A 389     5473   4958   2678   -635    452    207       C  
ATOM   3127  C   ILE A 389      38.568  71.966  37.333  1.00 35.60           C  
ANISOU 3127  C   ILE A 389     5103   4401   4022    -50    207   -223       C  
ATOM   3128  O   ILE A 389      39.381  71.119  37.784  1.00 49.19           O  
ANISOU 3128  O   ILE A 389     6565   5366   6760    377   -884    823       O  
ATOM   3129  CB  ILE A 389      40.489  73.459  36.505  1.00 35.98           C  
ANISOU 3129  CB  ILE A 389     5879   4956   2835   -249   1057   -443       C  
ATOM   3130  CG1 ILE A 389      40.562  74.692  35.590  1.00 36.82           C  
ANISOU 3130  CG1 ILE A 389     5711   5567   2710   -803    969   -122       C  
ATOM   3131  CG2 ILE A 389      40.940  72.242  35.747  1.00 46.56           C  
ANISOU 3131  CG2 ILE A 389     9005   5197   3489  -1045   2837  -1024       C  
ATOM   3132  CD1 ILE A 389      39.302  75.517  35.636  1.00 33.51           C  
ANISOU 3132  CD1 ILE A 389     4330   6455   1948  -1412    -13   1464       C  
ATOM   3133  OXT ILE A 389      37.367  71.641  37.097  1.00 37.20           O  
ANISOU 3133  OXT ILE A 389     4678   4861   4596   -185   1488   -673       O  
TER    3134      ILE A 389                                                      
HETATM 3135  O   HOH A 390      30.249  52.393  65.520  0.38  8.47           O  
ANISOU 3135  O   HOH A 390      850   1385    984    464    -78     45       O  
HETATM 3136  O   HOH A 391      45.499  50.807  65.281  0.99 12.69           O  
ANISOU 3136  O   HOH A 391     1562   1623   1635     67    -75     56       O  
HETATM 3137  O   HOH A 392      24.749  58.146  51.046  1.00 11.57           O  
ANISOU 3137  O   HOH A 392     1607   1468   1320    -41    144   -192       O  
HETATM 3138  O   HOH A 393      30.602  43.518  57.995  0.97 13.84           O  
ANISOU 3138  O   HOH A 393     1464   1739   2055    176      2   -118       O  
HETATM 3139  O   HOH A 394      37.833  47.100  65.590  0.94 14.54           O  
ANISOU 3139  O   HOH A 394     1851   1881   1790    -96    -23   -102       O  
HETATM 3140  O   HOH A 395      24.053  41.526  48.141  1.00 15.20           O  
ANISOU 3140  O   HOH A 395     1966   1729   2079    190     91   -238       O  
HETATM 3141  O   HOH A 396      13.674  56.762  62.491  1.00 13.75           O  
ANISOU 3141  O   HOH A 396     1498   1898   1827   -106    223     81       O  
HETATM 3142  O   HOH A 397      49.056  53.792  57.210  0.99 13.39           O  
ANISOU 3142  O   HOH A 397     1383   1836   1867     77     21    -13       O  
HETATM 3143  O   HOH A 398      22.075  72.232  58.323  1.00 13.30           O  
ANISOU 3143  O   HOH A 398     1607   1570   1875     90    293     55       O  
HETATM 3144  O   HOH A 399      36.183  41.498  61.265  1.00 15.40           O  
ANISOU 3144  O   HOH A 399     1896   2017   1937     35   -100    228       O  
HETATM 3145  O   HOH A 400      40.016  61.542  67.145  1.00 12.44           O  
ANISOU 3145  O   HOH A 400     1755   1560   1413     42    194   -210       O  
HETATM 3146  O   HOH A 401      23.823  67.482  39.239  0.98 15.70           O  
ANISOU 3146  O   HOH A 401     1625   2067   2276    152    252   -189       O  
HETATM 3147  O   HOH A 402      14.950  35.738  56.451  1.00 15.12           O  
ANISOU 3147  O   HOH A 402     1745   1869   2130     41    -47    -70       O  
HETATM 3148  O   HOH A 403      27.484  66.335  58.715  1.00 14.19           O  
ANISOU 3148  O   HOH A 403     1496   1710   2186    201    -80    107       O  
HETATM 3149  O   HOH A 404      32.455  56.388  40.824  0.89 16.34           O  
ANISOU 3149  O   HOH A 404     1983   1916   2308    213   -102   -120       O  
HETATM 3150  O   HOH A 405      40.349  46.238  66.612  1.00 14.18           O  
ANISOU 3150  O   HOH A 405     1670   2036   1684   -380    -92    242       O  
HETATM 3151  O   HOH A 406       8.286  56.863  53.517  1.00 21.07           O  
ANISOU 3151  O   HOH A 406     2589   2543   2874      0   -275   -204       O  
HETATM 3152  O   HOH A 407      24.735  31.395  66.709  1.00 12.87           O  
ANISOU 3152  O   HOH A 407     1604   1596   1688     72   -307    105       O  
HETATM 3153  O   HOH A 408      21.826  68.698  59.368  0.98 13.08           O  
ANISOU 3153  O   HOH A 408     1524   1682   1764    179    117     48       O  
HETATM 3154  O   HOH A 409      48.490  56.155  66.681  1.00 16.36           O  
ANISOU 3154  O   HOH A 409     2029   2419   1767   -458    246    115       O  
HETATM 3155  O   HOH A 410      32.469  43.605  60.000  0.99 15.49           O  
ANISOU 3155  O   HOH A 410     1530   2090   2264     39    178   -176       O  
HETATM 3156  O   HOH A 411      36.874  73.759  57.257  1.00 15.21           O  
ANISOU 3156  O   HOH A 411     1778   1868   2133    -51     78    186       O  
HETATM 3157  O   HOH A 412      24.765  59.452  53.605  1.00 12.76           O  
ANISOU 3157  O   HOH A 412     1440   1823   1586     55   -305    135       O  
HETATM 3158  O   HOH A 413      23.872  70.472  41.560  0.99 12.53           O  
ANISOU 3158  O   HOH A 413     1648   1443   1668    197   -183    252       O  
HETATM 3159  O   HOH A 414      27.943  66.733  37.479  1.00 16.04           O  
ANISOU 3159  O   HOH A 414     2178   2005   1911    184   -191     48       O  
HETATM 3160  O   HOH A 415      34.798  42.533  58.977  1.00 13.27           O  
ANISOU 3160  O   HOH A 415     1759   1682   1602    108    186     65       O  
HETATM 3161  O   HOH A 416      50.688  61.976  56.983  1.00 17.79           O  
ANISOU 3161  O   HOH A 416     1906   2327   2525     31    195     60       O  
HETATM 3162  O   HOH A 417      26.563  47.204  60.718  0.96 12.87           O  
ANISOU 3162  O   HOH A 417     1736   1619   1534    -26    243   -167       O  
HETATM 3163  O   HOH A 418      32.293  51.707  40.915  0.94 18.90           O  
ANISOU 3163  O   HOH A 418     2480   2574   2126    -91    670   -138       O  
HETATM 3164  O   HOH A 419      16.342  79.269  46.153  0.92 16.93           O  
ANISOU 3164  O   HOH A 419     1933   2296   2203    174     60    -46       O  
HETATM 3165  O   HOH A 420      44.335  64.785  68.573  1.00 15.08           O  
ANISOU 3165  O   HOH A 420     1938   1823   1968    173     73    248       O  
HETATM 3166  O   HOH A 421      23.103  66.042  42.253  1.00 16.55           O  
ANISOU 3166  O   HOH A 421     2130   1958   2202    -30   -560    334       O  
HETATM 3167  O   HOH A 422      22.556  49.750  50.337  0.94 15.56           O  
ANISOU 3167  O   HOH A 422     2128   2087   1698    170      8     -3       O  
HETATM 3168  O   HOH A 423      36.437  52.722  66.677  1.00 18.99           O  
ANISOU 3168  O   HOH A 423     2849   2250   2116     77   -375   -176       O  
HETATM 3169  O   HOH A 424      24.718  48.841  43.266  0.99 13.72           O  
ANISOU 3169  O   HOH A 424     2196   1786   1230    -85   -223    -94       O  
HETATM 3170  O   HOH A 425      43.591  72.825  54.077  0.99 16.28           O  
ANISOU 3170  O   HOH A 425     2050   1924   2213    -25   -145    520       O  
HETATM 3171  O   HOH A 426      38.288  50.562  66.398  1.00 19.72           O  
ANISOU 3171  O   HOH A 426     3085   2429   1978    695    166    131       O  
HETATM 3172  O   HOH A 427      46.810  41.492  64.783  0.98 15.60           O  
ANISOU 3172  O   HOH A 427     2158   2005   1765    108    132   -260       O  
HETATM 3173  O   HOH A 428      18.297  46.522  40.060  1.00 14.16           O  
ANISOU 3173  O   HOH A 428     2057   1712   1611    -36     84   -188       O  
HETATM 3174  O   HOH A 429      30.613  38.972  64.235  0.99 14.46           O  
ANISOU 3174  O   HOH A 429     1843   1706   1945    187    215   -109       O  
HETATM 3175  O   HOH A 430      23.916  44.926  59.902  0.95 14.97           O  
ANISOU 3175  O   HOH A 430     1742   1780   2167    315    224    -50       O  
HETATM 3176  O   HOH A 431      51.792  63.926  51.491  1.00 41.46           O  
ANISOU 3176  O   HOH A 431     5333   5575   4845   -321   -711    277       O  
HETATM 3177  O   HOH A 432      22.435  53.027  64.753  1.00 14.11           O  
ANISOU 3177  O   HOH A 432     1656   1848   1855    -79    -19    149       O  
HETATM 3178  O   HOH A 433      42.345  73.286  60.613  1.00 18.00           O  
ANISOU 3178  O   HOH A 433     2139   2286   2415      9   -155    161       O  
HETATM 3179  O   HOH A 434      13.585  78.047  40.540  1.00 16.46           O  
ANISOU 3179  O   HOH A 434     1653   2297   2304     31    -59    451       O  
HETATM 3180  O   HOH A 435      24.506  72.962  38.984  1.00 19.08           O  
ANISOU 3180  O   HOH A 435     2370   2303   2576     97    -34    168       O  
HETATM 3181  O   HOH A 436      45.483  67.251  57.958  0.97 14.06           O  
ANISOU 3181  O   HOH A 436     1578   1800   1964     78    -54     84       O  
HETATM 3182  O   HOH A 437      14.462  34.516  63.488  1.00 14.35           O  
ANISOU 3182  O   HOH A 437     1535   2018   1898     -7    281    -99       O  
HETATM 3183  O   HOH A 438      15.181  43.589  55.582  1.00 16.55           O  
ANISOU 3183  O   HOH A 438     2126   1828   2334     62    116    -48       O  
HETATM 3184  O   HOH A 439      22.580  46.877  55.852  0.99 18.38           O  
ANISOU 3184  O   HOH A 439     2165   2528   2290   -134     88    197       O  
HETATM 3185  O   HOH A 440      48.413  57.300  63.167  0.99 16.69           O  
ANISOU 3185  O   HOH A 440     1905   2208   2230     36    141    -60       O  
HETATM 3186  O   HOH A 441      29.098  68.382  35.849  1.00 18.72           O  
ANISOU 3186  O   HOH A 441     2306   2304   2501    224    406   -467       O  
HETATM 3187  O   HOH A 442      26.249  64.191  36.545  0.90 27.79           O  
ANISOU 3187  O   HOH A 442     3167   4049   3343    431   1162    -85       O  
HETATM 3188  O   HOH A 443      22.228  31.344  59.684  0.97 14.43           O  
