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***  TRANSFERASE/TRANSFERASE INHIBITOR 19-JUL-18 6E53  ***

elNémo ID: 200108194856145710

Job options:

ID        	=	 200108194856145710
JOBID     	=	 TRANSFERASE/TRANSFERASE INHIBITOR 19-JUL-18 6E53
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       19-JUL-18   6E53              
TITLE     STRUCTURE OF TERT IN COMPLEX WITH A NOVEL TELOMERASE INHIBITOR        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TELOMERASE REVERSE TRANSCRIPTASE;                          
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 2.7.7.49;                                                        
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: RNA/DNA HAIRPIN;                                           
COMPND   8 CHAIN: E;                                                            
COMPND   9 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: TRIBOLIUM CASTANEUM;                            
SOURCE   3 ORGANISM_COMMON: RED FLOUR BEETLE;                                   
SOURCE   4 ORGANISM_TAXID: 7070;                                                
SOURCE   5 GENE: TERT, TCASGA2_TC010963;                                        
SOURCE   6 EXPRESSION_SYSTEM: TRIBOLIUM CASTANEUM;                              
SOURCE   7 EXPRESSION_SYSTEM_COMMON: RED FLOUR BEETLE;                          
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7070;                                       
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: TRIBOLIUM CASTANEUM;                            
SOURCE  11 ORGANISM_COMMON: RED FLOUR BEETLE;                                   
SOURCE  12 ORGANISM_TAXID: 7070;                                                
SOURCE  13 EXPRESSION_SYSTEM: TRIBOLIUM CASTANEUM;                              
SOURCE  14 EXPRESSION_SYSTEM_COMMON: RED FLOUR BEETLE;                          
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 7070                                        
KEYWDS    TELOMERASE, CATALYTIC SUBUNIT, TELOMERASE INHIBITOR, TRANSFERASE-     
KEYWDS   2 TRANSFERASE INHIBITOR COMPLEX                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    W.HERNANDEZ-SANCHEZ,W.HUANG,B.PLUCINSKY,N.GARCIA-VAZQUEZ,A.J.BERDIS,  
AUTHOR   2 E.SKORDALAKES,D.J.TAYLOR                                             
REVDAT   3   04-DEC-19 6E53    1       REMARK                                   
REVDAT   2   09-OCT-19 6E53    1       JRNL                                     
REVDAT   1   27-MAR-19 6E53    0                                                
JRNL        AUTH   W.HERNANDEZ-SANCHEZ,W.HUANG,B.PLUCINSKY,N.GARCIA-VAZQUEZ,    
JRNL        AUTH 2 N.J.ROBINSON,W.P.SCHIEMANN,A.J.BERDIS,E.SKORDALAKES,         
JRNL        AUTH 3 D.J.TAYLOR                                                   
JRNL        TITL   A NON-NATURAL NUCLEOTIDE USES A SPECIFIC POCKET TO           
JRNL        TITL 2 SELECTIVELY INHIBIT TELOMERASE ACTIVITY.                     
JRNL        REF    PLOS BIOL.                    V.  17 00204 2019              
JRNL        REFN                   ESSN 1545-7885                               
JRNL        PMID   30951520                                                     
JRNL        DOI    10.1371/JOURNAL.PBIO.3000204                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.13_2998: ???)                              
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 : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.99                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 20452                          
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) : 0.230                           
REMARK   3   FREE R VALUE                     : 0.288                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1022                            
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 19.9861 -  5.3271    1.00     2856   150  0.2009 0.2725        
REMARK   3     2  5.3271 -  4.2416    1.00     2798   147  0.2050 0.2356        
REMARK   3     3  4.2416 -  3.7093    1.00     2752   145  0.2187 0.2872        
REMARK   3     4  3.7093 -  3.3719    1.00     2788   147  0.2349 0.2856        
REMARK   3     5  3.3719 -  3.1312    1.00     2753   145  0.2637 0.3040        
REMARK   3     6  3.1312 -  2.9472    1.00     2763   144  0.2980 0.4300        
REMARK   3     7  2.9472 -  2.8000    1.00     2720   144  0.3450 0.3894        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
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)     : 0.460            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 32.320           
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      :  0.005           5679                                  
REMARK   3   ANGLE     :  0.885           7767                                  
REMARK   3   CHIRALITY :  0.049            851                                  
REMARK   3   PLANARITY :  0.006            882                                  
REMARK   3   DIHEDRAL  :  7.926           3341                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: ALL                                                    
REMARK   3    ORIGIN FOR THE GROUP (A):   1.6028  -6.9832 125.0397              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2824 T22:   0.2874                                     
REMARK   3      T33:   0.2783 T12:  -0.0399                                     
REMARK   3      T13:  -0.0490 T23:   0.1040                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9232 L22:   1.8732                                     
REMARK   3      L33:   2.9752 L12:  -0.0918                                     
REMARK   3      L13:  -1.6687 L23:   0.5319                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1372 S12:  -0.5535 S13:  -0.1795                       
REMARK   3      S21:   0.1194 S22:  -0.1342 S23:   0.1043                       
REMARK   3      S31:   0.1254 S32:  -0.3934 S33:  -0.0799                       
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 6E53 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-JUL-18.                  
REMARK 100 THE DEPOSITION ID IS D_1000235728.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-JUN-18                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU MICROMAX-007 HF             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54178                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU SATURN 944+                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 20467                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : 20.00                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 13.2600                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.87                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 18.00                              
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: PDB ENTRY 3KYL                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.84                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.66                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES, PH 7.5, 8% PEG8000, 0.1 M   
REMARK 280  POTASSIUM CHLORIDE, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE      
REMARK 280  291K                                                                
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       26.05000            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2650 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 31950 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, E                                  
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 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500     DT E  21   O3'    DT E  21   C3'    -0.037                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    GLN A  47   N   -  CA  -  C   ANGL. DEV. = -16.4 DEGREES          
REMARK 500     DT E  16   O4' -  C1' -  N1  ANGL. DEV. =   1.8 DEGREES          
REMARK 500     DA E  23   O4' -  C1' -  N9  ANGL. DEV. =   2.1 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A  20     -166.11   -105.32                                   
REMARK 500    LYS A  39       31.15    -87.51                                   
REMARK 500    LYS A  44      -69.08   -142.64                                   
REMARK 500    HIS A  92       -0.80   -144.59                                   
REMARK 500    ILE A 126      -46.31   -131.26                                   
REMARK 500    LEU A 141       -1.63     66.36                                   
REMARK 500    GLN A 175       59.30     39.37                                   
REMARK 500    GLU A 177       43.78     34.47                                   
REMARK 500    LYS A 189      -88.06   -105.71                                   
REMARK 500    GLN A 190      -81.36   -132.76                                   
REMARK 500    PRO A 201       83.27    -62.06                                   
REMARK 500    SER A 227       41.48    -87.51                                   
REMARK 500    SER A 229      135.73   -173.66                                   
REMARK 500    ASN A 290       50.97   -109.95                                   
REMARK 500    ARG A 296     -115.46     52.32                                   
REMARK 500    THR A 341      -78.69   -115.70                                   
REMARK 500    VAL A 342      -87.33   -120.48                                   
REMARK 500    PHE A 448       69.73   -115.82                                   
REMARK 500    VAL A 456      -61.89    -99.25                                   
REMARK 500    SER A 488      -50.05   -132.54                                   
REMARK 500    ASN A 492      -70.05    -90.30                                   
REMARK 500    PHE A 494       32.60    -96.72                                   
REMARK 500    TYR A 519       53.03   -110.30                                   
REMARK 500    ARG A 525      -58.84   -121.70                                   
REMARK 500    LYS A 526      136.58   -175.46                                   
REMARK 500    ILE A 550      -69.35   -137.73                                   
REMARK 500    TYR A 551       24.21    -76.87                                   
REMARK 500    HIS A 569       56.19    -93.07                                   
REMARK 500    CYS A 579      -33.20   -136.14                                   
REMARK 500    ARG A 592       78.48   -110.86                                   
REMARK 500    ALA A 594      109.96    -49.79                                   
REMARK 500    SER A 595      -74.37    -78.74                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 601  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 251   OD1                                                    
REMARK 620 2 ASP A 251   OD2  52.8                                              
REMARK 620 3 ILE A 252   O   117.2  86.9                                        
REMARK 620 4 HUV A 603   O1G 109.4  67.8  91.2                                  
REMARK 620 5 HUV A 603   O1A  77.1  98.5 164.5  77.6                            
REMARK 620 6 HUV A 603   O2B 149.9 136.9  92.8  69.2  73.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 602  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 251   OD1                                                    
REMARK 620 2 ASP A 343   OD1  60.4                                              
REMARK 620 3 ASP A 344   OD1  63.0  69.2                                        
REMARK 620 4 ASP A 344   OD2 108.4  78.0  48.1                                  
REMARK 620 5  DA E  23   O3' 134.6  76.3 115.5  72.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 602                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HUV A 603                 
DBREF  6E53 A    1   596  UNP    Q0QHL8   Q0QHL8_TRICA     1    596             
DBREF  6E53 E    1    23  PDB    6E53     6E53             1     23             
SEQRES   1 A  596  MET VAL HIS TYR TYR ARG LEU SER LEU LYS SER ARG GLN          
SEQRES   2 A  596  LYS ALA PRO LYS ILE VAL ASN SER LYS TYR ASN SER ILE          
SEQRES   3 A  596  LEU ASN ILE ALA LEU LYS ASN PHE ARG LEU CYS LYS LYS          
SEQRES   4 A  596  HIS LYS THR LYS LYS PRO VAL GLN ILE LEU ALA LEU LEU          
SEQRES   5 A  596  GLN GLU ILE ILE PRO LYS SER TYR PHE GLY THR THR THR          
SEQRES   6 A  596  ASN LEU LYS ARG PHE TYR LYS VAL VAL GLU LYS ILE LEU          
SEQRES   7 A  596  THR GLN SER SER PHE GLU CYS ILE HIS LEU SER VAL LEU          
SEQRES   8 A  596  HIS LYS CYS TYR ASP TYR ASP ALA ILE PRO TRP LEU GLN          
SEQRES   9 A  596  ASN VAL GLU PRO ASN LEU ARG PRO LYS LEU LEU LEU LYS          
SEQRES  10 A  596  HIS ASN LEU PHE LEU LEU ASP ASN ILE VAL LYS PRO ILE          
SEQRES  11 A  596  ILE ALA PHE TYR TYR LYS PRO ILE LYS THR LEU ASN GLY          
SEQRES  12 A  596  HIS GLU ILE LYS PHE ILE ARG LYS GLU GLU TYR ILE SER          
SEQRES  13 A  596  PHE GLU SER LYS VAL PHE HIS LYS LEU LYS LYS MET LYS          
SEQRES  14 A  596  TYR LEU VAL GLU VAL GLN ASP GLU VAL LYS PRO ARG GLY          
SEQRES  15 A  596  VAL LEU ASN ILE ILE PRO LYS GLN ASP ASN PHE ARG ALA          
SEQRES  16 A  596  ILE VAL SER ILE PHE PRO ASP SER ALA ARG LYS PRO PHE          
SEQRES  17 A  596  PHE LYS LEU LEU THR SER LYS ILE TYR LYS VAL LEU GLU          
SEQRES  18 A  596  GLU LYS TYR LYS THR SER GLY SER LEU TYR THR CYS TRP          
SEQRES  19 A  596  SER GLU PHE THR GLN LYS THR GLN GLY GLN ILE TYR GLY          
SEQRES  20 A  596  ILE LYS VAL ASP ILE ARG ASP ALA TYR GLY ASN VAL LYS          
SEQRES  21 A  596  ILE PRO VAL LEU CYS LYS LEU ILE GLN SER ILE PRO THR          
SEQRES  22 A  596  HIS LEU LEU ASP SER GLU LYS LYS ASN PHE ILE VAL ASP          
SEQRES  23 A  596  HIS ILE SER ASN GLN PHE VAL ALA PHE ARG ARG LYS ILE          
SEQRES  24 A  596  TYR LYS TRP ASN HIS GLY LEU LEU GLN GLY ASP PRO LEU          
SEQRES  25 A  596  SER GLY CYS LEU CYS GLU LEU TYR MET ALA PHE MET ASP          
SEQRES  26 A  596  ARG LEU TYR PHE SER ASN LEU ASP LYS ASP ALA PHE ILE          
SEQRES  27 A  596  HIS ARG THR VAL ASP ASP TYR PHE PHE CYS SER PRO HIS          
SEQRES  28 A  596  PRO HIS LYS VAL TYR ASP PHE GLU LEU LEU ILE LYS GLY          
SEQRES  29 A  596  VAL TYR GLN VAL ASN PRO THR LYS THR ARG THR ASN LEU          
SEQRES  30 A  596  PRO THR HIS ARG HIS PRO GLN ASP GLU ILE PRO TYR CYS          
SEQRES  31 A  596  GLY LYS ILE PHE ASN LEU THR THR ARG GLN VAL ARG THR          
SEQRES  32 A  596  LEU TYR LYS LEU PRO PRO ASN TYR GLU ILE ARG HIS LYS          
SEQRES  33 A  596  PHE LYS LEU TRP ASN PHE ASN ASN GLN ILE SER ASP ASP          
SEQRES  34 A  596  ASN PRO ALA ARG PHE LEU GLN LYS ALA MET ASP PHE PRO          
SEQRES  35 A  596  PHE ILE CYS ASN SER PHE THR LYS PHE GLU PHE ASN THR          
SEQRES  36 A  596  VAL PHE ASN ASP GLN ARG THR VAL PHE ALA ASN PHE TYR          
SEQRES  37 A  596  ASP ALA MET ILE CYS VAL ALA TYR LYS PHE ASP ALA ALA          
SEQRES  38 A  596  MET MET ALA LEU ARG THR SER PHE LEU VAL ASN ASP PHE          
SEQRES  39 A  596  GLY PHE ILE TRP LEU VAL LEU SER SER THR VAL ARG ALA          
SEQRES  40 A  596  TYR ALA SER ARG ALA PHE LYS LYS ILE VAL THR TYR LYS          
SEQRES  41 A  596  GLY GLY LYS TYR ARG LYS VAL THR PHE GLN CYS LEU LYS          
SEQRES  42 A  596  SER ILE ALA TRP ARG ALA PHE LEU ALA VAL LEU LYS ARG          
SEQRES  43 A  596  ARG THR GLU ILE TYR LYS GLY LEU ILE ASP ARG ILE LYS          
SEQRES  44 A  596  SER ARG GLU LYS LEU THR MET LYS PHE HIS ASP GLY GLU          
SEQRES  45 A  596  VAL ASP ALA SER TYR PHE CYS LYS LEU PRO GLU LYS PHE          
SEQRES  46 A  596  ARG PHE VAL LYS ILE ASN ARG LYS ALA SER ILE                  
SEQRES   1 E   23    C   U   G   A   C   C   U   G   A   C  DT  DT  DC          
SEQRES   2 E   23   DG  DG  DT  DC  DA  DG  DG  DT  DC  DA                      
HET     MG  A 601       1                                                       
HET     MG  A 602       1                                                       
HET    HUV  A 603      33                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     HUV METHYL 1-{2-DEOXY-5-O-[(S)-HYDROXY{[(S)-                         
HETNAM   2 HUV  HYDROXY(PHOSPHONOOXY)PHOSPHORYL]OXY}PHOSPHORYL]-ALPHA-          
HETNAM   3 HUV  D-ERYTHRO-PENTOFURANOSYL}-1H-INDOLE-5-CARBOXYLATE               
FORMUL   3   MG    2(MG 2+)                                                     
FORMUL   5  HUV    C15 H20 N O14 P3                                             
HELIX    1 AA1 SER A    8  ARG A   12  5                                   5    
HELIX    2 AA2 ILE A   26  LYS A   39  1                                  14    
HELIX    3 AA3 GLN A   47  ILE A   56  1                                  10    
HELIX    4 AA4 PRO A   57  PHE A   61  5                                   5    
HELIX    5 AA5 THR A   63  THR A   79  1                                  17    
HELIX    6 AA6 SER A   89  HIS A   92  5                                   4    
HELIX    7 AA7 LEU A  110  ILE A  126  1                                  17    
HELIX    8 AA8 ILE A  126  TYR A  134  1                                   9    
HELIX    9 AA9 LYS A  151  MET A  168  1                                  18    
HELIX   10 AB1 ARG A  205  TYR A  224  1                                  20    
HELIX   11 AB2 SER A  229  THR A  241  1                                  13    
HELIX   12 AB3 LYS A  260  SER A  270  1                                  11    
HELIX   13 AB4 ASP A  277  ASN A  290  1                                  14    
HELIX   14 AB5 LEU A  312  PHE A  329  1                                  18    
HELIX   15 AB6 HIS A  351  TYR A  366  1                                  16    
HELIX   16 AB7 ASN A  369  THR A  373  5                                   5    
HELIX   17 AB8 GLU A  412  PHE A  417  5                                   6    
HELIX   18 AB9 ASN A  430  MET A  439  1                                  10    
HELIX   19 AC1 PHE A  441  ASN A  446  1                                   6    
HELIX   20 AC2 THR A  449  ASN A  454  1                                   6    
HELIX   21 AC3 ASP A  459  SER A  488  1                                  30    
HELIX   22 AC4 PHE A  494  TYR A  519  1                                  26    
HELIX   23 AC5 THR A  528  LYS A  545  1                                  18    
HELIX   24 AC6 ARG A  546  THR A  548  5                                   3    
HELIX   25 AC7 TYR A  551  GLU A  562  1                                  12    
HELIX   26 AC8 ALA A  575  CYS A  579  5                                   5    
SHEET    1 AA1 2 TYR A   4  ARG A   6  0                                        
SHEET    2 AA1 2 CYS A  85  HIS A  87 -1  O  ILE A  86   N  TYR A   5           
SHEET    1 AA2 2 TYR A 135  LYS A 139  0                                        
SHEET    2 AA2 2 ILE A 146  ARG A 150 -1  O  ILE A 149   N  LYS A 136           
SHEET    1 AA3 5 LEU A 171  GLU A 173  0                                        
SHEET    2 AA3 5 ILE A 299  TRP A 302 -1  O  LYS A 301   N  VAL A 172           
SHEET    3 AA3 5 PHE A 292  ALA A 294 -1  N  VAL A 293   O  TYR A 300           
SHEET    4 AA3 5 GLY A 182  PRO A 188  1  N  LEU A 184   O  ALA A 294           
SHEET    5 AA3 5 PHE A 193  ILE A 199 -1  O  ILE A 196   N  ASN A 185           
SHEET    1 AA4 4 PHE A 337  ARG A 340  0                                        
SHEET    2 AA4 4 ASP A 344  SER A 349 -1  O  CYS A 348   N  PHE A 337           
SHEET    3 AA4 4 TYR A 246  ASP A 251 -1  N  ILE A 248   O  PHE A 347           
SHEET    4 AA4 4 ARG A 374  THR A 375 -1  O  ARG A 374   N  LYS A 249           
SHEET    1 AA5 3 GLU A 386  TYR A 389  0                                        
SHEET    2 AA5 3 LYS A 392  ASN A 395 -1  O  PHE A 394   N  ILE A 387           
SHEET    3 AA5 3 VAL A 401  THR A 403 -1  O  ARG A 402   N  ILE A 393           
LINK         OD1 ASP A 251                MG    MG A 601     1555   1555  2.62  
LINK         OD1 ASP A 251                MG    MG A 602     1555   1555  2.50  
LINK         OD2 ASP A 251                MG    MG A 601     1555   1555  2.24  
LINK         O   ILE A 252                MG    MG A 601     1555   1555  2.30  
LINK         OD1 ASP A 343                MG    MG A 602     1555   1555  2.74  
LINK         OD1 ASP A 344                MG    MG A 602     1555   1555  2.88  
LINK         OD2 ASP A 344                MG    MG A 602     1555   1555  2.41  
LINK         O3'  DA E  23                MG    MG A 602     1555   1555  2.61  
LINK        MG    MG A 601                 O1G HUV A 603     1555   1555  2.54  
LINK        MG    MG A 601                 O1A HUV A 603     1555   1555  2.11  
LINK        MG    MG A 601                 O2B HUV A 603     1555   1555  2.23  
SITE     1 AC1  4 ASP A 251  ILE A 252  ASP A 343  HUV A 603                    
SITE     1 AC2  5 ASP A 251  ASP A 343  ASP A 344  HUV A 603                    
SITE     2 AC2  5  DA E  23                                                     
SITE     1 AC3 19 LEU A 141  ILE A 187  LYS A 189  ARG A 194                    
SITE     2 AC3 19 ILE A 196  ASP A 251  ILE A 252  ARG A 253                    
SITE     3 AC3 19 ASP A 254  ALA A 255  TYR A 256  GLN A 308                    
SITE     4 AC3 19 GLY A 309  ASP A 343  LYS A 372   MG A 601                    
SITE     5 AC3 19  MG A 602    U E   2   DA E  23                               
CRYST1   80.020   52.100  100.480  90.00  98.45  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      0.012497  0.000000  0.001858        0.00000                         
SCALE2      0.000000  0.019194  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010062        0.00000                         
ATOM      1  N   MET A   1     -15.241 -18.215 145.127  1.00 98.39           N  
ANISOU    1  N   MET A   1    11918  14707  10758  -2922   2612   2625       N  
ATOM      2  CA  MET A   1     -13.848 -17.816 144.989  1.00112.41           C  
ANISOU    2  CA  MET A   1    13828  16474  12410  -2733   2372   2702       C  
ATOM      3  C   MET A   1     -13.633 -17.025 143.705  1.00106.73           C  
ANISOU    3  C   MET A   1    12949  15773  11829  -2694   2154   2501       C  
ATOM      4  O   MET A   1     -12.499 -16.790 143.289  1.00100.56           O  
ANISOU    4  O   MET A   1    12257  14930  11020  -2556   1954   2551       O  
ATOM      5  CB  MET A   1     -12.935 -19.042 145.023  1.00119.71           C  
ANISOU    5  CB  MET A   1    15018  17090  13375  -2676   2390   2971       C  
ATOM      6  CG  MET A   1     -13.091 -19.962 143.832  1.00119.28           C  
ANISOU    6  CG  MET A   1    14965  16712  13646  -2778   2425   2961       C  
ATOM      7  SD  MET A   1     -11.627 -20.974 143.544  1.00118.59           S  
ANISOU    7  SD  MET A   1    15175  16278  13606  -2626   2342   3206       S  
ATOM      8  CE  MET A   1     -10.398 -19.707 143.249  1.00121.46           C  
ANISOU    8  CE  MET A   1    15493  16843  13813  -2410   1987   3134       C  
ATOM      9  N   VAL A   2     -14.729 -16.622 143.072  1.00103.78           N  
ANISOU    9  N   VAL A   2    12333  15491  11607  -2807   2198   2276       N  
ATOM     10  CA  VAL A   2     -14.685 -15.675 141.965  1.00 87.95           C  
ANISOU   10  CA  VAL A   2    10153  13570   9696  -2752   2013   2066       C  
ATOM     11  C   VAL A   2     -15.092 -14.307 142.510  1.00101.55           C  
ANISOU   11  C   VAL A   2    11720  15618  11247  -2674   2011   1886       C  
ATOM     12  O   VAL A   2     -16.202 -14.125 143.029  1.00114.61           O  
ANISOU   12  O   VAL A   2    13232  17427  12886  -2753   2174   1780       O  
ATOM     13  CB  VAL A   2     -15.561 -16.135 140.780  1.00 75.72           C  
ANISOU   13  CB  VAL A   2     8428  11908   8434  -2897   2038   1921       C  
ATOM     14  CG1 VAL A   2     -15.274 -17.597 140.453  1.00 79.79           C  
ANISOU   14  CG1 VAL A   2     9117  12082   9119  -2996   2108   2089       C  
ATOM     15  CG2 VAL A   2     -17.064 -15.947 141.016  1.00 81.01           C  
ANISOU   15  CG2 VAL A   2     8857  12763   9159  -3022   2204   1743       C  
ATOM     16  N   HIS A   3     -14.157 -13.363 142.462  1.00 93.69           N  
ANISOU   16  N   HIS A   3    10764  14715  10119  -2514   1843   1853       N  
ATOM     17  CA  HIS A   3     -14.403 -12.001 142.911  1.00 97.57           C  
ANISOU   17  CA  HIS A   3    11132  15480  10460  -2420   1845   1662       C  
ATOM     18  C   HIS A   3     -14.556 -11.026 141.758  1.00 92.68           C  
ANISOU   18  C   HIS A   3    10324  14916   9974  -2339   1735   1450       C  
ATOM     19  O   HIS A   3     -15.255 -10.020 141.905  1.00 95.96           O  
ANISOU   19  O   HIS A   3    10568  15529  10362  -2281   1798   1247       O  
ATOM     20  CB  HIS A   3     -13.265 -11.519 143.821  1.00107.08           C  
ANISOU   20  CB  HIS A   3    12512  16775  11400  -2295   1764   1740       C  
ATOM     21  CG  HIS A   3     -13.005 -12.407 144.998  1.00105.41           C  
ANISOU   21  CG  HIS A   3    12489  16538  11023  -2331   1853   1962       C  
ATOM     22  ND1 HIS A   3     -11.956 -13.299 145.036  1.00102.12           N  
ANISOU   22  ND1 HIS A   3    12278  15935  10587  -2286   1762   2201       N  
ATOM     23  CD2 HIS A   3     -13.646 -12.530 146.185  1.00104.26           C  
ANISOU   23  CD2 HIS A   3    12360  16530  10722  -2388   2032   1986       C  
ATOM     24  CE1 HIS A   3     -11.963 -13.939 146.192  1.00103.12           C  
ANISOU   24  CE1 HIS A   3    12541  16089  10550  -2304   1882   2369       C  
ATOM     25  NE2 HIS A   3     -12.978 -13.490 146.908  1.00106.92           N  
ANISOU   25  NE2 HIS A   3    12917  16768  10941  -2375   2047   2246       N  
ATOM     26  N   TYR A   4     -13.934 -11.309 140.615  1.00 87.45           N  
ANISOU   26  N   TYR A   4     9691  14073   9462  -2319   1584   1495       N  
ATOM     27  CA  TYR A   4     -13.950 -10.407 139.474  1.00 82.80           C  
ANISOU   27  CA  TYR A   4     8960  13493   9007  -2195   1454   1307       C  
ATOM     28  C   TYR A   4     -15.115 -10.722 138.530  1.00 68.04           C  
ANISOU   28  C   TYR A   4     6865  11623   7366  -2285   1486   1182       C  
ATOM     29  O   TYR A   4     -15.819 -11.726 138.657  1.00 67.72           O  
ANISOU   29  O   TYR A   4     6789  11538   7403  -2469   1603   1238       O  
ATOM     30  CB  TYR A   4     -12.636 -10.482 138.678  1.00 79.34           C  
ANISOU   30  CB  TYR A   4     8698  12809   8640  -2069   1234   1377       C  
ATOM     31  CG  TYR A   4     -11.325 -10.302 139.428  1.00 84.34           C  
ANISOU   31  CG  TYR A   4     9541  13432   9073  -1981   1160   1504       C  
ATOM     32  CD1 TYR A   4     -11.256  -9.631 140.646  1.00 94.15           C  
ANISOU   32  CD1 TYR A   4    10801  14906  10065  -1957   1245   1473       C  
ATOM     33  CD2 TYR A   4     -10.142 -10.789 138.883  1.00 82.39           C  
ANISOU   33  CD2 TYR A   4     9458  12960   8885  -1921   1002   1636       C  
ATOM     34  CE1 TYR A   4     -10.042  -9.471 141.304  1.00 88.04           C  
ANISOU   34  CE1 TYR A   4    10195  14162   9095  -1885   1158   1569       C  
ATOM     35  CE2 TYR A   4      -8.931 -10.636 139.528  1.00 73.55           C  
ANISOU   35  CE2 TYR A   4     8497  11862   7587  -1835    920   1744       C  
ATOM     36  CZ  TYR A   4      -8.884  -9.977 140.736  1.00 71.11           C  
ANISOU   36  CZ  TYR A   4     8191  11806   7019  -1821    990   1707       C  
ATOM     37  OH  TYR A   4      -7.671  -9.831 141.369  1.00 67.10           O  
ANISOU   37  OH  TYR A   4     7817  11359   6318  -1745    892   1797       O  
ATOM     38  N   TYR A   5     -15.294  -9.821 137.568  1.00 59.82           N  
ANISOU   38  N   TYR A   5     5696  10589   6445  -2110   1357    989       N  
ATOM     39  CA  TYR A   5     -16.171  -9.970 136.415  1.00 64.83           C  
ANISOU   39  CA  TYR A   5     6116  11230   7287  -2132   1309    855       C  
ATOM     40  C   TYR A   5     -15.430  -9.345 135.245  1.00 73.45           C  
ANISOU   40  C   TYR A   5     7269  12168   8472  -1912   1085    786       C  
ATOM     41  O   TYR A   5     -15.027  -8.181 135.324  1.00 81.63           O  
ANISOU   41  O   TYR A   5     8340  13233   9444  -1698   1034    705       O  
ATOM     42  CB  TYR A   5     -17.512  -9.270 136.628  1.00 69.79           C  
ANISOU   42  CB  TYR A   5     6454  12140   7925  -2106   1432    670       C  
ATOM     43  CG  TYR A   5     -18.320  -9.160 135.354  1.00 85.35           C  
ANISOU   43  CG  TYR A   5     8180  14166  10083  -2056   1333    511       C  
ATOM     44  CD1 TYR A   5     -18.787 -10.299 134.711  1.00 91.19           C  
ANISOU   44  CD1 TYR A   5     8829  14857  10960  -2274   1330    520       C  
ATOM     45  CD2 TYR A   5     -18.591  -7.923 134.777  1.00 85.02           C  
ANISOU   45  CD2 TYR A   5     8003  14223  10076  -1785   1245    352       C  
ATOM     46  CE1 TYR A   5     -19.513 -10.217 133.545  1.00 84.19           C  
ANISOU   46  CE1 TYR A   5     7705  14065  10218  -2236   1222    361       C  
ATOM     47  CE2 TYR A   5     -19.323  -7.830 133.599  1.00 79.44           C  
ANISOU   47  CE2 TYR A   5     7067  13603   9514  -1714   1138    226       C  
ATOM     48  CZ  TYR A   5     -19.781  -8.984 132.988  1.00 74.64           C  
ANISOU   48  CZ  TYR A   5     6354  12987   9018  -1946   1115    223       C  
ATOM     49  OH  TYR A   5     -20.509  -8.921 131.816  1.00 65.25           O  
ANISOU   49  OH  TYR A   5     4920  11927   7947  -1889    994     82       O  
ATOM     50  N   ARG A   6     -15.229 -10.101 134.173  1.00 62.40           N  
ANISOU   50  N   ARG A   6     5895  10594   7220  -1971    970    812       N  
ATOM     51  CA  ARG A   6     -14.341  -9.646 133.112  1.00 58.43           C  
ANISOU   51  CA  ARG A   6     5500   9916   6785  -1779    769    785       C  
ATOM     52  C   ARG A   6     -15.104  -8.851 132.060  1.00 60.65           C  
ANISOU   52  C   ARG A   6     5567  10314   7162  -1618    682    596       C  
ATOM     53  O   ARG A   6     -16.247  -9.172 131.719  1.00 69.90           O  
ANISOU   53  O   ARG A   6     6502  11647   8410  -1717    722    501       O  
ATOM     54  CB  ARG A   6     -13.600 -10.826 132.477  1.00 66.51           C  
ANISOU   54  CB  ARG A   6     6688  10680   7904  -1900    691    911       C  
ATOM     55  CG  ARG A   6     -14.434 -11.781 131.651  1.00 74.03           C  
ANISOU   55  CG  ARG A   6     7497  11623   9010  -2088    703    848       C  
ATOM     56  CD  ARG A   6     -13.566 -12.942 131.192  1.00 79.79           C  
ANISOU   56  CD  ARG A   6     8434  12056   9825  -2205    662    981       C  
ATOM     57  NE  ARG A   6     -13.926 -14.203 131.834  1.00 77.89           N  
ANISOU   57  NE  ARG A   6     8228  11753   9613  -2481    843   1100       N  
ATOM     58  CZ  ARG A   6     -13.057 -15.176 132.099  1.00 76.90           C  
ANISOU   58  CZ  ARG A   6     8340  11374   9504  -2565    886   1302       C  
ATOM     59  NH1 ARG A   6     -11.774 -15.024 131.799  1.00 57.87           N  
ANISOU   59  NH1 ARG A   6     6131   8776   7081  -2397    749   1395       N  
ATOM     60  NH2 ARG A   6     -13.465 -16.296 132.677  1.00 90.63           N  
ANISOU   60  NH2 ARG A   6    10116  13042  11277  -2811   1080   1418       N  
ATOM     61  N   LEU A   7     -14.456  -7.798 131.555  1.00 65.33           N  
ANISOU   61  N   LEU A   7     6241  10834   7748  -1364    567    547       N  
ATOM     62  CA  LEU A   7     -15.113  -6.855 130.657  1.00 60.69           C  
ANISOU   62  CA  LEU A   7     5477  10360   7223  -1150    496    399       C  
ATOM     63  C   LEU A   7     -15.216  -7.377 129.232  1.00 52.17           C  
ANISOU   63  C   LEU A   7     4345   9218   6261  -1154    342    366       C  
ATOM     64  O   LEU A   7     -15.900  -6.759 128.407  1.00 47.22           O  
ANISOU   64  O   LEU A   7     3539   8728   5674   -987    272    256       O  
ATOM     65  CB  LEU A   7     -14.359  -5.531 130.673  1.00 53.60           C  
ANISOU   65  CB  LEU A   7     4713   9376   6277   -884    465    368       C  
ATOM     66  CG  LEU A   7     -14.283  -4.897 132.063  1.00 63.84           C  
ANISOU   66  CG  LEU A   7     6053  10759   7445   -877    621    355       C  
ATOM     67  CD1 LEU A   7     -13.507  -3.596 132.027  1.00 59.22           C  
ANISOU   67  CD1 LEU A   7     5607  10063   6830   -642    606    295       C  
ATOM     68  CD2 LEU A   7     -15.683  -4.678 132.616  1.00 60.46           C  
ANISOU   68  CD2 LEU A   7     5364  10605   7003   -902    770    258       C  
ATOM     69  N   SER A   8     -14.552  -8.490 128.928  1.00 47.61           N  
ANISOU   69  N   SER A   8     3918   8445   5728  -1329    292    460       N  
ATOM     70  CA  SER A   8     -14.562  -9.048 127.585  1.00 52.57           C  
ANISOU   70  CA  SER A   8     4520   9000   6455  -1356    155    414       C  
ATOM     71  C   SER A   8     -15.989  -9.328 127.120  1.00 65.23           C  
ANISOU   71  C   SER A   8     5807  10866   8111  -1451    162    271       C  
ATOM     72  O   SER A   8     -16.906  -9.550 127.916  1.00 54.65           O  
ANISOU   72  O   SER A   8     4290   9712   6761  -1594    302    238       O  
ATOM     73  CB  SER A   8     -13.734 -10.331 127.534  1.00 67.81           C  
ANISOU   73  CB  SER A   8     6654  10675   8437  -1566    154    533       C  
ATOM     74  OG  SER A   8     -13.637 -10.820 126.210  1.00 76.90           O  
ANISOU   74  OG  SER A   8     7805  11737   9675  -1587     28    470       O  
ATOM     75  N   LEU A   9     -16.166  -9.311 125.801  1.00 68.11           N  
ANISOU   75  N   LEU A   9     6091  11265   8523  -1372     10    179       N  
ATOM     76  CA  LEU A   9     -17.492  -9.479 125.222  1.00 80.01           C  
ANISOU   76  CA  LEU A   9     7267  13069  10065  -1432    -21     21       C  
ATOM     77  C   LEU A   9     -17.933 -10.935 125.180  1.00 88.69           C  
ANISOU   77  C   LEU A   9     8292  14161  11247  -1806     43    -26       C  
ATOM     78  O   LEU A   9     -19.140 -11.202 125.160  1.00 76.07           O  
ANISOU   78  O   LEU A   9     6391  12834   9679  -1943     88   -161       O  
ATOM     79  CB  LEU A   9     -17.529  -8.884 123.812  1.00 74.10           C  
ANISOU   79  CB  LEU A   9     6453  12397   9303  -1193   -217    -58       C  
ATOM     80  CG  LEU A   9     -17.395  -7.361 123.737  1.00 71.14           C  
ANISOU   80  CG  LEU A   9     6097  12070   8864   -806   -256    -32       C  
ATOM     81  CD1 LEU A   9     -17.940  -6.833 122.419  1.00 65.23           C  
ANISOU   81  CD1 LEU A   9     5175  11521   8089   -579   -423   -119       C  
ATOM     82  CD2 LEU A   9     -18.092  -6.688 124.913  1.00 75.32           C  
ANISOU   82  CD2 LEU A   9     6482  12769   9367   -747    -98    -43       C  
ATOM     83  N   LYS A  10     -16.991 -11.882 125.176  1.00108.06           N  
ANISOU   83  N   LYS A  10    11006  16304  13747  -1975     64     75       N  
ATOM     84  CA  LYS A  10     -17.364 -13.291 125.171  1.00126.71           C  
ANISOU   84  CA  LYS A  10    13334  18604  16207  -2338    164     36       C  
ATOM     85  C   LYS A  10     -18.111 -13.679 126.437  1.00135.59           C  
ANISOU   85  C   LYS A  10    14347  19834  17335  -2549    384     69       C  
ATOM     86  O   LYS A  10     -18.838 -14.678 126.437  1.00146.58           O  
ANISOU   86  O   LYS A  10    15664  21213  18815  -2800    486    -13       O  
ATOM     87  CB  LYS A  10     -16.124 -14.176 125.002  1.00130.50           C  
ANISOU   87  CB  LYS A  10    14145  18696  16744  -2435    169    168       C  
ATOM     88  CG  LYS A  10     -15.699 -14.945 126.253  1.00137.48           C  
ANISOU   88  CG  LYS A  10    15217  19377  17641  -2615    366    357       C  
ATOM     89  CD  LYS A  10     -14.677 -16.030 125.915  1.00139.38           C  
ANISOU   89  CD  LYS A  10    15736  19250  17973  -2735    382    465       C  
ATOM     90  CE  LYS A  10     -15.333 -17.227 125.239  1.00140.73           C  
ANISOU   90  CE  LYS A  10    15811  19376  18282  -3050    450    321       C  
ATOM     91  NZ  LYS A  10     -14.425 -18.410 125.178  1.00144.88           N  
ANISOU   91  NZ  LYS A  10    16628  19502  18916  -3181    539    447       N  
ATOM     92  N   SER A  11     -17.975 -12.892 127.504  1.00130.44           N  
ANISOU   92  N   SER A  11    13741  19234  16586  -2401    463    174       N  
ATOM     93  CA  SER A  11     -18.682 -13.145 128.755  1.00127.74           C  
ANISOU   93  CA  SER A  11    13300  19018  16218  -2577    682    210       C  
ATOM     94  C   SER A  11     -20.194 -13.138 128.554  1.00130.12           C  
ANISOU   94  C   SER A  11    13297  19573  16570  -2615    711      8       C  
ATOM     95  O   SER A  11     -20.951 -13.569 129.431  1.00140.91           O  
ANISOU   95  O   SER A  11    14611  20980  17950  -2762    889      5       O  
ATOM     96  CB  SER A  11     -18.306 -12.096 129.795  1.00124.27           C  
ANISOU   96  CB  SER A  11    12954  18621  15643  -2357    731    310       C  
ATOM     97  OG  SER A  11     -16.929 -11.794 129.752  1.00122.57           O  
ANISOU   97  OG  SER A  11    13042  18152  15375  -2186    631    445       O  
ATOM     98  N   ARG A  12     -20.632 -12.665 127.392  1.00117.33           N  
ANISOU   98  N   ARG A  12    11489  18117  14972  -2468    532   -151       N  
ATOM     99  CA  ARG A  12     -22.045 -12.511 127.087  1.00111.38           C  
ANISOU   99  CA  ARG A  12    10439  17630  14249  -2444    520   -337       C  
ATOM    100  C   ARG A  12     -22.737 -13.871 127.004  1.00122.92           C  
ANISOU  100  C   ARG A  12    11870  19012  15823  -2766    617   -424       C  
ATOM    101  O   ARG A  12     -22.111 -14.899 126.698  1.00119.01           O  
ANISOU  101  O   ARG A  12    11571  18250  15398  -2959    633   -382       O  
ATOM    102  CB  ARG A  12     -22.200 -11.755 125.769  1.00 99.58           C  
ANISOU  102  CB  ARG A  12     8800  16305  12730  -2188    285   -453       C  
ATOM    103  CG  ARG A  12     -22.445 -12.643 124.561  1.00103.52           C  
ANISOU  103  CG  ARG A  12     9267  16772  13294  -2332    167   -587       C  
ATOM    104  CD  ARG A  12     -22.707 -11.844 123.304  1.00108.21           C  
ANISOU  104  CD  ARG A  12     9718  17571  13826  -2053    -60   -688       C  
ATOM    105  NE  ARG A  12     -21.505 -11.217 122.759  1.00102.59           N  
ANISOU  105  NE  ARG A  12     9186  16736  13057  -1838   -197   -584       N  
ATOM    106  CZ  ARG A  12     -20.741 -11.759 121.814  1.00102.17           C  
ANISOU  106  CZ  ARG A  12     9287  16517  13016  -1903   -313   -593       C  
ATOM    107  NH1 ARG A  12     -21.051 -12.945 121.302  1.00102.60           N  
ANISOU  107  NH1 ARG A  12     9344  16500  13140  -2176   -303   -711       N  
ATOM    108  NH2 ARG A  12     -19.675 -11.106 121.370  1.00 94.76           N  
ANISOU  108  NH2 ARG A  12     8503  15478  12023  -1693   -430   -493       N  
ATOM    109  N   GLN A  13     -24.032 -13.869 127.330  1.00136.70           N  
ANISOU  109  N   GLN A  13    13373  20977  17591  -2818    702   -544       N  
ATOM    110  CA  GLN A  13     -24.920 -15.003 127.130  1.00132.97           C  
ANISOU  110  CA  GLN A  13    12799  20498  17225  -3098    782   -671       C  
ATOM    111  C   GLN A  13     -26.025 -14.602 126.171  1.00128.72           C  
ANISOU  111  C   GLN A  13    11946  20280  16682  -2992    631   -885       C  
ATOM    112  O   GLN A  13     -26.296 -13.417 125.978  1.00124.10           O  
ANISOU  112  O   GLN A  13    11207  19928  16016  -2696    519   -908       O  
ATOM    113  CB  GLN A  13     -25.512 -15.498 128.458  1.00137.44           C  
ANISOU  113  CB  GLN A  13    13360  21037  17823  -3292   1043   -613       C  
ATOM    114  CG  GLN A  13     -25.920 -14.404 129.451  1.00145.74           C  
ANISOU  114  CG  GLN A  13    14295  22299  18780  -3106   1124   -571       C  
ATOM    115  CD  GLN A  13     -26.376 -14.985 130.780  1.00158.99           C  
ANISOU  115  CD  GLN A  13    16014  23920  20475  -3312   1392   -493       C  
ATOM    116  OE1 GLN A  13     -26.640 -14.260 131.738  1.00160.97           O  
ANISOU  116  OE1 GLN A  13    16216  24301  20645  -3203   1499   -448       O  
ATOM    117  NE2 GLN A  13     -26.469 -16.304 130.838  1.00165.98           N  
ANISOU  117  NE2 GLN A  13    16999  24600  21465  -3604   1514   -478       N  
ATOM    118  N   LYS A  14     -26.660 -15.608 125.582  1.00129.98           N  
ANISOU  118  N   LYS A  14    12019  20443  16926  -3229    637  -1035       N  
ATOM    119  CA  LYS A  14     -27.694 -15.366 124.588  1.00129.84           C  
ANISOU  119  CA  LYS A  14    11707  20739  16887  -3156    483  -1243       C  
ATOM    120  C   LYS A  14     -28.926 -14.747 125.237  1.00128.14           C  
ANISOU  120  C   LYS A  14    11203  20828  16654  -3075    560  -1307       C  
ATOM    121  O   LYS A  14     -29.470 -15.283 126.208  1.00131.98           O  
ANISOU  121  O   LYS A  14    11656  21285  17207  -3288    773  -1300       O  
ATOM    122  CB  LYS A  14     -28.059 -16.669 123.877  1.00130.32           C  
ANISOU  122  CB  LYS A  14    11753  20727  17037  -3466    495  -1403       C  
ATOM    123  CG  LYS A  14     -26.881 -17.318 123.164  1.00131.34           C  
ANISOU  123  CG  LYS A  14    12163  20547  17193  -3543    427  -1359       C  
ATOM    124  CD  LYS A  14     -27.265 -18.650 122.551  1.00135.32           C  
ANISOU  124  CD  LYS A  14    12665  20956  17795  -3864    478  -1529       C  
ATOM    125  CE  LYS A  14     -26.120 -19.240 121.743  1.00136.13           C  
ANISOU  125  CE  LYS A  14    13039  20761  17923  -3915    405  -1503       C  
ATOM    126  NZ  LYS A  14     -26.448 -20.598 121.222  1.00139.67           N  
ANISOU  126  NZ  LYS A  14    13515  21077  18478  -4240    490  -1670       N  
ATOM    127  N   ALA A  15     -29.361 -13.607 124.696  1.00121.02           N  
ANISOU  127  N   ALA A  15    10102  20213  15666  -2754    394  -1358       N  
ATOM    128  CA  ALA A  15     -30.497 -12.861 125.221  1.00116.94           C  
ANISOU  128  CA  ALA A  15     9306  19994  15132  -2616    449  -1413       C  
ATOM    129  C   ALA A  15     -31.752 -13.724 125.205  1.00134.54           C  
ANISOU  129  C   ALA A  15    11292  22389  17437  -2892    533  -1595       C  
ATOM    130  O   ALA A  15     -32.263 -14.053 124.127  1.00130.89           O  
ANISOU  130  O   ALA A  15    10676  22091  16965  -2934    388  -1756       O  
ATOM    131  CB  ALA A  15     -30.720 -11.583 124.412  1.00107.23           C  
ANISOU  131  CB  ALA A  15     7923  19017  13805  -2206    238  -1432       C  
ATOM    132  N   PRO A  16     -32.270 -14.117 126.368  1.00144.34           N  
ANISOU  132  N   PRO A  16    12494  23602  18746  -3090    771  -1578       N  
ATOM    133  CA  PRO A  16     -33.518 -14.886 126.396  1.00144.70           C  
ANISOU  133  CA  PRO A  16    12290  23820  18870  -3352    867  -1758       C  
ATOM    134  C   PRO A  16     -34.677 -14.008 125.962  1.00140.09           C  
ANISOU  134  C   PRO A  16    11336  23654  18237  -3121    747  -1893       C  
ATOM    135  O   PRO A  16     -34.637 -12.783 126.095  1.00137.38           O  
ANISOU  135  O   PRO A  16    10939  23437  17823  -2772    678  -1815       O  
ATOM    136  CB  PRO A  16     -33.653 -15.302 127.868  1.00145.89           C  
ANISOU  136  CB  PRO A  16    12525  23822  19085  -3555   1163  -1658       C  
ATOM    137  CG  PRO A  16     -32.359 -14.864 128.542  1.00147.19           C  
ANISOU  137  CG  PRO A  16    13013  23719  19193  -3420   1207  -1425       C  
ATOM    138  CD  PRO A  16     -31.839 -13.741 127.720  1.00146.12           C  
ANISOU  138  CD  PRO A  16    12872  23684  18960  -3054    964  -1404       C  
ATOM    139  N   LYS A  17     -35.721 -14.642 125.429  1.00140.11           N  
ANISOU  139  N   LYS A  17    11082  23872  18280  -3312    726  -2099       N  
ATOM    140  CA  LYS A  17     -36.767 -13.831 124.821  1.00139.80           C  
ANISOU  140  CA  LYS A  17    10690  24250  18180  -3070    573  -2227       C  
ATOM    141  C   LYS A  17     -37.724 -13.246 125.861  1.00137.91           C  
ANISOU  141  C   LYS A  17    10219  24204  17975  -2996    735  -2225       C  
ATOM    142  O   LYS A  17     -38.330 -12.204 125.607  1.00142.01           O  
ANISOU  142  O   LYS A  17    10508  25012  18439  -2675    625  -2246       O  
ATOM    143  CB  LYS A  17     -37.499 -14.634 123.745  1.00141.89           C  
