CNRS Nantes University UFIP UFIP
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***  TRANSFERASE 15-JUL-19 6S9W  ***

elNémo ID: 210223120635125832

Job options:

ID        	=	 210223120635125832
JOBID     	=	 TRANSFERASE 15-JUL-19 6S9W
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    TRANSFERASE                             15-JUL-19   6S9W              
TITLE     CRYSTAL STRUCTURE OF AKT1 IN COMPLEX WITH COVALENT-ALLOSTERIC AKT     
TITLE    2 INHIBITOR 16A                                                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RAC-ALPHA SERINE/THREONINE-PROTEIN KINASE;                 
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: PROTEIN KINASE B,PKB,PROTEIN KINASE B ALPHA,PKB ALPHA,PROTO-
COMPND   5 ONCOGENE C-AKT,RAC-PK-ALPHA;                                         
COMPND   6 EC: 2.7.11.1;                                                        
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: AKT1, PKB, RAC;                                                
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108                                        
KEYWDS    AKT1, AKT2, AKT3, BORUSSERTIB, COVALENT-ALLOSTERIC, TRANSFERASE       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    I.LANDEL,M.P.MUELLER,D.RAUH                                           
REVDAT   2   25-DEC-19 6S9W    1       JRNL                                     
REVDAT   1   16-OCT-19 6S9W    0                                                
JRNL        AUTH   L.QUAMBUSCH,I.LANDEL,L.DEPTA,J.WEISNER,N.UHLENBROCK,         
JRNL        AUTH 2 M.P.MULLER,F.GLANEMANN,K.ALTHOFF,J.T.SIVEKE,D.RAUH           
JRNL        TITL   COVALENT-ALLOSTERIC INHIBITORS TO ACHIEVE AKT                
JRNL        TITL 2 ISOFORM-SELECTIVITY.                                         
JRNL        REF    ANGEW.CHEM.INT.ED.ENGL.       V.  58 18823 2019              
JRNL        REFN                   ESSN 1521-3773                               
JRNL        PMID   31584233                                                     
JRNL        DOI    10.1002/ANIE.201909857                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.14_3260                                     
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 45.67                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 91.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 19149                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.210                           
REMARK   3   R VALUE            (WORKING SET) : 0.207                           
REMARK   3   FREE R VALUE                     : 0.263                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 957                             
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 45.6700 -  4.3986    1.00     2979   156  0.1749 0.2161        
REMARK   3     2  4.3986 -  3.4917    0.84     2399   127  0.1885 0.2299        
REMARK   3     3  3.4917 -  3.0504    0.89     2504   131  0.2505 0.3629        
REMARK   3     4  3.0504 -  2.7716    1.00     2811   148  0.2418 0.3200        
REMARK   3     5  2.7716 -  2.5729    0.69     1933   102  0.2681 0.2984        
REMARK   3     6  2.5729 -  2.4213    1.00     2783   147  0.2686 0.3484        
REMARK   3     7  2.4213 -  2.3000    1.00     2783   146  0.2878 0.3681        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.350            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.820           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 70.96                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :   NULL           NULL                                  
REMARK   3   ANGLE     :   NULL           NULL                                  
REMARK   3   CHIRALITY :   NULL           NULL                                  
REMARK   3   PLANARITY :   NULL           NULL                                  
REMARK   3   DIHEDRAL  :   NULL           NULL                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: (CHAIN A)                                              
REMARK   3    ORIGIN FOR THE GROUP (A): -13.6844 -12.4833  15.0602              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2794 T22:   0.3448                                     
REMARK   3      T33:   0.3188 T12:   0.0162                                     
REMARK   3      T13:  -0.0366 T23:  -0.0304                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6097 L22:   2.0926                                     
REMARK   3      L33:   1.5394 L12:  -0.3338                                     
REMARK   3      L13:  -0.0697 L23:  -0.1139                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0424 S12:  -0.0353 S13:  -0.0853                       
REMARK   3      S21:   0.0261 S22:  -0.0012 S23:   0.0189                       
REMARK   3      S31:   0.0155 S32:   0.0600 S33:   0.0575                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6S9W COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-JUL-19.                  
REMARK 100 THE DEPOSITION ID IS D_1292102615.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-MAY-18                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X10SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.91886                            
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 19153                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 45.670                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.8                               
REMARK 200  DATA REDUNDANCY                : 12.70                              
REMARK 200  R MERGE                    (I) : 0.09800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 15.0600                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.40                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 12.90                              
REMARK 200  R MERGE FOR SHELL          (I) : 1.63700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 1.620                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 6HHG                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 44.08                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.25 MM NA-ACETATE, 3.75 MM NA           
REMARK 280  -CITRATE, 24% V/V PEG 2000 MME, PH 7.0, 3 MG/ML AKT1 (IN 25 MM      
REMARK 280  TRIS, 100 MM NACL, 10% V/V GLYCEROL, 5 MM DTT, PH 7.5), 1 UL        
REMARK 280  RESERVOIR + 1 UL PROTEIN SOLUTION, VAPOR DIFFUSION, HANGING DROP,   
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       35.03500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       45.67000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       35.51500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       45.67000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       35.03500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       35.51500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2                             
REMARK 350 SURFACE AREA OF THE COMPLEX: 20230 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     GLN A   113                                                      
REMARK 465     ALA A   114                                                      
REMARK 465     ALA A   115                                                      
REMARK 465     ALA A   116                                                      
REMARK 465     GLU A   117                                                      
REMARK 465     MET A   118                                                      
REMARK 465     ASP A   119                                                      
REMARK 465     PHE A   120                                                      
REMARK 465     ARG A   121                                                      
REMARK 465     SER A   122                                                      
REMARK 465     GLY A   123                                                      
REMARK 465     SER A   124                                                      
REMARK 465     PRO A   125                                                      
REMARK 465     SER A   126                                                      
REMARK 465     ASP A   127                                                      
REMARK 465     ASN A   128                                                      
REMARK 465     SER A   129                                                      
REMARK 465     GLY A   130                                                      
REMARK 465     ALA A   131                                                      
REMARK 465     GLU A   132                                                      
REMARK 465     GLU A   133                                                      
REMARK 465     MET A   134                                                      
REMARK 465     GLU A   135                                                      
REMARK 465     VAL A   136                                                      
REMARK 465     SER A   137                                                      
REMARK 465     LEU A   138                                                      
REMARK 465     ALA A   139                                                      
REMARK 465     LYS A   140                                                      
REMARK 465     PRO A   141                                                      
REMARK 465     ASP A   302                                                      
REMARK 465     GLY A   303                                                      
REMARK 465     GLN A   445                                                      
REMARK 465     MET A   446                                                      
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    TRP A  80      -98.78     55.62                                   
REMARK 500    ILE A 186      -66.52    -93.51                                   
REMARK 500    ASN A 204       51.84     37.49                                   
REMARK 500    ASN A 204       52.10     37.49                                   
REMARK 500    THR A 219     -162.69   -102.89                                   
REMARK 500    ARG A 243      -47.58     64.84                                   
REMARK 500    ARG A 273      -19.15     74.55                                   
REMARK 500    ASP A 398     -117.01     56.64                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue L1Z A 501                 
DBREF  6S9W A    2   446  UNP    P31749   AKT1_HUMAN       2    446             
SEQADV 6S9W GLY A    1  UNP  P31749              EXPRESSION TAG                 
SEQADV 6S9W ALA A  114  UNP  P31749    GLU   114 ENGINEERED MUTATION            
SEQADV 6S9W ALA A  115  UNP  P31749    GLU   115 ENGINEERED MUTATION            
SEQADV 6S9W ALA A  116  UNP  P31749    GLU   116 ENGINEERED MUTATION            
SEQRES   1 A  446  GLY SER ASP VAL ALA ILE VAL LYS GLU GLY TRP LEU HIS          
SEQRES   2 A  446  LYS ARG GLY GLU TYR ILE LYS THR TRP ARG PRO ARG TYR          
SEQRES   3 A  446  PHE LEU LEU LYS ASN ASP GLY THR PHE ILE GLY TYR LYS          
SEQRES   4 A  446  GLU ARG PRO GLN ASP VAL ASP GLN ARG GLU ALA PRO LEU          
SEQRES   5 A  446  ASN ASN PHE SER VAL ALA GLN CYS GLN LEU MET LYS THR          
SEQRES   6 A  446  GLU ARG PRO ARG PRO ASN THR PHE ILE ILE ARG CYS LEU          
SEQRES   7 A  446  GLN TRP THR THR VAL ILE GLU ARG THR PHE HIS VAL GLU          
SEQRES   8 A  446  THR PRO GLU GLU ARG GLU GLU TRP THR THR ALA ILE GLN          
SEQRES   9 A  446  THR VAL ALA ASP GLY LEU LYS LYS GLN ALA ALA ALA GLU          
SEQRES  10 A  446  MET ASP PHE ARG SER GLY SER PRO SER ASP ASN SER GLY          
SEQRES  11 A  446  ALA GLU GLU MET GLU VAL SER LEU ALA LYS PRO LYS HIS          
SEQRES  12 A  446  ARG VAL THR MET ASN GLU PHE GLU TYR LEU LYS LEU LEU          
SEQRES  13 A  446  GLY LYS GLY THR PHE GLY LYS VAL ILE LEU VAL LYS GLU          
SEQRES  14 A  446  LYS ALA THR GLY ARG TYR TYR ALA MET LYS ILE LEU LYS          
SEQRES  15 A  446  LYS GLU VAL ILE VAL ALA LYS ASP GLU VAL ALA HIS THR          
SEQRES  16 A  446  LEU THR GLU ASN ARG VAL LEU GLN ASN SER ARG HIS PRO          
SEQRES  17 A  446  PHE LEU THR ALA LEU LYS TYR SER PHE GLN THR HIS ASP          
SEQRES  18 A  446  ARG LEU CYS PHE VAL MET GLU TYR ALA ASN GLY GLY GLU          
SEQRES  19 A  446  LEU PHE PHE HIS LEU SER ARG GLU ARG VAL PHE SER GLU          
SEQRES  20 A  446  ASP ARG ALA ARG PHE TYR GLY ALA GLU ILE VAL SER ALA          
SEQRES  21 A  446  LEU ASP TYR LEU HIS SER GLU LYS ASN VAL VAL TYR ARG          
SEQRES  22 A  446  ASP LEU LYS LEU GLU ASN LEU MET LEU ASP LYS ASP GLY          
SEQRES  23 A  446  HIS ILE LYS ILE THR ASP PHE GLY LEU CYS LYS GLU GLY          
SEQRES  24 A  446  ILE LYS ASP GLY ALA THR MET LYS THR PHE CYS GLY THR          
SEQRES  25 A  446  PRO GLU TYR LEU ALA PRO GLU VAL LEU GLU ASP ASN ASP          
SEQRES  26 A  446  TYR GLY ARG ALA VAL ASP TRP TRP GLY LEU GLY VAL VAL          
SEQRES  27 A  446  MET TYR GLU MET MET CYS GLY ARG LEU PRO PHE TYR ASN          
SEQRES  28 A  446  GLN ASP HIS GLU LYS LEU PHE GLU LEU ILE LEU MET GLU          
SEQRES  29 A  446  GLU ILE ARG PHE PRO ARG THR LEU GLY PRO GLU ALA LYS          
SEQRES  30 A  446  SER LEU LEU SER GLY LEU LEU LYS LYS ASP PRO LYS GLN          
SEQRES  31 A  446  ARG LEU GLY GLY GLY SER GLU ASP ALA LYS GLU ILE MET          
SEQRES  32 A  446  GLN HIS ARG PHE PHE ALA GLY ILE VAL TRP GLN HIS VAL          
SEQRES  33 A  446  TYR GLU LYS LYS LEU SER PRO PRO PHE LYS PRO GLN VAL          
SEQRES  34 A  446  THR SER GLU THR ASP THR ARG TYR PHE ASP GLU GLU PHE          
SEQRES  35 A  446  THR ALA GLN MET                                              
HET    L1Z  A 501      42                                                       
HETNAM     L1Z ~{N}-[3-[1-[[4-(5-METHYL-6-OXIDANYLIDENE-3-PHENYL-               
HETNAM   2 L1Z  1~{H}-PYRAZIN-2-YL)PHENYL]METHYL]PIPERIDIN-4-YL]-2-             
HETNAM   3 L1Z  OXIDANYLIDENE-1~{H}-BENZIMIDAZOL-5-YL]PROPANAMIDE               
FORMUL   2  L1Z    C33 H34 N6 O3                                                
FORMUL   3  HOH   *12(H2 O)                                                     
HELIX    1 AA1 LEU A   52  SER A   56  5                                   5    
HELIX    2 AA2 THR A   92  LYS A  112  1                                  21    
HELIX    3 AA3 THR A  146  ASN A  148  5                                   3    
HELIX    4 AA4 LYS A  183  VAL A  187  1                                   5    
HELIX    5 AA5 LYS A  189  GLN A  203  1                                  15    
HELIX    6 AA6 GLU A  234  ARG A  243  1                                  10    
HELIX    7 AA7 SER A  246  GLU A  267  1                                  22    
HELIX    8 AA8 LYS A  276  GLU A  278  5                                   3    
HELIX    9 AA9 ALA A  317  GLU A  322  1                                   6    
HELIX   10 AB1 ARG A  328  GLY A  345  1                                  18    
HELIX   11 AB2 ASP A  353  MET A  363  1                                  11    
HELIX   12 AB3 GLY A  373  LEU A  384  1                                  12    
HELIX   13 AB4 ASP A  387  ARG A  391  5                                   5    
HELIX   14 AB5 ASP A  398  GLN A  404  1                                   7    
HELIX   15 AB6 HIS A  405  ALA A  409  5                                   5    
HELIX   16 AB7 VAL A  412  GLU A  418  1                                   7    
HELIX   17 AB8 THR A  435  ALA A  444  5                                  10    
SHEET    1 AA1 6 PHE A  35  TYR A  38  0                                        
SHEET    2 AA1 6 TRP A  22  LYS A  30 -1  N  LEU A  28   O  ILE A  36           
SHEET    3 AA1 6 ILE A   6  ARG A  15 -1  N  LEU A  12   O  ARG A  25           
SHEET    4 AA1 6 THR A  82  HIS A  89 -1  O  HIS A  89   N  HIS A  13           
SHEET    5 AA1 6 THR A  72  GLN A  79 -1  N  ILE A  75   O  ARG A  86           
SHEET    6 AA1 6 GLN A  61  THR A  65 -1  N  MET A  63   O  ILE A  74           
SHEET    1 AA2 5 PHE A 150  GLY A 159  0                                        
SHEET    2 AA2 5 GLY A 162  GLU A 169 -1  O  LEU A 166   N  LYS A 154           
SHEET    3 AA2 5 TYR A 175  LYS A 182 -1  O  TYR A 176   N  VAL A 167           
SHEET    4 AA2 5 ARG A 222  GLU A 228 -1  O  LEU A 223   N  LEU A 181           
SHEET    5 AA2 5 LEU A 213  GLN A 218 -1  N  TYR A 215   O  VAL A 226           
SHEET    1 AA3 2 LEU A 280  LEU A 282  0                                        
SHEET    2 AA3 2 ILE A 288  ILE A 290 -1  O  LYS A 289   N  MET A 281           
LINK         SG  CYS A 310                 CBL L1Z A 501     1555   1555  1.83  
CISPEP   1 ARG A   67    PRO A   68          0         3.27                     
SITE     1 AC1 13 GLU A  17  TRP A  80  THR A 211  TYR A 272                    
SITE     2 AC1 13 ARG A 273  ASP A 274  ILE A 290  ASP A 292                    
SITE     3 AC1 13 CYS A 296  LYS A 297  CYS A 310  HOH A 603                    
SITE     4 AC1 13 HOH A 608                                                     
CRYST1   70.070   71.030   91.340  90.00  90.00  90.00 P 21 21 21    4          
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      0.014271  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014079  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010948        0.00000                         
ATOM      1  N   ASP A   3     -33.070 -34.713  15.603  1.00109.58           N  
ANISOU    1  N   ASP A   3    12538  12116  16980  -1668     93   -202       N  
ATOM      2  CA  ASP A   3     -32.468 -35.897  16.203  1.00102.21           C  
ANISOU    2  CA  ASP A   3    11752  10981  16101  -1684    203   -108       C  
ATOM      3  C   ASP A   3     -31.071 -35.598  16.743  1.00 94.87           C  
ANISOU    3  C   ASP A   3    11010  10103  14934  -1495    267    -33       C  
ATOM      4  O   ASP A   3     -30.191 -36.457  16.722  1.00 87.29           O  
ANISOU    4  O   ASP A   3    10214   8993  13960  -1455    275    -27       O  
ATOM      5  CB  ASP A   3     -32.412 -37.043  15.188  1.00100.99           C  
ANISOU    5  CB  ASP A   3    11670  10616  16086  -1786     76   -256       C  
ATOM      6  CG  ASP A   3     -31.866 -36.605  13.838  1.00 99.38           C  
ANISOU    6  CG  ASP A   3    11535  10483  15742  -1713   -125   -462       C  
ATOM      7  OD1 ASP A   3     -31.541 -35.409  13.681  1.00 97.52           O  
ANISOU    7  OD1 ASP A   3    11286  10454  15312  -1590   -164   -480       O  
ATOM      8  OD2 ASP A   3     -31.767 -37.457  12.930  1.00100.49           O  
ANISOU    8  OD2 ASP A   3    11752  10467  15963  -1779   -239   -606       O  
ATOM      9  N   VAL A   4     -30.875 -34.372  17.227  1.00 90.11           N  
ANISOU    9  N   VAL A   4    10377   9709  14152  -1377    306     21       N  
ATOM     10  CA  VAL A   4     -29.587 -33.984  17.793  1.00 86.24           C  
ANISOU   10  CA  VAL A   4    10043   9286  13440  -1205    355     92       C  
ATOM     11  C   VAL A   4     -29.427 -34.646  19.155  1.00 87.57           C  
ANISOU   11  C   VAL A   4    10278   9365  13629  -1197    539    293       C  
ATOM     12  O   VAL A   4     -30.261 -34.469  20.051  1.00 93.28           O  
ANISOU   12  O   VAL A   4    10901  10132  14408  -1249    672    416       O  
ATOM     13  CB  VAL A   4     -29.466 -32.458  17.896  1.00 80.35           C  
ANISOU   13  CB  VAL A   4     9246   8776  12507  -1094    334     80       C  
ATOM     14  CG1 VAL A   4     -28.212 -32.078  18.665  1.00 72.65           C  
ANISOU   14  CG1 VAL A   4     8415   7867  11321   -935    395    169       C  
ATOM     15  CG2 VAL A   4     -29.447 -31.833  16.510  1.00 80.04           C  
ANISOU   15  CG2 VAL A   4     9175   8815  12421  -1082    149   -105       C  
ATOM     16  N   ALA A   5     -28.350 -35.411  19.319  1.00 82.83           N  
ANISOU   16  N   ALA A   5     9849   8643  12979  -1123    552    331       N  
ATOM     17  CA  ALA A   5     -28.094 -36.129  20.557  1.00 76.30           C  
ANISOU   17  CA  ALA A   5     9112   7718  12161  -1102    711    528       C  
ATOM     18  C   ALA A   5     -26.615 -36.035  20.903  1.00 75.91           C  
ANISOU   18  C   ALA A   5     9230   7701  11911   -923    700    572       C  
ATOM     19  O   ALA A   5     -25.774 -35.724  20.056  1.00 66.36           O  
ANISOU   19  O   ALA A   5     8073   6535  10607   -838    575    441       O  
ATOM     20  CB  ALA A   5     -28.524 -37.599  20.458  1.00 71.73           C  
ANISOU   20  CB  ALA A   5     8559   6876  11819  -1238    750    558       C  
ATOM     21  N   ILE A   6     -26.309 -36.310  22.167  1.00 76.71           N  
ANISOU   21  N   ILE A   6     9412   7786  11950   -864    833    763       N  
ATOM     22  CA  ILE A   6     -24.932 -36.302  22.648  1.00 68.96           C  
ANISOU   22  CA  ILE A   6     8581   6832  10791   -695    824    828       C  
ATOM     23  C   ILE A   6     -24.304 -37.657  22.351  1.00 69.20           C  
ANISOU   23  C   ILE A   6     8735   6627  10932   -685    807    838       C  
ATOM     24  O   ILE A   6     -24.815 -38.696  22.782  1.00 80.74           O  
ANISOU   24  O   ILE A   6    10225   7904  12551   -773    903    946       O  
ATOM     25  CB  ILE A   6     -24.874 -35.990  24.149  1.00 63.88           C  
ANISOU   25  CB  ILE A   6     7980   6281  10010   -626    960   1027       C  
ATOM     26  CG1 ILE A   6     -25.525 -34.640  24.447  1.00 60.85           C  
ANISOU   26  CG1 ILE A   6     7480   6119   9521   -629    985   1005       C  
ATOM     27  CG2 ILE A   6     -23.434 -36.011  24.640  1.00 61.43           C  
ANISOU   27  CG2 ILE A   6     7817   6002   9523   -452    926   1092       C  
ATOM     28  CD1 ILE A   6     -25.425 -34.240  25.901  1.00 68.37           C  
ANISOU   28  CD1 ILE A   6     8490   7179  10307   -549   1113   1179       C  
ATOM     29  N   VAL A   7     -23.196 -37.650  21.615  1.00 64.35           N  
ANISOU   29  N   VAL A   7     8194   6013  10244   -576    694    727       N  
ATOM     30  CA  VAL A   7     -22.482 -38.891  21.340  1.00 66.28           C  
ANISOU   30  CA  VAL A   7     8565   6038  10582   -536    680    730       C  
ATOM     31  C   VAL A   7     -21.426 -39.179  22.407  1.00 66.80           C  
ANISOU   31  C   VAL A   7     8755   6097  10530   -380    736    906       C  
ATOM     32  O   VAL A   7     -21.199 -40.343  22.753  1.00 70.41           O  
ANISOU   32  O   VAL A   7     9315   6348  11090   -368    791   1008       O  
ATOM     33  CB  VAL A   7     -21.867 -38.850  19.929  1.00 60.49           C  
ANISOU   33  CB  VAL A   7     7846   5293   9844   -496    541    514       C  
ATOM     34  CG1 VAL A   7     -21.134 -37.549  19.704  1.00 68.70           C  
ANISOU   34  CG1 VAL A   7     8851   6577  10674   -380    468    447       C  
ATOM     35  CG2 VAL A   7     -20.937 -40.034  19.692  1.00 56.34           C  
ANISOU   35  CG2 VAL A   7     7461   4558   9387   -413    532    514       C  
ATOM     36  N   LYS A   8     -20.800 -38.146  22.966  1.00 62.38           N  
ANISOU   36  N   LYS A   8     8188   5753   9759   -262    720    947       N  
ATOM     37  CA  LYS A   8     -19.846 -38.342  24.046  1.00 62.22           C  
ANISOU   37  CA  LYS A   8     8276   5751   9614   -116    756   1116       C  
ATOM     38  C   LYS A   8     -19.777 -37.077  24.888  1.00 63.34           C  
ANISOU   38  C   LYS A   8     8380   6142   9546    -59    768   1173       C  
ATOM     39  O   LYS A   8     -19.957 -35.964  24.384  1.00 60.21           O  
ANISOU   39  O   LYS A   8     7888   5912   9077    -78    708   1046       O  
ATOM     40  CB  LYS A   8     -18.454 -38.704  23.516  1.00 64.30           C  
ANISOU   40  CB  LYS A   8     8616   5969   9848     31    663   1056       C  
ATOM     41  CG  LYS A   8     -17.497 -39.213  24.585  1.00 68.45           C  
ANISOU   41  CG  LYS A   8     9255   6461  10290    181    691   1241       C  
ATOM     42  CD  LYS A   8     -16.174 -39.670  23.983  1.00 69.84           C  
ANISOU   42  CD  LYS A   8     9487   6576  10475    326    605   1177       C  
ATOM     43  CE  LYS A   8     -15.257 -40.265  25.043  1.00 73.54           C  
ANISOU   43  CE  LYS A   8    10063   6997  10881    481    623   1371       C  
ATOM     44  NZ  LYS A   8     -15.891 -41.428  25.725  1.00 79.46           N  
ANISOU   44  NZ  LYS A   8    10909   7526  11756    425    734   1542       N  
ATOM     45  N   GLU A   9     -19.520 -37.263  26.181  1.00 61.11           N  
ANISOU   45  N   GLU A   9     8181   5876   9161     14    844   1367       N  
ATOM     46  CA  GLU A   9     -19.363 -36.150  27.103  1.00 69.19           C  
ANISOU   46  CA  GLU A   9     9197   7123   9968     82    853   1426       C  
ATOM     47  C   GLU A   9     -18.495 -36.589  28.272  1.00 72.11           C  
ANISOU   47  C   GLU A   9     9701   7487  10209    219    874   1613       C  
ATOM     48  O   GLU A   9     -18.354 -37.782  28.556  1.00 73.47           O  
ANISOU   48  O   GLU A   9     9967   7473  10477    236    924   1737       O  
ATOM     49  CB  GLU A   9     -20.716 -35.629  27.602  1.00 72.86           C  
ANISOU   49  CB  GLU A   9     9586   7660  10436    -36    970   1466       C  
ATOM     50  CG  GLU A   9     -21.618 -36.697  28.203  1.00 74.66           C  
ANISOU   50  CG  GLU A   9     9849   7717  10803   -133   1124   1626       C  
ATOM     51  CD  GLU A   9     -22.918 -36.125  28.740  1.00 82.45           C  
ANISOU   51  CD  GLU A   9    10743   8794  11788   -239   1254   1670       C  
ATOM     52  OE1 GLU A   9     -22.871 -35.106  29.461  1.00 87.58           O  
ANISOU   52  OE1 GLU A   9    11394   9640  12242   -172   1275   1695       O  
ATOM     53  OE2 GLU A   9     -23.991 -36.685  28.432  1.00 84.26           O  
ANISOU   53  OE2 GLU A   9    10896   8901  12220   -388   1334   1674       O  
ATOM     54  N   GLY A  10     -17.917 -35.608  28.947  1.00 68.34           N  
ANISOU   54  N   GLY A  10     9237   7212   9517    318    828   1632       N  
ATOM     55  CA  GLY A  10     -17.038 -35.878  30.064  1.00 66.70           C  
ANISOU   55  CA  GLY A  10     9151   7034   9158    458    817   1797       C  
ATOM     56  C   GLY A  10     -16.171 -34.674  30.356  1.00 65.66           C  
ANISOU   56  C   GLY A  10     9003   7129   8815    561    702   1734       C  
ATOM     57  O   GLY A  10     -16.299 -33.618  29.735  1.00 60.40           O  
ANISOU   57  O   GLY A  10     8237   6589   8123    520    648   1575       O  
ATOM     58  N   TRP A  11     -15.275 -34.860  31.322  1.00 67.48           N  
ANISOU   58  N   TRP A  11     9335   7403   8899    697    660   1867       N  
ATOM     59  CA  TRP A  11     -14.386 -33.795  31.764  1.00 59.90           C  
ANISOU   59  CA  TRP A  11     8371   6653   7736    796    541   1825       C  
ATOM     60  C   TRP A  11     -13.093 -33.814  30.959  1.00 58.51           C  
ANISOU   60  C   TRP A  11     8143   6480   7606    886    390   1725       C  
ATOM     61  O   TRP A  11     -12.502 -34.877  30.740  1.00 66.65           O  
ANISOU   61  O   TRP A  11     9215   7368   8743    954    372   1786       O  
ATOM     62  CB  TRP A  11     -14.082 -33.928  33.257  1.00 62.47           C  
ANISOU   62  CB  TRP A  11     8831   7044   7861    898    556   2015       C  
ATOM     63  CG  TRP A  11     -15.168 -33.389  34.135  1.00 64.38           C  
ANISOU   63  CG  TRP A  11     9111   7373   7979    832    686   2076       C  
ATOM     64  CD1 TRP A  11     -16.161 -34.101  34.744  1.00 60.91           C  
ANISOU   64  CD1 TRP A  11     8741   6831   7572    773    859   2230       C  
ATOM     65  CD2 TRP A  11     -15.377 -32.018  34.498  1.00 60.62           C  
ANISOU   65  CD2 TRP A  11     8605   7098   7331    822    665   1982       C  
ATOM     66  NE1 TRP A  11     -16.973 -33.259  35.467  1.00 66.45           N  
ANISOU   66  NE1 TRP A  11     9452   7670   8128    733    955   2239       N  
ATOM     67  CE2 TRP A  11     -16.513 -31.976  35.332  1.00 65.89           C  
ANISOU   67  CE2 TRP A  11     9326   7781   7927    767    836   2083       C  
ATOM     68  CE3 TRP A  11     -14.713 -30.824  34.201  1.00 59.49           C  
ANISOU   68  CE3 TRP A  11     8396   7114   7094    854    525   1824       C  
ATOM     69  CZ2 TRP A  11     -16.998 -30.787  35.872  1.00 59.99           C  
ANISOU   69  CZ2 TRP A  11     8574   7205   7014    755    870   2022       C  
ATOM     70  CZ3 TRP A  11     -15.197 -29.645  34.737  1.00 62.80           C  
ANISOU   70  CZ3 TRP A  11     8815   7690   7355    832    551   1764       C  
ATOM     71  CH2 TRP A  11     -16.328 -29.636  35.563  1.00 64.11           C  
ANISOU   71  CH2 TRP A  11     9042   7870   7449    790    721   1859       C  
ATOM     72  N   LEU A  12     -12.665 -32.633  30.520  1.00 59.63           N  
ANISOU   72  N   LEU A  12     8196   6784   7678    886    293   1575       N  
ATOM     73  CA  LEU A  12     -11.418 -32.453  29.796  1.00 65.56           C  
ANISOU   73  CA  LEU A  12     8879   7573   8456    966    159   1477       C  
ATOM     74  C   LEU A  12     -10.597 -31.365  30.470  1.00 64.09           C  
ANISOU   74  C   LEU A  12     8680   7592   8080   1038     43   1460       C  
ATOM     75  O   LEU A  12     -11.055 -30.684  31.391  1.00 71.95           O  
ANISOU   75  O   LEU A  12     9723   8697   8918   1020     65   1498       O  
ATOM     76  CB  LEU A  12     -11.659 -32.067  28.328  1.00 63.77           C  
ANISOU   76  CB  LEU A  12     8540   7326   8362    878    151   1287       C  
ATOM     77  CG  LEU A  12     -12.424 -33.044  27.444  1.00 69.60           C  
ANISOU   77  CG  LEU A  12     9277   7869   9298    795    236   1256       C  
ATOM     78  CD1 LEU A  12     -12.494 -32.520  26.020  1.00 66.26           C  
ANISOU   78  CD1 LEU A  12     8752   7463   8960    729    200   1061       C  
ATOM     79  CD2 LEU A  12     -11.760 -34.399  27.484  1.00 73.84           C  
ANISOU   79  CD2 LEU A  12     9885   8238   9933    890    237   1352       C  
ATOM     80  N   HIS A  13      -9.370 -31.206  29.988  1.00 57.64           N  
ANISOU   80  N   HIS A  13     7795   6823   7284   1119    -79   1396       N  
ATOM     81  CA  HIS A  13      -8.535 -30.054  30.296  1.00 59.09           C  
ANISOU   81  CA  HIS A  13     7925   7194   7331   1159   -206   1333       C  
ATOM     82  C   HIS A  13      -8.327 -29.268  29.009  1.00 55.34           C  
ANISOU   82  C   HIS A  13     7321   6763   6944   1095   -239   1150       C  
ATOM     83  O   HIS A  13      -7.742 -29.784  28.051  1.00 61.20           O  
ANISOU   83  O   HIS A  13     8002   7431   7820   1127   -254   1100       O  
ATOM     84  CB  HIS A  13      -7.197 -30.485  30.897  1.00 67.01           C  
ANISOU   84  CB  HIS A  13     8940   8234   8285   1309   -328   1426       C  
ATOM     85  CG  HIS A  13      -7.297 -30.936  32.320  1.00 73.97           C  
ANISOU   85  CG  HIS A  13     9959   9127   9018   1381   -326   1606       C  
ATOM     86  ND1 HIS A  13      -7.493 -32.253  32.674  1.00 74.36           N  
ANISOU   86  ND1 HIS A  13    10108   9020   9126   1437   -254   1764       N  
ATOM     87  CD2 HIS A  13      -7.238 -30.239  33.479  1.00 75.56           C  
ANISOU   87  CD2 HIS A  13    10227   9474   9007   1407   -385   1652       C  
ATOM     88  CE1 HIS A  13      -7.545 -32.350  33.990  1.00 77.41           C  
ANISOU   88  CE1 HIS A  13    10616   9461   9334   1498   -265   1913       C  
ATOM     89  NE2 HIS A  13      -7.394 -31.142  34.503  1.00 75.79           N  
ANISOU   89  NE2 HIS A  13    10396   9444   8956   1483   -346   1843       N  
ATOM     90  N   LYS A  14      -8.818 -28.032  28.979  1.00 52.87           N  
ANISOU   90  N   LYS A  14     6974   6561   6552   1012   -242   1054       N  
ATOM     91  CA  LYS A  14      -8.731 -27.183  27.800  1.00 51.97           C  
ANISOU   91  CA  LYS A  14     6751   6490   6504    945   -266    893       C  
ATOM     92  C   LYS A  14      -7.815 -26.004  28.085  1.00 56.78           C  
ANISOU   92  C   LYS A  14     7306   7260   7009    968   -388    834       C  
ATOM     93  O   LYS A  14      -7.930 -25.358  29.133  1.00 59.17           O  
ANISOU   93  O   LYS A  14     7661   7658   7162    972   -423    863       O  
ATOM     94  CB  LYS A  14     -10.109 -26.674  27.370  1.00 62.22           C  
ANISOU   94  CB  LYS A  14     8045   7769   7826    822   -171    822       C  
ATOM     95  CG  LYS A  14     -10.073 -25.808  26.117  1.00 58.90           C  
ANISOU   95  CG  LYS A  14     7526   7387   7466    758   -196    667       C  
ATOM     96  CD  LYS A  14     -11.250 -24.850  26.067  1.00 66.50           C  
ANISOU   96  CD  LYS A  14     8482   8394   8392    661   -144    604       C  
ATOM     97  CE  LYS A  14     -11.057 -23.807  24.981  1.00 71.63           C  
ANISOU   97  CE  LYS A  14     9046   9100   9069    613   -189    467       C  
ATOM     98  NZ  LYS A  14     -12.045 -22.700  25.096  1.00 87.44           N  
ANISOU   98  NZ  LYS A  14    11044  11162  11018    542   -159    412       N  
ATOM     99  N   ARG A  15      -6.915 -25.726  27.151  1.00 53.57           N  
ANISOU   99  N   ARG A  15     6794   6880   6682    980   -448    747       N  
ATOM    100  CA  ARG A  15      -6.029 -24.582  27.277  1.00 59.12           C  
ANISOU  100  CA  ARG A  15     7423   7722   7318    982   -561    682       C  
ATOM    101  C   ARG A  15      -6.765 -23.309  26.881  1.00 51.26           C  
ANISOU  101  C   ARG A  15     6409   6780   6289    871   -536    570       C  
ATOM    102  O   ARG A  15      -7.514 -23.288  25.900  1.00 48.76           O  
ANISOU  102  O   ARG A  15     6073   6400   6055    803   -455    506       O  
ATOM    103  CB  ARG A  15      -4.791 -24.776  26.406  1.00 55.92           C  
ANISOU  103  CB  ARG A  15     6901   7323   7023   1034   -616    642       C  
ATOM    104  CG  ARG A  15      -3.591 -23.970  26.851  1.00 65.24           C  
ANISOU  104  CG  ARG A  15     8000   8640   8150   1066   -753    624       C  
ATOM    105  CD  ARG A  15      -2.390 -24.310  25.994  1.00 71.19           C  
ANISOU  105  CD  ARG A  15     8623   9393   9030   1127   -783    601       C  
ATOM    106  NE  ARG A  15      -2.628 -23.984  24.592  1.00 73.67           N  
ANISOU  106  NE  ARG A  15     8879   9672   9439   1056   -700    495       N  
ATOM    107  CZ  ARG A  15      -1.766 -24.232  23.613  1.00 81.20           C  
ANISOU  107  CZ  ARG A  15     9728  10619  10505   1095   -685    457       C  
ATOM    108  NH1 ARG A  15      -2.067 -23.899  22.366  1.00 82.96           N  
ANISOU  108  NH1 ARG A  15     9920  10816  10785   1029   -606    364       N  
ATOM    109  NH2 ARG A  15      -0.606 -24.815  23.880  1.00 86.38           N  
ANISOU  109  NH2 ARG A  15    10311  11298  11213   1208   -747    515       N  
ATOM    110  N   GLY A  16      -6.554 -22.251  27.659  1.00 55.31           N  
ANISOU  110  N   GLY A  16     6933   7404   6679    856   -613    544       N  
ATOM    111  CA  GLY A  16      -7.244 -21.003  27.385  1.00 59.20           C  
ANISOU  111  CA  GLY A  16     7418   7937   7137    763   -591    443       C  
ATOM    112  C   GLY A  16      -6.851 -20.444  26.029  1.00 59.04           C  
ANISOU  112  C   GLY A  16     7290   7916   7226    712   -598    342       C  
ATOM    113  O   GLY A  16      -5.701 -20.553  25.598  1.00 57.02           O  
ANISOU  113  O   GLY A  16     6950   7685   7032    747   -660    332       O  
ATOM    114  N   GLU A  17      -7.826 -19.844  25.350  1.00 73.56           N  
ANISOU  114  N   GLU A  17     9130   9729   9091    633   -529    272       N  
ATOM    115  CA  GLU A  17      -7.576 -19.360  23.998  1.00 79.36           C  
ANISOU  115  CA  GLU A  17     9781  10455   9916    587   -522    187       C  
ATOM    116  C   GLU A  17      -6.816 -18.039  24.007  1.00 80.68           C  
ANISOU  116  C   GLU A  17     9894  10709  10050    552   -605    123       C  
ATOM    117  O   GLU A  17      -5.957 -17.811  23.149  1.00 81.10           O  
ANISOU  117  O   GLU A  17     9860  10779  10174    543   -628     87       O  
ATOM    118  CB  GLU A  17      -8.897 -19.234  23.237  1.00 86.76           C  
ANISOU  118  CB  GLU A  17    10739  11333  10893    522   -432    142       C  
ATOM    119  CG  GLU A  17      -9.523 -20.581  22.896  1.00 96.60           C  
ANISOU  119  CG  GLU A  17    12013  12477  12214    536   -355    186       C  
ATOM    120  CD  GLU A  17     -10.989 -20.470  22.532  1.00101.76           C  
ANISOU  120  CD  GLU A  17    12689  13082  12893    470   -280    157       C  
ATOM    121  OE1 GLU A  17     -11.582 -19.401  22.788  1.00104.52           O  
ANISOU  121  OE1 GLU A  17    13045  13482  13187    430   -280    120       O  
ATOM    122  OE2 GLU A  17     -11.550 -21.447  21.995  1.00102.42           O  
ANISOU  122  OE2 GLU A  17    12780  13075  13059    458   -225    166       O  
ATOM    123  N   TYR A  18      -7.100 -17.166  24.975  1.00 76.81           N  
ANISOU  123  N   TYR A  18     9458  10272   9456    531   -646    107       N  
ATOM    124  CA  TYR A  18      -6.404 -15.891  25.101  1.00 76.90           C  
ANISOU  124  CA  TYR A  18     9430  10351   9438    490   -735     41       C  
ATOM    125  C   TYR A  18      -5.506 -15.803  26.323  1.00 77.25           C  
ANISOU  125  C   TYR A  18     9486  10469   9395    532   -853     67       C  
ATOM    126  O   TYR A  18      -4.485 -15.114  26.275  1.00 77.89           O  
ANISOU  126  O   TYR A  18     9493  10605   9498    506   -949     25       O  
ATOM    127  CB  TYR A  18      -7.409 -14.735  25.140  1.00 81.24           C  
ANISOU  127  CB  TYR A  18    10034  10893   9941    427   -701    -27       C  
ATOM    128  CG  TYR A  18      -8.276 -14.660  23.904  1.00 82.95           C  
ANISOU  128  CG  TYR A  18    10231  11048  10239    385   -609    -58       C  
ATOM    129  CD1 TYR A  18      -9.458 -15.381  23.820  1.00 83.83           C  
ANISOU  129  CD1 TYR A  18    10385  11105  10361    394   -517    -27       C  
ATOM    130  CD2 TYR A  18      -7.910 -13.875  22.815  1.00 84.38           C  
ANISOU  130  CD2 TYR A  18    10348  11225  10487    333   -617   -114       C  
ATOM    131  CE1 TYR A  18     -10.252 -15.322  22.694  1.00 86.83           C  
ANISOU  131  CE1 TYR A  18    10743  11436  10814    356   -453    -60       C  
ATOM    132  CE2 TYR A  18      -8.705 -13.810  21.680  1.00 86.14           C  
ANISOU  132  CE2 TYR A  18    10564  11399  10768    302   -545   -139       C  
ATOM    133  CZ  TYR A  18      -9.876 -14.536  21.626  1.00 83.74           C  
ANISOU  133  CZ  TYR A  18    10299  11047  10470    315   -473   -117       C  
ATOM    134  OH  TYR A  18     -10.679 -14.483  20.505  1.00 73.25           O  
ANISOU  134  OH  TYR A  18     8959   9677   9197    285   -422   -146       O  
ATOM    135  N   ILE A  19      -5.858 -16.471  27.415  1.00 74.85           N  
ANISOU  135  N   ILE A  19     9275  10174   8993    592   -853    137       N  
ATOM    136  CA  ILE A  19      -4.967 -16.632  28.557  1.00 80.36           C  
ANISOU  136  CA  ILE A  19     9991  10944   9597    651   -975    180       C  
ATOM    137  C   ILE A  19      -4.584 -18.107  28.615  1.00 80.35           C  
ANISOU  137  C   ILE A  19     9980  10912   9639    743   -962    292       C  
ATOM    138  O   ILE A  19      -5.416 -18.969  28.919  1.00 82.35           O  
ANISOU  138  O   ILE A  19    10319  11107   9864    777   -872    366       O  
ATOM    139  CB  ILE A  19      -5.606 -16.139  29.863  1.00 89.21           C  
ANISOU  139  CB  ILE A  19    11247  12107  10541    659   -993    175       C  
ATOM    140  CG1 ILE A  19      -4.715 -16.483  31.059  1.00 94.19           C  
ANISOU  140  CG1 ILE A  19    11914  12817  11056    735  -1127    232       C  
ATOM    141  CG2 ILE A  19      -7.028 -16.668  30.022  1.00 92.66           C  
ANISOU  141  CG2 ILE A  19    11782  12482  10943    668   -842    224       C  
ATOM    142  CD1 ILE A  19      -5.106 -15.767  32.336  1.00 97.70           C  
ANISOU  142  CD1 ILE A  19    12494  13323  11305    739  -1173    200       C  
ATOM    143  N   LYS A  20      -3.321 -18.398  28.301  1.00 84.96           N  
ANISOU  143  N   LYS A  20    10451  11526  10304    781  -1047    305       N  
ATOM    144  CA  LYS A  20      -2.871 -19.757  28.001  1.00 89.03           C  
ANISOU  144  CA  LYS A  20    10930  11991  10906    870  -1021    395       C  
ATOM    145  C   LYS A  20      -2.574 -20.506  29.299  1.00 86.70           C  
ANISOU  145  C   LYS A  20    10712  11725  10504    971  -1097    505       C  
ATOM    146  O   LYS A  20      -1.426 -20.655  29.726  1.00 97.56           O  
ANISOU  146  O   LYS A  20    12021  13169  11880   1037  -1226    539       O  
ATOM    147  CB  LYS A  20      -1.656 -19.713  27.081  1.00100.66           C  
ANISOU  147  CB  LYS A  20    12241  13488  12518    879  -1064    361       C  
ATOM    148  CG  LYS A  20      -1.139 -21.083  26.663  1.00107.86           C  
ANISOU  148  CG  LYS A  20    13108  14339  13533    982  -1029    439       C  
ATOM    149  CD  LYS A  20       0.019 -20.987  25.674  1.00109.51           C  
ANISOU  149  CD  LYS A  20    13149  14578  13883    994  -1045    398       C  
ATOM    150  CE  LYS A  20       0.722 -22.336  25.522  1.00110.44           C  
ANISOU  150  CE  LYS A  20    13221  14649  14093   1125  -1035    480       C  
ATOM    151  NZ  LYS A  20       1.763 -22.357  24.446  1.00110.42           N  
ANISOU  151  NZ  LYS A  20    13054  14666  14236   1148  -1013    440       N  
ATOM    152  N   THR A  21      -3.642 -20.983  29.938  1.00 74.22           N  
ANISOU  152  N   THR A  21     9271  10097   8832    985  -1014    570       N  
ATOM    153  CA  THR A  21      -3.543 -21.885  31.077  1.00 71.52           C  
ANISOU  153  CA  THR A  21     9028   9759   8388   1086  -1048    701       C  
ATOM    154  C   THR A  21      -4.605 -22.964  30.931  1.00 70.53           C  
ANISOU  154  C   THR A  21     8991   9507   8301   1098   -890    786       C  
ATOM    155  O   THR A  21      -5.661 -22.738  30.337  1.00 73.01           O  
ANISOU  155  O   THR A  21     9321   9762   8659   1014   -769    733       O  
ATOM    156  CB  THR A  21      -3.725 -21.167  32.429  1.00 75.75           C  
ANISOU  156  CB  THR A  21     9677  10394   8712   1088  -1127    703       C  
ATOM    157  OG1 THR A  21      -5.035 -20.589  32.496  1.00 79.01           O  
ANISOU  157  OG1 THR A  21    10177  10782   9061   1011  -1005    654       O  
ATOM    158  CG2 THR A  21      -2.676 -20.078  32.628  1.00 73.76           C  
ANISOU  158  CG2 THR A  21     9340  10258   8426   1064  -1300    608       C  
ATOM    159  N   TRP A  22      -4.320 -24.141  31.481  1.00 63.09           N  
ANISOU  159  N   TRP A  22     8103   8518   7350   1200   -898    922       N  
ATOM    160  CA  TRP A  22      -5.252 -25.257  31.402  1.00 67.28           C  
ANISOU  160  CA  TRP A  22     8719   8912   7931   1209   -752   1015       C  
ATOM    161  C   TRP A  22      -6.360 -25.106  32.434  1.00 72.03           C  
ANISOU  161  C   TRP A  22     9465   9526   8376   1181   -674   1074       C  
ATOM    162  O   TRP A  22      -6.125 -24.655  33.559  1.00 82.27           O  
ANISOU  162  O   TRP A  22    10837  10928   9493   1221   -755   1107       O  
ATOM    163  CB  TRP A  22      -4.520 -26.584  31.609  1.00 62.61           C  
ANISOU  163  CB  TRP A  22     8141   8248   7398   1334   -783   1148       C  
ATOM    164  CG  TRP A  22      -3.458 -26.835  30.581  1.00 66.47           C  
ANISOU  164  CG  TRP A  22     8486   8719   8052   1376   -836   1094       C  
ATOM    165  CD1 TRP A  22      -2.149 -26.456  30.646  1.00 68.78           C  
ANISOU  165  CD1 TRP A  22     8668   9117   8349   1438   -984   1070       C  
ATOM    166  CD2 TRP A  22      -3.616 -27.515  29.329  1.00 60.49           C  
ANISOU  166  CD2 TRP A  22     7676   7831   7477   1361   -736   1053       C  
ATOM    167  NE1 TRP A  22      -1.482 -26.858  29.514  1.00 69.22           N  
ANISOU  167  NE1 TRP A  22     8600   9119   8581   1467   -966   1024       N  
ATOM    168  CE2 TRP A  22      -2.360 -27.511  28.690  1.00 59.79           C  
ANISOU  168  CE2 TRP A  22     7449   7779   7488   1424   -815   1008       C  
ATOM    169  CE3 TRP A  22      -4.698 -28.129  28.688  1.00 55.90           C  
ANISOU  169  CE3 TRP A  22     7148   7107   6985   1298   -590   1045       C  
ATOM    170  CZ2 TRP A  22      -2.154 -28.098  27.442  1.00 52.25           C  
ANISOU  170  CZ2 TRP A  22     6425   6725   6701   1437   -742    954       C  
ATOM    171  CZ3 TRP A  22      -4.492 -28.709  27.446  1.00 55.20           C  
ANISOU  171  CZ3 TRP A  22     6994   6916   7063   1304   -537    983       C  
ATOM    172  CH2 TRP A  22      -3.230 -28.690  26.837  1.00 53.74           C  
ANISOU  172  CH2 TRP A  22     6688   6772   6957   1377   -607    938       C  
ATOM    173  N   ARG A  23      -7.577 -25.483  32.042  1.00 75.53           N  
ANISOU  173  N   ARG A  23     9945   9866   8888   1113   -515   1084       N  
ATOM    174  CA  ARG A  23      -8.727 -25.427  32.927  1.00 78.84           C  
ANISOU  174  CA  ARG A  23    10484  10287   9185   1083   -407   1147       C  
ATOM    175  C   ARG A  23      -9.590 -26.665  32.731  1.00 74.05           C  
ANISOU  175  C   ARG A  23     9923   9524   8690   1066   -257   1252       C  
ATOM    176  O   ARG A  23      -9.787 -27.111  31.590  1.00 74.16           O  
ANISOU  176  O   ARG A  23     9860   9430   8887   1018   -209   1200       O  
ATOM    177  CB  ARG A  23      -9.575 -24.173  32.678  1.00 83.53           C  
ANISOU  177  CB  ARG A  23    11051  10940   9745    981   -357   1015       C  
ATOM    178  CG  ARG A  23      -9.045 -22.914  33.333  1.00 88.46           C  
ANISOU  178  CG  ARG A  23    11691  11712  10208    992   -477    935       C  
ATOM    179  CD  ARG A  23     -10.111 -21.835  33.330  1.00 90.96           C  
ANISOU  179  CD  ARG A  23    12022  12063  10476    910   -394    837       C  
ATOM    180  NE  ARG A  23      -9.606 -20.552  33.804  1.00 96.65           N  
ANISOU  180  NE  ARG A  23    12754  12903  11065    909   -510    733       N  
ATOM    181  CZ  ARG A  23      -8.986 -19.669  33.031  1.00101.26           C  
ANISOU  181  CZ  ARG A  23    13235  13518  11723    863   -604    607       C  
ATOM    182  NH1 ARG A  23      -8.792 -19.936  31.748  1.00105.35           N  
ANISOU  182  NH1 ARG A  23    13634  13967  12426    825   -591    571       N  
ATOM    183  NH2 ARG A  23      -8.556 -18.523  33.538  1.00101.65           N  
ANISOU  183  NH2 ARG A  23    13305  13660  11656    855   -710    515       N  
ATOM    184  N   PRO A  24     -10.119 -27.233  33.815  1.00 68.20           N  
ANISOU  184  N   PRO A  24     9310   8762   7840   1100   -179   1398       N  
ATOM    185  CA  PRO A  24     -11.069 -28.346  33.675  1.00 64.96           C  
ANISOU  185  CA  PRO A  24     8942   8193   7545   1061    -20   1501       C  
ATOM    186  C   PRO A  24     -12.391 -27.857  33.100  1.00 65.11           C  
ANISOU  186  C   PRO A  24     8908   8187   7642    931    109   1410       C  
ATOM    187  O   PRO A  24     -12.968 -26.877  33.577  1.00 62.36           O  
ANISOU  187  O   PRO A  24     8576   7944   7173    896    142   1362       O  
ATOM    188  CB  PRO A  24     -11.231 -28.856  35.110  1.00 63.41           C  
ANISOU  188  CB  PRO A  24     8904   8014   7177   1133     26   1685       C  
ATOM    189  CG  PRO A  24     -10.943 -27.653  35.960  1.00 56.84           C  
ANISOU  189  CG  PRO A  24     8113   7367   6116   1164    -61   1630       C  
ATOM    190  CD  PRO A  24      -9.881 -26.876  35.225  1.00 63.03           C  
ANISOU  190  CD  PRO A  24     8775   8227   6945   1172   -231   1476       C  
ATOM    191  N   ARG A  25     -12.870 -28.550  32.070  1.00 64.91           N  
ANISOU  191  N   ARG A  25     8819   8020   7822    863    177   1384       N  
ATOM    192  CA  ARG A  25     -14.124 -28.200  31.421  1.00 61.01           C  
ANISOU  192  CA  ARG A  25     8258   7495   7429    739    284   1300       C  
ATOM    193  C   ARG A  25     -14.904 -29.467  31.110  1.00 63.57           C  
ANISOU  193  C   ARG A  25     8593   7637   7923    681    404   1383       C  
ATOM    194  O   ARG A  25     -14.328 -30.508  30.782  1.00 69.10           O  
ANISOU  194  O   ARG A  25     9315   8215   8725    722    377   1434       O  
ATOM    195  CB  ARG A  25     -13.892 -27.401  30.132  1.00 55.38           C  
ANISOU  195  CB  ARG A  25     7421   6816   6805    691    204   1116       C  
ATOM    196  CG  ARG A  25     -13.410 -25.979  30.355  1.00 54.18           C  
ANISOU  196  CG  ARG A  25     7245   6828   6511    711    109   1018       C  
ATOM    197  CD  ARG A  25     -14.474 -25.150  31.048  1.00 57.11           C  
ANISOU  197  CD  ARG A  25     7646   7276   6778    667    198   1010       C  
ATOM    198  NE  ARG A  25     -14.068 -23.761  31.220  1.00 59.26           N  
ANISOU  198  NE  ARG A  25     7905   7685   6927    681    109    902       N  
ATOM    199  CZ  ARG A  25     -13.530 -23.273  32.332  1.00 63.76           C  
ANISOU  199  CZ  ARG A  25     8559   8359   7307    749     50    932       C  
ATOM    200  NH1 ARG A  25     -13.336 -24.064  33.378  1.00 59.00           N  
ANISOU  200  NH1 ARG A  25     8066   7751   6602    818     72   1077       N  
ATOM    201  NH2 ARG A  25     -13.192 -21.992  32.400  1.00 64.48           N  
ANISOU  201  NH2 ARG A  25     8635   8556   7308    747    -34    817       N  
ATOM    202  N   TYR A  26     -16.225 -29.370  31.221  1.00 63.05           N  
ANISOU  202  N   TYR A  26     8508   7550   7897    584    538   1394       N  
ATOM    203  CA  TYR A  26     -17.120 -30.467  30.881  1.00 61.70           C  
ANISOU  203  CA  TYR A  26     8327   7208   7910    498    655   1457       C  
ATOM    204  C   TYR A  26     -17.601 -30.245  29.453  1.00 64.29           C  
ANISOU  204  C   TYR A  26     8526   7489   8411    399    629   1290       C  
ATOM    205  O   TYR A  26     -18.328 -29.285  29.180  1.00 64.22           O  
ANISOU  205  O   TYR A  26     8438   7570   8393    336    646   1194       O  
ATOM    206  CB  TYR A  26     -18.288 -30.548  31.861  1.00 55.99           C  
ANISOU  206  CB  TYR A  26     7643   6489   7140    447    824   1578       C  
ATOM    207  CG  TYR A  26     -19.064 -31.836  31.743  1.00 59.93           C  
ANISOU  207  CG  TYR A  26     8150   6797   7825    364    948   1684       C  
ATOM    208  CD1 TYR A  26     -20.236 -31.899  31.003  1.00 67.31           C  
ANISOU  208  CD1 TYR A  26     8970   7663   8942    226   1025   1614       C  
ATOM    209  CD2 TYR A  26     -18.610 -32.995  32.354  1.00 58.86           C  
ANISOU  209  CD2 TYR A  26     8133   6539   7691    422    980   1854       C  
ATOM    210  CE1 TYR A  26     -20.941 -33.080  30.886  1.00 73.83           C  
ANISOU  210  CE1 TYR A  26     9795   8303   9954    134   1131   1703       C  
ATOM    211  CE2 TYR A  26     -19.305 -34.179  32.241  1.00 70.82           C  
ANISOU  211  CE2 TYR A  26     9660   7859   9390    338   1095   1952       C  
ATOM    212  CZ  TYR A  26     -20.471 -34.216  31.507  1.00 78.14           C  
ANISOU  212  CZ  TYR A  26    10467   8718  10504    187   1170   1872       C  
ATOM    213  OH  TYR A  26     -21.164 -35.398  31.395  1.00 83.93           O  
ANISOU  213  OH  TYR A  26    11206   9248  11435     88   1278   1964       O  
ATOM    214  N   PHE A  27     -17.190 -31.124  28.544  1.00 65.23           N  
ANISOU  214  N   PHE A  27     8632   7470   8681    392    583   1255       N  
ATOM    215  CA  PHE A  27     -17.423 -30.942  27.118  1.00 61.89           C  
ANISOU  215  CA  PHE A  27     8107   7011   8396    318    530   1087       C  
ATOM    216  C   PHE A  27     -18.524 -31.863  26.614  1.00 56.66           C  
ANISOU  216  C   PHE A  27     7414   6183   7932    197    617   1092       C  
ATOM    217  O   PHE A  27     -18.641 -33.011  27.052  1.00 60.09           O  
ANISOU  217  O   PHE A  27     7918   6469   8443    191    688   1217       O  
ATOM    218  CB  PHE A  27     -16.145 -31.190  26.318  1.00 63.73           C  
ANISOU  218  CB  PHE A  27     8345   7217   8653    399    413   1013       C  
ATOM    219  CG  PHE A  27     -15.358 -29.948  26.048  1.00 63.49           C  
ANISOU  219  CG  PHE A  27     8266   7356   8502    452    307    908       C  
ATOM    220  CD1 PHE A  27     -14.490 -29.445  26.999  1.00 64.65           C  
ANISOU  220  CD1 PHE A  27     8457   7621   8486    550    256    972       C  
ATOM    221  CD2 PHE A  27     -15.491 -29.275  24.845  1.00 61.80           C  
ANISOU  221  CD2 PHE A  27     7964   7180   8337    399    256    749       C  
ATOM    222  CE1 PHE A  27     -13.767 -28.297  26.757  1.00 63.29           C  
ANISOU  222  CE1 PHE A  27     8234   7592   8220    584    158    875       C  
ATOM    223  CE2 PHE A  27     -14.769 -28.127  24.596  1.00 61.31           C  
ANISOU  223  CE2 PHE A  27     7861   7261   8174    439    169    665       C  
ATOM    224  CZ  PHE A  27     -13.907 -27.635  25.555  1.00 62.18           C  
ANISOU  224  CZ  PHE A  27     8008   7479   8141    526    122    725       C  
ATOM    225  N   LEU A  28     -19.314 -31.348  25.675  1.00 59.98           N  
ANISOU  225  N   LEU A  28     7728   6624   8436    100    602    957       N  
ATOM    226  CA  LEU A  28     -20.400 -32.081  25.040  1.00 54.64           C  
ANISOU  226  CA  LEU A  28     6996   5807   7959    -31    654    928       C  
ATOM    227  C   LEU A  28     -20.093 -32.229  23.558  1.00 56.35           C  
ANISOU  227  C   LEU A  28     7174   5965   8272    -53    545    759       C  
ATOM    228  O   LEU A  28     -19.892 -31.230  22.861  1.00 60.10           O  
ANISOU  228  O   LEU A  28     7591   6562   8682    -39    462    634       O  
ATOM    229  CB  LEU A  28     -21.735 -31.360  25.227  1.00 60.79           C  
ANISOU  229  CB  LEU A  28     7672   6667   8759   -128    728    915       C  
ATOM    230  CG  LEU A  28     -22.625 -31.762  26.401  1.00 72.35           C  
ANISOU  230  CG  LEU A  28     9149   8099  10240   -175    890   1080       C  
ATOM    231  CD1 LEU A  28     -21.878 -31.670  27.721  1.00 75.74           C  
ANISOU  231  CD1 LEU A  28     9703   8600  10476    -55    933   1225       C  
ATOM    232  CD2 LEU A  28     -23.862 -30.878  26.420  1.00 76.23           C  
ANISOU  232  CD2 LEU A  28     9513   8696  10755   -254    951   1037       C  
ATOM    233  N   LEU A  29     -20.060 -33.467  23.081  1.00 58.63           N  
ANISOU  233  N   LEU A  29     7504   6063   8710    -87    549    758       N  
ATOM    234  CA  LEU A  29     -19.934 -33.760  21.661  1.00 58.88           C  
ANISOU  234  CA  LEU A  29     7512   6017   8841   -120    460    592       C  
ATOM    235  C   LEU A  29     -21.290 -34.232  21.156  1.00 60.87           C  
ANISOU  235  C   LEU A  29     7693   6161   9273   -281    489    543       C  
ATOM    236  O   LEU A  29     -21.851 -35.197  21.686  1.00 70.99           O  
ANISOU  236  O   LEU A  29     9002   7293  10680   -350    578    647       O  
ATOM    237  CB  LEU A  29     -18.858 -34.816  21.409  1.00 56.40           C  
ANISOU  237  CB  LEU A  29     7302   5559   8570    -32    434    601       C  
ATOM    238  CG  LEU A  29     -18.535 -35.109  19.942  1.00 56.84           C  
ANISOU  238  CG  LEU A  29     7356   5543   8696    -38    346    421       C  
ATOM    239  CD1 LEU A  29     -17.989 -33.864  19.251  1.00 56.01           C  
ANISOU  239  CD1 LEU A  29     7197   5630   8455     15    260    301       C  
ATOM    240  CD2 LEU A  29     -17.564 -36.277  19.821  1.00 46.43           C  
ANISOU  240  CD2 LEU A  29     6145   4057   7440     55    346    443       C  
ATOM    241  N   LYS A  30     -21.822 -33.544  20.151  1.00 55.76           N  
ANISOU  241  N   LYS A  30     6954   5589   8643   -344    412    392       N  
ATOM    242  CA  LYS A  30     -23.133 -33.852  19.603  1.00 62.27           C  
ANISOU  242  CA  LYS A  30     7687   6338   9635   -498    413    329       C  
ATOM    243  C   LYS A  30     -23.008 -34.277  18.145  1.00 65.05           C  
ANISOU  243  C   LYS A  30     8051   6602  10064   -532    297    149       C  
ATOM    244  O   LYS A  30     -22.028 -33.960  17.465  1.00 65.39           O  
ANISOU  244  O   LYS A  30     8145   6698  10001   -435    219     58       O  
ATOM    245  CB  LYS A  30     -24.076 -32.651  19.718  1.00 64.93           C  
ANISOU  245  CB  LYS A  30     7892   6846   9932   -546    418    311       C  
ATOM    246  CG  LYS A  30     -24.290 -32.169  21.138  1.00 68.48           C  
ANISOU  246  CG  LYS A  30     8334   7390  10294   -511    541    472       C  
ATOM    247  CD  LYS A  30     -25.245 -30.993  21.162  1.00 69.41           C  
ANISOU  247  CD  LYS A  30     8321   7666  10388   -549    548    437       C  
ATOM    248  CE  LYS A  30     -25.465 -30.491  22.574  1.00 70.73           C  
ANISOU  248  CE  LYS A  30     8492   7929  10453   -506    680    583       C  
ATOM    249  NZ  LYS A  30     -26.436 -29.364  22.614  1.00 72.31           N  
ANISOU  249  NZ  LYS A  30     8561   8271  10641   -533    700    546       N  
ATOM    250  N   ASN A  31     -24.027 -35.001  17.671  1.00 68.19           N  
ANISOU  250  N   ASN A  31     8397   6864  10646   -675    287     96       N  
ATOM    251  CA  ASN A  31     -24.011 -35.544  16.316  1.00 68.81           C  
ANISOU  251  CA  ASN A  31     8503   6838  10803   -720    174    -83       C  
ATOM    252  C   ASN A  31     -24.107 -34.464  15.244  1.00 65.97           C  
ANISOU  252  C   ASN A  31     8081   6644  10342   -708     52   -237       C  
ATOM    253  O   ASN A  31     -23.833 -34.748  14.073  1.00 61.68           O  
ANISOU  253  O   ASN A  31     7586   6050   9799   -707    -47   -391       O  
ATOM    254  CB  ASN A  31     -25.150 -36.551  16.138  1.00 69.33           C  
ANISOU  254  CB  ASN A  31     8521   6720  11101   -893    184   -103       C  
ATOM    255  CG  ASN A  31     -26.503 -35.976  16.516  1.00 68.26           C  
ANISOU  255  CG  ASN A  31     8217   6675  11043  -1013    217    -58       C  
ATOM    256  OD1 ASN A  31     -26.623 -34.792  16.824  1.00 69.66           O  
ANISOU  256  OD1 ASN A  31     8320   7052  11095   -961    225    -29       O  
ATOM    257  ND2 ASN A  31     -27.532 -36.814  16.487  1.00 73.93           N  
ANISOU  257  ND2 ASN A  31     8870   7242  11980  -1175    238    -56       N  
ATOM    258  N   ASP A  32     -24.494 -33.243  15.607  1.00 59.43           N  
ANISOU  258  N   ASP A  32     7155   6004   9421   -694     60   -198       N  
ATOM    259  CA  ASP A  32     -24.559 -32.160  14.635  1.00 65.13           C  
ANISOU  259  CA  ASP A  32     7826   6879  10040   -672    -52   -325       C  
ATOM    260  C   ASP A  32     -23.219 -31.465  14.434  1.00 67.39           C  
ANISOU  260  C   ASP A  32     8196   7275  10134   -523    -76   -342       C  
ATOM    261  O   ASP A  32     -23.120 -30.581  13.576  1.00 56.10           O  
ANISOU  261  O   ASP A  32     6745   5964   8607   -494   -162   -440       O  
ATOM    262  CB  ASP A  32     -25.623 -31.137  15.051  1.00 69.07           C  
ANISOU  262  CB  ASP A  32     8181   7520  10543   -720    -35   -282       C  
ATOM    263  CG  ASP A  32     -25.249 -30.378  16.309  1.00 80.22           C  
ANISOU  263  CG  ASP A  32     9595   9047  11837   -632     71   -139       C  
ATOM    264  OD1 ASP A  32     -24.429 -30.890  17.098  1.00 84.70           O  
ANISOU  264  OD1 ASP A  32    10260   9559  12364   -568    148    -40       O  
ATOM    265  OD2 ASP A  32     -25.782 -29.266  16.510  1.00 84.98           O  
ANISOU  265  OD2 ASP A  32    10108   9794  12386   -624     72   -129       O  
ATOM    266  N   GLY A  33     -22.191 -31.837  15.195  1.00 78.88           N  
ANISOU  266  N   GLY A  33     9739   8694  11537   -429     -3   -245       N  
ATOM    267  CA  GLY A  33     -20.854 -31.309  15.026  1.00 68.89           C  
ANISOU  267  CA  GLY A  33     8539   7520  10117   -294    -24   -259       C  
ATOM    268  C   GLY A  33     -20.396 -30.376  16.126  1.00 56.63           C  
ANISOU  268  C   GLY A  33     6969   6108   8439   -217     29   -140       C  
ATOM    269  O   GLY A  33     -19.195 -30.087  16.212  1.00 64.72           O  
ANISOU  269  O   GLY A  33     8044   7190   9356   -108     21   -126       O  
ATOM    270  N   THR A  34     -21.307 -29.900  16.969  1.00 55.00           N  
ANISOU  270  N   THR A  34     6692   5959   8248   -270     82    -58       N  
ATOM    271  CA  THR A  34     -20.930 -28.972  18.028  1.00 63.06           C  
ANISOU  271  CA  THR A  34     7708   7114   9138   -198    128     40       C  
ATOM    272  C   THR A  34     -20.108 -29.684  19.096  1.00 58.95           C  
ANISOU  272  C   THR A  34     7275   6533   8589   -125    196    169       C  
ATOM    273  O   THR A  34     -20.461 -30.779  19.542  1.00 64.73           O  
ANISOU  273  O   THR A  34     8039   7127   9428   -166    260    245       O  
ATOM    274  CB  THR A  34     -22.174 -28.348  18.657  1.00 65.70           C  
ANISOU  274  CB  THR A  34     7950   7517   9497   -265    183     88       C  
ATOM    275  OG1 THR A  34     -22.986 -29.380  19.230  1.00 76.69           O  
ANISOU  275  OG1 THR A  34     9328   8783  11027   -348    269    171       O  
ATOM    276  CG2 THR A  34     -22.982 -27.603  17.609  1.00 67.10           C  
ANISOU  276  CG2 THR A  34     8032   7758   9703   -323    102    -33       C  
ATOM    277  N   PHE A  35     -19.008 -29.056  19.506  1.00 54.45           N  
ANISOU  277  N   PHE A  35     6743   6067   7879    -17    176    199       N  
ATOM    278  CA  PHE A  35     -18.142 -29.561  20.571  1.00 49.15           C  
ANISOU  278  CA  PHE A  35     6149   5371   7154     70    217    325       C  
ATOM    279  C   PHE A  35     -17.894 -28.382  21.505  1.00 58.43           C  
ANISOU  279  C   PHE A  35     7315   6711   8174    122    221    379       C  
ATOM    280  O   PHE A  35     -16.975 -27.588  21.288  1.00 66.13           O  
ANISOU  280  O   PHE A  35     8286   7789   9050    189    154    331       O  
ATOM    281  CB  PHE A  35     -16.850 -30.135  20.004  1.00 46.45           C  
ANISOU  281  CB  PHE A  35     5862   4974   6811    160    166    289       C  
ATOM    282  CG  PHE A  35     -15.975 -30.792  21.028  1.00 50.40           C  
ANISOU  282  CG  PHE A  35     6438   5434   7278    257    194    422       C  
ATOM    283  CD1 PHE A  35     -16.459 -31.824  21.816  1.00 51.64           C  
ANISOU  283  CD1 PHE A  35     6651   5461   7511    234    273    545       C  
ATOM    284  CD2 PHE A  35     -14.663 -30.387  21.194  1.00 50.94           C  
ANISOU  284  CD2 PHE A  35     6518   5594   7245    372    140    431       C  
ATOM    285  CE1 PHE A  35     -15.653 -32.430  22.757  1.00 57.83           C  
ANISOU  285  CE1 PHE A  35     7512   6206   8253    334    292    679       C  
ATOM    286  CE2 PHE A  35     -13.853 -30.990  22.134  1.00 59.94           C  
ANISOU  286  CE2 PHE A  35     7719   6703   8352    470    149    556       C  
ATOM    287  CZ  PHE A  35     -14.348 -32.013  22.916  1.00 57.73           C  
ANISOU  287  CZ  PHE A  35     7508   6294   8134    457    222    683       C  
ATOM    288  N   ILE A  36     -18.725 -28.265  22.537  1.00 53.94           N  
ANISOU  288  N   ILE A  36     6743   6164   7588     89    305    474       N  
ATOM    289  CA  ILE A  36     -18.720 -27.116  23.432  1.00 58.83           C  
ANISOU  289  CA  ILE A  36     7358   6933   8061    128    318    508       C  
ATOM    290  C   ILE A  36     -18.419 -27.599  24.845  1.00 61.75           C  
ANISOU  290  C   ILE A  36     7817   7297   8350    187    385    663       C  
ATOM    291  O   ILE A  36     -18.874 -28.672  25.254  1.00 65.63           O  
ANISOU  291  O   ILE A  36     8343   7670   8923    155    466    761       O  
ATOM    292  CB  ILE A  36     -20.066 -26.361  23.370  1.00 68.12           C  
ANISOU  292  CB  ILE A  36     8450   8165   9269     47    365    470       C  
ATOM    293  CG1 ILE A  36     -20.104 -25.213  24.383  1.00 79.35           C  
ANISOU  293  CG1 ILE A  36     9885   9728  10538     96    394    503       C  
ATOM    294  CG2 ILE A  36     -21.233 -27.325  23.575  1.00 73.27           C  
ANISOU  294  CG2 ILE A  36     9073   8704  10064    -45    466    536       C  
ATOM    295  CD1 ILE A  36     -19.052 -24.146  24.148  1.00 89.68           C  
ANISOU  295  CD1 ILE A  36    11207  11143  11724    164    290    427       C  
ATOM    296  N   GLY A  37     -17.640 -26.808  25.582  1.00 58.39           N  
ANISOU  296  N   GLY A  37     7431   6994   7762    270    345    685       N  
ATOM    297  CA  GLY A  37     -17.290 -27.109  26.959  1.00 64.42           C  
ANISOU  297  CA  GLY A  37     8290   7779   8409    339    387    825       C  
ATOM    298  C   GLY A  37     -17.858 -26.083  27.921  1.00 59.15           C  
ANISOU  298  C   GLY A  37     7634   7238   7602    343    440    845       C  
ATOM    299  O   GLY A  37     -18.077 -24.925  27.558  1.00 70.05           O  
ANISOU  299  O   GLY A  37     8957   8711   8948    324    404    738       O  
ATOM    300  N   TYR A  38     -18.094 -26.519  29.157  1.00 49.33           N  
ANISOU  300  N   TYR A  38     6476   5993   6275    373    530    985       N  
ATOM    301  CA  TYR A  38     -18.686 -25.687  30.193  1.00 60.55           C  
ANISOU  301  CA  TYR A  38     7931   7526   7551    387    605   1015       C  
ATOM    302  C   TYR A  38     -17.877 -25.817  31.477  1.00 67.79           C  
ANISOU  302  C   TYR A  38     8980   8502   8274    490    588   1127       C  
ATOM    303  O   TYR A  38     -17.188 -26.816  31.700  1.00 66.06           O  
ANISOU  303  O   TYR A  38     8825   8209   8064    539    561   1227       O  
ATOM    304  CB  TYR A  38     -20.149 -26.073  30.455  1.00 62.33           C  
ANISOU  304  CB  TYR A  38     8119   7698   7865    305    775   1081       C  
ATOM    305  CG  TYR A  38     -21.007 -26.185  29.210  1.00 62.77           C  
ANISOU  305  CG  TYR A  38     8040   7679   8131    197    783    987       C  
ATOM    306  CD1 TYR A  38     -21.775 -25.114  28.775  1.00 67.04           C  
ANISOU  306  CD1 TYR A  38     8482   8297   8692    158    788    878       C  
ATOM    307  CD2 TYR A  38     -21.062 -27.369  28.481  1.00 63.54           C  
ANISOU  307  CD2 TYR A  38     8114   7624   8405    139    779   1005       C  
ATOM    308  CE1 TYR A  38     -22.568 -25.212  27.645  1.00 68.37           C  
ANISOU  308  CE1 TYR A  38     8527   8408   9044     65    778    795       C  
ATOM    309  CE2 TYR A  38     -21.852 -27.475  27.348  1.00 65.08           C  
ANISOU  309  CE2 TYR A  38     8191   7755   8780     38    770    910       C  
ATOM    310  CZ  TYR A  38     -22.602 -26.393  26.937  1.00 68.85           C  
ANISOU  310  CZ  TYR A  38     8568   8325   9267      2    764    808       C  
ATOM    311  OH  TYR A  38     -23.391 -26.490  25.815  1.00 74.52           O  
ANISOU  311  OH  TYR A  38     9169   8990  10156    -92    737    715       O  
ATOM    312  N   LYS A  39     -17.966 -24.789  32.327  1.00 76.96           N  
ANISOU  312  N   LYS A  39    10190   9796   9257    530    597   1108       N  
ATOM    313  CA  LYS A  39     -17.292 -24.848  33.623  1.00 81.99           C  
ANISOU  313  CA  LYS A  39    10965  10504   9684    628    575   1209       C  
ATOM    314  C   LYS A  39     -17.830 -25.994  34.470  1.00 81.00           C  
ANISOU  314  C   LYS A  39    10928  10303   9544    635    719   1398       C  
ATOM    315  O   LYS A  39     -17.069 -26.666  35.177  1.00 82.43           O  
ANISOU  315  O   LYS A  39    11218  10473   9628    716    679   1518       O  
ATOM    316  CB  LYS A  39     -17.445 -23.521  34.368  1.00 85.39           C  
ANISOU  316  CB  LYS A  39    11440  11081   9923    661    572   1137       C  
ATOM    317  CG  LYS A  39     -16.457 -22.443  33.953  1.00 89.70           C  
ANISOU  317  CG  LYS A  39    11954  11711  10418    686    395    990       C  
ATOM    318  CD  LYS A  39     -16.561 -21.219  34.857  1.00 99.67           C  
ANISOU  318  CD  LYS A  39    13291  13101  11478    725    390    925       C  
ATOM    319  CE  LYS A  39     -15.678 -20.086  34.356  1.00106.22           C  
ANISOU  319  CE  LYS A  39    14076  13994  12289    726    223    771       C  
ATOM    320  NZ  LYS A  39     -16.102 -18.763  34.905  1.00109.74           N  
ANISOU  320  NZ  LYS A  39    14566  14529  12601    736    241    670       N  
ATOM    321  N   GLU A  40     -19.139 -26.228  34.415  1.00 78.97           N  
ANISOU  321  N   GLU A  40    10623   9993   9390    552    887   1432       N  
ATOM    322  CA  GLU A  40     -19.775 -27.339  35.105  1.00 82.97           C  
ANISOU  322  CA  GLU A  40    11195  10408   9921    534   1048   1616       C  
ATOM    323  C   GLU A  40     -20.859 -27.910  34.200  1.00 83.61           C  
ANISOU  323  C   GLU A  40    11146  10361  10262    405   1149   1602       C  
ATOM    324  O   GLU A  40     -21.254 -27.294  33.207  1.00 91.44           O  
ANISOU  324  O   GLU A  40    12006  11364  11373    340   1108   1452       O  
ATOM    325  CB  GLU A  40     -20.351 -26.909  36.462  1.00 98.82           C  
ANISOU  325  CB  GLU A  40    13306  12523  11718    578   1186   1705       C  
ATOM    326  CG  GLU A  40     -19.288 -26.560  37.504  1.00109.57           C  
ANISOU  326  CG  GLU A  40    14825  14001  12805    708   1083   1744       C  
ATOM    327  CD  GLU A  40     -19.877 -26.169  38.843  1.00117.26           C  
ANISOU  327  CD  GLU A  40    15922  15081  13550    757   1227   1827       C  
ATOM    328  OE1 GLU A  40     -21.109 -25.964  38.918  1.00124.80           O  
ANISOU  328  OE1 GLU A  40    16819  16038  14561    693   1409   1831       O  
ATOM    329  OE2 GLU A  40     -19.107 -26.068  39.825  1.00115.86           O  
ANISOU  329  OE2 GLU A  40    15898  14991  13133    863   1156   1887       O  
ATOM    330  N   ARG A  41     -21.334 -29.101  34.547  1.00 91.97           N  
ANISOU  330  N   ARG A  41    12244  11292  11410    365   1277   1761       N  
ATOM    331  CA  ARG A  41     -22.333 -29.769  33.724  1.00 97.08           C  
ANISOU  331  CA  ARG A  41    12769  11800  12319    231   1363   1753       C  
ATOM    332  C   ARG A  41     -23.583 -28.903  33.614  1.00 99.22           C  
ANISOU  332  C   ARG A  41    12913  12153  12633    156   1469   1676       C  
ATOM    333  O   ARG A  41     -24.093 -28.424  34.636  1.00104.84           O  
ANISOU  333  O   ARG A  41    13671  12966  13199    190   1598   1744       O  
ATOM    334  CB  ARG A  41     -22.687 -31.133  34.313  1.00105.12           C  
ANISOU  334  CB  ARG A  41    13861  12667  13412    197   1504   1956       C  
ATOM    335  CG  ARG A  41     -21.490 -32.041  34.511  1.00109.00           C  
ANISOU  335  CG  ARG A  41    14486  13068  13863    287   1411   2053       C  
ATOM    336  CD  ARG A  41     -21.923 -33.441  34.898  1.00115.40           C  
ANISOU  336  CD  ARG A  41    15360  13691  14796    237   1550   2248       C  