ANISOU 3188  O   HOH A 443     2033   1807   1642     42    -89    241       O  
HETATM 3189  O   HOH A 444      36.225  65.053  27.709  0.95 24.19           O  
ANISOU 3189  O   HOH A 444     3082   2911   3196    220    414     95       O  
HETATM 3190  O   HOH A 445      13.083  57.383  65.270  0.98 14.69           O  
ANISOU 3190  O   HOH A 445     1684   1759   2140    124    193   -150       O  
HETATM 3191  O   HOH A 446      16.474  44.608  68.246  1.00 19.31           O  
ANISOU 3191  O   HOH A 446     2336   2645   2356   -350     84    314       O  
HETATM 3192  O   HOH A 447      46.663  51.886  45.725  0.96 20.07           O  
ANISOU 3192  O   HOH A 447     2334   2635   2657     45    160   -325       O  
HETATM 3193  O   HOH A 448     119.401 188.212   0.040  0.20 -0.02           O  
ANISOU 3193  O   HOH A 448       -3     -3     -3      0      0      0       O  
HETATM 3194  O   HOH A 449      28.013  78.871  44.724  1.00 15.56           O  
ANISOU 3194  O   HOH A 449     1805   1898   2208     94     70    332       O  
HETATM 3195  O   HOH A 450      14.762  33.184  65.911  0.99 18.19           O  
ANISOU 3195  O   HOH A 450     1997   2336   2577    -31   -586    602       O  
HETATM 3196  O   HOH A 451      20.792  70.954  60.539  0.96 14.63           O  
ANISOU 3196  O   HOH A 451     1913   1803   1843   -160    157    165       O  
HETATM 3197  O   HOH A 452      31.442  72.483  61.453  0.91 22.43           O  
ANISOU 3197  O   HOH A 452     2964   2857   2701    148   -350    496       O  
HETATM 3198  O   HOH A 453      29.830  57.402  40.770  0.95 15.63           O  
ANISOU 3198  O   HOH A 453     2219   2080   1640    -85     22     89       O  
HETATM 3199  O   HOH A 454      16.320  70.285  59.339  0.99 16.47           O  
ANISOU 3199  O   HOH A 454     1909   1983   2365    122   -131    405       O  
HETATM 3200  O   HOH A 455      34.105  43.843  43.304  1.00 17.54           O  
ANISOU 3200  O   HOH A 455     2374   2072   2218    300    510    -88       O  
HETATM 3201  O   HOH A 456      17.528  44.392  50.784  1.00 16.94           O  
ANISOU 3201  O   HOH A 456     1935   2214   2287   -101   -318     34       O  
HETATM 3202  O   HOH A 457      13.777  44.998  53.794  0.82 18.82           O  
ANISOU 3202  O   HOH A 457     1959   2597   2595   -139     61   -452       O  
HETATM 3203  O   HOH A 458      32.601  68.296  61.512  0.87 18.18           O  
ANISOU 3203  O   HOH A 458     1792   2202   2912    190     96   -133       O  
HETATM 3204  O   HOH A 459      47.558  69.034  72.354  1.00 19.83           O  
ANISOU 3204  O   HOH A 459     2451   2502   2581     16    212    101       O  
HETATM 3205  O   HOH A 460      18.219  31.556  65.520  0.39 11.56           O  
ANISOU 3205  O   HOH A 460     1636   1709   1047     63   -258    150       O  
HETATM 3206  O   HOH A 461      10.552  42.166  52.261  1.00 15.35           O  
ANISOU 3206  O   HOH A 461     1755   1945   2132    -62   -156     94       O  
HETATM 3207  O   HOH A 462      18.229  71.874  60.619  1.00 17.77           O  
ANISOU 3207  O   HOH A 462     2288   2007   2456     79     27    120       O  
HETATM 3208  O   HOH A 463      13.141  39.279  63.438  0.83 14.94           O  
ANISOU 3208  O   HOH A 463     1557   2149   1971    156      8   -116       O  
HETATM 3209  O   HOH A 464      41.824  72.442  65.520  0.39 10.29           O  
ANISOU 3209  O   HOH A 464     1245   1564   1102    277    146    -83       O  
HETATM 3210  O   HOH A 465      10.802  56.985  46.562  0.98 23.94           O  
ANISOU 3210  O   HOH A 465     2854   2846   3397    201    406    -72       O  
HETATM 3211  O   HOH A 466      16.642  47.814  33.979  0.98 21.84           O  
ANISOU 3211  O   HOH A 466     2587   3168   2542   -429   -307    335       O  
HETATM 3212  O   HOH A 467      20.904  54.606  62.769  0.92 16.41           O  
ANISOU 3212  O   HOH A 467     1888   1938   2410    108    352    -34       O  
HETATM 3213  O   HOH A 468      26.646  40.707  35.824  0.98 21.10           O  
ANISOU 3213  O   HOH A 468     3088   2567   2364    281    631   -596       O  
HETATM 3214  O   HOH A 469      27.153  32.260  54.600  1.00 17.33           O  
ANISOU 3214  O   HOH A 469     2200   1922   2464    193     15   -111       O  
HETATM 3215  O   HOH A 470      32.049  68.770  64.791  0.95 15.61           O  
ANISOU 3215  O   HOH A 470     2022   2052   1856     57    192   -138       O  
HETATM 3216  O   HOH A 471      17.028  69.028  40.730  1.00 19.57           O  
ANISOU 3216  O   HOH A 471     2461   2445   2529    179   -110    308       O  
HETATM 3217  O   HOH A 472       8.639  67.094  60.373  1.00 17.68           O  
ANISOU 3217  O   HOH A 472     2190   2189   2339    353     94    135       O  
HETATM 3218  O   HOH A 473      36.844  38.519  64.320  0.97 17.87           O  
ANISOU 3218  O   HOH A 473     2214   2276   2299   -204    185     16       O  
HETATM 3219  O   HOH A 474      51.696  53.357  48.883  1.00 26.50           O  
ANISOU 3219  O   HOH A 474     3412   3255   3404     94    376   -420       O  
HETATM 3220  O   HOH A 475       9.389  33.682  56.589  1.00 22.95           O  
ANISOU 3220  O   HOH A 475     3116   2756   2847   -583    346    -64       O  
HETATM 3221  O   HOH A 476      53.993  53.180  52.112  1.00 24.54           O  
ANISOU 3221  O   HOH A 476     2459   3984   2882   -159    457   -218       O  
HETATM 3222  O   HOH A 477      19.866  80.521  53.289  1.00 18.89           O  
ANISOU 3222  O   HOH A 477     2777   2121   2281    263    618    158       O  
HETATM 3223  O   HOH A 478       5.659  60.794  50.016  0.88 18.34           O  
ANISOU 3223  O   HOH A 478     2231   2522   2214   -113   -217    187       O  
HETATM 3224  O   HOH A 479      15.645  32.075  69.299  0.92 18.91           O  
ANISOU 3224  O   HOH A 479     2435   2588   2161    -89    552    -84       O  
HETATM 3225  O   HOH A 480      19.241  28.554  54.433  0.85 24.25           O  
ANISOU 3225  O   HOH A 480     2895   3194   3126   -128    304     25       O  
HETATM 3226  O   HOH A 481      47.575  48.473  49.703  0.75 23.54           O  
ANISOU 3226  O   HOH A 481     3413   2722   2808    246     52   -189       O  
HETATM 3227  O   HOH A 482      15.903  46.169  52.479  0.87 19.95           O  
ANISOU 3227  O   HOH A 482     2179   2526   2873     87   -166     18       O  
HETATM 3228  O   HOH A 483      45.623  64.335  45.855  1.00 16.82           O  
ANISOU 3228  O   HOH A 483     2170   2157   2064   -166   -144    562       O  
HETATM 3229  O   HOH A 484      16.873  80.035  41.783  0.95 22.61           O  
ANISOU 3229  O   HOH A 484     2580   2846   3165    595   -153    425       O  
HETATM 3230  O   HOH A 485      29.493  80.019  41.908  1.00 21.90           O  
ANISOU 3230  O   HOH A 485     2949   2871   2501   -277    -81    147       O  
HETATM 3231  O   HOH A 486      29.230  37.752  44.746  1.00 21.88           O  
ANISOU 3231  O   HOH A 486     2494   3038   2783     75     35    132       O  
HETATM 3232  O   HOH A 487       7.904  42.462  52.317  0.92 15.43           O  
ANISOU 3232  O   HOH A 487     1616   2148   2098    -88    252    116       O  
HETATM 3233  O   HOH A 488      26.003  74.353  37.119  1.00 19.57           O  
ANISOU 3233  O   HOH A 488     2497   2511   2429     51     20    153       O  
HETATM 3234  O   HOH A 489      11.063  63.454  66.027  0.81 16.66           O  
ANISOU 3234  O   HOH A 489     1943   1970   2417    515    351    131       O  
HETATM 3235  O   HOH A 490      12.301  43.822  57.421  1.00 22.06           O  
ANISOU 3235  O   HOH A 490     2766   2648   2970      7     80   -203       O  
HETATM 3236  O   HOH A 491      23.520  29.048  63.148  0.93 19.36           O  
ANISOU 3236  O   HOH A 491     2827   2282   2247    354    -80   -237       O  
HETATM 3237  O   HOH A 492      25.605  50.685  36.334  0.91 17.95           O  
ANISOU 3237  O   HOH A 492     2239   2338   2242    160    404     23       O  
HETATM 3238  O   HOH A 493      47.804  69.089  57.942  0.97 16.91           O  
ANISOU 3238  O   HOH A 493     1944   2311   2169   -188     91    231       O  
HETATM 3239  O   HOH A 494      18.045  71.450  63.622  0.85 24.69           O  
ANISOU 3239  O   HOH A 494     3620   2807   2955    301   -607    249       O  
HETATM 3240  O   HOH A 495       4.661  63.879  51.040  0.85 16.64           O  
ANISOU 3240  O   HOH A 495     1601   2338   2382    273     -7    180       O  
HETATM 3241  O   HOH A 496      21.313  51.757  55.645  0.95 21.04           O  
ANISOU 3241  O   HOH A 496     3034   2415   2546    -98   -108    213       O  
HETATM 3242  O   HOH A 497      42.740  64.187  43.064  0.98 27.86           O  
ANISOU 3242  O   HOH A 497     3893   3787   2903   -637    651    198       O  
HETATM 3243  O   HOH A 498      40.606  48.363  43.024  1.00 21.73           O  
ANISOU 3243  O   HOH A 498     2879   2926   2452   -200    472   -423       O  
HETATM 3244  O   HOH A 499      18.134  44.927  48.149  1.00 24.70           O  
ANISOU 3244  O   HOH A 499     2998   3271   3114   -304   -355    548       O  
HETATM 3245  O   HOH A 500      16.772  41.262  36.936  0.94 23.79           O  
ANISOU 3245  O   HOH A 500     2778   3020   3239    -82    524   -440       O  
HETATM 3246  O   HOH A 501       2.707  47.360  55.053  0.96 23.77           O  
ANISOU 3246  O   HOH A 501     2210   3512   3310    399    426    469       O  
HETATM 3247  O   HOH A 502      10.034  41.552  36.075  1.00 22.27           O  
ANISOU 3247  O   HOH A 502     2757   3035   2669   -598   -407    346       O  
HETATM 3248  O   HOH A 503      29.328  55.663  37.135  0.83 22.80           O  
ANISOU 3248  O   HOH A 503     2960   2829   2875     11    561   -109       O  
HETATM 3249  O   HOH A 504      -0.309  38.471  46.923  0.99 30.93           O  
ANISOU 3249  O   HOH A 504     3256   4308   4188   -272      1   -368       O  
HETATM 3250  O   HOH A 505      11.567  47.989  36.780  0.89 28.50           O  
