CNRS Nantes University UFIP UFIP
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***  z5k8  ***

elNémo ID: 22050620260775027

Job options:

ID        	=	 22050620260775027
JOBID     	=	 z5k8
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 z5k8

HEADER    MEMBRANE PROTEIN/INHIBITOR              23-MAR-18   5ZK8              
TITLE     CRYSTAL STRUCTURE OF M2 MUSCARINIC ACETYLCHOLINE RECEPTOR BOUND WITH  
TITLE    2 NMS                                                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MUSCARINIC ACETYLCHOLINE RECEPTOR M2,REDESIGNED APO-       
COMPND   3 CYTOCHROME B562,MUSCARINIC ACETYLCHOLINE RECEPTOR M2;                
COMPND   4 CHAIN: A;                                                            
COMPND   5 FRAGMENT: UNP RESIDUES 10-217,UNP RESIDUES 377-466;                  
COMPND   6 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: CHRM2;                                                         
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108                                        
KEYWDS    GPCR CRYSTALLOGRAPHY, MEMBRANE PROTEIN-INHIBITOR COMPLEX              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.SUNO,S.MAEDA,S.YASUDA,K.YAMASHITA,K.HIRATA,S.HORITA,M.S.TAWARAMOTO, 
AUTHOR   2 H.TSUJIMOTO,T.MURATA,M.KINOSHITA,M.YAMAMOTO,B.K.KOBILKA,S.IWATA,     
AUTHOR   3 T.KOBAYASHI                                                          
REVDAT   4   23-MAR-22 5ZK8    1       REMARK                                   
REVDAT   3   12-DEC-18 5ZK8    1       REMARK DBREF  SEQADV HELIX               
REVDAT   3 2                   1       SSBOND SITE   ATOM                       
REVDAT   2   28-NOV-18 5ZK8    1       JRNL                                     
REVDAT   1   21-NOV-18 5ZK8    0                                                
JRNL        AUTH   R.SUNO,S.LEE,S.MAEDA,S.YASUDA,K.YAMASHITA,K.HIRATA,S.HORITA, 
JRNL        AUTH 2 M.S.TAWARAMOTO,H.TSUJIMOTO,T.MURATA,M.KINOSHITA,M.YAMAMOTO,  
JRNL        AUTH 3 B.K.KOBILKA,N.VAIDEHI,S.IWATA,T.KOBAYASHI                    
JRNL        TITL   STRUCTURAL INSIGHTS INTO THE SUBTYPE-SELECTIVE ANTAGONIST    
JRNL        TITL 2 BINDING TO THE M2MUSCARINIC RECEPTOR                         
JRNL        REF    NAT. CHEM. BIOL.              V.  14  1150 2018              
JRNL        REFN                   ESSN 1552-4469                               
JRNL        PMID   30420692                                                     
JRNL        DOI    10.1038/S41589-018-0152-Y                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.11.1_2575: ???)                            
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) : 3.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 38.34                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 9702                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.233                           
REMARK   3   R VALUE            (WORKING SET) : 0.231                           
REMARK   3   FREE R VALUE                     : 0.270                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.380                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 522                             
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 38.3400 -  4.7601    1.00     2352   129  0.2336 0.2542        
REMARK   3     2  4.7601 -  3.7793    1.00     2279   130  0.2095 0.2687        
REMARK   3     3  3.7793 -  3.3019    1.00     2267   133  0.2419 0.2826        
REMARK   3     4  3.3019 -  3.0001    1.00     2282   130  0.2609 0.3026        
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)     : 0.340            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.750           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  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      :  0.002           3023                                  
REMARK   3   ANGLE     :  0.475           4127                                  
REMARK   3   CHIRALITY :  0.036            496                                  
REMARK   3   PLANARITY :  0.003            494                                  
REMARK   3   DIHEDRAL  : 11.276           1801                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 3                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 18 THROUGH 213 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): 184.7394  31.7294 532.5604              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1938 T22:   0.3308                                     
REMARK   3      T33:   0.2782 T12:  -0.0131                                     
REMARK   3      T13:   0.0264 T23:  -0.0557                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0323 L22:   2.6027                                     
REMARK   3      L33:   2.1712 L12:  -0.5177                                     
REMARK   3      L13:  -0.1352 L23:  -0.0718                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0602 S12:  -0.1751 S13:   0.0300                       
REMARK   3      S21:   0.2913 S22:   0.0155 S23:  -0.1316                       
REMARK   3      S31:  -0.0889 S32:   0.2399 S33:   0.0241                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND ((RESID 214 THROUGH 214 ) OR (RESID      
REMARK   3               1001 THROUGH 1079 ))                                   
REMARK   3    ORIGIN FOR THE GROUP (A): 169.8288  13.3744 569.8650              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.2061 T22:   2.0531                                     
REMARK   3      T33:   0.8823 T12:   0.0426                                     
REMARK   3      T13:  -0.3042 T23:   0.1827                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.9525 L22:   3.6953                                     
REMARK   3      L33:   2.0536 L12:  -1.8749                                     
REMARK   3      L13:   1.3920 L23:   0.1889                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.8617 S12:  -1.3281 S13:  -0.3724                       
REMARK   3      S21:  -0.6987 S22:  -0.0530 S23:  -0.4173                       
REMARK   3      S31:   1.1284 S32:  -0.5363 S33:  -0.7615                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND ((RESID 1080 THROUFH 1106 ) OR (RESID    
REMARK   3               384 THROUGH 459 ))                                     
REMARK   3    ORIGIN FOR THE GROUP (A):  176.545   25.580  534.766              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4528 T22:   0.5023                                     
REMARK   3      T33:   0.3518 T12:   0.0206                                     
REMARK   3      T13:   0.0327 T23:   0.0523                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5154 L22:   1.9580                                     
REMARK   3      L33:   2.4640 L12:   0.3133                                     
REMARK   3      L13:  -0.1837 L23:   0.0640                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0631 S12:  -0.7242 S13:  -0.0119                       
REMARK   3      S21:   0.4356 S22:   0.0266 S23:   0.1428                       
REMARK   3      S31:  -0.4279 S32:   0.1345 S33:  -0.0573                       
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 5ZK8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 27-MAR-18.                  
REMARK 100 THE DEPOSITION ID IS D_1300007223.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-DEC-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL32XU                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1                                  
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX225-HS                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 9702                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 116.6                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 14.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.18                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.81                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.55                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 50MM MES-NAOH PH 6.2-7.0, 26-32 %        
REMARK 280  PEG300, 300~500MM AMMONIUM FLUORIDE, 1% 1,2,3-HEPTANETRIOL,         
REMARK 280  0.5MM NMS AND 5% DMSO, LIPIDIC CUBIC PHASE, TEMPERATURE 293K        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       29.60500            
REMARK 290   SMTRY3   2  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 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     PRO A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     ASP A     2                                                      
REMARK 465     ASP A     3                                                      
REMARK 465     SER A     4                                                      
REMARK 465     THR A     5                                                      
REMARK 465     ASP A     6                                                      
REMARK 465     SER A     7                                                      
REMARK 465     SER A     8                                                      
REMARK 465     ASP A     9                                                      
REMARK 465     ASN A    10                                                      
REMARK 465     SER A    11                                                      
REMARK 465     LEU A    12                                                      
REMARK 465     ALA A    13                                                      
REMARK 465     LEU A    14                                                      
REMARK 465     THR A    15                                                      
REMARK 465     SER A    16                                                      
REMARK 465     PRO A    17                                                      
REMARK 465     SER A   215                                                      
REMARK 465     ARG A   216                                                      
REMARK 465     ILE A   217                                                      
REMARK 465     PRO A  1046                                                      
REMARK 465     LYS A  1047                                                      
REMARK 465     LEU A  1048                                                      
REMARK 465     GLU A  1049                                                      
REMARK 465     ASP A  1050                                                      
REMARK 465     LYS A  1051                                                      
REMARK 465     SER A  1052                                                      
REMARK 465     PRO A  1053                                                      
REMARK 465     ASP A  1054                                                      
REMARK 465     SER A  1055                                                      
REMARK 465     PRO A   377                                                      
REMARK 465     PRO A   378                                                      
REMARK 465     PRO A   379                                                      
REMARK 465     SER A   380                                                      
REMARK 465     ARG A   381                                                      
REMARK 465     GLU A   382                                                      
REMARK 465     TYR A   459                                                      
REMARK 465     LYS A   460                                                      
REMARK 465     ASN A   461                                                      
REMARK 465     ILE A   462                                                      
REMARK 465     GLY A   463                                                      
REMARK 465     ALA A   464                                                      
REMARK 465     THR A   465                                                      
REMARK 465     ARG A   466                                                      
REMARK 465     LEU A   467                                                      
REMARK 465     GLU A   468                                                      
REMARK 465     VAL A   469                                                      
REMARK 465     LEU A   470                                                      
REMARK 465     PHE A   471                                                      
REMARK 465     GLN A   472                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     PRO A1056    CG   CD                                             
REMARK 470     GLU A1057    CG   CD   OE1  OE2                                  
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    GLN A  55       78.64   -115.59                                   
REMARK 500    THR A 130      -41.31   -135.21                                   
REMARK 500    PHE A 195      -59.65   -136.66                                   
REMARK 500    ASN A1022     -153.15   -112.17                                   
REMARK 500    TYR A 440      -34.04   -133.90                                   
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 3C0 A 501                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5XB9   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5XBA   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5XBB   RELATED DB: PDB                                   
DBREF  5ZK8 A   10   217  UNP    P08172   ACM2_HUMAN      10    217             
DBREF  5ZK8 A 1001  1106  PDB    5ZK8     5ZK8          1001   1106             
DBREF  5ZK8 A  377   466  UNP    P08172   ACM2_HUMAN     377    466             
SEQADV 5ZK8 GLY A   -1  UNP  P08172              EXPRESSION TAG                 
SEQADV 5ZK8 PRO A    0  UNP  P08172              EXPRESSION TAG                 
SEQADV 5ZK8 MET A    1  UNP  P08172              EXPRESSION TAG                 
SEQADV 5ZK8 ASP A    2  UNP  P08172              EXPRESSION TAG                 
SEQADV 5ZK8 ASP A    3  UNP  P08172              EXPRESSION TAG                 
SEQADV 5ZK8 SER A    4  UNP  P08172              EXPRESSION TAG                 
SEQADV 5ZK8 THR A    5  UNP  P08172              EXPRESSION TAG                 
SEQADV 5ZK8 ASP A    6  UNP  P08172              EXPRESSION TAG                 
SEQADV 5ZK8 SER A    7  UNP  P08172              EXPRESSION TAG                 
SEQADV 5ZK8 SER A    8  UNP  P08172              EXPRESSION TAG                 
SEQADV 5ZK8 ASP A    9  UNP  P08172              EXPRESSION TAG                 
SEQADV 5ZK8 LEU A  467  UNP  P08172              EXPRESSION TAG                 
SEQADV 5ZK8 GLU A  468  UNP  P08172              EXPRESSION TAG                 
SEQADV 5ZK8 VAL A  469  UNP  P08172              EXPRESSION TAG                 
SEQADV 5ZK8 LEU A  470  UNP  P08172              EXPRESSION TAG                 
SEQADV 5ZK8 PHE A  471  UNP  P08172              EXPRESSION TAG                 
SEQADV 5ZK8 GLN A  472  UNP  P08172              EXPRESSION TAG                 
SEQRES   1 A  421  GLY PRO MET ASP ASP SER THR ASP SER SER ASP ASN SER          
SEQRES   2 A  421  LEU ALA LEU THR SER PRO TYR LYS THR PHE GLU VAL VAL          
SEQRES   3 A  421  PHE ILE VAL LEU VAL ALA GLY SER LEU SER LEU VAL THR          
SEQRES   4 A  421  ILE ILE GLY ASN ILE LEU VAL MET VAL SER ILE LYS VAL          
SEQRES   5 A  421  ASN ARG HIS LEU GLN THR VAL ASN ASN TYR PHE LEU PHE          
SEQRES   6 A  421  SER LEU ALA CYS ALA ASP LEU ILE ILE GLY VAL PHE SER          
SEQRES   7 A  421  MET ASN LEU TYR THR LEU TYR THR VAL ILE GLY TYR TRP          
SEQRES   8 A  421  PRO LEU GLY PRO VAL VAL CYS ASP LEU TRP LEU ALA LEU          
SEQRES   9 A  421  ASP TYR VAL VAL SER ASN ALA SER VAL MET ASN LEU LEU          
SEQRES  10 A  421  ILE ILE SER PHE ASP ARG TYR PHE CYS VAL THR LYS PRO          
SEQRES  11 A  421  LEU THR TYR PRO VAL LYS ARG THR THR LYS MET ALA GLY          
SEQRES  12 A  421  MET MET ILE ALA ALA ALA TRP VAL LEU SER PHE ILE LEU          
SEQRES  13 A  421  TRP ALA PRO ALA ILE LEU PHE TRP GLN PHE ILE VAL GLY          
SEQRES  14 A  421  VAL ARG THR VAL GLU ASP GLY GLU CYS TYR ILE GLN PHE          
SEQRES  15 A  421  PHE SER ASN ALA ALA VAL THR PHE GLY THR ALA ILE ALA          
SEQRES  16 A  421  ALA PHE TYR LEU PRO VAL ILE ILE MET THR VAL LEU TYR          
SEQRES  17 A  421  TRP HIS ILE SER ARG ALA SER LYS SER ARG ILE ALA ASP          
SEQRES  18 A  421  LEU GLU ASP ASN TRP GLU THR LEU ASN ASP ASN LEU LYS          
SEQRES  19 A  421  VAL ILE GLU LYS ALA ASP ASN ALA ALA GLN VAL LYS ASP          
SEQRES  20 A  421  ALA LEU THR LYS MET ARG ALA ALA ALA LEU ASP ALA GLN          
SEQRES  21 A  421  LYS ALA THR PRO PRO LYS LEU GLU ASP LYS SER PRO ASP          
SEQRES  22 A  421  SER PRO GLU MET LYS ASP PHE ARG HIS GLY PHE ASP ILE          
SEQRES  23 A  421  LEU VAL GLY GLN ILE ASP ASP ALA LEU LYS LEU ALA ASN          
SEQRES  24 A  421  GLU GLY LYS VAL LYS GLU ALA GLN ALA ALA ALA GLU GLN          
SEQRES  25 A  421  LEU LYS THR THR ARG ASN ALA TYR ILE GLN LYS TYR LEU          
SEQRES  26 A  421  PRO PRO PRO SER ARG GLU LYS LYS VAL THR ARG THR ILE          
SEQRES  27 A  421  LEU ALA ILE LEU LEU ALA PHE ILE ILE THR TRP ALA PRO          
SEQRES  28 A  421  TYR ASN VAL MET VAL LEU ILE ASN THR PHE CYS ALA PRO          
SEQRES  29 A  421  CYS ILE PRO ASN THR VAL TRP THR ILE GLY TYR TRP LEU          
SEQRES  30 A  421  CYS TYR ILE ASN SER THR ILE ASN PRO ALA CYS TYR ALA          
SEQRES  31 A  421  LEU CYS ASN ALA THR PHE LYS LYS THR PHE LYS HIS LEU          
SEQRES  32 A  421  LEU MET CYS HIS TYR LYS ASN ILE GLY ALA THR ARG LEU          
SEQRES  33 A  421  GLU VAL LEU PHE GLN                                          
HET    3C0  A 501      23                                                       
HETNAM     3C0 N-METHYL SCOPOLAMINE                                             
HETSYN     3C0 (1R,2R,4S,5S,7S)-7-{[(2S)-3-HYDROXY-2-                           
HETSYN   2 3C0  PHENYLPROPANOYL]OXY}-9,9-DIMETHYL-3-OXA-9-                      
HETSYN   3 3C0  AZONIATRICYCLO[3.3.1.0~2,4~]NONANE                              
FORMUL   2  3C0    C18 H24 N O4 1+                                              
FORMUL   3  HOH   *4(H2 O)                                                      
HELIX    1 AA1 TYR A   18  ASN A   51  1                                  34    
HELIX    2 AA2 ARG A   52  GLN A   55  5                                   4    
HELIX    3 AA3 THR A   56  PHE A   75  1                                  20    
HELIX    4 AA4 PHE A   75  GLY A   87  1                                  13    
HELIX    5 AA5 GLY A   92  LYS A  127  1                                  36    
HELIX    6 AA6 THR A  130  ARG A  135  1                                   6    
HELIX    7 AA7 THR A  136  GLY A  167  1                                  32    
HELIX    8 AA8 ILE A  178  SER A  182  5                                   5    
HELIX    9 AA9 ASN A  183  PHE A  195  1                                  13    
HELIX   10 AB1 PHE A  195  LYS A  214  1                                  20    
HELIX   11 AB2 ASP A 1002  ALA A 1020  1                                  19    
HELIX   12 AB3 ALA A 1023  ALA A 1043  1                                  21    
HELIX   13 AB4 GLU A 1057  ASN A 1080  1                                  24    
HELIX   14 AB5 LYS A 1083  ALA A 1090  1                                   8    
HELIX   15 AB6 ALA A 1090  LEU A 1106  1                                  17    
HELIX   16 AB7 LYS A  384  CYS A  413  1                                  30    
HELIX   17 AB8 PRO A  418  ASN A  436  1                                  19    
HELIX   18 AB9 TYR A  440  CYS A  443  5                                   4    
HELIX   19 AC1 ASN A  444  LEU A  455  1                                  12    
SSBOND   1 CYS A   96    CYS A  176                          1555   1555  2.03  
SSBOND   2 CYS A  413    CYS A  416                          1555   1555  2.03  
SITE     1 AC1 12 ASP A 103  TYR A 104  SER A 107  TRP A 155                    
SITE     2 AC1 12 ALA A 191  ALA A 194  TRP A 400  TYR A 403                    
SITE     3 AC1 12 ASN A 404  TYR A 426  CYS A 429  TYR A 430                    
CRYST1   46.280   59.210   88.960  90.00  98.54  90.00 P 1 21 1      2          
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      0.021608  0.000000  0.003245        0.00000                         
SCALE2      0.000000  0.016889  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011367        0.00000                         
ATOM      1  N   TYR A  18     157.146  27.227 510.877  1.00180.32           N  
ANISOU    1  N   TYR A  18    20064  24279  24170    -67  -2431  -1679       N  
ATOM      2  CA  TYR A  18     157.514  27.166 512.287  1.00176.13           C  
ANISOU    2  CA  TYR A  18    19478  23645  23797   -123  -2156  -1613       C  
ATOM      3  C   TYR A  18     158.764  27.999 512.556  1.00170.91           C  
ANISOU    3  C   TYR A  18    18984  22976  22979      2  -2036  -1551       C  
ATOM      4  O   TYR A  18     159.062  28.337 513.701  1.00172.75           O  
ANISOU    4  O   TYR A  18    19176  23151  23311      7  -1818  -1470       O  
ATOM      5  CB  TYR A  18     157.736  25.714 512.721  1.00183.08           C  
ANISOU    5  CB  TYR A  18    20376  24394  24792   -327  -2060  -1709       C  
ATOM      6  CG  TYR A  18     158.025  25.547 514.197  1.00189.23           C  
ANISOU    6  CG  TYR A  18    21101  25066  25730   -393  -1776  -1630       C  
ATOM      7  CD1 TYR A  18     156.995  25.533 515.128  1.00193.49           C  
ANISOU    7  CD1 TYR A  18    21428  25596  26494   -447  -1658  -1548       C  
ATOM      8  CD2 TYR A  18     159.327  25.400 514.659  1.00187.86           C  
ANISOU    8  CD2 TYR A  18    21095  24813  25471   -395  -1624  -1634       C  
ATOM      9  CE1 TYR A  18     157.253  25.382 516.478  1.00192.53           C  
ANISOU    9  CE1 TYR A  18    21284  25382  26486   -497  -1394  -1468       C  
ATOM     10  CE2 TYR A  18     159.595  25.249 516.007  1.00186.20           C  
ANISOU   10  CE2 TYR A  18    20851  24511  25387   -449  -1371  -1555       C  
ATOM     11  CZ  TYR A  18     158.554  25.240 516.911  1.00187.35           C  
ANISOU   11  CZ  TYR A  18    20807  24644  25734   -497  -1256  -1470       C  
ATOM     12  OH  TYR A  18     158.816  25.088 518.254  1.00183.00           O  
ANISOU   12  OH  TYR A  18    20247  24008  25275   -540  -1000  -1385       O  
ATOM     13  N   LYS A  19     159.486  28.335 511.485  1.00151.33           N  
ANISOU   13  N   LYS A  19    16699  20562  20240    103  -2178  -1588       N  
ATOM     14  CA  LYS A  19     160.735  29.077 511.636  1.00129.60           C  
ANISOU   14  CA  LYS A  19    14122  17806  17315    212  -2067  -1525       C  
ATOM     15  C   LYS A  19     160.491  30.460 512.226  1.00108.79           C  
ANISOU   15  C   LYS A  19    11428  15187  14720    359  -1969  -1357       C  
ATOM     16  O   LYS A  19     161.288  30.946 513.037  1.00106.86           O  
ANISOU   16  O   LYS A  19    11294  14858  14450    380  -1739  -1255       O  
ATOM     17  CB  LYS A  19     161.453  29.187 510.289  1.00133.06           C  
ANISOU   17  CB  LYS A  19    14818  18304  17434    296  -2205  -1556       C  
ATOM     18  CG  LYS A  19     161.976  27.863 509.737  1.00133.54           C  
ANISOU   18  CG  LYS A  19    15003  18325  17411    171  -2255  -1724       C  
ATOM     19  CD  LYS A  19     160.895  27.090 508.992  1.00130.84           C  
ANISOU   19  CD  LYS A  19    14567  18015  17131     92  -2474  -1844       C  
ATOM     20  CE  LYS A  19     161.344  25.675 508.672  1.00122.70           C  
ANISOU   20  CE  LYS A  19    13654  16893  16072    -52  -2477  -2008       C  
ATOM     21  NZ  LYS A  19     160.245  24.876 508.064  1.00119.53           N  
ANISOU   21  NZ  LYS A  19    13165  16492  15757   -154  -2656  -2105       N  
ATOM     22  N   THR A  20     159.395  31.113 511.830  1.00 98.72           N  
ANISOU   22  N   THR A  20     9999  14006  13503    463  -2134  -1321       N  
ATOM     23  CA  THR A  20     159.064  32.411 512.410  1.00 94.21           C  
ANISOU   23  CA  THR A  20     9349  13445  13002    620  -2055  -1182       C  
ATOM     24  C   THR A  20     158.716  32.276 513.887  1.00 94.56           C  
ANISOU   24  C   THR A  20     9230  13402  13294    538  -1811  -1145       C  
ATOM     25  O   THR A  20     159.054  33.149 514.695  1.00 87.95           O  
ANISOU   25  O   THR A  20     8429  12513  12475    626  -1635  -1045       O  
ATOM     26  CB  THR A  20     157.908  33.056 511.643  1.00 93.95           C  
ANISOU   26  CB  THR A  20     9219  13507  12970    742  -2254  -1125       C  
ATOM     27  OG1 THR A  20     156.740  32.232 511.744  1.00 93.61           O  
ANISOU   27  OG1 THR A  20     8968  13479  13120    610  -2304  -1182       O  
ATOM     28  CG2 THR A  20     158.272  33.231 510.176  1.00 97.00           C  
ANISOU   28  CG2 THR A  20     9802  13981  13074    835  -2485  -1144       C  
ATOM     29  N   PHE A  21     158.041  31.185 514.255  1.00 96.86           N  
ANISOU   29  N   PHE A  21     9387  13662  13753    366  -1777  -1206       N  
ATOM     30  CA  PHE A  21     157.743  30.930 515.660  1.00 92.78           C  
ANISOU   30  CA  PHE A  21     8747  13065  13438    281  -1532  -1162       C  
ATOM     31  C   PHE A  21     159.017  30.648 516.445  1.00 85.76           C  
ANISOU   31  C   PHE A  21     8004  12081  12503    221  -1331  -1170       C  
ATOM     32  O   PHE A  21     159.137  31.044 517.612  1.00 86.38           O  
ANISOU   32  O   PHE A  21     8058  12104  12659    240  -1114  -1096       O  
ATOM     33  CB  PHE A  21     156.764  29.760 515.773  1.00 97.69           C  
ANISOU   33  CB  PHE A  21     9209  13676  14232    107  -1553  -1217       C  
ATOM     34  CG  PHE A  21     156.323  29.460 517.178  1.00 97.11           C  
ANISOU   34  CG  PHE A  21     9009  13536  14351     24  -1305  -1156       C  
ATOM     35  CD1 PHE A  21     155.207  30.080 517.716  1.00103.81           C  
ANISOU   35  CD1 PHE A  21     9665  14438  15339     94  -1243  -1070       C  
ATOM     36  CD2 PHE A  21     157.013  28.544 517.956  1.00 88.71           C  
ANISOU   36  CD2 PHE A  21     8027  12362  13318   -116  -1130  -1180       C  
ATOM     37  CE1 PHE A  21     154.793  29.799 519.008  1.00101.83           C  
ANISOU   37  CE1 PHE A  21     9314  14139  15236     26  -1005  -1011       C  
ATOM     38  CE2 PHE A  21     156.607  28.261 519.247  1.00 90.50           C  
ANISOU   38  CE2 PHE A  21     8162  12534  13692   -183   -901  -1111       C  
ATOM     39  CZ  PHE A  21     155.495  28.888 519.773  1.00 95.48           C  
ANISOU   39  CZ  PHE A  21     8609  13226  14443   -114   -836  -1029       C  
ATOM     40  N   GLU A  22     159.984  29.974 515.814  1.00 87.96           N  
ANISOU   40  N   GLU A  22     8438  12342  12640    157  -1401  -1261       N  
ATOM     41  CA  GLU A  22     161.214  29.608 516.506  1.00 86.68           C  
ANISOU   41  CA  GLU A  22     8472  12068  12396     90  -1189  -1234       C  
ATOM     42  C   GLU A  22     162.068  30.825 516.824  1.00 81.39           C  
ANISOU   42  C   GLU A  22     7982  11371  11572    221  -1060  -1109       C  
ATOM     43  O   GLU A  22     162.787  30.826 517.826  1.00 80.28           O  
ANISOU   43  O   GLU A  22     7924  11147  11431    187   -854  -1060       O  
ATOM     44  CB  GLU A  22     162.020  28.611 515.673  1.00102.93           C  
ANISOU   44  CB  GLU A  22    10701  14097  14309      4  -1272  -1337       C  
ATOM     45  CG  GLU A  22     163.256  28.082 516.392  1.00109.62           C  
ANISOU   45  CG  GLU A  22    11721  14831  15098    -65  -1064  -1315       C  
ATOM     46  CD  GLU A  22     164.142  27.241 515.498  1.00107.88           C  
ANISOU   46  CD  GLU A  22    11687  14587  14716   -110  -1134  -1409       C  
ATOM     47  OE1 GLU A  22     163.713  26.914 514.373  1.00104.50           O  
ANISOU   47  OE1 GLU A  22    11252  14221  14231   -112  -1344  -1512       O  
ATOM     48  OE2 GLU A  22     165.270  26.910 515.921  1.00104.90           O  
ANISOU   48  OE2 GLU A  22    11463  14131  14263   -135   -982  -1385       O  
ATOM     49  N   VAL A  23     162.017  31.861 515.988  1.00 66.66           N  
ANISOU   49  N   VAL A  23     6185   9569   9574    368  -1184  -1057       N  
ATOM     50  CA  VAL A  23     162.753  33.085 516.289  1.00 65.89           C  
ANISOU   50  CA  VAL A  23     6250   9426   9358    483  -1064   -935       C  
ATOM     51  C   VAL A  23     162.247  33.694 517.591  1.00 79.47           C  
ANISOU   51  C   VAL A  23     7848  11102  11246    521   -896   -874       C  
ATOM     52  O   VAL A  23     163.031  34.012 518.494  1.00 80.37           O  
ANISOU   52  O   VAL A  23     8077  11133  11329    510   -708   -823       O  
ATOM     53  CB  VAL A  23     162.646  34.073 515.117  1.00 74.43           C  
ANISOU   53  CB  VAL A  23     7421  10575  10285    637  -1232   -877       C  
ATOM     54  CG1 VAL A  23     163.372  35.367 515.441  1.00 71.67           C  
ANISOU   54  CG1 VAL A  23     7240  10153   9840    743  -1103   -747       C  
ATOM     55  CG2 VAL A  23     163.212  33.437 513.866  1.00 81.48           C  
ANISOU   55  CG2 VAL A  23     8460  11517  10980    603  -1374   -942       C  
ATOM     56  N   VAL A  24     160.924  33.840 517.711  1.00 78.67           N  
ANISOU   56  N   VAL A  24     7506  11062  11323    569   -964   -884       N  
ATOM     57  CA  VAL A  24     160.328  34.392 518.927  1.00 61.45           C  
ANISOU   57  CA  VAL A  24     5192   8850   9305    621   -795   -835       C  
ATOM     58  C   VAL A  24     160.620  33.495 520.126  1.00 58.31           C  
ANISOU   58  C   VAL A  24     4772   8387   8995    473   -589   -861       C  
ATOM     59  O   VAL A  24     161.007  33.977 521.198  1.00 76.73           O  
ANISOU   59  O   VAL A  24     7178  10653  11323    500   -394   -809       O  
ATOM     60  CB  VAL A  24     158.813  34.594 518.738  1.00 49.12           C  
ANISOU   60  CB  VAL A  24     3343   7386   7936    699   -912   -847       C  
ATOM     61  CG1 VAL A  24     158.195  35.266 519.965  1.00 50.80           C  
ANISOU   61  CG1 VAL A  24     3452   7563   8286    775   -709   -781       C  
ATOM     62  CG2 VAL A  24     158.535  35.401 517.485  1.00 47.74           C  
ANISOU   62  CG2 VAL A  24     3201   7281   7655    853  -1143   -815       C  
ATOM     63  N   PHE A  25     160.426  32.180 519.971  1.00 44.60           N  
ANISOU   63  N   PHE A  25     2945   6663   7340    318   -634   -943       N  
ATOM     64  CA  PHE A  25     160.651  31.269 521.092  1.00 48.98           C  
ANISOU   64  CA  PHE A  25     3481   7147   7984    181   -440   -952       C  
ATOM     65  C   PHE A  25     162.102  31.315 521.557  1.00 54.28           C  
ANISOU   65  C   PHE A  25     4416   7731   8477    164   -309   -915       C  
ATOM     66  O   PHE A  25     162.377  31.312 522.763  1.00 57.51           O  
ANISOU   66  O   PHE A  25     4857   8083   8909    143   -112   -873       O  
ATOM     67  CB  PHE A  25     160.253  29.843 520.703  1.00 41.84           C  
ANISOU   67  CB  PHE A  25     2503   6232   7163     13   -522  -1026       C  
ATOM     68  CG  PHE A  25     160.421  28.833 521.813  1.00 56.46           C  
ANISOU   68  CG  PHE A  25     4371   7989   9091   -126   -324  -1006       C  
ATOM     69  CD1 PHE A  25     159.466  28.709 522.812  1.00 70.30           C  
ANISOU   69  CD1 PHE A  25     6003   9732  10977   -155   -175   -935       C  
ATOM     70  CD2 PHE A  25     161.526  27.997 521.847  1.00 50.33           C  
ANISOU   70  CD2 PHE A  25     3733   7141   8248   -218   -287  -1053       C  
ATOM     71  CE1 PHE A  25     159.617  27.777 523.829  1.00 65.61           C  
ANISOU   71  CE1 PHE A  25     5438   9054  10437   -273      4   -903       C  
ATOM     72  CE2 PHE A  25     161.682  27.064 522.859  1.00 48.58           C  
ANISOU   72  CE2 PHE A  25     3538   6827   8095   -331   -113  -1021       C  
ATOM     73  CZ  PHE A  25     160.727  26.954 523.850  1.00 58.04           C  
ANISOU   73  CZ  PHE A  25     4626   8013   9415   -359     30   -942       C  
ATOM     74  N   ILE A  26     163.042  31.379 520.615  1.00 49.25           N  
ANISOU   74  N   ILE A  26     3965   7090   7656    178   -415   -929       N  
ATOM     75  CA  ILE A  26     164.457  31.420 520.967  1.00 39.08           C  
ANISOU   75  CA  ILE A  26     2902   5732   6213    160   -304   -896       C  
ATOM     76  C   ILE A  26     164.808  32.746 521.630  1.00 47.37           C  
ANISOU   76  C   ILE A  26     4043   6753   7204    270   -195   -812       C  
ATOM     77  O   ILE A  26     165.606  32.788 522.574  1.00 62.00           O  
ANISOU   77  O   ILE A  26     6001   8544   9011    243    -47   -782       O  
ATOM     78  CB  ILE A  26     165.323  31.151 519.722  1.00 44.66           C  
ANISOU   78  CB  ILE A  26     3765   6455   6748    152   -434   -933       C  
ATOM     79  CG1 ILE A  26     165.235  29.676 519.328  1.00 56.47           C  
ANISOU   79  CG1 ILE A  26     5219   7941   8295     26   -499  -1033       C  
ATOM     80  CG2 ILE A  26     166.775  31.545 519.964  1.00 34.66           C  
ANISOU   80  CG2 ILE A  26     2710   5136   5323    166   -328   -879       C  
ATOM     81  CD1 ILE A  26     165.651  28.727 520.428  1.00 51.14           C  
ANISOU   81  CD1 ILE A  26     4554   7180   7698    -83   -334  -1034       C  
ATOM     82  N   VAL A  27     164.222  33.851 521.156  1.00 47.90           N  
ANISOU   82  N   VAL A  27     4075   6856   7270    399   -275   -776       N  
ATOM     83  CA  VAL A  27     164.484  35.143 521.788  1.00 46.36           C  
ANISOU   83  CA  VAL A  27     3972   6607   7036    505   -173   -707       C  
ATOM     84  C   VAL A  27     163.962  35.147 523.222  1.00 51.88           C  
ANISOU   84  C   VAL A  27     4575   7278   7859    502      5   -703       C  
ATOM     85  O   VAL A  27     164.637  35.624 524.143  1.00 52.68           O  
ANISOU   85  O   VAL A  27     4803   7313   7902    512    142   -678       O  
ATOM     86  CB  VAL A  27     163.876  36.291 520.955  1.00 42.81           C  
ANISOU   86  CB  VAL A  27     3505   6187   6573    658   -299   -662       C  
ATOM     87  CG1 VAL A  27     163.841  37.577 521.762  1.00 31.61           C  
ANISOU   87  CG1 VAL A  27     2145   4694   5171    774   -181   -605       C  
ATOM     88  CG2 VAL A  27     164.675  36.517 519.678  1.00 42.17           C  
ANISOU   88  CG2 VAL A  27     3590   6117   6314    675   -429   -637       C  
ATOM     89  N   LEU A  28     162.767  34.590 523.438  1.00 49.67           N  
ANISOU   89  N   LEU A  28     4070   7052   7750    483      7   -732       N  
ATOM     90  CA  LEU A  28     162.188  34.579 524.778  1.00 43.06           C  
ANISOU   90  CA  LEU A  28     3132   6200   7028    487    198   -720       C  
ATOM     91  C   LEU A  28     162.967  33.664 525.719  1.00 37.65           C  
ANISOU   91  C   LEU A  28     2542   5465   6300    360    343   -723       C  
ATOM     92  O   LEU A  28     163.234  34.031 526.870  1.00 44.81           O  
ANISOU   92  O   LEU A  28     3527   6330   7171    388    509   -698       O  
ATOM     93  CB  LEU A  28     160.719  34.159 524.709  1.00 40.11           C  
ANISOU   93  CB  LEU A  28     2470   5905   6865    485    171   -742       C  
ATOM     94  CG  LEU A  28     159.773  35.084 523.939  1.00 40.55           C  
ANISOU   94  CG  LEU A  28     2394   6025   6989    637     32   -730       C  
ATOM     95  CD1 LEU A  28     158.352  34.545 523.979  1.00 38.25           C  
ANISOU   95  CD1 LEU A  28     1894   5799   6841    594     16   -708       C  
ATOM     96  CD2 LEU A  28     159.833  36.500 524.494  1.00 41.01           C  
ANISOU   96  CD2 LEU A  28     2547   6032   7003    809    131   -682       C  
ATOM     97  N   VAL A  29     163.341  32.471 525.251  1.00 30.50           N  
ANISOU   97  N   VAL A  29     1643   4558   5390    230    278   -757       N  
ATOM     98  CA  VAL A  29     164.092  31.552 526.102  1.00 44.77           C  
ANISOU   98  CA  VAL A  29     3543   6308   7159    123    405   -749       C  
ATOM     99  C   VAL A  29     165.473  32.116 526.417  1.00 60.00           C  
ANISOU   99  C   VAL A  29     5707   8188   8903    154    445   -723       C  
ATOM    100  O   VAL A  29     165.928  32.075 527.568  1.00 71.45           O  
ANISOU  100  O   VAL A  29     7240   9601  10308    142    588   -695       O  
ATOM    101  CB  VAL A  29     164.181  30.163 525.442  1.00 37.58           C  
ANISOU  101  CB  VAL A  29     2595   5388   6295    -11    318   -798       C  
ATOM    102  CG1 VAL A  29     165.182  29.289 526.181  1.00 38.86           C  
ANISOU  102  CG1 VAL A  29     2895   5478   6390    -95    428   -778       C  
ATOM    103  CG2 VAL A  29     162.812  29.499 525.419  1.00 36.88           C  
ANISOU  103  CG2 VAL A  29     2259   5332   6420    -76    308   -824       C  
ATOM    104  N   ALA A  30     166.156  32.663 525.409  1.00 45.51           N  
ANISOU  104  N   ALA A  30     3979   6355   6957    192    317   -729       N  
ATOM    105  CA  ALA A  30     167.496  33.201 525.622  1.00 40.20           C  
ANISOU  105  CA  ALA A  30     3505   5638   6130    205    347   -704       C  
ATOM    106  C   ALA A  30     167.466  34.401 526.563  1.00 48.08           C  
ANISOU  106  C   ALA A  30     4562   6602   7105    291    448   -675       C  
ATOM    107  O   ALA A  30     168.268  34.489 527.503  1.00 56.40           O  
ANISOU  107  O   ALA A  30     5730   7615   8083    270    542   -666       O  
ATOM    108  CB  ALA A  30     168.124  33.577 524.279  1.00 38.16           C  
ANISOU  108  CB  ALA A  30     3334   5395   5772    227    206   -704       C  
ATOM    109  N   GLY A  31     166.543  35.336 526.327  1.00 33.26           N  
ANISOU  109  N   GLY A  31     2610   4737   5291    397    422   -668       N  
ATOM    110  CA  GLY A  31     166.419  36.475 527.222  1.00 29.58           C  
ANISOU  110  CA  GLY A  31     2203   4221   4813    493    524   -656       C  
ATOM    111  C   GLY A  31     166.051  36.067 528.635  1.00 31.81           C  
ANISOU  111  C   GLY A  31     2448   4504   5133    476    696   -665       C  
ATOM    112  O   GLY A  31     166.529  36.658 529.609  1.00 40.54           O  
ANISOU  112  O   GLY A  31     3682   5562   6160    507    794   -670       O  
ATOM    113  N   SER A  32     165.202  35.045 528.767  1.00 31.91           N  
ANISOU  113  N   SER A  32     2292   4570   5264    423    735   -667       N  
ATOM    114  CA  SER A  32     164.846  34.542 530.090  1.00 39.58           C  
ANISOU  114  CA  SER A  32     3229   5544   6264    399    917   -657       C  
ATOM    115  C   SER A  32     166.067  33.978 530.807  1.00 53.25           C  
ANISOU  115  C   SER A  32     5135   7239   7860    318    970   -646       C  
ATOM    116  O   SER A  32     166.302  34.273 531.985  1.00 72.65           O  
ANISOU  116  O   SER A  32     7691   9676  10236    349   1099   -640       O  
ATOM    117  CB  SER A  32     163.753  33.480 529.968  1.00 36.28           C  
ANISOU  117  CB  SER A  32     2588   5179   6018    330    943   -650       C  
ATOM    118  OG  SER A  32     162.634  33.980 529.257  1.00 48.41           O  
ANISOU  118  OG  SER A  32     3939   6766   7689    407    868   -663       O  
ATOM    119  N   LEU A  33     166.862  33.165 530.104  1.00 37.79           N  
ANISOU  119  N   LEU A  33     3218   5274   5866    224    867   -646       N  
ATOM    120  CA  LEU A  33     168.065  32.602 530.709  1.00 38.88           C  
ANISOU  120  CA  LEU A  33     3506   5381   5885    162    900   -631       C  
ATOM    121  C   LEU A  33     169.041  33.696 531.122  1.00 38.68           C  
ANISOU  121  C   LEU A  33     3652   5326   5720    214    893   -641       C  
ATOM    122  O   LEU A  33     169.621  33.643 532.215  1.00 45.21           O  
ANISOU  122  O   LEU A  33     4588   6139   6452    209    973   -633       O  
ATOM    123  CB  LEU A  33     168.730  31.626 529.739  1.00 43.74           C  
ANISOU  123  CB  LEU A  33     4127   5993   6498     76    786   -639       C  
ATOM    124  CG  LEU A  33     167.953  30.342 529.445  1.00 57.25           C  
ANISOU  124  CG  LEU A  33     5699   7708   8344     -6    789   -641       C  
ATOM    125  CD1 LEU A  33     168.478  29.671 528.187  1.00 60.20           C  
ANISOU  125  CD1 LEU A  33     6084   8076   8712    -61    645   -678       C  
ATOM    126  CD2 LEU A  33     168.024  29.393 530.632  1.00 44.84           C  
ANISOU  126  CD2 LEU A  33     4154   6105   6778    -61    932   -595       C  
ATOM    127  N   SER A  34     169.232  34.700 530.262  1.00 33.75           N  
ANISOU  127  N   SER A  34     3058   4686   5080    262    793   -657       N  
ATOM    128  CA  SER A  34     170.115  35.811 530.604  1.00 29.87           C  
ANISOU  128  CA  SER A  34     2722   4145   4482    297    783   -671       C  
ATOM    129  C   SER A  34     169.627  36.533 531.854  1.00 36.07           C  
ANISOU  129  C   SER A  34     3554   4905   5246    373    907   -693       C  
ATOM    130  O   SER A  34     170.409  36.812 532.772  1.00 48.28           O  
ANISOU  130  O   SER A  34     5236   6424   6682    363    943   -714       O  
ATOM    131  CB  SER A  34     170.216  36.780 529.426  1.00 41.84           C  
ANISOU  131  CB  SER A  34     4256   5634   6007    338    672   -667       C  
ATOM    132  OG  SER A  34     170.983  37.921 529.767  1.00 53.48           O  
ANISOU  132  OG  SER A  34     5876   7039   7405    360    671   -679       O  
ATOM    133  N   LEU A  35     168.326  36.831 531.913  1.00 38.78           N  
ANISOU  133  N   LEU A  35     3780   5263   5690    455    970   -696       N  
ATOM    134  CA  LEU A  35     167.783  37.544 533.064  1.00 40.96           C  
ANISOU  134  CA  LEU A  35     4099   5518   5944    548   1107   -725       C  
ATOM    135  C   LEU A  35     167.943  36.735 534.346  1.00 46.32           C  
ANISOU  135  C   LEU A  35     4826   6228   6545    507   1238   -717       C  
ATOM    136  O   LEU A  35     168.305  37.284 535.395  1.00 53.98           O  
ANISOU  136  O   LEU A  35     5941   7171   7397    549   1310   -753       O  
ATOM    137  CB  LEU A  35     166.313  37.884 532.821  1.00 45.39           C  
ANISOU  137  CB  LEU A  35     4490   6106   6651    651   1158   -722       C  
ATOM    138  CG  LEU A  35     165.639  38.752 533.883  1.00 63.73           C  
ANISOU  138  CG  LEU A  35     6846   8404   8964    780   1311   -759       C  
ATOM    139  CD1 LEU A  35     166.360  40.084 534.019  1.00 56.34           C  
ANISOU  139  CD1 LEU A  35     6111   7365   7932    843   1267   -810       C  
ATOM    140  CD2 LEU A  35     164.172  38.962 533.543  1.00 78.36           C  
ANISOU  140  CD2 LEU A  35     8486  10300  10988    885   1358   -747       C  
ATOM    141  N   VAL A  36     167.686  35.425 534.281  1.00 51.24           N  
ANISOU  141  N   VAL A  36     5342   6901   7227    426   1266   -670       N  
ATOM    142  CA  VAL A  36     167.840  34.577 535.461  1.00 44.87           C  
ANISOU  142  CA  VAL A  36     4590   6116   6342    389   1394   -637       C  
ATOM    143  C   VAL A  36     169.293  34.559 535.921  1.00 36.99           C  
ANISOU  143  C   VAL A  36     3784   5096   5175    348   1330   -647       C  
ATOM    144  O   VAL A  36     169.581  34.659 537.121  1.00 33.61           O  
ANISOU  144  O   VAL A  36     3484   4673   4615    378   1416   -653       O  
ATOM    145  CB  VAL A  36     167.319  33.157 535.171  1.00 43.04           C  
ANISOU  145  CB  VAL A  36     4210   5914   6229    297   1425   -578       C  
ATOM    146  CG1 VAL A  36     167.689  32.211 536.303  1.00 37.46           C  
ANISOU  146  CG1 VAL A  36     3593   5212   5429    252   1541   -522       C  
ATOM    147  CG2 VAL A  36     165.813  33.180 534.969  1.00 48.08           C  
ANISOU  147  CG2 VAL A  36     4638   6587   7042    333   1507   -571       C  
ATOM    148  N   THR A  37     170.230  34.437 534.976  1.00 37.85           N  
ANISOU  148  N   THR A  37     3913   5188   5281    286   1176   -650       N  
ATOM    149  CA  THR A  37     171.649  34.460 535.324  1.00 24.87           C  
ANISOU  149  CA  THR A  37     2417   3532   3501    247   1102   -659       C  
ATOM    150  C   THR A  37     172.019  35.761 536.028  1.00 41.80           C  
ANISOU  150  C   THR A  37     4703   5641   5539    305   1103   -724       C  
ATOM    151  O   THR A  37     172.631  35.750 537.106  1.00 57.27           O  
ANISOU  151  O   THR A  37     6789   7610   7362    307   1126   -740       O  
ATOM    152  CB  THR A  37     172.498  34.272 534.065  1.00 23.62           C  
ANISOU  152  CB  THR A  37     2232   3365   3376    184    955   -654       C  
ATOM    153  OG1 THR A  37     172.193  33.009 533.460  1.00 27.60           O  
ANISOU  153  OG1 THR A  37     2629   3891   3968    131    950   -613       O  
ATOM    154  CG2 THR A  37     173.979  34.321 534.405  1.00 23.04           C  
ANISOU  154  CG2 THR A  37     2279   3290   3186    144    880   -662       C  
ATOM    155  N   ILE A  38     171.639  36.895 535.432  1.00 35.93           N  
ANISOU  155  N   ILE A  38     3947   4850   4854    356   1070   -764       N  
ATOM    156  CA  ILE A  38     171.979  38.198 536.000  1.00 34.81           C  
ANISOU  156  CA  ILE A  38     3949   4644   4633    406   1063   -837       C  
ATOM    157  C   ILE A  38     171.403  38.338 537.404  1.00 48.84           C  
ANISOU  157  C   ILE A  38     5803   6434   6319    484   1209   -874       C  
ATOM    158  O   ILE A  38     172.109  38.714 538.349  1.00 60.07           O  
ANISOU  158  O   ILE A  38     7384   7842   7598    484   1200   -929       O  
ATOM    159  CB  ILE A  38     171.491  39.328 535.075  1.00 34.18           C  
ANISOU  159  CB  ILE A  38     3839   4494   4653    464   1020   -856       C  
ATOM    160  CG1 ILE A  38     172.198  39.256 533.720  1.00 36.46           C  
ANISOU  160  CG1 ILE A  38     4087   4774   4993    389    883   -815       C  
ATOM    161  CG2 ILE A  38     171.716  40.684 535.720  1.00 27.56           C  
ANISOU  161  CG2 ILE A  38     3159   3560   3750    522   1030   -939       C  
ATOM    162  CD1 ILE A  38     171.718  40.291 532.727  1.00 33.29           C  
ANISOU  162  CD1 ILE A  38     3664   4306   4678    452    835   -809       C  
ATOM    163  N   ILE A  39     170.114  38.028 537.564  1.00 28.54           N  
ANISOU  163  N   ILE A  39     3117   3899   3827    550   1344   -846       N  
ATOM    164  CA  ILE A  39     169.463  38.202 538.862  1.00 49.32           C  
ANISOU  164  CA  ILE A  39     5816   6551   6372    639   1515   -875       C  
ATOM    165  C   ILE A  39     170.117  37.312 539.912  1.00 39.32           C  
ANISOU  165  C   ILE A  39     4657   5339   4945    591   1554   -845       C  
ATOM    166  O   ILE A  39     170.415  37.754 541.029  1.00 46.84           O  
ANISOU  166  O   ILE A  39     5779   6290   5728    640   1602   -903       O  
ATOM    167  CB  ILE A  39     167.953  37.926 538.748  1.00 43.63           C  
ANISOU  167  CB  ILE A  39     4910   5873   5796    707   1663   -834       C  
ATOM    168  CG1 ILE A  39     167.280  38.994 537.883  1.00 38.94           C  
ANISOU  168  CG1 ILE A  39     4234   5225   5337    794   1622   -870       C  
ATOM    169  CG2 ILE A  39     167.315  37.879 540.126  1.00 39.74           C  
ANISOU  169  CG2 ILE A  39     4477   5420   5203    790   1874   -843       C  
ATOM    170  CD1 ILE A  39     165.801  38.763 537.674  1.00 32.72           C  
ANISOU  170  CD1 ILE A  39     3226   4489   4715    864   1741   -832       C  
ATOM    171  N   GLY A  40     170.362  36.047 539.566  1.00 29.36           N  
ANISOU  171  N   GLY A  40     3310   4121   3725    501   1527   -757       N  
ATOM    172  CA  GLY A  40     170.954  35.132 540.531  1.00 38.20           C  
ANISOU  172  CA  GLY A  40     4530   5285   4699    469   1563   -707       C  
ATOM    173  C   GLY A  40     172.337  35.564 540.977  1.00 42.31           C  
ANISOU  173  C   GLY A  40     5227   5796   5054    447   1424   -764       C  
ATOM    174  O   GLY A  40     172.618  35.663 542.177  1.00 43.68           O  
ANISOU  174  O   GLY A  40     5557   5996   5043    490   1469   -788       O  
ATOM    175  N   ASN A  41     173.222  35.841 540.014  1.00 42.26           N  
ANISOU  175  N   ASN A  41     5194   5755   5107    381   1253   -787       N  
ATOM    176  CA  ASN A  41     174.593  36.192 540.375  1.00 34.27           C  
ANISOU  176  CA  ASN A  41     4312   4740   3969    341   1110   -836       C  
ATOM    177  C   ASN A  41     174.657  37.534 541.097  1.00 34.14           C  
ANISOU  177  C   ASN A  41     4447   4677   3848    395   1105   -955       C  
ATOM    178  O   ASN A  41     175.475  37.713 542.009  1.00 34.15           O  
ANISOU  178  O   ASN A  41     4592   4697   3685    390   1040  -1007       O  
ATOM    179  CB  ASN A  41     175.477  36.196 539.131  1.00 26.93           C  
ANISOU  179  CB  ASN A  41     3300   3787   3145    255    956   -825       C  
ATOM    180  CG  ASN A  41     175.701  34.804 538.582  1.00 36.75           C  
ANISOU  180  CG  ASN A  41     4438   5073   4451    205    941   -728       C  
ATOM    181  OD1 ASN A  41     176.529  34.051 539.093  1.00 50.09           O  
ANISOU  181  OD1 ASN A  41     6173   6804   6054    184    897   -691       O  
ATOM    182  ND2 ASN A  41     174.957  34.450 537.542  1.00 42.80           N  
ANISOU  182  ND2 ASN A  41     5067   5826   5368    193    971   -692       N  
ATOM    183  N   ILE A  42     173.801  38.485 540.714  1.00 33.78           N  
ANISOU  183  N   ILE A  42     4376   4566   3894    454   1164  -1006       N  
ATOM    184  CA  ILE A  42     173.751  39.757 541.429  1.00 30.91           C  
ANISOU  184  CA  ILE A  42     4170   4135   3439    520   1178  -1129       C  
ATOM    185  C   ILE A  42     173.303  39.538 542.869  1.00 69.01           C  
ANISOU  185  C   ILE A  42     9121   9018   8082    606   1318  -1155       C  
ATOM    186  O   ILE A  42     173.865  40.121 543.806  1.00 71.29           O  
ANISOU  186  O   ILE A  42     9595   9293   8199    625   1274  -1256       O  
ATOM    187  CB  ILE A  42     172.839  40.756 540.693  1.00 31.14           C  
ANISOU  187  CB  ILE A  42     4140   4075   3618    589   1225  -1163       C  
ATOM    188  CG1 ILE A  42     173.538  41.295 539.445  1.00 35.13           C  
ANISOU  188  CG1 ILE A  42     4599   4505   4245    506   1069  -1157       C  
ATOM    189  CG2 ILE A  42     172.443  41.901 541.611  1.00 44.03           C  
ANISOU  189  CG2 ILE A  42     5936   5635   5156    696   1302  -1288       C  
ATOM    190  CD1 ILE A  42     172.764  42.384 538.737  1.00 40.90           C  
ANISOU  190  CD1 ILE A  42     5303   5131   5105    583   1093  -1183       C  
ATOM    191  N   LEU A  43     172.292  38.687 543.070  1.00 56.10           N  
ANISOU  191  N   LEU A  43     7390   7448   6477    655   1489  -1065       N  
ATOM    192  CA  LEU A  43     171.859  38.366 544.427  1.00 40.68           C  
ANISOU  192  CA  LEU A  43     5556   5561   4341    736   1649  -1063       C  
ATOM    193  C   LEU A  43     172.992  37.750 545.239  1.00 47.51           C  
ANISOU  193  C   LEU A  43     6564   6487   5003    689   1551  -1046       C  
ATOM    194  O   LEU A  43     173.173  38.083 546.418  1.00 52.13           O  
ANISOU  194  O   LEU A  43     7342   7098   5365    753   1582  -1116       O  
ATOM    195  CB  LEU A  43     170.654  37.427 544.387  1.00 35.27           C  
ANISOU  195  CB  LEU A  43     4712   4934   3756    765   1849   -943       C  
ATOM    196  CG  LEU A  43     169.311  38.062 544.026  1.00 41.86           C  
ANISOU  196  CG  LEU A  43     5419   5739   4746    857   1995   -968       C  
ATOM    197  CD1 LEU A  43     168.216  37.009 543.960  1.00 45.11           C  
ANISOU  197  CD1 LEU A  43     5643   6218   5281    853   2174   -842       C  
ATOM    198  CD2 LEU A  43     168.956  39.147 545.028  1.00 46.96           C  
ANISOU  198  CD2 LEU A  43     6237   6361   5245    992   2107  -1089       C  
ATOM    199  N   VAL A  44     173.771  36.855 544.626  1.00 46.96           N  
ANISOU  199  N   VAL A  44     6404   6441   4996    589   1425   -958       N  
ATOM    200  CA  VAL A  44     174.887  36.235 545.339  1.00 40.37           C  
ANISOU  200  CA  VAL A  44     5685   5667   3985    557   1314   -930       C  
ATOM    201  C   VAL A  44     175.918  37.286 545.736  1.00 37.09           C  
ANISOU  201  C   VAL A  44     5420   5226   3445    540   1137  -1074       C  
ATOM    202  O   VAL A  44     176.325  37.375 546.902  1.00 35.88           O  
ANISOU  202  O   VAL A  44     5448   5122   3063    584   1111  -1124       O  
ATOM    203  CB  VAL A  44     175.518  35.119 544.487  1.00 34.55           C  
ANISOU  203  CB  VAL A  44     4808   4948   3371    466   1217   -816       C  
ATOM    204  CG1 VAL A  44     176.773  34.586 545.160  1.00 32.36           C  
ANISOU  204  CG1 VAL A  44     4636   4731   2927    447   1075   -792       C  
ATOM    205  CG2 VAL A  44     174.517  33.997 544.258  1.00 32.70           C  
ANISOU  205  CG2 VAL A  44     4451   4730   3246    471   1387   -683       C  
ATOM    206  N   MET A  45     176.351  38.103 544.771  1.00 39.33           N  
ANISOU  206  N   MET A  45     5637   5431   3878    472   1011  -1142       N  
ATOM    207  CA  MET A  45     177.397  39.088 545.040  1.00 39.89           C  
ANISOU  207  CA  MET A  45     5826   5459   3872    425    832  -1275       C  
ATOM    208  C   MET A  45     176.960  40.088 546.105  1.00 48.85           C  
ANISOU  208  C   MET A  45     7163   6556   4842    514    895  -1418       C  
ATOM    209  O   MET A  45     177.687  40.338 547.075  1.00 51.76           O  
ANISOU  209  O   MET A  45     7698   6956   5012    514    790  -1509       O  
ATOM    210  CB  MET A  45     177.775  39.813 543.748  1.00 33.28           C  
ANISOU  210  CB  MET A  45     4875   4525   3243    336    727  -1302       C  
ATOM    211  CG  MET A  45     178.401  38.920 542.692  1.00 32.95           C  
ANISOU  211  CG  MET A  45     4658   4524   3339    247    647  -1185       C  
ATOM    212  SD  MET A  45     178.528  39.744 541.095  0.57 30.48           S  
ANISOU  212  SD  MET A  45     4218   4103   3258    170    587  -1189       S  
ATOM    213  CE  MET A  45     179.389  41.245 541.559  1.00 30.92           C  
ANISOU  213  CE  MET A  45     4426   4061   3262    112    450  -1349       C  
ATOM    214  N   VAL A  46     175.771  40.674 545.936  1.00 50.98           N  
ANISOU  214  N   VAL A  46     7421   6761   5188    600   1062  -1447       N  
ATOM    215  CA  VAL A  46     175.279  41.645 546.910  1.00 53.10           C  
ANISOU  215  CA  VAL A  46     7885   6983   5309    706   1146  -1592       C  
ATOM    216  C   VAL A  46     175.134  40.997 548.280  1.00 55.48           C  
ANISOU  216  C   VAL A  46     8336   7402   5341    789   1244  -1579       C  
ATOM    217  O   VAL A  46     175.483  41.596 549.306  1.00 46.22           O  
ANISOU  217  O   VAL A  46     7383   6228   3950    833   1198  -1716       O  
ATOM    218  CB  VAL A  46     173.954  42.264 546.427  1.00 50.07           C  
ANISOU  218  CB  VAL A  46     7427   6519   5077    805   1327  -1603       C  
ATOM    219  CG1 VAL A  46     173.371  43.178 547.494  1.00 53.08           C  
ANISOU  219  CG1 VAL A  46     8014   6858   5298    942   1448  -1752       C  
ATOM    220  CG2 VAL A  46     174.171  43.031 545.133  1.00 37.48           C  
ANISOU  220  CG2 VAL A  46     5727   4799   3714    735   1213  -1619       C  
ATOM    221  N   SER A  47     174.635  39.758 548.320  1.00 58.46           N  
ANISOU  221  N   SER A  47     8611   7878   5725    808   1376  -1413       N  
ATOM    222  CA  SER A  47     174.504  39.056 549.593  1.00 48.92           C  
ANISOU  222  CA  SER A  47     7550   6781   4258    886   1483  -1366       C  
ATOM    223  C   SER A  47     175.854  38.893 550.279  1.00 52.00           C  
ANISOU  223  C   SER A  47     8092   7229   4438    839   1261  -1408       C  
ATOM    224  O   SER A  47     175.961  39.051 551.501  1.00 57.24           O  
ANISOU  224  O   SER A  47     8976   7950   4821    919   1277  -1478       O  
ATOM    225  CB  SER A  47     173.846  37.695 549.377  1.00 40.70           C  
ANISOU  225  CB  SER A  47     6354   5808   3300    885   1645  -1163       C  
ATOM    226  OG  SER A  47     172.484  37.849 549.028  1.00 48.16           O  
ANISOU  226  OG  SER A  47     7175   6725   4399    947   1870  -1135       O  
ATOM    227  N   ILE A  48     176.899  38.579 549.510  1.00 56.04           N  
ANISOU  227  N   ILE A  48     8485   7736   5074    717   1049  -1369       N  
ATOM    228  CA  ILE A  48     178.222  38.425 550.105  1.00 52.68           C  
ANISOU  228  CA  ILE A  48     8165   7374   4476    672    819  -1407       C  
ATOM    229  C   ILE A  48     178.770  39.770 550.570  1.00 56.27           C  
ANISOU  229  C   ILE A  48     8784   7768   4827    655    667  -1627       C  
ATOM    230  O   ILE A  48     179.472  39.843 551.587  1.00 66.69           O  
ANISOU  230  O   ILE A  48    10281   9156   5902    674    534  -1706       O  
ATOM    231  CB  ILE A  48     179.170  37.732 549.109  1.00 42.03           C  
ANISOU  231  CB  ILE A  48     6620   6038   3313    555    653  -1305       C  
ATOM    232  CG1 ILE A  48     178.675  36.316 548.810  1.00 43.83           C  
ANISOU  232  CG1 ILE A  48     6724   6317   3612    577    794  -1100       C  
ATOM    233  CG2 ILE A  48     180.592  37.690 549.648  1.00 40.15           C  
ANISOU  233  CG2 ILE A  48     6455   5868   2932    507    394  -1355       C  
ATOM    234  CD1 ILE A  48     179.493  35.587 547.772  1.00 50.53           C  
ANISOU  234  CD1 ILE A  48     7383   7168   4648    482    661  -1005       C  
ATOM    235  N   LYS A  49     178.450  40.854 549.861  1.00 51.15           N  
ANISOU  235  N   LYS A  49     8093   6985   4357    623    680  -1732       N  
ATOM    236  CA  LYS A  49     179.024  42.150 550.212  1.00 47.24           C  
ANISOU  236  CA  LYS A  49     7753   6398   3799    586    526  -1945       C  
ATOM    237  C   LYS A  49     178.314  42.817 551.386  1.00 55.44           C  
ANISOU  237  C   LYS A  49     9043   7421   4599    723    651  -2091       C  
ATOM    238  O   LYS A  49     178.945  43.586 552.120  1.00 55.81           O  
ANISOU  238  O   LYS A  49     9283   7440   4484    708    498  -2273       O  
ATOM    239  CB  LYS A  49     179.011  43.081 548.999  1.00 51.44           C  
ANISOU  239  CB  LYS A  49     8162   6769   4614    500    489  -1992       C  
ATOM    240  CG  LYS A  49     180.167  42.852 548.041  1.00 61.07           C  
ANISOU  240  CG  LYS A  49     9204   7988   6012    337    289  -1930       C  
ATOM    241  CD  LYS A  49     181.500  42.970 548.766  1.00 65.52           C  
ANISOU  241  CD  LYS A  49     9860   8607   6429    254     39  -2030       C  
ATOM    242  CE  LYS A  49     182.666  42.645 547.847  1.00 75.93           C  
ANISOU  242  CE  LYS A  49    10973   9947   7930    102   -140  -1954       C  
ATOM    243  NZ  LYS A  49     183.963  42.635 548.580  1.00 88.21           N  
ANISOU  243  NZ  LYS A  49    12581  11583   9353     27   -390  -2037       N  
ATOM    244  N   VAL A  50     177.021  42.552 551.586  1.00 65.48           N  
ANISOU  244  N   VAL A  50    10317   8713   5849    857    927  -2023       N  
ATOM    245  CA  VAL A  50     176.260  43.248 552.620  1.00 65.08           C  
ANISOU  245  CA  VAL A  50    10441   8648   5638    976   1068  -2138       C  
ATOM    246  C   VAL A  50     176.179  42.468 553.923  1.00 67.61           C  
ANISOU  246  C   VAL A  50    10870   9129   5691   1038   1132  -2064       C  
ATOM    247  O   VAL A  50     175.640  42.989 554.909  1.00 70.03           O  
ANISOU  247  O   VAL A  50    11294   9447   5867   1112   1227  -2141       O  
ATOM    248  CB  VAL A  50     174.840  43.598 552.132  1.00 61.07           C  
ANISOU  248  CB  VAL A  50     9808   8070   5324   1067   1321  -2099       C  
ATOM    249  CG1 VAL A  50     174.903  44.356 550.815  1.00 64.09           C  
ANISOU  249  CG1 VAL A  50    10095   8287   5967   1016   1260  -2153       C  
ATOM    250  CG2 VAL A  50     173.991  42.342 552.007  1.00 51.73           C  
ANISOU  250  CG2 VAL A  50     8472   7002   4181   1117   1535  -1884       C  
ATOM    251  N   ASN A  51     176.701  41.244 553.967  1.00 68.35           N  
ANISOU  251  N   ASN A  51    10934   9342   5693   1017   1083  -1913       N  
ATOM    252  CA  ASN A  51     176.627  40.404 555.158  1.00 69.09           C  
ANISOU  252  CA  ASN A  51    11134   9579   5538   1080   1148  -1809       C  
ATOM    253  C   ASN A  51     178.027  39.935 555.528  1.00 72.50           C  
ANISOU  253  C   ASN A  51    11654  10098   5796   1022    871  -1809       C  
ATOM    254  O   ASN A  51     178.693  39.275 554.725  1.00 64.36           O  
ANISOU  254  O   ASN A  51    10515   9085   4853    969    754  -1727       O  
ATOM    255  CB  ASN A  51     175.701  39.205 554.930  1.00 63.78           C  
ANISOU  255  CB  ASN A  51    10326   8969   4940   1129   1399  -1578       C  
ATOM    256  CG  ASN A  51     175.476  38.393 556.192  1.00 66.60           C  
ANISOU  256  CG  ASN A  51    10801   9451   5052   1197   1502  -1457       C  
ATOM    257  OD1 ASN A  51     175.755  38.852 557.300  1.00 70.88           O  
ANISOU  257  OD1 ASN A  51    11531  10038   5364   1233   1432  -1557       O  