ATOM    337  NE  ARG A  41     -20.785 -34.348  34.989  1.00122.30           N  
ANISOU  337  NE  ARG A  41    16355  14458  15656    332   1454   2337       N  
ATOM    338  CZ  ARG A  41     -20.886 -35.671  35.059  1.00126.89           C  
ANISOU  338  CZ  ARG A  41    16998  14834  16380    301   1527   2483       C  
ATOM    339  NH1 ARG A  41     -19.792 -36.417  35.137  1.00128.88           N  
ANISOU  339  NH1 ARG A  41    17358  14996  16614    409   1429   2557       N  
ATOM    340  NH2 ARG A  41     -22.079 -36.249  35.045  1.00127.63           N  
ANISOU  340  NH2 ARG A  41    17040  14807  16646    161   1698   2556       N  
ATOM    341  N   PRO A  42     -24.095 -28.665  32.412  1.00 94.68           N  
ANISOU  341  N   PRO A  42    12184  11544  12248     66   1416   1535       N  
ATOM    342  CA  PRO A  42     -25.276 -27.814  32.265  1.00 92.47           C  
ANISOU  342  CA  PRO A  42    11769  11344  12020      7   1502   1461       C  
ATOM    343  C   PRO A  42     -26.557 -28.559  32.613  1.00100.18           C  
ANISOU  343  C   PRO A  42    12675  12241  13150    -98   1702   1582       C  
ATOM    344  O   PRO A  42     -26.624 -29.789  32.595  1.00 99.22           O  
ANISOU  344  O   PRO A  42    12577  11965  13155   -161   1752   1692       O  
ATOM    345  CB  PRO A  42     -25.247 -27.430  30.782  1.00 83.12           C  
ANISOU  345  CB  PRO A  42    10456  10139  10986    -46   1349   1278       C  
ATOM    346  CG  PRO A  42     -24.585 -28.594  30.126  1.00 84.38           C  
ANISOU  346  CG  PRO A  42    10652  10143  11264    -75   1263   1295       C  
ATOM    347  CD  PRO A  42     -23.565 -29.110  31.111  1.00 90.65           C  
ANISOU  347  CD  PRO A  42    11619  10928  11895     28   1266   1429       C  
ATOM    348  N   GLN A  43     -27.587 -27.775  32.939  1.00112.82           N  
ANISOU  348  N   GLN A  43    14181  13943  14743   -115   1825   1563       N  
ATOM    349  CA  GLN A  43     -28.891 -28.352  33.245  1.00121.70           C  
ANISOU  349  CA  GLN A  43    15203  15011  16028   -221   2028   1670       C  
ATOM    350  C   GLN A  43     -29.711 -28.599  31.985  1.00125.78           C  
ANISOU  350  C   GLN A  43    15516  15441  16835   -359   1977   1569       C  
ATOM    351  O   GLN A  43     -30.540 -29.516  31.961  1.00128.39           O  
ANISOU  351  O   GLN A  43    15762  15656  17364   -480   2093   1659       O  
ATOM    352  CB  GLN A  43     -29.661 -27.447  34.212  1.00126.29           C  
ANISOU  352  CB  GLN A  43    15765  15742  16476   -168   2201   1702       C  
ATOM    353  CG  GLN A  43     -30.326 -26.228  33.572  1.00128.39           C  
ANISOU  353  CG  GLN A  43    15868  16113  16800   -170   2161   1534       C  
ATOM    354  CD  GLN A  43     -29.331 -25.266  32.949  1.00126.01           C  
ANISOU  354  CD  GLN A  43    15615  15881  16382    -85   1939   1367       C  
ATOM    355  OE1 GLN A  43     -28.247 -25.038  33.487  1.00127.54           O  
ANISOU  355  OE1 GLN A  43    15978  16121  16359     16   1866   1376       O  
ATOM    356  NE2 GLN A  43     -29.695 -24.700  31.804  1.00121.74           N  
ANISOU  356  NE2 GLN A  43    14923  15348  15986   -129   1827   1218       N  
ATOM    357  N   ASP A  44     -29.496 -27.804  30.940  1.00123.87           N  
ANISOU  357  N   ASP A  44    15196  15250  16620   -347   1803   1386       N  
ATOM    358  CA  ASP A  44     -30.169 -27.984  29.661  1.00125.97           C  
ANISOU  358  CA  ASP A  44    15285  15445  17133   -466   1717   1274       C  
ATOM    359  C   ASP A  44     -29.196 -28.630  28.684  1.00124.46           C  
ANISOU  359  C   ASP A  44    15158  15139  16991   -479   1532   1201       C  
ATOM    360  O   ASP A  44     -28.069 -28.152  28.512  1.00121.82           O  
ANISOU  360  O   ASP A  44    14930  14858  16500   -378   1401   1134       O  
ATOM    361  CB  ASP A  44     -30.677 -26.648  29.115  1.00126.81           C  
ANISOU  361  CB  ASP A  44    15260  15686  17234   -438   1655   1127       C  
ATOM    362  CG  ASP A  44     -31.701 -26.819  28.003  1.00124.88           C  
ANISOU  362  CG  ASP A  44    14807  15390  17250   -565   1603   1040       C  
ATOM    363  OD1 ASP A  44     -31.461 -27.627  27.080  1.00123.05           O  
ANISOU  363  OD1 ASP A  44    14567  15035  17153   -644   1485    991       O  
ATOM    364  OD2 ASP A  44     -32.753 -26.148  28.053  1.00123.38           O  
ANISOU  364  OD2 ASP A  44    14463  15285  17132   -580   1678   1017       O  
ATOM    365  N   VAL A  45     -29.639 -29.711  28.041  1.00123.32           N  
ANISOU  365  N   VAL A  45    14946  14836  17073   -606   1524   1207       N  
ATOM    366  CA  VAL A  45     -28.740 -30.503  27.209  1.00121.83           C  
ANISOU  366  CA  VAL A  45    14839  14516  16937   -615   1377   1150       C  
ATOM    367  C   VAL A  45     -28.530 -29.847  25.848  1.00124.79           C  
ANISOU  367  C   VAL A  45    15141  14935  17339   -614   1184    950       C  
ATOM    368  O   VAL A  45     -27.399 -29.771  25.354  1.00126.60           O  
ANISOU  368  O   VAL A  45    15467  15162  17472   -538   1052    879       O  
ATOM    369  CB  VAL A  45     -29.275 -31.943  27.087  1.00116.77           C  
ANISOU  369  CB  VAL A  45    14174  13669  16523   -751   1446   1231       C  
ATOM    370  CG1 VAL A  45     -28.655 -32.654  25.898  1.00110.36           C  
ANISOU  370  CG1 VAL A  45    13398  12717  15816   -784   1279   1115       C  
ATOM    371  CG2 VAL A  45     -28.993 -32.711  28.370  1.00117.78           C  
ANISOU  371  CG2 VAL A  45    14443  13730  16578   -716   1604   1442       C  
ATOM    372  N   ASP A  46     -29.601 -29.357  25.224  1.00128.43           N  
ANISOU  372  N   ASP A  46    15429  15442  17928   -694   1167    863       N  
ATOM    373  CA  ASP A  46     -29.506 -28.720  23.911  1.00132.58           C  
ANISOU  373  CA  ASP A  46    15887  16013  18474   -693    985    683       C  
ATOM    374  C   ASP A  46     -30.432 -27.510  23.873  1.00130.11           C  
ANISOU  374  C   ASP A  46    15427  15849  18162   -685   1002    632       C  
ATOM    375  O   ASP A  46     -31.654 -27.655  23.979  1.00133.30           O  
ANISOU  375  O   ASP A  46    15677  16245  18726   -777   1087    662       O  
ATOM    376  CB  ASP A  46     -29.841 -29.709  22.790  1.00138.72           C  
ANISOU  376  CB  ASP A  46    16608  16639  19462   -819    890    602       C  
ATOM    377  CG  ASP A  46     -31.171 -30.413  23.001  1.00142.40           C  
ANISOU  377  CG  ASP A  46    16929  17019  20155   -969    999    666       C  
ATOM    378  OD1 ASP A  46     -31.631 -30.505  24.160  1.00143.82           O  
ANISOU  378  OD1 ASP A  46    17097  17217  20331   -974   1181    815       O  
ATOM    379  OD2 ASP A  46     -31.755 -30.883  22.001  1.00143.08           O  
ANISOU  379  OD2 ASP A  46    16916  17023  20426  -1084    902    568       O  
ATOM    380  N   GLN A  47     -29.853 -26.320  23.719  1.00127.22           N  
ANISOU  380  N   GLN A  47    15100  15610  17626   -574    922    556       N  
ATOM    381  CA  GLN A  47     -30.630 -25.093  23.624  1.00124.69           C  
ANISOU  381  CA  GLN A  47    14657  15422  17298   -545    924    500       C  
ATOM    382  C   GLN A  47     -31.242 -24.962  22.228  1.00118.58           C  
ANISOU  382  C   GLN A  47    13747  14637  16673   -616    776    369       C  
ATOM    383  O   GLN A  47     -30.744 -25.519  21.247  1.00115.77           O  
ANISOU  383  O   GLN A  47    13432  14201  16355   -654    642    291       O  
ATOM    384  CB  GLN A  47     -29.756 -23.877  23.960  1.00125.33           C  
ANISOU  384  CB  GLN A  47    14844  15624  17152   -406    887    466       C  
ATOM    385  CG  GLN A  47     -30.486 -22.531  24.013  1.00123.27           C  
ANISOU  385  CG  GLN A  47    14483  15490  16866   -353    905    416       C  
ATOM    386  CD  GLN A  47     -31.767 -22.583  24.827  1.00121.01           C  
ANISOU  386  CD  GLN A  47    14071  15231  16678   -389   1085    500       C  
ATOM    387  OE1 GLN A  47     -31.817 -23.197  25.891  1.00123.40           O  
ANISOU  387  OE1 GLN A  47    14428  15507  16952   -396   1240    623       O  
ATOM    388  NE2 GLN A  47     -32.815 -21.942  24.320  1.00116.93           N  
ANISOU  388  NE2 GLN A  47    13380  14767  16279   -406   1069    440       N  
ATOM    389  N   ARG A  48     -32.343 -24.211  22.153  1.00115.30           N  
ANISOU  389  N   ARG A  48    13167  14305  16335   -626    800    344       N  
ATOM    390  CA  ARG A  48     -33.146 -24.180  20.935  1.00111.71           C  
ANISOU  390  CA  ARG A  48    12557  13842  16044   -704    667    239       C  
ATOM    391  C   ARG A  48     -32.485 -23.378  19.820  1.00112.27           C  
ANISOU  391  C   ARG A  48    12684  13966  16010   -636    477    111       C  
ATOM    392  O   ARG A  48     -32.769 -23.620  18.642  1.00115.35           O  
ANISOU  392  O   ARG A  48    13011  14322  16495   -699    329     15       O  
ATOM    393  CB  ARG A  48     -34.532 -23.616  21.249  1.00105.97           C  
ANISOU  393  CB  ARG A  48    11625  13195  15443   -724    755    264       C  
ATOM    394  CG  ARG A  48     -35.222 -24.326  22.397  1.00105.04           C  
ANISOU  394  CG  ARG A  48    11446  13040  15426   -788    972    403       C  
ATOM    395  CD  ARG A  48     -36.442 -23.567  22.883  1.00108.54           C  
ANISOU  395  CD  ARG A  48    11699  13589  15952   -768   1092    435       C  
ATOM    396  NE  ARG A  48     -37.022 -24.213  24.058  1.00113.33           N  
ANISOU  396  NE  ARG A  48    12263  14167  16629   -820   1327    581       N  
ATOM    397  CZ  ARG A  48     -37.924 -25.189  24.028  1.00116.11           C  
ANISOU  397  CZ  ARG A  48    12464  14437  17217   -969   1394    636       C  
ATOM    398  NH1 ARG A  48     -38.381 -25.653  22.878  1.00118.49           N  
ANISOU  398  NH1 ARG A  48    12637  14674  17711  -1085   1230    544       N  
ATOM    399  NH2 ARG A  48     -38.370 -25.698  25.165  1.00117.04           N  
ANISOU  399  NH2 ARG A  48    12561  14534  17374  -1005   1628    785       N  
ATOM    400  N   GLU A  49     -31.612 -22.433  20.158  1.00106.61           N  
ANISOU  400  N   GLU A  49    12086  13328  15095   -514    476    108       N  
ATOM    401  CA  GLU A  49     -31.026 -21.570  19.142  1.00103.41           C  
ANISOU  401  CA  GLU A  49    11725  12974  14592   -450    315      1       C  
ATOM    402  C   GLU A  49     -30.120 -22.367  18.204  1.00 94.29           C  
ANISOU  402  C   GLU A  49    10673  11733  13419   -484    193    -61       C  
ATOM    403  O   GLU A  49     -29.618 -23.442  18.542  1.00 94.55           O  
ANISOU  403  O   GLU A  49    10786  11670  13468   -521    240    -15       O  
ATOM    404  CB  GLU A  49     -30.249 -20.425  19.790  1.00110.03           C  
ANISOU  404  CB  GLU A  49    12670  13900  15236   -325    350     17       C  
ATOM    405  CG  GLU A  49     -29.205 -20.862  20.796  1.00117.24           C  
ANISOU  405  CG  GLU A  49    13736  14786  16022   -287    436     93       C  
ATOM    406  CD  GLU A  49     -28.550 -19.681  21.480  1.00123.91           C  
ANISOU  406  CD  GLU A  49    14672  15720  16687   -174    461     97       C  
ATOM    407  OE1 GLU A  49     -28.789 -18.535  21.040  1.00125.21           O  
ANISOU  407  OE1 GLU A  49    14796  15952  16827   -126    402     33       O  
ATOM    408  OE2 GLU A  49     -27.804 -19.895  22.457  1.00126.41           O  
ANISOU  408  OE2 GLU A  49    15105  16037  16889   -133    531    163       O  
ATOM    409  N   ALA A  50     -29.915 -21.816  17.007  1.00 85.52           N  
ANISOU  409  N   ALA A  50     9567  10657  12271   -462     41   -164       N  
ATOM    410  CA  ALA A  50     -29.209 -22.537  15.959  1.00 80.41           C  
ANISOU  410  CA  ALA A  50     9004   9936  11613   -493    -75   -241       C  
ATOM    411  C   ALA A  50     -27.742 -22.741  16.342  1.00 79.35           C  
ANISOU  411  C   ALA A  50     9037   9777  11335   -425    -43   -211       C  
ATOM    412  O   ALA A  50     -27.151 -21.910  17.036  1.00 80.36           O  
ANISOU  412  O   ALA A  50     9221   9978  11336   -340      7   -168       O  
ATOM    413  CB  ALA A  50     -29.303 -21.787  14.633  1.00 78.60           C  
ANISOU  413  CB  ALA A  50     8753   9766  11345   -471   -235   -348       C  
ATOM    414  N   PRO A  51     -27.137 -23.844  15.905  1.00 75.50           N  
ANISOU  414  N   PRO A  51     8628   9186  10873   -460    -74   -238       N  
ATOM    415  CA  PRO A  51     -25.738 -24.102  16.259  1.00 73.96           C  
ANISOU  415  CA  PRO A  51     8575   8967  10560   -388    -46   -206       C  
ATOM    416  C   PRO A  51     -24.800 -23.085  15.630  1.00 76.68           C  
ANISOU  416  C   PRO A  51     8981   9399  10754   -302   -124   -264       C  
ATOM    417  O   PRO A  51     -25.076 -22.515  14.571  1.00 89.99           O  
ANISOU  417  O   PRO A  51    10635  11129  12428   -306   -223   -348       O  
ATOM    418  CB  PRO A  51     -25.485 -25.509  15.703  1.00 68.62           C  
ANISOU  418  CB  PRO A  51     7951   8149   9974   -445    -75   -242       C  
ATOM    419  CG  PRO A  51     -26.844 -26.113  15.552  1.00 77.50           C  
ANISOU  419  CG  PRO A  51     8960   9208  11279   -565    -74   -254       C  
ATOM    420  CD  PRO A  51     -27.743 -24.976  15.189  1.00 78.78           C  
ANISOU  420  CD  PRO A  51     9001   9489  11442   -567   -128   -294       C  
ATOM    421  N   LEU A  52     -23.677 -22.864  16.304  1.00 63.66           N  
ANISOU  421  N   LEU A  52     7420   7777   8991   -226    -81   -211       N  
ATOM    422  CA  LEU A  52     -22.659 -21.928  15.853  1.00 54.70           C  
ANISOU  422  CA  LEU A  52     6341   6719   7723   -151   -138   -251       C  
ATOM    423  C   LEU A  52     -21.458 -22.688  15.312  1.00 52.68           C  
ANISOU  423  C   LEU A  52     6174   6406   7435   -121   -166   -280       C  
ATOM    424  O   LEU A  52     -20.998 -23.659  15.920  1.00 52.89           O  
ANISOU  424  O   LEU A  52     6248   6359   7490   -113   -114   -225       O  
ATOM    425  CB  LEU A  52     -22.222 -21.005  16.990  1.00 44.71           C  
ANISOU  425  CB  LEU A  52     5099   5534   6354    -87    -80   -183       C  
ATOM    426  CG  LEU A  52     -23.278 -20.028  17.510  1.00 49.25           C  
ANISOU  426  CG  LEU A  52     5598   6177   6937    -89    -45   -165       C  
ATOM    427  CD1 LEU A  52     -22.769 -19.310  18.741  1.00 46.84           C  
ANISOU  427  CD1 LEU A  52     5343   5933   6522    -25     18   -106       C  
ATOM    428  CD2 LEU A  52     -23.652 -19.027  16.432  1.00 46.37           C  
ANISOU  428  CD2 LEU A  52     5189   5866   6564    -84   -135   -243       C  
ATOM    429  N   ASN A  53     -20.945 -22.230  14.169  1.00 44.38           N  
ANISOU  429  N   ASN A  53     5148   5391   6324    -98   -243   -360       N  
ATOM    430  CA  ASN A  53     -19.826 -22.906  13.525  1.00 52.78           C  
ANISOU  430  CA  ASN A  53     6288   6409   7358    -61   -262   -399       C  
ATOM    431  C   ASN A  53     -18.529 -22.777  14.307  1.00 51.52           C  
ANISOU  431  C   ASN A  53     6175   6278   7123     15   -217   -334       C  
ATOM    432  O   ASN A  53     -17.607 -23.564  14.076  1.00 56.38           O  
ANISOU  432  O   ASN A  53     6842   6839   7739     53   -209   -343       O  
ATOM    433  CB  ASN A  53     -19.625 -22.361  12.113  1.00 58.28           C  
ANISOU  433  CB  ASN A  53     7002   7150   7991    -51   -341   -495       C  
ATOM    434  CG  ASN A  53     -20.802 -22.642  11.215  1.00 60.49           C  
ANISOU  434  CG  ASN A  53     7246   7399   8339   -121   -411   -572       C  
ATOM    435  OD1 ASN A  53     -21.546 -23.598  11.431  1.00 65.58           O  
ANISOU  435  OD1 ASN A  53     7863   7955   9098   -184   -402   -575       O  
ATOM    436  ND2 ASN A  53     -20.984 -21.808  10.201  1.00 69.13           N  
ANISOU  436  ND2 ASN A  53     8338   8563   9365   -113   -486   -631       N  
ATOM    437  N   ASN A  54     -18.435 -21.808  15.220  1.00 55.55           N  
ANISOU  437  N   ASN A  54     6667   6870   7571     40   -194   -275       N  
ATOM    438  CA  ASN A  54     -17.212 -21.630  15.997  1.00 53.29           C  
ANISOU  438  CA  ASN A  54     6417   6620   7211    107   -173   -219       C  
ATOM    439  C   ASN A  54     -16.848 -22.883  16.782  1.00 56.67           C  
ANISOU  439  C   ASN A  54     6883   6965   7682    129   -125   -149       C  
ATOM    440  O   ASN A  54     -15.665 -23.133  17.043  1.00 58.04           O  
ANISOU  440  O   ASN A  54     7090   7144   7819    193   -127   -120       O  
ATOM    441  CB  ASN A  54     -17.375 -20.438  16.942  1.00 50.45           C  
ANISOU  441  CB  ASN A  54     6039   6348   6781    120   -160   -177       C  
ATOM    442  CG  ASN A  54     -17.832 -19.184  16.220  1.00 53.25           C  
ANISOU  442  CG  ASN A  54     6361   6766   7107    103   -204   -235       C  
ATOM    443  OD1 ASN A  54     -19.016 -19.018  15.926  1.00 47.77           O  
ANISOU  443  OD1 ASN A  54     5623   6066   6463     62   -208   -258       O  
ATOM    444  ND2 ASN A  54     -16.892 -18.291  15.932  1.00 51.19           N  
ANISOU  444  ND2 ASN A  54     6114   6563   6772    135   -237   -253       N  
ATOM    445  N   PHE A  55     -17.843 -23.685  17.157  1.00 51.42           N  
ANISOU  445  N   PHE A  55     6211   6222   7105     77    -82   -116       N  
ATOM    446  CA  PHE A  55     -17.629 -24.893  17.938  1.00 48.34           C  
ANISOU  446  CA  PHE A  55     5865   5737   6764     92    -27    -34       C  
ATOM    447  C   PHE A  55     -17.782 -26.163  17.114  1.00 47.58           C  
ANISOU  447  C   PHE A  55     5792   5504   6781     59    -32    -81       C  
ATOM    448  O   PHE A  55     -17.628 -27.261  17.658  1.00 44.18           O  
ANISOU  448  O   PHE A  55     5407   4967   6411     70     13    -14       O  
ATOM    449  CB  PHE A  55     -18.601 -24.924  19.126  1.00 51.98           C  
ANISOU  449  CB  PHE A  55     6310   6197   7244     55     48     58       C  
ATOM    450  CG  PHE A  55     -18.646 -23.638  19.908  1.00 53.69           C  
ANISOU  450  CG  PHE A  55     6511   6541   7349     84     56     84       C  
ATOM    451  CD1 PHE A  55     -19.731 -22.782  19.801  1.00 51.11           C  
ANISOU  451  CD1 PHE A  55     6119   6269   7033     38     66     51       C  
ATOM    452  CD2 PHE A  55     -17.597 -23.280  20.739  1.00 56.04           C  
ANISOU  452  CD2 PHE A  55     6859   6901   7535    160     47    136       C  
ATOM    453  CE1 PHE A  55     -19.767 -21.594  20.516  1.00 58.48           C  
ANISOU  453  CE1 PHE A  55     7049   7304   7865     72     77     64       C  
ATOM    454  CE2 PHE A  55     -17.632 -22.094  21.454  1.00 62.34           C  
ANISOU  454  CE2 PHE A  55     7654   7805   8228    183     48    144       C  
ATOM    455  CZ  PHE A  55     -18.716 -21.252  21.341  1.00 62.66           C  
ANISOU  455  CZ  PHE A  55     7641   7887   8278    141     68    106       C  
ATOM    456  N   SER A  56     -18.076 -26.045  15.823  1.00 47.31           N  
ANISOU  456  N   SER A  56     5739   5463   6772     22    -89   -195       N  
ATOM    457  CA  SER A  56     -18.338 -27.215  15.002  1.00 53.60           C  
ANISOU  457  CA  SER A  56     6567   6127   7674    -19   -104   -262       C  
ATOM    458  C   SER A  56     -17.063 -28.011  14.767  1.00 56.50           C  
ANISOU  458  C   SER A  56     7008   6426   8032     66    -96   -270       C  
ATOM    459  O   SER A  56     -15.954 -27.475  14.778  1.00 50.14           O  
ANISOU  459  O   SER A  56     6212   5703   7135    150   -103   -261       O  
ATOM    460  CB  SER A  56     -18.943 -26.811  13.660  1.00 55.10           C  
ANISOU  460  CB  SER A  56     6728   6343   7865    -71   -181   -390       C  
ATOM    461  OG  SER A  56     -19.166 -27.954  12.856  1.00 57.07           O  
ANISOU  461  OG  SER A  56     7018   6459   8206   -111   -206   -472       O  
ATOM    462  N   VAL A  57     -17.240 -29.313  14.544  1.00 65.89           N  
ANISOU  462  N   VAL A  57     8246   7458   9333     42    -79   -289       N  
ATOM    463  CA  VAL A  57     -16.135 -30.238  14.315  1.00 70.74           C  
ANISOU  463  CA  VAL A  57     8935   7979   9965    129    -63   -299       C  
ATOM    464  C   VAL A  57     -16.018 -30.628  12.844  1.00 68.64           C  
ANISOU  464  C   VAL A  57     8710   7658   9713    125   -108   -453       C  
ATOM    465  O   VAL A  57     -14.988 -31.189  12.435  1.00 66.47           O  
ANISOU  465  O   VAL A  57     8491   7332   9431    216    -93   -487       O  
ATOM    466  CB  VAL A  57     -16.305 -31.474  15.230  1.00 75.39           C  
ANISOU  466  CB  VAL A  57     9570   8409  10666    122     -2   -197       C  
ATOM    467  CG1 VAL A  57     -15.357 -32.601  14.888  1.00 84.36           C  
ANISOU  467  CG1 VAL A  57    10788   9410  11855    208     13   -219       C  
ATOM    468  CG2 VAL A  57     -16.118 -31.062  16.681  1.00 68.14           C  
ANISOU  468  CG2 VAL A  57     8634   7566   9689    159     43    -40       C  
ATOM    469  N   ALA A  58     -17.017 -30.299  12.029  1.00 70.93           N  
ANISOU  469  N   ALA A  58     8971   7966  10012     33   -165   -549       N  
ATOM    470  CA  ALA A  58     -17.001 -30.619  10.607  1.00 72.56           C  
ANISOU  470  CA  ALA A  58     9229   8131  10208     26   -220   -705       C  
ATOM    471  C   ALA A  58     -15.702 -30.180   9.940  1.00 70.00           C  
ANISOU  471  C   ALA A  58     8941   7894   9762    141   -211   -748       C  
ATOM    472  O   ALA A  58     -15.243 -29.048  10.118  1.00 65.39           O  
ANISOU  472  O   ALA A  58     8309   7459   9076    179   -209   -702       O  
ATOM    473  CB  ALA A  58     -18.189 -29.945   9.921  1.00 69.78           C  
ANISOU  473  CB  ALA A  58     8823   7846   9843    -74   -301   -782       C  
ATOM    474  N   GLN A  59     -15.120 -31.096   9.164  1.00 75.11           N  
ANISOU  474  N   GLN A  59     9673   8438  10427    194   -200   -840       N  
ATOM    475  CA  GLN A  59     -13.897 -30.855   8.395  1.00 72.35           C  
ANISOU  475  CA  GLN A  59     9359   8155   9974    306   -174   -895       C  
ATOM    476  C   GLN A  59     -12.754 -30.381   9.292  1.00 74.56           C  
ANISOU  476  C   GLN A  59     9587   8524  10220    402   -117   -769       C  
ATOM    477  O   GLN A  59     -12.092 -29.376   9.024  1.00 88.21           O  
ANISOU  477  O   GLN A  59    11276  10397  11845    444   -111   -761       O  
ATOM    478  CB  GLN A  59     -14.154 -29.866   7.258  1.00 73.70           C  
ANISOU  478  CB  GLN A  59     9528   8454  10020    280   -228   -987       C  
ATOM    479  CG  GLN A  59     -15.076 -30.413   6.186  1.00 86.55           C  
ANISOU  479  CG  GLN A  59    11222  10001  11662    207   -300  -1134       C  
ATOM    480  CD  GLN A  59     -15.838 -29.323   5.467  1.00 91.47           C  
ANISOU  480  CD  GLN A  59    11815  10755  12186    145   -383  -1179       C  
ATOM    481  OE1 GLN A  59     -15.339 -28.212   5.290  1.00 80.59           O  
ANISOU  481  OE1 GLN A  59    10407   9522  10692    188   -370  -1140       O  
ATOM    482  NE2 GLN A  59     -17.063 -29.632   5.058  1.00100.99           N  
ANISOU  482  NE2 GLN A  59    13024  11904  13445     42   -473  -1258       N  
ATOM    483  N   CYS A  60     -12.519 -31.129  10.364  1.00 63.32           N  
ANISOU  483  N   CYS A  60     8165   7007   8886    434    -79   -669       N  
ATOM    484  CA  CYS A  60     -11.439 -30.859  11.301  1.00 63.64           C  
ANISOU  484  CA  CYS A  60     8160   7117   8903    529    -43   -549       C  
ATOM    485  C   CYS A  60     -10.249 -31.767  11.023  1.00 57.71           C  
ANISOU  485  C   CYS A  60     7450   6286   8190    659      6   -568       C  
ATOM    486  O   CYS A  60     -10.351 -32.786  10.337  1.00 64.96           O  
ANISOU  486  O   CYS A  60     8449   7060   9171    674     23   -659       O  
ATOM    487  CB  CYS A  60     -11.906 -31.067  12.744  1.00 66.18           C  
ANISOU  487  CB  CYS A  60     8463   7401   9281    497    -35   -409       C  
ATOM    488  SG  CYS A  60     -12.183 -32.812  13.168  1.00 77.43           S  
ANISOU  488  SG  CYS A  60     9975   8583  10862    504      4   -374       S  
ATOM    489  N   GLN A  61      -9.110 -31.395  11.597  1.00 65.20           N  
ANISOU  489  N   GLN A  61     8339   7326   9107    756     27   -483       N  
ATOM    490  CA  GLN A  61      -7.917 -32.230  11.588  1.00 68.25           C  
ANISOU  490  CA  GLN A  61     8739   7648   9547    898     74   -469       C  
ATOM    491  C   GLN A  61      -7.544 -32.547  13.028  1.00 70.06           C  
ANISOU  491  C   GLN A  61     8941   7857   9823    951     67   -311       C  
ATOM    492  O   GLN A  61      -7.314 -31.633  13.829  1.00 65.78           O  
ANISOU  492  O   GLN A  61     8325   7453   9218    942     35   -222       O  
ATOM    493  CB  GLN A  61      -6.763 -31.536  10.863  1.00 74.93           C  
ANISOU  493  CB  GLN A  61     9520   8630  10318    979    102   -513       C  
ATOM    494  CG  GLN A  61      -5.560 -32.425  10.634  1.00 86.45           C  
ANISOU  494  CG  GLN A  61    10983  10024  11840   1134    163   -522       C  
ATOM    495  CD  GLN A  61      -4.513 -31.762   9.765  1.00 94.25           C  
ANISOU  495  CD  GLN A  61    11903  11146  12761   1203    211   -577       C  
ATOM    496  OE1 GLN A  61      -4.339 -30.543   9.802  1.00 94.61           O  
ANISOU  496  OE1 GLN A  61    11867  11354  12728   1154    190   -547       O  
ATOM    497  NE2 GLN A  61      -3.815 -32.562   8.968  1.00100.63           N  
ANISOU  497  NE2 GLN A  61    12749  11882  13605   1316    284   -657       N  
ATOM    498  N   LEU A  62      -7.496 -33.835  13.358  1.00 68.36           N  
ANISOU  498  N   LEU A  62     8795   7465   9713   1008     94   -276       N  
ATOM    499  CA  LEU A  62      -7.165 -34.275  14.705  1.00 60.68           C  
ANISOU  499  CA  LEU A  62     7818   6455   8781   1070     88   -115       C  
ATOM    500  C   LEU A  62      -5.677 -34.580  14.800  1.00 63.64           C  
ANISOU  500  C   LEU A  62     8148   6855   9179   1242    102    -75       C  
ATOM    501  O   LEU A  62      -5.139 -35.346  13.994  1.00 65.19           O  
ANISOU  501  O   LEU A  62     8378   6953   9439   1332    147   -156       O  
ATOM    502  CB  LEU A  62      -7.978 -35.509  15.088  1.00 52.90           C  
ANISOU  502  CB  LEU A  62     6938   5253   7909   1034    112    -75       C  
ATOM    503  CG  LEU A  62      -9.476 -35.285  15.256  1.00 65.13           C  
ANISOU  503  CG  LEU A  62     8509   6776   9460    864    101    -80       C  
ATOM    504  CD1 LEU A  62     -10.158 -36.610  15.516  1.00 67.49           C  
ANISOU  504  CD1 LEU A  62     8906   6841   9897    828    136    -46       C  
ATOM    505  CD2 LEU A  62      -9.735 -34.308  16.391  1.00 68.97           C  
ANISOU  505  CD2 LEU A  62     8934   7416   9857    821     76     42       C  
ATOM    506  N   MET A  63      -5.021 -33.980  15.788  1.00 55.63           N  
ANISOU  506  N   MET A  63     7052   5971   8112   1290     59     43       N  
ATOM    507  CA  MET A  63      -3.598 -34.173  16.017  1.00 58.50           C  
ANISOU  507  CA  MET A  63     7343   6381   8503   1451     53     97       C  
ATOM    508  C   MET A  63      -3.384 -34.608  17.456  1.00 62.74           C  
ANISOU  508  C   MET A  63     7893   6891   9054   1515      7    269       C  
ATOM    509  O   MET A  63      -3.894 -33.970  18.382  1.00 67.78           O  
ANISOU  509  O   MET A  63     8528   7613   9612   1438    -40    349       O  
ATOM    510  CB  MET A  63      -2.810 -32.893  15.735  1.00 67.55           C  
ANISOU  510  CB  MET A  63     8357   7743   9568   1451     26     65       C  
ATOM    511  CG  MET A  63      -2.795 -32.473  14.282  1.00 81.76           C  
ANISOU  511  CG  MET A  63    10142   9580  11343   1416     81    -88       C  
ATOM    512  SD  MET A  63      -1.914 -30.918  14.083  1.00 99.78           S  
ANISOU  512  SD  MET A  63    12269  12103  13539   1398     57    -95       S  
ATOM    513  CE  MET A  63      -0.445 -31.245  15.056  1.00105.60           C  
ANISOU  513  CE  MET A  63    12891  12891  14342   1558     17     28       C  
ATOM    514  N   LYS A  64      -2.635 -35.689  17.637  1.00 50.64           N  
ANISOU  514  N   LYS A  64     6383   5241   7617   1665     24    325       N  
ATOM    515  CA  LYS A  64      -2.236 -36.159  18.955  1.00 55.10           C  
ANISOU  515  CA  LYS A  64     6959   5784   8191   1759    -27    499       C  
ATOM    516  C   LYS A  64      -0.779 -35.777  19.173  1.00 58.71           C  
ANISOU  516  C   LYS A  64     7277   6389   8642   1898    -82    539       C  
ATOM    517  O   LYS A  64       0.092 -36.175  18.393  1.00 61.18           O  
ANISOU  517  O   LYS A  64     7535   6676   9036   2013    -41    475       O  
ATOM    518  CB  LYS A  64      -2.421 -37.671  19.077  1.00 61.14           C  
ANISOU  518  CB  LYS A  64     7849   6301   9081   1837     22    554       C  
ATOM    519  CG  LYS A  64      -3.817 -38.153  18.740  1.00 67.56           C  
ANISOU  519  CG  LYS A  64     8787   6948   9934   1692     80    500       C  
ATOM    520  CD  LYS A  64      -3.882 -39.668  18.765  1.00 72.60           C  
ANISOU  520  CD  LYS A  64     9547   7321  10716   1771    131    542       C  
ATOM    521  CE  LYS A  64      -5.216 -40.172  18.247  1.00 75.27           C  
ANISOU  521  CE  LYS A  64     9995   7485  11120   1616    184    460       C  
ATOM    522  NZ  LYS A  64      -5.219 -41.651  18.120  1.00 76.14           N  
ANISOU  522  NZ  LYS A  64    10226   7315  11387   1689    236    476       N  
ATOM    523  N   THR A  65      -0.517 -34.996  20.219  1.00 61.97           N  
ANISOU  523  N   THR A  65     7628   6959   8959   1888   -175    638       N  
ATOM    524  CA  THR A  65       0.827 -34.520  20.513  1.00 65.80           C  
ANISOU  524  CA  THR A  65     7962   7601   9437   1998   -251    676       C  
ATOM    525  C   THR A  65       1.195 -34.848  21.952  1.00 64.06           C  
ANISOU  525  C   THR A  65     7759   7398   9183   2091   -350    852       C  
ATOM    526  O   THR A  65       0.327 -34.991  22.817  1.00 56.52           O  
ANISOU  526  O   THR A  65     6921   6395   8157   2030   -364    941       O  
ATOM    527  CB  THR A  65       0.961 -33.001  20.288  1.00 70.41           C  
ANISOU  527  CB  THR A  65     8431   8395   9927   1886   -292    601       C  
ATOM    528  OG1 THR A  65       0.218 -32.296  21.290  1.00 69.01           O  
ANISOU  528  OG1 THR A  65     8303   8292   9626   1779   -358    662       O  
ATOM    529  CG2 THR A  65       0.432 -32.609  18.917  1.00 76.01           C  
ANISOU  529  CG2 THR A  65     9148   9091  10642   1783   -198    443       C  
ATOM    530  N   GLU A  66       2.499 -34.969  22.197  1.00 59.42           N  
ANISOU  530  N   GLU A  66     7048   6885   8643   2244   -417    905       N  
ATOM    531  CA  GLU A  66       3.038 -35.091  23.544  1.00 57.54           C  
ANISOU  531  CA  GLU A  66     6799   6710   8354   2342   -544   1066       C  
ATOM    532  C   GLU A  66       3.631 -33.783  24.051  1.00 66.59           C  
ANISOU  532  C   GLU A  66     7807   8095   9400   2294   -668   1060       C  
ATOM    533  O   GLU A  66       4.132 -33.740  25.179  1.00 68.01           O  
ANISOU  533  O   GLU A  66     7968   8357   9517   2368   -797   1179       O  
ATOM    534  CB  GLU A  66       4.098 -36.198  23.596  1.00 56.63           C  
ANISOU  534  CB  GLU A  66     6639   6508   8371   2561   -558   1146       C  
ATOM    535  CG  GLU A  66       3.618 -37.559  23.106  1.00 62.44           C  
ANISOU  535  CG  GLU A  66     7517   6982   9223   2623   -439   1150       C  
ATOM    536  CD  GLU A  66       2.236 -37.922  23.624  1.00 73.32           C  
ANISOU  536  CD  GLU A  66     9093   8225  10539   2505   -397   1209       C  
ATOM    537  OE1 GLU A  66       1.324 -38.119  22.792  1.00 72.89           O  
ANISOU  537  OE1 GLU A  66     9123   8050  10523   2393   -288   1100       O  
ATOM    538  OE2 GLU A  66       2.057 -38.008  24.858  1.00 73.74           O  
ANISOU  538  OE2 GLU A  66     9217   8298  10503   2523   -473   1363       O  
ATOM    539  N   ARG A  67       3.583 -32.722  23.246  1.00 61.48           N  
ANISOU  539  N   ARG A  67     7070   7555   8734   2172   -638    924       N  
ATOM    540  CA  ARG A  67       4.077 -31.405  23.605  1.00 66.44           C  
ANISOU  540  CA  ARG A  67     7571   8391   9282   2101   -745    898       C  
ATOM    541  C   ARG A  67       2.981 -30.372  23.390  1.00 71.77           C  
ANISOU  541  C   ARG A  67     8313   9107   9850   1906   -707    810       C  
ATOM    542  O   ARG A  67       2.232 -30.455  22.408  1.00 69.63           O  
ANISOU  542  O   ARG A  67     8099   8747   9608   1829   -587    718       O  
ATOM    543  CB  ARG A  67       5.314 -31.036  22.774  1.00 57.62           C  
ANISOU  543  CB  ARG A  67     6246   7374   8274   2155   -741    827       C  
ATOM    544  CG  ARG A  67       6.485 -31.981  22.959  1.00 59.14           C  
ANISOU  544  CG  ARG A  67     6340   7543   8588   2362   -780    910       C  
ATOM    545  CD  ARG A  67       6.922 -32.037  24.412  1.00 50.78           C  
ANISOU  545  CD  ARG A  67     5273   6561   7461   2439   -956   1051       C  
ATOM    546  NE  ARG A  67       8.142 -32.818  24.592  1.00 58.43           N  
ANISOU  546  NE  ARG A  67     6116   7532   8553   2644  -1015   1133       N  
ATOM    547  CZ  ARG A  67       8.169 -34.104  24.933  1.00 63.15           C  
ANISOU  547  CZ  ARG A  67     6809   7979   9206   2803  -1003   1241       C  
ATOM    548  NH1 ARG A  67       7.040 -34.768  25.138  1.00 64.59           N  
ANISOU  548  NH1 ARG A  67     7213   7993   9335   2767   -929   1282       N  
ATOM    549  NH2 ARG A  67       9.330 -34.726  25.070  1.00 56.82           N  
ANISOU  549  NH2 ARG A  67     5874   7190   8524   2998  -1063   1312       N  
ATOM    550  N   PRO A  68       2.862 -29.375  24.281  1.00 79.77           N  
ANISOU  550  N   PRO A  68     9320  10252  10736   1826   -813    830       N  
ATOM    551  CA  PRO A  68       3.740 -29.135  25.431  1.00 82.42           C  
ANISOU  551  CA  PRO A  68     9587  10711  11016   1901   -977    920       C  
ATOM    552  C   PRO A  68       3.480 -30.090  26.591  1.00 78.74           C  
ANISOU  552  C   PRO A  68     9260  10172  10488   2002  -1026   1071       C  
ATOM    553  O   PRO A  68       4.330 -30.229  27.469  1.00 87.85           O  
ANISOU  553  O   PRO A  68    10362  11403  11614   2110  -1163   1164       O  
ATOM    554  CB  PRO A  68       3.395 -27.703  25.830  1.00 76.40           C  
ANISOU  554  CB  PRO A  68     8817  10083  10126   1752  -1046    857       C  
ATOM    555  CG  PRO A  68       1.955 -27.579  25.478  1.00 78.81           C  
ANISOU  555  CG  PRO A  68     9269  10299  10378   1631   -924    807       C  
ATOM    556  CD  PRO A  68       1.767 -28.390  24.219  1.00 79.33           C  
ANISOU  556  CD  PRO A  68     9337  10228  10576   1655   -782    757       C  
ATOM    557  N   ARG A  69       2.316 -30.738  26.583  1.00 73.78           N  
ANISOU  557  N   ARG A  69     8801   9395   9838   1964   -916   1100       N  
ATOM    558  CA  ARG A  69       1.915 -31.655  27.636  1.00 74.91           C  
ANISOU  558  CA  ARG A  69     9095   9447   9919   2041   -931   1254       C  
ATOM    559  C   ARG A  69       1.547 -33.006  27.034  1.00 68.17           C  
ANISOU  559  C   ARG A  69     8325   8375   9200   2104   -802   1286       C  
ATOM    560  O   ARG A  69       0.887 -33.060  25.990  1.00 62.86           O  
ANISOU  560  O   ARG A  69     7672   7612   8600   2015   -679   1178       O  
ATOM    561  CB  ARG A  69       0.723 -31.087  28.427  1.00 73.70           C  
ANISOU  561  CB  ARG A  69     9082   9321   9598   1916   -916   1275       C  
ATOM    562  CG  ARG A  69       0.236 -31.978  29.558  1.00 81.55           C  
ANISOU  562  CG  ARG A  69    10244  10230  10510   1984   -913   1447       C  
ATOM    563  CD  ARG A  69      -1.038 -31.441  30.194  1.00 87.54           C  
ANISOU  563  CD  ARG A  69    11135  11008  11117   1854   -857   1456       C  
ATOM    564  NE  ARG A  69      -0.799 -30.374  31.160  1.00 93.96           N  
ANISOU  564  NE  ARG A  69    11944  12007  11748   1833   -984   1455       N  
ATOM    565  CZ  ARG A  69      -1.752 -29.807  31.894  1.00100.93           C  
ANISOU  565  CZ  ARG A  69    12941  12936  12473   1746   -953   1466       C  
ATOM    566  NH1 ARG A  69      -1.447 -28.841  32.750  1.00106.27           N  
ANISOU  566  NH1 ARG A  69    13620  13778  12981   1736  -1077   1449       N  
ATOM    567  NH2 ARG A  69      -3.012 -30.206  31.776  1.00100.18           N  
ANISOU  567  NH2 ARG A  69    12953  12720  12389   1668   -797   1489       N  
ATOM    568  N   PRO A  70       1.968 -34.109  27.656  1.00 61.55           N  
ANISOU  568  N   PRO A  70     7544   7444   8398   2259   -834   1432       N  
ATOM    569  CA  PRO A  70       1.578 -35.435  27.161  1.00 59.15           C  
ANISOU  569  CA  PRO A  70     7340   6906   8227   2316   -712   1467       C  
ATOM    570  C   PRO A  70       0.066 -35.629  27.178  1.00 70.74           C  
ANISOU  570  C   PRO A  70     8970   8249   9658   2171   -593   1466       C  
ATOM    571  O   PRO A  70      -0.668 -34.970  27.918  1.00 74.20           O  
ANISOU  571  O   PRO A  70     9473   8770   9951   2068   -609   1497       O  
ATOM    572  CB  PRO A  70       2.275 -36.398  28.134  1.00 71.40           C  
ANISOU  572  CB  PRO A  70     8937   8405   9787   2506   -794   1653       C  
ATOM    573  CG  PRO A  70       2.595 -35.564  29.343  1.00 72.14           C  
ANISOU  573  CG  PRO A  70     9012   8699   9698   2508   -949   1730       C  
ATOM    574  CD  PRO A  70       2.881 -34.199  28.805  1.00 72.01           C  
ANISOU  574  CD  PRO A  70     8840   8869   9651   2396   -993   1568       C  
ATOM    575  N   ASN A  71      -0.392 -36.558  26.334  1.00 66.53           N  
ANISOU  575  N   ASN A  71     8499   7512   9267   2166   -473   1424       N  
ATOM    576  CA  ASN A  71      -1.817 -36.872  26.184  1.00 57.74           C  
ANISOU  576  CA  ASN A  71     7519   6258   8163   2024   -356   1411       C  
ATOM    577  C   ASN A  71      -2.618 -35.644  25.752  1.00 57.44           C  
ANISOU  577  C   ASN A  71     7438   6345   8043   1840   -332   1276       C  
ATOM    578  O   ASN A  71      -3.753 -35.431  26.184  1.00 59.91           O  
ANISOU  578  O   ASN A  71     7834   6642   8286   1719   -283   1303       O  
ATOM    579  CB  ASN A  71      -2.390 -37.478  27.465  1.00 59.98           C  
ANISOU  579  CB  ASN A  71     7952   6464   8375   2040   -348   1605       C  
ATOM    580  CG  ASN A  71      -1.851 -38.861  27.737  1.00 83.18           C  
ANISOU  580  CG  ASN A  71    10965   9218  11423   2207   -342   1742       C  
ATOM    581  OD1 ASN A  71      -1.637 -39.644  26.812  1.00 92.51           O  
ANISOU  581  OD1 ASN A  71    12142  10238  12770   2256   -282   1674       O  
ATOM    582  ND2 ASN A  71      -1.619 -39.171  29.008  1.00 92.75           N  
ANISOU  582  ND2 ASN A  71    12255  10449  12537   2302   -405   1936       N  
ATOM    583  N   THR A  72      -2.019 -34.831  24.891  1.00 46.16           N  
ANISOU  583  N   THR A  72     5875   5038   6627   1825   -362   1135       N  
ATOM    584  CA  THR A  72      -2.696 -33.686  24.303  1.00 50.47           C  
ANISOU  584  CA  THR A  72     6376   5686   7113   1665   -339    999       C  
ATOM    585  C   THR A  72      -3.255 -34.068  22.938  1.00 51.79           C  
ANISOU  585  C   THR A  72     6558   5725   7395   1599   -237    864       C  
ATOM    586  O   THR A  72      -2.627 -34.818  22.185  1.00 51.66           O  
ANISOU  586  O   THR A  72     6522   5612   7493   1693   -206    821       O  
ATOM    587  CB  THR A  72      -1.733 -32.500  24.164  1.00 48.17           C  
ANISOU  587  CB  THR A  72     5936   5602   6764   1676   -430    932       C  
ATOM    588  OG1 THR A  72      -1.331 -32.049  25.464  1.00 54.61           O  
ANISOU  588  OG1 THR A  72     6748   6545   7457   1717   -541   1040       O  
ATOM    589  CG2 THR A  72      -2.381 -31.344  23.418  1.00 45.61           C  
ANISOU  589  CG2 THR A  72     5571   5363   6395   1521   -399    792       C  
ATOM    590  N   PHE A  73      -4.449 -33.573  22.630  1.00 44.05           N  
ANISOU  590  N   PHE A  73     5614   4741   6380   1443   -187    794       N  
ATOM    591  CA  PHE A  73      -4.971 -33.663  21.277  1.00 43.01           C  
ANISOU  591  CA  PHE A  73     5481   4533   6327   1365   -119    643       C  
ATOM    592  C   PHE A  73      -5.492 -32.300  20.851  1.00 42.15           C  
ANISOU  592  C   PHE A  73     5313   4573   6130   1236   -132    541       C  
ATOM    593  O   PHE A  73      -6.004 -31.527  21.665  1.00 51.27           O  
ANISOU  593  O   PHE A  73     6472   5825   7184   1168   -160    588       O  
ATOM    594  CB  PHE A  73      -6.055 -34.747  21.135  1.00 46.71           C  
ANISOU  594  CB  PHE A  73     6069   4789   6890   1305    -40    656       C  
ATOM    595  CG  PHE A  73      -7.307 -34.487  21.920  1.00 42.48           C  
ANISOU  595  CG  PHE A  73     5589   4254   6297   1181    -15    723       C  
ATOM    596  CD1 PHE A  73      -7.399 -34.858  23.253  1.00 47.60           C  
ANISOU  596  CD1 PHE A  73     6304   4883   6900   1220    -18    895       C  
ATOM    597  CD2 PHE A  73      -8.412 -33.922  21.308  1.00 41.80           C  
ANISOU  597  CD2 PHE A  73     5491   4184   6206   1032     16    619       C  
ATOM    598  CE1 PHE A  73      -8.561 -34.640  23.968  1.00 47.47           C  
ANISOU  598  CE1 PHE A  73     6338   4868   6829   1110     27    960       C  
ATOM    599  CE2 PHE A  73      -9.576 -33.698  22.014  1.00 46.68           C  
ANISOU  599  CE2 PHE A  73     6145   4805   6786    924     51    681       C  
ATOM    600  CZ  PHE A  73      -9.652 -34.060  23.347  1.00 42.17           C  
ANISOU  600  CZ  PHE A  73     5638   4217   6169    962     65    851       C  
ATOM    601  N   ILE A  74      -5.328 -32.004  19.567  1.00 49.66           N  
ANISOU  601  N   ILE A  74     6214   5540   7114   1212   -109    401       N  
ATOM    602  CA  ILE A  74      -5.620 -30.691  19.012  1.00 47.92           C  
ANISOU  602  CA  ILE A  74     5932   5459   6817   1111   -124    304       C  
ATOM    603  C   ILE A  74      -6.665 -30.852  17.920  1.00 53.08           C  
ANISOU  603  C   ILE A  74     6632   6024   7510   1010    -70    188       C  
ATOM    604  O   ILE A  74      -6.535 -31.724  17.053  1.00 60.86           O  
ANISOU  604  O   ILE A  74     7655   6891   8579   1049    -28    121       O  
ATOM    605  CB  ILE A  74      -4.349 -30.021  18.460  1.00 54.84           C  
ANISOU  605  CB  ILE A  74     6694   6463   7679   1176   -153    253       C  
ATOM    606  CG1 ILE A  74      -3.278 -29.936  19.551  1.00 59.86           C  
ANISOU  606  CG1 ILE A  74     7269   7184   8290   1277   -227    365       C  
ATOM    607  CG2 ILE A  74      -4.666 -28.642  17.894  1.00 59.04           C  
ANISOU  607  CG2 ILE A  74     7173   7125   8134   1068   -165    166       C  
ATOM    608  CD1 ILE A  74      -1.945 -29.430  19.056  1.00 61.93           C  
ANISOU  608  CD1 ILE A  74     7398   7561   8572   1347   -251    326       C  
ATOM    609  N   ILE A  75      -7.704 -30.023  17.974  1.00 47.59           N  
ANISOU  609  N   ILE A  75     5939   5388   6756    888    -77    162       N  
ATOM    610  CA  ILE A  75      -8.690 -29.916  16.905  1.00 51.20           C  
ANISOU  610  CA  ILE A  75     6418   5801   7235    786    -52     45       C  
ATOM    611  C   ILE A  75      -8.349 -28.676  16.094  1.00 56.08           C  
ANISOU  611  C   ILE A  75     6967   6564   7777    761    -76    -42       C  
ATOM    612  O   ILE A  75      -8.271 -27.569  16.641  1.00 52.57           O  
ANISOU  612  O   ILE A  75     6472   6250   7254    733   -112     -9       O  
ATOM    613  CB  ILE A  75     -10.122 -29.843  17.454  1.00 50.90           C  
ANISOU  613  CB  ILE A  75     6415   5727   7198    672    -40     79       C  
ATOM    614  CG1 ILE A  75     -10.393 -31.020  18.393  1.00 49.22           C  
ANISOU  614  CG1 ILE A  75     6271   5375   7055    695     -4    194       C  
ATOM    615  CG2 ILE A  75     -11.128 -29.836  16.314  1.00 37.05           C  
ANISOU  615  CG2 ILE A  75     4673   3923   5482    572    -31    -43       C  
ATOM    616  CD1 ILE A  75     -11.807 -31.058  18.929  1.00 58.81           C  
ANISOU  616  CD1 ILE A  75     7511   6545   8289    580     30    236       C  
ATOM    617  N   ARG A  76      -8.139 -28.858  14.794  1.00 55.00           N  
ANISOU  617  N   ARG A  76     6837   6400   7660    771    -52   -154       N  
ATOM    618  CA  ARG A  76      -7.707 -27.784  13.911  1.00 55.64           C  
ANISOU  618  CA  ARG A  76     6863   6608   7672    758    -59   -228       C  
ATOM    619  C   ARG A  76      -8.698 -27.648  12.766  1.00 57.24           C  
ANISOU  619  C   ARG A  76     7111   6781   7858    674    -55   -340       C  
ATOM    620  O   ARG A  76      -8.958 -28.618  12.049  1.00 59.92           O  
ANISOU  620  O   ARG A  76     7515   7002   8250    683    -32   -412       O  
ATOM    621  CB  ARG A  76      -6.300 -28.059  13.380  1.00 63.39           C  
ANISOU  621  CB  ARG A  76     7802   7611   8671    873    -27   -248       C  
ATOM    622  CG  ARG A  76      -5.858 -27.149  12.260  1.00 67.28           C  
ANISOU  622  CG  ARG A  76     8252   8210   9101    861     -7   -328       C  
ATOM    623  CD  ARG A  76      -4.494 -27.570  11.768  1.00 73.42           C  
ANISOU  623  CD  ARG A  76     8981   9000   9914    982     47   -342       C  
ATOM    624  NE  ARG A  76      -3.466 -27.341  12.778  1.00 76.53           N  
ANISOU  624  NE  ARG A  76     9276   9469  10333   1046     17   -241       N  
ATOM    625  CZ  ARG A  76      -2.239 -27.847  12.722  1.00 76.03           C  
ANISOU  625  CZ  ARG A  76     9147   9413  10329   1168     51   -221       C  
ATOM    626  NH1 ARG A  76      -1.370 -27.585  13.689  1.00 79.79           N  
ANISOU  626  NH1 ARG A  76     9523   9965  10827   1218      0   -127       N  
ATOM    627  NH2 ARG A  76      -1.884 -28.623  11.706  1.00 63.37           N  
ANISOU  627  NH2 ARG A  76     7575   7738   8762   1245    131   -299       N  
ATOM    628  N   CYS A  77      -9.249 -26.448  12.598  1.00 54.28           N  
ANISOU  628  N   CYS A  77     6705   6509   7411    595    -87   -358       N  
ATOM    629  CA  CYS A  77     -10.267 -26.195  11.588  1.00 58.73           C  
ANISOU  629  CA  CYS A  77     7303   7060   7950    515   -103   -452       C  
ATOM    630  C   CYS A  77      -9.967 -24.899  10.853  1.00 59.88           C  
ANISOU  630  C   CYS A  77     7413   7336   8001    500   -115   -487       C  
ATOM    631  O   CYS A  77      -9.450 -23.944  11.440  1.00 60.10           O  
ANISOU  631  O   CYS A  77     7381   7463   7991    504   -124   -426       O  
ATOM    632  CB  CYS A  77     -11.670 -26.107  12.206  1.00 59.09           C  
ANISOU  632  CB  CYS A  77     7355   7075   8024    420   -133   -425       C  
ATOM    633  SG  CYS A  77     -12.229 -27.593  13.059  1.00 76.11           S  
ANISOU  633  SG  CYS A  77     9556   9063  10298    411   -108   -369       S  
ATOM    634  N   LEU A  78     -10.294 -24.879   9.563  1.00 55.01           N  
ANISOU  634  N   LEU A  78     6841   6715   7345    481   -116   -585       N  
ATOM    635  CA  LEU A  78     -10.350 -23.643   8.794  1.00 45.85           C  
ANISOU  635  CA  LEU A  78     5667   5663   6091    449   -132   -613       C  
ATOM    636  C   LEU A  78     -11.774 -23.111   8.867  1.00 43.16           C  
ANISOU  636  C   LEU A  78     5330   5327   5742    358   -196   -621       C  
ATOM    637  O   LEU A  78     -12.711 -23.760   8.390  1.00 43.15           O  
ANISOU  637  O   LEU A  78     5373   5252   5771    317   -227   -686       O  
ATOM    638  CB  LEU A  78      -9.938 -23.857   7.337  1.00 45.09           C  
ANISOU  638  CB  LEU A  78     5628   5572   5934    487   -100   -707       C  
ATOM    639  CG  LEU A  78      -9.989 -22.591   6.471  1.00 45.86           C  
ANISOU  639  CG  LEU A  78     5725   5777   5921    458   -110   -722       C  
ATOM    640  CD1 LEU A  78      -8.887 -21.606   6.848  1.00 40.51           C  
ANISOU  640  CD1 LEU A  78     4971   5198   5223    483    -70   -643       C  
ATOM    641  CD2 LEU A  78      -9.934 -22.897   4.979  1.00 48.31           C  
ANISOU  641  CD2 LEU A  78     6122   6084   6149    486    -89   -824       C  
ATOM    642  N   GLN A  79     -11.938 -21.955   9.497  1.00 43.60           N  
ANISOU  642  N   GLN A  79     5335   5463   5769    327   -216   -559       N  
ATOM    643  CA  GLN A  79     -13.220 -21.266   9.560  1.00 49.56           C  
ANISOU  643  CA  GLN A  79     6079   6237   6517    256   -269   -562       C  
ATOM    644  C   GLN A  79     -13.112 -19.989   8.738  1.00 47.26           C  
ANISOU  644  C   GLN A  79     5787   6036   6135    248   -288   -576       C  
ATOM    645  O   GLN A  79     -12.346 -19.084   9.089  1.00 43.53           O  
ANISOU  645  O   GLN A  79     5281   5629   5629    263   -269   -525       O  
ATOM    646  CB  GLN A  79     -13.619 -20.964  11.005  1.00 54.97           C  
ANISOU  646  CB  GLN A  79     6718   6929   7240    233   -270   -480       C  
ATOM    647  CG  GLN A  79     -13.770 -22.217  11.852  1.00 67.71           C  
ANISOU  647  CG  GLN A  79     8342   8449   8937    240   -243   -446       C  
ATOM    648  CD  GLN A  79     -14.537 -21.969  13.135  1.00 74.28           C  
ANISOU  648  CD  GLN A  79     9144   9286   9795    206   -238   -374       C  
ATOM    649  OE1 GLN A  79     -14.543 -20.858  13.669  1.00 70.30           O  
ANISOU  649  OE1 GLN A  79     8610   8860   9240    202   -248   -340       O  
ATOM    650  NE2 GLN A  79     -15.194 -23.007  13.636  1.00 80.68           N  
ANISOU  650  NE2 GLN A  79     9965  10004  10685    181   -216   -351       N  
ATOM    651  N   TRP A  80     -13.872 -19.935   7.643  1.00 52.81           N  
ANISOU  651  N   TRP A  80     6529   6736   6799    223   -331   -643       N  
ATOM    652  CA  TRP A  80     -13.754 -18.901   6.621  1.00 50.05           C  
ANISOU  652  CA  TRP A  80     6205   6460   6351    227   -347   -657       C  
ATOM    653  C   TRP A  80     -12.326 -18.845   6.092  1.00 44.12           C  
ANISOU  653  C   TRP A  80     5473   5747   5545    282   -274   -653       C  
ATOM    654  O   TRP A  80     -11.950 -19.649   5.232  1.00 46.96           O  
ANISOU  654  O   TRP A  80     5887   6082   5874    318   -246   -717       O  
ATOM    655  CB  TRP A  80     -14.209 -17.537   7.155  1.00 41.76           C  
ANISOU  655  CB  TRP A  80     5112   5465   5290    197   -376   -596       C  
ATOM    656  CG  TRP A  80     -14.514 -16.541   6.055  1.00 50.38           C  
ANISOU  656  CG  TRP A  80     6240   6610   6292    193   -413   -607       C  
ATOM    657  CD1 TRP A  80     -14.047 -15.264   5.952  1.00 47.68           C  
ANISOU  657  CD1 TRP A  80     5895   6323   5900    197   -398   -553       C  
ATOM    658  CD2 TRP A  80     -15.340 -16.757   4.899  1.00 52.44           C  
ANISOU  658  CD2 TRP A  80     6554   6869   6502    186   -477   -673       C  
ATOM    659  NE1 TRP A  80     -14.536 -14.667   4.813  1.00 53.84           N  
ANISOU  659  NE1 TRP A  80     6727   7132   6597    199   -441   -569       N  
ATOM    660  CE2 TRP A  80     -15.330 -15.564   4.149  1.00 48.85           C  
ANISOU  660  CE2 TRP A  80     6130   6475   5956    195   -496   -644       C  
ATOM    661  CE3 TRP A  80     -16.089 -17.841   4.428  1.00 59.79           C  
ANISOU  661  CE3 TRP A  80     7512   7749   7458    168   -528   -754       C  
ATOM    662  CZ2 TRP A  80     -16.037 -15.426   2.956  1.00 50.35           C  
ANISOU  662  CZ2 TRP A  80     6381   6687   6064    198   -569   -688       C  
ATOM    663  CZ3 TRP A  80     -16.790 -17.702   3.242  1.00 60.45           C  
ANISOU  663  CZ3 TRP A  80     7649   7856   7465    163   -608   -812       C  
ATOM    664  CH2 TRP A  80     -16.759 -16.504   2.521  1.00 55.85           C  
ANISOU  664  CH2 TRP A  80     7100   7345   6777    183   -630   -776       C  
ATOM    665  N   THR A  81     -11.519 -17.905   6.590  1.00 37.81           N  
ANISOU  665  N   THR A  81     4625   5006   4736    288   -241   -582       N  
ATOM    666  CA  THR A  81     -10.146 -17.743   6.119  1.00 42.15           C  
ANISOU  666  CA  THR A  81     5165   5601   5251    331   -166   -567       C  
ATOM    667  C   THR A  81      -9.135 -17.755   7.258  1.00 39.72           C  
ANISOU  667  C   THR A  81     4776   5305   5012    351   -134   -506       C  
ATOM    668  O   THR A  81      -7.986 -17.341   7.065  1.00 52.78           O  
ANISOU  668  O   THR A  81     6387   7009   6656    373    -79   -476       O  
ATOM    669  CB  THR A  81      -9.997 -16.448   5.324  1.00 50.98           C  
ANISOU  669  CB  THR A  81     6300   6787   6284    312   -157   -541       C  
ATOM    670  OG1 THR A  81     -10.216 -15.342   6.205  1.00 50.59           O  
ANISOU  670  OG1 THR A  81     6202   6756   6263    269   -192   -478       O  
ATOM    671  CG2 THR A  81     -11.006 -16.404   4.186  1.00 50.12           C  
ANISOU  671  CG2 THR A  81     6277   6676   6091    302   -205   -596       C  
ATOM    672  N   THR A  82      -9.534 -18.201   8.445  1.00 39.78           N  
ANISOU  672  N   THR A  82     4758   5271   5087    342   -169   -482       N  
ATOM    673  CA  THR A  82      -8.643 -18.262   9.594  1.00 40.29           C  
ANISOU  673  CA  THR A  82     4756   5351   5204    366   -159   -422       C  
ATOM    674  C   THR A  82      -8.561 -19.696  10.094  1.00 49.36           C  
ANISOU  674  C   THR A  82     5913   6426   6415    415   -147   -426       C  
ATOM    675  O   THR A  82      -9.588 -20.367  10.233  1.00 49.74           O  
ANISOU  675  O   THR A  82     6006   6405   6488    394   -170   -449       O  
ATOM    676  CB  THR A  82      -9.124 -17.343  10.719  1.00 44.23           C  
ANISOU  676  CB  THR A  82     5227   5871   5706    319   -210   -375       C  
ATOM    677  OG1 THR A  82      -9.280 -16.009  10.218  1.00 54.55           O  
ANISOU  677  OG1 THR A  82     6537   7225   6965    276   -222   -372       O  
ATOM    678  CG2 THR A  82      -8.119 -17.338  11.855  1.00 49.89           C  
ANISOU  678  CG2 THR A  82     5882   6616   6457    344   -216   -320       C  
ATOM    679  N   VAL A  83      -7.343 -20.158  10.360  1.00 49.73           N  
ANISOU  679  N   VAL A  83     5912   6484   6498    479   -112   -400       N  
ATOM    680  CA  VAL A  83      -7.113 -21.474  10.944  1.00 44.72           C  
ANISOU  680  CA  VAL A  83     5286   5776   5931    540   -102   -385       C  
ATOM    681  C   VAL A  83      -7.099 -21.323  12.459  1.00 56.28           C  
ANISOU  681  C   VAL A  83     6714   7252   7418    534   -149   -305       C  
ATOM    682  O   VAL A  83      -6.236 -20.634  13.012  1.00 63.90           O  
ANISOU  682  O   VAL A  83     7609   8292   8377    543   -168   -260       O  
ATOM    683  CB  VAL A  83      -5.798 -22.089  10.439  1.00 53.95           C  
ANISOU  683  CB  VAL A  83     6418   6951   7131    630    -39   -395       C  
ATOM    684  CG1 VAL A  83      -5.499 -23.390  11.171  1.00 52.97           C  
ANISOU  684  CG1 VAL A  83     6299   6743   7085    706    -36   -364       C  
ATOM    685  CG2 VAL A  83      -5.862 -22.329   8.939  1.00 54.63           C  
ANISOU  685  CG2 VAL A  83     6562   7022   7174    645     18   -483       C  
ATOM    686  N   ILE A  84      -8.053 -21.962  13.130  1.00 53.91           N  
ANISOU  686  N   ILE A  84     6462   6880   7143    516   -167   -287       N  
ATOM    687  CA  ILE A  84      -8.157 -21.900  14.582  1.00 56.68           C  
ANISOU  687  CA  ILE A  84     6801   7240   7495    516   -202   -208       C  
ATOM    688  C   ILE A  84      -7.808 -23.263  15.159  1.00 58.10           C  
ANISOU  688  C   ILE A  84     7001   7338   7735    588   -186   -160       C  
ATOM    689  O   ILE A  84      -8.061 -24.309  14.548  1.00 46.60           O  
ANISOU  689  O   ILE A  84     5592   5784   6331    609   -150   -197       O  
ATOM    690  CB  ILE A  84      -9.558 -21.447  15.044  1.00 60.94           C  
ANISOU  690  CB  ILE A  84     7375   7769   8010    440   -220   -204       C  
ATOM    691  CG1 ILE A  84     -10.604 -22.524  14.752  1.00 73.22           C  
ANISOU  691  CG1 ILE A  84     8984   9216   9621    418   -195   -227       C  
ATOM    692  CG2 ILE A  84      -9.947 -20.146  14.358  1.00 62.46           C  
ANISOU  692  CG2 ILE A  84     7554   8027   8153    381   -236   -251       C  
ATOM    693  CD1 ILE A  84     -11.933 -22.278  15.432  1.00 81.22           C  
ANISOU  693  CD1 ILE A  84    10010  10215  10634    353   -199   -203       C  
ATOM    694  N   GLU A  85      -7.207 -23.247  16.345  1.00 57.41           N  
ANISOU  694  N   GLU A  85     6887   7286   7638    630   -219    -79       N  
ATOM    695  CA  GLU A  85      -6.810 -24.464  17.036  1.00 52.56           C  
ANISOU  695  CA  GLU A  85     6296   6600   7074    710   -214    -11       C  
ATOM    696  C   GLU A  85      -7.390 -24.476  18.442  1.00 61.28           C  
ANISOU  696  C   GLU A  85     7441   7704   8140    695   -241     76       C  
ATOM    697  O   GLU A  85      -7.388 -23.455  19.136  1.00 60.61           O  
ANISOU  697  O   GLU A  85     7335   7713   7981    664   -285     95       O  
ATOM    698  CB  GLU A  85      -5.283 -24.602  17.116  1.00 50.52           C  
ANISOU  698  CB  GLU A  85     5962   6393   6841    807   -233     18       C  
ATOM    699  CG  GLU A  85      -4.646 -25.341  15.951  1.00 67.34           C  
ANISOU  699  CG  GLU A  85     8077   8471   9039    872   -175    -40       C  
ATOM    700  CD  GLU A  85      -3.167 -25.604  16.174  1.00 76.87           C  
ANISOU  700  CD  GLU A  85     9193   9724  10290    983   -188      3       C  
ATOM    701  OE1 GLU A  85      -2.558 -24.903  17.011  1.00 79.86           O  
ANISOU  701  OE1 GLU A  85     9500  10203  10639    985   -256     58       O  
ATOM    702  OE2 GLU A  85      -2.613 -26.514  15.519  1.00 79.25           O  
ANISOU  702  OE2 GLU A  85     9492   9961  10661   1070   -134    -22       O  
ATOM    703  N   ARG A  86      -7.883 -25.640  18.853  1.00 54.53           N  
ANISOU  703  N   ARG A  86     6651   6736   7332    718   -208    129       N  
ATOM    704  CA  ARG A  86      -8.289 -25.887  20.229  1.00 43.28           C  
ANISOU  704  CA  ARG A  86     5276   5301   5868    725   -216    235       C  
ATOM    705  C   ARG A  86      -7.521 -27.098  20.731  1.00 51.96           C  
ANISOU  705  C   ARG A  86     6401   6324   7016    832   -217    322       C  
ATOM    706  O   ARG A  86      -7.597 -28.176  20.132  1.00 49.02           O  
ANISOU  706  O   ARG A  86     6062   5824   6738    859   -171    308       O  
ATOM    707  CB  ARG A  86      -9.798 -26.108  20.333  1.00 49.23           C  
ANISOU  707  CB  ARG A  86     6085   5981   6638    637   -161    237       C  
ATOM    708  CG  ARG A  86     -10.604 -24.853  20.064  1.00 53.71           C  
ANISOU  708  CG  ARG A  86     6624   6631   7152    547   -167    170       C  
ATOM    709  CD  ARG A  86     -12.029 -24.990  20.558  1.00 50.59           C  
ANISOU  709  CD  ARG A  86     6266   6191   6767    476   -115    201       C  
ATOM    710  NE  ARG A  86     -12.828 -25.860  19.704  1.00 48.39           N  
ANISOU  710  NE  ARG A  86     6000   5791   6597    425    -73    157       N  
ATOM    711  CZ  ARG A  86     -14.093 -26.180  19.948  1.00 54.36           C  
ANISOU  711  CZ  ARG A  86     6768   6486   7400    352    -23    179       C  
ATOM    712  NH1 ARG A  86     -14.701 -25.703  21.026  1.00 53.02           N  
ANISOU  712  NH1 ARG A  86     6604   6369   7171    332      9    249       N  
ATOM    713  NH2 ARG A  86     -14.751 -26.976  19.116  1.00 57.49           N  
ANISOU  713  NH2 ARG A  86     7169   6770   7905    298     -3    127       N  
ATOM    714  N   THR A  87      -6.772 -26.918  21.813  1.00 50.39           N  
ANISOU  714  N   THR A  87     6192   6201   6753    899   -278    408       N  
ATOM    715  CA  THR A  87      -5.924 -27.965  22.361  1.00 55.28           C  
ANISOU  715  CA  THR A  87     6828   6766   7410   1019   -298    504       C  
ATOM    716  C   THR A  87      -6.506 -28.455  23.679  1.00 57.41           C  
ANISOU  716  C   THR A  87     7193   6996   7622   1031   -290    633       C  
ATOM    717  O   THR A  87      -6.932 -27.650  24.516  1.00 53.45           O  
ANISOU  717  O   THR A  87     6714   6587   7007    986   -314    659       O  
ATOM    718  CB  THR A  87      -4.495 -27.466  22.572  1.00 60.13           C  
ANISOU  718  CB  THR A  87     7345   7502   8000   1100   -388    512       C  
ATOM    719  OG1 THR A  87      -4.455 -26.603  23.713  1.00 83.64           O  
ANISOU  719  OG1 THR A  87    10327  10599  10853   1082   -464    559       O  
ATOM    720  CG2 THR A  87      -4.011 -26.698  21.346  1.00 49.99           C  
ANISOU  720  CG2 THR A  87     5962   6282   6751   1064   -382    391       C  
ATOM    721  N   PHE A  88      -6.514 -29.771  23.859  1.00 50.19           N  
ANISOU  721  N   PHE A  88     6345   5942   6784   1095   -251    716       N  
ATOM    722  CA  PHE A  88      -7.115 -30.406  25.019  1.00 50.78           C  
ANISOU  722  CA  PHE A  88     6525   5953   6817   1107   -220    855       C  
ATOM    723  C   PHE A  88      -6.131 -31.399  25.620  1.00 51.45           C  
ANISOU  723  C   PHE A  88     6640   5981   6926   1254   -261    977       C  
ATOM    724  O   PHE A  88      -5.128 -31.769  25.005  1.00 56.22           O  
ANISOU  724  O   PHE A  88     7183   6566   7613   1344   -293    944       O  
ATOM    725  CB  PHE A  88      -8.425 -31.117  24.653  1.00 49.89           C  
ANISOU  725  CB  PHE A  88     6479   5684   6794   1013   -110    850       C  
ATOM    726  CG  PHE A  88      -9.374 -30.268  23.856  1.00 48.69           C  
ANISOU  726  CG  PHE A  88     6282   5572   6646    881    -78    722       C  
ATOM    727  CD1 PHE A  88     -10.380 -29.552  24.483  1.00 52.90           C  
ANISOU  727  CD1 PHE A  88     6832   6172   7097    795    -47    740       C  
ATOM    728  CD2 PHE A  88      -9.262 -30.190  22.476  1.00 52.24           C  
ANISOU  728  CD2 PHE A  88     6675   5995   7177    852    -77    584       C  
ATOM    729  CE1 PHE A  88     -11.255 -28.770  23.749  1.00 59.39           C  
ANISOU  729  CE1 PHE A  88     7605   7029   7931    686    -24    628       C  
ATOM    730  CE2 PHE A  88     -10.131 -29.413  21.738  1.00 55.94           C  
ANISOU  730  CE2 PHE A  88     7107   6503   7643    740    -60    475       C  
ATOM    731  CZ  PHE A  88     -11.130 -28.702  22.374  1.00 57.72           C  
ANISOU  731  CZ  PHE A  88     7340   6791   7800    658    -38    498       C  
ATOM    732  N   HIS A  89      -6.435 -31.836  26.839  1.00 47.32           N  
ANISOU  732  N   HIS A  89     6215   5434   6329   1286   -253   1126       N  
ATOM    733  CA  HIS A  89      -5.591 -32.791  27.542  1.00 60.38           C  
ANISOU  733  CA  HIS A  89     7916   7032   7992   1434   -298   1268       C  
ATOM    734  C   HIS A  89      -6.457 -33.690  28.410  1.00 59.96           C  
ANISOU  734  C   HIS A  89     8005   6850   7925   1426   -214   1423       C  
ATOM    735  O   HIS A  89      -7.347 -33.206  29.115  1.00 62.30           O  
ANISOU  735  O   HIS A  89     8359   7202   8111   1344   -172   1462       O  
ATOM    736  CB  HIS A  89      -4.550 -32.073  28.405  1.00 62.05           C  
ANISOU  736  CB  HIS A  89     8081   7426   8067   1521   -437   1312       C  
ATOM    737  CG  HIS A  89      -3.976 -32.926  29.491  1.00 60.48           C  
ANISOU  737  CG  HIS A  89     7962   7195   7822   1662   -491   1492       C  
ATOM    738  ND1 HIS A  89      -2.992 -33.863  29.259  1.00 65.40           N  
ANISOU  738  ND1 HIS A  89     8556   7735   8559   1805   -529   1545       N  
ATOM    739  CD2 HIS A  89      -4.249 -32.986  30.817  1.00 58.26           C  
ANISOU  739  CD2 HIS A  89     7795   6954   7388   1691   -512   1636       C  
ATOM    740  CE1 HIS A  89      -2.679 -34.460  30.395  1.00 62.04           C  
ANISOU  740  CE1 HIS A  89     8220   7297   8055   1918   -582   1720       C  
ATOM    741  NE2 HIS A  89      -3.430 -33.950  31.355  1.00 65.99           N  
ANISOU  741  NE2 HIS A  89     8813   7873   8386   1849   -571   1780       N  
ATOM    742  N   VAL A  90      -6.187 -34.993  28.354  1.00 57.61           N  
ANISOU  742  N   VAL A  90     7767   6377   7744   1513   -183   1513       N  
ATOM    743  CA  VAL A  90      -6.801 -35.978  29.233  1.00 68.26           C  
ANISOU  743  CA  VAL A  90     9258   7585   9092   1527   -107   1690       C  
ATOM    744  C   VAL A  90      -5.690 -36.672  30.010  1.00 71.94           C  
ANISOU  744  C   VAL A  90     9769   8036   9529   1713   -192   1845       C  
ATOM    745  O   VAL A  90      -4.515 -36.607  29.647  1.00 68.71           O  
ANISOU  745  O   VAL A  90     9268   7683   9155   1825   -291   1799       O  
ATOM    746  CB  VAL A  90      -7.648 -37.003  28.456  1.00 65.64           C  
ANISOU  746  CB  VAL A  90     8976   7016   8949   1449     17   1666       C  
ATOM    747  CG1 VAL A  90      -8.860 -36.327  27.855  1.00 62.09           C  
ANISOU  747  CG1 VAL A  90     8484   6591   8515   1265     90   1537       C  
ATOM    748  CG2 VAL A  90      -6.813 -37.648  27.370  1.00 55.04           C  
ANISOU  748  CG2 VAL A  90     7583   5564   7766   1533     -8   1574       C  
ATOM    749  N   GLU A  91      -6.073 -37.347  31.095  1.00 77.70           N  
ANISOU  749  N   GLU A  91    10637   8690  10195   1749   -150   2039       N  
ATOM    750  CA  GLU A  91      -5.060 -37.905  31.986  1.00 87.01           C  
ANISOU  750  CA  GLU A  91    11870   9879  11311   1933   -247   2206       C  
ATOM    751  C   GLU A  91      -4.477 -39.220  31.478  1.00 84.51           C  
ANISOU  751  C   GLU A  91    11575   9347  11189   2053   -232   2258       C  
ATOM    752  O   GLU A  91      -3.339 -39.554  31.825  1.00 86.38           O  
ANISOU  752  O   GLU A  91    11793   9611  11418   2228   -342   2339       O  
ATOM    753  CB  GLU A  91      -5.631 -38.093  33.392  1.00 94.02           C  
ANISOU  753  CB  GLU A  91    12914  10780  12030   1940   -210   2408       C  
ATOM    754  CG  GLU A  91      -5.168 -37.022  34.366  1.00101.51           C  
ANISOU  754  CG  GLU A  91    13854  11982  12733   1983   -338   2427       C  
ATOM    755  CD  GLU A  91      -3.652 -36.957  34.483  1.00106.36           C  
ANISOU  755  CD  GLU A  91    14385  12700  13328   2153   -526   2434       C  
ATOM    756  OE1 GLU A  91      -3.014 -38.026  34.597  1.00109.89           O  
ANISOU  756  OE1 GLU A  91    14870  13020  13863   2298   -554   2560       O  
ATOM    757  OE2 GLU A  91      -3.095 -35.837  34.450  1.00104.91           O  
ANISOU  757  OE2 GLU A  91    14090  12718  13053   2141   -646   2315       O  
ATOM    758  N   THR A  92      -5.219 -39.976  30.668  1.00 63.41           N  
ANISOU  758  N   THR A  92     8939   6458   8695   1969   -104   2208       N  
ATOM    759  CA  THR A  92      -4.698 -41.238  30.161  1.00 68.27           C  
ANISOU  759  CA  THR A  92     9589   6849   9501   2084    -83   2243       C  
ATOM    760  C   THR A  92      -4.718 -41.261  28.636  1.00 71.49           C  
ANISOU  760  C   THR A  92     9905   7180  10079   2023    -43   2020       C  
ATOM    761  O   THR A  92      -5.555 -40.600  28.010  1.00 67.66           O  
ANISOU  761  O   THR A  92     9374   6741   9591   1854      9   1876       O  
ATOM    762  CB  THR A  92      -5.499 -42.436  30.691  1.00 75.69           C  
ANISOU  762  CB  THR A  92    10701   7541  10517   2063     35   2418       C  
ATOM    763  OG1 THR A  92      -6.852 -42.357  30.227  1.00 82.80           O  
ANISOU  763  OG1 THR A  92    11620   8358  11481   1853    162   2335       O  
ATOM    764  CG2 THR A  92      -5.487 -42.459  32.212  1.00 74.66           C  
ANISOU  764  CG2 THR A  92    10682   7486  10199   2132      6   2654       C  
ATOM    765  N   PRO A  93      -3.798 -42.000  28.010  1.00 69.05           N  
ANISOU  765  N   PRO A  93     9568   6756   9911   2166    -66   1988       N  
ATOM    766  CA  PRO A  93      -3.856 -42.145  26.547  1.00 71.81           C  
ANISOU  766  CA  PRO A  93     9859   7012  10413   2115    -12   1778       C  
ATOM    767  C   PRO A  93      -5.113 -42.844  26.071  1.00 74.63           C  
ANISOU  767  C   PRO A  93    10321   7141  10893   1963    112   1738       C  
ATOM    768  O   PRO A  93      -5.573 -42.584  24.952  1.00 75.65           O  
ANISOU  768  O   PRO A  93    10404   7253  11087   1849    151   1545       O  
ATOM    769  CB  PRO A  93      -2.599 -42.967  26.223  1.00 71.75           C  
ANISOU  769  CB  PRO A  93     9827   6908  10527   2331    -50   1794       C  
ATOM    770  CG  PRO A  93      -1.701 -42.790  27.405  1.00 74.09           C  
ANISOU  770  CG  PRO A  93    10101   7346  10704   2486   -166   1972       C  
ATOM    771  CD  PRO A  93      -2.605 -42.642  28.587  1.00 68.75           C  
ANISOU  771  CD  PRO A  93     9540   6694   9887   2392   -150   2132       C  
ATOM    772  N   GLU A  94      -5.684 -43.728  26.893  1.00 73.17           N  
ANISOU  772  N   GLU A  94    10276   6780  10744   1955    173   1919       N  
ATOM    773  CA  GLU A  94      -6.900 -44.431  26.502  1.00 77.06           C  
ANISOU  773  CA  GLU A  94    10861   7044  11375   1797    290   1892       C  
ATOM    774  C   GLU A  94      -8.077 -43.471  26.368  1.00 70.48           C  
ANISOU  774  C   GLU A  94     9974   6341  10465   1579    328   1801       C  
ATOM    775  O   GLU A  94      -8.930 -43.649  25.491  1.00 62.95           O  
ANISOU  775  O   GLU A  94     9017   5273   9627   1433    387   1663       O  
ATOM    776  CB  GLU A  94      -7.214 -45.537  27.512  1.00 89.34           C  
ANISOU  776  CB  GLU A  94    12575   8390  12981   1834    354   2132       C  
ATOM    777  CG  GLU A  94      -6.158 -46.640  27.601  1.00100.35           C  
ANISOU  777  CG  GLU A  94    14039   9606  14484   2053    325   2231       C  
ATOM    778  CD  GLU A  94      -4.958 -46.259  28.457  1.00110.42           C  
ANISOU  778  CD  GLU A  94    15270  11075  15608   2255    206   2361       C  
ATOM    779  OE1 GLU A  94      -4.885 -45.097  28.910  1.00111.13           O  
ANISOU  779  OE1 GLU A  94    15276  11441  15509   2220    138   2351       O  
ATOM    780  OE2 GLU A  94      -4.086 -47.126  28.680  1.00113.94           O  
ANISOU  780  OE2 GLU A  94    15768  11393  16132   2451    173   2471       O  
ATOM    781  N   GLU A  95      -8.139 -42.446  27.225  1.00 82.17           N  