ANISOU 3250  O   HOH A 505     3674   3792   3361    117   -831     87       O  
HETATM 3251  O   HOH A 506      20.623  38.911  43.097  1.00 25.42           O  
ANISOU 3251  O   HOH A 506     2790   3479   3389    151    179   -149       O  
HETATM 3252  O   HOH A 507      32.236  40.574  42.965  0.98 20.95           O  
ANISOU 3252  O   HOH A 507     2847   2599   2516    483    325    -85       O  
HETATM 3253  O   HOH A 508       9.902  43.601  58.763  0.90 27.45           O  
ANISOU 3253  O   HOH A 508     3076   3573   3783    154    400    182       O  
HETATM 3254  O   HOH A 509      15.545  80.294  52.600  0.97 24.37           O  
ANISOU 3254  O   HOH A 509     3041   3249   2969    247    253      7       O  
HETATM 3255  O   HOH A 510      17.444  48.569  58.101  0.99 21.48           O  
ANISOU 3255  O   HOH A 510     2677   2850   2633   -225   -386    190       O  
HETATM 3256  O   HOH A 511      10.020  48.530  64.627  1.00 40.36           O  
ANISOU 3256  O   HOH A 511     5359   5033   4942    -43    595   -872       O  
HETATM 3257  O   HOH A 512      31.787  76.307  34.292  0.99 19.61           O  
ANISOU 3257  O   HOH A 512     3326   2072   2052     59    149    226       O  
HETATM 3258  O   HOH A 513      12.285  73.555  57.163  0.90 17.64           O  
ANISOU 3258  O   HOH A 513     2000   1891   2810    447    202    -19       O  
HETATM 3259  O   HOH A 514      34.031  47.567  41.044  0.93 18.57           O  
ANISOU 3259  O   HOH A 514     2012   2683   2360   -112    680   -261       O  
HETATM 3260  O   HOH A 515      31.088  40.277  45.389  0.97 23.79           O  
ANISOU 3260  O   HOH A 515     3434   2676   2930    -90    158     20       O  
HETATM 3261  O   HOH A 516      24.044  55.518  63.704  0.95 31.46           O  
ANISOU 3261  O   HOH A 516     4505   3866   3580    252     41   -245       O  
HETATM 3262  O   HOH A 517      34.369  50.043  39.823  0.74 18.25           O  
ANISOU 3262  O   HOH A 517     2292   2395   2246     91    429   -175       O  
HETATM 3263  O   HOH A 518      43.810  74.499  51.886  0.86 19.50           O  
ANISOU 3263  O   HOH A 518     2799   2452   2159    -48      5    667       O  
HETATM 3264  O   HOH A 519      19.178  26.998  59.005  0.92 24.32           O  
ANISOU 3264  O   HOH A 519     3134   3362   2745    211    496    -56       O  
HETATM 3265  O   HOH A 520      18.371  49.278  55.882  0.95 24.92           O  
ANISOU 3265  O   HOH A 520     3207   3039   3223    -98    129    -84       O  
HETATM 3266  O   HOH A 521      15.338  59.937  39.335  1.00 22.78           O  
ANISOU 3266  O   HOH A 521     2703   2406   3547    408   -352    -22       O  
HETATM 3267  O   HOH A 522      16.621  29.344  48.122  0.97 23.99           O  
ANISOU 3267  O   HOH A 522     3089   3147   2879   -130    185   -135       O  
HETATM 3268  O   HOH A 523      38.545  69.571  31.809  0.97 35.87           O  
ANISOU 3268  O   HOH A 523     4143   4659   4828   -237    130    128       O  
HETATM 3269  O   HOH A 524      24.767  68.016  35.055  1.00 30.48           O  
ANISOU 3269  O   HOH A 524     3864   3850   3869   -287    274    438       O  
HETATM 3270  O   HOH A 525      41.349  38.974  64.058  0.97 21.89           O  
ANISOU 3270  O   HOH A 525     2646   2686   2985    232   -402     27       O  
HETATM 3271  O   HOH A 526      13.264  30.037  51.033  0.74 29.77           O  
ANISOU 3271  O   HOH A 526     3584   4006   3719   -196    941   -573       O  
HETATM 3272  O   HOH A 527      42.311  72.797  50.193  1.00 26.28           O  
ANISOU 3272  O   HOH A 527     3453   3210   3322   -377     39    385       O  
HETATM 3273  O   HOH A 528      35.634  77.480  43.736  0.96 27.20           O  
ANISOU 3273  O   HOH A 528     3791   3206   3337     51    177    163       O  
HETATM 3274  O   HOH A 529      12.847  65.981  37.889  1.00 26.25           O  
ANISOU 3274  O   HOH A 529     3627   3634   2713   -248   -372    427       O  
HETATM 3275  O   HOH A 530      38.046  75.433  47.473  0.88 40.52           O  
ANISOU 3275  O   HOH A 530     5013   4933   5449    352    422   -510       O  
HETATM 3276  O   HOH A 531      13.297  67.545  66.435  0.91 19.99           O  
ANISOU 3276  O   HOH A 531     2681   2576   2338    254    249   -349       O  
HETATM 3277  O   HOH A 532      51.701  51.432  55.441  0.95 23.96           O  
ANISOU 3277  O   HOH A 532     2882   3183   3038   -180    398     24       O  
HETATM 3278  O   HOH A 533      14.658  69.309  61.209  0.87 29.19           O  
ANISOU 3278  O   HOH A 533     3433   3930   3729   -315   1117   -238       O  
HETATM 3279  O   HOH A 534      33.428  38.058  49.852  0.90 17.99           O  
ANISOU 3279  O   HOH A 534     2244   2306   2287    -19   -287    261       O  
HETATM 3280  O   HOH A 535      11.622  72.859  54.129  1.00 22.13           O  
ANISOU 3280  O   HOH A 535     2132   2788   3487    437    -23    300       O  
HETATM 3281  O   HOH A 536      17.442  58.047  38.858  1.00 14.97           O  
ANISOU 3281  O   HOH A 536     1807   1852   2029     -6   -228   -113       O  
HETATM 3282  O   HOH A 537      27.438  30.308  63.943  0.90 20.25           O  
ANISOU 3282  O   HOH A 537     2173   2356   3166    352      0    603       O  
HETATM 3283  O   HOH A 538      24.305  47.781  53.880  0.97 18.49           O  
ANISOU 3283  O   HOH A 538     2249   2247   2530    -77   -165    -74       O  
HETATM 3284  O   HOH A 539      21.115  49.181  55.094  1.00 21.88           O  
ANISOU 3284  O   HOH A 539     2747   2809   2759   -186    -31    296       O  
HETATM 3285  O   HOH A 540      16.386  42.990  46.871  0.93 22.13           O  
ANISOU 3285  O   HOH A 540     2715   3052   2643    103   -447     65       O  
HETATM 3286  O   HOH A 541       9.932  71.400  60.624  1.00 31.23           O  
ANISOU 3286  O   HOH A 541     4483   3600   3785    129    648   -115       O  
HETATM 3287  O   HOH A 542      28.775  68.015  33.059  0.83 24.10           O  
ANISOU 3287  O   HOH A 542     3016   3137   3004     30    676   -131       O  
HETATM 3288  O   HOH A 543       9.991  67.111  40.349  0.98 37.13           O  
ANISOU 3288  O   HOH A 543     3739   5184   5186    334   -258     56       O  
HETATM 3289  O   HOH A 544      16.053  29.666  66.181  1.00 41.06           O  
ANISOU 3289  O   HOH A 544     5692   4794   5117   -117   -847     41       O  
HETATM 3290  O   HOH A 545      15.493  73.220  33.472  0.97 39.80           O  
ANISOU 3290  O   HOH A 545     4883   4931   5309    155   -503    579       O  
HETATM 3291  O   HOH A 546       3.995  60.514  58.012  1.00 32.99           O  
ANISOU 3291  O   HOH A 546     3952   3918   4664    859   -306    533       O  
HETATM 3292  O   HOH A 547      40.215  57.864  41.337  0.99 36.87           O  
ANISOU 3292  O   HOH A 547     5288   4541   4179   -164   1121  -1101       O  
HETATM 3293  O   HOH A 548      36.944  39.674  57.572  0.98 28.30           O  
ANISOU 3293  O   HOH A 548     3200   3733   3819    400   -404     17       O  
HETATM 3294  O   HOH A 549      21.300  71.877  63.033  0.98 24.77           O  
ANISOU 3294  O   HOH A 549     3289   3750   2372   -608    -69    118       O  
HETATM 3295  O   HOH A 550       6.660  62.367  45.044  1.00 23.88           O  
ANISOU 3295  O   HOH A 550     3112   3102   2859     -1     -6   -333       O  
HETATM 3296  O   HOH A 551      47.426  63.301  44.115  1.00 39.92           O  
ANISOU 3296  O   HOH A 551     5276   4941   4952   -167    112    -38       O  
HETATM 3297  O   HOH A 552       9.117  45.704  57.871  0.92 25.58           O  
ANISOU 3297  O   HOH A 552     2904   3497   3318   -117    224   -242       O  
HETATM 3298  O   HOH A 553      46.918  75.617  54.737  0.80 32.51           O  
ANISOU 3298  O   HOH A 553     4299   4144   3911     55   -160    507       O  
HETATM 3299  O   HOH A 554      27.763  33.050  43.233  1.00 23.87           O  
ANISOU 3299  O   HOH A 554     3021   3049   3000     95    796    204       O  
HETATM 3300  O   HOH A 555      40.350  68.189  41.440  0.92 25.47           O  
ANISOU 3300  O   HOH A 555     2939   3947   2792    -35     42   -262       O  
HETATM 3301  O   HOH A 556      42.499  49.394  41.245  0.73 33.14           O  
ANISOU 3301  O   HOH A 556     3931   4657   4005     95     96    -58       O  
HETATM 3302  O   HOH A 557       4.940  64.692  56.775  1.00 41.25           O  
ANISOU 3302  O   HOH A 557     4714   5019   5942    815    142    220       O  
HETATM 3303  O   HOH A 558      23.698  72.766  64.299  0.94 28.00           O  
ANISOU 3303  O   HOH A 558     4132   2914   3593    100    399   -510       O  
HETATM 3304  O   HOH A 559      19.880  47.344  52.423  0.93 23.44           O  
ANISOU 3304  O   HOH A 559     3263   3111   2531   -564    931   -374       O  
HETATM 3305  O   HOH A 560      14.537  28.423  58.839  0.75 53.29           O  
ANISOU 3305  O   HOH A 560     6817   6668   6765    -96    -97    107       O  
HETATM 3306  O   HOH A 561      17.322  48.341  53.355  0.89 19.77           O  
ANISOU 3306  O   HOH A 561     2378   2657   2479     69    498   -454       O  
HETATM 3307  O   HOH A 562       8.905  66.062  67.718  0.98 39.09           O  
ANISOU 3307  O   HOH A 562     4848   5134   4870    -79    959   -448       O  
HETATM 3308  O   HOH A 563      11.540  55.578  69.161  0.97 44.01           O  
ANISOU 3308  O   HOH A 563     5401   5629   5693    145   1591   -193       O  
HETATM 3309  O   HOH A 564      41.967  76.550  51.216  1.00 21.92           O  
ANISOU 3309  O   HOH A 564     3026   2591   2713   -295   -357    678       O  
HETATM 3310  O   HOH A 565      43.186  70.733  42.502  1.00 21.48           O  
ANISOU 3310  O   HOH A 565     2599   2791   2771     -1    186    219       O  
HETATM 3311  O   HOH A 566       9.215  76.340  49.856  0.91 22.79           O  
ANISOU 3311  O   HOH A 566     2636   2682   3342    434   -408    397       O  