ANISOU  143  CB  LYS A  17    10748  24718  18447  -3273    460  -2462       C  
ATOM    144  CG  LYS A  17     -36.559 -15.490 122.894  1.00137.58           C  
ANISOU  144  CG  LYS A  17    10460  23920  17894  -3444    371  -2481       C  
ATOM    145  CD  LYS A  17     -35.350 -14.690 122.379  1.00129.93           C  
ANISOU  145  CD  LYS A  17     9737  22804  16826  -3120    194  -2310       C  
ATOM    146  CE  LYS A  17     -35.290 -14.570 120.858  1.00120.52           C  
ANISOU  146  CE  LYS A  17     8486  21785  15521  -2982    -74  -2415       C  
ATOM    147  NZ  LYS A  17     -33.979 -13.988 120.423  1.00112.56           N  
ANISOU  147  NZ  LYS A  17     7770  20561  14437  -2730   -206  -2240       N  
ATOM    148  N   ILE A  18     -37.849 -13.856 127.040  1.00131.81           N  
ANISOU  148  N   ILE A  18     9518  23273  17292  -3263   1003  -2186       N  
ATOM    149  CA  ILE A  18     -38.419 -13.191 128.211  1.00126.20           C  
ANISOU  149  CA  ILE A  18     8687  22663  16600  -3161   1186  -2129       C  
ATOM    150  C   ILE A  18     -37.872 -13.855 129.469  1.00116.84           C  
ANISOU  150  C   ILE A  18     7772  21155  15466  -3417   1459  -1991       C  
ATOM    151  O   ILE A  18     -37.739 -15.084 129.530  1.00109.64           O  
ANISOU  151  O   ILE A  18     6984  20048  14627  -3771   1567  -2016       O  
ATOM    152  CB  ILE A  18     -39.965 -13.203 128.219  1.00139.58           C  
ANISOU  152  CB  ILE A  18     9961  24730  18344  -3222   1230  -2320       C  
ATOM    153  CG1 ILE A  18     -40.484 -12.745 129.597  1.00132.73           C  
ANISOU  153  CG1 ILE A  18     9016  23903  17515  -3193   1480  -2256       C  
ATOM    154  CG2 ILE A  18     -40.523 -14.585 127.812  1.00144.42           C  
ANISOU  154  CG2 ILE A  18    10476  25360  19037  -3644   1278  -2506       C  
ATOM    155  CD1 ILE A  18     -41.938 -12.329 129.635  1.00128.80           C  
ANISOU  155  CD1 ILE A  18     8085  23801  17052  -3118   1501  -2412       C  
ATOM    156  N   VAL A  19     -37.554 -13.027 130.486  1.00117.47           N  
ANISOU  156  N   VAL A  19     7953  21177  15503  -3229   1580  -1842       N  
ATOM    157  CA  VAL A  19     -36.948 -13.508 131.726  1.00132.17           C  
ANISOU  157  CA  VAL A  19    10094  22752  17374  -3418   1829  -1681       C  
ATOM    158  C   VAL A  19     -37.970 -14.349 132.488  1.00150.23           C  
ANISOU  158  C   VAL A  19    12231  25097  19752  -3740   2078  -1759       C  
ATOM    159  O   VAL A  19     -39.189 -14.234 132.288  1.00159.54           O  
ANISOU  159  O   VAL A  19    13062  26578  20979  -3751   2078  -1930       O  
ATOM    160  CB  VAL A  19     -36.415 -12.340 132.588  1.00131.46           C  
ANISOU  160  CB  VAL A  19    10129  22630  17191  -3126   1892  -1531       C  
ATOM    161  CG1 VAL A  19     -37.548 -11.690 133.438  1.00129.61           C  
ANISOU  161  CG1 VAL A  19     9629  22648  16970  -3037   2058  -1593       C  
ATOM    162  CG2 VAL A  19     -35.176 -12.778 133.398  1.00132.88           C  
ANISOU  162  CG2 VAL A  19    10711  22454  17322  -3249   2024  -1327       C  
ATOM    163  N   ASN A  20     -37.475 -15.225 133.365  1.00158.91           N  
ANISOU  163  N   ASN A  20    13597  25905  20875  -4003   2298  -1626       N  
ATOM    164  CA  ASN A  20     -38.325 -16.206 134.030  1.00167.83           C  
ANISOU  164  CA  ASN A  20    14637  27030  22100  -4345   2549  -1679       C  
ATOM    165  C   ASN A  20     -38.589 -15.834 135.494  1.00163.93           C  
ANISOU  165  C   ASN A  20    14171  26549  21564  -4327   2813  -1564       C  
ATOM    166  O   ASN A  20     -38.316 -14.713 135.938  1.00161.21           O  
ANISOU  166  O   ASN A  20    13851  26280  21123  -4036   2792  -1490       O  
ATOM    167  CB  ASN A  20     -37.707 -17.602 133.909  1.00173.14           C  
ANISOU  167  CB  ASN A  20    15582  27361  22844  -4673   2631  -1614       C  
ATOM    168  CG  ASN A  20     -36.261 -17.641 134.347  1.00166.87           C  
ANISOU  168  CG  ASN A  20    15204  26222  21976  -4606   2650  -1363       C  
ATOM    169  OD1 ASN A  20     -35.854 -16.919 135.258  1.00161.64           O  
ANISOU  169  OD1 ASN A  20    14662  25541  21214  -4433   2732  -1212       O  
ATOM    170  ND2 ASN A  20     -35.468 -18.472 133.685  1.00165.40           N  
ANISOU  170  ND2 ASN A  20    15239  25771  21835  -4737   2575  -1324       N  
ATOM    171  N   SER A  21     -39.109 -16.816 136.243  1.00154.30           N  
ANISOU  171  N   SER A  21    12965  25245  20418  -4650   3076  -1551       N  
ATOM    172  CA  SER A  21     -39.699 -16.577 137.559  1.00148.65           C  
ANISOU  172  CA  SER A  21    12195  24610  19675  -4678   3346  -1491       C  
ATOM    173  C   SER A  21     -38.711 -15.920 138.514  1.00144.80           C  
ANISOU  173  C   SER A  21    12010  23967  19040  -4485   3420  -1267       C  
ATOM    174  O   SER A  21     -39.072 -14.999 139.257  1.00134.74           O  
ANISOU  174  O   SER A  21    10638  22862  17694  -4302   3511  -1263       O  
ATOM    175  CB  SER A  21     -40.197 -17.900 138.144  1.00150.11           C  
ANISOU  175  CB  SER A  21    12420  24658  19958  -5078   3619  -1475       C  
ATOM    176  OG  SER A  21     -40.728 -18.731 137.131  1.00148.88           O  
ANISOU  176  OG  SER A  21    12094  24542  19930  -5300   3532  -1666       O  
ATOM    177  N   LYS A  22     -37.462 -16.399 138.520  1.00148.93           N  
ANISOU  177  N   LYS A  22    12901  24172  19516  -4526   3389  -1085       N  
ATOM    178  CA  LYS A  22     -36.440 -15.867 139.419  1.00152.21           C  
ANISOU  178  CA  LYS A  22    13621  24438  19773  -4365   3452   -872       C  
ATOM    179  C   LYS A  22     -36.335 -14.353 139.314  1.00149.18           C  
ANISOU  179  C   LYS A  22    13130  24259  19292  -3993   3304   -928       C  
ATOM    180  O   LYS A  22     -36.367 -13.640 140.324  1.00153.86           O  
ANISOU  180  O   LYS A  22    13762  24922  19776  -3866   3445   -869       O  
ATOM    181  CB  LYS A  22     -35.086 -16.507 139.110  1.00154.30           C  
ANISOU  181  CB  LYS A  22    14250  24365  20012  -4417   3367   -698       C  
ATOM    182  CG  LYS A  22     -33.928 -15.825 139.822  1.00154.60           C  
ANISOU  182  CG  LYS A  22    14582  24286  19871  -4212   3364   -503       C  
ATOM    183  CD  LYS A  22     -33.914 -16.174 141.299  1.00157.84           C  
ANISOU  183  CD  LYS A  22    15178  24613  20183  -4326   3658   -324       C  
ATOM    184  CE  LYS A  22     -32.582 -15.827 141.949  1.00151.17           C  
ANISOU  184  CE  LYS A  22    14687  23602  19150  -4181   3648   -106       C  
ATOM    185  NZ  LYS A  22     -32.408 -16.554 143.241  1.00151.26           N  
ANISOU  185  NZ  LYS A  22    14939  23466  19067  -4336   3920    114       N  
ATOM    186  N   TYR A  23     -36.224 -13.848 138.091  1.00141.26           N  
ANISOU  186  N   TYR A  23    11998  23351  18325  -3811   3029  -1044       N  
ATOM    187  CA  TYR A  23     -35.932 -12.445 137.858  1.00135.39           C  
ANISOU  187  CA  TYR A  23    11203  22742  17497  -3437   2874  -1068       C  
ATOM    188  C   TYR A  23     -37.183 -11.589 137.948  1.00133.13           C  
ANISOU  188  C   TYR A  23    10551  22785  17248  -3271   2909  -1227       C  
ATOM    189  O   TYR A  23     -38.262 -11.980 137.495  1.00138.87           O  
ANISOU  189  O   TYR A  23    10982  23695  18085  -3388   2901  -1379       O  
ATOM    190  CB  TYR A  23     -35.292 -12.248 136.488  1.00131.64           C  
ANISOU  190  CB  TYR A  23    10749  22230  17039  -3290   2571  -1105       C  
ATOM    191  CG  TYR A  23     -33.892 -12.776 136.401  1.00122.66           C  
ANISOU  191  CG  TYR A  23     9983  20774  15850  -3363   2517   -937       C  
ATOM    192  CD1 TYR A  23     -33.651 -14.125 136.190  1.00121.24           C  
ANISOU  192  CD1 TYR A  23     9942  20377  15747  -3670   2560   -891       C  
ATOM    193  CD2 TYR A  23     -32.806 -11.928 136.544  1.00119.20           C  
ANISOU  193  CD2 TYR A  23     9756  20244  15291  -3124   2436   -824       C  
ATOM    194  CE1 TYR A  23     -32.363 -14.616 136.116  1.00126.36           C  
ANISOU  194  CE1 TYR A  23    10931  20725  16357  -3721   2517   -726       C  
ATOM    195  CE2 TYR A  23     -31.514 -12.406 136.470  1.00117.09           C  
ANISOU  195  CE2 TYR A  23     9816  19699  14974  -3187   2384   -668       C  
ATOM    196  CZ  TYR A  23     -31.298 -13.751 136.258  1.00122.74           C  
ANISOU  196  CZ  TYR A  23    10664  20202  15771  -3478   2424   -612       C  
ATOM    197  OH  TYR A  23     -30.010 -14.233 136.186  1.00123.72           O  
ANISOU  197  OH  TYR A  23    11113  20040  15854  -3524   2378   -446       O  
ATOM    198  N   ASN A  24     -37.019 -10.416 138.543  1.00120.25           N  
ANISOU  198  N   ASN A  24     8944  21222  15523  -2996   2952  -1195       N  
ATOM    199  CA  ASN A  24     -38.002  -9.354 138.428  1.00115.59           C  
ANISOU  199  CA  ASN A  24     8030  20918  14970  -2736   2936  -1332       C  
ATOM    200  C   ASN A  24     -38.209  -9.002 136.958  1.00126.58           C  
ANISOU  200  C   ASN A  24     9216  22449  16430  -2544   2642  -1441       C  
ATOM    201  O   ASN A  24     -37.256  -8.943 136.176  1.00134.18           O  
ANISOU  201  O   ASN A  24    10354  23273  17357  -2451   2441  -1383       O  
ATOM    202  CB  ASN A  24     -37.518  -8.145 139.219  1.00110.84           C  
ANISOU  202  CB  ASN A  24     7567  20295  14254  -2456   3019  -1267       C  
ATOM    203  CG  ASN A  24     -38.385  -6.926 139.031  1.00115.07           C  
ANISOU  203  CG  ASN A  24     7806  21079  14838  -2128   2997  -1388       C  
ATOM    204  OD1 ASN A  24     -39.354  -6.914 138.276  1.00128.86           O  
ANISOU  204  OD1 ASN A  24     9227  23041  16692  -2080   2898  -1512       O  
ATOM    205  ND2 ASN A  24     -38.019  -5.872 139.721  1.00109.53           N  
ANISOU  205  ND2 ASN A  24     7222  20343  14051  -1891   3094  -1351       N  
ATOM    206  N   SER A  25     -39.466  -8.759 136.586  1.00135.33           N  
ANISOU  206  N   SER A  25     9949  23845  17626  -2476   2620  -1594       N  
ATOM    207  CA  SER A  25     -39.833  -8.454 135.208  1.00139.94           C  
ANISOU  207  CA  SER A  25    10303  24611  18256  -2292   2345  -1700       C  
ATOM    208  C   SER A  25     -39.763  -6.965 134.883  1.00136.90           C  
ANISOU  208  C   SER A  25     9849  24329  17836  -1826   2228  -1687       C  
ATOM    209  O   SER A  25     -40.226  -6.558 133.811  1.00135.17           O  
ANISOU  209  O   SER A  25     9410  24303  17647  -1618   2017  -1763       O  
ATOM    210  CB  SER A  25     -41.239  -8.979 134.898  1.00154.27           C  
ANISOU  210  CB  SER A  25    11734  26707  20176  -2453   2363  -1875       C  
ATOM    211  OG  SER A  25     -41.862  -8.184 133.905  1.00158.32           O  
ANISOU  211  OG  SER A  25    11957  27489  20707  -2147   2150  -1972       O  
ATOM    212  N   ILE A  26     -39.210  -6.146 135.782  1.00113.49           N  
ANISOU  212  N   ILE A  26     7075  21241  14806  -1654   2369  -1591       N  
ATOM    213  CA  ILE A  26     -38.956  -4.748 135.443  1.00111.09           C  
ANISOU  213  CA  ILE A  26     6771  20963  14477  -1212   2270  -1565       C  
ATOM    214  C   ILE A  26     -37.987  -4.654 134.272  1.00113.40           C  
ANISOU  214  C   ILE A  26     7226  21132  14727  -1076   1997  -1504       C  
ATOM    215  O   ILE A  26     -38.100  -3.760 133.422  1.00110.91           O  
ANISOU  215  O   ILE A  26     6806  20913  14423   -730   1828  -1512       O  
ATOM    216  CB  ILE A  26     -38.441  -3.979 136.676  1.00113.30           C  
ANISOU  216  CB  ILE A  26     7264  21098  14685  -1100   2494  -1490       C  
ATOM    217  CG1 ILE A  26     -39.527  -3.897 137.748  1.00111.63           C  
ANISOU  217  CG1 ILE A  26     6856  21044  14514  -1173   2761  -1562       C  
ATOM    218  CG2 ILE A  26     -37.972  -2.583 136.293  1.00105.15           C  
ANISOU  218  CG2 ILE A  26     6299  20019  13633   -660   2404  -1455       C  
ATOM    219  CD1 ILE A  26     -40.330  -2.618 137.714  1.00108.57           C  
ANISOU  219  CD1 ILE A  26     6227  20834  14192   -791   2798  -1629       C  
ATOM    220  N   LEU A  27     -37.034  -5.585 134.195  1.00119.44           N  
ANISOU  220  N   LEU A  27     8253  21680  15448  -1340   1956  -1433       N  
ATOM    221  CA  LEU A  27     -36.000  -5.531 133.170  1.00121.11           C  
ANISOU  221  CA  LEU A  27     8651  21749  15616  -1230   1719  -1367       C  
ATOM    222  C   LEU A  27     -36.446  -6.094 131.831  1.00121.89           C  
ANISOU  222  C   LEU A  27     8567  21988  15757  -1279   1485  -1455       C  
ATOM    223  O   LEU A  27     -35.685  -6.012 130.862  1.00113.62           O  
ANISOU  223  O   LEU A  27     7649  20850  14670  -1165   1277  -1410       O  
ATOM    224  CB  LEU A  27     -34.740  -6.268 133.644  1.00113.53           C  
ANISOU  224  CB  LEU A  27     8053  20489  14592  -1476   1776  -1246       C  
ATOM    225  CG  LEU A  27     -34.744  -7.713 134.168  1.00113.85           C  
ANISOU  225  CG  LEU A  27     8186  20417  14656  -1921   1908  -1231       C  
ATOM    226  CD1 LEU A  27     -34.937  -8.749 133.065  1.00119.00           C  
ANISOU  226  CD1 LEU A  27     8755  21082  15376  -2126   1742  -1304       C  
ATOM    227  CD2 LEU A  27     -33.443  -7.979 134.920  1.00102.93           C  
ANISOU  227  CD2 LEU A  27     7182  18746  13181  -2033   2001  -1070       C  
ATOM    228  N   ASN A  28     -37.635  -6.683 131.754  1.00125.73           N  
ANISOU  228  N   ASN A  28     8762  22695  16314  -1456   1520  -1586       N  
ATOM    229  CA  ASN A  28     -38.113  -7.163 130.467  1.00134.29           C  
ANISOU  229  CA  ASN A  28     9658  23948  17419  -1495   1296  -1694       C  
ATOM    230  C   ASN A  28     -38.647  -6.030 129.611  1.00136.75           C  
ANISOU  230  C   ASN A  28     9749  24500  17710  -1073   1114  -1722       C  
ATOM    231  O   ASN A  28     -38.738  -6.186 128.394  1.00142.37           O  
ANISOU  231  O   ASN A  28    10376  25327  18391  -1013    882  -1773       O  
ATOM    232  CB  ASN A  28     -39.177  -8.239 130.645  1.00137.79           C  
ANISOU  232  CB  ASN A  28     9865  24546  17941  -1854   1398  -1839       C  
ATOM    233  CG  ASN A  28     -38.637  -9.490 131.319  1.00142.78           C  
ANISOU  233  CG  ASN A  28    10739  24912  18601  -2277   1567  -1796       C  
ATOM    234  OD1 ASN A  28     -38.658 -10.574 130.742  1.00141.27           O  
ANISOU  234  OD1 ASN A  28    10554  24676  18446  -2559   1510  -1869       O  
ATOM    235  ND2 ASN A  28     -38.176  -9.348 132.541  1.00143.80           N  
ANISOU  235  ND2 ASN A  28    11068  24863  18708  -2318   1784  -1677       N  
ATOM    236  N   ILE A  29     -38.971  -4.891 130.219  1.00125.06           N  
ANISOU  236  N   ILE A  29     8193  23083  16240   -773   1222  -1683       N  
ATOM    237  CA  ILE A  29     -39.062  -3.641 129.472  1.00121.50           C  
ANISOU  237  CA  ILE A  29     7665  22739  15762   -306   1066  -1639       C  
ATOM    238  C   ILE A  29     -37.789  -3.442 128.654  1.00130.21           C  
ANISOU  238  C   ILE A  29     9066  23624  16785   -168    880  -1526       C  
ATOM    239  O   ILE A  29     -37.830  -3.259 127.431  1.00137.18           O  
ANISOU  239  O   ILE A  29     9887  24613  17620     11    645  -1528       O  
ATOM    240  CB  ILE A  29     -39.317  -2.479 130.447  1.00112.51           C  
ANISOU  240  CB  ILE A  29     6501  21589  14660    -32   1269  -1594       C  
ATOM    241  CG1 ILE A  29     -40.549  -2.799 131.309  1.00115.12           C  
ANISOU  241  CG1 ILE A  29     6544  22125  15071   -211   1473  -1708       C  
ATOM    242  CG2 ILE A  29     -39.485  -1.187 129.704  1.00104.71           C  
ANISOU  242  CG2 ILE A  29     5435  20684  13664    460   1137  -1539       C  
ATOM    243  CD1 ILE A  29     -40.899  -1.738 132.325  1.00113.52           C  
ANISOU  243  CD1 ILE A  29     6301  21920  14912     26   1702  -1686       C  
ATOM    244  N   ALA A  30     -36.630  -3.552 129.313  1.00126.06           N  
ANISOU  244  N   ALA A  30     8869  22797  16231   -273    983  -1428       N  
ATOM    245  CA  ALA A  30     -35.353  -3.385 128.624  1.00117.00           C  
ANISOU  245  CA  ALA A  30     8012  21428  15015   -161    827  -1320       C  
ATOM    246  C   ALA A  30     -35.060  -4.536 127.669  1.00118.63           C  
ANISOU  246  C   ALA A  30     8260  21616  15198   -424    648  -1362       C  
ATOM    247  O   ALA A  30     -34.408  -4.331 126.640  1.00119.93           O  
ANISOU  247  O   ALA A  30     8546  21717  15304   -264    448  -1309       O  
ATOM    248  CB  ALA A  30     -34.223  -3.249 129.642  1.00112.35           C  
ANISOU  248  CB  ALA A  30     7741  20548  14398   -228    994  -1217       C  
ATOM    249  N   LEU A  31     -35.511  -5.750 127.989  1.00123.47           N  
ANISOU  249  N   LEU A  31     8790  22266  15859   -827    730  -1457       N  
ATOM    250  CA  LEU A  31     -35.328  -6.868 127.066  1.00126.92           C  
ANISOU  250  CA  LEU A  31     9254  22680  16288  -1086    581  -1523       C  
ATOM    251  C   LEU A  31     -36.151  -6.662 125.793  1.00127.36           C  
ANISOU  251  C   LEU A  31     9047  23032  16311   -915    358  -1627       C  
ATOM    252  O   LEU A  31     -35.666  -6.924 124.681  1.00123.25           O  
ANISOU  252  O   LEU A  31     8615  22483  15730   -896    158  -1631       O  
ATOM    253  CB  LEU A  31     -35.691  -8.175 127.774  1.00133.40           C  
ANISOU  253  CB  LEU A  31    10052  23449  17184  -1548    759  -1601       C  
ATOM    254  CG  LEU A  31     -35.183  -9.512 127.223  1.00137.85           C  
ANISOU  254  CG  LEU A  31    10764  23846  17768  -1899    702  -1640       C  
ATOM    255  CD1 LEU A  31     -35.760  -9.813 125.842  1.00141.23           C  
ANISOU  255  CD1 LEU A  31    10992  24495  18174  -1892    478  -1787       C  
ATOM    256  CD2 LEU A  31     -33.647  -9.551 127.235  1.00130.54           C  
ANISOU  256  CD2 LEU A  31    10218  22582  16800  -1885    673  -1482       C  
ATOM    257  N   LYS A  32     -37.390  -6.177 125.941  1.00130.88           N  
ANISOU  257  N   LYS A  32     9170  23774  16786   -781    392  -1708       N  
ATOM    258  CA  LYS A  32     -38.170  -5.703 124.809  1.00135.23           C  
ANISOU  258  CA  LYS A  32     9465  24633  17282   -527    182  -1774       C  
ATOM    259  C   LYS A  32     -37.417  -4.632 124.031  1.00129.66           C  
ANISOU  259  C   LYS A  32     8932  23846  16487   -104     14  -1629       C  
ATOM    260  O   LYS A  32     -37.381  -4.663 122.797  1.00135.00           O  
ANISOU  260  O   LYS A  32     9586  24633  17076      3   -208  -1646       O  
ATOM    261  CB  LYS A  32     -39.512  -5.161 125.319  1.00140.71           C  
ANISOU  261  CB  LYS A  32     9808  25623  18034   -399    283  -1847       C  
ATOM    262  CG  LYS A  32     -40.315  -4.394 124.293  1.00144.53           C  
ANISOU  262  CG  LYS A  32    10028  26430  18456    -44     84  -1873       C  
ATOM    263  CD  LYS A  32     -41.209  -3.353 124.981  1.00151.44           C  
ANISOU  263  CD  LYS A  32    10674  27470  19396    245    214  -1852       C  
ATOM    264  CE  LYS A  32     -41.077  -1.987 124.319  1.00144.67           C  
ANISOU  264  CE  LYS A  32     9846  26643  18477    776     84  -1713       C  
ATOM    265  NZ  LYS A  32     -41.904  -0.931 124.957  1.00141.95           N  
ANISOU  265  NZ  LYS A  32     9299  26426  18212   1083    223  -1686       N  
ATOM    266  N   ASN A  33     -36.827  -3.667 124.731  1.00131.16           N  
ANISOU  266  N   ASN A  33     9300  23844  16692    140    129  -1490       N  
ATOM    267  CA  ASN A  33     -36.200  -2.532 124.060  1.00130.60           C  
ANISOU  267  CA  ASN A  33     9387  23683  16551    569      4  -1347       C  
ATOM    268  C   ASN A  33     -34.942  -2.942 123.300  1.00140.76           C  
ANISOU  268  C   ASN A  33    10977  24740  17766    501   -139  -1278       C  
ATOM    269  O   ASN A  33     -34.622  -2.338 122.275  1.00139.78           O  
ANISOU  269  O   ASN A  33    10931  24622  17558    793   -312  -1199       O  
ATOM    270  CB  ASN A  33     -35.883  -1.435 125.084  1.00120.76           C  
ANISOU  270  CB  ASN A  33     8263  22266  15355    814    199  -1240       C  
ATOM    271  CG  ASN A  33     -37.136  -0.740 125.592  1.00117.92           C  
ANISOU  271  CG  ASN A  33     7603  22139  15062   1003    314  -1290       C  
ATOM    272  OD1 ASN A  33     -38.115  -0.577 124.858  1.00115.36           O  
ANISOU  272  OD1 ASN A  33     7004  22106  14721   1150    187  -1343       O  
ATOM    273  ND2 ASN A  33     -37.113  -0.333 126.856  1.00125.12           N  
ANISOU  273  ND2 ASN A  33     8562  22934  16044   1000    561  -1276       N  
ATOM    274  N   PHE A  34     -34.205  -3.934 123.805  1.00149.66           N  
ANISOU  274  N   PHE A  34    12288  25653  18924    131    -57  -1293       N  
ATOM    275  CA  PHE A  34     -33.046  -4.474 123.092  1.00141.68           C  
ANISOU  275  CA  PHE A  34    11545  24426  17861     25   -185  -1243       C  
ATOM    276  C   PHE A  34     -33.454  -4.970 121.706  1.00138.16           C  
ANISOU  276  C   PHE A  34    10975  24177  17342     -2   -410  -1337       C  
ATOM    277  O   PHE A  34     -32.787  -4.672 120.708  1.00144.58           O  
ANISOU  277  O   PHE A  34    11944  24922  18069    184   -577  -1265       O  
ATOM    278  CB  PHE A  34     -32.414  -5.567 123.972  1.00136.96           C  
ANISOU  278  CB  PHE A  34    11116  23597  17326   -397    -31  -1255       C  
ATOM    279  CG  PHE A  34     -31.210  -6.278 123.386  1.00130.96           C  
ANISOU  279  CG  PHE A  34    10631  22591  16538   -560   -130  -1209       C  
ATOM    280  CD1 PHE A  34     -30.047  -5.596 123.091  1.00130.00           C  
ANISOU  280  CD1 PHE A  34    10765  22264  16365   -325   -200  -1069       C  
ATOM    281  CD2 PHE A  34     -31.190  -7.666 123.286  1.00131.53           C  
ANISOU  281  CD2 PHE A  34    10724  22597  16653   -972   -114  -1302       C  
ATOM    282  CE1 PHE A  34     -28.916  -6.278 122.595  1.00128.48           C  
ANISOU  282  CE1 PHE A  34    10820  21841  16157   -484   -280  -1027       C  
ATOM    283  CE2 PHE A  34     -30.068  -8.340 122.805  1.00130.84           C  
ANISOU  283  CE2 PHE A  34    10896  22260  16556  -1124   -184  -1258       C  
ATOM    284  CZ  PHE A  34     -28.940  -7.642 122.461  1.00128.41           C  
ANISOU  284  CZ  PHE A  34    10820  21778  16191   -879   -272  -1121       C  
ATOM    285  N   ARG A  35     -34.611  -5.635 121.612  1.00122.73           N  
ANISOU  285  N   ARG A  35     8728  22491  15413   -205   -412  -1501       N  
ATOM    286  CA  ARG A  35     -35.140  -6.053 120.313  1.00113.91           C  
ANISOU  286  CA  ARG A  35     7451  21618  14211   -223   -619  -1616       C  
ATOM    287  C   ARG A  35     -35.630  -4.860 119.492  1.00103.16           C  
ANISOU  287  C   ARG A  35     5956  20492  12746    243   -774  -1551       C  
ATOM    288  O   ARG A  35     -35.359  -4.771 118.284  1.00 96.20           O  
ANISOU  288  O   ARG A  35     5136  19671  11746    384   -970  -1532       O  
ATOM    289  CB  ARG A  35     -36.266  -7.071 120.514  1.00 97.98           C  
ANISOU  289  CB  ARG A  35     5144  19830  12254   -579   -557  -1823       C  
ATOM    290  CG  ARG A  35     -35.892  -8.244 121.418  1.00100.52           C  
ANISOU  290  CG  ARG A  35     5599  19903  12689  -1036   -365  -1871       C  
ATOM    291  CD  ARG A  35     -37.094  -9.109 121.764  1.00117.03           C  
ANISOU  291  CD  ARG A  35     7399  22210  14857  -1361   -261  -2064       C  
ATOM    292  NE  ARG A  35     -37.502  -8.970 123.159  1.00127.76           N  
ANISOU  292  NE  ARG A  35     8695  23531  16318  -1438    -17  -2035       N  
ATOM    293  CZ  ARG A  35     -38.116  -9.921 123.858  1.00134.26           C  
ANISOU  293  CZ  ARG A  35     9407  24366  17240  -1813    162  -2150       C  
ATOM    294  NH1 ARG A  35     -38.392 -11.093 123.300  1.00137.48           N  
ANISOU  294  NH1 ARG A  35     9755  24810  17669  -2152    132  -2311       N  
ATOM    295  NH2 ARG A  35     -38.453  -9.705 125.122  1.00133.89           N  
ANISOU  295  NH2 ARG A  35     9318  24286  17268  -1851    388  -2107       N  
ATOM    296  N   LEU A  36     -36.349  -3.930 120.132  1.00111.55           N  
ANISOU  296  N   LEU A  36     6849  21681  13853    494   -678  -1508       N  
ATOM    297  CA  LEU A  36     -36.877  -2.772 119.412  1.00125.91           C  
ANISOU  297  CA  LEU A  36     8541  23711  15588    955   -802  -1428       C  
ATOM    298  C   LEU A  36     -35.762  -1.923 118.803  1.00122.19           C  
ANISOU  298  C   LEU A  36     8393  22999  15036   1284   -888  -1235       C  
ATOM    299  O   LEU A  36     -35.946  -1.334 117.729  1.00126.51           O  
ANISOU  299  O   LEU A  36     8909  23695  15464   1588  -1055  -1173       O  
ATOM    300  CB  LEU A  36     -37.757  -1.933 120.345  1.00138.10           C  
ANISOU  300  CB  LEU A  36     9874  25374  17223   1155   -644  -1410       C  
ATOM    301  CG  LEU A  36     -38.182  -0.524 119.930  1.00130.39           C  
ANISOU  301  CG  LEU A  36     8821  24518  16203   1681   -699  -1281       C  
ATOM    302  CD1 LEU A  36     -38.922  -0.511 118.594  1.00130.74           C  
ANISOU  302  CD1 LEU A  36     8645  24919  16110   1837   -936  -1323       C  
ATOM    303  CD2 LEU A  36     -39.045   0.093 121.018  1.00121.49           C  
ANISOU  303  CD2 LEU A  36     7482  23478  15199   1795   -502  -1295       C  
ATOM    304  N   CYS A  37     -34.600  -1.862 119.453  1.00125.47           N  
ANISOU  304  N   CYS A  37     9119  23049  15506   1224   -773  -1137       N  
ATOM    305  CA  CYS A  37     -33.467  -1.136 118.897  1.00121.56           C  
ANISOU  305  CA  CYS A  37     8944  22300  14944   1497   -840   -965       C  
ATOM    306  C   CYS A  37     -32.652  -1.972 117.917  1.00118.23           C  
ANISOU  306  C   CYS A  37     8702  21785  14436   1310   -998   -985       C  
ATOM    307  O   CYS A  37     -32.128  -1.418 116.946  1.00103.56           O  
ANISOU  307  O   CYS A  37     7006  19868  12473   1572  -1126   -874       O  
ATOM    308  CB  CYS A  37     -32.556  -0.629 120.021  1.00115.92           C  
ANISOU  308  CB  CYS A  37     8476  21249  14321   1534   -645   -859       C  
ATOM    309  SG  CYS A  37     -30.880  -0.194 119.514  1.00116.62           S  
ANISOU  309  SG  CYS A  37     8999  20956  14354   1691   -697   -688       S  
ATOM    310  N   LYS A  38     -32.503  -3.285 118.152  1.00122.53           N  
ANISOU  310  N   LYS A  38     9239  22291  15026    863   -976  -1119       N  
ATOM    311  CA  LYS A  38     -31.759  -4.142 117.229  1.00113.26           C  
ANISOU  311  CA  LYS A  38     8230  21018  13786    668  -1111  -1157       C  
ATOM    312  C   LYS A  38     -32.483  -4.282 115.903  1.00121.44           C  
ANISOU  312  C   LYS A  38     9083  22370  14687    747  -1311  -1245       C  
ATOM    313  O   LYS A  38     -31.870  -4.654 114.897  1.00124.66           O  
ANISOU  313  O   LYS A  38     9640  22723  15003    712  -1446  -1249       O  
ATOM    314  CB  LYS A  38     -31.573  -5.537 117.819  1.00111.44           C  
ANISOU  314  CB  LYS A  38     8017  20672  13652    168  -1014  -1287       C  
ATOM    315  CG  LYS A  38     -30.369  -5.774 118.642  1.00113.79           C  
ANISOU  315  CG  LYS A  38     8603  20601  14030     20   -886  -1192       C  
ATOM    316  CD  LYS A  38     -30.616  -6.973 119.534  1.00121.49           C  
ANISOU  316  CD  LYS A  38     9520  21521  15119   -433   -731  -1307       C  
ATOM    317  CE  LYS A  38     -31.740  -7.791 118.939  1.00124.44           C  
ANISOU  317  CE  LYS A  38     9621  22179  15481   -645   -798  -1506       C  
ATOM    318  NZ  LYS A  38     -32.392  -8.568 120.030  1.00129.51           N  
ANISOU  318  NZ  LYS A  38    10129  22834  16244   -986   -599  -1604       N  
ATOM    319  N   LYS A  39     -33.778  -3.986 115.878  1.00119.51           N  
ANISOU  319  N   LYS A  39     8512  22472  14426    856  -1331  -1320       N  
ATOM    320  CA  LYS A  39     -34.493  -3.937 114.611  1.00116.77           C  
ANISOU  320  CA  LYS A  39     7975  22465  13926    994  -1528  -1386       C  
ATOM    321  C   LYS A  39     -34.334  -2.517 114.058  1.00128.07           C  
ANISOU  321  C   LYS A  39     9504  23902  15257   1518  -1599  -1178       C  
ATOM    322  O   LYS A  39     -35.204  -1.986 113.362  1.00114.05           O  
ANISOU  322  O   LYS A  39     7516  22447  13373   1777  -1712  -1173       O  
ATOM    323  CB  LYS A  39     -35.947  -4.397 114.818  1.00101.94           C  
ANISOU  323  CB  LYS A  39     5686  20970  12076    832  -1519  -1579       C  
ATOM    324  CG  LYS A  39     -36.960  -4.058 113.736  1.00108.76           C  
ANISOU  324  CG  LYS A  39     6269  22269  12784   1057  -1703  -1635       C  
ATOM    325  CD  LYS A  39     -38.178  -4.954 113.753  1.00111.66           C  
ANISOU  325  CD  LYS A  39     6260  22995  13171    753  -1715  -1886       C  
ATOM    326  CE  LYS A  39     -38.075  -6.065 112.725  1.00113.86           C  
ANISOU  326  CE  LYS A  39     6531  23383  13349    456  -1850  -2066       C  
ATOM    327  NZ  LYS A  39     -38.052  -5.506 111.347  1.00114.63           N  
ANISOU  327  NZ  LYS A  39     6632  23692  13229    778  -2069  -2001       N  
ATOM    328  N   HIS A  40     -33.206  -1.880 114.360  1.00159.73           N  
ANISOU  328  N   HIS A  40    13843  27546  19300   1683  -1524   -998       N  
ATOM    329  CA  HIS A  40     -32.890  -0.601 113.746  1.00170.12           C  
ANISOU  329  CA  HIS A  40    15316  28797  20523   2153  -1573   -794       C  
ATOM    330  C   HIS A  40     -31.568  -0.681 112.994  1.00175.21           C  
ANISOU  330  C   HIS A  40    16316  29163  21092   2167  -1644   -695       C  
ATOM    331  O   HIS A  40     -30.682  -1.477 113.316  1.00172.85           O  
ANISOU  331  O   HIS A  40    16195  28621  20858   1864  -1603   -740       O  
ATOM    332  CB  HIS A  40     -32.837   0.538 114.768  1.00168.22           C  
ANISOU  332  CB  HIS A  40    15144  28374  20397   2424  -1393   -652       C  
ATOM    333  CG  HIS A  40     -32.821   1.894 114.140  1.00170.00           C  
ANISOU  333  CG  HIS A  40    15477  28576  20541   2920  -1421   -455       C  
ATOM    334  ND1 HIS A  40     -33.333   2.130 112.882  1.00174.20           N  
ANISOU  334  ND1 HIS A  40    15909  29376  20903   3137  -1597   -423       N  
ATOM    335  CD2 HIS A  40     -32.348   3.082 114.583  1.00169.36           C  
ANISOU  335  CD2 HIS A  40    15604  28224  20522   3237  -1283   -279       C  
ATOM    336  CE1 HIS A  40     -33.179   3.405 112.579  1.00174.80           C  
ANISOU  336  CE1 HIS A  40    16134  29340  20942   3571  -1562   -220       C  
ATOM    337  NE2 HIS A  40     -32.586   4.006 113.595  1.00172.25           N  
ANISOU  337  NE2 HIS A  40    16004  28677  20766   3635  -1368   -134       N  
ATOM    338  N   LYS A  41     -31.461   0.171 111.976  1.00182.45           N  
ANISOU  338  N   LYS A  41    17333  30120  21868   2532  -1743   -553       N  
ATOM    339  CA  LYS A  41     -30.306   0.252 111.092  1.00175.10           C  
ANISOU  339  CA  LYS A  41    16729  28959  20842   2606  -1813   -444       C  
ATOM    340  C   LYS A  41     -29.891   1.713 110.983  1.00171.09           C  
ANISOU  340  C   LYS A  41    16444  28248  20314   3060  -1740   -203       C  
ATOM    341  O   LYS A  41     -30.716   2.572 110.653  1.00183.13           O  
ANISOU  341  O   LYS A  41    17829  29978  21772   3390  -1762   -123       O  
ATOM    342  CB  LYS A  41     -30.643  -0.330 109.713  1.00175.36           C  
ANISOU  342  CB  LYS A  41    16659  29282  20689   2556  -2016   -536       C  
ATOM    343  CG  LYS A  41     -31.910   0.264 109.097  1.00179.00           C  
ANISOU  343  CG  LYS A  41    16830  30161  21022   2843  -2115   -527       C  
ATOM    344  CD  LYS A  41     -32.466  -0.563 107.943  1.00178.50           C  
ANISOU  344  CD  LYS A  41    16570  30468  20786   2696  -2309   -691       C  
ATOM    345  CE  LYS A  41     -31.450  -0.795 106.834  1.00171.87           C  
ANISOU  345  CE  LYS A  41    16008  29485  19808   2691  -2407   -642       C  
ATOM    346  NZ  LYS A  41     -31.725  -2.062 106.092  1.00169.81           N  
ANISOU  346  NZ  LYS A  41    15593  29473  19455   2346  -2544   -880       N  
ATOM    347  N   THR A  42     -28.630   2.002 111.300  1.00151.56           N  
ANISOU  347  N   THR A  42    14313  25366  17907   3074  -1640    -90       N  
ATOM    348  CA  THR A  42     -28.067   3.332 111.114  1.00149.53           C  
ANISOU  348  CA  THR A  42    14323  24855  17636   3466  -1551    132       C  
ATOM    349  C   THR A  42     -26.696   3.181 110.476  1.00151.11           C  
ANISOU  349  C   THR A  42    14876  24752  17786   3419  -1575    210       C  
ATOM    350  O   THR A  42     -26.063   2.127 110.573  1.00150.57           O  
ANISOU  350  O   THR A  42    14865  24596  17749   3081  -1615    102       O  
ATOM    351  CB  THR A  42     -27.946   4.112 112.431  1.00140.54           C  
ANISOU  351  CB  THR A  42    13247  23481  16671   3570  -1337    195       C  
ATOM    352  OG1 THR A  42     -27.070   3.414 113.324  1.00137.84           O  
ANISOU  352  OG1 THR A  42    13028  22898  16448   3251  -1254    122       O  
ATOM    353  CG2 THR A  42     -29.307   4.284 113.090  1.00138.67           C  
ANISOU  353  CG2 THR A  42    12657  23536  16493   3621  -1296    116       C  
ATOM    354  N   LYS A  43     -26.232   4.246 109.822  1.00166.83           N  
ANISOU  354  N   LYS A  43    17111  26570  19707   3759  -1538    401       N  
ATOM    355  CA  LYS A  43     -24.956   4.185 109.130  1.00170.69           C  
ANISOU  355  CA  LYS A  43    17936  26776  20141   3736  -1551    482       C  
ATOM    356  C   LYS A  43     -23.932   5.219 109.582  1.00174.99           C  
ANISOU  356  C   LYS A  43    18826  26878  20784   3920  -1359    648       C  
ATOM    357  O   LYS A  43     -22.779   5.132 109.145  1.00184.62           O  
ANISOU  357  O   LYS A  43    20333  27829  21985   3867  -1347    705       O  
ATOM    358  CB  LYS A  43     -25.150   4.320 107.610  1.00167.56           C  
ANISOU  358  CB  LYS A  43    17559  26575  19532   3916  -1696    545       C  
ATOM    359  CG  LYS A  43     -26.497   3.859 107.047  1.00163.03           C  
ANISOU  359  CG  LYS A  43    16611  26503  18829   3909  -1865    427       C  
ATOM    360  CD  LYS A  43     -26.678   2.350 107.049  1.00154.96           C  
ANISOU  360  CD  LYS A  43    15395  25675  17807   3477  -1991    188       C  
ATOM    361  CE  LYS A  43     -27.971   1.973 106.342  1.00153.15           C  
ANISOU  361  CE  LYS A  43    14812  25946  17432   3485  -2155     67       C  
ATOM    362  NZ  LYS A  43     -28.694   0.884 107.039  1.00151.22           N  
ANISOU  362  NZ  LYS A  43    14265  25910  17281   3117  -2183   -168       N  
ATOM    363  N   LYS A  44     -24.295   6.186 110.440  1.00171.08           N  
ANISOU  363  N   LYS A  44    18316  26289  20400   4122  -1197    717       N  
ATOM    364  CA  LYS A  44     -23.251   7.071 110.955  1.00162.82           C  
ANISOU  364  CA  LYS A  44    17603  24797  19464   4235   -997    836       C  
ATOM    365  C   LYS A  44     -23.380   7.507 112.420  1.00164.13           C  
ANISOU  365  C   LYS A  44    17700  24851  19811   4212   -822    790       C  
ATOM    366  O   LYS A  44     -22.565   7.073 113.242  1.00151.17           O  
ANISOU  366  O   LYS A  44    16120  23047  18270   3959   -766    708       O  
ATOM    367  CB  LYS A  44     -23.128   8.336 110.091  1.00153.80           C  
ANISOU  367  CB  LYS A  44    16678  23515  18242   4608   -925   1035       C  
ATOM    368  CG  LYS A  44     -22.349   8.144 108.790  1.00148.09           C  
ANISOU  368  CG  LYS A  44    16174  22723  17372   4612  -1016   1107       C  
ATOM    369  CD  LYS A  44     -21.117   9.041 108.712  1.00142.89           C  
ANISOU  369  CD  LYS A  44    15922  21600  16770   4721   -830   1249       C  
ATOM    370  CE  LYS A  44     -20.107   8.491 107.709  1.00135.14           C  
ANISOU  370  CE  LYS A  44    15150  20512  15684   4593   -913   1263       C  
ATOM    371  NZ  LYS A  44     -19.281   9.560 107.081  1.00132.28           N  
ANISOU  371  NZ  LYS A  44    15136  19825  15298   4800   -758   1436       N  
ATOM    372  N   PRO A  45     -24.371   8.350 112.814  1.00177.40           N  
ANISOU  372  N   PRO A  45    19252  26616  21538   4470   -723    835       N  
ATOM    373  CA  PRO A  45     -24.276   8.928 114.165  1.00176.04           C  
ANISOU  373  CA  PRO A  45    19112  26230  21544   4484   -505    810       C  
ATOM    374  C   PRO A  45     -24.733   7.991 115.279  1.00168.30           C  
ANISOU  374  C   PRO A  45    17860  25439  20648   4188   -510    629       C  
ATOM    375  O   PRO A  45     -25.935   7.779 115.474  1.00174.27           O  
ANISOU  375  O   PRO A  45    18292  26522  21401   4193   -559    552       O  
ATOM    376  CB  PRO A  45     -25.171  10.169 114.069  1.00180.57           C  
ANISOU  376  CB  PRO A  45    19628  26846  22134   4860   -407    916       C  
ATOM    377  CG  PRO A  45     -26.225   9.781 113.089  1.00185.35           C  
ANISOU  377  CG  PRO A  45    19963  27879  22583   4942   -617    916       C  
ATOM    378  CD  PRO A  45     -25.632   8.748 112.153  1.00183.56           C  
ANISOU  378  CD  PRO A  45    19795  27731  22217   4721   -811    880       C  
ATOM    379  N   VAL A  46     -23.747   7.440 115.985  1.00147.11           N  
ANISOU  379  N   VAL A  46    15303  22554  18040   3929   -447    562       N  
ATOM    380  CA  VAL A  46     -23.983   6.508 117.078  1.00133.75           C  
ANISOU  380  CA  VAL A  46    13389  21011  16418   3617   -429    403       C  
ATOM    381  C   VAL A  46     -23.067   6.732 118.285  1.00127.74           C  
ANISOU  381  C   VAL A  46    12825  19934  15776   3542   -226    389       C  
ATOM    382  O   VAL A  46     -21.844   6.800 118.169  1.00130.01           O  
ANISOU  382  O   VAL A  46    13415  19917  16066   3552   -192    460       O  
ATOM    383  CB  VAL A  46     -23.838   5.047 116.609  1.00124.62           C  
ANISOU  383  CB  VAL A  46    12127  20038  15186   3277   -626    307       C  
ATOM    384  CG1 VAL A  46     -25.052   4.629 115.793  1.00119.32           C  
ANISOU  384  CG1 VAL A  46    11173  19751  14412   3288   -801    254       C  
ATOM    385  CG2 VAL A  46     -22.560   4.873 115.802  1.00123.77           C  
ANISOU  385  CG2 VAL A  46    12327  19679  15022   3238   -697    384       C  
ATOM    386  N   GLN A  47     -23.709   6.839 119.440  1.00113.81           N  
ANISOU  386  N   GLN A  47    10890  18248  14106   3460    -78    289       N  
ATOM    387  CA  GLN A  47     -23.108   7.027 120.731  1.00 98.93           C  
ANISOU  387  CA  GLN A  47     9160  16116  12312   3353    122    244       C  
ATOM    388  C   GLN A  47     -23.605   5.714 121.287  1.00 92.65           C  
ANISOU  388  C   GLN A  47     8103  15546  11552   3057    182     97       C  
ATOM    389  O   GLN A  47     -24.682   5.252 120.911  1.00104.23           O  
ANISOU  389  O   GLN A  47     9507  17002  13092   3088    381     33       O  
ATOM    390  CB  GLN A  47     -23.746   8.201 121.466  1.00 99.49           C  
ANISOU  390  CB  GLN A  47     9427  15903  12472   3647    350    297       C  
ATOM    391  CG  GLN A  47     -22.950   8.689 122.665  1.00105.08           C  
ANISOU  391  CG  GLN A  47    10351  16324  13252   3531    555    239       C  
ATOM    392  CD  GLN A  47     -21.686   9.425 122.266  1.00107.47           C  
ANISOU  392  CD  GLN A  47    10981  16321  13531   3515    520    319       C  
ATOM    393  OE1 GLN A  47     -21.528   9.830 121.114  1.00108.60           O  
ANISOU  393  OE1 GLN A  47    11128  16541  13595   3390    319    361       O  
ATOM    394  NE2 GLN A  47     -20.778   9.603 123.218  1.00104.96           N  
ANISOU  394  NE2 GLN A  47    10946  15645  13289   3620    728    325       N  
ATOM    395  N   ILE A  48     -22.810   5.066 122.130  1.00 86.84           N  
ANISOU  395  N   ILE A  48     7221  15012  10761   2752     18     39       N  
ATOM    396  CA  ILE A  48     -23.205   3.772 122.677  1.00 85.11           C  
ANISOU  396  CA  ILE A  48     6880  14898  10560   2368     63    -69       C  
ATOM    397  C   ILE A  48     -23.935   3.946 123.995  1.00 94.34           C  
ANISOU  397  C   ILE A  48     7887  16167  11791   2321    274   -161       C  
ATOM    398  O   ILE A  48     -24.996   3.363 124.223  1.00101.32           O  
ANISOU  398  O   ILE A  48     8496  17317  12682   2207    255   -242       O  
ATOM    399  CB  ILE A  48     -21.987   2.855 122.893  1.00 80.91           C  
ANISOU  399  CB  ILE A  48     6597  14122  10023   2214     86    -34       C  
ATOM    400  CG1 ILE A  48     -21.268   2.603 121.566  1.00 88.74           C  
ANISOU  400  CG1 ILE A  48     7744  15018  10957   2221   -123     47       C  
ATOM    401  CG2 ILE A  48     -22.415   1.542 123.530  1.00 80.05           C  
ANISOU  401  CG2 ILE A  48     6370  14129   9917   1804    125   -119       C  
ATOM    402  CD1 ILE A  48     -20.671   3.849 120.949  1.00 86.45           C  
ANISOU  402  CD1 ILE A  48     7684  14517  10646   2585   -145    167       C  
ATOM    403  N   LEU A  49     -23.348   4.760 124.859  1.00 93.70           N  
ANISOU  403  N   LEU A  49     7984  15870  11749   2390    484   -164       N  
ATOM    404  CA  LEU A  49     -23.912   5.047 126.177  1.00 81.57           C  
ANISOU  404  CA  LEU A  49     6339  14400  10256   2327    711   -263       C  
ATOM    405  C   LEU A  49     -25.318   5.673 126.075  1.00 98.09           C  
ANISOU  405  C   LEU A  49     8208  16664  12399   2543    743   -289       C  
ATOM    406  O   LEU A  49     -26.246   5.283 126.799  1.00 85.48           O  
ANISOU  406  O   LEU A  49     6375  15284  10821   2386    818   -383       O  
ATOM    407  CB  LEU A  49     -23.013   6.008 126.941  1.00 76.57           C  
ANISOU  407  CB  LEU A  49     5974  13474   9647   2443    932   -270       C  
ATOM    408  CG  LEU A  49     -21.728   5.414 127.504  1.00 90.90           C  
ANISOU  408  CG  LEU A  49     7970  15166  11404   2185    971   -281       C  
ATOM    409  CD1 LEU A  49     -21.115   6.360 128.539  1.00 89.60           C  
ANISOU  409  CD1 LEU A  49     8033  14762  11249   2239   1228   -349       C  
ATOM    410  CD2 LEU A  49     -21.985   4.053 128.075  1.00 91.57           C  
ANISOU  410  CD2 LEU A  49     7888  15469  11436   1774    924   -328       C  
ATOM    411  N   ALA A  50     -25.465   6.643 125.172  1.00111.82           N  
ANISOU  411  N   ALA A  50    10026  18302  14159   2903    692   -196       N  
ATOM    412  CA  ALA A  50     -26.731   7.346 125.013  1.00116.45           C  
ANISOU  412  CA  ALA A  50    10410  19039  14796   3153    723   -199       C  
ATOM    413  C   ALA A  50     -27.868   6.379 124.691  1.00113.97           C  
ANISOU  413  C   ALA A  50     9750  19108  14445   2985    562   -259       C  
ATOM    414  O   ALA A  50     -28.934   6.433 125.309  1.00107.89           O  
ANISOU  414  O   ALA A  50     8734  18533  13727   2971    660   -342       O  
ATOM    415  CB  ALA A  50     -26.589   8.416 123.929  1.00110.09           C  
ANISOU  415  CB  ALA A  50     9775  18059  13994   3541    668    -58       C  
ATOM    416  N   LEU A  51     -27.647   5.463 123.749  1.00104.60           N  
ANISOU  416  N   LEU A  51     8545  18024  13174   2834    330   -236       N  
ATOM    417  CA  LEU A  51     -28.704   4.542 123.337  1.00 96.15           C  
ANISOU  417  CA  LEU A  51     7164  17300  12068   2658    178   -315       C  
ATOM    418  C   LEU A  51     -28.976   3.476 124.388  1.00 96.70           C  
ANISOU  418  C   LEU A  51     7079  17496  12167   2246    268   -447       C  
ATOM    419  O   LEU A  51     -30.129   3.046 124.559  1.00 98.16           O  
ANISOU  419  O   LEU A  51     6972  17951  12372   2134    265   -542       O  
ATOM    420  CB  LEU A  51     -28.332   3.871 122.015  1.00 93.54           C  
ANISOU  420  CB  LEU A  51     6889  17016  11636   2596    -76   -273       C  
ATOM    421  CG  LEU A  51     -28.221   4.770 120.785  1.00110.18           C  