ATOM    258  ND2 ASN A  51     174.961  37.181 556.030  1.00 65.02           N  
ANISOU  258  ND2 ASN A  51    10496   9301   4907   1211   1670  -1238       N  
ATOM    259  N   ARG A  52     178.465  40.267 556.747  1.00 73.54           N  
ANISOU  259  N   ARG A  52    11971  10291   5682   1040    761  -1902       N  
ATOM    260  CA  ARG A  52     179.787  39.843 557.200  1.00 69.21           C  
ANISOU  260  CA  ARG A  52    11492   9838   4966    992    479  -1901       C  
ATOM    261  C   ARG A  52     179.847  38.341 557.445  1.00 65.42           C  
ANISOU  261  C   ARG A  52    10994   9487   4376   1051    537  -1660       C  
ATOM    262  O   ARG A  52     180.906  37.728 557.266  1.00 65.00           O  
ANISOU  262  O   ARG A  52    10905   9500   4291   1014    316  -1602       O  
ATOM    263  CB  ARG A  52     180.186  40.594 558.472  1.00 80.68           C  
ANISOU  263  CB  ARG A  52    13146  11326   6182    999    350  -2063       C  
ATOM    264  CG  ARG A  52     180.405  42.090 558.296  1.00 90.57           C  
ANISOU  264  CG  ARG A  52    14434  12442   7536    919    235  -2314       C  
ATOM    265  CD  ARG A  52     179.116  42.872 558.492  1.00 98.98           C  
ANISOU  265  CD  ARG A  52    15547  13417   8643   1003    501  -2389       C  
ATOM    266  NE  ARG A  52     179.373  44.235 558.945  1.00103.18           N  
ANISOU  266  NE  ARG A  52    16206  13854   9145    962    387  -2635       N  
ATOM    267  CZ  ARG A  52     179.515  44.579 560.221  1.00107.05           C  
ANISOU  267  CZ  ARG A  52    16888  14408   9379   1002    341  -2743       C  
ATOM    268  NH1 ARG A  52     179.427  43.657 561.171  1.00101.58           N  
ANISOU  268  NH1 ARG A  52    16286  13877   8431   1087    398  -2615       N  
ATOM    269  NH2 ARG A  52     179.748  45.842 560.550  1.00115.48           N  
ANISOU  269  NH2 ARG A  52    18064  15372  10442    956    239  -2976       N  
ATOM    270  N   HIS A  53     178.731  37.734 557.858  1.00 56.50           N  
ANISOU  270  N   HIS A  53     9877   8388   3202   1142    828  -1512       N  
ATOM    271  CA  HIS A  53     178.702  36.291 558.063  1.00 56.33           C  
ANISOU  271  CA  HIS A  53     9840   8459   3104   1190    911  -1266       C  
ATOM    272  C   HIS A  53     178.933  35.524 556.768  1.00 61.05           C  
ANISOU  272  C   HIS A  53    10245   9027   3922   1144    899  -1143       C  
ATOM    273  O   HIS A  53     179.343  34.359 556.814  1.00 52.84           O  
ANISOU  273  O   HIS A  53     9195   8056   2826   1168    869   -962       O  
ATOM    274  CB  HIS A  53     177.370  35.873 558.688  1.00 58.36           C  
ANISOU  274  CB  HIS A  53    10123   8733   3318   1272   1244  -1138       C  
ATOM    275  CG  HIS A  53     177.170  36.382 560.082  1.00 78.49           C  
ANISOU  275  CG  HIS A  53    12879  11342   5603   1340   1271  -1224       C  
ATOM    276  ND1 HIS A  53     177.630  35.709 561.193  1.00 83.37           N  
ANISOU  276  ND1 HIS A  53    13661  12073   5943   1395   1207  -1127       N  
ATOM    277  CD2 HIS A  53     176.559  37.498 560.545  1.00 83.40           C  
ANISOU  277  CD2 HIS A  53    13574  11925   6190   1371   1357  -1398       C  
ATOM    278  CE1 HIS A  53     177.312  36.388 562.281  1.00 87.58           C  
ANISOU  278  CE1 HIS A  53    14364  12641   6272   1453   1254  -1243       C  
ATOM    279  NE2 HIS A  53     176.662  37.478 561.915  1.00 87.70           N  
ANISOU  279  NE2 HIS A  53    14328  12565   6431   1440   1348  -1411       N  
ATOM    280  N   LEU A  54     178.679  36.150 555.618  1.00 60.38           N  
ANISOU  280  N   LEU A  54    10016   8838   4086   1086    922  -1236       N  
ATOM    281  CA  LEU A  54     178.947  35.557 554.315  1.00 63.52           C  
ANISOU  281  CA  LEU A  54    10133   9180   4821    972    867  -1118       C  
ATOM    282  C   LEU A  54     180.267  36.040 553.723  1.00 64.16           C  
ANISOU  282  C   LEU A  54    10121   9238   5018    854    545  -1226       C  
ATOM    283  O   LEU A  54     180.430  36.055 552.499  1.00 77.50           O  
ANISOU  283  O   LEU A  54    11587  10853   7007    751    503  -1203       O  
ATOM    284  CB  LEU A  54     177.797  35.852 553.352  1.00 72.73           C  
ANISOU  284  CB  LEU A  54    11124  10241   6270    946   1086  -1108       C  
ATOM    285  CG  LEU A  54     176.476  35.130 553.615  1.00 75.18           C  
ANISOU  285  CG  LEU A  54    11420  10569   6575   1026   1415   -956       C  
ATOM    286  CD1 LEU A  54     175.385  35.656 552.697  1.00 80.16           C  
ANISOU  286  CD1 LEU A  54    11873  11104   7481   1007   1588   -989       C  
ATOM    287  CD2 LEU A  54     176.651  33.630 553.438  1.00 73.19           C  
ANISOU  287  CD2 LEU A  54    11074  10356   6380   1000   1442   -725       C  
ATOM    288  N   GLN A  55     181.214  36.439 554.569  1.00 64.76           N  
ANISOU  288  N   GLN A  55    10362   9383   4860    865    316  -1344       N  
ATOM    289  CA  GLN A  55     182.518  36.938 554.132  1.00 66.57           C  
ANISOU  289  CA  GLN A  55    10498   9602   5192    745      2  -1455       C  
ATOM    290  C   GLN A  55     183.590  35.971 554.624  1.00 65.02           C  
ANISOU  290  C   GLN A  55    10310   9540   4857    767   -200  -1345       C  
ATOM    291  O   GLN A  55     184.272  36.222 555.620  1.00 63.92           O  
ANISOU  291  O   GLN A  55    10342   9489   4453    805   -394  -1441       O  
ATOM    292  CB  GLN A  55     182.757  38.364 554.638  1.00 66.30           C  
ANISOU  292  CB  GLN A  55    10628   9519   5042    718   -127  -1717       C  
ATOM    293  CG  GLN A  55     181.843  39.401 554.008  1.00 58.71           C  
ANISOU  293  CG  GLN A  55     9640   8404   4265    694     40  -1829       C  
ATOM    294  CD  GLN A  55     182.129  40.805 554.499  1.00 67.79           C  
ANISOU  294  CD  GLN A  55    10967   9477   5315    665    -94  -2094       C  
ATOM    295  OE1 GLN A  55     182.944  41.007 555.399  1.00 77.09           O  
ANISOU  295  OE1 GLN A  55    12269  10724   6299    644   -301  -2187       O  
ATOM    296  NE2 GLN A  55     181.458  41.787 553.908  1.00 71.51           N  
ANISOU  296  NE2 GLN A  55    11416   9792   5963    644     22  -2196       N  
ATOM    297  N   THR A  56     183.732  34.855 553.915  1.00 59.49           N  
ANISOU  297  N   THR A  56     9422   8848   4334    753   -163  -1148       N  
ATOM    298  CA  THR A  56     184.755  33.856 554.188  1.00 50.33           C  
ANISOU  298  CA  THR A  56     8228   7794   3099    784   -346  -1021       C  
ATOM    299  C   THR A  56     185.531  33.588 552.904  1.00 65.14           C  
ANISOU  299  C   THR A  56     9818   9631   5302    671   -464   -977       C  
ATOM    300  O   THR A  56     185.238  34.154 551.847  1.00 76.52           O  
ANISOU  300  O   THR A  56    11109  10968   6999    572   -397  -1035       O  
ATOM    301  CB  THR A  56     184.140  32.563 554.739  1.00 55.44           C  
ANISOU  301  CB  THR A  56     8969   8488   3606    911   -154   -795       C  
ATOM    302  OG1 THR A  56     183.175  32.056 553.809  1.00 62.19           O  
ANISOU  302  OG1 THR A  56     9674   9242   4714    880    102   -676       O  
ATOM    303  CG2 THR A  56     183.464  32.819 556.078  1.00 51.49           C  
ANISOU  303  CG2 THR A  56     8767   8049   2750   1031    -33   -831       C  
ATOM    304  N   VAL A  57     186.532  32.711 553.001  1.00 67.04           N  
ANISOU  304  N   VAL A  57     9987   9959   5524    701   -637   -867       N  
ATOM    305  CA  VAL A  57     187.351  32.384 551.835  1.00 69.40           C  
ANISOU  305  CA  VAL A  57    10017  10237   6116    614   -743   -822       C  
ATOM    306  C   VAL A  57     186.502  31.709 550.764  1.00 67.79           C  
ANISOU  306  C   VAL A  57     9678   9930   6150    599   -497   -691       C  
ATOM    307  O   VAL A  57     186.550  32.075 549.580  1.00 73.76           O  
ANISOU  307  O   VAL A  57    10249  10610   7167    495   -479   -732       O  
ATOM    308  CB  VAL A  57     188.543  31.503 552.252  1.00 67.50           C  
ANISOU  308  CB  VAL A  57     9734  10117   5795    682   -964   -721       C  
ATOM    309  CG1 VAL A  57     189.449  31.238 551.064  1.00 69.49           C  
ANISOU  309  CG1 VAL A  57     9700  10355   6347    601  -1067   -690       C  
ATOM    310  CG2 VAL A  57     189.316  32.160 553.385  1.00 67.68           C  
ANISOU  310  CG2 VAL A  57     9901  10256   5560    701  -1225   -858       C  
ATOM    311  N   ASN A  58     185.707  30.713 551.169  1.00 65.09           N  
ANISOU  311  N   ASN A  58     9433   9582   5716    699   -306   -529       N  
ATOM    312  CA  ASN A  58     184.814  30.039 550.232  1.00 68.97           C  
ANISOU  312  CA  ASN A  58     9807   9972   6428    677    -77   -415       C  
ATOM    313  C   ASN A  58     183.894  31.033 549.538  1.00 79.02           C  
ANISOU  313  C   ASN A  58    11026  11152   7846    594     62   -533       C  
ATOM    314  O   ASN A  58     183.680  30.947 548.324  1.00 97.38           O  
ANISOU  314  O   ASN A  58    13172  13402  10427    521    122   -519       O  
ATOM    315  CB  ASN A  58     183.993  28.973 550.960  1.00 70.61           C  
ANISOU  315  CB  ASN A  58    10155  10178   6496    783    121   -238       C  
ATOM    316  CG  ASN A  58     184.855  27.891 551.578  1.00 65.24           C  
ANISOU  316  CG  ASN A  58     9533   9569   5685    882     -5    -90       C  
ATOM    317  OD1 ASN A  58     185.930  27.572 551.072  1.00 76.28           O  
ANISOU  317  OD1 ASN A  58    10792  10992   7200    869   -191    -77       O  
ATOM    318  ND2 ASN A  58     184.384  27.318 552.680  1.00 60.94           N  
ANISOU  318  ND2 ASN A  58     9197   9060   4897    991    105     30       N  
ATOM    319  N   ASN A  59     183.350  31.993 550.288  1.00 72.24           N  
ANISOU  319  N   ASN A  59    10329  10300   6821    615    111   -655       N  
ATOM    320  CA  ASN A  59     182.464  32.983 549.691  1.00 65.11           C  
ANISOU  320  CA  ASN A  59     9385   9303   6052    559    240   -766       C  
ATOM    321  C   ASN A  59     183.221  34.023 548.874  1.00 67.55           C  
ANISOU  321  C   ASN A  59     9576   9568   6523    445     65   -911       C  
ATOM    322  O   ASN A  59     182.602  34.730 548.072  1.00 77.30           O  
ANISOU  322  O   ASN A  59    10736  10710   7926    391    156   -973       O  
ATOM    323  CB  ASN A  59     181.633  33.663 550.778  1.00 57.84           C  
ANISOU  323  CB  ASN A  59     8682   8394   4900    638    364   -852       C  
ATOM    324  CG  ASN A  59     180.703  32.696 551.485  1.00 55.46           C  
ANISOU  324  CG  ASN A  59     8482   8125   4465    741    595   -694       C  
ATOM    325  OD1 ASN A  59     180.254  31.711 550.900  1.00 47.68           O  
ANISOU  325  OD1 ASN A  59     7373   7105   3639    729    724   -539       O  
ATOM    326  ND2 ASN A  59     180.413  32.972 552.750  1.00 64.79           N  
ANISOU  326  ND2 ASN A  59     9896   9369   5351    838    652   -734       N  
ATOM    327  N   TYR A  60     184.537  34.139 549.060  1.00 58.74           N  
ANISOU  327  N   TYR A  60     8438   8516   5366    406   -183   -959       N  
ATOM    328  CA  TYR A  60     185.333  34.971 548.163  1.00 56.85           C  
ANISOU  328  CA  TYR A  60     8049   8231   5319    278   -333  -1063       C  
ATOM    329  C   TYR A  60     185.525  34.281 546.818  1.00 48.45           C  
ANISOU  329  C   TYR A  60     6756   7136   4515    228   -294   -949       C  
ATOM    330  O   TYR A  60     185.346  34.897 545.758  1.00 46.79           O  
ANISOU  330  O   TYR A  60     6432   6842   4503    144   -254   -992       O  
ATOM    331  CB  TYR A  60     186.682  35.298 548.805  1.00 54.56           C  
ANISOU  331  CB  TYR A  60     7782   8029   4919    243   -611  -1152       C  
ATOM    332  CG  TYR A  60     186.722  36.646 549.490  1.00 68.24           C  
ANISOU  332  CG  TYR A  60     9672   9728   6527    202   -705  -1357       C  
ATOM    333  CD1 TYR A  60     185.993  36.880 550.649  1.00 71.25           C  
ANISOU  333  CD1 TYR A  60    10301  10127   6644    303   -627  -1418       C  
ATOM    334  CD2 TYR A  60     187.492  37.683 548.981  1.00 78.83           C  
ANISOU  334  CD2 TYR A  60    10921  11013   8016     60   -864  -1493       C  
ATOM    335  CE1 TYR A  60     186.026  38.109 551.278  1.00 80.82           C  
ANISOU  335  CE1 TYR A  60    11676  11297   7736    273   -713  -1624       C  
ATOM    336  CE2 TYR A  60     187.532  38.916 549.604  1.00 89.37           C  
ANISOU  336  CE2 TYR A  60    12412  12293   9251     14   -955  -1692       C  
ATOM    337  CZ  TYR A  60     186.797  39.123 550.752  1.00 95.36           C  
ANISOU  337  CZ  TYR A  60    13427  13066   9740    125   -884  -1765       C  
ATOM    338  OH  TYR A  60     186.834  40.349 551.377  1.00107.77           O  
ANISOU  338  OH  TYR A  60    15172  14572  11204     88   -974  -1981       O  
ATOM    339  N   PHE A  61     185.883  32.994 546.844  1.00 41.85           N  
ANISOU  339  N   PHE A  61     5866   6363   3673    288   -303   -803       N  
ATOM    340  CA  PHE A  61     185.977  32.229 545.604  1.00 40.90           C  
ANISOU  340  CA  PHE A  61     5553   6206   3780    259   -246   -700       C  
ATOM    341  C   PHE A  61     184.637  32.209 544.876  1.00 47.32           C  
ANISOU  341  C   PHE A  61     6343   6921   4714    250    -22   -671       C  
ATOM    342  O   PHE A  61     184.566  32.461 543.666  1.00 66.28           O  
ANISOU  342  O   PHE A  61     8605   9265   7315    180      7   -686       O  
ATOM    343  CB  PHE A  61     186.451  30.807 545.901  1.00 50.74           C  
ANISOU  343  CB  PHE A  61     6783   7513   4981    348   -273   -549       C  
ATOM    344  CG  PHE A  61     187.815  30.737 546.529  1.00 51.56           C  
ANISOU  344  CG  PHE A  61     6877   7728   4987    371   -513   -563       C  
ATOM    345  CD1 PHE A  61     188.745  31.742 546.318  1.00 41.40           C  
ANISOU  345  CD1 PHE A  61     5502   6472   3757    274   -693   -694       C  
ATOM    346  CD2 PHE A  61     188.168  29.663 547.330  1.00 54.84           C  
ANISOU  346  CD2 PHE A  61     7364   8212   5259    490   -562   -439       C  
ATOM    347  CE1 PHE A  61     190.000  31.677 546.895  1.00 43.68           C  
ANISOU  347  CE1 PHE A  61     5753   6873   3972    288   -928   -712       C  
ATOM    348  CE2 PHE A  61     189.421  29.592 547.909  1.00 54.23           C  
ANISOU  348  CE2 PHE A  61     7264   8249   5093    524   -801   -450       C  
ATOM    349  CZ  PHE A  61     190.338  30.601 547.692  1.00 49.22           C  
ANISOU  349  CZ  PHE A  61     6519   7657   4525    420   -990   -592       C  
ATOM    350  N   LEU A  62     183.557  31.920 545.607  1.00 44.35           N  
ANISOU  350  N   LEU A  62     6098   6534   4217    324    139   -628       N  
ATOM    351  CA  LEU A  62     182.226  31.947 545.011  1.00 46.53           C  
ANISOU  351  CA  LEU A  62     6337   6730   4613    317    346   -608       C  
ATOM    352  C   LEU A  62     181.839  33.351 544.571  1.00 48.30           C  
ANISOU  352  C   LEU A  62     6552   6893   4907    263    353   -746       C  
ATOM    353  O   LEU A  62     181.021  33.511 543.659  1.00 56.56           O  
ANISOU  353  O   LEU A  62     7504   7871   6114    237    464   -740       O  
ATOM    354  CB  LEU A  62     181.196  31.397 545.999  1.00 41.22           C  
ANISOU  354  CB  LEU A  62     5800   6070   3794    404    526   -531       C  
ATOM    355  CG  LEU A  62     181.376  29.942 546.436  1.00 35.56           C  
ANISOU  355  CG  LEU A  62     5110   5383   3017    463    558   -365       C  
ATOM    356  CD1 LEU A  62     180.302  29.547 547.436  1.00 35.18           C  
ANISOU  356  CD1 LEU A  62     5204   5341   2821    538    762   -286       C  
ATOM    357  CD2 LEU A  62     181.370  29.009 545.234  1.00 43.07           C  
ANISOU  357  CD2 LEU A  62     5889   6274   4203    419    588   -278       C  
ATOM    358  N   PHE A  63     182.406  34.379 545.207  1.00 37.53           N  
ANISOU  358  N   PHE A  63     5291   5544   3425    247    229   -873       N  
ATOM    359  CA  PHE A  63     182.161  35.746 544.761  1.00 39.87           C  
ANISOU  359  CA  PHE A  63     5590   5756   3803    192    222  -1005       C  
ATOM    360  C   PHE A  63     182.766  35.981 543.384  1.00 47.46           C  
ANISOU  360  C   PHE A  63     6374   6673   4987     90    144  -1001       C  
ATOM    361  O   PHE A  63     182.103  36.510 542.484  1.00 58.97           O  
ANISOU  361  O   PHE A  63     7769   8049   6588     65    227  -1014       O  
ATOM    362  CB  PHE A  63     182.721  36.742 545.778  1.00 35.19           C  
ANISOU  362  CB  PHE A  63     5158   5174   3038    186     91  -1153       C  
ATOM    363  CG  PHE A  63     182.428  38.180 545.448  1.00 37.55           C  
ANISOU  363  CG  PHE A  63     5495   5360   3414    138     93  -1294       C  
ATOM    364  CD1 PHE A  63     181.278  38.791 545.920  1.00 45.13           C  
ANISOU  364  CD1 PHE A  63     6582   6262   4304    218    247  -1359       C  
ATOM    365  CD2 PHE A  63     183.303  38.922 544.669  1.00 38.90           C  
ANISOU  365  CD2 PHE A  63     5573   5473   3733     17    -49  -1355       C  
ATOM    366  CE1 PHE A  63     181.005  40.112 545.619  1.00 62.13           C  
ANISOU  366  CE1 PHE A  63     8781   8292   6535    190    250  -1486       C  
ATOM    367  CE2 PHE A  63     183.035  40.243 544.365  1.00 46.34           C  
ANISOU  367  CE2 PHE A  63     6565   6287   4753    -27    -42  -1472       C  
ATOM    368  CZ  PHE A  63     181.884  40.839 544.840  1.00 64.73           C  
ANISOU  368  CZ  PHE A  63     9033   8549   7013     65    102  -1539       C  
ATOM    369  N   SER A  64     184.031  35.591 543.200  1.00 45.09           N  
ANISOU  369  N   SER A  64     5988   6432   4712     40    -13   -976       N  
ATOM    370  CA  SER A  64     184.657  35.729 541.888  1.00 37.33           C  
ANISOU  370  CA  SER A  64     4834   5421   3929    -50    -65   -958       C  
ATOM    371  C   SER A  64     183.927  34.896 540.840  1.00 38.36           C  
ANISOU  371  C   SER A  64     4856   5526   4194    -26     74   -852       C  
ATOM    372  O   SER A  64     183.711  35.354 539.709  1.00 44.43           O  
ANISOU  372  O   SER A  64     5538   6234   5108    -77    109   -858       O  
ATOM    373  CB  SER A  64     186.129  35.327 541.965  1.00 41.76           C  
ANISOU  373  CB  SER A  64     5305   6068   4492    -90   -241   -941       C  
ATOM    374  OG  SER A  64     186.746  35.404 540.692  1.00 52.50           O  
ANISOU  374  OG  SER A  64     6495   7413   6041   -169   -265   -915       O  
ATOM    375  N   LEU A  65     183.535  33.671 541.202  1.00 40.36           N  
ANISOU  375  N   LEU A  65     5121   5819   4394     49    149   -754       N  
ATOM    376  CA  LEU A  65     182.775  32.834 540.278  1.00 36.89           C  
ANISOU  376  CA  LEU A  65     4590   5346   4083     63    274   -669       C  
ATOM    377  C   LEU A  65     181.466  33.507 539.880  1.00 40.11           C  
ANISOU  377  C   LEU A  65     5006   5682   4554     65    402   -705       C  
ATOM    378  O   LEU A  65     181.080  33.489 538.703  1.00 34.74           O  
ANISOU  378  O   LEU A  65     4222   4961   4017     35    441   -688       O  
ATOM    379  CB  LEU A  65     182.514  31.468 540.913  1.00 28.20           C  
ANISOU  379  CB  LEU A  65     3526   4276   2912    136    341   -561       C  
ATOM    380  CG  LEU A  65     182.031  30.341 539.999  1.00 40.50           C  
ANISOU  380  CG  LEU A  65     4983   5795   4609    138    432   -472       C  
ATOM    381  CD1 LEU A  65     183.041  30.078 538.894  1.00 48.92           C  
ANISOU  381  CD1 LEU A  65     5921   6871   5794     99    337   -467       C  
ATOM    382  CD2 LEU A  65     181.777  29.078 540.807  1.00 41.71           C  
ANISOU  382  CD2 LEU A  65     5203   5956   4688    204    503   -362       C  
ATOM    383  N   ALA A  66     180.778  34.121 540.847  1.00 43.00           N  
ANISOU  383  N   ALA A  66     5497   6036   4806    109    465   -757       N  
ATOM    384  CA  ALA A  66     179.548  34.844 540.545  1.00 36.44           C  
ANISOU  384  CA  ALA A  66     4667   5141   4039    131    584   -797       C  
ATOM    385  C   ALA A  66     179.812  36.058 539.666  1.00 44.36           C  
ANISOU  385  C   ALA A  66     5635   6077   5144     73    513   -873       C  
ATOM    386  O   ALA A  66     178.948  36.443 538.869  1.00 62.10           O  
ANISOU  386  O   ALA A  66     7822   8268   7503     84    585   -872       O  
ATOM    387  CB  ALA A  66     178.853  35.267 541.839  1.00 39.22           C  
ANISOU  387  CB  ALA A  66     5169   5498   4233    206    676   -845       C  
ATOM    388  N  ACYS A  67     180.988  36.676 539.796  0.45 45.81           N  
ANISOU  388  N  ACYS A  67     5849   6260   5295     12    371   -933       N  
ATOM    389  N  BCYS A  67     180.987  36.679 539.797  0.55 45.85           N  
ANISOU  389  N  BCYS A  67     5855   6266   5300     12    371   -934       N  
ATOM    390  CA ACYS A  67     181.331  37.794 538.923  0.45 40.56           C  
ANISOU  390  CA ACYS A  67     5151   5519   4740    -59    311   -987       C  
ATOM    391  CA BCYS A  67     181.334  37.793 538.921  0.55 39.29           C  
ANISOU  391  CA BCYS A  67     4990   5358   4580    -59    310   -987       C  
ATOM    392  C  ACYS A  67     181.524  37.326 537.486  0.45 46.11           C  
ANISOU  392  C  ACYS A  67     5703   6225   5591   -101    311   -906       C  
ATOM    393  C  BCYS A  67     181.519  37.322 537.485  0.55 46.26           C  
ANISOU  393  C  BCYS A  67     5722   6244   5610   -101    311   -906       C  
ATOM    394  O  ACYS A  67     181.020  37.955 536.547  0.45 41.27           O  
ANISOU  394  O  ACYS A  67     5056   5545   5079   -110    347   -905       O  
ATOM    395  O  BCYS A  67     181.012  37.946 536.544  0.55 41.26           O  
ANISOU  395  O  BCYS A  67     5055   5544   5079   -110    348   -904       O  
ATOM    396  CB ACYS A  67     182.590  38.493 539.437  0.45 40.77           C  
ANISOU  396  CB ACYS A  67     5231   5546   4714   -136    157  -1069       C  
ATOM    397  CB BCYS A  67     182.599  38.487 539.427  0.55 40.16           C  
ANISOU  397  CB BCYS A  67     5153   5469   4638   -136    157  -1068       C  
ATOM    398  SG ACYS A  67     183.120  39.913 538.453  0.45 38.37           S  
ANISOU  398  SG ACYS A  67     4899   5125   4555   -246     91  -1124       S  
ATOM    399  SG BCYS A  67     182.412  39.329 541.011  0.55 43.90           S  
ANISOU  399  SG BCYS A  67     5836   5918   4926    -94    131  -1204       S  
ATOM    400  N   ALA A  68     182.246  36.217 537.297  1.00 43.71           N  
ANISOU  400  N   ALA A  68     5318   5998   5292   -115    271   -839       N  
ATOM    401  CA  ALA A  68     182.444  35.680 535.954  1.00 37.06           C  
ANISOU  401  CA  ALA A  68     4347   5164   4569   -142    279   -773       C  
ATOM    402  C   ALA A  68     181.116  35.265 535.330  1.00 35.39           C  
ANISOU  402  C   ALA A  68     4103   4926   4419    -92    392   -735       C  
ATOM    403  O   ALA A  68     180.826  35.599 534.174  1.00 21.96           O  
ANISOU  403  O   ALA A  68     2345   3191   2809   -108    405   -723       O  
ATOM    404  CB  ALA A  68     183.415  34.499 536.003  1.00 24.03           C  
ANISOU  404  CB  ALA A  68     2629   3595   2905   -141    227   -717       C  
ATOM    405  N   ASP A  69     180.288  34.542 536.090  1.00 34.49           N  
ANISOU  405  N   ASP A  69     4021   4828   4254    -32    473   -712       N  
ATOM    406  CA  ASP A  69     178.975  34.154 535.584  1.00 38.95           C  
ANISOU  406  CA  ASP A  69     4533   5370   4895      4    575   -681       C  
ATOM    407  C   ASP A  69     178.110  35.370 535.280  1.00 44.26           C  
ANISOU  407  C   ASP A  69     5221   5983   5612     26    610   -730       C  
ATOM    408  O   ASP A  69     177.304  35.340 534.342  1.00 51.40           O  
ANISOU  408  O   ASP A  69     6047   6870   6614     39    641   -711       O  
ATOM    409  CB  ASP A  69     178.276  33.238 536.588  1.00 51.87           C  
ANISOU  409  CB  ASP A  69     6202   7030   6477     52    672   -641       C  
ATOM    410  CG  ASP A  69     179.017  31.932 536.801  1.00 71.26           C  
ANISOU  410  CG  ASP A  69     8646   9524   8905     46    645   -574       C  
ATOM    411  OD1 ASP A  69     179.724  31.490 535.870  1.00 70.42           O  
ANISOU  411  OD1 ASP A  69     8467   9424   8866     13    580   -557       O  
ATOM    412  OD2 ASP A  69     178.892  31.347 537.897  1.00 75.64           O  
ANISOU  412  OD2 ASP A  69     9273  10100   9367     84    696   -535       O  
ATOM    413  N   LEU A  70     178.263  36.447 536.055  1.00 42.23           N  
ANISOU  413  N   LEU A  70     5068   5691   5285     37    596   -797       N  
ATOM    414  CA  LEU A  70     177.531  37.675 535.764  1.00 48.02           C  
ANISOU  414  CA  LEU A  70     5830   6347   6067     71    625   -845       C  
ATOM    415  C   LEU A  70     177.986  38.287 534.445  1.00 59.69           C  
ANISOU  415  C   LEU A  70     7260   7780   7637     20    553   -830       C  
ATOM    416  O   LEU A  70     177.155  38.725 533.639  1.00 60.95           O  
ANISOU  416  O   LEU A  70     7380   7899   7878     59    581   -815       O  
ATOM    417  CB  LEU A  70     177.705  38.674 536.908  1.00 44.43           C  
ANISOU  417  CB  LEU A  70     5522   5848   5512     92    620   -936       C  
ATOM    418  CG  LEU A  70     177.054  40.045 536.709  1.00 47.30           C  
ANISOU  418  CG  LEU A  70     5942   6104   5926    137    648   -996       C  
ATOM    419  CD1 LEU A  70     175.549  39.908 536.538  1.00 57.83           C  
ANISOU  419  CD1 LEU A  70     7210   7440   7323    238    773   -969       C  
ATOM    420  CD2 LEU A  70     177.384  40.973 537.867  1.00 40.23           C  
ANISOU  420  CD2 LEU A  70     5211   5153   4920    148    629  -1107       C  
ATOM    421  N   ILE A  71     179.300  38.322 534.206  1.00 60.92           N  
ANISOU  421  N   ILE A  71     7414   7949   7782    -62    462   -827       N  
ATOM    422  CA  ILE A  71     179.804  38.852 532.941  1.00 50.71           C  
ANISOU  422  CA  ILE A  71     6078   6621   6568   -116    415   -796       C  
ATOM    423  C   ILE A  71     179.315  38.003 531.773  1.00 47.51           C  
ANISOU  423  C   ILE A  71     5569   6261   6221    -93    441   -728       C  
ATOM    424  O   ILE A  71     178.998  38.525 530.697  1.00 38.25           O  
ANISOU  424  O   ILE A  71     4377   5052   5103    -85    437   -700       O  
ATOM    425  CB  ILE A  71     181.341  38.947 532.972  1.00 43.18           C  
ANISOU  425  CB  ILE A  71     5115   5689   5602   -214    328   -801       C  
ATOM    426  CG1 ILE A  71     181.792  39.911 534.071  1.00 42.20           C  
ANISOU  426  CG1 ILE A  71     5098   5508   5426   -249    278   -888       C  
ATOM    427  CG2 ILE A  71     181.878  39.401 531.624  1.00 38.33           C  
ANISOU  427  CG2 ILE A  71     4449   5048   5066   -272    310   -750       C  
ATOM    428  CD1 ILE A  71     183.294  40.065 534.169  1.00 49.05           C  
ANISOU  428  CD1 ILE A  71     5934   6401   6299   -358    176   -902       C  
ATOM    429  N   ILE A  72     179.235  36.684 531.967  1.00 52.95           N  
ANISOU  429  N   ILE A  72     6202   7022   6893    -80    462   -703       N  
ATOM    430  CA  ILE A  72     178.701  35.816 530.921  1.00 41.60           C  
ANISOU  430  CA  ILE A  72     4677   5619   5512    -62    478   -660       C  
ATOM    431  C   ILE A  72     177.222  36.107 530.688  1.00 42.61           C  
ANISOU  431  C   ILE A  72     4781   5717   5691      1    525   -665       C  
ATOM    432  O   ILE A  72     176.744  36.093 529.547  1.00 49.95           O  
ANISOU  432  O   ILE A  72     5656   6650   6671     15    505   -644       O  
ATOM    433  CB  ILE A  72     178.941  34.337 531.278  1.00 31.47           C  
ANISOU  433  CB  ILE A  72     3354   4392   4213    -65    493   -637       C  
ATOM    434  CG1 ILE A  72     180.435  34.018 531.254  1.00 26.43           C  
ANISOU  434  CG1 ILE A  72     2709   3791   3542   -110    435   -625       C  
ATOM    435  CG2 ILE A  72     178.191  33.419 530.325  1.00 23.86           C  
ANISOU  435  CG2 ILE A  72     2312   3442   3313    -51    511   -616       C  
ATOM    436  CD1 ILE A  72     181.078  34.226 529.902  1.00 28.84           C  
ANISOU  436  CD1 ILE A  72     2967   4107   3883   -142    403   -606       C  
ATOM    437  N   GLY A  73     176.479  36.388 531.759  1.00 40.11           N  
ANISOU  437  N   GLY A  73     4501   5381   5358     47    588   -694       N  
ATOM    438  CA  GLY A  73     175.054  36.634 531.609  1.00 48.51           C  
ANISOU  438  CA  GLY A  73     5514   6429   6488    116    643   -697       C  
ATOM    439  C   GLY A  73     174.745  37.960 530.938  1.00 39.66           C  
ANISOU  439  C   GLY A  73     4421   5244   5405    158    612   -706       C  
ATOM    440  O   GLY A  73     173.780  38.068 530.177  1.00 28.37           O  
ANISOU  440  O   GLY A  73     2917   3816   4047    211    608   -687       O  
ATOM    441  N   VAL A  74     175.557  38.983 531.204  1.00 39.34           N  
ANISOU  441  N   VAL A  74     4486   5138   5322    134    582   -731       N  
ATOM    442  CA  VAL A  74     175.265  40.313 530.676  1.00 33.46           C  
ANISOU  442  CA  VAL A  74     3793   4302   4619    178    564   -733       C  
ATOM    443  C   VAL A  74     175.723  40.440 529.228  1.00 37.17           C  
ANISOU  443  C   VAL A  74     4237   4771   5116    142    495   -669       C  
ATOM    444  O   VAL A  74     174.960  40.870 528.355  1.00 39.09           O  
ANISOU  444  O   VAL A  74     4454   4992   5406    208    479   -634       O  
ATOM    445  CB  VAL A  74     175.905  41.395 531.565  1.00 28.96           C  
ANISOU  445  CB  VAL A  74     3360   3639   4006    156    562   -795       C  
ATOM    446  CG1 VAL A  74     175.703  42.772 530.951  1.00 25.07           C  
ANISOU  446  CG1 VAL A  74     2936   3021   3570    193    543   -786       C  
ATOM    447  CG2 VAL A  74     175.321  41.346 532.967  1.00 24.90           C  
ANISOU  447  CG2 VAL A  74     2892   3129   3440    216    639   -863       C  
ATOM    448  N   PHE A  75     176.971  40.068 528.946  1.00 39.65           N  
ANISOU  448  N   PHE A  75     4555   5116   5393     48    457   -651       N  
ATOM    449  CA  PHE A  75     177.582  40.321 527.646  1.00 38.43           C  
ANISOU  449  CA  PHE A  75     4399   4958   5245      9    415   -588       C  
ATOM    450  C   PHE A  75     177.484  39.137 526.691  1.00 41.03           C  
ANISOU  450  C   PHE A  75     4638   5388   5563     12    397   -554       C  
ATOM    451  O   PHE A  75     177.034  39.298 525.553  1.00 50.99           O  
ANISOU  451  O   PHE A  75     5887   6657   6830     52    370   -511       O  
ATOM    452  CB  PHE A  75     179.054  40.714 527.828  1.00 39.38           C  
ANISOU  452  CB  PHE A  75     4565   5054   5346    -97    395   -587       C  
ATOM    453  CG  PHE A  75     179.252  42.019 528.549  1.00 46.21           C  
ANISOU  453  CG  PHE A  75     5534   5795   6229   -119    393   -628       C  
ATOM    454  CD1 PHE A  75     179.315  42.061 529.932  1.00 46.91           C  
ANISOU  454  CD1 PHE A  75     5668   5870   6286   -125    397   -712       C  
ATOM    455  CD2 PHE A  75     179.381  43.203 527.841  1.00 46.09           C  
ANISOU  455  CD2 PHE A  75     5588   5670   6255   -133    387   -584       C  
ATOM    456  CE1 PHE A  75     179.499  43.261 530.597  1.00 41.95           C  
ANISOU  456  CE1 PHE A  75     5153   5120   5668   -146    386   -771       C  
ATOM    457  CE2 PHE A  75     179.565  44.405 528.499  1.00 46.25           C  
ANISOU  457  CE2 PHE A  75     5717   5550   6304   -159    383   -631       C  
ATOM    458  CZ  PHE A  75     179.624  44.434 529.879  1.00 44.31           C  
ANISOU  458  CZ  PHE A  75     5516   5291   6028   -167    379   -736       C  
ATOM    459  N   SER A  76     177.897  37.947 527.131  1.00 38.75           N  
ANISOU  459  N   SER A  76     4299   5171   5254    -24    407   -576       N  
ATOM    460  CA  SER A  76     178.070  36.831 526.205  1.00 40.74           C  
ANISOU  460  CA  SER A  76     4487   5499   5493    -33    389   -556       C  
ATOM    461  C   SER A  76     176.732  36.320 525.680  1.00 42.20           C  
ANISOU  461  C   SER A  76     4611   5709   5714     28    375   -564       C  
ATOM    462  O   SER A  76     176.565  36.122 524.470  1.00 48.56           O  
ANISOU  462  O   SER A  76     5399   6547   6505     45    333   -546       O  
ATOM    463  CB  SER A  76     178.847  35.708 526.889  1.00 40.13           C  
ANISOU  463  CB  SER A  76     4380   5470   5398    -74    403   -575       C  
ATOM    464  OG  SER A  76     180.091  36.182 527.371  1.00 24.97           O  
ANISOU  464  OG  SER A  76     2494   3542   3454   -131    396   -572       O  
ATOM    465  N   MET A  77     175.768  36.097 526.576  1.00 47.11           N  
ANISOU  465  N   MET A  77     5197   6323   6381     60    410   -594       N  
ATOM    466  CA  MET A  77     174.492  35.519 526.162  1.00 47.02           C  
ANISOU  466  CA  MET A  77     5095   6342   6430    101    395   -606       C  
ATOM    467  C   MET A  77     173.761  36.422 525.177  1.00 39.78           C  
ANISOU  467  C   MET A  77     4170   5413   5530    168    338   -584       C  
ATOM    468  O   MET A  77     173.221  35.945 524.171  1.00 52.09           O  
ANISOU  468  O   MET A  77     5672   7019   7101    185    273   -585       O  
ATOM    469  CB  MET A  77     173.615  35.248 527.384  1.00 51.94           C  
ANISOU  469  CB  MET A  77     5672   6957   7107    121    470   -629       C  
ATOM    470  CG  MET A  77     174.101  34.109 528.262  1.00 48.12           C  
ANISOU  470  CG  MET A  77     5189   6489   6604     68    521   -635       C  
ATOM    471  SD  MET A  77     172.952  33.752 529.603  0.82 50.16           S  
ANISOU  471  SD  MET A  77     5397   6745   6916     94    634   -641       S  
ATOM    472  CE  MET A  77     173.731  32.322 530.345  1.00 56.22           C  
ANISOU  472  CE  MET A  77     6192   7523   7645     31    674   -621       C  
ATOM    473  N   ASN A  78     173.733  37.729 525.445  1.00 36.81           N  
ANISOU  473  N   ASN A  78     3862   4971   5154    211    353   -565       N  
ATOM    474  CA  ASN A  78     172.992  38.644 524.582  1.00 44.08           C  
ANISOU  474  CA  ASN A  78     4785   5868   6096    296    299   -529       C  
ATOM    475  C   ASN A  78     173.654  38.782 523.216  1.00 44.66           C  
ANISOU  475  C   ASN A  78     4912   5961   6095    281    233   -477       C  
ATOM    476  O   ASN A  78     172.972  38.749 522.184  1.00 51.32           O  
ANISOU  476  O   ASN A  78     5723   6846   6931    339    157   -455       O  
ATOM    477  CB  ASN A  78     172.857  40.007 525.259  1.00 39.19           C  
ANISOU  477  CB  ASN A  78     4245   5145   5499    350    341   -524       C  
ATOM    478  CG  ASN A  78     172.019  39.949 526.521  1.00 47.96           C  
ANISOU  478  CG  ASN A  78     5307   6247   6669    395    419   -577       C  
ATOM    479  OD1 ASN A  78     171.042  39.203 526.599  1.00 47.45           O  
ANISOU  479  OD1 ASN A  78     5118   6247   6663    423    429   -594       O  
ATOM    480  ND2 ASN A  78     172.398  40.737 527.520  1.00 50.84           N  
ANISOU  480  ND2 ASN A  78     5771   6530   7016    397    478   -607       N  
ATOM    481  N   LEU A  79     174.980  38.936 523.187  1.00 32.49           N  
ANISOU  481  N   LEU A  79     3451   4399   4496    206    262   -454       N  
ATOM    482  CA  LEU A  79     175.677  39.071 521.913  1.00 30.80           C  
ANISOU  482  CA  LEU A  79     3291   4209   4204    191    230   -395       C  
ATOM    483  C   LEU A  79     175.574  37.794 521.088  1.00 43.32           C  
ANISOU  483  C   LEU A  79     4817   5897   5744    186    186   -423       C  
ATOM    484  O   LEU A  79     175.410  37.849 519.863  1.00 60.78           O  
ANISOU  484  O   LEU A  79     7057   8150   7887    227    129   -389       O  
ATOM    485  CB  LEU A  79     177.141  39.443 522.150  1.00 32.35           C  
ANISOU  485  CB  LEU A  79     3552   4369   4370    100    285   -368       C  
ATOM    486  CG  LEU A  79     177.393  40.838 522.728  1.00 47.11           C  
ANISOU  486  CG  LEU A  79     5505   6115   6278     87    314   -342       C  
ATOM    487  CD1 LEU A  79     178.883  41.092 522.896  1.00 45.90           C  
ANISOU  487  CD1 LEU A  79     5387   5940   6113    -26    354   -322       C  
ATOM    488  CD2 LEU A  79     176.761  41.906 521.851  1.00 24.50           C  
ANISOU  488  CD2 LEU A  79     2711   3187   3411    169    284   -266       C  
ATOM    489  N   TYR A  80     175.664  36.633 521.740  1.00 38.37           N  
ANISOU  489  N   TYR A  80     4124   5308   5148    140    209   -487       N  
ATOM    490  CA  TYR A  80     175.517  35.378 521.009  1.00 35.42           C  
ANISOU  490  CA  TYR A  80     3705   5007   4747    133    166   -530       C  
ATOM    491  C   TYR A  80     174.088  35.197 520.510  1.00 36.11           C  
ANISOU  491  C   TYR A  80     3722   5124   4875    192     80   -558       C  
ATOM    492  O   TYR A  80     173.869  34.645 519.423  1.00 23.33           O  
ANISOU  492  O   TYR A  80     2101   3562   3202    208      4   -582       O  
ATOM    493  CB  TYR A  80     175.938  34.204 521.892  1.00 41.81           C  
ANISOU  493  CB  TYR A  80     4470   5822   5595     74    216   -581       C  
ATOM    494  CG  TYR A  80     176.122  32.910 521.135  1.00 41.73           C  
ANISOU  494  CG  TYR A  80     4442   5859   5554     59    186   -629       C  
ATOM    495  CD1 TYR A  80     177.224  32.716 520.313  1.00 44.22           C  
ANISOU  495  CD1 TYR A  80     4814   6209   5778     52    201   -616       C  
ATOM    496  CD2 TYR A  80     175.197  31.880 521.245  1.00 35.23           C  
ANISOU  496  CD2 TYR A  80     3545   5040   4801     49    153   -690       C  
ATOM    497  CE1 TYR A  80     177.399  31.536 519.619  1.00 36.59           C  
ANISOU  497  CE1 TYR A  80     3848   5277   4777     52    181   -675       C  
ATOM    498  CE2 TYR A  80     175.365  30.695 520.555  1.00 42.51           C  
ANISOU  498  CE2 TYR A  80     4468   5983   5702     32    122   -750       C  
ATOM    499  CZ  TYR A  80     176.467  30.529 519.744  1.00 41.53           C  
ANISOU  499  CZ  TYR A  80     4417   5889   5472     42    135   -747       C  
ATOM    500  OH  TYR A  80     176.639  29.351 519.053  1.00 51.19           O  
ANISOU  500  OH  TYR A  80     5657   7125   6668     38    110   -820       O  
ATOM    501  N   THR A  81     173.103  35.658 521.287  1.00 39.05           N  
ANISOU  501  N   THR A  81     4032   5463   5341    228     89   -562       N  
ATOM    502  CA  THR A  81     171.717  35.605 520.835  1.00 39.96           C  
ANISOU  502  CA  THR A  81     4050   5614   5517    289      3   -582       C  
ATOM    503  C   THR A  81     171.510  36.479 519.605  1.00 46.00           C  
ANISOU  503  C   THR A  81     4874   6399   6206    372    -92   -527       C  
ATOM    504  O   THR A  81     170.854  36.065 518.642  1.00 56.63           O  
ANISOU  504  O   THR A  81     6176   7813   7529    405   -206   -552       O  
ATOM    505  CB  THR A  81     170.776  36.039 521.958  1.00 41.16           C  
ANISOU  505  CB  THR A  81     4120   5731   5789    326     58   -588       C  
ATOM    506  OG1 THR A  81     170.979  35.206 523.104  1.00 51.55           O  
ANISOU  506  OG1 THR A  81     5401   7033   7152    254    153   -625       O  
ATOM    507  CG2 THR A  81     169.326  35.927 521.511  1.00 52.92           C  
ANISOU  507  CG2 THR A  81     5470   7271   7367    388    -31   -609       C  
ATOM    508  N   LEU A  82     172.061  37.695 519.621  1.00 43.36           N  
ANISOU  508  N   LEU A  82     4646   6000   5827    405    -51   -451       N  
ATOM    509  CA  LEU A  82     171.993  38.552 518.442  1.00 44.42           C  
ANISOU  509  CA  LEU A  82     4865   6139   5874    484   -125   -373       C  
ATOM    510  C   LEU A  82     172.674  37.893 517.249  1.00 46.04           C  
ANISOU  510  C   LEU A  82     5134   6421   5939    455   -168   -372       C  
ATOM    511  O   LEU A  82     172.145  37.912 516.129  1.00 39.60           O  
ANISOU  511  O   LEU A  82     4335   5667   5043    525   -279   -355       O  
ATOM    512  CB  LEU A  82     172.636  39.905 518.749  1.00 35.62           C  
ANISOU  512  CB  LEU A  82     3869   4915   4751    497    -51   -288       C  
ATOM    513  CG  LEU A  82     172.443  41.028 517.731  1.00 37.75           C  
ANISOU  513  CG  LEU A  82     4240   5149   4953    594   -108   -180       C  
ATOM    514  CD1 LEU A  82     170.978  41.418 517.651  1.00 46.15           C  
ANISOU  514  CD1 LEU A  82     5222   6222   6092    726   -202   -178       C  
ATOM    515  CD2 LEU A  82     173.303  42.228 518.094  1.00 34.33           C  
ANISOU  515  CD2 LEU A  82     3934   4583   4526    566    -15   -103       C  
ATOM    516  N   TYR A  83     173.842  37.288 517.481  1.00 47.24           N  
ANISOU  516  N   TYR A  83     5321   6575   6054    363    -82   -393       N  
ATOM    517  CA  TYR A  83     174.589  36.635 516.410  1.00 40.49           C  
ANISOU  517  CA  TYR A  83     4530   5791   5065    345    -93   -399       C  
ATOM    518  C   TYR A  83     173.770  35.525 515.761  1.00 48.12           C  
ANISOU  518  C   TYR A  83     5434   6839   6010    364   -207   -493       C  
ATOM    519  O   TYR A  83     173.617  35.488 514.534  1.00 42.65           O  
ANISOU  519  O   TYR A  83     4804   6212   5189    418   -293   -487       O  
ATOM    520  CB  TYR A  83     175.902  36.082 516.968  1.00 33.94           C  
ANISOU  520  CB  TYR A  83     3711   4950   4236    253     23   -418       C  
ATOM    521  CG  TYR A  83     176.840  35.494 515.936  1.00 38.03           C  
ANISOU  521  CG  TYR A  83     4295   5535   4619    243     49   -419       C  
ATOM    522  CD1 TYR A  83     176.838  35.945 514.623  1.00 29.68           C  
ANISOU  522  CD1 TYR A  83     3335   4526   3417    305     11   -360       C  
ATOM    523  CD2 TYR A  83     177.729  34.483 516.278  1.00 51.02           C  
ANISOU  523  CD2 TYR A  83     5912   7198   6276    186    117   -476       C  
ATOM    524  CE1 TYR A  83     177.697  35.407 513.682  1.00 38.91           C  
ANISOU  524  CE1 TYR A  83     4573   5764   4448    307     55   -365       C  
ATOM    525  CE2 TYR A  83     178.590  33.939 515.344  1.00 46.66           C  
ANISOU  525  CE2 TYR A  83     5416   6707   5604    194    157   -484       C  
ATOM    526  CZ  TYR A  83     178.570  34.404 514.048  1.00 43.74           C  
ANISOU  526  CZ  TYR A  83     5145   6391   5083    253    133   -432       C  
ATOM    527  OH  TYR A  83     179.426  33.865 513.116  1.00 51.03           O  
ANISOU  527  OH  TYR A  83     6133   7383   5872    270    192   -443       O  
ATOM    528  N   THR A  84     173.229  34.612 516.571  1.00 54.16           N  
ANISOU  528  N   THR A  84     6083   7597   6900    316   -212   -583       N  
ATOM    529  CA  THR A  84     172.514  33.468 516.011  1.00 48.68           C  
ANISOU  529  CA  THR A  84     5324   6960   6211    307   -319   -685       C  
ATOM    530  C   THR A  84     171.175  33.881 515.411  1.00 42.51           C  
ANISOU  530  C   THR A  84     4479   6225   5448    383   -470   -688       C  
ATOM    531  O   THR A  84     170.780  33.369 514.357  1.00 29.00           O  
ANISOU  531  O   THR A  84     2779   4585   3656    406   -600   -747       O  
ATOM    532  CB  THR A  84     172.308  32.398 517.083  1.00 57.84           C  
ANISOU  532  CB  THR A  84     6379   8081   7515    224   -268   -762       C  
ATOM    533  OG1 THR A  84     171.535  32.942 518.160  1.00 77.99           O  
ANISOU  533  OG1 THR A  84     8835  10593  10205    231   -232   -733       O  
ATOM    534  CG2 THR A  84     173.648  31.915 517.618  1.00 47.93           C  
ANISOU  534  CG2 THR A  84     5186   6790   6235    166   -141   -758       C  
ATOM    535  N   VAL A  85     170.465  34.805 516.062  1.00 50.92           N  
ANISOU  535  N   VAL A  85     5477   7254   6616    432   -461   -632       N  
ATOM    536  CA  VAL A  85     169.136  35.190 515.591  1.00 41.71           C  
ANISOU  536  CA  VAL A  85     4217   6136   5496    519   -606   -632       C  
ATOM    537  C   VAL A  85     169.232  35.963 514.281  1.00 39.81           C  
ANISOU  537  C   VAL A  85     4102   5943   5082    621   -709   -558       C  
ATOM    538  O   VAL A  85     168.478  35.705 513.334  1.00 50.48           O  
ANISOU  538  O   VAL A  85     5421   7379   6380    674   -878   -596       O  
ATOM    539  CB  VAL A  85     168.394  35.995 516.673  1.00 44.83           C  
ANISOU  539  CB  VAL A  85     4510   6475   6049    564   -547   -591       C  
ATOM    540  CG1 VAL A  85     167.197  36.714 516.074  1.00 36.52           C  
ANISOU  540  CG1 VAL A  85     3381   5468   5026    692   -691   -557       C  
ATOM    541  CG2 VAL A  85     167.946  35.073 517.797  1.00 55.81           C  
ANISOU  541  CG2 VAL A  85     5752   7849   7603    475   -475   -668       C  
ATOM    542  N   ILE A  86     170.159  36.922 514.200  1.00 44.54           N  
ANISOU  542  N   ILE A  86     4850   6487   5588    648   -612   -448       N  
ATOM    543  CA  ILE A  86     170.292  37.688 512.964  1.00 46.77           C  
ANISOU  543  CA  ILE A  86     5271   6803   5695    745   -687   -353       C  
ATOM    544  C   ILE A  86     170.843  36.816 511.840  1.00 56.09           C  
ANISOU  544  C   ILE A  86     6545   8077   6691    722   -737   -405       C  
ATOM    545  O   ILE A  86     170.449  36.966 510.676  1.00 67.04           O  
ANISOU  545  O   ILE A  86     8000   9543   7929    811   -874   -384       O  
ATOM    546  CB  ILE A  86     171.158  38.940 513.206  1.00 48.07           C  
ANISOU  546  CB  ILE A  86     5568   6865   5830    760   -554   -215       C  
ATOM    547  CG1 ILE A  86     170.374  39.969 514.023  1.00 53.05           C  
ANISOU  547  CG1 ILE A  86     6137   7405   6613    831   -547   -166       C  
ATOM    548  CG2 ILE A  86     171.628  39.550 511.893  1.00 48.17           C  
ANISOU  548  CG2 ILE A  86     5757   6909   5636    830   -584   -102       C  
ATOM    549  CD1 ILE A  86     170.986  41.351 514.021  1.00 65.08           C  
ANISOU  549  CD1 ILE A  86     7811   8812   8106    869   -460    -26       C  
ATOM    550  N   GLY A  87     171.734  35.880 512.163  1.00 45.50           N  
ANISOU  550  N   GLY A  87     5212   6729   5349    617   -633   -479       N  
ATOM    551  CA  GLY A  87     172.326  34.998 511.181  1.00 31.49           C  
ANISOU  551  CA  GLY A  87     3530   5029   3405    602   -654   -544       C  
ATOM    552  C   GLY A  87     173.756  35.332 510.817  1.00 39.62           C  
ANISOU  552  C   GLY A  87     4709   6050   4296    588   -500   -458       C  
ATOM    553  O   GLY A  87     174.388  34.563 510.082  1.00 51.91           O  
ANISOU  553  O   GLY A  87     6343   7667   5714    579   -480   -516       O  
ATOM    554  N   TYR A  88     174.279  36.450 511.310  1.00 39.01           N  
ANISOU  554  N   TYR A  88     4667   5895   4259    584   -387   -329       N  
ATOM    555  CA  TYR A  88     175.648  36.866 511.041  1.00 35.96           C  
ANISOU  555  CA  TYR A  88     4395   5494   3777    552   -229   -235       C  
ATOM    556  C   TYR A  88     176.022  37.926 512.066  1.00 33.07           C  
ANISOU  556  C   TYR A  88     4008   5009   3549    506   -124   -140       C  
ATOM    557  O   TYR A  88     175.176  38.412 512.820  1.00 29.35           O  
ANISOU  557  O   TYR A  88     3465   4473   3212    526   -175   -142       O  
ATOM    558  CB  TYR A  88     175.803  37.394 509.611  1.00 32.45           C  
ANISOU  558  CB  TYR A  88     4111   5115   3103    641   -255   -136       C  
ATOM    559  CG  TYR A  88     174.841  38.508 509.274  1.00 33.72           C  
ANISOU  559  CG  TYR A  88     4315   5251   3247    744   -367    -30       C  
ATOM    560  CD1 TYR A  88     173.568  38.229 508.792  1.00 56.45           C  
ANISOU  560  CD1 TYR A  88     7152   8200   6097    832   -569    -93       C  
ATOM    561  CD2 TYR A  88     175.202  39.837 509.441  1.00 34.03           C  
ANISOU  561  CD2 TYR A  88     4429   5189   3313    755   -277    132       C  
ATOM    562  CE1 TYR A  88     172.683  39.243 508.486  1.00 59.80           C  
ANISOU  562  CE1 TYR A  88     7603   8605   6512    947   -680      9       C  
ATOM    563  CE2 TYR A  88     174.325  40.857 509.138  1.00 37.05           C  
ANISOU  563  CE2 TYR A  88     4859   5531   3687    867   -377    235       C  
ATOM    564  CZ  TYR A  88     173.066  40.555 508.661  1.00 54.41           C  
ANISOU  564  CZ  TYR A  88     7010   7813   5852    972   -580    177       C  
ATOM    565  OH  TYR A  88     172.188  41.569 508.355  1.00 62.72           O  
ANISOU  565  OH  TYR A  88     8098   8831   6901   1104   -688    285       O  
ATOM    566  N   TRP A  89     177.300  38.281 512.085  1.00 43.61           N  
ANISOU  566  N   TRP A  89     5403   6315   4853    444     25    -66       N  
ATOM    567  CA  TRP A  89     177.784  39.260 513.049  1.00 43.87           C  
ANISOU  567  CA  TRP A  89     5423   6228   5017    381    119      7       C  
ATOM    568  C   TRP A  89     177.501  40.670 512.546  1.00 44.49           C  
ANISOU  568  C   TRP A  89     5615   6232   5057    444    109    155       C  
ATOM    569  O   TRP A  89     178.013  41.053 511.487  1.00 52.69           O  
ANISOU  569  O   TRP A  89     6773   7300   5947    469    155    263       O  
ATOM    570  CB  TRP A  89     179.273  39.079 513.301  1.00 28.29           C  
ANISOU  570  CB  TRP A  89     3444   4254   3052    277    269     25       C  
ATOM    571  CG  TRP A  89     179.771  39.956 514.395  1.00 27.72           C  
ANISOU  571  CG  TRP A  89     3345   4062   3125    194    340     66       C  
ATOM    572  CD1 TRP A  89     180.519  41.086 514.262  1.00 34.90           C  
ANISOU  572  CD1 TRP A  89     4326   4890   4044    143    430    190       C  
ATOM    573  CD2 TRP A  89     179.534  39.792 515.798  1.00 35.07           C  
ANISOU  573  CD2 TRP A  89     4180   4936   4209    147    323    -20       C  
ATOM    574  NE1 TRP A  89     180.775  41.632 515.497  1.00 41.22           N  
ANISOU  574  NE1 TRP A  89     5081   5582   4998     63    455    168       N  
ATOM    575  CE2 TRP A  89     180.180  40.856 516.457  1.00 35.00           C  
ANISOU  575  CE2 TRP A  89     4197   4816   4287     73    392     41       C  
ATOM    576  CE3 TRP A  89     178.843  38.846 516.561  1.00 32.47           C  
ANISOU  576  CE3 TRP A  89     3753   4635   3948    158    263   -140       C  
ATOM    577  CZ2 TRP A  89     180.156  41.000 517.843  1.00 30.49           C  
ANISOU  577  CZ2 TRP A  89     3568   4173   3845     21    390    -26       C  
ATOM    578  CZ3 TRP A  89     178.820  38.990 517.935  1.00 34.72           C  
ANISOU  578  CZ3 TRP A  89     3980   4851   4360    109    280   -186       C  
ATOM    579  CH2 TRP A  89     179.473  40.059 518.562  1.00 41.95           C  
ANISOU  579  CH2 TRP A  89     4934   5668   5338     48    338   -136       C  
ATOM    580  N   PRO A  90     176.706  41.468 513.261  1.00 44.96           N  
ANISOU  580  N   PRO A  90     5651   6191   5242    479     61    171       N  
ATOM    581  CA  PRO A  90     176.330  42.791 512.748  1.00 43.40           C  
ANISOU  581  CA  PRO A  90     5570   5905   5013    562     39    313       C  
ATOM    582  C   PRO A  90     177.162  43.935 513.309  1.00 45.92           C  
ANISOU  582  C   PRO A  90     5956   6067   5423    482    164    407       C  
ATOM    583  O   PRO A  90     177.163  45.035 512.747  1.00 44.78           O  
ANISOU  583  O   PRO A  90     5941   5833   5242    529    181    551       O  
ATOM    584  CB  PRO A  90     174.860  42.921 513.180  1.00 39.73           C  
ANISOU  584  CB  PRO A  90     5025   5424   4645    668    -94    260       C  
ATOM    585  CG  PRO A  90     174.611  41.774 514.181  1.00 35.39           C  
ANISOU  585  CG  PRO A  90     4314   4927   4206    603   -104     94       C  
ATOM    586  CD  PRO A  90     175.929  41.119 514.458  1.00 38.08           C  
ANISOU  586  CD  PRO A  90     4649   5290   4529    472     14     58       C  
ATOM    587  N   LEU A  91     177.871  43.695 514.411  1.00 55.25           N  
ANISOU  587  N   LEU A  91     7059   7209   6724    359    242    329       N  
ATOM    588  CA  LEU A  91     178.518  44.768 515.153  1.00 55.21           C  
ANISOU  588  CA  LEU A  91     7099   7043   6835    273    328    380       C  
ATOM    589  C   LEU A  91     179.909  45.119 514.639  1.00 57.77           C  
ANISOU  589  C   LEU A  91     7485   7349   7118    160    456    484       C  
ATOM    590  O   LEU A  91     180.434  46.177 515.003  1.00 70.79           O  
ANISOU  590  O   LEU A  91     9194   8847   8857     84    522    552       O  
ATOM    591  CB  LEU A  91     178.597  44.400 516.638  1.00 46.66           C  
ANISOU  591  CB  LEU A  91     5907   5931   5891    199    336    243       C  
ATOM    592  CG  LEU A  91     177.243  44.115 517.293  1.00 42.13           C  
ANISOU  592  CG  LEU A  91     5260   5367   5380    299    243    147       C  
ATOM    593  CD1 LEU A  91     177.405  43.821 518.774  1.00 42.17           C  
ANISOU  593  CD1 LEU A  91     5185   5340   5496    227    273     29       C  
ATOM    594  CD2 LEU A  91     176.286  45.277 517.074  1.00 43.28           C  
ANISOU  594  CD2 LEU A  91     5487   5399   5557    421    195    222       C  
ATOM    595  N   GLY A  92     180.519  44.273 513.813  1.00 49.85           N  
ANISOU  595  N   GLY A  92     6465   6487   5987    145    499    493       N  
ATOM    596  CA  GLY A  92     181.802  44.585 513.232  1.00 53.54           C  
ANISOU  596  CA  GLY A  92     6975   6955   6411     49    640    602       C  
ATOM    597  C   GLY A  92     182.936  43.751 513.795  1.00 60.29           C  
ANISOU  597  C   GLY A  92     7698   7886   7323    -71    718    517       C  
ATOM    598  O   GLY A  92     182.759  42.961 514.727  1.00 55.68           O  
ANISOU  598  O   GLY A  92     7004   7339   6813    -83    661    377       O  
ATOM    599  N   PRO A  93     184.137  43.927 513.237  1.00 57.10           N  
ANISOU  599  N   PRO A  93     7299   7506   6889   -156    857    612       N  
ATOM    600  CA  PRO A  93     185.262  43.077 513.665  1.00 53.73           C  
ANISOU  600  CA  PRO A  93     6728   7172   6513   -250    932    538       C  
ATOM    601  C   PRO A  93     185.773  43.403 515.058  1.00 46.58           C  
ANISOU  601  C   PRO A  93     5721   6174   5802   -376    919    472       C  
ATOM    602  O   PRO A  93     186.116  42.483 515.814  1.00 58.29           O  
ANISOU  602  O   PRO A  93     7080   7731   7337   -401    893    355       O  
ATOM    603  CB  PRO A  93     186.322  43.345 512.588  1.00 51.82           C  
ANISOU  603  CB  PRO A  93     6521   6980   6189   -296   1098    680       C  
ATOM    604  CG  PRO A  93     186.017  44.724 512.104  1.00 45.04           C  
ANISOU  604  CG  PRO A  93     5814   5979   5321   -300   1123    840       C  
ATOM    605  CD  PRO A  93     184.521  44.868 512.171  1.00 44.82           C  
ANISOU  605  CD  PRO A  93     5875   5903   5251   -164    962    800       C  
ATOM    606  N   VAL A  94     185.835  44.687 515.419  1.00 32.02           N  
ANISOU  606  N   VAL A  94     3940   4164   4062   -452    930    541       N  
ATOM    607  CA  VAL A  94     186.381  45.076 516.718  1.00 39.89           C  
ANISOU  607  CA  VAL A  94     4858   5068   5231   -581    908    468       C  
ATOM    608  C   VAL A  94     185.537  44.497 517.846  1.00 39.83           C  
ANISOU  608  C   VAL A  94     4809   5069   5257   -519    782    311       C  
ATOM    609  O   VAL A  94     186.055  43.854 518.769  1.00 54.67           O  
ANISOU  609  O   VAL A  94     6572   7002   7197   -574    757    209       O  
ATOM    610  CB  VAL A  94     186.482  46.608 516.821  1.00 48.13           C  
ANISOU  610  CB  VAL A  94     6007   5905   6376   -668    937    562       C  
ATOM    611  CG1 VAL A  94     187.038  47.013 518.178  1.00 33.15           C  
ANISOU  611  CG1 VAL A  94     4039   3910   4646   -805    895    462       C  
ATOM    612  CG2 VAL A  94     187.344  47.161 515.697  1.00 49.88           C  
ANISOU  612  CG2 VAL A  94     6268   6115   6568   -741   1084    738       C  
ATOM    613  N   VAL A  95     184.221  44.714 517.788  1.00 32.94           N  
ANISOU  613  N   VAL A  95     4026   4146   4344   -396    705    299       N  
ATOM    614  CA  VAL A  95     183.331  44.195 518.822  1.00 33.30           C  
ANISOU  614  CA  VAL A  95     4030   4201   4423   -333    607    164       C  
ATOM    615  C   VAL A  95     183.355  42.672 518.839  1.00 30.59           C  
ANISOU  615  C   VAL A  95     3579   4024   4019   -295    588     80       C  
ATOM    616  O   VAL A  95     183.183  42.052 519.895  1.00 40.48           O  
ANISOU  616  O   VAL A  95     4761   5300   5318   -298    542    -29       O  
ATOM    617  CB  VAL A  95     181.904  44.740 518.616  1.00 42.83           C  
ANISOU  617  CB  VAL A  95     5331   5333   5608   -200    541    182       C  
ATOM    618  CG1 VAL A  95     181.011  44.364 519.789  1.00 43.75           C  
ANISOU  618  CG1 VAL A  95     5398   5444   5781   -147    468     51       C  
ATOM    619  CG2 VAL A  95     181.937  46.249 518.428  1.00 42.89           C  
ANISOU  619  CG2 VAL A  95     5467   5158   5672   -223    571    285       C  
ATOM    620  N   CYS A  96     183.575  42.046 517.681  1.00 30.13           N  
ANISOU  620  N   CYS A  96     3520   4078   3851   -254    627    128       N  
ATOM    621  CA  CYS A  96     183.697  40.592 517.637  1.00 39.42           C  
ANISOU  621  CA  CYS A  96     4609   5393   4978   -220    617     43       C  
ATOM    622  C   CYS A  96     184.920  40.123 518.416  1.00 46.57           C  
ANISOU  622  C   CYS A  96     5400   6335   5959   -318    662      0       C  
ATOM    623  O   CYS A  96     184.831  39.209 519.246  1.00 51.01           O  
ANISOU  623  O   CYS A  96     5889   6939   6553   -306    618    -97       O  
ATOM    624  CB  CYS A  96     183.769  40.115 516.186  1.00 43.72           C  
ANISOU  624  CB  CYS A  96     5198   6039   5376   -154    657     96       C  
ATOM    625  SG  CYS A  96     184.356  38.416 516.007  0.78 46.82           S  
ANISOU  625  SG  CYS A  96     5494   6579   5716   -131    685      0       S  
ATOM    626  N   ASP A  97     186.075  40.744 518.161  1.00 49.58           N  
ANISOU  626  N   ASP A  97     5761   6702   6375   -415    750     79       N  
ATOM    627  CA  ASP A  97     187.291  40.365 518.872  1.00 47.68           C  
ANISOU  627  CA  ASP A  97     5389   6507   6220   -507    780     43       C  
ATOM    628  C   ASP A  97     187.162  40.630 520.368  1.00 47.45           C  
ANISOU  628  C   ASP A  97     5333   6403   6294   -560    691    -42       C  
ATOM    629  O   ASP A  97     187.591  39.810 521.190  1.00 47.35           O  
ANISOU  629  O   ASP A  97     5223   6453   6313   -568    656   -118       O  
ATOM    630  CB  ASP A  97     188.491  41.113 518.291  1.00 54.53           C  
ANISOU  630  CB  ASP A  97     6224   7367   7127   -616    893    152       C  
ATOM    631  CG  ASP A  97     188.708  40.813 516.819  1.00 69.24           C  
ANISOU  631  CG  ASP A  97     8123   9321   8864   -557   1004    240       C  
ATOM    632  OD1 ASP A  97     188.365  39.695 516.382  1.00 74.88           O  
ANISOU  632  OD1 ASP A  97     8835  10138   9476   -447    994    184       O  
ATOM    633  OD2 ASP A  97     189.223  41.695 516.099  1.00 73.41           O  
ANISOU  633  OD2 ASP A  97     8691   9811   9392   -620   1107    365       O  
ATOM    634  N   LEU A  98     186.564  41.766 520.740  1.00 48.63           N  
ANISOU  634  N   LEU A  98     5577   6414   6485   -583    655    -31       N  
ATOM    635  CA  LEU A  98     186.373  42.069 522.155  1.00 42.79           C  
ANISOU  635  CA  LEU A  98     4837   5601   5819   -620    575   -124       C  
ATOM    636  C   LEU A  98     185.428  41.070 522.813  1.00 40.66           C  
ANISOU  636  C   LEU A  98     4558   5386   5506   -516    513   -216       C  
ATOM    637  O   LEU A  98     185.599  40.721 523.987  1.00 56.00           O  
ANISOU  637  O   LEU A  98     6460   7341   7477   -536    464   -297       O  
ATOM    638  CB  LEU A  98     185.844  43.494 522.321  1.00 37.57           C  
ANISOU  638  CB  LEU A  98     4301   4767   5208   -645    561    -99       C  
ATOM    639  CG  LEU A  98     186.761  44.628 521.858  1.00 40.93           C  
ANISOU  639  CG  LEU A  98     4751   5094   5707   -775    623     -6       C  
ATOM    640  CD1 LEU A  98     186.083  45.978 522.046  1.00 40.48           C  
ANISOU  640  CD1 LEU A  98     4841   4839   5701   -775    604     12       C  
ATOM    641  CD2 LEU A  98     188.091  44.584 522.596  1.00 37.11           C  
ANISOU  641  CD2 LEU A  98     4145   4638   5316   -922    612    -50       C  
ATOM    642  N   TRP A  99     184.425  40.598 522.070  1.00 27.95           N  
ANISOU  642  N   TRP A  99     2984   3811   3825   -407    512   -203       N  
ATOM    643  CA  TRP A  99     183.487  39.622 522.615  1.00 28.58           C  