HETATM 3312  O   HOH A 567      12.868  79.237  51.909  1.00 30.61           O  
ANISOU 3312  O   HOH A 567     3960   3561   4108   -248    325    283       O  
HETATM 3313  O   HOH A 568       8.569  34.024  53.298  0.96 26.84           O  
ANISOU 3313  O   HOH A 568     2896   3730   3571   -150   -662    400       O  
HETATM 3314  O   HOH A 569      47.539  71.024  43.920  0.94 31.19           O  
ANISOU 3314  O   HOH A 569     3737   3955   4158   -176     42    650       O  
HETATM 3315  O   HOH A 570       9.231  57.754  40.544  0.87 18.39           O  
ANISOU 3315  O   HOH A 570     2102   2410   2475    525   -231    -64       O  
HETATM 3316  O   HOH A 571      13.786  30.724  65.900  0.99 26.51           O  
ANISOU 3316  O   HOH A 571     3350   3496   3226   -591  -1087   -206       O  
HETATM 3317  O   HOH A 572      45.519  63.234  42.839  0.60 24.25           O  
ANISOU 3317  O   HOH A 572     2705   3078   3432    379   1121   -245       O  
HETATM 3318  O   HOH A 573      15.485  69.345  63.827  0.92 23.98           O  
ANISOU 3318  O   HOH A 573     2826   2932   3353    122    185     19       O  
HETATM 3319  O   HOH A 574      12.375  53.299  36.963  0.99 25.21           O  
ANISOU 3319  O   HOH A 574     3556   3550   2473   -505    337   -334       O  
HETATM 3320  O   HOH A 575      20.001  42.605  47.600  1.00 26.20           O  
ANISOU 3320  O   HOH A 575     3820   3280   2855   -357   -162     61       O  
HETATM 3321  O   HOH A 576      11.699  63.545  38.605  1.00 25.25           O  
ANISOU 3321  O   HOH A 576     3449   3191   2955   -410    -86     82       O  
HETATM 3322  O   HOH A 577      35.254  36.878  61.854  0.90 26.36           O  
ANISOU 3322  O   HOH A 577     3523   3045   3448    -70     12   -318       O  
HETATM 3323  O   HOH A 578      28.172  58.416  34.641  0.98 28.51           O  
ANISOU 3323  O   HOH A 578     4250   3179   3401    393   -219   -149       O  
HETATM 3324  O   HOH A 579       2.036  61.959  54.155  0.81 34.85           O  
ANISOU 3324  O   HOH A 579     3821   4848   4571    149   -347    415       O  
HETATM 3325  O   HOH A 580      27.943  81.669  45.813  0.96 37.53           O  
ANISOU 3325  O   HOH A 580     4868   4682   4711    -25    -62    139       O  
HETATM 3326  O   HOH A 581       8.269  58.316  43.128  0.83 28.58           O  
ANISOU 3326  O   HOH A 581     3681   3883   3296     96    171    -50       O  
HETATM 3327  O   HOH A 582       6.778  71.146  52.808  1.00 34.78           O  
ANISOU 3327  O   HOH A 582     4355   4644   4216    101   -266    379       O  
HETATM 3328  O   HOH A 583      47.853  62.544  63.347  0.98 25.46           O  
ANISOU 3328  O   HOH A 583     2973   3256   3447     47    -17    191       O  
HETATM 3329  O   HOH A 584      -1.290  33.416  38.912  0.98 22.95           O  
ANISOU 3329  O   HOH A 584     2833   3207   2679   -559   -446   -312       O  
HETATM 3330  O   HOH A 585      33.307  45.002  39.693  1.00 35.97           O  
ANISOU 3330  O   HOH A 585     4542   4926   4198   -327   1060   -943       O  
HETATM 3331  O   HOH A 586      16.811  51.325  58.589  0.87 20.56           O  
ANISOU 3331  O   HOH A 586     2283   2676   2853    200    125   -162       O  
HETATM 3332  O   HOH A 587      21.166  38.138  40.673  0.95 30.64           O  
ANISOU 3332  O   HOH A 587     4279   3567   3796   -205    114   -262       O  
HETATM 3333  O   HOH A 588      48.948  60.441  63.784  0.89 43.02           O  
ANISOU 3333  O   HOH A 588     5705   5374   5266     98    107   -334       O  
HETATM 3334  O   HOH A 589       7.901  60.988  43.189  0.98 24.76           O  
ANISOU 3334  O   HOH A 589     2798   3233   3375    157    267   -124       O  
HETATM 3335  O   HOH A 590      10.683  60.077  39.969  1.00 23.15           O  
ANISOU 3335  O   HOH A 590     3728   2326   2742    502    413   -116       O  
HETATM 3336  O   HOH A 591       1.286  32.688  39.340  0.96 30.43           O  
ANISOU 3336  O   HOH A 591     4220   3606   3735    166   -632    344       O  
HETATM 3337  O   HOH A 592      27.845  77.750  57.745  1.00 27.23           O  
ANISOU 3337  O   HOH A 592     3746   3209   3391   -117   -640    603       O  
HETATM 3338  O   HOH A 593      30.222  81.971  43.878  0.93 32.26           O  
ANISOU 3338  O   HOH A 593     4188   3914   4157    341   -106   -113       O  
HETATM 3339  O   HOH A 594      39.376  65.664  40.130  0.89 24.59           O  
ANISOU 3339  O   HOH A 594     3359   3106   2877   -287   -276    678       O  
HETATM 3340  O   HOH A 595      28.245  57.524  38.527  0.95 23.12           O  
ANISOU 3340  O   HOH A 595     2619   2991   3173   -101   -149    204       O  
HETATM 3341  O   HOH A 596      35.626  36.855  49.211  0.91 25.35           O  
ANISOU 3341  O   HOH A 596     2964   3060   3607    538    722    121       O  
HETATM 3342  O   HOH A 597      11.107  72.352  40.517  0.96 31.32           O  
ANISOU 3342  O   HOH A 597     4215   3533   4150     75   -224   -189       O  
HETATM 3343  O   HOH A 598      42.033  71.331  40.147  0.92 29.58           O  
ANISOU 3343  O   HOH A 598     3721   3843   3674    345   -191     89       O  
HETATM 3344  O   HOH A 599      37.833  40.478  53.236  0.97 24.14           O  
ANISOU 3344  O   HOH A 599     2751   3003   3417     36    312   -183       O  
HETATM 3345  O   HOH A 600      39.060  39.552  51.162  0.97 24.09           O  
ANISOU 3345  O   HOH A 600     3003   2924   3227    369   -204    118       O  
HETATM 3346  O   HOH A 601      17.956  65.516  36.948  0.84 30.41           O  
ANISOU 3346  O   HOH A 601     3045   3954   4554    453      5    109       O  
HETATM 3347  O   HOH A 602      50.651  56.763  59.630  0.99 31.30           O  
ANISOU 3347  O   HOH A 602     3788   3907   4199    303   -658    370       O  
HETATM 3348  O   HOH A 603      52.521  64.854  55.679  1.00 47.44           O  
ANISOU 3348  O   HOH A 603     6058   5888   6081    -32   1491   -723       O  
HETATM 3349  O   HOH A 604       5.740  41.424  37.061  0.93 33.65           O  
ANISOU 3349  O   HOH A 604     4291   4242   4254   -239   -509     12       O  
HETATM 3350  O   HOH A 605      42.493  55.390  40.802  0.96 26.81           O  
ANISOU 3350  O   HOH A 605     2985   3675   3526    101    -57     97       O  
HETATM 3351  O   HOH A 606      54.348  46.552  64.689  0.91 36.72           O  
ANISOU 3351  O   HOH A 606     4444   4533   4976     86    -69    743       O  
HETATM 3352  O   HOH A 607      24.610  32.551  40.428  0.98 25.32           O  
ANISOU 3352  O   HOH A 607     3802   3340   2477   -521    838   -505       O  
HETATM 3353  O   HOH A 608      40.667  41.190  49.466  0.86 24.77           O  
ANISOU 3353  O   HOH A 608     3092   3328   2990     45   -381    419       O  
HETATM 3354  O   HOH A 609      44.291  56.878  39.117  1.00 31.86           O  
ANISOU 3354  O   HOH A 609     4550   4055   3500   -225   -406     -7       O  
HETATM 3355  O   HOH A 610      51.469  64.628  53.650  1.00 33.48           O  
ANISOU 3355  O   HOH A 610     3248   4305   5169    307    -84    125       O  
HETATM 3356  O   HOH A 611      10.872  50.671  67.997  1.00 79.58           O  
ANISOU 3356  O   HOH A 611     9974  10179  10086    -92    181    -40       O  
HETATM 3357  O   HOH A 612      22.219  83.645  47.049  0.73 29.41           O  
ANISOU 3357  O   HOH A 612     3878   3379   3915    182   -297    605       O  
HETATM 3358  O   HOH A 613      40.295  76.493  43.645  1.00 24.86           O  
ANISOU 3358  O   HOH A 613     2796   3616   3033   -651   -184    241       O  
HETATM 3359  O   HOH A 614      13.805  50.814  36.289  0.98 32.93           O  
ANISOU 3359  O   HOH A 614     4061   4258   4192    167   -806     23       O  
HETATM 3360  O   HOH A 615      31.185  48.257  38.112  0.93 43.14           O  
ANISOU 3360  O   HOH A 615     5020   6096   5275   -544   -210   -326       O  
HETATM 3361  O   HOH A 616       6.405  66.995  49.987  0.85 28.92           O  
ANISOU 3361  O   HOH A 616     3573   3833   3581   -267    803   -266       O  
HETATM 3362  O   HOH A 617      52.571  46.514  52.494  1.00 46.97           O  
ANISOU 3362  O   HOH A 617     5265   5732   6851    956      7    149       O  
HETATM 3363  O   HOH A 618      36.623  54.638  41.081  1.00 27.01           O  
ANISOU 3363  O   HOH A 618     4427   3358   2478   -635    446   -474       O  
HETATM 3364  O   HOH A 619      32.158  34.391  53.050  0.99 35.60           O  
ANISOU 3364  O   HOH A 619     4356   4524   4646    193   -768    318       O  
HETATM 3365  O   HOH A 620      20.900  88.351  54.706  0.88 59.31           O  
ANISOU 3365  O   HOH A 620     7703   7447   7387   -246   -291    213       O  
HETATM 3366  O   HOH A 621      21.154  86.168  52.764  0.92 50.85           O  
ANISOU 3366  O   HOH A 621     6251   6347   6721    302    195   -289       O  
HETATM 3367  O   HOH A 622      22.403  86.049  54.691  0.93 34.28           O  
ANISOU 3367  O   HOH A 622     3837   4503   4684    283    657   -419       O  
HETATM 3368  O   HOH A 623      28.893  26.492  46.232  0.79 32.05           O  
ANISOU 3368  O   HOH A 623     3831   3985   4364    182    -25    238       O  
HETATM 3369  O   HOH A 624      -2.313  37.378  45.521  1.00 36.22           O  
ANISOU 3369  O   HOH A 624     4368   5144   4251   -670    787     89       O  
HETATM 3370  O   HOH A 625      11.901  56.557  50.602  1.00 43.52           O  
ANISOU 3370  O   HOH A 625     5257   5560   5717   -404    982   -107       O  
HETATM 3371  O   HOH A 626      24.849  27.831  52.531  0.96 32.26           O  
ANISOU 3371  O   HOH A 626     4556   3786   3915    711   -503     40       O  
HETATM 3372  O   HOH A 627      16.906  57.669  53.400  0.98 31.05           O  
ANISOU 3372  O   HOH A 627     4046   4141   3610    -30   -793    453       O  
HETATM 3373  O   HOH A 628      13.550  55.509  51.795  1.00 37.47           O  