ANISOU  421  CG  LEU A  51     9213  18967  13685   2954   -171   -123       C  
ATOM    422  CD1 LEU A  51     -27.711   3.969 119.631  1.00111.30           C  
ANISOU  422  CD1 LEU A  51     9703  18755  13830   2937   -119    -46       C  
ATOM    423  CD2 LEU A  51     -29.594   5.365 120.452  1.00116.56           C  
ANISOU  423  CD2 LEU A  51     9915  19997  14374   2931   -422   -122       C  
ATOM    424  N   LEU A  52     -27.936   3.009 125.078  1.00 94.18           N  
ANISOU  424  N   LEU A  52     6953  16987  11844   2008    352   -451       N  
ATOM    425  CA  LEU A  52     -28.189   2.107 126.195  1.00 93.74           C  
ANISOU  425  CA  LEU A  52     6786  17022  11810   1631    480   -552       C  
ATOM    426  C   LEU A  52     -29.092   2.773 127.218  1.00113.26           C  
ANISOU  426  C   LEU A  52     9106  19583  14344   1727    697   -616       C  
ATOM    427  O   LEU A  52     -30.036   2.144 127.712  1.00120.36           O  
ANISOU  427  O   LEU A  52     9771  20692  15268   1513    750   -709       O  
ATOM    428  CB  LEU A  52     -26.881   1.656 126.847  1.00 70.61           C  
ANISOU  428  CB  LEU A  52     4108  13868   8851   1400    556   -522       C  
ATOM    429  CG  LEU A  52     -26.464   0.290 126.316  1.00 66.69           C  
ANISOU  429  CG  LEU A  52     3632  13387   8319   1063    394   -525       C  
ATOM    430  CD1 LEU A  52     -25.220  -0.155 127.022  1.00 66.70           C  
ANISOU  430  CD1 LEU A  52     3866  13183   8295    838    478   -481       C  
ATOM    431  CD2 LEU A  52     -27.582  -0.721 126.491  1.00 68.37           C  
ANISOU  431  CD2 LEU A  52     3585  13836   8557    770    390   -632       C  
ATOM    432  N   GLN A  53     -28.851   4.060 127.505  1.00114.84           N  
ANISOU  432  N   GLN A  53     9440  19613  14580   2051    834   -573       N  
ATOM    433  CA  GLN A  53     -29.723   4.809 128.411  1.00113.59           C  
ANISOU  433  CA  GLN A  53     9148  19517  14495   2180   1052   -639       C  
ATOM    434  C   GLN A  53     -31.198   4.705 128.043  1.00111.33           C  
ANISOU  434  C   GLN A  53     8512  19538  14249   2246    984   -688       C  
ATOM    435  O   GLN A  53     -32.055   4.856 128.919  1.00121.10           O  
ANISOU  435  O   GLN A  53     9572  20896  15545   2213   1159   -771       O  
ATOM    436  CB  GLN A  53     -29.318   6.287 128.455  1.00110.97           C  
ANISOU  436  CB  GLN A  53     9019  18929  14214   2565   1185   -583       C  
ATOM    437  CG  GLN A  53     -28.251   6.603 129.484  1.00107.31           C  
ANISOU  437  CG  GLN A  53     8830  18206  13737   2473   1394   -613       C  
ATOM    438  CD  GLN A  53     -27.826   8.061 129.484  1.00107.57           C  
ANISOU  438  CD  GLN A  53     9089  17946  13838   2827   1543   -581       C  
ATOM    439  OE1 GLN A  53     -28.656   8.966 129.396  1.00110.84           O  
ANISOU  439  OE1 GLN A  53     9403  18368  14342   3108   1626   -583       O  
ATOM    440  NE2 GLN A  53     -26.520   8.293 129.572  1.00102.57           N  
ANISOU  440  NE2 GLN A  53     8765  17037  13169   2807   1585   -555       N  
ATOM    441  N   GLU A  54     -31.519   4.445 126.778  1.00106.77           N  
ANISOU  441  N   GLU A  54     7832  19102  13634   2332    740   -646       N  
ATOM    442  CA  GLU A  54     -32.907   4.292 126.368  1.00103.27           C  
ANISOU  442  CA  GLU A  54     7042  18984  13211   2382    658   -704       C  
ATOM    443  C   GLU A  54     -33.382   2.851 126.377  1.00107.66           C  
ANISOU  443  C   GLU A  54     7400  19766  13740   1962    571   -813       C  
ATOM    444  O   GLU A  54     -34.566   2.606 126.635  1.00107.89           O  
ANISOU  444  O   GLU A  54     7128  20053  13813   1890    610   -909       O  
ATOM    445  CB  GLU A  54     -33.120   4.887 124.974  1.00101.40           C  
ANISOU  445  CB  GLU A  54     6787  18811  12929   2728    451   -605       C  
ATOM    446  CG  GLU A  54     -32.436   6.224 124.795  1.00104.51           C  
ANISOU  446  CG  GLU A  54     7453  18910  13347   3117    527   -472       C  
ATOM    447  CD  GLU A  54     -32.931   7.258 125.789  1.00120.33           C  
ANISOU  447  CD  GLU A  54     9415  20835  15468   3320    790   -498       C  
ATOM    448  OE1 GLU A  54     -32.118   8.099 126.225  1.00123.42           O  
ANISOU  448  OE1 GLU A  54    10083  20906  15904   3466    953   -452       O  
ATOM    449  OE2 GLU A  54     -34.131   7.228 126.138  1.00129.72           O1-
ANISOU  449  OE2 GLU A  54    10297  22278  16713   3326    845   -577       O1-
ATOM    450  N   ILE A  55     -32.504   1.889 126.096  1.00116.03           N  
ANISOU  450  N   ILE A  55     8622  20723  14740   1679    467   -807       N  
ATOM    451  CA  ILE A  55     -32.925   0.495 126.261  1.00128.38           C  
ANISOU  451  CA  ILE A  55    10033  22442  16303   1246    439   -918       C  
ATOM    452  C   ILE A  55     -33.252   0.211 127.723  1.00134.22           C  
ANISOU  452  C   ILE A  55    10716  23181  17101   1007    695   -987       C  
ATOM    453  O   ILE A  55     -34.319  -0.329 128.043  1.00138.29           O  
ANISOU  453  O   ILE A  55    10970  23916  17658    826    750  -1092       O  
ATOM    454  CB  ILE A  55     -31.878  -0.493 125.717  1.00125.39           C  
ANISOU  454  CB  ILE A  55     9863  21914  15867    984    303   -893       C  
ATOM    455  CG1 ILE A  55     -31.911  -0.497 124.190  1.00117.41           C  
ANISOU  455  CG1 ILE A  55     8827  20996  14786   1143     41   -870       C  
ATOM    456  CG2 ILE A  55     -32.181  -1.900 126.210  1.00130.76           C  
ANISOU  456  CG2 ILE A  55    10450  22660  16573    509    358   -999       C  
ATOM    457  CD1 ILE A  55     -30.586  -0.860 123.557  1.00113.50           C  
ANISOU  457  CD1 ILE A  55     8625  20266  14234   1077    -79   -792       C  
ATOM    458  N   ILE A  56     -32.356   0.575 128.636  1.00136.67           N  
ANISOU  458  N   ILE A  56    11270  23253  17403    999    863   -934       N  
ATOM    459  CA  ILE A  56     -32.672   0.330 130.041  1.00131.46           C  
ANISOU  459  CA  ILE A  56    10576  22603  16771    776   1114   -994       C  
ATOM    460  C   ILE A  56     -33.440   1.535 130.578  1.00133.23           C  
ANISOU  460  C   ILE A  56    10672  22894  17055   1088   1279  -1020       C  
ATOM    461  O   ILE A  56     -32.964   2.674 130.484  1.00137.99           O  
ANISOU  461  O   ILE A  56    11424  23340  17666   1421   1313   -959       O  
ATOM    462  CB  ILE A  56     -31.412  -0.042 130.849  1.00128.92           C  
ANISOU  462  CB  ILE A  56    10564  22031  16387    554   1224   -939       C  
ATOM    463  CG1 ILE A  56     -30.185   0.777 130.471  1.00128.21           C  
ANISOU  463  CG1 ILE A  56    10750  21706  16257    806   1168   -842       C  
ATOM    464  CG2 ILE A  56     -31.045  -1.488 130.581  1.00125.94           C  
ANISOU  464  CG2 ILE A  56    10238  21629  15984    161   1124   -935       C  
ATOM    465  CD1 ILE A  56     -30.118   2.117 131.150  1.00135.00           C  
ANISOU  465  CD1 ILE A  56    11693  22463  17137   1104   1357   -842       C  
ATOM    466  N   PRO A  57     -34.660   1.346 131.071  1.00128.30           N  
ANISOU  466  N   PRO A  57     9768  22492  16489   1004   1386  -1114       N  
ATOM    467  CA  PRO A  57     -35.395   2.498 131.597  1.00122.65           C  
ANISOU  467  CA  PRO A  57     8928  21829  15844   1306   1558  -1140       C  
ATOM    468  C   PRO A  57     -34.751   3.019 132.866  1.00114.33           C  
ANISOU  468  C   PRO A  57     8108  20560  14772   1290   1820  -1138       C  
ATOM    469  O   PRO A  57     -34.264   2.256 133.707  1.00115.85           O  
ANISOU  469  O   PRO A  57     8437  20680  14899    955   1927  -1150       O  
ATOM    470  CB  PRO A  57     -36.796   1.946 131.871  1.00125.19           C  
ANISOU  470  CB  PRO A  57     8892  22448  16226   1147   1613  -1249       C  
ATOM    471  CG  PRO A  57     -36.602   0.477 131.979  1.00120.82           C  
ANISOU  471  CG  PRO A  57     8362  21918  15628    684   1570  -1284       C  
ATOM    472  CD  PRO A  57     -35.451   0.107 131.103  1.00120.09           C  
ANISOU  472  CD  PRO A  57     8508  21656  15464    646   1361  -1203       C  
ATOM    473  N   LYS A  58     -34.783   4.351 133.010  1.00102.86           N  
ANISOU  473  N   LYS A  58     6709  19001  13374   1659   1935  -1123       N  
ATOM    474  CA  LYS A  58     -34.305   4.962 134.245  1.00 95.41           C  
ANISOU  474  CA  LYS A  58     5970  17868  12414   1660   2210  -1155       C  
ATOM    475  C   LYS A  58     -35.008   4.354 135.447  1.00108.82           C  
ANISOU  475  C   LYS A  58     7537  19711  14100   1364   2417  -1244       C  
ATOM    476  O   LYS A  58     -34.474   4.380 136.561  1.00 94.35           O  
ANISOU  476  O   LYS A  58     5905  17752  12192   1212   2618  -1269       O  
ATOM    477  CB  LYS A  58     -34.536   6.471 134.238  1.00 92.68           C  
ANISOU  477  CB  LYS A  58     5647  17401  12165   2093   2340  -1156       C  
ATOM    478  CG  LYS A  58     -34.401   7.196 132.903  1.00 94.24           C  
ANISOU  478  CG  LYS A  58     5866  17528  12414   2465   2142  -1060       C  
ATOM    479  CD  LYS A  58     -33.139   6.886 132.119  1.00117.68           C  
ANISOU  479  CD  LYS A  58     9096  20324  15295   2423   1941   -964       C  
ATOM    480  CE  LYS A  58     -33.442   6.809 130.631  1.00122.08           C  
ANISOU  480  CE  LYS A  58     9529  21000  15854   2610   1653   -877       C  
ATOM    481  NZ  LYS A  58     -33.807   5.421 130.213  1.00126.96           N  
ANISOU  481  NZ  LYS A  58     9956  21872  16411   2281   1459   -906       N  
ATOM    482  N   SER A  59     -36.195   3.790 135.226  1.00128.19           N  
ANISOU  482  N   SER A  59     9660  22433  16612   1275   2371  -1294       N  
ATOM    483  CA  SER A  59     -36.992   3.216 136.296  1.00124.05           C  
ANISOU  483  CA  SER A  59     8985  22057  16091   1006   2574  -1376       C  
ATOM    484  C   SER A  59     -36.318   2.008 136.928  1.00125.93           C  
ANISOU  484  C   SER A  59     9409  22224  16213    565   2607  -1355       C  
ATOM    485  O   SER A  59     -36.679   1.625 138.045  1.00130.23           O  
ANISOU  485  O   SER A  59     9942  22815  16725    340   2823  -1398       O  
ATOM    486  CB  SER A  59     -38.358   2.822 135.750  1.00115.75           C  
ANISOU  486  CB  SER A  59     7533  21311  15134   1000   2488  -1437       C  
ATOM    487  OG  SER A  59     -38.779   3.748 134.771  1.00114.09           O  
ANISOU  487  OG  SER A  59     7177  21167  15006   1407   2353  -1415       O  
ATOM    488  N   TYR A  60     -35.356   1.389 136.240  1.00128.74           N  
ANISOU  488  N   TYR A  60     9944  22465  16508    443   2405  -1281       N  
ATOM    489  CA  TYR A  60     -34.600   0.302 136.855  1.00114.42           C  
ANISOU  489  CA  TYR A  60     8344  20542  14588     52   2447  -1236       C  
ATOM    490  C   TYR A  60     -33.709   0.813 137.981  1.00112.93           C  
ANISOU  490  C   TYR A  60     8457  20164  14287     47   2643  -1210       C  
ATOM    491  O   TYR A  60     -33.354   0.049 138.885  1.00110.45           O  
ANISOU  491  O   TYR A  60     8295  19800  13871   -262   2760  -1179       O  
ATOM    492  CB  TYR A  60     -33.752  -0.417 135.806  1.00 94.28           C  
ANISOU  492  CB  TYR A  60     5914  17897  12010    -51   2191  -1161       C  
ATOM    493  CG  TYR A  60     -32.870  -1.525 136.358  1.00 88.96           C  
ANISOU  493  CG  TYR A  60     5486  17076  11238   -427   2226  -1090       C  
ATOM    494  CD1 TYR A  60     -33.342  -2.817 136.489  1.00 91.83           C  
ANISOU  494  CD1 TYR A  60     5763  17507  11621   -783   2244  -1099       C  
ATOM    495  CD2 TYR A  60     -31.563  -1.275 136.734  1.00 83.82           C  
ANISOU  495  CD2 TYR A  60     5158  16209  10479   -419   2248  -1010       C  
ATOM    496  CE1 TYR A  60     -32.532  -3.821 136.981  1.00 92.84           C  
ANISOU  496  CE1 TYR A  60     6135  17470  11668  -1101   2288  -1008       C  
ATOM    497  CE2 TYR A  60     -30.749  -2.261 137.220  1.00 83.50           C  
ANISOU  497  CE2 TYR A  60     5343  16038  10345   -735   2273   -924       C  
ATOM    498  CZ  TYR A  60     -31.234  -3.530 137.348  1.00 92.63           C  
ANISOU  498  CZ  TYR A  60     6424  17243  11527  -1067   2296   -912       C  
ATOM    499  OH  TYR A  60     -30.403  -4.506 137.841  1.00 92.61           O  
ANISOU  499  OH  TYR A  60     6671  17080  11437  -1359   2334   -801       O  
ATOM    500  N   PHE A  61     -33.341   2.093 137.940  1.00113.42           N  
ANISOU  500  N   PHE A  61     8621  20111  14361    385   2685  -1222       N  
ATOM    501  CA  PHE A  61     -32.417   2.701 138.886  1.00114.71           C  
ANISOU  501  CA  PHE A  61     9085  20086  14414    404   2853  -1223       C  
ATOM    502  C   PHE A  61     -33.090   3.724 139.786  1.00122.41           C  
ANISOU  502  C   PHE A  61    10005  21085  15421    585   3116  -1320       C  
ATOM    503  O   PHE A  61     -32.692   3.863 140.945  1.00113.12           O  
ANISOU  503  O   PHE A  61     9022  19835  14124    465   3312  -1351       O  
ATOM    504  CB  PHE A  61     -31.264   3.352 138.116  1.00114.45           C  
ANISOU  504  CB  PHE A  61     9271  19844  14370    624   2710  -1170       C  
ATOM    505  CG  PHE A  61     -30.514   2.397 137.228  1.00106.89           C  
ANISOU  505  CG  PHE A  61     8388  18846  13379    460   2462  -1073       C  
ATOM    506  CD1 PHE A  61     -31.066   1.984 136.026  1.00105.36           C  
ANISOU  506  CD1 PHE A  61     7980  18774  13280    512   2245  -1051       C  
ATOM    507  CD2 PHE A  61     -29.282   1.870 137.625  1.00 76.87           C  
ANISOU  507  CD2 PHE A  61     4869  14895   9442    239   2449  -1007       C  
ATOM    508  CE1 PHE A  61     -30.396   1.105 135.184  1.00106.72           C  
ANISOU  508  CE1 PHE A  61     8225  18899  13425    358   2026   -975       C  
ATOM    509  CE2 PHE A  61     -28.584   0.968 136.792  1.00 93.23           C  
ANISOU  509  CE2 PHE A  61     7011  16915  11499     88   2232   -914       C  
ATOM    510  CZ  PHE A  61     -29.147   0.578 135.566  1.00 92.88           C  
ANISOU  510  CZ  PHE A  61     6755  16974  11560    143   2025   -903       C  
ATOM    511  N   GLY A  62     -34.112   4.416 139.287  1.00143.53           N  
ANISOU  511  N   GLY A  62    12420  23867  18248    867   3124  -1367       N  
ATOM    512  CA  GLY A  62     -34.951   5.263 140.109  1.00159.79           C  
ANISOU  512  CA  GLY A  62    14373  25974  20366   1024   3385  -1461       C  
ATOM    513  C   GLY A  62     -34.329   6.590 140.487  1.00166.66           C  
ANISOU  513  C   GLY A  62    15482  26606  21236   1291   3547  -1502       C  
ATOM    514  O   GLY A  62     -35.045   7.543 140.813  1.00176.95           O  
ANISOU  514  O   GLY A  62    16684  27907  22642   1532   3739  -1574       O  
ATOM    515  N   THR A  63     -33.000   6.674 140.451  1.00157.20           N  
ANISOU  515  N   THR A  63    14602  25196  19930   1248   3484  -1464       N  
ATOM    516  CA  THR A  63     -32.294   7.881 140.854  1.00151.20           C  
ANISOU  516  CA  THR A  63    14105  24185  19159   1453   3649  -1522       C  
ATOM    517  C   THR A  63     -31.143   8.140 139.892  1.00139.38           C  
ANISOU  517  C   THR A  63    12817  22478  17664   1577   3458  -1452       C  
ATOM    518  O   THR A  63     -30.855   7.342 138.995  1.00132.28           O  
ANISOU  518  O   THR A  63    11868  21637  16753   1491   3201  -1354       O  
ATOM    519  CB  THR A  63     -31.786   7.778 142.297  1.00146.87           C  
ANISOU  519  CB  THR A  63    13787  23597  18422   1204   3857  -1592       C  
ATOM    520  OG1 THR A  63     -31.237   6.473 142.523  1.00134.61           O  
ANISOU  520  OG1 THR A  63    12311  22128  16708    834   3725  -1516       O  
ATOM    521  CG2 THR A  63     -32.923   8.035 143.283  1.00150.14           C  
ANISOU  521  CG2 THR A  63    14037  24150  18859   1205   4119  -1684       C  
ATOM    522  N   THR A  64     -30.479   9.276 140.096  1.00138.44           N  
ANISOU  522  N   THR A  64    12941  22099  17561   1775   3600  -1509       N  
ATOM    523  CA  THR A  64     -29.405   9.741 139.230  1.00126.24           C  
ANISOU  523  CA  THR A  64    11612  20313  16040   1932   3469  -1457       C  
ATOM    524  C   THR A  64     -28.021   9.324 139.721  1.00111.05           C  
ANISOU  524  C   THR A  64     9991  18276  13925   1671   3439  -1462       C  
ATOM    525  O   THR A  64     -27.039   9.495 138.990  1.00105.29           O  
ANISOU  525  O   THR A  64     9437  17370  13198   1746   3307  -1412       O  
ATOM    526  CB  THR A  64     -29.485  11.271 139.096  1.00129.08           C  
ANISOU  526  CB  THR A  64    12073  20413  16559   2300   3659  -1523       C  
ATOM    527  OG1 THR A  64     -30.855  11.663 138.943  1.00132.32           O  
ANISOU  527  OG1 THR A  64    12193  20952  17131   2515   3737  -1536       O  
ATOM    528  CG2 THR A  64     -28.706  11.765 137.884  1.00125.35           C  
ANISOU  528  CG2 THR A  64    11749  19710  16168   2526   3496  -1442       C  
ATOM    529  N   THR A  65     -27.917   8.763 140.925  1.00109.11           N  
ANISOU  529  N   THR A  65     9812  18137  13509   1367   3549  -1514       N  
ATOM    530  CA  THR A  65     -26.636   8.313 141.462  1.00111.52           C  
ANISOU  530  CA  THR A  65    10392  18367  13612   1106   3505  -1512       C  
ATOM    531  C   THR A  65     -26.346   6.855 141.099  1.00121.01           C  
ANISOU  531  C   THR A  65    11534  19717  14727    825   3273  -1377       C  
ATOM    532  O   THR A  65     -25.259   6.538 140.597  1.00112.49           O  
ANISOU  532  O   THR A  65    10615  18535  13590    759   3112  -1310       O  
ATOM    533  CB  THR A  65     -26.616   8.506 142.983  1.00106.63           C  
ANISOU  533  CB  THR A  65     9907  17778  12828    933   3736  -1626       C  
ATOM    534  OG1 THR A  65     -26.848   9.885 143.297  1.00114.60           O  
ANISOU  534  OG1 THR A  65    10991  18624  13926   1193   3967  -1756       O  
ATOM    535  CG2 THR A  65     -25.278   8.080 143.566  1.00 94.70           C  
ANISOU  535  CG2 THR A  65     8681  16208  11093    671   3673  -1623       C  
ATOM    536  N   ASN A  66     -27.318   5.966 141.329  1.00146.03           N  
ANISOU  536  N   ASN A  66    14475  23110  17899    657   3267  -1338       N  
ATOM    537  CA  ASN A  66     -27.155   4.561 140.970  1.00145.07           C  
ANISOU  537  CA  ASN A  66    14296  23100  17723    384   3075  -1212       C  
ATOM    538  C   ASN A  66     -26.882   4.411 139.480  1.00141.73           C  
ANISOU  538  C   ASN A  66    13803  22628  17418    527   2826  -1127       C  
ATOM    539  O   ASN A  66     -26.056   3.580 139.062  1.00143.25           O  
ANISOU  539  O   ASN A  66    14099  22784  17547    354   2658  -1028       O  
ATOM    540  CB  ASN A  66     -28.414   3.778 141.365  1.00147.59           C  
ANISOU  540  CB  ASN A  66    14362  23643  18073    217   3140  -1207       C  
ATOM    541  CG  ASN A  66     -28.656   3.753 142.872  1.00145.82           C  
ANISOU  541  CG  ASN A  66    14221  23480  17706     42   3380  -1267       C  
ATOM    542  OD1 ASN A  66     -27.735   3.534 143.661  1.00137.46           O  
ANISOU  542  OD1 ASN A  66    13419  22353  16458   -136   3416  -1245       O  
ATOM    543  ND2 ASN A  66     -29.899   3.988 143.274  1.00150.41           N  
ANISOU  543  ND2 ASN A  66    14581  24202  18368    101   3540  -1340       N  
ATOM    544  N   LEU A  67     -27.563   5.218 138.661  1.00119.82           N  
ANISOU  544  N   LEU A  67    10864  19850  14813    854   2801  -1155       N  
ATOM    545  CA  LEU A  67     -27.397   5.096 137.222  1.00101.41           C  
ANISOU  545  CA  LEU A  67     8462  17492  12576   1010   2555  -1067       C  
ATOM    546  C   LEU A  67     -25.965   5.457 136.797  1.00 99.88           C  
ANISOU  546  C   LEU A  67     8554  17064  12332   1085   2474  -1026       C  
ATOM    547  O   LEU A  67     -25.376   4.774 135.949  1.00 84.93           O  
ANISOU  547  O   LEU A  67     6688  15156  10426   1013   2262   -928       O  
ATOM    548  CB  LEU A  67     -28.433   5.961 136.507  1.00 90.75           C  
ANISOU  548  CB  LEU A  67     6898  16187  11396   1367   2551  -1090       C  
ATOM    549  CG  LEU A  67     -29.431   5.057 135.812  1.00 81.39           C  
ANISOU  549  CG  LEU A  67     5406  15248  10270   1281   2379  -1050       C  
ATOM    550  CD1 LEU A  67     -30.221   5.702 134.689  1.00 79.99           C  
ANISOU  550  CD1 LEU A  67     5030  15131  10230   1631   2258  -1026       C  
ATOM    551  CD2 LEU A  67     -28.674   3.931 135.226  1.00 90.44           C  
ANISOU  551  CD2 LEU A  67     6626  16392  11345   1039   2164   -963       C  
ATOM    552  N   LYS A  68     -25.375   6.521 137.367  1.00106.65           N  
ANISOU  552  N   LYS A  68     9631  17727  13165   1218   2649  -1108       N  
ATOM    553  CA  LYS A  68     -23.995   6.838 137.008  1.00 94.30           C  
ANISOU  553  CA  LYS A  68     8339  15938  11552   1262   2586  -1086       C  
ATOM    554  C   LYS A  68     -23.031   5.800 137.568  1.00 81.30           C  
ANISOU  554  C   LYS A  68     6840  14326   9724    898   2524  -1043       C  
ATOM    555  O   LYS A  68     -21.997   5.526 136.957  1.00 83.19           O  
ANISOU  555  O   LYS A  68     7216  14461   9930    869   2379   -971       O  
ATOM    556  CB  LYS A  68     -23.623   8.229 137.480  1.00 95.67           C  
ANISOU  556  CB  LYS A  68     8719  15875  11756   1466   2802  -1208       C  
ATOM    557  CG  LYS A  68     -24.326   9.328 136.681  1.00 97.61           C  
ANISOU  557  CG  LYS A  68     8881  16001  12204   1869   2844  -1206       C  
ATOM    558  CD  LYS A  68     -23.818  10.692 137.051  1.00105.90           C  
ANISOU  558  CD  LYS A  68    10180  16746  13310   2051   3071  -1322       C  
ATOM    559  CE  LYS A  68     -23.428  11.501 135.831  1.00115.79           C  
ANISOU  559  CE  LYS A  68    11548  17738  14711   2371   2995  -1250       C  
ATOM    560  NZ  LYS A  68     -23.787  12.940 135.976  1.00127.96           N  
ANISOU  560  NZ  LYS A  68    13175  19028  16415   2641   3239  -1350       N  
ATOM    561  N   ARG A  69     -23.368   5.178 138.708  1.00 97.35           N  
ANISOU  561  N   ARG A  69     8849  16501  11636    622   2630  -1067       N  
ATOM    562  CA  ARG A  69     -22.538   4.079 139.212  1.00 94.95           C  
ANISOU  562  CA  ARG A  69     8685  16233  11161    279   2559   -983       C  
ATOM    563  C   ARG A  69     -22.537   2.885 138.255  1.00 96.51           C  
ANISOU  563  C   ARG A  69     8764  16499  11407    150   2336   -834       C  
ATOM    564  O   ARG A  69     -21.550   2.147 138.162  1.00 94.46           O  
ANISOU  564  O   ARG A  69     8652  16183  11056    -38   2226   -733       O  
ATOM    565  CB  ARG A  69     -23.032   3.654 140.584  1.00 96.69           C  
ANISOU  565  CB  ARG A  69     8906  16585  11249     41   2721  -1013       C  
ATOM    566  CG  ARG A  69     -22.424   4.473 141.708  1.00109.78           C  
ANISOU  566  CG  ARG A  69    10796  18156  12761     32   2892  -1134       C  
ATOM    567  CD  ARG A  69     -22.374   3.669 142.993  1.00115.22           C  
ANISOU  567  CD  ARG A  69    11572  18966  13241   -275   2966  -1093       C  
ATOM    568  NE  ARG A  69     -21.731   4.418 144.066  1.00115.02           N  
ANISOU  568  NE  ARG A  69    11773  18881  13050   -297   3098  -1216       N  
ATOM    569  CZ  ARG A  69     -20.935   3.883 144.985  1.00121.48           C  
ANISOU  569  CZ  ARG A  69    12785  19736  13635   -531   3080  -1166       C  
ATOM    570  NH1 ARG A  69     -20.664   2.579 144.963  1.00128.39           N  
ANISOU  570  NH1 ARG A  69    13677  20679  14427   -751   2951   -974       N  
ATOM    571  NH2 ARG A  69     -20.396   4.662 145.916  1.00118.46           N  
ANISOU  571  NH2 ARG A  69    12588  19316  13106   -536   3187  -1307       N  
ATOM    572  N   PHE A  70     -23.656   2.676 137.555  1.00 93.12           N  
ANISOU  572  N   PHE A  70     8068  16192  11121    239   2270   -825       N  
ATOM    573  CA  PHE A  70     -23.768   1.666 136.506  1.00 88.11           C  
ANISOU  573  CA  PHE A  70     7305  15614  10556    142   2054   -721       C  
ATOM    574  C   PHE A  70     -23.024   2.093 135.242  1.00 99.96           C  
ANISOU  574  C   PHE A  70     8871  16983  12125    375   1876   -674       C  
ATOM    575  O   PHE A  70     -22.428   1.269 134.523  1.00 89.95           O  
ANISOU  575  O   PHE A  70     7665  15653  10861    248   1689   -571       O  
ATOM    576  CB  PHE A  70     -25.245   1.445 136.215  1.00 86.17           C  
ANISOU  576  CB  PHE A  70     6754  15557  10429    174   2047   -762       C  
ATOM    577  CG  PHE A  70     -25.529   0.213 135.410  1.00 88.74           C  
ANISOU  577  CG  PHE A  70     6946  15964  10807    -23   1862   -692       C  
ATOM    578  CD1 PHE A  70     -25.769  -1.000 136.034  1.00 95.66           C  
ANISOU  578  CD1 PHE A  70     7812  16898  11637   -383   1912   -654       C  
ATOM    579  CD2 PHE A  70     -25.579   0.270 134.031  1.00 82.20           C  
ANISOU  579  CD2 PHE A  70     6021  15139  10074    151   1648   -667       C  
ATOM    580  CE1 PHE A  70     -26.038  -2.134 135.304  1.00 92.50           C  
ANISOU  580  CE1 PHE A  70     7310  16535  11300   -580   1767   -611       C  
ATOM    581  CE2 PHE A  70     -25.847  -0.856 133.289  1.00 81.25           C  
ANISOU  581  CE2 PHE A  70     5790  15085   9995    -47   1484   -633       C  
ATOM    582  CZ  PHE A  70     -26.085  -2.060 133.925  1.00 89.23           C  
ANISOU  582  CZ  PHE A  70     6792  16133  10977   -420   1551   -615       C  
ATOM    583  N   TYR A  71     -23.056   3.378 134.939  1.00119.23           N  
ANISOU  583  N   TYR A  71    11342  19324  14634    720   1931   -737       N  
ATOM    584  CA  TYR A  71     -22.449   3.780 133.685  1.00115.76           C  
ANISOU  584  CA  TYR A  71    10982  18735  14265    961   1762   -672       C  
ATOM    585  C   TYR A  71     -20.947   3.927 133.790  1.00108.24           C  
ANISOU  585  C   TYR A  71    10424  17452  13251    888   1712   -625       C  
ATOM    586  O   TYR A  71     -20.267   3.937 132.756  1.00102.87           O  
ANISOU  586  O   TYR A  71     9882  16584  12619    986   1532   -538       O  
ATOM    587  CB  TYR A  71     -23.124   5.037 133.162  1.00120.37           C  
ANISOU  587  CB  TYR A  71    11492  19272  14972   1367   1812   -713       C  
ATOM    588  CG  TYR A  71     -24.339   4.621 132.381  1.00121.34           C  
ANISOU  588  CG  TYR A  71    11325  19599  15181   1425   1667   -682       C  
ATOM    589  CD1 TYR A  71     -25.260   3.739 132.932  1.00120.53           C  
ANISOU  589  CD1 TYR A  71    11008  19723  15063   1163   1694   -720       C  
ATOM    590  CD2 TYR A  71     -24.552   5.066 131.091  1.00123.88           C  
ANISOU  590  CD2 TYR A  71    11600  19885  15582   1720   1503   -613       C  
ATOM    591  CE1 TYR A  71     -26.360   3.321 132.221  1.00120.82           C  
ANISOU  591  CE1 TYR A  71    10777  19958  15171   1187   1562   -716       C  
ATOM    592  CE2 TYR A  71     -25.658   4.663 130.377  1.00128.56           C  
ANISOU  592  CE2 TYR A  71    11927  20694  16224   1753   1356   -600       C  
ATOM    593  CZ  TYR A  71     -26.557   3.798 130.951  1.00125.21           C  
ANISOU  593  CZ  TYR A  71    11278  20504  15792   1482   1388   -664       C  
ATOM    594  OH  TYR A  71     -27.646   3.405 130.229  1.00124.41           O  
ANISOU  594  OH  TYR A  71    10911  20622  15737   1502   1247   -673       O  
ATOM    595  N   LYS A  72     -20.417   3.964 135.012  1.00 97.44           N  
ANISOU  595  N   LYS A  72     9225  16037  11762    700   1859   -681       N  
ATOM    596  CA  LYS A  72     -18.982   3.776 135.178  1.00 85.52           C  
ANISOU  596  CA  LYS A  72     8044  14279  10169    552   1777   -627       C  
ATOM    597  C   LYS A  72     -18.535   2.429 134.617  1.00 88.99           C  
ANISOU  597  C   LYS A  72     8520  14695  10597    325   1553   -473       C  
ATOM    598  O   LYS A  72     -17.537   2.351 133.887  1.00 94.68           O  
ANISOU  598  O   LYS A  72     9437  15191  11345    351   1395   -397       O  
ATOM    599  CB  LYS A  72     -18.599   3.898 136.650  1.00 85.99           C  
ANISOU  599  CB  LYS A  72     8233  14374  10065    363   1958   -714       C  
ATOM    600  CG  LYS A  72     -19.026   5.205 137.280  1.00 95.96           C  
ANISOU  600  CG  LYS A  72     9474  15651  11336    559   2208   -896       C  
ATOM    601  CD  LYS A  72     -17.861   6.160 137.474  1.00110.70           C  
ANISOU  601  CD  LYS A  72    11636  17250  13175    627   2263   -987       C  
ATOM    602  CE  LYS A  72     -17.514   6.315 138.940  1.00106.59           C  
ANISOU  602  CE  LYS A  72    11226  16814  12461    425   2439  -1119       C  
ATOM    603  NZ  LYS A  72     -16.161   6.907 139.167  1.00101.17           N  
ANISOU  603  NZ  LYS A  72    10828  15900  11711    384   2436  -1201       N  
ATOM    604  N   VAL A  73     -19.250   1.352 134.946  1.00 81.99           N  
ANISOU  604  N   VAL A  73     7451  14023   9679     96   1556   -431       N  
ATOM    605  CA  VAL A  73     -18.793   0.051 134.464  1.00 79.60           C  
ANISOU  605  CA  VAL A  73     7208  13661   9377   -132   1376   -293       C  
ATOM    606  C   VAL A  73     -19.085  -0.115 132.977  1.00 69.50           C  
ANISOU  606  C   VAL A  73     5809  12363   8233      6   1185   -260       C  
ATOM    607  O   VAL A  73     -18.297  -0.746 132.260  1.00 68.64           O  
ANISOU  607  O   VAL A  73     5849  12086   8145    -71   1013   -164       O  
ATOM    608  CB  VAL A  73     -19.372  -1.116 135.292  1.00 85.25           C  
ANISOU  608  CB  VAL A  73     7805  14566  10021   -451   1463   -249       C  
ATOM    609  CG1 VAL A  73     -18.573  -1.284 136.589  1.00 86.97           C  
ANISOU  609  CG1 VAL A  73     8250  14736  10060   -629   1570   -207       C  
ATOM    610  CG2 VAL A  73     -20.838  -0.928 135.588  1.00 88.24           C  
ANISOU  610  CG2 VAL A  73     7853  15236  10438   -420   1617   -356       C  
ATOM    611  N   VAL A  74     -20.182   0.453 132.467  1.00 70.23           N  
ANISOU  611  N   VAL A  74     5636  12638   8410    223   1208   -337       N  
ATOM    612  CA  VAL A  74     -20.336   0.353 131.012  1.00 68.05           C  
ANISOU  612  CA  VAL A  74     5271  12358   8228    375   1004   -300       C  
ATOM    613  C   VAL A  74     -19.252   1.171 130.291  1.00 72.43           C  
ANISOU  613  C   VAL A  74     6100  12618   8802    609    915   -252       C  
ATOM    614  O   VAL A  74     -18.763   0.764 129.225  1.00 53.19           O  
ANISOU  614  O   VAL A  74     3742  10071   6396    621    727   -179       O  
ATOM    615  CB  VAL A  74     -21.756   0.744 130.556  1.00 77.68           C  
ANISOU  615  CB  VAL A  74     6118  13879   9519    578   1021   -379       C  
ATOM    616  CG1 VAL A  74     -22.789  -0.164 131.224  1.00 92.23           C  
ANISOU  616  CG1 VAL A  74     7680  16011  11353    302   1114   -436       C  
ATOM    617  CG2 VAL A  74     -22.037   2.182 130.842  1.00 82.36           C  
ANISOU  617  CG2 VAL A  74     6696  14461  10135    918   1176   -445       C  
ATOM    618  N   GLU A  75     -18.814   2.299 130.874  1.00 78.44           N  
ANISOU  618  N   GLU A  75     7022  13236   9546    774   1064   -303       N  
ATOM    619  CA  GLU A  75     -17.693   3.049 130.307  1.00 73.33           C  
ANISOU  619  CA  GLU A  75     6657  12282   8922    947   1017   -268       C  
ATOM    620  C   GLU A  75     -16.418   2.218 130.305  1.00 64.72           C  
ANISOU  620  C   GLU A  75     5814  10996   7781    699    896   -185       C  
ATOM    621  O   GLU A  75     -15.687   2.183 129.304  1.00 52.62           O  
ANISOU  621  O   GLU A  75     4425   9280   6289    773    752   -114       O  
ATOM    622  CB  GLU A  75     -17.481   4.342 131.100  1.00 70.70           C  
ANISOU  622  CB  GLU A  75     6447  11834   8583   1107   1238   -372       C  
ATOM    623  CG  GLU A  75     -16.518   5.336 130.473  1.00 74.75           C  
ANISOU  623  CG  GLU A  75     7220  12031   9152   1324   1241   -361       C  
ATOM    624  CD  GLU A  75     -17.235   6.541 129.905  1.00 98.45           C  
ANISOU  624  CD  GLU A  75    10135  15017  12253   1719   1344   -386       C  
ATOM    625  OE1 GLU A  75     -16.591   7.588 129.693  1.00102.81           O  
ANISOU  625  OE1 GLU A  75    10904  15299  12859   1910   1444   -408       O  
ATOM    626  OE2 GLU A  75     -18.455   6.438 129.673  1.00118.25           O1-
ANISOU  626  OE2 GLU A  75    12353  17786  14791   1843   1333   -382       O1-
ATOM    627  N   LYS A  76     -16.125   1.563 131.431  1.00 61.58           N  
ANISOU  627  N   LYS A  76     5471  10639   7288    420    962   -185       N  
ATOM    628  CA  LYS A  76     -14.955   0.694 131.497  1.00 65.41           C  
ANISOU  628  CA  LYS A  76     6168  10964   7722    198    850    -88       C  
ATOM    629  C   LYS A  76     -15.019  -0.397 130.435  1.00 64.77           C  
ANISOU  629  C   LYS A  76     6030  10876   7702    108    661      9       C  
ATOM    630  O   LYS A  76     -13.993  -0.762 129.848  1.00 48.44           O  
ANISOU  630  O   LYS A  76     4150   8604   5650     71    534     86       O  
ATOM    631  CB  LYS A  76     -14.831   0.087 132.893  1.00 60.81           C  
ANISOU  631  CB  LYS A  76     5616  10481   7008    -67    955    -79       C  
ATOM    632  CG  LYS A  76     -14.114   0.988 133.889  1.00 52.23           C  
ANISOU  632  CG  LYS A  76     4699   9325   5821    -42   1088   -166       C  
ATOM    633  CD  LYS A  76     -13.331   0.182 134.914  1.00 49.91           C  
ANISOU  633  CD  LYS A  76     4541   9049   5373   -303   1086    -91       C  
ATOM    634  CE  LYS A  76     -12.851   1.071 136.051  1.00 52.57           C  
ANISOU  634  CE  LYS A  76     4990   9409   5576   -304   1233   -216       C  
ATOM    635  NZ  LYS A  76     -11.991   0.325 137.009  1.00 62.78           N  
ANISOU  635  NZ  LYS A  76     6418  10746   6691   -530   1205   -130       N  
ATOM    636  N   ILE A  77     -16.216  -0.927 130.166  1.00 64.30           N  
ANISOU  636  N   ILE A  77     5705  11045   7681     63    647    -10       N  
ATOM    637  CA  ILE A  77     -16.356  -1.879 129.065  1.00 61.95           C  
ANISOU  637  CA  ILE A  77     5337  10757   7445    -19    473     42       C  
ATOM    638  C   ILE A  77     -15.969  -1.222 127.748  1.00 63.17           C  
ANISOU  638  C   ILE A  77     5567  10780   7653    247    338     54       C  
ATOM    639  O   ILE A  77     -15.220  -1.790 126.942  1.00 51.11           O  
ANISOU  639  O   ILE A  77     4180   9094   6147    190    198    119       O  
ATOM    640  CB  ILE A  77     -17.786  -2.443 129.005  1.00 66.55           C  
ANISOU  640  CB  ILE A  77     5584  11643   8058   -113    493    -19       C  
ATOM    641  CG1 ILE A  77     -17.982  -3.510 130.077  1.00 65.23           C  
ANISOU  641  CG1 ILE A  77     5390  11546   7847   -453    604     10       C  
ATOM    642  CG2 ILE A  77     -18.063  -3.029 127.624  1.00 74.34           C  
ANISOU  642  CG2 ILE A  77     6460  12676   9108   -108    304    -20       C  
ATOM    643  CD1 ILE A  77     -19.393  -4.022 130.175  1.00 70.30           C  
ANISOU  643  CD1 ILE A  77     5695  12489   8526   -580    669    -70       C  
ATOM    644  N   LEU A  78     -16.475  -0.009 127.516  1.00 61.95           N  
ANISOU  644  N   LEU A  78     5332  10686   7521    551    396      0       N  
ATOM    645  CA  LEU A  78     -16.193   0.689 126.264  1.00 47.27           C  
ANISOU  645  CA  LEU A  78     3548   8713   5701    835    291     33       C  
ATOM    646  C   LEU A  78     -14.704   0.938 126.063  1.00 62.83           C  
ANISOU  646  C   LEU A  78     5856  10348   7671    842    265     91       C  
ATOM    647  O   LEU A  78     -14.227   0.963 124.921  1.00 52.92           O  
ANISOU  647  O   LEU A  78     4700   8969   6437    953    139    147       O  
ATOM    648  CB  LEU A  78     -16.940   2.018 126.219  1.00 51.88           C  
ANISOU  648  CB  LEU A  78     4017   9384   6313   1181    401    -15       C  
ATOM    649  CG  LEU A  78     -18.448   1.894 126.081  1.00 69.39           C  
ANISOU  649  CG  LEU A  78     5861  11961   8544   1255    393    -67       C  
ATOM    650  CD1 LEU A  78     -19.042   3.266 125.853  1.00 83.36           C  
ANISOU  650  CD1 LEU A  78     7548  13773  10351   1662    491    -82       C  
ATOM    651  CD2 LEU A  78     -18.753   0.960 124.929  1.00 53.61           C  
ANISOU  651  CD2 LEU A  78     3725  10104   6540   1179    173    -39       C  
ATOM    652  N   THR A  79     -13.957   1.135 127.149  1.00 62.43           N  
ANISOU  652  N   THR A  79     5970  10165   7584    724    384     72       N  
ATOM    653  CA  THR A  79     -12.544   1.478 127.061  1.00 45.75           C  
ANISOU  653  CA  THR A  79     4149   7761   5474    729    377    102       C  
ATOM    654  C   THR A  79     -11.638   0.339 127.522  1.00 51.12           C  
ANISOU  654  C   THR A  79     4950   8363   6111    431    308    163       C  
ATOM    655  O   THR A  79     -10.507   0.582 127.956  1.00 48.51           O  
ANISOU  655  O   THR A  79     4821   7856   5755    380    339    165       O  
ATOM    656  CB  THR A  79     -12.272   2.736 127.879  1.00 46.42           C  
ANISOU  656  CB  THR A  79     4337   7751   5551    850    568     11       C  
ATOM    657  OG1 THR A  79     -12.543   2.467 129.261  1.00 47.95           O  
ANISOU  657  OG1 THR A  79     4464   8093   5664    657    680    -48       O  
ATOM    658  CG2 THR A  79     -13.156   3.882 127.399  1.00 40.36           C  
ANISOU  658  CG2 THR A  79     3466   7026   4844   1180    658    -30       C  
ATOM    659  N   GLN A  80     -12.104  -0.902 127.408  1.00 40.85           N  
ANISOU  659  N   GLN A  80     3528   7187   4806    237    222    213       N  
ATOM    660  CA  GLN A  80     -11.431  -2.026 128.046  1.00 35.59           C  
ANISOU  660  CA  GLN A  80     2959   6467   4099    -38    197    288       C  
ATOM    661  C   GLN A  80     -10.076  -2.319 127.412  1.00 37.74           C  
ANISOU  661  C   GLN A  80     3455   6483   4400    -53     88    361       C  
ATOM    662  O   GLN A  80      -9.830  -2.031 126.237  1.00 43.97           O  
ANISOU  662  O   GLN A  80     4296   7161   5249     95      1    364       O  
ATOM    663  CB  GLN A  80     -12.311  -3.277 127.974  1.00 45.73           C  
ANISOU  663  CB  GLN A  80     4065   7910   5398   -240    160    318       C  
ATOM    664  CG  GLN A  80     -12.495  -3.823 126.559  1.00 50.04           C  
ANISOU  664  CG  GLN A  80     4561   8431   6020   -217      8    327       C  
ATOM    665  CD  GLN A  80     -13.438  -5.010 126.497  1.00 52.41           C  
ANISOU  665  CD  GLN A  80     4668   8899   6347   -443     -6    315       C  
ATOM    666  OE1 GLN A  80     -13.121  -6.092 126.988  1.00 52.31           O  
ANISOU  666  OE1 GLN A  80     4725   8814   6335   -688     20    386       O  
ATOM    667  NE2 GLN A  80     -14.603  -4.814 125.888  1.00 60.31           N  
ANISOU  667  NE2 GLN A  80     5419  10124   7372   -358    -39    226       N  
ATOM    668  N   SER A  81      -9.189  -2.881 128.224  1.00 49.99           N  
ANISOU  668  N   SER A  81     5136   7958   5899   -223    100    426       N  
ATOM    669  CA  SER A  81      -8.022  -3.604 127.755  1.00 46.84           C  
ANISOU  669  CA  SER A  81     4904   7359   5533   -299     -5    519       C  
ATOM    670  C   SER A  81      -8.313  -5.093 127.895  1.00 49.58           C  
ANISOU  670  C   SER A  81     5204   7745   5890   -523    -37    615       C  
ATOM    671  O   SER A  81      -9.144  -5.500 128.713  1.00 69.50           O  
ANISOU  671  O   SER A  81     7605  10439   8364   -650     46    622       O  
ATOM    672  CB  SER A  81      -6.783  -3.229 128.567  1.00 60.72           C  
ANISOU  672  CB  SER A  81     6827   9018   7226   -319     27    532       C  
ATOM    673  OG  SER A  81      -6.808  -1.864 128.946  1.00 67.87           O  
ANISOU  673  OG  SER A  81     7741   9945   8100   -177    127    410       O  
ATOM    674  N   SER A  82      -7.644  -5.907 127.083  1.00 45.53           N  
ANISOU  674  N   SER A  82     4792   7061   5447   -575   -137    686       N  
ATOM    675  CA  SER A  82      -7.849  -7.346 127.182  1.00 51.76           C  
ANISOU  675  CA  SER A  82     5564   7836   6268   -791   -141    776       C  
ATOM    676  C   SER A  82      -7.426  -7.853 128.560  1.00 55.68           C  
ANISOU  676  C   SER A  82     6129   8353   6675   -927    -60    892       C  
ATOM    677  O   SER A  82      -6.514  -7.316 129.194  1.00 53.65           O  
ANISOU  677  O   SER A  82     5980   8063   6342   -864    -56    918       O  
ATOM    678  CB  SER A  82      -7.084  -8.078 126.079  1.00 50.57           C  
ANISOU  678  CB  SER A  82     5535   7468   6213   -808   -243    821       C  
ATOM    679  OG  SER A  82      -5.867  -7.430 125.767  1.00 65.80           O  
ANISOU  679  OG  SER A  82     7620   9236   8145   -665   -294    832       O  
ATOM    680  N   PHE A  83      -8.110  -8.902 129.021  1.00 57.33           N  
ANISOU  680  N   PHE A  83     6270   8628   6886  -1120     10    959       N  
ATOM    681  CA  PHE A  83      -7.928  -9.463 130.366  1.00 52.65           C  
ANISOU  681  CA  PHE A  83     5731   8088   6187  -1252    108   1093       C  
ATOM    682  C   PHE A  83      -7.975  -8.383 131.443  1.00 64.15           C  
ANISOU  682  C   PHE A  83     7158   9724   7492  -1172    176   1037       C  
ATOM    683  O   PHE A  83      -7.125  -8.324 132.335  1.00 85.10           O  
ANISOU  683  O   PHE A  83     9923  12384  10027  -1173    186   1120       O  
ATOM    684  CB  PHE A  83      -6.626 -10.256 130.492  1.00 39.78           C  
ANISOU  684  CB  PHE A  83     4296   6257   4561  -1280     60   1263       C  
ATOM    685  CG  PHE A  83      -6.200 -10.947 129.240  1.00 47.56           C  
ANISOU  685  CG  PHE A  83     5353   7016   5703  -1285    -26   1277       C  
ATOM    686  CD1 PHE A  83      -6.817 -12.118 128.832  1.00 53.12           C  
ANISOU  686  CD1 PHE A  83     6027   7645   6510  -1456     21   1310       C  
ATOM    687  CD2 PHE A  83      -5.148 -10.449 128.492  1.00 60.84           C  
ANISOU  687  CD2 PHE A  83     7137   8552   7427  -1134   -136   1249       C  
ATOM    688  CE1 PHE A  83      -6.408 -12.762 127.685  1.00 64.71           C  
ANISOU  688  CE1 PHE A  83     7568   8902   8115  -1471    -46   1300       C  
ATOM    689  CE2 PHE A  83      -4.735 -11.089 127.345  1.00 60.97           C  
ANISOU  689  CE2 PHE A  83     7225   8364   7576  -1139   -202   1255       C  
ATOM    690  CZ  PHE A  83      -5.365 -12.247 126.941  1.00 64.15           C  
ANISOU  690  CZ  PHE A  83     7601   8699   8074  -1305   -160   1276       C  
ATOM    691  N   GLU A  84      -8.979  -7.522 131.361  1.00 35.37           N  
ANISOU  691  N   GLU A  84     3353   6239   3846  -1099    226    886       N  
ATOM    692  CA  GLU A  84      -9.199  -6.512 132.383  1.00 43.67           C  
ANISOU  692  CA  GLU A  84     4363   7462   4766  -1036    325    805       C  
ATOM    693  C   GLU A  84     -10.577  -6.709 132.990  1.00 65.71           C  
ANISOU  693  C   GLU A  84     6968  10476   7525  -1144    462    768       C  
ATOM    694  O   GLU A  84     -11.559  -6.925 132.271  1.00 68.32           O  
ANISOU  694  O   GLU A  84     7135  10862   7961  -1161    459    705       O  
ATOM    695  CB  GLU A  84      -9.057  -5.101 131.819  1.00 35.14           C  
ANISOU  695  CB  GLU A  84     3277   6352   3722   -812    296    651       C  
ATOM    696  CG  GLU A  84      -9.156  -4.014 132.858  1.00 64.16           C  
ANISOU  696  CG  GLU A  84     6938  10165   7274   -749    416    543       C  
ATOM    697  CD  GLU A  84      -9.707  -2.723 132.299  1.00 52.73           C  
ANISOU  697  CD  GLU A  84     5410   8729   5897   -537    456    382       C  
ATOM    698  OE1 GLU A  84      -9.799  -1.740 133.066  1.00 54.41           O  
ANISOU  698  OE1 GLU A  84     5619   9021   6032   -471    575    268       O  
ATOM    699  OE2 GLU A  84     -10.025  -2.686 131.094  1.00 53.43           O1-