ANISOU  643  CA  TRP A  99     3042   3936   3882   -323    464   -282       C  
ATOM    644  C   TRP A  99     184.162  38.271 522.826  1.00 30.78           C  
ANISOU  644  C   TRP A  99     3224   4324   4146   -326    471   -322       C  
ATOM    645  O   TRP A  99     184.064  37.678 523.910  1.00 23.63           O  
ANISOU  645  O   TRP A  99     2286   3432   3261   -320    438   -386       O  
ATOM    646  CB  TRP A  99     182.277  39.498 521.686  1.00 30.18           C  
ANISOU  646  CB  TRP A  99     3291   4149   4029   -220    447   -260       C  
ATOM    647  CG  TRP A  99     181.369  38.344 521.987  1.00 30.00           C  
ANISOU  647  CG  TRP A  99     3220   4183   3994   -151    408   -333       C  
ATOM    648  CD1 TRP A  99     180.690  38.115 523.147  1.00 38.44           C  
ANISOU  648  CD1 TRP A  99     4270   5227   5108   -133    384   -397       C  
ATOM    649  CD2 TRP A  99     181.023  37.273 521.101  1.00 30.70           C  
ANISOU  649  CD2 TRP A  99     3283   4357   4025    -97    394   -348       C  
ATOM    650  NE1 TRP A  99     179.952  36.960 523.043  1.00 39.08           N  
ANISOU  650  NE1 TRP A  99     4302   5367   5181    -83    364   -440       N  
ATOM    651  CE2 TRP A  99     180.139  36.425 521.796  1.00 31.31           C  
ANISOU  651  CE2 TRP A  99     3313   4445   4137    -63    360   -419       C  
ATOM    652  CE3 TRP A  99     181.381  36.945 519.789  1.00 41.93           C  
ANISOU  652  CE3 TRP A  99     4724   5845   5364    -75    413   -312       C  
ATOM    653  CZ2 TRP A  99     179.606  35.271 521.224  1.00 36.83           C  
ANISOU  653  CZ2 TRP A  99     3979   5203   4812    -23    332   -462       C  
ATOM    654  CZ3 TRP A  99     180.851  35.799 519.223  1.00 45.71           C  
ANISOU  654  CZ3 TRP A  99     5182   6389   5796    -22    378   -367       C  
ATOM    655  CH2 TRP A  99     179.974  34.976 519.940  1.00 45.13           C  
ANISOU  655  CH2 TRP A  99     5057   6311   5780     -3    332   -444       C  
ATOM    656  N   LEU A 100     184.864  37.776 521.801  1.00 29.14           N  
ANISOU  656  N   LEU A 100     2981   4195   3898   -324    522   -280       N  
ATOM    657  CA  LEU A 100     185.557  36.495 521.917  1.00 34.49           C  
ANISOU  657  CA  LEU A 100     3570   4965   4568   -309    537   -317       C  
ATOM    658  C   LEU A 100     186.596  36.528 523.033  1.00 50.26           C  
ANISOU  658  C   LEU A 100     5490   6971   6635   -380    521   -336       C  
ATOM    659  O   LEU A 100     186.652  35.624 523.876  1.00 49.41           O  
ANISOU  659  O   LEU A 100     5340   6895   6537   -352    485   -388       O  
ATOM    660  CB  LEU A 100     186.213  36.135 520.583  1.00 31.51           C  
ANISOU  660  CB  LEU A 100     3177   4664   4131   -288    613   -269       C  
ATOM    661  CG  LEU A 100     185.285  35.946 519.383  1.00 33.07           C  
ANISOU  661  CG  LEU A 100     3458   4878   4230   -208    613   -260       C  
ATOM    662  CD1 LEU A 100     186.092  35.805 518.103  1.00 28.74           C  
ANISOU  662  CD1 LEU A 100     2914   4406   3600   -192    706   -205       C  
ATOM    663  CD2 LEU A 100     184.386  34.737 519.589  1.00 33.20           C  
ANISOU  663  CD2 LEU A 100     3470   4912   4231   -136    554   -348       C  
ATOM    664  N   ALA A 101     187.433  37.569 523.050  1.00 58.42           N  
ANISOU  664  N   ALA A 101     6505   7973   7719   -476    540   -293       N  
ATOM    665  CA  ALA A 101     188.419  37.695 524.118  1.00 50.36           C  
ANISOU  665  CA  ALA A 101     5402   6964   6769   -555    497   -322       C  
ATOM    666  C   ALA A 101     187.744  37.800 525.479  1.00 39.51           C  
ANISOU  666  C   ALA A 101     4083   5533   5394   -545    410   -396       C  
ATOM    667  O   ALA A 101     188.239  37.252 526.471  1.00 32.44           O  
ANISOU  667  O   ALA A 101     3133   4684   4509   -548    355   -440       O  
ATOM    668  CB  ALA A 101     189.316  38.908 523.866  1.00 38.68           C  
ANISOU  668  CB  ALA A 101     3895   5439   5361   -682    528   -267       C  
ATOM    669  N   LEU A 102     186.597  38.481 525.539  1.00 38.85           N  
ANISOU  669  N   LEU A 102     4111   5358   5293   -519    401   -408       N  
ATOM    670  CA  LEU A 102     185.907  38.673 526.810  1.00 31.15           C  
ANISOU  670  CA  LEU A 102     3199   4329   4309   -500    344   -479       C  
ATOM    671  C   LEU A 102     185.416  37.346 527.378  1.00 31.52           C  
ANISOU  671  C   LEU A 102     3222   4442   4311   -416    332   -514       C  
ATOM    672  O   LEU A 102     185.786  36.958 528.492  1.00 47.29           O  
ANISOU  672  O   LEU A 102     5204   6468   6295   -421    286   -554       O  
ATOM    673  CB  LEU A 102     184.744  39.650 526.637  1.00 39.89           C  
ANISOU  673  CB  LEU A 102     4416   5326   5416   -467    355   -478       C  
ATOM    674  CG  LEU A 102     183.937  39.923 527.909  1.00 39.38           C  
ANISOU  674  CG  LEU A 102     4424   5203   5336   -431    321   -554       C  
ATOM    675  CD1 LEU A 102     184.838  40.466 529.008  1.00 36.08           C  
ANISOU  675  CD1 LEU A 102     4019   4757   4933   -519    264   -613       C  
ATOM    676  CD2 LEU A 102     182.789  40.882 527.629  1.00 42.09           C  
ANISOU  676  CD2 LEU A 102     4860   5439   5693   -377    342   -549       C  
ATOM    677  N   ASP A 103     184.577  36.629 526.624  1.00 40.57           N  
ANISOU  677  N   ASP A 103     4372   5611   5432   -340    367   -498       N  
ATOM    678  CA  ASP A 103     184.008  35.403 527.180  1.00 42.25           C  
ANISOU  678  CA  ASP A 103     4571   5860   5622   -274    364   -528       C  
ATOM    679  C   ASP A 103     185.052  34.298 527.300  1.00 42.92           C  
ANISOU  679  C   ASP A 103     4579   6022   5706   -269    359   -521       C  
ATOM    680  O   ASP A 103     184.922  33.420 528.162  1.00 56.38           O  
ANISOU  680  O   ASP A 103     6282   7744   7397   -231    344   -538       O  
ATOM    681  CB  ASP A 103     182.810  34.934 526.350  1.00 47.56           C  
ANISOU  681  CB  ASP A 103     5258   6527   6287   -210    388   -525       C  
ATOM    682  CG  ASP A 103     183.206  34.395 524.993  1.00 59.08           C  
ANISOU  682  CG  ASP A 103     6683   8036   7729   -196    411   -498       C  
ATOM    683  OD1 ASP A 103     184.154  34.930 524.393  1.00 68.05           O  
ANISOU  683  OD1 ASP A 103     7804   9191   8861   -237    431   -460       O  
ATOM    684  OD2 ASP A 103     182.559  33.437 524.522  1.00 60.19           O  
ANISOU  684  OD2 ASP A 103     6815   8196   7859   -147    413   -518       O  
ATOM    685  N   TYR A 104     186.098  34.326 526.469  1.00 34.04           N  
ANISOU  685  N   TYR A 104     3391   4944   4598   -298    380   -488       N  
ATOM    686  CA  TYR A 104     187.162  33.336 526.612  1.00 27.74           C  
ANISOU  686  CA  TYR A 104     2505   4222   3813   -278    378   -481       C  
ATOM    687  C   TYR A 104     187.980  33.585 527.876  1.00 36.45           C  
ANISOU  687  C   TYR A 104     3571   5345   4932   -320    307   -495       C  
ATOM    688  O   TYR A 104     188.250  32.653 528.647  1.00 38.12           O  
ANISOU  688  O   TYR A 104     3759   5593   5131   -269    273   -502       O  
ATOM    689  CB  TYR A 104     188.054  33.337 525.371  1.00 23.55           C  
ANISOU  689  CB  TYR A 104     1905   3746   3297   -289    438   -442       C  
ATOM    690  CG  TYR A 104     187.657  32.298 524.344  1.00 26.01           C  
ANISOU  690  CG  TYR A 104     2231   4080   3572   -206    491   -449       C  
ATOM    691  CD1 TYR A 104     186.602  32.523 523.471  1.00 32.04           C  
ANISOU  691  CD1 TYR A 104     3074   4808   4291   -187    509   -453       C  
ATOM    692  CD2 TYR A 104     188.336  31.090 524.253  1.00 37.23           C  
ANISOU  692  CD2 TYR A 104     3590   5554   5003   -142    513   -458       C  
ATOM    693  CE1 TYR A 104     186.235  31.575 522.532  1.00 39.32           C  
ANISOU  693  CE1 TYR A 104     4018   5751   5172   -118    538   -478       C  
ATOM    694  CE2 TYR A 104     187.976  30.136 523.319  1.00 40.23           C  
ANISOU  694  CE2 TYR A 104     4001   5939   5348    -68    557   -483       C  
ATOM    695  CZ  TYR A 104     186.925  30.383 522.462  1.00 43.38           C  
ANISOU  695  CZ  TYR A 104     4483   6306   5695    -63    565   -499       C  
ATOM    696  OH  TYR A 104     186.566  29.436 521.531  1.00 47.86           O  
ANISOU  696  OH  TYR A 104     5088   6878   6220      4    590   -542       O  
ATOM    697  N   VAL A 105     188.377  34.839 528.110  1.00 32.25           N  
ANISOU  697  N   VAL A 105     3043   4783   4428   -411    276   -501       N  
ATOM    698  CA  VAL A 105     189.108  35.173 529.331  1.00 23.21           C  
ANISOU  698  CA  VAL A 105     1873   3656   3291   -461    184   -534       C  
ATOM    699  C   VAL A 105     188.261  34.872 530.562  1.00 33.36           C  
ANISOU  699  C   VAL A 105     3259   4914   4503   -407    141   -577       C  
ATOM    700  O   VAL A 105     188.745  34.288 531.540  1.00 34.38           O  
ANISOU  700  O   VAL A 105     3369   5095   4598   -378     74   -588       O  
ATOM    701  CB  VAL A 105     189.556  36.647 529.302  1.00 24.16           C  
ANISOU  701  CB  VAL A 105     1996   3718   3463   -585    158   -547       C  
ATOM    702  CG1 VAL A 105     189.907  37.128 530.702  1.00 25.02           C  
ANISOU  702  CG1 VAL A 105     2132   3817   3556   -635     43   -614       C  
ATOM    703  CG2 VAL A 105     190.746  36.822 528.374  1.00 40.13           C  
ANISOU  703  CG2 VAL A 105     3885   5795   5567   -654    199   -493       C  
ATOM    704  N   VAL A 106     186.983  35.256 530.528  1.00 40.51           N  
ANISOU  704  N   VAL A 106     4268   5742   5379   -383    183   -593       N  
ATOM    705  CA  VAL A 106     186.103  35.035 531.674  1.00 37.21           C  
ANISOU  705  CA  VAL A 106     3945   5301   4893   -330    172   -628       C  
ATOM    706  C   VAL A 106     185.939  33.545 531.946  1.00 36.48           C  
ANISOU  706  C   VAL A 106     3832   5258   4771   -247    192   -596       C  
ATOM    707  O   VAL A 106     186.015  33.095 533.098  1.00 44.54           O  
ANISOU  707  O   VAL A 106     4893   6304   5728   -213    156   -601       O  
ATOM    708  CB  VAL A 106     184.746  35.726 531.443  1.00 33.53           C  
ANISOU  708  CB  VAL A 106     3565   4751   4426   -310    230   -646       C  
ATOM    709  CG1 VAL A 106     183.707  35.206 532.421  1.00 31.43           C  
ANISOU  709  CG1 VAL A 106     3367   4476   4098   -239    261   -663       C  
ATOM    710  CG2 VAL A 106     184.895  37.235 531.576  1.00 28.20           C  
ANISOU  710  CG2 VAL A 106     2946   3999   3769   -379    200   -686       C  
ATOM    711  N   SER A 107     185.719  32.754 530.893  1.00 28.38           N  
ANISOU  711  N   SER A 107     2758   4240   3784   -213    250   -562       N  
ATOM    712  CA  SER A 107     185.563  31.315 531.077  1.00 32.03           C  
ANISOU  712  CA  SER A 107     3211   4721   4238   -141    273   -534       C  
ATOM    713  C   SER A 107     186.833  30.687 531.638  1.00 34.80           C  
ANISOU  713  C   SER A 107     3505   5139   4580   -117    213   -511       C  
ATOM    714  O   SER A 107     186.771  29.834 532.533  1.00 45.85           O  
ANISOU  714  O   SER A 107     4940   6543   5937    -58    199   -486       O  
ATOM    715  CB  SER A 107     185.181  30.659 529.753  1.00 39.84           C  
ANISOU  715  CB  SER A 107     4166   5698   5273   -116    331   -524       C  
ATOM    716  OG  SER A 107     183.965  31.187 529.251  1.00 50.31           O  
ANISOU  716  OG  SER A 107     5534   6974   6608   -127    366   -542       O  
ATOM    717  N   ASN A 108     187.997  31.098 531.125  1.00 35.92           N  
ANISOU  717  N   ASN A 108     3551   5332   4764   -157    179   -509       N  
ATOM    718  CA  ASN A 108     189.256  30.587 531.658  1.00 45.75           C  
ANISOU  718  CA  ASN A 108     4713   6654   6017   -130    108   -488       C  
ATOM    719  C   ASN A 108     189.404  30.930 533.136  1.00 52.78           C  
ANISOU  719  C   ASN A 108     5659   7562   6833   -138      9   -507       C  
ATOM    720  O   ASN A 108     189.803  30.081 533.945  1.00 55.90           O  
ANISOU  720  O   ASN A 108     6055   7999   7186    -65    -44   -476       O  
ATOM    721  CB  ASN A 108     190.429  31.147 530.853  1.00 44.98           C  
ANISOU  721  CB  ASN A 108     4481   6613   5994   -190    101   -484       C  
ATOM    722  CG  ASN A 108     191.721  30.400 531.108  1.00 41.41           C  
ANISOU  722  CG  ASN A 108     3901   6253   5579   -137     47   -455       C  
ATOM    723  OD1 ASN A 108     192.078  29.484 530.366  1.00 34.89           O  
ANISOU  723  OD1 ASN A 108     3011   5453   4793    -62    108   -426       O  
ATOM    724  ND2 ASN A 108     192.431  30.786 532.162  1.00 45.88           N  
ANISOU  724  ND2 ASN A 108     4429   6871   6131   -168    -75   -469       N  
ATOM    725  N   ALA A 109     189.071  32.170 533.507  1.00 23.84           N  
ANISOU  725  N   ALA A 109     2056   3862   3141   -217    -19   -559       N  
ATOM    726  CA  ALA A 109     189.146  32.574 534.907  1.00 28.09           C  
ANISOU  726  CA  ALA A 109     2674   4414   3585   -223   -115   -599       C  
ATOM    727  C   ALA A 109     188.190  31.769 535.776  1.00 34.49           C  
ANISOU  727  C   ALA A 109     3606   5203   4293   -131    -74   -573       C  
ATOM    728  O   ALA A 109     188.495  31.495 536.942  1.00 49.58           O  
ANISOU  728  O   ALA A 109     5572   7160   6105    -89   -152   -570       O  
ATOM    729  CB  ALA A 109     188.856  34.069 535.038  1.00 25.02           C  
ANISOU  729  CB  ALA A 109     2350   3963   3194   -319   -135   -673       C  
ATOM    730  N   SER A 110     187.033  31.382 535.234  1.00 41.08           N  
ANISOU  730  N   SER A 110     4483   5975   5151   -102     46   -551       N  
ATOM    731  CA  SER A 110     186.113  30.548 536.001  1.00 40.14           C  
ANISOU  731  CA  SER A 110     4461   5831   4959    -28    107   -513       C  
ATOM    732  C   SER A 110     186.670  29.142 536.185  1.00 47.85           C  
ANISOU  732  C   SER A 110     5407   6839   5935     51     93   -437       C  
ATOM    733  O   SER A 110     186.539  28.551 537.266  1.00 60.80           O  
ANISOU  733  O   SER A 110     7132   8490   7479    113     85   -393       O  
ATOM    734  CB  SER A 110     184.747  30.503 535.319  1.00 32.32           C  
ANISOU  734  CB  SER A 110     3492   4767   4022    -30    229   -513       C  
ATOM    735  OG  SER A 110     184.834  29.900 534.040  1.00 50.62           O  
ANISOU  735  OG  SER A 110     5722   7072   6439    -31    263   -492       O  
ATOM    736  N   VAL A 111     187.300  28.591 535.143  1.00 46.19           N  
ANISOU  736  N   VAL A 111     5087   6640   5823     60     98   -417       N  
ATOM    737  CA  VAL A 111     187.895  27.260 535.255  1.00 43.22           C  
ANISOU  737  CA  VAL A 111     4682   6279   5462    150     87   -349       C  
ATOM    738  C   VAL A 111     188.993  27.257 536.312  1.00 51.70           C  
ANISOU  738  C   VAL A 111     5742   7438   6462    191    -44   -328       C  
ATOM    739  O   VAL A 111     188.998  26.426 537.230  1.00 59.46           O  
ANISOU  739  O   VAL A 111     6799   8424   7371    276    -65   -263       O  
ATOM    740  CB  VAL A 111     188.424  26.790 533.889  1.00 36.72           C  
ANISOU  740  CB  VAL A 111     3745   5455   4753    161    122   -351       C  
ATOM    741  CG1 VAL A 111     189.213  25.499 534.042  1.00 29.33           C  
ANISOU  741  CG1 VAL A 111     2772   4531   3840    270    101   -289       C  
ATOM    742  CG2 VAL A 111     187.272  26.599 532.915  1.00 45.43           C  
ANISOU  742  CG2 VAL A 111     4879   6476   5907    135    231   -373       C  
ATOM    743  N   MET A 112     189.939  28.195 536.204  1.00 45.31           N  
ANISOU  743  N   MET A 112     4839   6701   5675    128   -140   -378       N  
ATOM    744  CA  MET A 112     190.992  28.276 537.209  1.00 36.09           C  
ANISOU  744  CA  MET A 112     3642   5627   4443    155   -293   -373       C  
ATOM    745  C   MET A 112     190.448  28.644 538.584  1.00 40.00           C  
ANISOU  745  C   MET A 112     4299   6124   4775    163   -344   -390       C  
ATOM    746  O   MET A 112     191.092  28.335 539.592  1.00 41.24           O  
ANISOU  746  O   MET A 112     4480   6354   4836    226   -465   -363       O  
ATOM    747  CB  MET A 112     192.067  29.273 536.774  1.00 27.99           C  
ANISOU  747  CB  MET A 112     2466   4670   3499     58   -382   -432       C  
ATOM    748  CG  MET A 112     192.909  28.782 535.605  1.00 38.06           C  
ANISOU  748  CG  MET A 112     3565   5979   4915     78   -341   -401       C  
ATOM    749  SD  MET A 112     194.523  29.578 535.494  0.55 44.32           S  
ANISOU  749  SD  MET A 112     4142   6893   5806     -5   -472   -433       S  
ATOM    750  CE  MET A 112     194.042  31.278 535.217  1.00 41.16           C  
ANISOU  750  CE  MET A 112     3792   6427   5419   -188   -455   -521       C  
ATOM    751  N   ASN A 113     189.280  29.287 538.649  1.00 34.79           N  
ANISOU  751  N   ASN A 113     3752   5393   4074    113   -253   -434       N  
ATOM    752  CA  ASN A 113     188.632  29.509 539.937  1.00 37.36           C  
ANISOU  752  CA  ASN A 113     4247   5716   4231    142   -260   -445       C  
ATOM    753  C   ASN A 113     188.170  28.190 540.545  1.00 34.39           C  
ANISOU  753  C   ASN A 113     3961   5324   3780    256   -194   -334       C  
ATOM    754  O   ASN A 113     188.373  27.944 541.741  1.00 40.11           O  
ANISOU  754  O   ASN A 113     4792   6100   4349    323   -263   -300       O  
ATOM    755  CB  ASN A 113     187.456  30.472 539.772  1.00 49.91           C  
ANISOU  755  CB  ASN A 113     5917   7230   5817     79   -156   -514       C  
ATOM    756  CG  ASN A 113     186.974  31.046 541.092  1.00 68.29           C  
ANISOU  756  CG  ASN A 113     8413   9567   7966     98   -175   -562       C  
ATOM    757  OD1 ASN A 113     187.205  30.476 542.159  1.00 74.90           O  
ANISOU  757  OD1 ASN A 113     9340  10461   8659    175   -226   -517       O  
ATOM    758  ND2 ASN A 113     186.296  32.184 541.024  1.00 75.09           N  
ANISOU  758  ND2 ASN A 113     9330  10373   8827     41   -128   -652       N  
ATOM    759  N   LEU A 114     187.551  27.327 539.733  1.00 34.52           N  
ANISOU  759  N   LEU A 114     3948   5264   3903    276    -62   -275       N  
ATOM    760  CA  LEU A 114     187.183  25.998 540.213  1.00 36.31           C  
ANISOU  760  CA  LEU A 114     4252   5450   4092    371      7   -161       C  
ATOM    761  C   LEU A 114     188.413  25.219 540.661  1.00 38.98           C  
ANISOU  761  C   LEU A 114     4560   5853   4399    468   -120    -90       C  
ATOM    762  O   LEU A 114     188.374  24.510 541.676  1.00 43.80           O  
ANISOU  762  O   LEU A 114     5285   6468   4887    559   -129      3       O  
ATOM    763  CB  LEU A 114     186.431  25.237 539.122  1.00 35.20           C  
ANISOU  763  CB  LEU A 114     4066   5206   4101    357    145   -133       C  
ATOM    764  CG  LEU A 114     185.124  25.868 538.644  1.00 36.90           C  
ANISOU  764  CG  LEU A 114     4297   5361   4362    276    264   -190       C  
ATOM    765  CD1 LEU A 114     184.480  25.014 537.564  1.00 36.54           C  
ANISOU  765  CD1 LEU A 114     4198   5224   4462    262    367   -170       C  
ATOM    766  CD2 LEU A 114     184.177  26.069 539.814  1.00 27.72           C  
ANISOU  766  CD2 LEU A 114     3273   4191   3070    290    339   -166       C  
ATOM    767  N   LEU A 115     189.517  25.342 539.919  1.00 34.60           N  
ANISOU  767  N   LEU A 115     3844   5351   3949    458   -212   -123       N  
ATOM    768  CA  LEU A 115     190.767  24.726 540.354  1.00 44.84           C  
ANISOU  768  CA  LEU A 115     5080   6729   5229    559   -350    -64       C  
ATOM    769  C   LEU A 115     191.210  25.276 541.704  1.00 42.15           C  
ANISOU  769  C   LEU A 115     4817   6490   4707    579   -506    -77       C  
ATOM    770  O   LEU A 115     191.680  24.524 542.567  1.00 48.56           O  
ANISOU  770  O   LEU A 115     5686   7345   5419    698   -591     14       O  
ATOM    771  CB  LEU A 115     191.855  24.945 539.302  1.00 49.77           C  
ANISOU  771  CB  LEU A 115     5494   7408   6008    531   -407   -110       C  
ATOM    772  CG  LEU A 115     191.660  24.256 537.950  1.00 48.29           C  
ANISOU  772  CG  LEU A 115     5231   7139   5979    542   -272    -99       C  
ATOM    773  CD1 LEU A 115     192.713  24.720 536.955  1.00 44.72           C  
ANISOU  773  CD1 LEU A 115     4578   6759   5653    502   -311   -153       C  
ATOM    774  CD2 LEU A 115     191.703  22.746 538.109  1.00 34.23           C  
ANISOU  774  CD2 LEU A 115     3499   5293   4214    684   -234      8       C  
ATOM    775  N   ILE A 116     191.060  26.589 541.908  1.00 32.80           N  
ANISOU  775  N   ILE A 116     3652   5339   3472    469   -552   -190       N  
ATOM    776  CA  ILE A 116     191.446  27.201 543.177  1.00 33.92           C  
ANISOU  776  CA  ILE A 116     3885   5573   3430    477   -711   -232       C  
ATOM    777  C   ILE A 116     190.615  26.633 544.320  1.00 41.70           C  
ANISOU  777  C   ILE A 116     5093   6536   4214    572   -647   -151       C  
ATOM    778  O   ILE A 116     191.143  26.323 545.396  1.00 42.10           O  
ANISOU  778  O   ILE A 116     5227   6670   4099    665   -780   -103       O  
ATOM    779  CB  ILE A 116     191.321  28.734 543.091  1.00 33.59           C  
ANISOU  779  CB  ILE A 116     3841   5533   3389    334   -749   -384       C  
ATOM    780  CG1 ILE A 116     192.461  29.319 542.256  1.00 39.11           C  
ANISOU  780  CG1 ILE A 116     4320   6283   4259    242   -857   -448       C  
ATOM    781  CG2 ILE A 116     191.307  29.353 544.479  1.00 35.34           C  
ANISOU  781  CG2 ILE A 116     4227   5816   3386    346   -870   -446       C  
ATOM    782  CD1 ILE A 116     192.384  30.822 542.087  1.00 36.66           C  
ANISOU  782  CD1 ILE A 116     4007   5946   3977     91   -889   -586       C  
ATOM    783  N   ILE A 117     189.306  26.482 544.108  1.00 37.70           N  
ANISOU  783  N   ILE A 117     4683   5925   3718    552   -443   -128       N  
ATOM    784  CA  ILE A 117     188.446  25.924 545.151  1.00 36.72           C  
ANISOU  784  CA  ILE A 117     4761   5774   3416    633   -343    -36       C  
ATOM    785  C   ILE A 117     188.845  24.484 545.453  1.00 49.41           C  
ANISOU  785  C   ILE A 117     6395   7371   5006    764   -352    128       C  
ATOM    786  O   ILE A 117     188.982  24.087 546.618  1.00 62.42           O  
ANISOU  786  O   ILE A 117     8193   9071   6455    866   -407    213       O  
ATOM    787  CB  ILE A 117     186.967  26.023 544.739  1.00 36.63           C  
ANISOU  787  CB  ILE A 117     4801   5653   3466    575   -114    -41       C  
ATOM    788  CG1 ILE A 117     186.579  27.480 544.484  1.00 35.48           C  
ANISOU  788  CG1 ILE A 117     4640   5509   3333    468   -110   -197       C  
ATOM    789  CG2 ILE A 117     186.074  25.409 545.808  1.00 34.38           C  
ANISOU  789  CG2 ILE A 117     4708   5342   3012    651     18     68       C  
ATOM    790  CD1 ILE A 117     185.139  27.663 544.058  1.00 31.17           C  
ANISOU  790  CD1 ILE A 117     4118   4868   2856    422     99   -208       C  
ATOM    791  N   SER A 118     189.047  23.683 544.403  1.00 50.95           N  
ANISOU  791  N   SER A 118     6460   7495   5403    774   -299    177       N  
ATOM    792  CA  SER A 118     189.374  22.272 544.592  1.00 44.60           C  
ANISOU  792  CA  SER A 118     5689   6647   4612    905   -291    332       C  
ATOM    793  C   SER A 118     190.684  22.105 545.354  1.00 49.67           C  
ANISOU  793  C   SER A 118     6314   7415   5144   1019   -514    374       C  
ATOM    794  O   SER A 118     190.762  21.331 546.317  1.00 55.52           O  
ANISOU  794  O   SER A 118     7195   8161   5737   1146   -541    508       O  
ATOM    795  CB  SER A 118     189.441  21.566 543.238  1.00 42.90           C  
ANISOU  795  CB  SER A 118     5331   6331   4638    892   -208    339       C  
ATOM    796  OG  SER A 118     188.211  21.682 542.542  1.00 37.52           O  
ANISOU  796  OG  SER A 118     4662   5541   4053    789    -25    299       O  
ATOM    797  N   PHE A 119     191.729  22.827 544.939  1.00 54.86           N  
ANISOU  797  N   PHE A 119     6794   8175   5874    976   -678    268       N  
ATOM    798  CA  PHE A 119     193.006  22.732 545.639  1.00 63.87           C  
ANISOU  798  CA  PHE A 119     7884   9455   6930   1076   -914    295       C  
ATOM    799  C   PHE A 119     192.921  23.300 547.051  1.00 61.08           C  
ANISOU  799  C   PHE A 119     7710   9198   6301   1098  -1033    279       C  
ATOM    800  O   PHE A 119     193.616  22.817 547.953  1.00 59.57           O  
ANISOU  800  O   PHE A 119     7573   9096   5966   1231  -1194    363       O  
ATOM    801  CB  PHE A 119     194.100  23.446 544.847  1.00 39.45           C  
ANISOU  801  CB  PHE A 119     4536   6452   4000   1000  -1048    179       C  
ATOM    802  CG  PHE A 119     194.688  22.616 543.744  1.00 42.89           C  
ANISOU  802  CG  PHE A 119     4790   6847   4658   1058   -999    228       C  
ATOM    803  CD1 PHE A 119     195.586  21.600 544.030  1.00 44.92           C  
ANISOU  803  CD1 PHE A 119     4994   7145   4928   1231  -1102    342       C  
ATOM    804  CD2 PHE A 119     194.352  22.853 542.422  1.00 36.87           C  
ANISOU  804  CD2 PHE A 119     3919   6007   4081    954   -851    159       C  
ATOM    805  CE1 PHE A 119     196.133  20.833 543.019  1.00 42.37           C  
ANISOU  805  CE1 PHE A 119     4511   6780   4808   1301  -1045    376       C  
ATOM    806  CE2 PHE A 119     194.895  22.090 541.407  1.00 45.24           C  
ANISOU  806  CE2 PHE A 119     4830   7034   5325   1018   -797    192       C  
ATOM    807  CZ  PHE A 119     195.787  21.079 541.706  1.00 45.20           C  
ANISOU  807  CZ  PHE A 119     4771   7063   5339   1192   -887    296       C  
ATOM    808  N   ASP A 120     192.083  24.317 547.260  1.00 55.72           N  
ANISOU  808  N   ASP A 120     7130   8503   5536    981   -961    168       N  
ATOM    809  CA  ASP A 120     191.916  24.878 548.597  1.00 56.26           C  
ANISOU  809  CA  ASP A 120     7396   8656   5322   1007  -1053    135       C  
ATOM    810  C   ASP A 120     191.310  23.851 549.546  1.00 51.90           C  
ANISOU  810  C   ASP A 120     7072   8072   4576   1149   -953    311       C  
ATOM    811  O   ASP A 120     191.795  23.661 550.669  1.00 46.39           O  
ANISOU  811  O   ASP A 120     6503   7478   3647   1262  -1106    368       O  
ATOM    812  CB  ASP A 120     191.047  26.135 548.531  1.00 63.83           C  
ANISOU  812  CB  ASP A 120     8421   9580   6253    867   -958    -20       C  
ATOM    813  CG  ASP A 120     190.805  26.750 549.897  1.00 68.51           C  
ANISOU  813  CG  ASP A 120     9239  10250   6542    898  -1032    -76       C  
ATOM    814  OD1 ASP A 120     191.750  27.341 550.459  1.00 71.08           O  
ANISOU  814  OD1 ASP A 120     9549  10695   6764    894  -1279   -169       O  
ATOM    815  OD2 ASP A 120     189.670  26.642 550.406  1.00 64.22           O  
ANISOU  815  OD2 ASP A 120     8886   9652   5864    927   -842    -31       O  
ATOM    816  N   ARG A 121     190.247  23.172 549.107  1.00 55.04           N  
ANISOU  816  N   ARG A 121     7522   8325   5064   1142   -698    405       N  
ATOM    817  CA  ARG A 121     189.644  22.137 549.941  1.00 55.17           C  
ANISOU  817  CA  ARG A 121     7747   8289   4927   1261   -573    592       C  
ATOM    818  C   ARG A 121     190.592  20.959 550.132  1.00 63.14           C  
ANISOU  818  C   ARG A 121     8738   9310   5944   1420   -695    753       C  
ATOM    819  O   ARG A 121     190.672  20.388 551.228  1.00 68.37           O  
ANISOU  819  O   ARG A 121     9588  10010   6381   1556   -735    893       O  
ATOM    820  CB  ARG A 121     188.325  21.675 549.324  1.00 54.40           C  
ANISOU  820  CB  ARG A 121     7671   8026   4973   1193   -280    647       C  
ATOM    821  CG  ARG A 121     187.572  20.653 550.153  1.00 64.48           C  
ANISOU  821  CG  ARG A 121     9158   9226   6115   1286   -111    846       C  
ATOM    822  CD  ARG A 121     187.119  21.233 551.479  1.00 80.41           C  
ANISOU  822  CD  ARG A 121    11399  11338   7813   1323    -92    847       C  
ATOM    823  NE  ARG A 121     186.332  20.271 552.242  1.00 83.98           N  
ANISOU  823  NE  ARG A 121    12055  11715   8140   1402    106   1053       N  
ATOM    824  CZ  ARG A 121     185.809  20.514 553.439  1.00 85.63           C  
ANISOU  824  CZ  ARG A 121    12490  11990   8055   1456    182   1101       C  
ATOM    825  NH1 ARG A 121     185.106  19.576 554.058  1.00 92.82           N  
ANISOU  825  NH1 ARG A 121    13573  12822   8873   1520    386   1310       N  
ATOM    826  NH2 ARG A 121     185.988  21.694 554.016  1.00 86.66           N  
ANISOU  826  NH2 ARG A 121    12683  12260   7984   1445     63    940       N  
ATOM    827  N   TYR A 122     191.322  20.585 549.076  1.00 59.90           N  
ANISOU  827  N   TYR A 122     8108   8867   5782   1419   -750    738       N  
ATOM    828  CA  TYR A 122     192.282  19.491 549.182  1.00 54.53           C  
ANISOU  828  CA  TYR A 122     7388   8194   5135   1586   -868    880       C  
ATOM    829  C   TYR A 122     193.352  19.793 550.224  1.00 59.63           C  
ANISOU  829  C   TYR A 122     8059   9029   5570   1694  -1153    883       C  
ATOM    830  O   TYR A 122     193.698  18.930 551.040  1.00 51.12           O  
ANISOU  830  O   TYR A 122     7107   7969   4348   1868  -1228   1051       O  
ATOM    831  CB  TYR A 122     192.917  19.223 547.816  1.00 51.30           C  
ANISOU  831  CB  TYR A 122     6724   7738   5029   1562   -874    828       C  
ATOM    832  CG  TYR A 122     194.011  18.178 547.829  1.00 57.67           C  
ANISOU  832  CG  TYR A 122     7454   8558   5899   1747  -1003    953       C  
ATOM    833  CD1 TYR A 122     193.706  16.824 547.882  1.00 66.94           C  
ANISOU  833  CD1 TYR A 122     8747   9576   7111   1874   -879   1134       C  
ATOM    834  CD2 TYR A 122     195.349  18.546 547.773  1.00 52.55           C  
ANISOU  834  CD2 TYR A 122     6606   8070   5292   1794  -1244    890       C  
ATOM    835  CE1 TYR A 122     194.703  15.867 547.889  1.00 66.81           C  
ANISOU  835  CE1 TYR A 122     8666   9557   7160   2063   -993   1249       C  
ATOM    836  CE2 TYR A 122     196.352  17.596 547.780  1.00 59.79           C  
ANISOU  836  CE2 TYR A 122     7433   9005   6278   1982  -1361   1004       C  
ATOM    837  CZ  TYR A 122     196.024  16.258 547.838  1.00 68.29           C  
ANISOU  837  CZ  TYR A 122     8646   9920   7383   2126  -1234   1184       C  
ATOM    838  OH  TYR A 122     197.020  15.308 547.844  1.00 81.98           O  
ANISOU  838  OH  TYR A 122    10298  11659   9193   2332  -1347   1301       O  
ATOM    839  N   PHE A 123     193.884  21.018 550.218  1.00 58.88           N  
ANISOU  839  N   PHE A 123     7849   9069   5453   1591  -1323    699       N  
ATOM    840  CA  PHE A 123     194.859  21.406 551.229  1.00 57.93           C  
ANISOU  840  CA  PHE A 123     7748   9136   5129   1669  -1617    673       C  
ATOM    841  C   PHE A 123     194.227  21.584 552.603  1.00 64.14           C  
ANISOU  841  C   PHE A 123     8841   9969   5562   1723  -1616    715       C  
ATOM    842  O   PHE A 123     194.929  21.473 553.613  1.00 72.18           O  
ANISOU  842  O   PHE A 123     9944  11124   6356   1850  -1844    762       O  
ATOM    843  CB  PHE A 123     195.573  22.691 550.807  1.00 65.77           C  
ANISOU  843  CB  PHE A 123     8529  10239   6220   1518  -1792    454       C  
ATOM    844  CG  PHE A 123     196.498  22.512 549.636  1.00 69.88           C  
ANISOU  844  CG  PHE A 123     8737  10765   7049   1495  -1842    428       C  
ATOM    845  CD1 PHE A 123     197.175  21.318 549.447  1.00 67.60           C  
ANISOU  845  CD1 PHE A 123     8359  10469   6859   1667  -1880    580       C  
ATOM    846  CD2 PHE A 123     196.685  23.535 548.721  1.00 67.04           C  
ANISOU  846  CD2 PHE A 123     8180  10412   6879   1312  -1837    256       C  
ATOM    847  CE1 PHE A 123     198.026  21.149 548.371  1.00 66.26           C  
ANISOU  847  CE1 PHE A 123     7900  10309   6965   1661  -1905    552       C  
ATOM    848  CE2 PHE A 123     197.534  23.372 547.642  1.00 70.45           C  
ANISOU  848  CE2 PHE A 123     8329  10858   7581   1295  -1859    240       C  
ATOM    849  CZ  PHE A 123     198.205  22.178 547.467  1.00 71.57           C  
ANISOU  849  CZ  PHE A 123     8376  11003   7813   1472  -1889    383       C  
ATOM    850  N   CYS A 124     192.921  21.856 552.665  1.00 65.50           N  
ANISOU  850  N   CYS A 124     9176  10041   5672   1638  -1366    698       N  
ATOM    851  CA  CYS A 124     192.252  21.926 553.959  1.00 67.88           C  
ANISOU  851  CA  CYS A 124     9780  10382   5630   1706  -1318    757       C  
ATOM    852  C   CYS A 124     192.111  20.544 554.587  1.00 75.09           C  
ANISOU  852  C   CYS A 124    10869  11241   6421   1890  -1241   1022       C  
ATOM    853  O   CYS A 124     192.236  20.398 555.808  1.00 78.87           O  
ANISOU  853  O   CYS A 124    11569  11818   6580   2019  -1338   1109       O  
ATOM    854  CB  CYS A 124     190.883  22.592 553.813  1.00 70.54           C  
ANISOU  854  CB  CYS A 124    10216  10628   5960   1572  -1051    670       C  
ATOM    855  SG  CYS A 124     190.923  24.402 553.785  1.00 84.73           S  
ANISOU  855  SG  CYS A 124    11965  12511   7719   1405  -1167    370       S  
ATOM    856  N   VAL A 125     191.854  19.517 553.771  1.00 75.24           N  
ANISOU  856  N   VAL A 125    10807  11096   6683   1908  -1069   1154       N  
ATOM    857  CA  VAL A 125     191.659  18.173 554.308  1.00 68.50           C  
ANISOU  857  CA  VAL A 125    10130  10151   5745   2071   -971   1415       C  
ATOM    858  C   VAL A 125     192.962  17.390 554.444  1.00 69.83           C  
ANISOU  858  C   VAL A 125    10223  10380   5932   2256  -1215   1531       C  
ATOM    859  O   VAL A 125     193.027  16.451 555.249  1.00 72.19           O  
ANISOU  859  O   VAL A 125    10713  10654   6062   2431  -1219   1750       O  
ATOM    860  CB  VAL A 125     190.669  17.365 553.448  1.00 63.66           C  
ANISOU  860  CB  VAL A 125     9499   9308   5382   2002   -659   1508       C  
ATOM    861  CG1 VAL A 125     189.301  18.045 553.417  1.00 69.38           C  
ANISOU  861  CG1 VAL A 125    10301   9979   6080   1842   -410   1422       C  
ATOM    862  CG2 VAL A 125     191.217  17.167 552.047  1.00 62.69           C  
ANISOU  862  CG2 VAL A 125     9095   9112   5613   1948   -691   1425       C  
ATOM    863  N   THR A 126     194.000  17.743 553.686  1.00 66.44           N  
ANISOU  863  N   THR A 126     9514  10026   5703   2229  -1412   1400       N  
ATOM    864  CA  THR A 126     195.264  17.021 553.759  1.00 66.82           C  
ANISOU  864  CA  THR A 126     9451  10140   5797   2413  -1643   1501       C  
ATOM    865  C   THR A 126     196.287  17.687 554.666  1.00 74.46           C  
ANISOU  865  C   THR A 126    10401  11352   6540   2485  -1991   1430       C  
ATOM    866  O   THR A 126     197.197  17.003 555.148  1.00 79.95           O  
ANISOU  866  O   THR A 126    11085  12123   7168   2684  -2195   1563       O  
ATOM    867  CB  THR A 126     195.877  16.854 552.362  1.00 69.54           C  
ANISOU  867  CB  THR A 126     9480  10427   6515   2368  -1641   1422       C  
ATOM    868  OG1 THR A 126     196.035  18.139 551.749  1.00 70.55           O  
ANISOU  868  OG1 THR A 126     9413  10647   6748   2172  -1699   1179       O  
ATOM    869  CG2 THR A 126     194.995  15.970 551.489  1.00 78.76           C  
ANISOU  869  CG2 THR A 126    10676  11348   7900   2334  -1334   1508       C  
ATOM    870  N   LYS A 127     196.165  18.990 554.909  1.00 74.91           N  
ANISOU  870  N   LYS A 127    10453  11526   6483   2332  -2073   1222       N  
ATOM    871  CA  LYS A 127     197.094  19.733 555.760  1.00 73.86           C  
ANISOU  871  CA  LYS A 127    10304  11621   6140   2367  -2419   1116       C  
ATOM    872  C   LYS A 127     196.304  20.528 556.793  1.00 80.23           C  
ANISOU  872  C   LYS A 127    11397  12485   6601   2312  -2389   1038       C  
ATOM    873  O   LYS A 127     196.202  21.757 556.706  1.00 81.17           O  
ANISOU  873  O   LYS A 127    11469  12661   6712   2142  -2439    810       O  
ATOM    874  CB  LYS A 127     197.984  20.653 554.924  1.00 64.68           C  
ANISOU  874  CB  LYS A 127     8801  10549   5226   2219  -2595    897       C  
ATOM    875  CG  LYS A 127     198.748  19.944 553.817  1.00 63.22           C  
ANISOU  875  CG  LYS A 127     8317  10313   5389   2268  -2593    955       C  
ATOM    876  CD  LYS A 127     199.556  20.925 552.982  1.00 70.03           C  
ANISOU  876  CD  LYS A 127     8847  11266   6494   2102  -2728    744       C  
ATOM    877  CE  LYS A 127     200.300  20.211 551.865  1.00 77.90           C  
ANISOU  877  CE  LYS A 127     9552  12221   7825   2164  -2696    803       C  
ATOM    878  NZ  LYS A 127     201.072  21.155 551.010  1.00 73.69           N  
ANISOU  878  NZ  LYS A 127     8690  11775   7535   1995  -2794    615       N  
ATOM    879  N   PRO A 128     195.731  19.852 557.795  1.00 78.76           N  
ANISOU  879  N   PRO A 128    11512  12261   6151   2435  -2280   1221       N  
ATOM    880  CA  PRO A 128     194.915  20.571 558.786  1.00 82.65           C  
ANISOU  880  CA  PRO A 128    12271  12781   6351   2362  -2190   1142       C  
ATOM    881  C   PRO A 128     195.730  21.393 559.767  1.00 81.88           C  
ANISOU  881  C   PRO A 128    12187  12843   6081   2314  -2483    986       C  
ATOM    882  O   PRO A 128     195.187  22.335 560.358  1.00 78.97           O  
ANISOU  882  O   PRO A 128    11973  12509   5524   2214  -2445    835       O  
ATOM    883  CB  PRO A 128     194.156  19.444 559.508  1.00 83.71           C  
ANISOU  883  CB  PRO A 128    12678  12804   6325   2490  -1958   1407       C  
ATOM    884  CG  PRO A 128     194.382  18.202 558.677  1.00 78.76           C  
ANISOU  884  CG  PRO A 128    11933  12051   5942   2605  -1885   1609       C  
ATOM    885  CD  PRO A 128     195.708  18.399 558.023  1.00 75.15           C  
ANISOU  885  CD  PRO A 128    11158  11692   5702   2613  -2179   1502       C  
ATOM    886  N   LEU A 129     197.008  21.073 559.962  1.00 84.65           N  
ANISOU  886  N   LEU A 129    12377  13286   6500   2380  -2767   1016       N  
ATOM    887  CA  LEU A 129     197.839  21.738 560.955  1.00 82.29           C  
ANISOU  887  CA  LEU A 129    12090  13139   6036   2340  -3058    894       C  
ATOM    888  C   LEU A 129     198.684  22.864 560.374  1.00 78.14           C  
ANISOU  888  C   LEU A 129    11281  12703   5705   2168  -3288    642       C  
ATOM    889  O   LEU A 129     199.420  23.515 561.123  1.00 82.36           O  
ANISOU  889  O   LEU A 129    11801  13359   6133   2105  -3541    521       O  
ATOM    890  CB  LEU A 129     198.751  20.716 561.641  1.00 89.37           C  
ANISOU  890  CB  LEU A 129    12987  14092   6876   2513  -3242   1089       C  
ATOM    891  CG  LEU A 129     198.065  19.489 562.247  1.00 91.52           C  
ANISOU  891  CG  LEU A 129    13529  14263   6981   2686  -3032   1366       C  
ATOM    892  CD1 LEU A 129     199.094  18.514 562.799  1.00 93.49           C  
ANISOU  892  CD1 LEU A 129    13742  14564   7215   2857  -3241   1548       C  
ATOM    893  CD2 LEU A 129     197.081  19.903 563.329  1.00 90.45           C  
ANISOU  893  CD2 LEU A 129    13726  14136   6503   2656  -2883   1347       C  
ATOM    894  N   THR A 130     198.599  23.112 559.076  1.00 83.10           N  
ANISOU  894  N   THR A 130    11687  13272   6616   2084  -3203    563       N  
ATOM    895  CA  THR A 130     199.448  24.113 558.437  1.00 87.30           C  
ANISOU  895  CA  THR A 130    11923  13872   7376   1910  -3400    346       C  
ATOM    896  C   THR A 130     198.691  25.017 557.477  1.00 89.82           C  
ANISOU  896  C   THR A 130    12186  14115   7826   1748  -3231    172       C  
ATOM    897  O   THR A 130     198.933  26.226 557.462  1.00 88.31           O  
ANISOU  897  O   THR A 130    11925  13957   7674   1565  -3345    -50       O  
ATOM    898  CB  THR A 130     200.603  23.416 557.693  1.00 87.35           C  
ANISOU  898  CB  THR A 130    11598  13912   7679   1978  -3536    435       C  
ATOM    899  OG1 THR A 130     201.381  22.652 558.622  1.00103.17           O  
ANISOU  899  OG1 THR A 130    13644  15992   9565   2127  -3719    585       O  
ATOM    900  CG2 THR A 130     201.501  24.435 557.012  1.00 75.75           C  
ANISOU  900  CG2 THR A 130     9803  12507   6469   1782  -3710    228       C  
ATOM    901  N   TYR A 131     197.774  24.466 556.678  1.00 88.34           N  
ANISOU  901  N   TYR A 131    12033  13821   7713   1806  -2962    272       N  
ATOM    902  CA  TYR A 131     197.111  25.277 555.660  1.00 80.23           C  
ANISOU  902  CA  TYR A 131    10910  12690   6885   1621  -2773    121       C  
ATOM    903  C   TYR A 131     196.107  26.269 556.241  1.00 74.39           C  
ANISOU  903  C   TYR A 131    10425  11918   5922   1523  -2662    -27       C  
ATOM    904  O   TYR A 131     196.115  27.436 555.814  1.00 81.98           O  
ANISOU  904  O   TYR A 131    11290  12859   7000   1338  -2691   -240       O  
ATOM    905  CB  TYR A 131     196.463  24.368 554.612  1.00 89.40           C  
ANISOU  905  CB  TYR A 131    11997  13673   8299   1634  -2456    275       C  
ATOM    906  CG  TYR A 131     195.822  25.120 553.468  1.00 85.00           C  
ANISOU  906  CG  TYR A 131    11314  12985   7996   1430  -2244    139       C  
ATOM    907  CD1 TYR A 131     196.596  25.702 552.474  1.00 76.08           C  
ANISOU  907  CD1 TYR A 131     9883  11873   7153   1296  -2338     14       C  
ATOM    908  CD2 TYR A 131     194.442  25.245 553.381  1.00 77.25           C  
ANISOU  908  CD2 TYR A 131    10513  11869   6971   1376  -1946    145       C  
ATOM    909  CE1 TYR A 131     196.015  26.391 551.426  1.00 70.09           C  
ANISOU  909  CE1 TYR A 131     9027  10995   6609   1121  -2147    -95       C  
ATOM    910  CE2 TYR A 131     193.851  25.931 552.337  1.00 69.16           C  
ANISOU  910  CE2 TYR A 131     9374  10731   6172   1206  -1770     29       C  
ATOM    911  CZ  TYR A 131     194.642  26.502 551.362  1.00 71.74           C  
ANISOU  911  CZ  TYR A 131     9424  11073   6761   1082  -1874    -88       C  
ATOM    912  OH  TYR A 131     194.058  27.186 550.320  1.00 79.23           O  
ANISOU  912  OH  TYR A 131    10276  11909   7917    924  -1701   -189       O  
ATOM    913  N   PRO A 132     195.224  25.897 557.179  1.00 70.11           N  
ANISOU  913  N   PRO A 132    10207  11362   5071   1639  -2520     77       N  
ATOM    914  CA  PRO A 132     194.199  26.860 557.626  1.00 62.13           C  
ANISOU  914  CA  PRO A 132     9420  10309   3876   1551  -2371    -71       C  
ATOM    915  C   PRO A 132     194.750  28.132 558.253  1.00 64.11           C  
ANISOU  915  C   PRO A 132     9685  10629   4046   1416  -2598   -313       C  
ATOM    916  O   PRO A 132     194.027  29.135 558.299  1.00 63.43           O  
ANISOU  916  O   PRO A 132     9709  10483   3908   1308  -2487   -484       O  
ATOM    917  CB  PRO A 132     193.379  26.051 558.641  1.00 64.59           C  
ANISOU  917  CB  PRO A 132    10042  10599   3899   1703  -2180    123       C  
ATOM    918  CG  PRO A 132     193.563  24.643 558.226  1.00 65.24           C  
ANISOU  918  CG  PRO A 132    10052  10645   4093   1845  -2119    381       C  
ATOM    919  CD  PRO A 132     194.982  24.562 557.756  1.00 69.60           C  
ANISOU  919  CD  PRO A 132    10316  11287   4844   1846  -2427    346       C  
ATOM    920  N   VAL A 133     195.993  28.136 558.737  1.00 68.46           N  
ANISOU  920  N   VAL A 133    10122  11286   4604   1409  -2899   -331       N  
ATOM    921  CA  VAL A 133     196.518  29.356 559.344  1.00 68.90           C  
ANISOU  921  CA  VAL A 133    10189  11391   4598   1258  -3106   -558       C  
ATOM    922  C   VAL A 133     196.900  30.377 558.275  1.00 76.29           C  
ANISOU  922  C   VAL A 133    10871  12281   5835   1055  -3175   -758       C  
ATOM    923  O   VAL A 133     196.876  31.586 558.532  1.00 77.02           O  
ANISOU  923  O   VAL A 133    11015  12345   5905    900  -3235   -970       O  
ATOM    924  CB  VAL A 133     197.703  29.036 560.275  1.00 72.76           C  
ANISOU  924  CB  VAL A 133    10644  12018   4982   1310  -3405   -508       C  
ATOM    925  CG1 VAL A 133     198.943  28.666 559.478  1.00 80.08           C  
ANISOU  925  CG1 VAL A 133    11213  13001   6213   1290  -3605   -463       C  
ATOM    926  CG2 VAL A 133     197.986  30.212 561.202  1.00 75.64           C  
ANISOU  926  CG2 VAL A 133    11120  12435   5184   1179  -3577   -723       C  
ATOM    927  N   LYS A 134     197.244  29.924 557.071  1.00 81.70           N  
ANISOU  927  N   LYS A 134    11284  12950   6810   1052  -3156   -692       N  
ATOM    928  CA  LYS A 134     197.533  30.813 555.954  1.00 83.88           C  
ANISOU  928  CA  LYS A 134    11309  13172   7388    861  -3179   -855       C  
ATOM    929  C   LYS A 134     196.309  31.086 555.092  1.00 85.90           C  
ANISOU  929  C   LYS A 134    11618  13285   7735    813  -2872   -885       C  
ATOM    930  O   LYS A 134     196.409  31.835 554.115  1.00 93.01           O  
ANISOU  930  O   LYS A 134    12328  14097   8913    637  -2824   -995       O  
ATOM    931  CB  LYS A 134     198.650  30.226 555.085  1.00 89.28           C  
ANISOU  931  CB  LYS A 134    11635  13917   8371    864  -3304   -767       C  
ATOM    932  CG  LYS A 134     199.964  30.012 555.815  1.00108.91           C  
ANISOU  932  CG  LYS A 134    14009  16525  10845    881  -3591   -729       C  
ATOM    933  CD  LYS A 134     200.986  29.335 554.916  1.00117.67           C  
ANISOU  933  CD  LYS A 134    14762  17685  12261    910  -3665   -622       C  
ATOM    934  CE  LYS A 134     200.465  28.004 554.401  1.00117.62           C  
ANISOU  934  CE  LYS A 134    14769  17650  12269   1120  -3474   -412       C  
ATOM    935  NZ  LYS A 134     200.065  27.103 555.514  1.00124.00           N  
ANISOU  935  NZ  LYS A 134    15866  18481  12767   1324  -3458   -246       N  
ATOM    936  N   ARG A 135     195.163  30.497 555.430  1.00 81.19           N  
ANISOU  936  N   ARG A 135    11259  12622   6968    930  -2611   -759       N  
ATOM    937  CA  ARG A 135     193.936  30.639 554.649  1.00 72.80           C  
ANISOU  937  CA  ARG A 135    10225  11385   6049    865  -2261   -741       C  
ATOM    938  C   ARG A 135     193.209  31.886 555.135  1.00 76.24           C  
ANISOU  938  C   ARG A 135    10866  11770   6332    781  -2210   -945       C  
ATOM    939  O   ARG A 135     192.331  31.826 555.996  1.00 81.11           O  
ANISOU  939  O   ARG A 135    11761  12386   6672    878  -2076   -927       O  
ATOM    940  CB  ARG A 135     193.079  29.386 554.784  1.00 66.97           C  
ANISOU  940  CB  ARG A 135     9618  10599   5228   1020  -2008   -506       C  
ATOM    941  CG  ARG A 135     191.881  29.324 553.856  1.00 64.83           C  
ANISOU  941  CG  ARG A 135     9321  10159   5152    957  -1663   -463       C  
ATOM    942  CD  ARG A 135     191.221  27.957 553.945  1.00 62.65           C  
ANISOU  942  CD  ARG A 135     9133   9835   4838   1094  -1448   -221       C  
ATOM    943  NE  ARG A 135     190.069  27.833 553.058  1.00 61.13           N  
ANISOU  943  NE  ARG A 135     8898   9487   4840   1029  -1136   -181       N  
ATOM    944  CZ  ARG A 135     188.810  28.018 553.440  1.00 61.64           C  
ANISOU  944  CZ  ARG A 135     9145   9490   4785   1038   -897   -177       C  
ATOM    945  NH1 ARG A 135     188.534  28.336 554.697  1.00 54.85           N  
ANISOU  945  NH1 ARG A 135     8541   8706   3594   1115   -915   -209       N  
ATOM    946  NH2 ARG A 135     187.825  27.882 552.564  1.00 74.03           N  
ANISOU  946  NH2 ARG A 135    10638  10929   6561    974   -641   -143       N  
ATOM    947  N   THR A 136     193.583  33.031 554.575  1.00 78.00           N  
ANISOU  947  N   THR A 136    10954  11944   6740    602  -2306  -1139       N  
ATOM    948  CA  THR A 136     193.032  34.322 554.963  1.00 83.44           C  
ANISOU  948  CA  THR A 136    11820  12562   7320    512  -2286  -1358       C  
ATOM    949  C   THR A 136     192.350  34.977 553.761  1.00 81.64           C  
ANISOU  949  C   THR A 136    11476  12158   7386    377  -2058  -1407       C  
ATOM    950  O   THR A 136     192.238  34.389 552.682  1.00 87.43           O  
ANISOU  950  O   THR A 136    12012  12834   8372    358  -1910  -1271       O  
ATOM    951  CB  THR A 136     194.127  35.222 555.542  1.00 86.79           C  
ANISOU  951  CB  THR A 136    12224  13063   7687    408  -2630  -1557       C  
ATOM    952  OG1 THR A 136     195.174  35.384 554.578  1.00 82.17           O  
ANISOU  952  OG1 THR A 136    11311  12492   7419    274  -2790  -1583       O  
ATOM    953  CG2 THR A 136     194.701  34.613 556.814  1.00 90.65           C  
ANISOU  953  CG2 THR A 136    12830  13687   7925    516  -2792  -1467       C  
ATOM    954  N   THR A 137     191.892  36.215 553.961  1.00 80.42           N  
ANISOU  954  N   THR A 137    11457  11913   7187    290  -2037  -1608       N  
ATOM    955  CA  THR A 137     191.206  36.948 552.903  1.00 83.89           C  
ANISOU  955  CA  THR A 137    11815  12180   7880    176  -1834  -1660       C  
ATOM    956  C   THR A 137     192.185  37.489 551.867  1.00 86.79           C  
ANISOU  956  C   THR A 137    11905  12506   8566     -6  -1974  -1717       C  
ATOM    957  O   THR A 137     191.939  37.382 550.659  1.00 88.86           O  
ANISOU  957  O   THR A 137    11990  12679   9093    -64  -1811  -1632       O  
ATOM    958  CB  THR A 137     190.384  38.089 553.507  1.00 82.79           C  
ANISOU  958  CB  THR A 137    11928  11945   7583    165  -1759  -1852       C  
ATOM    959  OG1 THR A 137     189.298  37.547 554.270  1.00 77.88           O  
ANISOU  959  OG1 THR A 137    11536  11348   6705    335  -1549  -1770       O  
ATOM    960  CG2 THR A 137     189.831  38.994 552.417  1.00 88.26           C  
ANISOU  960  CG2 THR A 137    12530  12453   8550     44  -1599  -1919       C  
ATOM    961  N   LYS A 138     193.298  38.069 552.323  1.00 81.35           N  
ANISOU  961  N   LYS A 138    11172  11885   7853   -100  -2275  -1860       N  
ATOM    962  CA  LYS A 138     194.285  38.620 551.399  1.00 74.11           C  
ANISOU  962  CA  LYS A 138     9980  10935   7244   -287  -2406  -1912       C  
ATOM    963  C   LYS A 138     194.844  37.543 550.477  1.00 76.25           C  
ANISOU  963  C   LYS A 138     9969  11276   7726   -259  -2366  -1709       C  
ATOM    964  O   LYS A 138     195.040  37.781 549.279  1.00 71.79           O  
ANISOU  964  O   LYS A 138     9194  10633   7449   -374  -2278  -1677       O  
ATOM    965  CB  LYS A 138     195.406  39.297 552.190  1.00 66.60           C  
ANISOU  965  CB  LYS A 138     9022  10066   6217   -387  -2756  -2095       C  
ATOM    966  CG  LYS A 138     196.614  39.704 551.367  1.00 74.30           C  
ANISOU  966  CG  LYS A 138     9677  11033   7519   -585  -2897  -2106       C  
ATOM    967  CD  LYS A 138     197.603  40.492 552.213  1.00 92.73           C  
ANISOU  967  CD  LYS A 138    12025  13384   9825   -729  -3136  -2214       C  
ATOM    968  CE  LYS A 138     198.937  40.655 551.506  1.00104.16           C  
ANISOU  968  CE  LYS A 138    13129  14866  11580   -902  -3278  -2178       C  
ATOM    969  NZ  LYS A 138     199.633  39.349 551.339  1.00109.46           N  
ANISOU  969  NZ  LYS A 138    13581  15719  12290   -775  -3350  -1998       N  
ATOM    970  N   MET A 139     195.094  36.348 551.016  1.00 72.99           N  
ANISOU  970  N   MET A 139     9563  11005   7166    -97  -2422  -1567       N  
ATOM    971  CA  MET A 139     195.609  35.256 550.196  1.00 69.37           C  
ANISOU  971  CA  MET A 139     8858  10603   6895    -45  -2379  -1379       C  
ATOM    972  C   MET A 139     194.607  34.850 549.120  1.00 66.69           C  
ANISOU  972  C   MET A 139     8493  10136   6710    -24  -2055  -1258       C  
ATOM    973  O   MET A 139     194.977  34.657 547.955  1.00 66.77           O  
ANISOU  973  O   MET A 139     8270  10117   6982    -87  -1987  -1192       O  
ATOM    974  CB  MET A 139     195.968  34.067 551.090  1.00 73.54           C  
ANISOU  974  CB  MET A 139     9444  11285   7211    146  -2497  -1248       C  
ATOM    975  CG  MET A 139     196.246  32.765 550.357  1.00 84.58           C  
ANISOU  975  CG  MET A 139    10657  12716   8766    250  -2403  -1036       C  
ATOM    976  SD  MET A 139     194.806  31.679 550.330  0.53 90.02           S  
ANISOU  976  SD  MET A 139    11546  13310   9346    412  -2072   -852       S  
ATOM    977  CE  MET A 139     195.552  30.142 549.795  1.00 97.46           C  
ANISOU  977  CE  MET A 139    12283  14315  10432    548  -2082   -636       C  
ATOM    978  N   ALA A 140     193.330  34.724 549.491  1.00 62.17           N  
ANISOU  978  N   ALA A 140     8153   9491   5976     63  -1852  -1231       N  
ATOM    979  CA  ALA A 140     192.305  34.380 548.512  1.00 51.19           C  
ANISOU  979  CA  ALA A 140     6737   7983   4730     76  -1561  -1131       C  
ATOM    980  C   ALA A 140     192.183  35.457 547.441  1.00 49.83           C  
ANISOU  980  C   ALA A 140     6454   7686   4792    -88  -1491  -1228       C  
ATOM    981  O   ALA A 140     192.010  35.149 546.255  1.00 51.43           O  
ANISOU  981  O   ALA A 140     6505   7831   5206   -116  -1347  -1142       O  
ATOM    982  CB  ALA A 140     190.965  34.161 549.214  1.00 43.04           C  
ANISOU  982  CB  ALA A 140     5962   6906   3485    188  -1366  -1099       C  
ATOM    983  N   GLY A 141     192.275  36.727 547.841  1.00 46.27           N  
ANISOU  983  N   GLY A 141     6094   7187   4302   -193  -1593  -1409       N  
ATOM    984  CA  GLY A 141     192.232  37.801 546.862  1.00 50.79           C  
ANISOU  984  CA  GLY A 141     6575   7626   5097   -350  -1538  -1493       C  
ATOM    985  C   GLY A 141     193.406  37.762 545.903  1.00 65.38           C  
ANISOU  985  C   GLY A 141     8135   9510   7195   -466  -1634  -1453       C  
ATOM    986  O   GLY A 141     193.249  38.003 544.703  1.00 59.87           O  
ANISOU  986  O   GLY A 141     7314   8724   6709   -540  -1497  -1410       O  
ATOM    987  N   MET A 142     194.600  37.454 546.418  1.00 73.39           N  
ANISOU  987  N   MET A 142     9036  10663   8185   -474  -1868  -1463       N  
ATOM    988  CA  MET A 142     195.768  37.345 545.548  1.00 62.40           C  
ANISOU  988  CA  MET A 142     7345   9327   7037   -571  -1949  -1417       C  
ATOM    989  C   MET A 142     195.634  36.169 544.588  1.00 50.76           C  
ANISOU  989  C   MET A 142     5732   7876   5677   -470  -1773  -1232       C  
ATOM    990  O   MET A 142     196.052  36.260 543.427  1.00 52.68           O  
ANISOU  990  O   MET A 142     5773   8094   6148   -553  -1699  -1187       O  
ATOM    991  CB  MET A 142     197.040  37.217 546.386  1.00 64.00           C  
ANISOU  991  CB  MET A 142     7444   9689   7185   -583  -2250  -1467       C  
ATOM    992  CG  MET A 142     197.391  38.469 547.174  1.00 74.89           C  
ANISOU  992  CG  MET A 142     8916  11040   8499   -725  -2459  -1677       C  
ATOM    993  SD  MET A 142     198.988  38.359 548.006  0.52 78.44           S  
ANISOU  993  SD  MET A 142     9185  11690   8929   -765  -2846  -1744       S  
ATOM    994  CE  MET A 142     198.719  36.953 549.082  1.00 69.39           C  
ANISOU  994  CE  MET A 142     8200  10699   7465   -487  -2894  -1618       C  
ATOM    995  N   MET A 143     195.051  35.059 545.050  1.00 51.92           N  
ANISOU  995  N   MET A 143     5995   8066   5666   -292  -1698  -1123       N  
ATOM    996  CA  MET A 143     194.825  33.928 544.154  1.00 55.04           C  
ANISOU  996  CA  MET A 143     6288   8457   6169   -197  -1525   -963       C  
ATOM    997  C   MET A 143     193.820  34.276 543.061  1.00 64.35           C  
ANISOU  997  C   MET A 143     7489   9493   7468   -251  -1286   -951       C  
ATOM    998  O   MET A 143     194.034  33.948 541.887  1.00 69.78           O  
ANISOU  998  O   MET A 143     8012  10164   8338   -272  -1186   -881       O  
ATOM    999  CB  MET A 143     194.354  32.710 544.947  1.00 59.38           C  
ANISOU  999  CB  MET A 143     6981   9055   6527     -9  -1492   -850       C  
ATOM   1000  CG  MET A 143     195.479  31.816 545.442  1.00 68.00           C  
ANISOU 1000  CG  MET A 143     7959  10291   7586     94  -1678   -773       C  
ATOM   1001  SD  MET A 143     194.867  30.307 546.218  1.00 82.05           S  
ANISOU 1001  SD  MET A 143     9919  12091   9165    319  -1600   -603       S  
ATOM   1002  CE  MET A 143     196.372  29.343 546.321  1.00 86.46           C  
ANISOU 1002  CE  MET A 143    10264  12799   9788    431  -1809   -505       C  
ATOM   1003  N   ILE A 144     192.721  34.941 543.426  1.00 67.92           N  
ANISOU 1003  N   ILE A 144     8145   9847   7815   -263  -1194  -1021       N  
ATOM   1004  CA  ILE A 144     191.709  35.309 542.437  1.00 66.36           C  
ANISOU 1004  CA  ILE A 144     7969   9519   7725   -300   -984  -1010       C  
ATOM   1005  C   ILE A 144     192.292  36.274 541.411  1.00 66.58           C  
ANISOU 1005  C   ILE A 144     7848   9492   7958   -456   -999  -1060       C  
ATOM   1006  O   ILE A 144     192.138  36.089 540.196  1.00 70.88           O  
ANISOU 1006  O   ILE A 144     8283   9995   8652   -475   -867   -989       O  
ATOM   1007  CB  ILE A 144     190.472  35.903 543.134  1.00 68.33           C  
ANISOU 1007  CB  ILE A 144     8454   9684   7823   -269   -895  -1082       C  
ATOM   1008  CG1 ILE A 144     189.745  34.825 543.943  1.00 74.03           C  
ANISOU 1008  CG1 ILE A 144     9311  10452   8365   -113   -815   -995       C  
ATOM   1009  CG2 ILE A 144     189.541  36.544 542.116  1.00 65.90           C  
ANISOU 1009  CG2 ILE A 144     8150   9244   7646   -319   -720  -1092       C  
ATOM   1010  CD1 ILE A 144     188.558  35.343 544.724  1.00 81.94           C  
ANISOU 1010  CD1 ILE A 144    10535  11392   9205    -67   -711  -1060       C  
ATOM   1011  N   ALA A 145     192.973  37.320 541.889  1.00 58.81           N  
ANISOU 1011  N   ALA A 145     6864   8502   6979   -575  -1160  -1183       N  
ATOM   1012  CA  ALA A 145     193.584  38.284 540.979  1.00 39.24           C  
ANISOU 1012  CA  ALA A 145     4246   5960   4705   -742  -1171  -1222       C  
ATOM   1013  C   ALA A 145     194.605  37.613 540.070  1.00 36.04           C  
ANISOU 1013  C   ALA A 145     3579   5647   4466   -761  -1173  -1119       C  
ATOM   1014  O   ALA A 145     194.674  37.914 538.872  1.00 51.36           O  
ANISOU 1014  O   ALA A 145     5412   7531   6570   -834  -1056  -1073       O  
ATOM   1015  CB  ALA A 145     194.231  39.418 541.772  1.00 38.63           C  
ANISOU 1015  CB  ALA A 145     4208   5859   4609   -876  -1368  -1379       C  
ATOM   1016  N   ALA A 146     195.404  36.694 540.620  1.00 42.17           N  
ANISOU 1016  N   ALA A 146     4257   6569   5195   -681  -1300  -1077       N  
ATOM   1017  CA  ALA A 146     196.359  35.961 539.797  1.00 46.85           C  
ANISOU 1017  CA  ALA A 146     4599   7257   5944   -667  -1289   -978       C  
ATOM   1018  C   ALA A 146     195.648  35.145 538.726  1.00 50.91           C  
ANISOU 1018  C   ALA A 146     5110   7728   6504   -572  -1064   -864       C  
ATOM   1019  O   ALA A 146     196.127  35.044 537.589  1.00 47.88           O  
ANISOU 1019  O   ALA A 146     4557   7355   6279   -610   -975   -807       O  
ATOM   1020  CB  ALA A 146     197.227  35.060 540.674  1.00 38.62           C  
ANISOU 1020  CB  ALA A 146     3473   6372   4827   -562  -1469   -948       C  
ATOM   1021  N   ALA A 147     194.496  34.561 539.067  1.00 53.84           N  
ANISOU 1021  N   ALA A 147     5669   8052   6736   -453   -968   -833       N  
ATOM   1022  CA  ALA A 147     193.739  33.789 538.087  1.00 39.60           C  
ANISOU 1022  CA  ALA A 147     3872   6198   4976   -374   -773   -742       C  
ATOM   1023  C   ALA A 147     193.234  34.678 536.957  1.00 44.29           C  
ANISOU 1023  C   ALA A 147     4463   6686   5678   -477   -641   -761       C  
ATOM   1024  O   ALA A 147     193.397  34.353 535.775  1.00 56.58           O  
ANISOU 1024  O   ALA A 147     5908   8243   7346   -477   -534   -699       O  
ATOM   1025  CB  ALA A 147     192.576  33.070 538.772  1.00 38.94           C  
ANISOU 1025  CB  ALA A 147     3982   6079   4736   -250   -702   -710       C  
ATOM   1026  N   TRP A 148     192.619  35.814 537.302  1.00 43.22           N  
ANISOU 1026  N   TRP A 148     4462   6456   5502   -556   -647   -845       N  
ATOM   1027  CA  TRP A 148     192.091  36.702 536.269  1.00 40.56           C  
ANISOU 1027  CA  TRP A 148     4143   6008   5261   -638   -529   -851       C  
ATOM   1028  C   TRP A 148     193.203  37.252 535.382  1.00 53.08           C  