ANISOU 3373  O   HOH A 628     5085   4829   4322    -71   1151    128       O  
HETATM 3374  O   HOH A 629      43.097  41.018  49.470  0.67 26.13           O  
ANISOU 3374  O   HOH A 629     2928   3605   3395    -24    165   -258       O  
HETATM 3375  O   HOH A 630      57.256  52.280  60.666  0.77 54.17           O  
ANISOU 3375  O   HOH A 630     6926   6788   6867    271   -316    -55       O  
HETATM 3376  O   HOH A 631       6.988  40.688  60.924  0.90 29.29           O  
ANISOU 3376  O   HOH A 631     3643   3780   3705    177   -685    115       O  
HETATM 3377  O   HOH A 632      49.875  63.643  61.460  0.87 31.47           O  
ANISOU 3377  O   HOH A 632     4208   3614   4134     45    129   -151       O  
HETATM 3378  O   HOH A 633      11.062  76.810  51.775  0.93 32.12           O  
ANISOU 3378  O   HOH A 633     4152   3683   4369    237   -338    111       O  
HETATM 3379  O   HOH A 634      38.381  39.490  55.699  0.94 34.73           O  
ANISOU 3379  O   HOH A 634     4379   4606   4213     34    565   -163       O  
HETATM 3380  O   HOH A 635      21.966  48.725  52.756  0.81 21.56           O  
ANISOU 3380  O   HOH A 635     2513   2730   2949    270   -304   -141       O  
HETATM 3381  O   HOH A 636       9.438  53.225  44.390  1.00 43.73           O  
ANISOU 3381  O   HOH A 636     6187   5548   4882   -628   -482    218       O  
HETATM 3382  O   HOH A 637      28.491  33.405  50.210  0.94 24.40           O  
ANISOU 3382  O   HOH A 637     3208   3029   3035    342    470   -525       O  
HETATM 3383  O   HOH A 638      51.988  66.437  69.915  0.88 20.02           O  
ANISOU 3383  O   HOH A 638     2126   2678   2800   -315    245    115       O  
HETATM 3384  O   HOH A 639      46.799  76.637  69.250  1.00 32.91           O  
ANISOU 3384  O   HOH A 639     4420   4461   3624  -1051    550   -604       O  
HETATM 3385  O   HOH A 640      21.612  55.742  33.731  1.00 30.21           O  
ANISOU 3385  O   HOH A 640     3306   4322   3850    253   -307    276       O  
HETATM 3386  O   HOH A 641      30.254  74.578  63.297  1.00 35.36           O  
ANISOU 3386  O   HOH A 641     4151   4902   4381   -392    597     33       O  
HETATM 3387  O   HOH A 642      49.913  66.369  64.710  0.79 31.50           O  
ANISOU 3387  O   HOH A 642     3585   4228   4157     32    543    -58       O  
HETATM 3388  O   HOH A 643      22.601  76.085  38.397  1.00 33.93           O  
ANISOU 3388  O   HOH A 643     4268   4418   4207    315     97    325       O  
HETATM 3389  O   HOH A 644      26.887  72.892  63.343  1.00 30.71           O  
ANISOU 3389  O   HOH A 644     4728   3400   3542     70     91   -447       O  
HETATM 3390  O   HOH A 645      32.922  36.687  46.182  1.00 41.27           O  
ANISOU 3390  O   HOH A 645     4608   5720   5352    269   -825   -216       O  
HETATM 3391  O   HOH A 646      50.660  57.941  62.662  0.96 49.16           O  
ANISOU 3391  O   HOH A 646     5550   6271   6858    187    334    201       O  
HETATM 3392  O   HOH A 647       3.178  49.309  44.660  0.97 35.09           O  
ANISOU 3392  O   HOH A 647     4086   4739   4506    663    107    -18       O  
HETATM 3393  O   HOH A 648      22.017  74.161  35.903  0.93101.79           O  
ANISOU 3393  O   HOH A 648    12823  12932  12921    -17    282     -4       O  
HETATM 3394  O   HOH A 649       2.728  37.558  51.972  0.97 29.93           O  
ANISOU 3394  O   HOH A 649     3249   4327   3797   -320   -170    -24       O  
HETATM 3395  O   HOH A 650      40.628  75.921  46.716  0.95 41.98           O  
ANISOU 3395  O   HOH A 650     5214   4927   5810    -40    378   -174       O  
HETATM 3396  O   HOH A 651      17.604  81.510  40.183  0.94 30.48           O  
ANISOU 3396  O   HOH A 651     3147   4132   4303    165   -180    886       O  
HETATM 3397  O   HOH A 652       4.070  49.379  37.047  1.00 45.50           O  
ANISOU 3397  O   HOH A 652     6041   5910   5336   -442  -1193    498       O  
HETATM 3398  O   HOH A 653      31.460  46.248  39.179  1.00 38.03           O  
ANISOU 3398  O   HOH A 653     5194   4616   4642    -10    455     26       O  
HETATM 3399  O   HOH A 654      26.051  29.894  55.005  0.87 26.14           O  
ANISOU 3399  O   HOH A 654     3407   2982   3542    186    288     36       O  
HETATM 3400  O   HOH A 655      42.730  74.309  46.239  1.00 38.36           O  
ANISOU 3400  O   HOH A 655     4736   5040   4800   -111    400    343       O  
HETATM 3401  O   HOH A 656       7.312  61.714  66.080  0.90 31.86           O  
ANISOU 3401  O   HOH A 656     3986   3610   4508    721    501    -63       O  
HETATM 3402  O   HOH A 657       9.539  74.137  55.160  0.99 29.76           O  
ANISOU 3402  O   HOH A 657     3866   3752   3691    279   -649    434       O  
HETATM 3403  O   HOH A 658      21.861  83.792  42.392  0.99 34.56           O  
ANISOU 3403  O   HOH A 658     4077   4560   4492    395   -375    642       O  
HETATM 3404  O   HOH A 659      32.895  34.139  56.977  0.86 30.51           O  
ANISOU 3404  O   HOH A 659     3479   3973   4142    322    190    224       O  
HETATM 3405  O   HOH A 660      25.731  70.062  35.455  0.98 46.65           O  
ANISOU 3405  O   HOH A 660     6006   5928   5791     56    -77   -244       O  
HETATM 3406  O   HOH A 661      25.612  72.587  35.269  1.00 41.08           O  
ANISOU 3406  O   HOH A 661     5067   5032   5508    139   -246   -100       O  
HETATM 3407  O   HOH A 662      19.943  41.173  35.373  0.91 25.58           O  
ANISOU 3407  O   HOH A 662     3019   2984   3717    253   -434   -281       O  
HETATM 3408  O   HOH A 663      29.274  32.809  53.094  0.98 32.42           O  
ANISOU 3408  O   HOH A 663     4318   3906   4092   -220    868   -135       O  
HETATM 3409  O   HOH A 664      26.423  28.777  51.166  0.98 38.29           O  
ANISOU 3409  O   HOH A 664     4436   4953   5161    232   -129   -434       O  
HETATM 3410  O   HOH A 665      10.129  34.159  50.579  0.98 30.87           O  
ANISOU 3410  O   HOH A 665     4157   3988   3584    -78   -351    185       O  
HETATM 3411  O   HOH A 666      18.885  85.008  46.021  0.96 45.04           O  
ANISOU 3411  O   HOH A 666     5925   5179   6008    285   -394    310       O  
HETATM 3412  O   HOH A 667      49.814  44.059  51.737  1.00 59.07           O  
ANISOU 3412  O   HOH A 667     7413   7492   7538    196    272   -148       O  
HETATM 3413  O   HOH A 668      39.686  43.272  47.635  0.93 21.66           O  
ANISOU 3413  O   HOH A 668     2411   2946   2871     -1    339   -190       O  
HETATM 3414  O   HOH A 669      -2.529  34.457  45.296  1.00 49.22           O  
ANISOU 3414  O   HOH A 669     5197   6672   6834    494  -1226    587       O  
HETATM 3415  O   HOH A 670      14.395  60.741  36.768  1.00 35.13           O  
ANISOU 3415  O   HOH A 670     4258   4299   4790    339  -1336    371       O  
HETATM 3416  O   HOH A 671      49.063  46.297  59.076  0.97 34.68           O  
ANISOU 3416  O   HOH A 671     3922   4216   5039     91    215    -36       O  
HETATM 3417  O   HOH A 672      47.743  42.897  61.222  1.00 33.03           O  
ANISOU 3417  O   HOH A 672     4106   4896   3549   -513   -421    731       O  
HETATM 3418  O   HOH A 673      10.365  63.067  70.514  1.00 39.21           O  
ANISOU 3418  O   HOH A 673     5407   5126   4365   -511   -670   -185       O  
HETATM 3419  O   HOH A 674      13.462  27.943  54.240  0.96 47.17           O  
ANISOU 3419  O   HOH A 674     5442   5850   6629    587    752   -248       O  
HETATM 3420  O   HOH A 675      49.129  43.965  56.370  0.86 29.38           O  
ANISOU 3420  O   HOH A 675     3123   3799   4240    319   -497    589       O  
HETATM 3421  O   HOH A 676      15.662  82.340  46.194  0.89 30.21           O  
ANISOU 3421  O   HOH A 676     3263   4424   3791    315   -432    125       O  
HETATM 3422  O   HOH A 677      35.088  74.242  28.124  1.00 61.25           O  
ANISOU 3422  O   HOH A 677     8401   7695   7177   -126    814   -490       O  
HETATM 3423  O   HOH A 678      15.281  80.614  48.086  1.00 62.82           O  
ANISOU 3423  O   HOH A 678     7794   7778   8297    149   -495     65       O  
HETATM 3424  O   HOH A 679      11.431  43.202  63.687  1.00 39.29           O  
ANISOU 3424  O   HOH A 679     5594   4482   4851   -217   -327    985       O  
HETATM 3425  O   HOH A 680      25.249  74.457  64.385  0.66 57.46           O  
ANISOU 3425  O   HOH A 680     7297   7330   7204      8   -312    -58       O  
HETATM 3426  O   HOH A 681      13.917  78.779  48.198  1.00 46.94           O  
ANISOU 3426  O   HOH A 681     5129   6334   6373    246   -852    516       O  
HETATM 3427  O   HOH A 682       8.834  72.038  40.631  1.00 56.09           O  
ANISOU 3427  O   HOH A 682     7151   7175   6985    -54   -621    559       O  
HETATM 3428  O   HOH A 683      52.694  68.936  69.294  0.97 25.66           O  
ANISOU 3428  O   HOH A 683     3313   3054   3383   -261    -77    477       O  
HETATM 3429  O   HOH A 684       0.768  38.101  55.652  0.53 28.78           O  
ANISOU 3429  O   HOH A 684     3938   3842   3157    -41    736   -486       O  
HETATM 3430  O   HOH A 685      20.776  78.576  38.298  1.00 40.19           O  
ANISOU 3430  O   HOH A 685     6155   4542   4574   -322   -223    754       O  
HETATM 3431  O   HOH A 686      17.728  80.873  37.871  1.00 44.50           O  
ANISOU 3431  O   HOH A 686     5068   5769   6071   -192    405   -415       O  
HETATM 3432  O   HOH A 687      21.040  87.242  49.982  1.00 47.00           O  
ANISOU 3432  O   HOH A 687     5790   6287   5779   -188   -568    157       O  
HETATM 3433  O   HOH A 688      55.372  69.406  70.039  0.95 28.76           O  
ANISOU 3433  O   HOH A 688     3201   3664   4065   -350   -134    118       O  
HETATM 3434  O   HOH A 689      28.758  39.647  42.628  0.92 34.17           O  
ANISOU 3434  O   HOH A 689     4664   4175   4143   -306   -825    -23       O  