ANISOU  699  OE2 GLU A  84     5447   8743   6111   -429    375    371       O1-
ATOM    700  N   CYS A  85     -10.642  -6.654 134.316  1.00 59.74           N  
ANISOU  700  N   CYS A  85     6225   9865   6609  -1223    584    800       N  
ATOM    701  CA  CYS A  85     -11.854  -7.005 135.031  1.00 42.54           C  
ANISOU  701  CA  CYS A  85     3887   7891   4383  -1360    740    791       C  
ATOM    702  C   CYS A  85     -12.287  -5.860 135.935  1.00 58.96           C  
ANISOU  702  C   CYS A  85     5894  10169   6337  -1275    867    655       C  
ATOM    703  O   CYS A  85     -11.607  -4.843 136.084  1.00 59.93           O  
ANISOU  703  O   CYS A  85     6106  10261   6405  -1131    842    568       O  
ATOM    704  CB  CYS A  85     -11.663  -8.277 135.867  1.00 43.17           C  
ANISOU  704  CB  CYS A  85     4062   7966   4375  -1576    812    993       C  
ATOM    705  SG  CYS A  85     -11.227  -9.750 134.915  1.00 52.22           S  
ANISOU  705  SG  CYS A  85     5305   8850   5684  -1699    717   1154       S  
ATOM    706  N   ILE A  86     -13.458  -6.051 136.528  1.00 61.27           N  
ANISOU  706  N   ILE A  86     6018  10663   6597  -1380   1022    622       N  
ATOM    707  CA  ILE A  86     -13.993  -5.214 137.587  1.00 59.28           C  
ANISOU  707  CA  ILE A  86     5692  10625   6208  -1349   1189    508       C  
ATOM    708  C   ILE A  86     -14.366  -6.159 138.716  1.00 73.83           C  
ANISOU  708  C   ILE A  86     7536  12607   7908  -1580   1337    637       C  
ATOM    709  O   ILE A  86     -14.432  -7.370 138.530  1.00 71.73           O  
ANISOU  709  O   ILE A  86     7292  12266   7695  -1745   1327    792       O  
ATOM    710  CB  ILE A  86     -15.213  -4.399 137.112  1.00 62.16           C  
ANISOU  710  CB  ILE A  86     5811  11118   6688  -1215   1257    325       C  
ATOM    711  CG1 ILE A  86     -16.276  -5.339 136.540  1.00 71.66           C  
ANISOU  711  CG1 ILE A  86     6809  12395   8022  -1348   1266    352       C  
ATOM    712  CG2 ILE A  86     -14.791  -3.394 136.050  1.00 56.79           C  
ANISOU  712  CG2 ILE A  86     5163  10289   6126   -959   1129    225       C  
ATOM    713  CD1 ILE A  86     -17.692  -4.908 136.833  1.00 58.96           C  
ANISOU  713  CD1 ILE A  86     4920  11043   6437  -1329   1426    213       C  
ATOM    714  N   HIS A  87     -14.567  -5.623 139.908  1.00 86.04           N  
ANISOU  714  N   HIS A  87     9081  14345   9266  -1595   1491    579       N  
ATOM    715  CA  HIS A  87     -15.062  -6.486 140.967  1.00 79.13           C  
ANISOU  715  CA  HIS A  87     8197  13624   8247  -1809   1660    705       C  
ATOM    716  C   HIS A  87     -16.569  -6.626 140.817  1.00 78.00           C  
ANISOU  716  C   HIS A  87     7787  13630   8221  -1885   1809    611       C  
ATOM    717  O   HIS A  87     -17.265  -5.647 140.525  1.00 78.58           O  
ANISOU  717  O   HIS A  87     7682  13802   8373  -1737   1848    413       O  
ATOM    718  CB  HIS A  87     -14.692  -5.940 142.343  1.00 89.18           C  
ANISOU  718  CB  HIS A  87     9573  15074   9239  -1815   1772    682       C  
ATOM    719  CG  HIS A  87     -13.254  -6.149 142.699  1.00 97.49           C  
ANISOU  719  CG  HIS A  87    10866  16041  10135  -1804   1638    820       C  
ATOM    720  ND1 HIS A  87     -12.255  -5.301 142.274  1.00 98.06           N  
ANISOU  720  ND1 HIS A  87    11031  16000  10226  -1644   1485    716       N  
ATOM    721  CD2 HIS A  87     -12.645  -7.118 143.424  1.00 98.15           C  
ANISOU  721  CD2 HIS A  87    11120  16106  10068  -1906   1617   1048       C  
ATOM    722  CE1 HIS A  87     -11.093  -5.737 142.725  1.00100.18           C  
ANISOU  722  CE1 HIS A  87    11481  16245  10339  -1674   1384    869       C  
ATOM    723  NE2 HIS A  87     -11.301  -6.837 143.426  1.00 97.43           N  
ANISOU  723  NE2 HIS A  87    11177  15978   9865  -1829   1467   1089       N  
ATOM    724  N   LEU A  88     -17.070  -7.851 140.991  1.00 77.57           N  
ANISOU  724  N   LEU A  88     7732  13525   8215  -2078   1871    743       N  
ATOM    725  CA  LEU A  88     -18.510  -8.065 141.073  1.00 68.32           C  
ANISOU  725  CA  LEU A  88     6346  12457   7156  -2153   2006    641       C  
ATOM    726  C   LEU A  88     -19.077  -7.117 142.122  1.00 70.99           C  
ANISOU  726  C   LEU A  88     6626  12987   7360  -2070   2161    501       C  
ATOM    727  O   LEU A  88     -20.230  -6.682 142.030  1.00 84.86           O  
ANISOU  727  O   LEU A  88     8154  14871   9217  -2025   2253    342       O  
ATOM    728  CB  LEU A  88     -18.827  -9.526 141.407  1.00 69.92           C  
ANISOU  728  CB  LEU A  88     6625  12544   7398  -2381   2090    808       C  
ATOM    729  CG  LEU A  88     -18.507 -10.553 140.316  1.00 61.75           C  
ANISOU  729  CG  LEU A  88     5627  11294   6543  -2484   1972    908       C  
ATOM    730  CD1 LEU A  88     -18.097 -11.898 140.912  1.00 60.87           C  
ANISOU  730  CD1 LEU A  88     5747  10989   6394  -2649   2045   1146       C  
ATOM    731  CD2 LEU A  88     -19.703 -10.716 139.385  1.00 68.02           C  
ANISOU  731  CD2 LEU A  88     6144  12141   7561  -2538   1974    743       C  
ATOM    732  N   SER A  89     -18.243  -6.792 143.113  1.00 72.55           N  
ANISOU  732  N   SER A  89     7029  13207   7330  -2043   2182    554       N  
ATOM    733  CA  SER A  89     -18.478  -5.752 144.107  1.00 70.07           C  
ANISOU  733  CA  SER A  89     6710  13051   6860  -1950   2307    403       C  
ATOM    734  C   SER A  89     -19.169  -4.525 143.524  1.00 62.02           C  
ANISOU  734  C   SER A  89     5475  12114   5975  -1759   2337    160       C  
ATOM    735  O   SER A  89     -20.224  -4.119 144.018  1.00 80.91           O  
ANISOU  735  O   SER A  89     7723  14631   8388  -1734   2493     34       O  
ATOM    736  CB  SER A  89     -17.151  -5.337 144.747  1.00 81.26           C  
ANISOU  736  CB  SER A  89     8366  14459   8050  -1899   2233    444       C  
ATOM    737  OG  SER A  89     -16.391  -6.466 145.146  1.00 74.28           O  
ANISOU  737  OG  SER A  89     7682  13486   7057  -2024   2169    694       O  
ATOM    738  N   VAL A  90     -18.593  -3.945 142.467  1.00 74.46           N  
ANISOU  738  N   VAL A  90     7028  13612   7650  -1610   2198    104       N  
ATOM    739  CA  VAL A  90     -19.072  -2.672 141.934  1.00 78.67           C  
ANISOU  739  CA  VAL A  90     7399  14194   8299  -1375   2228   -109       C  
ATOM    740  C   VAL A  90     -20.515  -2.726 141.451  1.00 83.44           C  
ANISOU  740  C   VAL A  90     7717  14892   9094  -1336   2285   -192       C  
ATOM    741  O   VAL A  90     -21.123  -1.672 141.227  1.00 87.85           O  
ANISOU  741  O   VAL A  90     8130  15508   9740  -1122   2345   -358       O  
ATOM    742  CB  VAL A  90     -18.152  -2.191 140.789  1.00 85.91           C  
ANISOU  742  CB  VAL A  90     8383  14945   9313  -1209   2043   -118       C  
ATOM    743  CG1 VAL A  90     -18.295  -0.680 140.577  1.00100.02           C  
ANISOU  743  CG1 VAL A  90    10126  16713  11165   -933   2097   -328       C  
ATOM    744  CG2 VAL A  90     -16.708  -2.550 141.076  1.00 89.19           C  
ANISOU  744  CG2 VAL A  90     9091  15207   9591  -1285   1916     13       C  
ATOM    745  N   LEU A  91     -21.085  -3.916 141.284  1.00 89.97           N  
ANISOU  745  N   LEU A  91     8463  15725   9995  -1530   2273    -84       N  
ATOM    746  CA  LEU A  91     -22.462  -4.055 140.831  1.00 94.13           C  
ANISOU  746  CA  LEU A  91     8706  16359  10699  -1520   2315   -173       C  
ATOM    747  C   LEU A  91     -23.460  -4.124 141.979  1.00 93.85           C  
ANISOU  747  C   LEU A  91     8600  16455  10605  -1612   2530   -221       C  
ATOM    748  O   LEU A  91     -24.659  -4.283 141.730  1.00 80.80           O  
ANISOU  748  O   LEU A  91     6702  14907   9090  -1624   2584   -297       O  
ATOM    749  CB  LEU A  91     -22.594  -5.293 139.943  1.00 89.20           C  
ANISOU  749  CB  LEU A  91     8022  15661  10209  -1693   2194    -70       C  
ATOM    750  CG  LEU A  91     -21.390  -5.457 139.016  1.00 76.92           C  
ANISOU  750  CG  LEU A  91     6607  13948   8672  -1660   1996     25       C  
ATOM    751  CD1 LEU A  91     -21.192  -6.916 138.635  1.00 69.85           C  
ANISOU  751  CD1 LEU A  91     5784  12915   7841  -1908   1929    175       C  
ATOM    752  CD2 LEU A  91     -21.527  -4.570 137.785  1.00 66.32           C  
ANISOU  752  CD2 LEU A  91     5093  12639   7467  -1401   1862    -97       C  
ATOM    753  N   HIS A  92     -22.997  -4.001 143.224  1.00 99.73           N  
ANISOU  753  N   HIS A  92     9544  17207  11141  -1674   2649   -184       N  
ATOM    754  CA  HIS A  92     -23.891  -3.860 144.369  1.00 98.67           C  
ANISOU  754  CA  HIS A  92     9353  17205  10931  -1725   2867   -248       C  
ATOM    755  C   HIS A  92     -23.357  -2.946 145.458  1.00 98.06           C  
ANISOU  755  C   HIS A  92     9451  17162  10644  -1642   2968   -321       C  
ATOM    756  O   HIS A  92     -24.062  -2.737 146.450  1.00126.17           O  
ANISOU  756  O   HIS A  92    12975  20836  14128  -1672   3156   -385       O  
ATOM    757  CB  HIS A  92     -24.212  -5.231 144.986  1.00 98.56           C  
ANISOU  757  CB  HIS A  92     9393  17185  10872  -2000   2956    -87       C  
ATOM    758  CG  HIS A  92     -23.081  -5.833 145.761  1.00 94.16           C  
ANISOU  758  CG  HIS A  92     9146  16535  10097  -2123   2939    100       C  
ATOM    759  ND1 HIS A  92     -23.065  -5.885 147.138  1.00 98.19           N  
ANISOU  759  ND1 HIS A  92     9796  17120  10391  -2195   3097    145       N  
ATOM    760  CD2 HIS A  92     -21.935  -6.423 145.350  1.00 90.20           C  
ANISOU  760  CD2 HIS A  92     8835  15881   9557  -2170   2778    262       C  
ATOM    761  CE1 HIS A  92     -21.956  -6.479 147.542  1.00 95.75           C  
ANISOU  761  CE1 HIS A  92     9747  16719   9914  -2270   3022    332       C  
ATOM    762  NE2 HIS A  92     -21.250  -6.810 146.477  1.00 91.69           N  
ANISOU  762  NE2 HIS A  92     9268  16060   9509  -2254   2831    407       N  
ATOM    763  N   LYS A  93     -22.163  -2.378 145.309  1.00 82.02           N  
ANISOU  763  N   LYS A  93     7601  15040   8521  -1544   2856   -328       N  
ATOM    764  CA  LYS A  93     -21.542  -1.619 146.387  1.00 94.34           C  
ANISOU  764  CA  LYS A  93     9351  16629   9864  -1505   2936   -405       C  
ATOM    765  C   LYS A  93     -22.078  -0.194 146.456  1.00103.01           C  
ANISOU  765  C   LYS A  93    10345  17762  11031  -1283   3058   -645       C  
ATOM    766  O   LYS A  93     -22.175   0.497 145.440  1.00 85.21           O  
ANISOU  766  O   LYS A  93     7979  15439   8957  -1085   2997   -736       O  
ATOM    767  CB  LYS A  93     -20.025  -1.602 146.219  1.00104.75           C  
ANISOU  767  CB  LYS A  93    10903  17838  11060  -1504   2768   -331       C  
ATOM    768  CG  LYS A  93     -19.304  -0.888 147.349  1.00108.25           C  
ANISOU  768  CG  LYS A  93    11551  18285  11296  -1705   2727   -116       C  
ATOM    769  CD  LYS A  93     -17.791  -0.944 147.155  1.00114.07           C  
ANISOU  769  CD  LYS A  93    12247  18938  12156  -1847   2649     96       C  
ATOM    770  CE  LYS A  93     -17.039  -0.208 148.272  1.00104.80           C  
ANISOU  770  CE  LYS A  93    11304  17651  10865  -1930   2490    315       C  
ATOM    771  NZ  LYS A  93     -15.549  -0.278 148.057  1.00113.88           N  
ANISOU  771  NZ  LYS A  93    12650  18880  11741  -2017   2553    421       N  
ATOM    772  N   CYS A  94     -22.415   0.236 147.669  1.00124.66           N  
ANISOU  772  N   CYS A  94    13137  20600  13627  -1307   3238   -739       N  
ATOM    773  CA  CYS A  94     -22.866   1.598 147.964  1.00139.35           C  
ANISOU  773  CA  CYS A  94    14945  22472  15530  -1110   3391   -967       C  
ATOM    774  C   CYS A  94     -23.925   2.069 146.971  1.00134.32           C  
ANISOU  774  C   CYS A  94    14036  21828  15172   -910   3418  -1048       C  
ATOM    775  O   CYS A  94     -23.815   3.136 146.363  1.00134.41           O  
ANISOU  775  O   CYS A  94    14025  21737  15308   -671   3414  -1173       O  
ATOM    776  CB  CYS A  94     -21.692   2.573 147.999  1.00151.39           C  
ANISOU  776  CB  CYS A  94    16675  23877  16969  -1003   3337  -1083       C  
ATOM    777  SG  CYS A  94     -20.160   1.846 148.546  1.00155.93           S  
ANISOU  777  SG  CYS A  94    17532  24443  17271  -1205   3175   -939       S  
ATOM    778  N   TYR A  95     -24.962   1.254 146.812  1.00131.90           N  
ANISOU  778  N   TYR A  95    13522  21629  14966  -1004   3447   -972       N  
ATOM    779  CA  TYR A  95     -26.178   1.653 146.122  1.00117.51           C  
ANISOU  779  CA  TYR A  95    11406  19864  13380   -831   3496  -1056       C  
ATOM    780  C   TYR A  95     -27.171   2.212 147.131  1.00117.52           C  
ANISOU  780  C   TYR A  95    11315  19980  13356   -791   3747  -1181       C  
ATOM    781  O   TYR A  95     -27.158   1.839 148.306  1.00104.84           O  
ANISOU  781  O   TYR A  95     9826  18449  11560   -973   3873  -1158       O  
ATOM    782  CB  TYR A  95     -26.823   0.461 145.407  1.00105.26           C  
ANISOU  782  CB  TYR A  95     9656  18380  11957   -974   3393   -934       C  
ATOM    783  CG  TYR A  95     -26.220   0.071 144.077  1.00103.08           C  
ANISOU  783  CG  TYR A  95     9369  18005  11791   -942   3148   -847       C  
ATOM    784  CD1 TYR A  95     -24.851  -0.076 143.928  1.00 99.94           C  
ANISOU  784  CD1 TYR A  95     9220  17472  11279   -988   3016   -762       C  
ATOM    785  CD2 TYR A  95     -27.028  -0.172 142.972  1.00104.20           C  
ANISOU  785  CD2 TYR A  95     9245  18203  12142   -869   3045   -852       C  
ATOM    786  CE1 TYR A  95     -24.299  -0.441 142.713  1.00 85.22           C  
ANISOU  786  CE1 TYR A  95     7347  15517   9515   -959   2803   -682       C  
ATOM    787  CE2 TYR A  95     -26.484  -0.541 141.751  1.00104.30           C  
ANISOU  787  CE2 TYR A  95     9252  18134  12243   -842   2819   -778       C  
ATOM    788  CZ  TYR A  95     -25.119  -0.673 141.628  1.00 89.58           C  
ANISOU  788  CZ  TYR A  95     7644  16123  10271   -887   2707   -691       C  
ATOM    789  OH  TYR A  95     -24.576  -1.036 140.419  1.00 80.38           O  
ANISOU  789  OH  TYR A  95     6474  14874   9194   -860   2493   -617       O  
ATOM    790  N   ASP A  96     -28.045   3.103 146.667  1.00122.70           N  
ANISOU  790  N   ASP A  96    11763  20653  14204   -540   3822  -1301       N  
ATOM    791  CA  ASP A  96     -29.227   3.463 147.445  1.00130.99           C  
ANISOU  791  CA  ASP A  96    12655  21835  15281   -502   4058  -1400       C  
ATOM    792  C   ASP A  96     -30.283   2.395 147.189  1.00128.90           C  
ANISOU  792  C   ASP A  96    12128  21727  15120   -657   4044  -1319       C  
ATOM    793  O   ASP A  96     -30.777   2.261 146.066  1.00142.33           O  
ANISOU  793  O   ASP A  96    13608  23454  17019   -555   3911  -1303       O  
ATOM    794  CB  ASP A  96     -29.734   4.854 147.074  1.00140.77           C  
ANISOU  794  CB  ASP A  96    13782  23014  16691   -154   4157  -1547       C  
ATOM    795  CG  ASP A  96     -30.905   5.302 147.942  1.00153.92           C  
ANISOU  795  CG  ASP A  96    15297  24807  18380   -101   4421  -1653       C  
ATOM    796  OD1 ASP A  96     -31.307   4.554 148.861  1.00159.35           O  
ANISOU  796  OD1 ASP A  96    15971  25635  18938   -340   4529  -1621       O  
ATOM    797  OD2 ASP A  96     -31.433   6.408 147.695  1.00158.83           O1-
ANISOU  797  OD2 ASP A  96    15816  25378  19154    193   4531  -1759       O1-
ATOM    798  N   TYR A  97     -30.628   1.626 148.223  1.00117.27           N  
ANISOU  798  N   TYR A  97    10685  20362  13511   -905   4182  -1271       N  
ATOM    799  CA  TYR A  97     -31.435   0.430 148.013  1.00110.63           C  
ANISOU  799  CA  TYR A  97     9650  19632  12752  -1113   4169  -1179       C  
ATOM    800  C   TYR A  97     -32.935   0.677 148.080  1.00135.46           C  
ANISOU  800  C   TYR A  97    12470  22944  16057  -1034   4328  -1281       C  
ATOM    801  O   TYR A  97     -33.686  -0.019 147.399  1.00133.43           O  
ANISOU  801  O   TYR A  97    11971  22772  15956  -1110   4257  -1251       O  
ATOM    802  CB  TYR A  97     -31.057  -0.658 149.022  1.00 94.94           C  
ANISOU  802  CB  TYR A  97     7865  17656  10554  -1427   4243  -1043       C  
ATOM    803  CG  TYR A  97     -29.914  -1.530 148.553  1.00 95.55           C  
ANISOU  803  CG  TYR A  97     8147  17597  10562  -1574   4035   -877       C  
ATOM    804  CD1 TYR A  97     -30.111  -2.509 147.589  1.00 91.37           C  
ANISOU  804  CD1 TYR A  97     7493  17039  10184  -1691   3892   -783       C  
ATOM    805  CD2 TYR A  97     -28.635  -1.371 149.072  1.00102.04           C  
ANISOU  805  CD2 TYR A  97     9283  18322  11167  -1595   3983   -821       C  
ATOM    806  CE1 TYR A  97     -29.070  -3.308 147.157  1.00 86.00           C  
ANISOU  806  CE1 TYR A  97     7005  16219   9452  -1818   3717   -628       C  
ATOM    807  CE2 TYR A  97     -27.586  -2.167 148.644  1.00 91.90           C  
ANISOU  807  CE2 TYR A  97     8179  16915   9824  -1714   3797   -659       C  
ATOM    808  CZ  TYR A  97     -27.811  -3.132 147.689  1.00 88.35           C  
ANISOU  808  CZ  TYR A  97     7610  16420   9539  -1821   3673   -558       C  
ATOM    809  OH  TYR A  97     -26.770  -3.923 147.263  1.00 83.85           O  
ANISOU  809  OH  TYR A  97     7226  15712   8923  -1931   3502   -394       O  
ATOM    810  N   ASP A  98     -33.413   1.619 148.886  1.00153.79           N  
ANISOU  810  N   ASP A  98    14770  25319  18346   -893   4545  -1405       N  
ATOM    811  CA  ASP A  98     -34.846   1.885 148.899  1.00164.07           C  
ANISOU  811  CA  ASP A  98    15743  26782  19813   -796   4695  -1497       C  
ATOM    812  C   ASP A  98     -35.252   2.967 147.906  1.00168.34           C  
ANISOU  812  C   ASP A  98    16086  27303  20572   -435   4628  -1591       C  
ATOM    813  O   ASP A  98     -36.421   3.364 147.884  1.00171.90           O  
ANISOU  813  O   ASP A  98    16258  27887  21171   -298   4751  -1672       O  
ATOM    814  CB  ASP A  98     -35.333   2.244 150.311  1.00169.02           C  
ANISOU  814  CB  ASP A  98    16415  27498  20305   -838   4994  -1574       C  
ATOM    815  CG  ASP A  98     -34.418   3.212 151.029  1.00165.72           C  
ANISOU  815  CG  ASP A  98    16298  26958  19710   -725   5071  -1647       C  
ATOM    816  OD1 ASP A  98     -33.290   2.814 151.383  1.00162.06           O1-
ANISOU  816  OD1 ASP A  98    16125  26406  19044   -882   4983  -1567       O1-
ATOM    817  OD2 ASP A  98     -34.838   4.366 151.260  1.00169.26           O  
ANISOU  817  OD2 ASP A  98    16689  27400  20220   -482   5227  -1786       O  
ATOM    818  N   ALA A  99     -34.321   3.436 147.074  1.00152.30           N  
ANISOU  818  N   ALA A  99    14191  25108  18567   -271   4439  -1571       N  
ATOM    819  CA  ALA A  99     -34.660   4.347 145.989  1.00132.11           C  
ANISOU  819  CA  ALA A  99    11459  22515  16222     77   4349  -1621       C  
ATOM    820  C   ALA A  99     -35.023   3.625 144.698  1.00126.34           C  
ANISOU  820  C   ALA A  99    10494  21868  15641     61   4100  -1550       C  
ATOM    821  O   ALA A  99     -35.667   4.225 143.829  1.00123.24           O  
ANISOU  821  O   ALA A  99     9872  21522  15431    336   4032  -1585       O  
ATOM    822  CB  ALA A  99     -33.506   5.317 145.722  1.00113.53           C  
ANISOU  822  CB  ALA A  99     9376  19929  13831    286   4295  -1641       C  
ATOM    823  N   ILE A 100     -34.624   2.367 144.542  1.00126.36           N  
ANISOU  823  N   ILE A 100    10557  21886  15570   -245   3963  -1450       N  
ATOM    824  CA  ILE A 100     -35.098   1.580 143.408  1.00124.27           C  
ANISOU  824  CA  ILE A 100    10057  21720  15440   -305   3750  -1406       C  
ATOM    825  C   ILE A 100     -36.527   1.166 143.740  1.00124.71           C  
ANISOU  825  C   ILE A 100     9796  22001  15589   -407   3887  -1466       C  
ATOM    826  O   ILE A 100     -36.844   0.919 144.914  1.00136.59           O  
ANISOU  826  O   ILE A 100    11343  23555  17000   -583   4116  -1483       O  
ATOM    827  CB  ILE A 100     -34.163   0.392 143.106  1.00123.94           C  
ANISOU  827  CB  ILE A 100    10204  21582  15305   -594   3578  -1284       C  
ATOM    828  CG1 ILE A 100     -33.745  -0.348 144.379  1.00125.08           C  
ANISOU  828  CG1 ILE A 100    10579  21685  15261   -906   3742  -1219       C  
ATOM    829  CG2 ILE A 100     -32.904   0.859 142.383  1.00128.51           C  
ANISOU  829  CG2 ILE A 100    11006  21972  15851   -435   3391  -1234       C  
ATOM    830  CD1 ILE A 100     -34.826  -1.153 145.011  1.00132.82           C  
ANISOU  830  CD1 ILE A 100    11379  22821  16264  -1140   3907  -1229       C  
ATOM    831  N   PRO A 101     -37.436   1.142 142.767  1.00110.03           N  
ANISOU  831  N   PRO A 101     7611  20293  13903   -289   3761  -1505       N  
ATOM    832  CA  PRO A 101     -38.816   0.757 143.083  1.00113.85           C  
ANISOU  832  CA  PRO A 101     7772  21007  14480   -393   3894  -1575       C  
ATOM    833  C   PRO A 101     -39.021  -0.736 143.271  1.00124.02           C  
ANISOU  833  C   PRO A 101     9033  22354  15736   -811   3893  -1532       C  
ATOM    834  O   PRO A 101     -40.047  -1.127 143.843  1.00137.87           O  
ANISOU  834  O   PRO A 101    10581  24270  17533   -958   4066  -1586       O  
ATOM    835  CB  PRO A 101     -39.609   1.275 141.875  1.00116.81           C  
ANISOU  835  CB  PRO A 101     7820  21525  15036   -105   3724  -1628       C  
ATOM    836  CG  PRO A 101     -38.757   2.394 141.343  1.00106.46           C  
ANISOU  836  CG  PRO A 101     6692  20032  13724    242   3623  -1597       C  
ATOM    837  CD  PRO A 101     -37.359   1.877 141.495  1.00111.33           C  
ANISOU  837  CD  PRO A 101     7677  20437  14186     43   3546  -1508       C  
ATOM    838  N   TRP A 102     -38.088  -1.581 142.833  1.00104.71           N  
ANISOU  838  N   TRP A 102     6793  19769  13225  -1008   3724  -1435       N  
ATOM    839  CA  TRP A 102     -38.402  -2.983 142.597  1.00115.84           C  
ANISOU  839  CA  TRP A 102     8123  21222  14670  -1357   3676  -1404       C  
ATOM    840  C   TRP A 102     -37.735  -3.957 143.561  1.00106.87           C  
ANISOU  840  C   TRP A 102     7283  19935  13387  -1694   3812  -1289       C  
ATOM    841  O   TRP A 102     -38.009  -5.161 143.487  1.00105.62           O  
ANISOU  841  O   TRP A 102     7086  19777  13266  -1998   3821  -1253       O  
ATOM    842  CB  TRP A 102     -38.060  -3.349 141.151  1.00123.34           C  
ANISOU  842  CB  TRP A 102     9023  22143  15697  -1328   3368  -1389       C  
ATOM    843  CG  TRP A 102     -36.654  -3.112 140.729  1.00125.65           C  
ANISOU  843  CG  TRP A 102     9624  22217  15900  -1233   3204  -1293       C  
ATOM    844  CD1 TRP A 102     -36.163  -1.997 140.114  1.00128.66           C  
ANISOU  844  CD1 TRP A 102    10050  22546  16290   -883   3075  -1300       C  
ATOM    845  CD2 TRP A 102     -35.554  -4.026 140.840  1.00128.16           C  
ANISOU  845  CD2 TRP A 102    10246  22332  16116  -1485   3154  -1170       C  
ATOM    846  NE1 TRP A 102     -34.823  -2.151 139.854  1.00129.38           N  
ANISOU  846  NE1 TRP A 102    10445  22427  16288   -913   2949  -1201       N  
ATOM    847  CE2 TRP A 102     -34.425  -3.387 140.290  1.00123.77           C  
ANISOU  847  CE2 TRP A 102     9893  21626  15507  -1276   2989  -1119       C  
ATOM    848  CE3 TRP A 102     -35.412  -5.318 141.360  1.00128.68           C  
ANISOU  848  CE3 TRP A 102    10439  22316  16139  -1856   3245  -1088       C  
ATOM    849  CZ2 TRP A 102     -33.171  -3.991 140.247  1.00107.24           C  
ANISOU  849  CZ2 TRP A 102     8104  19326  13315  -1429   2904   -995       C  
ATOM    850  CZ3 TRP A 102     -34.168  -5.921 141.305  1.00120.38           C  
ANISOU  850  CZ3 TRP A 102     9703  21043  14994  -1992   3161   -952       C  
ATOM    851  CH2 TRP A 102     -33.063  -5.255 140.756  1.00104.82           C  
ANISOU  851  CH2 TRP A 102     7912  18947  12967  -1781   2988   -910       C  
ATOM    852  N   LEU A 103     -36.878  -3.487 144.462  1.00115.02           N  
ANISOU  852  N   LEU A 103     8614  20837  14251  -1648   3922  -1228       N  
ATOM    853  CA  LEU A 103     -36.507  -4.275 145.627  1.00121.77           C  
ANISOU  853  CA  LEU A 103     9713  21608  14948  -1931   4107  -1120       C  
ATOM    854  C   LEU A 103     -37.133  -3.700 146.885  1.00142.07           C  
ANISOU  854  C   LEU A 103    12253  24288  17438  -1891   4391  -1181       C  
ATOM    855  O   LEU A 103     -36.886  -4.213 147.980  1.00146.14           O  
ANISOU  855  O   LEU A 103    12973  24758  17794  -2092   4568  -1093       O  
ATOM    856  CB  LEU A 103     -34.985  -4.342 145.801  1.00117.68           C  
ANISOU  856  CB  LEU A 103     9585  20872  14255  -1953   4014   -990       C  
ATOM    857  CG  LEU A 103     -34.104  -5.022 144.751  1.00 95.70           C  
ANISOU  857  CG  LEU A 103     6918  17935  11509  -2028   3760   -896       C  
ATOM    858  CD1 LEU A 103     -33.319  -3.953 143.972  1.00101.97           C  
ANISOU  858  CD1 LEU A 103     7776  18662  12306  -1721   3566   -933       C  
ATOM    859  CD2 LEU A 103     -33.162  -6.050 145.348  1.00 94.29           C  
ANISOU  859  CD2 LEU A 103     7065  17580  11181  -2289   3795   -714       C  
ATOM    860  N   GLN A 104     -37.923  -2.630 146.749  1.00163.04           N  
ANISOU  860  N   GLN A 104    14667  27082  20197  -1621   4441  -1321       N  
ATOM    861  CA  GLN A 104     -38.680  -2.080 147.866  1.00171.33           C  
ANISOU  861  CA  GLN A 104    15641  28252  21202  -1575   4724  -1398       C  
ATOM    862  C   GLN A 104     -39.652  -3.097 148.447  1.00181.45           C  
ANISOU  862  C   GLN A 104    16767  29664  22513  -1870   4909  -1385       C  
ATOM    863  O   GLN A 104     -40.146  -2.901 149.562  1.00193.60           O  
ANISOU  863  O   GLN A 104    18306  31283  23968  -1909   5171  -1414       O  
ATOM    864  CB  GLN A 104     -39.434  -0.828 147.406  1.00175.84           C  
ANISOU  864  CB  GLN A 104    15943  28939  21928  -1216   4728  -1540       C  
ATOM    865  CG  GLN A 104     -39.961   0.061 148.525  1.00183.26           C  
ANISOU  865  CG  GLN A 104    16866  29951  22813  -1085   5016  -1630       C  
ATOM    866  CD  GLN A 104     -38.894   0.971 149.096  1.00184.42           C  
ANISOU  866  CD  GLN A 104    17351  29928  22792   -931   5062  -1633       C  
ATOM    867  OE1 GLN A 104     -38.123   0.569 149.967  1.00185.80           O  
ANISOU  867  OE1 GLN A 104    17826  30019  22752  -1124   5132  -1561       O  
ATOM    868  NE2 GLN A 104     -38.838   2.202 148.602  1.00183.56           N  
ANISOU  868  NE2 GLN A 104    17200  29766  22780   -579   5023  -1714       N  
ATOM    869  N   ASN A 105     -39.924  -4.183 147.719  1.00165.24           N  
ANISOU  869  N   ASN A 105    14588  27622  20573  -2084   4789  -1347       N  
ATOM    870  CA  ASN A 105     -40.878  -5.206 148.131  1.00152.56           C  
ANISOU  870  CA  ASN A 105    12816  26124  19026  -2379   4961  -1344       C  
ATOM    871  C   ASN A 105     -40.203  -6.556 148.364  1.00136.88           C  
ANISOU  871  C   ASN A 105    11093  23960  16953  -2716   4968  -1176       C  
ATOM    872  O   ASN A 105     -40.882  -7.586 148.417  1.00121.14           O  
ANISOU  872  O   ASN A 105     8976  22007  15045  -2986   5066  -1161       O  
ATOM    873  CB  ASN A 105     -41.990  -5.327 147.084  1.00151.64           C  
ANISOU  873  CB  ASN A 105    12277  26195  19143  -2349   4848  -1472       C  
ATOM    874  CG  ASN A 105     -43.292  -5.842 147.663  1.00148.97           C  
ANISOU  874  CG  ASN A 105    11669  26045  18886  -2544   5086  -1540       C  
ATOM    875  OD1 ASN A 105     -43.561  -5.688 148.854  1.00152.00           O  
ANISOU  875  OD1 ASN A 105    12119  26465  19169  -2591   5357  -1526       O  
ATOM    876  ND2 ASN A 105     -44.117  -6.446 146.815  1.00145.30           N  
ANISOU  876  ND2 ASN A 105    10895  25714  18599  -2661   4988  -1623       N  
ATOM    877  N   VAL A 106     -38.878  -6.571 148.498  1.00127.05           N  
ANISOU  877  N   VAL A 106    10211  22514  15550  -2701   4872  -1047       N  
ATOM    878  CA  VAL A 106     -38.116  -7.786 148.753  1.00132.33           C  
ANISOU  878  CA  VAL A 106    11163  22990  16126  -2978   4880   -859       C  
ATOM    879  C   VAL A 106     -37.437  -7.618 150.114  1.00134.83           C  
ANISOU  879  C   VAL A 106    11808  23241  16182  -2994   5060   -741       C  
ATOM    880  O   VAL A 106     -37.416  -6.526 150.685  1.00131.77           O  
ANISOU  880  O   VAL A 106    11441  22935  15689  -2788   5134   -824       O  
ATOM    881  CB  VAL A 106     -37.096  -8.076 147.626  1.00123.09           C  
ANISOU  881  CB  VAL A 106    10129  21644  14996  -2953   4585   -795       C  
ATOM    882  CG1 VAL A 106     -36.411  -9.434 147.795  1.00121.24           C  
ANISOU  882  CG1 VAL A 106    10161  21197  14708  -3240   4603   -596       C  
ATOM    883  CG2 VAL A 106     -37.783  -8.008 146.269  1.00111.26           C  
ANISOU  883  CG2 VAL A 106     8296  20253  13726  -2880   4390   -939       C  
ATOM    884  N   GLU A 107     -36.916  -8.726 150.648  1.00138.86           N  
ANISOU  884  N   GLU A 107    12572  23603  16584  -3238   5141   -546       N  
ATOM    885  CA  GLU A 107     -36.266  -8.713 151.951  1.00150.77           C  
ANISOU  885  CA  GLU A 107    14401  25065  17822  -3269   5302   -409       C  
ATOM    886  C   GLU A 107     -35.239  -7.586 152.018  1.00161.13           C  
ANISOU  886  C   GLU A 107    15902  26348  18973  -3016   5160   -448       C  
ATOM    887  O   GLU A 107     -34.426  -7.441 151.096  1.00158.08           O  
ANISOU  887  O   GLU A 107    15585  25846  18632  -2920   4910   -437       O  
ATOM    888  CB  GLU A 107     -35.587 -10.057 152.230  1.00145.30           C  
ANISOU  888  CB  GLU A 107    13987  24173  17049  -3510   5335   -157       C  
ATOM    889  CG  GLU A 107     -35.025 -10.199 153.649  1.00135.61           C  
ANISOU  889  CG  GLU A 107    13078  22923  15524  -3554   5520     13       C  
ATOM    890  CD  GLU A 107     -34.901 -11.646 154.095  1.00127.22           C  
ANISOU  890  CD  GLU A 107    12200  21709  14429  -3811   5665    265       C  
ATOM    891  OE1 GLU A 107     -34.232 -11.907 155.119  1.00117.22           O  
ANISOU  891  OE1 GLU A 107    11236  20393  12909  -3833   5771    454       O  
ATOM    892  OE2 GLU A 107     -35.470 -12.523 153.414  1.00117.70           O1-
ANISOU  892  OE2 GLU A 107    10837  20431  13451  -3984   5673    274       O1-
ATOM    893  N   PRO A 108     -35.239  -6.780 153.083  1.00190.54           N  
ANISOU  893  N   PRO A 108    19716  30171  22508  -2910   5318   -500       N  
ATOM    894  CA  PRO A 108     -34.336  -5.617 153.127  1.00196.14           C  
ANISOU  894  CA  PRO A 108    20583  30856  23083  -2671   5196   -577       C  
ATOM    895  C   PRO A 108     -32.874  -5.997 153.086  1.00195.03           C  
ANISOU  895  C   PRO A 108    20782  30544  22777  -2706   5021   -410       C  
ATOM    896  O   PRO A 108     -32.038  -5.192 152.649  1.00195.49           O  
ANISOU  896  O   PRO A 108    20933  30544  22800  -2524   4843   -473       O  
ATOM    897  CB  PRO A 108     -34.699  -4.954 154.463  1.00200.16           C  
ANISOU  897  CB  PRO A 108    21145  31503  23403  -2625   5448   -650       C  
ATOM    898  CG  PRO A 108     -35.192  -6.087 155.300  1.00202.50           C  
ANISOU  898  CG  PRO A 108    21486  31832  23624  -2885   5665   -499       C  
ATOM    899  CD  PRO A 108     -35.947  -6.977 154.359  1.00199.67           C  
ANISOU  899  CD  PRO A 108    20878  31449  23540  -3027   5624   -477       C  
ATOM    900  N   ASN A 109     -32.549  -7.217 153.517  1.00190.51           N  
ANISOU  900  N   ASN A 109    20394  29880  22110  -2929   5077   -192       N  
ATOM    901  CA  ASN A 109     -31.167  -7.634 153.703  1.00183.66           C  
ANISOU  901  CA  ASN A 109    19868  28865  21050  -2959   4945     -5       C  
ATOM    902  C   ASN A 109     -30.692  -8.612 152.638  1.00175.94           C  
ANISOU  902  C   ASN A 109    18921  27697  20229  -3061   4761    132       C  
ATOM    903  O   ASN A 109     -29.504  -8.950 152.607  1.00167.47           O  
ANISOU  903  O   ASN A 109    18113  26488  19032  -3063   4623    289       O  
ATOM    904  CB  ASN A 109     -30.985  -8.239 155.102  1.00186.55           C  
ANISOU  904  CB  ASN A 109    20475  29256  21150  -3094   5150    174       C  
ATOM    905  CG  ASN A 109     -29.656  -7.920 155.682  1.00184.03           C  
ANISOU  905  CG  ASN A 109    20475  28906  20544  -3011   5041    260       C  
ATOM    906  OD1 ASN A 109     -28.644  -8.507 155.320  1.00179.62           O  
ANISOU  906  OD1 ASN A 109    20107  28195  19944  -3037   4872    429       O  
ATOM    907  ND2 ASN A 109     -29.648  -6.968 156.620  1.00183.45           N  
ANISOU  907  ND2 ASN A 109    20456  28983  20264  -2909   5140    134       N  
ATOM    908  N   LEU A 110     -31.578  -9.053 151.759  1.00166.45           N  
ANISOU  908  N   LEU A 110    17454  26491  19297  -3140   4751     68       N  
ATOM    909  CA  LEU A 110     -31.249  -9.967 150.679  1.00150.77           C  
ANISOU  909  CA  LEU A 110    15471  24331  17485  -3245   4586    161       C  
ATOM    910  C   LEU A 110     -31.070  -9.257 149.347  1.00130.39           C  
ANISOU  910  C   LEU A 110    12727  21747  15067  -3070   4328      5       C  
ATOM    911  O   LEU A 110     -30.821  -9.919 148.332  1.00125.23           O  
ANISOU  911  O   LEU A 110    12054  20963  14565  -3141   4172     51       O  
ATOM    912  CB  LEU A 110     -32.343 -11.019 150.550  1.00148.48           C  
ANISOU  912  CB  LEU A 110    14996  24036  17384  -3475   4741    182       C  
ATOM    913  CG  LEU A 110     -32.255 -12.158 151.559  1.00140.64           C  
ANISOU  913  CG  LEU A 110    14225  22940  16273  -3686   4963    421       C  
ATOM    914  CD1 LEU A 110     -33.220 -13.274 151.195  1.00132.54           C  
ANISOU  914  CD1 LEU A 110    13021  21861  15477  -3927   5088    438       C  
ATOM    915  CD2 LEU A 110     -30.835 -12.678 151.633  1.00139.14           C  
ANISOU  915  CD2 LEU A 110    14394  22538  15934  -3681   4844    653       C  
ATOM    916  N   ARG A 111     -31.183  -7.937 149.335  1.00123.03           N  
ANISOU  916  N   ARG A 111    11692  20947  14109  -2837   4293   -171       N  
ATOM    917  CA  ARG A 111     -31.098  -7.096 148.150  1.00119.92           C  
ANISOU  917  CA  ARG A 111    11136  20568  13861  -2623   4079   -319       C  
ATOM    918  C   ARG A 111     -29.736  -7.113 147.457  1.00123.24           C  
ANISOU  918  C   ARG A 111    11772  20818  14237  -2560   3838   -228       C  
ATOM    919  O   ARG A 111     -29.699  -7.090 146.218  1.00123.46           O  
ANISOU  919  O   ARG A 111    11671  20805  14435  -2492   3648   -278       O  
ATOM    920  CB  ARG A 111     -31.481  -5.660 148.514  1.00117.17           C  
ANISOU  920  CB  ARG A 111    10677  20366  13475  -2376   4151   -503       C  
ATOM    921  CG  ARG A 111     -32.924  -5.532 148.971  1.00118.00           C  
ANISOU  921  CG  ARG A 111    10509  20654  13672  -2399   4367   -618       C  
ATOM    922  CD  ARG A 111     -33.193  -4.255 149.724  1.00122.02           C  
ANISOU  922  CD  ARG A 111    10994  21276  14091  -2193   4509   -761       C  
ATOM    923  NE  ARG A 111     -34.617  -4.100 149.995  1.00123.58           N  
ANISOU  923  NE  ARG A 111    10893  21653  14410  -2190   4700   -878       N  
ATOM    924  CZ  ARG A 111     -35.115  -3.165 150.792  1.00127.69           C  
ANISOU  924  CZ  ARG A 111    11362  22286  14871  -2051   4888   -998       C  
ATOM    925  NH1 ARG A 111     -34.299  -2.309 151.389  1.00132.75           N  
ANISOU  925  NH1 ARG A 111    12238  22872  15329  -1916   4908  -1030       N  
ATOM    926  NH2 ARG A 111     -36.422  -3.083 150.992  1.00121.08           N  
ANISOU  926  NH2 ARG A 111    10235  21613  14156  -2051   5060  -1096       N  
ATOM    927  N   PRO A 112     -28.588  -7.118 148.199  1.00117.43           N  
ANISOU  927  N   PRO A 112    11357  19994  13268  -2568   3831    -97       N  
ATOM    928  CA  PRO A 112     -27.284  -7.062 147.519  1.00104.02           C  
ANISOU  928  CA  PRO A 112     9844  18146  11533  -2494   3600    -21       C  
ATOM    929  C   PRO A 112     -27.103  -8.078 146.400  1.00103.76           C  
ANISOU  929  C   PRO A 112     9785  17965  11675  -2613   3448     76       C  
ATOM    930  O   PRO A 112     -26.843  -7.699 145.254  1.00120.81           O  
ANISOU  930  O   PRO A 112    11853  20087  13961  -2490   3255      3       O  
ATOM    931  CB  PRO A 112     -26.288  -7.326 148.655  1.00108.77           C  
ANISOU  931  CB  PRO A 112    10775  18696  11855  -2559   3650    144       C  
ATOM    932  CG  PRO A 112     -26.953  -6.839 149.860  1.00118.44           C  
ANISOU  932  CG  PRO A 112    11975  20082  12945  -2552   3875     65       C  
ATOM    933  CD  PRO A 112     -28.419  -7.089 149.667  1.00122.98           C  
ANISOU  933  CD  PRO A 112    12254  20752  13720  -2624   4020    -27       C  
ATOM    934  N   LYS A 113     -27.250  -9.366 146.708  1.00100.97           N  
ANISOU  934  N   LYS A 113     9514  17514  11337  -2847   3545    236       N  
ATOM    935  CA  LYS A 113     -26.801 -10.386 145.769  1.00105.16           C  
ANISOU  935  CA  LYS A 113    10103  17849  12002  -2968   3410    351       C  
ATOM    936  C   LYS A 113     -27.753 -10.564 144.593  1.00106.94           C  
ANISOU  936  C   LYS A 113    10022  18117  12492  -3001   3338    199       C  
ATOM    937  O   LYS A 113     -27.305 -10.864 143.482  1.00109.21           O  
ANISOU  937  O   LYS A 113    10308  18288  12898  -2998   3149    205       O  
ATOM    938  CB  LYS A 113     -26.576 -11.710 146.501  1.00107.63           C  
ANISOU  938  CB  LYS A 113    10636  18006  12251  -3187   3555    586       C  
ATOM    939  CG  LYS A 113     -25.363 -11.668 147.429  1.00103.72           C  
ANISOU  939  CG  LYS A 113    10475  17448  11487  -3133   3550    772       C  
ATOM    940  CD  LYS A 113     -24.333 -10.656 146.932  1.00 93.24           C  
ANISOU  940  CD  LYS A 113     9214  16133  10081  -2924   3322    705       C  
ATOM    941  CE  LYS A 113     -23.116 -11.330 146.321  1.00 84.05           C  
ANISOU  941  CE  LYS A 113     8264  14747   8926  -2940   3144    883       C  
ATOM    942  NZ  LYS A 113     -21.964 -10.386 146.237  1.00 77.46           N  
ANISOU  942  NZ  LYS A 113     7553  13934   7943  -2752   2965    861       N  
ATOM    943  N   LEU A 114     -29.051 -10.343 144.781  1.00114.73           N  
ANISOU  943  N   LEU A 114    10741  19283  13569  -3020   3472     54       N  
ATOM    944  CA  LEU A 114     -29.951 -10.460 143.636  1.00121.47           C  
ANISOU  944  CA  LEU A 114    11286  20211  14655  -3032   3376   -102       C  
ATOM    945  C   LEU A 114     -30.023  -9.169 142.816  1.00115.45           C  
ANISOU  945  C   LEU A 114    10339  19584  13941  -2740   3200   -273       C  
ATOM    946  O   LEU A 114     -30.286  -9.222 141.603  1.00115.01           O  
ANISOU  946  O   LEU A 114    10105  19551  14043  -2697   3025   -364       O  
ATOM    947  CB  LEU A 114     -31.341 -10.889 144.088  1.00116.80           C  
ANISOU  947  CB  LEU A 114    10464  19757  14159  -3189   3584   -179       C  
ATOM    948  CG  LEU A 114     -31.356 -12.217 144.852  1.00111.01           C  
ANISOU  948  CG  LEU A 114     9905  18872  13402  -3477   3783     -1       C  
ATOM    949  CD1 LEU A 114     -32.771 -12.778 144.953  1.00121.77           C  
ANISOU  949  CD1 LEU A 114    10997  20355  14916  -3662   3956   -100       C  
ATOM    950  CD2 LEU A 114     -30.418 -13.203 144.153  1.00109.57           C  
ANISOU  950  CD2 LEU A 114     9931  18424  13276  -3594   3651    143       C  
ATOM    951  N   LEU A 115     -29.706  -8.008 143.415  1.00113.38           N  
ANISOU  951  N   LEU A 115    10141  19396  13541  -2526   3235   -313       N  
ATOM    952  CA  LEU A 115     -29.420  -6.850 142.574  1.00113.46           C  
ANISOU  952  CA  LEU A 115    10066  19452  13592  -2233   3058   -424       C  
ATOM    953  C   LEU A 115     -28.142  -7.066 141.770  1.00101.81           C  
ANISOU  953  C   LEU A 115     8790  17793  12098  -2211   2843   -324       C  
ATOM    954  O   LEU A 115     -28.044  -6.641 140.612  1.00 77.17           O  
ANISOU  954  O   LEU A 115     5555  14680   9085  -2048   2654   -394       O  
ATOM    955  CB  LEU A 115     -29.306  -5.595 143.424  1.00113.27           C  
ANISOU  955  CB  LEU A 115    10097  19506  13435  -2024   3170   -495       C  
ATOM    956  CG  LEU A 115     -28.603  -4.395 142.763  1.00100.52           C  
ANISOU  956  CG  LEU A 115     8518  17856  11820  -1723   3018   -564       C  
ATOM    957  CD1 LEU A 115     -29.393  -3.902 141.561  1.00 95.71           C  
ANISOU  957  CD1 LEU A 115     7607  17347  11410  -1525   2891   -687       C  
ATOM    958  CD2 LEU A 115     -28.358  -3.278 143.759  1.00102.35           C  
ANISOU  958  CD2 LEU A 115     8867  18116  11904  -1565   3161   -632       C  
ATOM    959  N   LEU A 116     -27.154  -7.734 142.369  1.00116.34           N  
ANISOU  959  N   LEU A 116    10930  19473  13801  -2361   2870   -148       N  
ATOM    960  CA  LEU A 116     -25.944  -8.096 141.639  1.00114.88           C  
ANISOU  960  CA  LEU A 116    10936  19104  13608  -2367   2679    -34       C  
ATOM    961  C   LEU A 116     -26.271  -9.015 140.468  1.00109.53           C  
ANISOU  961  C   LEU A 116    10134  18354  13127  -2494   2557    -42       C  
ATOM    962  O   LEU A 116     -25.788  -8.814 139.349  1.00105.70           O  
ANISOU  962  O   LEU A 116     9628  17817  12717  -2387   2355    -68       O  
ATOM    963  CB  LEU A 116     -24.946  -8.753 142.596  1.00118.54           C  
ANISOU  963  CB  LEU A 116    11731  19420  13888  -2507   2748    173       C  
ATOM    964  CG  LEU A 116     -23.743  -9.473 141.979  1.00116.05           C  
ANISOU  964  CG  LEU A 116    11634  18884  13575  -2570   2585    337       C  
ATOM    965  CD1 LEU A 116     -22.508  -9.215 142.820  1.00115.78           C  
ANISOU  965  CD1 LEU A 116    11895  18788  13308  -2516   2577    474       C  
ATOM    966  CD2 LEU A 116     -23.995 -10.968 141.842  1.00117.10           C  
ANISOU  966  CD2 LEU A 116    11812  18860  13820  -2826   2643    459       C  
ATOM    967  N   LYS A 117     -27.080 -10.045 140.720  1.00118.51           N  
ANISOU  967  N   LYS A 117    11197  19484  14347  -2730   2687    -24       N  
ATOM    968  CA  LYS A 117     -27.490 -10.948 139.650  1.00113.95           C  
ANISOU  968  CA  LYS A 117    10494  18844  13959  -2875   2591    -66       C  
ATOM    969  C   LYS A 117     -28.254 -10.201 138.563  1.00110.11           C  
ANISOU  969  C   LYS A 117     9692  18548  13598  -2694   2438   -269       C  
ATOM    970  O   LYS A 117     -28.048 -10.448 137.367  1.00110.64           O  
ANISOU  970  O   LYS A 117     9709  18564  13764  -2681   2245   -309       O  
ATOM    971  CB  LYS A 117     -28.330 -12.089 140.227  1.00114.82           C  
ANISOU  971  CB  LYS A 117    10564  18925  14138  -3156   2796    -32       C  
ATOM    972  CG  LYS A 117     -29.458 -12.562 139.326  1.00112.36           C  
ANISOU  972  CG  LYS A 117     9956  18710  14028  -3266   2755   -198       C  
ATOM    973  CD  LYS A 117     -30.143 -13.777 139.914  1.00113.16           C  
ANISOU  973  CD  LYS A 117    10056  18738  14201  -3567   2975   -148       C  
ATOM    974  CE  LYS A 117     -29.265 -15.008 139.793  1.00114.67           C  
ANISOU  974  CE  LYS A 117    10534  18612  14425  -3760   2986     32       C  
ATOM    975  NZ  LYS A 117     -29.652 -16.050 140.783  1.00107.31           N  
ANISOU  975  NZ  LYS A 117     9704  17566  13502  -4004   3257    162       N  
ATOM    976  N   HIS A 118     -29.120  -9.264 138.954  1.00104.41           N  
ANISOU  976  N   HIS A 118     8761  18046  12865  -2535   2519   -392       N  
ATOM    977  CA  HIS A 118     -29.839  -8.468 137.966  1.00 95.86           C  