ANISOU 1028  C   TRP A 148     5547   7611   7011   -765   -544   -835       C  
ATOM   1029  O   TRP A 148     193.066  37.290 534.152  1.00 48.20           O  
ANISOU 1029  O   TRP A 148     4872   6959   6481   -781   -414   -773       O  
ATOM   1030  CB  TRP A 148     191.296  37.841 536.907  1.00 32.07           C  
ANISOU 1030  CB  TRP A 148     3249   4819   4117   -684   -542   -950       C  
ATOM   1031  CG  TRP A 148     189.916  37.438 537.340  1.00 41.80           C  
ANISOU 1031  CG  TRP A 148     4648   6011   5225   -564   -446   -945       C  
ATOM   1032  CD1 TRP A 148     189.537  37.008 538.579  1.00 42.46           C  
ANISOU 1032  CD1 TRP A 148     4853   6132   5147   -477   -488   -973       C  
ATOM   1033  CD2 TRP A 148     188.733  37.426 536.532  1.00 43.94           C  
ANISOU 1033  CD2 TRP A 148     4969   6202   5525   -518   -288   -903       C  
ATOM   1034  NE1 TRP A 148     188.191  36.730 538.592  1.00 35.25           N  
ANISOU 1034  NE1 TRP A 148     4053   5166   4176   -388   -348   -948       N  
ATOM   1035  CE2 TRP A 148     187.674  36.979 537.348  1.00 44.29           C  
ANISOU 1035  CE2 TRP A 148     5146   6241   5443   -413   -234   -910       C  
ATOM   1036  CE3 TRP A 148     188.466  37.751 535.199  1.00 48.16           C  
ANISOU 1036  CE3 TRP A 148     5447   6677   6174   -553   -189   -856       C  
ATOM   1037  CZ2 TRP A 148     186.370  36.849 536.874  1.00 55.42           C  
ANISOU 1037  CZ2 TRP A 148     6607   7588   6861   -351    -93   -879       C  
ATOM   1038  CZ3 TRP A 148     187.170  37.622 534.730  1.00 48.08           C  
ANISOU 1038  CZ3 TRP A 148     5506   6609   6154   -481    -68   -828       C  
ATOM   1039  CH2 TRP A 148     186.139  37.175 535.565  1.00 49.92           C  
ANISOU 1039  CH2 TRP A 148     5845   6839   6284   -385    -25   -843       C  
ATOM   1040  N   VAL A 149     194.317  37.675 535.987  1.00 67.19           N  
ANISOU 1040  N   VAL A 149     7236   9455   8839   -857   -701   -889       N  
ATOM   1041  CA  VAL A 149     195.425  38.215 535.202  1.00 56.78           C  
ANISOU 1041  CA  VAL A 149     5720   8157   7696   -994   -707   -869       C  
ATOM   1042  C   VAL A 149     196.009  37.142 534.291  1.00 48.48           C  
ANISOU 1042  C   VAL A 149     4486   7215   6719   -917   -618   -760       C  
ATOM   1043  O   VAL A 149     196.289  37.394 533.112  1.00 44.29           O  
ANISOU 1043  O   VAL A 149     3856   6668   6304   -975   -496   -701       O  
ATOM   1044  CB  VAL A 149     196.495  38.821 536.130  1.00 40.80           C  
ANISOU 1044  CB  VAL A 149     3610   6183   5711  -1114   -916   -960       C  
ATOM   1045  CG1 VAL A 149     197.735  39.203 535.337  1.00 37.11           C  
ANISOU 1045  CG1 VAL A 149     2892   5760   5448  -1256   -914   -922       C  
ATOM   1046  CG2 VAL A 149     195.936  40.035 536.854  1.00 36.42           C  
ANISOU 1046  CG2 VAL A 149     3250   5491   5098  -1207   -985  -1084       C  
ATOM   1047  N   LEU A 150     196.191  35.927 534.816  1.00 45.41           N  
ANISOU 1047  N   LEU A 150     4065   6931   6258   -774   -670   -729       N  
ATOM   1048  CA  LEU A 150     196.721  34.843 533.994  1.00 49.09           C  
ANISOU 1048  CA  LEU A 150     4373   7486   6791   -678   -582   -637       C  
ATOM   1049  C   LEU A 150     195.794  34.525 532.828  1.00 57.20           C  
ANISOU 1049  C   LEU A 150     5482   8439   7811   -622   -383   -583       C  
ATOM   1050  O   LEU A 150     196.257  34.271 531.710  1.00 60.13           O  
ANISOU 1050  O   LEU A 150     5729   8845   8272   -617   -271   -526       O  
ATOM   1051  CB  LEU A 150     196.956  33.597 534.848  1.00 61.79           C  
ANISOU 1051  CB  LEU A 150     5972   9190   8316   -519   -676   -611       C  
ATOM   1052  CG  LEU A 150     198.329  33.493 535.513  1.00 72.86           C  
ANISOU 1052  CG  LEU A 150     7178  10728   9777   -533   -857   -622       C  
ATOM   1053  CD1 LEU A 150     198.415  32.247 536.379  1.00 72.33           C  
ANISOU 1053  CD1 LEU A 150     7141  10737   9603   -351   -947   -580       C  
ATOM   1054  CD2 LEU A 150     199.427  33.494 534.461  1.00 73.10           C  
ANISOU 1054  CD2 LEU A 150     6945  10834   9994   -581   -790   -574       C  
ATOM   1055  N   SER A 151     194.480  34.536 533.065  1.00 52.80           N  
ANISOU 1055  N   SER A 151     5130   7786   7144   -575   -338   -603       N  
ATOM   1056  CA  SER A 151     193.536  34.287 531.980  1.00 37.49           C  
ANISOU 1056  CA  SER A 151     3265   5780   5199   -529   -176   -563       C  
ATOM   1057  C   SER A 151     193.623  35.379 530.919  1.00 43.10           C  
ANISOU 1057  C   SER A 151     3947   6434   5994   -648    -93   -551       C  
ATOM   1058  O   SER A 151     193.668  35.092 529.715  1.00 50.75           O  
ANISOU 1058  O   SER A 151     4866   7416   7002   -625     29   -495       O  
ATOM   1059  CB  SER A 151     192.116  34.183 532.535  1.00 37.25           C  
ANISOU 1059  CB  SER A 151     3434   5666   5055   -469   -155   -589       C  
ATOM   1060  OG  SER A 151     192.002  33.101 533.441  1.00 40.04           O  
ANISOU 1060  OG  SER A 151     3824   6064   5326   -356   -204   -577       O  
ATOM   1061  N   PHE A 152     193.656  36.643 531.354  1.00 41.18           N  
ANISOU 1061  N   PHE A 152     3751   6122   5776   -774   -157   -602       N  
ATOM   1062  CA  PHE A 152     193.749  37.751 530.407  1.00 46.46           C  
ANISOU 1062  CA  PHE A 152     4409   6712   6530   -894    -77   -578       C  
ATOM   1063  C   PHE A 152     195.016  37.658 529.567  1.00 46.40           C  
ANISOU 1063  C   PHE A 152     4193   6794   6643   -953    -25   -514       C  
ATOM   1064  O   PHE A 152     194.975  37.853 528.346  1.00 52.20           O  
ANISOU 1064  O   PHE A 152     4912   7509   7411   -969    113   -445       O  
ATOM   1065  CB  PHE A 152     193.698  39.085 531.152  1.00 53.93           C  
ANISOU 1065  CB  PHE A 152     5440   7552   7497  -1023   -170   -654       C  
ATOM   1066  CG  PHE A 152     193.832  40.285 530.257  1.00 53.67           C  
ANISOU 1066  CG  PHE A 152     5411   7415   7567  -1155    -92   -619       C  
ATOM   1067  CD1 PHE A 152     192.723  40.816 529.620  1.00 51.18           C  
ANISOU 1067  CD1 PHE A 152     5251   6980   7216  -1125      6   -592       C  
ATOM   1068  CD2 PHE A 152     195.065  40.884 530.054  1.00 53.99           C  
ANISOU 1068  CD2 PHE A 152     5294   7474   7747  -1308   -116   -604       C  
ATOM   1069  CE1 PHE A 152     192.841  41.920 528.795  1.00 40.46           C  
ANISOU 1069  CE1 PHE A 152     3914   5513   5944  -1235     79   -542       C  
ATOM   1070  CE2 PHE A 152     195.190  41.987 529.230  1.00 56.53           C  
ANISOU 1070  CE2 PHE A 152     5628   7684   8166  -1437    -29   -554       C  
ATOM   1071  CZ  PHE A 152     194.076  42.505 528.600  1.00 47.37           C  
ANISOU 1071  CZ  PHE A 152     4648   6396   6956  -1395     69   -518       C  
ATOM   1072  N   ILE A 153     196.153  37.365 530.203  1.00 44.17           N  
ANISOU 1072  N   ILE A 153     3745   6617   6421   -981   -132   -532       N  
ATOM   1073  CA  ILE A 153     197.405  37.249 529.462  1.00 48.49           C  
ANISOU 1073  CA  ILE A 153     4061   7264   7099  -1032    -74   -471       C  
ATOM   1074  C   ILE A 153     197.369  36.050 528.524  1.00 49.72           C  
ANISOU 1074  C   ILE A 153     4171   7497   7224   -878     63   -403       C  
ATOM   1075  O   ILE A 153     197.930  36.097 527.421  1.00 44.58           O  
ANISOU 1075  O   ILE A 153     3408   6888   6643   -902    200   -336       O  
ATOM   1076  CB  ILE A 153     198.594  37.171 530.439  1.00 49.77           C  
ANISOU 1076  CB  ILE A 153     4039   7533   7340  -1083   -244   -513       C  
ATOM   1077  CG1 ILE A 153     198.697  38.459 531.258  1.00 53.80           C  
ANISOU 1077  CG1 ILE A 153     4597   7955   7888  -1258   -383   -598       C  
ATOM   1078  CG2 ILE A 153     199.895  36.916 529.695  1.00 46.29           C  
ANISOU 1078  CG2 ILE A 153     3324   7216   7048  -1113   -174   -445       C  
ATOM   1079  CD1 ILE A 153     199.841  38.458 532.248  1.00 55.70           C  
ANISOU 1079  CD1 ILE A 153     4659   8303   8200  -1322   -583   -656       C  
ATOM   1080  N   LEU A 154     196.700  34.969 528.926  1.00 49.74           N  
ANISOU 1080  N   LEU A 154     4269   7511   7118   -722     39   -419       N  
ATOM   1081  CA  LEU A 154     196.664  33.775 528.089  1.00 48.96           C  
ANISOU 1081  CA  LEU A 154     4141   7466   6994   -576    157   -374       C  
ATOM   1082  C   LEU A 154     195.818  33.990 526.839  1.00 54.90           C  
ANISOU 1082  C   LEU A 154     5014   8148   7697   -568    310   -343       C  
ATOM   1083  O   LEU A 154     196.233  33.620 525.734  1.00 43.61           O  
ANISOU 1083  O   LEU A 154     3510   6771   6288   -527    441   -297       O  
ATOM   1084  CB  LEU A 154     196.138  32.582 528.888  1.00 50.67           C  
ANISOU 1084  CB  LEU A 154     4444   7688   7122   -425     88   -396       C  
ATOM   1085  CG  LEU A 154     197.118  31.854 529.812  1.00 58.28           C  
ANISOU 1085  CG  LEU A 154     5269   8756   8118   -356    -34   -395       C  
ATOM   1086  CD1 LEU A 154     196.449  30.647 530.452  1.00 43.72           C  
ANISOU 1086  CD1 LEU A 154     3548   6887   6176   -200    -68   -393       C  
ATOM   1087  CD2 LEU A 154     198.372  31.440 529.057  1.00 61.70           C  
ANISOU 1087  CD2 LEU A 154     5473   9303   8668   -322     35   -349       C  
ATOM   1088  N   TRP A 155     194.636  34.590 526.984  1.00 59.14           N  
ANISOU 1088  N   TRP A 155     5734   8572   8164   -598    297   -369       N  
ATOM   1089  CA  TRP A 155     193.660  34.613 525.898  1.00 33.34           C  
ANISOU 1089  CA  TRP A 155     2594   5245   4830   -558    410   -345       C  
ATOM   1090  C   TRP A 155     193.537  35.946 525.178  1.00 30.30           C  
ANISOU 1090  C   TRP A 155     2254   4789   4471   -674    472   -306       C  
ATOM   1091  O   TRP A 155     193.308  35.958 523.968  1.00 33.97           O  
ANISOU 1091  O   TRP A 155     2755   5254   4899   -647    589   -255       O  
ATOM   1092  CB  TRP A 155     192.283  34.205 526.423  1.00 27.36           C  
ANISOU 1092  CB  TRP A 155     2002   4415   3981   -481    366   -390       C  
ATOM   1093  CG  TRP A 155     192.181  32.745 526.692  1.00 36.85           C  
ANISOU 1093  CG  TRP A 155     3195   5660   5148   -351    356   -405       C  
ATOM   1094  CD1 TRP A 155     192.190  32.130 527.910  1.00 38.40           C  
ANISOU 1094  CD1 TRP A 155     3397   5867   5326   -302    262   -430       C  
ATOM   1095  CD2 TRP A 155     192.076  31.705 525.716  1.00 27.15           C  
ANISOU 1095  CD2 TRP A 155     1962   4458   3894   -249    447   -393       C  
ATOM   1096  NE1 TRP A 155     192.085  30.769 527.752  1.00 26.86           N  
ANISOU 1096  NE1 TRP A 155     1936   4425   3845   -180    293   -423       N  
ATOM   1097  CE2 TRP A 155     192.015  30.483 526.413  1.00 25.27           C  
ANISOU 1097  CE2 TRP A 155     1728   4229   3644   -147    403   -411       C  
ATOM   1098  CE3 TRP A 155     192.023  31.689 524.320  1.00 27.14           C  
ANISOU 1098  CE3 TRP A 155     1972   4470   3870   -230    559   -371       C  
ATOM   1099  CZ2 TRP A 155     191.903  29.259 525.761  1.00 26.03           C  
ANISOU 1099  CZ2 TRP A 155     1835   4329   3725    -35    467   -418       C  
ATOM   1100  CZ3 TRP A 155     191.913  30.476 523.675  1.00 32.74           C  
ANISOU 1100  CZ3 TRP A 155     2695   5200   4546   -114    617   -389       C  
ATOM   1101  CH2 TRP A 155     191.854  29.277 524.395  1.00 35.86           C  
ANISOU 1101  CH2 TRP A 155     3091   5586   4948    -22    570   -417       C  
ATOM   1102  N   ALA A 156     193.667  37.073 525.876  1.00 29.81           N  
ANISOU 1102  N   ALA A 156     2207   4657   4462   -799    397   -327       N  
ATOM   1103  CA  ALA A 156     193.403  38.362 525.235  1.00 30.65           C  
ANISOU 1103  CA  ALA A 156     2391   4659   4595   -902    456   -284       C  
ATOM   1104  C   ALA A 156     194.387  38.696 524.120  1.00 44.35           C  
ANISOU 1104  C   ALA A 156     4009   6442   6401   -974    584   -191       C  
ATOM   1105  O   ALA A 156     193.932  39.016 523.006  1.00 48.51           O  
ANISOU 1105  O   ALA A 156     4623   6931   6876   -957    696   -122       O  
ATOM   1106  CB  ALA A 156     193.360  39.464 526.298  1.00 41.66           C  
ANISOU 1106  CB  ALA A 156     3839   5949   6041  -1019    342   -343       C  
ATOM   1107  N   PRO A 157     195.714  38.648 524.319  1.00 51.63           N  
ANISOU 1107  N   PRO A 157     4730   7451   7434  -1052    579   -179       N  
ATOM   1108  CA  PRO A 157     196.613  39.096 523.241  1.00 41.34           C  
ANISOU 1108  CA  PRO A 157     3311   6186   6209  -1136    728    -78       C  
ATOM   1109  C   PRO A 157     196.529  38.249 521.984  1.00 39.15           C  
ANISOU 1109  C   PRO A 157     3041   5996   5838  -1003    886    -19       C  
ATOM   1110  O   PRO A 157     196.606  38.790 520.874  1.00 53.99           O  
ANISOU 1110  O   PRO A 157     4954   7859   7699  -1040   1032     75       O  
ATOM   1111  CB  PRO A 157     198.005  39.013 523.886  1.00 40.48           C  
ANISOU 1111  CB  PRO A 157     2955   6177   6249  -1226    668    -95       C  
ATOM   1112  CG  PRO A 157     197.756  39.001 525.354  1.00 45.89           C  
ANISOU 1112  CG  PRO A 157     3676   6829   6931  -1235    462   -205       C  
ATOM   1113  CD  PRO A 157     196.476  38.253 525.518  1.00 44.21           C  
ANISOU 1113  CD  PRO A 157     3654   6585   6561  -1071    438   -246       C  
ATOM   1114  N   ALA A 158     196.380  36.931 522.124  1.00 36.58           N  
ANISOU 1114  N   ALA A 158     2698   5756   5445   -847    863    -70       N  
ATOM   1115  CA  ALA A 158     196.306  36.068 520.950  1.00 45.15           C  
ANISOU 1115  CA  ALA A 158     3804   6917   6435   -715   1004    -38       C  
ATOM   1116  C   ALA A 158     195.040  36.340 520.147  1.00 50.74           C  
ANISOU 1116  C   ALA A 158     4735   7541   7005   -668   1044    -21       C  
ATOM   1117  O   ALA A 158     195.093  36.511 518.923  1.00 57.57           O  
ANISOU 1117  O   ALA A 158     5642   8431   7800   -649   1184     50       O  
ATOM   1118  CB  ALA A 158     196.375  34.600 521.373  1.00 30.69           C  
ANISOU 1118  CB  ALA A 158     1922   5162   4576   -562    956   -107       C  
ATOM   1119  N   ILE A 159     193.891  36.393 520.825  1.00 36.93           N  
ANISOU 1119  N   ILE A 159     3125   5699   5208   -643    920    -83       N  
ATOM   1120  CA  ILE A 159     192.622  36.609 520.136  1.00 36.20           C  
ANISOU 1120  CA  ILE A 159     3222   5535   4997   -587    933    -73       C  
ATOM   1121  C   ILE A 159     192.585  37.991 519.496  1.00 47.56           C  
ANISOU 1121  C   ILE A 159     4730   6895   6443   -688    998     21       C  
ATOM   1122  O   ILE A 159     192.155  38.147 518.345  1.00 50.60           O  
ANISOU 1122  O   ILE A 159     5219   7281   6724   -638   1082     82       O  
ATOM   1123  CB  ILE A 159     191.449  36.406 521.113  1.00 30.21           C  
ANISOU 1123  CB  ILE A 159     2563   4700   4214   -545    796   -156       C  
ATOM   1124  CG1 ILE A 159     191.385  34.952 521.583  1.00 29.93           C  
ANISOU 1124  CG1 ILE A 159     2486   4727   4158   -436    753   -229       C  
ATOM   1125  CG2 ILE A 159     190.132  36.813 520.469  1.00 44.57           C  
ANISOU 1125  CG2 ILE A 159     4551   6445   5941   -499    793   -143       C  
ATOM   1126  CD1 ILE A 159     190.266  34.680 522.578  1.00 24.21           C  
ANISOU 1126  CD1 ILE A 159     1849   3934   3414   -399    642   -297       C  
ATOM   1127  N   LEU A 160     193.045  39.015 520.220  1.00 40.37           N  
ANISOU 1127  N   LEU A 160     3775   5911   5653   -829    955     36       N  
ATOM   1128  CA  LEU A 160     192.914  40.380 519.726  1.00 58.47           C  
ANISOU 1128  CA  LEU A 160     6159   8088   7969   -929   1007    126       C  
ATOM   1129  C   LEU A 160     193.958  40.728 518.672  1.00 54.77           C  
ANISOU 1129  C   LEU A 160     5607   7674   7528  -1000   1177    248       C  
ATOM   1130  O   LEU A 160     193.666  41.501 517.752  1.00 50.93           O  
ANISOU 1130  O   LEU A 160     5240   7123   6990  -1017   1268    353       O  
ATOM   1131  CB  LEU A 160     193.006  41.370 520.888  1.00 63.84           C  
ANISOU 1131  CB  LEU A 160     6838   8645   8773  -1062    899     82       C  
ATOM   1132  CG  LEU A 160     191.910  41.293 521.953  1.00 58.24           C  
ANISOU 1132  CG  LEU A 160     6236   7861   8029  -1001    754    -26       C  
ATOM   1133  CD1 LEU A 160     192.145  42.341 523.030  1.00 56.22           C  
ANISOU 1133  CD1 LEU A 160     5992   7485   7886  -1136    660    -77       C  
ATOM   1134  CD2 LEU A 160     190.541  41.463 521.324  1.00 60.69           C  
ANISOU 1134  CD2 LEU A 160     6724   8105   8229   -893    765     -2       C  
ATOM   1135  N   PHE A 161     195.167  40.177 518.776  1.00 45.18           N  
ANISOU 1135  N   PHE A 161     4191   6580   6396  -1033   1229    245       N  
ATOM   1136  CA  PHE A 161     196.287  40.640 517.969  1.00 43.55           C  
ANISOU 1136  CA  PHE A 161     3866   6423   6258  -1131   1400    363       C  
ATOM   1137  C   PHE A 161     196.884  39.580 517.053  1.00 39.40           C  
ANISOU 1137  C   PHE A 161     3247   6067   5655  -1013   1549    390       C  
ATOM   1138  O   PHE A 161     197.859  39.877 516.349  1.00 44.51           O  
ANISOU 1138  O   PHE A 161     3779   6778   6354  -1082   1719    492       O  
ATOM   1139  CB  PHE A 161     197.385  41.198 518.884  1.00 47.35           C  
ANISOU 1139  CB  PHE A 161     4148   6892   6950  -1311   1348    350       C  
ATOM   1140  CG  PHE A 161     196.901  42.258 519.831  1.00 45.97           C  
ANISOU 1140  CG  PHE A 161     4070   6543   6854  -1431   1202    303       C  
ATOM   1141  CD1 PHE A 161     196.031  43.247 519.402  1.00 43.07           C  
ANISOU 1141  CD1 PHE A 161     3914   6015   6437  -1455   1224    364       C  
ATOM   1142  CD2 PHE A 161     197.310  42.259 521.154  1.00 53.34           C  
ANISOU 1142  CD2 PHE A 161     4894   7472   7903  -1508   1037    195       C  
ATOM   1143  CE1 PHE A 161     195.584  44.223 520.274  1.00 36.96           C  
ANISOU 1143  CE1 PHE A 161     3239   5068   5737  -1551   1099    311       C  
ATOM   1144  CE2 PHE A 161     196.867  43.232 522.030  1.00 58.70           C  
ANISOU 1144  CE2 PHE A 161     5679   7987   8638  -1610    906    134       C  
ATOM   1145  CZ  PHE A 161     196.002  44.215 521.590  1.00 44.30           C  
ANISOU 1145  CZ  PHE A 161     4065   5993   6774  -1631    944    189       C  
ATOM   1146  N   TRP A 162     196.340  38.359 517.033  1.00 39.27           N  
ANISOU 1146  N   TRP A 162     3278   6120   5521   -841   1501    300       N  
ATOM   1147  CA  TRP A 162     196.888  37.333 516.151  1.00 45.35           C  
ANISOU 1147  CA  TRP A 162     3982   7037   6214   -715   1644    307       C  
ATOM   1148  C   TRP A 162     196.779  37.732 514.685  1.00 60.05           C  
ANISOU 1148  C   TRP A 162     5966   8918   7933   -689   1827    420       C  
ATOM   1149  O   TRP A 162     197.659  37.395 513.883  1.00 61.74           O  
ANISOU 1149  O   TRP A 162     6083   9249   8124   -654   2010    476       O  
ATOM   1150  CB  TRP A 162     196.186  35.997 516.391  1.00 44.01           C  
ANISOU 1150  CB  TRP A 162     3877   6898   5945   -543   1548    183       C  
ATOM   1151  CG  TRP A 162     196.710  34.890 515.533  1.00 40.47           C  
ANISOU 1151  CG  TRP A 162     3380   6579   5416   -401   1686    167       C  
ATOM   1152  CD1 TRP A 162     196.048  34.245 514.530  1.00 45.39           C  
ANISOU 1152  CD1 TRP A 162     4165   7226   5854   -263   1742    137       C  
ATOM   1153  CD2 TRP A 162     198.016  34.304 515.593  1.00 44.90           C  
ANISOU 1153  CD2 TRP A 162     3716   7261   6081   -374   1782    171       C  
ATOM   1154  NE1 TRP A 162     196.858  33.289 513.966  1.00 54.54           N  
ANISOU 1154  NE1 TRP A 162     5232   8504   6986   -149   1876    114       N  
ATOM   1155  CE2 TRP A 162     198.072  33.306 514.601  1.00 52.91           C  
ANISOU 1155  CE2 TRP A 162     4782   8361   6961   -208   1909    140       C  
ATOM   1156  CE3 TRP A 162     199.142  34.526 516.392  1.00 44.34           C  
ANISOU 1156  CE3 TRP A 162     3409   7227   6210   -467   1759    192       C  
ATOM   1157  CZ2 TRP A 162     199.210  32.531 514.387  1.00 66.23           C  
ANISOU 1157  CZ2 TRP A 162     6339  10103   8724   -124   2005    120       C  
ATOM   1158  CZ3 TRP A 162     200.271  33.756 516.177  1.00 45.72           C  
ANISOU 1158  CZ3 TRP A 162     3451   7453   6467   -376   1841    183       C  
ATOM   1159  CH2 TRP A 162     200.296  32.771 515.183  1.00 60.95           C  
ANISOU 1159  CH2 TRP A 162     5459   9431   8267   -209   1969    141       C  
ATOM   1160  N   GLN A 163     195.714  38.451 514.319  1.00 64.43           N  
ANISOU 1160  N   GLN A 163     6734   9363   8383   -693   1785    460       N  
ATOM   1161  CA  GLN A 163     195.570  38.924 512.946  1.00 47.30           C  
ANISOU 1161  CA  GLN A 163     4706   7207   6059   -664   1943    583       C  
ATOM   1162  C   GLN A 163     196.711  39.858 512.562  1.00 43.89           C  
ANISOU 1162  C   GLN A 163     4160   6781   5735   -815   2126    736       C  
ATOM   1163  O   GLN A 163     197.200  39.820 511.427  1.00 42.02           O  
ANISOU 1163  O   GLN A 163     3939   6635   5393   -777   2330    836       O  
ATOM   1164  CB  GLN A 163     194.221  39.622 512.774  1.00 49.21           C  
ANISOU 1164  CB  GLN A 163     5182   7319   6198   -643   1835    605       C  
ATOM   1165  CG  GLN A 163     193.892  40.611 513.881  1.00 58.17           C  
ANISOU 1165  CG  GLN A 163     6318   8294   7492   -774   1697    598       C  
ATOM   1166  CD  GLN A 163     192.576  41.326 513.654  1.00 58.32           C  
ANISOU 1166  CD  GLN A 163     6558   8186   7417   -731   1606    628       C  
ATOM   1167  OE1 GLN A 163     192.173  41.560 512.516  1.00 59.12           O  
ANISOU 1167  OE1 GLN A 163     6807   8298   7356   -659   1682    722       O  
ATOM   1168  NE2 GLN A 163     191.896  41.673 514.741  1.00 58.82           N  
ANISOU 1168  NE2 GLN A 163     6644   8132   7572   -763   1443    549       N  
ATOM   1169  N   PHE A 164     197.149  40.706 513.496  1.00 50.63           N  
ANISOU 1169  N   PHE A 164     4901   7538   6800   -993   2061    752       N  
ATOM   1170  CA  PHE A 164     198.291  41.571 513.224  1.00 43.83           C  
ANISOU 1170  CA  PHE A 164     3898   6673   6083  -1166   2227    889       C  
ATOM   1171  C   PHE A 164     199.598  40.792 513.256  1.00 48.28           C  
ANISOU 1171  C   PHE A 164     4204   7407   6732  -1161   2313    854       C  
ATOM   1172  O   PHE A 164     200.554  41.162 512.564  1.00 46.75           O  
ANISOU 1172  O   PHE A 164     3948   7270   6546  -1233   2451    934       O  
ATOM   1173  CB  PHE A 164     198.335  42.723 514.227  1.00 45.14           C  
ANISOU 1173  CB  PHE A 164     4035   6667   6450  -1366   2104    892       C  
ATOM   1174  CG  PHE A 164     197.076  43.541 514.267  1.00 47.27           C  
ANISOU 1174  CG  PHE A 164     4565   6754   6641  -1357   1996    908       C  
ATOM   1175  CD1 PHE A 164     196.818  44.489 513.291  1.00 48.11           C  
ANISOU 1175  CD1 PHE A 164     4840   6766   6674  -1389   2125   1073       C  
ATOM   1176  CD2 PHE A 164     196.153  43.366 515.285  1.00 42.47           C  
ANISOU 1176  CD2 PHE A 164     4033   6071   6034  -1306   1775    765       C  
ATOM   1177  CE1 PHE A 164     195.662  45.244 513.326  1.00 45.32           C  
ANISOU 1177  CE1 PHE A 164     4719   6243   6257  -1361   2022   1092       C  
ATOM   1178  CE2 PHE A 164     194.995  44.118 515.326  1.00 47.31           C  
ANISOU 1178  CE2 PHE A 164     4866   6522   6587  -1282   1685    778       C  
ATOM   1179  CZ  PHE A 164     194.749  45.059 514.345  1.00 49.89           C  
ANISOU 1179  CZ  PHE A 164     5353   6754   6851  -1305   1802    940       C  
ATOM   1180  N   ILE A 165     199.662  39.720 514.050  1.00 49.82           N  
ANISOU 1180  N   ILE A 165     4282   7680   6965  -1067   2190    711       N  
ATOM   1181  CA  ILE A 165     200.865  38.891 514.080  1.00 47.51           C  
ANISOU 1181  CA  ILE A 165     3792   7537   6721  -1026   2219    639       C  
ATOM   1182  C   ILE A 165     201.075  38.215 512.730  1.00 45.19           C  
ANISOU 1182  C   ILE A 165     3575   7348   6247   -878   2409    657       C  
ATOM   1183  O   ILE A 165     202.189  38.195 512.192  1.00 47.56           O  
ANISOU 1183  O   ILE A 165     3756   7738   6576   -907   2539    682       O  
ATOM   1184  CB  ILE A 165     200.783  37.861 515.221  1.00 60.16           C  
ANISOU 1184  CB  ILE A 165     5291   9173   8395   -935   2043    490       C  
ATOM   1185  CG1 ILE A 165     200.814  38.566 516.578  1.00 63.00           C  
ANISOU 1185  CG1 ILE A 165     5555   9457   8926  -1089   1844    480       C  
ATOM   1186  CG2 ILE A 165     201.921  36.857 515.118  1.00 67.12           C  
ANISOU 1186  CG2 ILE A 165     6004  10175   9324   -842   2098    410       C  
ATOM   1187  CD1 ILE A 165     202.088  39.338 516.833  1.00 65.73           C  
ANISOU 1187  CD1 ILE A 165     5716   9833   9428  -1271   1842    522       C  
ATOM   1188  N   VAL A 166     200.007  37.650 512.161  1.00 53.04           N  
ANISOU 1188  N   VAL A 166     4768   8339   7045   -716   2424    638       N  
ATOM   1189  CA  VAL A 166     200.125  37.019 510.850  1.00 52.81           C  
ANISOU 1189  CA  VAL A 166     4847   8403   6816   -571   2588    641       C  
ATOM   1190  C   VAL A 166     200.082  38.036 509.716  1.00 53.76           C  
ANISOU 1190  C   VAL A 166     5112   8504   6813   -636   2747    802       C  
ATOM   1191  O   VAL A 166     200.577  37.748 508.619  1.00 48.86           O  
ANISOU 1191  O   VAL A 166     4534   7972   6057   -565   2909    826       O  
ATOM   1192  CB  VAL A 166     199.029  35.961 510.644  1.00 58.25           C  
ANISOU 1192  CB  VAL A 166     5700   9108   7325   -370   2523    542       C  
ATOM   1193  CG1 VAL A 166     199.188  34.832 511.649  1.00 41.65           C  
ANISOU 1193  CG1 VAL A 166     3465   7021   5337   -290   2389    393       C  
ATOM   1194  CG2 VAL A 166     197.650  36.590 510.755  1.00 66.32           C  
ANISOU 1194  CG2 VAL A 166     6914  10032   8254   -383   2415    585       C  
ATOM   1195  N   GLY A 167     199.508  39.214 509.945  1.00 51.43           N  
ANISOU 1195  N   GLY A 167     4901   8082   6557   -762   2707    915       N  
ATOM   1196  CA  GLY A 167     199.461  40.254 508.939  1.00 50.79           C  
ANISOU 1196  CA  GLY A 167     4970   7954   6373   -828   2849   1086       C  
ATOM   1197  C   GLY A 167     198.227  40.267 508.067  1.00 52.78           C  
ANISOU 1197  C   GLY A 167     5508   8185   6361   -686   2868   1140       C  
ATOM   1198  O   GLY A 167     198.172  41.059 507.118  1.00 49.75           O  
ANISOU 1198  O   GLY A 167     5277   7770   5854   -712   2986   1290       O  
ATOM   1199  N   VAL A 168     197.238  39.425 508.352  1.00 50.22           N  
ANISOU 1199  N   VAL A 168     5264   7879   5937   -536   2740   1023       N  
ATOM   1200  CA  VAL A 168     196.022  39.361 507.549  1.00 47.83           C  
ANISOU 1200  CA  VAL A 168     5244   7557   5372   -399   2669   1017       C  
ATOM   1201  C   VAL A 168     194.884  38.880 508.437  1.00 47.35           C  
ANISOU 1201  C   VAL A 168     5237   7418   5337   -344   2389    849       C  
ATOM   1202  O   VAL A 168     195.071  38.012 509.295  1.00 46.51           O  
ANISOU 1202  O   VAL A 168     4986   7340   5348   -325   2296    706       O  
ATOM   1203  CB  VAL A 168     196.209  38.448 506.315  1.00 52.85           C  
ANISOU 1203  CB  VAL A 168     5969   8359   5753   -222   2827    997       C  
ATOM   1204  CG1 VAL A 168     196.588  37.034 506.739  1.00 52.35           C  
ANISOU 1204  CG1 VAL A 168     5766   8385   5741   -125   2779    801       C  
ATOM   1205  CG2 VAL A 168     194.954  38.440 505.452  1.00 46.31           C  
ANISOU 1205  CG2 VAL A 168     5434   7518   4644    -88   2730    989       C  
ATOM   1206  N   ARG A 169     193.704  39.463 508.240  1.00 56.80           N  
ANISOU 1206  N   ARG A 169     6637   8515   6430   -316   2260    877       N  
ATOM   1207  CA  ARG A 169     192.495  39.063 508.955  1.00 52.47           C  
ANISOU 1207  CA  ARG A 169     6149   7897   5890   -257   2012    732       C  
ATOM   1208  C   ARG A 169     191.691  38.146 508.040  1.00 59.03           C  
ANISOU 1208  C   ARG A 169     7139   8817   6471    -77   1963    646       C  
ATOM   1209  O   ARG A 169     191.053  38.603 507.088  1.00 75.81           O  
ANISOU 1209  O   ARG A 169     9457  10943   8405    -10   1964    727       O  
ATOM   1210  CB  ARG A 169     191.680  40.280 509.379  1.00 43.60           C  
ANISOU 1210  CB  ARG A 169     5126   6607   4834   -332   1892    805       C  
ATOM   1211  CG  ARG A 169     190.361  39.923 510.042  1.00 39.99           C  
ANISOU 1211  CG  ARG A 169     4728   6088   4379   -261   1658    669       C  
ATOM   1212  CD  ARG A 169     189.619  41.157 510.524  1.00 38.68           C  
ANISOU 1212  CD  ARG A 169     4646   5754   4298   -323   1556    737       C  
ATOM   1213  NE  ARG A 169     188.391  40.800 511.226  1.00 44.49           N  
ANISOU 1213  NE  ARG A 169     5408   6441   5054   -254   1352    606       N  
ATOM   1214  CZ  ARG A 169     188.332  40.491 512.517  1.00 55.10           C  
ANISOU 1214  CZ  ARG A 169     6633   7742   6560   -306   1254    489       C  
ATOM   1215  NH1 ARG A 169     189.435  40.498 513.253  1.00 62.15           N  
ANISOU 1215  NH1 ARG A 169     7373   8636   7606   -421   1317    479       N  
ATOM   1216  NH2 ARG A 169     187.171  40.176 513.074  1.00 66.25           N  
ANISOU 1216  NH2 ARG A 169     8074   9116   7980   -239   1093    386       N  
ATOM   1217  N   THR A 170     191.724  36.845 508.330  1.00 43.02           N  
ANISOU 1217  N   THR A 170     5038   6861   4449      3   1912    479       N  
ATOM   1218  CA  THR A 170     190.984  35.873 507.538  1.00 39.04           C  
ANISOU 1218  CA  THR A 170     4676   6428   3730    161   1849    365       C  
ATOM   1219  C   THR A 170     189.502  35.830 507.886  1.00 56.44           C  
ANISOU 1219  C   THR A 170     6979   8550   5918    195   1608    280       C  
ATOM   1220  O   THR A 170     188.734  35.176 507.172  1.00 67.98           O  
ANISOU 1220  O   THR A 170     8570  10059   7201    310   1525    190       O  
ATOM   1221  CB  THR A 170     191.590  34.478 507.711  1.00 42.60           C  
ANISOU 1221  CB  THR A 170     5017   6960   4208    233   1893    218       C  
ATOM   1222  OG1 THR A 170     191.477  34.072 509.080  1.00 47.99           O  
ANISOU 1222  OG1 THR A 170     5556   7569   5108    178   1758    122       O  
ATOM   1223  CG2 THR A 170     193.058  34.485 507.310  1.00 50.98           C  
ANISOU 1223  CG2 THR A 170     5959   8121   5289    219   2144    301       C  
ATOM   1224  N   VAL A 171     189.084  36.502 508.955  1.00 58.15           N  
ANISOU 1224  N   VAL A 171     7132   8646   6315    100   1494    298       N  
ATOM   1225  CA  VAL A 171     187.677  36.553 509.335  1.00 51.79           C  
ANISOU 1225  CA  VAL A 171     6398   7765   5515    132   1284    229       C  
ATOM   1226  C   VAL A 171     186.982  37.561 508.426  1.00 60.28           C  
ANISOU 1226  C   VAL A 171     7648   8817   6439    173   1260    355       C  
ATOM   1227  O   VAL A 171     187.215  38.768 508.527  1.00 65.37           O  
ANISOU 1227  O   VAL A 171     8313   9380   7146     96   1316    501       O  
ATOM   1228  CB  VAL A 171     187.505  36.925 510.812  1.00 49.99           C  
ANISOU 1228  CB  VAL A 171     6051   7423   5520     31   1191    202       C  
ATOM   1229  CG1 VAL A 171     186.031  36.940 511.187  1.00 63.71           C  
ANISOU 1229  CG1 VAL A 171     7848   9094   7266     76    998    133       C  
ATOM   1230  CG2 VAL A 171     188.277  35.955 511.695  1.00 31.76           C  
ANISOU 1230  CG2 VAL A 171     3578   5145   3345      1   1214    100       C  
ATOM   1231  N   GLU A 172     186.127  37.067 507.534  1.00 68.20           N  
ANISOU 1231  N   GLU A 172     8783   9885   7245    294   1167    297       N  
ATOM   1232  CA  GLU A 172     185.451  37.930 506.580  1.00 68.48           C  
ANISOU 1232  CA  GLU A 172     8995   9917   7106    360   1127    418       C  
ATOM   1233  C   GLU A 172     184.381  38.767 507.279  1.00 64.70           C  
ANISOU 1233  C   GLU A 172     8517   9312   6753    341    964    447       C  
ATOM   1234  O   GLU A 172     184.062  38.572 508.455  1.00 61.13           O  
ANISOU 1234  O   GLU A 172     7940   8788   6498    285    878    354       O  
ATOM   1235  CB  GLU A 172     184.830  37.101 505.457  1.00 64.36           C  
ANISOU 1235  CB  GLU A 172     8610   9514   6332    500   1045    326       C  
ATOM   1236  CG  GLU A 172     185.784  36.100 504.827  1.00 77.25           C  
ANISOU 1236  CG  GLU A 172    10247  11267   7838    542   1196    254       C  
ATOM   1237  CD  GLU A 172     185.145  35.314 503.700  1.00 95.83           C  
ANISOU 1237  CD  GLU A 172    12759  13727   9924    680   1102    145       C  
ATOM   1238  OE1 GLU A 172     184.377  35.911 502.918  1.00103.98           O  
ANISOU 1238  OE1 GLU A 172    13947  14781  10779    752   1005    220       O  
ATOM   1239  OE2 GLU A 172     185.407  34.097 503.601  1.00101.82           O  
ANISOU 1239  OE2 GLU A 172    13493  14543  10651    721   1115    -20       O  
ATOM   1240  N   ASP A 173     183.824  39.717 506.531  1.00 73.52           N  
ANISOU 1240  N   ASP A 173     9786  10404   7746    402    929    583       N  
ATOM   1241  CA  ASP A 173     182.779  40.576 507.069  1.00 72.30           C  
ANISOU 1241  CA  ASP A 173     9645  10128   7698    413    783    621       C  
ATOM   1242  C   ASP A 173     181.521  39.765 507.353  1.00 67.28           C  
ANISOU 1242  C   ASP A 173     8960   9526   7078    488    568    452       C  
ATOM   1243  O   ASP A 173     181.103  38.932 506.545  1.00 79.90           O  
ANISOU 1243  O   ASP A 173    10615  11240   8505    577    487    365       O  
ATOM   1244  CB  ASP A 173     182.467  41.710 506.093  1.00 79.80           C  
ANISOU 1244  CB  ASP A 173    10779  11046   8493    487    790    816       C  
ATOM   1245  CG  ASP A 173     181.542  42.755 506.688  1.00 85.52           C  
ANISOU 1245  CG  ASP A 173    11518  11621   9355    503    671    877       C  
ATOM   1246  OD1 ASP A 173     181.369  42.766 507.925  1.00 86.68           O  
ANISOU 1246  OD1 ASP A 173    11530  11677   9726    430    628    787       O  
ATOM   1247  OD2 ASP A 173     180.985  43.565 505.916  1.00 88.16           O  
ANISOU 1247  OD2 ASP A 173    12005  11928   9564    601    622   1017       O  
ATOM   1248  N   GLY A 174     180.917  40.014 508.514  1.00 47.45           N  
ANISOU 1248  N   GLY A 174     6342   6911   4775    446    480    401       N  
ATOM   1249  CA  GLY A 174     179.744  39.285 508.939  1.00 39.48           C  
ANISOU 1249  CA  GLY A 174     5255   5923   3824    495    300    250       C  
ATOM   1250  C   GLY A 174     180.027  38.019 509.717  1.00 38.91           C  
ANISOU 1250  C   GLY A 174     5045   5882   3857    431    309     83       C  
ATOM   1251  O   GLY A 174     179.105  37.474 510.338  1.00 40.46           O  
ANISOU 1251  O   GLY A 174     5152   6065   4154    440    185    -32       O  
ATOM   1252  N   GLU A 175     181.262  37.531 509.700  1.00 37.82           N  
ANISOU 1252  N   GLU A 175     4883   5782   3705    372    457     74       N  
ATOM   1253  CA  GLU A 175     181.661  36.364 510.470  1.00 48.39           C  
ANISOU 1253  CA  GLU A 175     6099   7137   5149    321    477    -64       C  
ATOM   1254  C   GLU A 175     182.316  36.796 511.777  1.00 46.58           C  
ANISOU 1254  C   GLU A 175     5759   6818   5119    214    552    -37       C  
ATOM   1255  O   GLU A 175     182.757  37.938 511.932  1.00 32.65           O  
ANISOU 1255  O   GLU A 175     4018   4987   3399    163    621     85       O  
ATOM   1256  CB  GLU A 175     182.624  35.486 509.667  1.00 60.20           C  
ANISOU 1256  CB  GLU A 175     7627   8734   6510    345    588   -102       C  
ATOM   1257  CG  GLU A 175     182.044  34.945 508.373  1.00 66.77           C  
ANISOU 1257  CG  GLU A 175     8586   9662   7120    454    510   -159       C  
ATOM   1258  CD  GLU A 175     183.056  34.152 507.569  1.00 88.21           C  
ANISOU 1258  CD  GLU A 175    11351  12475   9691    491    645   -198       C  
ATOM   1259  OE1 GLU A 175     184.260  34.215 507.897  1.00 93.85           O  
ANISOU 1259  OE1 GLU A 175    11996  13189  10473    436    815   -145       O  
ATOM   1260  OE2 GLU A 175     182.647  33.464 506.610  1.00100.09           O  
ANISOU 1260  OE2 GLU A 175    12961  14057  11013    578    577   -289       O  
ATOM   1261  N   CYS A 176     182.375  35.862 512.723  1.00 49.74           N  
ANISOU 1261  N   CYS A 176     6049   7211   5638    179    531   -153       N  
ATOM   1262  CA  CYS A 176     182.995  36.130 514.017  1.00 46.28           C  
ANISOU 1262  CA  CYS A 176     5510   6706   5370     86    580   -145       C  
ATOM   1263  C   CYS A 176     183.487  34.812 514.598  1.00 44.80           C  
ANISOU 1263  C   CYS A 176     5228   6555   5239     74    598   -254       C  
ATOM   1264  O   CYS A 176     182.684  34.004 515.073  1.00 47.07           O  
ANISOU 1264  O   CYS A 176     5483   6828   5573     96    510   -353       O  
ATOM   1265  CB  CYS A 176     182.019  36.817 514.967  1.00 44.23           C  
ANISOU 1265  CB  CYS A 176     5233   6349   5225     71    489   -148       C  
ATOM   1266  SG  CYS A 176     182.764  37.273 516.542  0.89 46.67           S  
ANISOU 1266  SG  CYS A 176     5452   6575   5707    -38    535   -148       S  
ATOM   1267  N   TYR A 177     184.801  34.604 514.561  1.00 46.15           N  
ANISOU 1267  N   TYR A 177     5349   6769   5418     41    715   -228       N  
ATOM   1268  CA  TYR A 177     185.407  33.403 515.117  1.00 39.30           C  
ANISOU 1268  CA  TYR A 177     4391   5931   4611     45    739   -315       C  
ATOM   1269  C   TYR A 177     186.878  33.681 515.380  1.00 41.63           C  
ANISOU 1269  C   TYR A 177     4595   6257   4966    -14    859   -251       C  
ATOM   1270  O   TYR A 177     187.459  34.622 514.833  1.00 44.02           O  
ANISOU 1270  O   TYR A 177     4916   6573   5238    -54    945   -147       O  
ATOM   1271  CB  TYR A 177     185.236  32.198 514.183  1.00 32.32           C  
ANISOU 1271  CB  TYR A 177     3558   5110   3612    135    738   -405       C  
ATOM   1272  CG  TYR A 177     185.867  32.374 512.817  1.00 40.31           C  
ANISOU 1272  CG  TYR A 177     4646   6206   4463    183    845   -354       C  
ATOM   1273  CD1 TYR A 177     185.179  33.005 511.788  1.00 44.36           C  
ANISOU 1273  CD1 TYR A 177     5286   6740   4829    223    810   -307       C  
ATOM   1274  CD2 TYR A 177     187.146  31.899 512.555  1.00 48.98           C  
ANISOU 1274  CD2 TYR A 177     5690   7372   5550    200    985   -347       C  
ATOM   1275  CE1 TYR A 177     185.750  33.165 510.540  1.00 49.21           C  
ANISOU 1275  CE1 TYR A 177     5990   7439   5271    275    919   -250       C  
ATOM   1276  CE2 TYR A 177     187.725  32.055 511.309  1.00 58.26           C  
ANISOU 1276  CE2 TYR A 177     6937   8632   6567    250   1108   -296       C  
ATOM   1277  CZ  TYR A 177     187.022  32.688 510.306  1.00 61.89           C  
ANISOU 1277  CZ  TYR A 177     7541   9110   6863    285   1078   -246       C  
ATOM   1278  OH  TYR A 177     187.594  32.845 509.064  1.00 67.77           O  
ANISOU 1278  OH  TYR A 177     8377   9947   7426    342   1211   -185       O  
ATOM   1279  N   ILE A 178     187.473  32.848 516.235  1.00 37.28           N  
ANISOU 1279  N   ILE A 178     3939   5715   4509    -19    862   -308       N  
ATOM   1280  CA  ILE A 178     188.890  32.982 516.548  1.00 40.05           C  
ANISOU 1280  CA  ILE A 178     4171   6111   4936    -67    956   -260       C  
ATOM   1281  C   ILE A 178     189.714  32.590 515.331  1.00 43.83           C  
ANISOU 1281  C   ILE A 178     4650   6687   5318     -8   1094   -237       C  
ATOM   1282  O   ILE A 178     189.518  31.517 514.745  1.00 44.40           O  
ANISOU 1282  O   ILE A 178     4768   6795   5307     92   1104   -317       O  
ATOM   1283  CB  ILE A 178     189.252  32.132 517.774  1.00 42.98           C  
ANISOU 1283  CB  ILE A 178     4437   6474   5420    -64    905   -323       C  
ATOM   1284  CG1 ILE A 178     188.669  32.760 519.041  1.00 46.43           C  
ANISOU 1284  CG1 ILE A 178     4872   6827   5941   -135    799   -326       C  
ATOM   1285  CG2 ILE A 178     190.757  31.974 517.892  1.00 42.66           C  
ANISOU 1285  CG2 ILE A 178     4253   6508   5447    -79    996   -288       C  
ATOM   1286  CD1 ILE A 178     189.067  32.050 520.311  1.00 53.74           C  
ANISOU 1286  CD1 ILE A 178     5711   7750   6957   -133    746   -369       C  
ATOM   1287  N   GLN A 179     190.647  33.463 514.944  1.00 46.25           N  
ANISOU 1287  N   GLN A 179     4906   7030   5637    -72   1209   -131       N  
ATOM   1288  CA  GLN A 179     191.387  33.261 513.702  1.00 60.16           C  
ANISOU 1288  CA  GLN A 179     6679   8891   7288    -15   1369    -89       C  
ATOM   1289  C   GLN A 179     192.315  32.055 513.797  1.00 66.62           C  
ANISOU 1289  C   GLN A 179     7379   9786   8146     62   1440   -157       C  
ATOM   1290  O   GLN A 179     192.260  31.152 512.952  1.00 70.34           O  
ANISOU 1290  O   GLN A 179     7920  10310   8496    180   1495   -222       O  
ATOM   1291  CB  GLN A 179     192.169  34.526 513.349  1.00 64.53           C  
ANISOU 1291  CB  GLN A 179     7192   9455   7870   -120   1492     57       C  
ATOM   1292  CG  GLN A 179     192.865  34.472 512.001  1.00 61.58           C  
ANISOU 1292  CG  GLN A 179     6848   9187   7363    -65   1685    126       C  
ATOM   1293  CD  GLN A 179     193.274  35.845 511.505  1.00 65.19           C  
ANISOU 1293  CD  GLN A 179     7324   9624   7820   -173   1799    292       C  
ATOM   1294  OE1 GLN A 179     192.697  36.857 511.902  1.00 63.79           O  
ANISOU 1294  OE1 GLN A 179     7207   9337   7694   -260   1713    347       O  
ATOM   1295  NE2 GLN A 179     194.274  35.886 510.633  1.00 74.22           N  
ANISOU 1295  NE2 GLN A 179     8419  10867   8912   -164   2007    377       N  
ATOM   1296  N   PHE A 180     193.167  32.011 514.824  1.00 60.76           N  
ANISOU 1296  N   PHE A 180     6464   9052   7571      7   1430   -149       N  
ATOM   1297  CA  PHE A 180     194.108  30.901 514.944  1.00 64.56           C  
ANISOU 1297  CA  PHE A 180     6819   9607   8105     96   1495   -199       C  
ATOM   1298  C   PHE A 180     193.429  29.573 515.255  1.00 60.21           C  
ANISOU 1298  C   PHE A 180     6336   9011   7530    209   1399   -326       C  
ATOM   1299  O   PHE A 180     194.117  28.548 515.311  1.00 63.30           O  
ANISOU 1299  O   PHE A 180     6649   9443   7958    308   1449   -375       O  
ATOM   1300  CB  PHE A 180     195.174  31.208 516.002  1.00 61.03           C  
ANISOU 1300  CB  PHE A 180     6159   9186   7845     12   1481   -156       C  
ATOM   1301  CG  PHE A 180     194.621  31.550 517.358  1.00 54.40           C  
ANISOU 1301  CG  PHE A 180     5316   8254   7098    -70   1301   -179       C  
ATOM   1302  CD1 PHE A 180     194.318  30.554 518.272  1.00 50.10           C  
ANISOU 1302  CD1 PHE A 180     4767   7678   6593      0   1189   -261       C  
ATOM   1303  CD2 PHE A 180     194.432  32.872 517.728  1.00 52.76           C  
ANISOU 1303  CD2 PHE A 180     5121   7988   6937   -214   1256   -117       C  
ATOM   1304  CE1 PHE A 180     193.819  30.867 519.522  1.00 58.98           C  
ANISOU 1304  CE1 PHE A 180     5901   8729   7781    -67   1041   -278       C  
ATOM   1305  CE2 PHE A 180     193.935  33.192 518.978  1.00 63.23           C  
ANISOU 1305  CE2 PHE A 180     6458   9234   8333   -277   1101   -151       C  
ATOM   1306  CZ  PHE A 180     193.629  32.188 519.876  1.00 72.23           C  
ANISOU 1306  CZ  PHE A 180     7593  10359   9492   -202    998   -230       C  
ATOM   1307  N   PHE A 181     192.113  29.561 515.458  1.00 44.34           N  
ANISOU 1307  N   PHE A 181     4463   6911   5472    198   1269   -376       N  
ATOM   1308  CA  PHE A 181     191.351  28.325 515.556  1.00 48.36           C  
ANISOU 1308  CA  PHE A 181     5055   7366   5954    289   1191   -493       C  
ATOM   1309  C   PHE A 181     190.903  27.807 514.196  1.00 66.13           C  
ANISOU 1309  C   PHE A 181     7449   9640   8037    381   1240   -559       C  
ATOM   1310  O   PHE A 181     190.051  26.914 514.137  1.00 68.23           O  
ANISOU 1310  O   PHE A 181     7808   9843   8271    434   1157   -665       O  
ATOM   1311  CB  PHE A 181     190.134  28.518 516.464  1.00 50.15           C  
ANISOU 1311  CB  PHE A 181     5338   7492   6227    227   1033   -517       C  
ATOM   1312  CG  PHE A 181     190.439  28.376 517.928  1.00 44.08           C  
ANISOU 1312  CG  PHE A 181     4463   6686   5598    189    965   -506       C  
ATOM   1313  CD1 PHE A 181     191.676  27.917 518.350  1.00 45.93           C  
ANISOU 1313  CD1 PHE A 181     4563   6974   5915    225   1016   -489       C  
ATOM   1314  CD2 PHE A 181     189.486  28.691 518.881  1.00 42.72           C  
ANISOU 1314  CD2 PHE A 181     4327   6435   5469    129    849   -512       C  
ATOM   1315  CE1 PHE A 181     191.959  27.782 519.697  1.00 40.35           C  
ANISOU 1315  CE1 PHE A 181     3770   6244   5317    201    934   -477       C  
ATOM   1316  CE2 PHE A 181     189.763  28.557 520.229  1.00 56.26           C  
ANISOU 1316  CE2 PHE A 181     5967   8124   7284    103    787   -502       C  
ATOM   1317  CZ  PHE A 181     191.001  28.102 520.637  1.00 39.28           C  
ANISOU 1317  CZ  PHE A 181     3695   6030   5201    139    820   -484       C  
ATOM   1318  N   SER A 182     191.451  28.350 513.104  1.00 78.09           N  
ANISOU 1318  N   SER A 182     8989  11243   9439    397   1373   -500       N  
ATOM   1319  CA  SER A 182     191.117  27.848 511.776  1.00 80.12           C  
ANISOU 1319  CA  SER A 182     9398  11539   9505    498   1424   -568       C  
ATOM   1320  C   SER A 182     191.556  26.403 511.583  1.00 82.19           C  
ANISOU 1320  C   SER A 182     9660  11805   9763    628   1474   -691       C  
ATOM   1321  O   SER A 182     191.002  25.707 510.725  1.00 89.19           O  
ANISOU 1321  O   SER A 182    10695  12683  10509    712   1458   -801       O  
ATOM   1322  CB  SER A 182     191.751  28.735 510.703  1.00 82.67           C  
ANISOU 1322  CB  SER A 182     9747  11965   9701    495   1585   -459       C  
ATOM   1323  OG  SER A 182     191.278  30.068 510.797  1.00 82.34           O  
ANISOU 1323  OG  SER A 182     9734  11894   9658    384   1537   -345       O  
ATOM   1324  N   ASN A 183     192.534  25.939 512.356  1.00 81.86           N  
ANISOU 1324  N   ASN A 183     9460  11772   9873    652   1526   -679       N  
ATOM   1325  CA  ASN A 183     192.980  24.554 512.324  1.00 76.59           C  
ANISOU 1325  CA  ASN A 183     8785  11084   9232    787   1569   -787       C  
ATOM   1326  C   ASN A 183     192.290  23.781 513.441  1.00 78.07           C  
ANISOU 1326  C   ASN A 183     8978  11140   9547    774   1409   -851       C  
ATOM   1327  O   ASN A 183     192.208  24.263 514.576  1.00 83.75           O  
ANISOU 1327  O   ASN A 183     9602  11827  10390    681   1323   -781       O  
ATOM   1328  CB  ASN A 183     194.500  24.467 512.470  1.00 76.53           C  
ANISOU 1328  CB  ASN A 183     8589  11171   9319    844   1724   -724       C  
ATOM   1329  CG  ASN A 183     195.008  23.041 512.446  1.00 77.46           C  
ANISOU 1329  CG  ASN A 183     8698  11260   9475   1008   1775   -830       C  
ATOM   1330  OD1 ASN A 183     195.227  22.432 513.492  1.00 74.24           O  
ANISOU 1330  OD1 ASN A 183     8197  10789   9220   1032   1702   -837       O  
ATOM   1331  ND2 ASN A 183     195.197  22.498 511.249  1.00 82.00           N  
ANISOU 1331  ND2 ASN A 183     9401  11839   9917   1111   1885   -898       N  
ATOM   1332  N   ALA A 184     191.796  22.584 513.115  1.00 75.72           N  
ANISOU 1332  N   ALA A 184     8799  10760   9211    865   1376   -987       N  
ATOM   1333  CA  ALA A 184     191.024  21.813 514.085  1.00 59.38           C  
ANISOU 1333  CA  ALA A 184     6755   8550   7258    842   1237  -1042       C  
ATOM   1334  C   ALA A 184     191.907  21.268 515.200  1.00 59.29           C  
ANISOU 1334  C   ALA A 184     6603   8512   7412    890   1252   -996       C  
ATOM   1335  O   ALA A 184     191.488  21.221 516.363  1.00 65.75           O  
ANISOU 1335  O   ALA A 184     7387   9255   8340    826   1145   -959       O  
ATOM   1336  CB  ALA A 184     190.286  20.675 513.380  1.00 54.99           C  
ANISOU 1336  CB  ALA A 184     6366   7897   6631    913   1198  -1203       C  
ATOM   1337  N   ALA A 185     193.131  20.849 514.868  1.00 58.94           N  
ANISOU 1337  N   ALA A 185     6476   8536   7382   1011   1386   -994       N  
ATOM   1338  CA  ALA A 185     194.018  20.289 515.883  1.00 57.20           C  
ANISOU 1338  CA  ALA A 185     6114   8302   7318   1079   1388   -947       C  
ATOM   1339  C   ALA A 185     194.401  21.326 516.930  1.00 60.90           C  
ANISOU 1339  C   ALA A 185     6421   8838   7880    964   1330   -815       C  
ATOM   1340  O   ALA A 185     194.612  20.979 518.098  1.00 64.01           O  
ANISOU 1340  O   ALA A 185     6740   9188   8392    973   1249   -775       O  
ATOM   1341  CB  ALA A 185     195.270  19.708 515.227  1.00 59.77           C  
ANISOU 1341  CB  ALA A 185     6363   8704   7645   1245   1553   -971       C  
ATOM   1342  N   VAL A 186     194.496  22.598 516.536  1.00 61.47           N  
ANISOU 1342  N   VAL A 186     6450   9009   7897    856   1366   -746       N  
ATOM   1343  CA  VAL A 186     194.768  23.655 517.505  1.00 64.38           C  
ANISOU 1343  CA  VAL A 186     6688   9421   8353    728   1298   -639       C  
ATOM   1344  C   VAL A 186     193.605  23.793 518.478  1.00 50.98           C  
ANISOU 1344  C   VAL A 186     5079   7615   6678    637   1137   -644       C  
ATOM   1345  O   VAL A 186     193.803  23.908 519.695  1.00 49.08           O  
ANISOU 1345  O   VAL A 186     4757   7361   6531    599   1049   -596       O  
ATOM   1346  CB  VAL A 186     195.062  24.981 516.780  1.00 73.49           C  
ANISOU 1346  CB  VAL A 186     7802  10675   9447    628   1383   -566       C  
ATOM   1347  CG1 VAL A 186     195.380  26.079 517.783  1.00 71.39           C  
ANISOU 1347  CG1 VAL A 186     7407  10434   9285    487   1307   -472       C  
ATOM   1348  CG2 VAL A 186     196.206  24.803 515.793  1.00 74.08           C  
ANISOU 1348  CG2 VAL A 186     7786  10865   9495    722   1572   -553       C  
ATOM   1349  N   THR A 187     192.374  23.777 517.960  1.00 47.94           N  
ANISOU 1349  N   THR A 187     4855   7158   6201    604   1097   -704       N  
ATOM   1350  CA  THR A 187     191.202  23.840 518.827  1.00 42.10           C  
ANISOU 1350  CA  THR A 187     4189   6318   5490    527    965   -712       C  
ATOM   1351  C   THR A 187     191.140  22.631 519.753  1.00 39.36           C  
ANISOU 1351  C   THR A 187     3849   5877   5230    595    913   -738       C  
ATOM   1352  O   THR A 187     190.720  22.746 520.911  1.00 49.60           O  
ANISOU 1352  O   THR A 187     5139   7124   6584    539    825   -699       O  
ATOM   1353  CB  THR A 187     189.930  23.936 517.983  1.00 40.47           C  
ANISOU 1353  CB  THR A 187     4131   6064   5181    494    933   -778       C  
ATOM   1354  OG1 THR A 187     190.074  24.984 517.016  1.00 61.21           O  
ANISOU 1354  OG1 THR A 187     6769   8779   7708    457    992   -740       O  
ATOM   1355  CG2 THR A 187     188.723  24.233 518.861  1.00 32.63           C  
ANISOU 1355  CG2 THR A 187     3180   4989   4228    403    814   -770       C  
ATOM   1356  N   PHE A 188     191.564  21.463 519.264  1.00 34.08           N  
ANISOU 1356  N   PHE A 188     3206   5174   4568    723    974   -802       N  
ATOM   1357  CA  PHE A 188     191.550  20.269 520.102  1.00 31.47           C  
ANISOU 1357  CA  PHE A 188     2896   4733   4328    799    933   -815       C  
ATOM   1358  C   PHE A 188     192.592  20.356 521.209  1.00 45.54           C  
ANISOU 1358  C   PHE A 188     4532   6571   6198    833    910   -718       C  
ATOM   1359  O   PHE A 188     192.314  19.995 522.358  1.00 58.20           O  
ANISOU 1359  O   PHE A 188     6151   8105   7859    827    829   -677       O  
ATOM   1360  CB  PHE A 188     191.777  19.023 519.250  1.00 33.33           C  
ANISOU 1360  CB  PHE A 188     3208   4902   4553    937   1007   -915       C  
ATOM   1361  CG  PHE A 188     191.655  17.738 520.015  1.00 44.65           C  
ANISOU 1361  CG  PHE A 188     4694   6186   6085   1016    970   -928       C  
ATOM   1362  CD1 PHE A 188     190.561  17.507 520.833  1.00 44.31           C  
ANISOU 1362  CD1 PHE A 188     4730   6022   6084    929    878   -915       C  
ATOM   1363  CD2 PHE A 188     192.628  16.758 519.912  1.00 61.42           C  
ANISOU 1363  CD2 PHE A 188     6789   8283   8263   1183   1039   -946       C  
ATOM   1364  CE1 PHE A 188     190.443  16.326 521.539  1.00 48.51           C  
ANISOU 1364  CE1 PHE A 188     5322   6403   6708    996    857   -908       C  
ATOM   1365  CE2 PHE A 188     192.515  15.573 520.613  1.00 61.16           C  
ANISOU 1365  CE2 PHE A 188     6821   8092   8325   1263   1006   -945       C  
ATOM   1366  CZ  PHE A 188     191.421  15.357 521.429  1.00 60.56           C  
ANISOU 1366  CZ  PHE A 188     6835   7890   8287   1163    917   -920       C  
ATOM   1367  N   GLY A 189     193.801  20.820 520.882  1.00 42.69           N  
ANISOU 1367  N   GLY A 189     4027   6344   5851    870    980   -679       N  
ATOM   1368  CA  GLY A 189     194.798  21.035 521.918  1.00 43.85           C  
ANISOU 1368  CA  GLY A 189     4012   6565   6086    886    933   -593       C  
ATOM   1369  C   GLY A 189     194.346  22.052 522.946  1.00 50.13           C  
ANISOU 1369  C   GLY A 189     4794   7372   6880    740    818   -534       C  
ATOM   1370  O   GLY A 189     194.614  21.905 524.143  1.00 47.06           O  
ANISOU 1370  O   GLY A 189     4359   6981   6542    753    725   -482       O  
ATOM   1371  N   THR A 190     193.647  23.096 522.493  1.00 47.14           N  
ANISOU 1371  N   THR A 190     4470   7006   6437    611    822   -543       N  
ATOM   1372  CA  THR A 190     193.048  24.048 523.422  1.00 46.13           C  
ANISOU 1372  CA  THR A 190     4361   6864   6302    482    722   -506       C  
ATOM   1373  C   THR A 190     192.023  23.368 524.322  1.00 55.14           C  
ANISOU 1373  C   THR A 190     5623   7887   7441    491    646   -516       C  
ATOM   1374  O   THR A 190     191.965  23.641 525.527  1.00 61.62           O  
ANISOU 1374  O   THR A 190     6433   8704   8275    454    560   -473       O  
ATOM   1375  CB  THR A 190     192.405  25.198 522.644  1.00 52.14           C  
ANISOU 1375  CB  THR A 190     5176   7637   6996    368    751   -514       C  
ATOM   1376  OG1 THR A 190     193.427  26.075 522.153  1.00 66.54           O  
ANISOU 1376  OG1 THR A 190     6875   9569   8837    324    813   -470       O  
ATOM   1377  CG2 THR A 190     191.445  25.979 523.525  1.00 46.26           C  
ANISOU 1377  CG2 THR A 190     4499   6839   6238    262    657   -500       C  
ATOM   1378  N   ALA A 191     191.213  22.469 523.757  1.00 53.74           N  
ANISOU 1378  N   ALA A 191     5562   7611   7246    537    679   -576       N  
ATOM   1379  CA  ALA A 191     190.223  21.761 524.561  1.00 40.91           C  
ANISOU 1379  CA  ALA A 191     4042   5864   5638    534    627   -578       C  
ATOM   1380  C   ALA A 191     190.880  20.830 525.571  1.00 43.06           C  
ANISOU 1380  C   ALA A 191     4289   6105   5966    635    596   -524       C  
ATOM   1381  O   ALA A 191     190.341  20.627 526.665  1.00 51.46           O  
ANISOU 1381  O   ALA A 191     5409   7108   7034    615    541   -479       O  
ATOM   1382  CB  ALA A 191     189.273  20.977 523.656  1.00 44.30           C  
ANISOU 1382  CB  ALA A 191     4587   6189   6055    548    663   -663       C  
ATOM   1383  N   ILE A 192     192.036  20.260 525.230  1.00 47.02           N  
ANISOU 1383  N   ILE A 192     4708   6650   6507    754    636   -521       N  
ATOM   1384  CA  ILE A 192     192.730  19.371 526.154  1.00 48.12           C  
ANISOU 1384  CA  ILE A 192     4817   6763   6703    874    597   -460       C  
ATOM   1385  C   ILE A 192     193.395  20.164 527.272  1.00 48.70           C  
ANISOU 1385  C   ILE A 192     4782   6948   6772    840    501   -381       C  
ATOM   1386  O   ILE A 192     193.339  19.773 528.443  1.00 61.06           O  
ANISOU 1386  O   ILE A 192     6387   8479   8336    876    425   -317       O  
ATOM   1387  CB  ILE A 192     193.750  18.507 525.391  1.00 43.94           C  
ANISOU 1387  CB  ILE A 192     4223   6245   6227   1032    674   -488       C  
ATOM   1388  CG1 ILE A 192     193.035  17.568 524.417  1.00 39.03           C  
ANISOU 1388  CG1 ILE A 192     3744   5486   5602   1074    751   -583       C  
ATOM   1389  CG2 ILE A 192     194.618  17.714 526.359  1.00 37.01           C  
ANISOU 1389  CG2 ILE A 192     3287   5361   5414   1174    621   -409       C  
ATOM   1390  CD1 ILE A 192     193.974  16.654 523.656  1.00 36.58           C  
ANISOU 1390  CD1 ILE A 192     3398   5166   5334   1247    840   -628       C  
ATOM   1391  N   ALA A 193     194.025  21.292 526.938  1.00 40.49           N  
ANISOU 1391  N   ALA A 193     3615   6041   5727    765    500   -383       N  
ATOM   1392  CA  ALA A 193     194.758  22.051 527.944  1.00 39.85           C  
ANISOU 1392  CA  ALA A 193     3420   6066   5654    724    394   -328       C  
ATOM   1393  C   ALA A 193     193.842  22.880 528.836  1.00 44.13           C  
ANISOU 1393  C   ALA A 193     4060   6581   6127    597    316   -320       C  
ATOM   1394  O   ALA A 193     194.152  23.079 530.016  1.00 53.99           O  
ANISOU 1394  O   ALA A 193     5289   7869   7354    596    206   -277       O  
ATOM   1395  CB  ALA A 193     195.788  22.958 527.269  1.00 50.63           C  
ANISOU 1395  CB  ALA A 193     4605   7569   7062    673    428   -333       C  
ATOM   1396  N   ALA A 194     192.720  23.363 528.307  1.00 43.53           N  
ANISOU 1396  N   ALA A 194     4088   6442   6009    502    366   -364       N  
ATOM   1397  CA  ALA A 194     191.865  24.298 529.026  1.00 39.99           C  
ANISOU 1397  CA  ALA A 194     3718   5975   5503    387    312   -365       C  
ATOM   1398  C   ALA A 194     190.597  23.663 529.582  1.00 51.75           C  
ANISOU 1398  C   ALA A 194     5360   7348   6956    396    320   -359       C  
ATOM   1399  O   ALA A 194     189.831  24.351 530.265  1.00 59.70           O  
ANISOU 1399  O   ALA A 194     6435   8338   7912    321    290   -359       O  
ATOM   1400  CB  ALA A 194     191.491  25.474 528.118  1.00 39.57           C  
ANISOU 1400  CB  ALA A 194     3659   5940   5436    273    357   -406       C  
ATOM   1401  N   PHE A 195     190.350  22.381 529.316  1.00 47.49           N  
ANISOU 1401  N   PHE A 195     4875   6720   6449    485    369   -356       N  
ATOM   1402  CA  PHE A 195     189.139  21.751 529.832  1.00 41.48           C  
ANISOU 1402  CA  PHE A 195     4246   5839   5676    476    389   -343       C  
ATOM   1403  C   PHE A 195     189.400  20.359 530.395  1.00 44.35           C  
ANISOU 1403  C   PHE A 195     4659   6121   6073    594    391   -284       C  
ATOM   1404  O   PHE A 195     189.143  20.109 531.577  1.00 44.71           O  
ANISOU 1404  O   PHE A 195     4773   6137   6080    610    359   -213       O  
ATOM   1405  CB  PHE A 195     188.065  21.672 528.745  1.00 30.44           C  
ANISOU 1405  CB  PHE A 195     2900   4367   4298    419    456   -414       C  
ATOM   1406  CG  PHE A 195     186.843  20.901 529.162  1.00 27.51           C  
ANISOU 1406  CG  PHE A 195     2635   3867   3950    400    486   -404       C  
ATOM   1407  CD1 PHE A 195     185.929  21.452 530.044  1.00 28.16           C  
ANISOU 1407  CD1 PHE A 195     2764   3941   3996    328    479   -374       C  
ATOM   1408  CD2 PHE A 195     186.613  19.623 528.679  1.00 24.27           C  
ANISOU 1408  CD2 PHE A 195     2277   3338   3605    451    529   -427       C  
ATOM   1409  CE1 PHE A 195     184.809  20.745 530.436  1.00 23.30           C  
ANISOU 1409  CE1 PHE A 195     2225   3212   3414    302    525   -354       C  
ATOM   1410  CE2 PHE A 195     185.492  18.911 529.067  1.00 28.02           C  
ANISOU 1410  CE2 PHE A 195     2839   3685   4124    413    561   -412       C  
ATOM   1411  CZ  PHE A 195     184.589  19.474 529.945  1.00 23.99           C  
ANISOU 1411  CZ  PHE A 195     2354   3178   3582    335    564   -369       C  
ATOM   1412  N   TYR A 196     189.905  19.447 529.560  1.00 29.54           N  
ANISOU 1412  N   TYR A 196     2762   4202   4261    685    436   -311       N  
ATOM   1413  CA  TYR A 196     189.997  18.047 529.964  1.00 34.82           C  