HETATM 3435  O   HOH A 690      22.913  39.227  37.265  0.97 32.53           O  
ANISOU 3435  O   HOH A 690     4329   4071   3960    168    758   -620       O  
HETATM 3436  O   HOH A 691      16.626  55.586  35.450  0.86 33.18           O  
ANISOU 3436  O   HOH A 691     3947   4316   4345    138   -144    135       O  
HETATM 3437  O   HOH A 692       5.957  64.623  44.060  1.00 36.51           O  
ANISOU 3437  O   HOH A 692     4811   4774   4287     42   -504    171       O  
HETATM 3438  O   HOH A 693      15.148  54.805  53.282  1.00 45.93           O  
ANISOU 3438  O   HOH A 693     5273   6222   5958    199    458   -232       O  
HETATM 3439  O   HOH A 694      54.516  49.511  63.866  1.00 47.42           O  
ANISOU 3439  O   HOH A 694     5426   6083   6508    468   -703     81       O  
HETATM 3440  O   HOH A 695      15.465  65.025  36.125  0.62 30.53           O  
ANISOU 3440  O   HOH A 695     4576   3835   3187   -671   -502    342       O  
HETATM 3441  O   HOH A 696      17.248  26.747  47.818  0.98 30.17           O  
ANISOU 3441  O   HOH A 696     3657   3512   4293      0    128    116       O  
HETATM 3442  O   HOH A 697      34.518  41.467  41.886  0.81 35.73           O  
ANISOU 3442  O   HOH A 697     4122   4353   5100    149   -931    -62       O  
HETATM 3443  O   HOH A 698       6.306  65.530  59.587  0.93 43.48           O  
ANISOU 3443  O   HOH A 698     5931   4900   5689    544   -470   -419       O  
HETATM 3444  O   HOH A 699      56.330  54.410  52.982  0.90 31.25           O  
ANISOU 3444  O   HOH A 699     3473   4130   4272    279    583   -284       O  
HETATM 3445  O   HOH A 700      16.808  55.708  54.571  1.00 37.15           O  
ANISOU 3445  O   HOH A 700     4732   4811   4572      1   1179   -878       O  
HETATM 3446  O   HOH A 701      17.121  26.275  56.271  0.86 60.15           O  
ANISOU 3446  O   HOH A 701     7911   7558   7385   -149    -48   -153       O  
HETATM 3447  O   HOH A 702      20.242  73.890  34.153  1.00 61.44           O  
ANISOU 3447  O   HOH A 702     8283   7646   7414   -279   -193   -165       O  
HETATM 3448  O   HOH A 703      51.040  71.971  53.705  1.00 44.92           O  
ANISOU 3448  O   HOH A 703     5513   6026   5529   -212    217    284       O  
HETATM 3449  O   HOH A 704      38.865  41.247  45.692  0.76 35.36           O  
ANISOU 3449  O   HOH A 704     3809   4822   4803    589   1171   -308       O  
HETATM 3450  O   HOH A 705      38.371  61.298  38.392  0.82 30.30           O  
ANISOU 3450  O   HOH A 705     3807   3861   3845     44    168    232       O  
HETATM 3451  O   HOH A 706      28.370  29.823  47.452  0.83 40.24           O  
ANISOU 3451  O   HOH A 706     5211   4739   5339    213   -344   -142       O  
HETATM 3452  O   HOH A 707      34.633  37.688  45.014  1.00 34.70           O  
ANISOU 3452  O   HOH A 707     4831   3829   4525    226   -457    141       O  
HETATM 3453  O   HOH A 708      47.097  76.474  63.902  0.98 50.90           O  
ANISOU 3453  O   HOH A 708     6676   6095   6569   -127     55    358       O  
HETATM 3454  O   HOH A 709      45.970  76.467  75.749  0.75 29.82           O  
ANISOU 3454  O   HOH A 709     3825   3738   3766   -477   -280     35       O  
HETATM 3455  O   HOH A 710      49.886  72.593  59.149  0.81 37.82           O  
ANISOU 3455  O   HOH A 710     4792   4935   4642    276    362   -312       O  
HETATM 3456  O   HOH A 711       7.734  35.180  50.868  0.98 40.25           O  
ANISOU 3456  O   HOH A 711     5305   5086   4904   -247     48    501       O  
HETATM 3457  O   HOH A 712      22.572  35.723  39.872  0.79 21.31           O  
ANISOU 3457  O   HOH A 712     2993   2500   2603   -110     52   -182       O  
HETATM 3458  O   HOH A 713      41.298  68.648  36.598  0.95 30.22           O  
ANISOU 3458  O   HOH A 713     3638   4072   3772    -64    361   -582       O  
HETATM 3459  O   HOH A 714      26.740  80.393  41.847  0.82 25.71           O  
ANISOU 3459  O   HOH A 714     3392   3213   3165    357    -50    149       O  
HETATM 3460  O   HOH A 715      14.532  53.500  33.723  1.00 57.23           O  
ANISOU 3460  O   HOH A 715     6765   7457   7522    298    -52    137       O  
HETATM 3461  O   HOH A 716       7.033  30.397  43.716  1.00 30.17           O  
ANISOU 3461  O   HOH A 716     3364   4112   3987     46   -432    325       O  
HETATM 3462  O   HOH A 717      43.370  73.136  44.028  0.98 29.91           O  
ANISOU 3462  O   HOH A 717     3927   3437   4000    273   -609    637       O  
HETATM 3463  O   HOH A 718      20.669  80.569  39.798  1.00 45.89           O  
ANISOU 3463  O   HOH A 718     5929   5475   6033     -8     99     30       O  
HETATM 3464  O   HOH A 719      42.711  74.777  41.737  0.64 38.20           O  
ANISOU 3464  O   HOH A 719     5181   4762   4572   -155   -606    543       O  
HETATM 3465  O   HOH A 720      37.519  72.192  32.824  1.00 45.96           O  
ANISOU 3465  O   HOH A 720     5782   6086   5594     86    377    129       O  
HETATM 3466  O   HOH A 721      40.538  59.571  39.389  0.94 52.62           O  
ANISOU 3466  O   HOH A 721     6337   6670   6986    557    -49   -304       O  
HETATM 3467  O   HOH A 722      49.981  68.792  55.646  0.96 39.06           O  
ANISOU 3467  O   HOH A 722     5440   4558   4843    144    537   -225       O  
HETATM 3468  O   HOH A 723       5.853  57.815  39.358  0.75 52.48           O  
ANISOU 3468  O   HOH A 723     7032   6530   6379   -172   -382    222       O  
HETATM 3469  O   HOH A 724      29.655  31.506  48.348  0.90 35.57           O  
ANISOU 3469  O   HOH A 724     4810   3986   4717     66   -500   -330       O  
HETATM 3470  O   HOH A 725      50.350  62.368  41.774  0.88 98.44           O  
ANISOU 3470  O   HOH A 725    12485  12525  12391      5   -147    163       O  
HETATM 3471  O   HOH A 726      38.161  81.748  50.947  0.97 40.72           O  
ANISOU 3471  O   HOH A 726     5787   4925   4761   -224    708    538       O  
HETATM 3472  O   HOH A 727      42.466  62.334  39.097  1.00 36.01           O  
ANISOU 3472  O   HOH A 727     4750   4627   4306    205    233    470       O  
HETATM 3473  O   HOH A 728      15.964  76.623  44.699  0.96 42.00           O  
ANISOU 3473  O   HOH A 728     5164   5272   5520    182   -635    603       O  
HETATM 3474  O   HOH A 729      49.866  55.943  46.364  1.00 35.07           O  
ANISOU 3474  O   HOH A 729     4254   5056   4014   -284    296   -667       O  
HETATM 3475  O   HOH A 730       5.748  71.948  45.997  0.77 34.94           O  
ANISOU 3475  O   HOH A 730     3918   4320   5038    190    152     52       O  
HETATM 3476  O   HOH A 731      30.133  43.499  36.307  1.00 39.18           O  
ANISOU 3476  O   HOH A 731     4721   5251   4915   -397    497   -188       O  
HETATM 3477  O   HOH A 732      53.830  51.049  52.985  1.00 43.61           O  
ANISOU 3477  O   HOH A 732     5856   5376   5338   -713    563   -495       O  
HETATM 3478  O   HOH A 733      32.142  31.175  60.924  1.00 43.69           O  
ANISOU 3478  O   HOH A 733     6138   5332   5129   -386    121   -161       O  
HETATM 3479  O   HOH A 734      31.401  60.267  34.650  1.00 84.50           O  
ANISOU 3479  O   HOH A 734    10656  10712  10738    -17   -122    278       O  
HETATM 3480  O   HOH A 735       7.469  47.834  59.638  0.37 19.62           O  
ANISOU 3480  O   HOH A 735     2084   2430   2939    354   -366    166       O  
HETATM 3481  O   HOH A 736       7.789  74.004  42.600  0.96 38.91           O  
ANISOU 3481  O   HOH A 736     4431   5044   5309   -469  -1139    999       O  
HETATM 3482  O   HOH A 737      32.207  83.052  48.217  0.93 27.35           O  
ANISOU 3482  O   HOH A 737     3047   3531   3812    -25    -63    277       O  
HETATM 3483  O   HOH A 738       1.495  37.665  39.034  1.00 57.71           O  
ANISOU 3483  O   HOH A 738     7040   7354   7533    348   -294    154       O  
HETATM 3484  O   HOH A 739       6.714  68.641  61.367  0.82 29.33           O  
ANISOU 3484  O   HOH A 739     3977   3269   3899    505    -12    229       O  
HETATM 3485  O   HOH A 740      50.150  75.521  79.799  1.00 21.74           O  
ANISOU 3485  O   HOH A 740     3258   2345   2655    -13   -446    110       O  
HETATM 3486  O   HOH A 741       7.021  56.932  51.505  0.89 71.49           O  
ANISOU 3486  O   HOH A 741     9156   9027   8981   -138   -179     73       O  
HETATM 3487  O   HOH A 742       4.077  57.292  53.309  1.00 41.96           O  
ANISOU 3487  O   HOH A 742     5031   5470   5441   -210   -158   -296       O  
HETATM 3488  O   HOH A 743      32.160  34.203  59.822  0.80 34.95           O  
ANISOU 3488  O   HOH A 743     4230   4686   4363    -68   -638    329       O  
HETATM 3489  O   HOH A 744       5.499  53.799  53.984  1.00 44.20           O  
ANISOU 3489  O   HOH A 744     5106   5935   5753   -186   -549    481       O  
HETATM 3490  O   HOH A 745       4.571  70.640  53.310  0.98 79.75           O  
ANISOU 3490  O   HOH A 745    10080  10135  10087   -114   -422    117       O  
HETATM 3491  O   HOH A 746       5.226  51.627  52.360  1.00 41.44           O  
ANISOU 3491  O   HOH A 746     4857   4957   5932    625   -445    328       O  
HETATM 3492  O   HOH A 747       5.765  68.910  46.227  0.89 31.46           O  
ANISOU 3492  O   HOH A 747     4107   4038   3808     89    333    -93       O  
HETATM 3493  O   HOH A 748      19.489  60.729  35.091  0.95 49.01           O  
ANISOU 3493  O   HOH A 748     5970   6378   6275    443    149    334       O  
HETATM 3494  O   HOH A 749      16.873  34.210  36.174  0.62 58.95           O  
ANISOU 3494  O   HOH A 749     7323   7516   7559    140   -495    -48       O  
HETATM 3495  O   HOH A 750      52.263  68.850  57.396  1.00 58.57           O  
ANISOU 3495  O   HOH A 750     7388   7296   7571   -188    737   -484       O  
HETATM 3496  O   HOH A 751      54.209  48.095  58.781  0.67 54.09           O  