ANISOU  977  CA  HIS A 118     7385  17150  11887  -2311   2373   -560       C  
ATOM    978  C   HIS A 118     -28.875  -7.661 137.099  1.00 94.89           C  
ANISOU  978  C   HIS A 118     7351  16966  11738  -2053   2159   -547       C  
ATOM    979  O   HIS A 118     -28.927  -7.744 135.870  1.00100.00           O  
ANISOU  979  O   HIS A 118     7887  17630  12477  -1987   1960   -602       O  
ATOM    980  CB  HIS A 118     -30.850  -7.560 138.662  1.00107.79           C  
ANISOU  980  CB  HIS A 118     8689  18877  13388  -2161   2525   -670       C  
ATOM    981  CG  HIS A 118     -32.194  -8.191 138.856  1.00108.90           C  
ANISOU  981  CG  HIS A 118     8576  19167  13633  -2345   2651   -759       C  
ATOM    982  ND1 HIS A 118     -32.395  -9.276 139.683  1.00108.72           N  
ANISOU  982  ND1 HIS A 118     8646  19065  13598  -2657   2842   -682       N  
ATOM    983  CD2 HIS A 118     -33.405  -7.888 138.333  1.00108.05           C  
ANISOU  983  CD2 HIS A 118     8124  19287  13643  -2255   2617   -913       C  
ATOM    984  CE1 HIS A 118     -33.672  -9.612 139.662  1.00112.17           C  
ANISOU  984  CE1 HIS A 118     8801  19670  14148  -2767   2930   -798       C  
ATOM    985  NE2 HIS A 118     -34.307  -8.786 138.849  1.00112.74           N  
ANISOU  985  NE2 HIS A 118     8599  19941  14297  -2531   2789   -943       N  
ATOM    986  N   ASN A 119     -27.979  -6.887 137.724  1.00 98.77           N  
ANISOU  986  N   ASN A 119     8049  17386  12095  -1908   2199   -479       N  
ATOM    987  CA  ASN A 119     -26.990  -6.106 136.974  1.00 87.64           C  
ANISOU  987  CA  ASN A 119     6742  15899  10659  -1669   2022   -460       C  
ATOM    988  C   ASN A 119     -26.154  -6.993 136.056  1.00 75.19           C  
ANISOU  988  C   ASN A 119     5297  14151   9122  -1801   1845   -370       C  
ATOM    989  O   ASN A 119     -25.831  -6.608 134.919  1.00 66.58           O  
ANISOU  989  O   ASN A 119     4162  13050   8086  -1627   1649   -400       O  
ATOM    990  CB  ASN A 119     -26.078  -5.355 137.945  1.00 84.06           C  
ANISOU  990  CB  ASN A 119     6526  15373  10042  -1570   2124   -400       C  
ATOM    991  CG  ASN A 119     -26.653  -4.024 138.378  1.00 76.95           C  
ANISOU  991  CG  ASN A 119     5504  14607   9127  -1304   2231   -526       C  
ATOM    992  OD1 ASN A 119     -27.615  -3.526 137.792  1.00 74.13           O  
ANISOU  992  OD1 ASN A 119     4889  14387   8890  -1132   2197   -637       O  
ATOM    993  ND2 ASN A 119     -26.065  -3.440 139.415  1.00 72.67           N  
ANISOU  993  ND2 ASN A 119     5157  14020   8436  -1265   2364   -510       N  
ATOM    994  N   LEU A 120     -25.764  -8.169 136.552  1.00 73.98           N  
ANISOU  994  N   LEU A 120     5325  13844   8940  -2093   1921   -248       N  
ATOM    995  CA  LEU A 120     -25.087  -9.151 135.717  1.00 88.75           C  
ANISOU  995  CA  LEU A 120     7319  15527  10874  -2245   1784   -168       C  
ATOM    996  C   LEU A 120     -25.911  -9.468 134.482  1.00 95.41           C  
ANISOU  996  C   LEU A 120     7917  16460  11873  -2256   1644   -306       C  
ATOM    997  O   LEU A 120     -25.376  -9.535 133.370  1.00 84.81           O  
ANISOU  997  O   LEU A 120     6602  15045  10577  -2194   1450   -312       O  
ATOM    998  CB  LEU A 120     -24.823 -10.424 136.520  1.00 87.62           C  
ANISOU  998  CB  LEU A 120     7382  15205  10705  -2548   1932    -20       C  
ATOM    999  CG  LEU A 120     -23.599 -10.440 137.432  1.00 88.64           C  
ANISOU  999  CG  LEU A 120     7833  15180  10665  -2559   1991    172       C  
ATOM   1000  CD1 LEU A 120     -23.129 -11.865 137.640  1.00 93.83           C  
ANISOU 1000  CD1 LEU A 120     8711  15593  11348  -2815   2051    344       C  
ATOM   1001  CD2 LEU A 120     -22.492  -9.587 136.832  1.00 92.36           C  
ANISOU 1001  CD2 LEU A 120     8403  15609  11081  -2341   1813    192       C  
ATOM   1002  N   PHE A 121     -27.219  -9.673 134.661  1.00 96.00           N  
ANISOU 1002  N   PHE A 121     7751  16705  12020  -2336   1739   -423       N  
ATOM   1003  CA  PHE A 121     -28.081  -9.925 133.510  1.00 89.72           C  
ANISOU 1003  CA  PHE A 121     6702  16039  11349  -2340   1599   -572       C  
ATOM   1004  C   PHE A 121     -28.086  -8.739 132.556  1.00 96.42           C  
ANISOU 1004  C   PHE A 121     7414  17031  12191  -1986   1400   -649       C  
ATOM   1005  O   PHE A 121     -27.969  -8.917 131.339  1.00 71.18           O  
ANISOU 1005  O   PHE A 121     4171  13832   9041  -1942   1200   -696       O  
ATOM   1006  CB  PHE A 121     -29.508 -10.247 133.955  1.00 83.34           C  
ANISOU 1006  CB  PHE A 121     5640  15416  10608  -2475   1747   -686       C  
ATOM   1007  CG  PHE A 121     -30.399 -10.690 132.829  1.00 91.64           C  
ANISOU 1007  CG  PHE A 121     6437  16608  11774  -2533   1611   -843       C  
ATOM   1008  CD1 PHE A 121     -31.047  -9.763 132.025  1.00 90.03           C  
ANISOU 1008  CD1 PHE A 121     5979  16648  11582  -2255   1454   -965       C  
ATOM   1009  CD2 PHE A 121     -30.561 -12.035 132.552  1.00 99.80           C  
ANISOU 1009  CD2 PHE A 121     7502  17524  12896  -2856   1642   -866       C  
ATOM   1010  CE1 PHE A 121     -31.853 -10.173 130.980  1.00 91.46           C  
ANISOU 1010  CE1 PHE A 121     5929  16985  11836  -2306   1316  -1110       C  
ATOM   1011  CE2 PHE A 121     -31.365 -12.451 131.507  1.00102.23           C  
ANISOU 1011  CE2 PHE A 121     7579  17974  13290  -2924   1516  -1033       C  
ATOM   1012  CZ  PHE A 121     -32.012 -11.519 130.721  1.00 97.45           C  
ANISOU 1012  CZ  PHE A 121     6711  17644  12671  -2651   1345  -1156       C  
ATOM   1013  N   LEU A 122     -28.249  -7.526 133.093  1.00 94.57           N  
ANISOU 1013  N   LEU A 122     7122  16911  11897  -1723   1464   -662       N  
ATOM   1014  CA  LEU A 122     -28.194  -6.318 132.274  1.00 96.40           C  
ANISOU 1014  CA  LEU A 122     7264  17238  12127  -1348   1306   -705       C  
ATOM   1015  C   LEU A 122     -26.994  -6.361 131.338  1.00100.05           C  
ANISOU 1015  C   LEU A 122     7916  17530  12570  -1279   1113   -628       C  
ATOM   1016  O   LEU A 122     -27.135  -6.339 130.108  1.00105.92           O  
ANISOU 1016  O   LEU A 122     8563  18327  13354  -1168    914   -678       O  
ATOM   1017  CB  LEU A 122     -28.122  -5.061 133.150  1.00 94.80           C  
ANISOU 1017  CB  LEU A 122     7092  17071  11858  -1098   1444   -696       C  
ATOM   1018  CG  LEU A 122     -29.375  -4.404 133.727  1.00 92.12           C  
ANISOU 1018  CG  LEU A 122     6511  16940  11550   -973   1587   -798       C  
ATOM   1019  CD1 LEU A 122     -30.319  -4.053 132.609  1.00 87.00           C  
ANISOU 1019  CD1 LEU A 122     5583  16485  10990   -770   1425   -893       C  
ATOM   1020  CD2 LEU A 122     -30.063  -5.238 134.784  1.00 94.65           C  
ANISOU 1020  CD2 LEU A 122     6781  17309  11872  -1283   1794   -816       C  
ATOM   1021  N   LEU A 123     -25.798  -6.472 131.917  1.00 99.47           N  
ANISOU 1021  N   LEU A 123     8119  17255  12423  -1356   1170   -502       N  
ATOM   1022  CA  LEU A 123     -24.581  -6.350 131.115  1.00 91.95           C  
ANISOU 1022  CA  LEU A 123     7347  16141  11449  -1258   1003   -423       C  
ATOM   1023  C   LEU A 123     -24.372  -7.555 130.192  1.00 97.67           C  
ANISOU 1023  C   LEU A 123     8111  16759  12241  -1485    866   -418       C  
ATOM   1024  O   LEU A 123     -23.978  -7.391 129.031  1.00110.21           O  
ANISOU 1024  O   LEU A 123     9708  18320  13848  -1349    669   -429       O  
ATOM   1025  CB  LEU A 123     -23.372  -6.157 132.013  1.00 80.17           C  
ANISOU 1025  CB  LEU A 123     6127  14480   9854  -1289   1104   -293       C  
ATOM   1026  CG  LEU A 123     -23.565  -5.003 132.996  1.00 73.21           C  
ANISOU 1026  CG  LEU A 123     5232  13689   8897  -1092   1265   -326       C  
ATOM   1027  CD1 LEU A 123     -22.531  -5.032 134.135  1.00 77.68           C  
ANISOU 1027  CD1 LEU A 123     6068  14122   9326  -1204   1398   -215       C  
ATOM   1028  CD2 LEU A 123     -23.520  -3.705 132.202  1.00 73.30           C  
ANISOU 1028  CD2 LEU A 123     5168  13748   8935   -699   1160   -383       C  
ATOM   1029  N   ASP A 124     -24.649  -8.778 130.674  1.00 86.61           N  
ANISOU 1029  N   ASP A 124     6747  15283  10878  -1826    978   -404       N  
ATOM   1030  CA  ASP A 124     -24.361  -9.961 129.862  1.00 87.31           C  
ANISOU 1030  CA  ASP A 124     6914  15219  11041  -2053    882   -404       C  
ATOM   1031  C   ASP A 124     -25.372 -10.146 128.741  1.00 90.97           C  
ANISOU 1031  C   ASP A 124     7128  15858  11580  -2034    744   -574       C  
ATOM   1032  O   ASP A 124     -25.027 -10.707 127.697  1.00107.62           O  
ANISOU 1032  O   ASP A 124     9287  17879  13727  -2098    596   -606       O  
ATOM   1033  CB  ASP A 124     -24.318 -11.202 130.744  1.00100.11           C  
ANISOU 1033  CB  ASP A 124     8680  16667  12691  -2399   1071   -323       C  
ATOM   1034  CG  ASP A 124     -22.998 -11.344 131.481  1.00 97.47           C  
ANISOU 1034  CG  ASP A 124     8664  16098  12274  -2445   1138   -121       C  
ATOM   1035  OD1 ASP A 124     -22.049 -10.615 131.143  1.00 96.29           O  
ANISOU 1035  OD1 ASP A 124     8618  15905  12063  -2250   1019    -62       O  
ATOM   1036  OD2 ASP A 124     -22.907 -12.189 132.403  1.00 98.21           O1-
ANISOU 1036  OD2 ASP A 124     8907  16052  12357  -2666   1313    -13       O1-
ATOM   1037  N   ASN A 125     -26.609  -9.670 128.912  1.00 92.84           N  
ANISOU 1037  N   ASN A 125     7097  16350  11829  -1942    788   -688       N  
ATOM   1038  CA  ASN A 125     -27.660  -9.934 127.945  1.00 96.14           C  
ANISOU 1038  CA  ASN A 125     7263  16966  12302  -1954    669   -850       C  
ATOM   1039  C   ASN A 125     -28.041  -8.727 127.101  1.00 91.47           C  
ANISOU 1039  C   ASN A 125     6497  16592  11664  -1568    494   -905       C  
ATOM   1040  O   ASN A 125     -28.746  -8.897 126.102  1.00 73.51           O  
ANISOU 1040  O   ASN A 125     4040  14486   9404  -1542    351  -1023       O  
ATOM   1041  CB  ASN A 125     -28.912 -10.457 128.664  1.00 96.58           C  
ANISOU 1041  CB  ASN A 125     7115  17166  12416  -2163    845   -944       C  
ATOM   1042  CG  ASN A 125     -28.698 -11.813 129.299  1.00 96.61           C  
ANISOU 1042  CG  ASN A 125     7281  16947  12481  -2553   1015   -896       C  
ATOM   1043  OD1 ASN A 125     -29.052 -12.839 128.724  1.00 94.13           O  
ANISOU 1043  OD1 ASN A 125     6922  16598  12244  -2789    994   -987       O  
ATOM   1044  ND2 ASN A 125     -28.113 -11.825 130.490  1.00 97.27           N  
ANISOU 1044  ND2 ASN A 125     7565  16874  12521  -2616   1194   -747       N  
ATOM   1045  N   ILE A 126     -27.608  -7.518 127.461  1.00103.51           N  
ANISOU 1045  N   ILE A 126     8083  18115  13132  -1262    509   -821       N  
ATOM   1046  CA  ILE A 126     -28.028  -6.352 126.692  1.00100.31           C  
ANISOU 1046  CA  ILE A 126     7531  17888  12695   -870    369   -852       C  
ATOM   1047  C   ILE A 126     -26.845  -5.469 126.328  1.00 98.92           C  
ANISOU 1047  C   ILE A 126     7571  17553  12463   -587    280   -734       C  
ATOM   1048  O   ILE A 126     -26.711  -5.046 125.180  1.00114.38           O  
ANISOU 1048  O   ILE A 126     9527  19542  14390   -359     91   -729       O  
ATOM   1049  CB  ILE A 126     -29.089  -5.537 127.454  1.00 98.04           C  
ANISOU 1049  CB  ILE A 126     7029  17801  12420   -708    507   -900       C  
ATOM   1050  CG1 ILE A 126     -30.454  -6.218 127.350  1.00110.09           C  
ANISOU 1050  CG1 ILE A 126     8267  19559  14002   -895    524  -1041       C  
ATOM   1051  CG2 ILE A 126     -29.161  -4.111 126.915  1.00 89.85           C  
ANISOU 1051  CG2 ILE A 126     5945  16845  11349   -245    414   -867       C  
ATOM   1052  CD1 ILE A 126     -31.551  -5.502 128.095  1.00118.76           C  
ANISOU 1052  CD1 ILE A 126     9136  20863  15126   -755    666  -1094       C  
ATOM   1053  N   VAL A 127     -25.981  -5.197 127.301  1.00 87.92           N  
ANISOU 1053  N   VAL A 127     6371  15989  11045   -604    420   -638       N  
ATOM   1054  CA  VAL A 127     -24.961  -4.158 127.159  1.00 83.13           C  
ANISOU 1054  CA  VAL A 127     5945  15250  10392   -307    383   -540       C  
ATOM   1055  C   VAL A 127     -23.835  -4.611 126.229  1.00 75.24           C  
ANISOU 1055  C   VAL A 127     5138  14070   9378   -349    212   -472       C  
ATOM   1056  O   VAL A 127     -23.602  -4.029 125.154  1.00 65.66           O  
ANISOU 1056  O   VAL A 127     3952  12851   8143    -81     48   -453       O  
ATOM   1057  CB  VAL A 127     -24.453  -3.749 128.554  1.00 78.01           C  
ANISOU 1057  CB  VAL A 127     5427  14506   9708   -337    603   -485       C  
ATOM   1058  CG1 VAL A 127     -23.443  -2.635 128.469  1.00 57.82           C  
ANISOU 1058  CG1 VAL A 127     3047  11811   7110    -35    595   -411       C  
ATOM   1059  CG2 VAL A 127     -25.650  -3.321 129.441  1.00 75.97           C  
ANISOU 1059  CG2 VAL A 127     4972  14429   9465   -298    778   -568       C  
ATOM   1060  N   LYS A 128     -23.116  -5.651 126.628  1.00 74.28           N  
ANISOU 1060  N   LYS A 128     5172  13785   9265   -678    258   -423       N  
ATOM   1061  CA  LYS A 128     -22.104  -6.194 125.729  1.00 67.32           C  
ANISOU 1061  CA  LYS A 128     4465  12728   8385   -746    101   -369       C  
ATOM   1062  C   LYS A 128     -22.699  -6.730 124.426  1.00 72.95           C  
ANISOU 1062  C   LYS A 128     5064  13534   9120   -773    -80   -471       C  
ATOM   1063  O   LYS A 128     -22.029  -6.619 123.384  1.00 83.60           O  
ANISOU 1063  O   LYS A 128     6522  14798  10443   -648   -247   -442       O  
ATOM   1064  CB  LYS A 128     -21.282  -7.256 126.467  1.00 74.95           C  
ANISOU 1064  CB  LYS A 128     5649  13465   9366  -1093    203   -281       C  
ATOM   1065  CG  LYS A 128     -20.900  -6.792 127.861  1.00 71.49           C  
ANISOU 1065  CG  LYS A 128     5373  12919   8873  -1076    390   -191       C  
ATOM   1066  CD  LYS A 128     -20.423  -7.930 128.726  1.00 70.03           C  
ANISOU 1066  CD  LYS A 128     5369  12556   8685  -1420    516    -96       C  
ATOM   1067  CE  LYS A 128     -19.036  -7.634 129.254  1.00 73.44           C  
ANISOU 1067  CE  LYS A 128     6171  12686   9046  -1339    522     52       C  
ATOM   1068  NZ  LYS A 128     -18.403  -8.836 129.847  1.00 78.55           N  
ANISOU 1068  NZ  LYS A 128     7025  13133   9690  -1632    598    181       N  
ATOM   1069  N   PRO A 129     -23.913  -7.291 124.394  1.00 80.43           N  
ANISOU 1069  N   PRO A 129     5797  14658  10103   -925    -54   -595       N  
ATOM   1070  CA  PRO A 129     -24.509  -7.630 123.090  1.00 85.51           C  
ANISOU 1070  CA  PRO A 129     6316  15434  10740   -908   -233   -706       C  
ATOM   1071  C   PRO A 129     -24.830  -6.442 122.196  1.00 83.70           C  
ANISOU 1071  C   PRO A 129     5999  15365  10438   -490   -383   -702       C  
ATOM   1072  O   PRO A 129     -24.647  -6.565 120.984  1.00 82.36           O  
ANISOU 1072  O   PRO A 129     5865  15206  10221   -418   -560   -725       O  
ATOM   1073  CB  PRO A 129     -25.769  -8.406 123.489  1.00 83.68           C  
ANISOU 1073  CB  PRO A 129     5860  15370  10565  -1167   -133   -838       C  
ATOM   1074  CG  PRO A 129     -25.377  -9.084 124.735  1.00 73.63           C  
ANISOU 1074  CG  PRO A 129     4718  13914   9345  -1454     75   -773       C  
ATOM   1075  CD  PRO A 129     -24.535  -8.073 125.477  1.00 79.79           C  
ANISOU 1075  CD  PRO A 129     5646  14597  10075  -1235    142   -632       C  
ATOM   1076  N   ILE A 130     -25.313  -5.309 122.719  1.00 78.79           N  
ANISOU 1076  N   ILE A 130     5277  14857   9803   -209   -307   -669       N  
ATOM   1077  CA  ILE A 130     -25.561  -4.165 121.841  1.00 72.56           C  
ANISOU 1077  CA  ILE A 130     4447  14172   8950    210   -432   -634       C  
ATOM   1078  C   ILE A 130     -24.247  -3.664 121.263  1.00 61.71           C  
ANISOU 1078  C   ILE A 130     3350  12566   7533    406   -519   -508       C  
ATOM   1079  O   ILE A 130     -24.162  -3.309 120.074  1.00 67.71           O  
ANISOU 1079  O   ILE A 130     4156  13347   8224    621   -680   -481       O  
ATOM   1080  CB  ILE A 130     -26.338  -3.047 122.572  1.00 76.35           C  
ANISOU 1080  CB  ILE A 130     4784  14780   9447    474   -304   -621       C  
ATOM   1081  CG1 ILE A 130     -26.571  -1.857 121.644  1.00 73.74           C  
ANISOU 1081  CG1 ILE A 130     4445  14515   9057    919   -415   -557       C  
ATOM   1082  CG2 ILE A 130     -25.606  -2.531 123.780  1.00 79.14           C  
ANISOU 1082  CG2 ILE A 130     5291  14950   9828    502   -114   -544       C  
ATOM   1083  CD1 ILE A 130     -27.632  -2.102 120.615  1.00 75.62           C  
ANISOU 1083  CD1 ILE A 130     4461  15027   9245    955   -573   -641       C  
ATOM   1084  N   ILE A 131     -23.184  -3.679 122.074  1.00 72.08           N  
ANISOU 1084  N   ILE A 131     4856  13656   8875    319   -412   -427       N  
ATOM   1085  CA  ILE A 131     -21.872  -3.322 121.532  1.00 78.77           C  
ANISOU 1085  CA  ILE A 131     5966  14274   9690    469   -493   -316       C  
ATOM   1086  C   ILE A 131     -21.462  -4.304 120.436  1.00 78.72           C  
ANISOU 1086  C   ILE A 131     6039  14211   9659    287   -664   -346       C  
ATOM   1087  O   ILE A 131     -21.170  -3.909 119.301  1.00 53.74           O  
ANISOU 1087  O   ILE A 131     2971  11016   6431    506   -808   -309       O  
ATOM   1088  CB  ILE A 131     -20.818  -3.243 122.647  1.00 76.53           C  
ANISOU 1088  CB  ILE A 131     5874  13767   9436    374   -343   -233       C  
ATOM   1089  CG1 ILE A 131     -20.935  -1.908 123.380  1.00 73.25           C  
ANISOU 1089  CG1 ILE A 131     5482  13329   9022    675   -192   -196       C  
ATOM   1090  CG2 ILE A 131     -19.419  -3.392 122.058  1.00 80.59           C  
ANISOU 1090  CG2 ILE A 131     6762  13923   9935    371   -430   -136       C  
ATOM   1091  CD1 ILE A 131     -20.790  -2.023 124.872  1.00 74.18           C  
ANISOU 1091  CD1 ILE A 131     5677  13350   9156    476     19   -199       C  
ATOM   1092  N   ALA A 132     -21.451  -5.603 120.757  1.00 70.64           N  
ANISOU 1092  N   ALA A 132     4995  13157   8687   -118   -632   -415       N  
ATOM   1093  CA  ALA A 132     -21.057  -6.621 119.786  1.00 78.74           C  
ANISOU 1093  CA  ALA A 132     6108  14102   9708   -323   -762   -467       C  
ATOM   1094  C   ALA A 132     -21.936  -6.605 118.542  1.00 85.20           C  
ANISOU 1094  C   ALA A 132     6781  15132  10457   -210   -916   -570       C  
ATOM   1095  O   ALA A 132     -21.525  -7.110 117.492  1.00 91.61           O  
ANISOU 1095  O   ALA A 132     7690  15889  11228   -266  -1047   -604       O  
ATOM   1096  CB  ALA A 132     -21.090  -8.008 120.435  1.00 73.37           C  
ANISOU 1096  CB  ALA A 132     5427  13337   9115   -776   -653   -528       C  
ATOM   1097  N   PHE A 133     -23.138  -6.039 118.643  1.00 74.22           N  
ANISOU 1097  N   PHE A 133     5158  13996   9046    -56   -899   -620       N  
ATOM   1098  CA  PHE A 133     -23.972  -5.829 117.467  1.00 72.91           C  
ANISOU 1098  CA  PHE A 133     4848  14066   8790    108  -1050   -692       C  
ATOM   1099  C   PHE A 133     -23.434  -4.682 116.623  1.00 77.65           C  
ANISOU 1099  C   PHE A 133     5604  14606   9292    521  -1152   -559       C  
ATOM   1100  O   PHE A 133     -23.328  -4.799 115.396  1.00 83.34           O  
ANISOU 1100  O   PHE A 133     6377  15371   9918    591  -1302   -575       O  
ATOM   1101  CB  PHE A 133     -25.416  -5.558 117.898  1.00 69.48           C  
ANISOU 1101  CB  PHE A 133     4109  13923   8368    151   -992   -774       C  
ATOM   1102  CG  PHE A 133     -26.379  -5.415 116.752  1.00 83.46           C  
ANISOU 1102  CG  PHE A 133     5690  15984  10038    294  -1146   -856       C  
ATOM   1103  CD1 PHE A 133     -26.790  -6.524 116.031  1.00 94.82           C  
ANISOU 1103  CD1 PHE A 133     7025  17548  11453     16  -1236  -1016       C  
ATOM   1104  CD2 PHE A 133     -26.877  -4.172 116.400  1.00 85.95           C  
ANISOU 1104  CD2 PHE A 133     5933  16446  10279    705  -1191   -773       C  
ATOM   1105  CE1 PHE A 133     -27.678  -6.393 114.977  1.00102.76           C  
ANISOU 1105  CE1 PHE A 133     7841  18856  12345    144  -1381  -1099       C  
ATOM   1106  CE2 PHE A 133     -27.764  -4.034 115.344  1.00 89.89           C  
ANISOU 1106  CE2 PHE A 133     6251  17236  10668    845  -1336   -833       C  
ATOM   1107  CZ  PHE A 133     -28.164  -5.146 114.633  1.00100.08           C  
ANISOU 1107  CZ  PHE A 133     7422  18685  11919    562  -1437  -1001       C  
ATOM   1108  N   TYR A 134     -23.076  -3.565 117.261  1.00 70.80           N  
ANISOU 1108  N   TYR A 134     4831  13625   8444    795  -1054   -428       N  
ATOM   1109  CA  TYR A 134     -22.620  -2.412 116.492  1.00 73.87           C  
ANISOU 1109  CA  TYR A 134     5391  13922   8753   1196  -1114   -292       C  
ATOM   1110  C   TYR A 134     -21.125  -2.419 116.183  1.00 88.14           C  
ANISOU 1110  C   TYR A 134     7517  15417  10554   1210  -1139   -191       C  
ATOM   1111  O   TYR A 134     -20.713  -1.762 115.219  1.00 89.78           O  
ANISOU 1111  O   TYR A 134     7892  15541  10680   1474  -1213    -98       O  
ATOM   1112  CB  TYR A 134     -22.978  -1.113 117.220  1.00 71.33           C  
ANISOU 1112  CB  TYR A 134     5040  13598   8465   1512   -977   -207       C  
ATOM   1113  CG  TYR A 134     -24.343  -0.572 116.852  1.00 89.74           C  
ANISOU 1113  CG  TYR A 134     7128  16219  10749   1718  -1012   -240       C  
ATOM   1114  CD1 TYR A 134     -25.208  -1.303 116.046  1.00 98.65           C  
ANISOU 1114  CD1 TYR A 134     8051  17624  11810   1586  -1153   -356       C  
ATOM   1115  CD2 TYR A 134     -24.772   0.663 117.318  1.00 94.02           C  
ANISOU 1115  CD2 TYR A 134     7643  16762  11319   2041   -895   -161       C  
ATOM   1116  CE1 TYR A 134     -26.459  -0.818 115.715  1.00100.03           C  
ANISOU 1116  CE1 TYR A 134     7981  18092  11934   1778  -1193   -385       C  
ATOM   1117  CE2 TYR A 134     -26.024   1.157 116.991  1.00 96.07           C  
ANISOU 1117  CE2 TYR A 134     7670  17292  11540   2239   -928   -182       C  
ATOM   1118  CZ  TYR A 134     -26.860   0.410 116.190  1.00101.28           C  
ANISOU 1118  CZ  TYR A 134     8111  18248  12121   2110  -1085   -290       C  
ATOM   1119  OH  TYR A 134     -28.106   0.893 115.859  1.00110.92           O  
ANISOU 1119  OH  TYR A 134     9082  19766  13297   2312  -1127   -310       O  
ATOM   1120  N   TYR A 135     -20.304  -3.140 116.951  1.00 87.07           N  
ANISOU 1120  N   TYR A 135     7476  15109  10497    935  -1075   -198       N  
ATOM   1121  CA  TYR A 135     -18.855  -3.045 116.808  1.00 66.55           C  
ANISOU 1121  CA  TYR A 135     5170  12217   7901    971  -1085    -92       C  
ATOM   1122  C   TYR A 135     -18.199  -4.416 116.869  1.00 68.34           C  
ANISOU 1122  C   TYR A 135     5455  12342   8169    576  -1122   -152       C  
ATOM   1123  O   TYR A 135     -18.702  -5.342 117.515  1.00 59.09           O  
ANISOU 1123  O   TYR A 135     4133  11258   7062    252  -1064   -249       O  
ATOM   1124  CB  TYR A 135     -18.223  -2.186 117.912  1.00 57.01           C  
ANISOU 1124  CB  TYR A 135     4082  10826   6754   1113   -923     11       C  
ATOM   1125  CG  TYR A 135     -18.648  -0.745 117.903  1.00 65.46           C  
ANISOU 1125  CG  TYR A 135     5152  11914   7806   1519   -848     82       C  
ATOM   1126  CD1 TYR A 135     -19.831  -0.353 118.508  1.00 60.97           C  
ANISOU 1126  CD1 TYR A 135     4350  11555   7261   1583   -761     26       C  
ATOM   1127  CD2 TYR A 135     -17.883   0.222 117.283  1.00 62.27           C  
ANISOU 1127  CD2 TYR A 135     5008  11282   7371   1823   -842    204       C  
ATOM   1128  CE1 TYR A 135     -20.236   0.958 118.501  1.00 69.21           C  
ANISOU 1128  CE1 TYR A 135     5414  12581   8300   1946   -676     92       C  
ATOM   1129  CE2 TYR A 135     -18.279   1.536 117.280  1.00 59.31           C  
ANISOU 1129  CE2 TYR A 135     4671  10869   6996   2168   -741    272       C  
ATOM   1130  CZ  TYR A 135     -19.459   1.899 117.879  1.00 69.75           C  
ANISOU 1130  CZ  TYR A 135     5754  12404   8344   2235   -664    217       C  
ATOM   1131  OH  TYR A 135     -19.860   3.213 117.862  1.00 78.71           O  
ANISOU 1131  OH  TYR A 135     6937  13481   9488   2579   -555    288       O  
ATOM   1132  N   LYS A 136     -17.044  -4.521 116.205  1.00 65.30           N  
ANISOU 1132  N   LYS A 136     5360  11690   7761    596  -1179    -84       N  
ATOM   1133  CA  LYS A 136     -16.087  -5.559 116.540  1.00 61.52           C  
ANISOU 1133  CA  LYS A 136     5110  10902   7360    268  -1126    -82       C  
ATOM   1134  C   LYS A 136     -14.933  -4.954 117.326  1.00 62.67           C  
ANISOU 1134  C   LYS A 136     5566  10684   7561    351   -993     55       C  
ATOM   1135  O   LYS A 136     -14.451  -3.860 116.992  1.00 68.11           O  
ANISOU 1135  O   LYS A 136     6403  11261   8213    655   -987    143       O  
ATOM   1136  CB  LYS A 136     -15.534  -6.249 115.291  1.00 76.08           C  
ANISOU 1136  CB  LYS A 136     7078  12672   9156    186  -1261   -124       C  
ATOM   1137  CG  LYS A 136     -14.737  -7.520 115.603  1.00 83.11           C  
ANISOU 1137  CG  LYS A 136     8153  13279  10147   -177  -1200   -144       C  
ATOM   1138  CD  LYS A 136     -14.199  -8.178 114.350  1.00 77.79           C  
ANISOU 1138  CD  LYS A 136     7602  12524   9429   -251  -1314   -203       C  
ATOM   1139  CE  LYS A 136     -14.145  -9.693 114.466  1.00 89.21           C  
ANISOU 1139  CE  LYS A 136     9054  13870  10971   -660  -1272   -311       C  
ATOM   1140  NZ  LYS A 136     -15.482 -10.329 114.331  1.00101.64           N  
ANISOU 1140  NZ  LYS A 136    10285  15799  12533   -867  -1315   -497       N  
ATOM   1141  N   PRO A 137     -14.490  -5.633 118.382  1.00 55.54           N  
ANISOU 1141  N   PRO A 137     4760   9603   6740     85   -877     73       N  
ATOM   1142  CA  PRO A 137     -13.233  -5.258 119.030  1.00 42.31           C  
ANISOU 1142  CA  PRO A 137     3383   7591   5101    119   -780    186       C  
ATOM   1143  C   PRO A 137     -12.063  -5.943 118.348  1.00 60.28           C  
ANISOU 1143  C   PRO A 137     5905   9597   7400     15   -839    223       C  
ATOM   1144  O   PRO A 137     -12.151  -7.096 117.925  1.00 68.77           O  
ANISOU 1144  O   PRO A 137     6949  10678   8501   -216   -892    164       O  
ATOM   1145  CB  PRO A 137     -13.423  -5.787 120.457  1.00 42.36           C  
ANISOU 1145  CB  PRO A 137     3342   7596   5157   -120   -644    192       C  
ATOM   1146  CG  PRO A 137     -14.243  -7.040 120.249  1.00 55.91           C  
ANISOU 1146  CG  PRO A 137     4862   9481   6901   -403   -680     97       C  
ATOM   1147  CD  PRO A 137     -15.133  -6.778 119.051  1.00 58.33           C  
ANISOU 1147  CD  PRO A 137     4949  10066   7150   -258   -822     -4       C  
ATOM   1148  N   ILE A 138     -10.952  -5.228 118.216  1.00 57.18           N  
ANISOU 1148  N   ILE A 138     5759   8958   7009    182   -815    308       N  
ATOM   1149  CA  ILE A 138      -9.747  -5.833 117.665  1.00 49.81           C  
ANISOU 1149  CA  ILE A 138     5061   7755   6109     93   -849    348       C  
ATOM   1150  C   ILE A 138      -8.562  -5.485 118.553  1.00 60.18           C  
ANISOU 1150  C   ILE A 138     6589   8807   7469     94   -746    437       C  
ATOM   1151  O   ILE A 138      -8.471  -4.374 119.093  1.00 58.86           O  
ANISOU 1151  O   ILE A 138     6451   8627   7286    265   -670    461       O  
ATOM   1152  CB  ILE A 138      -9.479  -5.409 116.203  1.00 54.70           C  
ANISOU 1152  CB  ILE A 138     5763   8356   6664    294   -952    343       C  
ATOM   1153  CG1 ILE A 138      -9.329  -3.893 116.078  1.00 63.45           C  
ANISOU 1153  CG1 ILE A 138     6945   9433   7731    626   -907    408       C  
ATOM   1154  CG2 ILE A 138     -10.564  -5.943 115.274  1.00 54.63           C  
ANISOU 1154  CG2 ILE A 138     5536   8634   6585    254  -1079    237       C  
ATOM   1155  CD1 ILE A 138      -8.106  -3.492 115.283  1.00 61.10           C  
ANISOU 1155  CD1 ILE A 138     6914   8872   7430    751   -904    471       C  
ATOM   1156  N   LYS A 139      -7.653  -6.448 118.708  1.00 60.54           N  
ANISOU 1156  N   LYS A 139     6779   8651   7575    -97   -739    478       N  
ATOM   1157  CA  LYS A 139      -6.444  -6.242 119.493  1.00 58.73           C  
ANISOU 1157  CA  LYS A 139     6734   8201   7380   -106   -665    560       C  
ATOM   1158  C   LYS A 139      -5.393  -5.546 118.638  1.00 53.21           C  
ANISOU 1158  C   LYS A 139     6223   7308   6686     72   -684    582       C  
ATOM   1159  O   LYS A 139      -5.036  -6.029 117.557  1.00 54.43           O  
ANISOU 1159  O   LYS A 139     6454   7375   6853     65   -752    572       O  
ATOM   1160  CB  LYS A 139      -5.915  -7.568 120.040  1.00 63.40           C  
ANISOU 1160  CB  LYS A 139     7389   8668   8032   -354   -645    617       C  
ATOM   1161  CG  LYS A 139      -6.987  -8.505 120.559  1.00 65.28           C  
ANISOU 1161  CG  LYS A 139     7457   9066   8279   -565   -618    592       C  
ATOM   1162  CD  LYS A 139      -6.523  -9.947 120.539  1.00 86.54           C  
ANISOU 1162  CD  LYS A 139    10238  11591  11052   -788   -604    641       C  
ATOM   1163  CE  LYS A 139      -6.633 -10.536 119.149  1.00 99.75           C  
ANISOU 1163  CE  LYS A 139    11917  13222  12760   -828   -684    551       C  
ATOM   1164  NZ  LYS A 139      -5.662 -11.640 118.941  1.00 90.42           N  
ANISOU 1164  NZ  LYS A 139    10910  11773  11672   -958   -659    610       N  
ATOM   1165  N   THR A 140      -4.916  -4.397 119.124  1.00 62.26           N  
ANISOU 1165  N   THR A 140     7446   8387   7823    219   -608    598       N  
ATOM   1166  CA  THR A 140      -3.858  -3.661 118.445  1.00 52.63           C  
ANISOU 1166  CA  THR A 140     6413   6963   6622    368   -588    616       C  
ATOM   1167  C   THR A 140      -2.532  -4.405 118.481  1.00 70.08           C  
ANISOU 1167  C   THR A 140     8771   8961   8895    237   -594    660       C  
ATOM   1168  O   THR A 140      -1.646  -4.118 117.666  1.00 72.10           O  
ANISOU 1168  O   THR A 140     9172   9046   9177    321   -591    669       O  
ATOM   1169  CB  THR A 140      -3.697  -2.288 119.097  1.00 44.89           C  
ANISOU 1169  CB  THR A 140     5472   5952   5633    517   -473    599       C  
ATOM   1170  OG1 THR A 140      -4.988  -1.698 119.275  1.00 65.87           O  
ANISOU 1170  OG1 THR A 140     7969   8816   8243    634   -451    565       O  
ATOM   1171  CG2 THR A 140      -2.844  -1.367 118.240  1.00 60.70           C  
ANISOU 1171  CG2 THR A 140     7653   7754   7657    694   -426    609       C  
ATOM   1172  N   LEU A 141      -2.389  -5.354 119.410  1.00 66.66           N  
ANISOU 1172  N   LEU A 141     8302   8539   8486     43   -592    697       N  
ATOM   1173  CA  LEU A 141      -1.138  -6.028 119.741  1.00 59.71           C  
ANISOU 1173  CA  LEU A 141     7539   7485   7665    -62   -587    761       C  
ATOM   1174  C   LEU A 141      -0.135  -5.062 120.366  1.00 66.78           C  
ANISOU 1174  C   LEU A 141     8516   8298   8558     11   -522    758       C  
ATOM   1175  O   LEU A 141       0.966  -5.473 120.743  1.00 74.30           O  
ANISOU 1175  O   LEU A 141     9540   9142   9548    -55   -522    806       O  
ATOM   1176  CB  LEU A 141      -0.535  -6.716 118.515  1.00 47.14           C  
ANISOU 1176  CB  LEU A 141     6050   5730   6131    -70   -637    768       C  
ATOM   1177  CG  LEU A 141      -1.471  -7.626 117.722  1.00 63.44           C  
ANISOU 1177  CG  LEU A 141     8040   7872   8193   -154   -699    729       C  
ATOM   1178  CD1 LEU A 141      -0.755  -8.162 116.495  1.00 78.70           C  
ANISOU 1178  CD1 LEU A 141    10099   9635  10171   -150   -731    714       C  
ATOM   1179  CD2 LEU A 141      -1.978  -8.764 118.601  1.00 61.95           C  
ANISOU 1179  CD2 LEU A 141     7764   7743   8032   -362   -684    767       C  
ATOM   1180  N   ASN A 142      -0.500  -3.787 120.490  1.00 42.88           N  
ANISOU 1180  N   ASN A 142     5474   5327   5493    146   -460    694       N  
ATOM   1181  CA  ASN A 142       0.294  -2.820 121.246  1.00 34.32           C  
ANISOU 1181  CA  ASN A 142     4448   4189   4404    179   -375    653       C  
ATOM   1182  C   ASN A 142      -0.173  -2.886 122.696  1.00 48.21           C  
ANISOU 1182  C   ASN A 142     6101   6124   6094     77   -343    646       C  
ATOM   1183  O   ASN A 142      -1.147  -2.230 123.080  1.00 34.52           O  
ANISOU 1183  O   ASN A 142     4282   4521   4313    135   -286    592       O  
ATOM   1184  CB  ASN A 142       0.150  -1.417 120.669  1.00 57.90           C  
ANISOU 1184  CB  ASN A 142     7493   7109   7397    371   -288    585       C  
ATOM   1185  CG  ASN A 142       1.347  -0.537 120.987  1.00 77.65           C  
ANISOU 1185  CG  ASN A 142    10106   9462   9936    384   -191    525       C  
ATOM   1186  OD1 ASN A 142       1.672  -0.321 122.154  1.00 76.85           O  
ANISOU 1186  OD1 ASN A 142     9970   9425   9804    292   -148    476       O  
ATOM   1187  ND2 ASN A 142       2.014  -0.033 119.953  1.00 88.58           N  
ANISOU 1187  ND2 ASN A 142    11621  10659  11378    486   -149    519       N  
ATOM   1188  N   GLY A 143       0.531  -3.670 123.506  1.00 37.92           N  
ANISOU 1188  N   GLY A 143     4802   4830   4774    -61   -372    708       N  
ATOM   1189  CA  GLY A 143      -0.017  -3.980 124.799  1.00 42.15           C  
ANISOU 1189  CA  GLY A 143     5242   5553   5221   -169   -351    732       C  
ATOM   1190  C   GLY A 143      -1.353  -4.670 124.646  1.00 43.56           C  
ANISOU 1190  C   GLY A 143     5311   5848   5391   -218   -369    765       C  
ATOM   1191  O   GLY A 143      -1.621  -5.372 123.665  1.00 40.06           O  
ANISOU 1191  O   GLY A 143     4870   5340   5011   -228   -428    795       O  
ATOM   1192  N   HIS A 144      -2.221  -4.445 125.622  1.00 52.89           N  
ANISOU 1192  N   HIS A 144     6386   7218   6492   -259   -308    739       N  
ATOM   1193  CA  HIS A 144      -3.560  -5.005 125.607  1.00 47.02           C  
ANISOU 1193  CA  HIS A 144     5506   6619   5740   -321   -304    748       C  
ATOM   1194  C   HIS A 144      -4.581  -4.037 125.036  1.00 50.94           C  
ANISOU 1194  C   HIS A 144     5908   7204   6243   -167   -274    644       C  
ATOM   1195  O   HIS A 144      -5.782  -4.216 125.261  1.00 53.44           O  
ANISOU 1195  O   HIS A 144     6070   7699   6536   -202   -249    621       O  
ATOM   1196  CB  HIS A 144      -3.940  -5.439 127.019  1.00 35.50           C  
ANISOU 1196  CB  HIS A 144     3978   5325   4185   -463   -241    795       C  
ATOM   1197  CG  HIS A 144      -2.938  -6.363 127.636  1.00 44.68           C  
ANISOU 1197  CG  HIS A 144     5235   6420   5322   -579   -269    927       C  
ATOM   1198  ND1 HIS A 144      -1.927  -5.921 128.462  1.00 42.69           N  
ANISOU 1198  ND1 HIS A 144     5052   6181   4990   -567   -261    934       N  
ATOM   1199  CD2 HIS A 144      -2.776  -7.702 127.524  1.00 45.30           C  
ANISOU 1199  CD2 HIS A 144     5348   6417   5447   -697   -301   1059       C  
ATOM   1200  CE1 HIS A 144      -1.190  -6.951 128.840  1.00 51.84           C  
ANISOU 1200  CE1 HIS A 144     6271   7291   6135   -651   -301   1082       C  
ATOM   1201  NE2 HIS A 144      -1.687  -8.043 128.288  1.00 52.83           N  
ANISOU 1201  NE2 HIS A 144     6389   7339   6345   -726   -315   1167       N  
ATOM   1202  N   GLU A 145      -4.124  -3.013 124.315  1.00 55.11           N  
ANISOU 1202  N   GLU A 145     6522   7611   6804     10   -266    589       N  
ATOM   1203  CA  GLU A 145      -5.021  -2.062 123.675  1.00 51.63           C  
ANISOU 1203  CA  GLU A 145     6012   7234   6371    203   -236    522       C  
ATOM   1204  C   GLU A 145      -6.033  -2.782 122.800  1.00 48.77           C  
ANISOU 1204  C   GLU A 145     5519   6990   6023    196   -326    537       C  
ATOM   1205  O   GLU A 145      -5.682  -3.673 122.021  1.00 42.46           O  
ANISOU 1205  O   GLU A 145     4768   6108   5259    119   -418    578       O  
ATOM   1206  CB  GLU A 145      -4.217  -1.068 122.833  1.00 61.07           C  
ANISOU 1206  CB  GLU A 145     7362   8229   7611    385   -212    499       C  
ATOM   1207  CG  GLU A 145      -5.076  -0.134 121.996  1.00 59.35           C  
ANISOU 1207  CG  GLU A 145     7098   8052   7399    625   -184    470       C  
ATOM   1208  CD  GLU A 145      -4.259   0.835 121.169  1.00 57.14           C  
ANISOU 1208  CD  GLU A 145     6999   7548   7162    803   -131    469       C  
ATOM   1209  OE1 GLU A 145      -3.049   0.593 120.991  1.00 52.34           O  
ANISOU 1209  OE1 GLU A 145     6535   6762   6590    721   -146    487       O  
ATOM   1210  OE2 GLU A 145      -4.831   1.839 120.693  1.00 61.01           O1-
ANISOU 1210  OE2 GLU A 145     7487   8038   7655   1032    -64    459       O1-
ATOM   1211  N   ILE A 146      -7.297  -2.407 122.952  1.00 50.73           N  
ANISOU 1211  N   ILE A 146     5589   7445   6243    268   -293    487       N  
ATOM   1212  CA  ILE A 146      -8.366  -2.869 122.080  1.00 46.14           C  
ANISOU 1212  CA  ILE A 146     4842   7028   5661    289   -381    469       C  
ATOM   1213  C   ILE A 146      -8.965  -1.648 121.407  1.00 51.15           C  
ANISOU 1213  C   ILE A 146     5424   7731   6281    583   -366    436       C  
ATOM   1214  O   ILE A 146      -9.386  -0.704 122.086  1.00 51.96           O  
ANISOU 1214  O   ILE A 146     5475   7896   6372    706   -252    400       O  
ATOM   1215  CB  ILE A 146      -9.444  -3.651 122.853  1.00 51.68           C  
ANISOU 1215  CB  ILE A 146     5333   7957   6345    103   -357    444       C  
ATOM   1216  CG1 ILE A 146      -8.858  -4.934 123.458  1.00 53.38           C  
ANISOU 1216  CG1 ILE A 146     5625   8081   6578   -174   -357    509       C  
ATOM   1217  CG2 ILE A 146     -10.634  -3.946 121.952  1.00 64.89           C  
ANISOU 1217  CG2 ILE A 146     6793   9846   8016    136   -443    389       C  
ATOM   1218  CD1 ILE A 146      -8.850  -6.118 122.516  1.00 54.82           C  
ANISOU 1218  CD1 ILE A 146     5807   8212   6810   -311   -458    519       C  
ATOM   1219  N   LYS A 147      -8.981  -1.653 120.079  1.00 56.62           N  
ANISOU 1219  N   LYS A 147     6139   8408   6966    708   -468    453       N  
ATOM   1220  CA  LYS A 147      -9.657  -0.615 119.319  1.00 58.18           C  
ANISOU 1220  CA  LYS A 147     6273   8703   7131   1011   -471    453       C  
ATOM   1221  C   LYS A 147     -11.015  -1.133 118.876  1.00 61.16           C  
ANISOU 1221  C   LYS A 147     6371   9403   7463   1007   -575    409       C  
ATOM   1222  O   LYS A 147     -11.143  -2.283 118.439  1.00 68.82           O  
ANISOU 1222  O   LYS A 147     7276  10447   8425    807   -686    381       O  
ATOM   1223  CB  LYS A 147      -8.839  -0.170 118.104  1.00 60.88           C  
ANISOU 1223  CB  LYS A 147     6816   8851   7463   1184   -511    511       C  
ATOM   1224  CG  LYS A 147      -7.781   0.870 118.425  1.00 71.62           C  
ANISOU 1224  CG  LYS A 147     8411   9932   8872   1293   -368    536       C  
ATOM   1225  CD  LYS A 147      -6.419   0.478 117.871  1.00 74.59           C  
ANISOU 1225  CD  LYS A 147     9009  10055   9276   1199   -398    571       C  
ATOM   1226  CE  LYS A 147      -5.765   1.611 117.105  1.00 74.83           C  
ANISOU 1226  CE  LYS A 147     9241   9873   9318   1438   -312    617       C  
ATOM   1227  NZ  LYS A 147      -4.642   1.111 116.278  1.00 60.05           N  
ANISOU 1227  NZ  LYS A 147     7546   7811   7460   1364   -363    650       N  
ATOM   1228  N   PHE A 148     -12.024  -0.283 119.002  1.00 62.17           N  
ANISOU 1228  N   PHE A 148     6328   9725   7570   1225   -530    392       N  
ATOM   1229  CA  PHE A 148     -13.382  -0.637 118.625  1.00 71.72           C  
ANISOU 1229  CA  PHE A 148     7228  11288   8735   1249   -626    338       C  
ATOM   1230  C   PHE A 148     -13.669  -0.101 117.232  1.00 70.55           C  
ANISOU 1230  C   PHE A 148     7056  11239   8509   1545   -740    382       C  
ATOM   1231  O   PHE A 148     -13.607   1.112 117.001  1.00 71.19           O  
ANISOU 1231  O   PHE A 148     7226  11242   8582   1867   -667    454       O  
ATOM   1232  CB  PHE A 148     -14.382  -0.105 119.646  1.00 70.03           C  
ANISOU 1232  CB  PHE A 148     6802  11267   8540   1312   -506    291       C  
ATOM   1233  CG  PHE A 148     -14.573  -1.023 120.810  1.00 59.32           C  
ANISOU 1233  CG  PHE A 148     5356   9967   7217    974   -443    233       C  
ATOM   1234  CD1 PHE A 148     -15.266  -2.209 120.658  1.00 58.88           C  
ANISOU 1234  CD1 PHE A 148     5094  10122   7157    728   -532    169       C  
ATOM   1235  CD2 PHE A 148     -14.018  -0.727 122.041  1.00 56.10           C  
ANISOU 1235  CD2 PHE A 148     5082   9397   6836    890   -287    239       C  
ATOM   1236  CE1 PHE A 148     -15.434  -3.072 121.726  1.00 75.95           C  
ANISOU 1236  CE1 PHE A 148     7195  12313   9350    418   -448    136       C  
ATOM   1237  CE2 PHE A 148     -14.182  -1.581 123.112  1.00 51.87           C  
ANISOU 1237  CE2 PHE A 148     4480   8923   6306    594   -224    210       C  
ATOM   1238  CZ  PHE A 148     -14.892  -2.756 122.955  1.00 73.51           C  
ANISOU 1238  CZ  PHE A 148     7028  11850   9051    362   -296    171       C  
ATOM   1239  N   ILE A 149     -13.963  -1.009 116.307  1.00 63.25           N  
ANISOU 1239  N   ILE A 149     6027  10482   7524   1434   -909    339       N  
ATOM   1240  CA  ILE A 149     -14.177  -0.674 114.908  1.00 57.35           C  
ANISOU 1240  CA  ILE A 149     5263   9863   6665   1684  -1044    379       C  
ATOM   1241  C   ILE A 149     -15.586  -1.111 114.543  1.00 64.01           C  
ANISOU 1241  C   ILE A 149     5750  11130   7440   1661  -1168    280       C  
ATOM   1242  O   ILE A 149     -15.968  -2.258 114.802  1.00 66.39           O  
ANISOU 1242  O   ILE A 149     5870  11591   7763   1345  -1228    162       O  
ATOM   1243  CB  ILE A 149     -13.134  -1.358 114.005  1.00 56.03           C  
ANISOU 1243  CB  ILE A 149     5326   9497   6467   1552  -1130    390       C  
ATOM   1244  CG1 ILE A 149     -11.718  -1.100 114.533  1.00 67.29           C  
ANISOU 1244  CG1 ILE A 149     7083  10497   7986   1493   -992    459       C  
ATOM   1245  CG2 ILE A 149     -13.259  -0.878 112.570  1.00 69.19           C  
ANISOU 1245  CG2 ILE A 149     7028  11266   7995   1826  -1243    445       C  
ATOM   1246  CD1 ILE A 149     -11.281   0.356 114.471  1.00 72.07           C  
ANISOU 1246  CD1 ILE A 149     7871  10916   8597   1827   -869    569       C  
ATOM   1247  N   ARG A 150     -16.354  -0.206 113.940  1.00 67.46           N  
ANISOU 1247  N   ARG A 150     6148  11672   7813   1940  -1165    318       N  
ATOM   1248  CA  ARG A 150     -17.738  -0.523 113.610  1.00 75.82           C  
ANISOU 1248  CA  ARG A 150     6914  13078   8816   1902  -1248    217       C  
ATOM   1249  C   ARG A 150     -17.808  -1.713 112.662  1.00 73.81           C  
ANISOU 1249  C   ARG A 150     6602  12953   8487   1658  -1413    107       C  
ATOM   1250  O   ARG A 150     -17.174  -1.715 111.604  1.00 80.62           O  
ANISOU 1250  O   ARG A 150     7655  13712   9266   1727  -1488    151       O  
ATOM   1251  CB  ARG A 150     -18.435   0.703 113.016  1.00 79.38           C  
ANISOU 1251  CB  ARG A 150     7359  13609   9194   2273  -1225    303       C  
ATOM   1252  CG  ARG A 150     -18.570   1.799 114.055  1.00 99.30           C  
ANISOU 1252  CG  ARG A 150     9896  16025  11808   2478  -1042    372       C  
ATOM   1253  CD  ARG A 150     -19.441   2.999 113.665  1.00116.28           C  
ANISOU 1253  CD  ARG A 150    12002  18270  13911   2829   -996    451       C  
ATOM   1254  NE  ARG A 150     -20.706   2.730 112.964  1.00131.01           N  
ANISOU 1254  NE  ARG A 150    13599  20504  15676   2858  -1130    388       N  