ANISOU 1413  CA  TYR A 196     3503   4749   4977    800    452   -261       C  
ATOM   1414  C   TYR A 196     190.956  17.864 531.135  1.00 41.30           C  
ANISOU 1414  C   TYR A 196     4287   5630   5774    901    372   -159       C  
ATOM   1415  O   TYR A 196     190.622  17.200 532.124  1.00 44.54           O  
ANISOU 1415  O   TYR A 196     4799   5957   6166    943    357    -73       O  
ATOM   1416  CB  TYR A 196     190.412  17.183 528.772  1.00 33.72           C  
ANISOU 1416  CB  TYR A 196     3353   4549   4909    890    518   -330       C  
ATOM   1417  CG  TYR A 196     189.282  16.942 527.796  1.00 50.53           C  
ANISOU 1417  CG  TYR A 196     5569   6573   7057    810    579   -427       C  
ATOM   1418  CD1 TYR A 196     188.309  15.986 528.057  1.00 46.97           C  
ANISOU 1418  CD1 TYR A 196     5242   5947   6658    791    605   -422       C  
ATOM   1419  CD2 TYR A 196     189.182  17.675 526.621  1.00 55.03           C  
ANISOU 1419  CD2 TYR A 196     6095   7219   7596    750    605   -519       C  
ATOM   1420  CE1 TYR A 196     187.271  15.763 527.174  1.00 38.03           C  
ANISOU 1420  CE1 TYR A 196     4171   4724   5554    707    638   -521       C  
ATOM   1421  CE2 TYR A 196     188.146  17.459 525.731  1.00 46.76           C  
ANISOU 1421  CE2 TYR A 196     5126   6088   6553    683    635   -612       C  
ATOM   1422  CZ  TYR A 196     187.194  16.501 526.013  1.00 41.43           C  
ANISOU 1422  CZ  TYR A 196     4557   5245   5940    659    643   -620       C  
ATOM   1423  OH  TYR A 196     186.161  16.280 525.132  1.00 49.71           O  
ANISOU 1423  OH  TYR A 196     5667   6216   7006    582    651   -723       O  
ATOM   1424  N   LEU A 197     192.151  18.448 531.046  1.00 36.76           N  
ANISOU 1424  N   LEU A 197     3565   5204   5199    939    317   -160       N  
ATOM   1425  CA  LEU A 197     193.094  18.351 532.161  1.00 41.58           C  
ANISOU 1425  CA  LEU A 197     4120   5893   5784   1032    210    -70       C  
ATOM   1426  C   LEU A 197     192.566  19.009 533.429  1.00 43.78           C  
ANISOU 1426  C   LEU A 197     4476   6205   5954    954    131    -21       C  
ATOM   1427  O   LEU A 197     192.684  18.397 534.507  1.00 46.00           O  
ANISOU 1427  O   LEU A 197     4831   6460   6188   1043     75     74       O  
ATOM   1428  CB  LEU A 197     194.453  18.925 531.746  1.00 47.51           C  
ANISOU 1428  CB  LEU A 197     4667   6808   6579   1064    165    -92       C  
ATOM   1429  CG  LEU A 197     195.238  18.127 530.703  1.00 53.43           C  
ANISOU 1429  CG  LEU A 197     5328   7546   7429   1194    245   -121       C  
ATOM   1430  CD1 LEU A 197     196.608  18.746 530.475  1.00 47.23           C  
ANISOU 1430  CD1 LEU A 197     4312   6940   6693   1221    203   -123       C  
ATOM   1431  CD2 LEU A 197     195.366  16.671 531.126  1.00 54.19           C  
ANISOU 1431  CD2 LEU A 197     5509   7516   7565   1371    248    -54       C  
ATOM   1432  N   PRO A 198     191.990  20.220 533.401  1.00 37.55           N  
ANISOU 1432  N   PRO A 198     3688   5467   5112    805    127    -77       N  
ATOM   1433  CA  PRO A 198     191.365  20.742 534.629  1.00 38.39           C  
ANISOU 1433  CA  PRO A 198     3897   5585   5104    748     74    -40       C  
ATOM   1434  C   PRO A 198     190.265  19.847 535.176  1.00 48.40           C  
ANISOU 1434  C   PRO A 198     5334   6711   6345    770    148     24       C  
ATOM   1435  O   PRO A 198     190.148  19.700 536.399  1.00 75.35           O  
ANISOU 1435  O   PRO A 198     8841  10129   9659    807    103    104       O  
ATOM   1436  CB  PRO A 198     190.823  22.108 534.189  1.00 31.67           C  
ANISOU 1436  CB  PRO A 198     3023   4777   4233    594     91   -127       C  
ATOM   1437  CG  PRO A 198     191.717  22.518 533.084  1.00 30.23           C  
ANISOU 1437  CG  PRO A 198     2685   4669   4133    580     94   -182       C  
ATOM   1438  CD  PRO A 198     192.049  21.253 532.347  1.00 30.66           C  
ANISOU 1438  CD  PRO A 198     2719   4660   4270    697    160   -167       C  
ATOM   1439  N   VAL A 199     189.454  19.241 534.305  1.00 36.26           N  
ANISOU 1439  N   VAL A 199     3840   5048   4890    743    259    -10       N  
ATOM   1440  CA  VAL A 199     188.392  18.353 534.773  1.00 37.64           C  
ANISOU 1440  CA  VAL A 199     4158   5075   5070    742    340     52       C  
ATOM   1441  C   VAL A 199     188.984  17.133 535.468  1.00 45.88           C  
ANISOU 1441  C   VAL A 199     5265   6050   6117    890    319    168       C  
ATOM   1442  O   VAL A 199     188.486  16.693 536.512  1.00 49.49           O  
ANISOU 1442  O   VAL A 199     5847   6446   6510    911    340    272       O  
ATOM   1443  CB  VAL A 199     187.470  17.953 533.605  1.00 40.84           C  
ANISOU 1443  CB  VAL A 199     4576   5360   5580    673    440    -26       C  
ATOM   1444  CG1 VAL A 199     186.589  16.776 533.997  1.00 36.62           C  
ANISOU 1444  CG1 VAL A 199     4168   4650   5096    679    522     43       C  
ATOM   1445  CG2 VAL A 199     186.610  19.132 533.186  1.00 42.09           C  
ANISOU 1445  CG2 VAL A 199     4704   5573   5715    535    459   -108       C  
ATOM   1446  N   ILE A 200     190.058  16.572 534.907  1.00 41.10           N  
ANISOU 1446  N   ILE A 200     4579   5453   5584   1005    287    161       N  
ATOM   1447  CA  ILE A 200     190.701  15.417 535.530  1.00 40.81           C  
ANISOU 1447  CA  ILE A 200     4597   5348   5562   1172    259    276       C  
ATOM   1448  C   ILE A 200     191.310  15.806 536.872  1.00 42.88           C  
ANISOU 1448  C   ILE A 200     4867   5736   5689   1234    134    373       C  
ATOM   1449  O   ILE A 200     191.216  15.059 537.855  1.00 34.87           O  
ANISOU 1449  O   ILE A 200     3981   4653   4617   1323    124    504       O  
ATOM   1450  CB  ILE A 200     191.755  14.816 534.581  1.00 42.39           C  
ANISOU 1450  CB  ILE A 200     4689   5543   5875   1297    256    234       C  
ATOM   1451  CG1 ILE A 200     191.091  14.293 533.306  1.00 42.19           C  
ANISOU 1451  CG1 ILE A 200     4697   5374   5958   1248    376    132       C  
ATOM   1452  CG2 ILE A 200     192.526  13.704 535.272  1.00 43.37           C  
ANISOU 1452  CG2 ILE A 200     4857   5606   6016   1494    211    360       C  
ATOM   1453  CD1 ILE A 200     192.070  13.761 532.285  1.00 33.40           C  
ANISOU 1453  CD1 ILE A 200     3491   4259   4939   1373    397     69       C  
ATOM   1454  N   ILE A 201     191.936  16.984 536.937  1.00 32.98           N  
ANISOU 1454  N   ILE A 201     3487   4665   4380   1184     33    312       N  
ATOM   1455  CA  ILE A 201     192.537  17.443 538.187  1.00 38.30           C  
ANISOU 1455  CA  ILE A 201     4164   5471   4916   1230   -112    377       C  
ATOM   1456  C   ILE A 201     191.469  17.610 539.261  1.00 55.44           C  
ANISOU 1456  C   ILE A 201     6520   7601   6942   1172    -79    437       C  
ATOM   1457  O   ILE A 201     191.634  17.162 540.401  1.00 35.66           O  
ANISOU 1457  O   ILE A 201     4124   5104   4320   1272   -139    556       O  
ATOM   1458  CB  ILE A 201     193.319  18.749 537.957  1.00 36.17           C  
ANISOU 1458  CB  ILE A 201     3722   5385   4638   1152   -221    278       C  
ATOM   1459  CG1 ILE A 201     194.540  18.489 537.074  1.00 40.43           C  
ANISOU 1459  CG1 ILE A 201     4063   5985   5313   1236   -251    249       C  
ATOM   1460  CG2 ILE A 201     193.739  19.363 539.285  1.00 39.53           C  
ANISOU 1460  CG2 ILE A 201     4173   5940   4905   1164   -383    314       C  
ATOM   1461  CD1 ILE A 201     195.348  19.730 536.768  1.00 39.76           C  
ANISOU 1461  CD1 ILE A 201     3788   6068   5250   1143   -339    161       C  
ATOM   1462  N   MET A 202     190.353  18.254 538.910  1.00 52.88           N  
ANISOU 1462  N   MET A 202     6234   7239   6619   1021     23    362       N  
ATOM   1463  CA  MET A 202     189.278  18.443 539.879  1.00 42.75           C  
ANISOU 1463  CA  MET A 202     5111   5923   5209    967     85    413       C  
ATOM   1464  C   MET A 202     188.621  17.123 540.258  1.00 42.13           C  
ANISOU 1464  C   MET A 202     5180   5676   5150   1030    198    544       C  
ATOM   1465  O   MET A 202     188.113  16.984 541.377  1.00 40.64           O  
ANISOU 1465  O   MET A 202     5139   5476   4827   1049    230    645       O  
ATOM   1466  CB  MET A 202     188.238  19.418 539.327  1.00 41.34           C  
ANISOU 1466  CB  MET A 202     4914   5740   5054    805    172    300       C  
ATOM   1467  CG  MET A 202     188.781  20.812 539.066  1.00 47.97           C  
ANISOU 1467  CG  MET A 202     5639   6722   5867    731     72    183       C  
ATOM   1468  SD  MET A 202     187.553  21.936 538.378  0.85 59.94           S  
ANISOU 1468  SD  MET A 202     7142   8214   7417    567    172     66       S  
ATOM   1469  CE  MET A 202     187.028  21.030 536.926  1.00 66.30           C  
ANISOU 1469  CE  MET A 202     7897   8886   8407    548    290     43       C  
ATOM   1470  N   THR A 203     188.621  16.146 539.349  1.00 45.15           N  
ANISOU 1470  N   THR A 203     5538   5922   5696   1061    268    545       N  
ATOM   1471  CA  THR A 203     188.058  14.838 539.670  1.00 41.50           C  
ANISOU 1471  CA  THR A 203     5217   5271   5279   1113    374    671       C  
ATOM   1472  C   THR A 203     188.942  14.088 540.658  1.00 49.94           C  
ANISOU 1472  C   THR A 203     6368   6344   6261   1294    288    826       C  
ATOM   1473  O   THR A 203     188.439  13.469 541.604  1.00 50.70           O  
ANISOU 1473  O   THR A 203     6631   6353   6278   1332    350    973       O  
ATOM   1474  CB  THR A 203     187.863  14.019 538.394  1.00 36.18           C  
ANISOU 1474  CB  THR A 203     4503   4439   4806   1097    456    605       C  
ATOM   1475  OG1 THR A 203     186.969  14.709 537.512  1.00 32.63           O  
ANISOU 1475  OG1 THR A 203     3987   3991   4419    934    522    470       O  
ATOM   1476  CG2 THR A 203     187.287  12.649 538.720  1.00 39.90           C  
ANISOU 1476  CG2 THR A 203     5127   4686   5348   1136    564    731       C  
ATOM   1477  N   VAL A 204     190.261  14.132 540.458  1.00 50.41           N  
ANISOU 1477  N   VAL A 204     6309   6509   6335   1413    147    806       N  
ATOM   1478  CA  VAL A 204     191.174  13.486 541.396  1.00 42.77           C  
ANISOU 1478  CA  VAL A 204     5399   5570   5283   1603     35    953       C  
ATOM   1479  C   VAL A 204     191.137  14.191 542.747  1.00 44.08           C  
ANISOU 1479  C   VAL A 204     5655   5880   5213   1603    -57   1017       C  
ATOM   1480  O   VAL A 204     191.094  13.543 543.802  1.00 44.23           O  
ANISOU 1480  O   VAL A 204     5839   5857   5108   1712    -66   1182       O  
ATOM   1481  CB  VAL A 204     192.597  13.449 540.812  1.00 43.65           C  
ANISOU 1481  CB  VAL A 204     5321   5781   5484   1726    -97    903       C  
ATOM   1482  CG1 VAL A 204     193.565  12.837 541.808  1.00 42.82           C  
ANISOU 1482  CG1 VAL A 204     5254   5724   5290   1937   -239   1055       C  
ATOM   1483  CG2 VAL A 204     192.612  12.674 539.505  1.00 55.13           C  
ANISOU 1483  CG2 VAL A 204     6717   7083   7147   1747     11    837       C  
ATOM   1484  N   LEU A 205     191.149  15.526 542.737  1.00 42.66           N  
ANISOU 1484  N   LEU A 205     5386   5864   4960   1486   -125    887       N  
ATOM   1485  CA  LEU A 205     191.096  16.281 543.985  1.00 43.97           C  
ANISOU 1485  CA  LEU A 205     5649   6166   4892   1480   -216    915       C  
ATOM   1486  C   LEU A 205     189.811  15.988 544.748  1.00 44.76           C  
ANISOU 1486  C   LEU A 205     5965   6162   4879   1438    -53   1015       C  
ATOM   1487  O   LEU A 205     189.840  15.734 545.957  1.00 56.23           O  
ANISOU 1487  O   LEU A 205     7580   7648   6136   1532    -90   1146       O  
ATOM   1488  CB  LEU A 205     191.228  17.778 543.703  1.00 44.22           C  
ANISOU 1488  CB  LEU A 205     5553   6351   4899   1342   -294    739       C  
ATOM   1489  CG  LEU A 205     192.619  18.261 543.290  1.00 47.67           C  
ANISOU 1489  CG  LEU A 205     5778   6934   5400   1377   -481    657       C  
ATOM   1490  CD1 LEU A 205     192.620  19.763 543.062  1.00 40.04           C  
ANISOU 1490  CD1 LEU A 205     4715   6086   4414   1217   -537    494       C  
ATOM   1491  CD2 LEU A 205     193.650  17.875 544.337  1.00 41.38           C  
ANISOU 1491  CD2 LEU A 205     5003   6244   4474   1546   -674    763       C  
ATOM   1492  N   TYR A 206     188.669  16.010 544.054  1.00 49.39           N  
ANISOU 1492  N   TYR A 206     6553   6628   5586   1299    130    959       N  
ATOM   1493  CA  TYR A 206     187.419  15.655 544.716  1.00 52.76           C  
ANISOU 1493  CA  TYR A 206     7155   6949   5942   1252    309   1062       C  
ATOM   1494  C   TYR A 206     187.437  14.212 545.198  1.00 54.56           C  
ANISOU 1494  C   TYR A 206     7529   7022   6180   1375    373   1264       C  
ATOM   1495  O   TYR A 206     186.809  13.890 546.212  1.00 53.93           O  
ANISOU 1495  O   TYR A 206     7630   6903   5959   1396    471   1406       O  
ATOM   1496  CB  TYR A 206     186.224  15.878 543.789  1.00 37.59           C  
ANISOU 1496  CB  TYR A 206     5171   4928   4183   1082    478    962       C  
ATOM   1497  CG  TYR A 206     184.932  15.406 544.413  1.00 38.45           C  
ANISOU 1497  CG  TYR A 206     5428   4920   4259   1027    679   1076       C  
ATOM   1498  CD1 TYR A 206     184.273  16.183 545.355  1.00 38.81           C  
ANISOU 1498  CD1 TYR A 206     5566   5061   4118    989    738   1086       C  
ATOM   1499  CD2 TYR A 206     184.387  14.170 544.086  1.00 39.17           C  
ANISOU 1499  CD2 TYR A 206     5569   4803   4511   1014    816   1174       C  
ATOM   1500  CE1 TYR A 206     183.103  15.751 545.944  1.00 64.19           C  
ANISOU 1500  CE1 TYR A 206     8902   8181   7307    942    943   1201       C  
ATOM   1501  CE2 TYR A 206     183.216  13.729 544.671  1.00 60.07           C  
ANISOU 1501  CE2 TYR A 206     8335   7343   7148    950   1011   1290       C  
ATOM   1502  CZ  TYR A 206     182.578  14.525 545.598  1.00 67.07           C  
ANISOU 1502  CZ  TYR A 206     9295   8342   7847    915   1081   1308       C  
ATOM   1503  OH  TYR A 206     181.411  14.094 546.185  1.00 79.81           O  
ANISOU 1503  OH  TYR A 206    11011   9859   9454    852   1297   1431       O  
ATOM   1504  N   TRP A 207     188.133  13.329 544.482  1.00 48.11           N  
ANISOU 1504  N   TRP A 207     6644   6105   5530   1463    333   1283       N  
ATOM   1505  CA  TRP A 207     188.241  11.944 544.926  1.00 45.67           C  
ANISOU 1505  CA  TRP A 207     6482   5626   5243   1597    384   1478       C  
ATOM   1506  C   TRP A 207     188.977  11.857 546.257  1.00 54.64           C  
ANISOU 1506  C   TRP A 207     7744   6878   6139   1768    248   1632       C  
ATOM   1507  O   TRP A 207     188.540  11.151 547.175  1.00 50.89           O  
ANISOU 1507  O   TRP A 207     7473   6308   5555   1830    338   1824       O  
ATOM   1508  CB  TRP A 207     188.950  11.110 543.859  1.00 46.16           C  
ANISOU 1508  CB  TRP A 207     6441   5570   5530   1677    353   1442       C  
ATOM   1509  CG  TRP A 207     188.810   9.631 544.035  1.00 62.07           C  
ANISOU 1509  CG  TRP A 207     8608   7340   7634   1779    449   1616       C  
ATOM   1510  CD1 TRP A 207     187.957   8.980 544.876  1.00 73.32           C  
ANISOU 1510  CD1 TRP A 207    10238   8622   8997   1764    591   1794       C  
ATOM   1511  CD2 TRP A 207     189.549   8.616 543.346  1.00 76.90           C  
ANISOU 1511  CD2 TRP A 207    10453   9075   9690   1914    422   1630       C  
ATOM   1512  NE1 TRP A 207     188.117   7.621 544.753  1.00 80.93           N  
ANISOU 1512  NE1 TRP A 207    11306   9348  10098   1872    648   1924       N  
ATOM   1513  CE2 TRP A 207     189.090   7.372 543.821  1.00 84.72           C  
ANISOU 1513  CE2 TRP A 207    11645   9820  10724   1973    542   1819       C  
ATOM   1514  CE3 TRP A 207     190.554   8.638 542.374  1.00 72.58           C  
ANISOU 1514  CE3 TRP A 207     9727   8579   9269   1996    320   1502       C  
ATOM   1515  CZ2 TRP A 207     189.601   6.162 543.358  1.00 90.59           C  
ANISOU 1515  CZ2 TRP A 207    12428  10355  11638   2115    553   1875       C  
ATOM   1516  CZ3 TRP A 207     191.060   7.435 541.915  1.00 75.68           C  
ANISOU 1516  CZ3 TRP A 207    10151   8782   9822   2146    339   1554       C  
ATOM   1517  CH2 TRP A 207     190.583   6.215 542.407  1.00 87.32           C  
ANISOU 1517  CH2 TRP A 207    11839   9999  11340   2206    449   1734       C  
ATOM   1518  N   HIS A 208     190.089  12.586 546.389  1.00 60.74           N  
ANISOU 1518  N   HIS A 208     8397   7859   6823   1842     30   1553       N  
ATOM   1519  CA  HIS A 208     190.832  12.572 547.644  1.00 56.73           C  
ANISOU 1519  CA  HIS A 208     7996   7484   6073   2005   -137   1681       C  
ATOM   1520  C   HIS A 208     190.077  13.283 548.760  1.00 51.11           C  
ANISOU 1520  C   HIS A 208     7454   6870   5096   1942    -94   1709       C  
ATOM   1521  O   HIS A 208     190.210  12.907 549.930  1.00 56.69           O  
ANISOU 1521  O   HIS A 208     8350   7610   5580   2072   -137   1878       O  
ATOM   1522  CB  HIS A 208     192.208  13.207 547.449  1.00 58.88           C  
ANISOU 1522  CB  HIS A 208     8067   7961   6345   2079   -393   1570       C  
ATOM   1523  CG  HIS A 208     193.081  12.466 546.485  1.00 62.22           C  
ANISOU 1523  CG  HIS A 208     8328   8312   7003   2183   -437   1560       C  
ATOM   1524  ND1 HIS A 208     193.380  11.129 546.631  1.00 66.01           N  
ANISOU 1524  ND1 HIS A 208     8903   8635   7544   2365   -414   1735       N  
ATOM   1525  CD2 HIS A 208     193.722  12.876 545.366  1.00 62.89           C  
ANISOU 1525  CD2 HIS A 208     8169   8456   7272   2141   -489   1398       C  
ATOM   1526  CE1 HIS A 208     194.165  10.746 545.640  1.00 65.45           C  
ANISOU 1526  CE1 HIS A 208     8650   8530   7686   2438   -451   1669       C  
ATOM   1527  NE2 HIS A 208     194.390  11.788 544.860  1.00 64.49           N  
ANISOU 1527  NE2 HIS A 208     8320   8546   7637   2303   -492   1468       N  
ATOM   1528  N   ILE A 209     189.288  14.305 548.427  1.00 48.61           N  
ANISOU 1528  N   ILE A 209     7081   6601   4789   1757     -6   1550       N  
ATOM   1529  CA  ILE A 209     188.521  15.014 549.448  1.00 50.23           C  
ANISOU 1529  CA  ILE A 209     7446   6893   4748   1703     58   1561       C  
ATOM   1530  C   ILE A 209     187.387  14.136 549.966  1.00 54.88           C  
ANISOU 1530  C   ILE A 209     8236   7313   5303   1696    307   1747       C  
ATOM   1531  O   ILE A 209     187.160  14.035 551.178  1.00 59.06           O  
ANISOU 1531  O   ILE A 209     8975   7889   5575   1774    338   1886       O  
ATOM   1532  CB  ILE A 209     187.995  16.349 548.892  1.00 57.20           C  
ANISOU 1532  CB  ILE A 209     8204   7857   5674   1522     88   1338       C  
ATOM   1533  CG1 ILE A 209     189.160  17.295 548.594  1.00 45.97           C  
ANISOU 1533  CG1 ILE A 209     6607   6610   4249   1524   -162   1174       C  
ATOM   1534  CG2 ILE A 209     187.020  16.991 549.868  1.00 74.30           C  
ANISOU 1534  CG2 ILE A 209    10541  10079   7612   1470    207   1346       C  
ATOM   1535  CD1 ILE A 209     188.805  18.419 547.649  1.00 42.04           C  
ANISOU 1535  CD1 ILE A 209     5948   6140   3886   1348   -130    964       C  
ATOM   1536  N   SER A 210     186.661  13.486 549.054  1.00 65.39           N  
ANISOU 1536  N   SER A 210     9509   8445   6891   1598    490   1752       N  
ATOM   1537  CA  SER A 210     185.567  12.610 549.462  1.00 64.24           C  
ANISOU 1537  CA  SER A 210     9528   8119   6762   1565    737   1928       C  
ATOM   1538  C   SER A 210     186.088  11.386 550.202  1.00 67.78           C  
ANISOU 1538  C   SER A 210    10158   8467   7130   1748    717   2175       C  
ATOM   1539  O   SER A 210     185.451  10.910 551.149  1.00 66.09           O  
ANISOU 1539  O   SER A 210    10151   8189   6769   1774    870   2367       O  
ATOM   1540  CB  SER A 210     184.744  12.194 548.243  1.00 64.20           C  
ANISOU 1540  CB  SER A 210     9399   7922   7072   1408    901   1854       C  
ATOM   1541  OG  SER A 210     185.541  11.498 547.300  1.00 77.30           O  
ANISOU 1541  OG  SER A 210    10952   9479   8938   1468    804   1822       O  
ATOM   1542  N   ARG A 211     187.243  10.858 549.787  1.00 80.88           N  
ANISOU 1542  N   ARG A 211    11741  10107   8882   1884    539   2184       N  
ATOM   1543  CA  ARG A 211     187.855   9.773 550.545  1.00 87.15           C  
ANISOU 1543  CA  ARG A 211    12708  10824   9583   2090    487   2422       C  
ATOM   1544  C   ARG A 211     188.443  10.257 551.864  1.00 90.86           C  
ANISOU 1544  C   ARG A 211    13315  11512   9697   2234    320   2506       C  
ATOM   1545  O   ARG A 211     188.656   9.443 552.769  1.00 93.20           O  
ANISOU 1545  O   ARG A 211    13817  11756   9839   2398    316   2741       O  
ATOM   1546  CB  ARG A 211     188.930   9.076 549.710  1.00 94.70           C  
ANISOU 1546  CB  ARG A 211    13532  11700  10751   2215    347   2401       C  
ATOM   1547  CG  ARG A 211     188.378   7.993 548.794  1.00 97.19           C  
ANISOU 1547  CG  ARG A 211    13845  11718  11366   2153    531   2433       C  
ATOM   1548  CD  ARG A 211     189.480   7.114 548.220  1.00102.95           C  
ANISOU 1548  CD  ARG A 211    14507  12348  12260   2334    409   2460       C  
ATOM   1549  NE  ARG A 211     190.064   7.673 547.005  1.00106.51           N  
ANISOU 1549  NE  ARG A 211    14698  12887  12885   2287    307   2218       N  
ATOM   1550  CZ  ARG A 211     191.190   8.377 546.967  1.00108.00           C  
ANISOU 1550  CZ  ARG A 211    14724  13306  13005   2379     84   2121       C  
ATOM   1551  NH1 ARG A 211     191.868   8.613 548.083  1.00113.51           N  
ANISOU 1551  NH1 ARG A 211    15490  14176  13462   2524    -86   2230       N  
ATOM   1552  NH2 ARG A 211     191.641   8.842 545.810  1.00 98.73           N  
ANISOU 1552  NH2 ARG A 211    13319  12193  12001   2321     32   1917       N  
ATOM   1553  N   ALA A 212     188.702  11.559 551.995  1.00 92.70           N  
ANISOU 1553  N   ALA A 212    13450  11981   9791   2177    178   2319       N  
ATOM   1554  CA  ALA A 212     189.165  12.104 553.267  1.00 87.85           C  
ANISOU 1554  CA  ALA A 212    12979  11580   8821   2293     15   2368       C  
ATOM   1555  C   ALA A 212     188.012  12.273 554.247  1.00 92.39           C  
ANISOU 1555  C   ALA A 212    13791  12152   9159   2240    229   2469       C  
ATOM   1556  O   ALA A 212     188.164  11.995 555.442  1.00104.57           O  
ANISOU 1556  O   ALA A 212    15565  13760  10406   2386    192   2646       O  
ATOM   1557  CB  ALA A 212     189.877  13.437 553.042  1.00 82.95           C  
ANISOU 1557  CB  ALA A 212    12171  11192   8154   2240   -218   2119       C  
ATOM   1558  N   SER A 213     186.854  12.729 553.762  1.00 90.58           N  
ANISOU 1558  N   SER A 213    13506  11858   9050   2042    455   2364       N  
ATOM   1559  CA  SER A 213     185.672  12.810 554.612  1.00 92.45           C  
ANISOU 1559  CA  SER A 213    13944  12079   9105   1989    703   2468       C  
ATOM   1560  C   SER A 213     185.129  11.433 554.970  1.00 88.12           C  
ANISOU 1560  C   SER A 213    13576  11310   8595   2038    921   2753       C  
ATOM   1561  O   SER A 213     184.373  11.310 555.940  1.00 84.70           O  
ANISOU 1561  O   SER A 213    13357  10877   7950   2049   1111   2908       O  
ATOM   1562  CB  SER A 213     184.583  13.635 553.924  1.00 98.90           C  
ANISOU 1562  CB  SER A 213    14620  12880  10077   1772    883   2280       C  
ATOM   1563  OG  SER A 213     185.035  14.950 553.647  1.00107.70           O  
ANISOU 1563  OG  SER A 213    15594  14181  11148   1724    698   2029       O  
ATOM   1564  N   LYS A 214     185.496  10.403 554.214  1.00162.26           N  
ANISOU 1564  N   LYS A 214    23511  20609  17532   7478   1573    -66       N  
ATOM   1565  CA  LYS A 214     185.060   9.039 554.489  1.00151.86           C  
ANISOU 1565  CA  LYS A 214    22540  19154  16008   7385    809    -55       C  
ATOM   1566  C   LYS A 214     185.959   8.377 555.528  1.00147.60           C  
ANISOU 1566  C   LYS A 214    21616  18631  15833   7272    554   -108       C  
ATOM   1567  O   LYS A 214     185.478   7.801 556.504  1.00147.29           O  
ANISOU 1567  O   LYS A 214    21468  18697  15797   6880    -39    -27       O  
ATOM   1568  CB  LYS A 214     185.047   8.215 553.200  1.00149.48           C  
ANISOU 1568  CB  LYS A 214    22953  18500  15342   7896    729   -121       C  
ATOM   1569  CG  LYS A 214     184.853   6.722 553.411  1.00148.29           C  
ANISOU 1569  CG  LYS A 214    23155  18120  15070   7882    -38   -142       C  
ATOM   1570  CD  LYS A 214     184.965   5.966 552.097  1.00151.29           C  
ANISOU 1570  CD  LYS A 214    24225  18142  15116   8458    -83   -263       C  
ATOM   1571  CE  LYS A 214     184.914   4.463 552.315  1.00150.86           C  
ANISOU 1571  CE  LYS A 214    24494  17806  15019   8475   -849   -310       C  
ATOM   1572  NZ  LYS A 214     183.640   4.035 552.955  1.00146.84           N  
ANISOU 1572  NZ  LYS A 214    24063  17339  14389   7947  -1565   -153       N  
ATOM   1573  N   ALA A1001     185.889  12.371 564.598  1.00173.81           N  
ANISOU 1573  N   ALA A1001    20792  24485  20762   4568    -84   -198       N  
ATOM   1574  CA  ALA A1001     185.357  11.984 563.296  1.00174.80           C  
ANISOU 1574  CA  ALA A1001    21528  24301  20586   4764      0    -84       C  
ATOM   1575  C   ALA A1001     183.985  11.333 563.440  1.00176.69           C  
ANISOU 1575  C   ALA A1001    22133  24649  20351   4468   -528    139       C  
ATOM   1576  O   ALA A1001     183.040  11.696 562.741  1.00177.38           O  
ANISOU 1576  O   ALA A1001    22500  24720  20175   4433   -435    210       O  
ATOM   1577  CB  ALA A1001     186.320  11.043 562.589  1.00174.63           C  
ANISOU 1577  CB  ALA A1001    21812  23874  20664   5163     28   -119       C  
ATOM   1578  N   ASP A1002     183.885  10.366 564.354  1.00174.57           N  
ANISOU 1578  N   ASP A1002    21851  24484  19993   4256  -1089    262       N  
ATOM   1579  CA  ASP A1002     182.615   9.685 564.585  1.00173.88           C  
ANISOU 1579  CA  ASP A1002    22057  24498  19509   3940  -1610    509       C  
ATOM   1580  C   ASP A1002     181.660  10.561 565.389  1.00169.19           C  
ANISOU 1580  C   ASP A1002    21106  24391  18787   3553  -1622    557       C  
ATOM   1581  O   ASP A1002     180.504  10.757 564.995  1.00172.77           O  
ANISOU 1581  O   ASP A1002    21772  24911  18962   3395  -1681    668       O  
ATOM   1582  CB  ASP A1002     182.862   8.353 565.297  1.00179.75           C  
ANISOU 1582  CB  ASP A1002    22901  25173  20223   3843  -2189    664       C  
ATOM   1583  CG  ASP A1002     181.719   7.370 565.118  1.00185.65           C  
ANISOU 1583  CG  ASP A1002    24106  25814  20621   3627  -2718    937       C  
ATOM   1584  OD1 ASP A1002     180.547   7.801 565.124  1.00187.22           O  
ANISOU 1584  OD1 ASP A1002    24318  26235  20582   3357  -2759   1050       O  
ATOM   1585  OD2 ASP A1002     181.995   6.162 564.969  1.00188.77           O  
ANISOU 1585  OD2 ASP A1002    24833  25885  21005   3729  -3107   1034       O  
ATOM   1586  N   LEU A1003     182.132  11.097 566.519  1.00154.73           N  
ANISOU 1586  N   LEU A1003    18725  22908  17159   3418  -1580    452       N  
ATOM   1587  CA  LEU A1003     181.307  11.999 567.316  1.00144.60           C  
ANISOU 1587  CA  LEU A1003    17068  22113  15761   3098  -1565    448       C  
ATOM   1588  C   LEU A1003     180.900  13.232 566.520  1.00148.63           C  
ANISOU 1588  C   LEU A1003    17550  22614  16307   3181  -1076    311       C  
ATOM   1589  O   LEU A1003     179.827  13.800 566.758  1.00146.95           O  
ANISOU 1589  O   LEU A1003    17246  22707  15883   2935  -1113    362       O  
ATOM   1590  CB  LEU A1003     182.055  12.407 568.586  1.00136.28           C  
ANISOU 1590  CB  LEU A1003    15437  21396  14948   3027  -1582    294       C  
ATOM   1591  CG  LEU A1003     181.257  13.161 569.652  1.00128.35           C  
ANISOU 1591  CG  LEU A1003    14025  20958  13785   2705  -1669    283       C  
ATOM   1592  CD1 LEU A1003     180.247  12.240 570.322  1.00129.34           C  
ANISOU 1592  CD1 LEU A1003    14312  21338  13495   2374  -2198    612       C  
ATOM   1593  CD2 LEU A1003     182.189  13.783 570.680  1.00118.48           C  
ANISOU 1593  CD2 LEU A1003    12204  19967  12844   2747  -1588     27       C  
ATOM   1594  N   GLU A1004     181.742  13.659 565.575  1.00149.27           N  
ANISOU 1594  N   GLU A1004    17704  22354  16658   3533   -610    150       N  
ATOM   1595  CA  GLU A1004     181.367  14.751 564.682  1.00152.64           C  
ANISOU 1595  CA  GLU A1004    18183  22708  17105   3644   -141     67       C  
ATOM   1596  C   GLU A1004     180.136  14.387 563.862  1.00153.84           C  
ANISOU 1596  C   GLU A1004    18860  22756  16835   3588   -319    252       C  
ATOM   1597  O   GLU A1004     179.226  15.208 563.695  1.00151.76           O  
ANISOU 1597  O   GLU A1004    18559  22666  16437   3461   -199    251       O  
ATOM   1598  CB  GLU A1004     182.539  15.099 563.763  1.00154.60           C  
ANISOU 1598  CB  GLU A1004    18462  22581  17697   4051    389    -76       C  
ATOM   1599  CG  GLU A1004     183.829  15.440 564.493  1.00148.00           C  
ANISOU 1599  CG  GLU A1004    17088  21797  17348   4127    568   -275       C  
ATOM   1600  CD  GLU A1004     183.786  16.805 565.151  1.00141.81           C  
ANISOU 1600  CD  GLU A1004    15740  21314  16829   3969    814   -454       C  
ATOM   1601  OE1 GLU A1004     183.067  17.690 564.642  1.00140.18           O  
ANISOU 1601  OE1 GLU A1004    15584  21141  16538   3934   1072   -451       O  
ATOM   1602  OE2 GLU A1004     184.470  16.992 566.179  1.00140.81           O  
ANISOU 1602  OE2 GLU A1004    15123  21381  16998   3895    726   -612       O  
ATOM   1603  N   ASP A1005     180.090  13.157 563.344  1.00156.07           N  
ANISOU 1603  N   ASP A1005    19633  22743  16925   3692   -635    395       N  
ATOM   1604  CA  ASP A1005     178.922  12.714 562.591  1.00155.37           C  
ANISOU 1604  CA  ASP A1005    20046  22529  16458   3638   -884    555       C  
ATOM   1605  C   ASP A1005     177.708  12.537 563.493  1.00148.84           C  
ANISOU 1605  C   ASP A1005    19079  22083  15390   3183  -1333    726       C  
ATOM   1606  O   ASP A1005     176.576  12.789 563.061  1.00148.06           O  
ANISOU 1606  O   ASP A1005    19166  22041  15050   3065  -1404    802       O  
ATOM   1607  CB  ASP A1005     179.232  11.410 561.855  1.00161.45           C  
ANISOU 1607  CB  ASP A1005    21359  22864  17121   3878  -1153    633       C  
ATOM   1608  CG  ASP A1005     180.416  11.537 560.916  1.00162.08           C  
ANISOU 1608  CG  ASP A1005    21591  22588  17403   4362   -687    471       C  
ATOM   1609  OD1 ASP A1005     180.691  12.663 560.451  1.00159.78           O  
ANISOU 1609  OD1 ASP A1005    21141  22316  17254   4525   -133    350       O  
ATOM   1610  OD2 ASP A1005     181.071  10.510 560.640  1.00163.75           O  
ANISOU 1610  OD2 ASP A1005    22075  22501  17643   4584   -871    473       O  
ATOM   1611  N   ASN A1006     177.918  12.104 564.738  1.00143.65           N  
ANISOU 1611  N   ASN A1006    18093  21699  14787   2936  -1635    798       N  
ATOM   1612  CA  ASN A1006     176.808  11.979 565.679  1.00133.65           C  
ANISOU 1612  CA  ASN A1006    16640  20852  13287   2507  -2011    985       C  
ATOM   1613  C   ASN A1006     176.172  13.337 565.955  1.00126.24           C  
ANISOU 1613  C   ASN A1006    15329  20305  12330   2371  -1716    861       C  
ATOM   1614  O   ASN A1006     174.962  13.523 565.771  1.00121.61           O  
ANISOU 1614  O   ASN A1006    14838  19864  11504   2180  -1834    965       O  
ATOM   1615  CB  ASN A1006     177.292  11.334 566.979  1.00124.97           C  
ANISOU 1615  CB  ASN A1006    15246  19992  12243   2321  -2334   1083       C  
ATOM   1616  CG  ASN A1006     177.517   9.842 566.844  1.00121.64           C  
ANISOU 1616  CG  ASN A1006    15220  19230  11770   2345  -2782   1290       C  
ATOM   1617  OD1 ASN A1006     178.624   9.393 566.549  1.00121.47           O  
ANISOU 1617  OD1 ASN A1006    15318  18882  11955   2635  -2723   1189       O  
ATOM   1618  ND2 ASN A1006     176.465   9.063 567.066  1.00120.13           N  
ANISOU 1618  ND2 ASN A1006    15216  19101  11326   2040  -3241   1583       N  
ATOM   1619  N   TRP A1007     176.981  14.303 566.400  1.00121.13           N  
ANISOU 1619  N   TRP A1007    14243  19818  11964   2473  -1349    622       N  
ATOM   1620  CA  TRP A1007     176.456  15.637 566.673  1.00119.03           C  
ANISOU 1620  CA  TRP A1007    13608  19892  11726   2374  -1075    467       C  
ATOM   1621  C   TRP A1007     175.871  16.263 565.414  1.00122.95           C  
ANISOU 1621  C   TRP A1007    14414  20146  12153   2530   -788    433       C  
ATOM   1622  O   TRP A1007     174.863  16.979 565.479  1.00126.10           O  
ANISOU 1622  O   TRP A1007    14699  20804  12409   2371   -763    421       O  
ATOM   1623  CB  TRP A1007     177.553  16.525 567.261  1.00119.23           C  
ANISOU 1623  CB  TRP A1007    13133  20032  12137   2498   -746    191       C  
ATOM   1624  CG  TRP A1007     177.025  17.774 567.891  1.00125.44           C  
ANISOU 1624  CG  TRP A1007    13464  21239  12956   2349   -592     20       C  
ATOM   1625  CD1 TRP A1007     177.178  19.052 567.439  1.00130.70           C  
ANISOU 1625  CD1 TRP A1007    13948  21838  13876   2496   -147   -203       C  
ATOM   1626  CD2 TRP A1007     176.245  17.864 569.089  1.00128.54           C  
ANISOU 1626  CD2 TRP A1007    13530  22188  13120   2039   -887     58       C  
ATOM   1627  NE1 TRP A1007     176.547  19.933 568.285  1.00135.77           N  
ANISOU 1627  NE1 TRP A1007    14171  22941  14476   2303   -174   -336       N  
ATOM   1628  CE2 TRP A1007     175.965  19.227 569.305  1.00132.59           C  
ANISOU 1628  CE2 TRP A1007    13671  22948  13759   2033   -613   -186       C  
ATOM   1629  CE3 TRP A1007     175.759  16.923 570.001  1.00120.90           C  
ANISOU 1629  CE3 TRP A1007    12549  21536  11853   1775  -1347    290       C  
ATOM   1630  CZ2 TRP A1007     175.221  19.672 570.395  1.00125.00           C  
ANISOU 1630  CZ2 TRP A1007    12328  22557  12611   1797   -787   -239       C  
ATOM   1631  CZ3 TRP A1007     175.017  17.365 571.079  1.00119.03           C  
ANISOU 1631  CZ3 TRP A1007    11929  21880  11416   1530  -1488    274       C  
ATOM   1632  CH2 TRP A1007     174.757  18.727 571.269  1.00118.30           C  
ANISOU 1632  CH2 TRP A1007    11471  22043  11432   1555  -1209     -5       C  
ATOM   1633  N   GLU A1008     176.489  15.998 564.259  1.00120.06           N  
ANISOU 1633  N   GLU A1008    14448  19297  11873   2864   -571    415       N  
ATOM   1634  CA  GLU A1008     175.921  16.431 562.985  1.00122.70           C  
ANISOU 1634  CA  GLU A1008    15169  19377  12074   3050   -343    418       C  
ATOM   1635  C   GLU A1008     174.499  15.911 562.816  1.00125.47           C  
ANISOU 1635  C   GLU A1008    15814  19815  12044   2823   -767    606       C  
ATOM   1636  O   GLU A1008     173.577  16.673 562.503  1.00130.76           O  
ANISOU 1636  O   GLU A1008    16482  20610  12589   2761   -676    584       O  
ATOM   1637  CB  GLU A1008     176.807  15.958 561.833  1.00122.81           C  
ANISOU 1637  CB  GLU A1008    15619  18881  12162   3460   -121    404       C  
ATOM   1638  CG  GLU A1008     176.104  15.920 560.486  1.00117.41           C  
ANISOU 1638  CG  GLU A1008    15499  17907  11204   3665    -71    468       C  
ATOM   1639  CD  GLU A1008     176.874  15.126 559.450  1.00122.79           C  
ANISOU 1639  CD  GLU A1008    16673  18123  11858   4063     11    477       C  
ATOM   1640  OE1 GLU A1008     178.116  15.053 559.557  1.00123.33           O  
ANISOU 1640  OE1 GLU A1008    16581  18067  12211   4258    266    390       O  
ATOM   1641  OE2 GLU A1008     176.236  14.568 558.532  1.00129.63           O  
ANISOU 1641  OE2 GLU A1008    18080  18751  12422   4195   -194    555       O  
ATOM   1642  N   THR A1009     174.306  14.606 563.026  1.00123.27           N  
ANISOU 1642  N   THR A1009    15775  19455  11607   2694  -1249    795       N  
ATOM   1643  CA  THR A1009     172.969  14.026 562.949  1.00120.29           C  
ANISOU 1643  CA  THR A1009    15629  19150  10926   2438  -1695    993       C  
ATOM   1644  C   THR A1009     172.023  14.697 563.938  1.00121.72           C  
ANISOU 1644  C   THR A1009    15345  19880  11023   2069  -1772   1024       C  
ATOM   1645  O   THR A1009     170.846  14.931 563.627  1.00130.25           O  
ANISOU 1645  O   THR A1009    16517  21061  11911   1935  -1892   1086       O  
ATOM   1646  CB  THR A1009     173.042  12.520 563.209  1.00117.45           C  
ANISOU 1646  CB  THR A1009    15514  18619  10492   2323  -2210   1204       C  
ATOM   1647  OG1 THR A1009     174.045  11.938 562.366  1.00123.46           O  
ANISOU 1647  OG1 THR A1009    16663  18894  11352   2705  -2118   1131       O  
ATOM   1648  CG2 THR A1009     171.706  11.856 562.921  1.00114.38           C  
ANISOU 1648  CG2 THR A1009    15418  18193   9848   2092  -2675   1413       C  
ATOM   1649  N   LEU A1010     172.528  15.034 565.129  1.00116.87           N  
ANISOU 1649  N   LEU A1010    14223  19635  10548   1928  -1704    961       N  
ATOM   1650  CA  LEU A1010     171.682  15.658 566.143  1.00112.44           C  
ANISOU 1650  CA  LEU A1010    13202  19639   9880   1611  -1772    969       C  
ATOM   1651  C   LEU A1010     171.187  17.025 565.684  1.00116.51           C  
ANISOU 1651  C   LEU A1010    13586  20253  10429   1703  -1410    766       C  
ATOM   1652  O   LEU A1010     169.979  17.291 565.685  1.00123.34           O  
ANISOU 1652  O   LEU A1010    14418  21349  11096   1516  -1541    831       O  
ATOM   1653  CB  LEU A1010     172.440  15.774 567.467  1.00115.08           C  
ANISOU 1653  CB  LEU A1010    13046  20332  10346   1513  -1766    898       C  
ATOM   1654  CG  LEU A1010     172.957  14.475 568.093  1.00121.59           C  
ANISOU 1654  CG  LEU A1010    13946  21111  11140   1413  -2140   1108       C  
ATOM   1655  CD1 LEU A1010     173.200  14.649 569.585  1.00123.48           C  
ANISOU 1655  CD1 LEU A1010    13667  21878  11373   1225  -2230   1090       C  
ATOM   1656  CD2 LEU A1010     172.005  13.323 567.836  1.00120.72           C  
ANISOU 1656  CD2 LEU A1010    14205  20881  10781   1195  -2594   1441       C  
ATOM   1657  N   ASN A1011     172.107  17.910 565.282  1.00129.72           N  
ANISOU 1657  N   ASN A1011    15170  21742  12377   1992   -953    528       N  
ATOM   1658  CA  ASN A1011     171.682  19.233 564.836  1.00132.74           C  
ANISOU 1658  CA  ASN A1011    15433  22177  12826   2088   -608    350       C  
ATOM   1659  C   ASN A1011     170.919  19.181 563.519  1.00132.54           C  
ANISOU 1659  C   ASN A1011    15920  21827  12610   2227   -605    434       C  
ATOM   1660  O   ASN A1011     170.220  20.143 563.186  1.00139.26           O  
ANISOU 1660  O   ASN A1011    16713  22769  13431   2248   -439    343       O  
ATOM   1661  CB  ASN A1011     172.879  20.186 564.718  1.00139.78           C  
ANISOU 1661  CB  ASN A1011    16090  22911  14110   2349   -117    106       C  
ATOM   1662  CG  ASN A1011     173.913  19.726 563.703  1.00142.98           C  
ANISOU 1662  CG  ASN A1011    16884  22782  14659   2682    108    131       C  
ATOM   1663  OD1 ASN A1011     174.998  19.280 564.072  1.00142.13           O  
ANISOU 1663  OD1 ASN A1011    16663  22582  14757   2760    135     97       O  
ATOM   1664  ND2 ASN A1011     173.594  19.859 562.420  1.00145.67           N  
ANISOU 1664  ND2 ASN A1011    17679  22782  14887   2906    277    180       N  
ATOM   1665  N   ASP A1012     171.038  18.090 562.760  1.00124.82           N  
ANISOU 1665  N   ASP A1012    15452  20470  11504   2345   -805    588       N  
ATOM   1666  CA  ASP A1012     170.221  17.941 561.560  1.00113.19           C  
ANISOU 1666  CA  ASP A1012    14486  18713   9807   2476   -892    660       C  
ATOM   1667  C   ASP A1012     168.777  17.618 561.924  1.00111.32           C  
ANISOU 1667  C   ASP A1012    14212  18766   9320   2134  -1335    804       C  
ATOM   1668  O   ASP A1012     167.853  18.373 561.593  1.00111.85           O  
ANISOU 1668  O   ASP A1012    14257  18949   9290   2112  -1282    751       O  
ATOM   1669  CB  ASP A1012     170.806  16.856 560.653  1.00111.50           C  
ANISOU 1669  CB  ASP A1012    14828  18004   9531   2737  -1001    744       C  
ATOM   1670  CG  ASP A1012     172.090  17.293 559.976  1.00114.02           C  
ANISOU 1670  CG  ASP A1012    15253  18003  10068   3143   -490    606       C  
ATOM   1671  OD1 ASP A1012     172.262  18.510 559.753  1.00104.70           O  
ANISOU 1671  OD1 ASP A1012    13881  16864   9037   3271    -42    474       O  
ATOM   1672  OD2 ASP A1012     172.927  16.418 559.667  1.00106.92           O  
ANISOU 1672  OD2 ASP A1012    14614  16803   9206   3334   -535    638       O  
ATOM   1673  N   ASN A1013     168.564  16.499 562.623  1.00111.63           N  
ANISOU 1673  N   ASN A1013    14222  18921   9270   1859  -1775   1001       N  
ATOM   1674  CA  ASN A1013     167.201  16.077 562.933  1.00113.59           C  
ANISOU 1674  CA  ASN A1013    14433  19414   9311   1518  -2202   1184       C  
ATOM   1675  C   ASN A1013     166.502  17.048 563.878  1.00112.87           C  
ANISOU 1675  C   ASN A1013    13781  19903   9201   1270  -2103   1118       C  
ATOM   1676  O   ASN A1013     165.271  17.175 563.832  1.00103.59           O  
ANISOU 1676  O   ASN A1013    12562  18922   7875   1082  -2300   1189       O  
ATOM   1677  CB  ASN A1013     167.211  14.668 563.525  1.00110.29           C  
ANISOU 1677  CB  ASN A1013    14082  18979   8844   1269  -2671   1446       C  
ATOM   1678  CG  ASN A1013     167.665  13.623 562.526  1.00111.79           C  
ANISOU 1678  CG  ASN A1013    14867  18582   9027   1507  -2867   1504       C  
ATOM   1679  OD1 ASN A1013     166.848  12.956 561.891  1.00112.02           O  
ANISOU 1679  OD1 ASN A1013    15253  18381   8928   1456  -3233   1623       O  
ATOM   1680  ND2 ASN A1013     168.975  13.481 562.376  1.00107.95           N  
ANISOU 1680  ND2 ASN A1013    14478  17844   8692   1784  -2637   1400       N  
ATOM   1681  N   LEU A1014     167.260  17.745 564.730  1.00112.06           N  
ANISOU 1681  N   LEU A1014    13237  20081   9259   1282  -1814    962       N  
ATOM   1682  CA  LEU A1014     166.641  18.693 565.652  1.00114.60           C  
ANISOU 1682  CA  LEU A1014    13023  20965   9555   1089  -1726    856       C  
ATOM   1683  C   LEU A1014     165.987  19.846 564.900  1.00121.53           C  
ANISOU 1683  C   LEU A1014    13930  21806  10439   1239  -1485    675       C  
ATOM   1684  O   LEU A1014     164.929  20.341 565.306  1.00118.73           O  
ANISOU 1684  O   LEU A1014    13302  21844   9967   1051  -1571    658       O  
ATOM   1685  CB  LEU A1014     167.677  19.212 566.649  1.00103.04           C  
ANISOU 1685  CB  LEU A1014    11113  19753   8285   1124  -1490    679       C  
ATOM   1686  CG  LEU A1014     167.117  20.003 567.832  1.00101.07           C  
ANISOU 1686  CG  LEU A1014    10283  20145   7973    919  -1474    566       C  
ATOM   1687  CD1 LEU A1014     165.997  19.228 568.508  1.00102.24           C  
ANISOU 1687  CD1 LEU A1014    10331  20689   7825    556  -1875    850       C  
ATOM   1688  CD2 LEU A1014     168.220  20.320 568.827  1.00115.24           C  
ANISOU 1688  CD2 LEU A1014    11685  22150   9952    971  -1326    390       C  
ATOM   1689  N   LYS A1015     166.600  20.287 563.799  1.00125.00           N  
ANISOU 1689  N   LYS A1015    14699  21785  11011   1589  -1175    548       N  
ATOM   1690  CA  LYS A1015     165.959  21.280 562.944  1.00132.16           C  
ANISOU 1690  CA  LYS A1015    15727  22588  11901   1757   -976    422       C  
ATOM   1691  C   LYS A1015     164.920  20.646 562.029  1.00137.70           C  
ANISOU 1691  C   LYS A1015    16890  23075  12356   1745  -1302    581       C  
ATOM   1692  O   LYS A1015     163.961  21.318 561.628  1.00142.12           O  
ANISOU 1692  O   LYS A1015    17456  23714  12831   1758  -1306    518       O  
ATOM   1693  CB  LYS A1015     167.004  22.027 562.111  1.00137.66           C  
ANISOU 1693  CB  LYS A1015    16596  22882  12828   2142   -494    264       C  
ATOM   1694  CG  LYS A1015     167.672  23.202 562.821  1.00136.41           C  
ANISOU 1694  CG  LYS A1015    15921  22936  12974   2177   -124     30       C  
ATOM   1695  CD  LYS A1015     168.646  22.739 563.891  1.00134.84           C  
ANISOU 1695  CD  LYS A1015    15394  22910  12927   2063   -159      9       C  
ATOM   1696  CE  LYS A1015     169.539  23.872 564.361  1.00132.53           C  
ANISOU 1696  CE  LYS A1015    14665  22684  13008   2178    227   -252       C  
ATOM   1697  NZ  LYS A1015     170.639  23.373 565.231  1.00131.61           N  
ANISOU 1697  NZ  LYS A1015    14294  22646  13065   2134    197   -286       N  
ATOM   1698  N   VAL A1016     165.092  19.364 561.688  1.00130.53           N  
ANISOU 1698  N   VAL A1016    16365  21879  11350   1733  -1602    767       N  
ATOM   1699  CA  VAL A1016     164.062  18.654 560.935  1.00129.37           C  
ANISOU 1699  CA  VAL A1016    16622  21538  10995   1686  -2001    908       C  
ATOM   1700  C   VAL A1016     162.752  18.629 561.713  1.00115.06           C  
ANISOU 1700  C   VAL A1016    14446  20196   9076   1289  -2322   1012       C  
ATOM   1701  O   VAL A1016     161.666  18.674 561.120  1.00112.69           O  
ANISOU 1701  O   VAL A1016    14312  19852   8654   1262  -2538   1035       O  
ATOM   1702  CB  VAL A1016     164.544  17.233 560.576  1.00104.58           C  
ANISOU 1702  CB  VAL A1016    13913  18011   7812   1726  -2307   1074       C  
ATOM   1703  CG1 VAL A1016     163.406  16.398 560.008  1.00106.23           C  
ANISOU 1703  CG1 VAL A1016    14460  18054   7847   1604  -2818   1224       C  
ATOM   1704  CG2 VAL A1016     165.688  17.301 559.579  1.00104.79           C  
ANISOU 1704  CG2 VAL A1016    14357  17557   7902   2179  -1976    958       C  
ATOM   1705  N   ILE A1017     162.828  18.577 563.046  1.00107.67           N  
ANISOU 1705  N   ILE A1017    12999  19731   8178    993  -2352   1073       N  
ATOM   1706  CA  ILE A1017     161.617  18.642 563.862  1.00105.75           C  
ANISOU 1706  CA  ILE A1017    12349  20006   7824    631  -2587   1176       C  
ATOM   1707  C   ILE A1017     160.873  19.948 563.613  1.00106.76           C  
ANISOU 1707  C   ILE A1017    12284  20336   7944    725  -2375    957       C  
ATOM   1708  O   ILE A1017     159.641  19.966 563.490  1.00114.93           O  
ANISOU 1708  O   ILE A1017    13262  21535   8871    566  -2612   1019       O  
ATOM   1709  CB  ILE A1017     161.963  18.463 565.352  1.00109.05           C  
ANISOU 1709  CB  ILE A1017    12259  20926   8250    363  -2590   1260       C  
ATOM   1710  CG1 ILE A1017     162.456  17.041 565.621  1.00109.37           C  
ANISOU 1710  CG1 ILE A1017    12499  20777   8279    218  -2899   1536       C  
ATOM   1711  CG2 ILE A1017     160.760  18.788 566.227  1.00104.28           C  
ANISOU 1711  CG2 ILE A1017    11171  20936   7516     45  -2716   1325       C  
ATOM   1712  CD1 ILE A1017     162.653  16.735 567.090  1.00105.79           C  
ANISOU 1712  CD1 ILE A1017    11583  20834   7781    -63  -2967   1681       C  
ATOM   1713  N   GLU A1018     161.605  21.062 563.525  1.00112.86           N  
ANISOU 1713  N   GLU A1018    12942  21080   8860    986  -1937    700       N  
ATOM   1714  CA  GLU A1018     160.957  22.348 563.290  1.00135.41           C  
ANISOU 1714  CA  GLU A1018    15618  24092  11740   1097  -1735    484       C  
ATOM   1715  C   GLU A1018     160.441  22.458 561.861  1.00150.89           C  
ANISOU 1715  C   GLU A1018    18099  25605  13628   1339  -1785    473       C  
ATOM   1716  O   GLU A1018     159.342  22.977 561.631  1.00148.29           O  
ANISOU 1716  O   GLU A1018    17696  25426  13222   1306  -1890    417       O  
ATOM   1717  CB  GLU A1018     161.924  23.491 563.602  1.00137.83           C  
ANISOU 1717  CB  GLU A1018    15652  24444  12272   1300  -1275    222       C  
ATOM   1718  CG  GLU A1018     161.345  24.875 563.345  1.00135.56           C  
ANISOU 1718  CG  GLU A1018    15189  24264  12055   1439  -1060    -12       C  
ATOM   1719  CD  GLU A1018     162.292  25.990 563.740  1.00130.85           C  
ANISOU 1719  CD  GLU A1018    14277  23702  11739   1608   -644   -271       C  
ATOM   1720  OE1 GLU A1018     163.227  25.728 564.526  1.00124.53           O  
ANISOU 1720  OE1 GLU A1018    13251  23010  11053   1548   -570   -291       O  
ATOM   1721  OE2 GLU A1018     162.102  27.130 563.264  1.00127.88           O  
ANISOU 1721  OE2 GLU A1018    13875  23226  11488   1804   -412   -455       O  
ATOM   1722  N   LYS A1019     161.211  21.970 560.886  1.00165.64           N  
ANISOU 1722  N   LYS A1019    20498  26934  15503   1608  -1718    518       N  
ATOM   1723  CA  LYS A1019     160.787  22.046 559.492  1.00169.55           C  
ANISOU 1723  CA  LYS A1019    21536  27001  15883   1891  -1767    503       C  
ATOM   1724  C   LYS A1019     159.694  21.043 559.143  1.00173.24           C  
ANISOU 1724  C   LYS A1019    22253  27404  16167   1716  -2309    670       C  
ATOM   1725  O   LYS A1019     159.200  21.070 558.009  1.00181.00           O  
ANISOU 1725  O   LYS A1019    23684  28059  17028   1946  -2426    641       O  
ATOM   1726  CB  LYS A1019     161.983  21.828 558.562  1.00172.04           C  
ANISOU 1726  CB  LYS A1019    22342  26790  16236   2267  -1504    495       C  
ATOM   1727  CG  LYS A1019     162.293  20.362 558.304  1.00174.68           C  
ANISOU 1727  CG  LYS A1019    23062  26837  16472   2242  -1838    669       C  
ATOM   1728  CD  LYS A1019     163.366  20.184 557.244  1.00173.92           C  
ANISOU 1728  CD  LYS A1019    23487  26225  16369   2673  -1574    639       C  
ATOM   1729  CE  LYS A1019     164.710  20.701 557.723  1.00172.36           C  
ANISOU 1729  CE  LYS A1019    23016  26054  16419   2777  -1086    556       C  
ATOM   1730  NZ  LYS A1019     165.784  20.443 556.725  1.00173.57           N  
ANISOU 1730  NZ  LYS A1019    23646  25728  16575   3190   -813    552       N  
ATOM   1731  N   ALA A1020     159.302  20.177 560.075  1.00152.36           N  
ANISOU 1731  N   ALA A1020    19331  25052  13507   1325  -2646    848       N  
ATOM   1732  CA  ALA A1020     158.368  19.102 559.765  1.00138.84           C  
ANISOU 1732  CA  ALA A1020    17845  23219  11689   1132  -3183   1036       C  
ATOM   1733  C   ALA A1020     156.995  19.649 559.389  1.00134.13           C  
ANISOU 1733  C   ALA A1020    17178  22764  11021   1087  -3366    972       C  
ATOM   1734  O   ALA A1020     156.468  20.557 560.040  1.00129.46           O  
ANISOU 1734  O   ALA A1020    16102  22626  10460    963  -3210    876       O  
ATOM   1735  CB  ALA A1020     158.246  18.152 560.954  1.00140.70           C  
ANISOU 1735  CB  ALA A1020    17727  23776  11956    693  -3460   1279       C  
ATOM   1736  N   ASP A1021     156.419  19.082 558.327  1.00140.90           N  
ANISOU 1736  N   ASP A1021    18523  23226  11788   1210  -3720   1004       N  
ATOM   1737  CA  ASP A1021     155.101  19.460 557.832  1.00141.89           C  
ANISOU 1737  CA  ASP A1021    18648  23410  11853   1195  -3972    941       C  
ATOM   1738  C   ASP A1021     153.991  18.562 558.358  1.00147.45           C  
ANISOU 1738  C   ASP A1021    19100  24327  12598    751  -4494   1150       C  
ATOM   1739  O   ASP A1021     152.909  19.055 558.692  1.00146.85           O  
ANISOU 1739  O   ASP A1021    18638  24619  12542    563  -4593   1128       O  
ATOM   1740  CB  ASP A1021     155.084  19.435 556.300  1.00142.20           C  
ANISOU 1740  CB  ASP A1021    19383  22886  11760   1631  -4074    828       C  
ATOM   1741  CG  ASP A1021     156.158  20.312 555.687  1.00141.15           C  
ANISOU 1741  CG  ASP A1021    19522  22522  11588   2082  -3532    668       C  
ATOM   1742  OD1 ASP A1021     156.528  21.328 556.309  1.00136.78           O  
ANISOU 1742  OD1 ASP A1021    18565  22269  11138   2073  -3100    574       O  
ATOM   1743  OD2 ASP A1021     156.637  19.983 554.581  1.00142.98           O  
ANISOU 1743  OD2 ASP A1021    20366  22267  11692   2454  -3538    636       O  
ATOM   1744  N   ASN A1022     154.230  17.254 558.436  1.00152.95           N  
ANISOU 1744  N   ASN A1022    19992  24792  13331    581  -4832   1361       N  
ATOM   1745  CA  ASN A1022     153.274  16.285 558.935  1.00152.76           C  
ANISOU 1745  CA  ASN A1022    19741  24907  13395    136  -5335   1613       C  
ATOM   1746  C   ASN A1022     153.787  15.711 560.260  1.00150.98           C  
ANISOU 1746  C   ASN A1022    19106  25019  13241   -226  -5268   1860       C  
ATOM   1747  O   ASN A1022     154.547  16.387 560.977  1.00148.13           O  
ANISOU 1747  O   ASN A1022    18457  24969  12855   -179  -4820   1783       O  
ATOM   1748  CB  ASN A1022     153.028  15.232 557.857  1.00156.95           C  
ANISOU 1748  CB  ASN A1022    20865  24836  13932    248  -5850   1653       C  
ATOM   1749  CG  ASN A1022     154.295  14.503 557.456  1.00161.57           C  
ANISOU 1749  CG  ASN A1022    21943  24957  14487    494  -5809   1662       C  
ATOM   1750  OD1 ASN A1022     155.392  15.054 557.529  1.00164.65           O  
ANISOU 1750  OD1 ASN A1022    22380  25357  14821    745  -5326   1549       O  
ATOM   1751  ND2 ASN A1022     154.147  13.254 557.029  1.00162.81           N  
ANISOU 1751  ND2 ASN A1022    22457  24695  14708    427  -6328   1787       N  
ATOM   1752  N   ALA A1023     153.382  14.485 560.583  1.00146.37           N  
ANISOU 1752  N   ALA A1023    18498  24362  12754   -577  -5723   2154       N  
ATOM   1753  CA  ALA A1023     153.711  13.877 561.865  1.00139.19           C  
ANISOU 1753  CA  ALA A1023    17213  23701  11971   -921  -5647   2401       C  
ATOM   1754  C   ALA A1023     154.817  12.836 561.783  1.00135.93           C  
ANISOU 1754  C   ALA A1023    17172  22918  11557   -867  -5801   2547       C  
ATOM   1755  O   ALA A1023     155.519  12.622 562.775  1.00134.17           O  
ANISOU 1755  O   ALA A1023    16699  22920  11362  -1008  -5609   2678       O  
ATOM   1756  CB  ALA A1023     152.465  13.231 562.480  1.00143.96           C  
ANISOU 1756  CB  ALA A1023    17462  24422  12814  -1358  -5905   2631       C  
ATOM   1757  N   ALA A1024     154.994  12.179 560.634  1.00147.61           N  
ANISOU 1757  N   ALA A1024    19259  23790  13034   -633  -6127   2494       N  
ATOM   1758  CA  ALA A1024     156.005  11.130 560.538  1.00158.41           C  
ANISOU 1758  CA  ALA A1024    20997  24734  14457   -552  -6277   2597       C  
ATOM   1759  C   ALA A1024     157.419  11.689 560.651  1.00176.33           C  
ANISOU 1759  C   ALA A1024    23338  27009  16651   -219  -5751   2415       C  
ATOM   1760  O   ALA A1024     158.316  11.006 561.163  1.00159.55           O  
ANISOU 1760  O   ALA A1024    21239  24802  14583   -267  -5756   2548       O  
ATOM   1761  CB  ALA A1024     155.844  10.361 559.227  1.00147.86           C  
ANISOU 1761  CB  ALA A1024    20314  22719  13147   -308  -6723   2509       C  
ATOM   1762  N   GLN A1025     157.633  12.923 560.190  1.00192.34           N  
ANISOU 1762  N   GLN A1025    25382  29119  18578    113  -5306   2122       N  
ATOM   1763  CA  GLN A1025     158.975  13.496 560.203  1.00193.40           C  
ANISOU 1763  CA  GLN A1025    25579  29211  18693    439  -4801   1944       C  
ATOM   1764  C   GLN A1025     159.474  13.717 561.625  1.00190.91           C  
ANISOU 1764  C   GLN A1025    24698  29408  18432    181  -4551   2047       C  
ATOM   1765  O   GLN A1025     160.664  13.526 561.906  1.00192.63           O  
ANISOU 1765  O   GLN A1025    24961  29530  18702    313  -4350   2027       O  
ATOM   1766  CB  GLN A1025     158.993  14.806 559.414  1.00195.42           C  
ANISOU 1766  CB  GLN A1025    25944  29442  18866    817  -4391   1645       C  
ATOM   1767  CG  GLN A1025     158.586  14.654 557.957  1.00201.25           C  
ANISOU 1767  CG  GLN A1025    27287  29679  19498   1145  -4608   1524       C  
ATOM   1768  CD  GLN A1025     158.679  15.954 557.182  1.00202.03           C  
ANISOU 1768  CD  GLN A1025    27517  29743  19503   1537  -4175   1268       C  
ATOM   1769  OE1 GLN A1025     159.360  16.891 557.599  1.00202.09           O  
ANISOU 1769  OE1 GLN A1025    27249  29973  19563   1632  -3672   1162       O  
ATOM   1770  NE2 GLN A1025     157.991  16.018 556.048  1.00201.47           N  
ANISOU 1770  NE2 GLN A1025    27870  29375  19304   1773  -4388   1170       N  
ATOM   1771  N   VAL A1026     158.585  14.114 562.540  1.00182.58           N  
ANISOU 1771  N   VAL A1026    23104  28912  17357   -167  -4567   2149       N  
ATOM   1772  CA  VAL A1026     159.022  14.333 563.915  1.00169.20           C  
ANISOU 1772  CA  VAL A1026    20880  27741  15665   -383  -4348   2234       C  
ATOM   1773  C   VAL A1026     159.360  13.007 564.588  1.00161.50           C  
ANISOU 1773  C   VAL A1026    19918  26709  14737   -653  -4672   2564       C  
ATOM   1774  O   VAL A1026     160.277  12.943 565.413  1.00156.56           O  
ANISOU 1774  O   VAL A1026    19098  26263  14123   -665  -4496   2596       O  
ATOM   1775  CB  VAL A1026     157.968  15.129 564.715  1.00161.09           C  
ANISOU 1775  CB  VAL A1026    19274  27365  14570   -645  -4263   2240       C  
ATOM   1776  CG1 VAL A1026     157.486  16.329 563.919  1.00156.48           C  
ANISOU 1776  CG1 VAL A1026    18738  26758  13961   -381  -4036   1933       C  
ATOM   1777  CG2 VAL A1026     156.795  14.252 565.132  1.00161.79           C  
ANISOU 1777  CG2 VAL A1026    19210  27521  14740  -1064  -4645   2543       C  
ATOM   1778  N   LYS A1027     158.657  11.927 564.235  1.00157.99           N  
ANISOU 1778  N   LYS A1027    19706  25983  14340   -861  -5170   2809       N  
ATOM   1779  CA  LYS A1027     158.955  10.633 564.841  1.00153.67           C  
ANISOU 1779  CA  LYS A1027    19196  25302  13889  -1114  -5489   3135       C  
ATOM   1780  C   LYS A1027     160.251  10.052 564.291  1.00153.27           C  
ANISOU 1780  C   LYS A1027    19623  24731  13884   -794  -5508   3052       C  
ATOM   1781  O   LYS A1027     161.070   9.521 565.050  1.00153.13           O  
ANISOU 1781  O   LYS A1027    19513  24767  13903   -867  -5507   3197       O  
ATOM   1782  CB  LYS A1027     157.794   9.663 564.624  1.00158.86           C  
ANISOU 1782  CB  LYS A1027    19949  25671  14739  -1398  -5930   3348       C  
ATOM   1783  CG  LYS A1027     156.656   9.816 565.623  1.00160.51           C  
ANISOU 1783  CG  LYS A1027    19601  26342  15043  -1798  -5849   3520       C  
ATOM   1784  CD  LYS A1027     155.398  10.344 564.957  1.00158.53           C  
ANISOU 1784  CD  LYS A1027    19307  26112  14816  -1818  -5935   3397       C  
ATOM   1785  CE  LYS A1027     154.948   9.434 563.826  1.00156.53           C  
ANISOU 1785  CE  LYS A1027    19536  25246  14694  -1777  -6444   3432       C  
ATOM   1786  NZ  LYS A1027     153.742   9.963 563.133  1.00160.91           N  
ANISOU 1786  NZ  LYS A1027    20060  25808  15273  -1763  -6557   3286       N  
ATOM   1787  N   ASP A1028     160.456  10.142 562.974  1.00152.32           N  
ANISOU 1787  N   ASP A1028    20017  24092  13766   -409  -5506   2805       N  
ATOM   1788  CA  ASP A1028     161.695   9.640 562.387  1.00149.76           C  
ANISOU 1788  CA  ASP A1028    20147  23264  13489    -49  -5464   2686       C  
ATOM   1789  C   ASP A1028     162.896  10.438 562.882  1.00143.00           C  
ANISOU 1789  C   ASP A1028    19065  22633  12637    166  -4922   2503       C  
ATOM   1790  O   ASP A1028     163.890   9.866 563.352  1.00143.12           O  
ANISOU 1790  O   ASP A1028    19092  22559  12729    198  -4921   2572       O  
ATOM   1791  CB  ASP A1028     161.606   9.684 560.862  1.00153.27           C  
ANISOU 1791  CB  ASP A1028    21178  23175  13884    355  -5528   2448       C  
ATOM   1792  CG  ASP A1028     162.814   9.064 560.189  1.00156.28           C  
ANISOU 1792  CG  ASP A1028    22053  23030  14296    747  -5513   2332       C  
ATOM   1793  OD1 ASP A1028     162.910   7.819 560.170  1.00160.17           O  
ANISOU 1793  OD1 ASP A1028    22794  23185  14877    654  -5970   2501       O  
ATOM   1794  OD2 ASP A1028     163.668   9.820 559.681  1.00154.61           O  
ANISOU 1794  OD2 ASP A1028    21970  22737  14037   1151  -5041   2078       O  
ATOM   1795  N   ALA A1029     162.815  11.769 562.790  1.00137.89           N  
ANISOU 1795  N   ALA A1029    18195  22263  11932    316  -4477   2263       N  
ATOM   1796  CA  ALA A1029     163.905  12.617 563.263  1.00127.40           C  
ANISOU 1796  CA  ALA A1029    16606  21140  10659    507  -3973   2070       C  
ATOM   1797  C   ALA A1029     164.158  12.409 564.750  1.00125.47           C  
ANISOU 1797  C   ALA A1029    15864  21372  10438    188  -3998   2246       C  
ATOM   1798  O   ALA A1029     165.313  12.399 565.196  1.00132.51           O  
ANISOU 1798  O   ALA A1029    16667  22260  11420    319  -3801   2177       O  