ANISOU  781  N   GLU A  95    11413   8058  11750   1561    288   1870       N  
ATOM    782  CA  GLU A  95      -9.200 -41.450  27.107  1.00 81.72           C  
ANISOU  782  CA  GLU A  95    11296   8137  11617   1375    322   1780       C  
ATOM    783  C   GLU A  95      -9.043 -40.621  25.838  1.00 74.41           C  
ANISOU  783  C   GLU A  95    10242   7325  10704   1324    274   1538       C  
ATOM    784  O   GLU A  95     -10.038 -40.272  25.192  1.00 73.29           O  
ANISOU  784  O   GLU A  95    10065   7178  10604   1162    319   1416       O  
ATOM    785  CB  GLU A  95      -9.216 -40.537  28.334  1.00 87.57           C  
ANISOU  785  CB  GLU A  95    12035   9100  12138   1388    290   1901       C  
ATOM    786  CG  GLU A  95      -9.705 -41.193  29.616  1.00 96.59           C  
ANISOU  786  CG  GLU A  95    13314  10154  13233   1397    366   2141       C  
ATOM    787  CD  GLU A  95      -9.776 -40.215  30.778  1.00102.04           C  
ANISOU  787  CD  GLU A  95    14011  11078  13682   1406    337   2235       C  
ATOM    788  OE1 GLU A  95     -10.328 -39.108  30.598  1.00103.55           O  
ANISOU  788  OE1 GLU A  95    14120  11433  13789   1295    340   2116       O  
ATOM    789  OE2 GLU A  95      -9.271 -40.551  31.870  1.00106.46           O  
ANISOU  789  OE2 GLU A  95    14666  11655  14129   1531    308   2425       O  
ATOM    790  N   ARG A  96      -7.801 -40.291  25.469  1.00 72.16           N  
ANISOU  790  N   ARG A  96     9884   7148  10386   1461    185   1472       N  
ATOM    791  CA  ARG A  96      -7.579 -39.477  24.278  1.00 66.51           C  
ANISOU  791  CA  ARG A  96     9053   6547   9670   1419    149   1258       C  
ATOM    792  C   ARG A  96      -8.040 -40.201  23.021  1.00 68.15           C  
ANISOU  792  C   ARG A  96     9288   6561  10046   1353    207   1110       C  
ATOM    793  O   ARG A  96      -8.597 -39.582  22.108  1.00 73.81           O  
ANISOU  793  O   ARG A  96     9947   7336  10761   1235    211    946       O  
ATOM    794  CB  ARG A  96      -6.104 -39.093  24.163  1.00 54.15           C  
ANISOU  794  CB  ARG A  96     7399   5121   8056   1584     56   1235       C  
ATOM    795  CG  ARG A  96      -5.792 -38.240  22.948  1.00 60.81           C  
ANISOU  795  CG  ARG A  96     8125   6087   8893   1547     33   1032       C  
ATOM    796  CD  ARG A  96      -4.375 -37.706  22.988  1.00 58.24           C  
ANISOU  796  CD  ARG A  96     7688   5927   8513   1689    -54   1028       C  
ATOM    797  NE  ARG A  96      -3.381 -38.772  22.980  1.00 59.13           N  
ANISOU  797  NE  ARG A  96     7819   5916   8732   1871    -59   1089       N  
ATOM    798  CZ  ARG A  96      -2.073 -38.564  22.874  1.00 62.51           C  
ANISOU  798  CZ  ARG A  96     8138   6452   9162   2016   -123   1082       C  
ATOM    799  NH1 ARG A  96      -1.608 -37.326  22.764  1.00 54.09           N  
ANISOU  799  NH1 ARG A  96     6941   5613   7997   1985   -185   1017       N  
ATOM    800  NH2 ARG A  96      -1.232 -39.589  22.876  1.00 51.54           N  
ANISOU  800  NH2 ARG A  96     6764   4937   7883   2191   -121   1142       N  
ATOM    801  N   GLU A  97      -7.821 -41.517  22.957  1.00 63.99           N  
ANISOU  801  N   GLU A  97     8855   5795   9661   1432    246   1164       N  
ATOM    802  CA  GLU A  97      -8.261 -42.274  21.791  1.00 67.61           C  
ANISOU  802  CA  GLU A  97     9358   6050  10280   1370    295   1013       C  
ATOM    803  C   GLU A  97      -9.781 -42.318  21.705  1.00 74.39           C  
ANISOU  803  C   GLU A  97    10249   6825  11191   1156    352    985       C  
ATOM    804  O   GLU A  97     -10.350 -42.188  20.614  1.00 80.82           O  
ANISOU  804  O   GLU A  97    11039   7611  12060   1046    355    803       O  
ATOM    805  CB  GLU A  97      -7.689 -43.689  21.830  1.00 76.63           C  
ANISOU  805  CB  GLU A  97    10606   6937  11571   1508    326   1083       C  
ATOM    806  CG  GLU A  97      -7.851 -44.432  20.521  1.00 88.82           C  
ANISOU  806  CG  GLU A  97    12197   8282  13269   1481    362    894       C  
ATOM    807  CD  GLU A  97      -7.030 -43.812  19.411  1.00 98.00           C  
ANISOU  807  CD  GLU A  97    13266   9588  14383   1554    324    705       C  
ATOM    808  OE1 GLU A  97      -5.914 -43.330  19.701  1.00101.00           O  
ANISOU  808  OE1 GLU A  97    13564  10132  14679   1702    279    753       O  
ATOM    809  OE2 GLU A  97      -7.501 -43.792  18.254  1.00101.59           O  
ANISOU  809  OE2 GLU A  97    13726   9996  14878   1461    338    510       O  
ATOM    810  N   GLU A  98     -10.454 -42.507  22.843  1.00 68.06           N  
ANISOU  810  N   GLU A  98     9499   5989  10371   1098    399   1167       N  
ATOM    811  CA  GLU A  98     -11.914 -42.507  22.852  1.00 64.25           C  
ANISOU  811  CA  GLU A  98     9022   5443   9946    892    463   1156       C  
ATOM    812  C   GLU A  98     -12.461 -41.175  22.359  1.00 66.39           C  
ANISOU  812  C   GLU A  98     9173   5939  10112    778    427   1017       C  
ATOM    813  O   GLU A  98     -13.401 -41.135  21.557  1.00 74.81           O  
ANISOU  813  O   GLU A  98    10210   6954  11261    629    440    884       O  
ATOM    814  CB  GLU A  98     -12.431 -42.813  24.258  1.00 66.39           C  
ANISOU  814  CB  GLU A  98     9363   5676  10188    868    533   1395       C  
ATOM    815  CG  GLU A  98     -12.161 -44.237  24.718  1.00 84.86           C  
ANISOU  815  CG  GLU A  98    11838   7747  12658    949    585   1547       C  
ATOM    816  CD  GLU A  98     -12.671 -44.506  26.120  1.00 98.33           C  
ANISOU  816  CD  GLU A  98    13622   9426  14315    927    665   1799       C  
ATOM    817  OE1 GLU A  98     -13.024 -43.536  26.824  1.00101.07           O  
ANISOU  817  OE1 GLU A  98    13918   9989  14496    885    670   1856       O  
ATOM    818  OE2 GLU A  98     -12.721 -45.690  26.517  1.00104.14           O  
ANISOU  818  OE2 GLU A  98    14477   9918  15174    954    728   1940       O  
ATOM    819  N   TRP A  99     -11.873 -40.070  22.822  1.00 61.10           N  
ANISOU  819  N   TRP A  99     8435   5515   9265    847    373   1043       N  
ATOM    820  CA  TRP A  99     -12.318 -38.751  22.387  1.00 57.23           C  
ANISOU  820  CA  TRP A  99     7837   5233   8674    753    338    919       C  
ATOM    821  C   TRP A  99     -12.024 -38.529  20.908  1.00 57.47           C  
ANISOU  821  C   TRP A  99     7818   5276   8745    747    289    704       C  
ATOM    822  O   TRP A  99     -12.904 -38.105  20.150  1.00 62.16           O  
ANISOU  822  O   TRP A  99     8365   5891   9361    615    286    576       O  
ATOM    823  CB  TRP A  99     -11.654 -37.667  23.236  1.00 57.45           C  
ANISOU  823  CB  TRP A  99     7816   5499   8511    835    286    994       C  
ATOM    824  CG  TRP A  99     -12.317 -37.443  24.560  1.00 63.88           C  
ANISOU  824  CG  TRP A  99     8666   6368   9237    792    337   1159       C  
ATOM    825  CD1 TRP A  99     -11.867 -37.845  25.785  1.00 63.99           C  
ANISOU  825  CD1 TRP A  99     8758   6375   9181    893    347   1351       C  
ATOM    826  CD2 TRP A  99     -13.554 -36.758  24.793  1.00 65.26           C  
ANISOU  826  CD2 TRP A  99     8800   6619   9376    647    389   1149       C  
ATOM    827  NE1 TRP A  99     -12.746 -37.453  26.764  1.00 63.59           N  
ANISOU  827  NE1 TRP A  99     8729   6391   9040    817    411   1459       N  
ATOM    828  CE2 TRP A  99     -13.792 -36.785  26.181  1.00 66.64           C  
ANISOU  828  CE2 TRP A  99     9038   6829   9454    667    443   1336       C  
ATOM    829  CE3 TRP A  99     -14.484 -36.125  23.961  1.00 60.23           C  
ANISOU  829  CE3 TRP A  99     8080   6027   8778    510    394   1003       C  
ATOM    830  CZ2 TRP A  99     -14.918 -36.201  26.758  1.00 66.44           C  
ANISOU  830  CZ2 TRP A  99     8990   6881   9373    556    518   1376       C  
ATOM    831  CZ3 TRP A  99     -15.603 -35.548  24.534  1.00 59.69           C  
ANISOU  831  CZ3 TRP A  99     7979   6033   8668    402    456   1046       C  
ATOM    832  CH2 TRP A  99     -15.811 -35.590  25.920  1.00 62.94           C  
ANISOU  832  CH2 TRP A  99     8450   6477   8987    426    526   1228       C  
ATOM    833  N   THR A 100     -10.792 -38.812  20.477  1.00 49.53           N  
ANISOU  833  N   THR A 100     6817   4258   7743    896    253    664       N  
ATOM    834  CA  THR A 100     -10.420 -38.537  19.091  1.00 61.33           C  
ANISOU  834  CA  THR A 100     8268   5784   9249    905    221    465       C  
ATOM    835  C   THR A 100     -11.213 -39.404  18.118  1.00 62.76           C  
ANISOU  835  C   THR A 100     8513   5759   9575    808    250    339       C  
ATOM    836  O   THR A 100     -11.607 -38.937  17.043  1.00 62.92           O  
ANISOU  836  O   THR A 100     8497   5829   9581    730    224    171       O  
ATOM    837  CB  THR A 100      -8.915 -38.736  18.892  1.00 62.63           C  
ANISOU  837  CB  THR A 100     8420   5974   9401   1094    195    461       C  
ATOM    838  OG1 THR A 100      -8.520 -40.008  19.420  1.00 69.68           O  
ANISOU  838  OG1 THR A 100     9405   6669  10401   1198    227    576       O  
ATOM    839  CG2 THR A 100      -8.131 -37.627  19.589  1.00 62.67           C  
ANISOU  839  CG2 THR A 100     8333   6221   9258   1163    140    535       C  
ATOM    840  N   THR A 101     -11.465 -40.665  18.475  1.00 59.23           N  
ANISOU  840  N   THR A 101     8164   5075   9266    810    299    417       N  
ATOM    841  CA  THR A 101     -12.279 -41.521  17.617  1.00 71.98           C  
ANISOU  841  CA  THR A 101     9842   6475  11031    700    318    294       C  
ATOM    842  C   THR A 101     -13.704 -40.992  17.515  1.00 75.70           C  
ANISOU  842  C   THR A 101    10259   6994  11510    496    315    251       C  
ATOM    843  O   THR A 101     -14.271 -40.905  16.419  1.00 81.30           O  
ANISOU  843  O   THR A 101    10953   7683  12255    399    279     73       O  
ATOM    844  CB  THR A 101     -12.285 -42.958  18.143  1.00 74.22           C  
ANISOU  844  CB  THR A 101    10245   6480  11473    735    376    407       C  
ATOM    845  OG1 THR A 101     -10.960 -43.499  18.078  1.00 79.91           O  
ANISOU  845  OG1 THR A 101    11013   7144  12206    938    374    424       O  
ATOM    846  CG2 THR A 101     -13.223 -43.821  17.313  1.00 60.44           C  
ANISOU  846  CG2 THR A 101     8565   4504   9898    594    389    274       C  
ATOM    847  N   ALA A 102     -14.302 -40.642  18.656  1.00 65.03           N  
ANISOU  847  N   ALA A 102     8876   5710  10122    434    352    413       N  
ATOM    848  CA  ALA A 102     -15.656 -40.096  18.651  1.00 63.83           C  
ANISOU  848  CA  ALA A 102     8652   5616   9985    252    359    387       C  
ATOM    849  C   ALA A 102     -15.721 -38.801  17.853  1.00 65.07           C  
ANISOU  849  C   ALA A 102     8709   5996  10017    226    288    240       C  
ATOM    850  O   ALA A 102     -16.642 -38.595  17.054  1.00 68.32           O  
ANISOU  850  O   ALA A 102     9077   6405  10478     96    255    111       O  
ATOM    851  CB  ALA A 102     -16.138 -39.871  20.085  1.00 57.96           C  
ANISOU  851  CB  ALA A 102     7896   4930   9198    222    428    595       C  
ATOM    852  N   ILE A 103     -14.743 -37.916  18.056  1.00 58.92           N  
ANISOU  852  N   ILE A 103     7895   5409   9084    347    257    260       N  
ATOM    853  CA  ILE A 103     -14.706 -36.663  17.308  1.00 55.31           C  
ANISOU  853  CA  ILE A 103     7352   5153   8509    330    195    134       C  
ATOM    854  C   ILE A 103     -14.573 -36.939  15.816  1.00 62.46           C  
ANISOU  854  C   ILE A 103     8280   5996   9456    323    151    -62       C  
ATOM    855  O   ILE A 103     -15.226 -36.291  14.989  1.00 70.09           O  
ANISOU  855  O   ILE A 103     9198   7042  10392    234    104   -186       O  
ATOM    856  CB  ILE A 103     -13.563 -35.770  17.828  1.00 57.61           C  
ANISOU  856  CB  ILE A 103     7606   5636   8647    460    172    198       C  
ATOM    857  CG1 ILE A 103     -13.868 -35.267  19.240  1.00 49.82           C  
ANISOU  857  CG1 ILE A 103     6599   4746   7586    448    202    364       C  
ATOM    858  CG2 ILE A 103     -13.327 -34.597  16.901  1.00 53.62           C  
ANISOU  858  CG2 ILE A 103     7029   5307   8039    456    115     63       C  
ATOM    859  CD1 ILE A 103     -12.717 -34.524  19.877  1.00 61.59           C  
ANISOU  859  CD1 ILE A 103     8063   6401   8936    574    166    432       C  
ATOM    860  N   GLN A 104     -13.741 -37.917  15.449  1.00 56.24           N  
ANISOU  860  N   GLN A 104     7573   5063   8731    426    165    -94       N  
ATOM    861  CA  GLN A 104     -13.527 -38.215  14.037  1.00 60.88           C  
ANISOU  861  CA  GLN A 104     8201   5591   9339    438    133   -288       C  
ATOM    862  C   GLN A 104     -14.778 -38.806  13.397  1.00 65.55           C  
ANISOU  862  C   GLN A 104     8826   6031  10050    280    110   -397       C  
ATOM    863  O   GLN A 104     -15.114 -38.472  12.254  1.00 70.12           O  
ANISOU  863  O   GLN A 104     9397   6653  10591    226     53   -566       O  
ATOM    864  CB  GLN A 104     -12.341 -39.166  13.877  1.00 64.04           C  
ANISOU  864  CB  GLN A 104     8682   5861   9788    599    167   -292       C  
ATOM    865  CG  GLN A 104     -11.923 -39.403  12.437  1.00 68.49           C  
ANISOU  865  CG  GLN A 104     9294   6386  10342    645    150   -494       C  
ATOM    866  CD  GLN A 104     -11.459 -38.132  11.755  1.00 70.62           C  
ANISOU  866  CD  GLN A 104     9486   6897  10448    676    119   -572       C  
ATOM    867  OE1 GLN A 104     -10.358 -37.644  12.009  1.00 77.58           O  
ANISOU  867  OE1 GLN A 104    10317   7907  11254    801    137   -513       O  
ATOM    868  NE2 GLN A 104     -12.302 -37.585  10.890  1.00 67.40           N  
ANISOU  868  NE2 GLN A 104     9065   6552   9992    558     68   -700       N  
ATOM    869  N   THR A 105     -15.479 -39.685  14.119  1.00 66.02           N  
ANISOU  869  N   THR A 105     8920   5913  10252    201    151   -301       N  
ATOM    870  CA  THR A 105     -16.692 -40.285  13.574  1.00 68.68           C  
ANISOU  870  CA  THR A 105     9272   6096  10728     33    126   -400       C  
ATOM    871  C   THR A 105     -17.794 -39.250  13.384  1.00 72.29           C  
ANISOU  871  C   THR A 105     9613   6717  11137   -106     74   -441       C  
ATOM    872  O   THR A 105     -18.549 -39.324  12.408  1.00 77.64           O  
ANISOU  872  O   THR A 105    10281   7358  11862   -215      4   -598       O  
ATOM    873  CB  THR A 105     -17.165 -41.418  14.485  1.00 72.23           C  
ANISOU  873  CB  THR A 105     9776   6318  11351    -25    196   -263       C  
ATOM    874  OG1 THR A 105     -16.121 -42.392  14.609  1.00 75.84           O  
ANISOU  874  OG1 THR A 105    10347   6611  11857    120    237   -226       O  
ATOM    875  CG2 THR A 105     -18.406 -42.087  13.913  1.00 71.99           C  
ANISOU  875  CG2 THR A 105     9751   6113  11490   -213    165   -370       C  
ATOM    876  N   VAL A 106     -17.895 -38.277  14.291  1.00 67.37           N  
ANISOU  876  N   VAL A 106     8903   6276  10419    -99    101   -307       N  
ATOM    877  CA  VAL A 106     -18.858 -37.197  14.110  1.00 58.09           C  
ANISOU  877  CA  VAL A 106     7613   5268   9191   -206     56   -345       C  
ATOM    878  C   VAL A 106     -18.498 -36.358  12.892  1.00 64.66           C  
ANISOU  878  C   VAL A 106     8429   6244   9894   -166    -30   -508       C  
ATOM    879  O   VAL A 106     -19.372 -35.969  12.108  1.00 73.29           O  
ANISOU  879  O   VAL A 106     9472   7382  10995   -267   -103   -622       O  
ATOM    880  CB  VAL A 106     -18.941 -36.333  15.381  1.00 58.16           C  
ANISOU  880  CB  VAL A 106     7550   5432   9114   -186    114   -171       C  
ATOM    881  CG1 VAL A 106     -19.799 -35.102  15.129  1.00 43.15           C  
ANISOU  881  CG1 VAL A 106     5533   3714   7148   -266     67   -220       C  
ATOM    882  CG2 VAL A 106     -19.492 -37.147  16.539  1.00 44.57           C  
ANISOU  882  CG2 VAL A 106     5847   3574   7514   -244    208     -7       C  
ATOM    883  N   ALA A 107     -17.209 -36.061  12.713  1.00 64.71           N  
ANISOU  883  N   ALA A 107     8476   6330   9783    -17    -23   -514       N  
ATOM    884  CA  ALA A 107     -16.790 -35.272  11.560  1.00 61.06           C  
ANISOU  884  CA  ALA A 107     8007   6002   9191     26    -85   -654       C  
ATOM    885  C   ALA A 107     -17.035 -36.028  10.261  1.00 72.25           C  
ANISOU  885  C   ALA A 107     9501   7290  10660    -12   -139   -840       C  
ATOM    886  O   ALA A 107     -17.513 -35.449   9.278  1.00 75.77           O  
ANISOU  886  O   ALA A 107     9927   7821  11039    -64   -217   -966       O  
ATOM    887  CB  ALA A 107     -15.316 -34.892  11.689  1.00 55.90           C  
ANISOU  887  CB  ALA A 107     7369   5447   8424    190    -51   -612       C  
ATOM    888  N   ASP A 108     -16.711 -37.324  10.237  1.00 69.90           N  
ANISOU  888  N   ASP A 108     9301   6780  10476     19   -104   -862       N  
ATOM    889  CA  ASP A 108     -16.963 -38.127   9.045  1.00 80.15           C  
ANISOU  889  CA  ASP A 108    10691   7933  11828    -19   -157  -1052       C  
ATOM    890  C   ASP A 108     -18.453 -38.288   8.781  1.00 83.79           C  
ANISOU  890  C   ASP A 108    11110   8330  12395   -208   -234  -1119       C  
ATOM    891  O   ASP A 108     -18.873 -38.341   7.619  1.00 84.70           O  
ANISOU  891  O   ASP A 108    11261   8435  12488   -262   -324  -1298       O  
ATOM    892  CB  ASP A 108     -16.299 -39.497   9.178  1.00 89.85           C  
ANISOU  892  CB  ASP A 108    12038   8927  13173     60    -96  -1053       C  
ATOM    893  CG  ASP A 108     -14.787 -39.426   9.075  1.00 99.98           C  
ANISOU  893  CG  ASP A 108    13362  10267  14357    258    -38  -1039       C  
ATOM    894  OD1 ASP A 108     -14.274 -38.434   8.514  1.00101.34           O  
ANISOU  894  OD1 ASP A 108    13494  10639  14371    319    -54  -1086       O  
ATOM    895  OD2 ASP A 108     -14.112 -40.365   9.546  1.00104.15           O  
ANISOU  895  OD2 ASP A 108    13958  10639  14975    354     27   -977       O  
ATOM    896  N   GLY A 109     -19.264 -38.371   9.838  1.00 83.21           N  
ANISOU  896  N   GLY A 109    10960   8222  12437   -309   -200   -979       N  
ATOM    897  CA  GLY A 109     -20.702 -38.450   9.650  1.00 83.50           C  
ANISOU  897  CA  GLY A 109    10922   8216  12589   -492   -266  -1029       C  
ATOM    898  C   GLY A 109     -21.292 -37.182   9.071  1.00 80.57           C  
ANISOU  898  C   GLY A 109    10448   8064  12099   -535   -356  -1092       C  
ATOM    899  O   GLY A 109     -22.337 -37.222   8.414  1.00 83.97           O  
ANISOU  899  O   GLY A 109    10832   8476  12594   -664   -454  -1203       O  
ATOM    900  N   LEU A 110     -20.638 -36.044   9.301  1.00 80.70           N  
ANISOU  900  N   LEU A 110    10427   8287  11948   -429   -331  -1023       N  
ATOM    901  CA  LEU A 110     -21.087 -34.777   8.742  1.00 85.71           C  
ANISOU  901  CA  LEU A 110    10979   9126  12461   -450   -411  -1073       C  
ATOM    902  C   LEU A 110     -20.602 -34.546   7.320  1.00 98.46           C  
ANISOU  902  C   LEU A 110    12674  10796  13941   -391   -493  -1245       C  
ATOM    903  O   LEU A 110     -21.094 -33.620   6.665  1.00103.98           O  
ANISOU  903  O   LEU A 110    13321  11640  14547   -420   -578  -1304       O  
ATOM    904  CB  LEU A 110     -20.625 -33.615   9.621  1.00 81.69           C  
ANISOU  904  CB  LEU A 110    10400   8801  11836   -370   -348   -926       C  
ATOM    905  CG  LEU A 110     -21.263 -33.470  11.001  1.00 83.78           C  
ANISOU  905  CG  LEU A 110    10573   9075  12184   -426   -274   -758       C  
ATOM    906  CD1 LEU A 110     -20.835 -32.149  11.613  1.00 81.56           C  
ANISOU  906  CD1 LEU A 110    10236   8995  11760   -347   -242   -660       C  
ATOM    907  CD2 LEU A 110     -22.779 -33.569  10.909  1.00 87.06           C  
ANISOU  907  CD2 LEU A 110    10888   9457  12735   -586   -323   -787       C  
ATOM    908  N   LYS A 111     -19.648 -35.347   6.837  1.00104.72           N  
ANISOU  908  N   LYS A 111    13594  11479  14714   -302   -462  -1321       N  
ATOM    909  CA  LYS A 111     -19.155 -35.190   5.474  1.00112.02           C  
ANISOU  909  CA  LYS A 111    14610  12454  15498   -238   -520  -1487       C  
ATOM    910  C   LYS A 111     -20.313 -35.198   4.484  1.00118.14           C  
ANISOU  910  C   LYS A 111    15380  13223  16284   -362   -663  -1640       C  
ATOM    911  O   LYS A 111     -20.499 -34.248   3.716  1.00121.67           O  
ANISOU  911  O   LYS A 111    15808  13833  16587   -355   -740  -1697       O  
ATOM    912  CB  LYS A 111     -18.147 -36.296   5.153  1.00117.28           C  
ANISOU  912  CB  LYS A 111    15416  12960  16185   -137   -458  -1557       C  
ATOM    913  CG  LYS A 111     -17.040 -35.866   4.205  1.00120.92           C  
ANISOU  913  CG  LYS A 111    15954  13530  16459      4   -436  -1642       C  
ATOM    914  CD  LYS A 111     -16.181 -34.776   4.830  1.00119.86           C  
ANISOU  914  CD  LYS A 111    15738  13583  16219    103   -361  -1493       C  
ATOM    915  CE  LYS A 111     -15.051 -34.355   3.900  1.00117.29           C  
ANISOU  915  CE  LYS A 111    15475  13365  15724    236   -322  -1564       C  
ATOM    916  NZ  LYS A 111     -14.193 -33.300   4.510  1.00109.37           N  
ANISOU  916  NZ  LYS A 111    14383  12535  14638    317   -254  -1422       N  
ATOM    917  N   LYS A 112     -21.114 -36.261   4.512  1.00115.25           N  
ANISOU  917  N   LYS A 112    15028  12667  16095   -481   -705  -1701       N  
ATOM    918  CA  LYS A 112     -22.384 -36.324   3.790  1.00111.56           C  
ANISOU  918  CA  LYS A 112    14520  12184  15684   -628   -854  -1828       C  
ATOM    919  C   LYS A 112     -22.268 -35.963   2.314  1.00110.20           C  
ANISOU  919  C   LYS A 112    14437  12103  15330   -589   -970  -2013       C  
ATOM    920  O   LYS A 112     -22.821 -34.958   1.871  1.00110.86           O  
ANISOU  920  O   LYS A 112    14448  12359  15313   -613  -1063  -2024       O  
ATOM    921  CB  LYS A 112     -23.408 -35.407   4.463  1.00109.31           C  
ANISOU  921  CB  LYS A 112    14052  12033  15449   -719   -881  -1707       C  
ATOM    922  CG  LYS A 112     -24.096 -36.025   5.671  1.00110.26           C  
ANISOU  922  CG  LYS A 112    14078  12024  15792   -828   -811  -1578       C  
ATOM    923  CD  LYS A 112     -24.855 -34.981   6.475  1.00107.96           C  
ANISOU  923  CD  LYS A 112    13612  11892  15517   -873   -792  -1436       C  
ATOM    924  CE  LYS A 112     -25.608 -34.016   5.571  1.00106.33           C  
ANISOU  924  CE  LYS A 112    13327  11850  15222   -909   -939  -1528       C  
ATOM    925  NZ  LYS A 112     -26.584 -34.710   4.687  1.00109.73           N  
ANISOU  925  NZ  LYS A 112    13747  12179  15765  -1046  -1089  -1693       N  
ATOM    926  N   LYS A 142      -4.911 -13.323 -14.783  1.00123.58           N  
ANISOU  926  N   LYS A 142    17296  16952  12706   1005   1155   -503       N  
ATOM    927  CA  LYS A 142      -5.264 -13.972 -16.039  1.00128.18           C  
ANISOU  927  CA  LYS A 142    18113  17590  13000   1100   1143   -626       C  
ATOM    928  C   LYS A 142      -6.504 -14.838 -15.854  1.00126.96           C  
ANISOU  928  C   LYS A 142    18015  17372  12853   1096    883   -804       C  
ATOM    929  O   LYS A 142      -7.383 -14.507 -15.054  1.00126.28           O  
ANISOU  929  O   LYS A 142    17838  17225  12918   1018    690   -780       O  
ATOM    930  CB  LYS A 142      -4.090 -14.806 -16.559  1.00131.99           C  
ANISOU  930  CB  LYS A 142    18620  18115  13413   1195   1389   -701       C  
ATOM    931  CG  LYS A 142      -2.803 -14.008 -16.740  1.00133.07           C  
ANISOU  931  CG  LYS A 142    18674  18321  13565   1194   1666   -525       C  
ATOM    932  CD  LYS A 142      -1.725 -14.812 -17.456  1.00133.30           C  
ANISOU  932  CD  LYS A 142    18752  18411  13484   1309   1920   -601       C  
ATOM    933  CE  LYS A 142      -0.527 -13.936 -17.796  1.00133.44           C  
ANISOU  933  CE  LYS A 142    18699  18511  13491   1303   2202   -412       C  
ATOM    934  NZ  LYS A 142       0.520 -14.667 -18.566  1.00136.21           N  
ANISOU  934  NZ  LYS A 142    19097  18934  13722   1426   2474   -478       N  
ATOM    935  N   HIS A 143      -6.582 -15.939 -16.604  1.00124.94           N  
ANISOU  935  N   HIS A 143    17909  17125  12436   1179    883   -984       N  
ATOM    936  CA  HIS A 143      -7.661 -16.896 -16.383  1.00121.11           C  
ANISOU  936  CA  HIS A 143    17462  16564  11992   1164    649  -1168       C  
ATOM    937  C   HIS A 143      -7.598 -17.451 -14.966  1.00113.71           C  
ANISOU  937  C   HIS A 143    16307  15515  11384   1104    611  -1200       C  
ATOM    938  O   HIS A 143      -8.617 -17.531 -14.270  1.00108.43           O  
ANISOU  938  O   HIS A 143    15570  14778  10851   1032    402  -1231       O  
ATOM    939  CB  HIS A 143      -7.596 -18.023 -17.412  1.00125.46           C  
ANISOU  939  CB  HIS A 143    18214  17130  12326   1263    678  -1367       C  
ATOM    940  CG  HIS A 143      -8.793 -18.921 -17.391  1.00126.56           C  
ANISOU  940  CG  HIS A 143    18420  17193  12474   1238    421  -1558       C  
ATOM    941  ND1 HIS A 143      -8.981 -19.887 -16.427  1.00124.89           N  
ANISOU  941  ND1 HIS A 143    18083  16857  12513   1199    351  -1668       N  
ATOM    942  CD2 HIS A 143      -9.870 -18.991 -18.208  1.00127.80           C  
ANISOU  942  CD2 HIS A 143    18751  17379  12427   1241    212  -1652       C  
ATOM    943  CE1 HIS A 143     -10.120 -20.517 -16.653  1.00125.21           C  
ANISOU  943  CE1 HIS A 143    18212  16847  12516   1169    120  -1823       C  
ATOM    944  NE2 HIS A 143     -10.679 -19.992 -17.728  1.00127.22           N  
ANISOU  944  NE2 HIS A 143    18643  17197  12498   1193     23  -1822       N  
ATOM    945  N   ARG A 144      -6.406 -17.837 -14.524  1.00105.31           N  
ANISOU  945  N   ARG A 144    15128  14435  10449   1138    815  -1186       N  
ATOM    946  CA  ARG A 144      -6.141 -18.117 -13.122  1.00 96.82           C  
ANISOU  946  CA  ARG A 144    13833  13272   9681   1085    807  -1164       C  
ATOM    947  C   ARG A 144      -5.315 -16.972 -12.552  1.00 82.61           C  
ANISOU  947  C   ARG A 144    11873  11516   8000   1038    937   -963       C  
ATOM    948  O   ARG A 144      -4.449 -16.416 -13.237  1.00 87.87           O  
ANISOU  948  O   ARG A 144    12571  12266   8549   1076   1127   -872       O  
ATOM    949  CB  ARG A 144      -5.415 -19.457 -12.938  1.00100.91           C  
ANISOU  949  CB  ARG A 144    14326  13730  10286   1162    917  -1300       C  
ATOM    950  CG  ARG A 144      -3.896 -19.398 -13.035  1.00102.34           C  
ANISOU  950  CG  ARG A 144    14423  13966  10494   1233   1190  -1229       C  
ATOM    951  CD  ARG A 144      -3.273 -20.745 -12.692  1.00101.51           C  
ANISOU  951  CD  ARG A 144    14273  13783  10514   1315   1273  -1360       C  
ATOM    952  NE  ARG A 144      -1.827 -20.658 -12.507  1.00102.64           N  
ANISOU  952  NE  ARG A 144    14273  13974  10751   1374   1515  -1275       N  
ATOM    953  CZ  ARG A 144      -1.046 -21.693 -12.211  1.00107.91           C  
ANISOU  953  CZ  ARG A 144    14872  14589  11540   1464   1625  -1356       C  
ATOM    954  NH1 ARG A 144       0.260 -21.519 -12.060  1.00113.73           N  
ANISOU  954  NH1 ARG A 144    15458  15384  12369   1517   1840  -1266       N  
ATOM    955  NH2 ARG A 144      -1.568 -22.903 -12.068  1.00107.24           N  
ANISOU  955  NH2 ARG A 144    14864  14389  11494   1503   1521  -1523       N  
ATOM    956  N   VAL A 145      -5.607 -16.598 -11.316  1.00 73.26           N  
ANISOU  956  N   VAL A 145    10520  10272   7043    951    835   -894       N  
ATOM    957  CA  VAL A 145      -4.908 -15.501 -10.661  1.00 73.78           C  
ANISOU  957  CA  VAL A 145    10429  10363   7240    891    926   -719       C  
ATOM    958  C   VAL A 145      -3.653 -16.055  -9.996  1.00 72.19           C  
ANISOU  958  C   VAL A 145    10066  10149   7215    921   1086   -718       C  
ATOM    959  O   VAL A 145      -3.692 -17.105  -9.344  1.00 71.82           O  
ANISOU  959  O   VAL A 145     9961  10030   7296    944   1038   -822       O  
ATOM    960  CB  VAL A 145      -5.824 -14.792  -9.648  1.00 77.91           C  
ANISOU  960  CB  VAL A 145    10861  10831   7911    790    739   -653       C  
ATOM    961  CG1 VAL A 145      -6.509 -15.810  -8.746  1.00 79.55           C  
ANISOU  961  CG1 VAL A 145    11010  10947   8268    775    592   -774       C  
ATOM    962  CG2 VAL A 145      -5.038 -13.778  -8.831  1.00 81.62           C  
ANISOU  962  CG2 VAL A 145    11162  11306   8542    725    825   -498       C  
ATOM    963  N   THR A 146      -2.532 -15.364 -10.181  1.00 72.74           N  
ANISOU  963  N   THR A 146    10058  10284   7295    921   1277   -595       N  
ATOM    964  CA  THR A 146      -1.258 -15.764  -9.605  1.00 75.72           C  
ANISOU  964  CA  THR A 146    10258  10667   7844    951   1434   -577       C  
ATOM    965  C   THR A 146      -0.727 -14.650  -8.712  1.00 76.87           C  
ANISOU  965  C   THR A 146    10216  10820   8169    851   1452   -419       C  
ATOM    966  O   THR A 146      -1.281 -13.550  -8.649  1.00 77.24           O  
ANISOU  966  O   THR A 146    10288  10865   8195    766   1370   -322       O  
ATOM    967  CB  THR A 146      -0.226 -16.095 -10.693  1.00 77.33           C  
ANISOU  967  CB  THR A 146    10518  10952   7912   1053   1677   -591       C  
ATOM    968  OG1 THR A 146       0.195 -14.885 -11.334  1.00 79.12           O  
ANISOU  968  OG1 THR A 146    10762  11260   8039   1013   1804   -438       O  
ATOM    969  CG2 THR A 146      -0.822 -17.037 -11.732  1.00 89.27           C  
ANISOU  969  CG2 THR A 146    12258  12461   9201   1150   1653   -752       C  
ATOM    970  N   MET A 147       0.375 -14.951  -8.022  1.00 76.61           N  
ANISOU  970  N   MET A 147     9995  10792   8321    864   1555   -396       N  
ATOM    971  CA  MET A 147       1.032 -13.943  -7.196  1.00 63.79           C  
ANISOU  971  CA  MET A 147     8183   9180   6874    768   1579   -258       C  
ATOM    972  C   MET A 147       1.610 -12.813  -8.040  1.00 68.54           C  
ANISOU  972  C   MET A 147     8801   9855   7386    728   1740   -122       C  
ATOM    973  O   MET A 147       1.786 -11.694  -7.543  1.00 58.96           O  
ANISOU  973  O   MET A 147     7492   8632   6276    620   1721     -1       O  
ATOM    974  CB  MET A 147       2.134 -14.593  -6.361  1.00 67.02           C  
ANISOU  974  CB  MET A 147     8384   9590   7491    803   1650   -270       C  
ATOM    975  CG  MET A 147       2.539 -13.797  -5.139  1.00 80.39           C  
ANISOU  975  CG  MET A 147     9879  11268   9397    697   1583   -171       C  
ATOM    976  SD  MET A 147       1.323 -13.946  -3.821  1.00 89.57           S  
ANISOU  976  SD  MET A 147    11050  12331  10652    640   1312   -223       S  
ATOM    977  CE  MET A 147       1.432 -15.695  -3.450  1.00 86.03           C  
ANISOU  977  CE  MET A 147    10587  11839  10263    763   1295   -359       C  
ATOM    978  N   ASN A 148       1.907 -13.084  -9.316  1.00 68.75           N  
ANISOU  978  N   ASN A 148     8957   9947   7217    812   1903   -141       N  
ATOM    979  CA  ASN A 148       2.507 -12.086 -10.197  1.00 71.93           C  
ANISOU  979  CA  ASN A 148     9387  10424   7519    782   2086     -1       C  
ATOM    980  C   ASN A 148       1.558 -10.941 -10.523  1.00 68.45           C  
ANISOU  980  C   ASN A 148     9086   9962   6959    702   1976     90       C  
ATOM    981  O   ASN A 148       2.016  -9.879 -10.959  1.00 62.82           O  
ANISOU  981  O   ASN A 148     8368   9282   6219    642   2098    240       O  
ATOM    982  CB  ASN A 148       2.978 -12.755 -11.489  1.00 76.96           C  
ANISOU  982  CB  ASN A 148    10153  11140   7947    908   2289    -56       C  
ATOM    983  CG  ASN A 148       4.008 -13.841 -11.236  1.00 90.03           C  
ANISOU  983  CG  ASN A 148    11664  12815   9728   1004   2426   -137       C  
ATOM    984  OD1 ASN A 148       4.838 -13.719 -10.336  1.00102.78           O  
ANISOU  984  OD1 ASN A 148    13043  14427  11583    962   2460    -82       O  
ATOM    985  ND2 ASN A 148       3.955 -14.912 -12.022  1.00 84.67           N  
ANISOU  985  ND2 ASN A 148    11128  12155   8888   1138   2496   -274       N  
ATOM    986  N   GLU A 149       0.254 -11.127 -10.330  1.00 64.02           N  
ANISOU  986  N   GLU A 149     8645   9344   6337    699   1752     10       N  
ATOM    987  CA  GLU A 149      -0.699 -10.062 -10.607  1.00 56.25           C  
ANISOU  987  CA  GLU A 149     7785   8336   5251    638   1632     96       C  
ATOM    988  C   GLU A 149      -0.723  -8.991  -9.530  1.00 63.53           C  
ANISOU  988  C   GLU A 149     8564   9193   6381    515   1548    203       C  
ATOM    989  O   GLU A 149      -1.389  -7.966  -9.713  1.00 64.62           O  
ANISOU  989  O   GLU A 149     8787   9302   6462    462   1469    294       O  
ATOM    990  CB  GLU A 149      -2.104 -10.637 -10.773  1.00 59.74           C  
ANISOU  990  CB  GLU A 149     8385   8745   5570    680   1417    -30       C  
ATOM    991  CG  GLU A 149      -2.347 -11.313 -12.104  1.00 73.85           C  
ANISOU  991  CG  GLU A 149    10382  10594   7085    786   1467   -116       C  
ATOM    992  CD  GLU A 149      -3.818 -11.570 -12.349  1.00 88.36           C  
ANISOU  992  CD  GLU A 149    12374  12401   8798    802   1232   -211       C  
ATOM    993  OE1 GLU A 149      -4.628 -10.641 -12.143  1.00 93.38           O  
ANISOU  993  OE1 GLU A 149    13031  13007   9443    742   1092   -129       O  
ATOM    994  OE2 GLU A 149      -4.168 -12.705 -12.732  1.00 93.27           O  
ANISOU  994  OE2 GLU A 149    13090  13024   9324    876   1183   -372       O  
ATOM    995  N   PHE A 150      -0.021  -9.195  -8.422  1.00 65.47           N  
ANISOU  995  N   PHE A 150     8601   9413   6860    473   1556    193       N  
ATOM    996  CA  PHE A 150      -0.058  -8.276  -7.298  1.00 54.11           C  
ANISOU  996  CA  PHE A 150     7031   7909   5618    359   1457    267       C  
ATOM    997  C   PHE A 150       1.339  -7.762  -6.989  1.00 51.21           C  
ANISOU  997  C   PHE A 150     6475   7567   5416    293   1620    366       C  
ATOM    998  O   PHE A 150       2.336  -8.460  -7.192  1.00 58.13           O  
ANISOU  998  O   PHE A 150     7257   8505   6325    347   1772    342       O  
ATOM    999  CB  PHE A 150      -0.645  -8.950  -6.055  1.00 55.74           C  
ANISOU  999  CB  PHE A 150     7161   8056   5964    357   1270    157       C  
ATOM   1000  CG  PHE A 150      -2.056  -9.434  -6.235  1.00 51.63           C  
ANISOU 1000  CG  PHE A 150     6794   7502   5321    403   1100     60       C  
ATOM   1001  CD1 PHE A 150      -3.128  -8.619  -5.911  1.00 46.29           C  
ANISOU 1001  CD1 PHE A 150     6174   6769   4644    349    942     95       C  
ATOM   1002  CD2 PHE A 150      -2.310 -10.706  -6.718  1.00 50.00           C  
ANISOU 1002  CD2 PHE A 150     6669   7316   5013    499   1096    -68       C  
ATOM   1003  CE1 PHE A 150      -4.426  -9.062  -6.070  1.00 51.45           C  
ANISOU 1003  CE1 PHE A 150     6945   7400   5204    388    783      9       C  
ATOM   1004  CE2 PHE A 150      -3.606 -11.154  -6.878  1.00 52.40           C  
ANISOU 1004  CE2 PHE A 150     7101   7588   5223    527    931   -160       C  
ATOM   1005  CZ  PHE A 150      -4.665 -10.331  -6.554  1.00 53.74           C  
ANISOU 1005  CZ  PHE A 150     7306   7713   5398    470    774   -118       C  
ATOM   1006  N   GLU A 151       1.400  -6.529  -6.497  1.00 55.41           N  
ANISOU 1006  N   GLU A 151     6947   8047   6060    176   1585    476       N  
ATOM   1007  CA  GLU A 151       2.639  -5.916  -6.033  1.00 60.06           C  
ANISOU 1007  CA  GLU A 151     7337   8642   6841     84   1699    568       C  
ATOM   1008  C   GLU A 151       2.622  -5.883  -4.510  1.00 57.61           C  
ANISOU 1008  C   GLU A 151     6871   8272   6746     19   1534    519       C  
ATOM   1009  O   GLU A 151       1.693  -5.334  -3.910  1.00 54.52           O  
ANISOU 1009  O   GLU A 151     6540   7803   6373    -28   1365    510       O  
ATOM   1010  CB  GLU A 151       2.807  -4.505  -6.597  1.00 58.78           C  
ANISOU 1010  CB  GLU A 151     7225   8451   6657    -12   1788    730       C  
ATOM   1011  CG  GLU A 151       3.958  -3.729  -5.965  1.00 73.20           C  
ANISOU 1011  CG  GLU A 151     8837  10260   8717   -140   1868    822       C  
ATOM   1012  CD  GLU A 151       4.116  -2.330  -6.533  1.00 97.32           C  
ANISOU 1012  CD  GLU A 151    11949  13265  11763   -245   1962    988       C  
ATOM   1013  OE1 GLU A 151       3.945  -2.154  -7.760  1.00107.76           O  
ANISOU 1013  OE1 GLU A 151    13435  14623  12886   -198   2087   1064       O  
ATOM   1014  OE2 GLU A 151       4.409  -1.401  -5.749  1.00104.42           O  
ANISOU 1014  OE2 GLU A 151    12738  14085  12852   -375   1908   1044       O  
ATOM   1015  N   TYR A 152       3.645  -6.468  -3.895  1.00 67.39           N  
ANISOU 1015  N   TYR A 152     7913   9550   8141     24   1584    487       N  
ATOM   1016  CA  TYR A 152       3.780  -6.427  -2.445  1.00 68.89           C  
ANISOU 1016  CA  TYR A 152     7951   9697   8528    -36   1434    449       C  
ATOM   1017  C   TYR A 152       4.025  -4.997  -1.978  1.00 63.64           C  
ANISOU 1017  C   TYR A 152     7220   8971   7988   -186   1404    548       C  
ATOM   1018  O   TYR A 152       4.829  -4.263  -2.562  1.00 69.68           O  
ANISOU 1018  O   TYR A 152     7930   9754   8791   -255   1557    656       O  
ATOM   1019  CB  TYR A 152       4.924  -7.341  -2.002  1.00 80.93           C  
ANISOU 1019  CB  TYR A 152     9274  11287  10187     11   1502    409       C  
ATOM   1020  CG  TYR A 152       5.251  -7.307  -0.523  1.00 84.48           C  
ANISOU 1020  CG  TYR A 152     9553  11709  10835    -47   1354    379       C  
ATOM   1021  CD1 TYR A 152       4.659  -8.200   0.362  1.00 84.43           C  
ANISOU 1021  CD1 TYR A 152     9562  11678  10839     19   1197    277       C  
ATOM   1022  CD2 TYR A 152       6.176  -6.401  -0.015  1.00 86.41           C  
ANISOU 1022  CD2 TYR A 152     9623  11954  11257   -169   1371    455       C  
ATOM   1023  CE1 TYR A 152       4.966  -8.178   1.712  1.00 85.19           C  
ANISOU 1023  CE1 TYR A 152     9518  11758  11093    -26   1062    255       C  
ATOM   1024  CE2 TYR A 152       6.485  -6.372   1.331  1.00 87.26           C  
ANISOU 1024  CE2 TYR A 152     9583  12043  11528   -219   1221    420       C  
ATOM   1025  CZ  TYR A 152       5.878  -7.262   2.188  1.00 87.54           C  
ANISOU 1025  CZ  TYR A 152     9650  12062  11548   -142   1068    322       C  
ATOM   1026  OH  TYR A 152       6.190  -7.233   3.528  1.00 90.08           O  
ANISOU 1026  OH  TYR A 152     9842  12374  12011   -184    919    292       O  
ATOM   1027  N   LEU A 153       3.322  -4.600  -0.920  1.00 59.67           N  
ANISOU 1027  N   LEU A 153     6729   8391   7553   -238   1213    508       N  
ATOM   1028  CA  LEU A 153       3.459  -3.267  -0.345  1.00 60.42           C  
ANISOU 1028  CA  LEU A 153     6778   8407   7772   -377   1158    577       C  
ATOM   1029  C   LEU A 153       3.958  -3.295   1.091  1.00 59.54           C  
ANISOU 1029  C   LEU A 153     6493   8281   7850   -436   1033    523       C  
ATOM   1030  O   LEU A 153       4.962  -2.645   1.406  1.00 65.57           O  
ANISOU 1030  O   LEU A 153     7102   9042   8771   -543   1073    577       O  
ATOM   1031  CB  LEU A 153       2.118  -2.512  -0.403  1.00 60.77           C  
ANISOU 1031  CB  LEU A 153     7014   8359   7718   -389   1043    585       C  
ATOM   1032  CG  LEU A 153       1.462  -2.257  -1.762  1.00 66.50           C  
ANISOU 1032  CG  LEU A 153     7935   9086   8247   -339   1124    650       C  
ATOM   1033  CD1 LEU A 153       0.385  -1.181  -1.647  1.00 66.86           C  
ANISOU 1033  CD1 LEU A 153     8119   9023   8260   -379   1008    687       C  
ATOM   1034  CD2 LEU A 153       2.501  -1.878  -2.805  1.00 73.96           C  
ANISOU 1034  CD2 LEU A 153     8846  10078   9177   -374   1343    769       C  
ATOM   1035  N   LYS A 154       3.290  -4.040   1.971  1.00 54.28           N  
ANISOU 1035  N   LYS A 154     5847   7606   7170   -372    881    419       N  
ATOM   1036  CA  LYS A 154       3.547  -3.937   3.400  1.00 61.46           C  
ANISOU 1036  CA  LYS A 154     6636   8492   8224   -427    736    369       C  
ATOM   1037  C   LYS A 154       3.028  -5.182   4.104  1.00 56.48           C  
ANISOU 1037  C   LYS A 154     6018   7887   7554   -318    630    268       C  
ATOM   1038  O   LYS A 154       1.979  -5.718   3.738  1.00 52.44           O  
ANISOU 1038  O   LYS A 154     5655   7361   6908   -237    605    227       O  
ATOM   1039  CB  LYS A 154       2.879  -2.681   3.973  1.00 65.44           C  
ANISOU 1039  CB  LYS A 154     7219   8888   8756   -525    620    380       C  
ATOM   1040  CG  LYS A 154       3.130  -2.422   5.441  1.00 70.38           C  
ANISOU 1040  CG  LYS A 154     7743   9486   9513   -590    467    323       C  
ATOM   1041  CD  LYS A 154       2.501  -1.099   5.834  1.00 79.66           C  
ANISOU 1041  CD  LYS A 154     9014  10543  10710   -684    381    334       C  
ATOM   1042  CE  LYS A 154       2.977  -0.627   7.193  1.00 89.89           C  
ANISOU 1042  CE  LYS A 154    10205  11807  12143   -772    246    281       C  
ATOM   1043  NZ  LYS A 154       2.731   0.833   7.372  1.00 92.42           N  
ANISOU 1043  NZ  LYS A 154    10595  12002  12520   -888    205    305       N  
ATOM   1044  N   LEU A 155       3.769  -5.637   5.111  1.00 64.41           N  
ANISOU 1044  N   LEU A 155     6867   8927   8680   -319    564    233       N  
ATOM   1045  CA  LEU A 155       3.322  -6.748   5.940  1.00 61.38           C  
ANISOU 1045  CA  LEU A 155     6493   8554   8273   -226    456    152       C  
ATOM   1046  C   LEU A 155       2.351  -6.239   6.995  1.00 56.74           C  
ANISOU 1046  C   LEU A 155     5991   7895   7671   -266    290    109       C  
ATOM   1047  O   LEU A 155       2.658  -5.298   7.735  1.00 65.72           O  
ANISOU 1047  O   LEU A 155     7073   9001   8897   -365    215    118       O  
ATOM   1048  CB  LEU A 155       4.507  -7.442   6.609  1.00 64.71           C  
ANISOU 1048  CB  LEU A 155     6720   9046   8823   -198    445    142       C  
ATOM   1049  CG  LEU A 155       4.136  -8.569   7.576  1.00 64.98           C  
ANISOU 1049  CG  LEU A 155     6762   9084   8843   -103    329     74       C  
ATOM   1050  CD1 LEU A 155       3.730  -9.831   6.824  1.00 64.68           C  
ANISOU 1050  CD1 LEU A 155     6809   9058   8709     28    410     42       C  
ATOM   1051  CD2 LEU A 155       5.281  -8.851   8.532  1.00 69.40           C  
ANISOU 1051  CD2 LEU A 155     7125   9700   9545   -104    264     77       C  
ATOM   1052  N   LEU A 156       1.174  -6.857   7.055  1.00 58.93           N  
ANISOU 1052  N   LEU A 156     6403   8146   7841   -191    238     59       N  
ATOM   1053  CA  LEU A 156       0.162  -6.486   8.034  1.00 55.99           C  
ANISOU 1053  CA  LEU A 156     6114   7713   7447   -211    100     17       C  
ATOM   1054  C   LEU A 156       0.193  -7.351   9.282  1.00 60.10           C  
ANISOU 1054  C   LEU A 156     6584   8253   7998   -162     -3    -35       C  
ATOM   1055  O   LEU A 156      -0.236  -6.895  10.347  1.00 63.28           O  
ANISOU 1055  O   LEU A 156     7011   8621   8411   -197   -115    -63       O  
ATOM   1056  CB  LEU A 156      -1.237  -6.559   7.413  1.00 53.28           C  
ANISOU 1056  CB  LEU A 156     5938   7326   6978   -165     98      0       C  
ATOM   1057  CG  LEU A 156      -1.491  -5.645   6.220  1.00 60.33           C  
ANISOU 1057  CG  LEU A 156     6916   8192   7814   -202    177     57       C  
ATOM   1058  CD1 LEU A 156      -2.975  -5.599   5.880  1.00 59.05           C  
ANISOU 1058  CD1 LEU A 156     6908   7986   7544   -160    127     34       C  
ATOM   1059  CD2 LEU A 156      -0.951  -4.261   6.516  1.00 59.87           C  
ANISOU 1059  CD2 LEU A 156     6814   8089   7845   -315    168    107       C  
ATOM   1060  N   GLY A 157       0.681  -8.584   9.179  1.00 55.82           N  
ANISOU 1060  N   GLY A 157     5981   7762   7466    -76     37    -45       N  
ATOM   1061  CA  GLY A 157       0.748  -9.453  10.335  1.00 57.86           C  
ANISOU 1061  CA  GLY A 157     6198   8036   7751    -21    -56    -78       C  
ATOM   1062  C   GLY A 157       1.302 -10.827  10.026  1.00 60.90           C  
ANISOU 1062  C   GLY A 157     6526   8462   8153     86      6    -82       C  
ATOM   1063  O   GLY A 157       1.107 -11.352   8.926  1.00 60.61           O  
ANISOU 1063  O   GLY A 157     6543   8423   8061    138    110    -88       O  
ATOM   1064  N   LYS A 158       2.006 -11.414  10.988  1.00 61.54           N  
ANISOU 1064  N   LYS A 158     6502   8577   8304    125    -60    -80       N  
ATOM   1065  CA  LYS A 158       2.516 -12.771  10.875  1.00 62.93           C  
ANISOU 1065  CA  LYS A 158     6625   8778   8508    241    -16    -83       C  
ATOM   1066  C   LYS A 158       1.847 -13.647  11.923  1.00 69.78           C  
ANISOU 1066  C   LYS A 158     7560   9609   9344    304   -116   -103       C  
ATOM   1067  O   LYS A 158       1.595 -13.207  13.048  1.00 80.81           O  
ANISOU 1067  O   LYS A 158     8967  11002  10734    262   -233   -103       O  
ATOM   1068  CB  LYS A 158       4.039 -12.816  11.044  1.00 67.27           C  
ANISOU 1068  CB  LYS A 158     6975   9402   9183    253      0    -47       C  
ATOM   1069  CG  LYS A 158       4.808 -12.308   9.835  1.00 80.07           C  
ANISOU 1069  CG  LYS A 158     8516  11063  10844    218    146    -18       C  
ATOM   1070  CD  LYS A 158       6.313 -12.351  10.064  1.00 91.73           C  
ANISOU 1070  CD  LYS A 158     9768  12620  12467    226    161     20       C  
ATOM   1071  CE  LYS A 158       7.077 -11.941   8.811  1.00101.08           C  
ANISOU 1071  CE  LYS A 158    10867  13848  13692    200    338     58       C  
ATOM   1072  NZ  LYS A 158       8.540 -11.813   9.062  1.00106.83           N  
ANISOU 1072  NZ  LYS A 158    11347  14657  14585    185    352    100       N  
ATOM   1073  N   GLY A 159       1.551 -14.890  11.542  1.00 63.56           N  
ANISOU 1073  N   GLY A 159     6827   8789   8532    404    -63   -121       N  
ATOM   1074  CA  GLY A 159       0.930 -15.840  12.436  1.00 61.35           C  
ANISOU 1074  CA  GLY A 159     6614   8463   8231    466   -136   -128       C  
ATOM   1075  C   GLY A 159       1.649 -17.180  12.390  1.00 65.88           C  
ANISOU 1075  C   GLY A 159     7131   9034   8865    589    -96   -118       C  
ATOM   1076  O   GLY A 159       2.625 -17.357  11.662  1.00 69.36           O  
ANISOU 1076  O   GLY A 159     7475   9516   9364    632     -9   -113       O  
ATOM   1077  N   THR A 160       1.131 -18.110  13.188  1.00 68.34           N  
ANISOU 1077  N   THR A 160     7509   9292   9166    649   -153   -111       N  
ATOM   1078  CA  THR A 160       1.734 -19.437  13.238  1.00 71.25           C  
ANISOU 1078  CA  THR A 160     7841   9636   9596    776   -124    -96       C  
ATOM   1079  C   THR A 160       1.558 -20.174  11.915  1.00 67.63           C  
ANISOU 1079  C   THR A 160     7443   9125   9128    832      4   -149       C  
ATOM   1080  O   THR A 160       2.452 -20.913  11.488  1.00 69.66           O  
ANISOU 1080  O   THR A 160     7630   9387   9451    932     75   -149       O  
ATOM   1081  CB  THR A 160       1.126 -20.242  14.386  1.00 73.08           C  
ANISOU 1081  CB  THR A 160     8149   9806   9811    820   -208    -65       C  
ATOM   1082  OG1 THR A 160       1.147 -19.456  15.585  1.00 76.57           O  
ANISOU 1082  OG1 THR A 160     8565  10301  10228    762   -326    -29       O  
ATOM   1083  CG2 THR A 160       1.914 -21.525  14.612  1.00 66.85           C  
ANISOU 1083  CG2 THR A 160     7309   8990   9102    958   -196    -31       C  
ATOM   1084  N   PHE A 161       0.423 -19.972  11.244  1.00 67.75           N  
ANISOU 1084  N   PHE A 161     7590   9092   9061    773     33   -198       N  
ATOM   1085  CA  PHE A 161       0.081 -20.728  10.046  1.00 70.83           C  
ANISOU 1085  CA  PHE A 161     8068   9423   9420    822    131   -263       C  
ATOM   1086  C   PHE A 161       0.129 -19.881   8.776  1.00 65.30           C  
ANISOU 1086  C   PHE A 161     7380   8773   8656    771    215   -296       C  
ATOM   1087  O   PHE A 161      -0.498 -20.240   7.775  1.00 60.75           O  
ANISOU 1087  O   PHE A 161     6916   8155   8013    781    270   -359       O  
ATOM   1088  CB  PHE A 161      -1.299 -21.367  10.205  1.00 73.19           C  
ANISOU 1088  CB  PHE A 161     8513   9621   9676    805     90   -298       C  
ATOM   1089  CG  PHE A 161      -1.438 -22.216  11.439  1.00 80.31           C  
ANISOU 1089  CG  PHE A 161     9421  10463  10630    851     21   -253       C  
ATOM   1090  CD1 PHE A 161      -0.679 -23.364  11.593  1.00 82.98           C  
ANISOU 1090  CD1 PHE A 161     9726  10757  11044    969     51   -237       C  
ATOM   1091  CD2 PHE A 161      -2.331 -21.869  12.442  1.00 82.60           C  
ANISOU 1091  CD2 PHE A 161     9755  10739  10890    783    -65   -219       C  
ATOM   1092  CE1 PHE A 161      -0.800 -24.148  12.725  1.00 82.05           C  
ANISOU 1092  CE1 PHE A 161     9627  10580  10969   1017    -12   -180       C  
ATOM   1093  CE2 PHE A 161      -2.458 -22.652  13.578  1.00 79.73           C  
ANISOU 1093  CE2 PHE A 161     9410  10324  10560    828   -117   -165       C  
ATOM   1094  CZ  PHE A 161      -1.692 -23.792  13.718  1.00 76.76           C  
ANISOU 1094  CZ  PHE A 161     9008   9901  10256    943    -93   -140       C  
ATOM   1095  N   GLY A 162       0.859 -18.772   8.791  1.00 61.03           N  
ANISOU 1095  N   GLY A 162     6734   8320   8134    714    223   -253       N  
ATOM   1096  CA  GLY A 162       1.000 -17.946   7.615  1.00 61.92           C  
ANISOU 1096  CA  GLY A 162     6857   8479   8191    667    315   -263       C  
ATOM   1097  C   GLY A 162       1.086 -16.483   7.992  1.00 64.07           C  
ANISOU 1097  C   GLY A 162     7074   8803   8468    551    265   -213       C  
ATOM   1098  O   GLY A 162       1.333 -16.138   9.146  1.00 66.06           O  
ANISOU 1098  O   GLY A 162     7251   9070   8779    517    167   -178       O  
ATOM   1099  N   LYS A 163       0.872 -15.620   6.998  1.00 55.78           N  
ANISOU 1099  N   LYS A 163     6073   7773   7349    491    329   -212       N  
ATOM   1100  CA  LYS A 163       0.998 -14.182   7.181  1.00 57.97           C  
ANISOU 1100  CA  LYS A 163     6308   8082   7637    380    300   -164       C  
ATOM   1101  C   LYS A 163      -0.040 -13.461   6.332  1.00 54.81           C  
ANISOU 1101  C   LYS A 163     6048   7654   7123    325    313   -175       C  
ATOM   1102  O   LYS A 163      -0.659 -14.040   5.436  1.00 55.72           O  
ANISOU 1102  O   LYS A 163     6276   7747   7149    373    358   -219       O  
ATOM   1103  CB  LYS A 163       2.410 -13.696   6.826  1.00 63.98           C  
ANISOU 1103  CB  LYS A 163     6915   8916   8479    363    394   -114       C  
ATOM   1104  CG  LYS A 163       2.903 -14.171   5.470  1.00 68.47           C  
ANISOU 1104  CG  LYS A 163     7493   9516   9006    432    560   -123       C  
ATOM   1105  CD  LYS A 163       4.352 -13.771   5.248  1.00 76.02           C  
ANISOU 1105  CD  LYS A 163     8267  10551  10066    419    663    -65       C  
ATOM   1106  CE  LYS A 163       4.920 -14.401   3.984  1.00 81.69           C  
ANISOU 1106  CE  LYS A 163     8987  11307  10743    511    847    -79       C  
ATOM   1107  NZ  LYS A 163       6.358 -14.059   3.793  1.00 82.91           N  
ANISOU 1107  NZ  LYS A 163     8939  11544  11017    503    962    -17       N  
ATOM   1108  N   VAL A 164      -0.224 -12.177   6.634  1.00 48.81           N  
ANISOU 1108  N   VAL A 164     5284   6892   6370    227    265   -136       N  
ATOM   1109  CA  VAL A 164      -1.134 -11.296   5.910  1.00 39.05           C  
ANISOU 1109  CA  VAL A 164     4168   5628   5041    175    267   -128       C  
ATOM   1110  C   VAL A 164      -0.329 -10.105   5.410  1.00 56.30           C  
ANISOU 1110  C   VAL A 164     6295   7843   7255     99    341    -59       C  
ATOM   1111  O   VAL A 164       0.457  -9.522   6.167  1.00 55.78           O  
ANISOU 1111  O   VAL A 164     6109   7791   7294     38    312    -27       O  
ATOM   1112  CB  VAL A 164      -2.303 -10.832   6.798  1.00 46.23           C  
ANISOU 1112  CB  VAL A 164     5145   6483   5937    132    138   -145       C  
ATOM   1113  CG1 VAL A 164      -3.270  -9.970   6.004  1.00 51.34           C  
ANISOU 1113  CG1 VAL A 164     5911   7101   6496     97    136   -133       C  
ATOM   1114  CG2 VAL A 164      -3.024 -12.027   7.403  1.00 54.82           C  
ANISOU 1114  CG2 VAL A 164     6272   7540   7017    196     76   -199       C  
ATOM   1115  N   ILE A 165      -0.513  -9.750   4.139  1.00 57.96           N  
ANISOU 1115  N   ILE A 165     6590   8062   7371     99    434    -35       N  
ATOM   1116  CA  ILE A 165       0.245  -8.669   3.523  1.00 52.98           C  
ANISOU 1116  CA  ILE A 165     5917   7454   6761     28    529     45       C  
ATOM   1117  C   ILE A 165      -0.695  -7.750   2.759  1.00 55.63           C  
ANISOU 1117  C   ILE A 165     6402   7749   6987     -8    525     79       C  
ATOM   1118  O   ILE A 165      -1.705  -8.183   2.192  1.00 53.97           O  
ANISOU 1118  O   ILE A 165     6323   7525   6656     49    498     38       O  
ATOM   1119  CB  ILE A 165       1.361  -9.189   2.586  1.00 54.58           C  
ANISOU 1119  CB  ILE A 165     6050   7726   6960     78    698     68       C  
ATOM   1120  CG1 ILE A 165       0.771 -10.027   1.452  1.00 61.12           C  
ANISOU 1120  CG1 ILE A 165     7023   8567   7633    174    764     20       C  
ATOM   1121  CG2 ILE A 165       2.393  -9.994   3.365  1.00 55.24           C  
ANISOU 1121  CG2 ILE A 165     5963   7851   7175    118    701     47       C  
ATOM   1122  CD1 ILE A 165       1.792 -10.458   0.425  1.00 64.96           C  
ANISOU 1122  CD1 ILE A 165     7469   9123   8090    233    949     39       C  
ATOM   1123  N   LEU A 166      -0.355  -6.464   2.757  1.00 46.61           N  
ANISOU 1123  N   LEU A 166     5233   6581   5894   -104    543    154       N  
ATOM   1124  CA  LEU A 166      -1.046  -5.485   1.933  1.00 42.86           C  
ANISOU 1124  CA  LEU A 166     4893   6066   5326   -134    559    212       C  
ATOM   1125  C   LEU A 166      -0.458  -5.511   0.530  1.00 46.86           C  
ANISOU 1125  C   LEU A 166     5436   6628   5742   -110    728    273       C  
ATOM   1126  O   LEU A 166       0.760  -5.399   0.355  1.00 56.70           O  
ANISOU 1126  O   LEU A 166     6563   7917   7065   -143    849    324       O  
ATOM   1127  CB  LEU A 166      -0.917  -4.088   2.537  1.00 49.46           C  
ANISOU 1127  CB  LEU A 166     5698   6832   6262   -247    513    269       C  
ATOM   1128  CG  LEU A 166      -1.646  -2.967   1.797  1.00 52.60           C  
ANISOU 1128  CG  LEU A 166     6237   7167   6582   -277    519    341       C  
ATOM   1129  CD1 LEU A 166      -3.152  -3.102   1.961  1.00 46.80           C  
ANISOU 1129  CD1 LEU A 166     5628   6392   5761   -217    391    286       C  
ATOM   1130  CD2 LEU A 166      -1.167  -1.609   2.277  1.00 55.42           C  
ANISOU 1130  CD2 LEU A 166     6546   7448   7064   -397    511    406       C  
ATOM   1131  N   VAL A 167      -1.322  -5.675  -0.467  1.00 47.17           N  
ANISOU 1131  N   VAL A 167     5636   6672   5615    -48    736    268       N  
ATOM   1132  CA  VAL A 167      -0.903  -5.787  -1.855  1.00 49.49           C  
ANISOU 1132  CA  VAL A 167     6000   7024   5779     -7    893    316       C  
ATOM   1133  C   VAL A 167      -1.740  -4.837  -2.697  1.00 47.50           C  
ANISOU 1133  C   VAL A 167     5914   6737   5396    -19    877    389       C  
ATOM   1134  O   VAL A 167      -2.727  -4.263  -2.237  1.00 48.68           O  
ANISOU 1134  O   VAL A 167     6123   6818   5555    -41    740    386       O  
ATOM   1135  CB  VAL A 167      -1.027  -7.227  -2.393  1.00 51.41           C  
ANISOU 1135  CB  VAL A 167     6291   7325   5916    109    924    218       C  
ATOM   1136  CG1 VAL A 167      -0.102  -8.167  -1.631  1.00 47.14           C  
ANISOU 1136  CG1 VAL A 167     5587   6815   5510    136    955    162       C  
ATOM   1137  CG2 VAL A 167      -2.474  -7.697  -2.318  1.00 48.04           C  
ANISOU 1137  CG2 VAL A 167     5991   6861   5400    158    767    133       C  
ATOM   1138  N   LYS A 168      -1.322  -4.685  -3.952  1.00 47.99           N  
ANISOU 1138  N   LYS A 168     6054   6850   5331      5   1027    460       N  
ATOM   1139  CA  LYS A 168      -2.029  -3.885  -4.946  1.00 55.24           C  
ANISOU 1139  CA  LYS A 168     7148   7749   6091     14   1028    542       C  
ATOM   1140  C   LYS A 168      -2.089  -4.688  -6.236  1.00 56.22           C  
ANISOU 1140  C   LYS A 168     7402   7960   6001    117   1119    514       C  
ATOM   1141  O   LYS A 168      -1.052  -5.140  -6.729  1.00 55.15           O  
ANISOU 1141  O   LYS A 168     7215   7893   5846    139   1291    525       O  
ATOM   1142  CB  LYS A 168      -1.319  -2.547  -5.184  1.00 65.75           C  
ANISOU 1142  CB  LYS A 168     8456   9042   7483    -84   1141    698       C  
ATOM   1143  CG  LYS A 168      -1.931  -1.690  -6.287  1.00 71.67           C  
ANISOU 1143  CG  LYS A 168     9397   9771   8063    -69   1163    809       C  
ATOM   1144  CD  LYS A 168      -0.991  -0.565  -6.719  1.00 81.45           C  
ANISOU 1144  CD  LYS A 168    10614  10982   9353   -161   1330    975       C  
ATOM   1145  CE  LYS A 168      -0.116  -0.983  -7.898  1.00 86.50           C  
ANISOU 1145  CE  LYS A 168    11282  11726   9857   -119   1552   1031       C  
ATOM   1146  NZ  LYS A 168       0.863   0.077  -8.276  1.00 90.31           N  
ANISOU 1146  NZ  LYS A 168    11720  12182  10410   -221   1735   1202       N  
ATOM   1147  N   GLU A 169      -3.290  -4.877  -6.779  1.00 58.64           N  
ANISOU 1147  N   GLU A 169     7870   8264   6145    181   1002    471       N  
ATOM   1148  CA  GLU A 169      -3.409  -5.526  -8.078  1.00 58.95           C  
ANISOU 1148  CA  GLU A 169     8060   8383   5955    276   1071    441       C  
ATOM   1149  C   GLU A 169      -2.877  -4.595  -9.160  1.00 59.66           C  
ANISOU 1149  C   GLU A 169     8245   8503   5919    262   1233    596       C  
ATOM   1150  O   GLU A 169      -3.306  -3.442  -9.266  1.00 67.07           O  
ANISOU 1150  O   GLU A 169     9248   9386   6849    216   1189    712       O  
ATOM   1151  CB  GLU A 169      -4.861  -5.909  -8.364  1.00 64.42           C  
ANISOU 1151  CB  GLU A 169     8894   9067   6515    339    881    355       C  
ATOM   1152  CG  GLU A 169      -5.066  -6.534  -9.740  1.00 68.07           C  
ANISOU 1152  CG  GLU A 169     9535   9610   6719    435    926    313       C  
ATOM   1153  CD  GLU A 169      -6.452  -7.123  -9.921  1.00 80.75           C  
ANISOU 1153  CD  GLU A 169    11247  11209   8223    489    719    197       C  
ATOM   1154  OE1 GLU A 169      -6.561  -8.217 -10.515  1.00 84.44           O  
ANISOU 1154  OE1 GLU A 169    11794  11725   8564    561    719     76       O  
ATOM   1155  OE2 GLU A 169      -7.430  -6.496  -9.464  1.00 87.34           O  
ANISOU 1155  OE2 GLU A 169    12083  11988   9114    460    557    224       O  
ATOM   1156  N   LYS A 170      -1.933  -5.097  -9.961  1.00 61.64           N  
ANISOU 1156  N   LYS A 170     8506   8839   6076    307   1431    604       N  
ATOM   1157  CA  LYS A 170      -1.260  -4.243 -10.934  1.00 62.91           C  
ANISOU 1157  CA  LYS A 170     8736   9034   6132    287   1624    766       C  
ATOM   1158  C   LYS A 170      -2.222  -3.711 -11.988  1.00 60.58           C  
ANISOU 1158  C   LYS A 170     8681   8747   5591    337   1560    831       C  
ATOM   1159  O   LYS A 170      -2.065  -2.577 -12.453  1.00 67.26           O  
ANISOU 1159  O   LYS A 170     9592   9566   6398    290   1638   1000       O  
ATOM   1160  CB  LYS A 170      -0.117  -5.005 -11.606  1.00 71.86           C  
ANISOU 1160  CB  LYS A 170     9837  10268   7199    343   1858    747       C  
ATOM   1161  CG  LYS A 170       1.020  -5.398 -10.676  1.00 75.72           C  
ANISOU 1161  CG  LYS A 170    10074  10760   7937    297   1948    716       C  
ATOM   1162  CD  LYS A 170       2.050  -6.238 -11.416  1.00 75.76           C  
ANISOU 1162  CD  LYS A 170    10053  10869   7864    380   2180    686       C  
ATOM   1163  CE  LYS A 170       3.170  -6.698 -10.498  1.00 76.51           C  
ANISOU 1163  CE  LYS A 170     9884  10973   8213    351   2256    652       C  
ATOM   1164  NZ  LYS A 170       3.990  -5.564  -9.997  1.00 75.79           N  
ANISOU 1164  NZ  LYS A 170     9620  10849   8325    212   2334    801       N  
ATOM   1165  N   ALA A 171      -3.225  -4.503 -12.369  1.00 59.74           N  
ANISOU 1165  N   ALA A 171     8705   8670   5322    429   1412    705       N  
ATOM   1166  CA  ALA A 171      -4.095  -4.109 -13.472  1.00 68.27           C  
ANISOU 1166  CA  ALA A 171    10016   9778   6143    492   1345    759       C  
ATOM   1167  C   ALA A 171      -5.060  -3.001 -13.064  1.00 70.69           C  
ANISOU 1167  C   ALA A 171    10352   9992   6516    445   1168    849       C  
ATOM   1168  O   ALA A 171      -5.338  -2.092 -13.854  1.00 71.54           O  
ANISOU 1168  O   ALA A 171    10607  10095   6478    458   1182    991       O  
ATOM   1169  CB  ALA A 171      -4.862  -5.324 -13.994  1.00 59.73           C  
ANISOU 1169  CB  ALA A 171     9056   8758   4880    597   1225    582       C  
ATOM   1170  N   THR A 172      -5.580  -3.054 -11.837  1.00 65.67           N  
ANISOU 1170  N   THR A 172     9581   9279   6093    398   1007    772       N  
ATOM   1171  CA  THR A 172      -6.602  -2.117 -11.396  1.00 66.51           C  
ANISOU 1171  CA  THR A 172     9710   9295   6266    373    830    830       C  
ATOM   1172  C   THR A 172      -6.094  -1.047 -10.443  1.00 70.13           C  
ANISOU 1172  C   THR A 172    10036   9649   6961    262    872    933       C  
ATOM   1173  O   THR A 172      -6.758  -0.017 -10.290  1.00 75.15           O  
ANISOU 1173  O   THR A 172    10721  10201   7633    244    776   1022       O  
ATOM   1174  CB  THR A 172      -7.751  -2.868 -10.707  1.00 60.15           C  
ANISOU 1174  CB  THR A 172     8864   8472   5518    405    604    670       C  
ATOM   1175  OG1 THR A 172      -7.265  -3.473  -9.504  1.00 55.58           O  
ANISOU 1175  OG1 THR A 172     8096   7865   5156    352    616    572       O  
ATOM   1176  CG2 THR A 172      -8.305  -3.952 -11.619  1.00 58.77           C  
ANISOU 1176  CG2 THR A 172     8817   8388   5125    502    540    550       C  
ATOM   1177  N   GLY A 173      -4.948  -1.259  -9.802  1.00 67.89           N  
ANISOU 1177  N   GLY A 173     9588   9364   6842    192   1005    920       N  
ATOM   1178  CA  GLY A 173      -4.466  -0.312  -8.820  1.00 54.40           C  
ANISOU 1178  CA  GLY A 173     7747   7555   5368     79   1022    992       C  
ATOM   1179  C   GLY A 173      -5.197  -0.346  -7.497  1.00 63.34           C  
ANISOU 1179  C   GLY A 173     8780   8611   6673     54    833    892       C  
ATOM   1180  O   GLY A 173      -4.916   0.488  -6.630  1.00 66.92           O  
ANISOU 1180  O   GLY A 173     9142   8973   7312    -36    823    937       O  
ATOM   1181  N   ARG A 174      -6.128  -1.281  -7.317  1.00 55.67           N  
ANISOU 1181  N   ARG A 174     7830   7675   5649    128    688    756       N  
ATOM   1182  CA  ARG A 174      -6.875  -1.388  -6.074  1.00 55.68           C  
ANISOU 1182  CA  ARG A 174     7741   7614   5803    112    523    662       C  
ATOM   1183  C   ARG A 174      -6.091  -2.196  -5.046  1.00 54.78           C  
ANISOU 1183  C   ARG A 174     7454   7516   5845     72    558    565       C  
ATOM   1184  O   ARG A 174      -5.362  -3.134  -5.382  1.00 54.93           O  
ANISOU 1184  O   ARG A 174     7438   7611   5822     99    659    516       O  
ATOM   1185  CB  ARG A 174      -8.243  -2.028  -6.318  1.00 61.76           C  
ANISOU 1185  CB  ARG A 174     8595   8410   6462    199    354    568       C  
ATOM   1186  CG  ARG A 174      -9.223  -1.130  -7.065  1.00 69.81           C  
ANISOU 1186  CG  ARG A 174     9762   9400   7362    244    265    659       C  
ATOM   1187  CD  ARG A 174     -10.655  -1.653  -6.987  1.00 81.39           C  
ANISOU 1187  CD  ARG A 174    11260  10879   8787    312     67    559       C  
ATOM   1188  NE  ARG A 174     -10.833  -2.916  -7.703  1.00 95.49           N  
ANISOU 1188  NE  ARG A 174    13099  12760  10422    373     48    451       N  
ATOM   1189  CZ  ARG A 174     -11.182  -3.007  -8.986  1.00105.01           C  
ANISOU 1189  CZ  ARG A 174    14462  14032  11406    442     28    474       C  
ATOM   1190  NH1 ARG A 174     -11.386  -1.907  -9.707  1.00104.20           N  
ANISOU 1190  NH1 ARG A 174    14477  13912  11202    464     28    619       N  
ATOM   1191  NH2 ARG A 174     -11.323  -4.200  -9.555  1.00110.80           N  
ANISOU 1191  NH2 ARG A 174    15244  14842  12013    492      4    353       N  
ATOM   1192  N   TYR A 175      -6.256  -1.824  -3.781  1.00 47.96           N  
ANISOU 1192  N   TYR A 175     6487   6577   5157     16    471    537       N  
ATOM   1193  CA  TYR A 175      -5.473  -2.394  -2.694  1.00 59.15           C  
ANISOU 1193  CA  TYR A 175     7741   8001   6731    -29    491    466       C  
ATOM   1194  C   TYR A 175      -6.224  -3.538  -2.026  1.00 54.19           C  
ANISOU 1194  C   TYR A 175     7081   7392   6116     26    372    329       C  
ATOM   1195  O   TYR A 175      -7.451  -3.504  -1.901  1.00 53.33           O  
ANISOU 1195  O   TYR A 175     7036   7255   5974     62    242    292       O  
ATOM   1196  CB  TYR A 175      -5.130  -1.311  -1.671  1.00 58.43           C  
ANISOU 1196  CB  TYR A 175     7566   7820   6816   -127    468    512       C  
ATOM   1197  CG  TYR A 175      -4.297  -0.201  -2.266  1.00 80.15           C  
ANISOU 1197  CG  TYR A 175    10333  10536   9585   -200    595    650       C  
ATOM   1198  CD1 TYR A 175      -3.178  -0.490  -3.035  1.00 92.71           C  
ANISOU 1198  CD1 TYR A 175    11888  12199  11138   -211    766    704       C  
ATOM   1199  CD2 TYR A 175      -4.642   1.131  -2.088  1.00 83.23           C  
ANISOU 1199  CD2 TYR A 175    10777  10815  10033   -255    555    732       C  
ATOM   1200  CE1 TYR A 175      -2.414   0.514  -3.592  1.00 98.88           C  
ANISOU 1200  CE1 TYR A 175    12678  12948  11944   -287    898    842       C  
ATOM   1201  CE2 TYR A 175      -3.884   2.145  -2.644  1.00 92.35           C  
ANISOU 1201  CE2 TYR A 175    11950  11923  11215   -331    677    868       C  
ATOM   1202  CZ  TYR A 175      -2.770   1.829  -3.396  1.00 99.56           C  
ANISOU 1202  CZ  TYR A 175    12820  12915  12094   -351    851    926       C  
ATOM   1203  OH  TYR A 175      -2.007   2.828  -3.955  1.00102.58           O  
ANISOU 1203  OH  TYR A 175    13214  13250  12511   -436    988   1072       O  
ATOM   1204  N   TYR A 176      -5.473  -4.552  -1.597  1.00 44.24           N  
ANISOU 1204  N   TYR A 176     5717   6178   4914     33    420    260       N  
ATOM   1205  CA  TYR A 176      -6.045  -5.764  -1.031  1.00 38.60           C  
ANISOU 1205  CA  TYR A 176     4977   5478   4213     84    331    139       C  
ATOM   1206  C   TYR A 176      -5.175  -6.266   0.110  1.00 43.13           C  
ANISOU 1206  C   TYR A 176     5397   6054   4936     55    348    100       C  
ATOM   1207  O   TYR A 176      -3.971  -5.999   0.163  1.00 56.63           O  
ANISOU 1207  O   TYR A 176     7017   7786   6715     14    451    150       O  
ATOM   1208  CB  TYR A 176      -6.178  -6.882  -2.080  1.00 43.91           C  
ANISOU 1208  CB  TYR A 176     5731   6213   4740    167    369     77       C  
ATOM   1209  CG  TYR A 176      -7.162  -6.598  -3.190  1.00 45.80           C  
ANISOU 1209  CG  TYR A 176     6129   6463   4810    209    318     93       C  
ATOM   1210  CD1 TYR A 176      -8.508  -6.916  -3.049  1.00 48.55           C  
ANISOU 1210  CD1 TYR A 176     6528   6789   5132    239    164     25       C  
ATOM   1211  CD2 TYR A 176      -6.747  -6.019  -4.381  1.00 47.62           C  
ANISOU 1211  CD2 TYR A 176     6455   6730   4907    220    422    181       C  
ATOM   1212  CE1 TYR A 176      -9.414  -6.660  -4.064  1.00 49.60           C  
ANISOU 1212  CE1 TYR A 176     6795   6939   5112    282     97     39       C  
ATOM   1213  CE2 TYR A 176      -7.646  -5.759  -5.403  1.00 51.51           C  
ANISOU 1213  CE2 TYR A 176     7102   7238   5229    268    361    201       C  
ATOM   1214  CZ  TYR A 176      -8.978  -6.081  -5.237  1.00 54.33           C  
ANISOU 1214  CZ  TYR A 176     7500   7577   5567    300    189    126       C  
ATOM   1215  OH  TYR A 176      -9.879  -5.824  -6.243  1.00 65.64           O  
ANISOU 1215  OH  TYR A 176     9075   9032   6834    350    109    145       O  
ATOM   1216  N   ALA A 177      -5.798  -7.007   1.019  1.00 42.82           N  
ANISOU 1216  N   ALA A 177     5326   5996   4949     77    245     17       N  
ATOM   1217  CA  ALA A 177      -5.091  -7.768   2.039  1.00 42.65           C  
ANISOU 1217  CA  ALA A 177     5180   5984   5040     76    248    -28       C  
ATOM   1218  C   ALA A 177      -5.085  -9.231   1.616  1.00 46.52           C  
ANISOU 1218  C   ALA A 177     5689   6509   5477    156    276   -106       C  
ATOM   1219  O   ALA A 177      -6.146  -9.808   1.352  1.00 42.65           O  
ANISOU 1219  O   ALA A 177     5283   6003   4919    196    205   -166       O  
ATOM   1220  CB  ALA A 177      -5.748  -7.604   3.409  1.00 37.56           C  
ANISOU 1220  CB  ALA A 177     4497   5290   4485     49    125    -59       C  
ATOM   1221  N   MET A 178      -3.899  -9.825   1.541  1.00 49.19           N  
ANISOU 1221  N   MET A 178     5945   6889   5856    180    378   -107       N  
ATOM   1222  CA  MET A 178      -3.754 -11.207   1.106  1.00 48.27           C  
ANISOU 1222  CA  MET A 178     5848   6793   5698    265    421   -182       C  
ATOM   1223  C   MET A 178      -3.304 -12.064   2.281  1.00 45.11           C  
ANISOU 1223  C   MET A 178     5335   6378   5425    286    388   -218       C  
ATOM   1224  O   MET A 178      -2.229 -11.837   2.846  1.00 48.73           O  
ANISOU 1224  O   MET A 178     5666   6863   5985    265    430   -175       O  
ATOM   1225  CB  MET A 178      -2.763 -11.319  -0.051  1.00 37.59           C  
ANISOU 1225  CB  MET A 178     4503   5502   4277    304    583   -158       C  