ATOM   1255  CZ  ARG A 150     -21.606   1.788 113.257  1.00133.55           C  
ANISOU 1255  CZ  ARG A 150    13615  21124  16003   2618  -1209    237       C  
ATOM   1256  NH1 ARG A 150     -21.440   0.950 114.271  1.00135.89           N  
ANISOU 1256  NH1 ARG A 150    13825  21405  16401   2310  -1164    135       N  
ATOM   1257  NH2 ARG A 150     -22.700   1.690 112.517  1.00131.02           N  
ANISOU 1257  NH2 ARG A 150    13074  21127  15582   2683  -1325    187       N  
ATOM   1258  N   LYS A 151     -18.590  -2.731 113.052  1.00 74.90           N  
ANISOU 1258  N   LYS A 151     6487  13310   8662   1359  -1447    -46       N  
ATOM   1259  CA  LYS A 151     -18.573  -3.998 112.328  1.00 76.39           C  
ANISOU 1259  CA  LYS A 151     6636  13577   8814   1061  -1567   -181       C  
ATOM   1260  C   LYS A 151     -18.937  -3.810 110.861  1.00 90.38           C  
ANISOU 1260  C   LYS A 151     8409  15504  10428   1225  -1701   -194       C  
ATOM   1261  O   LYS A 151     -18.513  -4.597 110.009  1.00 88.52           O  
ANISOU 1261  O   LYS A 151     8252  15247  10133   1065  -1796   -267       O  
ATOM   1262  CB  LYS A 151     -19.514  -5.022 112.981  1.00 82.91           C  
ANISOU 1262  CB  LYS A 151     7186  14602   9713    719  -1544   -350       C  
ATOM   1263  CG  LYS A 151     -19.413  -6.390 112.304  1.00 87.56           C  
ANISOU 1263  CG  LYS A 151     7766  15211  10292    376  -1631   -505       C  
ATOM   1264  CD  LYS A 151     -20.058  -7.547 113.060  1.00 89.99           C  
ANISOU 1264  CD  LYS A 151     7883  15596  10711    -25  -1557   -661       C  
ATOM   1265  CE  LYS A 151     -21.241  -7.120 113.899  1.00 98.72           C  
ANISOU 1265  CE  LYS A 151     8735  16920  11856     28  -1472   -683       C  
ATOM   1266  NZ  LYS A 151     -21.880  -8.306 114.531  1.00103.69           N  
ANISOU 1266  NZ  LYS A 151     9200  17608  12588   -377  -1385   -837       N  
ATOM   1267  N   GLU A 152     -19.699  -2.766 110.535  1.00107.52           N  
ANISOU 1267  N   GLU A 152    10499  17833  12522   1547  -1702   -121       N  
ATOM   1268  CA  GLU A 152     -20.070  -2.533 109.143  1.00115.18           C  
ANISOU 1268  CA  GLU A 152    11462  18980  13322   1720  -1824   -115       C  
ATOM   1269  C   GLU A 152     -18.847  -2.338 108.248  1.00107.65           C  
ANISOU 1269  C   GLU A 152    10831  17776  12294   1822  -1851    -12       C  
ATOM   1270  O   GLU A 152     -18.716  -2.986 107.197  1.00105.68           O  
ANISOU 1270  O   GLU A 152    10606  17612  11934   1718  -1967    -90       O  
ATOM   1271  CB  GLU A 152     -21.026  -1.334 109.044  1.00124.37           C  
ANISOU 1271  CB  GLU A 152    12504  20326  14424   2077  -1799    -21       C  
ATOM   1272  CG  GLU A 152     -20.519   0.001 109.589  1.00132.99           C  
ANISOU 1272  CG  GLU A 152    13797  21156  15577   2390  -1647    171       C  
ATOM   1273  CD  GLU A 152     -21.637   1.004 109.741  1.00139.17           C  
ANISOU 1273  CD  GLU A 152    14406  22137  16335   2681  -1604    229       C  
ATOM   1274  OE1 GLU A 152     -22.659   0.643 110.360  1.00146.09           O  
ANISOU 1274  OE1 GLU A 152    14990  23261  17257   2565  -1610    114       O  
ATOM   1275  OE2 GLU A 152     -21.510   2.150 109.260  1.00143.01           O1-
ANISOU 1275  OE2 GLU A 152    15049  22525  16762   3020  -1551    389       O1-
ATOM   1276  N   GLU A 153     -17.929  -1.462 108.677  1.00103.39           N  
ANISOU 1276  N   GLU A 153    10543  16922  11819   2010  -1729    152       N  
ATOM   1277  CA  GLU A 153     -16.704  -1.242 107.925  1.00101.58           C  
ANISOU 1277  CA  GLU A 153    10635  16422  11540   2095  -1722    254       C  
ATOM   1278  C   GLU A 153     -15.732  -2.409 108.057  1.00 92.26           C  
ANISOU 1278  C   GLU A 153     9562  15075  10418   1774  -1759    168       C  
ATOM   1279  O   GLU A 153     -15.008  -2.716 107.100  1.00 85.55           O  
ANISOU 1279  O   GLU A 153     8889  14133   9484   1751  -1818    171       O  
ATOM   1280  CB  GLU A 153     -16.034   0.046 108.386  1.00100.47           C  
ANISOU 1280  CB  GLU A 153    10729  15976  11467   2366  -1555    435       C  
ATOM   1281  CG  GLU A 153     -16.641   1.309 107.796  1.00111.92           C  
ANISOU 1281  CG  GLU A 153    12195  17502  12827   2726  -1509    558       C  
ATOM   1282  CD  GLU A 153     -16.481   2.522 108.689  1.00114.19           C  
ANISOU 1282  CD  GLU A 153    12595  17565  13228   2940  -1317    678       C  
ATOM   1283  OE1 GLU A 153     -17.486   3.227 108.925  1.00115.66           O  
ANISOU 1283  OE1 GLU A 153    12622  17919  13405   3133  -1280    706       O  
ATOM   1284  OE2 GLU A 153     -15.352   2.774 109.149  1.00109.32           O1-
ANISOU 1284  OE2 GLU A 153    12224  16604  12708   2911  -1198    735       O1-
ATOM   1285  N   TYR A 154     -15.707  -3.084 109.212  1.00 84.83           N  
ANISOU 1285  N   TYR A 154     8516  14103   9614   1522  -1719     91       N  
ATOM   1286  CA  TYR A 154     -14.736  -4.161 109.383  1.00 66.71           C  
ANISOU 1286  CA  TYR A 154     6335  11634   7380   1227  -1741     26       C  
ATOM   1287  C   TYR A 154     -15.100  -5.378 108.548  1.00 70.58           C  
ANISOU 1287  C   TYR A 154     6712  12306   7800    956  -1867   -158       C  
ATOM   1288  O   TYR A 154     -14.211  -6.055 108.031  1.00 79.12           O  
ANISOU 1288  O   TYR A 154     7959  13242   8861    812  -1909   -198       O  
ATOM   1289  CB  TYR A 154     -14.595  -4.575 110.847  1.00 68.61           C  
ANISOU 1289  CB  TYR A 154     6495  11796   7776   1016  -1651      5       C  
ATOM   1290  CG  TYR A 154     -13.912  -5.930 110.975  1.00 67.29           C  
ANISOU 1290  CG  TYR A 154     6407  11477   7684    632  -1659    -94       C  
ATOM   1291  CD1 TYR A 154     -12.526  -6.031 111.032  1.00 61.36           C  
ANISOU 1291  CD1 TYR A 154     6000  10306   7008    586  -1570     -6       C  
ATOM   1292  CD2 TYR A 154     -14.653  -7.110 110.993  1.00 81.60           C  
ANISOU 1292  CD2 TYR A 154     7992  13493   9519    299  -1710   -279       C  
ATOM   1293  CE1 TYR A 154     -11.899  -7.270 111.127  1.00 70.41           C  
ANISOU 1293  CE1 TYR A 154     7263  11239   8249    248  -1535    -81       C  
ATOM   1294  CE2 TYR A 154     -14.038  -8.342 111.070  1.00 85.38           C  
ANISOU 1294  CE2 TYR A 154     8607  13736  10099    -54  -1660   -359       C  
ATOM   1295  CZ  TYR A 154     -12.666  -8.420 111.149  1.00 83.07           C  
ANISOU 1295  CZ  TYR A 154     8659  13024   9880    -64  -1573   -251       C  
ATOM   1296  OH  TYR A 154     -12.069  -9.656 111.243  1.00 88.12           O  
ANISOU 1296  OH  TYR A 154     9429  13424  10630   -388  -1513   -317       O  
ATOM   1297  N   ILE A 155     -16.387  -5.730 108.480  1.00 74.52           N  
ANISOU 1297  N   ILE A 155     6927  13113   8274    858  -1915   -289       N  
ATOM   1298  CA  ILE A 155     -16.797  -6.840 107.621  1.00 74.60           C  
ANISOU 1298  CA  ILE A 155     6831  13300   8215    602  -2020   -485       C  
ATOM   1299  C   ILE A 155     -16.381  -6.559 106.188  1.00 74.90           C  
ANISOU 1299  C   ILE A 155     7031  13353   8074    782  -2115   -450       C  
ATOM   1300  O   ILE A 155     -15.918  -7.451 105.471  1.00 65.00           O  
ANISOU 1300  O   ILE A 155     5860  12064   6772    578  -2176   -570       O  
ATOM   1301  CB  ILE A 155     -18.314  -7.093 107.721  1.00 67.55           C  
ANISOU 1301  CB  ILE A 155     5602  12754   7311    515  -2047   -623       C  
ATOM   1302  CG1 ILE A 155     -18.703  -7.639 109.093  1.00 76.20           C  
ANISOU 1302  CG1 ILE A 155     6544  13825   8584    255  -1936   -688       C  
ATOM   1303  CG2 ILE A 155     -18.771  -8.073 106.647  1.00 59.66           C  
ANISOU 1303  CG2 ILE A 155     4501  11955   6210    300  -2156   -827       C  
ATOM   1304  CD1 ILE A 155     -20.177  -7.961 109.200  1.00 91.43           C  
ANISOU 1304  CD1 ILE A 155     8147  16085  10509    144  -1947   -837       C  
ATOM   1305  N   SER A 156     -16.517  -5.302 105.760  1.00 77.73           N  
ANISOU 1305  N   SER A 156     7452  13747   8333   1163  -2110   -284       N  
ATOM   1306  CA  SER A 156     -16.058  -4.910 104.433  1.00 78.75           C  
ANISOU 1306  CA  SER A 156     7763  13868   8289   1359  -2172   -216       C  
ATOM   1307  C   SER A 156     -14.557  -5.131 104.283  1.00 79.25           C  
ANISOU 1307  C   SER A 156     8144  13586   8381   1304  -2131   -157       C  
ATOM   1308  O   SER A 156     -14.102  -5.708 103.290  1.00 74.03           O  
ANISOU 1308  O   SER A 156     7588  12930   7608   1212  -2203   -233       O  
ATOM   1309  CB  SER A 156     -16.428  -3.451 104.172  1.00 85.54           C  
ANISOU 1309  CB  SER A 156     8656  14774   9072   1773  -2127    -24       C  
ATOM   1310  OG  SER A 156     -15.523  -2.849 103.268  1.00 95.72           O  
ANISOU 1310  OG  SER A 156    10230  15881  10260   1978  -2103    114       O  
ATOM   1311  N   PHE A 157     -13.773  -4.677 105.265  1.00 82.34           N  
ANISOU 1311  N   PHE A 157     8687  13682   8914   1361  -2012    -29       N  
ATOM   1312  CA  PHE A 157     -12.315  -4.805 105.188  1.00 71.24           C  
ANISOU 1312  CA  PHE A 157     7585  11943   7542   1335  -1962     39       C  
ATOM   1313  C   PHE A 157     -11.895  -6.279 105.170  1.00 64.47           C  
ANISOU 1313  C   PHE A 157     6713  11067   6716    960  -2029   -148       C  
ATOM   1314  O   PHE A 157     -11.048  -6.704 104.363  1.00 54.64           O  
ANISOU 1314  O   PHE A 157     5659   9708   5392    910  -2061   -182       O  
ATOM   1315  CB  PHE A 157     -11.695  -4.037 106.368  1.00 77.51           C  
ANISOU 1315  CB  PHE A 157     8503  12458   8491   1454  -1816    193       C  
ATOM   1316  CG  PHE A 157     -10.362  -4.557 106.838  1.00 84.00           C  
ANISOU 1316  CG  PHE A 157     9542  12957   9416   1301  -1760    209       C  
ATOM   1317  CD1 PHE A 157     -10.284  -5.555 107.800  1.00 88.54           C  
ANISOU 1317  CD1 PHE A 157    10063  13411  10167    950  -1701    109       C  
ATOM   1318  CD2 PHE A 157      -9.187  -4.010 106.351  1.00 87.13           C  
ANISOU 1318  CD2 PHE A 157    10255  13047   9802   1452  -1675    333       C  
ATOM   1319  CE1 PHE A 157      -9.056  -6.024 108.238  1.00 86.71           C  
ANISOU 1319  CE1 PHE A 157    10079  12781  10087    773  -1579    138       C  
ATOM   1320  CE2 PHE A 157      -7.957  -4.471 106.788  1.00 88.99           C  
ANISOU 1320  CE2 PHE A 157    10723  12891  10200   1255  -1551    340       C  
ATOM   1321  CZ  PHE A 157      -7.890  -5.480 107.732  1.00 86.17           C  
ANISOU 1321  CZ  PHE A 157    10297  12434  10007    928  -1512    247       C  
ATOM   1322  N   GLU A 158     -12.488  -7.070 106.068  1.00 70.16           N  
ANISOU 1322  N   GLU A 158     7215  11886   7558    683  -2028   -278       N  
ATOM   1323  CA  GLU A 158     -12.325  -8.518 106.083  1.00 73.38           C  
ANISOU 1323  CA  GLU A 158     7582  12269   8029    275  -2050   -481       C  
ATOM   1324  C   GLU A 158     -12.661  -9.119 104.725  1.00 72.32           C  
ANISOU 1324  C   GLU A 158     7416  12324   7737    185  -2159   -649       C  
ATOM   1325  O   GLU A 158     -11.951 -10.003 104.232  1.00 65.49           O  
ANISOU 1325  O   GLU A 158     6684  11336   6863    -30  -2170   -773       O  
ATOM   1326  CB  GLU A 158     -13.219  -9.077 107.193  1.00 79.35           C  
ANISOU 1326  CB  GLU A 158     8075  13144   8930     25  -2004   -577       C  
ATOM   1327  CG  GLU A 158     -13.419 -10.569 107.234  1.00 92.42           C  
ANISOU 1327  CG  GLU A 158     9653  14780  10682   -421  -1980   -798       C  
ATOM   1328  CD  GLU A 158     -14.144 -10.993 108.498  1.00108.19           C  
ANISOU 1328  CD  GLU A 158    11446  16816  12845   -646  -1882   -838       C  
ATOM   1329  OE1 GLU A 158     -15.071 -10.274 108.929  1.00115.58           O  
ANISOU 1329  OE1 GLU A 158    12195  17955  13766   -475  -1878   -784       O  
ATOM   1330  OE2 GLU A 158     -13.785 -12.039 109.068  1.00111.77           O1-
ANISOU 1330  OE2 GLU A 158    11993  17005  13470   -972  -1753   -891       O1-
ATOM   1331  N   SER A 159     -13.730  -8.620 104.095  1.00 82.70           N  
ANISOU 1331  N   SER A 159     8565  13931   8924    353  -2226   -656       N  
ATOM   1332  CA  SER A 159     -14.136  -9.088 102.777  1.00 90.84           C  
ANISOU 1332  CA  SER A 159     9552  15181   9783    295  -2330   -806       C  
ATOM   1333  C   SER A 159     -13.093  -8.752 101.719  1.00 91.62           C  
ANISOU 1333  C   SER A 159     9936  15146   9730    469  -2355   -722       C  
ATOM   1334  O   SER A 159     -12.851  -9.552 100.816  1.00 91.53           O  
ANISOU 1334  O   SER A 159     9985  15172   9622    295  -2407   -885       O  
ATOM   1335  CB  SER A 159     -15.485  -8.476 102.399  1.00 92.53           C  
ANISOU 1335  CB  SER A 159     9519  15757   9883    484  -2398   -800       C  
ATOM   1336  OG  SER A 159     -16.428  -8.595 103.450  1.00 94.72           O  
ANISOU 1336  OG  SER A 159     9543  16148  10296    376  -2355   -848       O  
ATOM   1337  N   LYS A 160     -12.474  -7.570 101.802  1.00 92.52           N  
ANISOU 1337  N   LYS A 160    10239  15090   9825    805  -2296   -476       N  
ATOM   1338  CA  LYS A 160     -11.480  -7.202 100.790  1.00 92.77           C  
ANISOU 1338  CA  LYS A 160    10555  14976   9715    975  -2288   -382       C  
ATOM   1339  C   LYS A 160     -10.209  -8.039 100.917  1.00 91.54           C  
ANISOU 1339  C   LYS A 160    10618  14538   9626    762  -2251   -459       C  
ATOM   1340  O   LYS A 160      -9.585  -8.390  99.907  1.00 89.57           O  
ANISOU 1340  O   LYS A 160    10538  14253   9242    734  -2275   -525       O  
ATOM   1341  CB  LYS A 160     -11.113  -5.717 100.851  1.00102.65           C  
ANISOU 1341  CB  LYS A 160    11976  16066  10961   1365  -2187   -104       C  
ATOM   1342  CG  LYS A 160     -12.225  -4.689 100.661  1.00117.71           C  
ANISOU 1342  CG  LYS A 160    13720  18207  12797   1636  -2197      0       C  
ATOM   1343  CD  LYS A 160     -12.368  -3.829 101.890  1.00123.90           C  
ANISOU 1343  CD  LYS A 160    14476  18845  13753   1777  -2078    140       C  
ATOM   1344  CE  LYS A 160     -11.252  -2.827 102.029  1.00124.06           C  
ANISOU 1344  CE  LYS A 160    14806  18494  13838   1993  -1917    346       C  
ATOM   1345  NZ  LYS A 160     -11.336  -2.163 103.359  1.00115.22           N  
ANISOU 1345  NZ  LYS A 160    13656  17220  12903   2062  -1795    435       N  
ATOM   1346  N   VAL A 161      -9.792  -8.376 102.137  1.00 92.58           N  
ANISOU 1346  N   VAL A 161    10762  14438   9976    604  -2166   -452       N  
ATOM   1347  CA  VAL A 161      -8.584  -9.201 102.184  1.00 77.58           C  
ANISOU 1347  CA  VAL A 161     9127  12113   8239    369  -2029   -495       C  
ATOM   1348  C   VAL A 161      -8.917 -10.663 101.909  1.00 72.94           C  
ANISOU 1348  C   VAL A 161     8431  11601   7681    -26  -2062   -772       C  
ATOM   1349  O   VAL A 161      -8.081 -11.403 101.385  1.00 71.65           O  
ANISOU 1349  O   VAL A 161     8470  11202   7553   -186  -1995   -860       O  
ATOM   1350  CB  VAL A 161      -7.817  -9.043 103.504  1.00 66.63           C  
ANISOU 1350  CB  VAL A 161     7873  10317   7125    331  -1853   -346       C  
ATOM   1351  CG1 VAL A 161      -7.742  -7.587 103.923  1.00 64.42           C  
ANISOU 1351  CG1 VAL A 161     7639  10008   6828    684  -1813   -116       C  
ATOM   1352  CG2 VAL A 161      -8.424  -9.915 104.552  1.00 76.61           C  
ANISOU 1352  CG2 VAL A 161     8944  11597   8566     29  -1823   -453       C  
ATOM   1353  N   PHE A 162     -10.134 -11.112 102.239  1.00 72.83           N  
ANISOU 1353  N   PHE A 162     8100  11908   7664   -198  -2150   -927       N  
ATOM   1354  CA  PHE A 162     -10.567 -12.426 101.772  1.00 84.96           C  
ANISOU 1354  CA  PHE A 162     9519  13571   9192   -571  -2186  -1225       C  
ATOM   1355  C   PHE A 162     -10.605 -12.451 100.251  1.00110.57           C  
ANISOU 1355  C   PHE A 162    12808  17037  12168   -495  -2302  -1342       C  
ATOM   1356  O   PHE A 162     -10.268 -13.462  99.615  1.00117.77           O  
ANISOU 1356  O   PHE A 162    13808  17867  13072   -757  -2275  -1555       O  
ATOM   1357  CB  PHE A 162     -11.935 -12.756 102.365  1.00 77.26           C  
ANISOU 1357  CB  PHE A 162     8206  12865   8283   -736  -2216  -1338       C  
ATOM   1358  CG  PHE A 162     -12.491 -14.078 101.923  1.00 84.35           C  
ANISOU 1358  CG  PHE A 162     9005  13817   9226  -1111  -2191  -1620       C  
ATOM   1359  CD1 PHE A 162     -11.773 -15.249 102.116  1.00 87.92           C  
ANISOU 1359  CD1 PHE A 162     9610  13948   9848  -1458  -2065  -1763       C  
ATOM   1360  CD2 PHE A 162     -13.734 -14.149 101.322  1.00 91.75           C  
ANISOU 1360  CD2 PHE A 162     9706  15107  10048  -1114  -2273  -1741       C  
ATOM   1361  CE1 PHE A 162     -12.291 -16.467 101.714  1.00 88.53           C  
ANISOU 1361  CE1 PHE A 162     9621  14029   9988  -1788  -2005  -2014       C  
ATOM   1362  CE2 PHE A 162     -14.256 -15.361 100.916  1.00 95.57           C  
ANISOU 1362  CE2 PHE A 162    10099  15641  10572  -1456  -2236  -2008       C  
ATOM   1363  CZ  PHE A 162     -13.534 -16.521 101.112  1.00 91.46           C  
ANISOU 1363  CZ  PHE A 162     9747  14773  10230  -1790  -2095  -2144       C  
ATOM   1364  N   HIS A 163     -11.009 -11.327  99.658  1.00137.74           N  
ANISOU 1364  N   HIS A 163    16224  20689  15423   -131  -2381  -1174       N  
ATOM   1365  CA  HIS A 163     -10.852 -11.110  98.229  1.00142.96           C  
ANISOU 1365  CA  HIS A 163    17000  21482  15836     15  -2449  -1188       C  
ATOM   1366  C   HIS A 163      -9.417 -11.342  97.799  1.00130.81           C  
ANISOU 1366  C   HIS A 163    15787  19655  14260      0  -2386  -1193       C  
ATOM   1367  O   HIS A 163      -9.161 -12.088  96.860  1.00126.32           O  
ANISOU 1367  O   HIS A 163    15305  19106  13585   -169  -2397  -1383       O  
ATOM   1368  CB  HIS A 163     -11.270  -9.688  97.870  1.00158.84           C  
ANISOU 1368  CB  HIS A 163    18994  23657  17703    442  -2489   -936       C  
ATOM   1369  CG  HIS A 163     -12.695  -9.558  97.454  1.00173.61           C  
ANISOU 1369  CG  HIS A 163    20574  25923  19468    485  -2590  -1002       C  
ATOM   1370  ND1 HIS A 163     -13.306  -8.334  97.287  1.00177.01           N  
ANISOU 1370  ND1 HIS A 163    20930  26522  19805    843  -2614   -798       N  
ATOM   1371  CD2 HIS A 163     -13.632 -10.492  97.170  1.00178.65           C  
ANISOU 1371  CD2 HIS A 163    20976  26818  20084    217  -2660  -1256       C  
ATOM   1372  CE1 HIS A 163     -14.559  -8.522  96.916  1.00181.87           C  
ANISOU 1372  CE1 HIS A 163    21264  27508  20329    806  -2713   -923       C  
ATOM   1373  NE2 HIS A 163     -14.783  -9.821  96.838  1.00182.66           N  
ANISOU 1373  NE2 HIS A 163    21259  27675  20470    427  -2744  -1202       N  
ATOM   1374  N   LYS A 164      -8.467 -10.664  98.442  1.00111.11           N  
ANISOU 1374  N   LYS A 164    13499  16839  11880    186  -2281   -968       N  
ATOM   1375  CA  LYS A 164      -7.075 -10.805  98.022  1.00 98.76           C  
ANISOU 1375  CA  LYS A 164    12284  14867  10373    187  -2133   -912       C  
ATOM   1376  C   LYS A 164      -6.581 -12.240  98.171  1.00 93.38           C  
ANISOU 1376  C   LYS A 164    11678  13909   9894   -216  -2021  -1128       C  
ATOM   1377  O   LYS A 164      -5.774 -12.706  97.359  1.00 89.27           O  
ANISOU 1377  O   LYS A 164    11368  13222   9328   -285  -1955  -1214       O  
ATOM   1378  CB  LYS A 164      -6.184  -9.843  98.802  1.00 93.66           C  
ANISOU 1378  CB  LYS A 164    11837  13852   9899    417  -1984   -621       C  
ATOM   1379  CG  LYS A 164      -6.006  -8.509  98.109  1.00 90.50           C  
ANISOU 1379  CG  LYS A 164    11560  13547   9279    826  -2009   -407       C  
ATOM   1380  CD  LYS A 164      -5.378  -7.474  99.028  1.00 91.49           C  
ANISOU 1380  CD  LYS A 164    11819  13355   9586   1034  -1863   -148       C  
ATOM   1381  CE  LYS A 164      -5.797  -6.066  98.629  1.00 94.71           C  
ANISOU 1381  CE  LYS A 164    12231  13963   9793   1449  -1909     61       C  
ATOM   1382  NZ  LYS A 164      -5.504  -5.079  99.700  1.00 88.73           N  
ANISOU 1382  NZ  LYS A 164    11531  12954   9229   1616  -1774    266       N  
ATOM   1383  N   LEU A 165      -7.087 -12.964  99.170  1.00 89.59           N  
ANISOU 1383  N   LEU A 165    11029  13378   9633   -481  -1986  -1219       N  
ATOM   1384  CA  LEU A 165      -6.603 -14.310  99.458  1.00 83.70           C  
ANISOU 1384  CA  LEU A 165    10373  12311   9118   -844  -1844  -1384       C  
ATOM   1385  C   LEU A 165      -7.232 -15.383  98.573  1.00 88.31           C  
ANISOU 1385  C   LEU A 165    10841  13132   9582  -1143  -1911  -1729       C  
ATOM   1386  O   LEU A 165      -6.628 -16.449  98.401  1.00 81.28           O  
ANISOU 1386  O   LEU A 165    10102  11949   8834  -1401  -1775  -1881       O  
ATOM   1387  CB  LEU A 165      -6.837 -14.644 100.934  1.00 74.61           C  
ANISOU 1387  CB  LEU A 165     9119  10979   8251  -1000  -1750  -1314       C  
ATOM   1388  CG  LEU A 165      -6.173 -13.675 101.919  1.00 70.46           C  
ANISOU 1388  CG  LEU A 165     8706  10208   7856   -751  -1670  -1006       C  
ATOM   1389  CD1 LEU A 165      -6.601 -13.948 103.353  1.00 72.23           C  
ANISOU 1389  CD1 LEU A 165     8793  10351   8300   -895  -1602   -949       C  
ATOM   1390  CD2 LEU A 165      -4.653 -13.678 101.782  1.00 48.26           C  
ANISOU 1390  CD2 LEU A 165     6214   6968   5154   -678  -1525   -889       C  
ATOM   1391  N   LYS A 166      -8.424 -15.144  98.018  1.00104.07           N  
ANISOU 1391  N   LYS A 166    12564  15651  11326  -1118  -2109  -1866       N  
ATOM   1392  CA  LYS A 166      -8.970 -16.077  97.037  1.00117.90           C  
ANISOU 1392  CA  LYS A 166    14234  17599  12965  -1364  -2150  -2168       C  
ATOM   1393  C   LYS A 166      -8.799 -15.610  95.592  1.00133.58           C  
ANISOU 1393  C   LYS A 166    16327  19795  14631  -1146  -2247  -2172       C  
ATOM   1394  O   LYS A 166      -8.854 -16.447  94.683  1.00145.83           O  
ANISOU 1394  O   LYS A 166    17915  21378  16114  -1342  -2227  -2402       O  
ATOM   1395  CB  LYS A 166     -10.455 -16.357  97.309  1.00128.77           C  
ANISOU 1395  CB  LYS A 166    15278  19267  14382  -1483  -2208  -2257       C  
ATOM   1396  CG  LYS A 166     -10.951 -17.631  96.631  1.00139.76           C  
ANISOU 1396  CG  LYS A 166    16606  20701  15796  -1819  -2158  -2565       C  
ATOM   1397  CD  LYS A 166     -12.459 -17.778  96.690  1.00144.08           C  
ANISOU 1397  CD  LYS A 166    16813  21613  16318  -1897  -2233  -2665       C  
ATOM   1398  CE  LYS A 166     -12.949 -18.721  95.601  1.00143.93           C  
ANISOU 1398  CE  LYS A 166    16733  21759  16196  -2126  -2237  -2960       C  
ATOM   1399  NZ  LYS A 166     -14.298 -19.268  95.908  1.00147.45           N  
ANISOU 1399  NZ  LYS A 166    16866  22445  16712  -2335  -2235  -3119       N  
ATOM   1400  N   LYS A 167      -8.612 -14.300  95.358  1.00135.14           N  
ANISOU 1400  N   LYS A 167    16585  20121  14641   -743  -2332  -1912       N  
ATOM   1401  CA  LYS A 167      -8.219 -13.748  94.065  1.00133.30           C  
ANISOU 1401  CA  LYS A 167    16522  20010  14118   -505  -2382  -1851       C  
ATOM   1402  C   LYS A 167      -6.752 -13.988  93.788  1.00125.07           C  
ANISOU 1402  C   LYS A 167    15813  18631  13076   -529  -2258  -1880       C  
ATOM   1403  O   LYS A 167      -6.334 -13.950  92.628  1.00116.09           O  
ANISOU 1403  O   LYS A 167    14842  17545  11721   -453  -2256  -1920       O  
ATOM   1404  CB  LYS A 167      -8.464 -12.235  94.003  1.00136.29           C  
ANISOU 1404  CB  LYS A 167    16884  20549  14351    -58  -2454  -1521       C  
ATOM   1405  CG  LYS A 167      -9.907 -11.815  93.893  1.00140.12           C  
ANISOU 1405  CG  LYS A 167    17062  21416  14761     43  -2577  -1488       C  
ATOM   1406  CD  LYS A 167     -10.059 -10.706  92.888  1.00139.30           C  
ANISOU 1406  CD  LYS A 167    17015  21517  14397    413  -2638  -1284       C  
ATOM   1407  CE  LYS A 167     -10.670 -11.221  91.612  1.00134.11           C  
ANISOU 1407  CE  LYS A 167    16265  21186  13505    315  -2743  -1483       C  
ATOM   1408  NZ  LYS A 167     -11.185 -10.059  90.849  1.00126.85           N  
ANISOU 1408  NZ  LYS A 167    15305  20534  12360    689  -2820  -1266       N  
ATOM   1409  N   MET A 168      -5.963 -14.160  94.836  1.00121.41           N  
ANISOU 1409  N   MET A 168    15487  17681  12962   -595  -2072  -1749       N  
ATOM   1410  CA  MET A 168      -4.682 -14.821  94.735  1.00107.66           C  
ANISOU 1410  CA  MET A 168    14037  15459  11409   -728  -1864  -1779       C  
ATOM   1411  C   MET A 168      -4.952 -16.309  94.913  1.00104.00           C  
ANISOU 1411  C   MET A 168    13496  14895  11123  -1164  -1794  -2090       C  
ATOM   1412  O   MET A 168      -6.098 -16.765  94.858  1.00107.81           O  
ANISOU 1412  O   MET A 168    13716  15725  11523  -1361  -1919  -2310       O  
ATOM   1413  CB  MET A 168      -3.713 -14.256  95.770  1.00100.38           C  
ANISOU 1413  CB  MET A 168    13280  14095  10766   -569  -1706  -1477       C  
ATOM   1414  CG  MET A 168      -2.262 -14.230  95.318  1.00108.91           C  
ANISOU 1414  CG  MET A 168    14682  14792  11907   -489  -1531  -1396       C  
ATOM   1415  SD  MET A 168      -1.399 -12.752  95.893  1.00116.00           S  
ANISOU 1415  SD  MET A 168    15735  15460  12881   -113  -1448  -1009       S  
ATOM   1416  CE  MET A 168       0.203 -12.960  95.104  1.00120.06           C  
ANISOU 1416  CE  MET A 168    16587  15597  13434    -89  -1246  -1003       C  
ATOM   1417  N   LYS A 169      -3.906 -17.084  95.155  1.00 89.76           N  
ANISOU 1417  N   LYS A 169    11915  12610   9581  -1320  -1581  -2112       N  
ATOM   1418  CA  LYS A 169      -4.058 -18.512  95.373  1.00 92.29           C  
ANISOU 1418  CA  LYS A 169    12206  12749  10110  -1721  -1467  -2382       C  
ATOM   1419  C   LYS A 169      -3.589 -18.914  96.766  1.00 83.33           C  
ANISOU 1419  C   LYS A 169    11120  11173   9369  -1807  -1296  -2215       C  
ATOM   1420  O   LYS A 169      -3.272 -20.084  97.003  1.00 81.27           O  
ANISOU 1420  O   LYS A 169    10941  10593   9343  -2082  -1126  -2356       O  
ATOM   1421  CB  LYS A 169      -3.302 -19.277  94.292  1.00107.35           C  
ANISOU 1421  CB  LYS A 169    14335  14491  11964  -1853  -1348  -2601       C  
ATOM   1422  CG  LYS A 169      -3.693 -18.844  92.884  1.00111.08           C  
ANISOU 1422  CG  LYS A 169    14780  15420  12005  -1749  -1517  -2751       C  
ATOM   1423  CD  LYS A 169      -2.488 -18.781  91.957  1.00112.18           C  
ANISOU 1423  CD  LYS A 169    15226  15340  12057  -1628  -1391  -2736       C  
ATOM   1424  CE  LYS A 169      -2.575 -17.605  90.999  1.00119.28           C  
ANISOU 1424  CE  LYS A 169    16155  16614  12552  -1293  -1550  -2609       C  
ATOM   1425  NZ  LYS A 169      -1.975 -17.937  89.677  1.00124.60           N  
ANISOU 1425  NZ  LYS A 169    17034  17307  13000  -1324  -1484  -2796       N  
ATOM   1426  N   TYR A 170      -3.540 -17.955  97.694  1.00 77.22           N  
ANISOU 1426  N   TYR A 170    10302  10377   8664  -1569  -1332  -1915       N  
ATOM   1427  CA  TYR A 170      -3.056 -18.198  99.046  1.00 64.78           C  
ANISOU 1427  CA  TYR A 170     8771   8425   7417  -1610  -1189  -1728       C  
ATOM   1428  C   TYR A 170      -4.050 -18.975  99.895  1.00 74.29           C  
ANISOU 1428  C   TYR A 170     9765   9687   8772  -1895  -1178  -1840       C  
ATOM   1429  O   TYR A 170      -3.684 -19.436 100.982  1.00 68.88           O  
ANISOU 1429  O   TYR A 170     9131   8679   8360  -1982  -1037  -1715       O  
ATOM   1430  CB  TYR A 170      -2.742 -16.867  99.732  1.00 61.00           C  
ANISOU 1430  CB  TYR A 170     8302   7944   6933  -1277  -1233  -1405       C  
ATOM   1431  CG  TYR A 170      -1.511 -16.174  99.199  1.00 69.85           C  
ANISOU 1431  CG  TYR A 170     9665   8870   8005  -1024  -1170  -1251       C  
ATOM   1432  CD1 TYR A 170      -0.672 -16.807  98.294  1.00 88.21           C  
ANISOU 1432  CD1 TYR A 170    12189  10999  10328  -1096  -1064  -1380       C  
ATOM   1433  CD2 TYR A 170      -1.193 -14.882  99.592  1.00 71.92           C  
ANISOU 1433  CD2 TYR A 170     9956   9139   8230   -723  -1197   -993       C  
ATOM   1434  CE1 TYR A 170       0.456 -16.178  97.801  1.00 93.40           C  
ANISOU 1434  CE1 TYR A 170    13058  11484  10946   -876   -988  -1246       C  
ATOM   1435  CE2 TYR A 170      -0.069 -14.243  99.104  1.00 83.04           C  
ANISOU 1435  CE2 TYR A 170    11582  10364   9606   -514  -1117   -864       C  
ATOM   1436  CZ  TYR A 170       0.752 -14.897  98.208  1.00 93.71           C  
ANISOU 1436  CZ  TYR A 170    13117  11534  10953   -592  -1015   -988       C  
ATOM   1437  OH  TYR A 170       1.874 -14.273  97.715  1.00 90.80           O  
ANISOU 1437  OH  TYR A 170    12956  10987  10558   -397   -918   -867       O  
ATOM   1438  N   LEU A 171      -5.293 -19.124  99.442  1.00 82.03           N  
ANISOU 1438  N   LEU A 171    10507  11086   9576  -2040  -1319  -2066       N  
ATOM   1439  CA  LEU A 171      -6.327 -19.736 100.268  1.00 80.44           C  
ANISOU 1439  CA  LEU A 171    10075  10981   9508  -2307  -1306  -2170       C  
ATOM   1440  C   LEU A 171      -7.279 -20.487  99.348  1.00 86.26           C  
ANISOU 1440  C   LEU A 171    10646  12022  10108  -2564  -1370  -2521       C  
ATOM   1441  O   LEU A 171      -8.046 -19.863  98.610  1.00 82.00           O  
ANISOU 1441  O   LEU A 171     9931  11933   9293  -2421  -1564  -2578       O  
ATOM   1442  CB  LEU A 171      -7.061 -18.671 101.080  1.00 76.97           C  
ANISOU 1442  CB  LEU A 171     9421  10814   9010  -2101  -1436  -1968       C  
ATOM   1443  CG  LEU A 171      -7.732 -19.251 102.317  1.00 81.92           C  
ANISOU 1443  CG  LEU A 171     9889  11377   9861  -2336  -1347  -1965       C  
ATOM   1444  CD1 LEU A 171      -6.756 -20.201 102.999  1.00 88.95           C  
ANISOU 1444  CD1 LEU A 171    11020  11720  11057  -2493  -1106  -1885       C  
ATOM   1445  CD2 LEU A 171      -8.190 -18.168 103.279  1.00 80.32           C  
ANISOU 1445  CD2 LEU A 171     9532  11345   9641  -2103  -1426  -1725       C  
ATOM   1446  N   VAL A 172      -7.249 -21.817  99.396  1.00 89.00           N  
ANISOU 1446  N   VAL A 172    11060  12075  10679  -2827  -1176  -2650       N  
ATOM   1447  CA  VAL A 172      -7.979 -22.656  98.446  1.00 91.86           C  
ANISOU 1447  CA  VAL A 172    11327  12615  10960  -3003  -1173  -2918       C  
ATOM   1448  C   VAL A 172      -8.997 -23.500  99.203  1.00102.10           C  
ANISOU 1448  C   VAL A 172    12436  13911  12447  -3249  -1073  -2984       C  
ATOM   1449  O   VAL A 172      -8.629 -24.266 100.099  1.00104.76           O  
ANISOU 1449  O   VAL A 172    12885  13847  13072  -3378   -867  -2894       O  
ATOM   1450  CB  VAL A 172      -7.031 -23.560  97.643  1.00 79.03           C  
ANISOU 1450  CB  VAL A 172     9964  10655   9407  -3095  -1007  -3044       C  
ATOM   1451  CG1 VAL A 172      -7.731 -24.086  96.405  1.00 71.66           C  
ANISOU 1451  CG1 VAL A 172     8930  10014   8282  -3223  -1063  -3330       C  
ATOM   1452  CG2 VAL A 172      -5.755 -22.807  97.275  1.00 75.72           C  
ANISOU 1452  CG2 VAL A 172     9793  10080   8899  -2863  -1025  -2917       C  
ATOM   1453  N   GLU A 173     -10.270 -23.389  98.829  1.00111.85           N  
ANISOU 1453  N   GLU A 173    13392  15589  13517  -3299  -1207  -3129       N  
ATOM   1454  CA  GLU A 173     -11.288 -24.203  99.484  1.00119.79           C  
ANISOU 1454  CA  GLU A 173    14215  16613  14686  -3548  -1099  -3219       C  
ATOM   1455  C   GLU A 173     -11.021 -25.680  99.218  1.00115.26           C  
ANISOU 1455  C   GLU A 173    13797  15697  14301  -3824   -863  -3394       C  
ATOM   1456  O   GLU A 173     -10.811 -26.092  98.074  1.00125.47           O  
ANISOU 1456  O   GLU A 173    15166  17029  15477  -3878   -864  -3591       O  
ATOM   1457  CB  GLU A 173     -12.688 -23.811  99.005  1.00138.67           C  
ANISOU 1457  CB  GLU A 173    16273  19560  16853  -3542  -1283  -3361       C  
ATOM   1458  CG  GLU A 173     -12.909 -23.918  97.505  1.00153.27           C  
ANISOU 1458  CG  GLU A 173    18088  21701  18445  -3546  -1395  -3592       C  
ATOM   1459  CD  GLU A 173     -14.338 -23.609  97.108  1.00161.94           C  
ANISOU 1459  CD  GLU A 173    18841  23343  19346  -3543  -1560  -3721       C  
ATOM   1460  OE1 GLU A 173     -15.201 -23.509  98.005  1.00162.05           O  
ANISOU 1460  OE1 GLU A 173    18644  23473  19457  -3590  -1551  -3670       O  
ATOM   1461  OE2 GLU A 173     -14.598 -23.474  95.895  1.00165.18           O1-
ANISOU 1461  OE2 GLU A 173    19191  24070  19501  -3491  -1693  -3871       O1-
ATOM   1462  N   VAL A 174     -11.000 -26.477 100.284  1.00102.50           N  
ANISOU 1462  N   VAL A 174    12239  13737  12969  -3980   -651  -3307       N  
ATOM   1463  CA  VAL A 174     -10.688 -27.894 100.144  1.00121.40           C  
ANISOU 1463  CA  VAL A 174    14802  15762  15562  -4203   -402  -3429       C  
ATOM   1464  C   VAL A 174     -11.966 -28.719 100.245  1.00145.49           C  
ANISOU 1464  C   VAL A 174    17643  18980  18656  -4487   -322  -3641       C  
ATOM   1465  O   VAL A 174     -12.105 -29.739  99.560  1.00146.37           O  
ANISOU 1465  O   VAL A 174    17798  19020  18796  -4696   -195  -3878       O  
ATOM   1466  CB  VAL A 174      -9.633 -28.340 101.180  1.00114.24           C  
ANISOU 1466  CB  VAL A 174    14150  14312  14942  -4148   -195  -3162       C  
ATOM   1467  CG1 VAL A 174     -10.164 -28.214 102.605  1.00108.25           C  
ANISOU 1467  CG1 VAL A 174    13283  13520  14329  -4171   -149  -2966       C  
ATOM   1468  CG2 VAL A 174      -9.172 -29.765 100.898  1.00118.84           C  
ANISOU 1468  CG2 VAL A 174    14931  14512  15711  -4313     57  -3265       C  
ATOM   1469  N   GLN A 175     -12.913 -28.261 101.062  1.00157.35           N  
ANISOU 1469  N   GLN A 175    18912  20719  20154  -4497   -391  -3571       N  
ATOM   1470  CA  GLN A 175     -14.163 -28.969 101.352  1.00179.07           C  
ANISOU 1470  CA  GLN A 175    21449  23624  22963  -4761   -302  -3746       C  
ATOM   1471  C   GLN A 175     -13.937 -30.473 101.490  1.00202.73           C  
ANISOU 1471  C   GLN A 175    24629  26201  26199  -5018     -5  -3844       C  
ATOM   1472  O   GLN A 175     -14.488 -31.292 100.754  1.00208.13           O  
ANISOU 1472  O   GLN A 175    25248  26979  26854  -5251     70  -4137       O  
ATOM   1473  CB  GLN A 175     -15.233 -28.681 100.298  1.00176.07           C  
ANISOU 1473  CB  GLN A 175    20787  23793  22318  -4817   -490  -4023       C  
ATOM   1474  CG  GLN A 175     -16.661 -28.538 100.860  1.00172.07           C  
ANISOU 1474  CG  GLN A 175    19949  23640  21791  -4925   -532  -4090       C  
ATOM   1475  CD  GLN A 175     -17.054 -29.645 101.828  1.00167.16           C  
ANISOU 1475  CD  GLN A 175    19353  22721  21439  -5201   -259  -4109       C  
ATOM   1476  OE1 GLN A 175     -17.216 -30.801 101.438  1.00174.56           O  
ANISOU 1476  OE1 GLN A 175    20347  23513  22465  -5466    -80  -4333       O  
ATOM   1477  NE2 GLN A 175     -17.220 -29.289 103.098  1.00155.21           N  
ANISOU 1477  NE2 GLN A 175    17801  21122  20049  -5139   -219  -3874       N  
ATOM   1478  N   ASP A 176     -13.086 -30.822 102.447  1.00225.68           N  
ANISOU 1478  N   ASP A 176    27769  28642  29338  -4958    168  -3587       N  
ATOM   1479  CA  ASP A 176     -12.967 -32.195 102.906  1.00239.31           C  
ANISOU 1479  CA  ASP A 176    29655  29959  31314  -5160    463  -3601       C  
ATOM   1480  C   ASP A 176     -13.739 -32.415 104.197  1.00239.18           C  
ANISOU 1480  C   ASP A 176    29528  29908  31440  -5270    572  -3480       C  
ATOM   1481  O   ASP A 176     -13.604 -33.478 104.813  1.00246.77           O  
ANISOU 1481  O   ASP A 176    30639  30504  32619  -5401    823  -3422       O  
ATOM   1482  CB  ASP A 176     -11.493 -32.568 103.096  1.00247.77           C  
ANISOU 1482  CB  ASP A 176    31064  30531  32547  -4998    598  -3379       C  
ATOM   1483  CG  ASP A 176     -11.262 -34.073 103.107  1.00259.86           C  
ANISOU 1483  CG  ASP A 176    32779  31668  34290  -5185    893  -3459       C  
ATOM   1484  OD1 ASP A 176     -12.089 -34.809 102.527  1.00265.70           O  
ANISOU 1484  OD1 ASP A 176    33412  32533  35007  -5455    978  -3767       O  
ATOM   1485  OD2 ASP A 176     -10.258 -34.521 103.701  1.00260.19           O1-
ANISOU 1485  OD2 ASP A 176    33062  31283  34514  -5056   1042  -3213       O1-
ATOM   1486  N   GLU A 177     -14.557 -31.430 104.603  1.00210.91           N  
ANISOU 1486  N   GLU A 177    25690  26712  27734  -5209    392  -3440       N  
ATOM   1487  CA  GLU A 177     -15.130 -31.291 105.943  1.00183.38           C  
ANISOU 1487  CA  GLU A 177    22103  23217  24357  -5233    456  -3256       C  
ATOM   1488  C   GLU A 177     -14.084 -31.807 106.917  1.00167.01           C  
ANISOU 1488  C   GLU A 177    20311  20643  22501  -5129    633  -2929       C  
ATOM   1489  O   GLU A 177     -14.396 -32.536 107.864  1.00161.99           O  
ANISOU 1489  O   GLU A 177    19689  19839  22020  -5229    802  -2803       O  
ATOM   1490  CB  GLU A 177     -16.416 -32.113 106.086  1.00171.73           C  
ANISOU 1490  CB  GLU A 177    20439  21876  22933  -5546    591  -3486       C  
ATOM   1491  CG  GLU A 177     -16.186 -33.611 106.135  1.00166.05           C  
ANISOU 1491  CG  GLU A 177    19928  20738  22424  -5773    890  -3567       C  
ATOM   1492  CD  GLU A 177     -17.241 -34.401 105.433  1.00165.04           C  
ANISOU 1492  CD  GLU A 177    19632  20812  22265  -6090    972  -3947       C  
ATOM   1493  OE1 GLU A 177     -16.875 -35.432 104.816  1.00164.55           O  
ANISOU 1493  OE1 GLU A 177    19739  20497  22287  -6238   1144  -4111       O  
ATOM   1494  OE2 GLU A 177     -18.429 -34.016 105.529  1.00165.48           O1-
ANISOU 1494  OE2 GLU A 177    19383  21273  22220  -6191    878  -4082       O1-
ATOM   1495  N   VAL A 178     -12.844 -31.415 106.683  1.00160.08           N  
ANISOU 1495  N   VAL A 178    19653  19545  21623  -4916    591  -2786       N  
ATOM   1496  CA  VAL A 178     -11.718 -31.909 107.456  1.00150.46           C  
ANISOU 1496  CA  VAL A 178    18718  17849  20600  -4792    755  -2494       C  
ATOM   1497  C   VAL A 178     -11.589 -31.086 108.726  1.00145.18           C  
ANISOU 1497  C   VAL A 178    18019  17187  19955  -4622    701  -2177       C  
ATOM   1498  O   VAL A 178     -11.863 -29.881 108.729  1.00141.39           O  
ANISOU 1498  O   VAL A 178    17370  17032  19321  -4504    497  -2158       O  
ATOM   1499  CB  VAL A 178     -10.440 -31.845 106.601  1.00142.29           C  
ANISOU 1499  CB  VAL A 178    17900  16624  19542  -4612    715  -2472       C  
ATOM   1500  CG1 VAL A 178     -10.319 -30.473 105.949  1.00137.69           C  
ANISOU 1500  CG1 VAL A 178    17205  16378  18733  -4436    445  -2508       C  
ATOM   1501  CG2 VAL A 178      -9.205 -32.170 107.424  1.00141.34           C  
ANISOU 1501  CG2 VAL A 178    18039  16066  19596  -4418    841  -2136       C  
ATOM   1502  N   LYS A 179     -11.205 -31.747 109.821  1.00137.92           N  
ANISOU 1502  N   LYS A 179    17256  15927  19219  -4607    887  -1928       N  
ATOM   1503  CA  LYS A 179     -10.815 -31.078 111.053  1.00130.97           C  
ANISOU 1503  CA  LYS A 179    16402  14991  18368  -4421    860  -1592       C  
ATOM   1504  C   LYS A 179      -9.881 -29.920 110.722  1.00118.45           C  
ANISOU 1504  C   LYS A 179    14863  13474  16671  -4151    666  -1481       C  
ATOM   1505  O   LYS A 179      -8.748 -30.147 110.281  1.00108.94           O  
ANISOU 1505  O   LYS A 179    13864  12020  15508  -4008    683  -1410       O  
ATOM   1506  CB  LYS A 179     -10.118 -32.049 112.004  1.00131.96           C  
ANISOU 1506  CB  LYS A 179    16759  14694  18685  -4376   1071  -1321       C  
ATOM   1507  CG  LYS A 179     -10.932 -33.276 112.378  1.00133.08           C  
ANISOU 1507  CG  LYS A 179    16900  14709  18957  -4639   1298  -1409       C  
ATOM   1508  CD  LYS A 179     -11.941 -32.974 113.473  1.00128.16           C  
ANISOU 1508  CD  LYS A 179    16100  14269  18327  -4739   1327  -1325       C  
ATOM   1509  CE  LYS A 179     -11.843 -33.995 114.604  1.00122.26           C  
ANISOU 1509  CE  LYS A 179    15509  13198  17744  -4791   1566  -1096       C  
ATOM   1510  NZ  LYS A 179     -10.487 -34.059 115.225  1.00114.80           N  
ANISOU 1510  NZ  LYS A 179    14803  11958  16856  -4520   1581   -743       N  
ATOM   1511  N   PRO A 180     -10.309 -28.673 110.889  1.00111.08           N  
ANISOU 1511  N   PRO A 180    13740  12875  15592  -4073    487  -1471       N  
ATOM   1512  CA  PRO A 180      -9.405 -27.554 110.631  1.00105.20           C  
ANISOU 1512  CA  PRO A 180    13052  12175  14744  -3824    322  -1361       C  
ATOM   1513  C   PRO A 180      -8.561 -27.231 111.851  1.00100.12           C  
ANISOU 1513  C   PRO A 180    12538  11316  14185  -3635    372  -1008       C  
ATOM   1514  O   PRO A 180      -8.927 -27.513 112.993  1.00107.07           O  
ANISOU 1514  O   PRO A 180    13392  12142  15147  -3685    481   -848       O  
ATOM   1515  CB  PRO A 180     -10.375 -26.412 110.300  1.00 97.21           C  
ANISOU 1515  CB  PRO A 180    11757  11650  13529  -3833    116  -1519       C  
ATOM   1516  CG  PRO A 180     -11.544 -26.688 111.192  1.00 93.50           C  
ANISOU 1516  CG  PRO A 180    11102  11319  13105  -3997    200  -1522       C  
ATOM   1517  CD  PRO A 180     -11.648 -28.205 111.302  1.00102.43           C  
ANISOU 1517  CD  PRO A 180    12360  12144  14413  -4198    430  -1567       C  
ATOM   1518  N   ARG A 181      -7.398 -26.639 111.584  1.00 94.06           N  
ANISOU 1518  N   ARG A 181    11914  10436  13389  -3412    294   -888       N  
ATOM   1519  CA  ARG A 181      -6.503 -26.266 112.670  1.00 88.25           C  
ANISOU 1519  CA  ARG A 181    11293   9525  12713  -3207    322   -559       C  
ATOM   1520  C   ARG A 181      -7.148 -25.253 113.605  1.00 76.06           C  
ANISOU 1520  C   ARG A 181     9577   8244  11077  -3199    257   -468       C  
ATOM   1521  O   ARG A 181      -6.966 -25.324 114.826  1.00 74.88           O  
ANISOU 1521  O   ARG A 181     9467   7993  10993  -3141    346   -224       O  
ATOM   1522  CB  ARG A 181      -5.205 -25.706 112.099  1.00 80.36           C  
ANISOU 1522  CB  ARG A 181    10447   8405  11682  -2972    239   -486       C  
ATOM   1523  CG  ARG A 181      -4.002 -25.958 112.958  1.00 73.53           C  
ANISOU 1523  CG  ARG A 181     9750   7259  10930  -2755    309   -170       C  
ATOM   1524  CD  ARG A 181      -2.746 -25.774 112.147  1.00 77.73           C  
ANISOU 1524  CD  ARG A 181    10426   7651  11459  -2553    255   -154       C  
ATOM   1525  NE  ARG A 181      -2.487 -26.900 111.260  1.00 87.15           N  
ANISOU 1525  NE  ARG A 181    11727   8666  12722  -2620    333   -288       N  
ATOM   1526  CZ  ARG A 181      -1.413 -27.000 110.486  1.00 89.94           C  
ANISOU 1526  CZ  ARG A 181    12210   8882  13083  -2467    316   -294       C  
ATOM   1527  NH1 ARG A 181      -0.503 -26.034 110.488  1.00 72.56           N  
ANISOU 1527  NH1 ARG A 181    10038   6702  10832  -2237    219   -171       N  
ATOM   1528  NH2 ARG A 181      -1.250 -28.060 109.707  1.00 96.80           N  
ANISOU 1528  NH2 ARG A 181    13172   9597  14011  -2547    410   -432       N  
ATOM   1529  N   GLY A 182      -7.904 -24.314 113.055  1.00 69.61           N  
ANISOU 1529  N   GLY A 182     8562   7795  10092  -3246     96   -656       N  
ATOM   1530  CA  GLY A 182      -8.543 -23.301 113.864  1.00 71.43           C  
ANISOU 1530  CA  GLY A 182     8607   8319  10214  -3225     18   -582       C  
ATOM   1531  C   GLY A 182      -9.252 -22.302 112.975  1.00 89.67           C  
ANISOU 1531  C   GLY A 182    10691  11057  12322  -3216   -200   -798       C  
ATOM   1532  O   GLY A 182      -9.451 -22.535 111.781  1.00 81.76           O  
ANISOU 1532  O   GLY A 182     9657  10145  11263  -3265   -273  -1028       O  