ATOM   1799  CB  ALA A1029     163.594  14.084 562.971  1.00124.77           C  
ANISOU 1799  CB  ALA A1029    16085  21031  10293    668  -3553   1809       C  
ATOM   1800  N   LEU A1030     163.090  12.238 565.533  1.00137.21           N  
ANISOU 1800  N   LEU A1030    17014  23282  11838   -219  -4237   2478       N  
ATOM   1801  CA  LEU A1030     163.249  11.935 566.951  1.00112.48           C  
ANISOU 1801  CA  LEU A1030    13443  20622   8672   -522  -4295   2694       C  
ATOM   1802  C   LEU A1030     164.035  10.644 567.145  1.00130.88           C  
ANISOU 1802  C   LEU A1030    16023  22622  11084   -553  -4589   2916       C  
ATOM   1803  O   LEU A1030     165.125  10.649 567.724  1.00136.84           O  
ANISOU 1803  O   LEU A1030    16662  23440  11890   -437  -4425   2854       O  
ATOM   1804  CB  LEU A1030     161.881  11.844 567.632  1.00113.98           C  
ANISOU 1804  CB  LEU A1030    13276  21288   8742   -949  -4517   2957       C  
ATOM   1805  CG  LEU A1030     161.330  13.109 568.299  1.00112.64           C  
ANISOU 1805  CG  LEU A1030    12583  21734   8482  -1009  -4176   2783       C  
ATOM   1806  CD1 LEU A1030     159.942  12.852 568.866  1.00114.74           C  
ANISOU 1806  CD1 LEU A1030    12592  22181   8822  -1381  -4281   2982       C  
ATOM   1807  CD2 LEU A1030     162.267  13.606 569.382  1.00112.46           C  
ANISOU 1807  CD2 LEU A1030    12188  22114   8426   -948  -3889   2670       C  
ATOM   1808  N   THR A1031     163.505   9.528 566.635  1.00123.30           N  
ANISOU 1808  N   THR A1031    15413  21273  10161   -692  -5049   3156       N  
ATOM   1809  CA  THR A1031     164.110   8.222 566.892  1.00126.45           C  
ANISOU 1809  CA  THR A1031    16033  21359  10653   -767  -5399   3407       C  
ATOM   1810  C   THR A1031     165.561   8.169 566.422  1.00128.91           C  
ANISOU 1810  C   THR A1031    16639  21271  11069   -339  -5199   3157       C  
ATOM   1811  O   THR A1031     166.456   7.775 567.181  1.00132.85           O  
ANISOU 1811  O   THR A1031    17021  21838  11620   -342  -5200   3236       O  
ATOM   1812  CB  THR A1031     163.288   7.121 566.220  1.00131.98           C  
ANISOU 1812  CB  THR A1031    17105  21615  11426   -936  -5938   3640       C  
ATOM   1813  OG1 THR A1031     163.104   7.437 564.835  1.00132.35           O  
ANISOU 1813  OG1 THR A1031    17573  21233  11480   -611  -5904   3354       O  
ATOM   1814  CG2 THR A1031     161.930   6.985 566.894  1.00132.71           C  
ANISOU 1814  CG2 THR A1031    16839  22028  11557  -1380  -6064   3891       C  
ATOM   1815  N   LYS A1032     165.815   8.562 565.170  1.00134.76           N  
ANISOU 1815  N   LYS A1032    17761  21604  11837     46  -5021   2860       N  
ATOM   1816  CA  LYS A1032     167.184   8.522 564.663  1.00133.57           C  
ANISOU 1816  CA  LYS A1032    17878  21081  11791    470  -4792   2630       C  
ATOM   1817  C   LYS A1032     168.088   9.467 565.447  1.00131.43           C  
ANISOU 1817  C   LYS A1032    17171  21195  11570    569  -4317   2450       C  
ATOM   1818  O   LYS A1032     169.239   9.129 565.757  1.00130.28           O  
ANISOU 1818  O   LYS A1032    17025  20929  11546    724  -4254   2408       O  
ATOM   1819  CB  LYS A1032     167.205   8.858 563.172  1.00127.81           C  
ANISOU 1819  CB  LYS A1032    17621  19904  11038    875  -4641   2367       C  
ATOM   1820  CG  LYS A1032     168.589   8.808 562.544  1.00123.63           C  
ANISOU 1820  CG  LYS A1032    17379  18986  10607   1341  -4369   2142       C  
ATOM   1821  CD  LYS A1032     168.509   8.630 561.036  1.00124.17           C  
ANISOU 1821  CD  LYS A1032    18047  18529  10603   1722  -4405   1981       C  
ATOM   1822  CE  LYS A1032     167.693   9.732 560.383  1.00120.05           C  
ANISOU 1822  CE  LYS A1032    17528  18138   9949   1801  -4151   1835       C  
ATOM   1823  NZ  LYS A1032     167.583   9.534 558.912  1.00116.09           N  
ANISOU 1823  NZ  LYS A1032    17640  17141   9328   2196  -4212   1688       N  
ATOM   1824  N   MET A1033     167.572  10.649 565.797  1.00136.88           N  
ANISOU 1824  N   MET A1033    17472  22346  12190    484  -4010   2329       N  
ATOM   1825  CA  MET A1033     168.346  11.589 566.600  1.00150.77           C  
ANISOU 1825  CA  MET A1033    18782  24484  14021    560  -3605   2136       C  
ATOM   1826  C   MET A1033     168.677  11.016 567.972  1.00162.59           C  
ANISOU 1826  C   MET A1033    19948  26328  15501    304  -3804   2347       C  
ATOM   1827  O   MET A1033     169.683  11.399 568.578  1.00153.04           O  
ANISOU 1827  O   MET A1033    18483  25269  14398    436  -3575   2190       O  
ATOM   1828  CB  MET A1033     167.581  12.904 566.752  1.00151.24           C  
ANISOU 1828  CB  MET A1033    18489  24971  14003    495  -3314   1974       C  
ATOM   1829  CG  MET A1033     168.434  14.070 567.223  1.00151.72           C  
ANISOU 1829  CG  MET A1033    18167  25283  14197    678  -2850   1674       C  
ATOM   1830  SD  MET A1033     167.454  15.423 567.899  1.00147.25           S  
ANISOU 1830  SD  MET A1033    17064  25362  13524    502  -2641   1535       S  
ATOM   1831  CE  MET A1033     165.982  15.313 566.887  1.00146.36           C  
ANISOU 1831  CE  MET A1033    17270  25088  13253    405  -2845   1655       C  
ATOM   1832  N   ARG A1034     167.852  10.101 568.478  1.00181.57           N  
ANISOU 1832  N   ARG A1034    22348  28857  17783    -57  -4234   2711       N  
ATOM   1833  CA  ARG A1034     168.098   9.537 569.798  1.00184.67           C  
ANISOU 1833  CA  ARG A1034    22444  29604  18119   -304  -4428   2963       C  
ATOM   1834  C   ARG A1034     169.032   8.341 569.745  1.00183.05           C  
ANISOU 1834  C   ARG A1034    22555  28951  18043   -206  -4707   3100       C  
ATOM   1835  O   ARG A1034     169.810   8.130 570.684  1.00184.96           O  
ANISOU 1835  O   ARG A1034    22581  29392  18304   -215  -4724   3150       O  
ATOM   1836  CB  ARG A1034     166.781   9.139 570.472  1.00190.92           C  
ANISOU 1836  CB  ARG A1034    23028  30789  18725   -759  -4725   3341       C  
ATOM   1837  CG  ARG A1034     165.780  10.280 570.620  1.00195.96           C  
ANISOU 1837  CG  ARG A1034    23312  31920  19225   -869  -4478   3217       C  
ATOM   1838  CD  ARG A1034     166.469  11.637 570.725  1.00200.32           C  
ANISOU 1838  CD  ARG A1034    23597  32695  19822   -576  -3989   2782       C  
ATOM   1839  NE  ARG A1034     165.536  12.756 570.616  1.00207.93           N  
ANISOU 1839  NE  ARG A1034    24305  34006  20694   -615  -3761   2610       N  
ATOM   1840  CZ  ARG A1034     165.909  14.030 570.539  1.00212.70           C  
ANISOU 1840  CZ  ARG A1034    24697  34752  21366   -374  -3354   2226       C  
ATOM   1841  NH1 ARG A1034     165.000  14.990 570.447  1.00215.56           N  
ANISOU 1841  NH1 ARG A1034    24839  35415  21651   -414  -3191   2085       N  
ATOM   1842  NH2 ARG A1034     167.197  14.346 570.558  1.00212.65           N  
ANISOU 1842  NH2 ARG A1034    24685  34573  21537    -92  -3119   1981       N  
ATOM   1843  N   ALA A1035     168.977   7.553 568.670  1.00165.68           N  
ANISOU 1843  N   ALA A1035    20869  26152  15931    -89  -4948   3142       N  
ATOM   1844  CA  ALA A1035     170.014   6.551 568.452  1.00156.13           C  
ANISOU 1844  CA  ALA A1035    19988  24459  14875    109  -5156   3172       C  
ATOM   1845  C   ALA A1035     171.377   7.219 568.329  1.00147.06           C  
ANISOU 1845  C   ALA A1035    18763  23241  13872    512  -4729   2807       C  
ATOM   1846  O   ALA A1035     172.343   6.825 568.997  1.00151.76           O  
ANISOU 1846  O   ALA A1035    19247  23850  14565    576  -4781   2828       O  
ATOM   1847  CB  ALA A1035     169.695   5.728 567.205  1.00158.46           C  
ANISOU 1847  CB  ALA A1035    20859  24121  15229    228  -5461   3202       C  
ATOM   1848  N   ALA A1036     171.466   8.257 567.490  1.00143.30           N  
ANISOU 1848  N   ALA A1036    18323  22694  13430    782  -4303   2482       N  
ATOM   1849  CA  ALA A1036     172.699   9.026 567.390  1.00141.97           C  
ANISOU 1849  CA  ALA A1036    18010  22489  13442   1134  -3848   2149       C  
ATOM   1850  C   ALA A1036     173.043   9.737 568.692  1.00143.04           C  
ANISOU 1850  C   ALA A1036    17563  23189  13596   1002  -3669   2084       C  
ATOM   1851  O   ALA A1036     174.220  10.020 568.937  1.00134.35           O  
ANISOU 1851  O   ALA A1036    16297  22056  12695   1233  -3445   1877       O  
ATOM   1852  CB  ALA A1036     172.597  10.045 566.253  1.00112.80           C  
ANISOU 1852  CB  ALA A1036    14456  18628   9773   1413  -3420   1868       C  
ATOM   1853  N   ALA A1037     172.050  10.024 569.536  1.00139.87           N  
ANISOU 1853  N   ALA A1037    16840  23309  12996    653  -3773   2245       N  
ATOM   1854  CA  ALA A1037     172.330  10.684 570.806  1.00140.20           C  
ANISOU 1854  CA  ALA A1037    16341  23920  13009    554  -3636   2167       C  
ATOM   1855  C   ALA A1037     172.940   9.719 571.816  1.00143.36           C  
ANISOU 1855  C   ALA A1037    16664  24412  13395    451  -3961   2388       C  
ATOM   1856  O   ALA A1037     173.852  10.093 572.562  1.00145.82           O  
ANISOU 1856  O   ALA A1037    16665  24934  13806    573  -3829   2212       O  
ATOM   1857  CB  ALA A1037     171.052  11.309 571.361  1.00144.23           C  
ANISOU 1857  CB  ALA A1037    16536  24986  13279    251  -3626   2257       C  
ATOM   1858  N   LEU A1038     172.448   8.478 571.859  1.00148.37           N  
ANISOU 1858  N   LEU A1038    17575  24876  13925    229  -4407   2775       N  
ATOM   1859  CA  LEU A1038     173.037   7.485 572.752  1.00142.74           C  
ANISOU 1859  CA  LEU A1038    16840  24187  13206    144  -4743   3022       C  
ATOM   1860  C   LEU A1038     174.410   7.049 572.256  1.00148.02           C  
ANISOU 1860  C   LEU A1038    17752  24339  14150    510  -4725   2829       C  
ATOM   1861  O   LEU A1038     175.356   6.934 573.048  1.00161.31           O  
ANISOU 1861  O   LEU A1038    19230  26147  15913    607  -4754   2775       O  
ATOM   1862  CB  LEU A1038     172.106   6.282 572.891  1.00139.06           C  
ANISOU 1862  CB  LEU A1038    16602  23634  12599   -207  -5230   3515       C  
ATOM   1863  CG  LEU A1038     170.723   6.558 573.485  1.00144.16           C  
ANISOU 1863  CG  LEU A1038    16973  24820  12982   -604  -5280   3776       C  
ATOM   1864  CD1 LEU A1038     169.906   5.278 573.560  1.00126.35           C  
ANISOU 1864  CD1 LEU A1038    14960  22337  10710   -938  -5730   4251       C  
ATOM   1865  CD2 LEU A1038     170.844   7.203 574.857  1.00123.48           C  
ANISOU 1865  CD2 LEU A1038    13829  22918  10172   -695  -5127   3763       C  
ATOM   1866  N   ASP A1039     174.540   6.804 570.948  1.00154.55           N  
ANISOU 1866  N   ASP A1039    19012  24596  15114    739  -4679   2711       N  
ATOM   1867  CA  ASP A1039     175.853   6.497 570.390  1.00159.74           C  
ANISOU 1867  CA  ASP A1039    19879  24783  16033   1132  -4590   2489       C  
ATOM   1868  C   ASP A1039     176.821   7.658 570.578  1.00157.40           C  
ANISOU 1868  C   ASP A1039    19206  24674  15924   1392  -4102   2099       C  
ATOM   1869  O   ASP A1039     178.032   7.443 570.703  1.00158.39           O  
ANISOU 1869  O   ASP A1039    19289  24616  16276   1643  -4058   1950       O  
ATOM   1870  CB  ASP A1039     175.724   6.134 568.910  1.00162.30           C  
ANISOU 1870  CB  ASP A1039    20734  24518  16415   1360  -4587   2413       C  
ATOM   1871  CG  ASP A1039     175.108   4.763 568.700  1.00163.94           C  
ANISOU 1871  CG  ASP A1039    21352  24392  16546   1176  -5152   2756       C  
ATOM   1872  OD1 ASP A1039     173.962   4.547 569.147  1.00161.88           O  
ANISOU 1872  OD1 ASP A1039    21019  24382  16106    784  -5413   3057       O  
ATOM   1873  OD2 ASP A1039     175.771   3.900 568.088  1.00166.35           O  
ANISOU 1873  OD2 ASP A1039    22038  24177  16990   1428  -5340   2722       O  
ATOM   1874  N   ALA A1040     176.310   8.891 570.602  1.00155.43           N  
ANISOU 1874  N   ALA A1040    18667  24772  15617   1338  -3749   1924       N  
ATOM   1875  CA  ALA A1040     177.132  10.037 570.962  1.00150.01           C  
ANISOU 1875  CA  ALA A1040    17553  24310  15135   1525  -3334   1573       C  
ATOM   1876  C   ALA A1040     177.398  10.109 572.459  1.00144.16           C  
ANISOU 1876  C   ALA A1040    16360  24081  14333   1365  -3492   1606       C  
ATOM   1877  O   ALA A1040     178.355  10.771 572.874  1.00144.67           O  
ANISOU 1877  O   ALA A1040    16085  24254  14628   1553  -3266   1313       O  
ATOM   1878  CB  ALA A1040     176.469  11.334 570.495  1.00151.10           C  
ANISOU 1878  CB  ALA A1040    17541  24623  15245   1526  -2938   1374       C  
ATOM   1879  N   GLN A1041     176.575   9.445 573.272  1.00144.28           N  
ANISOU 1879  N   GLN A1041    16357  24414  14048   1031  -3876   1961       N  
ATOM   1880  CA  GLN A1041     176.810   9.408 574.711  1.00146.19           C  
ANISOU 1880  CA  GLN A1041    16217  25161  14167    901  -4053   2033       C  
ATOM   1881  C   GLN A1041     177.918   8.427 575.067  1.00148.21           C  
ANISOU 1881  C   GLN A1041    16582  25160  14572   1045  -4330   2107       C  
ATOM   1882  O   GLN A1041     178.749   8.714 575.936  1.00145.24           O  
ANISOU 1882  O   GLN A1041    15872  25030  14283   1159  -4319   1935       O  
ATOM   1883  CB  GLN A1041     175.517   9.046 575.446  1.00144.47           C  
ANISOU 1883  CB  GLN A1041    15937  25397  13559    497  -4330   2429       C  
ATOM   1884  CG  GLN A1041     175.691   8.686 576.919  1.00146.26           C  
ANISOU 1884  CG  GLN A1041    15876  26120  13577    355  -4593   2625       C  
ATOM   1885  CD  GLN A1041     175.962   9.890 577.804  1.00147.95           C  
ANISOU 1885  CD  GLN A1041    15568  26897  13748    444  -4342   2284       C  
ATOM   1886  OE1 GLN A1041     176.932  10.621 577.605  1.00155.70           O  
ANISOU 1886  OE1 GLN A1041    16386  27741  15033    737  -4082   1862       O  
ATOM   1887  NE2 GLN A1041     175.100  10.100 578.794  1.00141.28           N  
ANISOU 1887  NE2 GLN A1041    14448  26694  12538    198  -4422   2465       N  
ATOM   1888  N   LYS A1042     177.948   7.267 574.405  1.00147.78           N  
ANISOU 1888  N   LYS A1042    16993  24599  14560   1060  -4606   2342       N  
ATOM   1889  CA  LYS A1042     178.999   6.294 574.686  1.00145.42           C  
ANISOU 1889  CA  LYS A1042    16821  24012  14420   1219  -4892   2407       C  
ATOM   1890  C   LYS A1042     180.367   6.792 574.235  1.00151.80           C  
ANISOU 1890  C   LYS A1042    17528  24538  15613   1635  -4572   1972       C  
ATOM   1891  O   LYS A1042     181.383   6.448 574.849  1.00152.72           O  
ANISOU 1891  O   LYS A1042    17505  24635  15885   1786  -4716   1903       O  
ATOM   1892  CB  LYS A1042     178.666   4.959 574.022  1.00139.67           C  
ANISOU 1892  CB  LYS A1042    16625  22773  13671   1151  -5277   2733       C  
ATOM   1893  CG  LYS A1042     177.361   4.348 574.505  1.00141.33           C  
ANISOU 1893  CG  LYS A1042    16914  23218  13565    714  -5632   3211       C  
ATOM   1894  CD  LYS A1042     177.013   3.090 573.731  1.00144.68           C  
ANISOU 1894  CD  LYS A1042    17867  23067  14039    655  -6022   3492       C  
ATOM   1895  CE  LYS A1042     175.672   2.531 574.174  1.00141.43           C  
ANISOU 1895  CE  LYS A1042    17493  22871  13373    192  -6356   3980       C  
ATOM   1896  NZ  LYS A1042     175.278   1.338 573.376  1.00136.34           N  
ANISOU 1896  NZ  LYS A1042    17354  21625  12825    124  -6768   4231       N  
ATOM   1897  N   ALA A1043     180.417   7.600 573.178  1.00167.90           N  
ANISOU 1897  N   ALA A1043    19618  26357  17817   1825  -4138   1691       N  
ATOM   1898  CA  ALA A1043     181.668   8.167 572.697  1.00170.76           C  
ANISOU 1898  CA  ALA A1043    19845  26463  18571   2206  -3766   1300       C  
ATOM   1899  C   ALA A1043     181.966   9.472 573.423  1.00170.56           C  
ANISOU 1899  C   ALA A1043    19252  26884  18667   2217  -3457    997       C  
ATOM   1900  O   ALA A1043     181.060  10.259 573.709  1.00168.96           O  
ANISOU 1900  O   ALA A1043    18855  27075  18265   2009  -3339    994       O  
ATOM   1901  CB  ALA A1043     181.608   8.408 571.188  1.00171.33           C  
ANISOU 1901  CB  ALA A1043    20260  26079  18759   2426  -3426   1173       C  
ATOM   1902  N   THR A1044     183.248   9.697 573.722  1.00166.55           N  
ANISOU 1902  N   THR A1044    18467  26302  18511   2472  -3346    722       N  
ATOM   1903  CA  THR A1044     183.663  10.874 574.470  1.00159.22           C  
ANISOU 1903  CA  THR A1044    16980  25754  17763   2506  -3117    399       C  
ATOM   1904  C   THR A1044     185.068  11.278 574.042  1.00151.24           C  
ANISOU 1904  C   THR A1044    15772  24406  17287   2863  -2802     47       C  
ATOM   1905  O   THR A1044     185.953  10.410 573.973  1.00150.71           O  
ANISOU 1905  O   THR A1044    15835  24034  17393   3050  -2980     70       O  
ATOM   1906  CB  THR A1044     183.638  10.619 575.979  1.00161.41           C  
ANISOU 1906  CB  THR A1044    16971  26534  17823   2340  -3515    491       C  
ATOM   1907  OG1 THR A1044     182.376  10.052 576.353  1.00163.89           O  
ANISOU 1907  OG1 THR A1044    17494  27129  17650   2006  -3817    891       O  
ATOM   1908  CG2 THR A1044     183.847  11.917 576.745  1.00159.90           C  
ANISOU 1908  CG2 THR A1044    16217  26778  17760   2363  -3307    133       C  
ATOM   1909  N   PRO A1045     185.308  12.566 573.749  1.00144.94           N  
ANISOU 1909  N   PRO A1045    14647  23642  16782   2964  -2341   -271       N  
ATOM   1910  CA  PRO A1045     186.652  13.043 573.404  1.00139.68           C  
ANISOU 1910  CA  PRO A1045    13713  22679  16681   3278  -2012   -598       C  
ATOM   1911  C   PRO A1045     187.600  13.033 574.600  1.00144.00           C  
ANISOU 1911  C   PRO A1045    13811  23446  17458   3345  -2261   -799       C  
ATOM   1912  O   PRO A1045     187.129  12.941 575.734  1.00147.26           O  
ANISOU 1912  O   PRO A1045    14071  24317  17563   3146  -2619   -726       O  
ATOM   1913  CB  PRO A1045     186.402  14.474 572.920  1.00134.87           C  
ANISOU 1913  CB  PRO A1045    12857  22111  16274   3287  -1506   -826       C  
ATOM   1914  CG  PRO A1045     185.148  14.885 573.610  1.00136.15           C  
ANISOU 1914  CG  PRO A1045    12943  22773  16016   2978  -1680   -733       C  
ATOM   1915  CD  PRO A1045     184.307  13.644 573.676  1.00141.35           C  
ANISOU 1915  CD  PRO A1045    14058  23475  16172   2788  -2100   -329       C  
ATOM   1916  N   PRO A1056     185.027  15.964 588.019  1.00140.32           N  
ANISOU 1916  N   PRO A1056    10785  28483  14049   2595  -4772  -1616       N  
ATOM   1917  CA  PRO A1056     184.917  14.961 586.966  1.00138.47           C  
ANISOU 1917  CA  PRO A1056    10801  28002  13811   2508  -4838  -1209       C  
ATOM   1918  C   PRO A1056     184.050  15.456 585.810  1.00137.39           C  
ANISOU 1918  C   PRO A1056    10678  27825  13700   2372  -4510  -1163       C  
ATOM   1919  O   PRO A1056     182.821  15.421 585.881  1.00133.78           O  
ANISOU 1919  O   PRO A1056    10426  27589  12816   2116  -4400   -867       O  
ATOM   1920  CB  PRO A1056     184.358  13.665 587.528  1.00140.47           C  
ANISOU 1920  CB  PRO A1056    11471  28364  13538   2304  -5109   -612       C  
ATOM   1921  N   GLU A1057     184.706  15.915 584.741  1.00141.99           N  
ANISOU 1921  N   GLU A1057    11105  27998  14845   2533  -4283  -1443       N  
ATOM   1922  CA  GLU A1057     183.984  16.388 583.567  1.00144.86           C  
ANISOU 1922  CA  GLU A1057    11635  28082  15325   2400  -3868  -1387       C  
ATOM   1923  C   GLU A1057     183.301  15.251 582.819  1.00156.10           C  
ANISOU 1923  C   GLU A1057    13599  29243  16469   2190  -3899   -830       C  
ATOM   1924  O   GLU A1057     182.311  15.491 582.118  1.00148.11           O  
ANISOU 1924  O   GLU A1057    12764  28196  15313   2016  -3668   -677       O  
ATOM   1925  CB  GLU A1057     184.934  17.135 582.629  1.00127.99           C  
ANISOU 1925  CB  GLU A1057     9334  25374  13922   2604  -3505  -1777       C  
ATOM   1926  N   MET A1058     183.803  14.021 582.958  1.00172.79           N  
ANISOU 1926  N   MET A1058    15975  31157  18520   2212  -4207   -536       N  
ATOM   1927  CA  MET A1058     183.171  12.884 582.299  1.00175.20           C  
ANISOU 1927  CA  MET A1058    16794  31188  18586   2016  -4301    -15       C  
ATOM   1928  C   MET A1058     181.767  12.640 582.832  1.00174.32           C  
ANISOU 1928  C   MET A1058    16782  31597  17855   1702  -4440    377       C  
ATOM   1929  O   MET A1058     180.894  12.176 582.090  1.00174.34           O  
ANISOU 1929  O   MET A1058    17127  31412  17702   1493  -4385    717       O  
ATOM   1930  CB  MET A1058     184.029  11.632 582.475  1.00189.04           C  
ANISOU 1930  CB  MET A1058    18774  32643  20409   2119  -4654    198       C  
ATOM   1931  CG  MET A1058     185.400  11.715 581.828  1.00196.02           C  
ANISOU 1931  CG  MET A1058    19594  32967  21920   2429  -4508   -139       C  
ATOM   1932  SD  MET A1058     185.326  11.657 580.029  1.00189.27           S  
ANISOU 1932  SD  MET A1058    19115  31406  21393   2467  -4094    -99       S  
ATOM   1933  CE  MET A1058     184.614  10.033 579.776  1.00186.29           C  
ANISOU 1933  CE  MET A1058    19342  30832  20609   2256  -4471    522       C  
ATOM   1934  N   LYS A1059     181.531  12.946 584.110  1.00169.04           N  
ANISOU 1934  N   LYS A1059    15808  31590  16830   1676  -4622    330       N  
ATOM   1935  CA  LYS A1059     180.205  12.748 584.683  1.00152.19           C  
ANISOU 1935  CA  LYS A1059    13867  29724  14235   1351  -4578    691       C  
ATOM   1936  C   LYS A1059     179.208  13.774 584.161  1.00147.71           C  
ANISOU 1936  C   LYS A1059    13181  29317  13626   1240  -4223    541       C  
ATOM   1937  O   LYS A1059     178.018  13.467 584.035  1.00146.81           O  
ANISOU 1937  O   LYS A1059    13292  29255  13235    959  -4151    895       O  
ATOM   1938  CB  LYS A1059     180.277  12.801 586.208  1.00146.41           C  
ANISOU 1938  CB  LYS A1059    13033  29316  13278   1358  -4668    650       C  
ATOM   1939  CG  LYS A1059     181.098  11.681 586.826  1.00145.69           C  
ANISOU 1939  CG  LYS A1059    13114  29081  13160   1432  -5049    876       C  
ATOM   1940  CD  LYS A1059     181.071  11.747 588.343  1.00153.93           C  
ANISOU 1940  CD  LYS A1059    14077  30489  13920   1449  -5132    859       C  
ATOM   1941  CE  LYS A1059     181.841  10.591 588.958  1.00161.97           C  
ANISOU 1941  CE  LYS A1059    15294  31354  14892   1519  -5533   1116       C  
ATOM   1942  NZ  LYS A1059     181.280   9.274 588.549  1.00159.37           N  
ANISOU 1942  NZ  LYS A1059    15389  30755  14409   1268  -5706   1725       N  
ATOM   1943  N   ASP A1060     179.667  14.989 583.855  1.00152.98           N  
ANISOU 1943  N   ASP A1060    13484  30034  14606   1456  -4003     16       N  
ATOM   1944  CA  ASP A1060     178.780  15.986 583.265  1.00151.32           C  
ANISOU 1944  CA  ASP A1060    13165  29932  14398   1378  -3681   -142       C  
ATOM   1945  C   ASP A1060     178.542  15.703 581.786  1.00149.37           C  
ANISOU 1945  C   ASP A1060    13253  29146  14356   1319  -3508     28       C  
ATOM   1946  O   ASP A1060     177.410  15.828 581.301  1.00151.50           O  
ANISOU 1946  O   ASP A1060    13659  29488  14416   1122  -3386    214       O  
ATOM   1947  CB  ASP A1060     179.360  17.387 583.458  1.00151.81           C  
ANISOU 1947  CB  ASP A1060    12787  30079  14816   1616  -3466   -759       C  
ATOM   1948  CG  ASP A1060     178.347  18.481 583.180  1.00158.46           C  
ANISOU 1948  CG  ASP A1060    13518  31084  15605   1527  -3151   -928       C  
ATOM   1949  OD1 ASP A1060     177.151  18.160 583.020  1.00161.31           O  
ANISOU 1949  OD1 ASP A1060    14114  31564  15610   1279  -3104   -575       O  
ATOM   1950  OD2 ASP A1060     178.747  19.662 583.121  1.00160.99           O  
ANISOU 1950  OD2 ASP A1060    13520  31369  16279   1705  -2950  -1416       O  
ATOM   1951  N   PHE A1061     179.602  15.331 581.061  1.00140.79           N  
ANISOU 1951  N   PHE A1061    12344  27444  13705   1498  -3457    -50       N  
ATOM   1952  CA  PHE A1061     179.448  14.863 579.687  1.00128.42           C  
ANISOU 1952  CA  PHE A1061    11211  25271  12311   1469  -3298    144       C  
ATOM   1953  C   PHE A1061     178.420  13.742 579.616  1.00124.53           C  
ANISOU 1953  C   PHE A1061    11098  24832  11388   1182  -3559    692       C  
ATOM   1954  O   PHE A1061     177.538  13.739 578.750  1.00127.05           O  
ANISOU 1954  O   PHE A1061    11666  24977  11630   1046  -3431    851       O  
ATOM   1955  CB  PHE A1061     180.802  14.393 579.146  1.00125.23           C  
ANISOU 1955  CB  PHE A1061    10938  24282  12360   1721  -3281     29       C  
ATOM   1956  CG  PHE A1061     180.781  13.991 577.695  1.00126.76           C  
ANISOU 1956  CG  PHE A1061    11571  23847  12746   1768  -3087    160       C  
ATOM   1957  CD1 PHE A1061     180.359  12.726 577.313  1.00129.42           C  
ANISOU 1957  CD1 PHE A1061    12372  23947  12855   1634  -3350    590       C  
ATOM   1958  CD2 PHE A1061     181.206  14.872 576.714  1.00125.02           C  
ANISOU 1958  CD2 PHE A1061    11304  23262  12937   1963  -2652   -146       C  
ATOM   1959  CE1 PHE A1061     180.343  12.356 575.982  1.00125.49           C  
ANISOU 1959  CE1 PHE A1061    12291  22881  12507   1716  -3201    672       C  
ATOM   1960  CE2 PHE A1061     181.197  14.504 575.382  1.00117.83           C  
ANISOU 1960  CE2 PHE A1061    10815  21804  12150   2045  -2467    -29       C  
ATOM   1961  CZ  PHE A1061     180.766  13.244 575.016  1.00116.95           C  
ANISOU 1961  CZ  PHE A1061    11174  21479  11782   1935  -2752    361       C  
ATOM   1962  N   ARG A1062     178.520  12.778 580.533  1.00123.31           N  
ANISOU 1962  N   ARG A1062    10985  24906  10962   1087  -3945    994       N  
ATOM   1963  CA  ARG A1062     177.541  11.703 580.601  1.00124.43           C  
ANISOU 1963  CA  ARG A1062    11437  25121  10720    785  -4219   1549       C  
ATOM   1964  C   ARG A1062     176.195  12.187 581.121  1.00124.80           C  
ANISOU 1964  C   ARG A1062    11306  25745  10368    524  -4153   1684       C  
ATOM   1965  O   ARG A1062     175.179  11.526 580.881  1.00127.91           O  
ANISOU 1965  O   ARG A1062    11995  26002  10605    243  -4207   2078       O  
ATOM   1966  CB  ARG A1062     178.075  10.574 581.484  1.00133.08           C  
ANISOU 1966  CB  ARG A1062    12614  26289  11662    765  -4638   1851       C  
ATOM   1967  CG  ARG A1062     177.428   9.220 581.246  1.00135.43           C  
ANISOU 1967  CG  ARG A1062    13335  26362  11760    503  -4949   2435       C  
ATOM   1968  CD  ARG A1062     178.474   8.143 580.972  1.00138.69           C  
ANISOU 1968  CD  ARG A1062    14053  26213  12430    662  -5213   2537       C  
ATOM   1969  NE  ARG A1062     179.473   8.047 582.035  1.00140.91           N  
ANISOU 1969  NE  ARG A1062    14101  26726  12712    843  -5406   2420       N  
ATOM   1970  CZ  ARG A1062     180.702   8.548 581.957  1.00136.98           C  
ANISOU 1970  CZ  ARG A1062    13420  26033  12594   1176  -5279   1959       C  
ATOM   1971  NH1 ARG A1062     181.094   9.186 580.862  1.00141.02           N  
ANISOU 1971  NH1 ARG A1062    13954  26119  13510   1358  -4923   1601       N  
ATOM   1972  NH2 ARG A1062     181.542   8.413 582.974  1.00135.21           N  
ANISOU 1972  NH2 ARG A1062    12982  26040  12351   1333  -5510   1865       N  
ATOM   1973  N   HIS A1063     176.161  13.323 581.817  1.00132.82           N  
ANISOU 1973  N   HIS A1063    11943  27143  11380    607  -3922   1310       N  
ATOM   1974  CA  HIS A1063     174.924  13.862 582.362  1.00134.22           C  
ANISOU 1974  CA  HIS A1063    12027  27648  11324    395  -3706   1352       C  
ATOM   1975  C   HIS A1063     174.300  14.927 581.468  1.00130.31           C  
ANISOU 1975  C   HIS A1063    11410  27193  10910    415  -3423   1102       C  
ATOM   1976  O   HIS A1063     173.380  15.627 581.903  1.00133.17           O  
ANISOU 1976  O   HIS A1063    11612  27861  11126    309  -3212   1023       O  
ATOM   1977  CB  HIS A1063     175.156  14.427 583.766  1.00137.57           C  
ANISOU 1977  CB  HIS A1063    12146  28486  11637    487  -3644   1114       C  
ATOM   1978  CG  HIS A1063     173.908  14.514 584.588  1.00128.36           C  
ANISOU 1978  CG  HIS A1063    10938  27691  10144    259  -3507   1317       C  
ATOM   1979  ND1 HIS A1063     173.274  13.401 585.097  1.00131.00           N  
ANISOU 1979  ND1 HIS A1063    11489  28045  10238      4  -3655   1834       N  
ATOM   1980  CD2 HIS A1063     173.166  15.579 584.975  1.00128.07           C  
ANISOU 1980  CD2 HIS A1063    10640  28029   9993    260  -3232   1075       C  
ATOM   1981  CE1 HIS A1063     172.201  13.776 585.768  1.00132.32           C  
ANISOU 1981  CE1 HIS A1063    11498  28626  10154   -140  -3462   1909       C  
ATOM   1982  NE2 HIS A1063     172.111  15.092 585.709  1.00130.54           N  
ANISOU 1982  NE2 HIS A1063    10991  28623   9987     19  -3207   1448       N  
ATOM   1983  N   GLY A1064     174.781  15.074 580.238  1.00126.14           N  
ANISOU 1983  N   GLY A1064    10971  26326  10630    570  -3384    970       N  
ATOM   1984  CA  GLY A1064     174.076  15.892 579.271  1.00130.93           C  
ANISOU 1984  CA  GLY A1064    11621  26772  11353    558  -3081    816       C  
ATOM   1985  C   GLY A1064     173.039  15.081 578.520  1.00150.88           C  
ANISOU 1985  C   GLY A1064    14540  29090  13699    308  -3189   1251       C  
ATOM   1986  O   GLY A1064     171.893  15.512 578.341  1.00151.38           O  
ANISOU 1986  O   GLY A1064    14547  29395  13577    149  -3101   1308       O  
ATOM   1987  N   PHE A1065     173.435  13.881 578.090  1.00164.01           N  
ANISOU 1987  N   PHE A1065    16593  30291  15431    280  -3411   1549       N  
ATOM   1988  CA  PHE A1065     172.537  13.034 577.315  1.00169.80           C  
ANISOU 1988  CA  PHE A1065    17725  30739  16053     61  -3567   1940       C  
ATOM   1989  C   PHE A1065     171.445  12.398 578.165  1.00171.95           C  
ANISOU 1989  C   PHE A1065    17977  31335  16021   -294  -3755   2350       C  
ATOM   1990  O   PHE A1065     170.401  12.028 577.621  1.00174.04           O  
ANISOU 1990  O   PHE A1065    18462  31424  16240   -511  -3797   2594       O  
ATOM   1991  CB  PHE A1065     173.329  11.945 576.592  1.00179.03           C  
ANISOU 1991  CB  PHE A1065    19339  31237  17446    170  -3743   2087       C  
ATOM   1992  CG  PHE A1065     174.142  12.452 575.437  1.00182.08           C  
ANISOU 1992  CG  PHE A1065    19899  31065  18218    493  -3437   1731       C  
ATOM   1993  CD1 PHE A1065     173.534  12.780 574.236  1.00182.88           C  
ANISOU 1993  CD1 PHE A1065    20257  30849  18381    523  -3252   1682       C  
ATOM   1994  CD2 PHE A1065     175.514  12.597 575.548  1.00181.77           C  
ANISOU 1994  CD2 PHE A1065    19760  30824  18479    777  -3333   1458       C  
ATOM   1995  CE1 PHE A1065     174.279  13.246 573.169  1.00180.11           C  
ANISOU 1995  CE1 PHE A1065    20076  30007  18351    835  -2941   1392       C  
ATOM   1996  CE2 PHE A1065     176.263  13.057 574.485  1.00180.70           C  
ANISOU 1996  CE2 PHE A1065    19761  30191  18705   1071  -3014   1167       C  
ATOM   1997  CZ  PHE A1065     175.646  13.385 573.295  1.00179.34           C  
ANISOU 1997  CZ  PHE A1065    19860  29723  18557   1103  -2804   1146       C  
ATOM   1998  N   ASP A1066     171.653  12.252 579.476  1.00167.35           N  
ANISOU 1998  N   ASP A1066    17197  31039  15350   -345  -3779   2391       N  
ATOM   1999  CA  ASP A1066     170.598  11.674 580.303  1.00155.50           C  
ANISOU 1999  CA  ASP A1066    15709  29707  13666   -661  -3816   2755       C  
ATOM   2000  C   ASP A1066     169.505  12.695 580.601  1.00139.51           C  
ANISOU 2000  C   ASP A1066    13389  28099  11518   -757  -3509   2607       C  
ATOM   2001  O   ASP A1066     168.314  12.374 580.514  1.00131.78           O  
ANISOU 2001  O   ASP A1066    12469  27146  10457  -1023  -3501   2888       O  
ATOM   2002  CB  ASP A1066     171.184  11.098 581.597  1.00157.02           C  
ANISOU 2002  CB  ASP A1066    15824  30085  13754   -659  -3957   2891       C  
ATOM   2003  CG  ASP A1066     171.908  12.135 582.439  1.00158.19           C  
ANISOU 2003  CG  ASP A1066    15596  30635  13874   -409  -3781   2458       C  
ATOM   2004  OD1 ASP A1066     171.805  13.342 582.141  1.00157.09           O  
ANISOU 2004  OD1 ASP A1066    15217  30676  13793   -274  -3524   2066       O  
ATOM   2005  OD2 ASP A1066     172.586  11.737 583.408  1.00163.14           O  
ANISOU 2005  OD2 ASP A1066    16173  31381  14431   -336  -3920   2500       O  
ATOM   2006  N   ILE A1067     169.889  13.927 580.949  1.00133.11           N  
ANISOU 2006  N   ILE A1067    12244  27615  10719   -536  -3270   2157       N  
ATOM   2007  CA  ILE A1067     168.907  14.993 581.090  1.00130.90           C  
ANISOU 2007  CA  ILE A1067    11695  27690  10351   -576  -2983   1960       C  
ATOM   2008  C   ILE A1067     168.295  15.342 579.742  1.00121.46           C  
ANISOU 2008  C   ILE A1067    10647  26234   9267   -600  -2915   1911       C  
ATOM   2009  O   ILE A1067     167.178  15.869 579.686  1.00121.90           O  
ANISOU 2009  O   ILE A1067    10581  26489   9245   -720  -2750   1900       O  
ATOM   2010  CB  ILE A1067     169.539  16.233 581.758  1.00135.58           C  
ANISOU 2010  CB  ILE A1067    11915  28633  10966   -305  -2779   1454       C  
ATOM   2011  CG1 ILE A1067     168.459  17.235 582.175  1.00142.21           C  
ANISOU 2011  CG1 ILE A1067    12473  29894  11666   -350  -2505   1285       C  
ATOM   2012  CG2 ILE A1067     170.543  16.898 580.832  1.00126.89           C  
ANISOU 2012  CG2 ILE A1067    10787  27288  10138    -25  -2746   1065       C  
ATOM   2013  CD1 ILE A1067     169.008  18.515 582.768  1.00140.50           C  
ANISOU 2013  CD1 ILE A1067    11915  29971  11496    -72  -2320    749       C  
ATOM   2014  N   LEU A1068     168.995  15.047 578.644  1.00123.32           N  
ANISOU 2014  N   LEU A1068    11147  26045   9664   -468  -3047   1886       N  
ATOM   2015  CA  LEU A1068     168.393  15.202 577.325  1.00126.53           C  
ANISOU 2015  CA  LEU A1068    11772  26175  10128   -485  -3027   1898       C  
ATOM   2016  C   LEU A1068     167.317  14.145 577.089  1.00129.44           C  
ANISOU 2016  C   LEU A1068    12426  26320  10433   -803  -3218   2353       C  
ATOM   2017  O   LEU A1068     166.173  14.473 576.753  1.00119.70           O  
ANISOU 2017  O   LEU A1068    11167  25151   9165   -944  -3129   2389       O  
ATOM   2018  CB  LEU A1068     169.477  15.129 576.248  1.00125.22           C  
ANISOU 2018  CB  LEU A1068    11831  25619  10127   -216  -3090   1757       C  
ATOM   2019  CG  LEU A1068     169.152  15.709 574.870  1.00121.15           C  
ANISOU 2019  CG  LEU A1068    11564  24652   9814    -88  -2861   1572       C  
ATOM   2020  CD1 LEU A1068     168.932  17.212 574.951  1.00109.02           C  
ANISOU 2020  CD1 LEU A1068     9670  23412   8340     46  -2527   1162       C  
ATOM   2021  CD2 LEU A1068     170.251  15.375 573.872  1.00109.66           C  
ANISOU 2021  CD2 LEU A1068    10493  22489   8684    178  -2780   1465       C  
ATOM   2022  N   VAL A1069     167.662  12.870 577.293  1.00147.41           N  
ANISOU 2022  N   VAL A1069    14953  28336  12719   -918  -3501   2696       N  
ATOM   2023  CA  VAL A1069     166.755  11.774 576.960  1.00159.01           C  
ANISOU 2023  CA  VAL A1069    16710  29515  14192  -1206  -3739   3121       C  
ATOM   2024  C   VAL A1069     165.546  11.760 577.890  1.00176.47           C  
ANISOU 2024  C   VAL A1069    18655  32127  16267  -1502  -3645   3338       C  
ATOM   2025  O   VAL A1069     164.421  11.467 577.461  1.00164.87           O  
ANISOU 2025  O   VAL A1069    17262  30571  14810  -1727  -3711   3549       O  
ATOM   2026  CB  VAL A1069     167.516  10.434 576.986  1.00154.16           C  
ANISOU 2026  CB  VAL A1069    16415  28512  13645  -1228  -4081   3413       C  
ATOM   2027  CG1 VAL A1069     166.552   9.260 576.982  1.00156.58           C  
ANISOU 2027  CG1 VAL A1069    16930  28595  13968  -1565  -4339   3876       C  
ATOM   2028  CG2 VAL A1069     168.457  10.340 575.795  1.00141.06           C  
ANISOU 2028  CG2 VAL A1069    15070  26419  12107   -953  -4197   3258       C  
ATOM   2029  N   GLY A1070     165.753  12.084 579.171  1.00199.53           N  
ANISOU 2029  N   GLY A1070    21247  35519  19047  -1490  -3495   3288       N  
ATOM   2030  CA  GLY A1070     164.651  12.062 580.124  1.00216.03           C  
ANISOU 2030  CA  GLY A1070    23056  38070  20956  -1746  -3384   3518       C  
ATOM   2031  C   GLY A1070     163.473  12.911 579.690  1.00227.48           C  
ANISOU 2031  C   GLY A1070    24326  39719  22386  -1817  -3179   3389       C  
ATOM   2032  O   GLY A1070     162.316  12.552 579.921  1.00230.98           O  
ANISOU 2032  O   GLY A1070    24664  40347  22751  -2100  -3192   3695       O  
ATOM   2033  N   GLN A1071     163.750  14.047 579.054  1.00235.16           N  
ANISOU 2033  N   GLN A1071    25243  40670  23436  -1563  -2995   2943       N  
ATOM   2034  CA  GLN A1071     162.709  14.862 578.444  1.00234.61           C  
ANISOU 2034  CA  GLN A1071    25065  40697  23380  -1590  -2836   2792       C  
ATOM   2035  C   GLN A1071     162.407  14.441 577.011  1.00231.57           C  
ANISOU 2035  C   GLN A1071    25062  39771  23151  -1626  -3035   2880       C  
ATOM   2036  O   GLN A1071     161.291  14.674 576.529  1.00231.70           O  
ANISOU 2036  O   GLN A1071    25049  39811  23176  -1750  -3014   2919       O  
ATOM   2037  CB  GLN A1071     163.116  16.340 578.492  1.00238.13           C  
ANISOU 2037  CB  GLN A1071    25250  41395  23832  -1290  -2546   2267       C  
ATOM   2038  CG  GLN A1071     162.174  17.293 577.777  1.00240.80           C  
ANISOU 2038  CG  GLN A1071    25496  41793  24205  -1258  -2387   2055       C  
ATOM   2039  CD  GLN A1071     162.690  17.691 576.410  1.00238.42           C  
ANISOU 2039  CD  GLN A1071    25458  41063  24068  -1041  -2422   1822       C  
ATOM   2040  OE1 GLN A1071     163.889  17.901 576.227  1.00238.77           O  
ANISOU 2040  OE1 GLN A1071    25557  40975  24190   -808  -2414   1613       O  
ATOM   2041  NE2 GLN A1071     161.788  17.794 575.441  1.00235.69           N  
ANISOU 2041  NE2 GLN A1071    25263  40524  23764  -1104  -2467   1862       N  
ATOM   2042  N   ILE A1072     163.369  13.811 576.332  1.00208.20           N  
ANISOU 2042  N   ILE A1072    22464  36340  20304  -1504  -3244   2911       N  
ATOM   2043  CA  ILE A1072     163.136  13.324 574.973  1.00175.13           C  
ANISOU 2043  CA  ILE A1072    18687  31625  16229  -1504  -3463   2999       C  
ATOM   2044  C   ILE A1072     161.967  12.349 574.948  1.00160.15           C  
ANISOU 2044  C   ILE A1072    16888  29609  14350  -1853  -3696   3410       C  
ATOM   2045  O   ILE A1072     161.056  12.467 574.120  1.00153.82           O  
ANISOU 2045  O   ILE A1072    16192  28655  13599  -1921  -3759   3415       O  
ATOM   2046  CB  ILE A1072     164.414  12.681 574.409  1.00164.22           C  
ANISOU 2046  CB  ILE A1072    17663  29805  14927  -1308  -3659   3002       C  
ATOM   2047  CG1 ILE A1072     165.352  13.755 573.858  1.00158.40           C  
ANISOU 2047  CG1 ILE A1072    16878  29107  14201   -941  -3442   2579       C  
ATOM   2048  CG2 ILE A1072     164.064  11.649 573.354  1.00158.31           C  
ANISOU 2048  CG2 ILE A1072    17381  28501  14266  -1397  -3996   3252       C  
ATOM   2049  CD1 ILE A1072     166.787  13.306 573.744  1.00157.31           C  
ANISOU 2049  CD1 ILE A1072    16903  28758  14108   -719  -3554   2547       C  
ATOM   2050  N   ASP A1073     161.976  11.365 575.852  1.00154.23           N  
ANISOU 2050  N   ASP A1073    16097  28937  13569  -2079  -3843   3770       N  
ATOM   2051  CA  ASP A1073     160.865  10.420 575.905  1.00157.74           C  
ANISOU 2051  CA  ASP A1073    16573  29314  14047  -2442  -4068   4201       C  
ATOM   2052  C   ASP A1073     159.562  11.114 576.277  1.00159.36           C  
ANISOU 2052  C   ASP A1073    16386  30009  14153  -2621  -3855   4210       C  
ATOM   2053  O   ASP A1073     158.480  10.640 575.912  1.00159.43           O  
ANISOU 2053  O   ASP A1073    16415  29931  14229  -2879  -4025   4465       O  
ATOM   2054  CB  ASP A1073     161.173   9.290 576.886  1.00161.31           C  
ANISOU 2054  CB  ASP A1073    17017  29808  14466  -2647  -4241   4607       C  
ATOM   2055  CG  ASP A1073     162.245   8.351 576.371  1.00156.99           C  
ANISOU 2055  CG  ASP A1073    16909  28684  14057  -2519  -4545   4673       C  
ATOM   2056  OD1 ASP A1073     163.439   8.698 576.475  1.00150.30           O  
ANISOU 2056  OD1 ASP A1073    16107  27814  13186  -2230  -4457   4414       O  
ATOM   2057  OD2 ASP A1073     161.894   7.269 575.855  1.00159.26           O  
ANISOU 2057  OD2 ASP A1073    17483  28541  14487  -2702  -4888   4977       O  
ATOM   2058  N   ASP A1074     159.642  12.235 576.997  1.00156.34           N  
ANISOU 2058  N   ASP A1074    15635  30144  13623  -2478  -3502   3926       N  
ATOM   2059  CA  ASP A1074     158.455  13.041 577.250  1.00160.70           C  
ANISOU 2059  CA  ASP A1074    15821  31159  14077  -2579  -3281   3860       C  
ATOM   2060  C   ASP A1074     157.980  13.765 575.997  1.00157.65           C  
ANISOU 2060  C   ASP A1074    15574  30517  13810  -2439  -3270   3571       C  
ATOM   2061  O   ASP A1074     156.796  14.104 575.904  1.00154.04           O  
ANISOU 2061  O   ASP A1074    14915  30282  13329  -2581  -3215   3608       O  
ATOM   2062  CB  ASP A1074     158.727  14.050 578.368  1.00160.36           C  
ANISOU 2062  CB  ASP A1074    15369  31719  13842  -2422  -2927   3597       C  
ATOM   2063  CG  ASP A1074     159.210  13.390 579.645  1.00157.08           C  
ANISOU 2063  CG  ASP A1074    14818  31594  13271  -2521  -2938   3863       C  
ATOM   2064  OD1 ASP A1074     158.901  12.198 579.853  1.00158.13           O  
ANISOU 2064  OD1 ASP A1074    15049  31624  13410  -2810  -3170   4340       O  
ATOM   2065  OD2 ASP A1074     159.896  14.064 580.442  1.00153.74           O  
ANISOU 2065  OD2 ASP A1074    14192  31496  12725  -2306  -2731   3595       O  
ATOM   2066  N   ALA A1075     158.876  14.009 575.036  1.00156.00           N  
ANISOU 2066  N   ALA A1075    15695  29869  13708  -2157  -3322   3299       N  
ATOM   2067  CA  ALA A1075     158.465  14.608 573.771  1.00150.03           C  
ANISOU 2067  CA  ALA A1075    15127  28839  13038  -2008  -3342   3062       C  
ATOM   2068  C   ALA A1075     157.876  13.566 572.826  1.00147.70           C  
ANISOU 2068  C   ALA A1075    15204  28050  12864  -2177  -3723   3338       C  
ATOM   2069  O   ALA A1075     156.838  13.809 572.198  1.00146.52           O  
ANISOU 2069  O   ALA A1075    15057  27857  12758  -2243  -3788   3316       O  
ATOM   2070  CB  ALA A1075     159.650  15.317 573.114  1.00145.48           C  
ANISOU 2070  CB  ALA A1075    14735  28054  12488  -1630  -3227   2689       C  
ATOM   2071  N   LEU A1076     158.525  12.404 572.712  1.00146.62           N  
ANISOU 2071  N   LEU A1076    15386  27526  12797  -2233  -4000   3581       N  
ATOM   2072  CA  LEU A1076     157.965  11.322 571.908  1.00136.75           C  
ANISOU 2072  CA  LEU A1076    14482  25794  11684  -2403  -4405   3849       C  
ATOM   2073  C   LEU A1076     156.658  10.815 572.502  1.00136.76           C  
ANISOU 2073  C   LEU A1076    14194  26056  11711  -2814  -4509   4212       C  
ATOM   2074  O   LEU A1076     155.803  10.298 571.773  1.00129.35           O  
ANISOU 2074  O   LEU A1076    13416  24827  10903  -2968  -4801   4357       O  
ATOM   2075  CB  LEU A1076     158.980  10.185 571.777  1.00133.42           C  
ANISOU 2075  CB  LEU A1076    14435  24922  11336  -2365  -4679   4027       C  
ATOM   2076  CG  LEU A1076     158.666   9.047 570.802  1.00135.06           C  
ANISOU 2076  CG  LEU A1076    15090  24518  11709  -2453  -5139   4232       C  
ATOM   2077  CD1 LEU A1076     159.930   8.600 570.087  1.00134.55           C  
ANISOU 2077  CD1 LEU A1076    15495  23955  11672  -2151  -5297   4118       C  
ATOM   2078  CD2 LEU A1076     158.022   7.869 571.520  1.00129.31           C  
ANISOU 2078  CD2 LEU A1076    14244  23802  11086  -2875  -5398   4716       C  
ATOM   2079  N   LYS A1077     156.487  10.949 573.820  1.00151.42           N  
ANISOU 2079  N   LYS A1077    15618  28479  13437  -2991  -4283   4371       N  
ATOM   2080  CA  LYS A1077     155.199  10.648 574.435  1.00157.07           C  
ANISOU 2080  CA  LYS A1077    15979  29573  14127  -3374  -4308   4723       C  
ATOM   2081  C   LYS A1077     154.108  11.558 573.885  1.00160.48           C  
ANISOU 2081  C   LYS A1077    16236  30173  14567  -3349  -4202   4506       C  
ATOM   2082  O   LYS A1077     152.972  11.120 573.670  1.00162.58           O  
ANISOU 2082  O   LYS A1077    16409  30438  14925  -3630  -4401   4762       O  
ATOM   2083  CB  LYS A1077     155.302  10.783 575.954  1.00153.79           C  
ANISOU 2083  CB  LYS A1077    15130  29807  13497  -3494  -4031   4888       C  
ATOM   2084  CG  LYS A1077     153.981  10.639 576.691  1.00158.63           C  
ANISOU 2084  CG  LYS A1077    15300  30959  14013  -3867  -3975   5254       C  
ATOM   2085  CD  LYS A1077     154.167  10.813 578.190  1.00162.90           C  
ANISOU 2085  CD  LYS A1077    15436  32177  14282  -3927  -3685   5396       C  
ATOM   2086  CE  LYS A1077     152.836  10.782 578.922  1.00168.03           C  
ANISOU 2086  CE  LYS A1077    15602  33459  14782  -4271  -3581   5757       C  
ATOM   2087  NZ  LYS A1077     151.942  11.893 578.494  1.00168.37           N  
ANISOU 2087  NZ  LYS A1077    15429  33743  14799  -4164  -3385   5429       N  
ATOM   2088  N   LEU A1078     154.438  12.829 573.646  1.00158.04           N  
ANISOU 2088  N   LEU A1078    15869  29998  14181  -3016  -3908   4039       N  
ATOM   2089  CA  LEU A1078     153.496  13.753 573.031  1.00160.05           C  
ANISOU 2089  CA  LEU A1078    16004  30353  14454  -2937  -3821   3790       C  
ATOM   2090  C   LEU A1078     153.410  13.577 571.521  1.00163.25           C  
ANISOU 2090  C   LEU A1078    16877  30130  15022  -2794  -4122   3657       C  
ATOM   2091  O   LEU A1078     152.454  14.062 570.907  1.00188.60           O  
ANISOU 2091  O   LEU A1078    20037  33340  18280  -2784  -4166   3535       O  
ATOM   2092  CB  LEU A1078     153.882  15.198 573.356  1.00152.93           C  
ANISOU 2092  CB  LEU A1078    14863  29821  13424  -2632  -3408   3347       C  
ATOM   2093  CG  LEU A1078     154.047  15.557 574.834  1.00157.12           C  
ANISOU 2093  CG  LEU A1078    14947  30993  13760  -2683  -3091   3375       C  
ATOM   2094  CD1 LEU A1078     154.372  17.035 574.993  1.00138.96           C  
ANISOU 2094  CD1 LEU A1078    12440  28977  11382  -2355  -2738   2883       C  
ATOM   2095  CD2 LEU A1078     152.804  15.189 575.628  1.00128.47           C  
ANISOU 2095  CD2 LEU A1078    10934  27851  10030  -3038  -3078   3737       C  
ATOM   2096  N   ALA A1079     154.385  12.900 570.911  1.00169.64           N  
ANISOU 2096  N   ALA A1079    18143  30416  15897  -2658  -4337   3670       N  
ATOM   2097  CA  ALA A1079     154.346  12.673 569.471  1.00174.70           C  
ANISOU 2097  CA  ALA A1079    19268  30467  16642  -2487  -4636   3549       C  
ATOM   2098  C   ALA A1079     153.352  11.585 569.087  1.00184.81           C  
ANISOU 2098  C   ALA A1079    20664  31460  18093  -2791  -5070   3872       C  
ATOM   2099  O   ALA A1079     152.827  11.599 567.968  1.00186.61           O  
ANISOU 2099  O   ALA A1079    21168  31331  18404  -2689  -5314   3746       O  
ATOM   2100  CB  ALA A1079     155.740  12.313 568.957  1.00175.67           C  
ANISOU 2100  CB  ALA A1079    19839  30159  16749  -2215  -4710   3454       C  
ATOM   2101  N   ASN A1080     153.081  10.643 569.988  1.00160.57           N  
ANISOU 2101  N   ASN A1080    20508  23977  16524   -836   4582   2986       N  
ATOM   2102  CA  ASN A1080     152.172   9.539 569.716  1.00167.54           C  
ANISOU 2102  CA  ASN A1080    21245  24792  17620   -975   4674   3144       C  
ATOM   2103  C   ASN A1080     150.813   9.710 570.384  1.00183.35           C  
ANISOU 2103  C   ASN A1080    23139  26935  19590  -1061   5011   3055       C  
ATOM   2104  O   ASN A1080     149.961   8.825 570.260  1.00187.82           O  
ANISOU 2104  O   ASN A1080    23581  27467  20315  -1200   5118   3171       O  
ATOM   2105  CB  ASN A1080     152.806   8.215 570.162  1.00160.84           C  
ANISOU 2105  CB  ASN A1080    20611  23842  16659  -1106   4541   3413       C  
ATOM   2106  CG  ASN A1080     152.183   7.009 569.484  1.00156.32           C  
ANISOU 2106  CG  ASN A1080    19894  23128  16374  -1229   4536   3584       C  
ATOM   2107  OD1 ASN A1080     151.679   7.103 568.364  1.00155.32           O  
ANISOU 2107  OD1 ASN A1080    19511  22935  16567  -1190   4513   3526       O  
ATOM   2108  ND2 ASN A1080     152.211   5.867 570.162  1.00153.95           N  
ANISOU 2108  ND2 ASN A1080    19767  22771  15956  -1383   4555   3794       N  
ATOM   2109  N   GLU A1081     150.586  10.823 571.082  1.00191.96           N  
ANISOU 2109  N   GLU A1081    24275  28181  20482   -989   5184   2844       N  
ATOM   2110  CA  GLU A1081     149.316  11.049 571.758  1.00204.20           C  
ANISOU 2110  CA  GLU A1081    25720  29874  21992  -1060   5517   2740       C  
ATOM   2111  C   GLU A1081     148.252  11.648 570.849  1.00211.74           C  
ANISOU 2111  C   GLU A1081    26320  30855  23278   -965   5630   2573       C  
ATOM   2112  O   GLU A1081     147.059  11.518 571.148  1.00215.29           O  
ANISOU 2112  O   GLU A1081    26604  31400  23796  -1049   5883   2534       O  
ATOM   2113  CB  GLU A1081     149.512  11.965 572.971  1.00207.01           C  
ANISOU 2113  CB  GLU A1081    26296  30380  21977  -1026   5669   2576       C  
ATOM   2114  CG  GLU A1081     149.822  13.409 572.615  1.00207.62           C  
ANISOU 2114  CG  GLU A1081    26337  30493  22057   -822   5631   2309       C  
ATOM   2115  CD  GLU A1081     149.932  14.302 573.834  1.00212.64           C  
ANISOU 2115  CD  GLU A1081    27197  31269  22327   -807   5799   2128       C  
ATOM   2116  OE1 GLU A1081     149.813  13.784 574.964  1.00216.34           O  
ANISOU 2116  OE1 GLU A1081    27859  31811  22529   -954   5938   2221       O  
ATOM   2117  OE2 GLU A1081     150.138  15.522 573.663  1.00212.45           O  
ANISOU 2117  OE2 GLU A1081    27171  31272  22279   -651   5795   1890       O  
ATOM   2118  N   GLY A1082     148.650  12.300 569.754  1.00214.23           N  
ANISOU 2118  N   GLY A1082    26511  31087  23798   -793   5449   2474       N  
ATOM   2119  CA  GLY A1082     147.728  12.923 568.818  1.00212.87           C  
ANISOU 2119  CA  GLY A1082    26014  30923  23945   -674   5519   2318       C  
ATOM   2120  C   GLY A1082     147.993  14.400 568.597  1.00211.47           C  
ANISOU 2120  C   GLY A1082    25832  30775  23742   -450   5511   2062       C  
ATOM   2121  O   GLY A1082     147.697  14.922 567.517  1.00209.58           O  
ANISOU 2121  O   GLY A1082    25373  30473  23785   -307   5445   1964       O  
ATOM   2122  N   LYS A1083     148.541  15.083 569.599  1.00194.50           N  
ANISOU 2122  N   LYS A1083    23935  28711  21256   -420   5574   1949       N  
ATOM   2123  CA  LYS A1083     148.852  16.508 569.509  1.00168.43           C  
ANISOU 2123  CA  LYS A1083    20678  25427  17892   -221   5574   1692       C  
ATOM   2124  C   LYS A1083     150.355  16.657 569.298  1.00155.61           C  
ANISOU 2124  C   LYS A1083    19292  23707  16126   -176   5295   1733       C  
ATOM   2125  O   LYS A1083     151.144  16.501 570.234  1.00161.00           O  
ANISOU 2125  O   LYS A1083    20254  24434  16484   -260   5253   1783       O  
ATOM   2126  CB  LYS A1083     148.384  17.249 570.757  1.00159.69           C  
ANISOU 2126  CB  LYS A1083    19684  24482  16508   -224   5845   1502       C  
ATOM   2127  CG  LYS A1083     146.873  17.362 570.881  1.00155.86           C  
ANISOU 2127  CG  LYS A1083    18928  24106  16185   -226   6131   1406       C  
ATOM   2128  CD  LYS A1083     146.481  18.324 571.991  1.00150.89           C  
ANISOU 2128  CD  LYS A1083    18404  23629  15298   -187   6389   1168       C  
ATOM   2129  CE  LYS A1083     144.979  18.555 572.016  1.00148.52           C  
ANISOU 2129  CE  LYS A1083    17799  23444  15188   -155   6666   1046       C  
ATOM   2130  NZ  LYS A1083     144.590  19.570 573.034  1.00150.35           N  
ANISOU 2130  NZ  LYS A1083    18118  23823  15185    -95   6917    789       N  
ATOM   2131  N   VAL A1084     150.748  16.966 568.059  1.00137.90           N  
ANISOU 2131  N   VAL A1084    16934  21335  14127    -45   5101   1710       N  
ATOM   2132  CA  VAL A1084     152.160  17.121 567.719  1.00136.59           C  
ANISOU 2132  CA  VAL A1084    16957  21078  13862      1   4832   1742       C  
ATOM   2133  C   VAL A1084     152.668  18.537 567.955  1.00140.91           C  
ANISOU 2133  C   VAL A1084    17655  21651  14235    144   4840   1480       C  
ATOM   2134  O   VAL A1084     153.890  18.754 567.965  1.00140.03           O  
ANISOU 2134  O   VAL A1084    17745  21501  13959    156   4640   1480       O  
ATOM   2135  CB  VAL A1084     152.402  16.714 566.250  1.00134.60           C  
ANISOU 2135  CB  VAL A1084    16526  20667  13947     54   4618   1851       C  
ATOM   2136  CG1 VAL A1084     153.861  16.341 566.022  1.00129.92           C  
ANISOU 2136  CG1 VAL A1084    16124  19992  13249     29   4335   1978       C  
ATOM   2137  CG2 VAL A1084     151.484  15.565 565.861  1.00137.63           C  
ANISOU 2137  CG2 VAL A1084    16692  21022  14581    -65   4669   2033       C  
ATOM   2138  N   LYS A1085     151.772  19.507 568.159  1.00144.86           N  
ANISOU 2138  N   LYS A1085    18065  22210  14764    251   5061   1251       N  
ATOM   2139  CA  LYS A1085     152.202  20.890 568.341  1.00145.77           C  
ANISOU 2139  CA  LYS A1085    18333  22321  14733    392   5074    983       C  
ATOM   2140  C   LYS A1085     153.024  21.056 569.614  1.00146.19           C  
ANISOU 2140  C   LYS A1085    18716  22469  14359    286   5071    942       C  
ATOM   2141  O   LYS A1085     153.972  21.850 569.646  1.00146.82           O  
ANISOU 2141  O   LYS A1085    18992  22513  14281    342   4943    805       O  
ATOM   2142  CB  LYS A1085     150.988  21.817 568.356  1.00153.50           C  
ANISOU 2142  CB  LYS A1085    19141  23338  15843    531   5322    752       C  
ATOM   2143  CG  LYS A1085     150.173  21.778 567.073  1.00153.32           C  
ANISOU 2143  CG  LYS A1085    18791  23219  16243    653   5306    773       C  
ATOM   2144  CD  LYS A1085     148.969  22.702 567.143  1.00154.42           C  
ANISOU 2144  CD  LYS A1085    18758  23403  16511    805   5539    546       C  
ATOM   2145  CE  LYS A1085     148.167  22.659 565.852  1.00149.26           C  
ANISOU 2145  CE  LYS A1085    17775  22657  16278    927   5495    572       C  
ATOM   2146  NZ  LYS A1085     146.975  23.551 565.909  1.00148.52           N  
ANISOU 2146  NZ  LYS A1085    17496  22609  16325   1090   5705    357       N  
ATOM   2147  N   GLU A1086     152.680  20.319 570.673  1.00146.08           N  
ANISOU 2147  N   GLU A1086    18778  22575  14153    124   5206   1056       N  
ATOM   2148  CA  GLU A1086     153.472  20.378 571.899  1.00136.65           C  
ANISOU 2148  CA  GLU A1086    17910  21467  12544     11   5187   1042       C  
ATOM   2149  C   GLU A1086     154.800  19.650 571.731  1.00125.25           C  
ANISOU 2149  C   GLU A1086    16623  19960  11007    -62   4877   1250       C  
ATOM   2150  O   GLU A1086     155.841  20.121 572.211  1.00117.53           O  
ANISOU 2150  O   GLU A1086    15896  18997   9762    -75   4741   1175       O  
ATOM   2151  CB  GLU A1086     152.682  19.788 573.068  1.00138.68           C  
ANISOU 2151  CB  GLU A1086    18212  21858  12621   -139   5433   1111       C  
ATOM   2152  CG  GLU A1086     151.440  20.574 573.469  1.00143.61           C  
ANISOU 2152  CG  GLU A1086    18709  22585  13273    -79   5754    880       C  
ATOM   2153  CD  GLU A1086     150.223  20.239 572.624  1.00143.80           C  
ANISOU 2153  CD  GLU A1086    18364  22588  13687    -21   5872    924       C  
ATOM   2154  OE1 GLU A1086     150.394  19.724 571.499  1.00138.13           O  
ANISOU 2154  OE1 GLU A1086    17484  21747  13252     17   5686   1070       O  
ATOM   2155  OE2 GLU A1086     149.092  20.488 573.091  1.00145.68           O  
ANISOU 2155  OE2 GLU A1086    18470  22937  13945    -20   6148    809       O  
ATOM   2156  N   ALA A1087     154.782  18.497 571.054  1.00123.54           N  
ANISOU 2156  N   ALA A1087    16257  19670  11012   -113   4757   1506       N  
ATOM   2157  CA  ALA A1087     156.016  17.761 570.805  1.00123.55           C  
ANISOU 2157  CA  ALA A1087    16376  19603  10965   -166   4455   1706       C  
ATOM   2158  C   ALA A1087     157.008  18.605 570.017  1.00123.93           C  
ANISOU 2158  C   ALA A1087    16458  19577  11053    -44   4238   1575       C  
ATOM   2159  O   ALA A1087     158.215  18.569 570.283  1.00123.91           O  
ANISOU 2159  O   ALA A1087    16649  19580  10852    -79   4019   1615       O  
ATOM   2160  CB  ALA A1087     155.712  16.457 570.069  1.00119.79           C  
ANISOU 2160  CB  ALA A1087    15711  19035  10770   -227   4380   1972       C  
ATOM   2161  N   GLN A1088     156.518  19.373 569.041  1.00125.06           N  
ANISOU 2161  N   GLN A1088    16415  19648  11455    100   4291   1418       N  
ATOM   2162  CA  GLN A1088     157.385  20.321 568.350  1.00125.73           C  
ANISOU 2162  CA  GLN A1088    16556  19658  11558    216   4123   1259       C  
ATOM   2163  C   GLN A1088     157.696  21.529 569.223  1.00127.11           C  
ANISOU 2163  C   GLN A1088    16963  19903  11429    239   4197    992       C  
ATOM   2164  O   GLN A1088     158.728  22.182 569.029  1.00120.31           O  
ANISOU 2164  O   GLN A1088    16245  19006  10460    270   4019    882       O  
ATOM   2165  CB  GLN A1088     156.743  20.765 567.036  1.00130.10           C  
ANISOU 2165  CB  GLN A1088    16860  20091  12480    372   4158   1180       C  
ATOM   2166  CG  GLN A1088     156.675  19.678 565.977  1.00132.56           C  
ANISOU 2166  CG  GLN A1088    16964  20305  13099    348   4027   1422       C  
ATOM   2167  CD  GLN A1088     156.079  20.174 564.674  1.00131.69           C  
ANISOU 2167  CD  GLN A1088    16622  20074  13339    501   4048   1336       C  
ATOM   2168  OE1 GLN A1088     154.866  20.349 564.560  1.00137.04           O  
ANISOU 2168  OE1 GLN A1088    17116  20763  14191    556   4243   1271       O  
ATOM   2169  NE2 GLN A1088     156.933  20.409 563.684  1.00123.67           N  
ANISOU 2169  NE2 GLN A1088    15614  18946  12429    570   3842   1335       N  
ATOM   2170  N   ALA A1089     156.822  21.843 570.183  1.00136.91           N  
ANISOU 2170  N   ALA A1089    18247  21242  12530    212   4460    877       N  
ATOM   2171  CA  ALA A1089     157.087  22.948 571.096  1.00136.93           C  
ANISOU 2171  CA  ALA A1089    18489  21308  12230    213   4543    618       C  
ATOM   2172  C   ALA A1089     158.209  22.629 572.074  1.00136.31           C  
ANISOU 2172  C   ALA A1089    18703  21302  11784     69   4384    696       C  
ATOM   2173  O   ALA A1089     158.797  23.553 572.646  1.00134.31           O  
ANISOU 2173  O   ALA A1089    18681  21071  11280     60   4359    489       O  
ATOM   2174  CB  ALA A1089     155.816  23.323 571.859  1.00136.48           C  
ANISOU 2174  CB  ALA A1089    18382  21346  12127    219   4876    475       C  
ATOM   2175  N   ALA A1090     158.519  21.350 572.278  1.00126.21           N  
ANISOU 2175  N   ALA A1090    17428  20049  10476    -39   4267    988       N  
ATOM   2176  CA  ALA A1090     159.644  20.962 573.121  1.00106.99           C  
ANISOU 2176  CA  ALA A1090    15256  17670   7726   -147   4073   1094       C  
ATOM   2177  C   ALA A1090     160.995  21.131 572.432  1.00109.57           C  
ANISOU 2177  C   ALA A1090    15621  17937   8072   -117   3740   1103       C  
ATOM   2178  O   ALA A1090     162.027  20.847 573.052  1.00118.69           O  
ANISOU 2178  O   ALA A1090    16967  19142   8987   -190   3537   1185       O  
ATOM   2179  CB  ALA A1090     159.480  19.511 573.580  1.00 93.58           C  
ANISOU 2179  CB  ALA A1090    13548  16005   6003   -259   4062   1407       C  
ATOM   2180  N   ALA A1091     161.016  21.590 571.178  1.00 86.44           N  
ANISOU 2180  N   ALA A1091    12514  14907   5424     -8   3675   1020       N  
ATOM   2181  CA  ALA A1091     162.272  21.689 570.440  1.00118.64           C  
ANISOU 2181  CA  ALA A1091    16604  18932   9543      8   3366   1038       C  
ATOM   2182  C   ALA A1091     163.160  22.796 570.997  1.00144.51           C  
ANISOU 2182  C   ALA A1091    20126  22245  12537    -13   3271    797       C  
ATOM   2183  O   ALA A1091     164.364  22.597 571.193  1.00115.89           O  
ANISOU 2183  O   ALA A1091    16614  18657   8763    -81   3006    860       O  