ATOM   1226  CG  MET A 178      -2.723 -12.704  -0.664  1.00 52.26           C  
ANISOU 1226  CG  MET A 178     6417   7372   6069    402    632   -251       C  
ATOM   1227  SD  MET A 178      -1.392 -12.886  -1.855  1.00 57.66           S  
ANISOU 1227  SD  MET A 178     7087   8135   6688    462    849   -226       S  
ATOM   1228  CE  MET A 178      -1.915 -11.742  -3.132  1.00 60.90           C  
ANISOU 1228  CE  MET A 178     7651   8574   6915    428    885   -158       C  
ATOM   1229  N   LYS A 179      -4.123 -13.049   2.637  1.00 54.86           N  
ANISOU 1229  N   LYS A 179     6616   7571   6656    326    310   -292       N  
ATOM   1230  CA  LYS A 179      -3.775 -14.027   3.661  1.00 48.36           C  
ANISOU 1230  CA  LYS A 179     5712   6725   5936    362    283   -321       C  
ATOM   1231  C   LYS A 179      -3.069 -15.196   2.987  1.00 45.18           C  
ANISOU 1231  C   LYS A 179     5310   6335   5519    453    382   -369       C  
ATOM   1232  O   LYS A 179      -3.681 -15.932   2.208  1.00 51.19           O  
ANISOU 1232  O   LYS A 179     6183   7071   6198    497    387   -441       O  
ATOM   1233  CB  LYS A 179      -5.020 -14.508   4.397  1.00 55.08           C  
ANISOU 1233  CB  LYS A 179     6613   7514   6800    355    164   -365       C  
ATOM   1234  CG  LYS A 179      -5.648 -13.482   5.301  1.00 59.15           C  
ANISOU 1234  CG  LYS A 179     7113   8015   7348    283     74   -324       C  
ATOM   1235  CD  LYS A 179      -6.819 -14.090   6.039  1.00 61.05           C  
ANISOU 1235  CD  LYS A 179     7389   8201   7608    285    -18   -364       C  
ATOM   1236  CE  LYS A 179      -7.149 -13.299   7.281  1.00 60.39           C  
ANISOU 1236  CE  LYS A 179     7264   8107   7576    235    -89   -327       C  
ATOM   1237  NZ  LYS A 179      -8.257 -13.938   8.040  1.00 57.65           N  
ANISOU 1237  NZ  LYS A 179     6942   7711   7250    239   -156   -357       N  
ATOM   1238  N   ILE A 180      -1.790 -15.373   3.289  1.00 46.76           N  
ANISOU 1238  N   ILE A 180     5386   6573   5806    483    456   -337       N  
ATOM   1239  CA  ILE A 180      -1.000 -16.467   2.738  1.00 51.87           C  
ANISOU 1239  CA  ILE A 180     6017   7231   6461    584    563   -379       C  
ATOM   1240  C   ILE A 180      -0.852 -17.520   3.827  1.00 57.30           C  
ANISOU 1240  C   ILE A 180     6644   7869   7258    638    504   -400       C  
ATOM   1241  O   ILE A 180      -0.101 -17.330   4.789  1.00 63.65           O  
ANISOU 1241  O   ILE A 180     7314   8699   8170    629    478   -345       O  
ATOM   1242  CB  ILE A 180       0.364 -15.980   2.239  1.00 52.22           C  
ANISOU 1242  CB  ILE A 180     5950   7356   6534    594    703   -321       C  
ATOM   1243  CG1 ILE A 180       0.189 -14.725   1.383  1.00 54.79           C  
ANISOU 1243  CG1 ILE A 180     6331   7721   6764    520    750   -269       C  
ATOM   1244  CG2 ILE A 180       1.059 -17.082   1.453  1.00 48.10           C  
ANISOU 1244  CG2 ILE A 180     5434   6846   5995    714    835   -376       C  
ATOM   1245  CD1 ILE A 180       1.466 -13.949   1.177  1.00 53.36           C  
ANISOU 1245  CD1 ILE A 180     6016   7613   6647    487    870   -185       C  
ATOM   1246  N   LEU A 181      -1.562 -18.633   3.677  1.00 56.92           N  
ANISOU 1246  N   LEU A 181     6697   7748   7182    691    476   -477       N  
ATOM   1247  CA  LEU A 181      -1.603 -19.681   4.683  1.00 54.80           C  
ANISOU 1247  CA  LEU A 181     6400   7412   7010    740    418   -489       C  
ATOM   1248  C   LEU A 181      -0.920 -20.943   4.172  1.00 57.70           C  
ANISOU 1248  C   LEU A 181     6775   7746   7404    862    512   -545       C  
ATOM   1249  O   LEU A 181      -0.934 -21.236   2.974  1.00 67.11           O  
ANISOU 1249  O   LEU A 181     8054   8937   8508    904    598   -612       O  
ATOM   1250  CB  LEU A 181      -3.047 -19.998   5.079  1.00 50.90           C  
ANISOU 1250  CB  LEU A 181     6011   6837   6492    694    306   -527       C  
ATOM   1251  CG  LEU A 181      -3.822 -18.832   5.689  1.00 54.26           C  
ANISOU 1251  CG  LEU A 181     6432   7285   6901    590    213   -478       C  
ATOM   1252  CD1 LEU A 181      -5.243 -19.243   6.012  1.00 42.26           C  
ANISOU 1252  CD1 LEU A 181     5000   5689   5369    554    122   -517       C  
ATOM   1253  CD2 LEU A 181      -3.110 -18.344   6.933  1.00 56.37           C  
ANISOU 1253  CD2 LEU A 181     6575   7588   7255    571    176   -401       C  
ATOM   1254  N   LYS A 182      -0.331 -21.692   5.103  1.00 53.67           N  
ANISOU 1254  N   LYS A 182     6180   7203   7009    927    494   -518       N  
ATOM   1255  CA  LYS A 182       0.348 -22.935   4.761  1.00 50.79           C  
ANISOU 1255  CA  LYS A 182     5814   6790   6693   1058    579   -565       C  
ATOM   1256  C   LYS A 182      -0.667 -24.014   4.400  1.00 52.01           C  
ANISOU 1256  C   LYS A 182     6131   6820   6811   1082    553   -661       C  
ATOM   1257  O   LYS A 182      -1.631 -24.246   5.134  1.00 55.26           O  
ANISOU 1257  O   LYS A 182     6594   7160   7243   1028    446   -655       O  
ATOM   1258  CB  LYS A 182       1.226 -23.389   5.925  1.00 56.97           C  
ANISOU 1258  CB  LYS A 182     6459   7571   7614   1124    549   -495       C  
ATOM   1259  CG  LYS A 182       2.313 -22.390   6.290  1.00 73.60           C  
ANISOU 1259  CG  LYS A 182     8388   9801   9777   1097    563   -409       C  
ATOM   1260  CD  LYS A 182       3.198 -22.893   7.421  1.00 84.40           C  
ANISOU 1260  CD  LYS A 182     9616  11175  11277   1172    514   -344       C  
ATOM   1261  CE  LYS A 182       4.280 -21.875   7.770  1.00 89.30           C  
ANISOU 1261  CE  LYS A 182    10047  11920  11964   1132    512   -269       C  
ATOM   1262  NZ  LYS A 182       5.161 -22.341   8.877  1.00 88.70           N  
ANISOU 1262  NZ  LYS A 182     9826  11862  12013   1209    442   -206       N  
ATOM   1263  N   LYS A 183      -0.438 -24.685   3.269  1.00 61.46           N  
ANISOU 1263  N   LYS A 183     7409   7989   7955   1163    656   -752       N  
ATOM   1264  CA  LYS A 183      -1.444 -25.598   2.734  1.00 72.75           C  
ANISOU 1264  CA  LYS A 183     9005   9300   9335   1169    625   -864       C  
ATOM   1265  C   LYS A 183      -1.495 -26.911   3.506  1.00 76.07           C  
ANISOU 1265  C   LYS A 183     9441   9583   9879   1236    591   -877       C  
ATOM   1266  O   LYS A 183      -2.568 -27.513   3.620  1.00 72.01           O  
ANISOU 1266  O   LYS A 183     9035   8957   9368   1191    514   -930       O  
ATOM   1267  CB  LYS A 183      -1.175 -25.861   1.252  1.00 78.35           C  
ANISOU 1267  CB  LYS A 183     9814  10025   9929   1235    742   -970       C  
ATOM   1268  CG  LYS A 183      -2.435 -26.070   0.432  1.00 80.44           C  
ANISOU 1268  CG  LYS A 183    10258  10232  10075   1178    678  -1081       C  
ATOM   1269  CD  LYS A 183      -2.169 -25.878  -1.050  1.00 83.34           C  
ANISOU 1269  CD  LYS A 183    10722  10663  10279   1223    785  -1162       C  
ATOM   1270  CE  LYS A 183      -1.509 -27.102  -1.655  1.00 86.47           C  
ANISOU 1270  CE  LYS A 183    11185  10986  10685   1365    899  -1270       C  
ATOM   1271  NZ  LYS A 183      -2.426 -28.273  -1.615  1.00 89.64           N  
ANISOU 1271  NZ  LYS A 183    11718  11222  11119   1363    809  -1386       N  
ATOM   1272  N   GLU A 184      -0.356 -27.371   4.036  1.00 89.47           N  
ANISOU 1272  N   GLU A 184    11027  11282  11684   1344    647   -824       N  
ATOM   1273  CA  GLU A 184      -0.337 -28.623   4.791  1.00 95.92           C  
ANISOU 1273  CA  GLU A 184    11862  11960  12621   1422    618   -819       C  
ATOM   1274  C   GLU A 184      -1.282 -28.577   5.982  1.00 92.63           C  
ANISOU 1274  C   GLU A 184    11457  11490  12247   1326    483   -749       C  
ATOM   1275  O   GLU A 184      -1.874 -29.598   6.350  1.00 93.50           O  
ANISOU 1275  O   GLU A 184    11653  11455  12419   1339    446   -771       O  
ATOM   1276  CB  GLU A 184       1.078 -28.927   5.281  1.00106.33           C  
ANISOU 1276  CB  GLU A 184    13033  13315  14051   1555    680   -747       C  
ATOM   1277  CG  GLU A 184       2.110 -29.122   4.189  1.00115.96           C  
ANISOU 1277  CG  GLU A 184    14224  14583  15255   1674    837   -810       C  
ATOM   1278  CD  GLU A 184       3.488 -29.399   4.755  1.00119.56           C  
ANISOU 1278  CD  GLU A 184    14504  15081  15843   1805    889   -730       C  
ATOM   1279  OE1 GLU A 184       3.672 -29.212   5.976  1.00118.74           O  
ANISOU 1279  OE1 GLU A 184    14295  14998  15823   1786    787   -619       O  
ATOM   1280  OE2 GLU A 184       4.384 -29.805   3.987  1.00121.27           O  
ANISOU 1280  OE2 GLU A 184    14686  15314  16078   1933   1028   -778       O  
ATOM   1281  N   VAL A 185      -1.441 -27.398   6.584  1.00 85.73           N  
ANISOU 1281  N   VAL A 185    10503  10727  11343   1228    418   -666       N  
ATOM   1282  CA  VAL A 185      -2.234 -27.254   7.798  1.00 79.35           C  
ANISOU 1282  CA  VAL A 185     9695   9889  10567   1148    306   -592       C  
ATOM   1283  C   VAL A 185      -3.722 -27.423   7.509  1.00 79.52           C  
ANISOU 1283  C   VAL A 185     9845   9826  10542   1049    252   -657       C  
ATOM   1284  O   VAL A 185      -4.475 -27.938   8.344  1.00 81.41           O  
ANISOU 1284  O   VAL A 185    10122   9976  10835   1013    191   -623       O  
ATOM   1285  CB  VAL A 185      -1.920 -25.888   8.439  1.00 76.04           C  
ANISOU 1285  CB  VAL A 185     9159   9612  10121   1078    260   -502       C  
ATOM   1286  CG1 VAL A 185      -2.950 -25.521   9.481  1.00 77.13           C  
ANISOU 1286  CG1 VAL A 185     9322   9733  10251    980    155   -449       C  
ATOM   1287  CG2 VAL A 185      -0.521 -25.906   9.033  1.00 74.31           C  
ANISOU 1287  CG2 VAL A 185     8796   9457   9981   1170    279   -426       C  
ATOM   1288  N   ILE A 186      -4.172 -27.016   6.326  1.00 86.66           N  
ANISOU 1288  N   ILE A 186    10817  10761  11348   1004    274   -747       N  
ATOM   1289  CA  ILE A 186      -5.598 -26.864   6.063  1.00 89.95           C  
ANISOU 1289  CA  ILE A 186    11324  11137  11715    895    200   -799       C  
ATOM   1290  C   ILE A 186      -6.186 -28.127   5.442  1.00103.79           C  
ANISOU 1290  C   ILE A 186    13202  12741  13493    914    203   -912       C  
ATOM   1291  O   ILE A 186      -7.014 -28.804   6.062  1.00109.70           O  
ANISOU 1291  O   ILE A 186    13987  13376  14317    868    147   -906       O  
ATOM   1292  CB  ILE A 186      -5.846 -25.629   5.179  1.00 82.32           C  
ANISOU 1292  CB  ILE A 186    10365  10291  10624    831    198   -824       C  
ATOM   1293  CG1 ILE A 186      -5.151 -24.420   5.816  1.00 76.77           C  
ANISOU 1293  CG1 ILE A 186     9538   9713   9917    812    201   -715       C  
ATOM   1294  CG2 ILE A 186      -7.327 -25.365   5.055  1.00 84.62           C  
ANISOU 1294  CG2 ILE A 186    10721  10553  10877    722    104   -860       C  
ATOM   1295  CD1 ILE A 186      -5.094 -23.188   4.948  1.00 80.31           C  
ANISOU 1295  CD1 ILE A 186     9984  10273  10255    766    223   -719       C  
ATOM   1296  N   VAL A 187      -5.771 -28.452   4.218  1.00109.61           N  
ANISOU 1296  N   VAL A 187    14008  13474  14164    977    271  -1018       N  
ATOM   1297  CA  VAL A 187      -6.315 -29.582   3.474  1.00117.81           C  
ANISOU 1297  CA  VAL A 187    15182  14372  15209    992    268  -1153       C  
ATOM   1298  C   VAL A 187      -5.167 -30.467   3.003  1.00117.95           C  
ANISOU 1298  C   VAL A 187    15226  14337  15255   1142    382  -1207       C  
ATOM   1299  O   VAL A 187      -4.046 -29.995   2.782  1.00119.20           O  
ANISOU 1299  O   VAL A 187    15307  14604  15380   1223    473  -1169       O  
ATOM   1300  CB  VAL A 187      -7.189 -29.110   2.281  1.00125.28           C  
ANISOU 1300  CB  VAL A 187    16224  15361  16017    917    222  -1261       C  
ATOM   1301  CG1 VAL A 187      -7.299 -27.599   2.269  1.00127.27           C  
ANISOU 1301  CG1 VAL A 187    16403  15778  16175    851    196  -1182       C  
ATOM   1302  CG2 VAL A 187      -6.616 -29.576   0.959  1.00128.25           C  
ANISOU 1302  CG2 VAL A 187    16704  15729  16296   1010    307  -1391       C  
ATOM   1303  N   ALA A 188      -5.449 -31.767   2.860  1.00117.87           N  
ANISOU 1303  N   ALA A 188    15319  14151  15317   1179    382  -1297       N  
ATOM   1304  CA  ALA A 188      -4.418 -32.735   2.502  1.00114.18           C  
ANISOU 1304  CA  ALA A 188    14884  13603  14896   1335    491  -1353       C  
ATOM   1305  C   ALA A 188      -4.213 -32.886   1.000  1.00115.76           C  
ANISOU 1305  C   ALA A 188    15199  13818  14965   1392    564  -1513       C  
ATOM   1306  O   ALA A 188      -3.092 -33.176   0.567  1.00120.99           O  
ANISOU 1306  O   ALA A 188    15848  14501  15622   1534    690  -1539       O  
ATOM   1307  CB  ALA A 188      -4.747 -34.107   3.098  1.00109.68           C  
ANISOU 1307  CB  ALA A 188    14383  12814  14478   1360    464  -1370       C  
ATOM   1308  N   LYS A 189      -5.257 -32.705   0.193  1.00110.99           N  
ANISOU 1308  N   LYS A 189    14709  13210  14252   1293    490  -1621       N  
ATOM   1309  CA  LYS A 189      -5.220 -33.024  -1.229  1.00110.90           C  
ANISOU 1309  CA  LYS A 189    14846  13189  14103   1344    539  -1793       C  
ATOM   1310  C   LYS A 189      -5.361 -31.765  -2.073  1.00114.16           C  
ANISOU 1310  C   LYS A 189    15263  13791  14322   1293    538  -1792       C  
ATOM   1311  O   LYS A 189      -6.213 -30.917  -1.799  1.00114.82           O  
ANISOU 1311  O   LYS A 189    15308  13944  14376   1166    429  -1730       O  
ATOM   1312  CB  LYS A 189      -6.336 -34.012  -1.586  1.00111.00           C  
ANISOU 1312  CB  LYS A 189    15012  13021  14140   1277    438  -1942       C  
ATOM   1313  CG  LYS A 189      -6.311 -34.504  -3.021  1.00113.03           C  
ANISOU 1313  CG  LYS A 189    15448  13246  14254   1337    476  -2143       C  
ATOM   1314  CD  LYS A 189      -7.369 -35.582  -3.231  1.00111.73           C  
ANISOU 1314  CD  LYS A 189    15424  12876  14151   1263    363  -2294       C  
ATOM   1315  CE  LYS A 189      -7.235 -36.699  -2.202  1.00106.51           C  
ANISOU 1315  CE  LYS A 189    14739  12010  13721   1294    375  -2250       C  
ATOM   1316  NZ  LYS A 189      -8.565 -37.266  -1.830  1.00104.37           N  
ANISOU 1316  NZ  LYS A 189    14512  11580  13562   1139    228  -2291       N  
ATOM   1317  N   ASP A 190      -4.535 -31.661  -3.121  1.00113.64           N  
ANISOU 1317  N   ASP A 190    15251  13803  14124   1399    666  -1859       N  
ATOM   1318  CA  ASP A 190      -4.564 -30.480  -3.982  1.00113.34           C  
ANISOU 1318  CA  ASP A 190    15229  13942  13892   1363    685  -1845       C  
ATOM   1319  C   ASP A 190      -5.886 -30.353  -4.732  1.00106.25           C  
ANISOU 1319  C   ASP A 190    14475  13032  12864   1258    543  -1954       C  
ATOM   1320  O   ASP A 190      -6.276 -29.244  -5.118  1.00103.80           O  
ANISOU 1320  O   ASP A 190    14159  12855  12424   1188    498  -1904       O  
ATOM   1321  CB  ASP A 190      -3.398 -30.516  -4.976  1.00118.80           C  
ANISOU 1321  CB  ASP A 190    15961  14711  14466   1507    872  -1897       C  
ATOM   1322  CG  ASP A 190      -2.045 -30.323  -4.307  1.00121.35           C  
ANISOU 1322  CG  ASP A 190    16102  15096  14909   1600   1011  -1765       C  
ATOM   1323  OD1 ASP A 190      -2.008 -30.079  -3.079  1.00121.62           O  
ANISOU 1323  OD1 ASP A 190    15988  15125  15098   1551    948  -1633       O  
ATOM   1324  OD2 ASP A 190      -1.012 -30.414  -5.009  1.00123.49           O  
ANISOU 1324  OD2 ASP A 190    16376  15428  15119   1726   1182  -1795       O  
ATOM   1325  N   GLU A 191      -6.581 -31.471  -4.965  1.00103.29           N  
ANISOU 1325  N   GLU A 191    14227  12494  12524   1244    465  -2103       N  
ATOM   1326  CA  GLU A 191      -7.875 -31.402  -5.637  1.00 97.45           C  
ANISOU 1326  CA  GLU A 191    13608  11741  11679   1136    306  -2213       C  
ATOM   1327  C   GLU A 191      -8.942 -30.778  -4.747  1.00101.35           C  
ANISOU 1327  C   GLU A 191    13992  12249  12266    985    154  -2104       C  
ATOM   1328  O   GLU A 191      -9.835 -30.084  -5.248  1.00101.64           O  
ANISOU 1328  O   GLU A 191    14062  12365  12191    898     39  -2122       O  
ATOM   1329  CB  GLU A 191      -8.322 -32.793  -6.088  1.00 95.64           C  
ANISOU 1329  CB  GLU A 191    13536  11320  11483   1150    257  -2410       C  
ATOM   1330  CG  GLU A 191      -7.740 -33.245  -7.421  1.00 97.08           C  
ANISOU 1330  CG  GLU A 191    13896  11509  11482   1273    357  -2579       C  
ATOM   1331  CD  GLU A 191      -8.486 -34.432  -8.008  1.00103.13           C  
ANISOU 1331  CD  GLU A 191    14842  12094  12247   1250    256  -2799       C  
ATOM   1332  OE1 GLU A 191      -9.418 -34.933  -7.342  1.00103.67           O  
ANISOU 1332  OE1 GLU A 191    14883  12026  12481   1133    117  -2808       O  
ATOM   1333  OE2 GLU A 191      -8.146 -34.861  -9.132  1.00105.59           O  
ANISOU 1333  OE2 GLU A 191    15326  12399  12394   1345    319  -2965       O  
ATOM   1334  N   VAL A 192      -8.867 -31.011  -3.436  1.00107.49           N  
ANISOU 1334  N   VAL A 192    14641  12955  13244    960    153  -1991       N  
ATOM   1335  CA  VAL A 192      -9.838 -30.431  -2.514  1.00105.36           C  
ANISOU 1335  CA  VAL A 192    14264  12701  13065    828     31  -1883       C  
ATOM   1336  C   VAL A 192      -9.566 -28.945  -2.313  1.00104.90           C  
ANISOU 1336  C   VAL A 192    14098  12829  12930    809     52  -1739       C  
ATOM   1337  O   VAL A 192     -10.497 -28.142  -2.193  1.00106.78           O  
ANISOU 1337  O   VAL A 192    14300  13130  13143    708    -56  -1694       O  
ATOM   1338  CB  VAL A 192      -9.831 -31.202  -1.178  1.00 98.96           C  
ANISOU 1338  CB  VAL A 192    13372  11754  12475    815     34  -1807       C  
ATOM   1339  CG1 VAL A 192     -10.783 -30.557  -0.178  1.00 90.29           C  
ANISOU 1339  CG1 VAL A 192    12161  10685  11460    688    -68  -1689       C  
ATOM   1340  CG2 VAL A 192     -10.202 -32.660  -1.407  1.00 98.65           C  
ANISOU 1340  CG2 VAL A 192    13450  11508  12525    818      6  -1950       C  
ATOM   1341  N   ALA A 193      -8.291 -28.552  -2.285  1.00 99.22           N  
ANISOU 1341  N   ALA A 193    13322  12195  12183    905    192  -1664       N  
ATOM   1342  CA  ALA A 193      -7.956 -27.143  -2.114  1.00 94.53           C  
ANISOU 1342  CA  ALA A 193    12627  11762  11527    881    218  -1530       C  
ATOM   1343  C   ALA A 193      -8.393 -26.311  -3.312  1.00 97.25           C  
ANISOU 1343  C   ALA A 193    13064  12215  11670    855    185  -1573       C  
ATOM   1344  O   ALA A 193      -8.738 -25.135  -3.152  1.00 90.56           O  
ANISOU 1344  O   ALA A 193    12159  11467  10783    789    138  -1475       O  
ATOM   1345  CB  ALA A 193      -6.453 -26.982  -1.872  1.00 90.74           C  
ANISOU 1345  CB  ALA A 193    12057  11344  11077    985    375  -1449       C  
ATOM   1346  N   HIS A 194      -8.385 -26.896  -4.515  1.00111.71           N  
ANISOU 1346  N   HIS A 194    15050  14027  13368    910    207  -1717       N  
ATOM   1347  CA  HIS A 194      -8.886 -26.178  -5.684  1.00118.23           C  
ANISOU 1347  CA  HIS A 194    15984  14954  13982    889    158  -1761       C  
ATOM   1348  C   HIS A 194     -10.382 -25.921  -5.562  1.00114.13           C  
ANISOU 1348  C   HIS A 194    15473  14414  13475    768    -41  -1779       C  
ATOM   1349  O   HIS A 194     -10.864 -24.830  -5.891  1.00111.94           O  
ANISOU 1349  O   HIS A 194    15194  14244  13095    723   -104  -1716       O  
ATOM   1350  CB  HIS A 194      -8.578 -26.960  -6.962  1.00120.30           C  
ANISOU 1350  CB  HIS A 194    16426  15195  14088    980    219  -1927       C  
ATOM   1351  CG  HIS A 194      -9.091 -26.306  -8.206  1.00124.43           C  
ANISOU 1351  CG  HIS A 194    17085  15824  14370    968    161  -1977       C  
ATOM   1352  ND1 HIS A 194      -8.585 -25.117  -8.685  1.00124.88           N  
ANISOU 1352  ND1 HIS A 194    17133  16033  14284    991    246  -1865       N  
ATOM   1353  CD2 HIS A 194     -10.072 -26.671  -9.065  1.00126.50           C  
ANISOU 1353  CD2 HIS A 194    17498  16060  14508    936     20  -2122       C  
ATOM   1354  CE1 HIS A 194      -9.227 -24.781  -9.789  1.00126.21           C  
ANISOU 1354  CE1 HIS A 194    17449  16266  14239    982    163  -1931       C  
ATOM   1355  NE2 HIS A 194     -10.135 -25.707 -10.042  1.00126.92           N  
ANISOU 1355  NE2 HIS A 194    17636  16256  14333    950     18  -2091       N  
ATOM   1356  N   THR A 195     -11.135 -26.919  -5.093  1.00110.77           N  
ANISOU 1356  N   THR A 195    15053  13849  13185    716   -138  -1860       N  
ATOM   1357  CA  THR A 195     -12.546 -26.695  -4.805  1.00103.50           C  
ANISOU 1357  CA  THR A 195    14099  12908  12319    596   -317  -1861       C  
ATOM   1358  C   THR A 195     -12.727 -25.727  -3.641  1.00 95.43           C  
ANISOU 1358  C   THR A 195    12911  11940  11407    537   -329  -1687       C  
ATOM   1359  O   THR A 195     -13.747 -25.033  -3.565  1.00 80.45           O  
ANISOU 1359  O   THR A 195    10975  10088   9506    458   -450  -1652       O  
ATOM   1360  CB  THR A 195     -13.243 -28.025  -4.510  1.00 98.62           C  
ANISOU 1360  CB  THR A 195    13510  12116  11844    545   -399  -1978       C  
ATOM   1361  OG1 THR A 195     -12.808 -28.526  -3.240  1.00105.61           O  
ANISOU 1361  OG1 THR A 195    14290  12910  12928    550   -326  -1891       O  
ATOM   1362  CG2 THR A 195     -12.916 -29.053  -5.594  1.00 82.23           C  
ANISOU 1362  CG2 THR A 195    11608   9965   9669    615   -372  -2163       C  
ATOM   1363  N   LEU A 196     -11.747 -25.656  -2.736  1.00 97.30           N  
ANISOU 1363  N   LEU A 196    13051  12177  11742    581   -208  -1581       N  
ATOM   1364  CA  LEU A 196     -11.831 -24.726  -1.612  1.00 96.45           C  
ANISOU 1364  CA  LEU A 196    12800  12122  11726    531   -216  -1426       C  
ATOM   1365  C   LEU A 196     -11.679 -23.283  -2.082  1.00100.75           C  
ANISOU 1365  C   LEU A 196    13332  12811  12137    530   -206  -1344       C  
ATOM   1366  O   LEU A 196     -12.448 -22.403  -1.679  1.00100.71           O  
ANISOU 1366  O   LEU A 196    13267  12848  12151    463   -289  -1273       O  
ATOM   1367  CB  LEU A 196     -10.767 -25.072  -0.568  1.00 95.40           C  
ANISOU 1367  CB  LEU A 196    12576  11954  11720    583   -104  -1344       C  
ATOM   1368  CG  LEU A 196     -10.650 -24.148   0.647  1.00 92.68           C  
ANISOU 1368  CG  LEU A 196    12093  11665  11457    545   -103  -1192       C  
ATOM   1369  CD1 LEU A 196     -11.954 -24.099   1.428  1.00 91.88           C  
ANISOU 1369  CD1 LEU A 196    11946  11517  11448    448   -219  -1169       C  
ATOM   1370  CD2 LEU A 196      -9.505 -24.592   1.541  1.00 92.07           C  
ANISOU 1370  CD2 LEU A 196    11939  11559  11484    610     -5  -1127       C  
ATOM   1371  N   THR A 197     -10.678 -23.021  -2.925  1.00101.39           N  
ANISOU 1371  N   THR A 197    13471  12964  12089    607    -94  -1348       N  
ATOM   1372  CA  THR A 197     -10.531 -21.696  -3.524  1.00102.06           C  
ANISOU 1372  CA  THR A 197    13568  13175  12037    604    -75  -1270       C  
ATOM   1373  C   THR A 197     -11.716 -21.364  -4.423  1.00104.17           C  
ANISOU 1373  C   THR A 197    13933  13471  12174    564   -214  -1329       C  
ATOM   1374  O   THR A 197     -12.178 -20.217  -4.454  1.00 98.60           O  
ANISOU 1374  O   THR A 197    13203  12836  11425    526   -270  -1242       O  
ATOM   1375  CB  THR A 197      -9.224 -21.616  -4.320  1.00 99.43           C  
ANISOU 1375  CB  THR A 197    13282  12907  11590    695     90  -1266       C  
ATOM   1376  OG1 THR A 197      -9.241 -22.584  -5.380  1.00 99.42           O  
ANISOU 1376  OG1 THR A 197    13428  12872  11474    755    105  -1415       O  
ATOM   1377  CG2 THR A 197      -8.034 -21.896  -3.426  1.00 94.45           C  
ANISOU 1377  CG2 THR A 197    12530  12258  11100    739    215  -1202       C  
ATOM   1378  N   GLU A 198     -12.227 -22.360  -5.148  1.00115.79           N  
ANISOU 1378  N   GLU A 198    15519  14886  13592    574   -280  -1478       N  
ATOM   1379  CA  GLU A 198     -13.321 -22.127  -6.083  1.00119.94           C  
ANISOU 1379  CA  GLU A 198    16143  15446  13984    542   -429  -1548       C  
ATOM   1380  C   GLU A 198     -14.610 -21.780  -5.345  1.00116.33           C  
ANISOU 1380  C   GLU A 198    15584  14964  13651    446   -587  -1509       C  
ATOM   1381  O   GLU A 198     -15.318 -20.839  -5.719  1.00118.61           O  
ANISOU 1381  O   GLU A 198    15877  15328  13861    422   -684  -1463       O  
ATOM   1382  CB  GLU A 198     -13.503 -23.363  -6.968  1.00125.89           C  
ANISOU 1382  CB  GLU A 198    17041  16131  14661    571   -468  -1735       C  
ATOM   1383  CG  GLU A 198     -14.375 -23.167  -8.196  1.00130.49           C  
ANISOU 1383  CG  GLU A 198    17759  16771  15052    561   -612  -1826       C  
ATOM   1384  CD  GLU A 198     -14.393 -24.400  -9.086  1.00134.48           C  
ANISOU 1384  CD  GLU A 198    18424  17207  15467    597   -637  -2026       C  
ATOM   1385  OE1 GLU A 198     -13.675 -25.373  -8.770  1.00135.24           O  
ANISOU 1385  OE1 GLU A 198    18527  17206  15654    638   -526  -2086       O  
ATOM   1386  OE2 GLU A 198     -15.122 -24.399 -10.099  1.00136.37           O  
ANISOU 1386  OE2 GLU A 198    18786  17484  15544    589   -774  -2126       O  
ATOM   1387  N   ASN A 199     -14.919 -22.520  -4.276  1.00106.25           N  
ANISOU 1387  N   ASN A 199    14213  13584  12574    397   -605  -1518       N  
ATOM   1388  CA  ASN A 199     -16.180 -22.320  -3.568  1.00101.29           C  
ANISOU 1388  CA  ASN A 199    13483  12929  12074    307   -738  -1489       C  
ATOM   1389  C   ASN A 199     -16.174 -21.019  -2.777  1.00 90.83           C  
ANISOU 1389  C   ASN A 199    12045  11675  10790    292   -714  -1331       C  
ATOM   1390  O   ASN A 199     -17.109 -20.217  -2.877  1.00 79.51           O  
ANISOU 1390  O   ASN A 199    10578  10291   9340    256   -822  -1295       O  
ATOM   1391  CB  ASN A 199     -16.455 -23.499  -2.630  1.00105.94           C  
ANISOU 1391  CB  ASN A 199    14012  13383  12860    259   -741  -1531       C  
ATOM   1392  CG  ASN A 199     -16.781 -24.778  -3.371  1.00115.25           C  
ANISOU 1392  CG  ASN A 199    15297  14464  14027    248   -803  -1701       C  
ATOM   1393  OD1 ASN A 199     -17.221 -24.750  -4.523  1.00121.18           O  
ANISOU 1393  OD1 ASN A 199    16153  15255  14636    251   -898  -1801       O  
ATOM   1394  ND2 ASN A 199     -16.574 -25.913  -2.706  1.00114.92           N  
ANISOU 1394  ND2 ASN A 199    15241  14289  14136    237   -754  -1736       N  
ATOM   1395  N   ARG A 200     -15.123 -20.799  -1.978  1.00 93.53           N  
ANISOU 1395  N   ARG A 200    12326  12020  11190    323   -580  -1240       N  
ATOM   1396  CA  ARG A 200     -15.157 -19.758  -0.954  1.00 90.11           C  
ANISOU 1396  CA  ARG A 200    11778  11623  10835    296   -564  -1106       C  
ATOM   1397  C   ARG A 200     -15.358 -18.371  -1.549  1.00 91.88           C  
ANISOU 1397  C   ARG A 200    12023  11945  10941    303   -597  -1037       C  
ATOM   1398  O   ARG A 200     -15.898 -17.481  -0.881  1.00 89.12           O  
ANISOU 1398  O   ARG A 200    11594  11614  10653    271   -637   -955       O  
ATOM   1399  CB  ARG A 200     -13.873 -19.802  -0.125  1.00 83.87           C  
ANISOU 1399  CB  ARG A 200    10932  10827  10110    332   -425  -1035       C  
ATOM   1400  CG  ARG A 200     -13.933 -18.976   1.148  1.00 78.15           C  
ANISOU 1400  CG  ARG A 200    10090  10115   9487    298   -418   -920       C  
ATOM   1401  CD  ARG A 200     -13.466 -19.774   2.343  1.00 77.68           C  
ANISOU 1401  CD  ARG A 200     9963   9988   9562    300   -364   -898       C  
ATOM   1402  NE  ARG A 200     -14.313 -20.939   2.549  1.00 79.49           N  
ANISOU 1402  NE  ARG A 200    10202  10122   9877    267   -421   -971       N  
ATOM   1403  CZ  ARG A 200     -14.071 -21.884   3.449  1.00 77.56           C  
ANISOU 1403  CZ  ARG A 200     9925   9796   9747    271   -383   -963       C  
ATOM   1404  NH1 ARG A 200     -14.897 -22.914   3.569  1.00 78.65           N  
ANISOU 1404  NH1 ARG A 200    10076   9836   9970    230   -433  -1025       N  
ATOM   1405  NH2 ARG A 200     -12.999 -21.801   4.226  1.00 69.65           N  
ANISOU 1405  NH2 ARG A 200     8876   8808   8781    313   -299   -889       N  
ATOM   1406  N   VAL A 201     -14.951 -18.169  -2.803  1.00 97.16           N  
ANISOU 1406  N   VAL A 201    12807  12672  11438    350   -576  -1067       N  
ATOM   1407  CA  VAL A 201     -15.128 -16.862  -3.431  1.00101.92           C  
ANISOU 1407  CA  VAL A 201    13446  13358  11919    362   -605   -989       C  
ATOM   1408  C   VAL A 201     -16.611 -16.528  -3.572  1.00108.42           C  
ANISOU 1408  C   VAL A 201    14254  14188  12752    325   -778  -1004       C  
ATOM   1409  O   VAL A 201     -17.025 -15.375  -3.385  1.00114.02           O  
ANISOU 1409  O   VAL A 201    14924  14934  13464    318   -816   -910       O  
ATOM   1410  CB  VAL A 201     -14.390 -16.823  -4.783  1.00108.44           C  
ANISOU 1410  CB  VAL A 201    14414  14246  12542    425   -536  -1016       C  
ATOM   1411  CG1 VAL A 201     -14.963 -15.745  -5.676  1.00111.88           C  
ANISOU 1411  CG1 VAL A 201    14925  14757  12828    437   -616   -962       C  
ATOM   1412  CG2 VAL A 201     -12.904 -16.599  -4.553  1.00109.24           C  
ANISOU 1412  CG2 VAL A 201    14488  14368  12648    460   -352   -944       C  
ATOM   1413  N   LEU A 202     -17.439 -17.531  -3.871  1.00109.09           N  
ANISOU 1413  N   LEU A 202    14361  14231  12858    299   -886  -1125       N  
ATOM   1414  CA  LEU A 202     -18.854 -17.321  -4.155  1.00106.26           C  
ANISOU 1414  CA  LEU A 202    13980  13887  12508    264  -1064  -1154       C  
ATOM   1415  C   LEU A 202     -19.770 -17.532  -2.953  1.00104.36           C  
ANISOU 1415  C   LEU A 202    13586  13587  12480    197  -1118  -1140       C  
ATOM   1416  O   LEU A 202     -20.946 -17.161  -3.023  1.00 96.00           O  
ANISOU 1416  O   LEU A 202    12470  12549  11457    171  -1252  -1139       O  
ATOM   1417  CB  LEU A 202     -19.304 -18.247  -5.297  1.00101.62           C  
ANISOU 1417  CB  LEU A 202    13505  13294  11812    265  -1173  -1304       C  
ATOM   1418  CG  LEU A 202     -18.687 -18.019  -6.681  1.00 98.68           C  
ANISOU 1418  CG  LEU A 202    13306  12996  11191    337  -1150  -1331       C  
ATOM   1419  CD1 LEU A 202     -19.080 -19.125  -7.650  1.00 98.69           C  
ANISOU 1419  CD1 LEU A 202    13425  12975  11098    335  -1254  -1506       C  
ATOM   1420  CD2 LEU A 202     -19.091 -16.660  -7.235  1.00100.86           C  
ANISOU 1420  CD2 LEU A 202    13609  13366  11346    368  -1219  -1227       C  
ATOM   1421  N   GLN A 203     -19.270 -18.098  -1.853  1.00105.32           N  
ANISOU 1421  N   GLN A 203    13637  13641  12738    175  -1014  -1123       N  
ATOM   1422  CA  GLN A 203     -20.119 -18.525  -0.737  1.00110.17           C  
ANISOU 1422  CA  GLN A 203    14124  14192  13544    110  -1048  -1118       C  
ATOM   1423  C   GLN A 203     -20.569 -17.314   0.083  1.00123.27           C  
ANISOU 1423  C   GLN A 203    15680  15891  15267    107  -1048  -1002       C  
ATOM   1424  O   GLN A 203     -20.031 -17.009   1.152  1.00123.40           O  
ANISOU 1424  O   GLN A 203    15639  15893  15354    110   -947   -924       O  
ATOM   1425  CB  GLN A 203     -19.383 -19.551   0.119  1.00 99.35           C  
ANISOU 1425  CB  GLN A 203    12736  12736  12278     99   -936  -1130       C  
ATOM   1426  CG  GLN A 203     -19.289 -20.937  -0.526  1.00 95.54           C  
ANISOU 1426  CG  GLN A 203    12336  12177  11786     89   -956  -1262       C  
ATOM   1427  CD  GLN A 203     -18.333 -21.874   0.193  1.00 96.30           C  
ANISOU 1427  CD  GLN A 203    12437  12189  11965    107   -831  -1261       C  
ATOM   1428  OE1 GLN A 203     -17.368 -21.438   0.818  1.00 90.97           O  
ANISOU 1428  OE1 GLN A 203    11735  11540  11290    149   -720  -1171       O  
ATOM   1429  NE2 GLN A 203     -18.601 -23.172   0.104  1.00102.09           N  
ANISOU 1429  NE2 GLN A 203    13202  12815  12773     74   -857  -1361       N  
ATOM   1430  N   ASN A 204     -21.595 -16.631  -0.439  1.00139.56           N  
ANISOU 1430  N   ASN A 204    17721  18004  17302    106  -1173   -997       N  
ATOM   1431  CA  ASN A 204     -22.280 -15.503   0.215  1.00142.14           C  
ANISOU 1431  CA  ASN A 204    17949  18361  17698    112  -1196   -904       C  
ATOM   1432  C   ASN A 204     -21.310 -14.609   0.988  1.00131.61           C  
ANISOU 1432  C   ASN A 204    16613  17035  16358    144  -1064   -800       C  
ATOM   1433  O   ASN A 204     -21.499 -14.306   2.169  1.00131.13           O  
ANISOU 1433  O   ASN A 204    16460  16952  16410    129  -1015   -746       O  
ATOM   1434  CB  ASN A 204     -23.402 -15.999   1.129  1.00153.69           C  
ANISOU 1434  CB  ASN A 204    19271  19780  19344     52  -1236   -919       C  
ATOM   1435  CG  ASN A 204     -24.429 -16.846   0.393  1.00163.91           C  
ANISOU 1435  CG  ASN A 204    20547  21063  20670      3  -1381  -1024       C  
ATOM   1436  OD1 ASN A 204     -24.730 -16.601  -0.778  1.00167.30           O  
ANISOU 1436  OD1 ASN A 204    21042  21544  20982     28  -1499  -1066       O  
ATOM   1437  ND2 ASN A 204     -24.966 -17.855   1.076  1.00167.36           N  
ANISOU 1437  ND2 ASN A 204    20897  21429  21265    -69  -1376  -1065       N  
ATOM   1438  N  ASER A 205     -20.250 -14.184   0.298  0.58113.33           N  
ANISOU 1438  N  ASER A 205    14401  14752  13905    186  -1005   -774       N  
ATOM   1439  N  BSER A 205     -20.252 -14.179   0.297  0.42113.35           N  
ANISOU 1439  N  BSER A 205    14405  14756  13908    186  -1006   -774       N  
ATOM   1440  CA ASER A 205     -19.247 -13.335   0.932  0.58103.35           C  
ANISOU 1440  CA ASER A 205    13134  13494  12639    205   -889   -682       C  
ATOM   1441  CA BSER A 205     -19.247 -13.341   0.940  0.42103.35           C  
ANISOU 1441  CA BSER A 205    13134  13494  12641    205   -888   -682       C  
ATOM   1442  C  ASER A 205     -19.794 -11.948   1.243  0.58102.10           C  
ANISOU 1442  C  ASER A 205    12937  13355  12502    222   -921   -597       C  
ATOM   1443  C  BSER A 205     -19.772 -11.939   1.221  0.42102.04           C  
ANISOU 1443  C  BSER A 205    12931  13347  12491    223   -920   -597       C  
ATOM   1444  O  ASER A 205     -19.325 -11.291   2.180  0.58102.52           O  
ANISOU 1444  O  ASER A 205    12951  13391  12612    220   -845   -534       O  
ATOM   1445  O  BSER A 205     -19.271 -11.263   2.127  0.42101.74           O  
ANISOU 1445  O  BSER A 205    12857  13294  12506    221   -843   -532       O  
ATOM   1446  CB ASER A 205     -18.015 -13.212   0.031  0.58 94.91           C  
ANISOU 1446  CB ASER A 205    12175  12458  11430    239   -811   -672       C  
ATOM   1447  CB BSER A 205     -17.991 -13.268   0.071  0.42 95.07           C  
ANISOU 1447  CB BSER A 205    12192  12475  11454    238   -808   -674       C  
ATOM   1448  OG ASER A 205     -17.687 -14.447  -0.579  0.58 87.34           O  
ANISOU 1448  OG ASER A 205    11276  11487  10424    243   -801   -767       O  
ATOM   1449  OG BSER A 205     -17.046 -12.363   0.616  0.42 87.77           O  
ANISOU 1449  OG BSER A 205    11252  11557  10538    245   -707   -583       O  
ATOM   1450  N   ARG A 206     -20.786 -11.496   0.480  1.00 99.66           N  
ANISOU 1450  N   ARG A 206    12639  13076  12150    243  -1039   -599       N  
ATOM   1451  CA  ARG A 206     -21.171 -10.090   0.454  1.00 95.99           C  
ANISOU 1451  CA  ARG A 206    12171  12626  11674    282  -1070   -512       C  
ATOM   1452  C   ARG A 206     -22.253  -9.757   1.477  1.00 83.09           C  
ANISOU 1452  C   ARG A 206    10411  10970  10190    277  -1107   -497       C  
ATOM   1453  O   ARG A 206     -23.366 -10.294   1.426  1.00 82.20           O  
ANISOU 1453  O   ARG A 206    10225  10864  10144    263  -1202   -548       O  
ATOM   1454  CB  ARG A 206     -21.644  -9.710  -0.947  1.00102.50           C  
ANISOU 1454  CB  ARG A 206    13082  13501  12364    325  -1181   -507       C  
ATOM   1455  CG  ARG A 206     -20.623  -9.986  -2.034  1.00111.55           C  
ANISOU 1455  CG  ARG A 206    14365  14679  13339    340  -1133   -520       C  
ATOM   1456  CD  ARG A 206     -19.594  -8.867  -2.133  1.00115.43           C  
ANISOU 1456  CD  ARG A 206    14923  15170  13764    363  -1024   -411       C  
ATOM   1457  NE  ARG A 206     -18.530  -9.179  -3.085  1.00117.56           N  
ANISOU 1457  NE  ARG A 206    15311  15476  13883    376   -945   -417       N  
ATOM   1458  CZ  ARG A 206     -17.693  -8.282  -3.599  1.00118.49           C  
ANISOU 1458  CZ  ARG A 206    15509  15608  13903    396   -859   -322       C  
ATOM   1459  NH1 ARG A 206     -17.793  -7.003  -3.262  1.00115.65           N  
ANISOU 1459  NH1 ARG A 206    15136  15220  13587    404   -853   -217       N  
ATOM   1460  NH2 ARG A 206     -16.756  -8.665  -4.456  1.00121.06           N  
ANISOU 1460  NH2 ARG A 206    15933  15972  14094    410   -772   -332       N  
ATOM   1461  N   HIS A 207     -21.904  -8.875   2.409  1.00 69.24           N  
ANISOU 1461  N   HIS A 207     8631   9188   8491    286  -1027   -432       N  
ATOM   1462  CA  HIS A 207     -22.771  -7.965   3.128  1.00 57.34           C  
ANISOU 1462  CA  HIS A 207     7047   7662   7076    315  -1049   -390       C  
ATOM   1463  C   HIS A 207     -22.087  -6.614   2.986  1.00 40.28           C  
ANISOU 1463  C   HIS A 207     4965   5482   4857    350  -1005   -307       C  
ATOM   1464  O   HIS A 207     -20.852  -6.552   3.018  1.00 46.94           O  
ANISOU 1464  O   HIS A 207     5870   6315   5649    326   -917   -287       O  
ATOM   1465  CB  HIS A 207     -22.937  -8.344   4.609  1.00 58.69           C  
ANISOU 1465  CB  HIS A 207     7122   7802   7376    284   -976   -406       C  
ATOM   1466  CG  HIS A 207     -23.798  -7.396   5.386  1.00 49.90           C  
ANISOU 1466  CG  HIS A 207     5937   6671   6351    324   -978   -371       C  
ATOM   1467  ND1 HIS A 207     -23.307  -6.238   5.949  1.00 46.05           N  
ANISOU 1467  ND1 HIS A 207     5487   6150   5861    353   -917   -319       N  
ATOM   1468  CD2 HIS A 207     -25.116  -7.437   5.697  1.00 51.69           C  
ANISOU 1468  CD2 HIS A 207     6054   6908   6680    343  -1029   -384       C  
ATOM   1469  CE1 HIS A 207     -24.287  -5.605   6.572  1.00 53.63           C  
ANISOU 1469  CE1 HIS A 207     6375   7094   6907    396   -928   -307       C  
ATOM   1470  NE2 HIS A 207     -25.394  -6.312   6.435  1.00 48.87           N  
ANISOU 1470  NE2 HIS A 207     5675   6523   6371    394   -990   -341       N  
ATOM   1471  N   PRO A 208     -22.838  -5.530   2.793  1.00 37.85           N  
ANISOU 1471  N   PRO A 208     4653   5165   4564    407  -1065   -255       N  
ATOM   1472  CA  PRO A 208     -22.194  -4.248   2.446  1.00 44.14           C  
ANISOU 1472  CA  PRO A 208     5544   5928   5299    437  -1032   -169       C  
ATOM   1473  C   PRO A 208     -21.161  -3.753   3.446  1.00 53.68           C  
ANISOU 1473  C   PRO A 208     6764   7084   6550    401   -913   -148       C  
ATOM   1474  O   PRO A 208     -20.320  -2.929   3.071  1.00 58.09           O  
ANISOU 1474  O   PRO A 208     7405   7613   7053    398   -868    -84       O  
ATOM   1475  CB  PRO A 208     -23.377  -3.273   2.347  1.00 46.85           C  
ANISOU 1475  CB  PRO A 208     5856   6254   5691    513  -1119   -126       C  
ATOM   1476  CG  PRO A 208     -24.524  -3.974   2.997  1.00 46.68           C  
ANISOU 1476  CG  PRO A 208     5697   6255   5784    513  -1166   -191       C  
ATOM   1477  CD  PRO A 208     -24.303  -5.428   2.760  1.00 44.84           C  
ANISOU 1477  CD  PRO A 208     5448   6066   5524    449  -1171   -266       C  
ATOM   1478  N   PHE A 209     -21.178  -4.220   4.696  1.00 47.87           N  
ANISOU 1478  N   PHE A 209     5949   6334   5905    371   -862   -195       N  
ATOM   1479  CA  PHE A 209     -20.268  -3.702   5.712  1.00 43.31           C  
ANISOU 1479  CA  PHE A 209     5381   5710   5364    341   -771   -182       C  
ATOM   1480  C   PHE A 209     -19.271  -4.751   6.197  1.00 48.42           C  
ANISOU 1480  C   PHE A 209     6012   6380   6004    282   -704   -222       C  
ATOM   1481  O   PHE A 209     -18.621  -4.555   7.230  1.00 40.64           O  
ANISOU 1481  O   PHE A 209     5014   5370   5059    255   -644   -227       O  
ATOM   1482  CB  PHE A 209     -21.065  -3.122   6.882  1.00 41.64           C  
ANISOU 1482  CB  PHE A 209     5112   5460   5252    372   -764   -194       C  
ATOM   1483  CG  PHE A 209     -22.112  -2.125   6.461  1.00 45.98           C  
ANISOU 1483  CG  PHE A 209     5662   5981   5825    447   -829   -156       C  
ATOM   1484  CD1 PHE A 209     -21.802  -1.113   5.568  1.00 48.48           C  
ANISOU 1484  CD1 PHE A 209     6071   6263   6087    473   -853    -86       C  
ATOM   1485  CD2 PHE A 209     -23.414  -2.220   6.933  1.00 39.46           C  
ANISOU 1485  CD2 PHE A 209     4743   5166   5084    495   -864   -182       C  
ATOM   1486  CE1 PHE A 209     -22.765  -0.202   5.167  1.00 54.58           C  
ANISOU 1486  CE1 PHE A 209     6849   7005   6884    555   -920    -42       C  
ATOM   1487  CE2 PHE A 209     -24.382  -1.314   6.532  1.00 52.65           C  
ANISOU 1487  CE2 PHE A 209     6403   6815   6787    577   -929   -145       C  
ATOM   1488  CZ  PHE A 209     -24.055  -0.304   5.649  1.00 57.21           C  
ANISOU 1488  CZ  PHE A 209     7080   7352   7306    611   -963    -74       C  
ATOM   1489  N   LEU A 210     -19.138  -5.858   5.471  1.00 47.06           N  
ANISOU 1489  N   LEU A 210     5844   6253   5782    267   -719   -254       N  
ATOM   1490  CA  LEU A 210     -18.090  -6.840   5.700  1.00 43.15           C  
ANISOU 1490  CA  LEU A 210     5347   5775   5274    226   -655   -284       C  
ATOM   1491  C   LEU A 210     -17.094  -6.772   4.552  1.00 49.13           C  
ANISOU 1491  C   LEU A 210     6181   6556   5932    221   -624   -257       C  
ATOM   1492  O   LEU A 210     -17.488  -6.671   3.387  1.00 43.27           O  
ANISOU 1492  O   LEU A 210     5494   5836   5110    248   -673   -247       O  
ATOM   1493  CB  LEU A 210     -18.666  -8.254   5.807  1.00 34.69           C  
ANISOU 1493  CB  LEU A 210     4226   4721   4233    216   -680   -349       C  
ATOM   1494  CG  LEU A 210     -19.763  -8.464   6.853  1.00 47.86           C  
ANISOU 1494  CG  LEU A 210     5810   6374   6002    217   -698   -370       C  
ATOM   1495  CD1 LEU A 210     -20.187  -9.921   6.902  1.00 47.08           C  
ANISOU 1495  CD1 LEU A 210     5668   6279   5943    190   -711   -426       C  
ATOM   1496  CD2 LEU A 210     -19.296  -7.992   8.223  1.00 40.60           C  
ANISOU 1496  CD2 LEU A 210     4869   5429   5129    209   -630   -350       C  
ATOM   1497  N   THR A 211     -15.806  -6.810   4.878  1.00 40.14           N  
ANISOU 1497  N   THR A 211     5042   5416   4794    190   -543   -242       N  
ATOM   1498  CA  THR A 211     -14.793  -6.833   3.831  1.00 44.96           C  
ANISOU 1498  CA  THR A 211     5710   6055   5317    185   -488   -215       C  
ATOM   1499  C   THR A 211     -14.948  -8.102   3.004  1.00 53.09           C  
ANISOU 1499  C   THR A 211     6765   7123   6283    205   -503   -276       C  
ATOM   1500  O   THR A 211     -14.917  -9.212   3.542  1.00 51.67           O  
ANISOU 1500  O   THR A 211     6540   6942   6151    198   -496   -334       O  
ATOM   1501  CB  THR A 211     -13.391  -6.751   4.433  1.00 46.63           C  
ANISOU 1501  CB  THR A 211     5886   6263   5568    147   -400   -194       C  
ATOM   1502  OG1 THR A 211     -13.157  -7.884   5.276  1.00 56.27           O  
ANISOU 1502  OG1 THR A 211     7045   7493   6844    142   -387   -249       O  
ATOM   1503  CG2 THR A 211     -13.245  -5.481   5.246  1.00 44.19           C  
ANISOU 1503  CG2 THR A 211     5562   5906   5322    119   -398   -149       C  
ATOM   1504  N   ALA A 212     -15.141  -7.938   1.701  1.00 48.39           N  
ANISOU 1504  N   ALA A 212     6253   6558   5575    233   -527   -263       N  
ATOM   1505  CA  ALA A 212     -15.441  -9.065   0.833  1.00 53.06           C  
ANISOU 1505  CA  ALA A 212     6887   7182   6091    254   -561   -336       C  
ATOM   1506  C   ALA A 212     -14.171  -9.813   0.455  1.00 60.47           C  
ANISOU 1506  C   ALA A 212     7850   8145   6982    256   -455   -358       C  
ATOM   1507  O   ALA A 212     -13.105  -9.214   0.279  1.00 60.24           O  
ANISOU 1507  O   ALA A 212     7833   8128   6926    249   -361   -295       O  
ATOM   1508  CB  ALA A 212     -16.161  -8.592  -0.432  1.00 44.54           C  
ANISOU 1508  CB  ALA A 212     5899   6135   4889    292   -640   -318       C  
ATOM   1509  N   LEU A 213     -14.291 -11.133   0.345  1.00 53.39           N  
ANISOU 1509  N   LEU A 213     6953   7246   6086    265   -468   -448       N  
ATOM   1510  CA  LEU A 213     -13.222 -11.979  -0.168  1.00 53.05           C  
ANISOU 1510  CA  LEU A 213     6944   7222   5990    287   -373   -486       C  
ATOM   1511  C   LEU A 213     -13.368 -12.071  -1.683  1.00 53.96           C  
ANISOU 1511  C   LEU A 213     7184   7382   5936    326   -388   -514       C  
ATOM   1512  O   LEU A 213     -14.359 -12.617  -2.179  1.00 57.36           O  
ANISOU 1512  O   LEU A 213     7659   7810   6324    334   -494   -588       O  
ATOM   1513  CB  LEU A 213     -13.285 -13.364   0.471  1.00 45.51           C  
ANISOU 1513  CB  LEU A 213     5943   6226   5123    284   -378   -570       C  
ATOM   1514  CG  LEU A 213     -12.416 -14.445  -0.169  1.00 57.69           C  
ANISOU 1514  CG  LEU A 213     7534   7773   6612    324   -298   -635       C  
ATOM   1515  CD1 LEU A 213     -10.946 -14.103  -0.040  1.00 52.01           C  
ANISOU 1515  CD1 LEU A 213     6778   7084   5899    339   -163   -572       C  
ATOM   1516  CD2 LEU A 213     -12.702 -15.781   0.470  1.00 66.08           C  
ANISOU 1516  CD2 LEU A 213     8561   8771   7773    320   -323   -714       C  
ATOM   1517  N   LYS A 214     -12.388 -11.543  -2.418  1.00 48.76           N  
ANISOU 1517  N   LYS A 214     6581   6767   5180    346   -282   -456       N  
ATOM   1518  CA  LYS A 214     -12.527 -11.393  -3.864  1.00 56.79           C  
ANISOU 1518  CA  LYS A 214     7734   7836   6008    387   -289   -460       C  
ATOM   1519  C   LYS A 214     -11.899 -12.533  -4.661  1.00 59.64           C  
ANISOU 1519  C   LYS A 214     8168   8222   6271    433   -214   -552       C  
ATOM   1520  O   LYS A 214     -12.563 -13.120  -5.522  1.00 63.13           O  
ANISOU 1520  O   LYS A 214     8710   8679   6596    463   -295   -638       O  
ATOM   1521  CB  LYS A 214     -11.934 -10.056  -4.327  1.00 61.98           C  
ANISOU 1521  CB  LYS A 214     8431   8524   6596    386   -210   -329       C  
ATOM   1522  CG  LYS A 214     -12.317  -9.712  -5.760  1.00 83.98           C  
ANISOU 1522  CG  LYS A 214    11370  11363   9174    432   -242   -309       C  
ATOM   1523  CD  LYS A 214     -11.684  -8.417  -6.233  1.00 94.43           C  
ANISOU 1523  CD  LYS A 214    12741  12706  10432    427   -146   -163       C  
ATOM   1524  CE  LYS A 214     -12.115  -8.090  -7.655  1.00104.31           C  
ANISOU 1524  CE  LYS A 214    14161  14014  11458    482   -183   -132       C  
ATOM   1525  NZ  LYS A 214     -11.170  -7.143  -8.313  1.00112.57           N  
ANISOU 1525  NZ  LYS A 214    15274  15088  12411    484    -31      5       N  
ATOM   1526  N   TYR A 215     -10.628 -12.848  -4.418  1.00 61.15           N  
ANISOU 1526  N   TYR A 215     8311   8418   6504    444    -65   -539       N  
ATOM   1527  CA  TYR A 215      -9.962 -13.940  -5.112  1.00 51.99           C  
ANISOU 1527  CA  TYR A 215     7213   7276   5264    501     24   -628       C  
ATOM   1528  C   TYR A 215      -9.487 -14.985  -4.112  1.00 44.59           C  
ANISOU 1528  C   TYR A 215     6171   6282   4488    502     59   -687       C  
ATOM   1529  O   TYR A 215      -9.241 -14.695  -2.938  1.00 46.95           O  
ANISOU 1529  O   TYR A 215     6345   6553   4941    462     62   -629       O  
ATOM   1530  CB  TYR A 215      -8.752 -13.465  -5.934  1.00 53.52           C  
ANISOU 1530  CB  TYR A 215     7450   7537   5348    537    198   -559       C  
ATOM   1531  CG  TYR A 215      -8.977 -12.243  -6.799  1.00 53.10           C  
ANISOU 1531  CG  TYR A 215     7492   7536   5149    532    198   -457       C  
ATOM   1532  CD1 TYR A 215      -9.646 -12.333  -8.014  1.00 59.04           C  
ANISOU 1532  CD1 TYR A 215     8408   8329   5695    577    135   -500       C  
ATOM   1533  CD2 TYR A 215      -8.472 -11.005  -6.422  1.00 54.63           C  
ANISOU 1533  CD2 TYR A 215     7619   7733   5407    484    262   -315       C  
ATOM   1534  CE1 TYR A 215      -9.830 -11.214  -8.814  1.00 61.45           C  
ANISOU 1534  CE1 TYR A 215     8810   8680   5857    582    135   -391       C  
ATOM   1535  CE2 TYR A 215      -8.650  -9.886  -7.212  1.00 57.16           C  
ANISOU 1535  CE2 TYR A 215     8033   8084   5600    482    270   -209       C  
ATOM   1536  CZ  TYR A 215      -9.329  -9.994  -8.405  1.00 62.43           C  
ANISOU 1536  CZ  TYR A 215     8866   8795   6058    536    208   -240       C  
ATOM   1537  OH  TYR A 215      -9.503  -8.877  -9.191  1.00 84.41           O  
ANISOU 1537  OH  TYR A 215    11754  11610   8709    542    214   -120       O  
ATOM   1538  N   SER A 216      -9.341 -16.211  -4.603  1.00 52.14           N  
ANISOU 1538  N   SER A 216     7191   7219   5400    554     84   -803       N  
ATOM   1539  CA  SER A 216      -8.703 -17.273  -3.836  1.00 55.15           C  
ANISOU 1539  CA  SER A 216     7492   7544   5917    578    143   -852       C  
ATOM   1540  C   SER A 216      -7.950 -18.165  -4.808  1.00 60.85           C  
ANISOU 1540  C   SER A 216     8305   8279   6536    663    258   -940       C  
ATOM   1541  O   SER A 216      -8.541 -18.691  -5.756  1.00 56.17           O  
ANISOU 1541  O   SER A 216     7850   7681   5810    691    206  -1045       O  
ATOM   1542  CB  SER A 216      -9.722 -18.084  -3.036  1.00 60.09           C  
ANISOU 1542  CB  SER A 216     8089   8081   6662    541      9   -922       C  
ATOM   1543  OG  SER A 216      -9.064 -19.016  -2.194  1.00 66.97           O  
ANISOU 1543  OG  SER A 216     8883   8892   7670    566     68   -943       O  
ATOM   1544  N   PHE A 217      -6.651 -18.322  -4.577  1.00 64.56           N  
ANISOU 1544  N   PHE A 217     8697   8769   7066    709    411   -902       N  
ATOM   1545  CA  PHE A 217      -5.822 -19.208  -5.374  1.00 64.07           C  
ANISOU 1545  CA  PHE A 217     8699   8714   6929    805    545   -983       C  
ATOM   1546  C   PHE A 217      -4.861 -19.928  -4.443  1.00 63.48           C  
ANISOU 1546  C   PHE A 217     8489   8596   7033    847    626   -976       C  
ATOM   1547  O   PHE A 217      -4.885 -19.744  -3.222  1.00 69.16           O  
ANISOU 1547  O   PHE A 217     9081   9284   7912    797    567   -910       O  
ATOM   1548  CB  PHE A 217      -5.073 -18.439  -6.470  1.00 57.16           C  
ANISOU 1548  CB  PHE A 217     7881   7945   5891    841    690   -924       C  
ATOM   1549  CG  PHE A 217      -4.056 -17.463  -5.946  1.00 63.15           C  
ANISOU 1549  CG  PHE A 217     8489   8760   6745    810    801   -776       C  
ATOM   1550  CD1 PHE A 217      -4.436 -16.193  -5.539  1.00 53.35           C  
ANISOU 1550  CD1 PHE A 217     7200   7539   5531    720    732   -660       C  
ATOM   1551  CD2 PHE A 217      -2.719 -17.814  -5.868  1.00 64.68           C  
ANISOU 1551  CD2 PHE A 217     8583   8981   7009    872    971   -757       C  
ATOM   1552  CE1 PHE A 217      -3.498 -15.292  -5.060  1.00 54.27           C  
ANISOU 1552  CE1 PHE A 217     7181   7696   5745    679    825   -533       C  
ATOM   1553  CE2 PHE A 217      -1.778 -16.921  -5.389  1.00 60.57           C  
ANISOU 1553  CE2 PHE A 217     7909   8513   6590    831   1062   -625       C  
ATOM   1554  CZ  PHE A 217      -2.168 -15.658  -4.986  1.00 52.77           C  
ANISOU 1554  CZ  PHE A 217     6884   7538   5629    728    985   -517       C  
ATOM   1555  N   GLN A 218      -4.003 -20.754  -5.031  1.00 63.24           N  
ANISOU 1555  N   GLN A 218     8493   8567   6969    948    762  -1044       N  
ATOM   1556  CA  GLN A 218      -3.049 -21.535  -4.266  1.00 69.92           C  
ANISOU 1556  CA  GLN A 218     9217   9370   7978   1011    841  -1042       C  
ATOM   1557  C   GLN A 218      -1.764 -21.695  -5.060  1.00 67.74           C  
ANISOU 1557  C   GLN A 218     8931   9162   7646   1116   1049  -1046       C  
ATOM   1558  O   GLN A 218      -1.771 -21.716  -6.294  1.00 79.74           O  
ANISOU 1558  O   GLN A 218    10591  10725   8981   1163   1126  -1107       O  
ATOM   1559  CB  GLN A 218      -3.615 -22.915  -3.906  1.00 76.02           C  
ANISOU 1559  CB  GLN A 218    10046  10010   8826   1044    759  -1162       C  
ATOM   1560  CG  GLN A 218      -4.257 -23.633  -5.081  1.00 82.67           C  
ANISOU 1560  CG  GLN A 218    11086  10812   9510   1083    738  -1317       C  
ATOM   1561  CD  GLN A 218      -4.542 -25.093  -4.787  1.00 91.92           C  
ANISOU 1561  CD  GLN A 218    12310  11838  10779   1126    693  -1440       C  
ATOM   1562  OE1 GLN A 218      -4.070 -25.645  -3.791  1.00 98.24           O  
ANISOU 1562  OE1 GLN A 218    13000  12572  11754   1155    710  -1402       O  
ATOM   1563  NE2 GLN A 218      -5.314 -25.730  -5.659  1.00 92.56           N  
ANISOU 1563  NE2 GLN A 218    12562  11862  10743   1132    629  -1587       N  
ATOM   1564  N   THR A 219      -0.659 -21.788  -4.334  1.00 68.45           N  
ANISOU 1564  N   THR A 219     8850   9267   7891   1155   1138   -977       N  
ATOM   1565  CA  THR A 219       0.614 -22.204  -4.886  1.00 72.48           C  
ANISOU 1565  CA  THR A 219     9313   9824   8401   1273   1339   -990       C  
ATOM   1566  C   THR A 219       0.855 -23.657  -4.473  1.00 73.91           C  
ANISOU 1566  C   THR A 219     9489   9896   8697   1379   1343  -1086       C  
ATOM   1567  O   THR A 219      -0.075 -24.357  -4.056  1.00 69.78           O  
ANISOU 1567  O   THR A 219     9045   9259   8208   1357   1201  -1159       O  
ATOM   1568  CB  THR A 219       1.721 -21.247  -4.421  1.00 77.60           C  
ANISOU 1568  CB  THR A 219     9757  10571   9157   1242   1434   -841       C  
ATOM   1569  OG1 THR A 219       2.072 -21.542  -3.064  1.00 82.60           O  
ANISOU 1569  OG1 THR A 219    10224  11161  10001   1236   1359   -793       O  
ATOM   1570  CG2 THR A 219       1.245 -19.810  -4.508  1.00 76.02           C  
ANISOU 1570  CG2 THR A 219     9565  10435   8886   1111   1378   -739       C  
ATOM   1571  N   HIS A 220       2.102 -24.116  -4.569  1.00 83.21           N  
ANISOU 1571  N   HIS A 220    10567  11102   9948   1497   1508  -1080       N  
ATOM   1572  CA  HIS A 220       2.391 -25.506  -4.233  1.00 93.86           C  
ANISOU 1572  CA  HIS A 220    11917  12337  11408   1617   1523  -1168       C  
ATOM   1573  C   HIS A 220       2.256 -25.768  -2.740  1.00 82.48           C  
ANISOU 1573  C   HIS A 220    10351  10822  10168   1579   1382  -1100       C  
ATOM   1574  O   HIS A 220       1.840 -26.862  -2.339  1.00 83.96           O  
ANISOU 1574  O   HIS A 220    10602  10873  10425   1624   1311  -1174       O  
ATOM   1575  CB  HIS A 220       3.792 -25.888  -4.711  1.00108.52           C  
ANISOU 1575  CB  HIS A 220    13683  14250  13301   1767   1744  -1172       C  
ATOM   1576  CG  HIS A 220       3.914 -26.005  -6.195  1.00116.55           C  
ANISOU 1576  CG  HIS A 220    14860  15312  14111   1842   1901  -1271       C  
ATOM   1577  ND1 HIS A 220       4.190 -24.926  -7.006  1.00117.85           N  
ANISOU 1577  ND1 HIS A 220    15029  15616  14132   1798   2012  -1203       N  
ATOM   1578  CD2 HIS A 220       3.804 -27.076  -7.015  1.00118.51           C  
ANISOU 1578  CD2 HIS A 220    15282  15483  14264   1961   1968  -1433       C  
ATOM   1579  CE1 HIS A 220       4.246 -25.329  -8.263  1.00119.41           C  
ANISOU 1579  CE1 HIS A 220    15398  15831  14140   1891   2145  -1315       C  
ATOM   1580  NE2 HIS A 220       4.015 -26.629  -8.295  1.00120.55           N  
ANISOU 1580  NE2 HIS A 220    15650  15846  14309   1991   2118  -1464       N  
ATOM   1581  N   ASP A 221       2.604 -24.790  -1.904  1.00 73.43           N  
ANISOU 1581  N   ASP A 221     9033   9755   9111   1497   1340   -962       N  
ATOM   1582  CA  ASP A 221       2.606 -24.979  -0.459  1.00 73.59           C  
ANISOU 1582  CA  ASP A 221     8931   9724   9304   1471   1215   -889       C  
ATOM   1583  C   ASP A 221       1.853 -23.884   0.290  1.00 63.09           C  
ANISOU 1583  C   ASP A 221     7570   8427   7973   1313   1067   -803       C  
ATOM   1584  O   ASP A 221       1.913 -23.846   1.524  1.00 58.04           O  
ANISOU 1584  O   ASP A 221     6825   7770   7460   1283    968   -731       O  
ATOM   1585  CB  ASP A 221       4.046 -25.065   0.067  1.00 81.83           C  
ANISOU 1585  CB  ASP A 221     9762  10827  10502   1560   1307   -809       C  
ATOM   1586  CG  ASP A 221       4.836 -23.796  -0.190  1.00 90.04           C  
ANISOU 1586  CG  ASP A 221    10660  12017  11532   1501   1395   -712       C  
ATOM   1587  OD1 ASP A 221       4.470 -23.037  -1.115  1.00 95.01           O  
ANISOU 1587  OD1 ASP A 221    11384  12703  12011   1435   1445   -721       O  
ATOM   1588  OD2 ASP A 221       5.831 -23.559   0.527  1.00 93.54           O  
ANISOU 1588  OD2 ASP A 221    10898  12521  12122   1518   1409   -622       O  
ATOM   1589  N   ARG A 222       1.146 -22.997  -0.409  1.00 55.02           N  
ANISOU 1589  N   ARG A 222     6645   7453   6808   1220   1048   -808       N  
ATOM   1590  CA  ARG A 222       0.467 -21.878   0.225  1.00 58.72           C  
ANISOU 1590  CA  ARG A 222     7085   7952   7275   1082    924   -729       C  
ATOM   1591  C   ARG A 222      -0.962 -21.763  -0.285  1.00 60.17           C  
ANISOU 1591  C   ARG A 222     7443   8090   7329   1013    824   -794       C  
ATOM   1592  O   ARG A 222      -1.250 -22.034  -1.454  1.00 61.37           O  
ANISOU 1592  O   ARG A 222     7733   8241   7343   1048    876   -880       O  
ATOM   1593  CB  ARG A 222       1.203 -20.554  -0.023  1.00 55.75           C  
ANISOU 1593  CB  ARG A 222     6604   7697   6882   1025   1001   -629       C  
ATOM   1594  CG  ARG A 222       2.568 -20.456   0.641  1.00 59.78           C  
ANISOU 1594  CG  ARG A 222     6904   8263   7545   1061   1068   -549       C  
ATOM   1595  CD  ARG A 222       2.460 -20.562   2.154  1.00 60.42           C  
ANISOU 1595  CD  ARG A 222     6887   8304   7765   1028    921   -501       C  
ATOM   1596  NE  ARG A 222       3.743 -20.333   2.813  1.00 71.84           N  
ANISOU 1596  NE  ARG A 222     8124   9818   9354   1050    956   -422       N  
ATOM   1597  CZ  ARG A 222       4.605 -21.295   3.131  1.00 79.88           C  
ANISOU 1597  CZ  ARG A 222     9044  10824  10482   1171   1000   -428       C  
ATOM   1598  NH1 ARG A 222       4.324 -22.560   2.848  1.00 80.91           N  
ANISOU 1598  NH1 ARG A 222     9281  10864  10596   1281   1025   -512       N  
ATOM   1599  NH2 ARG A 222       5.747 -20.990   3.733  1.00 84.90           N  
ANISOU 1599  NH2 ARG A 222     9474  11533  11251   1183   1014   -351       N  
ATOM   1600  N   LEU A 223      -1.852 -21.353   0.613  1.00 59.68           N  
ANISOU 1600  N   LEU A 223     7370   7996   7310    919    679   -756       N  
ATOM   1601  CA  LEU A 223      -3.232 -21.027   0.280  1.00 57.98           C  
ANISOU 1601  CA  LEU A 223     7280   7753   6997    841    569   -795       C  
ATOM   1602  C   LEU A 223      -3.446 -19.536   0.502  1.00 54.72           C  
ANISOU 1602  C   LEU A 223     6819   7413   6559    742    527   -698       C  
ATOM   1603  O   LEU A 223      -3.112 -19.013   1.570  1.00 56.24           O  
ANISOU 1603  O   LEU A 223     6890   7621   6856    701    492   -616       O  
ATOM   1604  CB  LEU A 223      -4.210 -21.842   1.128  1.00 63.24           C  
ANISOU 1604  CB  LEU A 223     7975   8309   7744    816    444   -835       C  
ATOM   1605  CG  LEU A 223      -5.683 -21.746   0.736  1.00 73.91           C  
ANISOU 1605  CG  LEU A 223     9443   9623   9016    745    330   -894       C  
ATOM   1606  CD1 LEU A 223      -5.876 -22.298  -0.660  1.00 80.33           C  
ANISOU 1606  CD1 LEU A 223    10400  10425   9696    793    367  -1011       C  
ATOM   1607  CD2 LEU A 223      -6.561 -22.485   1.726  1.00 75.04           C  
ANISOU 1607  CD2 LEU A 223     9582   9662   9268    709    224   -910       C  
ATOM   1608  N   CYS A 224      -4.001 -18.859  -0.501  1.00 53.67           N  
ANISOU 1608  N   CYS A 224     6789   7320   6284    710    524   -708       N  
ATOM   1609  CA  CYS A 224      -4.075 -17.404  -0.520  1.00 43.24           C  
ANISOU 1609  CA  CYS A 224     5439   6062   4928    631    511   -612       C  
ATOM   1610  C   CYS A 224      -5.525 -16.946  -0.585  1.00 47.54           C  
ANISOU 1610  C   CYS A 224     6074   6579   5411    567    372   -628       C  
ATOM   1611  O   CYS A 224      -6.291 -17.410  -1.435  1.00 58.51           O  
ANISOU 1611  O   CYS A 224     7589   7951   6692    587    333   -709       O  
ATOM   1612  CB  CYS A 224      -3.293 -16.832  -1.704  1.00 50.14           C  
ANISOU 1612  CB  CYS A 224     6345   7018   5687    657    653   -579       C  
ATOM   1613  SG  CYS A 224      -1.550 -17.318  -1.749  1.00 65.88           S  
ANISOU 1613  SG  CYS A 224     8211   9060   7762    740    839   -557       S  
ATOM   1614  N   PHE A 225      -5.890 -16.033   0.313  1.00 40.31           N  
ANISOU 1614  N   PHE A 225     5090   5661   4564    493    295   -554       N  
ATOM   1615  CA  PHE A 225      -7.199 -15.393   0.327  1.00 48.42           C  
ANISOU 1615  CA  PHE A 225     6177   6671   5551    437    174   -549       C  
ATOM   1616  C   PHE A 225      -6.987 -13.898   0.146  1.00 53.27           C  
ANISOU 1616  C   PHE A 225     6777   7331   6131    388    195   -450       C  
ATOM   1617  O   PHE A 225      -6.286 -13.268   0.945  1.00 54.06           O  
ANISOU 1617  O   PHE A 225     6773   7440   6325    352    223   -380       O  
ATOM   1618  CB  PHE A 225      -7.947 -15.685   1.631  1.00 46.45           C  
ANISOU 1618  CB  PHE A 225     5868   6360   5419    401     68   -557       C  
ATOM   1619  CG  PHE A 225      -8.256 -17.142   1.843  1.00 51.30           C  
ANISOU 1619  CG  PHE A 225     6503   6909   6080    438     44   -643       C  
ATOM   1620  CD1 PHE A 225      -9.155 -17.801   1.021  1.00 54.87           C  
ANISOU 1620  CD1 PHE A 225     7060   7329   6461    448     -9   -734       C  
ATOM   1621  CD2 PHE A 225      -7.655 -17.852   2.871  1.00 50.25           C  
ANISOU 1621  CD2 PHE A 225     6288   6740   6063    461     67   -632       C  
ATOM   1622  CE1 PHE A 225      -9.442 -19.140   1.212  1.00 55.98           C  
ANISOU 1622  CE1 PHE A 225     7223   7390   6657    471    -31   -816       C  
ATOM   1623  CE2 PHE A 225      -7.940 -19.190   3.067  1.00 49.30           C  
ANISOU 1623  CE2 PHE A 225     6196   6542   5993    495     50   -701       C  
ATOM   1624  CZ  PHE A 225      -8.836 -19.833   2.237  1.00 51.62           C  
ANISOU 1624  CZ  PHE A 225     6595   6792   6227    495      5   -795       C  
ATOM   1625  N   VAL A 226      -7.584 -13.334  -0.899  1.00 54.25           N  
ANISOU 1625  N   VAL A 226     7010   7481   6123    386    176   -443       N  
ATOM   1626  CA  VAL A 226      -7.419 -11.924  -1.233  1.00 50.62           C  
ANISOU 1626  CA  VAL A 226     6562   7052   5620    346    203   -340       C  
ATOM   1627  C   VAL A 226      -8.705 -11.193  -0.879  1.00 48.26           C  
ANISOU 1627  C   VAL A 226     6289   6718   5330    307     65   -322       C  
ATOM   1628  O   VAL A 226      -9.773 -11.500  -1.422  1.00 49.18           O  
ANISOU 1628  O   VAL A 226     6489   6828   5368    327    -26   -376       O  
ATOM   1629  CB  VAL A 226      -7.067 -11.729  -2.714  1.00 47.09           C  
ANISOU 1629  CB  VAL A 226     6227   6663   5005    385    296   -322       C  
ATOM   1630  CG1 VAL A 226      -6.669 -10.291  -2.970  1.00 46.25           C  
ANISOU 1630  CG1 VAL A 226     6119   6577   4878    339    352   -195       C  
ATOM   1631  CG2 VAL A 226      -5.945 -12.662  -3.107  1.00 45.91           C  
ANISOU 1631  CG2 VAL A 226     6057   6546   4842    444    435   -365       C  
ATOM   1632  N   MET A 227      -8.602 -10.216   0.016  1.00 47.12           N  
ANISOU 1632  N   MET A 227     6072   6550   5283    253     47   -251       N  
ATOM   1633  CA  MET A 227      -9.758  -9.490   0.521  1.00 50.18           C  
ANISOU 1633  CA  MET A 227     6468   6898   5701    225    -70   -234       C  
ATOM   1634  C   MET A 227      -9.666  -8.015   0.171  1.00 50.28           C  
ANISOU 1634  C   MET A 227     6514   6905   5684    195    -53   -133       C  
ATOM   1635  O   MET A 227      -8.578  -7.433   0.161  1.00 54.60           O  
ANISOU 1635  O   MET A 227     7025   7461   6258    163     44    -67       O  
ATOM   1636  CB  MET A 227      -9.879  -9.641   2.025  1.00 54.12           C  
ANISOU 1636  CB  MET A 227     6865   7357   6342    196   -117   -251       C  
ATOM   1637  CG  MET A 227     -10.023 -11.071   2.452  1.00 83.05           C  
ANISOU 1637  CG  MET A 227    10500  11009  10045    223   -134   -334       C  
ATOM   1638  SD  MET A 227     -10.352 -11.176   4.207  1.00108.58           S  
ANISOU 1638  SD  MET A 227    13639  14199  13416    194   -192   -339       S  
ATOM   1639  CE  MET A 227     -10.344 -12.940   4.416  1.00118.56           C  
ANISOU 1639  CE  MET A 227    14891  15444  14713    233   -187   -417       C  
ATOM   1640  N   GLU A 228     -10.823  -7.415  -0.099  1.00 47.34           N  
ANISOU 1640  N   GLU A 228     6205   6512   5269    204   -150   -118       N  
ATOM   1641  CA  GLU A 228     -10.879  -5.990  -0.382  1.00 49.22           C  
ANISOU 1641  CA  GLU A 228     6487   6724   5489    184   -146    -18       C  
ATOM   1642  C   GLU A 228     -10.403  -5.205   0.831  1.00 42.89           C  
ANISOU 1642  C   GLU A 228     5596   5868   4830    124   -131     19       C  
ATOM   1643  O   GLU A 228     -10.776  -5.504   1.968  1.00 53.54           O  
ANISOU 1643  O   GLU A 228     6876   7192   6275    114   -188    -34       O  
ATOM   1644  CB  GLU A 228     -12.302  -5.579  -0.766  1.00 60.19           C  
ANISOU 1644  CB  GLU A 228     7946   8098   6827    220   -270    -15       C  
ATOM   1645  CG  GLU A 228     -12.742  -6.079  -2.133  1.00 65.08           C  
ANISOU 1645  CG  GLU A 228     8674   8773   7280    275   -301    -37       C  
ATOM   1646  CD  GLU A 228     -14.163  -5.669  -2.472  1.00 83.53           C  
ANISOU 1646  CD  GLU A 228    11059  11100   9577    313   -445    -33       C  
ATOM   1647  OE1 GLU A 228     -14.874  -5.182  -1.566  1.00 88.19           O  
ANISOU 1647  OE1 GLU A 228    11583  11640  10283    303   -513    -29       O  
ATOM   1648  OE2 GLU A 228     -14.569  -5.831  -3.642  1.00 90.02           O  
ANISOU 1648  OE2 GLU A 228    11983  11969  10250    359   -491    -36       O  
ATOM   1649  N   TYR A 229      -9.559  -4.213   0.584  1.00 48.20           N  
ANISOU 1649  N   TYR A 229     6277   6524   5513     81    -51    108       N  
ATOM   1650  CA  TYR A 229      -8.980  -3.381   1.629  1.00 52.87           C  
ANISOU 1650  CA  TYR A 229     6793   7059   6237     13    -38    139       C  
ATOM   1651  C   TYR A 229      -9.555  -1.978   1.500  1.00 54.26           C  
ANISOU 1651  C   TYR A 229     7038   7158   6419     -1    -77    214       C  
ATOM   1652  O   TYR A 229      -9.398  -1.333   0.457  1.00 57.81           O  
ANISOU 1652  O   TYR A 229     7570   7602   6791      1    -26    301       O  
ATOM   1653  CB  TYR A 229      -7.456  -3.358   1.518  1.00 51.45           C  
ANISOU 1653  CB  TYR A 229     6545   6906   6096    -39     86    180       C  
ATOM   1654  CG  TYR A 229      -6.751  -2.839   2.749  1.00 57.63           C  
ANISOU 1654  CG  TYR A 229     7224   7647   7027   -114     79    179       C  
ATOM   1655  CD1 TYR A 229      -6.363  -3.704   3.763  1.00 58.96           C  
ANISOU 1655  CD1 TYR A 229     7290   7844   7268   -114     54    106       C  
ATOM   1656  CD2 TYR A 229      -6.468  -1.487   2.894  1.00 57.73           C  
ANISOU 1656  CD2 TYR A 229     7247   7586   7104   -184     90    250       C  
ATOM   1657  CE1 TYR A 229      -5.714  -3.236   4.891  1.00 56.60           C  
ANISOU 1657  CE1 TYR A 229     6901   7514   7088   -179     30    100       C  
ATOM   1658  CE2 TYR A 229      -5.822  -1.011   4.018  1.00 59.11           C  
ANISOU 1658  CE2 TYR A 229     7330   7719   7409   -259     69    234       C  
ATOM   1659  CZ  TYR A 229      -5.445  -1.889   5.011  1.00 61.79           C  
ANISOU 1659  CZ  TYR A 229     7569   8102   7806   -255     34    157       C  
ATOM   1660  OH  TYR A 229      -4.800  -1.412   6.127  1.00 67.90           O  
ANISOU 1660  OH  TYR A 229     8261   8844   8696   -326     -3    136       O  
ATOM   1661  N   ALA A 230     -10.221  -1.510   2.550  1.00 44.23           N  
ANISOU 1661  N   ALA A 230     5743   5826   5237     -9   -159    182       N  
ATOM   1662  CA  ALA A 230     -10.829  -0.187   2.517  1.00 51.87           C  
ANISOU 1662  CA  ALA A 230     6777   6706   6226     -9   -200    243       C  
ATOM   1663  C   ALA A 230      -9.762   0.895   2.622  1.00 48.95           C  
ANISOU 1663  C   ALA A 230     6401   6269   5928    -94   -125    318       C  
ATOM   1664  O   ALA A 230      -8.827   0.796   3.422  1.00 54.40           O  
ANISOU 1664  O   ALA A 230     7002   6959   6709   -160    -93    288       O  
ATOM   1665  CB  ALA A 230     -11.844  -0.040   3.650  1.00 52.47           C  
ANISOU 1665  CB  ALA A 230     6825   6736   6377     17   -295    177       C  
ATOM   1666  N   ASN A 231      -9.910   1.942   1.809  1.00 41.08           N  
ANISOU 1666  N   ASN A 231     5500   5212   4897    -93   -105    421       N  
ATOM   1667  CA  ASN A 231      -8.922   3.010   1.728  1.00 44.29           C  
ANISOU 1667  CA  ASN A 231     5913   5542   5374   -183    -24    509       C  
ATOM   1668  C   ASN A 231      -9.416   4.315   2.347  1.00 48.57           C  
ANISOU 1668  C   ASN A 231     6501   5943   6012   -202    -81    530       C  
ATOM   1669  O   ASN A 231      -8.866   5.380   2.057  1.00 52.68           O  
ANISOU 1669  O   ASN A 231     7063   6370   6582   -266    -25    622       O  
ATOM   1670  CB  ASN A 231      -8.515   3.239   0.274  1.00 53.92           C  