ATOM   1533  N   VAL A 183      -9.609 -21.176 113.579  1.00110.25           N  
ANISOU 1533  N   VAL A 183    13142  13941  14807  -3100   -309   -702       N  
ATOM   1534  CA  VAL A 183     -10.387 -20.146 112.900  1.00111.49           C  
ANISOU 1534  CA  VAL A 183    13056  14539  14764  -2956   -522   -842       C  
ATOM   1535  C   VAL A 183      -9.439 -19.079 112.371  1.00103.79           C  
ANISOU 1535  C   VAL A 183    12220  13548  13665  -2589   -667   -721       C  
ATOM   1536  O   VAL A 183      -8.529 -18.631 113.083  1.00107.94           O  
ANISOU 1536  O   VAL A 183    12913  13874  14225  -2395   -631   -482       O  
ATOM   1537  CB  VAL A 183     -11.455 -19.544 113.832  1.00115.44           C  
ANISOU 1537  CB  VAL A 183    13296  15352  15213  -2946   -536   -801       C  
ATOM   1538  CG1 VAL A 183     -10.857 -19.184 115.178  1.00117.79           C  
ANISOU 1538  CG1 VAL A 183    13727  15467  15563  -2805   -440   -506       C  
ATOM   1539  CG2 VAL A 183     -12.115 -18.333 113.186  1.00111.07           C  
ANISOU 1539  CG2 VAL A 183    12515  15232  14456  -2709   -756   -889       C  
ATOM   1540  N   LEU A 184      -9.635 -18.691 111.111  1.00 88.72           N  
ANISOU 1540  N   LEU A 184    10244  11857  11608  -2502   -825   -892       N  
ATOM   1541  CA  LEU A 184      -8.844 -17.624 110.515  1.00 76.94           C  
ANISOU 1541  CA  LEU A 184     8875  10373   9984  -2158   -950   -787       C  
ATOM   1542  C   LEU A 184      -9.385 -16.267 110.937  1.00 77.79           C  
ANISOU 1542  C   LEU A 184     8816  10780   9960  -1892  -1062   -680       C  
ATOM   1543  O   LEU A 184     -10.590 -16.009 110.841  1.00 80.39           O  
ANISOU 1543  O   LEU A 184     8870  11476  10197  -1925  -1146   -802       O  
ATOM   1544  CB  LEU A 184      -8.846 -17.721 108.991  1.00 75.95           C  
ANISOU 1544  CB  LEU A 184     8758  10373   9726  -2154  -1064   -993       C  
ATOM   1545  CG  LEU A 184      -8.003 -16.646 108.296  1.00 81.70           C  
ANISOU 1545  CG  LEU A 184     9637  11092  10314  -1804  -1169   -878       C  
ATOM   1546  CD1 LEU A 184      -6.893 -17.283 107.482  1.00 77.40           C  
ANISOU 1546  CD1 LEU A 184     9353  10239   9818  -1845  -1105   -923       C  
ATOM   1547  CD2 LEU A 184      -8.862 -15.746 107.422  1.00 94.42           C  
ANISOU 1547  CD2 LEU A 184    11048  13146  11681  -1626  -1363   -975       C  
ATOM   1548  N   ASN A 185      -8.491 -15.399 111.396  1.00 74.29           N  
ANISOU 1548  N   ASN A 185     8532  10181   9513  -1630  -1054   -463       N  
ATOM   1549  CA  ASN A 185      -8.832 -14.028 111.735  1.00 61.69           C  
ANISOU 1549  CA  ASN A 185     6829   8806   7804  -1349  -1134   -359       C  
ATOM   1550  C   ASN A 185      -8.023 -13.076 110.869  1.00 58.94           C  
ANISOU 1550  C   ASN A 185     6640   8410   7345  -1050  -1215   -291       C  
ATOM   1551  O   ASN A 185      -6.834 -13.304 110.614  1.00 67.07           O  
ANISOU 1551  O   ASN A 185     7911   9139   8436  -1026  -1162   -227       O  
ATOM   1552  CB  ASN A 185      -8.568 -13.727 113.214  1.00 59.37           C  
ANISOU 1552  CB  ASN A 185     6571   8384   7603  -1318  -1025   -172       C  
ATOM   1553  CG  ASN A 185      -9.606 -14.335 114.129  1.00 76.10           C  
ANISOU 1553  CG  ASN A 185     8491  10637   9786  -1555   -947   -219       C  
ATOM   1554  OD1 ASN A 185      -9.324 -15.273 114.873  1.00 92.05           O  
ANISOU 1554  OD1 ASN A 185    10598  12438  11940  -1766   -811   -163       O  
ATOM   1555  ND2 ASN A 185     -10.814 -13.797 114.086  1.00 67.71           N  
ANISOU 1555  ND2 ASN A 185     7158   9939   8631  -1512  -1021   -312       N  
ATOM   1556  N   ILE A 186      -8.676 -12.018 110.405  1.00 56.97           N  
ANISOU 1556  N   ILE A 186     6253   8457   6935   -816  -1332   -300       N  
ATOM   1557  CA  ILE A 186      -8.001 -10.909 109.748  1.00 53.12           C  
ANISOU 1557  CA  ILE A 186     5916   7927   6341   -498  -1380   -197       C  
ATOM   1558  C   ILE A 186      -7.881  -9.778 110.752  1.00 67.03           C  
ANISOU 1558  C   ILE A 186     7685   9655   8129   -288  -1323    -29       C  
ATOM   1559  O   ILE A 186      -8.864  -9.416 111.410  1.00 87.45           O  
ANISOU 1559  O   ILE A 186    10060  12466  10700   -266  -1331    -34       O  
ATOM   1560  CB  ILE A 186      -8.752 -10.446 108.491  1.00 64.00           C  
ANISOU 1560  CB  ILE A 186     7165   9644   7509   -341  -1535   -295       C  
ATOM   1561  CG1 ILE A 186      -9.051 -11.640 107.582  1.00 56.23           C  
ANISOU 1561  CG1 ILE A 186     6127   8752   6486   -601  -1593   -513       C  
ATOM   1562  CG2 ILE A 186      -7.949  -9.361 107.800  1.00 62.92           C  
ANISOU 1562  CG2 ILE A 186     7229   9408   7269    -19  -1548   -164       C  
ATOM   1563  CD1 ILE A 186      -7.820 -12.355 107.087  1.00 54.95           C  
ANISOU 1563  CD1 ILE A 186     6243   8237   6398   -708  -1515   -526       C  
ATOM   1564  N   ILE A 187      -6.679  -9.230 110.883  1.00 69.79           N  
ANISOU 1564  N   ILE A 187     8269   9725   8522   -148  -1252    102       N  
ATOM   1565  CA  ILE A 187      -6.424  -8.182 111.864  1.00 65.40           C  
ANISOU 1565  CA  ILE A 187     7746   9101   8002     20  -1177    236       C  
ATOM   1566  C   ILE A 187      -5.730  -7.022 111.160  1.00 63.80           C  
ANISOU 1566  C   ILE A 187     7711   8803   7726    309  -1171    319       C  
ATOM   1567  O   ILE A 187      -4.713  -7.231 110.485  1.00 66.59           O  
ANISOU 1567  O   ILE A 187     8261   8947   8093    311  -1152    333       O  
ATOM   1568  CB  ILE A 187      -5.590  -8.718 113.040  1.00 60.55           C  
ANISOU 1568  CB  ILE A 187     7238   8229   7539   -146  -1064    310       C  
ATOM   1569  CG1 ILE A 187      -6.178 -10.040 113.544  1.00 67.98           C  
ANISOU 1569  CG1 ILE A 187     8061   9213   8557   -447  -1046    240       C  
ATOM   1570  CG2 ILE A 187      -5.538  -7.703 114.164  1.00 59.49           C  
ANISOU 1570  CG2 ILE A 187     7091   8092   7420    -17   -991    405       C  
ATOM   1571  CD1 ILE A 187      -5.389 -10.684 114.638  1.00 76.82           C  
ANISOU 1571  CD1 ILE A 187     9290  10092   9806   -596   -938    338       C  
ATOM   1572  N   PRO A 188      -6.246  -5.798 111.273  1.00 67.65           N  
ANISOU 1572  N   PRO A 188     8135   9426   8143    558  -1168    377       N  
ATOM   1573  CA  PRO A 188      -5.594  -4.657 110.620  1.00 70.02           C  
ANISOU 1573  CA  PRO A 188     8617   9604   8385    835  -1128    469       C  
ATOM   1574  C   PRO A 188      -4.149  -4.492 111.073  1.00 76.47           C  
ANISOU 1574  C   PRO A 188     9664  10068   9321    799  -1004    537       C  
ATOM   1575  O   PRO A 188      -3.793  -4.788 112.215  1.00 71.10           O  
ANISOU 1575  O   PRO A 188     8979   9281   8756    650   -939    547       O  
ATOM   1576  CB  PRO A 188      -6.451  -3.466 111.058  1.00 68.46           C  
ANISOU 1576  CB  PRO A 188     8296   9574   8142   1072  -1102    523       C  
ATOM   1577  CG  PRO A 188      -7.801  -4.055 111.319  1.00 62.33           C  
ANISOU 1577  CG  PRO A 188     7228   9125   7329    962  -1198    430       C  
ATOM   1578  CD  PRO A 188      -7.551  -5.439 111.856  1.00 65.62           C  
ANISOU 1578  CD  PRO A 188     7626   9457   7850    607  -1195    352       C  
ATOM   1579  N   LYS A 189      -3.313  -3.977 110.191  1.00101.64           N  
ANISOU 1579  N   LYS A 189    13049  13097  12472    938   -970    582       N  
ATOM   1580  CA  LYS A 189      -1.914  -3.695 110.488  1.00114.96           C  
ANISOU 1580  CA  LYS A 189    14939  14471  14268    930   -845    636       C  
ATOM   1581  C   LYS A 189      -1.786  -2.176 110.634  1.00130.86           C  
ANISOU 1581  C   LYS A 189    17036  16411  16273   1174   -733    713       C  
ATOM   1582  O   LYS A 189      -1.900  -1.647 111.730  1.00144.09           O  
ANISOU 1582  O   LYS A 189    18657  18073  18016   1172   -662    721       O  
ATOM   1583  CB  LYS A 189      -1.050  -4.177 109.359  1.00118.18           C  
ANISOU 1583  CB  LYS A 189    15516  14720  14666    891   -847    621       C  
ATOM   1584  CG  LYS A 189       0.309  -4.617 109.813  1.00124.54           C  
ANISOU 1584  CG  LYS A 189    16517  15222  15581    897   -714    669       C  
ATOM   1585  CD  LYS A 189       0.418  -6.118 109.852  1.00130.54           C  
ANISOU 1585  CD  LYS A 189    17240  15869  16491    707   -675    665       C  
ATOM   1586  CE  LYS A 189       1.486  -6.581 108.887  1.00125.00           C  
ANISOU 1586  CE  LYS A 189    16690  14917  15885    735   -549    698       C  
ATOM   1587  NZ  LYS A 189       2.481  -7.449 109.558  1.00119.35           N  
ANISOU 1587  NZ  LYS A 189    15927  14130  15289    575   -525    702       N  
ATOM   1588  N   GLN A 190      -1.548  -1.470 109.536  1.00122.53           N  
ANISOU 1588  N   GLN A 190    16124  15301  15133   1383   -700    769       N  
ATOM   1589  CA  GLN A 190      -1.548  -0.011 109.549  1.00119.32           C  
ANISOU 1589  CA  GLN A 190    15779  14823  14735   1572   -553    823       C  
ATOM   1590  C   GLN A 190      -2.377   0.491 108.373  1.00115.09           C  
ANISOU 1590  C   GLN A 190    15214  14468  14048   1762   -593    857       C  
ATOM   1591  O   GLN A 190      -3.547   0.847 108.539  1.00112.90           O  
ANISOU 1591  O   GLN A 190    14783  14411  13704   1897   -648    874       O  
ATOM   1592  CB  GLN A 190      -0.118   0.539 109.497  1.00120.56           C  
ANISOU 1592  CB  GLN A 190    16097  14698  15014   1467   -372    800       C  
ATOM   1593  CG  GLN A 190       0.769   0.037 110.630  1.00118.99           C  
ANISOU 1593  CG  GLN A 190    15901  14354  14956   1270   -340    759       C  
ATOM   1594  CD  GLN A 190       1.355   1.156 111.459  1.00115.65           C  
ANISOU 1594  CD  GLN A 190    15506  13801  14633   1249   -177    725       C  
ATOM   1595  OE1 GLN A 190       1.464   2.292 111.000  1.00112.25           O  
ANISOU 1595  OE1 GLN A 190    15137  13321  14194   1339    -59    722       O  
ATOM   1596  NE2 GLN A 190       1.745   0.840 112.687  1.00113.77           N  
ANISOU 1596  NE2 GLN A 190    15238  13511  14477   1133   -172    699       N  
ATOM   1597  N   ASP A 191      -1.780   0.528 107.185  1.00111.35           N  
ANISOU 1597  N   ASP A 191    14876  13918  13515   1777   -560    868       N  
ATOM   1598  CA  ASP A 191      -2.528   0.566 105.937  1.00102.87           C  
ANISOU 1598  CA  ASP A 191    13775  13059  12254   1932   -654    896       C  
ATOM   1599  C   ASP A 191      -2.707  -0.830 105.366  1.00 95.71           C  
ANISOU 1599  C   ASP A 191    12819  12315  11229   1841   -855    837       C  
ATOM   1600  O   ASP A 191      -3.114  -0.978 104.208  1.00 90.86           O  
ANISOU 1600  O   ASP A 191    12200  11884  10440   1928   -944    834       O  
ATOM   1601  CB  ASP A 191      -1.827   1.463 104.919  1.00109.43           C  
ANISOU 1601  CB  ASP A 191    14789  13740  13050   2022   -501    943       C  
ATOM   1602  CG  ASP A 191      -0.394   1.044 104.661  1.00113.28           C  
ANISOU 1602  CG  ASP A 191    15436  13983  13621   1857   -413    904       C  
ATOM   1603  OD1 ASP A 191      -0.179  -0.046 104.094  1.00111.49           O  
ANISOU 1603  OD1 ASP A 191    15242  13794  13325   1787   -525    870       O  
ATOM   1604  OD2 ASP A 191       0.524   1.807 105.027  1.00112.18           O1-
ANISOU 1604  OD2 ASP A 191    15379  13631  13613   1790   -236    894       O1-
ATOM   1605  N   ASN A 192      -2.413  -1.852 106.169  1.00 95.87           N  
ANISOU 1605  N   ASN A 192    12810  12280  11335   1661   -929    781       N  
ATOM   1606  CA  ASN A 192      -2.245  -3.222 105.708  1.00 89.38           C  
ANISOU 1606  CA  ASN A 192    11962  11498  10502   1416  -1025    659       C  
ATOM   1607  C   ASN A 192      -3.065  -4.164 106.580  1.00 89.07           C  
ANISOU 1607  C   ASN A 192    11685  11625  10533   1185  -1118    553       C  
ATOM   1608  O   ASN A 192      -3.888  -3.715 107.384  1.00 98.33           O  
ANISOU 1608  O   ASN A 192    12696  12940  11724   1242  -1129    574       O  
ATOM   1609  CB  ASN A 192      -0.759  -3.595 105.740  1.00 87.66           C  
ANISOU 1609  CB  ASN A 192    11949  10937  10423   1279   -906    655       C  
ATOM   1610  CG  ASN A 192      -0.392  -4.660 104.722  1.00 92.42           C  
ANISOU 1610  CG  ASN A 192    12619  11532  10964   1142   -960    559       C  
ATOM   1611  OD1 ASN A 192      -1.089  -5.664 104.571  1.00 98.76           O  
ANISOU 1611  OD1 ASN A 192    13280  12518  11726    978  -1078    441       O  
ATOM   1612  ND2 ASN A 192       0.713  -4.441 104.013  1.00 85.18           N  
ANISOU 1612  ND2 ASN A 192    11921  10398  10047   1198   -855    596       N  
ATOM   1613  N   PHE A 193      -2.834  -5.469 106.448  1.00 72.91           N  
ANISOU 1613  N   PHE A 193     9625   9543   8536    923  -1161    439       N  
ATOM   1614  CA  PHE A 193      -3.554  -6.467 107.225  1.00 61.85           C  
ANISOU 1614  CA  PHE A 193     8024   8263   7213    676  -1219    341       C  
ATOM   1615  C   PHE A 193      -2.573  -7.519 107.724  1.00 57.26           C  
ANISOU 1615  C   PHE A 193     7547   7402   6809    426  -1141    311       C  
ATOM   1616  O   PHE A 193      -1.370  -7.468 107.444  1.00 71.45           O  
ANISOU 1616  O   PHE A 193     9543   8941   8665    451  -1058    355       O  
ATOM   1617  CB  PHE A 193      -4.670  -7.117 106.399  1.00 69.26           C  
ANISOU 1617  CB  PHE A 193     8784   9529   8001    604  -1368    202       C  
ATOM   1618  CG  PHE A 193      -4.166  -8.021 105.310  1.00 70.63           C  
ANISOU 1618  CG  PHE A 193     9073   9641   8122    473  -1394     91       C  
ATOM   1619  CD1 PHE A 193      -3.796  -7.505 104.077  1.00 70.62           C  
ANISOU 1619  CD1 PHE A 193     9218   9663   7953    665  -1415    119       C  
ATOM   1620  CD2 PHE A 193      -4.067  -9.388 105.517  1.00 63.52           C  
ANISOU 1620  CD2 PHE A 193     8147   8647   7339    160  -1379    -40       C  
ATOM   1621  CE1 PHE A 193      -3.337  -8.333 103.077  1.00 74.58           C  
ANISOU 1621  CE1 PHE A 193     9828  10115   8394    540  -1427      1       C  
ATOM   1622  CE2 PHE A 193      -3.603 -10.222 104.518  1.00 60.79           C  
ANISOU 1622  CE2 PHE A 193     7915   8227   6955     37  -1382   -161       C  
ATOM   1623  CZ  PHE A 193      -3.240  -9.694 103.297  1.00 70.68           C  
ANISOU 1623  CZ  PHE A 193     9303   9524   8029    223  -1410   -149       C  
ATOM   1624  N   ARG A 194      -3.107  -8.489 108.465  1.00 59.41           N  
ANISOU 1624  N   ARG A 194     7676   7729   7169    192  -1160    242       N  
ATOM   1625  CA  ARG A 194      -2.334  -9.634 108.925  1.00 62.05           C  
ANISOU 1625  CA  ARG A 194     8094   7817   7667    -40  -1087    225       C  
ATOM   1626  C   ARG A 194      -3.305 -10.785 109.149  1.00 69.80           C  
ANISOU 1626  C   ARG A 194     8906   8939   8678   -294  -1128    103       C  
ATOM   1627  O   ARG A 194      -4.343 -10.604 109.798  1.00 65.37           O  
ANISOU 1627  O   ARG A 194     8150   8594   8094   -320  -1163     93       O  
ATOM   1628  CB  ARG A 194      -1.558  -9.297 110.203  1.00 39.01           C  
ANISOU 1628  CB  ARG A 194     5234   4703   4885    -28   -989    354       C  
ATOM   1629  CG  ARG A 194      -1.211 -10.479 111.085  1.00 51.20           C  
ANISOU 1629  CG  ARG A 194     6779   6089   6584   -259   -931    368       C  
ATOM   1630  CD  ARG A 194      -0.457 -10.034 112.335  1.00 57.80           C  
ANISOU 1630  CD  ARG A 194     7658   6794   7509   -218   -856    498       C  
ATOM   1631  NE  ARG A 194       0.990 -10.021 112.133  1.00 76.92           N  
ANISOU 1631  NE  ARG A 194    10255   8960  10010   -166   -793    554       N  
ATOM   1632  CZ  ARG A 194       1.788  -9.008 112.460  1.00 78.77           C  
ANISOU 1632  CZ  ARG A 194    10559   9117  10253    -24   -746    621       C  
ATOM   1633  NH1 ARG A 194       1.288  -7.910 113.011  1.00 76.27           N  
ANISOU 1633  NH1 ARG A 194    10173   8933   9873     87   -745    644       N  
ATOM   1634  NH2 ARG A 194       3.091  -9.094 112.239  1.00 82.48           N  
ANISOU 1634  NH2 ARG A 194    11162   9373  10803      1   -687    654       N  
ATOM   1635  N   ALA A 195      -2.981 -11.954 108.597  1.00 64.46           N  
ANISOU 1635  N   ALA A 195     8301   8133   8057   -486  -1106      1       N  
ATOM   1636  CA  ALA A 195      -3.854 -13.120 108.645  1.00 68.54           C  
ANISOU 1636  CA  ALA A 195     8680   8750   8612   -758  -1118   -145       C  
ATOM   1637  C   ALA A 195      -3.316 -14.098 109.677  1.00 63.92           C  
ANISOU 1637  C   ALA A 195     8164   7888   8234   -952   -989    -78       C  
ATOM   1638  O   ALA A 195      -2.166 -14.537 109.577  1.00 75.42           O  
ANISOU 1638  O   ALA A 195     9810   9051   9795   -958   -907    -25       O  
ATOM   1639  CB  ALA A 195      -3.956 -13.778 107.270  1.00 67.02           C  
ANISOU 1639  CB  ALA A 195     8522   8612   8332   -853  -1165   -332       C  
ATOM   1640  N   ILE A 196      -4.149 -14.440 110.661  1.00 47.98           N  
ANISOU 1640  N   ILE A 196     5990   5970   6270  -1098   -964    -71       N  
ATOM   1641  CA  ILE A 196      -3.720 -15.197 111.826  1.00 49.37           C  
ANISOU 1641  CA  ILE A 196     6226   5916   6616  -1239   -838     43       C  
ATOM   1642  C   ILE A 196      -4.630 -16.404 112.012  1.00 55.82           C  
ANISOU 1642  C   ILE A 196     6933   6766   7509  -1542   -779    -78       C  
ATOM   1643  O   ILE A 196      -5.777 -16.427 111.561  1.00 68.03           O  
ANISOU 1643  O   ILE A 196     8290   8588   8970  -1637   -849   -243       O  
ATOM   1644  CB  ILE A 196      -3.726 -14.323 113.102  1.00 58.00           C  
ANISOU 1644  CB  ILE A 196     7265   7072   7700  -1111   -826    210       C  
ATOM   1645  CG1 ILE A 196      -2.815 -14.913 114.171  1.00 77.96           C  
ANISOU 1645  CG1 ILE A 196     9920   9334  10368  -1170   -711    374       C  
ATOM   1646  CG2 ILE A 196      -5.129 -14.188 113.651  1.00 58.96           C  
ANISOU 1646  CG2 ILE A 196     7150   7484   7768  -1198   -851    153       C  
ATOM   1647  CD1 ILE A 196      -1.398 -14.522 113.997  1.00 90.33           C  
ANISOU 1647  CD1 ILE A 196    11666  10688  11966  -1000   -700    473       C  
ATOM   1648  N   VAL A 197      -4.108 -17.410 112.702  1.00 56.41           N  
ANISOU 1648  N   VAL A 197     7122   6561   7751  -1692   -639      9       N  
ATOM   1649  CA  VAL A 197      -4.887 -18.573 113.109  1.00 65.31           C  
ANISOU 1649  CA  VAL A 197     8176   7657   8984  -1991   -531    -66       C  
ATOM   1650  C   VAL A 197      -5.116 -18.506 114.609  1.00 78.09           C  
ANISOU 1650  C   VAL A 197     9740   9284  10645  -2012   -455    116       C  
ATOM   1651  O   VAL A 197      -4.182 -18.241 115.374  1.00 87.79           O  
ANISOU 1651  O   VAL A 197    11095  10356  11907  -1867   -421    322       O  
ATOM   1652  CB  VAL A 197      -4.182 -19.881 112.718  1.00 67.04           C  
ANISOU 1652  CB  VAL A 197     8585   7519   9367  -2154   -394   -101       C  
ATOM   1653  CG1 VAL A 197      -4.583 -21.008 113.659  1.00 68.95           C  
ANISOU 1653  CG1 VAL A 197     8829   7601   9766  -2406   -217    -47       C  
ATOM   1654  CG2 VAL A 197      -4.526 -20.232 111.285  1.00 78.84           C  
ANISOU 1654  CG2 VAL A 197    10059   9089  10808  -2264   -445   -371       C  
ATOM   1655  N   SER A 198      -6.360 -18.736 115.028  1.00 69.10           N  
ANISOU 1655  N   SER A 198     8406   8353   9495  -2195   -428     31       N  
ATOM   1656  CA  SER A 198      -6.688 -19.014 116.419  1.00 63.45           C  
ANISOU 1656  CA  SER A 198     7652   7620   8837  -2293   -308    181       C  
ATOM   1657  C   SER A 198      -6.877 -20.522 116.522  1.00 67.08           C  
ANISOU 1657  C   SER A 198     8180   7842   9464  -2600   -126    140       C  
ATOM   1658  O   SER A 198      -7.801 -21.083 115.919  1.00 60.16           O  
ANISOU 1658  O   SER A 198     7174   7071   8612  -2834   -105    -85       O  
ATOM   1659  CB  SER A 198      -7.933 -18.248 116.858  1.00 69.75           C  
ANISOU 1659  CB  SER A 198     8187   8793   9522  -2291   -368    118       C  
ATOM   1660  OG  SER A 198      -7.692 -16.854 116.813  1.00 67.31           O  
ANISOU 1660  OG  SER A 198     7845   8650   9078  -1992   -503    172       O  
ATOM   1661  N   ILE A 199      -5.955 -21.176 117.233  1.00 73.99           N  
ANISOU 1661  N   ILE A 199     9263   8393  10456  -2592      8    352       N  
ATOM   1662  CA  ILE A 199      -5.983 -22.624 117.391  1.00 75.22           C  
ANISOU 1662  CA  ILE A 199     9507   8278  10794  -2730    216    347       C  
ATOM   1663  C   ILE A 199      -7.165 -23.014 118.265  1.00 80.34           C  
ANISOU 1663  C   ILE A 199    10004   9057  11464  -2913    327    343       C  
ATOM   1664  O   ILE A 199      -7.482 -22.336 119.253  1.00 80.73           O  
ANISOU 1664  O   ILE A 199     9972   9287  11415  -2889    315    470       O  
ATOM   1665  CB  ILE A 199      -4.657 -23.112 118.003  1.00 88.06           C  
ANISOU 1665  CB  ILE A 199    11346   9591  12523  -2512    328    592       C  
ATOM   1666  CG1 ILE A 199      -3.510 -22.995 116.997  1.00 86.90           C  
ANISOU 1666  CG1 ILE A 199    11334   9290  12395  -2338    264    553       C  
ATOM   1667  CG2 ILE A 199      -4.768 -24.555 118.461  1.00 99.85           C  
ANISOU 1667  CG2 ILE A 199    12881  10848  14209  -2591    503    680       C  
ATOM   1668  CD1 ILE A 199      -3.737 -23.750 115.712  1.00 87.70           C  
ANISOU 1668  CD1 ILE A 199    11434   9301  12586  -2466    256    329       C  
ATOM   1669  N   PHE A 200      -7.840 -24.090 117.894  1.00 89.68           N  
ANISOU 1669  N   PHE A 200    11145  10165  12765  -3097    427    197       N  
ATOM   1670  CA  PHE A 200      -8.899 -24.625 118.736  1.00 93.15           C  
ANISOU 1670  CA  PHE A 200    11468  10679  13247  -3272    558    209       C  
ATOM   1671  C   PHE A 200      -8.293 -25.157 120.027  1.00100.03           C  
ANISOU 1671  C   PHE A 200    12493  11315  14197  -3176    709    526       C  
ATOM   1672  O   PHE A 200      -7.413 -26.027 119.975  1.00107.74           O  
ANISOU 1672  O   PHE A 200    13655  11990  15292  -3092    769    660       O  
ATOM   1673  CB  PHE A 200      -9.659 -25.725 118.006  1.00 90.95           C  
ANISOU 1673  CB  PHE A 200    11142  10349  13065  -3493    629    -12       C  
ATOM   1674  CG  PHE A 200     -10.591 -25.212 116.952  1.00 92.09           C  
ANISOU 1674  CG  PHE A 200    11063  10827  13101  -3607    487   -332       C  
ATOM   1675  CD1 PHE A 200     -11.523 -24.235 117.257  1.00 95.20           C  
ANISOU 1675  CD1 PHE A 200    11203  11605  13361  -3624    392   -402       C  
ATOM   1676  CD2 PHE A 200     -10.539 -25.701 115.657  1.00 92.97           C  
ANISOU 1676  CD2 PHE A 200    11203  10894  13226  -3675    440   -559       C  
ATOM   1677  CE1 PHE A 200     -12.385 -23.754 116.292  1.00 99.45           C  
ANISOU 1677  CE1 PHE A 200    11508  12492  13785  -3679    237   -675       C  
ATOM   1678  CE2 PHE A 200     -11.400 -25.225 114.687  1.00 93.73           C  
ANISOU 1678  CE2 PHE A 200    11080  11339  13195  -3754    292   -843       C  
ATOM   1679  CZ  PHE A 200     -12.325 -24.250 115.006  1.00 98.39           C  
ANISOU 1679  CZ  PHE A 200    11406  12325  13653  -3742    182   -893       C  
ATOM   1680  N   PRO A 201      -8.709 -24.663 121.192  1.00108.90           N  
ANISOU 1680  N   PRO A 201    13542  12595  15241  -3170    760    661       N  
ATOM   1681  CA  PRO A 201      -8.157 -25.179 122.453  1.00115.54           C  
ANISOU 1681  CA  PRO A 201    14524  13246  16131  -3069    905    968       C  
ATOM   1682  C   PRO A 201      -8.457 -26.655 122.652  1.00129.08           C  
ANISOU 1682  C   PRO A 201    16307  14736  18000  -3217   1054   1033       C  
ATOM   1683  O   PRO A 201      -9.434 -27.015 123.317  1.00140.29           O  
ANISOU 1683  O   PRO A 201    17640  16237  19428  -3386   1175   1036       O  
ATOM   1684  CB  PRO A 201      -8.842 -24.314 123.522  1.00112.80           C  
ANISOU 1684  CB  PRO A 201    14051  13185  15625  -3091    924   1025       C  
ATOM   1685  CG  PRO A 201      -9.401 -23.132 122.781  1.00109.36           C  
ANISOU 1685  CG  PRO A 201    13421  13082  15049  -3126    730    802       C  
ATOM   1686  CD  PRO A 201      -9.726 -23.622 121.413  1.00111.30           C  
ANISOU 1686  CD  PRO A 201    13611  13287  15389  -3246    677    544       C  
ATOM   1687  N   ASP A 202      -7.633 -27.513 122.051  1.00130.50           N  
ANISOU 1687  N   ASP A 202    16656  14650  18278  -3167   1042   1071       N  
ATOM   1688  CA  ASP A 202      -7.730 -28.966 122.189  1.00144.36           C  
ANISOU 1688  CA  ASP A 202    18540  16167  20141  -3299   1181   1129       C  
ATOM   1689  C   ASP A 202      -6.434 -29.431 122.839  1.00145.29           C  
ANISOU 1689  C   ASP A 202    18883  16081  20241  -3099   1168   1445       C  
ATOM   1690  O   ASP A 202      -5.489 -29.838 122.158  1.00127.07           O  
ANISOU 1690  O   ASP A 202    16723  13595  17962  -2995   1109   1435       O  
ATOM   1691  CB  ASP A 202      -7.971 -29.661 120.828  1.00149.23           C  
ANISOU 1691  CB  ASP A 202    19174  16678  20850  -3445   1190    835       C  
ATOM   1692  CG  ASP A 202      -9.246 -29.196 120.148  1.00150.86           C  
ANISOU 1692  CG  ASP A 202    19148  17151  21021  -3650   1158    505       C  
ATOM   1693  OD1 ASP A 202      -9.582 -27.996 120.243  1.00145.26           O  
ANISOU 1693  OD1 ASP A 202    18276  16720  20196  -3601   1046    454       O  
ATOM   1694  OD2 ASP A 202      -9.917 -30.035 119.514  1.00153.91           O1-
ANISOU 1694  OD2 ASP A 202    19510  17489  21481  -3862   1243    286       O1-
ATOM   1695  N   SER A 203      -6.391 -29.362 124.171  1.00148.71           N  
ANISOU 1695  N   SER A 203    19344  16569  20591  -3050   1217   1714       N  
ATOM   1696  CA  SER A 203      -5.158 -29.639 124.906  1.00142.08           C  
ANISOU 1696  CA  SER A 203    18732  15627  19627  -2866   1162   1988       C  
ATOM   1697  C   SER A 203      -5.008 -31.146 125.113  1.00137.14           C  
ANISOU 1697  C   SER A 203    18298  14717  19092  -2942   1321   2078       C  
ATOM   1698  O   SER A 203      -5.122 -31.682 126.218  1.00136.42           O  
ANISOU 1698  O   SER A 203    18299  14587  18949  -2971   1436   2288       O  
ATOM   1699  CB  SER A 203      -5.126 -28.879 126.224  1.00141.32           C  
ANISOU 1699  CB  SER A 203    18622  15761  19314  -2758   1139   2168       C  
ATOM   1700  OG  SER A 203      -6.423 -28.772 126.779  1.00144.24           O  
ANISOU 1700  OG  SER A 203    18786  16257  19760  -2915   1284   2165       O  
ATOM   1701  N   ALA A 204      -4.763 -31.828 123.996  1.00134.61           N  
ANISOU 1701  N   ALA A 204    18038  14195  18914  -2966   1345   1902       N  
ATOM   1702  CA  ALA A 204      -4.181 -33.161 123.997  1.00135.40           C  
ANISOU 1702  CA  ALA A 204    18348  13988  19109  -2942   1475   1982       C  
ATOM   1703  C   ALA A 204      -2.831 -33.205 123.305  1.00137.30           C  
ANISOU 1703  C   ALA A 204    18721  14104  19342  -2723   1363   1974       C  
ATOM   1704  O   ALA A 204      -2.013 -34.071 123.619  1.00142.28           O  
ANISOU 1704  O   ALA A 204    19534  14522  20003  -2605   1438   2122       O  
ATOM   1705  CB  ALA A 204      -5.123 -34.163 123.322  1.00137.15           C  
ANISOU 1705  CB  ALA A 204    18544  14046  19521  -3191   1664   1763       C  
ATOM   1706  N   ARG A 205      -2.577 -32.268 122.392  1.00133.20           N  
ANISOU 1706  N   ARG A 205    18107  13718  18786  -2655   1195   1807       N  
ATOM   1707  CA  ARG A 205      -1.331 -32.192 121.648  1.00117.43           C  
ANISOU 1707  CA  ARG A 205    16211  11633  16773  -2453   1087   1771       C  
ATOM   1708  C   ARG A 205      -0.470 -30.998 122.037  1.00102.21           C  
ANISOU 1708  C   ARG A 205    14299   9896  14640  -2244    901   1869       C  
ATOM   1709  O   ARG A 205       0.574 -30.791 121.420  1.00 99.77           O  
ANISOU 1709  O   ARG A 205    14058   9546  14302  -2071    809   1822       O  
ATOM   1710  CB  ARG A 205      -1.627 -32.140 120.140  1.00112.28           C  
ANISOU 1710  CB  ARG A 205    15475  10958  16230  -2541   1064   1470       C  
ATOM   1711  CG  ARG A 205      -2.052 -33.461 119.510  1.00118.60           C  
ANISOU 1711  CG  ARG A 205    16338  11516  17208  -2709   1258   1318       C  
ATOM   1712  CD  ARG A 205      -1.168 -34.617 119.933  1.00125.33           C  
ANISOU 1712  CD  ARG A 205    17395  12093  18130  -2594   1384   1495       C  
ATOM   1713  NE  ARG A 205      -1.113 -35.636 118.890  1.00123.94           N  
ANISOU 1713  NE  ARG A 205    17297  11682  18112  -2677   1523   1299       N  
ATOM   1714  CZ  ARG A 205      -0.527 -36.820 119.027  1.00118.45           C  
ANISOU 1714  CZ  ARG A 205    16772  10704  17530  -2619   1688   1391       C  
ATOM   1715  NH1 ARG A 205       0.050 -37.146 120.174  1.00115.21           N  
ANISOU 1715  NH1 ARG A 205    16469  10216  17088  -2472   1726   1685       N  
ATOM   1716  NH2 ARG A 205      -0.529 -37.682 118.020  1.00115.73           N  
ANISOU 1716  NH2 ARG A 205    16491  10155  17324  -2710   1825   1184       N  
ATOM   1717  N   LYS A 206      -0.871 -30.203 123.030  1.00 95.48           N  
ANISOU 1717  N   LYS A 206    13397   9252  13629  -2260    867   1977       N  
ATOM   1718  CA  LYS A 206      -0.069 -29.036 123.399  1.00 89.57           C  
ANISOU 1718  CA  LYS A 206    12699   8692  12641  -2042    760   1981       C  
ATOM   1719  C   LYS A 206       1.298 -29.424 123.964  1.00 80.71           C  
ANISOU 1719  C   LYS A 206    11766   7447  11455  -1808    764   2152       C  
ATOM   1720  O   LYS A 206       2.308 -28.847 123.521  1.00 78.33           O  
ANISOU 1720  O   LYS A 206    11496   7175  11092  -1609    678   2087       O  
ATOM   1721  CB  LYS A 206      -0.863 -28.147 124.367  1.00 95.65           C  
ANISOU 1721  CB  LYS A 206    13402   9702  13241  -2095    806   1995       C  
ATOM   1722  CG  LYS A 206      -0.034 -27.362 125.395  1.00 97.25           C  
ANISOU 1722  CG  LYS A 206    13705   9994  13252  -1840    855   2101       C  
ATOM   1723  CD  LYS A 206      -0.942 -26.468 126.250  1.00 95.94           C  
ANISOU 1723  CD  LYS A 206    13411  10031  13011  -1874    967   2108       C  
ATOM   1724  CE  LYS A 206      -0.199 -25.842 127.432  1.00 93.45           C  
ANISOU 1724  CE  LYS A 206    13092   9848  12566  -1632    925   2318       C  
ATOM   1725  NZ  LYS A 206      -0.497 -24.384 127.599  1.00 89.30           N  
ANISOU 1725  NZ  LYS A 206    12320   9608  12003  -1552    816   2282       N  
ATOM   1726  N   PRO A 207       1.423 -30.388 124.889  1.00 75.77           N  
ANISOU 1726  N   PRO A 207    11239   6691  10859  -1798    865   2367       N  
ATOM   1727  CA  PRO A 207       2.769 -30.856 125.266  1.00 73.02           C  
ANISOU 1727  CA  PRO A 207    11014   6233  10499  -1541    859   2516       C  
ATOM   1728  C   PRO A 207       3.516 -31.509 124.116  1.00 81.14           C  
ANISOU 1728  C   PRO A 207    12072   7064  11693  -1472    845   2418       C  
ATOM   1729  O   PRO A 207       4.746 -31.451 124.099  1.00 88.48           O  
ANISOU 1729  O   PRO A 207    13048   7975  12597  -1240    788   2466       O  
ATOM   1730  CB  PRO A 207       2.487 -31.845 126.399  1.00 59.34           C  
ANISOU 1730  CB  PRO A 207     9367   4393   8786  -1579   1000   2756       C  
ATOM   1731  CG  PRO A 207       1.067 -32.259 126.233  1.00 60.92           C  
ANISOU 1731  CG  PRO A 207     9496   4557   9095  -1878   1108   2691       C  
ATOM   1732  CD  PRO A 207       0.360 -31.075 125.656  1.00 69.32           C  
ANISOU 1732  CD  PRO A 207    10406   5841  10093  -1998   1003   2485       C  
ATOM   1733  N   PHE A 208       2.813 -32.110 123.150  1.00 71.58           N  
ANISOU 1733  N   PHE A 208    10821   5719  10659  -1661    908   2269       N  
ATOM   1734  CA  PHE A 208       3.480 -32.686 121.983  1.00 71.31           C  
ANISOU 1734  CA  PHE A 208    10819   5505  10772  -1599    918   2143       C  
ATOM   1735  C   PHE A 208       4.116 -31.598 121.122  1.00 70.91           C  
ANISOU 1735  C   PHE A 208    10708   5602  10632  -1485    750   1985       C  
ATOM   1736  O   PHE A 208       5.294 -31.688 120.749  1.00 70.68           O  
ANISOU 1736  O   PHE A 208    10728   5513  10614  -1293    712   1985       O  
ATOM   1737  CB  PHE A 208       2.477 -33.506 121.172  1.00 66.19           C  
ANISOU 1737  CB  PHE A 208    10136   4698  10314  -1836   1052   1983       C  
ATOM   1738  CG  PHE A 208       3.072 -34.200 119.977  1.00 71.10           C  
ANISOU 1738  CG  PHE A 208    10811   5120  11082  -1794   1104   1834       C  
ATOM   1739  CD1 PHE A 208       4.327 -34.781 120.046  1.00 72.19           C  
ANISOU 1739  CD1 PHE A 208    11064   5106  11258  -1578   1137   1945       C  
ATOM   1740  CD2 PHE A 208       2.367 -34.278 118.785  1.00 78.70           C  
ANISOU 1740  CD2 PHE A 208    11703   6055  12144  -1969   1135   1574       C  
ATOM   1741  CE1 PHE A 208       4.874 -35.420 118.946  1.00 63.02           C  
ANISOU 1741  CE1 PHE A 208     9950   3764  10230  -1542   1204   1805       C  
ATOM   1742  CE2 PHE A 208       2.907 -34.920 117.682  1.00 80.84           C  
ANISOU 1742  CE2 PHE A 208    12036   6149  12531  -1938   1200   1423       C  
ATOM   1743  CZ  PHE A 208       4.164 -35.491 117.763  1.00 69.59           C  
ANISOU 1743  CZ  PHE A 208    10728   4567  11144  -1725   1238   1542       C  
ATOM   1744  N   PHE A 209       3.338 -30.568 120.782  1.00 62.64           N  
ANISOU 1744  N   PHE A 209     9549   4746   9504  -1601    661   1849       N  
ATOM   1745  CA  PHE A 209       3.876 -29.436 120.039  1.00 64.05           C  
ANISOU 1745  CA  PHE A 209     9689   5070   9579  -1492    523   1709       C  
ATOM   1746  C   PHE A 209       5.024 -28.780 120.796  1.00 66.61           C  
ANISOU 1746  C   PHE A 209    10070   5498   9742  -1239    475   1817       C  
ATOM   1747  O   PHE A 209       5.988 -28.304 120.183  1.00 73.78           O  
ANISOU 1747  O   PHE A 209    10978   6436  10619  -1081    404   1740       O  
ATOM   1748  CB  PHE A 209       2.771 -28.413 119.757  1.00 46.20           C  
ANISOU 1748  CB  PHE A 209     7286   3020   7247  -1628    474   1563       C  
ATOM   1749  CG  PHE A 209       1.773 -28.846 118.710  1.00 60.91           C  
ANISOU 1749  CG  PHE A 209     9033   4808   9300  -1843    493   1404       C  
ATOM   1750  CD1 PHE A 209       2.160 -29.031 117.393  1.00 64.06           C  
ANISOU 1750  CD1 PHE A 209     9435   5108   9798  -1824    464   1242       C  
ATOM   1751  CD2 PHE A 209       0.440 -29.038 119.042  1.00 74.40           C  
ANISOU 1751  CD2 PHE A 209    10624   6554  11089  -2064    567   1392       C  
ATOM   1752  CE1 PHE A 209       1.241 -29.420 116.432  1.00 65.34           C  
ANISOU 1752  CE1 PHE A 209     9505   5221  10102  -2007    530   1035       C  
ATOM   1753  CE2 PHE A 209      -0.481 -29.429 118.087  1.00 70.77           C  
ANISOU 1753  CE2 PHE A 209    10057   6045  10787  -2250    634   1179       C  
ATOM   1754  CZ  PHE A 209      -0.080 -29.619 116.782  1.00 64.95           C  
ANISOU 1754  CZ  PHE A 209     9347   5219  10111  -2223    617    988       C  
ATOM   1755  N   LYS A 210       4.945 -28.742 122.130  1.00 56.03           N  
ANISOU 1755  N   LYS A 210     8755   4223   8312  -1193    522   1995       N  
ATOM   1756  CA  LYS A 210       6.037 -28.160 122.906  1.00 67.32           C  
ANISOU 1756  CA  LYS A 210    10184   5767   9627   -937    479   2105       C  
ATOM   1757  C   LYS A 210       7.293 -29.025 122.821  1.00 58.97           C  
ANISOU 1757  C   LYS A 210     9186   4557   8664   -766    474   2204       C  
ATOM   1758  O   LYS A 210       8.408 -28.510 122.673  1.00 49.47           O  
ANISOU 1758  O   LYS A 210     7944   3429   7425   -570    400   2188       O  
ATOM   1759  CB  LYS A 210       5.607 -27.977 124.357  1.00 77.33           C  
ANISOU 1759  CB  LYS A 210    11443   7151  10788   -928    528   2284       C  
ATOM   1760  CG  LYS A 210       6.625 -27.255 125.224  1.00100.39           C  
ANISOU 1760  CG  LYS A 210    14300  10244  13598   -676    455   2403       C  
ATOM   1761  CD  LYS A 210       6.207 -25.812 125.425  1.00104.68           C  
ANISOU 1761  CD  LYS A 210    14695  11037  14039   -659    409   2320       C  
ATOM   1762  CE  LYS A 210       7.394 -24.898 125.633  1.00 93.71           C  
ANISOU 1762  CE  LYS A 210    13193   9820  12593   -435    283   2337       C  
ATOM   1763  NZ  LYS A 210       8.549 -25.597 126.243  1.00 89.81           N  
ANISOU 1763  NZ  LYS A 210    12748   9277  12097   -267    253   2513       N  
ATOM   1764  N   LEU A 211       7.126 -30.349 122.914  1.00 67.56           N  
ANISOU 1764  N   LEU A 211    10352   5427   9889   -833    575   2307       N  
ATOM   1765  CA  LEU A 211       8.242 -31.264 122.695  1.00 69.68           C  
ANISOU 1765  CA  LEU A 211    10677   5518  10282   -672    613   2386       C  
ATOM   1766  C   LEU A 211       8.872 -31.034 121.328  1.00 70.75           C  
ANISOU 1766  C   LEU A 211    10779   5621  10480   -629    555   2186       C  
ATOM   1767  O   LEU A 211      10.097 -31.077 121.182  1.00 59.13           O  
ANISOU 1767  O   LEU A 211     9298   4133   9034   -430    529   2218       O  
ATOM   1768  CB  LEU A 211       7.749 -32.707 122.836  1.00 69.24           C  
ANISOU 1768  CB  LEU A 211    10715   5205  10390   -779    779   2488       C  
ATOM   1769  CG  LEU A 211       8.705 -33.904 122.892  1.00 72.29           C  
ANISOU 1769  CG  LEU A 211    11186   5358  10921   -616    888   2627       C  
ATOM   1770  CD1 LEU A 211       9.086 -34.373 121.493  1.00 77.89           C  
ANISOU 1770  CD1 LEU A 211    11903   5901  11789   -628    931   2440       C  
ATOM   1771  CD2 LEU A 211       9.942 -33.604 123.723  1.00 60.51           C  
ANISOU 1771  CD2 LEU A 211     9676   3977   9339   -339    816   2808       C  
ATOM   1772  N   LEU A 212       8.046 -30.759 120.318  1.00 69.26           N  
ANISOU 1772  N   LEU A 212    10558   5440  10318   -812    536   1984       N  
ATOM   1773  CA  LEU A 212       8.554 -30.616 118.956  1.00 61.09           C  
ANISOU 1773  CA  LEU A 212     9500   4369   9342   -786    492   1797       C  
ATOM   1774  C   LEU A 212       9.326 -29.311 118.769  1.00 55.90           C  
ANISOU 1774  C   LEU A 212     8781   3919   8541   -638    367   1727       C  
ATOM   1775  O   LEU A 212      10.424 -29.310 118.185  1.00 51.88           O  
ANISOU 1775  O   LEU A 212     8248   3373   8092   -487    367   1695       O  
ATOM   1776  CB  LEU A 212       7.391 -30.718 117.968  1.00 57.95           C  
ANISOU 1776  CB  LEU A 212     9068   3931   9020  -1019    512   1614       C  
ATOM   1777  CG  LEU A 212       7.094 -32.162 117.550  1.00 65.84           C  
ANISOU 1777  CG  LEU A 212    10128   4664  10225  -1122    677   1596       C  
ATOM   1778  CD1 LEU A 212       5.999 -32.223 116.497  1.00 52.77           C  
ANISOU 1778  CD1 LEU A 212     8416   2987   8649  -1345    707   1378       C  
ATOM   1779  CD2 LEU A 212       8.362 -32.829 117.046  1.00 81.86           C  
ANISOU 1779  CD2 LEU A 212    12218   6529  12357   -944    745   1604       C  
ATOM   1780  N   THR A 213       8.762 -28.191 119.237  1.00 52.79           N  
ANISOU 1780  N   THR A 213     8340   3729   7990   -672    309   1703       N  
ATOM   1781  CA  THR A 213       9.503 -26.932 119.198  1.00 44.15           C  
ANISOU 1781  CA  THR A 213     7179   2823   6771   -517    232   1645       C  
ATOM   1782  C   THR A 213      10.805 -27.037 119.988  1.00 46.91           C  
ANISOU 1782  C   THR A 213     7501   3198   7126   -295    218   1799       C  
ATOM   1783  O   THR A 213      11.848 -26.546 119.534  1.00 45.60           O  
ANISOU 1783  O   THR A 213     7266   3085   6974   -155    179   1753       O  
ATOM   1784  CB  THR A 213       8.650 -25.772 119.725  1.00 44.02           C  
ANISOU 1784  CB  THR A 213     7096   3006   6624   -564    230   1614       C  
ATOM   1785  OG1 THR A 213       8.431 -25.922 121.133  1.00 79.02           O  
ANISOU 1785  OG1 THR A 213    11516   7489  11019   -536    263   1800       O  
ATOM   1786  CG2 THR A 213       7.309 -25.700 118.997  1.00 39.22           C  
ANISOU 1786  CG2 THR A 213     6478   2394   6029   -779    259   1469       C  
ATOM   1787  N   SER A 214      10.773 -27.704 121.147  1.00 52.56           N  
ANISOU 1787  N   SER A 214     8246   3872   7852   -259    261   2001       N  
ATOM   1788  CA  SER A 214      11.991 -27.941 121.916  1.00 51.21           C  
ANISOU 1788  CA  SER A 214     8042   3721   7695    -44    243   2174       C  
ATOM   1789  C   SER A 214      13.025 -28.700 121.095  1.00 58.37           C  
ANISOU 1789  C   SER A 214     8953   4459   8767     62    287   2165       C  
ATOM   1790  O   SER A 214      14.201 -28.307 121.024  1.00 58.02           O  
ANISOU 1790  O   SER A 214     8824   4490   8732    233    241   2178       O  
ATOM   1791  CB  SER A 214      11.642 -28.713 123.187  1.00 50.40           C  
ANISOU 1791  CB  SER A 214     7991   3570   7587    -37    304   2408       C  
ATOM   1792  OG  SER A 214      12.695 -29.573 123.583  1.00 57.06           O  
ANISOU 1792  OG  SER A 214     8852   4312   8515    143    333   2584       O  
ATOM   1793  N   LYS A 215      12.600 -29.797 120.467  1.00 67.03           N  
ANISOU 1793  N   LYS A 215    10138   5326  10005    -42    391   2139       N  
ATOM   1794  CA  LYS A 215      13.532 -30.631 119.721  1.00 72.44           C  
ANISOU 1794  CA  LYS A 215    10835   5826  10861     64    474   2136       C  
ATOM   1795  C   LYS A 215      14.196 -29.849 118.600  1.00 68.35           C  
ANISOU 1795  C   LYS A 215    10241   5387  10342    107    418   1951       C  
ATOM   1796  O   LYS A 215      15.423 -29.894 118.440  1.00 74.41           O  
ANISOU 1796  O   LYS A 215    10954   6148  11171    280    426   1988       O  
ATOM   1797  CB  LYS A 215      12.815 -31.851 119.153  1.00 83.63           C  
ANISOU 1797  CB  LYS A 215    12357   6987  12433    -82    616   2099       C  
ATOM   1798  CG  LYS A 215      12.605 -32.946 120.143  1.00 91.18           C  
ANISOU 1798  CG  LYS A 215    13399   7789  13456    -63    729   2316       C  
ATOM   1799  CD  LYS A 215      12.912 -34.270 119.500  1.00 87.57           C  
ANISOU 1799  CD  LYS A 215    13024   7036  13212    -42    912   2317       C  
ATOM   1800  CE  LYS A 215      13.251 -35.283 120.549  1.00 89.27           C  
ANISOU 1800  CE  LYS A 215    13315   7104  13498     89   1029   2583       C  
ATOM   1801  NZ  LYS A 215      12.008 -35.697 121.227  1.00100.54           N  
ANISOU 1801  NZ  LYS A 215    14821   8476  14903    -95   1088   2655       N  
ATOM   1802  N   ILE A 216      13.409 -29.114 117.807  1.00 48.72           N  
ANISOU 1802  N   ILE A 216     7747   2980   7784    -48    364   1760       N  
ATOM   1803  CA  ILE A 216      14.060 -28.462 116.670  1.00 44.91           C  
ANISOU 1803  CA  ILE A 216     7208   2551   7307     -4    329   1597       C  
ATOM   1804  C   ILE A 216      14.759 -27.169 117.065  1.00 51.69           C  
ANISOU 1804  C   ILE A 216     7962   3638   8042    115    230   1600       C  
ATOM   1805  O   ILE A 216      15.614 -26.696 116.312  1.00 68.96           O  
ANISOU 1805  O   ILE A 216    10091   5862  10251    191    216   1512       O  
ATOM   1806  CB  ILE A 216      13.133 -28.196 115.466  1.00 44.20           C  
ANISOU 1806  CB  ILE A 216     7145   2450   7200   -185    311   1391       C  
ATOM   1807  CG1 ILE A 216      12.123 -27.085 115.746  1.00 46.68           C  
ANISOU 1807  CG1 ILE A 216     7441   2954   7341   -294    213   1332       C  
ATOM   1808  CG2 ILE A 216      12.470 -29.493 114.995  1.00 63.23           C  
ANISOU 1808  CG2 ILE A 216     9637   4632   9757   -316    422   1362       C  
ATOM   1809  CD1 ILE A 216      11.659 -26.397 114.466  1.00 63.01           C  
ANISOU 1809  CD1 ILE A 216     9498   5077   9364   -391    159   1135       C  
ATOM   1810  N   TYR A 217      14.502 -26.621 118.259  1.00 47.39           N  
ANISOU 1810  N   TYR A 217     7384   3242   7380    140    174   1705       N  