ANISOU 3496  O   HOH A 751     6654   7152   6746   -100    411   -225       O  
HETATM 3497  O   HOH A 752      22.724  44.372  54.628  0.98 24.33           O  
ANISOU 3497  O   HOH A 752     2781   3320   3141    -56    324    -33       O  
HETATM 3498  O   HOH A 753      38.678  77.955  36.854  0.87 37.05           O  
ANISOU 3498  O   HOH A 753     4502   5236   4339   -417   -528    146       O  
HETATM 3499  O   HOH A 754      11.845  38.364  33.301  1.00 37.59           O  
ANISOU 3499  O   HOH A 754     5591   4841   3852   -735   -632    475       O  
HETATM 3500  O   HOH A 755      24.767  76.571  36.832  0.90 24.91           O  
ANISOU 3500  O   HOH A 755     3301   2863   3300    251   -760    711       O  
HETATM 3501  O   HOH A 756      31.705  78.541  36.294  0.80 28.07           O  
ANISOU 3501  O   HOH A 756     4071   3315   3278     -3    577    113       O  
HETATM 3502  O   HOH A 757      31.709  36.478  51.272  0.64 21.45           O  
ANISOU 3502  O   HOH A 757     2344   3183   2622     67   -421    689       O  
HETATM 3503  O   HOH A 758      27.419  32.814  40.689  0.72 28.76           O  
ANISOU 3503  O   HOH A 758     3981   3645   3301    -74    593   -515       O  
HETATM 3504  O   HOH A 759       7.624  68.964  48.234  0.67 20.63           O  
ANISOU 3504  O   HOH A 759     2608   2236   2995    386    320   -169       O  
HETATM 3505  O   HOH A 760      20.224  38.361  38.330  0.69 25.66           O  
ANISOU 3505  O   HOH A 760     3498   3143   3110    -12   -207    -27       O  
HETATM 3506  O   HOH A 761      36.742  57.276  41.268  0.60 21.68           O  
ANISOU 3506  O   HOH A 761     2774   2895   2570    279    290    205       O  
HETATM 3507  O   HOH A 762       3.384  41.396  38.053  0.65 25.66           O  
ANISOU 3507  O   HOH A 762     3453   3357   2939   -228    -47    -61       O  
HETATM 3508  O   HOH A 763      32.825  35.767  62.024  0.78 30.93           O  
ANISOU 3508  O   HOH A 763     4445   3745   3560   -391    264    -80       O  
HETATM 3509  O   HOH A 764       5.150  60.048  45.731  0.65 32.83           O  
ANISOU 3509  O   HOH A 764     3937   4199   4337     57   -375    319       O  
HETATM 3510  O   HOH A 765      30.677  70.482  62.874  0.60 25.33           O  
ANISOU 3510  O   HOH A 765     3752   2625   3247    262   -469    312       O  
HETATM 3511  O   HOH A 766      25.453  82.216  45.637  0.73 29.15           O  
ANISOU 3511  O   HOH A 766     4101   3529   3448   -396    -58    286       O  
HETATM 3512  O   HOH A 767      51.916  64.815  68.022  0.80 27.04           O  
ANISOU 3512  O   HOH A 767     3904   3407   2963   -106     87    252       O  
HETATM 3513  O   HOH A 768      -0.561  42.497  48.161  0.65 24.89           O  
ANISOU 3513  O   HOH A 768     2603   3486   3369    252    138    425       O  
HETATM 3514  O   HOH A 769      39.199  38.449  62.893  0.66 21.98           O  
ANISOU 3514  O   HOH A 769     2562   2938   2850     33   -300   -233       O  
HETATM 3515  O   HOH A 770      41.356  66.062  37.511  0.50 27.00           O  
ANISOU 3515  O   HOH A 770     3241   3341   3675     36    401   -600       O  
HETATM 3516  O   HOH A 771      14.404  37.821  35.691  0.49 20.45           O  
ANISOU 3516  O   HOH A 771     2953   2451   2367    144    -25     32       O  
HETATM 3517  O   HOH A 772      41.807  51.324  38.979  0.53 57.60           O  
ANISOU 3517  O   HOH A 772     7379   7405   7101     34    331    -79       O  
HETATM 3518  O   HOH A 773      -0.297  44.262  50.271  0.85 27.16           O  
ANISOU 3518  O   HOH A 773     3333   3318   3669     -3   -718    556       O  
HETATM 3519  O   HOH A 774       4.251  55.293  55.197  0.82 40.74           O  
ANISOU 3519  O   HOH A 774     4984   5048   5448   -185   -628    -96       O  
HETATM 3520  O   HOH A 775      23.720  69.854  36.946  0.58 23.71           O  
ANISOU 3520  O   HOH A 775     2902   3198   2910     61   -642    675       O  
HETATM 3521  O   HOH A 776      49.400  56.426  41.962  0.38 22.27           O  
ANISOU 3521  O   HOH A 776     2675   2710   3076    478    599   -210       O  
HETATM 3522  O   HOH A 777      55.340  73.706  83.290  0.59 45.80           O  
ANISOU 3522  O   HOH A 777     6102   5763   5538   -199    427   -688       O  
HETATM 3523  O   HOH A 778       0.442  49.847  43.705  0.77 43.38           O  
ANISOU 3523  O   HOH A 778     5511   5338   5632    103    -32    446       O  
HETATM 3524  O   HOH A 779      52.419  54.850  46.514  0.80 34.74           O  
ANISOU 3524  O   HOH A 779     4747   4423   4032    -91   1055   -829       O  
HETATM 3525  O   HOH A 780       6.715  68.157  52.687  0.67 21.65           O  
ANISOU 3525  O   HOH A 780     2256   3279   2690    -55     27   -424       O  
HETATM 3526  O   HOH A 781      11.073  78.202  49.414  0.51 30.08           O  
ANISOU 3526  O   HOH A 781     4035   3767   3626   -242     98   -178       O  
HETATM 3527  O   HOH A 782      10.016  40.481  33.648  0.57 31.46           O  
ANISOU 3527  O   HOH A 782     4175   4233   3546   -483    363   -491       O  
HETATM 3528  O   HOH A 783       6.523  39.537  35.252  0.61 28.84           O  
ANISOU 3528  O   HOH A 783     3412   3899   3646   -180   -243     54       O  
HETATM 3529  O   HOH A 784      30.252  79.850  39.750  0.49 48.17           O  
ANISOU 3529  O   HOH A 784     6132   5959   6213   -135    -58   -197       O  
HETATM 3530  O   HOH A 785       3.016  35.470  39.263  0.54 24.83           O  
ANISOU 3530  O   HOH A 785     3203   3365   2864   -306   -119   -447       O  
HETATM 3531  O   HOH A 786       2.475  48.954  47.378  0.46 27.68           O  
ANISOU 3531  O   HOH A 786     3139   3552   3825     61    245   -631       O  
HETATM 3532  O   HOH A 787      52.908  45.674  59.764  0.69 35.31           O  
ANISOU 3532  O   HOH A 787     4726   4118   4572    159    554   -563       O  
HETATM 3533  O   HOH A 788      32.026  53.084  38.689  0.59 27.58           O  
ANISOU 3533  O   HOH A 788     3255   3479   3744    415   -480    390       O  
HETATM 3534  O   HOH A 789       2.868  53.996  60.590  0.62 29.94           O  
ANISOU 3534  O   HOH A 789     3515   3747   4113    340    514    131       O  
HETATM 3535  O   HOH A 790      32.431  81.404  35.175  0.54 40.68           O  
ANISOU 3535  O   HOH A 790     5071   5036   5348    236      0   -174       O  
HETATM 3536  O   HOH A 791      31.890  37.862  41.464  0.66 25.94           O  
ANISOU 3536  O   HOH A 791     3572   2722   3561    300   -301   -203       O  
HETATM 3537  O   HOH A 792      29.159  37.671  40.797  0.70 32.11           O  
ANISOU 3537  O   HOH A 792     4003   3783   4414     55    650    -82       O  
HETATM 3538  O   HOH A 793       8.431  73.542  57.480  0.70 28.69           O  
ANISOU 3538  O   HOH A 793     3659   2916   4327    428    603   -709       O  
HETATM 3539  O   HOH A 794      29.747  35.504  43.786  0.67 25.29           O  
ANISOU 3539  O   HOH A 794     2711   3651   3246    -46    340   -318       O  
HETATM 3540  O   HOH A 795      52.515  60.839  58.543  0.69 30.96           O  
ANISOU 3540  O   HOH A 795     3588   4311   3864    -83   -247     71       O  
HETATM 3541  O   HOH A 796       8.777  42.904  61.018  0.61 34.78           O  
ANISOU 3541  O   HOH A 796     4756   4357   4103   -561   -751    298       O  
HETATM 3542  O   HOH A 797      30.172  84.120  42.064  0.62 37.15           O  
ANISOU 3542  O   HOH A 797     4695   4373   5045    213    -13    210       O  
HETATM 3543  O   HOH A 798      16.841  37.678  35.664  0.50 29.55           O  
ANISOU 3543  O   HOH A 798     3725   3907   3595     92   -198   -383       O  
HETATM 3544  O   HOH A 799      25.300  80.631  39.666  0.57 32.23           O  
ANISOU 3544  O   HOH A 799     4570   3879   3796    133   -514     95       O  
HETATM 3545  O   HOH A 800      41.166  38.059  52.566  0.48 33.00           O  
ANISOU 3545  O   HOH A 800     4181   4088   4268     96   -165    166       O  
HETATM 3546  O   HOH A 801      25.189  35.869  38.889  0.42 25.90           O  
ANISOU 3546  O   HOH A 801     3424   3368   3049     91    145    119       O  
HETATM 3547  O   HOH A 802      31.414  59.221  36.669  0.58 26.94           O  
ANISOU 3547  O   HOH A 802     3220   3471   3543    133    223   -266       O  
HETATM 3548  O   HOH A 803      55.712  67.286  72.155  0.73 36.15           O  
ANISOU 3548  O   HOH A 803     4803   4284   4649   -172    120    234       O  
HETATM 3549  O   HOH A 804      42.032  46.029  43.835  0.58 28.94           O  
ANISOU 3549  O   HOH A 804     3412   3708   3878    120    485   -383       O  
HETATM 3550  O   HOH A 805      49.033  53.031  45.528  0.68 26.16           O  
ANISOU 3550  O   HOH A 805     2822   3300   3817    243    580   -229       O  
HETATM 3551  O   HOH A 806      48.015  64.359  65.662  0.71 26.05           O  
ANISOU 3551  O   HOH A 806     2649   3650   3601      8      4    -24       O  
HETATM 3552  O   HOH A 807      46.281  73.202  45.248  0.76 33.08           O  
ANISOU 3552  O   HOH A 807     4548   3914   4107   -431    124    -84       O  
HETATM 3553  O   HOH A 808      17.652  52.049  56.506  0.50 19.62           O  
ANISOU 3553  O   HOH A 808     2221   2809   2425    -51    -93    481       O  
HETATM 3554  O   HOH A 809       2.046  46.188  38.306  0.61 27.00           O  
ANISOU 3554  O   HOH A 809     3614   3518   3125    167   -970    479       O  
HETATM 3555  O   HOH A 810      38.732  36.429  54.746  0.63 26.55           O  
ANISOU 3555  O   HOH A 810     3175   3418   3496    348    289    104       O  
HETATM 3556  O   HOH A 811      51.818  62.217  64.509  0.56 33.56           O  
ANISOU 3556  O   HOH A 811     4415   4171   4167   -276    230   -334       O  
HETATM 3557  O   HOH A 812       9.911  29.823  42.621  0.55 31.59           O  
ANISOU 3557  O   HOH A 812     4504   4107   3390   -377    633   -314       O  