ANISOU 1670  CB  ASN A 231     7216   6789   6483   -178     74    629       C  
ATOM   1671  CG  ASN A 231      -9.616   3.880  -0.544  1.00 60.07           C  
ANISOU 1671  CG  ASN A 231     8133   7524   7166    -99     17    703       C  
ATOM   1672  OD1 ASN A 231     -10.787   3.520  -0.425  1.00 69.63           O  
ANISOU 1672  OD1 ASN A 231     9366   8755   8337    -15    -94    643       O  
ATOM   1673  ND2 ASN A 231      -9.245   4.847  -1.376  1.00 48.40           N  
ANISOU 1673  ND2 ASN A 231     6745   5986   5658   -126     91    840       N  
ATOM   1674  N   GLY A 232     -10.441   4.255   3.193  1.00 50.97           N  
ANISOU 1674  N   GLY A 232     6798   6222   6348   -146   -183    446       N  
ATOM   1675  CA  GLY A 232     -10.967   5.421   3.871  1.00 51.43           C  
ANISOU 1675  CA  GLY A 232     6901   6145   6497   -147   -235    445       C  
ATOM   1676  C   GLY A 232     -10.392   5.673   5.247  1.00 52.07           C  
ANISOU 1676  C   GLY A 232     6911   6173   6700   -223   -249    361       C  
ATOM   1677  O   GLY A 232     -10.915   6.527   5.972  1.00 48.03           O  
ANISOU 1677  O   GLY A 232     6438   5552   6259   -213   -299    329       O  
ATOM   1678  N   GLY A 233      -9.339   4.955   5.633  1.00 47.82           N  
ANISOU 1678  N   GLY A 233     6274   5710   6186   -293   -212    320       N  
ATOM   1679  CA  GLY A 233      -8.679   5.171   6.904  1.00 46.48           C  
ANISOU 1679  CA  GLY A 233     6036   5504   6122   -370   -238    242       C  
ATOM   1680  C   GLY A 233      -9.210   4.294   8.018  1.00 47.16           C  
ANISOU 1680  C   GLY A 233     6070   5654   6195   -318   -307    125       C  
ATOM   1681  O   GLY A 233     -10.415   4.039   8.090  1.00 45.01           O  
ANISOU 1681  O   GLY A 233     5835   5392   5873   -224   -350     96       O  
ATOM   1682  N   GLU A 234      -8.319   3.828   8.893  1.00 49.56           N  
ANISOU 1682  N   GLU A 234     6283   6004   6545   -378   -316     64       N  
ATOM   1683  CA  GLU A 234      -8.733   3.009  10.024  1.00 50.34           C  
ANISOU 1683  CA  GLU A 234     6340   6160   6625   -332   -375    -36       C  
ATOM   1684  C   GLU A 234      -9.542   3.844  11.007  1.00 52.02           C  
ANISOU 1684  C   GLU A 234     6618   6278   6868   -308   -436   -100       C  
ATOM   1685  O   GLU A 234      -9.316   5.047  11.155  1.00 60.78           O  
ANISOU 1685  O   GLU A 234     7779   7272   8045   -361   -445    -93       O  
ATOM   1686  CB  GLU A 234      -7.515   2.406  10.725  1.00 55.18           C  
ANISOU 1686  CB  GLU A 234     6848   6841   7279   -397   -380    -75       C  
ATOM   1687  CG  GLU A 234      -6.505   1.756   9.791  1.00 57.99           C  
ANISOU 1687  CG  GLU A 234     7128   7277   7629   -428   -305    -12       C  
ATOM   1688  CD  GLU A 234      -6.005   0.417  10.307  1.00 74.63           C  
ANISOU 1688  CD  GLU A 234     9139   9497   9722   -403   -314    -57       C  
ATOM   1689  OE1 GLU A 234      -6.798  -0.307  10.948  1.00 79.49           O  
ANISOU 1689  OE1 GLU A 234     9769  10145  10289   -332   -360   -114       O  
ATOM   1690  OE2 GLU A 234      -4.822   0.088  10.073  1.00 81.19           O  
ANISOU 1690  OE2 GLU A 234     9874  10380  10594   -450   -271    -31       O  
ATOM   1691  N   LEU A 235     -10.489   3.199  11.692  1.00 51.77           N  
ANISOU 1691  N   LEU A 235     6588   6292   6792   -227   -470   -163       N  
ATOM   1692  CA  LEU A 235     -11.380   3.959  12.560  1.00 48.39           C  
ANISOU 1692  CA  LEU A 235     6225   5781   6382   -183   -509   -224       C  
ATOM   1693  C   LEU A 235     -10.663   4.465  13.806  1.00 54.88           C  
ANISOU 1693  C   LEU A 235     7047   6557   7247   -249   -549   -303       C  
ATOM   1694  O   LEU A 235     -11.059   5.494  14.364  1.00 58.66           O  
ANISOU 1694  O   LEU A 235     7601   6928   7759   -242   -573   -349       O  
ATOM   1695  CB  LEU A 235     -12.601   3.124  12.942  1.00 51.62           C  
ANISOU 1695  CB  LEU A 235     6623   6255   6736    -81   -518   -262       C  
ATOM   1696  CG  LEU A 235     -13.815   3.963  13.354  1.00 61.94           C  
ANISOU 1696  CG  LEU A 235     7997   7478   8060     -4   -532   -294       C  
ATOM   1697  CD1 LEU A 235     -14.217   4.915  12.237  1.00 55.75           C  
ANISOU 1697  CD1 LEU A 235     7273   6605   7303     19   -526   -216       C  
ATOM   1698  CD2 LEU A 235     -14.989   3.083  13.752  1.00 74.46           C  
ANISOU 1698  CD2 LEU A 235     9547   9137   9606     86   -530   -327       C  
ATOM   1699  N   PHE A 236      -9.611   3.775  14.259  1.00 52.77           N  
ANISOU 1699  N   PHE A 236     6701   6370   6980   -309   -564   -326       N  
ATOM   1700  CA  PHE A 236      -8.846   4.319  15.376  1.00 51.99           C  
ANISOU 1700  CA  PHE A 236     6601   6231   6921   -382   -622   -402       C  
ATOM   1701  C   PHE A 236      -8.091   5.574  14.964  1.00 59.20           C  
ANISOU 1701  C   PHE A 236     7539   7025   7931   -486   -623   -375       C  
ATOM   1702  O   PHE A 236      -7.855   6.455  15.797  1.00 62.51           O  
ANISOU 1702  O   PHE A 236     8004   7353   8395   -537   -678   -449       O  
ATOM   1703  CB  PHE A 236      -7.890   3.265  15.958  1.00 52.71           C  
ANISOU 1703  CB  PHE A 236     6593   6441   6993   -413   -652   -425       C  
ATOM   1704  CG  PHE A 236      -6.651   3.008  15.129  1.00 53.38           C  
ANISOU 1704  CG  PHE A 236     6578   6569   7134   -492   -621   -355       C  
ATOM   1705  CD1 PHE A 236      -6.590   1.922  14.268  1.00 55.13           C  
ANISOU 1705  CD1 PHE A 236     6741   6886   7321   -450   -561   -292       C  
ATOM   1706  CD2 PHE A 236      -5.533   3.825  15.243  1.00 59.04           C  
ANISOU 1706  CD2 PHE A 236     7256   7231   7944   -610   -649   -360       C  
ATOM   1707  CE1 PHE A 236      -5.450   1.674  13.520  1.00 51.98           C  
ANISOU 1707  CE1 PHE A 236     6249   6531   6969   -511   -516   -231       C  
ATOM   1708  CE2 PHE A 236      -4.395   3.587  14.490  1.00 59.17           C  
ANISOU 1708  CE2 PHE A 236     7165   7295   8023   -681   -605   -290       C  
ATOM   1709  CZ  PHE A 236      -4.352   2.509  13.630  1.00 55.58           C  
ANISOU 1709  CZ  PHE A 236     6655   6940   7523   -625   -532   -226       C  
ATOM   1710  N   PHE A 237      -7.704   5.673  13.689  1.00 62.62           N  
ANISOU 1710  N   PHE A 237     7947   7452   8395   -521   -560   -270       N  
ATOM   1711  CA  PHE A 237      -7.081   6.896  13.198  1.00 54.99           C  
ANISOU 1711  CA  PHE A 237     7009   6358   7525   -621   -543   -222       C  
ATOM   1712  C   PHE A 237      -8.060   8.059  13.261  1.00 56.49           C  
ANISOU 1712  C   PHE A 237     7332   6394   7736   -578   -554   -236       C  
ATOM   1713  O   PHE A 237      -7.732   9.137  13.769  1.00 66.24           O  
ANISOU 1713  O   PHE A 237     8618   7497   9053   -651   -590   -280       O  
ATOM   1714  CB  PHE A 237      -6.577   6.691  11.767  1.00 47.04           C  
ANISOU 1714  CB  PHE A 237     5962   5388   6524   -650   -453    -94       C  
ATOM   1715  CG  PHE A 237      -6.082   7.950  11.105  1.00 50.01           C  
ANISOU 1715  CG  PHE A 237     6382   5626   6993   -745   -412    -16       C  
ATOM   1716  CD1 PHE A 237      -4.769   8.359  11.260  1.00 64.00           C  
ANISOU 1716  CD1 PHE A 237     8074   7369   8875   -888   -408     -9       C  
ATOM   1717  CD2 PHE A 237      -6.929   8.720  10.320  1.00 54.11           C  
ANISOU 1717  CD2 PHE A 237     7019   6042   7499   -692   -378     58       C  
ATOM   1718  CE1 PHE A 237      -4.309   9.516  10.651  1.00 69.80           C  
ANISOU 1718  CE1 PHE A 237     8847   7965   9709   -987   -360     72       C  
ATOM   1719  CE2 PHE A 237      -6.476   9.877   9.708  1.00 61.11           C  
ANISOU 1719  CE2 PHE A 237     7957   6788   8472   -779   -334    144       C  
ATOM   1720  CZ  PHE A 237      -5.164  10.274   9.875  1.00 68.05           C  
ANISOU 1720  CZ  PHE A 237     8759   7632   9467   -932   -319    152       C  
ATOM   1721  N   HIS A 238      -9.276   7.852  12.749  1.00 51.15           N  
ANISOU 1721  N   HIS A 238     6710   5731   6993   -457   -529   -201       N  
ATOM   1722  CA  HIS A 238     -10.264   8.925  12.729  1.00 46.89           C  
ANISOU 1722  CA  HIS A 238     6287   5049   6478   -394   -537   -203       C  
ATOM   1723  C   HIS A 238     -10.706   9.303  14.135  1.00 52.49           C  
ANISOU 1723  C   HIS A 238     7045   5703   7194   -363   -593   -338       C  
ATOM   1724  O   HIS A 238     -10.896  10.488  14.432  1.00 53.08           O  
ANISOU 1724  O   HIS A 238     7214   5619   7335   -372   -610   -372       O  
ATOM   1725  CB  HIS A 238     -11.466   8.513  11.882  1.00 48.44           C  
ANISOU 1725  CB  HIS A 238     6507   5294   6605   -267   -511   -138       C  
ATOM   1726  CG  HIS A 238     -11.167   8.432  10.420  1.00 46.99           C  
ANISOU 1726  CG  HIS A 238     6320   5133   6400   -284   -459     -4       C  
ATOM   1727  ND1 HIS A 238     -10.623   9.483   9.715  1.00 52.82           N  
ANISOU 1727  ND1 HIS A 238     7116   5749   7202   -354   -424     86       N  
ATOM   1728  CD2 HIS A 238     -11.330   7.425   9.530  1.00 43.16           C  
ANISOU 1728  CD2 HIS A 238     5791   4777   5830   -241   -431     54       C  
ATOM   1729  CE1 HIS A 238     -10.466   9.129   8.452  1.00 56.25           C  
ANISOU 1729  CE1 HIS A 238     7546   6246   7579   -347   -371    200       C  
ATOM   1730  NE2 HIS A 238     -10.888   7.885   8.314  1.00 53.78           N  
ANISOU 1730  NE2 HIS A 238     7174   6086   7173   -278   -378    175       N  
ATOM   1731  N   LEU A 239     -10.878   8.314  15.014  1.00 54.03           N  
ANISOU 1731  N   LEU A 239     7189   6023   7319   -322   -618   -416       N  
ATOM   1732  CA  LEU A 239     -11.320   8.615  16.370  1.00 56.53           C  
ANISOU 1732  CA  LEU A 239     7562   6301   7615   -283   -660   -544       C  
ATOM   1733  C   LEU A 239     -10.242   9.354  17.156  1.00 56.74           C  
ANISOU 1733  C   LEU A 239     7611   6245   7701   -403   -720   -624       C  
ATOM   1734  O   LEU A 239     -10.555  10.222  17.977  1.00 57.41           O  
ANISOU 1734  O   LEU A 239     7794   6219   7803   -388   -752   -722       O  
ATOM   1735  CB  LEU A 239     -11.720   7.331  17.093  1.00 50.67           C  
ANISOU 1735  CB  LEU A 239     6762   5715   6774   -214   -662   -589       C  
ATOM   1736  CG  LEU A 239     -12.358   7.551  18.465  1.00 50.57           C  
ANISOU 1736  CG  LEU A 239     6818   5682   6713   -149   -684   -711       C  
ATOM   1737  CD1 LEU A 239     -13.563   8.473  18.340  1.00 41.75           C  
ANISOU 1737  CD1 LEU A 239     5790   4447   5625    -49   -650   -722       C  
ATOM   1738  CD2 LEU A 239     -12.752   6.226  19.093  1.00 51.12           C  
ANISOU 1738  CD2 LEU A 239     6832   5907   6686    -85   -670   -729       C  
ATOM   1739  N   SER A 240      -8.968   9.033  16.914  1.00 54.74           N  
ANISOU 1739  N   SER A 240     7267   6046   7486   -521   -737   -591       N  
ATOM   1740  CA  SER A 240      -7.895   9.642  17.696  1.00 52.96           C  
ANISOU 1740  CA  SER A 240     7039   5759   7325   -647   -813   -673       C  
ATOM   1741  C   SER A 240      -7.712  11.116  17.352  1.00 63.71           C  
ANISOU 1741  C   SER A 240     8485   6915   8805   -725   -813   -666       C  
ATOM   1742  O   SER A 240      -7.406  11.927  18.233  1.00 73.82           O  
ANISOU 1742  O   SER A 240     9830   8087  10130   -786   -883   -777       O  
ATOM   1743  CB  SER A 240      -6.583   8.891  17.482  1.00 62.17           C  
ANISOU 1743  CB  SER A 240     8061   7043   8518   -748   -829   -630       C  
ATOM   1744  OG  SER A 240      -6.044   9.161  16.199  1.00 76.21           O  
ANISOU 1744  OG  SER A 240     9791   8786  10379   -818   -760   -505       O  
ATOM   1745  N   ARG A 241      -7.879  11.486  16.079  1.00 61.40           N  
ANISOU 1745  N   ARG A 241     8206   6561   8564   -725   -738   -535       N  
ATOM   1746  CA  ARG A 241      -7.684  12.886  15.713  1.00 70.73           C  
ANISOU 1746  CA  ARG A 241     9475   7533   9867   -801   -730   -509       C  
ATOM   1747  C   ARG A 241      -8.894  13.739  16.083  1.00 69.99           C  
ANISOU 1747  C   ARG A 241     9530   7294   9767   -688   -734   -568       C  
ATOM   1748  O   ARG A 241      -8.734  14.890  16.498  1.00 74.19           O  
ANISOU 1748  O   ARG A 241    10158   7642  10390   -745   -768   -633       O  
ATOM   1749  CB  ARG A 241      -7.352  13.015  14.222  1.00 75.80           C  
ANISOU 1749  CB  ARG A 241    10086   8158  10557   -844   -643   -335       C  
ATOM   1750  CG  ARG A 241      -8.448  12.576  13.268  1.00 77.52           C  
ANISOU 1750  CG  ARG A 241    10335   8434  10686   -699   -579   -233       C  
ATOM   1751  CD  ARG A 241      -7.938  12.541  11.832  1.00 85.11           C  
ANISOU 1751  CD  ARG A 241    11262   9412  11663   -748   -495    -66       C  
ATOM   1752  NE  ARG A 241      -7.622  13.869  11.313  1.00 93.39           N  
ANISOU 1752  NE  ARG A 241    12396  10261  12828   -831   -464     11       N  
ATOM   1753  CZ  ARG A 241      -7.068  14.090  10.125  1.00 99.66           C  
ANISOU 1753  CZ  ARG A 241    13181  11036  13651   -895   -381    164       C  
ATOM   1754  NH1 ARG A 241      -6.762  13.070   9.335  1.00110.03           N  
ANISOU 1754  NH1 ARG A 241    14405  12522  14879   -880   -321    244       N  
ATOM   1755  NH2 ARG A 241      -6.816  15.329   9.723  1.00 93.17           N  
ANISOU 1755  NH2 ARG A 241    12445  10015  12940   -972   -350    240       N  
ATOM   1756  N   GLU A 242     -10.108  13.199  15.963  1.00 69.69           N  
ANISOU 1756  N   GLU A 242     9511   7332   9634   -527   -701   -553       N  
ATOM   1757  CA  GLU A 242     -11.297  13.924  16.395  1.00 69.87           C  
ANISOU 1757  CA  GLU A 242     9656   7237   9655   -401   -699   -616       C  
ATOM   1758  C   GLU A 242     -11.644  13.679  17.859  1.00 68.71           C  
ANISOU 1758  C   GLU A 242     9538   7135   9435   -346   -743   -783       C  
ATOM   1759  O   GLU A 242     -12.613  14.265  18.354  1.00 67.53           O  
ANISOU 1759  O   GLU A 242     9487   6893   9279   -235   -732   -853       O  
ATOM   1760  CB  GLU A 242     -12.494  13.564  15.508  1.00 77.22           C  
ANISOU 1760  CB  GLU A 242    10582   8220  10536   -252   -643   -513       C  
ATOM   1761  CG  GLU A 242     -12.542  14.362  14.213  1.00 92.47           C  
ANISOU 1761  CG  GLU A 242    12566  10027  12541   -260   -605   -367       C  
ATOM   1762  CD  GLU A 242     -13.254  13.625  13.099  1.00 98.15           C  
ANISOU 1762  CD  GLU A 242    13236  10867  13188   -162   -568   -242       C  
ATOM   1763  OE1 GLU A 242     -13.966  14.277  12.304  1.00 99.66           O  
ANISOU 1763  OE1 GLU A 242    13497  10963  13406    -81   -551   -150       O  
ATOM   1764  OE2 GLU A 242     -13.102  12.388  13.020  1.00 97.54           O  
ANISOU 1764  OE2 GLU A 242    13054  10977  13028   -164   -563   -236       O  
ATOM   1765  N   ARG A 243     -10.880  12.826  18.543  1.00 63.63           N  
ANISOU 1765  N   ARG A 243     8813   6631   8732   -413   -788   -841       N  
ATOM   1766  CA  ARG A 243     -10.953  12.573  19.982  1.00 64.76           C  
ANISOU 1766  CA  ARG A 243     8990   6827   8790   -385   -840   -994       C  
ATOM   1767  C   ARG A 243     -12.277  11.940  20.417  1.00 65.52           C  
ANISOU 1767  C   ARG A 243     9101   7016   8777   -214   -788  -1020       C  
ATOM   1768  O   ARG A 243     -12.266  10.952  21.157  1.00 65.45           O  
ANISOU 1768  O   ARG A 243     9045   7159   8664   -187   -799  -1063       O  
ATOM   1769  CB  ARG A 243     -10.644  13.861  20.768  1.00 76.14           C  
ANISOU 1769  CB  ARG A 243    10557   8079  10294   -445   -900  -1127       C  
ATOM   1770  CG  ARG A 243     -11.813  14.679  21.300  1.00 90.31           C  
ANISOU 1770  CG  ARG A 243    12496   9743  12076   -312   -869  -1217       C  
ATOM   1771  CD  ARG A 243     -11.342  15.671  22.350  1.00 97.73           C  
ANISOU 1771  CD  ARG A 243    13559  10533  13042   -379   -947  -1387       C  
ATOM   1772  NE  ARG A 243     -10.330  16.582  21.821  1.00101.51           N  
ANISOU 1772  NE  ARG A 243    14049  10849  13673   -545   -994  -1360       N  
ATOM   1773  CZ  ARG A 243      -9.541  17.341  22.574  1.00104.08           C  
ANISOU 1773  CZ  ARG A 243    14444  11054  14050   -666  -1088  -1495       C  
ATOM   1774  NH1 ARG A 243      -9.638  17.295  23.896  1.00101.88           N  
ANISOU 1774  NH1 ARG A 243    14242  10806  13661   -629  -1151  -1671       N  
ATOM   1775  NH2 ARG A 243      -8.649  18.143  22.005  1.00106.64           N  
ANISOU 1775  NH2 ARG A 243    14761  11224  14532   -827  -1119  -1453       N  
ATOM   1776  N   VAL A 244     -13.419  12.468  19.973  1.00 65.90           N  
ANISOU 1776  N   VAL A 244     9208   6978   8854    -96   -729   -987       N  
ATOM   1777  CA  VAL A 244     -14.718  11.904  20.330  1.00 64.57           C  
ANISOU 1777  CA  VAL A 244     9032   6896   8606     63   -671  -1003       C  
ATOM   1778  C   VAL A 244     -15.641  12.044  19.127  1.00 52.03           C  
ANISOU 1778  C   VAL A 244     7420   5278   7072    152   -618   -880       C  
ATOM   1779  O   VAL A 244     -15.551  13.006  18.362  1.00 58.14           O  
ANISOU 1779  O   VAL A 244     8248   5904   7939    132   -621   -822       O  
ATOM   1780  CB  VAL A 244     -15.354  12.576  21.580  1.00 72.53           C  
ANISOU 1780  CB  VAL A 244    10160   7822   9576    150   -662  -1155       C  
ATOM   1781  CG1 VAL A 244     -16.597  11.820  22.017  1.00 64.39           C  
ANISOU 1781  CG1 VAL A 244     9093   6912   8460    302   -587  -1164       C  
ATOM   1782  CG2 VAL A 244     -14.372  12.664  22.738  1.00 84.08           C  
ANISOU 1782  CG2 VAL A 244    11675   9289  10983     54   -737  -1288       C  
ATOM   1783  N   PHE A 245     -16.523  11.066  18.958  1.00 56.63           N  
ANISOU 1783  N   PHE A 245     7920   6000   7595    249   -575   -836       N  
ATOM   1784  CA  PHE A 245     -17.630  11.157  18.017  1.00 57.82           C  
ANISOU 1784  CA  PHE A 245     8044   6139   7785    360   -539   -743       C  
ATOM   1785  C   PHE A 245     -18.873  11.609  18.769  1.00 59.92           C  
ANISOU 1785  C   PHE A 245     8356   6357   8054    510   -493   -821       C  
ATOM   1786  O   PHE A 245     -19.050  11.288  19.947  1.00 58.75           O  
ANISOU 1786  O   PHE A 245     8220   6264   7837    540   -469   -926       O  
ATOM   1787  CB  PHE A 245     -17.909   9.813  17.331  1.00 48.79           C  
ANISOU 1787  CB  PHE A 245     6774   5172   6591    373   -526   -653       C  
ATOM   1788  CG  PHE A 245     -16.809   9.348  16.418  1.00 54.74           C  
ANISOU 1788  CG  PHE A 245     7481   5977   7343    251   -553   -566       C  
ATOM   1789  CD1 PHE A 245     -15.876  10.239  15.915  1.00 64.78           C  
ANISOU 1789  CD1 PHE A 245     8809   7128   8677    155   -575   -530       C  
ATOM   1790  CD2 PHE A 245     -16.716   8.013  16.056  1.00 47.74           C  
ANISOU 1790  CD2 PHE A 245     6491   5251   6397    235   -547   -520       C  
ATOM   1791  CE1 PHE A 245     -14.868   9.805  15.074  1.00 60.27           C  
ANISOU 1791  CE1 PHE A 245     8185   6611   8103     49   -581   -446       C  
ATOM   1792  CE2 PHE A 245     -15.709   7.572  15.215  1.00 53.34           C  
ANISOU 1792  CE2 PHE A 245     7158   6009   7101    137   -559   -446       C  
ATOM   1793  CZ  PHE A 245     -14.784   8.472  14.723  1.00 57.44           C  
ANISOU 1793  CZ  PHE A 245     7726   6420   7678     46   -570   -408       C  
ATOM   1794  N   SER A 246     -19.728  12.361  18.088  1.00 60.60           N  
ANISOU 1794  N   SER A 246     8467   6341   8215    611   -478   -765       N  
ATOM   1795  CA  SER A 246     -21.009  12.702  18.677  1.00 61.32           C  
ANISOU 1795  CA  SER A 246     8572   6403   8323    772   -424   -825       C  
ATOM   1796  C   SER A 246     -21.897  11.463  18.730  1.00 54.02           C  
ANISOU 1796  C   SER A 246     7511   5667   7346    843   -383   -797       C  
ATOM   1797  O   SER A 246     -21.607  10.427  18.126  1.00 60.89           O  
ANISOU 1797  O   SER A 246     8287   6669   8181    777   -406   -721       O  
ATOM   1798  CB  SER A 246     -21.691  13.813  17.880  1.00 60.02           C  
ANISOU 1798  CB  SER A 246     8459   6081   8264    873   -426   -761       C  
ATOM   1799  OG  SER A 246     -22.094  13.337  16.610  1.00 64.36           O  
ANISOU 1799  OG  SER A 246     8917   6707   8830    897   -451   -619       O  
ATOM   1800  N   GLU A 247     -22.996  11.573  19.474  1.00 49.58           N  
ANISOU 1800  N   GLU A 247     6938   5114   6789    978   -315   -861       N  
ATOM   1801  CA  GLU A 247     -23.930  10.457  19.540  1.00 52.58           C  
ANISOU 1801  CA  GLU A 247     7178   5659   7143   1043   -267   -830       C  
ATOM   1802  C   GLU A 247     -24.559  10.175  18.182  1.00 57.70           C  
ANISOU 1802  C   GLU A 247     7720   6348   7856   1080   -307   -702       C  
ATOM   1803  O   GLU A 247     -24.879   9.020  17.879  1.00 63.36           O  
ANISOU 1803  O   GLU A 247     8314   7211   8547   1062   -307   -653       O  
ATOM   1804  CB  GLU A 247     -25.003  10.727  20.593  1.00 63.72           C  
ANISOU 1804  CB  GLU A 247     8591   7064   8555   1185   -170   -919       C  
ATOM   1805  CG  GLU A 247     -24.457  10.772  22.012  1.00 75.28           C  
ANISOU 1805  CG  GLU A 247    10158   8527   9917   1155   -128  -1052       C  
ATOM   1806  CD  GLU A 247     -25.548  10.679  23.059  1.00 79.00           C  
ANISOU 1806  CD  GLU A 247    10610   9047  10360   1292     -7  -1126       C  
ATOM   1807  OE1 GLU A 247     -26.731  10.561  22.674  1.00 78.90           O  
ANISOU 1807  OE1 GLU A 247    10482   9070  10426   1406     45  -1072       O  
ATOM   1808  OE2 GLU A 247     -25.225  10.721  24.265  1.00 76.80           O  
ANISOU 1808  OE2 GLU A 247    10427   8775   9978   1287     36  -1237       O  
ATOM   1809  N   ASP A 248     -24.724  11.205  17.347  1.00 56.21           N  
ANISOU 1809  N   ASP A 248     7584   6026   7746   1129   -348   -645       N  
ATOM   1810  CA  ASP A 248     -25.251  10.996  16.000  1.00 51.69           C  
ANISOU 1810  CA  ASP A 248     6930   5493   7216   1165   -404   -519       C  
ATOM   1811  C   ASP A 248     -24.289  10.170  15.157  1.00 52.45           C  
ANISOU 1811  C   ASP A 248     7003   5676   7249   1023   -461   -445       C  
ATOM   1812  O   ASP A 248     -24.693   9.214  14.485  1.00 52.27           O  
ANISOU 1812  O   ASP A 248     6871   5781   7207   1022   -488   -385       O  
ATOM   1813  CB  ASP A 248     -25.526  12.340  15.324  1.00 55.39           C  
ANISOU 1813  CB  ASP A 248     7485   5788   7771   1250   -438   -464       C  
ATOM   1814  CG  ASP A 248     -26.658  13.103  15.977  1.00 81.93           C  
ANISOU 1814  CG  ASP A 248    10848   9068  11211   1422   -382   -524       C  
ATOM   1815  OD1 ASP A 248     -27.535  12.460  16.590  1.00 90.88           O  
ANISOU 1815  OD1 ASP A 248    11870  10316  12344   1496   -324   -570       O  
ATOM   1816  OD2 ASP A 248     -26.673  14.347  15.869  1.00 92.74           O  
ANISOU 1816  OD2 ASP A 248    12331  10255  12650   1485   -388   -523       O  
ATOM   1817  N   ARG A 249     -23.005  10.534  15.174  1.00 56.26           N  
ANISOU 1817  N   ARG A 249     7584   6088   7706    902   -478   -454       N  
ATOM   1818  CA  ARG A 249     -22.034   9.846  14.334  1.00 54.03           C  
ANISOU 1818  CA  ARG A 249     7280   5879   7370    776   -517   -381       C  
ATOM   1819  C   ARG A 249     -21.764   8.433  14.832  1.00 58.88           C  
ANISOU 1819  C   ARG A 249     7803   6659   7911    712   -499   -420       C  
ATOM   1820  O   ARG A 249     -21.501   7.533  14.026  1.00 56.36           O  
ANISOU 1820  O   ARG A 249     7421   6440   7552    660   -525   -357       O  
ATOM   1821  CB  ARG A 249     -20.738  10.653  14.274  1.00 56.63           C  
ANISOU 1821  CB  ARG A 249     7720   6086   7712    663   -530   -378       C  
ATOM   1822  CG  ARG A 249     -19.725  10.125  13.277  1.00 59.43           C  
ANISOU 1822  CG  ARG A 249     8055   6501   8025    544   -555   -289       C  
ATOM   1823  CD  ARG A 249     -18.518  11.041  13.185  1.00 58.77           C  
ANISOU 1823  CD  ARG A 249     8067   6284   7980    432   -559   -276       C  
ATOM   1824  NE  ARG A 249     -17.473  10.479  12.333  1.00 56.37           N  
ANISOU 1824  NE  ARG A 249     7730   6051   7636    317   -562   -196       N  
ATOM   1825  CZ  ARG A 249     -16.262  11.007  12.195  1.00 60.18           C  
ANISOU 1825  CZ  ARG A 249     8258   6456   8153    192   -557   -174       C  
ATOM   1826  NH1 ARG A 249     -15.942  12.112  12.855  1.00 53.54           N  
ANISOU 1826  NH1 ARG A 249     7502   5454   7386    157   -561   -232       N  
ATOM   1827  NH2 ARG A 249     -15.371  10.430  11.400  1.00 61.46           N  
ANISOU 1827  NH2 ARG A 249     8375   6698   8279    102   -543    -99       N  
ATOM   1828  N   ALA A 250     -21.825   8.217  16.148  1.00 51.38           N  
ANISOU 1828  N   ALA A 250     6855   5733   6935    721   -453   -522       N  
ATOM   1829  CA  ALA A 250     -21.645   6.871  16.680  1.00 47.99           C  
ANISOU 1829  CA  ALA A 250     6346   5452   6437    672   -431   -548       C  
ATOM   1830  C   ALA A 250     -22.871   6.003  16.431  1.00 42.76           C  
ANISOU 1830  C   ALA A 250     5562   4895   5789    750   -411   -516       C  
ATOM   1831  O   ALA A 250     -22.741   4.787  16.250  1.00 47.99           O  
ANISOU 1831  O   ALA A 250     6148   5674   6414    699   -414   -492       O  
ATOM   1832  CB  ALA A 250     -21.326   6.933  18.172  1.00 48.67           C  
ANISOU 1832  CB  ALA A 250     6485   5533   6474    661   -391   -658       C  
ATOM   1833  N   ARG A 251     -24.061   6.606  16.420  1.00 43.38           N  
ANISOU 1833  N   ARG A 251     5617   4931   5933    874   -391   -517       N  
ATOM   1834  CA  ARG A 251     -25.270   5.861  16.087  1.00 47.24           C  
ANISOU 1834  CA  ARG A 251     5972   5517   6460    944   -383   -481       C  
ATOM   1835  C   ARG A 251     -25.201   5.318  14.665  1.00 50.39           C  
ANISOU 1835  C   ARG A 251     6319   5969   6858    903   -465   -391       C  
ATOM   1836  O   ARG A 251     -25.661   4.203  14.394  1.00 53.91           O  
ANISOU 1836  O   ARG A 251     6657   6525   7301    887   -475   -372       O  
ATOM   1837  CB  ARG A 251     -26.494   6.761  16.275  1.00 49.52           C  
ANISOU 1837  CB  ARG A 251     6239   5740   6835   1092   -353   -495       C  
ATOM   1838  CG  ARG A 251     -27.823   6.134  15.892  1.00 54.52           C  
ANISOU 1838  CG  ARG A 251     6712   6469   7535   1170   -354   -456       C  
ATOM   1839  CD  ARG A 251     -28.975   7.135  16.005  1.00 59.84           C  
ANISOU 1839  CD  ARG A 251     7357   7071   8308   1330   -329   -462       C  
ATOM   1840  NE  ARG A 251     -29.240   7.531  17.388  1.00 80.58           N  
ANISOU 1840  NE  ARG A 251    10020   9664  10934   1395   -211   -556       N  
ATOM   1841  CZ  ARG A 251     -28.862   8.686  17.929  1.00 82.87           C  
ANISOU 1841  CZ  ARG A 251    10452   9817  11219   1437   -183   -616       C  
ATOM   1842  NH1 ARG A 251     -28.197   9.578  17.205  1.00 81.23           N  
ANISOU 1842  NH1 ARG A 251    10357   9485  11021   1414   -259   -581       N  
ATOM   1843  NH2 ARG A 251     -29.149   8.951  19.197  1.00 80.46           N  
ANISOU 1843  NH2 ARG A 251    10182   9494  10895   1500    -73   -712       N  
ATOM   1844  N   PHE A 252     -24.613   6.090  13.748  1.00 48.26           N  
ANISOU 1844  N   PHE A 252     6134   5618   6587    882   -522   -335       N  
ATOM   1845  CA  PHE A 252     -24.506   5.662  12.357  1.00 43.01           C  
ANISOU 1845  CA  PHE A 252     5444   5001   5895    852   -596   -248       C  
ATOM   1846  C   PHE A 252     -23.593   4.449  12.224  1.00 44.40           C  
ANISOU 1846  C   PHE A 252     5597   5275   5997    733   -595   -252       C  
ATOM   1847  O   PHE A 252     -23.999   3.414  11.684  1.00 46.54           O  
ANISOU 1847  O   PHE A 252     5785   5646   6252    723   -625   -234       O  
ATOM   1848  CB  PHE A 252     -24.003   6.825  11.500  1.00 45.35           C  
ANISOU 1848  CB  PHE A 252     5854   5180   6197    855   -636   -178       C  
ATOM   1849  CG  PHE A 252     -23.736   6.459  10.066  1.00 67.22           C  
ANISOU 1849  CG  PHE A 252     8629   8000   8912    821   -702    -86       C  
ATOM   1850  CD1 PHE A 252     -24.763   6.445   9.136  1.00 75.69           C  
ANISOU 1850  CD1 PHE A 252     9653   9107   9998    911   -774    -26       C  
ATOM   1851  CD2 PHE A 252     -22.453   6.145   9.644  1.00 72.90           C  
ANISOU 1851  CD2 PHE A 252     9402   8735   9563    705   -693    -61       C  
ATOM   1852  CE1 PHE A 252     -24.518   6.114   7.818  1.00 75.23           C  
ANISOU 1852  CE1 PHE A 252     9618   9100   9867    885   -839     52       C  
ATOM   1853  CE2 PHE A 252     -22.202   5.812   8.328  1.00 68.19           C  
ANISOU 1853  CE2 PHE A 252     8821   8187   8900    682   -739     20       C  
ATOM   1854  CZ  PHE A 252     -23.236   5.797   7.414  1.00 70.13           C  
ANISOU 1854  CZ  PHE A 252     9038   8468   9140    772   -814     74       C  
ATOM   1855  N   TYR A 253     -22.354   4.556  12.714  1.00 47.83           N  
ANISOU 1855  N   TYR A 253     6103   5679   6393    643   -566   -279       N  
ATOM   1856  CA  TYR A 253     -21.445   3.414  12.679  1.00 49.06           C  
ANISOU 1856  CA  TYR A 253     6231   5923   6486    543   -560   -285       C  
ATOM   1857  C   TYR A 253     -22.009   2.239  13.468  1.00 56.65           C  
ANISOU 1857  C   TYR A 253     7101   6981   7443    551   -526   -332       C  
ATOM   1858  O   TYR A 253     -21.906   1.085  13.038  1.00 52.37           O  
ANISOU 1858  O   TYR A 253     6501   6523   6872    510   -539   -318       O  
ATOM   1859  CB  TYR A 253     -20.075   3.811  13.229  1.00 50.71           C  
ANISOU 1859  CB  TYR A 253     6513   6082   6672    455   -539   -311       C  
ATOM   1860  CG  TYR A 253     -19.394   4.926  12.471  1.00 51.77           C  
ANISOU 1860  CG  TYR A 253     6734   6113   6823    423   -559   -257       C  
ATOM   1861  CD1 TYR A 253     -19.519   5.036  11.091  1.00 49.94           C  
ANISOU 1861  CD1 TYR A 253     6515   5883   6578    436   -592   -166       C  
ATOM   1862  CD2 TYR A 253     -18.628   5.871  13.138  1.00 46.47           C  
ANISOU 1862  CD2 TYR A 253     6138   5339   6178    376   -547   -294       C  
ATOM   1863  CE1 TYR A 253     -18.896   6.057  10.397  1.00 45.66           C  
ANISOU 1863  CE1 TYR A 253     6058   5241   6048    405   -596   -100       C  
ATOM   1864  CE2 TYR A 253     -18.003   6.897  12.455  1.00 45.28           C  
ANISOU 1864  CE2 TYR A 253     6065   5081   6059    335   -557   -236       C  
ATOM   1865  CZ  TYR A 253     -18.141   6.986  11.085  1.00 45.91           C  
ANISOU 1865  CZ  TYR A 253     6156   5162   6124    350   -575   -132       C  
ATOM   1866  OH  TYR A 253     -17.520   8.006  10.402  1.00 46.06           O  
ANISOU 1866  OH  TYR A 253     6258   5069   6171    308   -572    -58       O  
ATOM   1867  N   GLY A 254     -22.613   2.518  14.624  1.00 48.10           N  
ANISOU 1867  N   GLY A 254     6009   5880   6387    606   -476   -389       N  
ATOM   1868  CA  GLY A 254     -23.172   1.446  15.433  1.00 41.56           C  
ANISOU 1868  CA  GLY A 254     5099   5138   5554    613   -426   -422       C  
ATOM   1869  C   GLY A 254     -24.307   0.721  14.736  1.00 47.37           C  
ANISOU 1869  C   GLY A 254     5722   5939   6339    650   -449   -387       C  
ATOM   1870  O   GLY A 254     -24.459  -0.495  14.875  1.00 43.66           O  
ANISOU 1870  O   GLY A 254     5181   5546   5863    611   -432   -389       O  
ATOM   1871  N   ALA A 255     -25.123   1.454  13.977  1.00 46.75           N  
ANISOU 1871  N   ALA A 255     5623   5825   6315    725   -494   -355       N  
ATOM   1872  CA  ALA A 255     -26.210   0.814  13.246  1.00 42.67           C  
ANISOU 1872  CA  ALA A 255     4988   5373   5851    757   -539   -326       C  
ATOM   1873  C   ALA A 255     -25.676  -0.094  12.146  1.00 47.65           C  
ANISOU 1873  C   ALA A 255     5616   6058   6431    679   -609   -295       C  
ATOM   1874  O   ALA A 255     -26.230  -1.172  11.900  1.00 47.75           O  
ANISOU 1874  O   ALA A 255     5535   6142   6467    656   -629   -300       O  
ATOM   1875  CB  ALA A 255     -27.149   1.869  12.662  1.00 37.15           C  
ANISOU 1875  CB  ALA A 255     4271   4626   5219    866   -588   -294       C  
ATOM   1876  N   GLU A 256     -24.599   0.317  11.477  1.00 44.57           N  
ANISOU 1876  N   GLU A 256     5329   5632   5975    637   -639   -266       N  
ATOM   1877  CA  GLU A 256     -24.029  -0.527  10.434  1.00 50.35           C  
ANISOU 1877  CA  GLU A 256     6070   6415   6645    572   -689   -242       C  
ATOM   1878  C   GLU A 256     -23.395  -1.777  11.029  1.00 47.75           C  
ANISOU 1878  C   GLU A 256     5716   6138   6289    494   -641   -280       C  
ATOM   1879  O   GLU A 256     -23.473  -2.859  10.439  1.00 43.86           O  
ANISOU 1879  O   GLU A 256     5182   5701   5781    458   -672   -284       O  
ATOM   1880  CB  GLU A 256     -23.013   0.268   9.613  1.00 47.07           C  
ANISOU 1880  CB  GLU A 256     5768   5949   6168    549   -710   -193       C  
ATOM   1881  CG  GLU A 256     -23.571   1.559   9.034  1.00 52.67           C  
ANISOU 1881  CG  GLU A 256     6521   6589   6902    630   -755   -140       C  
ATOM   1882  CD  GLU A 256     -22.715   2.128   7.914  1.00 61.28           C  
ANISOU 1882  CD  GLU A 256     7717   7643   7922    603   -782    -69       C  
ATOM   1883  OE1 GLU A 256     -23.290   2.635   6.927  1.00 65.11           O  
ANISOU 1883  OE1 GLU A 256     8227   8117   8394    666   -850     -8       O  
ATOM   1884  OE2 GLU A 256     -21.471   2.066   8.012  1.00 60.25           O  
ANISOU 1884  OE2 GLU A 256     7641   7501   7751    522   -733    -68       O  
ATOM   1885  N   ILE A 257     -22.772  -1.652  12.202  1.00 48.19           N  
ANISOU 1885  N   ILE A 257     5801   6171   6337    471   -571   -310       N  
ATOM   1886  CA  ILE A 257     -22.181  -2.818  12.848  1.00 43.77           C  
ANISOU 1886  CA  ILE A 257     5221   5658   5751    410   -529   -335       C  
ATOM   1887  C   ILE A 257     -23.267  -3.794  13.287  1.00 40.55           C  
ANISOU 1887  C   ILE A 257     4714   5298   5397    423   -506   -352       C  
ATOM   1888  O   ILE A 257     -23.125  -5.012  13.127  1.00 52.85           O  
ANISOU 1888  O   ILE A 257     6236   6894   6949    375   -507   -355       O  
ATOM   1889  CB  ILE A 257     -21.294  -2.383  14.027  1.00 44.19           C  
ANISOU 1889  CB  ILE A 257     5334   5681   5775    389   -477   -362       C  
ATOM   1890  CG1 ILE A 257     -20.101  -1.573  13.522  1.00 45.45           C  
ANISOU 1890  CG1 ILE A 257     5575   5795   5900    350   -502   -343       C  
ATOM   1891  CG2 ILE A 257     -20.815  -3.597  14.805  1.00 49.54           C  
ANISOU 1891  CG2 ILE A 257     5987   6409   6426    345   -438   -378       C  
ATOM   1892  CD1 ILE A 257     -19.314  -0.900  14.624  1.00 44.86           C  
ANISOU 1892  CD1 ILE A 257     5558   5678   5810    328   -475   -379       C  
ATOM   1893  N   VAL A 258     -24.367  -3.277  13.839  1.00 41.03           N  
ANISOU 1893  N   VAL A 258     4723   5348   5517    488   -479   -361       N  
ATOM   1894  CA  VAL A 258     -25.496  -4.132  14.203  1.00 37.77           C  
ANISOU 1894  CA  VAL A 258     4196   4980   5175    497   -448   -367       C  
ATOM   1895  C   VAL A 258     -25.983  -4.905  12.986  1.00 46.30           C  
ANISOU 1895  C   VAL A 258     5210   6095   6288    470   -532   -355       C  
ATOM   1896  O   VAL A 258     -26.195  -6.123  13.039  1.00 44.56           O  
ANISOU 1896  O   VAL A 258     4929   5907   6096    418   -523   -363       O  
ATOM   1897  CB  VAL A 258     -26.629  -3.292  14.822  1.00 46.79           C  
ANISOU 1897  CB  VAL A 258     5285   6108   6387    586   -404   -375       C  
ATOM   1898  CG1 VAL A 258     -27.900  -4.114  14.923  1.00 50.26           C  
ANISOU 1898  CG1 VAL A 258     5576   6598   6922    592   -382   -370       C  
ATOM   1899  CG2 VAL A 258     -26.218  -2.768  16.187  1.00 37.10           C  
ANISOU 1899  CG2 VAL A 258     4128   4854   5114    609   -310   -405       C  
ATOM   1900  N   SER A 259     -26.150  -4.204  11.861  1.00 45.73           N  
ANISOU 1900  N   SER A 259     5156   6011   6207    504   -621   -335       N  
ATOM   1901  CA  SER A 259     -26.630  -4.847  10.641  1.00 44.49           C  
ANISOU 1901  CA  SER A 259     4951   5892   6062    486   -720   -332       C  
ATOM   1902  C   SER A 259     -25.681  -5.948  10.184  1.00 35.59           C  
ANISOU 1902  C   SER A 259     3873   4782   4868    404   -729   -348       C  
ATOM   1903  O   SER A 259     -26.119  -7.037   9.795  1.00 44.43           O  
ANISOU 1903  O   SER A 259     4932   5931   6020    362   -766   -372       O  
ATOM   1904  CB  SER A 259     -26.812  -3.802   9.538  1.00 44.78           C  
ANISOU 1904  CB  SER A 259     5031   5913   6072    546   -812   -298       C  
ATOM   1905  OG  SER A 259     -27.330  -4.382   8.352  1.00 47.98           O  
ANISOU 1905  OG  SER A 259     5397   6363   6470    536   -923   -300       O  
ATOM   1906  N   ALA A 260     -24.374  -5.688  10.237  1.00 38.16           N  
ANISOU 1906  N   ALA A 260     4304   5084   5111    380   -695   -338       N  
ATOM   1907  CA  ALA A 260     -23.399  -6.701   9.848  1.00 40.15           C  
ANISOU 1907  CA  ALA A 260     4599   5352   5305    317   -691   -353       C  
ATOM   1908  C   ALA A 260     -23.429  -7.890  10.802  1.00 45.10           C  
ANISOU 1908  C   ALA A 260     5175   5986   5976    275   -629   -376       C  
ATOM   1909  O   ALA A 260     -23.428  -9.048  10.366  1.00 53.53           O  
ANISOU 1909  O   ALA A 260     6223   7064   7050    233   -649   -399       O  
ATOM   1910  CB  ALA A 260     -22.001  -6.085   9.792  1.00 43.94           C  
ANISOU 1910  CB  ALA A 260     5179   5810   5707    304   -659   -331       C  
ATOM   1911  N   LEU A 261     -23.461  -7.625  12.112  1.00 49.86           N  
ANISOU 1911  N   LEU A 261     5765   6577   6603    288   -551   -371       N  
ATOM   1912  CA  LEU A 261     -23.477  -8.714  13.085  1.00 47.74           C  
ANISOU 1912  CA  LEU A 261     5460   6314   6364    253   -484   -376       C  
ATOM   1913  C   LEU A 261     -24.765  -9.523  13.015  1.00 44.52           C  
ANISOU 1913  C   LEU A 261     4945   5918   6053    238   -491   -384       C  
ATOM   1914  O   LEU A 261     -24.752 -10.726  13.298  1.00 43.07           O  
ANISOU 1914  O   LEU A 261     4736   5728   5900    189   -461   -386       O  
ATOM   1915  CB  LEU A 261     -23.277  -8.165  14.496  1.00 43.75           C  
ANISOU 1915  CB  LEU A 261     4980   5801   5842    280   -402   -367       C  
ATOM   1916  CG  LEU A 261     -21.895  -7.594  14.802  1.00 40.38           C  
ANISOU 1916  CG  LEU A 261     4649   5362   5333    274   -396   -367       C  
ATOM   1917  CD1 LEU A 261     -21.902  -6.896  16.149  1.00 41.97           C  
ANISOU 1917  CD1 LEU A 261     4880   5556   5513    307   -335   -374       C  
ATOM   1918  CD2 LEU A 261     -20.849  -8.693  14.773  1.00 42.14           C  
ANISOU 1918  CD2 LEU A 261     4896   5593   5521    227   -390   -361       C  
ATOM   1919  N   ASP A 262     -25.883  -8.882  12.658  1.00 46.16           N  
ANISOU 1919  N   ASP A 262     5081   6138   6320    277   -532   -384       N  
ATOM   1920  CA  ASP A 262     -27.129  -9.617  12.467  1.00 49.85           C  
ANISOU 1920  CA  ASP A 262     5422   6621   6896    254   -556   -394       C  
ATOM   1921  C   ASP A 262     -27.007 -10.602  11.314  1.00 49.02           C  
ANISOU 1921  C   ASP A 262     5322   6516   6788    195   -647   -425       C  
ATOM   1922  O   ASP A 262     -27.515 -11.727  11.391  1.00 51.20           O  
ANISOU 1922  O   ASP A 262     5529   6783   7143    136   -643   -441       O  
ATOM   1923  CB  ASP A 262     -28.281  -8.643  12.216  1.00 39.86           C  
ANISOU 1923  CB  ASP A 262     4073   5375   5698    321   -597   -387       C  
ATOM   1924  CG  ASP A 262     -29.636  -9.326  12.215  1.00 55.92           C  
ANISOU 1924  CG  ASP A 262     5945   7433   7869    296   -610   -394       C  
ATOM   1925  OD1 ASP A 262     -29.729 -10.474  12.702  1.00 64.46           O  
ANISOU 1925  OD1 ASP A 262     6985   8506   9001    225   -555   -397       O  
ATOM   1926  OD2 ASP A 262     -30.613  -8.713  11.730  1.00 61.07           O  
ANISOU 1926  OD2 ASP A 262     6506   8109   8587    346   -678   -393       O  
ATOM   1927  N   TYR A 263     -26.336 -10.194  10.235  1.00 43.72           N  
ANISOU 1927  N   TYR A 263     4738   5849   6024    209   -725   -436       N  
ATOM   1928  CA  TYR A 263     -26.127 -11.088   9.101  1.00 49.88           C  
ANISOU 1928  CA  TYR A 263     5547   6631   6774    164   -807   -476       C  
ATOM   1929  C   TYR A 263     -25.316 -12.311   9.511  1.00 51.04           C  
ANISOU 1929  C   TYR A 263     5735   6745   6913    107   -743   -493       C  
ATOM   1930  O   TYR A 263     -25.703 -13.449   9.226  1.00 54.80           O  
ANISOU 1930  O   TYR A 263     6174   7201   7447     52   -772   -531       O  
ATOM   1931  CB  TYR A 263     -25.436 -10.334   7.963  1.00 53.58           C  
ANISOU 1931  CB  TYR A 263     6121   7115   7123    200   -874   -472       C  
ATOM   1932  CG  TYR A 263     -25.059 -11.192   6.771  1.00 64.70           C  
ANISOU 1932  CG  TYR A 263     7588   8529   8465    166   -945   -520       C  
ATOM   1933  CD1 TYR A 263     -23.788 -11.746   6.662  1.00 66.95           C  
ANISOU 1933  CD1 TYR A 263     7966   8798   8675    145   -890   -532       C  
ATOM   1934  CD2 TYR A 263     -25.967 -11.434   5.748  1.00 66.97           C  
ANISOU 1934  CD2 TYR A 263     7840   8842   8763    161  -1071   -559       C  
ATOM   1935  CE1 TYR A 263     -23.437 -12.522   5.573  1.00 70.04           C  
ANISOU 1935  CE1 TYR A 263     8421   9192   8999    125   -942   -585       C  
ATOM   1936  CE2 TYR A 263     -25.623 -12.211   4.655  1.00 70.50           C  
ANISOU 1936  CE2 TYR A 263     8359   9294   9133    135  -1137   -617       C  
ATOM   1937  CZ  TYR A 263     -24.356 -12.752   4.574  1.00 72.35           C  
ANISOU 1937  CZ  TYR A 263     8694   9507   9289    119  -1065   -631       C  
ATOM   1938  OH  TYR A 263     -24.006 -13.525   3.491  1.00 77.22           O  
ANISOU 1938  OH  TYR A 263     9392  10126   9824    103  -1118   -697       O  
ATOM   1939  N   LEU A 264     -24.187 -12.095  10.191  1.00 50.68           N  
ANISOU 1939  N   LEU A 264     5763   6688   6805    120   -662   -465       N  
ATOM   1940  CA  LEU A 264     -23.328 -13.213  10.572  1.00 46.17           C  
ANISOU 1940  CA  LEU A 264     5233   6086   6225     83   -607   -471       C  
ATOM   1941  C   LEU A 264     -24.049 -14.178  11.504  1.00 51.91           C  
ANISOU 1941  C   LEU A 264     5885   6784   7056     42   -551   -461       C  
ATOM   1942  O   LEU A 264     -23.901 -15.398  11.378  1.00 54.38           O  
ANISOU 1942  O   LEU A 264     6204   7054   7403     -3   -547   -482       O  
ATOM   1943  CB  LEU A 264     -22.050 -12.692  11.226  1.00 36.33           C  
ANISOU 1943  CB  LEU A 264     4059   4843   4903    109   -543   -438       C  
ATOM   1944  CG  LEU A 264     -21.021 -12.034  10.300  1.00 43.77           C  
ANISOU 1944  CG  LEU A 264     5081   5802   5748    130   -574   -441       C  
ATOM   1945  CD1 LEU A 264     -19.850 -11.500  11.101  1.00 43.18           C  
ANISOU 1945  CD1 LEU A 264     5050   5730   5628    143   -515   -409       C  
ATOM   1946  CD2 LEU A 264     -20.535 -13.018   9.248  1.00 43.42           C  
ANISOU 1946  CD2 LEU A 264     5078   5750   5671    110   -604   -481       C  
ATOM   1947  N   HIS A 265     -24.843 -13.652  12.440  1.00 51.61           N  
ANISOU 1947  N   HIS A 265     5777   6760   7071     60   -500   -428       N  
ATOM   1948  CA  HIS A 265     -25.515 -14.514  13.409  1.00 50.99           C  
ANISOU 1948  CA  HIS A 265     5630   6658   7088     22   -422   -402       C  
ATOM   1949  C   HIS A 265     -26.648 -15.305  12.762  1.00 49.09           C  
ANISOU 1949  C   HIS A 265     5289   6399   6966    -38   -479   -434       C  
ATOM   1950  O   HIS A 265     -26.732 -16.528  12.919  1.00 52.68           O  
ANISOU 1950  O   HIS A 265     5728   6801   7487   -101   -454   -436       O  
ATOM   1951  CB  HIS A 265     -26.043 -13.679  14.577  1.00 45.69           C  
ANISOU 1951  CB  HIS A 265     4917   6015   6428     66   -336   -360       C  
ATOM   1952  CG  HIS A 265     -24.966 -13.068  15.416  1.00 52.25           C  
ANISOU 1952  CG  HIS A 265     5847   6856   7149    110   -281   -336       C  
ATOM   1953  ND1 HIS A 265     -25.234 -12.304  16.531  1.00 52.27           N  
ANISOU 1953  ND1 HIS A 265     5849   6881   7132    157   -202   -311       N  
ATOM   1954  CD2 HIS A 265     -23.618 -13.112  15.305  1.00 49.01           C  
ANISOU 1954  CD2 HIS A 265     5536   6438   6649    115   -297   -338       C  
ATOM   1955  CE1 HIS A 265     -24.096 -11.904  17.071  1.00 53.58           C  
ANISOU 1955  CE1 HIS A 265     6113   7050   7195    181   -186   -305       C  
ATOM   1956  NE2 HIS A 265     -23.101 -12.381  16.345  1.00 49.83           N  
ANISOU 1956  NE2 HIS A 265     5691   6560   6684    155   -243   -317       N  
ATOM   1957  N   SER A 266     -27.534 -14.624  12.034  1.00 50.11           N  
ANISOU 1957  N   SER A 266     5345   6565   7130    -21   -563   -459       N  
ATOM   1958  CA  SER A 266     -28.712 -15.294  11.492  1.00 61.45           C  
ANISOU 1958  CA  SER A 266     6661   7993   8694    -81   -632   -492       C  
ATOM   1959  C   SER A 266     -28.393 -16.048  10.204  1.00 65.30           C  
ANISOU 1959  C   SER A 266     7205   8455   9153   -126   -749   -563       C  
ATOM   1960  O   SER A 266     -28.759 -17.219  10.058  1.00 77.55           O  
ANISOU 1960  O   SER A 266     8718   9954  10794   -206   -767   -597       O  
ATOM   1961  CB  SER A 266     -29.831 -14.278  11.260  1.00 63.29           C  
ANISOU 1961  CB  SER A 266     6782   8283   8984    -35   -685   -488       C  
ATOM   1962  OG  SER A 266     -29.410 -13.249  10.385  1.00 73.85           O  
ANISOU 1962  OG  SER A 266     8195   9653  10212     33   -774   -501       O  
ATOM   1963  N   GLU A 267     -27.719 -15.393   9.258  1.00 56.30           N  
ANISOU 1963  N   GLU A 267     6162   7344   7885    -77   -826   -589       N  
ATOM   1964  CA  GLU A 267     -27.463 -16.016   7.963  1.00 55.98           C  
ANISOU 1964  CA  GLU A 267     6185   7290   7793   -106   -936   -663       C  
ATOM   1965  C   GLU A 267     -26.316 -17.016   8.027  1.00 60.54           C  
ANISOU 1965  C   GLU A 267     6872   7809   8323   -131   -877   -683       C  
ATOM   1966  O   GLU A 267     -26.400 -18.094   7.431  1.00 58.76           O  
ANISOU 1966  O   GLU A 267     6664   7533   8129   -187   -928   -751       O  
ATOM   1967  CB  GLU A 267     -27.166 -14.946   6.913  1.00 53.09           C  
ANISOU 1967  CB  GLU A 267     5892   6982   7298    -38  -1025   -670       C  
ATOM   1968  CG  GLU A 267     -28.284 -13.938   6.717  1.00 59.62           C  
ANISOU 1968  CG  GLU A 267     6620   7863   8171      4  -1100   -648       C  
ATOM   1969  CD  GLU A 267     -29.344 -14.428   5.753  1.00 81.13           C  
ANISOU 1969  CD  GLU A 267     9266  10605  10955    -36  -1253   -712       C  
ATOM   1970  OE1 GLU A 267     -29.055 -15.359   4.969  1.00 87.82           O  
ANISOU 1970  OE1 GLU A 267    10178  11427  11763    -86  -1317   -785       O  
ATOM   1971  OE2 GLU A 267     -30.463 -13.875   5.774  1.00 88.30           O  
ANISOU 1971  OE2 GLU A 267    10046  11552  11952    -15  -1313   -695       O  
ATOM   1972  N   LYS A 268     -25.243 -16.684   8.744  1.00 48.08           N  
ANISOU 1972  N   LYS A 268     5364   6230   6674    -89   -776   -631       N  
ATOM   1973  CA  LYS A 268     -24.034 -17.495   8.745  1.00 38.88           C  
ANISOU 1973  CA  LYS A 268     4297   5018   5456    -91   -725   -644       C  
ATOM   1974  C   LYS A 268     -23.864 -18.350   9.995  1.00 49.07           C  
ANISOU 1974  C   LYS A 268     5570   6250   6824   -119   -620   -598       C  
ATOM   1975  O   LYS A 268     -23.045 -19.274   9.978  1.00 52.51           O  
ANISOU 1975  O   LYS A 268     6072   6630   7248   -125   -588   -612       O  
ATOM   1976  CB  LYS A 268     -22.804 -16.595   8.570  1.00 43.16           C  
ANISOU 1976  CB  LYS A 268     4929   5604   5865    -26   -698   -617       C  
ATOM   1977  CG  LYS A 268     -22.752 -15.927   7.210  1.00 51.38           C  
ANISOU 1977  CG  LYS A 268     6022   6692   6809      3   -788   -654       C  
ATOM   1978  CD  LYS A 268     -22.829 -17.001   6.141  1.00 58.40           C  
ANISOU 1978  CD  LYS A 268     6954   7549   7685    -30   -856   -741       C  
ATOM   1979  CE  LYS A 268     -22.685 -16.461   4.735  1.00 67.33           C  
ANISOU 1979  CE  LYS A 268     8162   8732   8690      4   -942   -779       C  
ATOM   1980  NZ  LYS A 268     -22.565 -17.598   3.775  1.00 73.24           N  
ANISOU 1980  NZ  LYS A 268     8979   9444   9406    -21   -993   -878       N  
ATOM   1981  N   ASN A 269     -24.606 -18.067  11.067  1.00 51.36           N  
ANISOU 1981  N   ASN A 269     5777   6551   7188   -128   -560   -540       N  
ATOM   1982  CA  ASN A 269     -24.489 -18.797  12.332  1.00 51.67           C  
ANISOU 1982  CA  ASN A 269     5807   6542   7283   -147   -451   -479       C  
ATOM   1983  C   ASN A 269     -23.053 -18.793  12.852  1.00 46.49           C  
ANISOU 1983  C   ASN A 269     5251   5884   6527    -96   -393   -443       C  
ATOM   1984  O   ASN A 269     -22.550 -19.806  13.339  1.00 48.38           O  
ANISOU 1984  O   ASN A 269     5529   6062   6792   -108   -342   -418       O  
ATOM   1985  CB  ASN A 269     -25.017 -20.229  12.198  1.00 55.99           C  
ANISOU 1985  CB  ASN A 269     6326   6998   7951   -228   -454   -504       C  
ATOM   1986  CG  ASN A 269     -26.486 -20.276  11.805  1.00 66.93           C  
ANISOU 1986  CG  ASN A 269     7585   8386   9458   -292   -514   -536       C  
ATOM   1987  OD1 ASN A 269     -26.842 -20.820  10.758  1.00 73.81           O  
ANISOU 1987  OD1 ASN A 269     8449   9226  10370   -340   -615   -617       O  
ATOM   1988  ND2 ASN A 269     -27.344 -19.710  12.645  1.00 70.12           N  
ANISOU 1988  ND2 ASN A 269     7888   8832   9922   -289   -454   -478       N  
ATOM   1989  N   VAL A 270     -22.385 -17.645  12.752  1.00 37.21           N  
ANISOU 1989  N   VAL A 270     4115   4773   5250    -39   -406   -437       N  
ATOM   1990  CA  VAL A 270     -21.019 -17.475  13.236  1.00 42.33           C  
ANISOU 1990  CA  VAL A 270     4837   5434   5812      6   -365   -405       C  
ATOM   1991  C   VAL A 270     -20.980 -16.263  14.158  1.00 44.10           C  
ANISOU 1991  C   VAL A 270     5055   5714   5988     43   -331   -362       C  
ATOM   1992  O   VAL A 270     -21.652 -15.258  13.903  1.00 48.18           O  
ANISOU 1992  O   VAL A 270     5538   6267   6502     55   -359   -375       O  
ATOM   1993  CB  VAL A 270     -20.013 -17.302  12.076  1.00 50.76           C  
ANISOU 1993  CB  VAL A 270     5967   6517   6802     30   -415   -451       C  
ATOM   1994  CG1 VAL A 270     -18.591 -17.208  12.611  1.00 56.18           C  
ANISOU 1994  CG1 VAL A 270     6703   7217   7425     71   -372   -416       C  
ATOM   1995  CG2 VAL A 270     -20.129 -18.450  11.086  1.00 66.53           C  
ANISOU 1995  CG2 VAL A 270     7984   8457   8835      0   -453   -513       C  
ATOM   1996  N   VAL A 271     -20.202 -16.362  15.233  1.00 40.45           N  
ANISOU 1996  N   VAL A 271     4630   5255   5485     68   -275   -315       N  
ATOM   1997  CA  VAL A 271     -19.938 -15.237  16.124  1.00 54.01           C  
ANISOU 1997  CA  VAL A 271     6365   7021   7137    105   -251   -289       C  
ATOM   1998  C   VAL A 271     -18.588 -14.646  15.739  1.00 55.24           C  
ANISOU 1998  C   VAL A 271     6570   7202   7216    128   -289   -303       C  
ATOM   1999  O   VAL A 271     -17.631 -15.382  15.455  1.00 46.49           O  
ANISOU 1999  O   VAL A 271     5488   6078   6098    131   -294   -301       O  
ATOM   2000  CB  VAL A 271     -19.986 -15.667  17.609  1.00 62.35           C  
ANISOU 2000  CB  VAL A 271     7434   8074   8183    116   -175   -230       C  
ATOM   2001  CG1 VAL A 271     -18.795 -16.522  17.990  1.00 71.64           C  
ANISOU 2001  CG1 VAL A 271     8663   9232   9327    131   -168   -198       C  
ATOM   2002  CG2 VAL A 271     -20.070 -14.467  18.523  1.00 68.16           C  
ANISOU 2002  CG2 VAL A 271     8186   8857   8853    152   -151   -223       C  
ATOM   2003  N   TYR A 272     -18.518 -13.312  15.681  1.00 46.08           N  
ANISOU 2003  N   TYR A 272     5419   6074   6014    144   -311   -315       N  
ATOM   2004  CA  TYR A 272     -17.314 -12.663  15.167  1.00 36.57           C  
ANISOU 2004  CA  TYR A 272     4250   4888   4756    152   -344   -325       C  
ATOM   2005  C   TYR A 272     -16.192 -12.673  16.199  1.00 40.21           C  
ANISOU 2005  C   TYR A 272     4737   5366   5173    165   -329   -300       C  
ATOM   2006  O   TYR A 272     -15.043 -12.987  15.867  1.00 37.96           O  
ANISOU 2006  O   TYR A 272     4458   5090   4875    167   -342   -296       O  
ATOM   2007  CB  TYR A 272     -17.630 -11.233  14.717  1.00 39.70           C  
ANISOU 2007  CB  TYR A 272     4654   5297   5135    158   -374   -341       C  
ATOM   2008  CG  TYR A 272     -16.436 -10.499  14.144  1.00 42.68           C  
ANISOU 2008  CG  TYR A 272     5063   5685   5468    153   -397   -342       C  
ATOM   2009  CD1 TYR A 272     -15.861  -9.433  14.821  1.00 50.64           C  
ANISOU 2009  CD1 TYR A 272     6095   6698   6449    153   -401   -338       C  
ATOM   2010  CD2 TYR A 272     -15.879 -10.878  12.929  1.00 45.54           C  
ANISOU 2010  CD2 TYR A 272     5434   6051   5819    144   -411   -349       C  
ATOM   2011  CE1 TYR A 272     -14.771  -8.760  14.302  1.00 60.93           C  
ANISOU 2011  CE1 TYR A 272     7415   8005   7732    134   -417   -333       C  
ATOM   2012  CE2 TYR A 272     -14.786 -10.212  12.403  1.00 42.06           C  
ANISOU 2012  CE2 TYR A 272     5013   5623   5345    135   -414   -339       C  
ATOM   2013  CZ  TYR A 272     -14.236  -9.154  13.095  1.00 53.97           C  
ANISOU 2013  CZ  TYR A 272     6530   7133   6844    125   -417   -327       C  
ATOM   2014  OH  TYR A 272     -13.150  -8.480  12.588  1.00 50.18           O  
ANISOU 2014  OH  TYR A 272     6058   6660   6350    102   -415   -312       O  
ATOM   2015  N   ARG A 273     -16.504 -12.291  17.442  1.00 47.45           N  
ANISOU 2015  N   ARG A 273     5668   6296   6066    180   -305   -285       N  
ATOM   2016  CA  ARG A 273     -15.649 -12.473  18.618  1.00 54.46           C  
ANISOU 2016  CA  ARG A 273     6584   7205   6902    197   -301   -258       C  
ATOM   2017  C   ARG A 273     -14.460 -11.513  18.679  1.00 61.86           C  
ANISOU 2017  C   ARG A 273     7538   8168   7796    192   -350   -276       C  
ATOM   2018  O   ARG A 273     -13.890 -11.306  19.755  1.00 70.98           O  
ANISOU 2018  O   ARG A 273     8720   9348   8899    205   -366   -269       O  
ATOM   2019  CB  ARG A 273     -15.156 -13.924  18.699  1.00 59.46           C  
ANISOU 2019  CB  ARG A 273     7213   7822   7556    205   -286   -221       C  
ATOM   2020  CG  ARG A 273     -14.455 -14.301  19.997  1.00 67.09           C  
ANISOU 2020  CG  ARG A 273     8212   8811   8468    235   -285   -178       C  
ATOM   2021  CD  ARG A 273     -14.266 -15.807  20.106  1.00 74.32           C  
ANISOU 2021  CD  ARG A 273     9129   9691   9419    252   -259   -128       C  
ATOM   2022  NE  ARG A 273     -12.895 -16.176  20.452  1.00 83.52           N  
ANISOU 2022  NE  ARG A 273    10299  10878  10557    287   -299   -101       N  
ATOM   2023  CZ  ARG A 273     -12.484 -17.426  20.648  1.00 92.94           C  
ANISOU 2023  CZ  ARG A 273    11500  12038  11777    320   -286    -51       C  
ATOM   2024  NH1 ARG A 273     -13.337 -18.433  20.541  1.00 88.89           N  
ANISOU 2024  NH1 ARG A 273    10997  11457  11319    311   -231    -25       N  
ATOM   2025  NH2 ARG A 273     -11.218 -17.673  20.955  1.00102.87           N  
ANISOU 2025  NH2 ARG A 273    12748  13323  13016    362   -331    -25       N  
ATOM   2026  N   ASP A 274     -14.078 -10.909  17.557  1.00 62.74           N  
ANISOU 2026  N   ASP A 274     7636   8274   7928    171   -376   -298       N  
ATOM   2027  CA  ASP A 274     -12.933 -10.003  17.507  1.00 69.30           C  
ANISOU 2027  CA  ASP A 274     8469   9121   8740    151   -415   -309       C  
ATOM   2028  C   ASP A 274     -13.356  -8.572  17.190  1.00 55.22           C  
ANISOU 2028  C   ASP A 274     6709   7314   6957    133   -429   -336       C  
ATOM   2029  O   ASP A 274     -12.633  -7.831  16.521  1.00 55.39           O  
ANISOU 2029  O   ASP A 274     6728   7329   6990    104   -449   -338       O  
ATOM   2030  CB  ASP A 274     -11.901 -10.491  16.493  1.00 84.34           C  
ANISOU 2030  CB  ASP A 274    10338  11037  10671    140   -419   -297       C  
ATOM   2031  CG  ASP A 274     -10.782 -11.295  17.134  1.00 95.46           C  
ANISOU 2031  CG  ASP A 274    11720  12474  12078    157   -432   -274       C  
ATOM   2032  OD1 ASP A 274     -10.816 -11.494  18.366  1.00 98.82           O  
ANISOU 2032  OD1 ASP A 274    12164  12913  12471    177   -447   -262       O  
ATOM   2033  OD2 ASP A 274      -9.863 -11.723  16.402  1.00 99.33           O  
ANISOU 2033  OD2 ASP A 274    12170  12976  12594    160   -425   -265       O  
ATOM   2034  N   LEU A 275     -14.530  -8.163  17.668  1.00 36.10           N  
ANISOU 2034  N   LEU A 275     4311   4876   4531    155   -410   -351       N  
ATOM   2035  CA  LEU A 275     -15.035  -6.820  17.399  1.00 43.70           C  
ANISOU 2035  CA  LEU A 275     5300   5803   5501    155   -421   -374       C  
ATOM   2036  C   LEU A 275     -14.294  -5.818  18.278  1.00 51.43           C  
ANISOU 2036  C   LEU A 275     6321   6770   6449    139   -451   -404       C  
ATOM   2037  O   LEU A 275     -14.458  -5.812  19.501  1.00 54.76           O  
ANISOU 2037  O   LEU A 275     6775   7206   6827    161   -445   -426       O  
ATOM   2038  CB  LEU A 275     -16.540  -6.750  17.636  1.00 45.90           C  
ANISOU 2038  CB  LEU A 275     5575   6068   5796    195   -386   -382       C  
ATOM   2039  CG  LEU A 275     -17.201  -5.414  17.274  1.00 47.49           C  
ANISOU 2039  CG  LEU A 275     5799   6226   6019    215   -396   -402       C  
ATOM   2040  CD1 LEU A 275     -16.789  -4.999  15.874  1.00 52.32           C  
ANISOU 2040  CD1 LEU A 275     6411   6818   6652    190   -431   -382       C  
ATOM   2041  CD2 LEU A 275     -18.714  -5.492  17.379  1.00 43.10           C  
ANISOU 2041  CD2 LEU A 275     5210   5669   5499    262   -360   -404       C  
ATOM   2042  N   LYS A 276     -13.468  -4.982  17.653  1.00 46.92           N  
ANISOU 2042  N   LYS A 276     5754   6174   5899     97   -483   -406       N  
ATOM   2043  CA  LYS A 276     -12.727  -3.940  18.346  1.00 46.86           C  
ANISOU 2043  CA  LYS A 276     5782   6141   5881     64   -523   -443       C  
ATOM   2044  C   LYS A 276     -12.441  -2.821  17.356  1.00 47.31           C  
ANISOU 2044  C   LYS A 276     5851   6138   5985     24   -534   -434       C  
ATOM   2045  O   LYS A 276     -12.582  -2.994  16.143  1.00 43.53           O  
ANISOU 2045  O   LYS A 276     5351   5657   5529     23   -512   -391       O  
ATOM   2046  CB  LYS A 276     -11.428  -4.480  18.955  1.00 46.28           C  
ANISOU 2046  CB  LYS A 276     5678   6118   5790     33   -564   -442       C  
ATOM   2047  CG  LYS A 276     -10.549  -5.235  17.978  1.00 48.16           C  
ANISOU 2047  CG  LYS A 276     5845   6389   6065     10   -556   -395       C  
ATOM   2048  CD  LYS A 276      -9.282  -5.746  18.642  1.00 51.89           C  
ANISOU 2048  CD  LYS A 276     6270   6912   6532     -8   -601   -392       C  
ATOM   2049  CE  LYS A 276      -8.465  -6.584  17.678  1.00 58.36           C  
ANISOU 2049  CE  LYS A 276     7013   7766   7394    -13   -575   -347       C  
ATOM   2050  NZ  LYS A 276      -7.194  -7.048  18.289  1.00 60.83           N  
ANISOU 2050  NZ  LYS A 276     7263   8132   7719    -20   -624   -339       N  
ATOM   2051  N   LEU A 277     -12.038  -1.668  17.894  1.00 51.00           N  
ANISOU 2051  N   LEU A 277     6364   6553   6463    -10   -569   -474       N  
ATOM   2052  CA  LEU A 277     -11.802  -0.493  17.061  1.00 52.55           C  
ANISOU 2052  CA  LEU A 277     6585   6670   6712    -53   -573   -459       C  
ATOM   2053  C   LEU A 277     -10.760  -0.760  15.980  1.00 50.05           C  
ANISOU 2053  C   LEU A 277     6209   6378   6430   -110   -563   -400       C  
ATOM   2054  O   LEU A 277     -10.864  -0.219  14.872  1.00 46.69           O  
ANISOU 2054  O   LEU A 277     5798   5910   6030   -122   -538   -353       O  
ATOM   2055  CB  LEU A 277     -11.372   0.683  17.940  1.00 46.37           C  
ANISOU 2055  CB  LEU A 277     5858   5817   5943    -94   -619   -522       C  
ATOM   2056  CG  LEU A 277     -11.640   2.094  17.420  1.00 58.08           C  
ANISOU 2056  CG  LEU A 277     7406   7181   7482   -111   -617   -521       C  
ATOM   2057  CD1 LEU A 277     -13.137   2.343  17.294  1.00 54.63           C  
ANISOU 2057  CD1 LEU A 277     7015   6708   7033    -16   -581   -523       C  
ATOM   2058  CD2 LEU A 277     -10.994   3.114  18.344  1.00 61.77           C  
ANISOU 2058  CD2 LEU A 277     7926   7576   7970   -170   -673   -597       C  
ATOM   2059  N   GLU A 278      -9.761  -1.596  16.274  1.00 40.36           N  
ANISOU 2059  N   GLU A 278     4915   5221   5198   -136   -577   -396       N  
ATOM   2060  CA  GLU A 278      -8.703  -1.888  15.315  1.00 39.41           C  
ANISOU 2060  CA  GLU A 278     4727   5132   5114   -182   -552   -344       C  
ATOM   2061  C   GLU A 278      -9.184  -2.719  14.136  1.00 46.98           C  
ANISOU 2061  C   GLU A 278     5676   6124   6049   -137   -495   -297       C  
ATOM   2062  O   GLU A 278      -8.468  -2.812  13.136  1.00 43.59           O  
ANISOU 2062  O   GLU A 278     5212   5713   5638   -165   -456   -251       O  
ATOM   2063  CB  GLU A 278      -7.543  -2.610  16.007  1.00 47.03           C  
ANISOU 2063  CB  GLU A 278     5614   6167   6090   -206   -586   -354       C  
ATOM   2064  CG  GLU A 278      -6.841  -1.800  17.091  1.00 53.06           C  
ANISOU 2064  CG  GLU A 278     6377   6907   6877   -265   -662   -406       C  
ATOM   2065  CD  GLU A 278      -7.456  -1.982  18.472  1.00 57.76           C  
ANISOU 2065  CD  GLU A 278     7030   7514   7400   -217   -712   -467       C  
ATOM   2066  OE1 GLU A 278      -8.629  -2.410  18.562  1.00 52.99           O  
ANISOU 2066  OE1 GLU A 278     6477   6911   6745   -145   -673   -468       O  
ATOM   2067  OE2 GLU A 278      -6.759  -1.701  19.473  1.00 65.34           O  
ANISOU 2067  OE2 GLU A 278     7985   8486   8354   -252   -789   -514       O  
ATOM   2068  N   ASN A 279     -10.364  -3.330  14.227  1.00 45.28           N  
ANISOU 2068  N   ASN A 279     5488   5920   5795    -70   -488   -310       N  
ATOM   2069  CA  ASN A 279     -10.920  -4.109  13.132  1.00 43.72           C  
ANISOU 2069  CA  ASN A 279     5289   5749   5575    -32   -453   -281       C  
ATOM   2070  C   ASN A 279     -12.038  -3.370  12.408  1.00 47.97           C  
ANISOU 2070  C   ASN A 279     5883   6239   6105     -5   -454   -266       C  
ATOM   2071  O   ASN A 279     -12.851  -3.999  11.724  1.00 42.88           O  
ANISOU 2071  O   ASN A 279     5242   5615   5436     36   -449   -259       O  
ATOM   2072  CB  ASN A 279     -11.417  -5.461  13.643  1.00 48.31           C  
ANISOU 2072  CB  ASN A 279     5845   6375   6135     15   -451   -300       C  
ATOM   2073  CG  ASN A 279     -10.283  -6.385  14.050  1.00 52.83           C  
ANISOU 2073  CG  ASN A 279     6361   6997   6714      6   -447   -297       C  
ATOM   2074  OD1 ASN A 279      -9.128  -6.179  13.672  1.00 51.41           O  
ANISOU 2074  OD1 ASN A 279     6142   6832   6558    -31   -438   -278       O  
ATOM   2075  ND2 ASN A 279     -10.610  -7.417  14.818  1.00 59.05           N  
ANISOU 2075  ND2 ASN A 279     7139   7808   7489     43   -450   -308       N  
ATOM   2076  N   LEU A 280     -12.097  -2.050  12.550  1.00 36.82           N  
ANISOU 2076  N   LEU A 280     4514   4758   4717    -26   -468   -264       N  
ATOM   2077  CA  LEU A 280     -13.099  -1.227  11.889  1.00 50.71           C  
ANISOU 2077  CA  LEU A 280     6329   6462   6476     10   -475   -241       C  
ATOM   2078  C   LEU A 280     -12.402  -0.247  10.961  1.00 42.74           C  
ANISOU 2078  C   LEU A 280     5356   5403   5482    -36   -458   -182       C  
ATOM   2079  O   LEU A 280     -11.428   0.403  11.356  1.00 41.57           O  
ANISOU 2079  O   LEU A 280     5203   5216   5374   -103   -455   -183       O  
ATOM   2080  CB  LEU A 280     -13.956  -0.472  12.905  1.00 48.02           C  
ANISOU 2080  CB  LEU A 280     6024   6065   6158     45   -498   -286       C  
ATOM   2081  CG  LEU A 280     -14.887  -1.322  13.768  1.00 48.15           C  
ANISOU 2081  CG  LEU A 280     6010   6125   6159     99   -496   -329       C  
ATOM   2082  CD1 LEU A 280     -15.648  -0.433  14.730  1.00 43.78           C  
ANISOU 2082  CD1 LEU A 280     5498   5514   5623    140   -500   -374       C  
ATOM   2083  CD2 LEU A 280     -15.846  -2.117  12.898  1.00 33.21           C  
ANISOU 2083  CD2 LEU A 280     4089   4275   4256    145   -495   -306       C  
ATOM   2084  N   MET A 281     -12.898  -0.151   9.730  1.00 45.56           N  
ANISOU 2084  N   MET A 281     5747   5759   5804     -5   -450   -129       N  
ATOM   2085  CA  MET A 281     -12.383   0.798   8.756  1.00 48.01           C  
ANISOU 2085  CA  MET A 281     6109   6018   6115    -39   -423    -54       C  
ATOM   2086  C   MET A 281     -13.553   1.448   8.033  1.00 50.37           C  
ANISOU 2086  C   MET A 281     6476   6270   6392     28   -453    -13       C  
ATOM   2087  O   MET A 281     -14.694   0.983   8.104  1.00 57.60           O  
ANISOU 2087  O   MET A 281     7381   7215   7290     98   -493    -43       O  
ATOM   2088  CB  MET A 281     -11.448   0.126   7.743  1.00 48.90           C  
ANISOU 2088  CB  MET A 281     6198   6199   6182    -69   -367     -9       C  
ATOM   2089  CG  MET A 281     -10.306  -0.654   8.355  1.00 47.06           C  
ANISOU 2089  CG  MET A 281     5881   6024   5977   -118   -340    -43       C  
ATOM   2090  SD  MET A 281      -9.150  -1.227   7.096  1.00 60.65           S  
ANISOU 2090  SD  MET A 281     7574   7813   7655   -144   -251     16       S  
ATOM   2091  CE  MET A 281      -8.375   0.317   6.622  1.00 58.70           C  
ANISOU 2091  CE  MET A 281     7361   7483   7458   -226   -203    103       C  
ATOM   2092  N   LEU A 282     -13.258   2.537   7.331  1.00 52.25           N  
ANISOU 2092  N   LEU A 282     6781   6434   6638      7   -434     63       N  
ATOM   2093  CA  LEU A 282     -14.212   3.190   6.448  1.00 51.94           C  
ANISOU 2093  CA  LEU A 282     6816   6352   6568     76   -464    126       C  
ATOM   2094  C   LEU A 282     -13.795   2.986   4.998  1.00 48.23           C  
ANISOU 2094  C   LEU A 282     6389   5928   6007     71   -428    212       C  
ATOM   2095  O   LEU A 282     -12.604   2.982   4.674  1.00 48.92           O  
ANISOU 2095  O   LEU A 282     6470   6028   6090     -3   -357    250       O  
ATOM   2096  CB  LEU A 282     -14.306   4.689   6.742  1.00 50.20           C  
ANISOU 2096  CB  LEU A 282     6664   5989   6420     69   -470    159       C  
ATOM   2097  CG  LEU A 282     -14.704   5.129   8.149  1.00 46.34           C  
ANISOU 2097  CG  LEU A 282     6162   5434   6012     81   -497     70       C  
ATOM   2098  CD1 LEU A 282     -14.675   6.648   8.227  1.00 44.48           C  
ANISOU 2098  CD1 LEU A 282     6013   5040   5848     71   -497    107       C  
ATOM   2099  CD2 LEU A 282     -16.080   4.593   8.509  1.00 55.10           C  
ANISOU 2099  CD2 LEU A 282     7236   6591   7108    183   -543     17       C  
ATOM   2100  N   ASP A 283     -14.779   2.816   4.120  1.00 48.13           N  
ANISOU 2100  N   ASP A 283     6417   5948   5921    152   -477    242       N  
ATOM   2101  CA  ASP A 283     -14.481   2.785   2.695  1.00 50.53           C  
ANISOU 2101  CA  ASP A 283     6792   6291   6116    160   -449    330       C  
ATOM   2102  C   ASP A 283     -14.365   4.223   2.192  1.00 53.03           C  
ANISOU 2102  C   ASP A 283     7206   6497   6447    157   -430    443       C  
ATOM   2103  O   ASP A 283     -14.348   5.178   2.973  1.00 64.19           O  
ANISOU 2103  O   ASP A 283     8626   7798   7966    134   -432    443       O  
ATOM   2104  CB  ASP A 283     -15.527   1.975   1.928  1.00 53.10           C  
ANISOU 2104  CB  ASP A 283     7128   6703   6345    243   -525    310       C  
ATOM   2105  CG  ASP A 283     -16.949   2.457   2.165  1.00 67.28           C  
ANISOU 2105  CG  ASP A 283     8924   8458   8182    328   -626    302       C  
ATOM   2106  OD1 ASP A 283     -17.793   1.628   2.564  1.00 70.53           O  
ANISOU 2106  OD1 ASP A 283     9262   8925   8611    363   -686    221       O  
ATOM   2107  OD2 ASP A 283     -17.228   3.657   1.954  1.00 71.74           O  
ANISOU 2107  OD2 ASP A 283     9556   8931   8769    361   -641    380       O  
ATOM   2108  N   LYS A 284     -14.288   4.391   0.870  1.00 50.28           N  
ANISOU 2108  N   LYS A 284     6946   6172   5986    182   -410    543       N  
ATOM   2109  CA  LYS A 284     -14.130   5.726   0.303  1.00 53.04           C  
ANISOU 2109  CA  LYS A 284     7401   6411   6341    178   -381    673       C  
ATOM   2110  C   LYS A 284     -15.330   6.618   0.601  1.00 50.64           C  
ANISOU 2110  C   LYS A 284     7136   6008   6097    264   -475    687       C  
ATOM   2111  O   LYS A 284     -15.183   7.840   0.704  1.00 65.63           O  
ANISOU 2111  O   LYS A 284     9101   7769   8069    249   -454    761       O  
ATOM   2112  CB  LYS A 284     -13.908   5.626  -1.206  1.00 57.10           C  
ANISOU 2112  CB  LYS A 284     8014   6987   6695    204   -343    782       C  
ATOM   2113  CG  LYS A 284     -15.160   5.295  -2.000  1.00 63.13           C  
ANISOU 2113  CG  LYS A 284     8831   7816   7339    324   -458    788       C  
ATOM   2114  CD  LYS A 284     -14.899   5.363  -3.492  1.00 59.43           C  