ATOM   2184  CB  ALA A1091     161.990  21.917 568.955  1.00104.85           C  
ANISOU 2184  CB  ALA A1091    14621  17056   8162    135   3348   1009       C  
ATOM   2185  N   GLU A1092     162.584  23.975 571.248  1.00170.34           N  
ANISOU 2185  N   GLU A1092    23478  25499  15744     44   3479    514       N  
ATOM   2186  CA  GLU A1092     163.369  25.073 571.806  1.00170.88           C  
ANISOU 2186  CA  GLU A1092    23806  25575  15547     19   3405    268       C  
ATOM   2187  C   GLU A1092     163.916  24.726 573.184  1.00172.28           C  
ANISOU 2187  C   GLU A1092    24230  25870  15360    -83   3342    345       C  
ATOM   2188  O   GLU A1092     165.018  25.158 573.541  1.00175.28           O  
ANISOU 2188  O   GLU A1092    24781  26282  15536   -120   3125    265       O  
ATOM   2189  CB  GLU A1092     162.526  26.347 571.873  1.00176.47           C  
ANISOU 2189  CB  GLU A1092    24565  26219  16268    104   3669    -47       C  
ATOM   2190  CG  GLU A1092     162.801  27.340 570.754  1.00180.81           C  
ANISOU 2190  CG  GLU A1092    25055  26633  17011    203   3592   -253       C  
ATOM   2191  CD  GLU A1092     164.228  27.855 570.771  1.00183.08           C  
ANISOU 2191  CD  GLU A1092    25541  26899  17123    141   3313   -345       C  
ATOM   2192  OE1 GLU A1092     164.867  27.880 569.698  1.00180.53           O  
ANISOU 2192  OE1 GLU A1092    25103  26512  16979    154   3114   -327       O  
ATOM   2193  OE2 GLU A1092     164.712  28.228 571.860  1.00184.86           O  
ANISOU 2193  OE2 GLU A1092    26009  27191  17037    109   3277   -426       O  
ATOM   2194  N   GLN A1093     163.165  23.952 573.970  1.00158.73           N  
ANISOU 2194  N   GLN A1093    22524  24226  13561   -125   3519    500       N  
ATOM   2195  CA  GLN A1093     163.681  23.488 575.253  1.00145.59           C  
ANISOU 2195  CA  GLN A1093    21086  22675  11555   -201   3446    613       C  
ATOM   2196  C   GLN A1093     164.807  22.481 575.057  1.00133.32           C  
ANISOU 2196  C   GLN A1093    19493  21157  10007   -271   3104    866       C  
ATOM   2197  O   GLN A1093     165.807  22.506 575.785  1.00140.63           O  
ANISOU 2197  O   GLN A1093    20597  22164  10671   -318   2897    878       O  
ATOM   2198  CB  GLN A1093     162.553  22.884 576.086  1.00148.13           C  
ANISOU 2198  CB  GLN A1093    21430  23054  11800   -233   3736    722       C  
ATOM   2199  CG  GLN A1093     162.998  22.387 577.448  1.00151.63           C  
ANISOU 2199  CG  GLN A1093    22118  23616  11877   -293   3683    850       C  
ATOM   2200  CD  GLN A1093     162.605  20.947 577.694  1.00152.95           C  
ANISOU 2200  CD  GLN A1093    22212  23814  12088   -379   3714   1166       C  
ATOM   2201  OE1 GLN A1093     161.624  20.456 577.137  1.00150.09           O  
ANISOU 2201  OE1 GLN A1093    21639  23405  11985   -391   3890   1246       O  
ATOM   2202  NE2 GLN A1093     163.376  20.258 578.527  1.00155.54           N  
ANISOU 2202  NE2 GLN A1093    22708  24223  12167   -435   3532   1347       N  
ATOM   2203  N   LEU A1094     164.662  21.585 574.075  1.00122.95           N  
ANISOU 2203  N   LEU A1094    17938  19782   8997   -266   3035   1070       N  
ATOM   2204  CA  LEU A1094     165.759  20.690 573.721  1.00117.05           C  
ANISOU 2204  CA  LEU A1094    17135  19038   8302   -304   2708   1294       C  
ATOM   2205  C   LEU A1094     167.001  21.467 573.302  1.00119.11           C  
ANISOU 2205  C   LEU A1094    17434  19296   8525   -302   2439   1139       C  
ATOM   2206  O   LEU A1094     168.126  20.991 573.494  1.00111.70           O  
ANISOU 2206  O   LEU A1094    16536  18409   7494   -350   2155   1262       O  
ATOM   2207  CB  LEU A1094     165.325  19.745 572.600  1.00110.41           C  
ANISOU 2207  CB  LEU A1094    16025  18100   7826   -269   2702   1504       C  
ATOM   2208  CG  LEU A1094     164.524  18.504 572.997  1.00107.82           C  
ANISOU 2208  CG  LEU A1094    15650  17771   7545   -312   2837   1761       C  
ATOM   2209  CD1 LEU A1094     163.716  17.993 571.816  1.00105.33           C  
ANISOU 2209  CD1 LEU A1094    15060  17342   7619   -259   2927   1861       C  
ATOM   2210  CD2 LEU A1094     165.463  17.424 573.503  1.00 89.16           C  
ANISOU 2210  CD2 LEU A1094    13382  15439   5057   -371   2588   2015       C  
ATOM   2211  N   LYS A1095     166.818  22.661 572.736  1.00125.24           N  
ANISOU 2211  N   LYS A1095    18198  20010   9379   -250   2523    868       N  
ATOM   2212  CA  LYS A1095     167.954  23.468 572.305  1.00132.25           C  
ANISOU 2212  CA  LYS A1095    19126  20882  10240   -269   2283    698       C  
ATOM   2213  C   LYS A1095     168.601  24.188 573.484  1.00147.98           C  
ANISOU 2213  C   LYS A1095    21381  22968  11877   -329   2211    532       C  
ATOM   2214  O   LYS A1095     169.830  24.175 573.630  1.00153.26           O  
ANISOU 2214  O   LYS A1095    22095  23696  12439   -398   1919    544       O  
ATOM   2215  CB  LYS A1095     167.507  24.470 571.238  1.00131.36           C  
ANISOU 2215  CB  LYS A1095    18917  20647  10348   -190   2400    471       C  
ATOM   2216  CG  LYS A1095     168.620  24.919 570.308  1.00134.70           C  
ANISOU 2216  CG  LYS A1095    19283  21019  10876   -217   2135    384       C  
ATOM   2217  CD  LYS A1095     169.257  23.727 569.613  1.00133.90           C  
ANISOU 2217  CD  LYS A1095    18995  20928  10955   -230   1905    671       C  
ATOM   2218  CE  LYS A1095     170.362  24.154 568.663  1.00127.38           C  
ANISOU 2218  CE  LYS A1095    18100  20058  10240   -263   1654    587       C  
ATOM   2219  NZ  LYS A1095     171.105  22.978 568.129  1.00122.61           N  
ANISOU 2219  NZ  LYS A1095    17333  19470   9782   -269   1417    866       N  
ATOM   2220  N   THR A1096     167.790  24.821 574.338  1.00161.14           N  
ANISOU 2220  N   THR A1096    23209  24655  13363   -293   2470    375       N  
ATOM   2221  CA  THR A1096     168.339  25.488 575.514  1.00166.17           C  
ANISOU 2221  CA  THR A1096    24093  25392  13652   -329   2410    222       C  
ATOM   2222  C   THR A1096     168.957  24.498 576.493  1.00169.71           C  
ANISOU 2222  C   THR A1096    24631  25983  13870   -405   2239    455       C  
ATOM   2223  O   THR A1096     169.789  24.897 577.315  1.00174.37           O  
ANISOU 2223  O   THR A1096    25385  26674  14192   -458   2073    367       O  
ATOM   2224  CB  THR A1096     167.262  26.325 576.213  1.00174.34           C  
ANISOU 2224  CB  THR A1096    25264  26427  14552   -237   2742     18       C  
ATOM   2225  OG1 THR A1096     167.879  27.201 577.164  1.00179.70           O  
ANISOU 2225  OG1 THR A1096    26156  27198  14924   -260   2654   -185       O  
ATOM   2226  CG2 THR A1096     166.266  25.436 576.938  1.00178.64           C  
ANISOU 2226  CG2 THR A1096    25822  27030  15023   -221   2982    215       C  
ATOM   2227  N   THR A1097     168.570  23.221 576.426  1.00154.17           N  
ANISOU 2227  N   THR A1097    22556  24018  12004   -412   2271    749       N  
ATOM   2228  CA  THR A1097     169.303  22.188 577.146  1.00136.28           C  
ANISOU 2228  CA  THR A1097    20351  21858   9571   -473   2058    997       C  
ATOM   2229  C   THR A1097     170.531  21.738 576.364  1.00135.81           C  
ANISOU 2229  C   THR A1097    20146  21788   9669   -504   1703   1113       C  
ATOM   2230  O   THR A1097     171.545  21.361 576.964  1.00131.02           O  
ANISOU 2230  O   THR A1097    19613  21282   8888   -551   1447   1210       O  
ATOM   2231  CB  THR A1097     168.391  20.992 577.433  1.00126.62           C  
ANISOU 2231  CB  THR A1097    19090  20626   8394   -470   2238   1265       C  
ATOM   2232  OG1 THR A1097     167.184  21.449 578.057  1.00134.78           O  
ANISOU 2232  OG1 THR A1097    20227  21668   9316   -439   2594   1145       O  
ATOM   2233  CG2 THR A1097     169.080  19.997 578.357  1.00120.90           C  
ANISOU 2233  CG2 THR A1097    18481  20004   7450   -520   2044   1507       C  
ATOM   2234  N   ARG A1098     170.459  21.787 575.031  1.00141.46           N  
ANISOU 2234  N   ARG A1098    20650  22387  10712   -468   1686   1100       N  
ATOM   2235  CA  ARG A1098     171.600  21.422 574.199  1.00145.21           C  
ANISOU 2235  CA  ARG A1098    20971  22845  11355   -483   1370   1195       C  
ATOM   2236  C   ARG A1098     172.778  22.364 574.412  1.00152.51           C  
ANISOU 2236  C   ARG A1098    21986  23838  12123   -548   1138    983       C  
ATOM   2237  O   ARG A1098     173.936  21.937 574.324  1.00153.50           O  
ANISOU 2237  O   ARG A1098    22049  24021  12254   -584    839   1088       O  
ATOM   2238  CB  ARG A1098     171.173  21.406 572.726  1.00143.35           C  
ANISOU 2238  CB  ARG A1098    20506  22471  11488   -422   1434   1198       C  
ATOM   2239  CG  ARG A1098     172.288  21.194 571.701  1.00144.47           C  
ANISOU 2239  CG  ARG A1098    20480  22582  11830   -425   1141   1256       C  
ATOM   2240  CD  ARG A1098     172.877  22.515 571.209  1.00148.77           C  
ANISOU 2240  CD  ARG A1098    21047  23105  12375   -465   1062    957       C  
ATOM   2241  NE  ARG A1098     172.005  23.645 571.517  1.00151.77           N  
ANISOU 2241  NE  ARG A1098    21566  23446  12654   -454   1326    690       N  
ATOM   2242  CZ  ARG A1098     172.371  24.920 571.428  1.00150.39           C  
ANISOU 2242  CZ  ARG A1098    21491  23240  12412   -497   1304    395       C  
ATOM   2243  NH1 ARG A1098     173.600  25.235 571.042  1.00152.51           N  
ANISOU 2243  NH1 ARG A1098    21724  23522  12699   -574   1031    327       N  
ATOM   2244  NH2 ARG A1098     171.510  25.882 571.730  1.00147.14           N  
ANISOU 2244  NH2 ARG A1098    21209  22771  11925   -460   1559    164       N  
ATOM   2245  N   ASN A1099     172.506  23.643 574.687  1.00162.70           N  
ANISOU 2245  N   ASN A1099    23416  25117  13287   -563   1273    682       N  
ATOM   2246  CA  ASN A1099     173.583  24.627 574.775  1.00169.27           C  
ANISOU 2246  CA  ASN A1099    24322  25985  14006   -641   1063    455       C  
ATOM   2247  C   ASN A1099     174.559  24.286 575.896  1.00178.01           C  
ANISOU 2247  C   ASN A1099    25545  27259  14832   -712    825    536       C  
ATOM   2248  O   ASN A1099     175.777  24.457 575.744  1.00179.08           O  
ANISOU 2248  O   ASN A1099    25631  27448  14962   -784    536    500       O  
ATOM   2249  CB  ASN A1099     172.997  26.026 574.972  1.00172.86           C  
ANISOU 2249  CB  ASN A1099    24929  26377  14372   -631   1276    121       C  
ATOM   2250  CG  ASN A1099     173.909  27.121 574.452  1.00171.69           C  
ANISOU 2250  CG  ASN A1099    24789  26177  14268   -708   1101   -133       C  
ATOM   2251  OD1 ASN A1099     175.121  26.935 574.346  1.00170.18           O  
ANISOU 2251  OD1 ASN A1099    24537  26053  14071   -796    802    -86       O  
ATOM   2252  ND2 ASN A1099     173.329  28.270 574.122  1.00169.40           N  
ANISOU 2252  ND2 ASN A1099    24569  25759  14035   -675   1290   -405       N  
ATOM   2253  N   ALA A1100     174.043  23.792 577.026  1.00209.09           N  
ANISOU 2253  N   ALA A1100    29629  31281  18533   -693    943    651       N  
ATOM   2254  CA  ALA A1100     174.910  23.446 578.147  1.00195.90           C  
ANISOU 2254  CA  ALA A1100    28084  29775  16575   -749    725    736       C  
ATOM   2255  C   ALA A1100     175.866  22.316 577.789  1.00202.20           C  
ANISOU 2255  C   ALA A1100    28718  30610  17499   -751    428   1010       C  
ATOM   2256  O   ALA A1100     177.004  22.292 578.270  1.00174.29           O  
ANISOU 2256  O   ALA A1100    25206  27196  13820   -807    146   1020       O  
ATOM   2257  CB  ALA A1100     174.069  23.067 579.366  1.00104.91           C  
ANISOU 2257  CB  ALA A1100    16753  18325   4784   -719    936    825       C  
ATOM   2258  N   TYR A1101     175.429  21.375 576.949  1.00204.32           N  
ANISOU 2258  N   TYR A1101    28812  30777  18042   -684    483   1229       N  
ATOM   2259  CA  TYR A1101     176.307  20.284 576.542  1.00200.86           C  
ANISOU 2259  CA  TYR A1101    28211  30353  17755   -659    213   1486       C  
ATOM   2260  C   TYR A1101     177.290  20.737 575.468  1.00194.94           C  
ANISOU 2260  C   TYR A1101    27273  29573  17223   -683     -7   1379       C  
ATOM   2261  O   TYR A1101     178.490  20.453 575.556  1.00197.89           O  
ANISOU 2261  O   TYR A1101    27576  30035  17578   -706   -304   1447       O  
ATOM   2262  CB  TYR A1101     175.480  19.097 576.047  1.00201.87           C  
ANISOU 2262  CB  TYR A1101    28229  30368  18104   -578    354   1757       C  
ATOM   2263  CG  TYR A1101     176.314  17.991 575.436  1.00206.66           C  
ANISOU 2263  CG  TYR A1101    28652  30946  18924   -527     99   2009       C  
ATOM   2264  CD1 TYR A1101     176.562  17.957 574.070  1.00204.32           C  
ANISOU 2264  CD1 TYR A1101    28128  30543  18961   -488     32   2008       C  
ATOM   2265  CD2 TYR A1101     176.857  16.985 576.224  1.00213.07           C  
ANISOU 2265  CD2 TYR A1101    29524  31829  19604   -506    -72   2246       C  
ATOM   2266  CE1 TYR A1101     177.325  16.955 573.505  1.00206.46           C  
ANISOU 2266  CE1 TYR A1101    28232  30777  19436   -424   -188   2228       C  
ATOM   2267  CE2 TYR A1101     177.623  15.973 575.665  1.00214.65           C  
ANISOU 2267  CE2 TYR A1101    29559  31985  20014   -437   -297   2468       C  
ATOM   2268  CZ  TYR A1101     177.852  15.966 574.303  1.00212.74           C  
ANISOU 2268  CZ  TYR A1101    29087  31635  20111   -394   -350   2454       C  
ATOM   2269  OH  TYR A1101     178.608  14.970 573.729  1.00215.70           O  
ANISOU 2269  OH  TYR A1101    29298  31956  20704   -311   -560   2664       O  
ATOM   2270  N   ILE A1102     176.797  21.440 574.444  1.00178.09           N  
ANISOU 2270  N   ILE A1102    25051  27316  15298   -676    138   1212       N  
ATOM   2271  CA  ILE A1102     177.666  21.894 573.365  1.00157.52           C  
ANISOU 2271  CA  ILE A1102    22276  24672  12903   -706    -45   1106       C  
ATOM   2272  C   ILE A1102     178.690  22.900 573.868  1.00162.57           C  
ANISOU 2272  C   ILE A1102    23005  25414  13350   -822   -233    872       C  
ATOM   2273  O   ILE A1102     179.706  23.133 573.204  1.00159.12           O  
ANISOU 2273  O   ILE A1102    22426  24988  13045   -871   -451    817       O  
ATOM   2274  CB  ILE A1102     176.830  22.483 572.207  1.00130.83           C  
ANISOU 2274  CB  ILE A1102    18813  21133   9765   -673    170    969       C  
ATOM   2275  CG1 ILE A1102     177.643  22.495 570.910  1.00123.12           C  
ANISOU 2275  CG1 ILE A1102    17620  20097   9063   -678    -16    967       C  
ATOM   2276  CG2 ILE A1102     176.358  23.886 572.543  1.00120.77           C  
ANISOU 2276  CG2 ILE A1102    17718  19829   8339   -727    348    641       C  
ATOM   2277  CD1 ILE A1102     176.903  23.091 569.732  1.00124.07           C  
ANISOU 2277  CD1 ILE A1102    17664  20063   9412   -645    172    833       C  
ATOM   2278  N   GLN A1103     178.449  23.505 575.034  1.00159.10           N  
ANISOU 2278  N   GLN A1103    22794  25052  12603   -871   -150    730       N  
ATOM   2279  CA  GLN A1103     179.457  24.370 575.636  1.00158.05           C  
ANISOU 2279  CA  GLN A1103    22754  25028  12272   -988   -346    526       C  
ATOM   2280  C   GLN A1103     180.720  23.583 575.965  1.00152.89           C  
ANISOU 2280  C   GLN A1103    21997  24521  11574  -1009   -683    713       C  
ATOM   2281  O   GLN A1103     181.837  24.048 575.711  1.00149.28           O  
ANISOU 2281  O   GLN A1103    21447  24119  11153  -1097   -917    602       O  
ATOM   2282  CB  GLN A1103     178.896  25.033 576.894  1.00165.33           C  
ANISOU 2282  CB  GLN A1103    23948  26009  12861  -1017   -185    366       C  
ATOM   2283  CG  GLN A1103     179.548  26.359 577.244  1.00168.70           C  
ANISOU 2283  CG  GLN A1103    24492  26471  13137  -1142   -276     48       C  
ATOM   2284  CD  GLN A1103     178.972  27.514 576.448  1.00164.20           C  
ANISOU 2284  CD  GLN A1103    23945  25723  12721  -1152    -78   -227       C  
ATOM   2285  OE1 GLN A1103     177.765  27.581 576.216  1.00159.80           O  
ANISOU 2285  OE1 GLN A1103    23430  25054  12234  -1057    214   -243       O  
ATOM   2286  NE2 GLN A1103     179.835  28.430 576.023  1.00164.08           N  
ANISOU 2286  NE2 GLN A1103    23900  25676  12767  -1269   -233   -442       N  
ATOM   2287  N   LYS A1104     180.560  22.384 576.524  1.00158.66           N  
ANISOU 2287  N   LYS A1104    22738  25309  12237   -927   -708    999       N  
ATOM   2288  CA  LYS A1104     181.688  21.531 576.868  1.00145.32           C  
ANISOU 2288  CA  LYS A1104    20955  23746  10514   -915  -1017   1202       C  
ATOM   2289  C   LYS A1104     182.059  20.555 575.760  1.00145.51           C  
ANISOU 2289  C   LYS A1104    20717  23693  10878   -823  -1133   1423       C  
ATOM   2290  O   LYS A1104     183.072  19.858 575.886  1.00132.43           O  
ANISOU 2290  O   LYS A1104    18948  22125   9245   -793  -1398   1584       O  
ATOM   2291  CB  LYS A1104     181.389  20.754 578.156  1.00130.15           C  
ANISOU 2291  CB  LYS A1104    19215  21920   8315   -872   -998   1393       C  
ATOM   2292  CG  LYS A1104     181.143  21.639 579.368  1.00123.35           C  
ANISOU 2292  CG  LYS A1104    18619  21161   7086   -954   -911   1189       C  
ATOM   2293  CD  LYS A1104     181.051  20.824 580.646  1.00124.26           C  
ANISOU 2293  CD  LYS A1104    18908  21393   6911   -917   -940   1393       C  
ATOM   2294  CE  LYS A1104     180.920  21.729 581.859  1.00130.47           C  
ANISOU 2294  CE  LYS A1104    19955  22298   7319   -998   -877   1181       C  
ATOM   2295  NZ  LYS A1104     180.918  20.957 583.132  1.00134.15           N  
ANISOU 2295  NZ  LYS A1104    20599  22894   7477   -967   -925   1379       N  
ATOM   2296  N   TYR A1105     181.267  20.483 574.687  1.00157.49           N  
ANISOU 2296  N   TYR A1105    22134  25047  12659   -768   -941   1435       N  
ATOM   2297  CA  TYR A1105     181.625  19.626 573.561  1.00163.27           C  
ANISOU 2297  CA  TYR A1105    22617  25694  13722   -679  -1044   1623       C  
ATOM   2298  C   TYR A1105     182.892  20.120 572.872  1.00168.64           C  
ANISOU 2298  C   TYR A1105    23116  26423  14537   -738  -1290   1501       C  
ATOM   2299  O   TYR A1105     183.732  19.315 572.452  1.00172.76           O  
ANISOU 2299  O   TYR A1105    23449  26964  15228   -670  -1496   1674       O  
ATOM   2300  CB  TYR A1105     180.462  19.551 572.572  1.00162.49           C  
ANISOU 2300  CB  TYR A1105    22461  25417  13860   -618   -779   1637       C  
ATOM   2301  CG  TYR A1105     180.844  19.037 571.202  1.00156.34           C  
ANISOU 2301  CG  TYR A1105    21429  24536  13437   -547   -869   1742       C  
ATOM   2302  CD1 TYR A1105     181.069  17.684 570.983  1.00154.88           C  
ANISOU 2302  CD1 TYR A1105    21124  24309  13415   -432   -969   2037       C  
ATOM   2303  CD2 TYR A1105     180.968  19.905 570.125  1.00158.59           C  
ANISOU 2303  CD2 TYR A1105    21609  24753  13894   -592   -848   1542       C  
ATOM   2304  CE1 TYR A1105     181.415  17.212 569.731  1.00158.21           C  
ANISOU 2304  CE1 TYR A1105    21322  24626  14163   -357  -1042   2125       C  
ATOM   2305  CE2 TYR A1105     181.313  19.442 568.871  1.00161.18           C  
ANISOU 2305  CE2 TYR A1105    21714  24991  14536   -525   -924   1636       C  
ATOM   2306  CZ  TYR A1105     181.535  18.096 568.679  1.00158.47           C  
ANISOU 2306  CZ  TYR A1105    21249  24609  14351   -404  -1019   1925       C  
ATOM   2307  OH  TYR A1105     181.878  17.634 567.430  1.00149.78           O  
ANISOU 2307  OH  TYR A1105    19936  23407  13566   -328  -1086   2010       O  
ATOM   2308  N   LEU A1106     183.047  21.435 572.748  1.00174.06           N  
ANISOU 2308  N   LEU A1106    23856  27119  15159   -862  -1264   1200       N  
ATOM   2309  CA  LEU A1106     184.255  22.021 572.178  1.00166.18           C  
ANISOU 2309  CA  LEU A1106    22703  26172  14268   -952  -1485   1057       C  
ATOM   2310  C   LEU A1106     184.839  23.077 573.110  1.00163.60           C  
ANISOU 2310  C   LEU A1106    22525  25970  13666  -1105  -1583    816       C  
ATOM   2311  O   LEU A1106     185.771  22.804 573.867  1.00157.87           O  
ANISOU 2311  O   LEU A1106    21782  25404  12797  -1133  -1815    879       O  
ATOM   2312  CB  LEU A1106     183.965  22.632 570.805  1.00155.78           C  
ANISOU 2312  CB  LEU A1106    21276  24700  13213   -972  -1367    913       C  
ATOM   2313  CG  LEU A1106     184.015  21.681 569.609  1.00148.44           C  
ANISOU 2313  CG  LEU A1106    20110  23677  12612   -849  -1395   1122       C  
ATOM   2314  CD1 LEU A1106     183.647  22.410 568.326  1.00138.68           C  
ANISOU 2314  CD1 LEU A1106    18806  22294  11592   -881  -1263    956       C  
ATOM   2315  CD2 LEU A1106     185.391  21.045 569.491  1.00151.26           C  
ANISOU 2315  CD2 LEU A1106    20259  24144  13067   -827  -1695   1252       C  
ATOM   2316  N   LYS A 383     179.958  15.771 554.120  1.00 72.40           N  
ANISOU 2316  N   LYS A 383     8916  11599   6993    246   -539   1946       N  
ATOM   2317  CA  LYS A 383     179.876  17.134 554.632  1.00 77.53           C  
ANISOU 2317  CA  LYS A 383     9670  12342   7445    135   -499   1730       C  
ATOM   2318  C   LYS A 383     179.203  18.047 553.609  1.00 85.44           C  
ANISOU 2318  C   LYS A 383    10698  13150   8615    104   -365   1539       C  
ATOM   2319  O   LYS A 383     179.193  17.753 552.414  1.00 88.30           O  
ANISOU 2319  O   LYS A 383    10974  13343   9233    146   -356   1545       O  
ATOM   2320  CB  LYS A 383     181.271  17.656 554.988  1.00 76.54           C  
ANISOU 2320  CB  LYS A 383     9501  12404   7177     56   -685   1639       C  
ATOM   2321  CG  LYS A 383     181.273  18.885 555.885  1.00 68.64           C  
ANISOU 2321  CG  LYS A 383     8637  11543   5899    -70   -669   1450       C  
ATOM   2322  CD  LYS A 383     182.686  19.286 556.266  1.00 67.18           C  
ANISOU 2322  CD  LYS A 383     8393  11560   5572   -164   -873   1375       C  
ATOM   2323  CE  LYS A 383     182.693  20.544 557.117  1.00 74.95           C  
ANISOU 2323  CE  LYS A 383     9532  12666   6281   -308   -857   1165       C  
ATOM   2324  NZ  LYS A 383     184.078  20.974 557.454  1.00 79.66           N  
ANISOU 2324  NZ  LYS A 383    10059  13465   6742   -425  -1065   1079       N  
ATOM   2325  N   LYS A 384     178.637  19.156 554.090  1.00 93.26           N  
ANISOU 2325  N   LYS A 384    11818  14165   9453     36   -262   1369       N  
ATOM   2326  CA  LYS A 384     177.915  20.069 553.209  1.00 94.14           C  
ANISOU 2326  CA  LYS A 384    11972  14089   9709     24   -133   1197       C  
ATOM   2327  C   LYS A 384     178.854  20.763 552.228  1.00 90.48           C  
ANISOU 2327  C   LYS A 384    11462  13555   9362    -42   -223   1046       C  
ATOM   2328  O   LYS A 384     178.493  20.983 551.066  1.00 89.54           O  
ANISOU 2328  O   LYS A 384    11318  13244   9458    -20   -164    989       O  
ATOM   2329  CB  LYS A 384     177.146  21.094 554.046  1.00107.08           C  
ANISOU 2329  CB  LYS A 384    13768  15771  11145    -17     -1   1049       C  
ATOM   2330  CG  LYS A 384     176.568  22.263 553.260  1.00114.14           C  
ANISOU 2330  CG  LYS A 384    14731  16487  12152    -30    110    844       C  
ATOM   2331  CD  LYS A 384     177.391  23.527 553.471  1.00119.10           C  
ANISOU 2331  CD  LYS A 384    15460  17161  12632   -153     49    622       C  
ATOM   2332  CE  LYS A 384     176.847  24.689 552.658  1.00119.22           C  
ANISOU 2332  CE  LYS A 384    15561  16971  12764   -158    155    430       C  
ATOM   2333  NZ  LYS A 384     177.671  25.916 552.835  1.00120.09           N  
ANISOU 2333  NZ  LYS A 384    15787  17103  12738   -296     98    214       N  
ATOM   2334  N   VAL A 385     180.062  21.113 552.676  1.00 90.85           N  
ANISOU 2334  N   VAL A 385    11494  13763   9264   -134   -367    982       N  
ATOM   2335  CA  VAL A 385     181.004  21.822 551.811  1.00 77.26           C  
ANISOU 2335  CA  VAL A 385     9725  11993   7636   -223   -444    833       C  
ATOM   2336  C   VAL A 385     181.397  20.949 550.625  1.00 74.82           C  
ANISOU 2336  C   VAL A 385     9258  11576   7593   -152   -490    941       C  
ATOM   2337  O   VAL A 385     181.354  21.383 549.466  1.00 86.72           O  
ANISOU 2337  O   VAL A 385    10756  12915   9278   -170   -445    846       O  
ATOM   2338  CB  VAL A 385     182.236  22.271 552.616  1.00 72.23           C  
ANISOU 2338  CB  VAL A 385     9079  11582   6785   -346   -599    756       C  
ATOM   2339  CG1 VAL A 385     183.188  23.063 551.734  1.00 72.94           C  
ANISOU 2339  CG1 VAL A 385     9117  11626   6970   -464   -661    593       C  
ATOM   2340  CG2 VAL A 385     181.809  23.091 553.824  1.00 72.84           C  
ANISOU 2340  CG2 VAL A 385     9333  11763   6579   -419   -547    642       C  
ATOM   2341  N   THR A 386     181.787  19.701 550.901  1.00 68.60           N  
ANISOU 2341  N   THR A 386     8359  10878   6830    -65   -579   1141       N  
ATOM   2342  CA  THR A 386     182.125  18.772 549.826  1.00 61.85           C  
ANISOU 2342  CA  THR A 386     7365   9911   6224     19   -612   1247       C  
ATOM   2343  C   THR A 386     180.936  18.551 548.899  1.00 55.83           C  
ANISOU 2343  C   THR A 386     6641   8912   5661     85   -466   1267       C  
ATOM   2344  O   THR A 386     181.103  18.395 547.682  1.00 50.06           O  
ANISOU 2344  O   THR A 386     5847   8037   5138    104   -458   1243       O  
ATOM   2345  CB  THR A 386     182.604  17.445 550.418  1.00 52.44           C  
ANISOU 2345  CB  THR A 386     6076   8838   5010    120   -719   1471       C  
ATOM   2346  OG1 THR A 386     183.561  17.701 551.454  1.00 53.59           O  
ANISOU 2346  OG1 THR A 386     6199   9230   4932     60   -861   1460       O  
ATOM   2347  CG2 THR A 386     183.253  16.584 549.348  1.00 50.22           C  
ANISOU 2347  CG2 THR A 386     5646   8465   4972    201   -772   1549       C  
ATOM   2348  N   ARG A 387     179.723  18.547 549.459  1.00 49.12           N  
ANISOU 2348  N   ARG A 387     5890   8030   4745    117   -351   1305       N  
ATOM   2349  CA  ARG A 387     178.519  18.418 548.646  1.00 49.65           C  
ANISOU 2349  CA  ARG A 387     5980   7893   4990    171   -218   1315       C  
ATOM   2350  C   ARG A 387     178.396  19.578 547.666  1.00 44.21           C  
ANISOU 2350  C   ARG A 387     5341   7067   4390    113   -169   1118       C  
ATOM   2351  O   ARG A 387     178.148  19.379 546.469  1.00 41.93           O  
ANISOU 2351  O   ARG A 387     5015   6610   4308    144   -143   1116       O  
ATOM   2352  CB  ARG A 387     177.290  18.346 549.554  1.00 64.48           C  
ANISOU 2352  CB  ARG A 387     7942   9801   6758    201    -97   1374       C  
ATOM   2353  CG  ARG A 387     176.124  17.601 548.948  1.00 86.70           C  
ANISOU 2353  CG  ARG A 387    10725  12457   9762    275      7   1480       C  
ATOM   2354  CD  ARG A 387     176.531  16.178 548.647  1.00 98.61           C  
ANISOU 2354  CD  ARG A 387    12138  13932  11397    335    -69   1673       C  
ATOM   2355  NE  ARG A 387     175.890  15.669 547.442  1.00105.68           N  
ANISOU 2355  NE  ARG A 387    12987  14626  12541    375    -19   1703       N  
ATOM   2356  CZ  ARG A 387     176.375  14.670 546.717  1.00 99.87           C  
ANISOU 2356  CZ  ARG A 387    12177  13802  11968    419    -85   1802       C  
ATOM   2357  NH1 ARG A 387     177.508  14.084 547.075  1.00 86.80           N  
ANISOU 2357  NH1 ARG A 387    10472  12242  10266    446   -201   1886       N  
ATOM   2358  NH2 ARG A 387     175.734  14.265 545.632  1.00103.59           N  
ANISOU 2358  NH2 ARG A 387    12622  14091  12647    440    -37   1812       N  
ATOM   2359  N   THR A 388     178.568  20.805 548.164  1.00 45.86           N  
ANISOU 2359  N   THR A 388     5650   7338   4436     26   -157    950       N  
ATOM   2360  CA  THR A 388     178.518  21.983 547.304  1.00 50.54           C  
ANISOU 2360  CA  THR A 388     6315   7791   5095    -35   -114    764       C  
ATOM   2361  C   THR A 388     179.579  21.912 546.212  1.00 61.09           C  
ANISOU 2361  C   THR A 388     7565   9077   6570    -82   -201    735       C  
ATOM   2362  O   THR A 388     179.298  22.172 545.033  1.00 53.47           O  
ANISOU 2362  O   THR A 388     6613   7935   5768    -76   -158    684       O  
ATOM   2363  CB  THR A 388     178.696  23.246 548.148  1.00 50.41           C  
ANISOU 2363  CB  THR A 388     6434   7857   4863   -133   -100    592       C  
ATOM   2364  OG1 THR A 388     177.538  23.445 548.969  1.00 59.34           O  
ANISOU 2364  OG1 THR A 388     7660   8999   5889    -78     20    591       O  
ATOM   2365  CG2 THR A 388     178.909  24.460 547.261  1.00 45.24           C  
ANISOU 2365  CG2 THR A 388     5864   7055   4270   -215    -78    405       C  
ATOM   2366  N   ILE A 389     180.810  21.552 546.590  1.00 55.03           N  
ANISOU 2366  N   ILE A 389     6702   8472   5735   -126   -325    768       N  
ATOM   2367  CA  ILE A 389     181.895  21.463 545.616  1.00 43.34           C  
ANISOU 2367  CA  ILE A 389     5116   6971   4380   -171   -398    737       C  
ATOM   2368  C   ILE A 389     181.543  20.469 544.517  1.00 41.99           C  
ANISOU 2368  C   ILE A 389     4868   6646   4438    -66   -366    849       C  
ATOM   2369  O   ILE A 389     181.705  20.754 543.323  1.00 54.79           O  
ANISOU 2369  O   ILE A 389     6487   8133   6198    -95   -341    777       O  
ATOM   2370  CB  ILE A 389     183.215  21.092 546.316  1.00 53.66           C  
ANISOU 2370  CB  ILE A 389     6300   8507   5582   -210   -541    777       C  
ATOM   2371  CG1 ILE A 389     183.656  22.226 547.244  1.00 60.91           C  
ANISOU 2371  CG1 ILE A 389     7303   9568   6272   -351   -582    629       C  
ATOM   2372  CG2 ILE A 389     184.296  20.780 545.292  1.00 46.33           C  
ANISOU 2372  CG2 ILE A 389     5225   7568   4810   -227   -601    770       C  
ATOM   2373  CD1 ILE A 389     184.971  21.972 547.937  1.00 50.83           C  
ANISOU 2373  CD1 ILE A 389     5895   8537   4880   -407   -742    655       C  
ATOM   2374  N   LEU A 390     181.040  19.291 544.900  1.00 41.06           N  
ANISOU 2374  N   LEU A 390     4703   6539   4357     49   -364   1026       N  
ATOM   2375  CA  LEU A 390     180.633  18.311 543.897  1.00 38.60           C  
ANISOU 2375  CA  LEU A 390     4338   6070   4259    140   -331   1127       C  
ATOM   2376  C   LEU A 390     179.530  18.861 543.003  1.00 42.86           C  
ANISOU 2376  C   LEU A 390     4969   6413   4902    136   -226   1050       C  
ATOM   2377  O   LEU A 390     179.518  18.604 541.794  1.00 45.63           O  
ANISOU 2377  O   LEU A 390     5296   6621   5418    151   -212   1041       O  
ATOM   2378  CB  LEU A 390     180.171  17.016 544.564  1.00 34.98           C  
ANISOU 2378  CB  LEU A 390     3841   5641   3808    246   -337   1328       C  
ATOM   2379  CG  LEU A 390     179.696  15.962 543.558  1.00 33.84           C  
ANISOU 2379  CG  LEU A 390     3656   5318   3882    327   -302   1427       C  
ATOM   2380  CD1 LEU A 390     180.848  15.501 542.675  1.00 33.60           C  
ANISOU 2380  CD1 LEU A 390     3524   5266   3977    345   -369   1420       C  
ATOM   2381  CD2 LEU A 390     179.027  14.783 544.242  1.00 41.54           C  
ANISOU 2381  CD2 LEU A 390     4628   6294   4863    410   -284   1622       C  
ATOM   2382  N   ALA A 391     178.592  19.618 543.577  1.00 44.77           N  
ANISOU 2382  N   ALA A 391     5317   6649   5045    123   -152    993       N  
ATOM   2383  CA  ALA A 391     177.519  20.195 542.773  1.00 34.52           C  
ANISOU 2383  CA  ALA A 391     4096   5174   3845    137    -62    924       C  
ATOM   2384  C   ALA A 391     178.076  21.132 541.707  1.00 36.53           C  
ANISOU 2384  C   ALA A 391     4398   5328   4152     60    -74    777       C  
ATOM   2385  O   ALA A 391     177.721  21.031 540.525  1.00 43.95           O  
ANISOU 2385  O   ALA A 391     5344   6112   5243     80    -52    772       O  
ATOM   2386  CB  ALA A 391     176.525  20.929 543.672  1.00 47.05           C  
ANISOU 2386  CB  ALA A 391     5779   6790   5306    148     24    875       C  
ATOM   2387  N   ILE A 392     178.966  22.044 542.107  1.00 44.38           N  
ANISOU 2387  N   ILE A 392     5434   6411   5015    -41   -110    657       N  
ATOM   2388  CA  ILE A 392     179.525  22.998 541.152  1.00 47.48           C  
ANISOU 2388  CA  ILE A 392     5887   6708   5444   -138   -112    518       C  
ATOM   2389  C   ILE A 392     180.342  22.276 540.086  1.00 47.39           C  
ANISOU 2389  C   ILE A 392     5768   6665   5573   -144   -157    561       C  
ATOM   2390  O   ILE A 392     180.230  22.573 538.888  1.00 45.86           O  
ANISOU 2390  O   ILE A 392     5619   6319   5485   -164   -126    513       O  
ATOM   2391  CB  ILE A 392     180.363  24.060 541.889  1.00 49.02           C  
ANISOU 2391  CB  ILE A 392     6144   7016   5464   -268   -144    383       C  
ATOM   2392  CG1 ILE A 392     179.538  24.709 543.001  1.00 61.67           C  
ANISOU 2392  CG1 ILE A 392     7865   8651   6916   -252    -89    333       C  
ATOM   2393  CG2 ILE A 392     180.855  25.116 540.917  1.00 50.90           C  
ANISOU 2393  CG2 ILE A 392     6468   7135   5736   -385   -130    241       C  
ATOM   2394  CD1 ILE A 392     180.303  25.729 543.814  1.00 76.64           C  
ANISOU 2394  CD1 ILE A 392     9841  10657   8623   -388   -122    191       C  
ATOM   2395  N   LEU A 393     181.168  21.311 540.502  1.00 41.05           N  
ANISOU 2395  N   LEU A 393     4824   6003   4768   -118   -227    655       N  
ATOM   2396  CA  LEU A 393     181.995  20.580 539.546  1.00 39.77           C  
ANISOU 2396  CA  LEU A 393     4550   5819   4741   -106   -259    691       C  
ATOM   2397  C   LEU A 393     181.137  19.825 538.537  1.00 42.99           C  
ANISOU 2397  C   LEU A 393     4970   6048   5316    -16   -209    764       C  
ATOM   2398  O   LEU A 393     181.400  19.863 537.329  1.00 44.33           O  
ANISOU 2398  O   LEU A 393     5146   6109   5590    -42   -189    717       O  
ATOM   2399  CB  LEU A 393     182.930  19.620 540.282  1.00 39.17           C  
ANISOU 2399  CB  LEU A 393     4319   5925   4638    -60   -347    794       C  
ATOM   2400  CG  LEU A 393     183.984  20.254 541.193  1.00 50.13           C  
ANISOU 2400  CG  LEU A 393     5661   7521   5866   -160   -425    723       C  
ATOM   2401  CD1 LEU A 393     184.949  19.202 541.721  1.00 59.57           C  
ANISOU 2401  CD1 LEU A 393     6681   8888   7065    -90   -526    841       C  
ATOM   2402  CD2 LEU A 393     184.729  21.362 540.468  1.00 55.60           C  
ANISOU 2402  CD2 LEU A 393     6380   8193   6554   -313   -412    556       C  
ATOM   2403  N   LEU A 394     180.099  19.134 539.015  1.00 36.46           N  
ANISOU 2403  N   LEU A 394     4150   5192   4511     79   -187    877       N  
ATOM   2404  CA  LEU A 394     179.235  18.380 538.112  1.00 35.03           C  
ANISOU 2404  CA  LEU A 394     3976   4849   4486    150   -149    946       C  
ATOM   2405  C   LEU A 394     178.475  19.305 537.171  1.00 35.81           C  
ANISOU 2405  C   LEU A 394     4189   4792   4625    112    -98    845       C  
ATOM   2406  O   LEU A 394     178.252  18.961 536.003  1.00 35.03           O  
ANISOU 2406  O   LEU A 394     4101   4560   4650    125    -87    848       O  
ATOM   2407  CB  LEU A 394     178.267  17.508 538.910  1.00 28.89           C  
ANISOU 2407  CB  LEU A 394     3178   4084   3713    235   -131   1087       C  
ATOM   2408  CG  LEU A 394     178.888  16.301 539.614  1.00 32.18           C  
ANISOU 2408  CG  LEU A 394     3495   4604   4127    297   -185   1228       C  
ATOM   2409  CD1 LEU A 394     177.817  15.461 540.290  1.00 44.67           C  
ANISOU 2409  CD1 LEU A 394     5082   6170   5720    363   -150   1372       C  
ATOM   2410  CD2 LEU A 394     179.691  15.466 538.631  1.00 32.05           C  
ANISOU 2410  CD2 LEU A 394     3406   4519   4251    330   -216   1251       C  
ATOM   2411  N   ALA A 395     178.065  20.479 537.657  1.00 33.20           N  
ANISOU 2411  N   ALA A 395     3955   4472   4189     72    -68    757       N  
ATOM   2412  CA  ALA A 395     177.445  21.459 536.770  1.00 36.34           C  
ANISOU 2412  CA  ALA A 395     4471   4717   4618     46    -29    662       C  
ATOM   2413  C   ALA A 395     178.407  21.868 535.660  1.00 34.55           C  
ANISOU 2413  C   ALA A 395     4273   4429   4424    -42    -45    577       C  
ATOM   2414  O   ALA A 395     178.037  21.902 534.480  1.00 34.05           O  
ANISOU 2414  O   ALA A 395     4262   4221   4452    -38    -33    565       O  
ATOM   2415  CB  ALA A 395     176.988  22.679 537.569  1.00 28.09           C  
ANISOU 2415  CB  ALA A 395     3534   3691   3447     26      9    572       C  
ATOM   2416  N   PHE A 396     179.658  22.162 536.025  1.00 42.00           N  
ANISOU 2416  N   PHE A 396     5178   5491   5287   -129    -74    521       N  
ATOM   2417  CA  PHE A 396     180.658  22.558 535.036  1.00 37.42           C  
ANISOU 2417  CA  PHE A 396     4609   4877   4731   -230    -75    438       C  
ATOM   2418  C   PHE A 396     180.882  21.459 534.001  1.00 36.75           C  
ANISOU 2418  C   PHE A 396     4445   4736   4783   -182    -76    504       C  
ATOM   2419  O   PHE A 396     180.839  21.710 532.789  1.00 37.09           O  
ANISOU 2419  O   PHE A 396     4560   4650   4882   -219    -48    460       O  
ATOM   2420  CB  PHE A 396     181.963  22.914 535.751  1.00 35.24           C  
ANISOU 2420  CB  PHE A 396     4261   4775   4352   -332   -113    378       C  
ATOM   2421  CG  PHE A 396     183.134  23.107 534.831  1.00 32.15           C  
ANISOU 2421  CG  PHE A 396     3830   4392   3995   -440   -107    309       C  
ATOM   2422  CD1 PHE A 396     183.260  24.263 534.080  1.00 35.62           C  
ANISOU 2422  CD1 PHE A 396     4408   4720   4405   -563    -64    196       C  
ATOM   2423  CD2 PHE A 396     184.123  22.142 534.737  1.00 32.20           C  
ANISOU 2423  CD2 PHE A 396     3661   4516   4060   -415   -139    358       C  
ATOM   2424  CE1 PHE A 396     184.344  24.446 533.240  1.00 38.76           C  
ANISOU 2424  CE1 PHE A 396     4767   5135   4827   -678    -43    134       C  
ATOM   2425  CE2 PHE A 396     185.208  22.319 533.899  1.00 35.17           C  
ANISOU 2425  CE2 PHE A 396     3981   4914   4468   -514   -117    289       C  
ATOM   2426  CZ  PHE A 396     185.319  23.472 533.149  1.00 32.39           C  
ANISOU 2426  CZ  PHE A 396     3765   4461   4080   -654    -65    176       C  
ATOM   2427  N   ILE A 397     181.107  20.227 534.465  1.00 35.44           N  
ANISOU 2427  N   ILE A 397     4145   4657   4666    -97   -108    610       N  
ATOM   2428  CA  ILE A 397     181.429  19.129 533.557  1.00 37.64           C  
ANISOU 2428  CA  ILE A 397     4350   4879   5072    -45   -104    663       C  
ATOM   2429  C   ILE A 397     180.250  18.822 532.642  1.00 33.70           C  
ANISOU 2429  C   ILE A 397     3939   4199   4667      2    -77    693       C  
ATOM   2430  O   ILE A 397     180.404  18.720 531.419  1.00 35.77           O  
ANISOU 2430  O   ILE A 397     4240   4357   4994    -23    -54    654       O  
ATOM   2431  CB  ILE A 397     181.858  17.885 534.356  1.00 45.07           C  
ANISOU 2431  CB  ILE A 397     5147   5934   6044     51   -147    781       C  
ATOM   2432  CG1 ILE A 397     183.114  18.181 535.176  1.00 55.28           C  
ANISOU 2432  CG1 ILE A 397     6335   7426   7244      4   -194    750       C  
ATOM   2433  CG2 ILE A 397     182.090  16.706 533.422  1.00 40.44           C  
ANISOU 2433  CG2 ILE A 397     4505   5260   5600    121   -133    831       C  
ATOM   2434  CD1 ILE A 397     183.522  17.050 536.092  1.00 56.22           C  
ANISOU 2434  CD1 ILE A 397     6321   7667   7372    110   -254    879       C  
ATOM   2435  N   ILE A 398     179.056  18.670 533.219  1.00 35.89           N  
ANISOU 2435  N   ILE A 398     4243   4446   4946     66    -78    760       N  
ATOM   2436  CA  ILE A 398     177.892  18.298 532.420  1.00 36.39           C  
ANISOU 2436  CA  ILE A 398     4362   4359   5105    108    -66    796       C  
ATOM   2437  C   ILE A 398     177.516  19.410 531.447  1.00 37.27           C  
ANISOU 2437  C   ILE A 398     4606   4354   5200     49    -51    699       C  
ATOM   2438  O   ILE A 398     177.048  19.139 530.334  1.00 28.41           O  
ANISOU 2438  O   ILE A 398     3534   3108   4153     54    -54    700       O  
ATOM   2439  CB  ILE A 398     176.717  17.923 533.343  1.00 30.92           C  
ANISOU 2439  CB  ILE A 398     3645   3686   4418    179    -63    890       C  
ATOM   2440  CG1 ILE A 398     177.050  16.654 534.129  1.00 39.46           C  
ANISOU 2440  CG1 ILE A 398     4617   4850   5526    238    -79   1009       C  
ATOM   2441  CG2 ILE A 398     175.436  17.724 532.546  1.00 24.49           C  
ANISOU 2441  CG2 ILE A 398     2875   2733   3697    207    -58    914       C  
ATOM   2442  CD1 ILE A 398     175.939  16.192 535.045  1.00 53.08           C  
ANISOU 2442  CD1 ILE A 398     6319   6599   7251    292    -62   1114       C  
ATOM   2443  N   THR A 399     177.728  20.672 531.827  1.00 37.42           N  
ANISOU 2443  N   THR A 399     4699   4404   5115     -9    -39    615       N  
ATOM   2444  CA  THR A 399     177.368  21.762 530.929  1.00 33.09           C  
ANISOU 2444  CA  THR A 399     4298   3727   4549    -58    -26    535       C  
ATOM   2445  C   THR A 399     178.413  21.999 529.845  1.00 36.15           C  
ANISOU 2445  C   THR A 399     4730   4075   4932   -156    -13    466       C  
ATOM   2446  O   THR A 399     178.074  22.514 528.774  1.00 34.58           O  
ANISOU 2446  O   THR A 399     4653   3744   4741   -186     -8    431       O  
ATOM   2447  CB  THR A 399     177.143  23.051 531.719  1.00 37.27           C  
ANISOU 2447  CB  THR A 399     4916   4273   4972    -82     -9    467       C  
ATOM   2448  OG1 THR A 399     178.202  23.220 532.668  1.00 64.51           O  
ANISOU 2448  OG1 THR A 399     8307   7871   8331   -145     -9    431       O  
ATOM   2449  CG2 THR A 399     175.808  23.003 532.445  1.00 42.00           C  
ANISOU 2449  CG2 THR A 399     5504   4868   5584     24     -2    522       C  
ATOM   2450  N   TRP A 400     179.674  21.635 530.087  1.00 40.09           N  
ANISOU 2450  N   TRP A 400     5128   4690   5414   -204     -6    449       N  
ATOM   2451  CA  TRP A 400     180.743  21.929 529.140  1.00 40.49           C  
ANISOU 2451  CA  TRP A 400     5203   4727   5454   -310     26    375       C  
ATOM   2452  C   TRP A 400     181.225  20.718 528.350  1.00 31.85           C  
ANISOU 2452  C   TRP A 400     4021   3628   4454   -274     39    409       C  
ATOM   2453  O   TRP A 400     182.062  20.878 527.456  1.00 29.67           O  
ANISOU 2453  O   TRP A 400     3762   3338   4172   -355     83    346       O  
ATOM   2454  CB  TRP A 400     181.931  22.568 529.865  1.00 26.21           C  
ANISOU 2454  CB  TRP A 400     3339   3063   3558   -412     33    306       C  
ATOM   2455  CG  TRP A 400     181.704  23.990 530.271  1.00 32.57           C  
ANISOU 2455  CG  TRP A 400     4282   3833   4259   -495     40    229       C  
ATOM   2456  CD1 TRP A 400     180.536  24.546 530.704  1.00 26.40           C  
ANISOU 2456  CD1 TRP A 400     3609   2971   3451   -434     30    239       C  
ATOM   2457  CD2 TRP A 400     182.674  25.043 530.267  1.00 30.35           C  
ANISOU 2457  CD2 TRP A 400     4052   3588   3891   -655     64    124       C  
ATOM   2458  NE1 TRP A 400     180.720  25.880 530.978  1.00 27.68           N  
ANISOU 2458  NE1 TRP A 400     3901   3102   3515   -534     49    144       N  
ATOM   2459  CE2 TRP A 400     182.024  26.210 530.717  1.00 32.96           C  
ANISOU 2459  CE2 TRP A 400     4543   3837   4143   -682     67     73       C  
ATOM   2460  CE3 TRP A 400     184.029  25.113 529.928  1.00 28.33           C  
ANISOU 2460  CE3 TRP A 400     3715   3426   3621   -782     90     65       C  
ATOM   2461  CZ2 TRP A 400     182.684  27.430 530.838  1.00 46.52           C  
ANISOU 2461  CZ2 TRP A 400     6364   5547   5765   -842     91    -35       C  
ATOM   2462  CZ3 TRP A 400     184.681  26.325 530.050  1.00 29.34           C  
ANISOU 2462  CZ3 TRP A 400     3927   3566   3656   -952    113    -39       C  
ATOM   2463  CH2 TRP A 400     184.009  27.467 530.501  1.00 48.79           C  
ANISOU 2463  CH2 TRP A 400     6571   5929   6039   -986    111    -88       C  
ATOM   2464  N   ALA A 401     180.723  19.514 528.645  1.00 28.94           N  
ANISOU 2464  N   ALA A 401     3566   3261   4168   -159     14    503       N  
ATOM   2465  CA  ALA A 401     181.191  18.331 527.923  1.00 34.13           C  
ANISOU 2465  CA  ALA A 401     4155   3894   4919   -117     32    527       C  
ATOM   2466  C   ALA A 401     180.724  18.291 526.470  1.00 48.39           C  
ANISOU 2466  C   ALA A 401     6087   5542   6757   -144     54    493       C  
ATOM   2467  O   ALA A 401     181.550  17.985 525.589  1.00 63.59           O  
ANISOU 2467  O   ALA A 401     8005   7455   8701   -180    103    443       O  
ATOM   2468  CB  ALA A 401     180.780  17.065 528.681  1.00 29.90           C  
ANISOU 2468  CB  ALA A 401     3516   3384   4461      5     -1    642       C  
ATOM   2469  N   PRO A 402     179.448  18.561 526.141  1.00 43.16           N  
ANISOU 2469  N   PRO A 402     5534   4765   6099   -128     21    517       N  
ATOM   2470  CA  PRO A 402     179.022  18.412 524.735  1.00 43.12           C  
ANISOU 2470  CA  PRO A 402     5646   4621   6116   -153     24    491       C  
ATOM   2471  C   PRO A 402     179.821  19.244 523.747  1.00 45.69           C  
ANISOU 2471  C   PRO A 402     6077   4918   6365   -265     75    398       C  
ATOM   2472  O   PRO A 402     180.174  18.738 522.676  1.00 40.99           O  
ANISOU 2472  O   PRO A 402     5520   4268   5786   -290    111    365       O  
ATOM   2473  CB  PRO A 402     177.549  18.843 524.775  1.00 44.18           C  
ANISOU 2473  CB  PRO A 402     5862   4674   6253   -118    -36    532       C  
ATOM   2474  CG  PRO A 402     177.116  18.552 526.157  1.00 39.01           C  
ANISOU 2474  CG  PRO A 402     5094   4106   5624    -44    -55    602       C  
ATOM   2475  CD  PRO A 402     178.301  18.877 527.014  1.00 37.78           C  
ANISOU 2475  CD  PRO A 402     4862   4083   5410    -74    -22    572       C  
ATOM   2476  N   TYR A 403     180.116  20.507 524.066  1.00 46.76           N  
ANISOU 2476  N   TYR A 403     6271   5084   6412   -341     87    351       N  
ATOM   2477  CA  TYR A 403     180.897  21.331 523.146  1.00 31.81           C  
ANISOU 2477  CA  TYR A 403     4487   3159   4441   -468    146    269       C  
ATOM   2478  C   TYR A 403     182.271  20.722 522.892  1.00 29.37           C  
ANISOU 2478  C   TYR A 403     4060   2949   4152   -510    221    224       C  
ATOM   2479  O   TYR A 403     182.746  20.689 521.749  1.00 29.53           O  
ANISOU 2479  O   TYR A 403     4150   2922   4148   -578    283    174       O  
ATOM   2480  CB  TYR A 403     181.032  22.751 523.697  1.00 25.19           C  
ANISOU 2480  CB  TYR A 403     3729   2333   3511   -550    149    228       C  
ATOM   2481  CG  TYR A 403     181.868  23.673 522.834  1.00 26.52           C  
ANISOU 2481  CG  TYR A 403     4019   2464   3593   -705    217    149       C  
ATOM   2482  CD1 TYR A 403     181.287  24.423 521.820  1.00 32.13           C  
ANISOU 2482  CD1 TYR A 403     4943   3020   4245   -751    211    143       C  
ATOM   2483  CD2 TYR A 403     183.238  23.800 523.038  1.00 28.90           C  
ANISOU 2483  CD2 TYR A 403     4218   2893   3870   -810    284     88       C  
ATOM   2484  CE1 TYR A 403     182.045  25.268 521.031  1.00 34.24           C  
ANISOU 2484  CE1 TYR A 403     5339   3245   4424   -904    281     83       C  
ATOM   2485  CE2 TYR A 403     184.003  24.639 522.252  1.00 27.61           C  
ANISOU 2485  CE2 TYR A 403     4162   2701   3628   -971    359     18       C  
ATOM   2486  CZ  TYR A 403     183.402  25.372 521.253  1.00 37.07           C  
ANISOU 2486  CZ  TYR A 403     5593   3731   4762  -1022    363     18       C  
ATOM   2487  OH  TYR A 403     184.163  26.210 520.472  1.00 54.04           O  
ANISOU 2487  OH  TYR A 403     7866   5844   6823  -1194    445    -41       O  
ATOM   2488  N   ASN A 404     182.920  20.222 523.944  1.00 37.88           N  
ANISOU 2488  N   ASN A 404     4953   4169   5269   -464    218    244       N  
ATOM   2489  CA  ASN A 404     184.273  19.700 523.790  1.00 39.43           C  
ANISOU 2489  CA  ASN A 404     5009   4480   5494   -487    284    202       C  
ATOM   2490  C   ASN A 404     184.282  18.380 523.028  1.00 44.42           C  
ANISOU 2490  C   ASN A 404     5605   5055   6216   -397    314    220       C  
ATOM   2491  O   ASN A 404     185.209  18.117 522.251  1.00 55.17           O  
ANISOU 2491  O   ASN A 404     6933   6443   7586   -436    400    157       O  
ATOM   2492  CB  ASN A 404     184.933  19.553 525.159  1.00 27.02           C  
ANISOU 2492  CB  ASN A 404     3249   3083   3933   -452    251    227       C  
ATOM   2493  CG  ASN A 404     185.165  20.892 525.833  1.00 30.68           C  
ANISOU 2493  CG  ASN A 404     3752   3613   4294   -571    237    179       C  
ATOM   2494  OD1 ASN A 404     186.165  21.563 525.580  1.00 28.22           O  
ANISOU 2494  OD1 ASN A 404     3420   3371   3931   -704    290    100       O  
ATOM   2495  ND2 ASN A 404     184.234  21.291 526.691  1.00 37.31           N  
ANISOU 2495  ND2 ASN A 404     4649   4427   5100   -531    172    221       N  
ATOM   2496  N   VAL A 405     183.262  17.536 523.222  1.00 28.31           N  
ANISOU 2496  N   VAL A 405     3576   2935   4246   -284    254    297       N  
ATOM   2497  CA  VAL A 405     183.203  16.335 522.392  1.00 31.23           C  
ANISOU 2497  CA  VAL A 405     3952   3219   4695   -218    283    300       C  
ATOM   2498  C   VAL A 405     182.861  16.706 520.952  1.00 42.99           C  
ANISOU 2498  C   VAL A 405     5628   4580   6126   -303    317    237       C  
ATOM   2499  O   VAL A 405     183.260  16.005 520.012  1.00 61.06           O  
ANISOU 2499  O   VAL A 405     7940   6821   8439   -298    382    190       O  
ATOM   2500  CB  VAL A 405     182.222  15.296 522.972  1.00 30.43           C  
ANISOU 2500  CB  VAL A 405     3817   3058   4685    -96    212    400       C  
ATOM   2501  CG1 VAL A 405     182.495  15.072 524.454  1.00 30.96           C  
ANISOU 2501  CG1 VAL A 405     3727   3257   4780    -23    173    475       C  
ATOM   2502  CG2 VAL A 405     180.776  15.700 522.736  1.00 52.04           C  
ANISOU 2502  CG2 VAL A 405     6693   5683   7399   -116    144    432       C  
ATOM   2503  N   MET A 406     182.144  17.817 520.748  1.00 40.11           N  
ANISOU 2503  N   MET A 406     5408   4157   5676   -377    276    235       N  
ATOM   2504  CA  MET A 406     181.954  18.328 519.395  1.00 35.43           C  
ANISOU 2504  CA  MET A 406     5005   3457   5001   -470    303    181       C  
ATOM   2505  C   MET A 406     183.270  18.792 518.788  1.00 40.76           C  
ANISOU 2505  C   MET A 406     5684   4194   5610   -582    421     94       C  
ATOM   2506  O   MET A 406     183.449  18.716 517.567  1.00 57.44           O  
ANISOU 2506  O   MET A 406     7914   6239   7670   -642    482     41       O  
ATOM   2507  CB  MET A 406     180.945  19.478 519.388  1.00 27.78           C  
ANISOU 2507  CB  MET A 406     4185   2410   3959   -508    228    209       C  
ATOM   2508  CG  MET A 406     179.520  19.078 519.718  1.00 24.73           C  
ANISOU 2508  CG  MET A 406     3807   1956   3633   -409    119    288       C  
ATOM   2509  SD  MET A 406     178.482  20.519 520.033  0.75 24.45           S  
ANISOU 2509  SD  MET A 406     3895   1863   3531   -419     42    319       S  
ATOM   2510  CE  MET A 406     177.314  19.843 521.210  1.00 23.79           C  
ANISOU 2510  CE  MET A 406     3674   1809   3556   -284    -40    411       C  
ATOM   2511  N   VAL A 407     184.194  19.286 519.614  1.00 40.31           N  
ANISOU 2511  N   VAL A 407     5498   4272   5545   -622    456     74       N  
ATOM   2512  CA  VAL A 407     185.521  19.633 519.114  1.00 49.83           C  
ANISOU 2512  CA  VAL A 407     6664   5565   6706   -735    576    -10       C  
ATOM   2513  C   VAL A 407     186.293  18.373 518.741  1.00 44.39           C  
ANISOU 2513  C   VAL A 407     5838   4928   6102   -657    656    -42       C  
ATOM   2514  O   VAL A 407     186.876  18.279 517.651  1.00 51.44           O  
ANISOU 2514  O   VAL A 407     6785   5803   6955   -722    765   -114       O  
ATOM   2515  CB  VAL A 407     186.282  20.476 520.154  1.00 50.14           C  
ANISOU 2515  CB  VAL A 407     6585   5746   6718   -809    577    -27       C  
ATOM   2516  CG1 VAL A 407     187.707  20.735 519.689  1.00 58.89           C  
ANISOU 2516  CG1 VAL A 407     7608   6970   7797   -933    704   -113       C  
ATOM   2517  CG2 VAL A 407     185.553  21.787 520.411  1.00 35.36           C  
ANISOU 2517  CG2 VAL A 407     4884   3796   4757   -890    517    -13       C  
ATOM   2518  N   LEU A 408     186.297  17.380 519.638  1.00 37.69           N  
ANISOU 2518  N   LEU A 408     4820   4135   5366   -512    608     13       N  
ATOM   2519  CA  LEU A 408     187.011  16.133 519.375  1.00 36.22           C  
ANISOU 2519  CA  LEU A 408     4504   3981   5277   -408    679     -9       C  
ATOM   2520  C   LEU A 408     186.515  15.465 518.098  1.00 42.06           C  
ANISOU 2520  C   LEU A 408     5403   4565   6015   -393    722    -46       C  
ATOM   2521  O   LEU A 408     187.320  15.002 517.279  1.00 30.98           O  
ANISOU 2521  O   LEU A 408     3979   3174   4619   -396    842   -124       O  
ATOM   2522  CB  LEU A 408     186.870  15.187 520.568  1.00 38.75           C  
ANISOU 2522  CB  LEU A 408     4662   4350   5713   -245    598     81       C  
ATOM   2523  CG  LEU A 408     187.304  13.729 520.383  1.00 52.83           C  
ANISOU 2523  CG  LEU A 408     6344   6112   7619    -96    646     85       C  
ATOM   2524  CD1 LEU A 408     188.749  13.630 519.920  1.00 66.63           C  
ANISOU 2524  CD1 LEU A 408     7955   7979   9384   -107    776     -6       C  
ATOM   2525  CD2 LEU A 408     187.104  12.953 521.675  1.00 56.41           C  
ANISOU 2525  CD2 LEU A 408     6660   6605   8167     51    552    197       C  
ATOM   2526  N   ILE A 409     185.195  15.405 517.907  1.00 46.62           N  
ANISOU 2526  N   ILE A 409     6136   5000   6577   -379    627      5       N  
ATOM   2527  CA  ILE A 409     184.660  14.850 516.666  1.00 45.33           C  
ANISOU 2527  CA  ILE A 409     6141   4693   6391   -387    648    -35       C  
ATOM   2528  C   ILE A 409     184.976  15.770 515.492  1.00 43.59           C  
ANISOU 2528  C   ILE A 409     6084   4450   6026   -539    728   -115       C  
ATOM   2529  O   ILE A 409     185.241  15.309 514.376  1.00 56.80           O  
ANISOU 2529  O   ILE A 409     7851   6067   7662   -565    816   -189       O  
ATOM   2530  CB  ILE A 409     183.148  14.597 516.802  1.00 49.87           C  
ANISOU 2530  CB  ILE A 409     6817   5143   6988   -346    511     42       C  
ATOM   2531  CG1 ILE A 409     182.875  13.587 517.919  1.00 43.85           C  
ANISOU 2531  CG1 ILE A 409     5902   4394   6363   -207    452    125       C  
ATOM   2532  CG2 ILE A 409     182.564  14.105 515.487  1.00 49.35           C  
ANISOU 2532  CG2 ILE A 409     6935   4936   6881   -377    514     -6       C  
ATOM   2533  CD1 ILE A 409     181.409  13.306 518.138  1.00 37.82           C  
ANISOU 2533  CD1 ILE A 409     5209   3528   5634   -177    330    203       C  
ATOM   2534  N   ASN A 410     184.970  17.084 515.730  1.00 37.72           N  
ANISOU 2534  N   ASN A 410     5392   3746   5194   -647    706   -102       N  
ATOM   2535  CA  ASN A 410     185.250  18.047 514.672  1.00 32.99           C  
ANISOU 2535  CA  ASN A 410     4969   3115   4449   -803    779   -159       C  
ATOM   2536  C   ASN A 410     186.674  17.932 514.144  1.00 47.87           C  
ANISOU 2536  C   ASN A 410     6771   5103   6314   -869    954   -254       C  
ATOM   2537  O   ASN A 410     186.938  18.357 513.013  1.00 60.71           O  
ANISOU 2537  O   ASN A 410     8556   6692   7821   -989   1046   -312       O  
ATOM   2538  CB  ASN A 410     184.989  19.466 515.183  1.00 43.19           C  
ANISOU 2538  CB  ASN A 410     6329   4414   5666   -896    720   -121       C  
ATOM   2539  CG  ASN A 410     185.276  20.529 514.139  1.00 52.33           C  
ANISOU 2539  CG  ASN A 410     7690   5524   6669  -1065    794   -164       C  
ATOM   2540  OD1 ASN A 410     184.458  20.784 513.255  1.00 68.38           O  
ANISOU 2540  OD1 ASN A 410     9939   7427   8613  -1094    745   -145       O  
ATOM   2541  ND2 ASN A 410     186.441  21.159 514.240  1.00 41.09           N  
ANISOU 2541  ND2 ASN A 410     6196   4208   5209  -1185    908   -217       N  
ATOM   2542  N   THR A 411     187.595  17.369 514.930  1.00 49.84           N  
ANISOU 2542  N   THR A 411     6772   5490   6674   -792   1004   -267       N  
ATOM   2543  CA  THR A 411     188.971  17.216 514.462  1.00 45.25           C  
ANISOU 2543  CA  THR A 411     6074   5028   6093   -840   1175   -360       C  
ATOM   2544  C   THR A 411     189.039  16.364 513.198  1.00 41.18           C  
ANISOU 2544  C   THR A 411     5664   4426   5555   -814   1282   -434       C  
ATOM   2545  O   THR A 411     189.690  16.740 512.216  1.00 51.69           O  
ANISOU 2545  O   THR A 411     7073   5780   6785   -936   1426   -515       O  
ATOM   2546  CB  THR A 411     189.839  16.605 515.563  1.00 46.70           C  
ANISOU 2546  CB  THR A 411     5956   5372   6418   -723   1182   -348       C  
ATOM   2547  OG1 THR A 411     189.330  15.314 515.920  1.00 53.92           O  
ANISOU 2547  OG1 THR A 411     6815   6217   7454   -530   1115   -300       O  
ATOM   2548  CG2 THR A 411     189.841  17.496 516.785  1.00 47.34           C  
ANISOU 2548  CG2 THR A 411     5944   5549   6493   -770   1082   -290       C  
ATOM   2549  N   PHE A 412     188.369  15.210 513.202  1.00 34.04           N  
ANISOU 2549  N   PHE A 412     4775   3419   4738   -665   1220   -411       N  
ATOM   2550  CA  PHE A 412     188.443  14.273 512.090  1.00 41.44           C  
ANISOU 2550  CA  PHE A 412     5811   4268   5665   -627   1319   -494       C  
ATOM   2551  C   PHE A 412     187.196  14.248 511.218  1.00 50.90           C  
ANISOU 2551  C   PHE A 412     7285   5290   6764   -674   1231   -483       C  
ATOM   2552  O   PHE A 412     187.192  13.548 510.200  1.00 51.33           O  
ANISOU 2552  O   PHE A 412     7460   5263   6780   -667   1308   -563       O  
ATOM   2553  CB  PHE A 412     188.724  12.851 512.603  1.00 45.91           C  
ANISOU 2553  CB  PHE A 412     6205   4832   6406   -428   1331   -494       C  
ATOM   2554  CG  PHE A 412     187.718  12.354 513.605  1.00 47.08           C  
ANISOU 2554  CG  PHE A 412     6321   4908   6657   -315   1156   -380       C  
ATOM   2555  CD1 PHE A 412     186.585  11.671 513.192  1.00 47.17           C  
ANISOU 2555  CD1 PHE A 412     6498   4747   6676   -281   1071   -361       C  
ATOM   2556  CD2 PHE A 412     187.913  12.561 514.961  1.00 49.58           C  
ANISOU 2556  CD2 PHE A 412     6442   5339   7057   -254   1077   -293       C  
ATOM   2557  CE1 PHE A 412     185.661  11.212 514.111  1.00 52.29           C  
ANISOU 2557  CE1 PHE A 412     7109   5338   7421   -192    924   -254       C  
ATOM   2558  CE2 PHE A 412     186.992  12.103 515.886  1.00 53.38           C  
ANISOU 2558  CE2 PHE A 412     6900   5761   7621   -158    932   -185       C  
ATOM   2559  CZ  PHE A 412     185.865  11.428 515.460  1.00 55.12           C  
ANISOU 2559  CZ  PHE A 412     7278   5809   7857   -129    861   -164       C  
ATOM   2560  N   CYS A 413     186.144  14.978 511.581  1.00 50.82           N  
ANISOU 2560  N   CYS A 413     7373   5224   6711   -716   1073   -394       N  
ATOM   2561  CA  CYS A 413     184.931  15.020 510.767  1.00 47.40           C  
ANISOU 2561  CA  CYS A 413     7182   4642   6185   -758    970   -376       C  
ATOM   2562  C   CYS A 413     184.244  16.356 511.000  1.00 49.57           C  
ANISOU 2562  C   CYS A 413     7560   4903   6370   -847    857   -297       C  
ATOM   2563  O   CYS A 413     183.730  16.609 512.094  1.00 54.03           O  
ANISOU 2563  O   CYS A 413     8025   5489   7016   -787    745   -214       O  
ATOM   2564  CB  CYS A 413     183.998  13.861 511.104  1.00 52.91           C  
ANISOU 2564  CB  CYS A 413     7858   5243   7004   -630    856   -335       C  
ATOM   2565  SG  CYS A 413     182.450  13.887 510.173  0.64 62.40           S  
ANISOU 2565  SG  CYS A 413     9321   6286   8103   -689    702   -311       S  
ATOM   2566  N   ALA A 414     184.229  17.201 509.974  1.00 55.47           N  
ANISOU 2566  N   ALA A 414     8519   5610   6948   -983    891   -323       N  
ATOM   2567  CA  ALA A 414     183.574  18.501 510.052  1.00 59.26           C  
ANISOU 2567  CA  ALA A 414     9133   6049   7334  -1061    788   -250       C  
ATOM   2568  C   ALA A 414     182.065  18.399 509.823  1.00 57.17           C  
ANISOU 2568  C   ALA A 414     9004   5663   7056  -1012    602   -180       C  