HETATM 3558  O   HOH A 813      28.093  76.917  34.727  0.63 39.55           O  
ANISOU 3558  O   HOH A 813     5302   4778   4948    -34    -23    274       O  
HETATM 3559  O   HOH A 814      29.240  79.439  59.263  0.80 37.58           O  
ANISOU 3559  O   HOH A 814     4533   4678   5068     74   -659    306       O  
HETATM 3560  O   HOH A 815      36.670  37.328  59.087  0.57 25.67           O  
ANISOU 3560  O   HOH A 815     2974   3292   3486    145    360   -488       O  
HETATM 3561  O   HOH A 816      41.157  78.137  53.126  0.41 18.05           O  
ANISOU 3561  O   HOH A 816     2101   2116   2641    168   -222    246       O  
HETATM 3562  O   HOH A 817      29.342  83.392  47.509  0.75 39.54           O  
ANISOU 3562  O   HOH A 817     5134   4667   5222    216    135    129       O  
HETATM 3563  O   HOH A 818      29.404  47.932  35.571  0.65 24.36           O  
ANISOU 3563  O   HOH A 818     2750   2902   3603    348   -491    337       O  
HETATM 3564  O   HOH A 819      46.287  75.935  73.524  0.64 26.37           O  
ANISOU 3564  O   HOH A 819     2916   3384   3719    -20   -186     31       O  
HETATM 3565  O   HOH A 820      50.667  43.348  54.178  0.57 35.46           O  
ANISOU 3565  O   HOH A 820     4056   4394   5023    499    102    -47       O  
HETATM 3566  O   HOH A 821      11.538  61.205  37.748  0.54 27.12           O  
ANISOU 3566  O   HOH A 821     4648   3031   2624   -489   -194    -21       O  
HETATM 3567  O   HOH A 822      42.739  38.749  55.357  0.57 27.65           O  
ANISOU 3567  O   HOH A 822     3446   3521   3539    424    603   -112       O  
HETATM 3568  O   HOH A 823      29.341  26.617  43.678  0.38 24.95           O  
ANISOU 3568  O   HOH A 823     3172   3339   2967    270   -702    814       O  
HETATM 3569  O   HOH A 824       8.576  36.565  32.267  0.47 45.91           O  
ANISOU 3569  O   HOH A 824     5738   5895   5811   -177    202    -54       O  
HETATM 3570  O   HOH A 825      26.992  58.964  31.659  0.48 31.14           O  
ANISOU 3570  O   HOH A 825     4036   3788   4009   -268   -109    103       O  
HETATM 3571  O   HOH A 826      11.145  46.781  68.267  0.68 40.75           O  
ANISOU 3571  O   HOH A 826     5148   5103   5231    188    469   -222       O  
HETATM 3572  O   HOH A 827      24.137  88.914  52.371  0.45 37.87           O  
ANISOU 3572  O   HOH A 827     4742   4630   5017    205    304     48       O  
HETATM 3573  O   HOH A 828       9.869  45.490  65.210  0.69 39.07           O  
ANISOU 3573  O   HOH A 828     5100   5053   4692   -114    567    311       O  
HETATM 3574  O   HOH A 829      34.978  31.597  59.496  0.66 36.56           O  
ANISOU 3574  O   HOH A 829     4531   4681   4678    312    368   -265       O  
HETATM 3575  O   HOH A 830      17.410  72.765  30.657  0.68 29.55           O  
ANISOU 3575  O   HOH A 830     3385   4010   3831    -86   -116   -134       O  
HETATM 3576  O   HOH A 831      26.404  82.800  43.118  0.51 30.71           O  
ANISOU 3576  O   HOH A 831     3761   3829   4079    102   -330    336       O  
HETATM 3577  O   HOH A 832      30.588  85.384  55.618  0.59 37.39           O  
ANISOU 3577  O   HOH A 832     4759   4707   4740     93    194   -221       O  
HETATM 3578  O   HOH A 833      56.742  62.036  51.465  0.56 39.66           O  
ANISOU 3578  O   HOH A 833     5036   4968   5067    -45    177    164       O  
HETATM 3579  O   HOH A 834      12.210  27.982  57.498  0.58 40.39           O  
ANISOU 3579  O   HOH A 834     4661   5266   5420    187    312   -201       O  
HETATM 3580  O   HOH A 835      52.677  62.806  43.396  0.48 31.99           O  
ANISOU 3580  O   HOH A 835     4365   4101   3690   -297    250     11       O  
HETATM 3581  O   HOH A 836      55.772  71.811  71.258  0.38 31.55           O  
ANISOU 3581  O   HOH A 836     4262   3843   3881   -102     52    160       O  
HETATM 3582  O   HOH A 837      28.678  31.184  44.645  0.60 25.80           O  
ANISOU 3582  O   HOH A 837     3026   3152   3626    589   -393    476       O  
HETATM 3583  O   HOH A 838      45.468  70.859  42.002  0.54 31.45           O  
ANISOU 3583  O   HOH A 838     4091   4171   3688   -316   -410    262       O  
HETATM 3584  O   HOH A 839      21.629  53.228  30.768  0.52 35.82           O  
ANISOU 3584  O   HOH A 839     4464   4674   4473    -70    545   -105       O  
HETATM 3585  O   HOH A 840       4.763  62.558  65.782  0.46 31.03           O  
ANISOU 3585  O   HOH A 840     3634   4271   3886     52    167     46       O  
HETATM 3586  O   HOH A 841      23.385  45.385  32.072  0.62 38.26           O  
ANISOU 3586  O   HOH A 841     4920   5014   4604    -30   1116   -973       O  
HETATM 3587  O   HOH A 842      23.218  70.200  32.585  0.69 35.57           O  
ANISOU 3587  O   HOH A 842     4773   4665   4077   -247   -496    236       O  
HETATM 3588  O   HOH A 843       6.445  44.864  61.324  0.36 29.85           O  
ANISOU 3588  O   HOH A 843     3751   3918   3673   -120     84   -154       O  
HETATM 3589  O   HOH A 844      -1.707  46.060  50.555  0.49 50.09           O  
ANISOU 3589  O   HOH A 844     6239   6392   6402     29     52     75       O  
HETATM 3590  O   HOH A 845      50.483  74.385  53.746  0.75 43.09           O  
ANISOU 3590  O   HOH A 845     5281   5580   5513   -454   -711    297       O  
HETATM 3591  O   HOH A 846      27.729  64.986  30.059  0.60 40.08           O  
ANISOU 3591  O   HOH A 846     5203   5054   4970    -62   -416     59       O  
HETATM 3592  O   HOH A 847       9.620  65.500  70.884  0.57 43.82           O  
ANISOU 3592  O   HOH A 847     5325   5753   5572    187    -34    335       O  
HETATM 3593  O   HOH A 848      14.469  49.965  33.808  0.74 35.03           O  
ANISOU 3593  O   HOH A 848     4786   4209   4316    160   -309   -139       O  
HETATM 3594  O   HOH A 849       7.479  61.319  69.314  0.51 34.34           O  
ANISOU 3594  O   HOH A 849     4011   4196   4842    638    722   -378       O  
HETATM 3595  O   HOH A 850      34.810  81.440  49.161  0.59 31.08           O  
ANISOU 3595  O   HOH A 850     4041   3983   3785    -66   -631    401       O  
HETATM 3596  O   HOH A 851      32.100  59.326  31.042  0.47 29.83           O  
ANISOU 3596  O   HOH A 851     3462   3971   3901     91    877   -391       O  
HETATM 3597  O   HOH A 852      50.384  73.658  63.897  0.55 34.80           O  
ANISOU 3597  O   HOH A 852     4162   4374   4685     65   -465    120       O  
HETATM 3598  O   HOH A 853      26.286  31.203  51.699  0.93 32.24           O  
ANISOU 3598  O   HOH A 853     3794   4531   3924    -75  -1048    814       O  
HETATM 3599  O   HOH A 854      41.153  40.491  56.303  0.83 32.90           O  
ANISOU 3599  O   HOH A 854     3607   4272   4621    317   -778    322       O  
HETATM 3600  O   HOH A 855      -1.457  44.642  43.063  0.91 37.47           O  
ANISOU 3600  O   HOH A 855     4223   5230   4783   -210   -670    -15       O  
HETATM 3601  O   HOH A 856      63.657  69.597  79.272  0.79 43.83           O  
ANISOU 3601  O   HOH A 856     5285   5397   5971    299   -109    190       O  
HETATM 3602  O   HOH A 857      49.567  42.916  58.415  0.85 37.92           O  
ANISOU 3602  O   HOH A 857     4774   5260   4373   -186    158     64       O  
HETATM 3603  O   HOH A 858      10.441  60.528  35.138  0.93 43.90           O  
ANISOU 3603  O   HOH A 858     5911   5369   5399     77  -1104    762       O  
HETATM 3604  O   HOH A 859      26.530  65.787  33.014  0.83 47.20           O  
ANISOU 3604  O   HOH A 859     5794   6255   5886   -130   -426    531       O  
HETATM 3605  O   HOH A 860      31.897  76.819  31.831  0.64 33.93           O  
ANISOU 3605  O   HOH A 860     4926   3862   4104    228   -375    264       O  
HETATM 3606  O   HOH A 861       2.086  50.389  53.237  0.76 54.29           O  
ANISOU 3606  O   HOH A 861     7037   6680   6912     52     35   -314       O  
HETATM 3607  O   HOH A 862      18.586  63.306  35.528  0.97 42.15           O  
ANISOU 3607  O   HOH A 862     5518   5160   5339   -273   -279     75       O  
HETATM 3608  O   HOH A 863      23.641  78.850  37.902  1.00 50.33           O  
ANISOU 3608  O   HOH A 863     6819   6395   5908    -17   -203   -195       O  
HETATM 3609  O   HOH A 864      46.567  73.228  47.700  1.00 46.34           O  
ANISOU 3609  O   HOH A 864     6382   5545   5681   -300    340    368       O  
HETATM 3610  O   HOH A 865      17.431  37.003  32.671  0.79 47.83           O  
ANISOU 3610  O   HOH A 865     6077   6175   5921    154    302    111       O  
HETATM 3611  O   HOH A 866      10.198  51.693  33.755  1.00 47.53           O  
ANISOU 3611  O   HOH A 866     6304   5905   5852   -175    211   -255       O  
HETATM 3612  O   HOH A 867      21.979  55.539  28.299  0.98 51.07           O  
ANISOU 3612  O   HOH A 867     6765   6540   6097   -144   -811    541       O  
HETATM 3613  O   HOH A 868      57.692  55.766  51.389  1.00 51.98           O  
ANISOU 3613  O   HOH A 868     6485   6568   6698   -149    110    -18       O  
CONECT 1380 1382                                                                
CONECT 1382 1380 1383                                                           
CONECT 1383 1382 1384 1386                                                      
CONECT 1384 1383 1385                                                           
CONECT 1385 1384 1388 1389                                                      
CONECT 1386 1383 1387 1390                                                      
CONECT 1387 1386                                                                
CONECT 1388 1385                                                                
CONECT 1389 1385                                                                
CONECT 1390 1386                                                                
MASTER      251    0    1   15   11    0    1    6 3476    1   10   30          
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.