ANISOU 2114  CD  LYS A 284     8488   7400   6693    352   -421    906       C  
ATOM   2115  CE  LYS A 284     -16.185   5.288  -4.284  1.00 58.88           C  
ANISOU 2115  CE  LYS A 284     8486   7378   6509    475   -561    926       C  
ATOM   2116  NZ  LYS A 284     -16.846   6.621  -4.401  1.00 62.75           N  
ANISOU 2116  NZ  LYS A 284     9055   7745   7043    539   -618   1040       N  
ATOM   2117  N   ASP A 285     -16.518   6.029   0.750  1.00 47.70           N  
ANISOU 2117  N   ASP A 285     6719   5698   5707    354   -576    618       N  
ATOM   2118  CA  ASP A 285     -17.732   6.807   0.967  1.00 48.51           C  
ANISOU 2118  CA  ASP A 285     6841   5721   5867    454   -664    632       C  
ATOM   2119  C   ASP A 285     -17.955   7.164   2.429  1.00 52.30           C  
ANISOU 2119  C   ASP A 285     7255   6120   6496    443   -663    539       C  
ATOM   2120  O   ASP A 285     -18.727   8.084   2.715  1.00 61.09           O  
ANISOU 2120  O   ASP A 285     8399   7132   7683    518   -705    558       O  
ATOM   2121  CB  ASP A 285     -18.948   6.041   0.439  1.00 61.13           C  
ANISOU 2121  CB  ASP A 285     8405   7429   7392    554   -777    603       C  
ATOM   2122  CG  ASP A 285     -18.833   5.714  -1.035  1.00 82.05           C  
ANISOU 2122  CG  ASP A 285    11141  10162   9873    578   -796    684       C  
ATOM   2123  OD1 ASP A 285     -18.295   6.555  -1.789  1.00 88.09           O  
ANISOU 2123  OD1 ASP A 285    12022  10865  10582    570   -748    811       O  
ATOM   2124  OD2 ASP A 285     -19.279   4.620  -1.441  1.00 86.12           O  
ANISOU 2124  OD2 ASP A 285    11615  10800  10306    602   -858    622       O  
ATOM   2125  N   GLY A 286     -17.307   6.464   3.355  1.00 47.48           N  
ANISOU 2125  N   GLY A 286     6562   5553   5926    363   -617    440       N  
ATOM   2126  CA  GLY A 286     -17.505   6.694   4.768  1.00 55.66           C  
ANISOU 2126  CA  GLY A 286     7545   6531   7074    356   -617    343       C  
ATOM   2127  C   GLY A 286     -18.324   5.645   5.490  1.00 54.21           C  
ANISOU 2127  C   GLY A 286     7256   6444   6898    400   -656    236       C  
ATOM   2128  O   GLY A 286     -18.678   5.859   6.655  1.00 47.11           O  
ANISOU 2128  O   GLY A 286     6320   5501   6077    415   -654    160       O  
ATOM   2129  N   HIS A 287     -18.641   4.525   4.846  1.00 54.68           N  
ANISOU 2129  N   HIS A 287     7271   6627   6878    418   -688    227       N  
ATOM   2130  CA  HIS A 287     -19.383   3.456   5.496  1.00 51.16           C  
ANISOU 2130  CA  HIS A 287     6722   6266   6450    443   -718    133       C  
ATOM   2131  C   HIS A 287     -18.425   2.501   6.197  1.00 50.09           C  
ANISOU 2131  C   HIS A 287     6534   6188   6312    355   -659     66       C  
ATOM   2132  O   HIS A 287     -17.260   2.364   5.815  1.00 56.44           O  
ANISOU 2132  O   HIS A 287     7365   7004   7075    284   -609     94       O  
ATOM   2133  CB  HIS A 287     -20.241   2.694   4.485  1.00 43.54           C  
ANISOU 2133  CB  HIS A 287     5732   5394   5415    499   -794    146       C  
ATOM   2134  CG  HIS A 287     -21.358   3.507   3.910  1.00 56.40           C  
ANISOU 2134  CG  HIS A 287     7388   6985   7055    603   -875    205       C  
ATOM   2135  ND1 HIS A 287     -22.527   3.758   4.597  1.00 59.73           N  
ANISOU 2135  ND1 HIS A 287     7737   7386   7571    681   -915    167       N  
ATOM   2136  CD2 HIS A 287     -21.487   4.124   2.711  1.00 56.58           C  
ANISOU 2136  CD2 HIS A 287     7500   6992   7006    651   -922    305       C  
ATOM   2137  CE1 HIS A 287     -23.326   4.496   3.848  1.00 57.45           C  
ANISOU 2137  CE1 HIS A 287     7482   7067   7279    776   -991    239       C  
ATOM   2138  NE2 HIS A 287     -22.718   4.733   2.699  1.00 59.58           N  
ANISOU 2138  NE2 HIS A 287     7856   7337   7443    759  -1002    326       N  
ATOM   2139  N   ILE A 288     -18.936   1.836   7.234  1.00 56.48           N  
ANISOU 2139  N   ILE A 288     7262   7031   7166    366   -661    -17       N  
ATOM   2140  CA  ILE A 288     -18.112   0.947   8.043  1.00 48.86           C  
ANISOU 2140  CA  ILE A 288     6249   6112   6202    297   -614    -76       C  
ATOM   2141  C   ILE A 288     -17.787  -0.321   7.264  1.00 42.62           C  
ANISOU 2141  C   ILE A 288     5434   5417   5344    272   -614    -79       C  
ATOM   2142  O   ILE A 288     -18.632  -0.868   6.542  1.00 50.44           O  
ANISOU 2142  O   ILE A 288     6407   6454   6302    315   -665    -79       O  
ATOM   2143  CB  ILE A 288     -18.831   0.624   9.366  1.00 41.73           C  
ANISOU 2143  CB  ILE A 288     5283   5216   5356    325   -609   -151       C  
ATOM   2144  CG1 ILE A 288     -18.576   1.720  10.400  1.00 54.40           C  
ANISOU 2144  CG1 ILE A 288     6928   6730   7011    320   -583   -175       C  
ATOM   2145  CG2 ILE A 288     -18.404  -0.734   9.915  1.00 48.66           C  
ANISOU 2145  CG2 ILE A 288     6100   6172   6217    280   -582   -199       C  
ATOM   2146  CD1 ILE A 288     -17.155   1.745  10.921  1.00 53.55           C  
ANISOU 2146  CD1 ILE A 288     6839   6612   6897    230   -549   -192       C  
ATOM   2147  N   LYS A 289     -16.549  -0.790   7.402  1.00 48.54           N  
ANISOU 2147  N   LYS A 289     6177   6192   6076    205   -562    -86       N  
ATOM   2148  CA  LYS A 289     -16.144  -2.111   6.938  1.00 47.42           C  
ANISOU 2148  CA  LYS A 289     6005   6130   5883    186   -547   -108       C  
ATOM   2149  C   LYS A 289     -15.532  -2.864   8.111  1.00 55.34           C  
ANISOU 2149  C   LYS A 289     6947   7154   6925    148   -513   -162       C  
ATOM   2150  O   LYS A 289     -14.553  -2.400   8.702  1.00 48.37           O  
ANISOU 2150  O   LYS A 289     6063   6246   6069    102   -479   -157       O  
ATOM   2151  CB  LYS A 289     -15.142  -2.016   5.786  1.00 46.27           C  
ANISOU 2151  CB  LYS A 289     5910   6003   5667    156   -506    -52       C  
ATOM   2152  CG  LYS A 289     -15.661  -2.518   4.448  1.00 62.00           C  
ANISOU 2152  CG  LYS A 289     7945   8046   7567    198   -540    -36       C  
ATOM   2153  CD  LYS A 289     -16.822  -1.680   3.946  1.00 66.82           C  
ANISOU 2153  CD  LYS A 289     8598   8624   8165    258   -614      3       C  
ATOM   2154  CE  LYS A 289     -17.174  -2.038   2.509  1.00 67.01           C  
ANISOU 2154  CE  LYS A 289     8684   8704   8074    296   -658     27       C  
ATOM   2155  NZ  LYS A 289     -17.643  -3.443   2.378  1.00 55.05           N  
ANISOU 2155  NZ  LYS A 289     7123   7256   6536    303   -699    -56       N  
ATOM   2156  N   ILE A 290     -16.106  -4.014   8.449  1.00 47.24           N  
ANISOU 2156  N   ILE A 290     5872   6172   5906    166   -526   -209       N  
ATOM   2157  CA  ILE A 290     -15.535  -4.895   9.460  1.00 36.15           C  
ANISOU 2157  CA  ILE A 290     4419   4791   4526    140   -495   -247       C  
ATOM   2158  C   ILE A 290     -14.535  -5.812   8.767  1.00 43.08           C  
ANISOU 2158  C   ILE A 290     5292   5711   5365    118   -463   -244       C  
ATOM   2159  O   ILE A 290     -14.886  -6.522   7.817  1.00 45.84           O  
ANISOU 2159  O   ILE A 290     5654   6088   5674    137   -475   -253       O  
ATOM   2160  CB  ILE A 290     -16.621  -5.702  10.185  1.00 43.89           C  
ANISOU 2160  CB  ILE A 290     5352   5784   5540    167   -511   -287       C  
ATOM   2161  CG1 ILE A 290     -17.643  -4.761  10.823  1.00 40.90           C  
ANISOU 2161  CG1 ILE A 290     4972   5368   5200    202   -528   -291       C  
ATOM   2162  CG2 ILE A 290     -15.999  -6.596  11.242  1.00 38.40           C  
ANISOU 2162  CG2 ILE A 290     4623   5108   4859    147   -477   -310       C  
ATOM   2163  CD1 ILE A 290     -18.783  -5.487  11.493  1.00 47.61           C  
ANISOU 2163  CD1 ILE A 290     5763   6235   6092    228   -527   -320       C  
ATOM   2164  N   THR A 291     -13.295  -5.806   9.248  1.00 36.62           N  
ANISOU 2164  N   THR A 291     4453   4900   4561     82   -424   -237       N  
ATOM   2165  CA  THR A 291     -12.200  -6.471   8.558  1.00 43.04           C  
ANISOU 2165  CA  THR A 291     5254   5752   5348     69   -378   -226       C  
ATOM   2166  C   THR A 291     -12.083  -7.933   8.982  1.00 53.39           C  
ANISOU 2166  C   THR A 291     6524   7091   6670     87   -369   -265       C  
ATOM   2167  O   THR A 291     -12.574  -8.344  10.036  1.00 40.88           O  
ANISOU 2167  O   THR A 291     4915   5498   5120     96   -391   -289       O  
ATOM   2168  CB  THR A 291     -10.882  -5.740   8.823  1.00 42.10           C  
ANISOU 2168  CB  THR A 291     5111   5627   5257     20   -343   -194       C  
ATOM   2169  OG1 THR A 291     -10.541  -5.855  10.210  1.00 46.74           O  
ANISOU 2169  OG1 THR A 291     5652   6213   5894      4   -364   -221       O  
ATOM   2170  CG2 THR A 291     -11.017  -4.267   8.458  1.00 45.16           C  
ANISOU 2170  CG2 THR A 291     5548   5963   5647     -5   -349   -151       C  
ATOM   2171  N   ASP A 292     -11.421  -8.721   8.134  1.00 57.47           N  
ANISOU 2171  N   ASP A 292     7041   7638   7156     98   -329   -269       N  
ATOM   2172  CA  ASP A 292     -11.101 -10.116   8.428  1.00 49.17           C  
ANISOU 2172  CA  ASP A 292     5958   6601   6124    121   -311   -302       C  
ATOM   2173  C   ASP A 292      -9.651 -10.373   8.028  1.00 44.91           C  
ANISOU 2173  C   ASP A 292     5387   6095   5583    123   -245   -285       C  
ATOM   2174  O   ASP A 292      -9.347 -11.159   7.133  1.00 61.33           O  
ANISOU 2174  O   ASP A 292     7485   8191   7628    154   -203   -305       O  
ATOM   2175  CB  ASP A 292     -12.072 -11.067   7.727  1.00 47.92           C  
ANISOU 2175  CB  ASP A 292     5836   6433   5937    149   -333   -346       C  
ATOM   2176  CG  ASP A 292     -11.733 -12.533   7.958  1.00 65.35           C  
ANISOU 2176  CG  ASP A 292     8024   8632   8172    173   -309   -381       C  
ATOM   2177  OD1 ASP A 292     -12.012 -13.356   7.059  1.00 67.11           O  
ANISOU 2177  OD1 ASP A 292     8286   8849   8365    193   -308   -424       O  
ATOM   2178  OD2 ASP A 292     -11.166 -12.858   9.020  1.00 70.99           O  
ANISOU 2178  OD2 ASP A 292     8692   9344   8937    175   -296   -365       O  
ATOM   2179  N   PHE A 293      -8.741  -9.672   8.704  1.00 47.71           N  
ANISOU 2179  N   PHE A 293     5690   6459   5981     90   -236   -252       N  
ATOM   2180  CA  PHE A 293      -7.314  -9.736   8.411  1.00 50.67           C  
ANISOU 2180  CA  PHE A 293     6006   6870   6377     84   -174   -227       C  
ATOM   2181  C   PHE A 293      -6.537 -10.486   9.485  1.00 61.38           C  
ANISOU 2181  C   PHE A 293     7282   8244   7795    101   -185   -234       C  
ATOM   2182  O   PHE A 293      -5.303 -10.533   9.427  1.00 65.25           O  
ANISOU 2182  O   PHE A 293     7696   8770   8325     98   -144   -212       O  
ATOM   2183  CB  PHE A 293      -6.729  -8.326   8.245  1.00 42.88           C  
ANISOU 2183  CB  PHE A 293     5005   5881   5407     22   -158   -179       C  
ATOM   2184  CG  PHE A 293      -7.471  -7.460   7.254  1.00 51.20           C  
ANISOU 2184  CG  PHE A 293     6144   6909   6399     10   -152   -154       C  
ATOM   2185  CD1 PHE A 293      -7.506  -6.084   7.417  1.00 49.43           C  
ANISOU 2185  CD1 PHE A 293     5937   6645   6198    -43   -169   -116       C  
ATOM   2186  CD2 PHE A 293      -8.113  -8.014   6.153  1.00 50.31           C  
ANISOU 2186  CD2 PHE A 293     6101   6808   6204     55   -135   -170       C  
ATOM   2187  CE1 PHE A 293      -8.176  -5.275   6.517  1.00 50.76           C  
ANISOU 2187  CE1 PHE A 293     6190   6784   6311    -43   -167    -81       C  
ATOM   2188  CE2 PHE A 293      -8.787  -7.207   5.249  1.00 54.40           C  
ANISOU 2188  CE2 PHE A 293     6702   7310   6657     53   -144   -139       C  
ATOM   2189  CZ  PHE A 293      -8.816  -5.838   5.431  1.00 56.54           C  
ANISOU 2189  CZ  PHE A 293     6988   7540   6955      8   -157    -88       C  
ATOM   2190  N   GLY A 294      -7.228 -11.068  10.469  1.00 65.20           N  
ANISOU 2190  N   GLY A 294     7778   8706   8290    121   -239   -256       N  
ATOM   2191  CA  GLY A 294      -6.549 -11.686  11.586  1.00 53.62           C  
ANISOU 2191  CA  GLY A 294     6249   7255   6869    142   -263   -250       C  
ATOM   2192  C   GLY A 294      -6.011 -13.070  11.269  1.00 58.72           C  
ANISOU 2192  C   GLY A 294     6870   7908   7534    207   -219   -257       C  
ATOM   2193  O   GLY A 294      -6.435 -13.744  10.330  1.00 61.89           O  
ANISOU 2193  O   GLY A 294     7318   8289   7908    237   -179   -284       O  
ATOM   2194  N   LEU A 295      -5.042 -13.488  12.080  1.00 59.12           N  
ANISOU 2194  N   LEU A 295     6845   7984   7633    232   -235   -235       N  
ATOM   2195  CA  LEU A 295      -4.481 -14.830  12.021  1.00 63.53           C  
ANISOU 2195  CA  LEU A 295     7375   8539   8226    308   -203   -235       C  
ATOM   2196  C   LEU A 295      -4.115 -15.264  13.431  1.00 69.14           C  
ANISOU 2196  C   LEU A 295     8045   9258   8969    337   -267   -205       C  
ATOM   2197  O   LEU A 295      -3.667 -14.449  14.241  1.00 73.05           O  
ANISOU 2197  O   LEU A 295     8494   9790   9471    299   -326   -186       O  
ATOM   2198  CB  LEU A 295      -3.245 -14.898  11.117  1.00 65.12           C  
ANISOU 2198  CB  LEU A 295     7501   8784   8459    333   -127   -228       C  
ATOM   2199  CG  LEU A 295      -3.503 -15.042   9.618  1.00 66.68           C  
ANISOU 2199  CG  LEU A 295     7757   8971   8606    345    -42   -260       C  
ATOM   2200  CD1 LEU A 295      -2.204 -15.335   8.886  1.00 65.68           C  
ANISOU 2200  CD1 LEU A 295     7551   8891   8515    391     52   -250       C  
ATOM   2201  CD2 LEU A 295      -4.535 -16.130   9.358  1.00 70.04           C  
ANISOU 2201  CD2 LEU A 295     8280   9332   9000    387    -45   -308       C  
ATOM   2202  N   CYS A 296      -4.310 -16.549  13.715  1.00 80.30           N  
ANISOU 2202  N   CYS A 296     9484  10630  10397    404   -260   -201       N  
ATOM   2203  CA  CYS A 296      -3.961 -17.077  15.027  1.00 79.76           C  
ANISOU 2203  CA  CYS A 296     9391  10567  10349    445   -319   -158       C  
ATOM   2204  C   CYS A 296      -2.450 -17.054  15.222  1.00 75.19           C  
ANISOU 2204  C   CYS A 296     8692  10051   9826    481   -336   -129       C  
ATOM   2205  O   CYS A 296      -1.695 -17.568  14.392  1.00 74.82           O  
ANISOU 2205  O   CYS A 296     8590  10011   9827    531   -272   -135       O  
ATOM   2206  CB  CYS A 296      -4.496 -18.498  15.191  1.00 83.56           C  
ANISOU 2206  CB  CYS A 296     9931  10972  10843    509   -297   -150       C  
ATOM   2207  SG  CYS A 296      -6.290 -18.598  15.380  1.00 90.29           S  
ANISOU 2207  SG  CYS A 296    10897  11756  11653    460   -296   -168       S  
ATOM   2208  N   LYS A 297      -2.014 -16.441  16.317  1.00 70.20           N  
ANISOU 2208  N   LYS A 297     8016   9469   9188    458   -424   -103       N  
ATOM   2209  CA  LYS A 297      -0.616 -16.392  16.707  1.00 79.06           C  
ANISOU 2209  CA  LYS A 297     9008  10658  10371    486   -471    -73       C  
ATOM   2210  C   LYS A 297      -0.446 -17.070  18.059  1.00 90.76           C  
ANISOU 2210  C   LYS A 297    10497  12149  11838    550   -561    -27       C  
ATOM   2211  O   LYS A 297      -1.412 -17.312  18.788  1.00 95.39           O  
ANISOU 2211  O   LYS A 297    11191  12696  12356    552   -585    -16       O  
ATOM   2212  CB  LYS A 297      -0.110 -14.946  16.783  1.00 79.35           C  
ANISOU 2212  CB  LYS A 297     8978  10752  10418    389   -517    -89       C  
ATOM   2213  CG  LYS A 297      -0.348 -14.125  15.530  1.00 83.77           C  
ANISOU 2213  CG  LYS A 297     9550  11299  10980    319   -431   -119       C  
ATOM   2214  CD  LYS A 297      -0.772 -12.705  15.882  1.00 84.75           C  
ANISOU 2214  CD  LYS A 297     9711  11421  11070    215   -485   -141       C  
ATOM   2215  CE  LYS A 297       0.201 -12.051  16.853  1.00 85.33           C  
ANISOU 2215  CE  LYS A 297     9689  11549  11184    174   -591   -135       C  
ATOM   2216  NZ  LYS A 297      -0.291 -10.726  17.327  1.00 87.87           N  
ANISOU 2216  NZ  LYS A 297    10069  11849  11467     79   -651   -170       N  
ATOM   2217  N   GLU A 298       0.800 -17.385  18.388  1.00 95.78           N  
ANISOU 2217  N   GLU A 298    11013  12841  12539    607   -608      8       N  
ATOM   2218  CA  GLU A 298       1.148 -17.797  19.738  1.00100.81           C  
ANISOU 2218  CA  GLU A 298    11643  13507  13152    664   -722     59       C  
ATOM   2219  C   GLU A 298       1.562 -16.562  20.523  1.00 98.59           C  
ANISOU 2219  C   GLU A 298    11315  13302  12842    582   -839     40       C  
ATOM   2220  O   GLU A 298       2.440 -15.807  20.090  1.00101.85           O  
ANISOU 2220  O   GLU A 298    11603  13769  13326    529   -852     19       O  
ATOM   2221  CB  GLU A 298       2.269 -18.836  19.732  1.00111.99           C  
ANISOU 2221  CB  GLU A 298    12950  14943  14657    783   -729    109       C  
ATOM   2222  CG  GLU A 298       2.621 -19.370  21.116  1.00119.00           C  
ANISOU 2222  CG  GLU A 298    13842  15860  15512    860   -854    176       C  
ATOM   2223  CD  GLU A 298       1.508 -20.201  21.740  1.00120.93           C  
ANISOU 2223  CD  GLU A 298    14254  16022  15672    902   -838    217       C  
ATOM   2224  OE1 GLU A 298       0.543 -20.561  21.031  1.00120.88           O  
ANISOU 2224  OE1 GLU A 298    14341  15928  15660    883   -728    191       O  
ATOM   2225  OE2 GLU A 298       1.604 -20.502  22.948  1.00121.40           O  
ANISOU 2225  OE2 GLU A 298    14351  16105  15669    953   -937    277       O  
ATOM   2226  N   GLY A 299       0.923 -16.354  21.668  1.00 90.87           N  
ANISOU 2226  N   GLY A 299    10441  12326  11760    571   -919     46       N  
ATOM   2227  CA  GLY A 299       1.060 -15.116  22.402  1.00 83.82           C  
ANISOU 2227  CA  GLY A 299     9546  11485  10818    485  -1024      5       C  
ATOM   2228  C   GLY A 299       2.450 -14.896  22.973  1.00 80.63           C  
ANISOU 2228  C   GLY A 299     8998  11170  10467    493  -1156     17       C  
ATOM   2229  O   GLY A 299       3.383 -15.679  22.791  1.00 79.11           O  
ANISOU 2229  O   GLY A 299     8688  11009  10360    573  -1165     64       O  
ATOM   2230  N   ILE A 300       2.575 -13.784  23.694  1.00 83.57           N  
ANISOU 2230  N   ILE A 300     9378  11582  10792    410  -1267    -32       N  
ATOM   2231  CA  ILE A 300       3.825 -13.359  24.311  1.00 90.57           C  
ANISOU 2231  CA  ILE A 300    10129  12557  11728    389  -1421    -39       C  
ATOM   2232  C   ILE A 300       3.799 -13.725  25.790  1.00 89.45           C  
ANISOU 2232  C   ILE A 300    10068  12461  11459    455  -1566    -14       C  
ATOM   2233  O   ILE A 300       2.753 -13.676  26.447  1.00 91.42           O  
ANISOU 2233  O   ILE A 300    10491  12677  11567    462  -1557    -24       O  
ATOM   2234  CB  ILE A 300       4.047 -11.844  24.108  1.00 90.96           C  
ANISOU 2234  CB  ILE A 300    10136  12609  11816    241  -1459   -119       C  
ATOM   2235  CG1 ILE A 300       4.051 -11.505  22.616  1.00 97.76           C  
ANISOU 2235  CG1 ILE A 300    10932  13424  12787    182  -1304   -126       C  
ATOM   2236  CG2 ILE A 300       5.345 -11.393  24.748  1.00 85.26           C  
ANISOU 2236  CG2 ILE A 300     9260  11975  11159    203  -1630   -135       C  
ATOM   2237  CD1 ILE A 300       4.224 -10.030  22.327  1.00103.38           C  
ANISOU 2237  CD1 ILE A 300    11613  14119  13548     35  -1322   -189       C  
ATOM   2238  N   LYS A 301       4.961 -14.102  26.318  1.00 92.99           N  
ANISOU 2238  N   LYS A 301    10387  12991  11954    511  -1698     23       N  
ATOM   2239  CA  LYS A 301       5.082 -14.464  27.727  1.00100.04           C  
ANISOU 2239  CA  LYS A 301    11350  13942  12718    584  -1856     55       C  
ATOM   2240  C   LYS A 301       5.434 -13.249  28.582  1.00 98.74           C  
ANISOU 2240  C   LYS A 301    11187  13839  12492    485  -2029    -30       C  
ATOM   2241  O   LYS A 301       6.467 -12.609  28.378  1.00100.12           O  
ANISOU 2241  O   LYS A 301    11190  14066  12786    413  -2120    -70       O  
ATOM   2242  CB  LYS A 301       6.134 -15.563  27.910  1.00107.97           C  
ANISOU 2242  CB  LYS A 301    12222  15005  13799    714  -1927    146       C  
ATOM   2243  CG  LYS A 301       5.881 -16.807  27.067  1.00111.19           C  
ANISOU 2243  CG  LYS A 301    12630  15339  14279    819  -1762    221       C  
ATOM   2244  CD  LYS A 301       6.884 -17.915  27.363  1.00115.17           C  
ANISOU 2244  CD  LYS A 301    13017  15888  14853    967  -1837    315       C  
ATOM   2245  CE  LYS A 301       6.576 -19.165  26.543  1.00115.84           C  
ANISOU 2245  CE  LYS A 301    13127  15879  15008   1073  -1668    378       C  
ATOM   2246  NZ  LYS A 301       7.546 -20.270  26.791  1.00117.99           N  
ANISOU 2246  NZ  LYS A 301    13289  16179  15362   1233  -1731    471       N  
ATOM   2247  N   ALA A 304       3.523 -10.873  35.274  1.00118.97           N  
ANISOU 2247  N   ALA A 304    14614  16602  13988    494  -2661   -295       N  
ATOM   2248  CA  ALA A 304       3.242 -12.111  34.557  1.00117.86           C  
ANISOU 2248  CA  ALA A 304    14427  16419  13933    584  -2497   -156       C  
ATOM   2249  C   ALA A 304       4.470 -12.560  33.775  1.00120.02           C  
ANISOU 2249  C   ALA A 304    14454  16723  14426    591  -2549   -106       C  
ATOM   2250  O   ALA A 304       4.481 -12.524  32.544  1.00123.65           O  
ANISOU 2250  O   ALA A 304    14797  17120  15066    541  -2414   -106       O  
ATOM   2251  CB  ALA A 304       2.056 -11.930  33.628  1.00113.92           C  
ANISOU 2251  CB  ALA A 304    13990  15806  13489    538  -2261   -171       C  
ATOM   2252  N   THR A 305       5.501 -12.995  34.502  1.00121.20           N  
ANISOU 2252  N   THR A 305    14526  16975  14552    662  -2745    -62       N  
ATOM   2253  CA  THR A 305       6.785 -13.281  33.871  1.00119.28           C  
ANISOU 2253  CA  THR A 305    14023  16776  14522    666  -2818    -28       C  
ATOM   2254  C   THR A 305       6.711 -14.513  32.973  1.00123.75           C  
ANISOU 2254  C   THR A 305    14519  17286  15213    768  -2646     95       C  
ATOM   2255  O   THR A 305       7.203 -14.492  31.837  1.00123.35           O  
ANISOU 2255  O   THR A 305    14290  17209  15367    728  -2559     91       O  
ATOM   2256  CB  THR A 305       7.872 -13.443  34.938  1.00111.98           C  
ANISOU 2256  CB  THR A 305    13029  15981  13537    727  -3089    -10       C  
ATOM   2257  OG1 THR A 305       9.065 -13.958  34.331  1.00109.49           O  
ANISOU 2257  OG1 THR A 305    12452  15712  13439    766  -3137     51       O  
ATOM   2258  CG2 THR A 305       7.414 -14.376  36.056  1.00107.35           C  
ANISOU 2258  CG2 THR A 305    12638  15429  12722    879  -3133     93       C  
ATOM   2259  N   MET A 306       6.097 -15.597  33.459  1.00126.52           N  
ANISOU 2259  N   MET A 306    15018  17614  15442    899  -2587    204       N  
ATOM   2260  CA  MET A 306       6.014 -16.846  32.709  1.00124.30           C  
ANISOU 2260  CA  MET A 306    14692  17264  15272   1003  -2436    317       C  
ATOM   2261  C   MET A 306       4.591 -17.183  32.275  1.00118.08           C  
ANISOU 2261  C   MET A 306    14075  16357  14432    996  -2210    335       C  
ATOM   2262  O   MET A 306       4.287 -18.352  32.013  1.00113.57           O  
ANISOU 2262  O   MET A 306    13539  15720  13891   1096  -2100    438       O  
ATOM   2263  CB  MET A 306       6.605 -18.001  33.519  1.00127.57           C  
ANISOU 2263  CB  MET A 306    15107  17730  15634   1170  -2553    449       C  
ATOM   2264  CG  MET A 306       8.109 -17.903  33.758  1.00131.67           C  
ANISOU 2264  CG  MET A 306    15408  18367  16255   1201  -2769    451       C  
ATOM   2265  SD  MET A 306       9.005 -17.081  32.419  1.00131.26           S  
ANISOU 2265  SD  MET A 306    15071  18325  16477   1072  -2732    352       S  
ATOM   2266  CE  MET A 306       8.829 -18.239  31.066  1.00128.83           C  
ANISOU 2266  CE  MET A 306    14700  17907  16345   1160  -2480    435       C  
ATOM   2267  N   LYS A 307       3.717 -16.186  32.185  1.00116.73           N  
ANISOU 2267  N   LYS A 307    14005  16153  14195    881  -2143    237       N  
ATOM   2268  CA  LYS A 307       2.366 -16.371  31.672  1.00116.38           C  
ANISOU 2268  CA  LYS A 307    14091  16002  14126    859  -1935    241       C  
ATOM   2269  C   LYS A 307       2.303 -15.906  30.224  1.00111.06           C  
ANISOU 2269  C   LYS A 307    13304  15267  13628    767  -1808    176       C  
ATOM   2270  O   LYS A 307       2.771 -14.811  29.896  1.00107.31           O  
ANISOU 2270  O   LYS A 307    12739  14820  13215    663  -1863     83       O  
ATOM   2271  CB  LYS A 307       1.346 -15.605  32.514  1.00120.30           C  
ANISOU 2271  CB  LYS A 307    14777  16499  14431    811  -1928    182       C  
ATOM   2272  CG  LYS A 307       1.226 -16.107  33.942  1.00122.93           C  
ANISOU 2272  CG  LYS A 307    15260  16890  14556    908  -2020    254       C  
ATOM   2273  CD  LYS A 307       0.138 -15.361  34.698  1.00121.25           C  
ANISOU 2273  CD  LYS A 307    15240  16675  14154    867  -1978    190       C  
ATOM   2274  CE  LYS A 307      -0.053 -15.935  36.093  1.00121.25           C  
ANISOU 2274  CE  LYS A 307    15409  16734  13927    972  -2042    276       C  
ATOM   2275  NZ  LYS A 307      -1.116 -15.219  36.855  1.00121.04           N  
ANISOU 2275  NZ  LYS A 307    15574  16710  13704    943  -1982    212       N  
ATOM   2276  N   THR A 308       1.719 -16.737  29.366  1.00112.72           N  
ANISOU 2276  N   THR A 308    13527  15388  13913    802  -1641    226       N  
ATOM   2277  CA  THR A 308       1.597 -16.451  27.942  1.00113.50           C  
ANISOU 2277  CA  THR A 308    13539  15429  14158    733  -1512    176       C  
ATOM   2278  C   THR A 308       0.205 -15.884  27.674  1.00113.86           C  
ANISOU 2278  C   THR A 308    13718  15405  14140    657  -1391    123       C  
ATOM   2279  O   THR A 308      -0.786 -16.623  27.687  1.00114.83           O  
ANISOU 2279  O   THR A 308    13950  15462  14220    698  -1284    170       O  
ATOM   2280  CB  THR A 308       1.843 -17.712  27.114  1.00111.78           C  
ANISOU 2280  CB  THR A 308    13256  15156  14059    822  -1413    249       C  
ATOM   2281  OG1 THR A 308       3.093 -18.304  27.491  1.00114.01           O  
ANISOU 2281  OG1 THR A 308    13418  15503  14397    915  -1528    309       O  
ATOM   2282  CG2 THR A 308       1.882 -17.378  25.635  1.00110.22           C  
ANISOU 2282  CG2 THR A 308    12964  14917  13996    756  -1293    192       C  
ATOM   2283  N   PHE A 309       0.129 -14.575  27.442  1.00106.83           N  
ANISOU 2283  N   PHE A 309    12813  14523  13253    547  -1409     27       N  
ATOM   2284  CA  PHE A 309      -1.093 -13.931  26.985  1.00 99.83           C  
ANISOU 2284  CA  PHE A 309    12022  13570  12339    478  -1295    -28       C  
ATOM   2285  C   PHE A 309      -1.024 -13.715  25.482  1.00 91.05           C  
ANISOU 2285  C   PHE A 309    10816  12411  11367    424  -1193    -54       C  
ATOM   2286  O   PHE A 309       0.043 -13.450  24.922  1.00 97.47           O  
ANISOU 2286  O   PHE A 309    11489  13257  12287    396  -1230    -67       O  
ATOM   2287  CB  PHE A 309      -1.322 -12.594  27.689  1.00102.25           C  
ANISOU 2287  CB  PHE A 309    12398  13900  12553    402  -1372   -117       C  
ATOM   2288  CG  PHE A 309      -1.466 -12.717  29.169  1.00111.17           C  
ANISOU 2288  CG  PHE A 309    13645  15081  13514    455  -1466   -104       C  
ATOM   2289  CD1 PHE A 309      -2.674 -13.085  29.733  1.00113.04           C  
ANISOU 2289  CD1 PHE A 309    14034  15287  13629    499  -1377    -73       C  
ATOM   2290  CD2 PHE A 309      -0.389 -12.474  30.001  1.00119.14           C  
ANISOU 2290  CD2 PHE A 309    14610  16175  14483    462  -1644   -119       C  
ATOM   2291  CE1 PHE A 309      -2.802 -13.206  31.098  1.00116.97           C  
ANISOU 2291  CE1 PHE A 309    14652  15838  13953    554  -1449    -53       C  
ATOM   2292  CE2 PHE A 309      -0.513 -12.591  31.365  1.00122.73           C  
ANISOU 2292  CE2 PHE A 309    15189  16685  14759    518  -1737   -107       C  
ATOM   2293  CZ  PHE A 309      -1.722 -12.956  31.916  1.00121.32           C  
ANISOU 2293  CZ  PHE A 309    15177  16476  14444    567  -1633    -72       C  
ATOM   2294  N   CYS A 310      -2.177 -13.820  24.834  1.00 83.83           N  
ANISOU 2294  N   CYS A 310     9976  11423  10450    410  -1064    -61       N  
ATOM   2295  CA  CYS A 310      -2.278 -13.745  23.378  1.00 84.30           C  
ANISOU 2295  CA  CYS A 310     9976  11437  10616    373   -960    -80       C  
ATOM   2296  C   CYS A 310      -3.094 -12.512  23.002  1.00 75.74           C  
ANISOU 2296  C   CYS A 310     8948  10317   9512    284   -923   -148       C  
ATOM   2297  O   CYS A 310      -4.323 -12.511  23.120  1.00 76.22           O  
ANISOU 2297  O   CYS A 310     9112  10335   9515    286   -862   -156       O  
ATOM   2298  CB  CYS A 310      -2.906 -15.018  22.818  1.00 97.85           C  
ANISOU 2298  CB  CYS A 310    11728  13094  12358    437   -853    -31       C  
ATOM   2299  SG  CYS A 310      -2.877 -15.134  21.028  1.00109.06           S  
ANISOU 2299  SG  CYS A 310    13082  14468  13886    413   -739    -56       S  
ATOM   2300  N   GLY A 311      -2.412 -11.467  22.548  1.00 75.07           N  
ANISOU 2300  N   GLY A 311     8789  10247   9486    208   -957   -192       N  
ATOM   2301  CA  GLY A 311      -3.080 -10.246  22.157  1.00 79.36           C  
ANISOU 2301  CA  GLY A 311     9385  10746  10023    128   -927   -250       C  
ATOM   2302  C   GLY A 311      -3.397  -9.350  23.338  1.00 81.85           C  
ANISOU 2302  C   GLY A 311     9786  11066  10247    100  -1011   -304       C  
ATOM   2303  O   GLY A 311      -2.902  -9.525  24.454  1.00 82.21           O  
ANISOU 2303  O   GLY A 311     9840  11164  10231    126  -1111   -304       O  
ATOM   2304  N   THR A 312      -4.247  -8.364  23.072  1.00 85.65           N  
ANISOU 2304  N   THR A 312    10339  11491  10715     51   -970   -352       N  
ATOM   2305  CA  THR A 312      -4.671  -7.457  24.128  1.00 85.23           C  
ANISOU 2305  CA  THR A 312    10384  11427  10573     32  -1030   -418       C  
ATOM   2306  C   THR A 312      -6.032  -7.879  24.671  1.00 77.90           C  
ANISOU 2306  C   THR A 312     9573  10482   9546     97   -960   -408       C  
ATOM   2307  O   THR A 312      -6.891  -8.335  23.909  1.00 81.89           O  
ANISOU 2307  O   THR A 312    10083  10950  10080    119   -856   -376       O  
ATOM   2308  CB  THR A 312      -4.741  -6.018  23.608  1.00 92.58           C  
ANISOU 2308  CB  THR A 312    11326  12294  11557    -56  -1030   -480       C  
ATOM   2309  OG1 THR A 312      -5.310  -5.162  24.607  1.00 95.65           O  
ANISOU 2309  OG1 THR A 312    11830  12658  11856    -61  -1073   -554       O  
ATOM   2310  CG2 THR A 312      -5.570  -5.943  22.330  1.00 93.65           C  
ANISOU 2310  CG2 THR A 312    11465  12370  11746    -58   -911   -454       C  
ATOM   2311  N   PRO A 313      -6.261  -7.768  25.979  1.00 80.43           N  
ANISOU 2311  N   PRO A 313     9984  10830   9745    129  -1011   -436       N  
ATOM   2312  CA  PRO A 313      -7.524  -8.231  26.567  1.00 78.86           C  
ANISOU 2312  CA  PRO A 313     9887  10624   9452    193   -927   -415       C  
ATOM   2313  C   PRO A 313      -8.598  -7.163  26.720  1.00 67.21           C  
ANISOU 2313  C   PRO A 313     8500   9097   7940    181   -875   -485       C  
ATOM   2314  O   PRO A 313      -9.699  -7.491  27.176  1.00 63.45           O  
ANISOU 2314  O   PRO A 313     8093   8616   7397    234   -790   -468       O  
ATOM   2315  CB  PRO A 313      -7.078  -8.747  27.952  1.00 85.05           C  
ANISOU 2315  CB  PRO A 313    10728  11479  10108    246  -1007   -396       C  
ATOM   2316  CG  PRO A 313      -5.582  -8.369  28.092  1.00 86.50           C  
ANISOU 2316  CG  PRO A 313    10834  11708  10325    202  -1157   -427       C  
ATOM   2317  CD  PRO A 313      -5.294  -7.380  27.014  1.00 84.83           C  
ANISOU 2317  CD  PRO A 313    10549  11442  10242    114  -1152   -478       C  
ATOM   2318  N   GLU A 314      -8.319  -5.918  26.326  1.00 67.58           N  
ANISOU 2318  N   GLU A 314     8540   9098   8039    116   -915   -556       N  
ATOM   2319  CA  GLU A 314      -9.192  -4.797  26.656  1.00 75.30           C  
ANISOU 2319  CA  GLU A 314     9614  10020   8977    114   -886   -634       C  
ATOM   2320  C   GLU A 314     -10.585  -4.921  26.052  1.00 63.66           C  
ANISOU 2320  C   GLU A 314     8152   8502   7533    153   -755   -607       C  
ATOM   2321  O   GLU A 314     -11.529  -4.315  26.570  1.00 57.94           O  
ANISOU 2321  O   GLU A 314     7511   7750   6756    188   -706   -655       O  
ATOM   2322  CB  GLU A 314      -8.538  -3.491  26.199  1.00 89.04           C  
ANISOU 2322  CB  GLU A 314    11336  11699  10795     29   -954   -704       C  
ATOM   2323  CG  GLU A 314      -7.192  -3.210  26.858  1.00108.43           C  
ANISOU 2323  CG  GLU A 314    13770  14194  13233    -24  -1098   -747       C  
ATOM   2324  CD  GLU A 314      -7.312  -2.904  28.344  1.00129.68           C  
ANISOU 2324  CD  GLU A 314    16586  16915  15772     11  -1166   -824       C  
ATOM   2325  OE1 GLU A 314      -8.451  -2.784  28.846  1.00137.68           O  
ANISOU 2325  OE1 GLU A 314    17706  17911  16696     75  -1083   -848       O  
ATOM   2326  OE2 GLU A 314      -6.263  -2.774  29.017  1.00139.67           O  
ANISOU 2326  OE2 GLU A 314    17840  18225  17002    -24  -1302   -864       O  
ATOM   2327  N   TYR A 315     -10.740  -5.694  24.981  1.00 58.65           N  
ANISOU 2327  N   TYR A 315     7436   7865   6985    152   -700   -537       N  
ATOM   2328  CA  TYR A 315     -12.009  -5.805  24.280  1.00 64.21           C  
ANISOU 2328  CA  TYR A 315     8133   8530   7734    178   -599   -514       C  
ATOM   2329  C   TYR A 315     -12.707  -7.138  24.506  1.00 56.84           C  
ANISOU 2329  C   TYR A 315     7189   7630   6778    228   -525   -447       C  
ATOM   2330  O   TYR A 315     -13.821  -7.328  24.008  1.00 58.74           O  
ANISOU 2330  O   TYR A 315     7413   7845   7062    247   -446   -429       O  
ATOM   2331  CB  TYR A 315     -11.796  -5.596  22.777  1.00 60.51           C  
ANISOU 2331  CB  TYR A 315     7591   8022   7376    133   -594   -494       C  
ATOM   2332  CG  TYR A 315     -10.926  -6.654  22.129  1.00 68.23           C  
ANISOU 2332  CG  TYR A 315     8489   9037   8398    119   -607   -436       C  
ATOM   2333  CD1 TYR A 315      -9.540  -6.560  22.167  1.00 77.94           C  
ANISOU 2333  CD1 TYR A 315     9674  10294   9647     79   -682   -438       C  
ATOM   2334  CD2 TYR A 315     -11.489  -7.745  21.472  1.00 76.09           C  
ANISOU 2334  CD2 TYR A 315     9449  10036   9427    146   -545   -385       C  
ATOM   2335  CE1 TYR A 315      -8.739  -7.523  21.573  1.00 83.53           C  
ANISOU 2335  CE1 TYR A 315    10302  11035  10401     80   -683   -387       C  
ATOM   2336  CE2 TYR A 315     -10.693  -8.715  20.874  1.00 79.78           C  
ANISOU 2336  CE2 TYR A 315     9853  10526   9934    143   -551   -342       C  
ATOM   2337  CZ  TYR A 315      -9.318  -8.596  20.928  1.00 85.95           C  
ANISOU 2337  CZ  TYR A 315    10589  11337  10729    117   -614   -341       C  
ATOM   2338  OH  TYR A 315      -8.514  -9.548  20.339  1.00 90.97           O  
ANISOU 2338  OH  TYR A 315    11157  11997  11411    127   -609   -301       O  
ATOM   2339  N   LEU A 316     -12.086  -8.065  25.231  1.00 54.28           N  
ANISOU 2339  N   LEU A 316     6870   7358   6397    250   -553   -405       N  
ATOM   2340  CA  LEU A 316     -12.623  -9.413  25.351  1.00 49.05           C  
ANISOU 2340  CA  LEU A 316     6196   6709   5732    288   -484   -328       C  
ATOM   2341  C   LEU A 316     -13.814  -9.439  26.297  1.00 45.58           C  
ANISOU 2341  C   LEU A 316     5826   6276   5216    334   -397   -323       C  
ATOM   2342  O   LEU A 316     -13.771  -8.848  27.380  1.00 47.63           O  
ANISOU 2342  O   LEU A 316     6169   6564   5366    359   -415   -362       O  
ATOM   2343  CB  LEU A 316     -11.546 -10.376  25.845  1.00 57.26           C  
ANISOU 2343  CB  LEU A 316     7225   7793   6737    307   -542   -274       C  
ATOM   2344  CG  LEU A 316     -10.452 -10.736  24.839  1.00 65.61           C  
ANISOU 2344  CG  LEU A 316     8191   8849   7889    278   -595   -258       C  
ATOM   2345  CD1 LEU A 316      -9.434 -11.675  25.470  1.00 79.98           C  
ANISOU 2345  CD1 LEU A 316     9999  10715   9675    316   -655   -202       C  
ATOM   2346  CD2 LEU A 316     -11.059 -11.349  23.585  1.00 53.59           C  
ANISOU 2346  CD2 LEU A 316     6616   7280   6467    268   -520   -232       C  
ATOM   2347  N   ALA A 317     -14.872 -10.131  25.885  1.00 47.24           N  
ANISOU 2347  N   ALA A 317     6000   6462   5485    343   -302   -278       N  
ATOM   2348  CA  ALA A 317     -16.007 -10.347  26.763  1.00 50.64           C  
ANISOU 2348  CA  ALA A 317     6477   6904   5861    384   -198   -253       C  
ATOM   2349  C   ALA A 317     -15.569 -11.164  27.978  1.00 52.81           C  
ANISOU 2349  C   ALA A 317     6821   7224   6019    422   -195   -192       C  
ATOM   2350  O   ALA A 317     -14.631 -11.962  27.892  1.00 54.03           O  
ANISOU 2350  O   ALA A 317     6960   7388   6180    418   -256   -144       O  
ATOM   2351  CB  ALA A 317     -17.132 -11.066  26.020  1.00 42.42           C  
ANISOU 2351  CB  ALA A 317     5360   5827   4931    371   -108   -209       C  
ATOM   2352  N   PRO A 318     -16.217 -10.967  29.130  1.00 52.13           N  
ANISOU 2352  N   PRO A 318     6818   7170   5819    467   -123   -189       N  
ATOM   2353  CA  PRO A 318     -15.826 -11.743  30.320  1.00 54.12           C  
ANISOU 2353  CA  PRO A 318     7155   7471   5939    511   -119   -119       C  
ATOM   2354  C   PRO A 318     -15.904 -13.246  30.111  1.00 55.82           C  
ANISOU 2354  C   PRO A 318     7329   7662   6218    508    -70     -1       C  
ATOM   2355  O   PRO A 318     -14.963 -13.963  30.470  1.00 51.98           O  
ANISOU 2355  O   PRO A 318     6871   7195   5685    529   -138     56       O  
ATOM   2356  CB  PRO A 318     -16.814 -11.259  31.391  1.00 57.63           C  
ANISOU 2356  CB  PRO A 318     7688   7946   6264    560     -9   -135       C  
ATOM   2357  CG  PRO A 318     -17.220  -9.892  30.938  1.00 57.08           C  
ANISOU 2357  CG  PRO A 318     7601   7850   6237    549    -16   -250       C  
ATOM   2358  CD  PRO A 318     -17.243  -9.954  29.436  1.00 45.60           C  
ANISOU 2358  CD  PRO A 318     6021   6338   4966    491    -46   -254       C  
ATOM   2359  N   GLU A 319     -16.993 -13.745  29.518  1.00 50.76           N  
ANISOU 2359  N   GLU A 319     6620   6973   5693    483     38     34       N  
ATOM   2360  CA  GLU A 319     -17.114 -15.180  29.286  1.00 53.34           C  
ANISOU 2360  CA  GLU A 319     6914   7256   6097    470     86    137       C  
ATOM   2361  C   GLU A 319     -16.036 -15.709  28.347  1.00 65.35           C  
ANISOU 2361  C   GLU A 319     8381   8745   7705    448    -20    137       C  
ATOM   2362  O   GLU A 319     -15.747 -16.909  28.372  1.00 61.82           O  
ANISOU 2362  O   GLU A 319     7936   8262   7290    457    -10    222       O  
ATOM   2363  CB  GLU A 319     -18.500 -15.521  28.730  1.00 56.22           C  
ANISOU 2363  CB  GLU A 319     7200   7572   6591    432    206    156       C  
ATOM   2364  CG  GLU A 319     -18.820 -14.893  27.380  1.00 58.83           C  
ANISOU 2364  CG  GLU A 319     7431   7871   7052    386    165     70       C  
ATOM   2365  CD  GLU A 319     -19.447 -13.517  27.507  1.00 63.57           C  
ANISOU 2365  CD  GLU A 319     8032   8501   7621    403    186    -11       C  
ATOM   2366  OE1 GLU A 319     -19.093 -12.781  28.453  1.00 59.99           O  
ANISOU 2366  OE1 GLU A 319     7668   8095   7031    447    173    -42       O  
ATOM   2367  OE2 GLU A 319     -20.302 -13.177  26.662  1.00 63.86           O  
ANISOU 2367  OE2 GLU A 319     7984   8511   7768    378    209    -47       O  
ATOM   2368  N   VAL A 320     -15.438 -14.848  27.523  1.00 66.80           N  
ANISOU 2368  N   VAL A 320     8519   8934   7928    424   -112     49       N  
ATOM   2369  CA  VAL A 320     -14.316 -15.276  26.696  1.00 57.39           C  
ANISOU 2369  CA  VAL A 320     7277   7725   6803    412   -202     48       C  
ATOM   2370  C   VAL A 320     -13.031 -15.314  27.514  1.00 59.64           C  
ANISOU 2370  C   VAL A 320     7608   8064   6989    454   -299     69       C  
ATOM   2371  O   VAL A 320     -12.208 -16.224  27.356  1.00 57.23           O  
ANISOU 2371  O   VAL A 320     7281   7746   6717    476   -340    123       O  
ATOM   2372  CB  VAL A 320     -14.185 -14.360  25.465  1.00 63.52           C  
ANISOU 2372  CB  VAL A 320     7986   8489   7661    366   -247    -41       C  
ATOM   2373  CG1 VAL A 320     -12.978 -14.752  24.644  1.00 64.71           C  
ANISOU 2373  CG1 VAL A 320     8084   8632   7871    359   -323    -42       C  
ATOM   2374  CG2 VAL A 320     -15.440 -14.433  24.619  1.00 58.22           C  
ANISOU 2374  CG2 VAL A 320     7265   7770   7088    333   -171    -55       C  
ATOM   2375  N   LEU A 321     -12.845 -14.337  28.406  1.00 55.99           N  
ANISOU 2375  N   LEU A 321     7209   7660   6404    469   -343     23       N  
ATOM   2376  CA  LEU A 321     -11.665 -14.323  29.265  1.00 59.61           C  
ANISOU 2376  CA  LEU A 321     7711   8179   6757    507   -455     36       C  
ATOM   2377  C   LEU A 321     -11.618 -15.547  30.174  1.00 64.46           C  
ANISOU 2377  C   LEU A 321     8389   8803   7298    569   -427    154       C  
ATOM   2378  O   LEU A 321     -10.537 -16.083  30.446  1.00 68.25           O  
ANISOU 2378  O   LEU A 321     8864   9310   7756    607   -521    200       O  
ATOM   2379  CB  LEU A 321     -11.642 -13.042  30.098  1.00 64.52           C  
ANISOU 2379  CB  LEU A 321     8408   8854   7253    507   -504    -49       C  
ATOM   2380  CG  LEU A 321     -10.898 -11.844  29.511  1.00 72.01           C  
ANISOU 2380  CG  LEU A 321     9305   9805   8248    454   -607   -155       C  
ATOM   2381  CD1 LEU A 321     -11.020 -10.646  30.438  1.00 79.91           C  
ANISOU 2381  CD1 LEU A 321    10402  10838   9121    457   -646   -244       C  
ATOM   2382  CD2 LEU A 321      -9.440 -12.200  29.288  1.00 70.13           C  
ANISOU 2382  CD2 LEU A 321     8998   9597   8051    451   -732   -136       C  
ATOM   2383  N   GLU A 322     -12.776 -16.002  30.653  1.00 59.17           N  
ANISOU 2383  N   GLU A 322     7775   8111   6596    582   -296    212       N  
ATOM   2384  CA  GLU A 322     -12.862 -17.098  31.611  1.00 65.16           C  
ANISOU 2384  CA  GLU A 322     8614   8872   7271    639   -249    339       C  
ATOM   2385  C   GLU A 322     -12.951 -18.468  30.948  1.00 69.17           C  
ANISOU 2385  C   GLU A 322     9071   9293   7920    634   -195    431       C  
ATOM   2386  O   GLU A 322     -13.141 -19.468  31.650  1.00 70.69           O  
ANISOU 2386  O   GLU A 322     9329   9462   8069    674   -136    550       O  
ATOM   2387  CB  GLU A 322     -14.065 -16.895  32.537  1.00 69.95           C  
ANISOU 2387  CB  GLU A 322     9310   9499   7769    654   -116    365       C  
ATOM   2388  CG  GLU A 322     -13.887 -15.780  33.559  1.00 77.94           C  
ANISOU 2388  CG  GLU A 322    10422  10600   8593    688   -166    293       C  
ATOM   2389  CD  GLU A 322     -15.109 -15.587  34.439  1.00 88.67           C  
ANISOU 2389  CD  GLU A 322    11869  11981   9843    713    -11    315       C  
ATOM   2390  OE1 GLU A 322     -16.204 -16.040  34.047  1.00 91.57           O  
ANISOU 2390  OE1 GLU A 322    12184  12293  10317    684    135    361       O  
ATOM   2391  OE2 GLU A 322     -14.974 -14.983  35.525  1.00 94.44           O  
ANISOU 2391  OE2 GLU A 322    12719  12784  10379    762    -34    283       O  
ATOM   2392  N   ASP A 323     -12.818 -18.532  29.620  1.00 68.34           N  
ANISOU 2392  N   ASP A 323     8860   9133   7975    586   -212    377       N  
ATOM   2393  CA  ASP A 323     -12.906 -19.782  28.864  1.00 60.90           C  
ANISOU 2393  CA  ASP A 323     7872   8094   7171    577   -167    437       C  
ATOM   2394  C   ASP A 323     -14.219 -20.518  29.127  1.00 66.08           C  
ANISOU 2394  C   ASP A 323     8559   8686   7865    553    -21    512       C  
ATOM   2395  O   ASP A 323     -14.279 -21.746  29.046  1.00 72.45           O  
ANISOU 2395  O   ASP A 323     9375   9409   8745    561     23    599       O  
ATOM   2396  CB  ASP A 323     -11.713 -20.698  29.159  1.00 71.62           C  
ANISOU 2396  CB  ASP A 323     9248   9445   8520    647   -244    516       C  
ATOM   2397  CG  ASP A 323     -10.394 -20.127  28.664  1.00 91.10           C  
ANISOU 2397  CG  ASP A 323    11646  11967  11003    661   -379    445       C  
ATOM   2398  OD1 ASP A 323     -10.296 -19.791  27.463  1.00 98.29           O  
ANISOU 2398  OD1 ASP A 323    12470  12853  12023    614   -386    363       O  
ATOM   2399  OD2 ASP A 323      -9.453 -20.013  29.481  1.00 98.73           O  
ANISOU 2399  OD2 ASP A 323    12641  13002  11870    718   -480    474       O  
ATOM   2400  N   ASN A 324     -15.276 -19.780  29.454  1.00 72.54           N  
ANISOU 2400  N   ASN A 324     9387   9535   8641    524     59    479       N  
ATOM   2401  CA  ASN A 324     -16.602 -20.358  29.607  1.00 75.89           C  
ANISOU 2401  CA  ASN A 324     9807   9903   9124    487    206    541       C  
ATOM   2402  C   ASN A 324     -17.287 -20.429  28.243  1.00 72.78           C  
ANISOU 2402  C   ASN A 324     9301   9440   8911    411    226    473       C  
ATOM   2403  O   ASN A 324     -16.823 -19.849  27.258  1.00 77.78           O  
ANISOU 2403  O   ASN A 324     9877  10083   9595    393    138    376       O  
ATOM   2404  CB  ASN A 324     -17.434 -19.541  30.600  1.00 79.90           C  
ANISOU 2404  CB  ASN A 324    10368  10483   9507    502    293    538       C  
ATOM   2405  CG  ASN A 324     -18.529 -20.363  31.267  1.00 88.07           C  
ANISOU 2405  CG  ASN A 324    11430  11479  10554    490    458    654       C  
ATOM   2406  OD1 ASN A 324     -18.658 -21.564  31.024  1.00 91.34           O  
ANISOU 2406  OD1 ASN A 324    11829  11802  11074    464    501    741       O  
ATOM   2407  ND2 ASN A 324     -19.316 -19.716  32.124  1.00 90.50           N  
ANISOU 2407  ND2 ASN A 324    11779  11850  10756    509    560    656       N  
ATOM   2408  N   ASP A 325     -18.397 -21.164  28.184  1.00 65.35           N  
ANISOU 2408  N   ASP A 325     8331   8431   8069    363    341    528       N  
ATOM   2409  CA  ASP A 325     -19.152 -21.247  26.942  1.00 68.82           C  
ANISOU 2409  CA  ASP A 325     8663   8810   8675    287    350    461       C  
ATOM   2410  C   ASP A 325     -19.668 -19.865  26.561  1.00 64.08           C  
ANISOU 2410  C   ASP A 325     8007   8280   8060    275    332    355       C  
ATOM   2411  O   ASP A 325     -20.044 -19.063  27.420  1.00 73.18           O  
ANISOU 2411  O   ASP A 325     9192   9502   9110    306    381    354       O  
ATOM   2412  CB  ASP A 325     -20.315 -22.235  27.074  1.00 79.00           C  
ANISOU 2412  CB  ASP A 325     9921  10017  10080    228    475    540       C  
ATOM   2413  CG  ASP A 325     -21.433 -21.713  27.959  1.00 97.22           C  
ANISOU 2413  CG  ASP A 325    12220  12380  12340    224    602    575       C  
ATOM   2414  OD1 ASP A 325     -21.133 -21.126  29.020  1.00103.90           O  
ANISOU 2414  OD1 ASP A 325    13151  13309  13018    290    623    602       O  
ATOM   2415  OD2 ASP A 325     -22.617 -21.888  27.594  1.00104.11           O  
ANISOU 2415  OD2 ASP A 325    12997  13216  13343    156    681    572       O  
ATOM   2416  N   TYR A 326     -19.667 -19.579  25.264  1.00 59.07           N  
ANISOU 2416  N   TYR A 326     7298   7624   7523    236    261    265       N  
ATOM   2417  CA  TYR A 326     -20.072 -18.269  24.784  1.00 57.24           C  
ANISOU 2417  CA  TYR A 326     7018   7446   7285    231    230    172       C  
ATOM   2418  C   TYR A 326     -20.902 -18.434  23.522  1.00 53.31           C  
ANISOU 2418  C   TYR A 326     6420   6900   6934    169    218    120       C  
ATOM   2419  O   TYR A 326     -20.879 -19.480  22.870  1.00 59.13           O  
ANISOU 2419  O   TYR A 326     7135   7563   7767    129    205    131       O  
ATOM   2420  CB  TYR A 326     -18.860 -17.366  24.516  1.00 59.77           C  
ANISOU 2420  CB  TYR A 326     7372   7815   7522    266    118    106       C  
ATOM   2421  CG  TYR A 326     -17.947 -17.870  23.421  1.00 69.91           C  
ANISOU 2421  CG  TYR A 326     8635   9060   8866    252     33     79       C  
ATOM   2422  CD1 TYR A 326     -18.125 -17.469  22.102  1.00 77.05           C  
ANISOU 2422  CD1 TYR A 326     9480   9951   9844    217    -15      3       C  
ATOM   2423  CD2 TYR A 326     -16.903 -18.739  23.707  1.00 66.50           C  
ANISOU 2423  CD2 TYR A 326     8247   8608   8412    283      5    131       C  
ATOM   2424  CE1 TYR A 326     -17.292 -17.927  21.098  1.00 80.39           C  
ANISOU 2424  CE1 TYR A 326     9893  10343  10307    212    -76    -25       C  
ATOM   2425  CE2 TYR A 326     -16.064 -19.200  22.709  1.00 66.53           C  
ANISOU 2425  CE2 TYR A 326     8229   8578   8473    282    -56    101       C  
ATOM   2426  CZ  TYR A 326     -16.264 -18.791  21.407  1.00 81.38           C  
ANISOU 2426  CZ  TYR A 326    10055  10447  10417    245    -90     21       C  
ATOM   2427  OH  TYR A 326     -15.433 -19.248  20.411  1.00 90.05           O  
ANISOU 2427  OH  TYR A 326    11141  11517  11558    251   -136    -11       O  
ATOM   2428  N   GLY A 327     -21.628 -17.383  23.183  1.00 44.82           N  
ANISOU 2428  N   GLY A 327     5291   5864   5875    165    214     59       N  
ATOM   2429  CA  GLY A 327     -22.498 -17.386  22.019  1.00 45.94           C  
ANISOU 2429  CA  GLY A 327     5334   5977   6144    114    187      8       C  
ATOM   2430  C   GLY A 327     -22.560 -16.020  21.381  1.00 43.05           C  
ANISOU 2430  C   GLY A 327     4945   5658   5755    138    121    -71       C  
ATOM   2431  O   GLY A 327     -21.602 -15.245  21.450  1.00 42.37           O  
ANISOU 2431  O   GLY A 327     4922   5604   5574    175     67    -99       O  
ATOM   2432  N   ARG A 328     -23.707 -15.718  20.767  1.00 47.60           N  
ANISOU 2432  N   ARG A 328     5426   6234   6426    114    122   -101       N  
ATOM   2433  CA  ARG A 328     -23.875 -14.477  20.018  1.00 46.93           C  
ANISOU 2433  CA  ARG A 328     5316   6179   6334    140     53   -166       C  
ATOM   2434  C   ARG A 328     -23.737 -13.233  20.887  1.00 48.11           C  
ANISOU 2434  C   ARG A 328     5517   6375   6388    205     86   -177       C  
ATOM   2435  O   ARG A 328     -23.483 -12.148  20.355  1.00 50.21           O  
ANISOU 2435  O   ARG A 328     5800   6652   6626    231     21   -226       O  
ATOM   2436  CB  ARG A 328     -25.236 -14.491  19.319  1.00 41.31           C  
ANISOU 2436  CB  ARG A 328     4483   5463   5751    111     46   -186       C  
ATOM   2437  CG  ARG A 328     -25.377 -15.619  18.312  1.00 56.65           C  
ANISOU 2437  CG  ARG A 328     6382   7355   7787     40    -12   -200       C  
ATOM   2438  CD  ARG A 328     -26.817 -15.838  17.885  1.00 61.28           C  
ANISOU 2438  CD  ARG A 328     6832   7936   8515     -2    -13   -210       C  
ATOM   2439  NE  ARG A 328     -26.909 -16.846  16.831  1.00 65.50           N  
ANISOU 2439  NE  ARG A 328     7338   8418   9130    -73    -93   -244       N  
ATOM   2440  CZ  ARG A 328     -26.979 -18.155  17.052  1.00 65.67           C  
ANISOU 2440  CZ  ARG A 328     7353   8373   9224   -139    -52   -216       C  
ATOM   2441  NH1 ARG A 328     -26.970 -18.627  18.293  1.00 56.91           N  
ANISOU 2441  NH1 ARG A 328     6264   7248   8112   -140     72   -137       N  
ATOM   2442  NH2 ARG A 328     -27.058 -18.996  16.029  1.00 71.55           N  
ANISOU 2442  NH2 ARG A 328     8083   9062  10039   -201   -136   -267       N  
ATOM   2443  N   ALA A 329     -23.887 -13.362  22.207  1.00 40.31           N  
ANISOU 2443  N   ALA A 329     4565   5406   5343    231    186   -133       N  
ATOM   2444  CA  ALA A 329     -23.779 -12.204  23.087  1.00 38.62           C  
ANISOU 2444  CA  ALA A 329     4415   5232   5027    295    218   -158       C  
ATOM   2445  C   ALA A 329     -22.370 -11.624  23.128  1.00 45.49           C  
ANISOU 2445  C   ALA A 329     5387   6109   5789    311    130   -192       C  
ATOM   2446  O   ALA A 329     -22.202 -10.465  23.521  1.00 50.18           O  
ANISOU 2446  O   ALA A 329     6032   6718   6315    353    120   -239       O  
ATOM   2447  CB  ALA A 329     -24.233 -12.577  24.500  1.00 34.07           C  
ANISOU 2447  CB  ALA A 329     3870   4681   4392    323    350   -102       C  
ATOM   2448  N   VAL A 330     -21.356 -12.393  22.733  1.00 43.60           N  
ANISOU 2448  N   VAL A 330     5171   5853   5541    278     68   -174       N  
ATOM   2449  CA  VAL A 330     -19.987 -11.886  22.778  1.00 42.63           C  
ANISOU 2449  CA  VAL A 330     5121   5743   5333    288    -14   -201       C  
ATOM   2450  C   VAL A 330     -19.815 -10.698  21.837  1.00 45.47           C  
ANISOU 2450  C   VAL A 330     5469   6094   5714    285    -85   -264       C  
ATOM   2451  O   VAL A 330     -19.108  -9.734  22.157  1.00 43.86           O  
ANISOU 2451  O   VAL A 330     5323   5899   5444    300   -127   -301       O  
ATOM   2452  CB  VAL A 330     -18.996 -13.015  22.458  1.00 50.89           C  
ANISOU 2452  CB  VAL A 330     6174   6774   6387    263    -56   -164       C  
ATOM   2453  CG1 VAL A 330     -17.603 -12.455  22.274  1.00 59.21           C  
ANISOU 2453  CG1 VAL A 330     7267   7845   7385    266   -144   -195       C  
ATOM   2454  CG2 VAL A 330     -19.012 -14.031  23.577  1.00 44.12           C  
ANISOU 2454  CG2 VAL A 330     5354   5920   5488    278     10    -91       C  
ATOM   2455  N   ASP A 331     -20.457 -10.740  20.664  1.00 39.38           N  
ANISOU 2455  N   ASP A 331     4628   5299   5035    264   -106   -275       N  
ATOM   2456  CA  ASP A 331     -20.348  -9.616  19.735  1.00 47.13           C  
ANISOU 2456  CA  ASP A 331     5609   6268   6031    267   -170   -319       C  
ATOM   2457  C   ASP A 331     -21.028  -8.365  20.273  1.00 41.05           C  
ANISOU 2457  C   ASP A 331     4855   5496   5246    314   -141   -351       C  
ATOM   2458  O   ASP A 331     -20.576  -7.249  19.991  1.00 44.24           O  
ANISOU 2458  O   ASP A 331     5300   5879   5628    324   -188   -385       O  
ATOM   2459  CB  ASP A 331     -20.941  -9.974  18.373  1.00 40.62           C  
ANISOU 2459  CB  ASP A 331     4716   5427   5290    243   -207   -321       C  
ATOM   2460  CG  ASP A 331     -20.162 -11.061  17.668  1.00 46.94           C  
ANISOU 2460  CG  ASP A 331     5518   6219   6098    203   -241   -309       C  
ATOM   2461  OD1 ASP A 331     -20.792 -11.913  17.007  1.00 43.32           O  
ANISOU 2461  OD1 ASP A 331     5009   5746   5706    178   -247   -307       O  
ATOM   2462  OD2 ASP A 331     -18.919 -11.073  17.790  1.00 43.42           O  
ANISOU 2462  OD2 ASP A 331     5120   5779   5598    199   -264   -307       O  
ATOM   2463  N   TRP A 332     -22.112  -8.521  21.036  1.00 41.53           N  
ANISOU 2463  N   TRP A 332     4884   5571   5325    346    -55   -339       N  
ATOM   2464  CA  TRP A 332     -22.790  -7.348  21.573  1.00 49.28           C  
ANISOU 2464  CA  TRP A 332     5881   6547   6295    406    -14   -375       C  
ATOM   2465  C   TRP A 332     -21.971  -6.681  22.669  1.00 40.30           C  
ANISOU 2465  C   TRP A 332     4857   5414   5041    430     -9   -410       C  
ATOM   2466  O   TRP A 332     -22.015  -5.453  22.810  1.00 45.87           O  
ANISOU 2466  O   TRP A 332     5609   6091   5728    468    -21   -462       O  
ATOM   2467  CB  TRP A 332     -24.175  -7.732  22.082  1.00 42.17           C  
ANISOU 2467  CB  TRP A 332     4903   5668   5453    436     92   -351       C  
ATOM   2468  CG  TRP A 332     -24.966  -8.525  21.086  1.00 50.08           C  
ANISOU 2468  CG  TRP A 332     5785   6668   6577    398     74   -321       C  
ATOM   2469  CD1 TRP A 332     -25.576  -9.725  21.299  1.00 61.74           C  
ANISOU 2469  CD1 TRP A 332     7190   8156   8113    361    136   -274       C  
ATOM   2470  CD2 TRP A 332     -25.222  -8.184  19.714  1.00 51.97           C  
ANISOU 2470  CD2 TRP A 332     5968   6887   6890    388    -19   -339       C  
ATOM   2471  NE1 TRP A 332     -26.204 -10.148  20.153  1.00 59.15           N  
ANISOU 2471  NE1 TRP A 332     6759   7816   7899    323     79   -274       N  
ATOM   2472  CE2 TRP A 332     -26.001  -9.221  19.165  1.00 55.82           C  
ANISOU 2472  CE2 TRP A 332     6350   7382   7478    344    -20   -313       C  
ATOM   2473  CE3 TRP A 332     -24.871  -7.103  18.897  1.00 63.01           C  
ANISOU 2473  CE3 TRP A 332     7403   8261   8277    410   -103   -369       C  
ATOM   2474  CZ2 TRP A 332     -26.439  -9.208  17.841  1.00 55.47           C  
ANISOU 2474  CZ2 TRP A 332     6238   7331   7508    327   -114   -326       C  
ATOM   2475  CZ3 TRP A 332     -25.308  -7.092  17.584  1.00 62.00           C  
ANISOU 2475  CZ3 TRP A 332     7213   8126   8218    400   -184   -368       C  
ATOM   2476  CH2 TRP A 332     -26.082  -8.137  17.070  1.00 54.78           C  
ANISOU 2476  CH2 TRP A 332     6195   7229   7388    361   -195   -351       C  
ATOM   2477  N   TRP A 333     -21.218  -7.461  23.448  1.00 44.27           N  
ANISOU 2477  N   TRP A 333     5408   5947   5465    411     -1   -384       N  
ATOM   2478  CA  TRP A 333     -20.218  -6.867  24.328  1.00 44.83           C  
ANISOU 2478  CA  TRP A 333     5586   6027   5421    421    -37   -423       C  
ATOM   2479  C   TRP A 333     -19.202  -6.074  23.520  1.00 44.94           C  
ANISOU 2479  C   TRP A 333     5618   6005   5451    384   -145   -461       C  
ATOM   2480  O   TRP A 333     -18.876  -4.930  23.860  1.00 38.83           O  
ANISOU 2480  O   TRP A 333     4911   5204   4638    396   -177   -522       O  
ATOM   2481  CB  TRP A 333     -19.523  -7.953  25.152  1.00 38.64           C  
ANISOU 2481  CB  TRP A 333     4840   5286   4557    409    -31   -374       C  
ATOM   2482  CG  TRP A 333     -18.301  -7.474  25.909  1.00 40.66           C  
ANISOU 2482  CG  TRP A 333     5191   5560   4700    409   -107   -413       C  
ATOM   2483  CD1 TRP A 333     -17.032  -7.329  25.417  1.00 43.12           C  
ANISOU 2483  CD1 TRP A 333     5502   5865   5018    364   -215   -427       C  
ATOM   2484  CD2 TRP A 333     -18.237  -7.098  27.291  1.00 42.18           C  
ANISOU 2484  CD2 TRP A 333     5487   5785   4756    453    -83   -445       C  
ATOM   2485  NE1 TRP A 333     -16.189  -6.880  26.404  1.00 41.46           N  
ANISOU 2485  NE1 TRP A 333     5374   5679   4698    371   -273   -467       N  
ATOM   2486  CE2 TRP A 333     -16.903  -6.729  27.564  1.00 42.96           C  
ANISOU 2486  CE2 TRP A 333     5640   5894   4789    427   -199   -483       C  
ATOM   2487  CE3 TRP A 333     -19.179  -7.032  28.323  1.00 40.03           C  
ANISOU 2487  CE3 TRP A 333     5265   5538   4407    514     29   -447       C  
ATOM   2488  CZ2 TRP A 333     -16.488  -6.305  28.826  1.00 39.21           C  
ANISOU 2488  CZ2 TRP A 333     5277   5453   4168    458   -227   -531       C  
ATOM   2489  CZ3 TRP A 333     -18.764  -6.609  29.576  1.00 38.21           C  
ANISOU 2489  CZ3 TRP A 333     5158   5342   4018    552     18   -492       C  
ATOM   2490  CH2 TRP A 333     -17.431  -6.251  29.816  1.00 41.49           C  
ANISOU 2490  CH2 TRP A 333     5634   5766   4364    523   -118   -537       C  
ATOM   2491  N   GLY A 334     -18.697  -6.668  22.438  1.00 39.11           N  
ANISOU 2491  N   GLY A 334     4824   5262   4773    336   -196   -427       N  
ATOM   2492  CA  GLY A 334     -17.740  -5.967  21.597  1.00 44.85           C  
ANISOU 2492  CA  GLY A 334     5561   5960   5521    297   -280   -449       C  
ATOM   2493  C   GLY A 334     -18.318  -4.704  20.989  1.00 36.21           C  
ANISOU 2493  C   GLY A 334     4473   4812   4473    315   -288   -483       C  
ATOM   2494  O   GLY A 334     -17.631  -3.686  20.880  1.00 49.04           O  
ANISOU 2494  O   GLY A 334     6145   6397   6090    295   -338   -518       O  
ATOM   2495  N   LEU A 335     -19.588  -4.755  20.581  1.00 34.36           N  
ANISOU 2495  N   LEU A 335     4186   4570   4298    352   -244   -470       N  
ATOM   2496  CA  LEU A 335     -20.284  -3.536  20.186  1.00 41.04           C  
ANISOU 2496  CA  LEU A 335     5041   5365   5188    393   -247   -498       C  
ATOM   2497  C   LEU A 335     -20.257  -2.509  21.308  1.00 49.63           C  
ANISOU 2497  C   LEU A 335     6214   6422   6221    433   -223   -559       C  
ATOM   2498  O   LEU A 335     -19.998  -1.326  21.067  1.00 45.58           O  
ANISOU 2498  O   LEU A 335     5753   5842   5722    437   -260   -594       O  
ATOM   2499  CB  LEU A 335     -21.724  -3.853  19.793  1.00 34.38           C  
ANISOU 2499  CB  LEU A 335     4110   4534   4419    436   -202   -474       C  
ATOM   2500  CG  LEU A 335     -22.556  -2.631  19.397  1.00 49.73           C  
ANISOU 2500  CG  LEU A 335     6050   6426   6417    499   -206   -494       C  
ATOM   2501  CD1 LEU A 335     -22.020  -2.001  18.110  1.00 28.85           C  
ANISOU 2501  CD1 LEU A 335     3427   3736   3799    473   -292   -477       C  
ATOM   2502  CD2 LEU A 335     -24.019  -3.009  19.253  1.00 36.50           C  
ANISOU 2502  CD2 LEU A 335     4268   4778   4821    548   -158   -474       C  
ATOM   2503  N   GLY A 336     -20.515  -2.945  22.544  1.00 42.05           N  
ANISOU 2503  N   GLY A 336     5279   5504   5194    462   -158   -573       N  
ATOM   2504  CA  GLY A 336     -20.506  -2.013  23.659  1.00 39.99           C  
ANISOU 2504  CA  GLY A 336     5116   5219   4861    507   -133   -645       C  
ATOM   2505  C   GLY A 336     -19.168  -1.320  23.829  1.00 40.77           C  
ANISOU 2505  C   GLY A 336     5298   5281   4911    454   -225   -693       C  
ATOM   2506  O   GLY A 336     -19.107  -0.102  24.015  1.00 45.05           O  
ANISOU 2506  O   GLY A 336     5912   5751   5453    471   -245   -760       O  
ATOM   2507  N   VAL A 337     -18.076  -2.085  23.754  1.00 42.89           N  
ANISOU 2507  N   VAL A 337     5553   5592   5151    388   -283   -661       N  
ATOM   2508  CA  VAL A 337     -16.741  -1.508  23.897  1.00 48.04           C  
ANISOU 2508  CA  VAL A 337     6258   6220   5775    327   -377   -702       C  
ATOM   2509  C   VAL A 337     -16.491  -0.468  22.812  1.00 46.46           C  
ANISOU 2509  C   VAL A 337     6052   5934   5665    291   -421   -710       C  
ATOM   2510  O   VAL A 337     -15.986   0.630  23.081  1.00 46.01           O  
ANISOU 2510  O   VAL A 337     6065   5810   5606    267   -468   -772       O  
ATOM   2511  CB  VAL A 337     -15.674  -2.617  23.866  1.00 45.43           C  
ANISOU 2511  CB  VAL A 337     5883   5957   5420    275   -425   -652       C  
ATOM   2512  CG1 VAL A 337     -14.277  -2.014  23.912  1.00 49.32           C  
ANISOU 2512  CG1 VAL A 337     6399   6431   5909    205   -526   -689       C  
ATOM   2513  CG2 VAL A 337     -15.884  -3.591  25.021  1.00 42.27           C  
ANISOU 2513  CG2 VAL A 337     5508   5630   4922    316   -383   -634       C  
ATOM   2514  N   VAL A 338     -16.846  -0.797  21.569  1.00 38.56           N  
ANISOU 2514  N   VAL A 338     4977   4931   4742    285   -410   -645       N  
ATOM   2515  CA  VAL A 338     -16.633   0.126  20.459  1.00 32.50           C  
ANISOU 2515  CA  VAL A 338     4212   4088   4049    256   -445   -631       C  
ATOM   2516  C   VAL A 338     -17.495   1.373  20.628  1.00 35.50           C  
ANISOU 2516  C   VAL A 338     4652   4379   4457    316   -422   -677       C  
ATOM   2517  O   VAL A 338     -17.011   2.503  20.492  1.00 50.08           O  
ANISOU 2517  O   VAL A 338     6561   6134   6334    288   -460   -708       O  
ATOM   2518  CB  VAL A 338     -16.912  -0.574  19.117  1.00 47.17           C  
ANISOU 2518  CB  VAL A 338     5991   5975   5958    249   -439   -554       C  
ATOM   2519  CG1 VAL A 338     -16.877   0.434  17.981  1.00 42.22           C  
ANISOU 2519  CG1 VAL A 338     5381   5269   5390    236   -465   -529       C  
ATOM   2520  CG2 VAL A 338     -15.911  -1.699  18.884  1.00 45.47           C  
ANISOU 2520  CG2 VAL A 338     5726   5827   5722    192   -460   -518       C  
ATOM   2521  N   MET A 339     -18.787   1.187  20.913  1.00 41.33           N  
ANISOU 2521  N   MET A 339     5369   5135   5199    402   -356   -680       N  
ATOM   2522  CA  MET A 339     -19.666   2.335  21.122  1.00 41.84           C  
ANISOU 2522  CA  MET A 339     5483   5117   5297    480   -324   -725       C  
ATOM   2523  C   MET A 339     -19.189   3.190  22.290  1.00 43.51           C  
ANISOU 2523  C   MET A 339     5809   5273   5449    482   -332   -823       C  
ATOM   2524  O   MET A 339     -19.250   4.424  22.231  1.00 41.17           O  
ANISOU 2524  O   MET A 339     5585   4864   5192    503   -346   -869       O  
ATOM   2525  CB  MET A 339     -21.104   1.869  21.365  1.00 49.16           C  
ANISOU 2525  CB  MET A 339     6345   6092   6241    573   -240   -711       C  
ATOM   2526  CG  MET A 339     -21.727   1.031  20.255  1.00 64.78           C  
ANISOU 2526  CG  MET A 339     8207   8122   8285    573   -243   -630       C  
ATOM   2527  SD  MET A 339     -22.480   1.987  18.933  1.00 69.10           S  
ANISOU 2527  SD  MET A 339     8727   8593   8935    626   -281   -591       S  
ATOM   2528  CE  MET A 339     -23.065   3.418  19.828  1.00 74.55           C  
ANISOU 2528  CE  MET A 339     9502   9183   9640    726   -233   -669       C  
ATOM   2529  N   TYR A 340     -18.716   2.554  23.364  1.00 43.42           N  
ANISOU 2529  N   TYR A 340     5825   5334   5339    463   -328   -858       N  
ATOM   2530  CA  TYR A 340     -18.263   3.313  24.525  1.00 43.31           C  
ANISOU 2530  CA  TYR A 340     5931   5278   5248    465   -349   -963       C  
ATOM   2531  C   TYR A 340     -17.073   4.194  24.173  1.00 46.66           C  
ANISOU 2531  C   TYR A 340     6404   5615   5712    371   -450   -996       C  
ATOM   2532  O   TYR A 340     -17.016   5.361  24.574  1.00 55.28           O  
ANISOU 2532  O   TYR A 340     7594   6600   6811    380   -469  -1082       O  
ATOM   2533  CB  TYR A 340     -17.905   2.364  25.669  1.00 37.74           C  
ANISOU 2533  CB  TYR A 340     5245   4681   4414    461   -341   -978       C  
ATOM   2534  CG  TYR A 340     -17.550   3.056  26.968  1.00 44.77           C  
ANISOU 2534  CG  TYR A 340     6270   5546   5194    477   -365  -1096       C  
ATOM   2535  CD1 TYR A 340     -16.269   3.547  27.194  1.00 45.65           C  
ANISOU 2535  CD1 TYR A 340     6437   5623   5285    388   -484  -1153       C  
ATOM   2536  CD2 TYR A 340     -18.493   3.205  27.976  1.00 45.97           C  
ANISOU 2536  CD2 TYR A 340     6493   5714   5260    579   -269  -1153       C  
ATOM   2537  CE1 TYR A 340     -15.944   4.174  28.381  1.00 53.99           C  
ANISOU 2537  CE1 TYR A 340     7623   6657   6234    397   -523  -1274       C  
ATOM   2538  CE2 TYR A 340     -18.175   3.830  29.163  1.00 53.09           C  
ANISOU 2538  CE2 TYR A 340     7535   6596   6041    599   -292  -1271       C  
ATOM   2539  CZ  TYR A 340     -16.898   4.307  29.363  1.00 53.78           C  
ANISOU 2539  CZ  TYR A 340     7684   6647   6105    506   -429  -1336       C  
ATOM   2540  OH  TYR A 340     -16.578   4.929  30.547  1.00 62.35           O  
ANISOU 2540  OH  TYR A 340     8916   7712   7062    521   -470  -1467       O  
ATOM   2541  N   GLU A 341     -16.109   3.653  23.425  1.00 41.31           N  
ANISOU 2541  N   GLU A 341     5655   4973   5068    279   -509   -929       N  
ATOM   2542  CA  GLU A 341     -14.923   4.433  23.093  1.00 51.98           C  
ANISOU 2542  CA  GLU A 341     7032   6248   6470    177   -594   -950       C  
ATOM   2543  C   GLU A 341     -15.236   5.536  22.089  1.00 46.84           C  
ANISOU 2543  C   GLU A 341     6402   5467   5927    178   -587   -926       C  
ATOM   2544  O   GLU A 341     -14.609   6.601  22.125  1.00 46.67           O  
ANISOU 2544  O   GLU A 341     6446   5333   5952    117   -637   -974       O  
ATOM   2545  CB  GLU A 341     -13.824   3.520  22.554  1.00 44.37           C  
ANISOU 2545  CB  GLU A 341     5974   5368   5518     90   -641   -879       C  
ATOM   2546  CG  GLU A 341     -12.487   4.223  22.388  1.00 63.21           C  
ANISOU 2546  CG  GLU A 341     8365   7695   7958    -26   -726   -902       C  
ATOM   2547  CD  GLU A 341     -11.382   3.283  21.967  1.00 74.90           C  
ANISOU 2547  CD  GLU A 341     9739   9269   9451    -98   -762   -837       C  
ATOM   2548  OE1 GLU A 341     -11.668   2.084  21.772  1.00 78.68           O  
ANISOU 2548  OE1 GLU A 341    10154   9846   9894    -55   -722   -776       O  
ATOM   2549  OE2 GLU A 341     -10.227   3.741  21.834  1.00 82.08           O  
ANISOU 2549  OE2 GLU A 341    10624  10147  10415   -198   -827   -847       O  
ATOM   2550  N   MET A 342     -16.205   5.314  21.198  1.00 39.63           N  
ANISOU 2550  N   MET A 342     5437   4561   5058    244   -531   -851       N  
ATOM   2551  CA  MET A 342     -16.561   6.357  20.239  1.00 48.81           C  
ANISOU 2551  CA  MET A 342     6629   5602   6314    260   -529   -815       C  
ATOM   2552  C   MET A 342     -17.210   7.553  20.928  1.00 55.63           C  
ANISOU 2552  C   MET A 342     7600   6341   7195    333   -509   -904       C  
ATOM   2553  O   MET A 342     -16.886   8.706  20.620  1.00 61.43           O  
ANISOU 2553  O   MET A 342     8407   6933   7998    302   -538   -919       O  
ATOM   2554  CB  MET A 342     -17.487   5.792  19.161  1.00 48.72           C  
ANISOU 2554  CB  MET A 342     6536   5640   6334    322   -491   -718       C  
ATOM   2555  CG  MET A 342     -16.781   4.845  18.201  1.00 73.76           C  
ANISOU 2555  CG  MET A 342     9625   8898   9503    248   -512   -631       C  
ATOM   2556  SD  MET A 342     -17.785   4.416  16.766  1.00 87.18           S  
ANISOU 2556  SD  MET A 342    11256  10632  11237    310   -495   -529       S  
ATOM   2557  CE  MET A 342     -19.299   3.886  17.552  1.00 77.88           C  
ANISOU 2557  CE  MET A 342    10033   9514  10045    427   -441   -567       C  
ATOM   2558  N   MET A 343     -18.118   7.300  21.871  1.00 49.32           N  
ANISOU 2558  N   MET A 343     6817   5588   6336    432   -451   -964       N  