ATOM   2569  O   ALA A 414     181.300  19.011 510.579  1.00 54.74           O  
ANISOU 2569  O   ALA A 414     8675   5338   6785   -972    477    -96       O  
ATOM   2570  CB  ALA A 414     184.205  19.481 509.058  1.00 60.82           C  
ANISOU 2570  CB  ALA A 414     9513   6245   7351  -1231    902   -291       C  
ATOM   2571  N   PRO A 415     181.581  17.660 508.813  1.00 59.64           N  
ANISOU 2571  N   PRO A 415     9452   5894   7315  -1014    577   -217       N  
ATOM   2572  CA  PRO A 415     180.122  17.562 508.628  1.00 60.31           C  
ANISOU 2572  CA  PRO A 415     9638   5883   7395   -974    384   -149       C  
ATOM   2573  C   PRO A 415     179.408  16.781 509.720  1.00 61.67           C  
ANISOU 2573  C   PRO A 415     9621   6059   7751   -843    279    -94       C  
ATOM   2574  O   PRO A 415     178.170  16.762 509.725  1.00 65.76           O  
ANISOU 2574  O   PRO A 415    10182   6518   8286   -811    118    -31       O  
ATOM   2575  CB  PRO A 415     179.982  16.856 507.271  1.00 65.40           C  
ANISOU 2575  CB  PRO A 415    10462   6457   7929  -1028    401   -225       C  
ATOM   2576  CG  PRO A 415     181.291  17.043 506.597  1.00 67.08           C  
ANISOU 2576  CG  PRO A 415    10731   6719   8035  -1121    606   -317       C  
ATOM   2577  CD  PRO A 415     182.293  17.006 507.699  1.00 66.30           C  
ANISOU 2577  CD  PRO A 415    10385   6730   8076  -1069    719   -326       C  
ATOM   2578  N   CYS A 416     180.133  16.138 510.638  1.00 62.22           N  
ANISOU 2578  N   CYS A 416     9481   6202   7959   -769    364   -109       N  
ATOM   2579  CA  CYS A 416     179.481  15.370 511.692  1.00 54.10           C  
ANISOU 2579  CA  CYS A 416     8287   5173   7094   -652    274    -46       C  
ATOM   2580  C   CYS A 416     178.771  16.254 512.708  1.00 50.66           C  
ANISOU 2580  C   CYS A 416     7786   4770   6693   -618    166     54       C  
ATOM   2581  O   CYS A 416     177.925  15.755 513.458  1.00 59.71           O  
ANISOU 2581  O   CYS A 416     8832   5906   7949   -537     71    119       O  
ATOM   2582  CB  CYS A 416     180.498  14.480 512.410  1.00 64.26           C  
ANISOU 2582  CB  CYS A 416     9380   6529   8507   -572    389    -76       C  
ATOM   2583  SG  CYS A 416     181.096  13.071 511.445  1.00 70.20           S  
ANISOU 2583  SG  CYS A 416    10177   7216   9280   -552    506   -189       S  
ATOM   2584  N   ILE A 417     179.090  17.541 512.757  1.00 38.40           N  
ANISOU 2584  N   ILE A 417     6294   3249   5048   -681    187     63       N  
ATOM   2585  CA  ILE A 417     178.495  18.472 513.704  1.00 41.11           C  
ANISOU 2585  CA  ILE A 417     6593   3612   5413   -647    102    140       C  
ATOM   2586  C   ILE A 417     177.867  19.619 512.922  1.00 46.37           C  
ANISOU 2586  C   ILE A 417     7473   4200   5947   -711     30    164       C  
ATOM   2587  O   ILE A 417     178.568  20.495 512.413  1.00 49.70           O  
ANISOU 2587  O   ILE A 417     8017   4615   6252   -809    105    132       O  
ATOM   2588  CB  ILE A 417     179.533  18.995 514.714  1.00 36.74           C  
ANISOU 2588  CB  ILE A 417     5906   3168   4885   -655    194    128       C  
ATOM   2589  CG1 ILE A 417     180.369  17.844 515.278  1.00 36.98           C  
ANISOU 2589  CG1 ILE A 417     5742   3282   5027   -593    275    101       C  
ATOM   2590  CG2 ILE A 417     178.839  19.734 515.847  1.00 46.73           C  
ANISOU 2590  CG2 ILE A 417     7114   4453   6188   -600    108    200       C  
ATOM   2591  CD1 ILE A 417     179.580  16.874 516.130  1.00 47.65           C  
ANISOU 2591  CD1 ILE A 417     6963   4629   6512   -472    191    168       C  
ATOM   2592  N   PRO A 418     176.543  19.643 512.796  1.00 34.18           N  
ANISOU 2592  N   PRO A 418     5976   2592   4418   -658   -119    227       N  
ATOM   2593  CA  PRO A 418     175.875  20.787 512.165  1.00 30.13           C  
ANISOU 2593  CA  PRO A 418     5654   2004   3791   -688   -208    268       C  
ATOM   2594  C   PRO A 418     176.030  22.049 513.003  1.00 42.54           C  
ANISOU 2594  C   PRO A 418     7223   3587   5354   -678   -192    300       C  
ATOM   2595  O   PRO A 418     176.477  22.027 514.151  1.00 59.06           O  
ANISOU 2595  O   PRO A 418     9153   5757   7530   -643   -134    295       O  
ATOM   2596  CB  PRO A 418     174.410  20.349 512.083  1.00 35.01           C  
ANISOU 2596  CB  PRO A 418     6249   2583   4470   -608   -377    330       C  
ATOM   2597  CG  PRO A 418     174.450  18.855 512.167  1.00 27.75           C  
ANISOU 2597  CG  PRO A 418     5202   1690   3651   -589   -357    296       C  
ATOM   2598  CD  PRO A 418     175.610  18.534 513.059  1.00 27.12           C  
ANISOU 2598  CD  PRO A 418     4974   1689   3642   -577   -212    259       C  
ATOM   2599  N   ASN A 419     175.637  23.174 512.399  1.00 47.15           N  
ANISOU 2599  N   ASN A 419     8004   4084   5826   -709   -249    335       N  
ATOM   2600  CA  ASN A 419     175.765  24.463 513.075  1.00 48.03           C  
ANISOU 2600  CA  ASN A 419     8160   4173   5918   -708   -230    358       C  
ATOM   2601  C   ASN A 419     174.826  24.562 514.272  1.00 48.32           C  
ANISOU 2601  C   ASN A 419     8049   4234   6078   -569   -313    409       C  
ATOM   2602  O   ASN A 419     175.195  25.120 515.313  1.00 63.38           O  
ANISOU 2602  O   ASN A 419     9885   6178   8018   -557   -258    398       O  
ATOM   2603  CB  ASN A 419     175.497  25.599 512.088  1.00 60.86           C  
ANISOU 2603  CB  ASN A 419    10029   5699   7396   -752   -276    388       C  
ATOM   2604  CG  ASN A 419     175.477  26.960 512.756  1.00 76.92           C  
ANISOU 2604  CG  ASN A 419    12097   7713   9416   -727   -265    405       C  
ATOM   2605  OD1 ASN A 419     176.522  27.570 512.979  1.00 82.31           O  
ANISOU 2605  OD1 ASN A 419    12817   8407  10049   -832   -146    359       O  
ATOM   2606  ND2 ASN A 419     174.282  27.446 513.074  1.00 78.56           N  
ANISOU 2606  ND2 ASN A 419    12292   7886   9670   -592   -387    466       N  
ATOM   2607  N   THR A 420     173.609  24.029 514.140  1.00 47.05           N  
ANISOU 2607  N   THR A 420     7837   4059   5981   -472   -443    462       N  
ATOM   2608  CA  THR A 420     172.658  24.068 515.248  1.00 54.49           C  
ANISOU 2608  CA  THR A 420     8625   5037   7042   -341   -509    511       C  
ATOM   2609  C   THR A 420     173.214  23.353 516.473  1.00 54.11           C  
ANISOU 2609  C   THR A 420     8362   5101   7094   -323   -419    485       C  
ATOM   2610  O   THR A 420     173.025  23.807 517.608  1.00 62.97           O  
ANISOU 2610  O   THR A 420     9397   6264   8267   -258   -404    500       O  
ATOM   2611  CB  THR A 420     171.329  23.444 514.819  1.00 56.02           C  
ANISOU 2611  CB  THR A 420     8772   5219   7295   -265   -655    567       C  
ATOM   2612  OG1 THR A 420     170.887  24.049 513.597  1.00 56.80           O  
ANISOU 2612  OG1 THR A 420     9076   5223   7284   -286   -752    594       O  
ATOM   2613  CG2 THR A 420     170.268  23.652 515.890  1.00 53.38           C  
ANISOU 2613  CG2 THR A 420     8285   4921   7074   -129   -715    621       C  
ATOM   2614  N   VAL A 421     173.917  22.239 516.260  1.00 44.28           N  
ANISOU 2614  N   VAL A 421     7042   3907   5874   -375   -358    447       N  
ATOM   2615  CA  VAL A 421     174.516  21.508 517.371  1.00 48.41           C  
ANISOU 2615  CA  VAL A 421     7370   4534   6487   -350   -281    434       C  
ATOM   2616  C   VAL A 421     175.594  22.349 518.046  1.00 46.20           C  
ANISOU 2616  C   VAL A 421     7089   4305   6159   -401   -182    392       C  
ATOM   2617  O   VAL A 421     175.698  22.376 519.280  1.00 54.23           O  
ANISOU 2617  O   VAL A 421     7973   5402   7228   -354   -159    403       O  
ATOM   2618  CB  VAL A 421     175.066  20.158 516.876  1.00 42.37           C  
ANISOU 2618  CB  VAL A 421     6549   3790   5760   -382   -236    400       C  
ATOM   2619  CG1 VAL A 421     175.676  19.372 518.022  1.00 43.06           C  
ANISOU 2619  CG1 VAL A 421     6440   3979   5944   -338   -169    403       C  
ATOM   2620  CG2 VAL A 421     173.960  19.355 516.208  1.00 31.80           C  
ANISOU 2620  CG2 VAL A 421     5225   2393   4463   -353   -343    432       C  
ATOM   2621  N   TRP A 422     176.409  23.054 517.253  1.00 35.44           N  
ANISOU 2621  N   TRP A 422     5879   2902   4686   -511   -121    343       N  
ATOM   2622  CA  TRP A 422     177.397  23.962 517.827  1.00 41.25           C  
ANISOU 2622  CA  TRP A 422     6626   3679   5370   -588    -34    298       C  
ATOM   2623  C   TRP A 422     176.727  25.036 518.675  1.00 48.17           C  
ANISOU 2623  C   TRP A 422     7539   4521   6244   -532    -81    326       C  
ATOM   2624  O   TRP A 422     177.185  25.339 519.785  1.00 52.96           O  
ANISOU 2624  O   TRP A 422     8053   5205   6865   -535    -38    302       O  
ATOM   2625  CB  TRP A 422     178.233  24.606 516.721  1.00 37.01           C  
ANISOU 2625  CB  TRP A 422     6268   3085   4709   -731     39    250       C  
ATOM   2626  CG  TRP A 422     179.258  23.695 516.112  1.00 46.19           C  
ANISOU 2626  CG  TRP A 422     7369   4313   5867   -800    136    194       C  
ATOM   2627  CD1 TRP A 422     179.240  23.166 514.855  1.00 38.93           C  
ANISOU 2627  CD1 TRP A 422     6553   3341   4896   -837    145    179       C  
ATOM   2628  CD2 TRP A 422     180.455  23.211 516.734  1.00 55.20           C  
ANISOU 2628  CD2 TRP A 422     8330   5589   7055   -832    237    143       C  
ATOM   2629  NE1 TRP A 422     180.352  22.384 514.654  1.00 35.47           N  
ANISOU 2629  NE1 TRP A 422     6013   2988   4476   -883    263    114       N  
ATOM   2630  CE2 TRP A 422     181.113  22.393 515.793  1.00 50.13           C  
ANISOU 2630  CE2 TRP A 422     7685   4962   6399   -875    316     96       C  
ATOM   2631  CE3 TRP A 422     181.034  23.389 517.995  1.00 44.56           C  
ANISOU 2631  CE3 TRP A 422     6822   4354   5753   -825    265    131       C  
ATOM   2632  CZ2 TRP A 422     182.319  21.754 516.073  1.00 48.25           C  
ANISOU 2632  CZ2 TRP A 422     7275   4849   6208   -895    424     41       C  
ATOM   2633  CZ3 TRP A 422     182.232  22.754 518.271  1.00 43.08           C  
ANISOU 2633  CZ3 TRP A 422     6464   4298   5605   -854    355     83       C  
ATOM   2634  CH2 TRP A 422     182.861  21.947 517.314  1.00 45.19           C  
ANISOU 2634  CH2 TRP A 422     6718   4578   5875   -881    435     41       C  
ATOM   2635  N   THR A 423     175.636  25.618 518.169  1.00 49.40           N  
ANISOU 2635  N   THR A 423     7830   4562   6377   -474   -172    373       N  
ATOM   2636  CA  THR A 423     174.896  26.609 518.944  1.00 51.75           C  
ANISOU 2636  CA  THR A 423     8164   4815   6684   -392   -213    396       C  
ATOM   2637  C   THR A 423     174.387  26.015 520.252  1.00 50.78           C  
ANISOU 2637  C   THR A 423     7830   4798   6668   -281   -225    418       C  
ATOM   2638  O   THR A 423     174.428  26.672 521.301  1.00 57.41           O  
ANISOU 2638  O   THR A 423     8644   5664   7504   -255   -194    398       O  
ATOM   2639  CB  THR A 423     173.734  27.163 518.118  1.00 52.28           C  
ANISOU 2639  CB  THR A 423     8385   4752   6729   -319   -323    455       C  
ATOM   2640  OG1 THR A 423     174.232  27.699 516.885  1.00 43.22           O  
ANISOU 2640  OG1 THR A 423     7455   3505   5463   -429   -310    445       O  
ATOM   2641  CG2 THR A 423     173.008  28.261 518.882  1.00 63.57           C  
ANISOU 2641  CG2 THR A 423     9862   6119   8172   -217   -351    472       C  
ATOM   2642  N   ILE A 424     173.919  24.765 520.213  1.00 40.79           N  
ANISOU 2642  N   ILE A 424     6421   3590   5488   -225   -265    457       N  
ATOM   2643  CA  ILE A 424     173.395  24.124 521.418  1.00 41.44           C  
ANISOU 2643  CA  ILE A 424     6310   3770   5666   -130   -271    492       C  
ATOM   2644  C   ILE A 424     174.503  23.938 522.449  1.00 42.48           C  
ANISOU 2644  C   ILE A 424     6333   4017   5790   -175   -183    453       C  
ATOM   2645  O   ILE A 424     174.334  24.260 523.631  1.00 43.21           O  
ANISOU 2645  O   ILE A 424     6355   4172   5890   -126   -165    455       O  
ATOM   2646  CB  ILE A 424     172.718  22.788 521.064  1.00 36.99           C  
ANISOU 2646  CB  ILE A 424     5635   3226   5195    -87   -328    543       C  
ATOM   2647  CG1 ILE A 424     171.438  23.036 520.264  1.00 31.40           C  
ANISOU 2647  CG1 ILE A 424     4999   2431   4501    -30   -439    587       C  
ATOM   2648  CG2 ILE A 424     172.416  21.992 522.324  1.00 41.46           C  
ANISOU 2648  CG2 ILE A 424     6003   3899   5851    -18   -310    583       C  
ATOM   2649  CD1 ILE A 424     170.752  21.770 519.799  1.00 44.58           C  
ANISOU 2649  CD1 ILE A 424     6575   4111   6252    -16   -506    627       C  
ATOM   2650  N   GLY A 425     175.654  23.415 522.017  1.00 41.21           N  
ANISOU 2650  N   GLY A 425     6154   3895   5609   -266   -127    415       N  
ATOM   2651  CA  GLY A 425     176.753  23.211 522.951  1.00 45.65           C  
ANISOU 2651  CA  GLY A 425     6596   4583   6166   -304    -58    383       C  
ATOM   2652  C   GLY A 425     177.253  24.512 523.551  1.00 40.72           C  
ANISOU 2652  C   GLY A 425     6046   3970   5457   -368    -21    327       C  
ATOM   2653  O   GLY A 425     177.454  24.618 524.768  1.00 45.92           O  
ANISOU 2653  O   GLY A 425     6610   4727   6113   -348     -7    320       O  
ATOM   2654  N   TYR A 426     177.463  25.520 522.700  1.00 29.08           N  
ANISOU 2654  N   TYR A 426     4758   2389   3904   -455     -6    287       N  
ATOM   2655  CA  TYR A 426     177.830  26.850 523.178  1.00 33.52           C  
ANISOU 2655  CA  TYR A 426     5430   2922   4385   -527     27    231       C  
ATOM   2656  C   TYR A 426     176.845  27.340 524.235  1.00 50.85           C  
ANISOU 2656  C   TYR A 426     7618   5106   6598   -413     -9    250       C  
ATOM   2657  O   TYR A 426     177.238  27.796 525.319  1.00 54.49           O  
ANISOU 2657  O   TYR A 426     8043   5638   7023   -438     22    205       O  
ATOM   2658  CB  TYR A 426     177.877  27.819 521.995  1.00 26.86           C  
ANISOU 2658  CB  TYR A 426     4821   1923   3463   -613     36    212       C  
ATOM   2659  CG  TYR A 426     179.083  28.727 521.968  1.00 27.48           C  
ANISOU 2659  CG  TYR A 426     4990   2001   3450   -788    117    134       C  
ATOM   2660  CD1 TYR A 426     180.258  28.332 521.344  1.00 27.73           C  
ANISOU 2660  CD1 TYR A 426     4978   2101   3456   -919    189     96       C  
ATOM   2661  CD2 TYR A 426     179.042  29.985 522.553  1.00 28.25           C  
ANISOU 2661  CD2 TYR A 426     5217   2027   3491   -828    128     93       C  
ATOM   2662  CE1 TYR A 426     181.363  29.160 521.311  1.00 28.72           C  
ANISOU 2662  CE1 TYR A 426     5169   2240   3504  -1098    268     25       C  
ATOM   2663  CE2 TYR A 426     180.142  30.821 522.526  1.00 30.18           C  
ANISOU 2663  CE2 TYR A 426     5547   2266   3653  -1012    202     19       C  
ATOM   2664  CZ  TYR A 426     181.299  30.403 521.904  1.00 29.75           C  
ANISOU 2664  CZ  TYR A 426     5430   2295   3577  -1153    271    -13       C  
ATOM   2665  OH  TYR A 426     182.397  31.232 521.874  1.00 45.76           O  
ANISOU 2665  OH  TYR A 426     7526   4331   5529  -1355    349    -87       O  
ATOM   2666  N   TRP A 427     175.548  27.224 523.939  1.00 57.54           N  
ANISOU 2666  N   TRP A 427     8490   5875   7497   -287    -75    311       N  
ATOM   2667  CA  TRP A 427     174.538  27.720 524.864  1.00 44.02           C  
ANISOU 2667  CA  TRP A 427     6767   4151   5807   -167    -96    326       C  
ATOM   2668  C   TRP A 427     174.517  26.933 526.166  1.00 35.54           C  
ANISOU 2668  C   TRP A 427     5492   3236   4774   -112    -76    343       C  
ATOM   2669  O   TRP A 427     174.193  27.500 527.212  1.00 34.04           O  
ANISOU 2669  O   TRP A 427     5299   3075   4560    -63    -54    319       O  
ATOM   2670  CB  TRP A 427     173.162  27.705 524.203  1.00 27.38           C  
ANISOU 2670  CB  TRP A 427     4698   1946   3759    -42   -175    393       C  
ATOM   2671  CG  TRP A 427     172.725  29.069 523.794  1.00 31.35           C  
ANISOU 2671  CG  TRP A 427     5411   2290   4210    -15   -194    376       C  
ATOM   2672  CD1 TRP A 427     172.639  29.559 522.524  1.00 54.44           C  
ANISOU 2672  CD1 TRP A 427     8515   5077   7095    -47   -238    395       C  
ATOM   2673  CD2 TRP A 427     172.341  30.138 524.664  1.00 33.77           C  
ANISOU 2673  CD2 TRP A 427     5789   2548   4494     52   -165    337       C  
ATOM   2674  NE1 TRP A 427     172.210  30.864 522.549  1.00 62.48           N  
ANISOU 2674  NE1 TRP A 427     9711   5954   8074      5   -246    381       N  
ATOM   2675  CE2 TRP A 427     172.022  31.244 523.852  1.00 42.50           C  
ANISOU 2675  CE2 TRP A 427     7119   3471   5559     69   -197    339       C  
ATOM   2676  CE3 TRP A 427     172.230  30.266 526.052  1.00 35.17           C  
ANISOU 2676  CE3 TRP A 427     5874   2814   4674    103   -113    300       C  
ATOM   2677  CZ2 TRP A 427     171.599  32.460 524.381  1.00 39.07           C  
ANISOU 2677  CZ2 TRP A 427     6819   2925   5100    144   -175    302       C  
ATOM   2678  CZ3 TRP A 427     171.811  31.474 526.576  1.00 40.14           C  
ANISOU 2678  CZ3 TRP A 427     6636   3346   5270    168    -86    252       C  
ATOM   2679  CH2 TRP A 427     171.500  32.555 525.742  1.00 50.28           C  
ANISOU 2679  CH2 TRP A 427     8143   4433   6528    193   -116    251       C  
ATOM   2680  N   LEU A 428     174.849  25.640 526.134  1.00 24.80           N  
ANISOU 2680  N   LEU A 428     3979   1973   3470   -118    -81    385       N  
ATOM   2681  CA  LEU A 428     174.964  24.882 527.377  1.00 39.70           C  
ANISOU 2681  CA  LEU A 428     5693   4009   5383    -77    -62    413       C  
ATOM   2682  C   LEU A 428     176.134  25.386 528.213  1.00 40.48           C  
ANISOU 2682  C   LEU A 428     5783   4203   5393   -169    -15    343       C  
ATOM   2683  O   LEU A 428     176.003  25.602 529.431  1.00 33.18           O  
ANISOU 2683  O   LEU A 428     4812   3364   4433   -136      0    335       O  
ATOM   2684  CB  LEU A 428     175.120  23.392 527.075  1.00 34.39           C  
ANISOU 2684  CB  LEU A 428     4883   3390   4792    -62    -78    476       C  
ATOM   2685  CG  LEU A 428     173.878  22.666 526.557  1.00 45.25           C  
ANISOU 2685  CG  LEU A 428     6223   4706   6262     23   -131    550       C  
ATOM   2686  CD1 LEU A 428     174.180  21.196 526.314  1.00 48.93           C  
ANISOU 2686  CD1 LEU A 428     6576   5210   6804     20   -137    599       C  
ATOM   2687  CD2 LEU A 428     172.725  22.826 527.535  1.00 51.72           C  
ANISOU 2687  CD2 LEU A 428     6980   5560   7109    125   -137    592       C  
ATOM   2688  N   CYS A 429     177.291  25.582 527.569  1.00 28.68           N  
ANISOU 2688  N   CYS A 429     4332   2706   3859   -293      9    290       N  
ATOM   2689  CA  CYS A 429     178.416  26.212 528.251  1.00 25.80           C  
ANISOU 2689  CA  CYS A 429     3964   2429   3408   -405     45    212       C  
ATOM   2690  C   CYS A 429     178.008  27.537 528.879  1.00 26.53           C  
ANISOU 2690  C   CYS A 429     4197   2459   3423   -415     58    152       C  
ATOM   2691  O   CYS A 429     178.539  27.917 529.929  1.00 44.10           O  
ANISOU 2691  O   CYS A 429     6393   4784   5578   -466     73     99       O  
ATOM   2692  CB  CYS A 429     179.577  26.422 527.279  1.00 27.62           C  
ANISOU 2692  CB  CYS A 429     4241   2643   3609   -550     81    158       C  
ATOM   2693  SG  CYS A 429     180.375  24.907 526.698  1.00 58.40           S  
ANISOU 2693  SG  CYS A 429     7963   6639   7588   -545     91    199       S  
ATOM   2694  N   TYR A 430     177.064  28.250 528.258  1.00 36.73           N  
ANISOU 2694  N   TYR A 430     5646   3584   4724   -361     47    156       N  
ATOM   2695  CA  TYR A 430     176.498  29.424 528.916  1.00 37.05           C  
ANISOU 2695  CA  TYR A 430     5818   3549   4709   -327     63    104       C  
ATOM   2696  C   TYR A 430     175.584  29.037 530.076  1.00 31.11           C  
ANISOU 2696  C   TYR A 430     4954   2883   3983   -186     61    140       C  
ATOM   2697  O   TYR A 430     175.536  29.748 531.086  1.00 36.10           O  
ANISOU 2697  O   TYR A 430     5634   3539   4545   -183     93     77       O  
ATOM   2698  CB  TYR A 430     175.739  30.282 527.905  1.00 42.17           C  
ANISOU 2698  CB  TYR A 430     6664   3989   5368   -286     46    110       C  
ATOM   2699  CG  TYR A 430     176.633  31.069 526.975  1.00 39.61           C  
ANISOU 2699  CG  TYR A 430     6514   3556   4978   -445     69     58       C  
ATOM   2700  CD1 TYR A 430     177.943  31.364 527.327  1.00 42.26           C  
ANISOU 2700  CD1 TYR A 430     6845   3971   5242   -620    117    -20       C  
ATOM   2701  CD2 TYR A 430     176.166  31.522 525.749  1.00 48.04           C  
ANISOU 2701  CD2 TYR A 430     7749   4451   6052   -430     42     93       C  
ATOM   2702  CE1 TYR A 430     178.765  32.086 526.483  1.00 46.04           C  
ANISOU 2702  CE1 TYR A 430     7476   4356   5660   -785    152    -67       C  
ATOM   2703  CE2 TYR A 430     176.980  32.246 524.897  1.00 56.28           C  
ANISOU 2703  CE2 TYR A 430     8967   5394   7024   -588     75     54       C  
ATOM   2704  CZ  TYR A 430     178.278  32.524 525.270  1.00 53.08           C  
ANISOU 2704  CZ  TYR A 430     8549   5066   6553   -770    137    -27       C  
ATOM   2705  OH  TYR A 430     179.091  33.244 524.426  1.00 56.04           O  
ANISOU 2705  OH  TYR A 430     9090   5345   6856   -945    183    -64       O  
ATOM   2706  N   ILE A 431     174.866  27.915 529.956  1.00 29.62           N  
ANISOU 2706  N   ILE A 431     4624   2742   3887    -80     30    236       N  
ATOM   2707  CA  ILE A 431     173.903  27.516 530.980  1.00 38.94           C  
ANISOU 2707  CA  ILE A 431     5696   4002   5096     47     40    282       C  
ATOM   2708  C   ILE A 431     174.612  27.193 532.287  1.00 46.21           C  
ANISOU 2708  C   ILE A 431     6518   5096   5944      4     67    264       C  
ATOM   2709  O   ILE A 431     174.027  27.334 533.372  1.00 53.33           O  
ANISOU 2709  O   ILE A 431     7391   6062   6809     75    100    261       O  
ATOM   2710  CB  ILE A 431     173.050  26.330 530.481  1.00 38.56           C  
ANISOU 2710  CB  ILE A 431     5519   3963   5168    137      0    391       C  
ATOM   2711  CG1 ILE A 431     172.152  26.766 529.324  1.00 34.53           C  
ANISOU 2711  CG1 ILE A 431     5109   3295   4716    196    -43    408       C  
ATOM   2712  CG2 ILE A 431     172.193  25.746 531.597  1.00 26.09           C  
ANISOU 2712  CG2 ILE A 431     3803   2491   3617    240     24    449       C  
ATOM   2713  CD1 ILE A 431     171.361  28.019 529.607  1.00 27.00           C  
ANISOU 2713  CD1 ILE A 431     4274   2247   3736    281    -24    363       C  
ATOM   2714  N   ASN A 432     175.878  26.768 532.213  1.00 48.61           N  
ANISOU 2714  N   ASN A 432     6764   5486   6219   -109     56    251       N  
ATOM   2715  CA  ASN A 432     176.667  26.578 533.431  1.00 46.20           C  
ANISOU 2715  CA  ASN A 432     6372   5353   5829   -158     62    231       C  
ATOM   2716  C   ASN A 432     176.559  27.786 534.358  1.00 43.67           C  
ANISOU 2716  C   ASN A 432     6172   5030   5391   -183     98    131       C  
ATOM   2717  O   ASN A 432     176.318  27.645 535.563  1.00 47.11           O  
ANISOU 2717  O   ASN A 432     6555   5582   5762   -140    114    137       O  
ATOM   2718  CB  ASN A 432     178.130  26.315 533.076  1.00 46.78           C  
ANISOU 2718  CB  ASN A 432     6389   5502   5883   -288     43    203       C  
ATOM   2719  CG  ASN A 432     178.984  26.046 534.301  1.00 36.65           C  
ANISOU 2719  CG  ASN A 432     4995   4415   4514   -334     26    193       C  
ATOM   2720  OD1 ASN A 432     178.502  25.519 535.304  1.00 40.02           O  
ANISOU 2720  OD1 ASN A 432     5347   4940   4920   -250     21    253       O  
ATOM   2721  ND2 ASN A 432     180.258  26.413 534.227  1.00 29.37           N  
ANISOU 2721  ND2 ASN A 432     4060   3561   3537   -474     16    120       N  
ATOM   2722  N   SER A 433     176.722  28.989 533.801  1.00 40.90           N  
ANISOU 2722  N   SER A 433     5999   4537   5004   -255    116     37       N  
ATOM   2723  CA  SER A 433     176.618  30.202 534.605  1.00 35.11           C  
ANISOU 2723  CA  SER A 433     5412   3766   4162   -282    155    -72       C  
ATOM   2724  C   SER A 433     175.208  30.401 535.146  1.00 53.14           C  
ANISOU 2724  C   SER A 433     7723   6002   6465   -112    194    -54       C  
ATOM   2725  O   SER A 433     175.030  31.016 536.204  1.00 51.41           O  
ANISOU 2725  O   SER A 433     7566   5818   6150   -100    238   -129       O  
ATOM   2726  CB  SER A 433     177.043  31.414 533.776  1.00 33.09           C  
ANISOU 2726  CB  SER A 433     5361   3333   3879   -394    169   -164       C  
ATOM   2727  OG  SER A 433     178.398  31.310 533.379  1.00 43.40           O  
ANISOU 2727  OG  SER A 433     6631   4704   5156   -570    151   -194       O  
ATOM   2728  N   THR A 434     174.198  29.893 534.439  1.00 62.92           N  
ANISOU 2728  N   THR A 434     8911   7170   7825     16    181     38       N  
ATOM   2729  CA  THR A 434     172.823  30.049 534.899  1.00 46.97           C  
ANISOU 2729  CA  THR A 434     6884   5120   5841    182    221     60       C  
ATOM   2730  C   THR A 434     172.546  29.166 536.110  1.00 44.52           C  
ANISOU 2730  C   THR A 434     6413   5001   5503    233    250    114       C  
ATOM   2731  O   THR A 434     171.976  29.624 537.107  1.00 41.04           O  
ANISOU 2731  O   THR A 434     6000   4597   4995    300    315     68       O  
ATOM   2732  CB  THR A 434     171.848  29.726 533.766  1.00 40.23           C  
ANISOU 2732  CB  THR A 434     6003   4155   5127    289    184    145       C  
ATOM   2733  OG1 THR A 434     172.130  30.564 532.638  1.00 50.26           O  
ANISOU 2733  OG1 THR A 434     7444   5248   6404    239    154    105       O  
ATOM   2734  CG2 THR A 434     170.412  29.954 534.213  1.00 30.61           C  
ANISOU 2734  CG2 THR A 434     4755   2916   3958    464    226    163       C  
ATOM   2735  N   ILE A 435     172.947  27.891 536.044  1.00 52.76           N  
ANISOU 2735  N   ILE A 435     7295   6161   6590    204    208    214       N  
ATOM   2736  CA  ILE A 435     172.675  26.962 537.138  1.00 51.93           C  
ANISOU 2736  CA  ILE A 435     7046   6225   6459    250    231    290       C  
ATOM   2737  C   ILE A 435     173.725  27.019 538.237  1.00 52.35           C  
ANISOU 2737  C   ILE A 435     7098   6430   6361    153    230    243       C  
ATOM   2738  O   ILE A 435     173.569  26.342 539.263  1.00 50.29           O  
ANISOU 2738  O   ILE A 435     6744   6317   6046    184    249    305       O  
ATOM   2739  CB  ILE A 435     172.559  25.512 536.625  1.00 45.95           C  
ANISOU 2739  CB  ILE A 435     6131   5508   5822    272    187    428       C  
ATOM   2740  CG1 ILE A 435     173.890  25.045 536.032  1.00 42.20           C  
ANISOU 2740  CG1 ILE A 435     5629   5053   5351    163    125    433       C  
ATOM   2741  CG2 ILE A 435     171.439  25.396 535.602  1.00 47.05           C  
ANISOU 2741  CG2 ILE A 435     6259   5518   6102    360    176    475       C  
ATOM   2742  CD1 ILE A 435     173.885  23.596 535.598  1.00 51.98           C  
ANISOU 2742  CD1 ILE A 435     6729   6320   6700    187     88    558       C  
ATOM   2743  N   ASN A 436     174.790  27.802 538.063  1.00 61.12           N  
ANISOU 2743  N   ASN A 436     8310   7517   7396     28    205    139       N  
ATOM   2744  CA  ASN A 436     175.832  27.866 539.086  1.00 61.25           C  
ANISOU 2744  CA  ASN A 436     8312   7694   7265    -78    185     89       C  
ATOM   2745  C   ASN A 436     175.330  28.404 540.425  1.00 60.30           C  
ANISOU 2745  C   ASN A 436     8257   7649   7005    -43    246     28       C  
ATOM   2746  O   ASN A 436     175.605  27.770 541.456  1.00 57.03           O  
ANISOU 2746  O   ASN A 436     7756   7417   6498    -51    232     77       O  
ATOM   2747  CB  ASN A 436     177.020  28.681 538.562  1.00 64.48           C  
ANISOU 2747  CB  ASN A 436     8813   8057   7630   -238    151    -21       C  
ATOM   2748  CG  ASN A 436     178.347  27.973 538.762  1.00 57.82           C  
ANISOU 2748  CG  ASN A 436     7833   7384   6752   -343     80      9       C  
ATOM   2749  OD1 ASN A 436     178.470  27.089 539.609  1.00 54.34           O  
ANISOU 2749  OD1 ASN A 436     7264   7109   6272   -304     51     91       O  
ATOM   2750  ND2 ASN A 436     179.348  28.359 537.980  1.00 55.13           N  
ANISOU 2750  ND2 ASN A 436     7516   7005   6426   -474     53    -51       N  
ATOM   2751  N   PRO A 437     174.612  29.536 540.495  1.00 61.93           N  
ANISOU 2751  N   PRO A 437     8620   7726   7185      2    316    -76       N  
ATOM   2752  CA  PRO A 437     174.184  30.027 541.819  1.00 52.93           C  
ANISOU 2752  CA  PRO A 437     7548   6666   5897     35    389   -149       C  
ATOM   2753  C   PRO A 437     173.226  29.097 542.542  1.00 51.40           C  
ANISOU 2753  C   PRO A 437     7224   6592   5715    162    440    -34       C  
ATOM   2754  O   PRO A 437     173.171  29.123 543.778  1.00 37.17           O  
ANISOU 2754  O   PRO A 437     5436   4927   3761    160    485    -61       O  
ATOM   2755  CB  PRO A 437     173.519  31.374 541.495  1.00 42.22           C  
ANISOU 2755  CB  PRO A 437     6385   5104   4553     88    459   -275       C  
ATOM   2756  CG  PRO A 437     174.080  31.772 540.178  1.00 40.54           C  
ANISOU 2756  CG  PRO A 437     6241   4731   4433     11    401   -293       C  
ATOM   2757  CD  PRO A 437     174.253  30.490 539.432  1.00 51.47           C  
ANISOU 2757  CD  PRO A 437     7438   6175   5941     20    333   -142       C  
ATOM   2758  N   ALA A 438     172.468  28.274 541.815  1.00 59.30           N  
ANISOU 2758  N   ALA A 438     8103   7547   6881    260    438     94       N  
ATOM   2759  CA  ALA A 438     171.532  27.357 542.454  1.00 51.53           C  
ANISOU 2759  CA  ALA A 438     6989   6671   5919    361    494    211       C  
ATOM   2760  C   ALA A 438     172.224  26.190 543.146  1.00 59.38           C  
ANISOU 2760  C   ALA A 438     7866   7851   6846    303    443    324       C  
ATOM   2761  O   ALA A 438     171.569  25.469 543.907  1.00 51.13           O  
ANISOU 2761  O   ALA A 438     6738   6913   5776    362    498    420       O  
ATOM   2762  CB  ALA A 438     170.534  26.826 541.424  1.00 46.58           C  
ANISOU 2762  CB  ALA A 438     6266   5937   5495    462    494    308       C  
ATOM   2763  N   CYS A 439     173.519  25.989 542.907  1.00 67.91           N  
ANISOU 2763  N   CYS A 439     8934   8972   7897    193    344    321       N  
ATOM   2764  CA  CYS A 439     174.234  24.867 543.499  1.00 70.66           C  
ANISOU 2764  CA  CYS A 439     9167   9489   8194    157    280    438       C  
ATOM   2765  C   CYS A 439     174.793  25.167 544.882  1.00 80.08           C  
ANISOU 2765  C   CYS A 439    10409  10857   9160     95    276    387       C  
ATOM   2766  O   CYS A 439     175.131  24.227 545.610  1.00 90.33           O  
ANISOU 2766  O   CYS A 439    11620  12310  10392     95    236    504       O  
ATOM   2767  CB  CYS A 439     175.380  24.424 542.587  1.00 74.10           C  
ANISOU 2767  CB  CYS A 439     9538   9902   8714     85    175    464       C  
ATOM   2768  SG  CYS A 439     174.855  23.817 540.972  1.00 67.74           S  
ANISOU 2768  SG  CYS A 439     8671   8914   8151    145    165    539       S  
ATOM   2769  N   TYR A 440     174.906  26.439 545.263  1.00 77.74           N  
ANISOU 2769  N   TYR A 440    10261  10536   8739     42    312    219       N  
ATOM   2770  CA  TYR A 440     175.465  26.775 546.567  1.00 64.66           C  
ANISOU 2770  CA  TYR A 440     8668   9051   6850    -35    299    153       C  
ATOM   2771  C   TYR A 440     174.622  27.818 547.286  1.00 68.86           C  
ANISOU 2771  C   TYR A 440     9355   9547   7263      2    423     18       C  
ATOM   2772  O   TYR A 440     174.500  27.786 548.516  1.00 97.26           O  
ANISOU 2772  O   TYR A 440    12988  13294  10672     -3    463      9       O  
ATOM   2773  CB  TYR A 440     176.913  27.260 546.422  1.00 65.37           C  
ANISOU 2773  CB  TYR A 440     8784   9185   6870   -191    187     57       C  
ATOM   2774  CG  TYR A 440     177.124  28.425 545.476  1.00 66.65           C  
ANISOU 2774  CG  TYR A 440     9068   9158   7100   -260    199    -94       C  
ATOM   2775  CD1 TYR A 440     177.037  29.738 545.925  1.00 65.87           C  
ANISOU 2775  CD1 TYR A 440     9159   8996   6873   -320    255   -275       C  
ATOM   2776  CD2 TYR A 440     177.440  28.211 544.140  1.00 59.84           C  
ANISOU 2776  CD2 TYR A 440     8147   8172   6418   -271    158    -56       C  
ATOM   2777  CE1 TYR A 440     177.241  30.803 545.065  1.00 59.98           C  
ANISOU 2777  CE1 TYR A 440     8545   8058   6186   -388    267   -402       C  
ATOM   2778  CE2 TYR A 440     177.646  29.269 543.275  1.00 52.95           C  
ANISOU 2778  CE2 TYR A 440     7401   7124   5593   -342    171   -180       C  
ATOM   2779  CZ  TYR A 440     177.546  30.563 543.742  1.00 53.52           C  
ANISOU 2779  CZ  TYR A 440     7666   7126   5544   -401    224   -347       C  
ATOM   2780  OH  TYR A 440     177.749  31.621 542.886  1.00 48.05           O  
ANISOU 2780  OH  TYR A 440     7120   6239   4897   -476    239   -460       O  
ATOM   2781  N   ALA A 441     174.028  28.737 546.525  1.00 60.82           N  
ANISOU 2781  N   ALA A 441     8436   8328   6346     47    488    -84       N  
ATOM   2782  CA  ALA A 441     173.268  29.823 547.134  1.00 66.76           C  
ANISOU 2782  CA  ALA A 441     9347   9018   6998     97    611   -230       C  
ATOM   2783  C   ALA A 441     171.929  29.328 547.666  1.00 68.27           C  
ANISOU 2783  C   ALA A 441     9470   9259   7211    250    736   -146       C  
ATOM   2784  O   ALA A 441     171.551  29.630 548.804  1.00 79.77           O  
ANISOU 2784  O   ALA A 441    10998  10814   8496    271    831   -209       O  
ATOM   2785  CB  ALA A 441     173.063  30.953 546.125  1.00 76.12           C  
ANISOU 2785  CB  ALA A 441    10666   9959   8296    113    635   -352       C  
ATOM   2786  N   LEU A 442     171.202  28.556 546.862  1.00 66.86           N  
ANISOU 2786  N   LEU A 442     9149   9020   7234    348    743     -9       N  
ATOM   2787  CA  LEU A 442     169.886  28.061 547.243  1.00 76.13           C  
ANISOU 2787  CA  LEU A 442    10231  10237   8457    481    863     76       C  
ATOM   2788  C   LEU A 442     169.945  26.894 548.223  1.00 91.85           C  
ANISOU 2788  C   LEU A 442    12117  12439  10343    456    869    221       C  
ATOM   2789  O   LEU A 442     168.898  26.317 548.536  1.00 92.88           O  
ANISOU 2789  O   LEU A 442    12152  12621  10518    543    970    316       O  
ATOM   2790  CB  LEU A 442     169.101  27.647 545.996  1.00 71.38           C  
ANISOU 2790  CB  LEU A 442     9512   9498   8109    574    852    169       C  
ATOM   2791  CG  LEU A 442     168.835  28.760 544.980  1.00 69.90           C  
ANISOU 2791  CG  LEU A 442     9430   9095   8036    626    850     53       C  
ATOM   2792  CD1 LEU A 442     167.972  28.254 543.835  1.00 73.98           C  
ANISOU 2792  CD1 LEU A 442     9817   9508   8783    720    829    159       C  
ATOM   2793  CD2 LEU A 442     168.191  29.960 545.656  1.00 62.16           C  
ANISOU 2793  CD2 LEU A 442     8590   8068   6959    709    981   -104       C  
ATOM   2794  N   CYS A 443     171.134  26.533 548.708  1.00 99.53           N  
ANISOU 2794  N   CYS A 443    13101  13536  11178    340    762    247       N  
ATOM   2795  CA  CYS A 443     171.287  25.448 549.666  1.00 99.39           C  
ANISOU 2795  CA  CYS A 443    13006  13714  11043    318    751    396       C  
ATOM   2796  C   CYS A 443     171.923  25.893 550.976  1.00 97.69           C  
ANISOU 2796  C   CYS A 443    12911  13667  10541    236    747    310       C  
ATOM   2797  O   CYS A 443     172.176  25.046 551.841  1.00 99.88           O  
ANISOU 2797  O   CYS A 443    13146  14119  10686    209    719    435       O  
ATOM   2798  CB  CYS A 443     172.118  24.311 549.055  1.00105.07           C  
ANISOU 2798  CB  CYS A 443    13598  14451  11873    276    605    552       C  
ATOM   2799  SG  CYS A 443     171.440  23.639 547.521  1.00110.54           S  
ANISOU 2799  SG  CYS A 443    14160  14958  12884    353    596    656       S  
ATOM   2800  N   ASN A 444     172.184  27.185 551.149  1.00 83.92           N  
ANISOU 2800  N   ASN A 444    11326  11871   8689    190    769    104       N  
ATOM   2801  CA  ASN A 444     172.792  27.718 552.360  1.00 82.76           C  
ANISOU 2801  CA  ASN A 444    11313  11874   8257     94    759     -7       C  
ATOM   2802  C   ASN A 444     171.780  28.596 553.084  1.00 76.68           C  
ANISOU 2802  C   ASN A 444    10680  11083   7371    165    945   -148       C  
ATOM   2803  O   ASN A 444     171.144  29.454 552.463  1.00 74.68           O  
ANISOU 2803  O   ASN A 444    10490  10644   7240    240   1031   -265       O  
ATOM   2804  CB  ASN A 444     174.055  28.516 552.031  1.00 81.04           C  
ANISOU 2804  CB  ASN A 444    11182  11618   7992    -48    627   -149       C  
ATOM   2805  CG  ASN A 444     174.802  28.965 553.270  1.00 77.40           C  
ANISOU 2805  CG  ASN A 444    10843  11334   7230   -172    583   -256       C  
ATOM   2806  OD1 ASN A 444     174.528  30.029 553.823  1.00 77.72           O  
ANISOU 2806  OD1 ASN A 444    11062  11339   7127   -194    676   -443       O  
ATOM   2807  ND2 ASN A 444     175.756  28.153 553.712  1.00 80.16           N  
ANISOU 2807  ND2 ASN A 444    11101  11875   7481   -251    437   -141       N  
ATOM   2808  N   ALA A 445     171.639  28.382 554.394  1.00 69.56           N  
ANISOU 2808  N   ALA A 445     9829  10373   6227    147   1009   -136       N  
ATOM   2809  CA  ALA A 445     170.626  29.103 555.160  1.00 67.24           C  
ANISOU 2809  CA  ALA A 445     9654  10080   5812    226   1210   -264       C  
ATOM   2810  C   ALA A 445     170.933  30.593 555.233  1.00 68.04           C  
ANISOU 2810  C   ALA A 445     9971  10066   5817    177   1235   -529       C  
ATOM   2811  O   ALA A 445     170.021  31.426 555.141  1.00 74.76           O  
ANISOU 2811  O   ALA A 445    10906  10780   6718    288   1393   -659       O  
ATOM   2812  CB  ALA A 445     170.508  28.509 556.563  1.00 53.70           C  
ANISOU 2812  CB  ALA A 445     7962   8609   3832    198   1270   -188       C  
ATOM   2813  N   THR A 446     172.208  30.951 555.404  1.00 58.02           N  
ANISOU 2813  N   THR A 446     8790   8844   4411     13   1081   -613       N  
ATOM   2814  CA  THR A 446     172.573  32.362 555.468  1.00 63.56           C  
ANISOU 2814  CA  THR A 446     9710   9422   5017    -64   1096   -868       C  
ATOM   2815  C   THR A 446     172.303  33.058 554.140  1.00 64.94           C  
ANISOU 2815  C   THR A 446     9904   9316   5456      0   1110   -934       C  
ATOM   2816  O   THR A 446     171.869  34.217 554.115  1.00 63.56           O  
ANISOU 2816  O   THR A 446     9907   8971   5271     44   1220  -1122       O  
ATOM   2817  CB  THR A 446     174.043  32.509 555.863  1.00 65.04           C  
ANISOU 2817  CB  THR A 446     9957   9736   5020   -277    910   -929       C  
ATOM   2818  OG1 THR A 446     174.352  31.579 556.908  1.00 70.02           O  
ANISOU 2818  OG1 THR A 446    10520  10639   5443   -321    852   -799       O  
ATOM   2819  CG2 THR A 446     174.319  33.919 556.361  1.00 63.92           C  
ANISOU 2819  CG2 THR A 446    10076   9517   4695   -379    953  -1206       C  
ATOM   2820  N   PHE A 447     172.546  32.365 553.025  1.00 64.00           N  
ANISOU 2820  N   PHE A 447     9614   9137   5568     12   1003   -779       N  
ATOM   2821  CA  PHE A 447     172.212  32.924 551.719  1.00 59.10           C  
ANISOU 2821  CA  PHE A 447     9005   8257   5193     82   1014   -814       C  
ATOM   2822  C   PHE A 447     170.707  33.093 551.560  1.00 60.13           C  
ANISOU 2822  C   PHE A 447     9118   8279   5450    293   1189   -808       C  
ATOM   2823  O   PHE A 447     170.250  34.060 550.941  1.00 70.61           O  
ANISOU 2823  O   PHE A 447    10556   9387   6887    371   1250   -923       O  
ATOM   2824  CB  PHE A 447     172.770  32.040 550.604  1.00 61.70           C  
ANISOU 2824  CB  PHE A 447     9151   8568   5722     49    869   -645       C  
ATOM   2825  CG  PHE A 447     174.172  32.389 550.193  1.00 64.22           C  
ANISOU 2825  CG  PHE A 447     9516   8874   6013   -137    716   -711       C  
ATOM   2826  CD1 PHE A 447     174.435  33.567 549.512  1.00 63.00           C  
ANISOU 2826  CD1 PHE A 447     9523   8507   5909   -196    717   -869       C  
ATOM   2827  CD2 PHE A 447     175.224  31.531 550.468  1.00 61.44           C  
ANISOU 2827  CD2 PHE A 447     9039   8717   5588   -252    573   -609       C  
ATOM   2828  CE1 PHE A 447     175.723  33.889 549.125  1.00 55.84           C  
ANISOU 2828  CE1 PHE A 447     8645   7594   4977   -386    588   -929       C  
ATOM   2829  CE2 PHE A 447     176.514  31.847 550.082  1.00 58.92           C  
ANISOU 2829  CE2 PHE A 447     8730   8403   5252   -424    439   -671       C  
ATOM   2830  CZ  PHE A 447     176.763  33.027 549.410  1.00 52.06           C  
ANISOU 2830  CZ  PHE A 447     8017   7332   4431   -501    451   -834       C  
ATOM   2831  N   LYS A 448     169.920  32.163 552.106  1.00 55.85           N  
ANISOU 2831  N   LYS A 448     8433   7888   4899    388   1272   -670       N  
ATOM   2832  CA  LYS A 448     168.468  32.285 552.027  1.00 67.32           C  
ANISOU 2832  CA  LYS A 448     9837   9271   6472    584   1445   -663       C  
ATOM   2833  C   LYS A 448     167.976  33.492 552.816  1.00 84.35           C  
ANISOU 2833  C   LYS A 448    12198  11374   8478    646   1609   -882       C  
ATOM   2834  O   LYS A 448     167.197  34.307 552.305  1.00 99.87           O  
ANISOU 2834  O   LYS A 448    14221  13149  10577    789   1703   -976       O  
ATOM   2835  CB  LYS A 448     167.803  31.005 552.535  1.00 74.75           C  
ANISOU 2835  CB  LYS A 448    10583  10404   7416    638   1506   -469       C  
ATOM   2836  CG  LYS A 448     168.093  29.769 551.701  1.00 71.53           C  
ANISOU 2836  CG  LYS A 448     9975  10018   7186    605   1368   -251       C  
ATOM   2837  CD  LYS A 448     167.515  28.523 552.353  1.00 75.97           C  
ANISOU 2837  CD  LYS A 448    10380  10765   7719    632   1432    -64       C  
ATOM   2838  CE  LYS A 448     167.892  27.269 551.584  1.00 78.11           C  
ANISOU 2838  CE  LYS A 448    10479  11045   8155    590   1291    144       C  
ATOM   2839  NZ  LYS A 448     167.386  27.303 550.184  1.00 79.32           N  
ANISOU 2839  NZ  LYS A 448    10539  11008   8591    669   1260    171       N  
ATOM   2840  N   LYS A 449     168.425  33.621 554.068  1.00 80.21           N  
ANISOU 2840  N   LYS A 449    11793  11013   7669    547   1641   -968       N  
ATOM   2841  CA  LYS A 449     168.014  34.759 554.885  1.00 84.40           C  
ANISOU 2841  CA  LYS A 449    12542  11496   8032    595   1803  -1194       C  
ATOM   2842  C   LYS A 449     168.477  36.074 554.271  1.00 82.06           C  
ANISOU 2842  C   LYS A 449    12456  10943   7780    559   1762  -1391       C  
ATOM   2843  O   LYS A 449     167.758  37.079 554.322  1.00 83.87           O  
ANISOU 2843  O   LYS A 449    12830  11008   8030    689   1909  -1551       O  
ATOM   2844  CB  LYS A 449     168.559  34.613 556.306  1.00 99.20           C  
ANISOU 2844  CB  LYS A 449    14520  13604   9569    463   1816  -1249       C  
ATOM   2845  CG  LYS A 449     168.173  35.757 557.231  1.00108.19           C  
ANISOU 2845  CG  LYS A 449    15903  14703  10502    499   1991  -1499       C  
ATOM   2846  CD  LYS A 449     168.891  35.667 558.566  1.00112.99           C  
ANISOU 2846  CD  LYS A 449    16640  15540  10751    333   1966  -1565       C  
ATOM   2847  CE  LYS A 449     168.505  36.825 559.473  1.00122.45           C  
ANISOU 2847  CE  LYS A 449    18102  16688  11734    365   2149  -1834       C  
ATOM   2848  NZ  LYS A 449     168.787  38.143 558.839  1.00123.89           N  
ANISOU 2848  NZ  LYS A 449    18488  16582  12003    352   2132  -2049       N  
ATOM   2849  N   THR A 450     169.675  36.087 553.680  1.00 81.28           N  
ANISOU 2849  N   THR A 450    12379  10803   7700    384   1569  -1378       N  
ATOM   2850  CA  THR A 450     170.169  37.312 553.062  1.00 69.56           C  
ANISOU 2850  CA  THR A 450    11102   9071   6258    321   1529  -1553       C  
ATOM   2851  C   THR A 450     169.367  37.661 551.813  1.00 61.10           C  
ANISOU 2851  C   THR A 450     9996   7747   5473    497   1566  -1516       C  
ATOM   2852  O   THR A 450     169.081  38.838 551.564  1.00 56.51           O  
ANISOU 2852  O   THR A 450     9616   6931   4926    563   1640  -1678       O  
ATOM   2853  CB  THR A 450     171.653  37.176 552.727  1.00 64.35           C  
ANISOU 2853  CB  THR A 450    10445   8454   5552     80   1322  -1538       C  
ATOM   2854  OG1 THR A 450     172.334  36.546 553.820  1.00 62.52           O  
ANISOU 2854  OG1 THR A 450    10173   8501   5080    -58   1257  -1509       O  
ATOM   2855  CG2 THR A 450     172.265  38.547 552.493  1.00 56.61           C  
ANISOU 2855  CG2 THR A 450     9729   7257   4525    -41   1304  -1758       C  
ATOM   2856  N   PHE A 451     168.994  36.654 551.018  1.00 53.03           N  
ANISOU 2856  N   PHE A 451     8729   6763   4655    576   1511  -1303       N  
ATOM   2857  CA  PHE A 451     168.138  36.897 549.860  1.00 52.10           C  
ANISOU 2857  CA  PHE A 451     8559   6434   4801    752   1537  -1252       C  
ATOM   2858  C   PHE A 451     166.796  37.475 550.291  1.00 70.06           C  
ANISOU 2858  C   PHE A 451    10874   8643   7101    981   1738  -1339       C  
ATOM   2859  O   PHE A 451     166.343  38.493 549.754  1.00 79.30           O  
ANISOU 2859  O   PHE A 451    12183   9572   8376   1103   1789  -1444       O  
ATOM   2860  CB  PHE A 451     167.930  35.602 549.072  1.00 55.16           C  
ANISOU 2860  CB  PHE A 451     8671   6909   5376    783   1446  -1013       C  
ATOM   2861  CG  PHE A 451     169.153  35.124 548.341  1.00 61.33           C  
ANISOU 2861  CG  PHE A 451     9408   7700   6193    600   1257   -930       C  
ATOM   2862  CD1 PHE A 451     170.194  35.990 548.052  1.00 65.44           C  
ANISOU 2862  CD1 PHE A 451    10117   8098   6651    445   1176  -1059       C  
ATOM   2863  CD2 PHE A 451     169.258  33.802 547.937  1.00 61.17           C  
ANISOU 2863  CD2 PHE A 451     9158   7810   6275    581   1168   -727       C  
ATOM   2864  CE1 PHE A 451     171.318  35.545 547.377  1.00 55.00           C  
ANISOU 2864  CE1 PHE A 451     8732   6799   5366    279   1017   -986       C  
ATOM   2865  CE2 PHE A 451     170.378  33.353 547.264  1.00 62.60           C  
ANISOU 2865  CE2 PHE A 451     9291   8001   6493    431   1009   -659       C  
ATOM   2866  CZ  PHE A 451     171.409  34.226 546.984  1.00 60.00           C  
ANISOU 2866  CZ  PHE A 451     9129   7566   6101    282    936   -788       C  
ATOM   2867  N   LYS A 452     166.146  36.830 551.264  1.00 62.87           N  
ANISOU 2867  N   LYS A 452     9844   7947   6096   1048   1859  -1292       N  
ATOM   2868  CA  LYS A 452     164.880  37.343 551.781  1.00 70.31           C  
ANISOU 2868  CA  LYS A 452    10805   8861   7049   1265   2072  -1382       C  
ATOM   2869  C   LYS A 452     165.031  38.772 552.288  1.00 74.78           C  
ANISOU 2869  C   LYS A 452    11681   9259   7473   1278   2168  -1643       C  
ATOM   2870  O   LYS A 452     164.143  39.609 552.086  1.00 74.51           O  
ANISOU 2870  O   LYS A 452    11721   9046   7544   1483   2296  -1743       O  
ATOM   2871  CB  LYS A 452     164.364  36.432 552.894  1.00 74.13           C  
ANISOU 2871  CB  LYS A 452    11140   9626   7399   1282   2194  -1303       C  
ATOM   2872  CG  LYS A 452     163.092  36.923 553.562  1.00 88.39           C  
ANISOU 2872  CG  LYS A 452    12953  11442   9189   1495   2441  -1406       C  
ATOM   2873  CD  LYS A 452     163.016  36.451 555.004  1.00 97.85           C  
ANISOU 2873  CD  LYS A 452    14154  12905  10121   1434   2573  -1421       C  
ATOM   2874  CE  LYS A 452     164.179  37.000 555.818  1.00 95.12           C  
ANISOU 2874  CE  LYS A 452    14075  12588   9480   1237   2518  -1583       C  
ATOM   2875  NZ  LYS A 452     164.129  36.561 557.240  1.00 81.50           N  
ANISOU 2875  NZ  LYS A 452    12374  11127   7466   1173   2637  -1597       N  
ATOM   2876  N   HIS A 453     166.155  39.070 552.943  1.00 79.20           N  
ANISOU 2876  N   HIS A 453    12426   9870   7797   1062   2104  -1758       N  
ATOM   2877  CA  HIS A 453     166.396  40.426 553.422  1.00 78.57           C  
ANISOU 2877  CA  HIS A 453    12665   9619   7571   1037   2183  -2019       C  
ATOM   2878  C   HIS A 453     166.602  41.402 552.270  1.00 73.01           C  
ANISOU 2878  C   HIS A 453    12115   8583   7041   1060   2112  -2086       C  
ATOM   2879  O   HIS A 453     166.290  42.591 552.403  1.00 71.20           O  
ANISOU 2879  O   HIS A 453    12128   8133   6791   1152   2223  -2279       O  
ATOM   2880  CB  HIS A 453     167.608  40.439 554.354  1.00 73.77           C  
ANISOU 2880  CB  HIS A 453    12199   9164   6667    770   2103  -2116       C  
ATOM   2881  CG  HIS A 453     167.886  41.775 554.967  1.00 72.47           C  
ANISOU 2881  CG  HIS A 453    12373   8843   6321    714   2185  -2398       C  
ATOM   2882  ND1 HIS A 453     169.161  42.202 555.274  1.00 79.78           N  
ANISOU 2882  ND1 HIS A 453    13482   9774   7057    444   2058  -2520       N  
ATOM   2883  CD2 HIS A 453     167.055  42.778 555.336  1.00 79.43           C  
ANISOU 2883  CD2 HIS A 453    13445   9553   7182    890   2383  -2588       C  
ATOM   2884  CE1 HIS A 453     169.103  43.411 555.802  1.00 88.31           C  
ANISOU 2884  CE1 HIS A 453    14865  10684   8003    442   2172  -2777       C  
ATOM   2885  NE2 HIS A 453     167.837  43.783 555.852  1.00 83.18           N  
ANISOU 2885  NE2 HIS A 453    14234   9919   7454    719   2374  -2824       N  
ATOM   2886  N   LEU A 454     167.118  40.925 551.135  1.00 71.81           N  
ANISOU 2886  N   LEU A 454    11843   8386   7058    981   1935  -1928       N  
ATOM   2887  CA  LEU A 454     167.356  41.810 550.001  1.00 78.23           C  
ANISOU 2887  CA  LEU A 454    12811   8891   8024    984   1863  -1973       C  
ATOM   2888  C   LEU A 454     166.090  42.073 549.196  1.00 75.70           C  
ANISOU 2888  C   LEU A 454    12422   8391   7949   1274   1939  -1913       C  
ATOM   2889  O   LEU A 454     165.932  43.169 548.646  1.00 73.84           O  
ANISOU 2889  O   LEU A 454    12398   7865   7794   1357   1960  -2016       O  
ATOM   2890  CB  LEU A 454     168.439  41.228 549.091  1.00 72.82           C  
ANISOU 2890  CB  LEU A 454    12032   8231   7406    778   1654  -1837       C  
ATOM   2891  CG  LEU A 454     169.874  41.244 549.621  1.00 63.29           C  
ANISOU 2891  CG  LEU A 454    10921   7138   5988    476   1545  -1915       C  
ATOM   2892  CD1 LEU A 454     170.829  40.655 548.594  1.00 54.44           C  
ANISOU 2892  CD1 LEU A 454     9676   6035   4974    313   1358  -1772       C  
ATOM   2893  CD2 LEU A 454     170.296  42.655 550.003  1.00 59.44           C  
ANISOU 2893  CD2 LEU A 454    10777   6445   5363    380   1597  -2167       C  
ATOM   2894  N   LEU A 455     165.186  41.100 549.111  1.00 72.21           N  
ANISOU 2894  N   LEU A 455    11693   8114   7629   1427   1974  -1746       N  
ATOM   2895  CA  LEU A 455     163.971  41.250 548.320  1.00 69.79           C  
ANISOU 2895  CA  LEU A 455    11278   7675   7566   1698   2024  -1673       C  
ATOM   2896  C   LEU A 455     162.787  41.774 549.127  1.00 75.00           C  
ANISOU 2896  C   LEU A 455    11957   8331   8210   1944   2248  -1791       C  
ATOM   2897  O   LEU A 455     161.668  41.803 548.605  1.00 77.42           O  
ANISOU 2897  O   LEU A 455    12122   8577   8718   2190   2302  -1724       O  
ATOM   2898  CB  LEU A 455     163.596  39.919 547.660  1.00 59.00           C  
ANISOU 2898  CB  LEU A 455     9576   6475   6365   1722   1932  -1428       C  
ATOM   2899  CG  LEU A 455     164.340  39.543 546.376  1.00 56.65           C  
ANISOU 2899  CG  LEU A 455     9239   6095   6191   1590   1724  -1295       C  
ATOM   2900  CD1 LEU A 455     165.670  38.872 546.679  1.00 57.81           C  
ANISOU 2900  CD1 LEU A 455     9377   6402   6185   1308   1610  -1261       C  
ATOM   2901  CD2 LEU A 455     163.476  38.658 545.488  1.00 52.02           C  
ANISOU 2901  CD2 LEU A 455     8372   5560   5832   1724   1670  -1094       C  
ATOM   2902  N   MET A 456     162.999  42.191 550.371  1.00 79.69           N  
ANISOU 2902  N   MET A 456    12715   8995   8568   1888   2379  -1968       N  
ATOM   2903  CA  MET A 456     161.926  42.733 551.187  1.00 84.13           C  
ANISOU 2903  CA  MET A 456    13315   9555   9096   2120   2614  -2102       C  
ATOM   2904  C   MET A 456     161.981  44.260 551.164  1.00 97.52           C  
ANISOU 2904  C   MET A 456    15360  10926  10768   2202   2685  -2331       C  
ATOM   2905  O   MET A 456     162.674  44.869 550.343  1.00 93.40           O  
ANISOU 2905  O   MET A 456    15020  10166  10302   2107   2549  -2352       O  
ATOM   2906  CB  MET A 456     162.006  42.176 552.612  1.00 94.33           C  
ANISOU 2906  CB  MET A 456    14569  11140  10131   2023   2736  -2151       C  
ATOM   2907  CG  MET A 456     163.231  42.610 553.398  1.00109.74           C  
ANISOU 2907  CG  MET A 456    16795  13106  11796   1763   2693  -2314       C  
ATOM   2908  SD  MET A 456     163.179  42.048 555.112  1.00106.49           S  
ANISOU 2908  SD  MET A 456    16365  13035  11062   1682   2849  -2377       S  
ATOM   2909  CE  MET A 456     161.678  42.840 555.683  1.00 80.93           C  
ANISOU 2909  CE  MET A 456    13174   9717   7859   2017   3162  -2541       C  
ATOM   2910  N   CYS A 457     161.237  44.893 552.075  1.00123.10           N  
ANISOU 2910  N   CYS A 457    18693  14152  13926   2373   2901  -2501       N  
ATOM   2911  CA  CYS A 457     161.168  46.351 552.090  1.00126.96           C  
ANISOU 2911  CA  CYS A 457    19405  14374  14460   2413   2901  -2666       C  
ATOM   2912  C   CYS A 457     162.487  46.969 552.542  1.00128.64           C  
ANISOU 2912  C   CYS A 457    19910  14515  14454   2112   2812  -2818       C  
ATOM   2913  O   CYS A 457     162.892  48.020 552.033  1.00136.02           O  
ANISOU 2913  O   CYS A 457    21049  15179  15455   2057   2723  -2890       O  
ATOM   2914  CB  CYS A 457     160.024  46.811 552.993  1.00132.62           C  
ANISOU 2914  CB  CYS A 457    20053  15154  15183   2626   3100  -2776       C  
ATOM   2915  SG  CYS A 457     158.400  46.181 552.512  1.00137.91           S  
ANISOU 2915  SG  CYS A 457    20340  15930  16129   2970   3201  -2607       S  
ATOM   2916  N   HIS A 458     163.167  46.336 553.492  1.00122.11           N  
ANISOU 2916  N   HIS A 458    19095  13936  13365   1906   2827  -2858       N  
ATOM   2917  CA  HIS A 458     164.432  46.854 553.999  1.00110.60           C  
ANISOU 2917  CA  HIS A 458    17875  12457  11692   1603   2726  -2997       C  
ATOM   2918  C   HIS A 458     165.614  46.126 553.367  1.00113.86           C  
ANISOU 2918  C   HIS A 458    18279  12925  12057   1355   2542  -2888       C  
ATOM   2919  O   HIS A 458     166.205  46.604 552.399  1.00112.64           O  
ANISOU 2919  O   HIS A 458    18228  12551  12019   1263   2405  -2867       O  
ATOM   2920  CB  HIS A 458     164.488  46.731 555.523  1.00100.20           C  
ANISOU 2920  CB  HIS A 458    16586  11388  10097   1517   2834  -3124       C  
ATOM   2921  CG  HIS A 458     165.747  47.267 556.129  1.00 97.18           C  
ANISOU 2921  CG  HIS A 458    16423  11012   9490   1209   2720  -3269       C  
ATOM   2922  ND1 HIS A 458     166.900  46.519 556.236  1.00 76.90           N  
ANISOU 2922  ND1 HIS A 458    13837   8628   6755    935   2571  -3209       N  
ATOM   2923  CD2 HIS A 458     166.033  48.476 556.669  1.00 97.04           C  
ANISOU 2923  CD2 HIS A 458    16631  10847   9392   1133   2726  -3468       C  
ATOM   2924  CE1 HIS A 458     167.842  47.244 556.811  1.00 91.60           C  
ANISOU 2924  CE1 HIS A 458    15888  10467   8450    701   2482  -3362       C  
ATOM   2925  NE2 HIS A 458     167.342  48.436 557.084  1.00 93.63           N  
ANISOU 2925  NE2 HIS A 458    16303  10519   8754    813   2578  -3522       N  
TER    2926      HIS A 458                                                      
HETATM 2927  C10 3C0 A 501     187.885  24.340 525.974  1.00 37.45           C  
HETATM 2928  C13 3C0 A 501     183.918  26.952 524.854  1.00 43.91           C  
HETATM 2929  C15 3C0 A 501     183.412  29.472 524.621  1.00 41.85           C  
HETATM 2930  C17 3C0 A 501     184.674  29.179 526.642  1.00 42.24           C  
HETATM 2931  C20 3C0 A 501     182.141  30.804 526.283  1.00 47.88           C  
HETATM 2932  C21 3C0 A 501     181.148  28.921 525.374  1.00 56.87           C  
HETATM 2933  C22 3C0 A 501     183.227  28.618 526.686  1.00 44.48           C  
HETATM 2934  N19 3C0 A 501     182.466  29.465 525.749  1.00 47.53           N  
HETATM 2935  C14 3C0 A 501     183.459  28.093 523.919  1.00 47.67           C  
HETATM 2936  C16 3C0 A 501     184.796  29.771 525.261  1.00 43.54           C  
HETATM 2937  O18 3C0 A 501     184.918  30.608 526.458  1.00 57.54           O  
HETATM 2938  C23 3C0 A 501     183.255  27.146 526.237  1.00 38.87           C  
HETATM 2939  O12 3C0 A 501     185.370  26.858 524.900  1.00 43.59           O  
HETATM 2940  C02 3C0 A 501     185.871  25.746 525.504  1.00 31.52           C  
HETATM 2941  O01 3C0 A 501     185.203  24.792 525.901  1.00 33.77           O  
HETATM 2942  C03 3C0 A 501     187.395  25.748 525.637  1.00 27.63           C  
HETATM 2943  O11 3C0 A 501     187.385  23.423 524.996  1.00 38.53           O  
HETATM 2944  C04 3C0 A 501     187.780  26.646 526.627  1.00 30.87           C  
HETATM 2945  C05 3C0 A 501     188.343  27.866 526.268  1.00 28.17           C  
HETATM 2946  C06 3C0 A 501     188.729  28.771 527.250  1.00 32.41           C  
HETATM 2947  C07 3C0 A 501     188.552  28.456 528.593  1.00 30.84           C  
HETATM 2948  C08 3C0 A 501     187.988  27.237 528.952  1.00 37.08           C  
HETATM 2949  C09 3C0 A 501     187.601  26.331 527.970  1.00 41.19           C  
HETATM 2950  O   HOH A 601     181.924  33.442 522.358  1.00 56.17           O  
HETATM 2951  O   HOH A 602     196.704  13.303 549.184  1.00 41.60           O  
HETATM 2952  O   HOH A 603     177.740  31.752 540.377  1.00 55.10           O  
HETATM 2953  O   HOH A 604     177.996  22.059 525.840  1.00 28.67           O  
CONECT  625 1266                                                                
CONECT 1266  625                                                                
CONECT 2565 2583                                                                
CONECT 2583 2565                                                                
CONECT 2927 2942 2943                                                           
CONECT 2928 2935 2938 2939                                                      
CONECT 2929 2934 2935 2936                                                      
CONECT 2930 2933 2936 2937                                                      
CONECT 2931 2934                                                                
CONECT 2932 2934                                                                
CONECT 2933 2930 2934 2938                                                      
CONECT 2934 2929 2931 2932 2933                                                 
CONECT 2935 2928 2929                                                           
CONECT 2936 2929 2930 2937                                                      
CONECT 2937 2930 2936                                                           
CONECT 2938 2928 2933                                                           
CONECT 2939 2928 2940                                                           
CONECT 2940 2939 2941 2942                                                      
CONECT 2941 2940                                                                
CONECT 2942 2927 2940 2944                                                      
CONECT 2943 2927                                                                
CONECT 2944 2942 2945 2949                                                      
CONECT 2945 2944 2946                                                           
CONECT 2946 2945 2947                                                           
CONECT 2947 2946 2948                                                           
CONECT 2948 2947 2949                                                           
CONECT 2949 2944 2948                                                           
MASTER      329    0    1   19    0    0    3    6 2946    1   27   33          
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.