ATOM   2559  CA  MET A 343     -18.881   8.374  22.497  1.00 43.89           C  
ANISOU 2559  CA  MET A 343     6226   4789   5662    528   -412  -1052       C  
ATOM   2560  C   MET A 343     -18.203   8.973  23.722  1.00 48.65           C  
ANISOU 2560  C   MET A 343     6952   5336   6197    492   -447  -1187       C  
ATOM   2561  O   MET A 343     -18.538  10.100  24.111  1.00 67.07           O  
ANISOU 2561  O   MET A 343     9392   7533   8557    546   -434  -1273       O  
ATOM   2562  CB  MET A 343     -20.274   7.870  22.878  1.00 46.36           C  
ANISOU 2562  CB  MET A 343     6487   5177   5949    662   -314  -1049       C  
ATOM   2563  CG  MET A 343     -21.082   7.454  21.665  1.00 53.47           C  
ANISOU 2563  CG  MET A 343     7271   6115   6931    705   -297   -933       C  
ATOM   2564  SD  MET A 343     -22.831   7.162  21.995  1.00 52.17           S  
ANISOU 2564  SD  MET A 343     7027   6008   6788    866   -186   -930       S  
ATOM   2565  CE  MET A 343     -22.772   5.572  22.812  1.00 52.03           C  
ANISOU 2565  CE  MET A 343     6938   6167   6663    829   -137   -923       C  
ATOM   2566  N   CYS A 344     -17.258   8.257  24.332  1.00 51.31           N  
ANISOU 2566  N   CYS A 344     7279   5768   6447    407   -498  -1211       N  
ATOM   2567  CA  CYS A 344     -16.552   8.743  25.509  1.00 53.72           C  
ANISOU 2567  CA  CYS A 344     7699   6040   6674    367   -555  -1343       C  
ATOM   2568  C   CYS A 344     -15.090   9.070  25.250  1.00 59.49           C  
ANISOU 2568  C   CYS A 344     8430   6723   7450    212   -672  -1352       C  
ATOM   2569  O   CYS A 344     -14.456   9.702  26.101  1.00 62.83           O  
ANISOU 2569  O   CYS A 344     8952   7086   7836    162   -743  -1471       O  
ATOM   2570  CB  CYS A 344     -16.632   7.714  26.646  1.00 50.50           C  
ANISOU 2570  CB  CYS A 344     7292   5784   6110    403   -530  -1376       C  
ATOM   2571  SG  CYS A 344     -18.310   7.207  27.059  1.00 62.73           S  
ANISOU 2571  SG  CYS A 344     8821   7406   7608    572   -373  -1359       S  
ATOM   2572  N   GLY A 345     -14.539   8.655  24.113  1.00 61.82           N  
ANISOU 2572  N   GLY A 345     8617   7047   7826    133   -694  -1233       N  
ATOM   2573  CA  GLY A 345     -13.143   8.918  23.823  1.00 60.45           C  
ANISOU 2573  CA  GLY A 345     8418   6839   7710    -16   -788  -1228       C  
ATOM   2574  C   GLY A 345     -12.173   8.188  24.722  1.00 58.24           C  
ANISOU 2574  C   GLY A 345     8113   6678   7340    -80   -868  -1276       C  
ATOM   2575  O   GLY A 345     -11.070   8.685  24.966  1.00 60.91           O  
ANISOU 2575  O   GLY A 345     8462   6969   7713   -195   -965  -1331       O  
ATOM   2576  N   ARG A 346     -12.552   7.009  25.215  1.00 61.03           N  
ANISOU 2576  N   ARG A 346     8425   7181   7583    -11   -832  -1251       N  
ATOM   2577  CA  ARG A 346     -11.748   6.271  26.178  1.00 60.07           C  
ANISOU 2577  CA  ARG A 346     8293   7175   7355    -46   -907  -1290       C  
ATOM   2578  C   ARG A 346     -12.218   4.823  26.201  1.00 54.10           C  
ANISOU 2578  C   ARG A 346     7460   6570   6525     25   -841  -1200       C  
ATOM   2579  O   ARG A 346     -13.413   4.554  26.066  1.00 51.41           O  
ANISOU 2579  O   ARG A 346     7123   6241   6168    124   -736  -1167       O  
ATOM   2580  CB  ARG A 346     -11.859   6.893  27.578  1.00 62.07           C  
ANISOU 2580  CB  ARG A 346     8694   7396   7495    -12   -949  -1442       C  
ATOM   2581  CG  ARG A 346     -11.011   6.221  28.651  1.00 81.61           C  
ANISOU 2581  CG  ARG A 346    11176   9991   9840    -42  -1047  -1488       C  
ATOM   2582  CD  ARG A 346     -11.344   6.746  30.047  1.00 95.00           C  
ANISOU 2582  CD  ARG A 346    13039  11670  11385     18  -1069  -1638       C  
ATOM   2583  NE  ARG A 346     -12.564   6.150  30.592  1.00100.45           N  
ANISOU 2583  NE  ARG A 346    13778  12435  11954    161   -938  -1620       N  
ATOM   2584  CZ  ARG A 346     -12.586   5.121  31.436  1.00 98.86           C  
ANISOU 2584  CZ  ARG A 346    13587  12376  11598    213   -930  -1596       C  
ATOM   2585  NH1 ARG A 346     -11.452   4.565  31.843  1.00 95.62           N  
ANISOU 2585  NH1 ARG A 346    13144  12054  11132    144  -1058  -1589       N  
ATOM   2586  NH2 ARG A 346     -13.745   4.649  31.878  1.00 97.09           N  
ANISOU 2586  NH2 ARG A 346    13401  12207  11281    335   -791  -1571       N  
ATOM   2587  N   LEU A 347     -11.275   3.898  26.365  1.00 50.05           N  
ANISOU 2587  N   LEU A 347     6873   6166   5979    -26   -904  -1160       N  
ATOM   2588  CA  LEU A 347     -11.635   2.503  26.552  1.00 51.91           C  
ANISOU 2588  CA  LEU A 347     7054   6531   6139     38   -850  -1083       C  
ATOM   2589  C   LEU A 347     -12.420   2.342  27.852  1.00 57.90           C  
ANISOU 2589  C   LEU A 347     7919   7332   6747    134   -808  -1145       C  
ATOM   2590  O   LEU A 347     -12.150   3.035  28.840  1.00 52.95           O  
ANISOU 2590  O   LEU A 347     7402   6678   6037    131   -870  -1257       O  
ATOM   2591  CB  LEU A 347     -10.384   1.627  26.578  1.00 43.04           C  
ANISOU 2591  CB  LEU A 347     5840   5502   5011    -26   -936  -1036       C  
ATOM   2592  CG  LEU A 347      -9.753   1.317  25.222  1.00 51.41           C  
ANISOU 2592  CG  LEU A 347     6770   6560   6202    -92   -933   -942       C  
ATOM   2593  CD1 LEU A 347      -8.333   0.804  25.382  1.00 61.09           C  
ANISOU 2593  CD1 LEU A 347     7911   7859   7441   -162  -1034   -924       C  
ATOM   2594  CD2 LEU A 347     -10.606   0.298  24.494  1.00 55.73           C  
ANISOU 2594  CD2 LEU A 347     7261   7154   6760    -26   -827   -844       C  
ATOM   2595  N   PRO A 348     -13.408   1.443  27.883  1.00 57.21           N  
ANISOU 2595  N   PRO A 348     7807   7310   6620    219   -698  -1077       N  
ATOM   2596  CA  PRO A 348     -14.232   1.318  29.099  1.00 54.44           C  
ANISOU 2596  CA  PRO A 348     7558   7000   6126    314   -629  -1125       C  
ATOM   2597  C   PRO A 348     -13.435   0.897  30.321  1.00 59.12           C  
ANISOU 2597  C   PRO A 348     8220   7678   6565    308   -713  -1163       C  
ATOM   2598  O   PRO A 348     -13.504   1.558  31.366  1.00 71.67           O  
ANISOU 2598  O   PRO A 348     9941   9254   8036    341   -734  -1273       O  
ATOM   2599  CB  PRO A 348     -15.291   0.276  28.698  1.00 53.37           C  
ANISOU 2599  CB  PRO A 348     7343   6921   6014    378   -501  -1018       C  
ATOM   2600  CG  PRO A 348     -14.695  -0.470  27.571  1.00 48.74           C  
ANISOU 2600  CG  PRO A 348     6630   6356   5534    312   -538   -921       C  
ATOM   2601  CD  PRO A 348     -13.842   0.519  26.822  1.00 55.65           C  
ANISOU 2601  CD  PRO A 348     7491   7147   6505    228   -629   -958       C  
ATOM   2602  N   PHE A 349     -12.670  -0.182  30.218  1.00 62.35           N  
ANISOU 2602  N   PHE A 349     8549   8173   6968    275   -765  -1079       N  
ATOM   2603  CA  PHE A 349     -11.797  -0.636  31.288  1.00 72.40           C  
ANISOU 2603  CA  PHE A 349     9872   9532   8103    271   -867  -1098       C  
ATOM   2604  C   PHE A 349     -10.358  -0.509  30.816  1.00 77.90           C  
ANISOU 2604  C   PHE A 349    10484  10228   8888    166  -1018  -1100       C  
ATOM   2605  O   PHE A 349     -10.057  -0.784  29.651  1.00 76.18           O  
ANISOU 2605  O   PHE A 349    10140   9990   8815    117  -1007  -1026       O  
ATOM   2606  CB  PHE A 349     -12.125  -2.081  31.675  1.00 63.48           C  
ANISOU 2606  CB  PHE A 349     8722   8507   6892    335   -798   -985       C  
ATOM   2607  CG  PHE A 349     -13.599  -2.341  31.807  1.00 66.17           C  
ANISOU 2607  CG  PHE A 349     9093   8845   7204    421   -624   -951       C  
ATOM   2608  CD1 PHE A 349     -14.263  -2.065  32.993  1.00 70.24           C  
ANISOU 2608  CD1 PHE A 349     9745   9386   7558    499   -559  -1010       C  
ATOM   2609  CD2 PHE A 349     -14.327  -2.839  30.738  1.00 67.02           C  
ANISOU 2609  CD2 PHE A 349     9090   8927   7447    422   -524   -865       C  
ATOM   2610  CE1 PHE A 349     -15.623  -2.295  33.113  1.00 69.44           C  
ANISOU 2610  CE1 PHE A 349     9652   9287   7446    577   -385   -974       C  
ATOM   2611  CE2 PHE A 349     -15.687  -3.069  30.853  1.00 69.07           C  
ANISOU 2611  CE2 PHE A 349     9355   9188   7701    493   -370   -834       C  
ATOM   2612  CZ  PHE A 349     -16.335  -2.797  32.040  1.00 66.88           C  
ANISOU 2612  CZ  PHE A 349     9196   8937   7277    569   -295   -885       C  
ATOM   2613  N   TYR A 350      -9.475  -0.055  31.703  1.00 87.60           N  
ANISOU 2613  N   TYR A 350    11777  11477  10031    131  -1159  -1190       N  
ATOM   2614  CA  TYR A 350      -8.072   0.071  31.330  1.00 96.40           C  
ANISOU 2614  CA  TYR A 350    12790  12598  11241     26  -1307  -1194       C  
ATOM   2615  C   TYR A 350      -7.190   0.064  32.565  1.00100.27           C  
ANISOU 2615  C   TYR A 350    13344  13162  11591     17  -1469  -1265       C  
ATOM   2616  O   TYR A 350      -7.441   0.800  33.523  1.00 94.60           O  
ANISOU 2616  O   TYR A 350    12775  12423  10747     38  -1508  -1386       O  
ATOM   2617  CB  TYR A 350      -7.810   1.345  30.520  1.00103.61           C  
ANISOU 2617  CB  TYR A 350    13677  13382  12308    -71  -1333  -1259       C  
ATOM   2618  CG  TYR A 350      -6.351   1.529  30.154  1.00114.56           C  
ANISOU 2618  CG  TYR A 350    14946  14774  13807   -190  -1474  -1261       C  
ATOM   2619  CD1 TYR A 350      -5.774   0.800  29.120  1.00118.83           C  
ANISOU 2619  CD1 TYR A 350    15324  15353  14474   -225  -1453  -1144       C  
ATOM   2620  CD2 TYR A 350      -5.549   2.427  30.847  1.00120.24           C  
ANISOU 2620  CD2 TYR A 350    15714  15462  14511   -269  -1628  -1385       C  
ATOM   2621  CE1 TYR A 350      -4.438   0.963  28.785  1.00121.93           C  
ANISOU 2621  CE1 TYR A 350    15591  15757  14978   -330  -1566  -1141       C  
ATOM   2622  CE2 TYR A 350      -4.213   2.597  30.519  1.00123.69           C  
ANISOU 2622  CE2 TYR A 350    16021  15907  15069   -387  -1756  -1384       C  
ATOM   2623  CZ  TYR A 350      -3.664   1.864  29.488  1.00125.21           C  
ANISOU 2623  CZ  TYR A 350    16039  16143  15391   -414  -1718  -1257       C  
ATOM   2624  OH  TYR A 350      -2.338   2.033  29.164  1.00128.55           O  
ANISOU 2624  OH  TYR A 350    16318  16582  15945   -527  -1830  -1252       O  
ATOM   2625  N   ASN A 351      -6.153  -0.763  32.522  1.00107.24           N  
ANISOU 2625  N   ASN A 351    14115  14133  12498     -8  -1566  -1194       N  
ATOM   2626  CA  ASN A 351      -5.118  -0.774  33.542  1.00110.68           C  
ANISOU 2626  CA  ASN A 351    14575  14647  12832    -29  -1755  -1252       C  
ATOM   2627  C   ASN A 351      -3.898  -1.460  32.949  1.00107.40           C  
ANISOU 2627  C   ASN A 351    13970  14292  12546    -82  -1845  -1164       C  
ATOM   2628  O   ASN A 351      -4.031  -2.431  32.201  1.00104.00           O  
ANISOU 2628  O   ASN A 351    13440  13887  12189    -45  -1746  -1037       O  
ATOM   2629  CB  ASN A 351      -5.584  -1.491  34.813  1.00113.43           C  
ANISOU 2629  CB  ASN A 351    15063  15093  12942     88  -1748  -1238       C  
ATOM   2630  CG  ASN A 351      -4.674  -1.229  35.994  1.00112.75           C  
ANISOU 2630  CG  ASN A 351    15049  15078  12712     73  -1957  -1332       C  
ATOM   2631  OD1 ASN A 351      -3.461  -1.092  35.840  1.00115.48           O  
ANISOU 2631  OD1 ASN A 351    15278  15447  13151    -12  -2123  -1350       O  
ATOM   2632  ND2 ASN A 351      -5.258  -1.151  37.183  1.00110.34           N  
ANISOU 2632  ND2 ASN A 351    14935  14813  12175    157  -1950  -1393       N  
ATOM   2633  N   GLN A 352      -2.713  -0.942  33.277  1.00105.78           N  
ANISOU 2633  N   GLN A 352    13711  14106  12376   -169  -2033  -1237       N  
ATOM   2634  CA  GLN A 352      -1.492  -1.481  32.687  1.00100.27           C  
ANISOU 2634  CA  GLN A 352    12810  13464  11825   -223  -2116  -1160       C  
ATOM   2635  C   GLN A 352      -1.267  -2.929  33.108  1.00100.46           C  
ANISOU 2635  C   GLN A 352    12798  13612  11760   -115  -2132  -1042       C  
ATOM   2636  O   GLN A 352      -0.812  -3.753  32.306  1.00100.39           O  
ANISOU 2636  O   GLN A 352    12636  13633  11875   -105  -2090   -931       O  
ATOM   2637  CB  GLN A 352      -0.294  -0.608  33.063  1.00 97.05           C  
ANISOU 2637  CB  GLN A 352    12343  13056  11477   -342  -2325  -1269       C  
ATOM   2638  CG  GLN A 352       1.023  -1.052  32.440  1.00 95.47           C  
ANISOU 2638  CG  GLN A 352    11907  12914  11452   -406  -2409  -1195       C  
ATOM   2639  CD  GLN A 352       0.991  -1.053  30.920  1.00 95.91           C  
ANISOU 2639  CD  GLN A 352    11827  12901  11713   -454  -2250  -1110       C  
ATOM   2640  OE1 GLN A 352       0.271  -0.269  30.300  1.00 97.73           O  
ANISOU 2640  OE1 GLN A 352    12122  13015  11996   -495  -2135  -1141       O  
ATOM   2641  NE2 GLN A 352       1.772  -1.939  30.314  1.00 94.62           N  
ANISOU 2641  NE2 GLN A 352    11481  12809  11660   -441  -2244  -1001       N  
ATOM   2642  N   ASP A 353      -1.601  -3.266  34.351  1.00101.94           N  
ANISOU 2642  N   ASP A 353    13136  13869  11729    -26  -2183  -1061       N  
ATOM   2643  CA  ASP A 353      -1.427  -4.627  34.838  1.00100.81           C  
ANISOU 2643  CA  ASP A 353    12982  13833  11488     84  -2198   -939       C  
ATOM   2644  C   ASP A 353      -2.550  -5.516  34.315  1.00 94.97           C  
ANISOU 2644  C   ASP A 353    12271  13064  10748    167  -1977   -822       C  
ATOM   2645  O   ASP A 353      -3.732  -5.185  34.452  1.00 96.60           O  
ANISOU 2645  O   ASP A 353    12608  13217  10876    196  -1845   -854       O  
ATOM   2646  CB  ASP A 353      -1.394  -4.642  36.367  1.00103.80           C  
ANISOU 2646  CB  ASP A 353    13527  14296  11616    149  -2329   -992       C  
ATOM   2647  CG  ASP A 353      -0.824  -5.932  36.929  1.00107.56           C  
ANISOU 2647  CG  ASP A 353    13970  14890  12007    248  -2409   -867       C  
ATOM   2648  OD1 ASP A 353      -1.289  -7.019  36.530  1.00106.55           O  
ANISOU 2648  OD1 ASP A 353    13817  14763  11904    326  -2266   -728       O  
ATOM   2649  OD2 ASP A 353       0.096  -5.857  37.769  1.00111.82           O  
ANISOU 2649  OD2 ASP A 353    14511  15517  12459    248  -2623   -908       O  
ATOM   2650  N   HIS A 354      -2.177  -6.649  33.714  1.00 88.66           N  
ANISOU 2650  N   HIS A 354    11345  12296  10045    207  -1939   -692       N  
ATOM   2651  CA  HIS A 354      -3.178  -7.563  33.170  1.00 97.00           C  
ANISOU 2651  CA  HIS A 354    12419  13318  11119    275  -1744   -586       C  
ATOM   2652  C   HIS A 354      -4.010  -8.196  34.278  1.00 93.34           C  
ANISOU 2652  C   HIS A 354    12124  12896  10447    380  -1690   -538       C  
ATOM   2653  O   HIS A 354      -5.208  -8.446  34.097  1.00 85.16           O  
ANISOU 2653  O   HIS A 354    11156  11813   9389    415  -1517   -502       O  
ATOM   2654  CB  HIS A 354      -2.500  -8.642  32.324  1.00105.87           C  
ANISOU 2654  CB  HIS A 354    13379  14458  12389    296  -1727   -470       C  
ATOM   2655  CG  HIS A 354      -1.705  -8.101  31.178  1.00111.50           C  
ANISOU 2655  CG  HIS A 354    13924  15137  13305    200  -1750   -501       C  
ATOM   2656  ND1 HIS A 354      -2.291  -7.606  30.033  1.00111.38           N  
ANISOU 2656  ND1 HIS A 354    13878  15034  13407    142  -1617   -520       N  
ATOM   2657  CD2 HIS A 354      -0.368  -7.976  31.003  1.00113.81           C  
ANISOU 2657  CD2 HIS A 354    14065  15475  13702    153  -1884   -510       C  
ATOM   2658  CE1 HIS A 354      -1.349  -7.200  29.200  1.00112.42           C  
ANISOU 2658  CE1 HIS A 354    13860  15157  13696     63  -1659   -534       C  
ATOM   2659  NE2 HIS A 354      -0.174  -7.413  29.765  1.00112.56           N  
ANISOU 2659  NE2 HIS A 354    13794  15255  13719     65  -1815   -529       N  
ATOM   2660  N   GLU A 355      -3.392  -8.466  35.430  1.00107.47           N  
ANISOU 2660  N   GLU A 355    13977  14777  12080    432  -1836   -531       N  
ATOM   2661  CA  GLU A 355      -4.129  -9.020  36.561  1.00113.59           C  
ANISOU 2661  CA  GLU A 355    14928  15597  12632    533  -1785   -480       C  
ATOM   2662  C   GLU A 355      -5.226  -8.066  37.015  1.00114.75           C  
ANISOU 2662  C   GLU A 355    15234  15705  12660    526  -1689   -586       C  
ATOM   2663  O   GLU A 355      -6.372  -8.474  37.234  1.00122.24           O  
ANISOU 2663  O   GLU A 355    16278  16637  13531    586  -1517   -530       O  
ATOM   2664  CB  GLU A 355      -3.169  -9.321  37.712  1.00117.56           C  
ANISOU 2664  CB  GLU A 355    15480  16212  12975    588  -1987   -466       C  
ATOM   2665  CG  GLU A 355      -1.911 -10.061  37.286  1.00122.13           C  
ANISOU 2665  CG  GLU A 355    15880  16834  13690    594  -2114   -384       C  
ATOM   2666  CD  GLU A 355      -0.819 -10.005  38.336  1.00128.86           C  
ANISOU 2666  CD  GLU A 355    16750  17799  14414    623  -2362   -409       C  
ATOM   2667  OE1 GLU A 355      -1.126 -10.202  39.532  1.00131.07           O  
ANISOU 2667  OE1 GLU A 355    17208  18142  14449    704  -2401   -393       O  
ATOM   2668  OE2 GLU A 355       0.348  -9.755  37.965  1.00129.78           O  
ANISOU 2668  OE2 GLU A 355    16698  17943  14670    565  -2519   -443       O  
ATOM   2669  N   LYS A 356      -4.889  -6.782  37.163  1.00107.99           N  
ANISOU 2669  N   LYS A 356    14403  14829  11798    452  -1796   -741       N  
ATOM   2670  CA  LYS A 356      -5.898  -5.796  37.528  1.00101.09           C  
ANISOU 2670  CA  LYS A 356    13676  13903  10830    451  -1704   -854       C  
ATOM   2671  C   LYS A 356      -6.905  -5.582  36.408  1.00 91.07           C  
ANISOU 2671  C   LYS A 356    12348  12531   9725    424  -1508   -839       C  
ATOM   2672  O   LYS A 356      -8.083  -5.328  36.679  1.00 97.20           O  
ANISOU 2672  O   LYS A 356    13233  13276  10424    470  -1360   -862       O  
ATOM   2673  CB  LYS A 356      -5.239  -4.468  37.905  1.00104.43           C  
ANISOU 2673  CB  LYS A 356    14142  14309  11228    372  -1875  -1031       C  
ATOM   2674  CG  LYS A 356      -4.975  -4.335  39.392  1.00107.40           C  
ANISOU 2674  CG  LYS A 356    14692  14776  11338    428  -2011  -1100       C  
ATOM   2675  CD  LYS A 356      -6.203  -4.770  40.174  1.00106.19           C  
ANISOU 2675  CD  LYS A 356    14718  14652  10977    546  -1835  -1053       C  
ATOM   2676  CE  LYS A 356      -5.922  -4.874  41.661  1.00109.22           C  
ANISOU 2676  CE  LYS A 356    15286  15146  11066    622  -1958  -1088       C  
ATOM   2677  NZ  LYS A 356      -6.096  -3.567  42.349  1.00110.95           N  
ANISOU 2677  NZ  LYS A 356    15668  15338  11151    601  -2018  -1291       N  
ATOM   2678  N   LEU A 357      -6.469  -5.683  35.151  1.00 77.45           N  
ANISOU 2678  N   LEU A 357    10451  10757   8221    355  -1505   -800       N  
ATOM   2679  CA  LEU A 357      -7.390  -5.500  34.034  1.00 76.60           C  
ANISOU 2679  CA  LEU A 357    10287  10557   8261    332  -1338   -782       C  
ATOM   2680  C   LEU A 357      -8.471  -6.573  34.031  1.00 79.32           C  
ANISOU 2680  C   LEU A 357    10657  10911   8571    413  -1163   -665       C  
ATOM   2681  O   LEU A 357      -9.661  -6.269  33.885  1.00 77.69           O  
ANISOU 2681  O   LEU A 357    10498  10655   8364    435  -1018   -681       O  
ATOM   2682  CB  LEU A 357      -6.632  -5.512  32.709  1.00 77.19           C  
ANISOU 2682  CB  LEU A 357    10183  10593   8555    251  -1370   -752       C  
ATOM   2683  CG  LEU A 357      -7.592  -5.574  31.524  1.00 76.69           C  
ANISOU 2683  CG  LEU A 357    10064  10450   8624    243  -1202   -710       C  
ATOM   2684  CD1 LEU A 357      -8.466  -4.328  31.499  1.00 76.23           C  
ANISOU 2684  CD1 LEU A 357    10091  10312   8560    225  -1142   -813       C  
ATOM   2685  CD2 LEU A 357      -6.836  -5.740  30.220  1.00 79.26           C  
ANISOU 2685  CD2 LEU A 357    10227  10751   9139    178  -1220   -667       C  
ATOM   2686  N   PHE A 358      -8.071  -7.840  34.175  1.00 80.98           N  
ANISOU 2686  N   PHE A 358    10827  11178   8763    459  -1177   -543       N  
ATOM   2687  CA  PHE A 358      -9.044  -8.927  34.195  1.00 78.80           C  
ANISOU 2687  CA  PHE A 358    10574  10899   8468    524  -1015   -425       C  
ATOM   2688  C   PHE A 358     -10.113  -8.687  35.251  1.00 90.08           C  
ANISOU 2688  C   PHE A 358    12163  12347   9717    586   -912   -447       C  
ATOM   2689  O   PHE A 358     -11.306  -8.868  34.989  1.00 98.06           O  
ANISOU 2689  O   PHE A 358    13179  13317  10761    605   -741   -412       O  
ATOM   2690  CB  PHE A 358      -8.343 -10.264  34.439  1.00 76.54           C  
ANISOU 2690  CB  PHE A 358    10253  10665   8163    573  -1066   -296       C  
ATOM   2691  CG  PHE A 358      -7.410 -10.667  33.338  1.00 70.55           C  
ANISOU 2691  CG  PHE A 358     9329   9886   7592    530  -1129   -262       C  
ATOM   2692  CD1 PHE A 358      -6.332 -11.496  33.595  1.00 75.32           C  
ANISOU 2692  CD1 PHE A 358     9882  10544   8191    568  -1243   -188       C  
ATOM   2693  CD2 PHE A 358      -7.610 -10.217  32.042  1.00 66.90           C  
ANISOU 2693  CD2 PHE A 358     8762   9352   7305    461  -1072   -301       C  
ATOM   2694  CE1 PHE A 358      -5.471 -11.868  32.583  1.00 85.30           C  
ANISOU 2694  CE1 PHE A 358    10990  11791   9630    540  -1285   -160       C  
ATOM   2695  CE2 PHE A 358      -6.752 -10.586  31.025  1.00 78.77           C  
ANISOU 2695  CE2 PHE A 358    10122  10842   8966    428  -1113   -271       C  
ATOM   2696  CZ  PHE A 358      -5.681 -11.413  31.296  1.00 85.32           C  
ANISOU 2696  CZ  PHE A 358    10896  11725   9796    468  -1213   -203       C  
ATOM   2697  N   GLU A 359      -9.705  -8.253  36.445  1.00 87.01           N  
ANISOU 2697  N   GLU A 359    11904  12023   9134    619  -1013   -509       N  
ATOM   2698  CA  GLU A 359     -10.683  -7.944  37.481  1.00 90.05           C  
ANISOU 2698  CA  GLU A 359    12455  12432   9328    686   -906   -542       C  
ATOM   2699  C   GLU A 359     -11.581  -6.790  37.060  1.00 78.00           C  
ANISOU 2699  C   GLU A 359    10940  10829   7868    659   -808   -657       C  
ATOM   2700  O   GLU A 359     -12.790  -6.813  37.317  1.00 82.34           O  
ANISOU 2700  O   GLU A 359    11547  11367   8370    711   -632   -641       O  
ATOM   2701  CB  GLU A 359      -9.977  -7.633  38.802  1.00 95.46           C  
ANISOU 2701  CB  GLU A 359    13288  13205   9779    725  -1057   -605       C  
ATOM   2702  CG  GLU A 359      -9.064  -8.748  39.273  1.00102.14           C  
ANISOU 2702  CG  GLU A 359    14126  14131  10551    766  -1171   -484       C  
ATOM   2703  CD  GLU A 359      -9.693 -10.115  39.093  1.00107.50           C  
ANISOU 2703  CD  GLU A 359    14776  14803  11267    818  -1012   -303       C  
ATOM   2704  OE1 GLU A 359     -10.808 -10.330  39.614  1.00110.98           O  
ANISOU 2704  OE1 GLU A 359    15319  15247  11603    871   -835   -259       O  
ATOM   2705  OE2 GLU A 359      -9.081 -10.967  38.414  1.00107.36           O  
ANISOU 2705  OE2 GLU A 359    14630  14771  11392    803  -1056   -207       O  
ATOM   2706  N   LEU A 360     -11.013  -5.775  36.402  1.00 58.92           N  
ANISOU 2706  N   LEU A 360     8462   8354   5569    581   -914   -768       N  
ATOM   2707  CA  LEU A 360     -11.834  -4.680  35.894  1.00 63.51           C  
ANISOU 2707  CA  LEU A 360     9049   8846   6235    560   -826   -866       C  
ATOM   2708  C   LEU A 360     -12.879  -5.200  34.915  1.00 59.28           C  
ANISOU 2708  C   LEU A 360     8409   8264   5853    567   -653   -774       C  
ATOM   2709  O   LEU A 360     -14.062  -4.855  35.010  1.00 65.00           O  
ANISOU 2709  O   LEU A 360     9173   8957   6566    613   -506   -795       O  
ATOM   2710  CB  LEU A 360     -10.957  -3.613  35.229  1.00 64.37           C  
ANISOU 2710  CB  LEU A 360     9099   8889   6470    464   -969   -973       C  
ATOM   2711  CG  LEU A 360      -9.874  -2.900  36.045  1.00 66.81           C  
ANISOU 2711  CG  LEU A 360     9488   9224   6671    428  -1165  -1091       C  
ATOM   2712  CD1 LEU A 360      -9.475  -1.589  35.376  1.00 69.14           C  
ANISOU 2712  CD1 LEU A 360     9747   9415   7109    333  -1242  -1212       C  
ATOM   2713  CD2 LEU A 360     -10.306  -2.671  37.487  1.00 69.56           C  
ANISOU 2713  CD2 LEU A 360    10036   9627   6765    512  -1152  -1163       C  
ATOM   2714  N   ILE A 361     -12.460  -6.052  33.975  1.00 54.30           N  
ANISOU 2714  N   ILE A 361     7640   7627   5365    526   -671   -674       N  
ATOM   2715  CA  ILE A 361     -13.380  -6.579  32.971  1.00 49.87           C  
ANISOU 2715  CA  ILE A 361     6976   7020   4954    523   -532   -596       C  
ATOM   2716  C   ILE A 361     -14.341  -7.584  33.596  1.00 52.80           C  
ANISOU 2716  C   ILE A 361     7387   7429   5244    591   -384   -496       C  
ATOM   2717  O   ILE A 361     -15.504  -7.688  33.191  1.00 55.50           O  
ANISOU 2717  O   ILE A 361     7688   7738   5664    605   -240   -468       O  
ATOM   2718  CB  ILE A 361     -12.595  -7.209  31.807  1.00 54.30           C  
ANISOU 2718  CB  ILE A 361     7394   7562   5675    463   -597   -531       C  
ATOM   2719  CG1 ILE A 361     -11.759  -6.148  31.096  1.00 58.96           C  
ANISOU 2719  CG1 ILE A 361     7934   8107   6362    388   -713   -620       C  
ATOM   2720  CG2 ILE A 361     -13.538  -7.894  30.832  1.00 45.76           C  
ANISOU 2720  CG2 ILE A 361     6220   6438   4727    461   -467   -454       C  
ATOM   2721  CD1 ILE A 361     -10.951  -6.698  29.968  1.00 58.77           C  
ANISOU 2721  CD1 ILE A 361     7775   8073   6483    335   -762   -562       C  
ATOM   2722  N   LEU A 362     -13.878  -8.336  34.595  1.00 54.45           N  
ANISOU 2722  N   LEU A 362     7675   7710   5304    634   -417   -434       N  
ATOM   2723  CA  LEU A 362     -14.709  -9.394  35.166  1.00 59.58           C  
ANISOU 2723  CA  LEU A 362     8362   8389   5885    691   -270   -314       C  
ATOM   2724  C   LEU A 362     -15.632  -8.879  36.268  1.00 67.25           C  
ANISOU 2724  C   LEU A 362     9469   9395   6687    759   -150   -356       C  
ATOM   2725  O   LEU A 362     -16.769  -9.352  36.398  1.00 75.49           O  
ANISOU 2725  O   LEU A 362    10506  10435   7743    791     29   -285       O  
ATOM   2726  CB  LEU A 362     -13.831 -10.521  35.715  1.00 56.17           C  
ANISOU 2726  CB  LEU A 362     7959   8012   5370    717   -347   -205       C  
ATOM   2727  CG  LEU A 362     -13.143 -11.402  34.669  1.00 59.43           C  
ANISOU 2727  CG  LEU A 362     8234   8388   5957    673   -409   -129       C  
ATOM   2728  CD1 LEU A 362     -12.137 -12.339  35.327  1.00 48.89           C  
ANISOU 2728  CD1 LEU A 362     6939   7109   4529    715   -511    -37       C  
ATOM   2729  CD2 LEU A 362     -14.170 -12.182  33.861  1.00 56.23           C  
ANISOU 2729  CD2 LEU A 362     7742   7920   5703    654   -254    -48       C  
ATOM   2730  N   MET A 363     -15.173  -7.910  37.065  1.00 64.45           N  
ANISOU 2730  N   MET A 363     9238   9072   6177    782   -242   -474       N  
ATOM   2731  CA  MET A 363     -15.865  -7.514  38.290  1.00 72.24           C  
ANISOU 2731  CA  MET A 363    10386  10107   6954    863   -139   -517       C  
ATOM   2732  C   MET A 363     -16.306  -6.058  38.309  1.00 75.82           C  
ANISOU 2732  C   MET A 363    10891  10514   7403    872   -122   -683       C  
ATOM   2733  O   MET A 363     -17.475  -5.780  38.603  1.00 78.58           O  
ANISOU 2733  O   MET A 363    11277  10857   7724    931     55   -697       O  
ATOM   2734  CB  MET A 363     -14.969  -7.799  39.509  1.00 67.10           C  
ANISOU 2734  CB  MET A 363     9885   9548   6063    907   -259   -507       C  
ATOM   2735  CG  MET A 363     -14.501  -9.250  39.598  1.00 80.88           C  
ANISOU 2735  CG  MET A 363    11596  11334   7801    917   -280   -333       C  
ATOM   2736  SD  MET A 363     -15.864 -10.433  39.627  1.00 89.85           S  
ANISOU 2736  SD  MET A 363    12704  12459   8978    953    -13   -158       S  
ATOM   2737  CE  MET A 363     -16.606 -10.060  41.215  1.00 74.13           C  
ANISOU 2737  CE  MET A 363    10932  10551   6683   1058    124   -181       C  
ATOM   2738  N   GLU A 364     -15.413  -5.113  38.009  1.00 75.08           N  
ANISOU 2738  N   GLU A 364    10799  10381   7345    818   -296   -807       N  
ATOM   2739  CA  GLU A 364     -15.754  -3.696  38.108  1.00 79.82           C  
ANISOU 2739  CA  GLU A 364    11472  10920   7935    829   -291   -971       C  
ATOM   2740  C   GLU A 364     -16.845  -3.321  37.109  1.00 79.28           C  
ANISOU 2740  C   GLU A 364    11291  10767   8064    827   -150   -967       C  
ATOM   2741  O   GLU A 364     -16.820  -3.742  35.950  1.00 85.36           O  
ANISOU 2741  O   GLU A 364    11905  11499   9030    768   -156   -891       O  
ATOM   2742  CB  GLU A 364     -14.516  -2.827  37.869  1.00 85.53           C  
ANISOU 2742  CB  GLU A 364    12201  11602   8695    749   -512  -1089       C  
ATOM   2743  CG  GLU A 364     -14.766  -1.337  38.031  1.00 98.64           C  
ANISOU 2743  CG  GLU A 364    13956  13180  10343    754   -524  -1267       C  
ATOM   2744  CD  GLU A 364     -13.726  -0.473  37.334  1.00119.05           C  
ANISOU 2744  CD  GLU A 364    16485  15682  13065    646   -708  -1357       C  
ATOM   2745  OE1 GLU A 364     -12.925  -1.011  36.539  1.00124.15           O  
ANISOU 2745  OE1 GLU A 364    16992  16335  13842    568   -800  -1276       O  
ATOM   2746  OE2 GLU A 364     -13.713   0.752  37.576  1.00127.97           O  
ANISOU 2746  OE2 GLU A 364    17712  16735  14176    639   -752  -1511       O  
ATOM   2747  N   GLU A 365     -17.809  -2.524  37.564  1.00 75.01           N  
ANISOU 2747  N   GLU A 365    10833  10201   7467    900    -23  -1053       N  
ATOM   2748  CA  GLU A 365     -18.904  -2.093  36.707  1.00 79.96           C  
ANISOU 2748  CA  GLU A 365    11354  10752   8274    917    107  -1054       C  
ATOM   2749  C   GLU A 365     -18.508  -0.861  35.901  1.00 65.84           C  
ANISOU 2749  C   GLU A 365     9543   8851   6621    865     -7  -1169       C  
ATOM   2750  O   GLU A 365     -17.744  -0.007  36.360  1.00 66.96           O  
ANISOU 2750  O   GLU A 365     9800   8963   6680    846   -133  -1294       O  
ATOM   2751  CB  GLU A 365     -20.166  -1.796  37.520  1.00 86.15           C  
ANISOU 2751  CB  GLU A 365    12218  11557   8958   1031    309  -1086       C  
ATOM   2752  CG  GLU A 365     -21.354  -1.400  36.649  1.00102.42           C  
ANISOU 2752  CG  GLU A 365    14149  13549  11217   1059    442  -1078       C  
ATOM   2753  CD  GLU A 365     -22.675  -1.515  37.366  1.00116.89           C  
ANISOU 2753  CD  GLU A 365    16002  15427  12983   1169    673  -1057       C  
ATOM   2754  OE1 GLU A 365     -22.660  -1.849  38.563  1.00125.97           O  
ANISOU 2754  OE1 GLU A 365    17288  16659  13916   1224    741  -1053       O  
ATOM   2755  OE2 GLU A 365     -23.729  -1.278  36.736  1.00122.24           O  
ANISOU 2755  OE2 GLU A 365    16558  16064  13824   1202    790  -1040       O  
ATOM   2756  N   ILE A 366     -19.040  -0.783  34.683  1.00 63.90           N  
ANISOU 2756  N   ILE A 366     9151   8541   6587    839     35  -1122       N  
ATOM   2757  CA  ILE A 366     -18.725   0.315  33.783  1.00 65.23           C  
ANISOU 2757  CA  ILE A 366     9290   8597   6899    789    -58  -1200       C  
ATOM   2758  C   ILE A 366     -19.282   1.619  34.342  1.00 65.65           C  
ANISOU 2758  C   ILE A 366     9467   8575   6901    865     -7  -1344       C  
ATOM   2759  O   ILE A 366     -20.393   1.667  34.889  1.00 69.17           O  
ANISOU 2759  O   ILE A 366     9946   9042   7293    969    156  -1354       O  
ATOM   2760  CB  ILE A 366     -19.274   0.015  32.377  1.00 64.77           C  
ANISOU 2760  CB  ILE A 366     9058   8499   7054    760    -17  -1104       C  
ATOM   2761  CG1 ILE A 366     -18.846   1.104  31.399  1.00 65.43           C  
ANISOU 2761  CG1 ILE A 366     9119   8467   7277    705   -117  -1164       C  
ATOM   2762  CG2 ILE A 366     -20.789  -0.137  32.405  1.00 64.04           C  
ANISOU 2762  CG2 ILE A 366     8912   8418   7002    852    169  -1066       C  
ATOM   2763  CD1 ILE A 366     -17.356   1.321  31.383  1.00 72.14           C  
ANISOU 2763  CD1 ILE A 366    10003   9303   8104    606   -292  -1204       C  
ATOM   2764  N   ARG A 367     -18.498   2.685  34.218  1.00 62.28           N  
ANISOU 2764  N   ARG A 367     9109   8055   6497    813   -142  -1458       N  
ATOM   2765  CA  ARG A 367     -18.895   4.020  34.632  1.00 59.79           C  
ANISOU 2765  CA  ARG A 367     8921   7637   6158    875   -116  -1608       C  
ATOM   2766  C   ARG A 367     -18.915   4.942  33.421  1.00 62.80           C  
ANISOU 2766  C   ARG A 367     9233   7876   6752    833   -160  -1622       C  
ATOM   2767  O   ARG A 367     -18.143   4.764  32.473  1.00 63.01           O  
ANISOU 2767  O   ARG A 367     9161   7882   6898    726   -268  -1557       O  
ATOM   2768  CB  ARG A 367     -17.948   4.567  35.704  1.00 64.35           C  
ANISOU 2768  CB  ARG A 367     9676   8212   6562    850   -244  -1750       C  
ATOM   2769  CG  ARG A 367     -18.088   3.882  37.052  1.00 76.97           C  
ANISOU 2769  CG  ARG A 367    11389   9942   7913    923   -186  -1756       C  
ATOM   2770  CD  ARG A 367     -16.899   4.182  37.950  1.00 87.83           C  
ANISOU 2770  CD  ARG A 367    12910  11339   9121    871   -367  -1872       C  
ATOM   2771  NE  ARG A 367     -16.348   5.512  37.705  1.00 98.08           N  
ANISOU 2771  NE  ARG A 367    14272  12492  10503    809   -494  -2023       N  
ATOM   2772  CZ  ARG A 367     -16.804   6.630  38.263  1.00102.22           C  
ANISOU 2772  CZ  ARG A 367    14952  12920  10967    878   -453  -2186       C  
ATOM   2773  NH1 ARG A 367     -17.831   6.585  39.101  1.00101.01           N  
ANISOU 2773  NH1 ARG A 367    14902  12814  10663   1019   -280  -2220       N  
ATOM   2774  NH2 ARG A 367     -16.236   7.795  37.979  1.00105.02           N  
ANISOU 2774  NH2 ARG A 367    15359  13125  11419    806   -578  -2314       N  
ATOM   2775  N   PHE A 368     -19.809   5.934  33.458  1.00 55.75           N  
ANISOU 2775  N   PHE A 368     8396   6884   5902    925    -69  -1702       N  
ATOM   2776  CA  PHE A 368     -20.023   6.800  32.313  1.00 56.66           C  
ANISOU 2776  CA  PHE A 368     8451   6861   6217    910    -89  -1696       C  
ATOM   2777  C   PHE A 368     -19.753   8.255  32.671  1.00 66.75           C  
ANISOU 2777  C   PHE A 368     9886   7982   7493    920   -147  -1860       C  
ATOM   2778  O   PHE A 368     -20.014   8.672  33.805  1.00 75.89           O  
ANISOU 2778  O   PHE A 368    11193   9135   8505   1000    -98  -1987       O  
ATOM   2779  CB  PHE A 368     -21.463   6.667  31.790  1.00 55.31           C  
ANISOU 2779  CB  PHE A 368     8171   6694   6151   1021     71  -1620       C  
ATOM   2780  CG  PHE A 368     -21.887   5.249  31.538  1.00 56.17           C  
ANISOU 2780  CG  PHE A 368     8133   6945   6264   1015    141  -1474       C  
ATOM   2781  CD1 PHE A 368     -21.560   4.616  30.350  1.00 59.43           C  
ANISOU 2781  CD1 PHE A 368     8403   7376   6804    927     74  -1353       C  
ATOM   2782  CD2 PHE A 368     -22.610   4.548  32.489  1.00 60.25           C  
ANISOU 2782  CD2 PHE A 368     8662   7571   6658   1097    281  -1457       C  
ATOM   2783  CE1 PHE A 368     -21.945   3.311  30.116  1.00 60.28           C  
ANISOU 2783  CE1 PHE A 368     8384   7597   6922    917    134  -1230       C  
ATOM   2784  CE2 PHE A 368     -23.000   3.241  32.261  1.00 62.22           C  
ANISOU 2784  CE2 PHE A 368     8779   7934   6927   1081    347  -1320       C  
ATOM   2785  CZ  PHE A 368     -22.668   2.622  31.073  1.00 64.20           C  
ANISOU 2785  CZ  PHE A 368     8889   8190   7312    990    268  -1212       C  
ATOM   2786  N   PRO A 369     -19.230   9.046  31.740  1.00 72.31           N  
ANISOU 2786  N   PRO A 369    10571   8551   8353    840   -245  -1863       N  
ATOM   2787  CA  PRO A 369     -19.141  10.489  31.973  1.00 70.08           C  
ANISOU 2787  CA  PRO A 369    10434   8088   8104    856   -281  -2011       C  
ATOM   2788  C   PRO A 369     -20.525  11.115  31.954  1.00 73.14           C  
ANISOU 2788  C   PRO A 369    10845   8400   8547   1020   -128  -2039       C  
ATOM   2789  O   PRO A 369     -21.456  10.603  31.327  1.00 65.22           O  
ANISOU 2789  O   PRO A 369     9704   7452   7624   1090    -24  -1919       O  
ATOM   2790  CB  PRO A 369     -18.285  10.987  30.803  1.00 71.49           C  
ANISOU 2790  CB  PRO A 369    10553   8153   8458    722   -405  -1958       C  
ATOM   2791  CG  PRO A 369     -18.523   9.985  29.723  1.00 73.21           C  
ANISOU 2791  CG  PRO A 369    10582   8471   8763    702   -371  -1774       C  
ATOM   2792  CD  PRO A 369     -18.684   8.663  30.427  1.00 73.00           C  
ANISOU 2792  CD  PRO A 369    10510   8637   8590    731   -319  -1729       C  
ATOM   2793  N   ARG A 370     -20.655  12.240  32.659  1.00 87.18           N  
ANISOU 2793  N   ARG A 370    12795  10045  10285   1084   -118  -2204       N  
ATOM   2794  CA  ARG A 370     -21.946  12.912  32.751  1.00 89.69           C  
ANISOU 2794  CA  ARG A 370    13145  10281  10652   1258     33  -2248       C  
ATOM   2795  C   ARG A 370     -22.394  13.522  31.429  1.00 89.53           C  
ANISOU 2795  C   ARG A 370    13029  10128  10861   1277     35  -2157       C  
ATOM   2796  O   ARG A 370     -23.537  13.981  31.336  1.00 92.95           O  
ANISOU 2796  O   ARG A 370    13448  10505  11363   1431    159  -2162       O  
ATOM   2797  CB  ARG A 370     -21.898  13.991  33.834  1.00 92.44           C  
ANISOU 2797  CB  ARG A 370    13720  10506  10897   1323     38  -2463       C  
ATOM   2798  CG  ARG A 370     -21.879  13.438  35.251  1.00102.12           C  
ANISOU 2798  CG  ARG A 370    15058  11876  11867   1370     88  -2557       C  
ATOM   2799  CD  ARG A 370     -21.576  14.527  36.269  1.00107.43           C  
ANISOU 2799  CD  ARG A 370    15976  12420  12424   1403     48  -2789       C  
ATOM   2800  NE  ARG A 370     -20.603  14.066  37.258  1.00109.40           N  
ANISOU 2800  NE  ARG A 370    16334  12778  12455   1315    -67  -2870       N  
ATOM   2801  CZ  ARG A 370     -19.284  14.093  37.074  1.00108.56           C  
ANISOU 2801  CZ  ARG A 370    16233  12648  12368   1136   -274  -2885       C  
ATOM   2802  NH1 ARG A 370     -18.773  14.560  35.936  1.00113.44           N  
ANISOU 2802  NH1 ARG A 370    16760  13134  13209   1020   -374  -2822       N  
ATOM   2803  NH2 ARG A 370     -18.469  13.652  38.025  1.00 99.57           N  
ANISOU 2803  NH2 ARG A 370    15187  11621  11025   1073   -382  -2958       N  
ATOM   2804  N   THR A 371     -21.531  13.535  30.410  1.00 86.42           N  
ANISOU 2804  N   THR A 371    12568   9686  10581   1132    -94  -2069       N  
ATOM   2805  CA  THR A 371     -21.917  14.087  29.116  1.00 96.77           C  
ANISOU 2805  CA  THR A 371    13799  10878  12091   1150    -97  -1967       C  
ATOM   2806  C   THR A 371     -22.878  13.169  28.369  1.00 88.58           C  
ANISOU 2806  C   THR A 371    12570   9974  11111   1220    -11  -1807       C  
ATOM   2807  O   THR A 371     -23.651  13.640  27.527  1.00 93.23           O  
ANISOU 2807  O   THR A 371    13099  10483  11840   1304     25  -1739       O  
ATOM   2808  CB  THR A 371     -20.676  14.349  28.259  1.00106.40           C  
ANISOU 2808  CB  THR A 371    15009  12016  13402    970   -247  -1914       C  
ATOM   2809  OG1 THR A 371     -21.077  14.786  26.954  1.00110.67           O  
ANISOU 2809  OG1 THR A 371    15475  12459  14115    993   -244  -1792       O  
ATOM   2810  CG2 THR A 371     -19.835  13.085  28.128  1.00105.59           C  
ANISOU 2810  CG2 THR A 371    14796  12095  13228    839   -313  -1826       C  
ATOM   2811  N   LEU A 372     -22.851  11.871  28.659  1.00 78.53           N  
ANISOU 2811  N   LEU A 372    11202   8897   9738   1188     16  -1744       N  
ATOM   2812  CA  LEU A 372     -23.701  10.931  27.943  1.00 72.74           C  
ANISOU 2812  CA  LEU A 372    10284   8288   9068   1231     84  -1599       C  
ATOM   2813  C   LEU A 372     -25.157  11.087  28.357  1.00 70.34           C  
ANISOU 2813  C   LEU A 372     9945   7998   8781   1414    242  -1620       C  
ATOM   2814  O   LEU A 372     -25.473  11.228  29.542  1.00 68.03           O  
ANISOU 2814  O   LEU A 372     9749   7726   8372   1496    335  -1730       O  
ATOM   2815  CB  LEU A 372     -23.247   9.497  28.199  1.00 65.89           C  
ANISOU 2815  CB  LEU A 372     9336   7606   8094   1144     74  -1531       C  
ATOM   2816  CG  LEU A 372     -22.019   9.015  27.437  1.00 68.82           C  
ANISOU 2816  CG  LEU A 372     9660   8000   8487    978    -63  -1456       C  
ATOM   2817  CD1 LEU A 372     -21.805   7.543  27.716  1.00 65.17           C  
ANISOU 2817  CD1 LEU A 372     9112   7718   7933    928    -49  -1384       C  
ATOM   2818  CD2 LEU A 372     -22.183   9.264  25.949  1.00 69.76           C  
ANISOU 2818  CD2 LEU A 372     9683   8054   8769    958   -104  -1345       C  
ATOM   2819  N   GLY A 373     -26.046  11.055  27.369  1.00 63.93           N  
ANISOU 2819  N   GLY A 373     8993   7184   8115   1480    272  -1514       N  
ATOM   2820  CA  GLY A 373     -27.463  11.052  27.629  1.00 65.54           C  
ANISOU 2820  CA  GLY A 373     9112   7426   8365   1647    418  -1510       C  
ATOM   2821  C   GLY A 373     -27.912   9.713  28.174  1.00 65.84           C  
ANISOU 2821  C   GLY A 373     9037   7660   8319   1644    517  -1458       C  
ATOM   2822  O   GLY A 373     -27.152   8.739  28.204  1.00 66.11           O  
ANISOU 2822  O   GLY A 373     9052   7796   8273   1516    460  -1409       O  
ATOM   2823  N   PRO A 374     -29.167   9.639  28.621  1.00 66.56           N  
ANISOU 2823  N   PRO A 374     9049   7803   8437   1788    673  -1462       N  
ATOM   2824  CA  PRO A 374     -29.654   8.373  29.183  1.00 67.05           C  
ANISOU 2824  CA  PRO A 374     9004   8044   8430   1782    786  -1403       C  
ATOM   2825  C   PRO A 374     -29.797   7.278  28.144  1.00 58.67           C  
ANISOU 2825  C   PRO A 374     7748   7078   7466   1691    728  -1253       C  
ATOM   2826  O   PRO A 374     -29.612   6.102  28.479  1.00 57.39           O  
ANISOU 2826  O   PRO A 374     7536   7041   7227   1613    757  -1198       O  
ATOM   2827  CB  PRO A 374     -31.007   8.759  29.797  1.00 64.99           C  
ANISOU 2827  CB  PRO A 374     8693   7792   8207   1967    975  -1445       C  
ATOM   2828  CG  PRO A 374     -31.456   9.938  28.992  1.00 69.31           C  
ANISOU 2828  CG  PRO A 374     9226   8190   8919   2064    930  -1460       C  
ATOM   2829  CD  PRO A 374     -30.209  10.680  28.593  1.00 68.75           C  
ANISOU 2829  CD  PRO A 374     9319   7978   8825   1964    760  -1509       C  
ATOM   2830  N   GLU A 375     -30.110   7.623  26.893  1.00 59.76           N  
ANISOU 2830  N   GLU A 375     7784   7156   7764   1700    644  -1186       N  
ATOM   2831  CA  GLU A 375     -30.226   6.593  25.867  1.00 60.43           C  
ANISOU 2831  CA  GLU A 375     7699   7331   7931   1612    575  -1058       C  
ATOM   2832  C   GLU A 375     -28.869   5.977  25.552  1.00 54.84           C  
ANISOU 2832  C   GLU A 375     7054   6643   7138   1443    449  -1029       C  
ATOM   2833  O   GLU A 375     -28.762   4.758  25.374  1.00 56.06           O  
ANISOU 2833  O   GLU A 375     7117   6907   7278   1358    442   -955       O  
ATOM   2834  CB  GLU A 375     -30.872   7.167  24.606  1.00 70.57           C  
ANISOU 2834  CB  GLU A 375     8878   8549   9386   1672    503   -997       C  
ATOM   2835  CG  GLU A 375     -32.389   7.352  24.701  1.00 83.19           C  
ANISOU 2835  CG  GLU A 375    10326  10176  11106   1829    621   -984       C  
ATOM   2836  CD  GLU A 375     -32.788   8.573  25.512  1.00 91.92           C  
ANISOU 2836  CD  GLU A 375    11542  11177  12207   1985    722  -1092       C  
ATOM   2837  OE1 GLU A 375     -33.932   8.613  26.019  1.00 95.54           O  
ANISOU 2837  OE1 GLU A 375    11898  11681  12724   2118    868  -1105       O  
ATOM   2838  OE2 GLU A 375     -31.956   9.495  25.642  1.00 92.78           O  
ANISOU 2838  OE2 GLU A 375    11838  11154  12259   1973    660  -1168       O  
ATOM   2839  N   ALA A 376     -27.818   6.797  25.486  1.00 53.94           N  
ANISOU 2839  N   ALA A 376     7093   6420   6981   1393    352  -1087       N  
ATOM   2840  CA  ALA A 376     -26.477   6.247  25.321  1.00 48.71           C  
ANISOU 2840  CA  ALA A 376     6485   5783   6238   1240    244  -1068       C  
ATOM   2841  C   ALA A 376     -26.080   5.405  26.527  1.00 48.49           C  
ANISOU 2841  C   ALA A 376     6507   5858   6058   1203    302  -1102       C  
ATOM   2842  O   ALA A 376     -25.482   4.334  26.374  1.00 57.40           O  
ANISOU 2842  O   ALA A 376     7590   7074   7144   1102    259  -1039       O  
ATOM   2843  CB  ALA A 376     -25.466   7.371  25.093  1.00 50.45           C  
ANISOU 2843  CB  ALA A 376     6849   5862   6458   1192    139  -1128       C  
ATOM   2844  N   LYS A 377     -26.419   5.862  27.736  1.00 46.52           N  
ANISOU 2844  N   LYS A 377     6358   5601   5718   1292    404  -1199       N  
ATOM   2845  CA  LYS A 377     -26.070   5.101  28.931  1.00 51.52           C  
ANISOU 2845  CA  LYS A 377     7057   6336   6182   1269    461  -1225       C  
ATOM   2846  C   LYS A 377     -26.875   3.812  29.021  1.00 49.63           C  
ANISOU 2846  C   LYS A 377     6671   6229   5955   1278    569  -1122       C  
ATOM   2847  O   LYS A 377     -26.343   2.770  29.420  1.00 50.55           O  
ANISOU 2847  O   LYS A 377     6792   6437   5978   1203    563  -1076       O  
ATOM   2848  CB  LYS A 377     -26.274   5.953  30.184  1.00 55.49           C  
ANISOU 2848  CB  LYS A 377     7719   6796   6568   1371    548  -1361       C  
ATOM   2849  CG  LYS A 377     -25.246   7.060  30.337  1.00 65.64           C  
ANISOU 2849  CG  LYS A 377     9176   7953   7809   1330    426  -1478       C  
ATOM   2850  CD  LYS A 377     -25.232   7.644  31.741  1.00 65.37           C  
ANISOU 2850  CD  LYS A 377     9326   7902   7610   1408    493  -1625       C  
ATOM   2851  CE  LYS A 377     -26.511   8.401  32.051  1.00 70.80           C  
ANISOU 2851  CE  LYS A 377    10020   8536   8345   1580    649  -1685       C  
ATOM   2852  NZ  LYS A 377     -26.384   9.192  33.311  1.00 75.21           N  
ANISOU 2852  NZ  LYS A 377    10789   9043   8742   1658    697  -1855       N  
ATOM   2853  N   SER A 378     -28.158   3.863  28.652  1.00 43.85           N  
ANISOU 2853  N   SER A 378     5804   5506   5349   1367    666  -1082       N  
ATOM   2854  CA  SER A 378     -28.985   2.661  28.688  1.00 47.73           C  
ANISOU 2854  CA  SER A 378     6139   6115   5882   1364    770   -984       C  
ATOM   2855  C   SER A 378     -28.469   1.608  27.717  1.00 52.55           C  
ANISOU 2855  C   SER A 378     6650   6766   6549   1232    658   -883       C  
ATOM   2856  O   SER A 378     -28.423   0.418  28.047  1.00 58.64           O  
ANISOU 2856  O   SER A 378     7377   7626   7277   1174    702   -817       O  
ATOM   2857  CB  SER A 378     -30.439   3.014  28.372  1.00 53.63           C  
ANISOU 2857  CB  SER A 378     6737   6858   6782   1481    875   -965       C  
ATOM   2858  OG  SER A 378     -31.227   1.844  28.226  1.00 49.43           O  
ANISOU 2858  OG  SER A 378     6027   6430   6325   1454    954   -864       O  
ATOM   2859  N   LEU A 379     -28.074   2.029  26.515  1.00 49.14           N  
ANISOU 2859  N   LEU A 379     6193   6266   6211   1188    519   -867       N  
ATOM   2860  CA  LEU A 379     -27.546   1.086  25.537  1.00 44.01           C  
ANISOU 2860  CA  LEU A 379     5465   5652   5607   1071    414   -783       C  
ATOM   2861  C   LEU A 379     -26.199   0.533  25.981  1.00 42.28           C  
ANISOU 2861  C   LEU A 379     5352   5457   5255    972    351   -789       C  
ATOM   2862  O   LEU A 379     -25.966  -0.681  25.933  1.00 45.86           O  
ANISOU 2862  O   LEU A 379     5751   5981   5692    902    349   -722       O  
ATOM   2863  CB  LEU A 379     -27.419   1.761  24.172  1.00 46.44           C  
ANISOU 2863  CB  LEU A 379     5741   5881   6023   1059    290   -766       C  
ATOM   2864  CG  LEU A 379     -26.752   0.916  23.085  1.00 50.04           C  
ANISOU 2864  CG  LEU A 379     6142   6365   6507    944    177   -694       C  
ATOM   2865  CD1 LEU A 379     -27.753  -0.041  22.464  1.00 52.44           C  
ANISOU 2865  CD1 LEU A 379     6273   6737   6913    940    200   -621       C  
ATOM   2866  CD2 LEU A 379     -26.110   1.794  22.026  1.00 50.39           C  
ANISOU 2866  CD2 LEU A 379     6237   6321   6589    919     55   -694       C  
ATOM   2867  N   LEU A 380     -25.297   1.412  26.423  1.00 45.09           N  
ANISOU 2867  N   LEU A 380     5857   5751   5525    967    294   -871       N  
ATOM   2868  CA  LEU A 380     -23.955   0.974  26.792  1.00 53.70           C  
ANISOU 2868  CA  LEU A 380     7034   6866   6503    874    212   -879       C  
ATOM   2869  C   LEU A 380     -23.976   0.071  28.021  1.00 52.93           C  
ANISOU 2869  C   LEU A 380     6975   6863   6274    884    298   -867       C  
ATOM   2870  O   LEU A 380     -23.256  -0.932  28.071  1.00 52.11           O  
ANISOU 2870  O   LEU A 380     6862   6817   6122    810    255   -812       O  
ATOM   2871  CB  LEU A 380     -23.055   2.188  27.022  1.00 54.86           C  
ANISOU 2871  CB  LEU A 380     7323   6920   6603    860    125   -977       C  
ATOM   2872  CG  LEU A 380     -22.685   2.982  25.767  1.00 46.27           C  
ANISOU 2872  CG  LEU A 380     6215   5732   5632    820     23   -967       C  
ATOM   2873  CD1 LEU A 380     -21.899   4.227  26.125  1.00 43.33           C  
ANISOU 2873  CD1 LEU A 380     5986   5253   5226    805    -44  -1069       C  
ATOM   2874  CD2 LEU A 380     -21.897   2.116  24.811  1.00 46.61           C  
ANISOU 2874  CD2 LEU A 380     6182   5818   5711    713    -63   -881       C  
ATOM   2875  N   SER A 381     -24.795   0.402  29.022  1.00 48.74           N  
ANISOU 2875  N   SER A 381     6491   6349   5680    982    428   -914       N  
ATOM   2876  CA  SER A 381     -24.889  -0.469  30.190  1.00 54.83           C  
ANISOU 2876  CA  SER A 381     7304   7214   6313    999    528   -888       C  
ATOM   2877  C   SER A 381     -25.579  -1.785  29.850  1.00 53.99           C  
ANISOU 2877  C   SER A 381     7047   7178   6287    970    606   -764       C  
ATOM   2878  O   SER A 381     -25.260  -2.820  30.441  1.00 58.14           O  
ANISOU 2878  O   SER A 381     7594   7771   6724    935    635   -703       O  
ATOM   2879  CB  SER A 381     -25.626   0.239  31.328  1.00 44.64           C  
ANISOU 2879  CB  SER A 381     6108   5927   4925   1118    666   -970       C  
ATOM   2880  OG  SER A 381     -26.978   0.479  30.978  1.00 67.59           O  
ANISOU 2880  OG  SER A 381     8892   8824   7965   1200    787   -950       O  
ATOM   2881  N   GLY A 382     -26.517  -1.768  28.903  1.00 51.29           N  
ANISOU 2881  N   GLY A 382     6556   6817   6116    984    631   -725       N  
ATOM   2882  CA  GLY A 382     -27.123  -3.013  28.457  1.00 40.28           C  
ANISOU 2882  CA  GLY A 382     5011   5475   4819    937    679   -618       C  
ATOM   2883  C   GLY A 382     -26.152  -3.890  27.687  1.00 43.00           C  
ANISOU 2883  C   GLY A 382     5335   5820   5183    825    550   -562       C  
ATOM   2884  O   GLY A 382     -26.167  -5.118  27.818  1.00 45.99           O  
ANISOU 2884  O   GLY A 382     5668   6245   5563    774    586   -483       O  
ATOM   2885  N   LEU A 383     -25.288  -3.273  26.876  1.00 42.27           N  
ANISOU 2885  N   LEU A 383     5279   5672   5110    786    406   -601       N  
ATOM   2886  CA  LEU A 383     -24.349  -4.047  26.071  1.00 42.89           C  
ANISOU 2886  CA  LEU A 383     5333   5752   5211    690    293   -553       C  
ATOM   2887  C   LEU A 383     -23.184  -4.573  26.901  1.00 51.79           C  
ANISOU 2887  C   LEU A 383     6566   6912   6198    652    259   -549       C  
ATOM   2888  O   LEU A 383     -22.557  -5.571  26.524  1.00 47.78           O  
ANISOU 2888  O   LEU A 383     6029   6424   5702    587    208   -490       O  
ATOM   2889  CB  LEU A 383     -23.829  -3.199  24.908  1.00 42.93           C  
ANISOU 2889  CB  LEU A 383     5338   5691   5284    663    168   -585       C  
ATOM   2890  CG  LEU A 383     -24.821  -2.842  23.800  1.00 48.32           C  
ANISOU 2890  CG  LEU A 383     5909   6343   6107    690    161   -569       C  
ATOM   2891  CD1 LEU A 383     -24.220  -1.821  22.843  1.00 48.93           C  
ANISOU 2891  CD1 LEU A 383     6027   6348   6218    677     49   -598       C  
ATOM   2892  CD2 LEU A 383     -25.240  -4.092  23.049  1.00 40.32           C  
ANISOU 2892  CD2 LEU A 383     4772   5371   5179    637    156   -495       C  
ATOM   2893  N   LEU A 384     -22.879  -3.931  28.029  1.00 42.47           N  
ANISOU 2893  N   LEU A 384     5512   5739   4884    698    281   -612       N  
ATOM   2894  CA  LEU A 384     -21.715  -4.290  28.830  1.00 41.24           C  
ANISOU 2894  CA  LEU A 384     5463   5620   4588    669    220   -617       C  
ATOM   2895  C   LEU A 384     -22.089  -4.996  30.131  1.00 40.78           C  
ANISOU 2895  C   LEU A 384     5464   5632   4400    715    336   -578       C  
ATOM   2896  O   LEU A 384     -21.294  -5.005  31.076  1.00 49.45           O  
ANISOU 2896  O   LEU A 384     6681   6765   5343    722    296   -603       O  
ATOM   2897  CB  LEU A 384     -20.869  -3.049  29.117  1.00 43.37           C  
ANISOU 2897  CB  LEU A 384     5846   5845   4787    670    123   -725       C  
ATOM   2898  CG  LEU A 384     -20.391  -2.294  27.874  1.00 44.08           C  
ANISOU 2898  CG  LEU A 384     5893   5858   4998    618     15   -751       C  
ATOM   2899  CD1 LEU A 384     -19.638  -1.030  28.261  1.00 35.77           C  
ANISOU 2899  CD1 LEU A 384     4956   4746   3889    613    -68   -860       C  
ATOM   2900  CD2 LEU A 384     -19.530  -3.187  26.989  1.00 40.48           C  
ANISOU 2900  CD2 LEU A 384     5361   5420   4599    534    -70   -679       C  
ATOM   2901  N   LYS A 385     -23.282  -5.583  30.203  1.00 36.49           N  
ANISOU 2901  N   LYS A 385     4837   5113   3916    744    478   -515       N  
ATOM   2902  CA  LYS A 385     -23.618  -6.436  31.335  1.00 43.54           C  
ANISOU 2902  CA  LYS A 385     5775   6071   4696    775    601   -448       C  
ATOM   2903  C   LYS A 385     -22.684  -7.639  31.370  1.00 45.78           C  
ANISOU 2903  C   LYS A 385     6073   6379   4941    713    532   -363       C  
ATOM   2904  O   LYS A 385     -22.384  -8.245  30.337  1.00 48.03           O  
ANISOU 2904  O   LYS A 385     6264   6634   5351    646    459   -319       O  
ATOM   2905  CB  LYS A 385     -25.073  -6.898  31.248  1.00 43.37           C  
ANISOU 2905  CB  LYS A 385     5630   6063   4786    798    768   -384       C  
ATOM   2906  CG  LYS A 385     -26.093  -5.778  31.336  1.00 60.22           C  
ANISOU 2906  CG  LYS A 385     7739   8181   6960    881    859   -459       C  
ATOM   2907  CD  LYS A 385     -26.010  -5.054  32.671  1.00 73.95           C  
ANISOU 2907  CD  LYS A 385     9644   9951   8503    969    931   -533       C  
ATOM   2908  CE  LYS A 385     -27.072  -3.969  32.784  1.00 87.27           C  
ANISOU 2908  CE  LYS A 385    11306  11616  10238   1068   1040   -610       C  
ATOM   2909  NZ  LYS A 385     -26.915  -3.163  34.029  1.00 96.80           N  
ANISOU 2909  NZ  LYS A 385    12697  12840  11244   1158   1098   -708       N  
ATOM   2910  N   LYS A 386     -22.212  -7.977  32.570  1.00 43.44           N  
ANISOU 2910  N   LYS A 386     5904   6136   4464    744    552   -340       N  
ATOM   2911  CA  LYS A 386     -21.242  -9.059  32.705  1.00 42.67           C  
ANISOU 2911  CA  LYS A 386     5834   6061   4320    704    476   -257       C  
ATOM   2912  C   LYS A 386     -21.865 -10.408  32.368  1.00 53.77           C  
ANISOU 2912  C   LYS A 386     7138   7456   5836    668    570   -129       C  
ATOM   2913  O   LYS A 386     -21.229 -11.247  31.719  1.00 52.35           O  
ANISOU 2913  O   LYS A 386     6909   7249   5731    613    489    -74       O  
ATOM   2914  CB  LYS A 386     -20.673  -9.069  34.121  1.00 49.32           C  
ANISOU 2914  CB  LYS A 386     6842   6968   4929    758    471   -258       C  
ATOM   2915  CG  LYS A 386     -20.075  -7.745  34.548  1.00 50.79           C  
ANISOU 2915  CG  LYS A 386     7140   7158   5000    787    372   -399       C  
ATOM   2916  CD  LYS A 386     -18.583  -7.728  34.318  1.00 54.61           C  
ANISOU 2916  CD  LYS A 386     7646   7642   5462    737    170   -425       C  
ATOM   2917  CE  LYS A 386     -17.972  -6.417  34.771  1.00 52.02           C  
ANISOU 2917  CE  LYS A 386     7425   7309   5032    749     62   -570       C  
ATOM   2918  NZ  LYS A 386     -18.149  -5.348  33.753  1.00 60.65           N  
ANISOU 2918  NZ  LYS A 386     8447   8319   6279    715     27   -660       N  
ATOM   2919  N   ASP A 387     -23.101 -10.633  32.804  1.00 49.92           N  
ANISOU 2919  N   ASP A 387     6617   6984   5367    697    746    -82       N  
ATOM   2920  CA  ASP A 387     -23.809 -11.883  32.569  1.00 52.52           C  
ANISOU 2920  CA  ASP A 387     6848   7294   5813    653    851     39       C  
ATOM   2921  C   ASP A 387     -24.356 -11.908  31.146  1.00 52.23           C  
ANISOU 2921  C   ASP A 387     6643   7201   6003    592    814     18       C  
ATOM   2922  O   ASP A 387     -25.251 -11.118  30.814  1.00 54.71           O  
ANISOU 2922  O   ASP A 387     6881   7511   6397    614    864    -39       O  
ATOM   2923  CB  ASP A 387     -24.937 -12.048  33.591  1.00 58.23           C  
ANISOU 2923  CB  ASP A 387     7587   8061   6477    703   1063     98       C  
ATOM   2924  CG  ASP A 387     -25.655 -13.380  33.469  1.00 67.44           C  
ANISOU 2924  CG  ASP A 387     8656   9201   7769    645   1181    234       C  
ATOM   2925  OD1 ASP A 387     -25.199 -14.241  32.689  1.00 66.58           O  
ANISOU 2925  OD1 ASP A 387     8491   9037   7770    574   1090    279       O  
ATOM   2926  OD2 ASP A 387     -26.682 -13.563  34.159  1.00 74.24           O  
ANISOU 2926  OD2 ASP A 387     9495  10091   8621    671   1371    294       O  
ATOM   2927  N   PRO A 388     -23.856 -12.797  30.283  1.00 46.05           N  
ANISOU 2927  N   PRO A 388     5802   6371   5323    522    726     61       N  
ATOM   2928  CA  PRO A 388     -24.338 -12.815  28.892  1.00 49.33           C  
ANISOU 2928  CA  PRO A 388     6073   6737   5933    466    676     31       C  
ATOM   2929  C   PRO A 388     -25.824 -13.106  28.764  1.00 44.52           C  
ANISOU 2929  C   PRO A 388     5334   6122   5461    449    811     69       C  
ATOM   2930  O   PRO A 388     -26.467 -12.589  27.842  1.00 47.04           O  
ANISOU 2930  O   PRO A 388     5540   6424   5907    437    779     16       O  
ATOM   2931  CB  PRO A 388     -23.486 -13.914  28.239  1.00 53.59           C  
ANISOU 2931  CB  PRO A 388     6605   7232   6525    404    582     78       C  
ATOM   2932  CG  PRO A 388     -23.029 -14.768  29.373  1.00 49.61           C  
ANISOU 2932  CG  PRO A 388     6204   6745   5902    425    638    172       C  
ATOM   2933  CD  PRO A 388     -22.838 -13.833  30.529  1.00 46.91           C  
ANISOU 2933  CD  PRO A 388     5979   6471   5374    501    667    136       C  
ATOM   2934  N   LYS A 389     -26.395 -13.906  29.668  1.00 54.75           N  
ANISOU 2934  N   LYS A 389     6635   7432   6735    448    961    165       N  
ATOM   2935  CA  LYS A 389     -27.825 -14.188  29.609  1.00 62.76           C  
ANISOU 2935  CA  LYS A 389     7506   8444   7894    425   1101    207       C  
ATOM   2936  C   LYS A 389     -28.674 -12.974  29.974  1.00 59.93           C  
ANISOU 2936  C   LYS A 389     7116   8136   7518    504   1189    143       C  
ATOM   2937  O   LYS A 389     -29.872 -12.960  29.673  1.00 61.39           O  
ANISOU 2937  O   LYS A 389     7147   8324   7855    492   1276    153       O  
ATOM   2938  CB  LYS A 389     -28.171 -15.366  30.525  1.00 71.91           C  
ANISOU 2938  CB  LYS A 389     8687   9601   9036    398   1255    341       C  
ATOM   2939  CG  LYS A 389     -27.457 -16.666  30.163  1.00 77.41           C  
ANISOU 2939  CG  LYS A 389     9408  10227   9776    324   1184    413       C  
ATOM   2940  CD  LYS A 389     -28.295 -17.883  30.532  1.00 84.35           C  
ANISOU 2940  CD  LYS A 389    10222  11065  10762    259   1338    542       C  
ATOM   2941  CE  LYS A 389     -28.388 -18.071  32.038  1.00 90.77           C  
ANISOU 2941  CE  LYS A 389    11155  11928  11407    317   1507    644       C  
ATOM   2942  NZ  LYS A 389     -27.109 -18.566  32.619  1.00 90.38           N  
ANISOU 2942  NZ  LYS A 389    11284  11872  11186    350   1435    698       N  
ATOM   2943  N   GLN A 390     -28.087 -11.965  30.617  1.00 59.54           N  
ANISOU 2943  N   GLN A 390     7204   8123   7296    586   1166     73       N  
ATOM   2944  CA  GLN A 390     -28.778 -10.720  30.926  1.00 59.21           C  
ANISOU 2944  CA  GLN A 390     7152   8112   7232    674   1237     -6       C  
ATOM   2945  C   GLN A 390     -28.350  -9.572  30.022  1.00 59.03           C  
ANISOU 2945  C   GLN A 390     7130   8056   7241    694   1078   -121       C  
ATOM   2946  O   GLN A 390     -28.874  -8.462  30.162  1.00 61.01           O  
ANISOU 2946  O   GLN A 390     7377   8314   7489    772   1118   -195       O  
ATOM   2947  CB  GLN A 390     -28.545 -10.331  32.393  1.00 57.76           C  
ANISOU 2947  CB  GLN A 390     7139   7985   6822    760   1343    -13       C  
ATOM   2948  CG  GLN A 390     -29.185 -11.271  33.407  1.00 63.73           C  
ANISOU 2948  CG  GLN A 390     7900   8784   7531    763   1544    108       C  
ATOM   2949  CD  GLN A 390     -30.700 -11.159  33.442  1.00 77.77           C  
ANISOU 2949  CD  GLN A 390     9515  10582   9450    787   1730    132       C  
ATOM   2950  OE1 GLN A 390     -31.250 -10.069  33.606  1.00 86.78           O  
ANISOU 2950  OE1 GLN A 390    10643  11746  10582    874   1786     47       O  
ATOM   2951  NE2 GLN A 390     -31.381 -12.289  33.288  1.00 79.61           N  
ANISOU 2951  NE2 GLN A 390     9619  10802   9827    708   1826    247       N  
ATOM   2952  N   ARG A 391     -27.422  -9.810  29.102  1.00 49.10           N  
ANISOU 2952  N   ARG A 391     5880   6759   6017    629    909   -134       N  
ATOM   2953  CA  ARG A 391     -26.882  -8.753  28.261  1.00 55.54           C  
ANISOU 2953  CA  ARG A 391     6714   7540   6851    640    762   -227       C  
ATOM   2954  C   ARG A 391     -27.854  -8.403  27.141  1.00 52.04           C  
ANISOU 2954  C   ARG A 391     6112   7072   6590    636    742   -246       C  
ATOM   2955  O   ARG A 391     -28.555  -9.270  26.611  1.00 48.09           O  
ANISOU 2955  O   ARG A 391     5478   6569   6224    582    768   -189       O  
ATOM   2956  CB  ARG A 391     -25.539  -9.191  27.678  1.00 45.27           C  
ANISOU 2956  CB  ARG A 391     5468   6213   5519    574    608   -224       C  
ATOM   2957  CG  ARG A 391     -24.785  -8.119  26.917  1.00 39.42           C  
ANISOU 2957  CG  ARG A 391     4764   5437   4775    576    466   -308       C  
ATOM   2958  CD  ARG A 391     -23.440  -8.653  26.478  1.00 37.67           C  
ANISOU 2958  CD  ARG A 391     4589   5204   4521    514    341   -294       C  
ATOM   2959  NE  ARG A 391     -22.682  -9.166  27.616  1.00 40.09           N  
ANISOU 2959  NE  ARG A 391     5002   5545   4683    523    357   -263       N  
ATOM   2960  CZ  ARG A 391     -21.782 -10.140  27.542  1.00 45.02           C  
ANISOU 2960  CZ  ARG A 391     5645   6171   5288    481    299   -210       C  
ATOM   2961  NH1 ARG A 391     -21.525 -10.722  26.378  1.00 34.66           N  
ANISOU 2961  NH1 ARG A 391     4256   4825   4088    425    232   -191       N  
ATOM   2962  NH2 ARG A 391     -21.148 -10.540  28.637  1.00 32.68           N  
ANISOU 2962  NH2 ARG A 391     4183   4646   3588    504    309   -176       N  
ATOM   2963  N   LEU A 392     -27.896  -7.121  26.791  1.00 47.10           N  
ANISOU 2963  N   LEU A 392     5504   6422   5971    693    688   -327       N  
ATOM   2964  CA  LEU A 392     -28.722  -6.663  25.682  1.00 50.35           C  
ANISOU 2964  CA  LEU A 392     5779   6808   6541    704    643   -343       C  
ATOM   2965  C   LEU A 392     -28.330  -7.396  24.406  1.00 47.39           C  
ANISOU 2965  C   LEU A 392     5341   6411   6253    612    511   -315       C  
ATOM   2966  O   LEU A 392     -27.169  -7.361  23.989  1.00 49.38           O  
ANISOU 2966  O   LEU A 392     5682   6639   6442    573    399   -333       O  
ATOM   2967  CB  LEU A 392     -28.564  -5.154  25.508  1.00 47.97           C  
ANISOU 2967  CB  LEU A 392     5546   6468   6215    780    589   -428       C  
ATOM   2968  CG  LEU A 392     -29.403  -4.473  24.427  1.00 51.12           C  
ANISOU 2968  CG  LEU A 392     5825   6837   6762    817    536   -443       C  
ATOM   2969  CD1 LEU A 392     -30.884  -4.522  24.780  1.00 41.96           C  
ANISOU 2969  CD1 LEU A 392     4520   5715   5709    881    673   -421       C  
ATOM   2970  CD2 LEU A 392     -28.941  -3.041  24.220  1.00 48.75           C  
ANISOU 2970  CD2 LEU A 392     5628   6473   6423    878    464   -516       C  
ATOM   2971  N   GLY A 393     -29.297  -8.074  23.794  1.00 47.92           N  
ANISOU 2971  N   GLY A 393     5253   6486   6467    576    526   -275       N  
ATOM   2972  CA  GLY A 393     -29.031  -8.902  22.638  1.00 48.35           C  
ANISOU 2972  CA  GLY A 393     5253   6521   6598    488    411   -255       C  
ATOM   2973  C   GLY A 393     -28.626 -10.323  22.959  1.00 49.87           C  
ANISOU 2973  C   GLY A 393     5461   6710   6777    408    443   -196       C  
ATOM   2974  O   GLY A 393     -28.334 -11.092  22.032  1.00 45.28           O  
ANISOU 2974  O   GLY A 393     4850   6103   6253    336    352   -189       O  
ATOM   2975  N   GLY A 394     -28.593 -10.697  24.238  1.00 42.41           N  
ANISOU 2975  N   GLY A 394     4574   5788   5753    423    571   -154       N  
ATOM   2976  CA  GLY A 394     -28.241 -12.047  24.623  1.00 51.52           C  
ANISOU 2976  CA  GLY A 394     5751   6930   6895    357    611    -83       C  
ATOM   2977  C   GLY A 394     -29.384 -13.032  24.642  1.00 57.78           C  
ANISOU 2977  C   GLY A 394     6404   7716   7834    300    707    -19       C  
ATOM   2978  O   GLY A 394     -29.151 -14.231  24.815  1.00 59.55           O  
ANISOU 2978  O   GLY A 394     6641   7908   8076    234    733     45       O  
ATOM   2979  N   GLY A 395     -30.617 -12.557  24.480  1.00 61.97           N  
ANISOU 2979  N   GLY A 395     6794   8270   8480    324    761    -31       N  
ATOM   2980  CA  GLY A 395     -31.772 -13.424  24.407  1.00 58.07           C  
ANISOU 2980  CA  GLY A 395     6136   7771   8155    259    843     24       C  
ATOM   2981  C   GLY A 395     -31.930 -14.048  23.034  1.00 69.38           C  
ANISOU 2981  C   GLY A 395     7468   9160   9731    170    698      0       C  
ATOM   2982  O   GLY A 395     -31.087 -13.913  22.146  1.00 72.71           O  
ANISOU 2982  O   GLY A 395     7961   9557  10107    160    547    -51       O  
ATOM   2983  N   SER A 396     -33.058 -14.743  22.863  1.00 73.47           N  
ANISOU 2983  N   SER A 396     7816   9672  10428    102    750     35       N  
ATOM   2984  CA  SER A 396     -33.305 -15.481  21.630  1.00 75.82           C  
ANISOU 2984  CA  SER A 396     8018   9924  10867      4    614      7       C  
ATOM   2985  C   SER A 396     -33.578 -14.568  20.441  1.00 74.52           C  
ANISOU 2985  C   SER A 396     7786   9784  10743     43    454    -75       C  
ATOM   2986  O   SER A 396     -33.485 -15.023  19.295  1.00 72.52           O  
ANISOU 2986  O   SER A 396     7506   9499  10549    -21    306   -117       O  
ATOM   2987  CB  SER A 396     -34.474 -16.445  21.824  1.00 81.02           C  
ANISOU 2987  CB  SER A 396     8500  10564  11718    -90    709     65       C  
ATOM   2988  OG  SER A 396     -35.586 -15.780  22.395  1.00 88.17           O  
ANISOU 2988  OG  SER A 396     9267  11535  12698    -33    834     87       O  
ATOM   2989  N   GLU A 397     -33.907 -13.300  20.680  1.00 73.19           N  
ANISOU 2989  N   GLU A 397     7601   9668  10539    151    481    -98       N  
ATOM   2990  CA  GLU A 397     -34.175 -12.363  19.597  1.00 67.05           C  
ANISOU 2990  CA  GLU A 397     6771   8910   9795    202    334   -160       C  
ATOM   2991  C   GLU A 397     -32.915 -11.698  19.057  1.00 57.79           C  
ANISOU 2991  C   GLU A 397     5776   7717   8463    243    215   -206       C  
ATOM   2992  O   GLU A 397     -32.983 -11.045  18.009  1.00 62.53           O  
ANISOU 2992  O   GLU A 397     6359   8323   9077    273     79   -248       O  
ATOM   2993  CB  GLU A 397     -35.174 -11.299  20.060  1.00 69.56           C  
ANISOU 2993  CB  GLU A 397     6980   9279  10170    308    419   -160       C  
ATOM   2994  CG  GLU A 397     -36.559 -11.867  20.316  1.00 84.32           C  
ANISOU 2994  CG  GLU A 397     8625  11177  12234    266    515   -118       C  
ATOM   2995  CD  GLU A 397     -37.561 -10.810  20.721  1.00 98.45           C  
ANISOU 2995  CD  GLU A 397    10292  13023  14093    385    603   -120       C  
ATOM   2996  OE1 GLU A 397     -37.135  -9.681  21.045  1.00103.00           O  
ANISOU 2996  OE1 GLU A 397    10987  13602  14545    502    621   -151       O  
ATOM   2997  OE2 GLU A 397     -38.775 -11.106  20.713  1.00105.41           O  
ANISOU 2997  OE2 GLU A 397    10954  13938  15161    362    655    -93       O  
ATOM   2998  N   ASP A 398     -31.783 -11.845  19.746  1.00 55.11           N  
ANISOU 2998  N   ASP A 398     5602   7359   7979    245    264   -193       N  
ATOM   2999  CA  ASP A 398     -30.453 -11.475  19.246  1.00 59.85           C  
ANISOU 2999  CA  ASP A 398     6360   7937   8445    256    159   -228       C  
ATOM   3000  C   ASP A 398     -30.454 -10.002  18.851  1.00 63.28           C  
ANISOU 3000  C   ASP A 398     6820   8383   8840    347     97   -270       C  
ATOM   3001  O   ASP A 398     -30.663  -9.148  19.730  1.00 67.81           O  
ANISOU 3001  O   ASP A 398     7418   8972   9374    426    189   -272       O  
ATOM   3002  CB  ASP A 398     -30.062 -12.459  18.140  1.00 55.98           C  
ANISOU 3002  CB  ASP A 398     5868   7411   7989    168     40   -243       C  
ATOM   3003  CG  ASP A 398     -28.646 -12.237  17.632  1.00 67.10           C  
ANISOU 3003  CG  ASP A 398     7428   8801   9267    174    -47   -270       C  
ATOM   3004  OD1 ASP A 398     -27.695 -12.365  18.434  1.00 65.12           O  
ANISOU 3004  OD1 ASP A 398     7287   8542   8914    182      9   -250       O  
ATOM   3005  OD2 ASP A 398     -28.484 -11.933  16.429  1.00 71.22           O  
ANISOU 3005  OD2 ASP A 398     7955   9320   9787    173   -171   -309       O  
ATOM   3006  N   ALA A 399     -30.238  -9.654  17.581  1.00 60.41           N  
ANISOU 3006  N   ALA A 399     6463   8009   8481    344    -48   -301       N  
ATOM   3007  CA  ALA A 399     -30.015  -8.263  17.208  1.00 54.37           C  
ANISOU 3007  CA  ALA A 399     5757   7237   7663    427   -105   -328       C  
ATOM   3008  C   ALA A 399     -31.277  -7.419  17.289  1.00 45.37           C  
ANISOU 3008  C   ALA A 399     4499   6118   6621    511    -79   -329       C  
ATOM   3009  O   ALA A 399     -31.176  -6.188  17.337  1.00 58.41           O  
ANISOU 3009  O   ALA A 399     6208   7751   8234    597    -87   -346       O  
ATOM   3010  CB  ALA A 399     -29.432  -8.186  15.796  1.00 50.96           C  
ANISOU 3010  CB  ALA A 399     5372   6790   7199    401   -258   -346       C  
ATOM   3011  N   LYS A 400     -32.458  -8.041  17.306  1.00 45.67           N  
ANISOU 3011  N   LYS A 400     4367   6187   6797    489    -48   -311       N  
ATOM   3012  CA  LYS A 400     -33.691  -7.260  17.311  1.00 57.37           C  
ANISOU 3012  CA  LYS A 400     5710   7695   8392    577    -28   -310       C  
ATOM   3013  C   LYS A 400     -33.886  -6.516  18.625  1.00 60.02           C  
ANISOU 3013  C   LYS A 400     6078   8035   8694    669    135   -310       C  
ATOM   3014  O   LYS A 400     -34.478  -5.431  18.634  1.00 61.04           O  
ANISOU 3014  O   LYS A 400     6167   8161   8862    778    144   -324       O  
ATOM   3015  CB  LYS A 400     -34.891  -8.158  17.018  1.00 69.07           C  
ANISOU 3015  CB  LYS A 400     6982   9214  10046    520    -36   -292       C  
ATOM   3016  CG  LYS A 400     -34.828  -8.804  15.645  1.00 81.78           C  
ANISOU 3016  CG  LYS A 400     8563  10821  11691    439   -216   -310       C  
ATOM   3017  CD  LYS A 400     -36.198  -9.229  15.148  1.00 92.83           C  
ANISOU 3017  CD  LYS A 400     9733  12259  13278    412   -272   -307       C  
ATOM   3018  CE  LYS A 400     -36.134  -9.672  13.693  1.00 99.74           C  
ANISOU 3018  CE  LYS A 400    10601  13134  14162    350   -478   -342       C  
ATOM   3019  NZ  LYS A 400     -37.484  -9.957  13.134  1.00102.19           N  
ANISOU 3019  NZ  LYS A 400    10682  13488  14657    328   -567   -348       N  
ATOM   3020  N   GLU A 401     -33.404  -7.077  19.738  1.00 58.10           N  
ANISOU 3020  N   GLU A 401     5911   7794   8371    634    264   -295       N  
ATOM   3021  CA  GLU A 401     -33.437  -6.345  21.001  1.00 60.26           C  
ANISOU 3021  CA  GLU A 401     6253   8071   8571    724    413   -307       C  
ATOM   3022  C   GLU A 401     -32.695  -5.021  20.878  1.00 57.18           C  
ANISOU 3022  C   GLU A 401     6014   7635   8078    803    350   -357       C  
ATOM   3023  O   GLU A 401     -33.118  -4.005  21.439  1.00 55.55           O  
ANISOU 3023  O   GLU A 401     5821   7418   7868    912    424   -387       O  
ATOM   3024  CB  GLU A 401     -32.821  -7.183  22.123  1.00 63.82           C  
ANISOU 3024  CB  GLU A 401     6800   8533   8916    671    530   -279       C  
ATOM   3025  CG  GLU A 401     -33.478  -8.527  22.371  1.00 77.62           C  
ANISOU 3025  CG  GLU A 401     8421  10308  10762    585    613   -217       C  
ATOM   3026  CD  GLU A 401     -32.887  -9.233  23.579  1.00 89.53           C  
ANISOU 3026  CD  GLU A 401    10043  11824  12150    554    740   -176       C  
ATOM   3027  OE1 GLU A 401     -32.195  -8.566  24.379  1.00 93.18           O  
ANISOU 3027  OE1 GLU A 401    10661  12286  12456    618    781   -204       O  
ATOM   3028  OE2 GLU A 401     -33.111 -10.454  23.727  1.00 93.53           O  
ANISOU 3028  OE2 GLU A 401    10489  12331  12717    466    791   -116       O  
ATOM   3029  N   ILE A 402     -31.589  -5.017  20.136  1.00 50.66           N  
ANISOU 3029  N   ILE A 402     5299   6774   7175    748    220   -369       N  
ATOM   3030  CA  ILE A 402     -30.767  -3.820  20.010  1.00 59.90           C  
ANISOU 3030  CA  ILE A 402     6616   7889   8254    799    161   -409       C  
ATOM   3031  C   ILE A 402     -31.347  -2.869  18.973  1.00 58.62           C  
ANISOU 3031  C   ILE A 402     6399   7698   8177    869     64   -414       C  
ATOM   3032  O   ILE A 402     -31.277  -1.646  19.130  1.00 54.06           O  
ANISOU 3032  O   ILE A 402     5895   7067   7577    956     68   -444       O  
ATOM   3033  CB  ILE A 402     -29.322  -4.223  19.671  1.00 57.57           C  
ANISOU 3033  CB  ILE A 402     6449   7574   7851    710     77   -410       C  
ATOM   3034  CG1 ILE A 402     -28.828  -5.251  20.688  1.00 55.59           C  
ANISOU 3034  CG1 ILE A 402     6241   7354   7526    652    164   -394       C  
ATOM   3035  CG2 ILE A 402     -28.413  -3.003  19.636  1.00 59.36           C  
ANISOU 3035  CG2 ILE A 402     6822   7739   7994    746     27   -449       C  
ATOM   3036  CD1 ILE A 402     -27.389  -5.595  20.538  1.00 55.97           C  
ANISOU 3036  CD1 ILE A 402     6409   7386   7472    583     94   -396       C  
ATOM   3037  N   MET A 403     -31.932  -3.412  17.905  1.00 56.60           N  
ANISOU 3037  N   MET A 403     6017   7470   8017    835    -30   -384       N  
ATOM   3038  CA  MET A 403     -32.521  -2.559  16.881  1.00 50.77           C  
ANISOU 3038  CA  MET A 403     5225   6714   7353    908   -137   -377       C  
ATOM   3039  C   MET A 403     -33.726  -1.792  17.410  1.00 48.00           C  
ANISOU 3039  C   MET A 403     4766   6368   7106   1034    -54   -383       C  
ATOM   3040  O   MET A 403     -33.981  -0.665  16.971  1.00 51.04           O  
ANISOU 3040  O   MET A 403     5168   6706   7518   1134   -107   -385       O  
ATOM   3041  CB  MET A 403     -32.905  -3.398  15.660  1.00 46.35           C  
ANISOU 3041  CB  MET A 403     4556   6194   6860    841   -266   -352       C  
ATOM   3042  CG  MET A 403     -31.704  -3.944  14.898  1.00 55.32           C  
ANISOU 3042  CG  MET A 403     5812   7317   7891    743   -361   -351       C  
ATOM   3043  SD  MET A 403     -32.142  -4.794  13.372  1.00 67.95           S  
ANISOU 3043  SD  MET A 403     7315   8957   9544    679   -526   -341       S  
ATOM   3044  CE  MET A 403     -32.590  -6.413  13.986  1.00 62.68           C  
ANISOU 3044  CE  MET A 403     6529   8330   8958    573   -449   -346       C  
ATOM   3045  N   GLN A 404     -34.465  -2.372  18.351  1.00 46.23           N  
ANISOU 3045  N   GLN A 404     4432   6193   6940   1036     85   -380       N  
ATOM   3046  CA  GLN A 404     -35.632  -1.730  18.937  1.00 55.45           C  
ANISOU 3046  CA  GLN A 404     5481   7375   8212   1160    192   -385       C  
ATOM   3047  C   GLN A 404     -35.295  -0.897  20.167  1.00 57.16           C  
ANISOU 3047  C   GLN A 404     5836   7550   8331   1245    334   -432       C  
ATOM   3048  O   GLN A 404     -36.194  -0.274  20.739  1.00 60.35           O  
ANISOU 3048  O   GLN A 404     6166   7959   8807   1365    444   -447       O  
ATOM   3049  CB  GLN A 404     -36.682  -2.782  19.300  1.00 70.73           C  
ANISOU 3049  CB  GLN A 404     7210   9391  10274   1118    284   -353       C  
ATOM   3050  CG  GLN A 404     -37.169  -3.598  18.115  1.00 82.04           C  
ANISOU 3050  CG  GLN A 404     8489  10862  11822   1034    137   -322       C  
ATOM   3051  CD  GLN A 404     -37.920  -4.842  18.540  1.00 91.72           C  
ANISOU 3051  CD  GLN A 404     9541  12148  13160    946    229   -291       C  
ATOM   3052  OE1 GLN A 404     -38.199  -5.038  19.723  1.00 94.71           O  
ANISOU 3052  OE1 GLN A 404     9898  12548  13538    961    418   -280       O  
ATOM   3053  NE2 GLN A 404     -38.246  -5.695  17.576  1.00 94.79           N  
ANISOU 3053  NE2 GLN A 404     9812  12562  13643    848     97   -277       N  
ATOM   3054  N   HIS A 405     -34.033  -0.875  20.587  1.00 53.96           N  
ANISOU 3054  N   HIS A 405     5627   7107   7769   1189    333   -459       N  
ATOM   3055  CA  HIS A 405     -33.630  -0.035  21.704  1.00 53.15           C  
ANISOU 3055  CA  HIS A 405     5674   6959   7560   1263    440   -518       C  
ATOM   3056  C   HIS A 405     -33.807   1.435  21.346  1.00 54.58           C  
ANISOU 3056  C   HIS A 405     5908   7053   7777   1386    393   -555       C  
ATOM   3057  O   HIS A 405     -33.601   1.849  20.201  1.00 58.42           O  
ANISOU 3057  O   HIS A 405     6401   7495   8302   1380    247   -531       O  
ATOM   3058  CB  HIS A 405     -32.176  -0.317  22.084  1.00 48.58           C  
ANISOU 3058  CB  HIS A 405     5282   6359   6816   1167    409   -540       C  
ATOM   3059  CG  HIS A 405     -31.750   0.315  23.372  1.00 57.93           C  
ANISOU 3059  CG  HIS A 405     6620   7515   7876   1223    516   -608       C  
ATOM   3060  ND1 HIS A 405     -31.352   1.631  23.462  1.00 57.13           N  
ANISOU 3060  ND1 HIS A 405     6653   7321   7735   1294    485   -674       N  
ATOM   3061  CD2 HIS A 405     -31.656  -0.192  24.624  1.00 53.84           C  
ANISOU 3061  CD2 HIS A 405     6154   7046   7256   1217    648   -621       C  
ATOM   3062  CE1 HIS A 405     -31.032   1.908  24.713  1.00 63.03           C  
ANISOU 3062  CE1 HIS A 405     7527   8062   8360   1328    586   -739       C  
ATOM   3063  NE2 HIS A 405     -31.207   0.819  25.439  1.00 61.33           N  
ANISOU 3063  NE2 HIS A 405     7268   7939   8096   1286    686   -705       N  
ATOM   3064  N   ARG A 406     -34.189   2.231  22.346  1.00 54.79           N  
ANISOU 3064  N   ARG A 406     5982   7050   7785   1502    525   -611       N  
ATOM   3065  CA  ARG A 406     -34.540   3.624  22.095  1.00 56.64           C  
ANISOU 3065  CA  ARG A 406     6253   7189   8078   1640    502   -646       C  
ATOM   3066  C   ARG A 406     -33.366   4.448  21.580  1.00 52.65           C  
ANISOU 3066  C   ARG A 406     5938   6571   7494   1605    373   -671       C  
ATOM   3067  O   ARG A 406     -33.585   5.522  21.011  1.00 51.81           O  
ANISOU 3067  O   ARG A 406     5858   6372   7454   1697    313   -674       O  
ATOM   3068  CB  ARG A 406     -35.118   4.259  23.363  1.00 65.28           C  
ANISOU 3068  CB  ARG A 406     7381   8269   9154   1773    685   -717       C  
ATOM   3069  CG  ARG A 406     -34.359   3.938  24.645  1.00 74.31           C  
ANISOU 3069  CG  ARG A 406     8682   9434  10121   1724    792   -775       C  
ATOM   3070  CD  ARG A 406     -35.165   4.381  25.859  1.00 85.81           C  
ANISOU 3070  CD  ARG A 406    10140  10903  11561   1864    994   -836       C  
ATOM   3071  NE  ARG A 406     -34.548   4.000  27.127  1.00 91.54           N  
ANISOU 3071  NE  ARG A 406    11014  11667  12100   1825   1101   -885       N  
ATOM   3072  CZ  ARG A 406     -33.928   4.848  27.942  1.00 92.30           C  
ANISOU 3072  CZ  ARG A 406    11321  11690  12058   1875   1130   -991       C  
ATOM   3073  NH1 ARG A 406     -33.844   6.132  27.626  1.00 92.34           N  
ANISOU 3073  NH1 ARG A 406    11415  11566  12105   1961   1069  -1059       N  
ATOM   3074  NH2 ARG A 406     -33.399   4.411  29.078  1.00 92.95           N  
ANISOU 3074  NH2 ARG A 406    11532  11823  11960   1840   1214  -1029       N  
ATOM   3075  N   PHE A 407     -32.128   3.979  21.763  1.00 47.88           N  
ANISOU 3075  N   PHE A 407     5462   5969   6760   1477    332   -683       N  
ATOM   3076  CA  PHE A 407     -30.995   4.708  21.206  1.00 50.14           C  
ANISOU 3076  CA  PHE A 407     5905   6154   6991   1428    212   -697       C  
ATOM   3077  C   PHE A 407     -31.029   4.708  19.685  1.00 55.41           C  
ANISOU 3077  C   PHE A 407     6507   6809   7736   1399     67   -618       C  
ATOM   3078  O   PHE A 407     -30.576   5.673  19.059  1.00 46.87           O  
ANISOU 3078  O   PHE A 407     5524   5624   6662   1417    -15   -612       O  
ATOM   3079  CB  PHE A 407     -29.678   4.117  21.709  1.00 50.64           C  
ANISOU 3079  CB  PHE A 407     6089   6239   6913   1296    196   -721       C  
ATOM   3080  CG  PHE A 407     -28.453   4.830  21.192  1.00 53.24           C  
ANISOU 3080  CG  PHE A 407     6562   6469   7196   1231     83   -734       C  
ATOM   3081  CD1 PHE A 407     -27.990   5.980  21.814  1.00 50.32           C  
ANISOU 3081  CD1 PHE A 407     6346   5988   6785   1270     98   -816       C  
ATOM   3082  CD2 PHE A 407     -27.769   4.354  20.085  1.00 49.08           C  
ANISOU 3082  CD2 PHE A 407     6018   5959   6671   1128    -30   -667       C  
ATOM   3083  CE1 PHE A 407     -26.869   6.642  21.342  1.00 52.99           C  
ANISOU 3083  CE1 PHE A 407     6805   6229   7100   1197     -1   -823       C  
ATOM   3084  CE2 PHE A 407     -26.648   5.009  19.608  1.00 41.45           C  
ANISOU 3084  CE2 PHE A 407     5172   4906   5671   1064   -116   -670       C  
ATOM   3085  CZ  PHE A 407     -26.196   6.156  20.238  1.00 45.45           C  
ANISOU 3085  CZ  PHE A 407     5818   5298   6152   1093   -102   -744       C  
ATOM   3086  N   PHE A 408     -31.567   3.650  19.077  1.00 47.51           N  
ANISOU 3086  N   PHE A 408     5351   5910   6791   1354     34   -557       N  
ATOM   3087  CA  PHE A 408     -31.696   3.550  17.630  1.00 51.65           C  
ANISOU 3087  CA  PHE A 408     5811   6441   7374   1332   -108   -487       C  
ATOM   3088  C   PHE A 408     -33.098   3.900  17.146  1.00 55.80           C  
ANISOU 3088  C   PHE A 408     6178   6982   8042   1455   -126   -454       C  
ATOM   3089  O   PHE A 408     -33.504   3.458  16.065  1.00 62.39           O  
ANISOU 3089  O   PHE A 408     6907   7865   8932   1435   -237   -398       O  
ATOM   3090  CB  PHE A 408     -31.304   2.148  17.160  1.00 38.87           C  
ANISOU 3090  CB  PHE A 408     4135   4914   5719   1196   -159   -452       C  
ATOM   3091  CG  PHE A 408     -29.856   1.823  17.380  1.00 42.59           C  
ANISOU 3091  CG  PHE A 408     4749   5369   6062   1081   -170   -469       C  
ATOM   3092  CD1 PHE A 408     -28.869   2.456  16.639  1.00 42.58           C  
ANISOU 3092  CD1 PHE A 408     4871   5297   6009   1045   -261   -455       C  
ATOM   3093  CD2 PHE A 408     -29.479   0.885  18.326  1.00 45.12           C  
ANISOU 3093  CD2 PHE A 408     5077   5747   6319   1012    -88   -492       C  
ATOM   3094  CE1 PHE A 408     -27.532   2.157  16.840  1.00 44.17           C  
ANISOU 3094  CE1 PHE A 408     5182   5491   6111    941   -270   -470       C  
ATOM   3095  CE2 PHE A 408     -28.145   0.582  18.530  1.00 45.61           C  
ANISOU 3095  CE2 PHE A 408     5257   5800   6273    917   -109   -505       C  
ATOM   3096  CZ  PHE A 408     -27.171   1.220  17.785  1.00 46.31           C  
ANISOU 3096  CZ  PHE A 408     5449   5823   6322    880   -201   -497       C  
ATOM   3097  N   ALA A 409     -33.846   4.675  17.928  1.00 52.50           N  
ANISOU 3097  N   ALA A 409     5737   6526   7683   1588    -21   -493       N  
ATOM   3098  CA  ALA A 409     -35.138   5.162  17.471  1.00 57.31           C  
ANISOU 3098  CA  ALA A 409     6195   7140   8441   1726    -41   -461       C  
ATOM   3099  C   ALA A 409     -34.952   6.060  16.255  1.00 57.88           C  
ANISOU 3099  C   ALA A 409     6333   7126   8534   1774   -194   -410       C  
ATOM   3100  O   ALA A 409     -33.993   6.833  16.174  1.00 60.18           O  
ANISOU 3100  O   ALA A 409     6812   7306   8746   1757   -222   -422       O  
ATOM   3101  CB  ALA A 409     -35.844   5.922  18.594  1.00 55.43           C  
ANISOU 3101  CB  ALA A 409     5945   6863   8252   1873    117   -521       C  
ATOM   3102  N   GLY A 410     -35.871   5.946  15.296  1.00 64.10           N  
ANISOU 3102  N   GLY A 410     6964   7963   9427   1829   -298   -347       N  
ATOM   3103  CA  GLY A 410     -35.779   6.685  14.056  1.00 68.85           C  
ANISOU 3103  CA  GLY A 410     7622   8501  10039   1878   -453   -279       C  
ATOM   3104  C   GLY A 410     -34.905   6.052  12.999  1.00 78.39           C  
ANISOU 3104  C   GLY A 410     8899   9741  11142   1737   -585   -233       C  
ATOM   3105  O   GLY A 410     -34.886   6.539  11.862  1.00 89.94           O  
ANISOU 3105  O   GLY A 410    10402  11171  12600   1773   -719   -164       O  
ATOM   3106  N   ILE A 411     -34.184   4.987  13.328  1.00 69.73           N  
ANISOU 3106  N   ILE A 411     7825   8709   9961   1587   -547   -264       N  
ATOM   3107  CA  ILE A 411     -33.339   4.303  12.358  1.00 64.34           C  
ANISOU 3107  CA  ILE A 411     7204   8062   9179   1459   -655   -229       C  
ATOM   3108  C   ILE A 411     -34.193   3.312  11.579  1.00 61.52           C  
ANISOU 3108  C   ILE A 411     6671   7823   8883   1434   -755   -202       C  
ATOM   3109  O   ILE A 411     -34.784   2.394  12.158  1.00 55.43           O  
ANISOU 3109  O   ILE A 411     5755   7131   8174   1397   -693   -234       O  
ATOM   3110  CB  ILE A 411     -32.164   3.597  13.048  1.00 61.55           C  
ANISOU 3110  CB  ILE A 411     6950   7719   8716   1320   -576   -276       C  
ATOM   3111  CG1 ILE A 411     -31.164   4.622  13.582  1.00 61.56           C  
ANISOU 3111  CG1 ILE A 411     7139   7601   8650   1325   -521   -302       C  
ATOM   3112  CG2 ILE A 411     -31.482   2.643  12.088  1.00 59.16           C  
ANISOU 3112  CG2 ILE A 411     6669   7475   8333   1196   -671   -248       C  
ATOM   3113  CD1 ILE A 411     -30.579   5.505  12.507  1.00 58.97           C  
ANISOU 3113  CD1 ILE A 411     6936   7186   8286   1336   -621   -241       C  
ATOM   3114  N   VAL A 412     -34.266   3.500  10.266  1.00 62.11           N  
ANISOU 3114  N   VAL A 412     6761   7904   8936   1452   -910   -143       N  
ATOM   3115  CA  VAL A 412     -34.934   2.552   9.381  1.00 59.75           C  
ANISOU 3115  CA  VAL A 412     6320   7712   8669   1413  -1037   -128       C  
ATOM   3116  C   VAL A 412     -33.902   1.504   8.985  1.00 64.03           C  
ANISOU 3116  C   VAL A 412     6949   8292   9086   1256  -1061   -146       C  
ATOM   3117  O   VAL A 412     -32.948   1.801   8.262  1.00 67.88           O  
ANISOU 3117  O   VAL A 412     7597   8741   9453   1224  -1112   -114       O  
ATOM   3118  CB  VAL A 412     -35.533   3.245   8.152  1.00 66.50           C  
ANISOU 3118  CB  VAL A 412     7158   8565   9543   1519  -1205    -57       C  
ATOM   3119  CG1 VAL A 412     -36.353   2.254   7.331  1.00 68.03           C  
ANISOU 3119  CG1 VAL A 412     7187   8878   9782   1481  -1348    -58       C  
ATOM   3120  CG2 VAL A 412     -36.382   4.435   8.577  1.00 58.41           C  
ANISOU 3120  CG2 VAL A 412     6077   7476   8639   1692  -1170    -34       C  
ATOM   3121  N   TRP A 413     -34.093   0.272   9.460  1.00 53.41           N  
ANISOU 3121  N   TRP A 413     5499   7019   7777   1161  -1014   -192       N  
ATOM   3122  CA  TRP A 413     -33.052  -0.742   9.340  1.00 57.31           C  
ANISOU 3122  CA  TRP A 413     6080   7531   8163   1021  -1002   -218       C  
ATOM   3123  C   TRP A 413     -32.910  -1.290   7.927  1.00 59.14           C  
ANISOU 3123  C   TRP A 413     6336   7810   8325    971  -1161   -204       C  
ATOM   3124  O   TRP A 413     -31.842  -1.811   7.589  1.00 59.14           O  
ANISOU 3124  O   TRP A 413     6456   7806   8208    882  -1160   -215       O  
ATOM   3125  CB  TRP A 413     -33.316  -1.866  10.341  1.00 57.35           C  
ANISOU 3125  CB  TRP A 413     5977   7582   8233    942   -895   -264       C  
ATOM   3126  CG  TRP A 413     -33.073  -1.395  11.731  1.00 56.27           C  
ANISOU 3126  CG  TRP A 413     5880   7400   8101    974   -728   -283       C  
ATOM   3127  CD1 TRP A 413     -34.005  -0.973  12.631  1.00 48.67           C  
ANISOU 3127  CD1 TRP A 413     4810   6439   7245   1060   -631   -291       C  
ATOM   3128  CD2 TRP A 413     -31.802  -1.243  12.367  1.00 55.09           C  
ANISOU 3128  CD2 TRP A 413     5895   7199   7838    927   -644   -300       C  
ATOM   3129  NE1 TRP A 413     -33.393  -0.587  13.798  1.00 57.10           N  
ANISOU 3129  NE1 TRP A 413     5981   7459   8255   1070   -491   -318       N  
ATOM   3130  CE2 TRP A 413     -32.039  -0.741  13.660  1.00 50.76           C  
ANISOU 3130  CE2 TRP A 413     5342   6623   7320    986   -506   -324       C  
ATOM   3131  CE3 TRP A 413     -30.485  -1.492  11.971  1.00 58.80           C  
ANISOU 3131  CE3 TRP A 413     6508   7648   8184    844   -671   -299       C  
ATOM   3132  CZ2 TRP A 413     -31.009  -0.484  14.561  1.00 53.59           C  
ANISOU 3132  CZ2 TRP A 413     5842   6936   7585    959   -415   -353       C  
ATOM   3133  CZ3 TRP A 413     -29.464  -1.238  12.866  1.00 58.25           C  
ANISOU 3133  CZ3 TRP A 413     6558   7534   8040    816   -577   -320       C  
ATOM   3134  CH2 TRP A 413     -29.731  -0.740  14.147  1.00 57.70           C  
ANISOU 3134  CH2 TRP A 413     6487   7438   7998    870   -460   -349       C  
ATOM   3135  N   GLN A 414     -33.940  -1.177   7.088  1.00 51.85           N  
ANISOU 3135  N   GLN A 414     5305   6933   7463   1033  -1301   -183       N  
ATOM   3136  CA  GLN A 414     -33.758  -1.542   5.687  1.00 54.88           C  
ANISOU 3136  CA  GLN A 414     5745   7357   7748   1001  -1463   -171       C  
ATOM   3137  C   GLN A 414     -32.882  -0.521   4.969  1.00 63.12           C  
ANISOU 3137  C   GLN A 414     6986   8343   8653   1051  -1493   -107       C  
ATOM   3138  O   GLN A 414     -32.088  -0.882   4.091  1.00 60.24           O  
ANISOU 3138  O   GLN A 414     6744   7994   8151    992  -1547   -102       O  
ATOM   3139  CB  GLN A 414     -35.109  -1.677   4.987  1.00 53.34           C  
ANISOU 3139  CB  GLN A 414     5381   7235   7652   1055  -1623   -166       C  
ATOM   3140  CG  GLN A 414     -34.984  -2.088   3.532  1.00 68.94           C  
ANISOU 3140  CG  GLN A 414     7422   9262   9508   1026  -1806   -165       C  
ATOM   3141  CD  GLN A 414     -36.306  -2.049   2.801  1.00 82.28           C  
ANISOU 3141  CD  GLN A 414     8951  11023  11287   1094  -1992   -156       C  
ATOM   3142  OE1 GLN A 414     -37.366  -2.221   3.404  1.00 83.12           O  
ANISOU 3142  OE1 GLN A 414     8849  11161  11574   1114  -1982   -175       O  
ATOM   3143  NE2 GLN A 414     -36.254  -1.817   1.493  1.00 89.75           N  
ANISOU 3143  NE2 GLN A 414     9992  12002  12107   1132  -2165   -123       N  
ATOM   3144  N   HIS A 415     -33.010   0.759   5.335  1.00 65.13           N  
ANISOU 3144  N   HIS A 415     7275   8524   8946   1159  -1450    -58       N  
ATOM   3145  CA  HIS A 415     -32.169   1.804   4.758  1.00 57.66           C  
ANISOU 3145  CA  HIS A 415     6518   7500   7889   1200  -1459     12       C  
ATOM   3146  C   HIS A 415     -30.716   1.682   5.192  1.00 65.06           C  
ANISOU 3146  C   HIS A 415     7602   8388   8729   1098  -1336     -6       C  
ATOM   3147  O   HIS A 415     -29.830   2.176   4.487  1.00 65.52           O  
ANISOU 3147  O   HIS A 415     7814   8405   8674   1086  -1350     49       O  
ATOM   3148  CB  HIS A 415     -32.703   3.188   5.138  1.00 54.70           C  
ANISOU 3148  CB  HIS A 415     6143   7039   7602   1340  -1436     62       C  
ATOM   3149  CG  HIS A 415     -34.097   3.451   4.660  1.00 69.49           C  
ANISOU 3149  CG  HIS A 415     7868   8956   9577   1462  -1564     93       C  
ATOM   3150  ND1 HIS A 415     -34.775   2.581   3.833  1.00 72.16           N  
ANISOU 3150  ND1 HIS A 415     8096   9407   9914   1438  -1712     81       N  
ATOM   3151  CD2 HIS A 415     -34.941   4.484   4.891  1.00 72.34           C  
ANISOU 3151  CD2 HIS A 415     8169   9265  10050   1612  -1573    133       C  
ATOM   3152  CE1 HIS A 415     -35.977   3.066   3.577  1.00 73.11           C  
ANISOU 3152  CE1 HIS A 415     8082   9551  10145   1565  -1814    115       C  
ATOM   3153  NE2 HIS A 415     -36.103   4.220   4.207  1.00 74.05           N  
ANISOU 3153  NE2 HIS A 415     8227   9571  10336   1678  -1728    151       N  
ATOM   3154  N   VAL A 416     -30.456   1.046   6.336  1.00 59.81           N  
ANISOU 3154  N   VAL A 416     6888   7728   8108   1028  -1216    -73       N  
ATOM   3155  CA  VAL A 416     -29.081   0.825   6.770  1.00 58.45           C  
ANISOU 3155  CA  VAL A 416     6835   7523   7852    931  -1115    -93       C  
ATOM   3156  C   VAL A 416     -28.405  -0.208   5.878  1.00 51.41           C  
ANISOU 3156  C   VAL A 416     5990   6693   6851    837  -1165   -103       C  
ATOM   3157  O   VAL A 416     -27.274  -0.011   5.418  1.00 47.40           O  
ANISOU 3157  O   VAL A 416     5615   6159   6238    794  -1144    -75       O  
ATOM   3158  CB  VAL A 416     -29.046   0.402   8.250  1.00 59.37           C  
ANISOU 3158  CB  VAL A 416     6889   7634   8034    894   -985   -158       C  
ATOM   3159  CG1 VAL A 416     -27.623   0.073   8.668  1.00 57.71           C  
ANISOU 3159  CG1 VAL A 416     6788   7402   7736    795   -904   -179       C  
ATOM   3160  CG2 VAL A 416     -29.623   1.496   9.133  1.00 58.26           C  
ANISOU 3160  CG2 VAL A 416     6728   7425   7981    995   -922   -158       C  
ATOM   3161  N   TYR A 417     -29.088  -1.325   5.621  1.00 55.22           N  
ANISOU 3161  N   TYR A 417     6362   7255   7365    804  -1228   -147       N  
ATOM   3162  CA  TYR A 417     -28.512  -2.367   4.777  1.00 55.47           C  
ANISOU 3162  CA  TYR A 417     6441   7338   7295    722  -1276   -173       C  
ATOM   3163  C   TYR A 417     -28.264  -1.862   3.361  1.00 55.74           C  
ANISOU 3163  C   TYR A 417     6591   7384   7206    759  -1381   -116       C  
ATOM   3164  O   TYR A 417     -27.242  -2.188   2.748  1.00 63.75           O  
ANISOU 3164  O   TYR A 417     7720   8406   8096    706  -1363   -112       O  
ATOM   3165  CB  TYR A 417     -29.429  -3.589   4.755  1.00 58.58           C  
ANISOU 3165  CB  TYR A 417     6692   7799   7765    680  -1337   -236       C  
ATOM   3166  CG  TYR A 417     -29.021  -4.628   3.739  1.00 74.99           C  
ANISOU 3166  CG  TYR A 417     8826   9925   9744    610  -1412   -275       C  
ATOM   3167  CD1 TYR A 417     -28.020  -5.546   4.024  1.00 83.05           C  
ANISOU 3167  CD1 TYR A 417     9903  10937  10716    522  -1327   -317       C  
ATOM   3168  CD2 TYR A 417     -29.636  -4.692   2.495  1.00 79.18           C  
ANISOU 3168  CD2 TYR A 417     9356  10506  10222    641  -1573   -273       C  
ATOM   3169  CE1 TYR A 417     -27.641  -6.496   3.098  1.00 87.83           C  
ANISOU 3169  CE1 TYR A 417    10565  11576  11230    470  -1386   -362       C  
ATOM   3170  CE2 TYR A 417     -29.262  -5.638   1.563  1.00 86.56           C  
ANISOU 3170  CE2 TYR A 417    10356  11481  11051    583  -1641   -323       C  
ATOM   3171  CZ  TYR A 417     -28.264  -6.537   1.871  1.00 94.53           C  
ANISOU 3171  CZ  TYR A 417    11424  12473  12020    499  -1540   -370       C  
ATOM   3172  OH  TYR A 417     -27.889  -7.484   0.948  1.00104.63           O  
ANISOU 3172  OH  TYR A 417    12775  13783  13195    450  -1599   -429       O  
ATOM   3173  N   GLU A 418     -29.185  -1.064   2.828  1.00 57.75           N  
ANISOU 3173  N   GLU A 418     6816   7640   7487    858  -1484    -65       N  
ATOM   3174  CA  GLU A 418     -29.105  -0.573   1.460  1.00 57.94           C  
ANISOU 3174  CA  GLU A 418     6950   7680   7384    908  -1597      1       C  
ATOM   3175  C   GLU A 418     -28.282   0.704   1.332  1.00 60.89           C  
ANISOU 3175  C   GLU A 418     7474   7967   7696    949  -1532     94       C  
ATOM   3176  O   GLU A 418     -28.303   1.333   0.269  1.00 66.89           O  
ANISOU 3176  O   GLU A 418     8332   8725   8359   1009  -1615    175       O  
ATOM   3177  CB  GLU A 418     -30.514  -0.353   0.909  1.00 55.67           C  
ANISOU 3177  CB  GLU A 418     6556   7441   7157   1002  -1759     19       C  
ATOM   3178  CG  GLU A 418     -31.352  -1.618   0.924  1.00 65.45           C  
ANISOU 3178  CG  GLU A 418     7637   8763   8468    948  -1839    -72       C  
ATOM   3179  CD  GLU A 418     -32.817  -1.365   0.638  1.00 79.46           C  
ANISOU 3179  CD  GLU A 418     9257  10583  10349   1037  -1989    -60       C  
ATOM   3180  OE1 GLU A 418     -33.283  -0.225   0.849  1.00 81.17           O  
ANISOU 3180  OE1 GLU A 418     9454  10756  10632   1150  -1990     10       O  
ATOM   3181  OE2 GLU A 418     -33.504  -2.312   0.202  1.00 81.86           O  
ANISOU 3181  OE2 GLU A 418     9456  10964  10681    995  -2109   -123       O  
ATOM   3182  N   LYS A 419     -27.569   1.098   2.390  1.00 64.49           N  
ANISOU 3182  N   LYS A 419     7954   8346   8203    914  -1390     86       N  
ATOM   3183  CA  LYS A 419     -26.661   2.249   2.376  1.00 62.19           C  
ANISOU 3183  CA  LYS A 419     7801   7957   7872    924  -1316    162       C  
ATOM   3184  C   LYS A 419     -27.360   3.541   1.951  1.00 71.20           C  
ANISOU 3184  C   LYS A 419     8978   9032   9042   1047  -1386    254       C  
ATOM   3185  O   LYS A 419     -26.729   4.448   1.403  1.00 74.66           O  
ANISOU 3185  O   LYS A 419     9555   9399   9415   1064  -1368    344       O  
ATOM   3186  CB  LYS A 419     -25.442   1.985   1.485  1.00 58.60           C  
ANISOU 3186  CB  LYS A 419     7480   7522   7263    852  -1288    197       C  
ATOM   3187  CG  LYS A 419     -24.614   0.783   1.913  1.00 61.59           C  
ANISOU 3187  CG  LYS A 419     7833   7950   7618    742  -1209    114       C  
ATOM   3188  CD  LYS A 419     -23.211   0.823   1.322  1.00 67.20           C  
ANISOU 3188  CD  LYS A 419     8671   8653   8210    678  -1134    156       C  
ATOM   3189  CE  LYS A 419     -23.243   0.772  -0.193  1.00 70.37           C  
ANISOU 3189  CE  LYS A 419     9168   9108   8460    710  -1214    214       C  
ATOM   3190  NZ  LYS A 419     -21.872   0.825  -0.771  1.00 71.70           N  
ANISOU 3190  NZ  LYS A 419     9455   9274   8514    652  -1117    261       N  
ATOM   3191  N   LYS A 420     -28.665   3.644   2.205  1.00 76.15           N  
ANISOU 3191  N   LYS A 420     9477   9678   9778   1138  -1460    237       N  
ATOM   3192  CA  LYS A 420     -29.393   4.861   1.868  1.00 80.78           C  
ANISOU 3192  CA  LYS A 420    10085  10198  10411   1274  -1528    324       C  
ATOM   3193  C   LYS A 420     -29.124   5.991   2.851  1.00 80.83           C  
ANISOU 3193  C   LYS A 420    10137  10062  10512   1310  -1414    337       C  
ATOM   3194  O   LYS A 420     -29.436   7.148   2.547  1.00 81.15           O  
ANISOU 3194  O   LYS A 420    10241  10011  10581   1417  -1447    421       O  
ATOM   3195  CB  LYS A 420     -30.893   4.573   1.795  1.00 85.23           C  
ANISOU 3195  CB  LYS A 420    10473  10836  11073   1365  -1649    301       C  
ATOM   3196  CG  LYS A 420     -31.285   3.697   0.618  1.00 86.31           C  
ANISOU 3196  CG  LYS A 420    10582  11097  11113   1350  -1804    298       C  
ATOM   3197  CD  LYS A 420     -32.764   3.354   0.645  1.00 88.17           C  
ANISOU 3197  CD  LYS A 420    10617  11411  11474   1422  -1927    264       C  
ATOM   3198  CE  LYS A 420     -33.173   2.588  -0.602  1.00 91.59           C  
ANISOU 3198  CE  LYS A 420    11035  11960  11804   1410  -2110    258       C  
ATOM   3199  NZ  LYS A 420     -34.555   2.044  -0.495  1.00 93.15           N  
ANISOU 3199  NZ  LYS A 420    11006  12243  12144   1445  -2230    204       N  
ATOM   3200  N   LEU A 421     -28.558   5.685   4.013  1.00 86.75           N  
ANISOU 3200  N   LEU A 421    10866  10789  11307   1229  -1287    254       N  
ATOM   3201  CA  LEU A 421     -28.160   6.714   4.961  1.00 87.69           C  
ANISOU 3201  CA  LEU A 421    11049  10772  11496   1246  -1181    247       C  
ATOM   3202  C   LEU A 421     -26.862   7.361   4.496  1.00 85.07           C  
ANISOU 3202  C   LEU A 421    10892  10351  11078   1178  -1138    315       C  
ATOM   3203  O   LEU A 421     -25.895   6.666   4.173  1.00 88.13           O  
ANISOU 3203  O   LEU A 421    11322  10794  11370   1065  -1110    308       O  
ATOM   3204  CB  LEU A 421     -27.986   6.114   6.357  1.00 89.54           C  
ANISOU 3204  CB  LEU A 421    11209  11026  11788   1181  -1072    134       C  
ATOM   3205  CG  LEU A 421     -29.178   6.115   7.321  1.00 90.24           C  
ANISOU 3205  CG  LEU A 421    11156  11127  12005   1271  -1045     73       C  
ATOM   3206  CD1 LEU A 421     -30.453   5.649   6.636  1.00 96.35           C  
ANISOU 3206  CD1 LEU A 421    11787  11999  12823   1347  -1159     95       C  
ATOM   3207  CD2 LEU A 421     -28.876   5.250   8.539  1.00 78.62           C  
ANISOU 3207  CD2 LEU A 421     9625   9703  10545   1185   -938    -26       C  
ATOM   3208  N   SER A 422     -26.844   8.690   4.454  1.00 83.73           N  
ANISOU 3208  N   SER A 422    10822  10039  10954   1248  -1128    383       N  
ATOM   3209  CA  SER A 422     -25.622   9.367   4.043  1.00 85.18           C  
ANISOU 3209  CA  SER A 422    11164  10124  11077   1173  -1077    455       C  
ATOM   3210  C   SER A 422     -24.629   9.406   5.205  1.00 77.20           C  
ANISOU 3210  C   SER A 422    10175   9053  10106   1063   -960    369       C  
ATOM   3211  O   SER A 422     -25.011   9.709   6.338  1.00 75.59           O  
ANISOU 3211  O   SER A 422     9929   8794   9997   1099   -917    287       O  
ATOM   3212  CB  SER A 422     -25.921  10.785   3.567  1.00 96.69           C  
ANISOU 3212  CB  SER A 422    12730  11431  12576   1280  -1108    566       C  
ATOM   3213  OG  SER A 422     -24.754  11.403   3.049  1.00102.83           O  
ANISOU 3213  OG  SER A 422    13660  12114  13298   1197  -1057    653       O  
ATOM   3214  N   PRO A 423     -23.361   9.096   4.956  1.00 69.77           N  
ANISOU 3214  N   PRO A 423     9294   8127   9089    932   -909    383       N  
ATOM   3215  CA  PRO A 423     -22.373   9.081   6.038  1.00 68.45           C  
ANISOU 3215  CA  PRO A 423     9134   7915   8957    823   -818    301       C  
ATOM   3216  C   PRO A 423     -22.126  10.481   6.567  1.00 74.46           C  
ANISOU 3216  C   PRO A 423     9994   8488   9809    836   -780    311       C  
ATOM   3217  O   PRO A 423     -22.034  11.443   5.789  1.00 76.04           O  
ANISOU 3217  O   PRO A 423    10299   8580  10015    867   -795    420       O  
ATOM   3218  CB  PRO A 423     -21.115   8.509   5.364  1.00 66.16           C  
ANISOU 3218  CB  PRO A 423     8881   7687   8571    697   -784    341       C  
ATOM   3219  CG  PRO A 423     -21.614   7.830   4.122  1.00 69.05           C  
ANISOU 3219  CG  PRO A 423     9232   8169   8835    743   -854    403       C  
ATOM   3220  CD  PRO A 423     -22.788   8.640   3.680  1.00 69.10           C  
ANISOU 3220  CD  PRO A 423     9261   8118   8877    883   -933    468       C  
ATOM   3221  N   PRO A 424     -22.014  10.639   7.890  1.00 75.50           N  
ANISOU 3221  N   PRO A 424    10107   8571  10009    815   -730    198       N  
ATOM   3222  CA  PRO A 424     -21.766  11.973   8.455  1.00 72.93           C  
ANISOU 3222  CA  PRO A 424     9886   8053   9773    823   -698    186       C  
ATOM   3223  C   PRO A 424     -20.342  12.463   8.255  1.00 74.00           C  
ANISOU 3223  C   PRO A 424    10113   8098   9904    680   -659    225       C  
ATOM   3224  O   PRO A 424     -20.079  13.649   8.486  1.00 78.09           O  
ANISOU 3224  O   PRO A 424    10733   8436  10502    673   -641    236       O  
ATOM   3225  CB  PRO A 424     -22.082  11.781   9.941  1.00 70.39           C  
ANISOU 3225  CB  PRO A 424     9511   7739   9495    842   -661     37       C  
ATOM   3226  CG  PRO A 424     -21.733  10.351  10.195  1.00 61.16           C  
ANISOU 3226  CG  PRO A 424     8239   6749   8250    762   -650    -14       C  
ATOM   3227  CD  PRO A 424     -22.106   9.605   8.936  1.00 65.37           C  
ANISOU 3227  CD  PRO A 424     8719   7401   8718    785   -702     77       C  
ATOM   3228  N   PHE A 425     -19.421  11.597   7.840  1.00 69.63           N  
ANISOU 3228  N   PHE A 425     9522   7659   9273    566   -641    246       N  
ATOM   3229  CA  PHE A 425     -18.037  11.977   7.592  1.00 63.05           C  
ANISOU 3229  CA  PHE A 425     8749   6762   8446    424   -595    291       C  
ATOM   3230  C   PHE A 425     -17.593  11.399   6.257  1.00 60.05           C  
ANISOU 3230  C   PHE A 425     8367   6483   7966    387   -588    408       C  
ATOM   3231  O   PHE A 425     -17.747  10.198   6.014  1.00 52.69           O  
ANISOU 3231  O   PHE A 425     7352   5717   6950    394   -602    383       O  
ATOM   3232  CB  PHE A 425     -17.116  11.489   8.715  1.00 48.82           C  
ANISOU 3232  CB  PHE A 425     6892   4999   6661    307   -565    172       C  
ATOM   3233  CG  PHE A 425     -15.654  11.681   8.428  1.00 51.26           C  
ANISOU 3233  CG  PHE A 425     7220   5274   6982    153   -521    216       C  
ATOM   3234  CD1 PHE A 425     -15.079  12.938   8.498  1.00 50.79           C  
ANISOU 3234  CD1 PHE A 425     7254   5029   7016     87   -502    247       C  
ATOM   3235  CD2 PHE A 425     -14.852  10.602   8.097  1.00 45.20           C  
ANISOU 3235  CD2 PHE A 425     6374   4656   6145     74   -496    227       C  
ATOM   3236  CE1 PHE A 425     -13.735  13.116   8.238  1.00 60.71           C  
ANISOU 3236  CE1 PHE A 425     8509   6257   8302    -65   -457    292       C  
ATOM   3237  CE2 PHE A 425     -13.508  10.774   7.837  1.00 49.49           C  
ANISOU 3237  CE2 PHE A 425     6915   5177   6714    -63   -447    270       C  
ATOM   3238  CZ  PHE A 425     -12.949  12.031   7.906  1.00 61.03           C  
ANISOU 3238  CZ  PHE A 425     8454   6461   8274   -138   -428    305       C  
ATOM   3239  N   LYS A 426     -17.050  12.254   5.395  1.00 57.31           N  
ANISOU 3239  N   LYS A 426     8120   6032   7625    349   -559    534       N  
ATOM   3240  CA  LYS A 426     -16.569  11.823   4.090  1.00 61.53           C  
ANISOU 3240  CA  LYS A 426     8675   6654   8050    317   -535    653       C  
ATOM   3241  C   LYS A 426     -15.049  11.779   4.111  1.00 58.43           C  
ANISOU 3241  C   LYS A 426     8272   6255   7673    154   -449    667       C  
ATOM   3242  O   LYS A 426     -14.407  12.836   4.210  1.00 64.14           O  
ANISOU 3242  O   LYS A 426     9063   6820   8486     78   -407    715       O  
ATOM   3243  CB  LYS A 426     -17.069  12.762   2.989  1.00 62.88           C  
ANISOU 3243  CB  LYS A 426     8967   6727   8196    401   -555    809       C  
ATOM   3244  CG  LYS A 426     -18.536  12.575   2.634  1.00 69.53           C  
ANISOU 3244  CG  LYS A 426     9798   7625   8994    569   -653    818       C  
ATOM   3245  CD  LYS A 426     -18.757  11.238   1.944  1.00 75.74           C  
ANISOU 3245  CD  LYS A 426    10514   8621   9641    588   -689    807       C  
ATOM   3246  CE  LYS A 426     -20.222  10.995   1.618  1.00 78.64           C  
ANISOU 3246  CE  LYS A 426    10847   9053   9978    742   -802    805       C  
ATOM   3247  NZ  LYS A 426     -20.417   9.715   0.877  1.00 75.01           N  
ANISOU 3247  NZ  LYS A 426    10332   8783   9384    748   -847    789       N  
ATOM   3248  N   PRO A 427     -14.434  10.600   4.018  1.00 56.78           N  
ANISOU 3248  N   PRO A 427     7975   6207   7393     95   -420    628       N  
ATOM   3249  CA  PRO A 427     -12.969  10.526   4.031  1.00 47.33           C  
ANISOU 3249  CA  PRO A 427     6744   5015   6223    -53   -336    644       C  
ATOM   3250  C   PRO A 427     -12.362  11.307   2.876  1.00 49.38           C  
ANISOU 3250  C   PRO A 427     7098   5199   6465   -101   -263    810       C  
ATOM   3251  O   PRO A 427     -12.972  11.474   1.818  1.00 50.71           O  
ANISOU 3251  O   PRO A 427     7351   5376   6540    -13   -274    918       O  
ATOM   3252  CB  PRO A 427     -12.689   9.024   3.898  1.00 46.37           C  
ANISOU 3252  CB  PRO A 427     6521   5090   6006    -60   -324    589       C  
ATOM   3253  CG  PRO A 427     -13.940   8.358   4.366  1.00 56.32           C  
ANISOU 3253  CG  PRO A 427     7743   6420   7235     54   -410    497       C  
ATOM   3254  CD  PRO A 427     -15.056   9.268   3.947  1.00 55.19           C  
ANISOU 3254  CD  PRO A 427     7692   6181   7098    162   -463    562       C  
ATOM   3255  N   GLN A 428     -11.135  11.781   3.088  1.00 55.81           N  
ANISOU 3255  N   GLN A 428     7894   5941   7369   -243   -188    832       N  
ATOM   3256  CA  GLN A 428     -10.483  12.673   2.128  1.00 66.30           C  
ANISOU 3256  CA  GLN A 428     9311   7168   8712   -310   -100    997       C  
ATOM   3257  C   GLN A 428      -9.808  11.859   1.022  1.00 60.72           C  
ANISOU 3257  C   GLN A 428     8578   6615   7876   -334     -8   1083       C  
ATOM   3258  O   GLN A 428      -8.586  11.825   0.875  1.00 55.89           O  
ANISOU 3258  O   GLN A 428     7910   6019   7307   -459     93   1122       O  
ATOM   3259  CB  GLN A 428      -9.496  13.589   2.841  1.00 73.25           C  
ANISOU 3259  CB  GLN A 428    10175   7892   9765   -463    -60    983       C  
ATOM   3260  CG  GLN A 428      -8.995  14.733   1.969  1.00 84.74           C  
ANISOU 3260  CG  GLN A 428    11738   9193  11269   -532     28   1160       C  
ATOM   3261  CD  GLN A 428      -8.825  16.023   2.742  1.00 88.50           C  
ANISOU 3261  CD  GLN A 428    12267   9432  11928   -612      7   1136       C  
ATOM   3262  OE1 GLN A 428      -7.999  16.114   3.650  1.00 93.86           O  
ANISOU 3262  OE1 GLN A 428    12859  10073  12729   -743      4   1037       O  
ATOM   3263  NE2 GLN A 428      -9.615  17.030   2.388  1.00 84.11           N  
ANISOU 3263  NE2 GLN A 428    11858   8710  11392   -530    -17   1223       N  
ATOM   3264  N   VAL A 429     -10.646  11.194   0.228  1.00 63.90           N  
ANISOU 3264  N   VAL A 429     9024   7136   8121   -208    -46   1108       N  
ATOM   3265  CA  VAL A 429     -10.198  10.450  -0.943  1.00 65.90           C  
ANISOU 3265  CA  VAL A 429     9288   7532   8220   -201     34   1187       C  
ATOM   3266  C   VAL A 429     -11.215  10.653  -2.057  1.00 70.45           C  
ANISOU 3266  C   VAL A 429    10001   8121   8647    -68    -15   1292       C  
ATOM   3267  O   VAL A 429     -12.414  10.811  -1.811  1.00 76.72           O  
ANISOU 3267  O   VAL A 429    10825   8885   9441     42   -136   1254       O  
ATOM   3268  CB  VAL A 429     -10.003   8.940  -0.658  1.00 60.31           C  
ANISOU 3268  CB  VAL A 429     8456   7009   7450   -193     25   1056       C  
ATOM   3269  CG1 VAL A 429      -8.781   8.704   0.222  1.00 61.21           C  
ANISOU 3269  CG1 VAL A 429     8436   7130   7691   -325     88    984       C  
ATOM   3270  CG2 VAL A 429     -11.248   8.345  -0.021  1.00 59.30           C  
ANISOU 3270  CG2 VAL A 429     8297   6927   7306    -85   -111    931       C  
ATOM   3271  N   THR A 430     -10.721  10.653  -3.295  1.00 72.08           N  
ANISOU 3271  N   THR A 430    10288   8377   8722    -74     81   1429       N  
ATOM   3272  CA  THR A 430     -11.567  10.809  -4.472  1.00 77.13           C  
ANISOU 3272  CA  THR A 430    11070   9045   9189     51     35   1542       C  
ATOM   3273  C   THR A 430     -11.812   9.501  -5.210  1.00 75.39           C  
ANISOU 3273  C   THR A 430    10844   9029   8773    123     12   1489       C  
ATOM   3274  O   THR A 430     -12.790   9.404  -5.960  1.00 73.74           O  
ANISOU 3274  O   THR A 430    10727   8869   8423    246    -85   1526       O  
ATOM   3275  CB  THR A 430     -10.948  11.820  -5.445  1.00 81.48           C  
ANISOU 3275  CB  THR A 430    11757   9501   9701      8    156   1751       C  
ATOM   3276  OG1 THR A 430      -9.573  11.483  -5.672  1.00 84.22           O  
ANISOU 3276  OG1 THR A 430    12043   9907  10049   -117    324   1779       O  
ATOM   3277  CG2 THR A 430     -11.039  13.228  -4.879  1.00 79.87           C  
ANISOU 3277  CG2 THR A 430    11602   9067   9678    -31    145   1816       C  
ATOM   3278  N   SER A 431     -10.954   8.502  -5.019  1.00 69.43           N  
ANISOU 3278  N   SER A 431     9983   8388   8010     55     92   1401       N  
ATOM   3279  CA  SER A 431     -11.118   7.198  -5.641  1.00 64.18           C  
ANISOU 3279  CA  SER A 431     9310   7901   7174    118     76   1329       C  
ATOM   3280  C   SER A 431     -10.732   6.123  -4.635  1.00 66.02           C  
ANISOU 3280  C   SER A 431     9378   8207   7501     68     74   1158       C  
ATOM   3281  O   SER A 431     -10.278   6.416  -3.526  1.00 65.57           O  
ANISOU 3281  O   SER A 431     9219   8074   7621    -15     88   1106       O  
ATOM   3282  CB  SER A 431     -10.270   7.073  -6.911  1.00 61.49           C  
ANISOU 3282  CB  SER A 431     9060   7637   6667    103    226   1448       C  
ATOM   3283  OG  SER A 431      -9.960   5.716  -7.167  1.00 71.76           O  
ANISOU 3283  OG  SER A 431    10307   9096   7863    121    257   1340       O  
ATOM   3284  N   GLU A 432     -10.921   4.862  -5.029  1.00 62.70           N  
ANISOU 3284  N   GLU A 432     8939   7929   6954    122     50   1069       N  
ATOM   3285  CA  GLU A 432     -10.466   3.748  -4.208  1.00 70.00           C  
ANISOU 3285  CA  GLU A 432     9721   8925   7951     82     63    923       C  
ATOM   3286  C   GLU A 432      -9.010   3.390  -4.457  1.00 62.91           C  
ANISOU 3286  C   GLU A 432     8770   8081   7054      5    235    947       C  
ATOM   3287  O   GLU A 432      -8.438   2.614  -3.685  1.00 62.64           O  
ANISOU 3287  O   GLU A 432     8604   8087   7108    -37    258    845       O  
ATOM   3288  CB  GLU A 432     -11.343   2.514  -4.428  1.00 86.02           C  
ANISOU 3288  CB  GLU A 432    11747  11063   9873    170    -42    805       C  
ATOM   3289  CG  GLU A 432     -12.735   2.642  -3.837  1.00103.76           C  
ANISOU 3289  CG  GLU A 432    13980  13271  12176    233   -211    745       C  
ATOM   3290  CD  GLU A 432     -13.605   1.424  -4.084  1.00116.67           C  
ANISOU 3290  CD  GLU A 432    15601  15008  13721    303   -317    632       C  
ATOM   3291  OE1 GLU A 432     -13.075   0.395  -4.550  1.00120.27           O  
ANISOU 3291  OE1 GLU A 432    16055  15556  14086    300   -261    578       O  
ATOM   3292  OE2 GLU A 432     -14.822   1.500  -3.814  1.00121.65           O  
ANISOU 3292  OE2 GLU A 432    16220  15622  14382    362   -454    596       O  
ATOM   3293  N   THR A 433      -8.399   3.930  -5.505  1.00 59.91           N  
ANISOU 3293  N   THR A 433     8482   7703   6579    -11    359   1087       N  
ATOM   3294  CA  THR A 433      -6.959   3.838  -5.679  1.00 61.21           C  
ANISOU 3294  CA  THR A 433     8579   7900   6780    -97    542   1133       C  
ATOM   3295  C   THR A 433      -6.228   4.996  -5.016  1.00 57.64           C  
ANISOU 3295  C   THR A 433     8062   7316   6522   -220    602   1212       C  
ATOM   3296  O   THR A 433      -4.992   5.006  -5.000  1.00 63.65           O  
ANISOU 3296  O   THR A 433     8731   8094   7358   -311    746   1249       O  
ATOM   3297  CB  THR A 433      -6.606   3.781  -7.168  1.00 63.62           C  
ANISOU 3297  CB  THR A 433     9013   8282   6877    -55    671   1245       C  
ATOM   3298  OG1 THR A 433      -7.015   4.997  -7.805  1.00 69.98           O  
ANISOU 3298  OG1 THR A 433     9965   8998   7627    -45    669   1405       O  
ATOM   3299  CG2 THR A 433      -7.310   2.609  -7.831  1.00 58.63           C  
ANISOU 3299  CG2 THR A 433     8453   7777   6048     62    600   1148       C  
ATOM   3300  N   ASP A 434      -6.964   5.969  -4.479  1.00 55.66           N  
ANISOU 3300  N   ASP A 434     7854   6933   6361   -225    495   1234       N  
ATOM   3301  CA  ASP A 434      -6.357   7.051  -3.717  1.00 56.72           C  
ANISOU 3301  CA  ASP A 434     7932   6924   6694   -345    527   1280       C  
ATOM   3302  C   ASP A 434      -5.660   6.483  -2.488  1.00 56.93           C  
ANISOU 3302  C   ASP A 434     7776   6977   6879   -422    515   1145       C  
ATOM   3303  O   ASP A 434      -6.257   5.733  -1.710  1.00 53.63           O  
ANISOU 3303  O   ASP A 434     7302   6603   6472   -370    400   1007       O  
ATOM   3304  CB  ASP A 434      -7.428   8.066  -3.310  1.00 62.91           C  
ANISOU 3304  CB  ASP A 434     8805   7561   7535   -308    398   1299       C  
ATOM   3305  CG  ASP A 434      -6.847   9.399  -2.868  1.00 65.34           C  
ANISOU 3305  CG  ASP A 434     9114   7692   8020   -427    445   1380       C  
ATOM   3306  OD1 ASP A 434      -5.766   9.416  -2.241  1.00 64.11           O  
ANISOU 3306  OD1 ASP A 434     8830   7522   8005   -551    513   1347       O  
ATOM   3307  OD2 ASP A 434      -7.482  10.437  -3.149  1.00 68.34           O  
ANISOU 3307  OD2 ASP A 434     9622   7941   8404   -394    408   1476       O  
ATOM   3308  N   THR A 435      -4.390   6.844  -2.318  1.00 57.93           N  
ANISOU 3308  N   THR A 435     7806   7076   7129   -548    632   1194       N  
ATOM   3309  CA  THR A 435      -3.522   6.249  -1.311  1.00 69.33           C  
ANISOU 3309  CA  THR A 435     9066   8567   8709   -622    634   1084       C  
ATOM   3310  C   THR A 435      -3.257   7.192  -0.140  1.00 71.96           C  
ANISOU 3310  C   THR A 435     9336   8759   9247   -734    567   1052       C  
ATOM   3311  O   THR A 435      -2.247   7.056   0.554  1.00 74.23           O  
ANISOU 3311  O   THR A 435     9471   9063   9670   -832    590   1005       O  
ATOM   3312  CB  THR A 435      -2.202   5.816  -1.950  1.00 76.78           C  
ANISOU 3312  CB  THR A 435     9914   9607   9651   -678    811   1146       C  
ATOM   3313  OG1 THR A 435      -1.343   5.250  -0.953  1.00 93.05           O  
ANISOU 3313  OG1 THR A 435    11785  11716  11856   -742    798   1044       O  
ATOM   3314  CG2 THR A 435      -1.505   7.008  -2.594  1.00 67.68           C  
ANISOU 3314  CG2 THR A 435     8798   8358   8558   -785    947   1315       C  
ATOM   3315  N   ARG A 436      -4.164   8.142   0.105  1.00 66.40           N  
ANISOU 3315  N   ARG A 436     8746   7917   8566   -714    475   1067       N  
ATOM   3316  CA  ARG A 436      -3.877   9.197   1.072  1.00 71.51           C  
ANISOU 3316  CA  ARG A 436     9364   8406   9400   -825    427   1045       C  
ATOM   3317  C   ARG A 436      -3.749   8.649   2.490  1.00 69.81           C  
ANISOU 3317  C   ARG A 436     9022   8224   9278   -847    318    875       C  
ATOM   3318  O   ARG A 436      -2.893   9.102   3.257  1.00 61.05           O  
ANISOU 3318  O   ARG A 436     7817   7054   8325   -972    311    841       O  
ATOM   3319  CB  ARG A 436      -4.952  10.280   1.008  1.00 76.78           C  
ANISOU 3319  CB  ARG A 436    10193   8914  10066   -775    355   1092       C  
ATOM   3320  CG  ARG A 436      -4.603  11.513   1.816  1.00 85.19           C  
ANISOU 3320  CG  ARG A 436    11259   9787  11322   -894    325   1085       C  
ATOM   3321  CD  ARG A 436      -5.670  12.575   1.686  1.00 93.14           C  
ANISOU 3321  CD  ARG A 436    12433  10628  12329   -827    265   1137       C  
ATOM   3322  NE  ARG A 436      -6.000  13.153   2.983  1.00 96.04           N  
ANISOU 3322  NE  ARG A 436    12797  10866  12827   -850    152   1009       N  
ATOM   3323  CZ  ARG A 436      -5.367  14.189   3.521  1.00 96.38           C  
ANISOU 3323  CZ  ARG A 436    12839  10738  13041   -984    157   1008       C  
ATOM   3324  NH1 ARG A 436      -4.367  14.768   2.870  1.00 91.64           N  
ANISOU 3324  NH1 ARG A 436    12228  10073  12518  -1116    274   1140       N  
ATOM   3325  NH2 ARG A 436      -5.734  14.647   4.711  1.00101.50           N  
ANISOU 3325  NH2 ARG A 436    13500  11280  13785   -990     48    873       N  
ATOM   3326  N   TYR A 437      -4.582   7.680   2.861  1.00 70.66           N  
ANISOU 3326  N   TYR A 437     9128   8428   9291   -731    230    770       N  
ATOM   3327  CA  TYR A 437      -4.472   7.082   4.187  1.00 68.10           C  
ANISOU 3327  CA  TYR A 437     8696   8147   9034   -741    136    621       C  
ATOM   3328  C   TYR A 437      -3.407   5.997   4.253  1.00 70.91           C  
ANISOU 3328  C   TYR A 437     8899   8646   9399   -773    192    590       C  
ATOM   3329  O   TYR A 437      -3.291   5.320   5.280  1.00 69.87           O  
ANISOU 3329  O   TYR A 437     8677   8570   9301   -765    115    477       O  
ATOM   3330  CB  TYR A 437      -5.830   6.539   4.639  1.00 59.64           C  
ANISOU 3330  CB  TYR A 437     7682   7105   7875   -611     27    530       C  
ATOM   3331  CG  TYR A 437      -6.827   7.651   4.855  1.00 68.81           C  
ANISOU 3331  CG  TYR A 437     8966   8118   9062   -578    -40    539       C  
ATOM   3332  CD1 TYR A 437      -6.900   8.319   6.071  1.00 65.40           C  
ANISOU 3332  CD1 TYR A 437     8530   7580   8741   -621   -117    452       C  
ATOM   3333  CD2 TYR A 437      -7.669   8.060   3.831  1.00 75.46           C  
ANISOU 3333  CD2 TYR A 437     9932   8923   9815   -497    -27    635       C  
ATOM   3334  CE1 TYR A 437      -7.798   9.350   6.265  1.00 65.41           C  
ANISOU 3334  CE1 TYR A 437     8645   7436   8772   -579   -168    455       C  
ATOM   3335  CE2 TYR A 437      -8.570   9.088   4.015  1.00 76.26           C  
ANISOU 3335  CE2 TYR A 437    10139   8883   9952   -453    -87    650       C  
ATOM   3336  CZ  TYR A 437      -8.631   9.730   5.232  1.00 69.16           C  
ANISOU 3336  CZ  TYR A 437     9231   7873   9172   -492   -150    558       C  
ATOM   3337  OH  TYR A 437      -9.531  10.754   5.413  1.00 69.38           O  
ANISOU 3337  OH  TYR A 437     9368   7753   9239   -436   -201    567       O  
ATOM   3338  N   PHE A 438      -2.634   5.828   3.180  1.00 80.32           N  
ANISOU 3338  N   PHE A 438    10063   9896  10558   -799    329    692       N  
ATOM   3339  CA  PHE A 438      -1.422   5.026   3.197  1.00 85.35           C  
ANISOU 3339  CA  PHE A 438    10540  10649  11241   -843    405    680       C  
ATOM   3340  C   PHE A 438      -0.158   5.871   3.124  1.00 92.10           C  
ANISOU 3340  C   PHE A 438    11298  11447  12250   -996    495    760       C  
ATOM   3341  O   PHE A 438       0.937   5.337   3.336  1.00 98.17           O  
ANISOU 3341  O   PHE A 438    11900  12302  13099  -1048    544    743       O  
ATOM   3342  CB  PHE A 438      -1.427   4.022   2.034  1.00 83.26           C  
ANISOU 3342  CB  PHE A 438    10298  10514  10822   -747    512    722       C  
ATOM   3343  CG  PHE A 438      -2.712   3.256   1.896  1.00 80.45           C  
ANISOU 3343  CG  PHE A 438    10048  10204  10315   -608    429    657       C  
ATOM   3344  CD1 PHE A 438      -2.897   2.063   2.569  1.00 79.96           C  
ANISOU 3344  CD1 PHE A 438     9917  10228  10236   -543    360    540       C  
ATOM   3345  CD2 PHE A 438      -3.731   3.726   1.084  1.00 84.58           C  
ANISOU 3345  CD2 PHE A 438    10734  10682  10722   -543    416    718       C  
ATOM   3346  CE1 PHE A 438      -4.076   1.357   2.439  1.00 78.78           C  
ANISOU 3346  CE1 PHE A 438     9854  10112   9967   -430    286    481       C  
ATOM   3347  CE2 PHE A 438      -4.912   3.025   0.951  1.00 83.01           C  
ANISOU 3347  CE2 PHE A 438    10613  10528  10400   -424    330    655       C  
ATOM   3348  CZ  PHE A 438      -5.085   1.839   1.630  1.00 79.43           C  
ANISOU 3348  CZ  PHE A 438    10083  10154   9942   -375    268    535       C  
ATOM   3349  N   ASP A 439      -0.280   7.166   2.830  1.00 93.37           N  
ANISOU 3349  N   ASP A 439    11551  11461  12465  -1071    518    849       N  
ATOM   3350  CA  ASP A 439       0.858   8.070   2.759  1.00106.40           C  
ANISOU 3350  CA  ASP A 439    13115  13032  14280  -1235    602    931       C  
ATOM   3351  C   ASP A 439       1.354   8.410   4.167  1.00115.29           C  
ANISOU 3351  C   ASP A 439    14124  14098  15584  -1342    475    817       C  
ATOM   3352  O   ASP A 439       0.841   7.913   5.173  1.00109.81           O  
ANISOU 3352  O   ASP A 439    13423  13432  14866  -1281    335    682       O  
ATOM   3353  CB  ASP A 439       0.484   9.332   1.980  1.00107.65           C  
ANISOU 3353  CB  ASP A 439    13431  13034  14436  -1273    664   1069       C  
ATOM   3354  CG  ASP A 439       0.164   9.049   0.518  1.00107.91           C  
ANISOU 3354  CG  ASP A 439    13579  13137  14285  -1178    797   1198       C  
ATOM   3355  OD1 ASP A 439       0.609   8.004  -0.003  1.00107.29           O  
ANISOU 3355  OD1 ASP A 439    13427  13220  14119  -1125    886   1198       O  
ATOM   3356  OD2 ASP A 439      -0.530   9.878  -0.113  1.00107.26           O  
ANISOU 3356  OD2 ASP A 439    13666  12945  14142  -1150    810   1299       O  
ATOM   3357  N   GLU A 440       2.376   9.265   4.242  1.00128.84           N  
ANISOU 3357  N   GLU A 440    15748  15729  17476  -1509    525    872       N  
ATOM   3358  CA  GLU A 440       2.959   9.685   5.511  1.00134.14           C  
ANISOU 3358  CA  GLU A 440    16306  16337  18323  -1631    399    765       C  
ATOM   3359  C   GLU A 440       2.246  10.885   6.123  1.00130.78           C  
ANISOU 3359  C   GLU A 440    16028  15709  17955  -1675    288    721       C  
ATOM   3360  O   GLU A 440       2.752  11.463   7.091  1.00134.30           O  
ANISOU 3360  O   GLU A 440    16406  16068  18552  -1797    188    637       O  
ATOM   3361  CB  GLU A 440       4.452   9.989   5.335  1.00142.44           C  
ANISOU 3361  CB  GLU A 440    17163  17398  19560  -1802    494    833       C  
ATOM   3362  CG  GLU A 440       5.363   8.770   5.474  1.00146.47           C  
ANISOU 3362  CG  GLU A 440    17460  18107  20085  -1776    523    796       C  
ATOM   3363  CD  GLU A 440       5.422   7.922   4.213  1.00148.47           C  
ANISOU 3363  CD  GLU A 440    17717  18497  20198  -1668    704    898       C  
ATOM   3364  OE1 GLU A 440       4.412   7.856   3.483  1.00148.54           O  
ANISOU 3364  OE1 GLU A 440    17915  18492  20032  -1552    743    943       O  
ATOM   3365  OE2 GLU A 440       6.487   7.325   3.947  1.00149.55           O  
ANISOU 3365  OE2 GLU A 440    17665  18756  20400  -1695    806    930       O  
ATOM   3366  N   GLU A 441       1.098  11.283   5.570  1.00127.65           N  
ANISOU 3366  N   GLU A 441    15830  15231  17443  -1575    300    774       N  
ATOM   3367  CA  GLU A 441       0.152  12.105   6.312  1.00124.03           C  
ANISOU 3367  CA  GLU A 441    15515  14610  17000  -1551    174    694       C  
ATOM   3368  C   GLU A 441      -0.547  11.296   7.396  1.00121.01           C  
ANISOU 3368  C   GLU A 441    15129  14316  16534  -1438     31    527       C  
ATOM   3369  O   GLU A 441      -1.164  11.876   8.295  1.00121.78           O  
ANISOU 3369  O   GLU A 441    15312  14300  16659  -1427    -83    427       O  
ATOM   3370  CB  GLU A 441      -0.877  12.717   5.353  1.00125.04           C  
ANISOU 3370  CB  GLU A 441    15841  14637  17031  -1460    229    810       C  
ATOM   3371  CG  GLU A 441      -1.752  13.821   5.955  1.00128.34           C  
ANISOU 3371  CG  GLU A 441    16413  14850  17501  -1446    129    759       C  
ATOM   3372  CD  GLU A 441      -3.116  13.320   6.413  1.00130.69           C  
ANISOU 3372  CD  GLU A 441    16800  15194  17661  -1266     26    658       C  
ATOM   3373  OE1 GLU A 441      -3.544  12.240   5.955  1.00130.22           O  
ANISOU 3373  OE1 GLU A 441    16723  15303  17453  -1147     47    667       O  
ATOM   3374  OE2 GLU A 441      -3.762  14.010   7.230  1.00133.59           O  
ANISOU 3374  OE2 GLU A 441    17256  15426  18075  -1244    -71    568       O  
ATOM   3375  N   PHE A 442      -0.445   9.965   7.325  1.00118.09           N  
ANISOU 3375  N   PHE A 442    14666  14141  16064  -1354     45    499       N  
ATOM   3376  CA  PHE A 442      -0.994   9.090   8.356  1.00113.73           C  
ANISOU 3376  CA  PHE A 442    14096  13681  15437  -1256    -76    356       C  
ATOM   3377  C   PHE A 442      -0.376   9.373   9.721  1.00119.99           C  
ANISOU 3377  C   PHE A 442    14805  14437  16348  -1355   -200    230       C  
ATOM   3378  O   PHE A 442      -0.983   9.066  10.753  1.00114.65           O  
ANISOU 3378  O   PHE A 442    14164  13779  15618  -1286   -315    107       O  
ATOM   3379  CB  PHE A 442      -0.765   7.633   7.942  1.00106.35           C  
ANISOU 3379  CB  PHE A 442    13063  12944  14401  -1170    -23    365       C  
ATOM   3380  CG  PHE A 442      -1.542   6.628   8.744  1.00109.26           C  
ANISOU 3380  CG  PHE A 442    13443  13405  14667  -1046   -120    251       C  
ATOM   3381  CD1 PHE A 442      -2.908   6.473   8.559  1.00111.54           C  
ANISOU 3381  CD1 PHE A 442    13866  13680  14834   -919   -144    239       C  
ATOM   3382  CD2 PHE A 442      -0.898   5.808   9.656  1.00110.22           C  
ANISOU 3382  CD2 PHE A 442    13433  13629  14817  -1056   -186    165       C  
ATOM   3383  CE1 PHE A 442      -3.620   5.536   9.288  1.00109.06           C  
ANISOU 3383  CE1 PHE A 442    13554  13448  14438   -816   -219    143       C  
ATOM   3384  CE2 PHE A 442      -1.602   4.869  10.386  1.00110.30           C  
ANISOU 3384  CE2 PHE A 442    13460  13718  14731   -945   -263     75       C  
ATOM   3385  CZ  PHE A 442      -2.965   4.733  10.202  1.00108.69           C  
ANISOU 3385  CZ  PHE A 442    13389  13494  14415   -830   -273     65       C  
ATOM   3386  N   THR A 443       0.821   9.967   9.747  1.00126.86           N  
ANISOU 3386  N   THR A 443    15565  15258  17378  -1519   -180    259       N  
ATOM   3387  CA  THR A 443       1.480  10.261  11.017  1.00131.27           C  
ANISOU 3387  CA  THR A 443    16039  15786  18052  -1624   -315    134       C  
ATOM   3388  C   THR A 443       0.708  11.310  11.812  1.00127.84           C  
ANISOU 3388  C   THR A 443    15764  15172  17636  -1634   -421     39       C  
ATOM   3389  O   THR A 443       0.631  11.232  13.044  1.00133.34           O  
ANISOU 3389  O   THR A 443    16462  15875  18325  -1630   -560   -106       O  
ATOM   3390  CB  THR A 443       2.919  10.723  10.766  1.00137.89           C  
ANISOU 3390  CB  THR A 443    16712  16604  19077  -1809   -268    194       C  
ATOM   3391  OG1 THR A 443       2.908  12.033  10.185  1.00142.99           O  
ANISOU 3391  OG1 THR A 443    17451  17055  19824  -1915   -202    279       O  
ATOM   3392  CG2 THR A 443       3.624   9.761   9.818  1.00137.27           C  
ANISOU 3392  CG2 THR A 443    16488  16693  18977  -1783   -128    302       C  
ATOM   3393  N   ALA A 444       0.124  12.292  11.129  1.00119.46           N  
ANISOU 3393  N   ALA A 444    14847  13949  16593  -1638   -357    119       N  
ATOM   3394  CA  ALA A 444      -0.632  13.355  11.787  1.00112.21           C  
ANISOU 3394  CA  ALA A 444    14092  12840  15704  -1635   -441     36       C  
ATOM   3395  C   ALA A 444      -1.882  12.817  12.482  1.00105.24           C  
ANISOU 3395  C   ALA A 444    13309  12012  14666  -1459   -515    -71       C  
ATOM   3396  O   ALA A 444      -3.010  13.141  12.103  1.00103.74           O  
ANISOU 3396  O   ALA A 444    13261  11749  14406  -1346   -486    -38       O  
ATOM   3397  CB  ALA A 444      -1.011  14.432  10.778  1.00111.19           C  
ANISOU 3397  CB  ALA A 444    14095  12531  15623  -1654   -343    169       C  
TER    3398      ALA A 444                                                      
HETATM 3399  CAA L1Z A 501     -17.734 -16.376   7.926  1.00 46.32           C  
HETATM 3400  CAB L1Z A 501     -18.135 -15.426   6.997  1.00 46.75           C  
HETATM 3401  CAD L1Z A 501     -16.847 -13.750   8.044  1.00 48.35           C  
HETATM 3402  CAE L1Z A 501     -16.403 -14.671   9.019  1.00 42.57           C  
HETATM 3403  CAG L1Z A 501     -16.485 -12.398   7.983  1.00 41.34           C  
HETATM 3404  CAH L1Z A 501     -15.527 -14.366  10.070  1.00 38.59           C  
HETATM 3405  CAI L1Z A 501     -16.659 -11.540   9.066  1.00 32.23           C  
HETATM 3406  CAJ L1Z A 501     -16.293 -10.200   8.963  1.00 36.29           C  
HETATM 3407  CAK L1Z A 501     -15.770  -9.701   7.772  1.00 46.10           C  
HETATM 3408  CAL L1Z A 501     -15.611 -10.552   6.687  1.00 37.02           C  
HETATM 3409  CAM L1Z A 501     -15.975 -11.889   6.793  1.00 37.47           C  
HETATM 3410  CAN L1Z A 501     -15.831 -14.775  11.367  1.00 41.57           C  
HETATM 3411  CAO L1Z A 501     -14.962 -14.484  12.420  1.00 40.36           C  
HETATM 3412  CAP L1Z A 501     -13.772 -13.797  12.183  1.00 49.34           C  
HETATM 3413  CAQ L1Z A 501     -13.463 -13.402  10.890  1.00 30.27           C  
HETATM 3414  CAR L1Z A 501     -14.328 -13.695   9.844  1.00 39.05           C  
HETATM 3415  CAS L1Z A 501     -12.885 -13.486  13.216  1.00 43.21           C  
HETATM 3416  CAU L1Z A 501     -11.845 -15.619  13.586  1.00 50.71           C  
HETATM 3417  CAV L1Z A 501     -11.664 -16.779  14.548  1.00 56.70           C  
HETATM 3418  CAW L1Z A 501     -11.084 -16.259  15.857  1.00 63.75           C  
HETATM 3419  CAX L1Z A 501     -11.983 -15.177  16.430  1.00 51.95           C  
HETATM 3420  CAY L1Z A 501     -12.132 -14.070  15.407  1.00 51.96           C  
HETATM 3421  CBA L1Z A 501     -11.672 -18.318  17.275  1.00 77.83           C  
HETATM 3422  CBC L1Z A 501      -9.790 -18.579  18.275  1.00 80.13           C  
HETATM 3423  CBD L1Z A 501      -9.700 -17.522  17.463  1.00 81.34           C  
HETATM 3424  CBE L1Z A 501      -8.741 -18.951  19.017  1.00 83.63           C  
HETATM 3425  CBF L1Z A 501      -7.530 -18.258  18.960  1.00 86.20           C  
HETATM 3426  CBG L1Z A 501      -7.445 -17.139  18.131  1.00 92.99           C  
HETATM 3427  CBH L1Z A 501      -8.570 -16.826  17.377  1.00 91.13           C  
HETATM 3428  CBJ L1Z A 501      -5.542 -15.780  18.845  1.00 97.66           C  
HETATM 3429  CBK L1Z A 501      -5.750 -16.011  20.351  1.00 97.57           C  
HETATM 3430  CBL L1Z A 501      -4.371 -16.190  21.001  1.00 89.52           C  
HETATM 3431  CBO L1Z A 501     -19.005 -15.791   5.973  1.00 46.39           C  
HETATM 3432  NAC L1Z A 501     -17.686 -14.165   7.080  1.00 42.87           N  
HETATM 3433  NAF L1Z A 501     -16.862 -15.995   8.949  1.00 44.09           N  
HETATM 3434  NAT L1Z A 501     -12.729 -14.594  14.167  1.00 49.13           N  
HETATM 3435  NAZ L1Z A 501     -10.863 -17.357  16.837  1.00 77.10           N  
HETATM 3436  NBB L1Z A 501     -11.024 -19.077  18.159  1.00 78.87           N  
HETATM 3437  NBI L1Z A 501      -6.357 -16.366  17.921  1.00 98.44           N  
HETATM 3438  OBM L1Z A 501      -4.604 -15.067  18.492  1.00 91.93           O  
HETATM 3439  OBN L1Z A 501     -12.841 -18.488  16.921  1.00 78.09           O  
HETATM 3440  OBP L1Z A 501     -18.138 -17.536   7.858  1.00 48.99           O  
HETATM 3441  O   HOH A 601     -28.830  10.339  21.889  1.00 62.94           O  
HETATM 3442  O   HOH A 602     -11.465  -1.661  27.737  1.00 60.90           O  
HETATM 3443  O   HOH A 603     -16.023 -17.969  10.400  1.00 49.79           O  
HETATM 3444  O   HOH A 604      -9.440  -8.237  10.924  1.00 57.30           O  
HETATM 3445  O   HOH A 605     -13.254 -17.150  10.855  1.00 42.05           O  
HETATM 3446  O   HOH A 606     -11.717 -15.586   8.740  1.00 47.24           O  
HETATM 3447  O   HOH A 607     -35.352   1.613  14.937  1.00 53.21           O  
HETATM 3448  O   HOH A 608     -14.860 -16.267  15.241  1.00 45.54           O  
HETATM 3449  O   HOH A 609      -9.369  -2.078  21.380  1.00 56.87           O  
HETATM 3450  O   HOH A 610     -16.694  -9.517  19.153  1.00 50.69           O  
HETATM 3451  O   HOH A 611       7.231 -16.776   4.656  1.00 72.41           O  
HETATM 3452  O   HOH A 612     -12.085  -1.791  21.008  1.00 52.19           O  
CONECT 2299 3430                                                                
CONECT 3399 3400 3433 3440                                                      
CONECT 3400 3399 3431 3432                                                      
CONECT 3401 3402 3403 3432                                                      
CONECT 3402 3401 3404 3433                                                      
CONECT 3403 3401 3405 3409                                                      
CONECT 3404 3402 3410 3414                                                      
CONECT 3405 3403 3406                                                           
CONECT 3406 3405 3407                                                           
CONECT 3407 3406 3408                                                           
CONECT 3408 3407 3409                                                           
CONECT 3409 3403 3408                                                           
CONECT 3410 3404 3411                                                           
CONECT 3411 3410 3412                                                           
CONECT 3412 3411 3413 3415                                                      
CONECT 3413 3412 3414                                                           
CONECT 3414 3404 3413                                                           
CONECT 3415 3412 3434                                                           
CONECT 3416 3417 3434                                                           
CONECT 3417 3416 3418                                                           
CONECT 3418 3417 3419 3435                                                      
CONECT 3419 3418 3420                                                           
CONECT 3420 3419 3434                                                           
CONECT 3421 3435 3436 3439                                                      
CONECT 3422 3423 3424 3436                                                      
CONECT 3423 3422 3427 3435                                                      
CONECT 3424 3422 3425                                                           
CONECT 3425 3424 3426                                                           
CONECT 3426 3425 3427 3437                                                      
CONECT 3427 3423 3426                                                           
CONECT 3428 3429 3437 3438                                                      
CONECT 3429 3428 3430                                                           
CONECT 3430 2299 3429                                                           
CONECT 3431 3400                                                                
CONECT 3432 3400 3401                                                           
CONECT 3433 3399 3402                                                           
CONECT 3434 3415 3416 3420                                                      
CONECT 3435 3418 3421 3423                                                      
CONECT 3436 3421 3422                                                           
CONECT 3437 3426 3428                                                           
CONECT 3438 3428                                                                
CONECT 3439 3421                                                                
CONECT 3440 3399                                                                
MASTER      288    0    1   17   13    0    4    6 3445    1   43   35          
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.