ATOM   1811  CA  TYR A 217      15.383 -25.564 118.754  1.00 51.10           C  
ANISOU 1811  CA  TYR A 217     7734   3909   7771    277     97   1731       C  
ATOM   1812  C   TYR A 217      16.734 -26.123 119.188  1.00 61.55           C  
ANISOU 1812  C   TYR A 217     9004   5195   9188    468    107   1877       C  
ATOM   1813  O   TYR A 217      17.775 -25.481 118.984  1.00 74.60           O  
ANISOU 1813  O   TYR A 217    10554   6944  10847    576     65   1846       O  
ATOM   1814  CB  TYR A 217      14.706 -24.805 119.889  1.00 47.11           C  
ANISOU 1814  CB  TYR A 217     7197   3583   7120    250     42   1791       C  
ATOM   1815  CG  TYR A 217      13.935 -23.608 119.381  1.00 41.80           C  
ANISOU 1815  CG  TYR A 217     6496   3040   6347    147     16   1622       C  
ATOM   1816  CD1 TYR A 217      14.580 -22.591 118.690  1.00 33.39           C  
ANISOU 1816  CD1 TYR A 217     5347   2072   5269    195    -19   1503       C  
ATOM   1817  CD2 TYR A 217      12.562 -23.503 119.572  1.00 50.71           C  
ANISOU 1817  CD2 TYR A 217     7679   4186   7403      3     42   1589       C  
ATOM   1818  CE1 TYR A 217      13.884 -21.505 118.212  1.00 31.10           C  
ANISOU 1818  CE1 TYR A 217     5030   1889   4897    120    -28   1367       C  
ATOM   1819  CE2 TYR A 217      11.858 -22.416 119.095  1.00 46.01           C  
ANISOU 1819  CE2 TYR A 217     7042   3707   6731    -66     36   1448       C  
ATOM   1820  CZ  TYR A 217      12.526 -21.420 118.420  1.00 37.35           C  
ANISOU 1820  CZ  TYR A 217     5864   2702   5625      1     -1   1343       C  
ATOM   1821  OH  TYR A 217      11.841 -20.327 117.939  1.00 39.27           O  
ANISOU 1821  OH  TYR A 217     6060   3055   5808    -51      1   1222       O  
ATOM   1822  N   LYS A 218      16.744 -27.323 119.773  1.00 70.35           N  
ANISOU 1822  N   LYS A 218    10184   6164  10380    513    169   2043       N  
ATOM   1823  CA  LYS A 218      18.025 -27.985 120.028  1.00 81.64           C  
ANISOU 1823  CA  LYS A 218    11572   7532  11917    710    197   2185       C  
ATOM   1824  C   LYS A 218      18.751 -28.297 118.720  1.00 72.42           C  
ANISOU 1824  C   LYS A 218    10398   6231  10889    741    269   2062       C  
ATOM   1825  O   LYS A 218      19.989 -28.182 118.630  1.00 59.63           O  
ANISOU 1825  O   LYS A 218     8685   4646   9324    899    258   2095       O  
ATOM   1826  CB  LYS A 218      17.816 -29.264 120.843  1.00 87.61           C  
ANISOU 1826  CB  LYS A 218    12418   8134  12737    756    275   2396       C  
ATOM   1827  CG  LYS A 218      17.456 -29.017 122.298  1.00 94.46           C  
ANISOU 1827  CG  LYS A 218    13274   9154  13462    785    203   2569       C  
ATOM   1828  CD  LYS A 218      17.991 -30.118 123.216  1.00103.62           C  
ANISOU 1828  CD  LYS A 218    14468  10221  14681    951    255   2834       C  
ATOM   1829  CE  LYS A 218      19.494 -29.981 123.482  1.00107.14           C  
ANISOU 1829  CE  LYS A 218    14780  10773  15155   1196    195   2939       C  
ATOM   1830  NZ  LYS A 218      20.357 -30.192 122.280  1.00 99.83           N  
ANISOU 1830  NZ  LYS A 218    13824   9725  14383   1253    252   2816       N  
ATOM   1831  N   VAL A 219      17.991 -28.703 117.697  1.00 56.49           N  
ANISOU 1831  N   VAL A 219     8473   4065   8927    588    344   1918       N  
ATOM   1832  CA  VAL A 219      18.560 -28.894 116.366  1.00 50.04           C  
ANISOU 1832  CA  VAL A 219     7654   3141   8217    595    413   1774       C  
ATOM   1833  C   VAL A 219      19.169 -27.593 115.868  1.00 63.28           C  
ANISOU 1833  C   VAL A 219     9224   5004   9816    622    328   1651       C  
ATOM   1834  O   VAL A 219      20.275 -27.578 115.325  1.00 69.18           O  
ANISOU 1834  O   VAL A 219     9911   5731  10644    730    362   1625       O  
ATOM   1835  CB  VAL A 219      17.487 -29.420 115.397  1.00 58.07           C  
ANISOU 1835  CB  VAL A 219     8780   4007   9276    406    485   1628       C  
ATOM   1836  CG1 VAL A 219      17.909 -29.182 113.950  1.00 58.39           C  
ANISOU 1836  CG1 VAL A 219     8806   4017   9362    385    520   1438       C  
ATOM   1837  CG2 VAL A 219      17.241 -30.895 115.651  1.00 73.91           C  
ANISOU 1837  CG2 VAL A 219    10889   5771  11425    403    624   1737       C  
ATOM   1838  N   LEU A 220      18.463 -26.478 116.059  1.00 64.92           N  
ANISOU 1838  N   LEU A 220     9408   5386   9872    526    232   1577       N  
ATOM   1839  CA  LEU A 220      19.015 -25.182 115.682  1.00 63.40           C  
ANISOU 1839  CA  LEU A 220     9118   5364   9607    551    166   1472       C  
ATOM   1840  C   LEU A 220      20.351 -24.932 116.368  1.00 62.54           C  
ANISOU 1840  C   LEU A 220     8886   5345   9531    729    132   1585       C  
ATOM   1841  O   LEU A 220      21.339 -24.600 115.703  1.00 67.68           O  
ANISOU 1841  O   LEU A 220     9468   6007  10240    796    150   1520       O  
ATOM   1842  CB  LEU A 220      18.015 -24.072 116.010  1.00 57.17           C  
ANISOU 1842  CB  LEU A 220     8324   4741   8657    442     87   1409       C  
ATOM   1843  CG  LEU A 220      16.850 -23.987 115.023  1.00 54.93           C  
ANISOU 1843  CG  LEU A 220     8133   4409   8328    275    100   1256       C  
ATOM   1844  CD1 LEU A 220      15.835 -22.913 115.425  1.00 60.06           C  
ANISOU 1844  CD1 LEU A 220     8775   5220   8824    190     41   1211       C  
ATOM   1845  CD2 LEU A 220      17.368 -23.762 113.611  1.00 53.07           C  
ANISOU 1845  CD2 LEU A 220     7895   4133   8138    271    126   1111       C  
ATOM   1846  N   GLU A 221      20.414 -25.133 117.688  1.00 67.98           N  
ANISOU 1846  N   GLU A 221     9544   6101  10184    811     83   1761       N  
ATOM   1847  CA  GLU A 221      21.643 -24.813 118.413  1.00 75.32           C  
ANISOU 1847  CA  GLU A 221    10340   7155  11123    986     20   1871       C  
ATOM   1848  C   GLU A 221      22.822 -25.644 117.921  1.00 76.91           C  
ANISOU 1848  C   GLU A 221    10512   7225  11485   1130     93   1918       C  
ATOM   1849  O   GLU A 221      23.880 -25.094 117.590  1.00 88.62           O  
ANISOU 1849  O   GLU A 221    11880   8779  13010   1217     76   1875       O  
ATOM   1850  CB  GLU A 221      21.466 -24.992 119.919  1.00 83.09           C  
ANISOU 1850  CB  GLU A 221    11291   8242  12038   1060    -45   2077       C  
ATOM   1851  CG  GLU A 221      22.767 -24.775 120.726  1.00100.39           C  
ANISOU 1851  CG  GLU A 221    13291  10583  14270   1265   -108   2243       C  
ATOM   1852  CD  GLU A 221      23.517 -23.489 120.365  1.00116.26           C  
ANISOU 1852  CD  GLU A 221    15135  12751  16285   1277   -163   2134       C  
ATOM   1853  OE1 GLU A 221      23.783 -22.684 121.280  1.00121.10           O  
ANISOU 1853  OE1 GLU A 221    15594  13585  16833   1325   -266   2218       O  
ATOM   1854  OE2 GLU A 221      23.882 -23.289 119.188  1.00123.56           O1-
ANISOU 1854  OE2 GLU A 221    16078  13588  17283   1238   -103   1973       O1-
ATOM   1855  N   GLU A 222      22.671 -26.967 117.851  1.00 70.68           N  
ANISOU 1855  N   GLU A 222     9820   6233  10803   1161    192   2008       N  
ATOM   1856  CA  GLU A 222      23.852 -27.764 117.516  1.00 83.72           C  
ANISOU 1856  CA  GLU A 222    11433   7764  12612   1328    272   2075       C  
ATOM   1857  C   GLU A 222      24.114 -27.777 116.000  1.00 85.30           C  
ANISOU 1857  C   GLU A 222    11659   7845  12907   1264    373   1883       C  
ATOM   1858  O   GLU A 222      25.253 -27.605 115.553  1.00 90.76           O  
ANISOU 1858  O   GLU A 222    12258   8551  13676   1375    394   1856       O  
ATOM   1859  CB  GLU A 222      23.733 -29.184 118.059  1.00 99.73           C  
ANISOU 1859  CB  GLU A 222    13550   9608  14733   1415    360   2263       C  
ATOM   1860  CG  GLU A 222      24.750 -29.418 119.184  1.00114.79           C  
ANISOU 1860  CG  GLU A 222    15350  11615  16648   1653    295   2490       C  
ATOM   1861  CD  GLU A 222      24.894 -30.848 119.680  1.00122.85           C  
ANISOU 1861  CD  GLU A 222    16450  12446  17781   1790    400   2704       C  
ATOM   1862  OE1 GLU A 222      24.353 -31.794 119.072  1.00125.51           O  
ANISOU 1862  OE1 GLU A 222    16926  12534  18229   1713    553   2674       O  
ATOM   1863  OE2 GLU A 222      25.579 -31.009 120.705  1.00124.14           O1-
ANISOU 1863  OE2 GLU A 222    16517  12719  17932   1990    344   2923       O1-
ATOM   1864  N   LYS A 223      23.074 -27.968 115.181  1.00 81.45           N  
ANISOU 1864  N   LYS A 223    11292   7250  12407   1086    433   1746       N  
ATOM   1865  CA  LYS A 223      23.247 -27.967 113.730  1.00 84.53           C  
ANISOU 1865  CA  LYS A 223    11711   7546  12860   1020    521   1563       C  
ATOM   1866  C   LYS A 223      23.670 -26.590 113.228  1.00 86.29           C  
ANISOU 1866  C   LYS A 223    11839   7947  12999    991    449   1431       C  
ATOM   1867  O   LYS A 223      24.771 -26.436 112.697  1.00 78.48           O  
ANISOU 1867  O   LYS A 223    10775   6955  12088   1083    493   1396       O  
ATOM   1868  CB  LYS A 223      21.941 -28.462 113.092  1.00 93.66           C  
ANISOU 1868  CB  LYS A 223    13008   8577  14003    837    575   1456       C  
ATOM   1869  CG  LYS A 223      21.679 -28.249 111.584  1.00 92.87           C  
ANISOU 1869  CG  LYS A 223    12954   8429  13901    716    629   1240       C  
ATOM   1870  CD  LYS A 223      22.877 -28.061 110.655  1.00 86.15           C  
ANISOU 1870  CD  LYS A 223    12043   7564  13126    803    700   1161       C  
ATOM   1871  CE  LYS A 223      23.787 -29.272 110.529  1.00 83.22           C  
ANISOU 1871  CE  LYS A 223    11685   6996  12940    942    848   1238       C  
ATOM   1872  NZ  LYS A 223      24.696 -29.123 109.345  1.00 73.41           N  
ANISOU 1872  NZ  LYS A 223    10410   5719  11763    978    941   1113       N  
ATOM   1873  N   TYR A 224      22.825 -25.571 113.389  1.00 97.53           N  
ANISOU 1873  N   TYR A 224    13266   9519  14272    868    351   1360       N  
ATOM   1874  CA  TYR A 224      23.052 -24.342 112.642  1.00 94.34           C  
ANISOU 1874  CA  TYR A 224    12810   9237  13800    814    320   1212       C  
ATOM   1875  C   TYR A 224      23.960 -23.364 113.391  1.00106.98           C  
ANISOU 1875  C   TYR A 224    14268  11010  15372    911    242   1266       C  
ATOM   1876  O   TYR A 224      24.463 -23.637 114.484  1.00 91.44           O  
ANISOU 1876  O   TYR A 224    12229   9087  13428   1035    195   1420       O  
ATOM   1877  CB  TYR A 224      21.723 -23.685 112.272  1.00 67.19           C  
ANISOU 1877  CB  TYR A 224     9447   5860  10222    644    268   1097       C  
ATOM   1878  CG  TYR A 224      21.109 -24.310 111.049  1.00 72.89           C  
ANISOU 1878  CG  TYR A 224    10278   6441  10976    544    340    978       C  
ATOM   1879  CD1 TYR A 224      21.464 -23.881 109.781  1.00 60.20           C  
ANISOU 1879  CD1 TYR A 224     8671   4829   9371    518    383    839       C  
ATOM   1880  CD2 TYR A 224      20.178 -25.327 111.158  1.00 91.58           C  
ANISOU 1880  CD2 TYR A 224    12745   8679  13373    472    370   1004       C  
ATOM   1881  CE1 TYR A 224      20.913 -24.454 108.651  1.00 77.01           C  
ANISOU 1881  CE1 TYR A 224    10894   6840  11525    431    446    727       C  
ATOM   1882  CE2 TYR A 224      19.622 -25.908 110.035  1.00 95.88           C  
ANISOU 1882  CE2 TYR A 224    13379   9096  13956    373    437    884       C  
ATOM   1883  CZ  TYR A 224      19.991 -25.467 108.783  1.00 90.26           C  
ANISOU 1883  CZ  TYR A 224    12663   8394  13238    357    470    744       C  
ATOM   1884  OH  TYR A 224      19.432 -26.046 107.668  1.00 94.54           O  
ANISOU 1884  OH  TYR A 224    13292   8818  13812    262    536    619       O  
ATOM   1885  N   LYS A 225      24.149 -22.193 112.778  1.00139.40           N  
ANISOU 1885  N   LYS A 225    18330  15213  19422    855    226   1139       N  
ATOM   1886  CA  LYS A 225      25.150 -21.227 113.213  1.00147.73           C  
ANISOU 1886  CA  LYS A 225    19245  16404  20482    933    178   1152       C  
ATOM   1887  C   LYS A 225      24.849 -20.712 114.611  1.00151.40           C  
ANISOU 1887  C   LYS A 225    19633  17016  20876    957     73   1266       C  
ATOM   1888  O   LYS A 225      23.777 -20.152 114.861  1.00147.98           O  
ANISOU 1888  O   LYS A 225    19267  16654  20306    845     20   1221       O  
ATOM   1889  CB  LYS A 225      25.209 -20.058 112.229  1.00142.10           C  
ANISOU 1889  CB  LYS A 225    18527  15741  19723    840    202    990       C  
ATOM   1890  CG  LYS A 225      25.469 -20.452 110.784  1.00136.26           C  
ANISOU 1890  CG  LYS A 225    17847  14877  19048    811    315    882       C  
ATOM   1891  CD  LYS A 225      25.560 -19.225 109.881  1.00128.92           C  
ANISOU 1891  CD  LYS A 225    16912  14011  18060    731    338    745       C  
ATOM   1892  CE  LYS A 225      26.311 -19.548 108.600  1.00120.52           C  
ANISOU 1892  CE  LYS A 225    15861  12846  17086    748    463    662       C  
ATOM   1893  NZ  LYS A 225      26.756 -18.326 107.880  1.00108.35           N  
ANISOU 1893  NZ  LYS A 225    14286  11369  15514    702    502    560       N  
ATOM   1894  N   THR A 226      25.805 -20.899 115.520  1.00147.90           N  
ANISOU 1894  N   THR A 226    19023  16628  20545   1114     49   1429       N  
ATOM   1895  CA  THR A 226      25.742 -20.287 116.840  1.00142.25           C  
ANISOU 1895  CA  THR A 226    18170  16087  19790   1154    -59   1559       C  
ATOM   1896  C   THR A 226      25.752 -18.820 116.435  1.00133.84           C  
ANISOU 1896  C   THR A 226    17003  15137  18712   1071    -89   1456       C  
ATOM   1897  O   THR A 226      26.754 -18.316 115.916  1.00122.86           O  
ANISOU 1897  O   THR A 226    15433  13797  17450   1141    -84   1458       O  
ATOM   1898  CB  THR A 226      26.881 -20.800 117.720  1.00140.24           C  
ANISOU 1898  CB  THR A 226    17735  15906  19646   1363    -99   1757       C  
ATOM   1899  OG1 THR A 226      28.085 -20.092 117.406  1.00143.20           O  
ANISOU 1899  OG1 THR A 226    17911  16349  20151   1437    -90   1724       O  
ATOM   1900  CG2 THR A 226      27.102 -22.288 117.481  1.00132.70           C  
ANISOU 1900  CG2 THR A 226    16884  14777  18760   1461    -22   1831       C  
ATOM   1901  N   SER A 227      24.646 -18.122 116.683  1.00139.63           N  
ANISOU 1901  N   SER A 227    17840  15906  19305    926   -115   1368       N  
ATOM   1902  CA  SER A 227      24.553 -16.726 116.274  1.00140.89           C  
ANISOU 1902  CA  SER A 227    17963  16122  19448    827   -114   1239       C  
ATOM   1903  C   SER A 227      25.099 -15.758 117.319  1.00141.39           C  
ANISOU 1903  C   SER A 227    17794  16335  19591    870   -209   1334       C  
ATOM   1904  O   SER A 227      24.510 -14.696 117.546  1.00143.74           O  
ANISOU 1904  O   SER A 227    18082  16695  19837    772   -250   1279       O  
ATOM   1905  CB  SER A 227      23.096 -16.381 115.954  1.00136.87           C  
ANISOU 1905  CB  SER A 227    17634  15615  18757    683   -115   1127       C  
ATOM   1906  OG  SER A 227      22.690 -16.962 114.726  1.00131.11           O  
ANISOU 1906  OG  SER A 227    17086  14773  17956    629    -50   1005       O  
ATOM   1907  N   GLY A 228      26.226 -16.100 117.942  1.00133.08           N  
ANISOU 1907  N   GLY A 228    16543  15358  18663   1024   -258   1474       N  
ATOM   1908  CA  GLY A 228      26.849 -15.245 118.935  1.00121.51           C  
ANISOU 1908  CA  GLY A 228    14809  14097  17262   1082   -389   1563       C  
ATOM   1909  C   GLY A 228      25.909 -14.853 120.059  1.00114.89           C  
ANISOU 1909  C   GLY A 228    13966  13422  16265   1022   -518   1644       C  
ATOM   1910  O   GLY A 228      25.352 -15.716 120.743  1.00124.56           O  
ANISOU 1910  O   GLY A 228    15279  14689  17360   1056   -550   1762       O  
ATOM   1911  N   SER A 229      25.733 -13.546 120.252  1.00 89.88           N  
ANISOU 1911  N   SER A 229    10695  10334  13120    930   -585   1575       N  
ATOM   1912  CA  SER A 229      24.774 -12.970 121.192  1.00 60.19           C  
ANISOU 1912  CA  SER A 229     6937   6725   9208    845   -702   1620       C  
ATOM   1913  C   SER A 229      24.775 -11.461 120.994  1.00 57.15           C  
ANISOU 1913  C   SER A 229     6492   6394   8828    693   -693   1399       C  
ATOM   1914  O   SER A 229      25.850 -10.868 120.888  1.00 75.77           O  
ANISOU 1914  O   SER A 229     8672   8869  11248    675   -672   1251       O  
ATOM   1915  CB  SER A 229      25.120 -13.329 122.639  1.00 55.03           C  
ANISOU 1915  CB  SER A 229     6092   6401   8415    946   -868   1796       C  
ATOM   1916  OG  SER A 229      24.748 -12.292 123.528  1.00 37.99           O  
ANISOU 1916  OG  SER A 229     3823   4511   6099    831   -988   1731       O  
ATOM   1917  N   LEU A 230      23.598 -10.829 120.955  1.00 48.65           N  
ANISOU 1917  N   LEU A 230     5578   5262   7645    557   -671   1319       N  
ATOM   1918  CA  LEU A 230      23.516  -9.446 120.482  1.00 40.87           C  
ANISOU 1918  CA  LEU A 230     4626   4253   6650    403   -580   1061       C  
ATOM   1919  C   LEU A 230      24.422  -8.516 121.286  1.00 50.26           C  
ANISOU 1919  C   LEU A 230     5574   5745   7777    326   -629    900       C  
ATOM   1920  O   LEU A 230      25.153  -7.694 120.713  1.00 51.63           O  
ANISOU 1920  O   LEU A 230     5692   5877   8046    248   -521    700       O  
ATOM   1921  CB  LEU A 230      22.065  -8.959 120.513  1.00 25.35           C  
ANISOU 1921  CB  LEU A 230     2845   2225   4563    304   -567   1031       C  
ATOM   1922  CG  LEU A 230      21.888  -7.554 119.930  1.00 35.88           C  
ANISOU 1922  CG  LEU A 230     4252   3482   5897    177   -446    795       C  
ATOM   1923  CD1 LEU A 230      22.383  -7.508 118.495  1.00 24.80           C  
ANISOU 1923  CD1 LEU A 230     2952   1810   4661    202   -296    725       C  
ATOM   1924  CD2 LEU A 230      20.443  -7.086 120.011  1.00 27.83           C  
ANISOU 1924  CD2 LEU A 230     3392   2425   4758    113   -439    780       C  
ATOM   1925  N   TYR A 231      24.389  -8.634 122.618  1.00 51.75           N  
ANISOU 1925  N   TYR A 231     5615   6249   7797    333   -783    975       N  
ATOM   1926  CA  TYR A 231      25.225  -7.780 123.458  1.00 48.54           C  
ANISOU 1926  CA  TYR A 231     4961   6177   7304    242   -845    799       C  
ATOM   1927  C   TYR A 231      26.703  -8.012 123.179  1.00 52.26           C  
ANISOU 1927  C   TYR A 231     5209   6728   7918    317   -843    762       C  
ATOM   1928  O   TYR A 231      27.475  -7.057 123.071  1.00 34.10           O  
ANISOU 1928  O   TYR A 231     2767   4525   5664    190   -779    516       O  
ATOM   1929  CB  TYR A 231      24.911  -8.018 124.936  1.00 32.96           C  
ANISOU 1929  CB  TYR A 231     2875   4553   5095    259  -1023    913       C  
ATOM   1930  CG  TYR A 231      25.871  -7.346 125.898  1.00 50.92           C  
ANISOU 1930  CG  TYR A 231     4857   7238   7253    181  -1121    745       C  
ATOM   1931  CD1 TYR A 231      25.842  -5.968 126.089  1.00 49.01           C  
ANISOU 1931  CD1 TYR A 231     4580   7086   6956    -36  -1052    436       C  
ATOM   1932  CD2 TYR A 231      26.806  -8.089 126.615  1.00 63.39           C  
ANISOU 1932  CD2 TYR A 231     6189   9120   8774    328  -1279    890       C  
ATOM   1933  CE1 TYR A 231      26.716  -5.348 126.969  1.00 60.39           C  
ANISOU 1933  CE1 TYR A 231     5743   8915   8286   -138  -1136    245       C  
ATOM   1934  CE2 TYR A 231      27.686  -7.478 127.498  1.00 71.40           C  
ANISOU 1934  CE2 TYR A 231     6909  10559   9661    250  -1386    718       C  
ATOM   1935  CZ  TYR A 231      27.635  -6.108 127.669  1.00 69.88           C  
ANISOU 1935  CZ  TYR A 231     6682  10455   9414      0  -1314    381       C  
ATOM   1936  OH  TYR A 231      28.503  -5.488 128.540  1.00 77.56           O  
ANISOU 1936  OH  TYR A 231     7354  11857  10257   -109  -1413    171       O  
ATOM   1937  N   THR A 232      27.110  -9.274 123.040  1.00 50.24           N  
ANISOU 1937  N   THR A 232     4920   6422   7747    521   -892    999       N  
ATOM   1938  CA  THR A 232      28.509  -9.582 122.755  1.00 62.89           C  
ANISOU 1938  CA  THR A 232     6295   8101   9498    625   -886    983       C  
ATOM   1939  C   THR A 232      28.934  -9.023 121.400  1.00 60.61           C  
ANISOU 1939  C   THR A 232     6084   7528   9417    541   -680    784       C  
ATOM   1940  O   THR A 232      29.997  -8.399 121.277  1.00 55.65           O  
ANISOU 1940  O   THR A 232     5246   7030   8868    471   -632    590       O  
ATOM   1941  CB  THR A 232      28.728 -11.096 122.805  1.00 57.70           C  
ANISOU 1941  CB  THR A 232     5632   7384   8909    885   -948   1299       C  
ATOM   1942  OG1 THR A 232      27.878 -11.668 123.806  1.00 56.81           O  
ANISOU 1942  OG1 THR A 232     5588   7390   8607    947  -1079   1521       O  
ATOM   1943  CG2 THR A 232      30.181 -11.414 123.130  1.00 57.22           C  
ANISOU 1943  CG2 THR A 232     5239   7590   8913   1029  -1025   1323       C  
ATOM   1944  N   CYS A 233      28.116  -9.253 120.369  1.00 55.29           N  
ANISOU 1944  N   CYS A 233     5706   6478   8824    543   -551    827       N  
ATOM   1945  CA  CYS A 233      28.419  -8.782 119.024  1.00 53.13           C  
ANISOU 1945  CA  CYS A 233     5547   5923   8718    480   -347    668       C  
ATOM   1946  C   CYS A 233      28.593  -7.271 119.014  1.00 51.08           C  
ANISOU 1946  C   CYS A 233     5246   5734   8429    265   -254    386       C  
ATOM   1947  O   CYS A 233      29.596  -6.747 118.514  1.00 63.02           O  
ANISOU 1947  O   CYS A 233     6636   7239  10070    202   -133    215       O  
ATOM   1948  CB  CYS A 233      27.305  -9.194 118.057  1.00 39.44           C  
ANISOU 1948  CB  CYS A 233     4144   3834   7008    501   -254    755       C  
ATOM   1949  SG  CYS A 233      27.082 -10.967 117.804  1.00 48.56           S  
ANISOU 1949  SG  CYS A 233     5398   4805   8246    717   -290   1041       S  
ATOM   1950  N   TRP A 234      27.617  -6.554 119.579  1.00 52.25           N  
ANISOU 1950  N   TRP A 234     5496   5940   8417    147   -291    331       N  
ATOM   1951  CA  TRP A 234      27.696  -5.098 119.600  1.00 47.75           C  
ANISOU 1951  CA  TRP A 234     4917   5398   7826    -57   -176     63       C  
ATOM   1952  C   TRP A 234      28.879  -4.619 120.434  1.00 57.79           C  
ANISOU 1952  C   TRP A 234     5854   7012   9091   -149   -232   -109       C  
ATOM   1953  O   TRP A 234      29.604  -3.704 120.023  1.00 58.85           O  
ANISOU 1953  O   TRP A 234     5917   7113   9330   -293    -75   -344       O  
ATOM   1954  CB  TRP A 234      26.391  -4.505 120.129  1.00 38.49           C  
ANISOU 1954  CB  TRP A 234     3908   4232   6485   -139   -207     49       C  
ATOM   1955  CG  TRP A 234      26.396  -3.010 120.142  1.00 48.34           C  
ANISOU 1955  CG  TRP A 234     5179   5463   7724   -336    -61   -219       C  
ATOM   1956  CD1 TRP A 234      26.495  -2.200 121.233  1.00 45.08           C  
ANISOU 1956  CD1 TRP A 234     4618   5315   7196   -482   -106   -392       C  
ATOM   1957  CD2 TRP A 234      26.310  -2.142 119.003  1.00 44.59           C  
ANISOU 1957  CD2 TRP A 234     4900   4680   7363   -407    176   -346       C  
ATOM   1958  NE1 TRP A 234      26.473  -0.882 120.847  1.00 37.83           N  
ANISOU 1958  NE1 TRP A 234     3796   4245   6334   -647    102   -628       N  
ATOM   1959  CE2 TRP A 234      26.360  -0.820 119.483  1.00 42.90           C  
ANISOU 1959  CE2 TRP A 234     4653   4531   7115   -594    279   -588       C  
ATOM   1960  CE3 TRP A 234      26.189  -2.355 117.626  1.00 33.67           C  
ANISOU 1960  CE3 TRP A 234     3725   2974   6095   -329    319   -278       C  
ATOM   1961  CZ2 TRP A 234      26.292   0.285 118.637  1.00 42.88           C  
ANISOU 1961  CZ2 TRP A 234     4831   4257   7205   -691    531   -738       C  
ATOM   1962  CZ3 TRP A 234      26.125  -1.254 116.785  1.00 38.33           C  
ANISOU 1962  CZ3 TRP A 234     4486   3328   6750   -420    551   -421       C  
ATOM   1963  CH2 TRP A 234      26.174   0.046 117.294  1.00 41.42           C  
ANISOU 1963  CH2 TRP A 234     4851   3766   7120   -592    661   -637       C  
ATOM   1964  N   SER A 235      29.097  -5.232 121.601  1.00 60.19           N  
ANISOU 1964  N   SER A 235     5946   7656   9266    -70   -448      3       N  
ATOM   1965  CA  SER A 235      30.212  -4.869 122.466  1.00 52.45           C  
ANISOU 1965  CA  SER A 235     4613   7069   8245   -144   -539   -154       C  
ATOM   1966  C   SER A 235      31.532  -4.938 121.710  1.00 46.87           C  
ANISOU 1966  C   SER A 235     3725   6331   7753   -125   -434   -250       C  
ATOM   1967  O   SER A 235      32.278  -3.953 121.622  1.00 45.51           O  
ANISOU 1967  O   SER A 235     3403   6239   7650   -315   -319   -533       O  
ATOM   1968  CB  SER A 235      30.228  -5.803 123.681  1.00 59.18           C  
ANISOU 1968  CB  SER A 235     5291   8275   8920     12   -798     65       C  
ATOM   1969  OG  SER A 235      30.838  -5.199 124.805  1.00 75.29           O  
ANISOU 1969  OG  SER A 235     7036  10760  10810   -108   -920   -115       O  
ATOM   1970  N   GLU A 236      31.824  -6.107 121.138  1.00 46.89           N  
ANISOU 1970  N   GLU A 236     3743   6199   7875     98   -449    -26       N  
ATOM   1971  CA  GLU A 236      33.125  -6.315 120.519  1.00 46.98           C  
ANISOU 1971  CA  GLU A 236     3545   6219   8087    150   -363    -95       C  
ATOM   1972  C   GLU A 236      33.265  -5.532 119.219  1.00 50.01           C  
ANISOU 1972  C   GLU A 236     4099   6257   8645      6    -81   -289       C  
ATOM   1973  O   GLU A 236      34.354  -5.021 118.921  1.00 58.37           O  
ANISOU 1973  O   GLU A 236     4949   7391   9836    -94     34   -493       O  
ATOM   1974  CB  GLU A 236      33.362  -7.811 120.313  1.00 41.12           C  
ANISOU 1974  CB  GLU A 236     2784   5414   7425    444   -442    206       C  
ATOM   1975  CG  GLU A 236      33.610  -8.550 121.635  1.00 73.66           C  
ANISOU 1975  CG  GLU A 236     6658   9937  11391    609   -706    396       C  
ATOM   1976  CD  GLU A 236      33.496 -10.062 121.519  1.00 88.24           C  
ANISOU 1976  CD  GLU A 236     8581  11650  13295    910   -768    743       C  
ATOM   1977  OE1 GLU A 236      33.024 -10.551 120.472  1.00 84.62           O  
ANISOU 1977  OE1 GLU A 236     8399  10779  12974    966   -618    826       O  
ATOM   1978  OE2 GLU A 236      33.871 -10.761 122.487  1.00 93.13           O1-
ANISOU 1978  OE2 GLU A 236     8990  12579  13817   1092   -959    934       O1-
ATOM   1979  N   PHE A 237      32.178  -5.377 118.457  1.00 48.71           N  
ANISOU 1979  N   PHE A 237     4302   5734   8472    -13     36   -235       N  
ATOM   1980  CA  PHE A 237      32.249  -4.555 117.256  1.00 51.69           C  
ANISOU 1980  CA  PHE A 237     4864   5798   8978   -141    306   -402       C  
ATOM   1981  C   PHE A 237      32.577  -3.109 117.602  1.00 49.26           C  
ANISOU 1981  C   PHE A 237     4460   5599   8657   -402    417   -701       C  
ATOM   1982  O   PHE A 237      33.471  -2.504 116.999  1.00 59.56           O  
ANISOU 1982  O   PHE A 237     5679   6838  10114   -521    614   -894       O  
ATOM   1983  CB  PHE A 237      30.936  -4.636 116.476  1.00 49.25           C  
ANISOU 1983  CB  PHE A 237     4952   5143   8619    -99    379   -278       C  
ATOM   1984  CG  PHE A 237      30.907  -3.755 115.257  1.00 55.28           C  
ANISOU 1984  CG  PHE A 237     5934   5596   9475   -208    651   -418       C  
ATOM   1985  CD1 PHE A 237      31.473  -4.179 114.065  1.00 62.17           C  
ANISOU 1985  CD1 PHE A 237     6873   6249  10499   -133    811   -396       C  
ATOM   1986  CD2 PHE A 237      30.321  -2.498 115.305  1.00 47.28           C  
ANISOU 1986  CD2 PHE A 237     5066   4505   8392   -374    762   -565       C  
ATOM   1987  CE1 PHE A 237      31.452  -3.368 112.943  1.00 59.78           C  
ANISOU 1987  CE1 PHE A 237     6784   5672  10257   -225   1070   -506       C  
ATOM   1988  CE2 PHE A 237      30.300  -1.683 114.188  1.00 48.07           C  
ANISOU 1988  CE2 PHE A 237     5383   4313   8570   -451   1026   -663       C  
ATOM   1989  CZ  PHE A 237      30.865  -2.120 113.006  1.00 50.66           C  
ANISOU 1989  CZ  PHE A 237     5780   4441   9029   -377   1176   -628       C  
ATOM   1990  N   THR A 238      31.861  -2.536 118.574  1.00 51.41           N  
ANISOU 1990  N   THR A 238     4749   6029   8756   -504    313   -756       N  
ATOM   1991  CA  THR A 238      32.101  -1.144 118.934  1.00 51.53           C  
ANISOU 1991  CA  THR A 238     4696   6120   8762   -766    440  -1060       C  
ATOM   1992  C   THR A 238      33.471  -0.951 119.564  1.00 57.08           C  
ANISOU 1992  C   THR A 238     4986   7184   9517   -877    395  -1264       C  
ATOM   1993  O   THR A 238      34.068   0.122 119.419  1.00 68.63           O  
ANISOU 1993  O   THR A 238     6371   8633  11073  -1109    588  -1553       O  
ATOM   1994  CB  THR A 238      31.012  -0.648 119.883  1.00 55.40           C  
ANISOU 1994  CB  THR A 238     5291   6710   9049   -837    339  -1075       C  
ATOM   1995  OG1 THR A 238      30.778  -1.630 120.901  1.00 63.36           O  
ANISOU 1995  OG1 THR A 238     6158   8019   9896   -691     51   -881       O  
ATOM   1996  CG2 THR A 238      29.727  -0.393 119.117  1.00 34.93           C  
ANISOU 1996  CG2 THR A 238     3096   3742   6436   -792    460   -968       C  
ATOM   1997  N   GLN A 239      33.986  -1.963 120.266  1.00 73.52           N  
ANISOU 1997  N   GLN A 239     6796   9595  11542   -715    151  -1122       N  
ATOM   1998  CA  GLN A 239      35.332  -1.833 120.813  1.00 82.62           C  
ANISOU 1998  CA  GLN A 239     7520  11131  12742   -797     92  -1310       C  
ATOM   1999  C   GLN A 239      36.383  -1.853 119.711  1.00 76.58           C  
ANISOU 1999  C   GLN A 239     6666  10200  12231   -804    302  -1398       C  
ATOM   2000  O   GLN A 239      37.309  -1.033 119.718  1.00 89.50           O  
ANISOU 2000  O   GLN A 239     8074  11965  13966  -1022    432  -1694       O  
ATOM   2001  CB  GLN A 239      35.608  -2.938 121.826  1.00 88.55           C  
ANISOU 2001  CB  GLN A 239     8005  12287  13354   -580   -225  -1099       C  
ATOM   2002  CG  GLN A 239      35.013  -2.678 123.189  1.00 83.48           C  
ANISOU 2002  CG  GLN A 239     7301  11977  12441   -647   -432  -1120       C  
ATOM   2003  CD  GLN A 239      34.680  -3.960 123.906  1.00 86.62           C  
ANISOU 2003  CD  GLN A 239     7659  12572  12682   -363   -703   -770       C  
ATOM   2004  OE1 GLN A 239      33.551  -4.166 124.348  1.00 93.16           O  
ANISOU 2004  OE1 GLN A 239     8710  13341  13345   -316   -787   -610       O  
ATOM   2005  NE2 GLN A 239      35.665  -4.841 124.022  1.00 90.35           N  
ANISOU 2005  NE2 GLN A 239     7844  13274  13212   -165   -826   -640       N  
ATOM   2006  N   LYS A 240      36.258  -2.777 118.754  1.00 68.34           N  
ANISOU 2006  N   LYS A 240     5798   8871  11297   -583    353  -1160       N  
ATOM   2007  CA  LYS A 240      37.275  -2.893 117.716  1.00 62.70           C  
ANISOU 2007  CA  LYS A 240     4993   8014  10817   -569    554  -1231       C  
ATOM   2008  C   LYS A 240      37.170  -1.796 116.663  1.00 69.11           C  
ANISOU 2008  C   LYS A 240     6056   8455  11746   -783    891  -1426       C  
ATOM   2009  O   LYS A 240      38.170  -1.495 116.003  1.00 79.79           O  
ANISOU 2009  O   LYS A 240     7274   9760  13284   -874   1095  -1589       O  
ATOM   2010  CB  LYS A 240      37.192  -4.266 117.048  1.00 45.10           C  
ANISOU 2010  CB  LYS A 240     2874   5599   8664   -264    512   -929       C  
ATOM   2011  CG  LYS A 240      36.089  -4.395 116.009  1.00 50.79           C  
ANISOU 2011  CG  LYS A 240     4060   5856   9384   -211    652   -789       C  
ATOM   2012  CD  LYS A 240      36.083  -5.775 115.351  1.00 51.83           C  
ANISOU 2012  CD  LYS A 240     4283   5811   9600     64    629   -531       C  
ATOM   2013  CE  LYS A 240      35.742  -6.884 116.342  1.00 56.33           C  
ANISOU 2013  CE  LYS A 240     4759   6590  10053    280    343   -275       C  
ATOM   2014  NZ  LYS A 240      35.385  -8.152 115.649  1.00 61.77           N  
ANISOU 2014  NZ  LYS A 240     5648   7009  10813    517    356    -25       N  
ATOM   2015  N   THR A 241      36.000  -1.180 116.502  1.00 64.17           N  
ANISOU 2015  N   THR A 241     5786   7578  11019   -856    964  -1409       N  
ATOM   2016  CA  THR A 241      35.760  -0.227 115.422  1.00 68.55           C  
ANISOU 2016  CA  THR A 241     6638   7741  11667  -1000   1287  -1525       C  
ATOM   2017  C   THR A 241      36.021   1.191 115.922  1.00 70.99           C  
ANISOU 2017  C   THR A 241     6862   8127  11984  -1309   1434  -1845       C  
ATOM   2018  O   THR A 241      35.282   1.709 116.765  1.00 51.70           O  
ANISOU 2018  O   THR A 241     4477   5777   9390  -1394   1339  -1895       O  
ATOM   2019  CB  THR A 241      34.334  -0.374 114.897  1.00 61.02           C  
ANISOU 2019  CB  THR A 241     6112   6471  10600   -878   1290  -1313       C  
ATOM   2020  OG1 THR A 241      34.110  -1.735 114.511  1.00 74.24           O  
ANISOU 2020  OG1 THR A 241     7847   8090  12270   -618   1154  -1044       O  
ATOM   2021  CG2 THR A 241      34.106   0.533 113.700  1.00 55.55           C  
ANISOU 2021  CG2 THR A 241     5736   5384   9987   -977   1620  -1389       C  
ATOM   2022  N   GLN A 242      37.072   1.819 115.392  1.00 78.37           N  
ANISOU 2022  N   GLN A 242     7698   9015  13065  -1461   1671  -2058       N  
ATOM   2023  CA  GLN A 242      37.448   3.162 115.819  1.00 81.63           C  
ANISOU 2023  CA  GLN A 242     8138   9498  13379  -1667   1791  -2327       C  
ATOM   2024  C   GLN A 242      36.627   4.238 115.118  1.00 75.32           C  
ANISOU 2024  C   GLN A 242     7785   8325  12506  -1683   2047  -2323       C  
ATOM   2025  O   GLN A 242      36.198   5.205 115.756  1.00 75.03           O  
ANISOU 2025  O   GLN A 242     7839   8331  12340  -1787   2076  -2444       O  
ATOM   2026  CB  GLN A 242      38.938   3.392 115.557  1.00 95.34           C  
ANISOU 2026  CB  GLN A 242     9639  11358  15226  -1761   1910  -2523       C  
ATOM   2027  CG  GLN A 242      39.585   4.439 116.453  1.00107.85           C  
ANISOU 2027  CG  GLN A 242    11068  13195  16714  -1978   1921  -2819       C  
ATOM   2028  CD  GLN A 242      40.118   3.855 117.746  1.00117.38           C  
ANISOU 2028  CD  GLN A 242    11854  14924  17820  -1981   1590  -2857       C  
ATOM   2029  OE1 GLN A 242      39.441   3.866 118.772  1.00117.36           O  
ANISOU 2029  OE1 GLN A 242    11822  15122  17646  -1990   1389  -2837       O  
ATOM   2030  NE2 GLN A 242      41.340   3.335 117.699  1.00123.33           N  
ANISOU 2030  NE2 GLN A 242    12285  15917  18660  -1951   1531  -2897       N  
ATOM   2031  N   GLY A 243      36.400   4.091 113.815  1.00 72.40           N  
ANISOU 2031  N   GLY A 243     7685   7635  12187  -1546   2231  -2165       N  
ATOM   2032  CA  GLY A 243      35.865   5.159 112.994  1.00 71.71           C  
ANISOU 2032  CA  GLY A 243     7950   7309  11985  -1504   2484  -2121       C  
ATOM   2033  C   GLY A 243      34.357   5.274 113.042  1.00 63.56           C  
ANISOU 2033  C   GLY A 243     7198   6199  10753  -1372   2387  -1898       C  
ATOM   2034  O   GLY A 243      33.684   4.701 113.903  1.00 49.91           O  
ANISOU 2034  O   GLY A 243     5416   4572   8977  -1351   2144  -1839       O  
ATOM   2035  N   GLN A 244      33.820   6.044 112.094  1.00 65.02           N  
ANISOU 2035  N   GLN A 244     7662   6237  10807  -1286   2569  -1765       N  
ATOM   2036  CA  GLN A 244      32.381   6.258 112.039  1.00 58.26           C  
ANISOU 2036  CA  GLN A 244     7054   5347   9737  -1157   2465  -1545       C  
ATOM   2037  C   GLN A 244      31.682   4.993 111.565  1.00 65.08           C  
ANISOU 2037  C   GLN A 244     8011   6196  10519   -962   2248  -1288       C  
ATOM   2038  O   GLN A 244      32.096   4.359 110.590  1.00 66.54           O  
ANISOU 2038  O   GLN A 244     8219   6329  10734   -878   2288  -1192       O  
ATOM   2039  CB  GLN A 244      32.035   7.429 111.122  1.00 56.45           C  
ANISOU 2039  CB  GLN A 244     7052   5006   9390  -1127   2692  -1466       C  
ATOM   2040  CG  GLN A 244      30.579   7.434 110.638  1.00 56.86           C  
ANISOU 2040  CG  GLN A 244     7355   5031   9218   -949   2560  -1197       C  
ATOM   2041  CD  GLN A 244      29.580   7.802 111.731  1.00 70.33           C  
ANISOU 2041  CD  GLN A 244     9088   6790  10844   -962   2427  -1209       C  
ATOM   2042  OE1 GLN A 244      29.087   6.940 112.464  1.00 72.39           O  
ANISOU 2042  OE1 GLN A 244     9291   7129  11085   -921   2189  -1171       O  
ATOM   2043  NE2 GLN A 244      29.263   9.085 111.828  1.00 64.70           N  
ANISOU 2043  NE2 GLN A 244     8470   6022  10092  -1018   2600  -1261       N  
ATOM   2044  N   ILE A 245      30.614   4.642 112.248  1.00 64.04           N  
ANISOU 2044  N   ILE A 245     7939   6116  10279   -897   2030  -1187       N  
ATOM   2045  CA  ILE A 245      29.926   3.378 112.038  1.00 49.28           C  
ANISOU 2045  CA  ILE A 245     6134   4253   8337   -731   1805   -976       C  
ATOM   2046  C   ILE A 245      28.790   3.597 111.051  1.00 46.93           C  
ANISOU 2046  C   ILE A 245     6104   3934   7792   -580   1767   -762       C  
ATOM   2047  O   ILE A 245      27.982   4.520 111.214  1.00 37.97           O  
ANISOU 2047  O   ILE A 245     5086   2802   6540   -582   1788   -747       O  
ATOM   2048  CB  ILE A 245      29.408   2.811 113.372  1.00 45.13           C  
ANISOU 2048  CB  ILE A 245     5499   3804   7845   -759   1589  -1000       C  
ATOM   2049  CG1 ILE A 245      30.522   2.797 114.429  1.00 66.39           C  
ANISOU 2049  CG1 ILE A 245     7864   6595  10765   -966   1592  -1262       C  
ATOM   2050  CG2 ILE A 245      28.864   1.404 113.182  1.00 42.80           C  
ANISOU 2050  CG2 ILE A 245     5246   3497   7518   -594   1383   -791       C  
ATOM   2051  CD1 ILE A 245      30.763   4.099 115.121  1.00 72.82           C  
ANISOU 2051  CD1 ILE A 245     8615   7500  11552  -1153   1712  -1497       C  
ATOM   2052  N   TYR A 246      28.758   2.786 110.001  1.00 43.89           N  
ANISOU 2052  N   TYR A 246     5796   3538   7341   -462   1716   -620       N  
ATOM   2053  CA  TYR A 246      27.618   2.741 109.106  1.00 36.66           C  
ANISOU 2053  CA  TYR A 246     5084   2646   6197   -331   1613   -449       C  
ATOM   2054  C   TYR A 246      26.840   1.466 109.376  1.00 38.92           C  
ANISOU 2054  C   TYR A 246     5382   2998   6407   -230   1351   -333       C  
ATOM   2055  O   TYR A 246      27.415   0.430 109.714  1.00 40.47           O  
ANISOU 2055  O   TYR A 246     5464   3193   6721   -223   1290   -336       O  
ATOM   2056  CB  TYR A 246      28.043   2.812 107.640  1.00 40.09           C  
ANISOU 2056  CB  TYR A 246     5608   3038   6587   -293   1752   -402       C  
ATOM   2057  CG  TYR A 246      28.439   4.206 107.216  1.00 52.40           C  
ANISOU 2057  CG  TYR A 246     7221   4523   8165   -369   2018   -473       C  
ATOM   2058  CD1 TYR A 246      27.482   5.139 106.836  1.00 46.38           C  
ANISOU 2058  CD1 TYR A 246     6617   3741   7263   -324   2069   -406       C  
ATOM   2059  CD2 TYR A 246      29.769   4.597 107.210  1.00 55.89           C  
ANISOU 2059  CD2 TYR A 246     7548   4901   8788   -489   2257   -618       C  
ATOM   2060  CE1 TYR A 246      27.844   6.415 106.456  1.00 43.45           C  
ANISOU 2060  CE1 TYR A 246     6312   3280   6918   -388   2345   -461       C  
ATOM   2061  CE2 TYR A 246      30.139   5.872 106.830  1.00 55.05           C  
ANISOU 2061  CE2 TYR A 246     7498   4717   8701   -568   2525   -690       C  
ATOM   2062  CZ  TYR A 246      29.174   6.775 106.455  1.00 53.98           C  
ANISOU 2062  CZ  TYR A 246     7543   4555   8410   -512   2558   -600       C  
ATOM   2063  OH  TYR A 246      29.547   8.042 106.078  1.00 50.90           O  
ANISOU 2063  OH  TYR A 246     7225   4067   8050   -584   2850   -662       O  
ATOM   2064  N   GLY A 247      25.524   1.564 109.264  1.00 33.08           N  
ANISOU 2064  N   GLY A 247     4767   2309   5492   -156   1210   -239       N  
ATOM   2065  CA  GLY A 247      24.683   0.428 109.572  1.00 33.87           C  
ANISOU 2065  CA  GLY A 247     4880   2474   5516    -81    975   -147       C  
ATOM   2066  C   GLY A 247      23.360   0.513 108.854  1.00 36.30           C  
ANISOU 2066  C   GLY A 247     5312   2804   5676     -2    941    -63       C  
ATOM   2067  O   GLY A 247      22.968   1.563 108.334  1.00 39.07           O  
ANISOU 2067  O   GLY A 247     5748   3124   5972      6   1079    -63       O  
ATOM   2068  N   ILE A 248      22.673  -0.623 108.831  1.00 34.78           N  
ANISOU 2068  N   ILE A 248     5129   2658   5429     55    773      8       N  
ATOM   2069  CA  ILE A 248      21.348  -0.718 108.239  1.00 36.83           C  
ANISOU 2069  CA  ILE A 248     5479   2947   5568    119    720     73       C  
ATOM   2070  C   ILE A 248      20.575  -1.807 108.966  1.00 45.05           C  
ANISOU 2070  C   ILE A 248     6486   4043   6588    136    509    119       C  
ATOM   2071  O   ILE A 248      21.129  -2.831 109.373  1.00 46.77           O  
ANISOU 2071  O   ILE A 248     6651   4264   6855    127    428    129       O  
ATOM   2072  CB  ILE A 248      21.412  -0.993 106.717  1.00 29.56           C  
ANISOU 2072  CB  ILE A 248     4642   1998   4592    163    815    101       C  
ATOM   2073  CG1 ILE A 248      20.017  -0.888 106.095  1.00 30.31           C  
ANISOU 2073  CG1 ILE A 248     4835   2121   4561    228    774    155       C  
ATOM   2074  CG2 ILE A 248      22.024  -2.360 106.435  1.00 36.55           C  
ANISOU 2074  CG2 ILE A 248     5482   2878   5526    168    750    108       C  
ATOM   2075  CD1 ILE A 248      20.028  -0.687 104.615  1.00 46.87           C  
ANISOU 2075  CD1 ILE A 248     7054   4183   6574    274    908    177       C  
ATOM   2076  N   LYS A 249      19.287  -1.561 109.158  1.00 35.89           N  
ANISOU 2076  N   LYS A 249     5361   2920   5356    164    438    151       N  
ATOM   2077  CA  LYS A 249      18.362  -2.590 109.594  1.00 33.73           C  
ANISOU 2077  CA  LYS A 249     5068   2693   5055    177    264    200       C  
ATOM   2078  C   LYS A 249      17.237  -2.686 108.579  1.00 37.57           C  
ANISOU 2078  C   LYS A 249     5609   3194   5470    227    261    236       C  
ATOM   2079  O   LYS A 249      16.683  -1.663 108.139  1.00 52.24           O  
ANISOU 2079  O   LYS A 249     7529   5051   7268    264    349    238       O  
ATOM   2080  CB  LYS A 249      17.762  -2.315 110.972  1.00 29.06           C  
ANISOU 2080  CB  LYS A 249     4447   2137   4459    153    168    205       C  
ATOM   2081  CG  LYS A 249      16.714  -3.360 111.334  1.00 42.48           C  
ANISOU 2081  CG  LYS A 249     6140   3878   6124    160     10    265       C  
ATOM   2082  CD  LYS A 249      15.890  -2.954 112.515  1.00 47.02           C  
ANISOU 2082  CD  LYS A 249     6696   4505   6665    144    -52    274       C  
ATOM   2083  CE  LYS A 249      14.695  -2.148 112.047  1.00 53.04           C  
ANISOU 2083  CE  LYS A 249     7455   5269   7430    187    -17    286       C  
ATOM   2084  NZ  LYS A 249      14.015  -2.828 110.918  1.00 68.49           N  
ANISOU 2084  NZ  LYS A 249     9410   7238   9374    223    -24    327       N  
ATOM   2085  N   VAL A 250      16.922  -3.928 108.201  1.00 26.92           N  
ANISOU 2085  N   VAL A 250     4250   1852   4126    230    172    263       N  
ATOM   2086  CA  VAL A 250      15.855  -4.204 107.247  1.00 34.63           C  
ANISOU 2086  CA  VAL A 250     5272   2842   5045    268    165    289       C  
ATOM   2087  C   VAL A 250      14.928  -5.276 107.812  1.00 36.71           C  
ANISOU 2087  C   VAL A 250     5464   3134   5352    244     28    328       C  
ATOM   2088  O   VAL A 250      15.342  -6.146 108.588  1.00 32.62           O  
ANISOU 2088  O   VAL A 250     4891   2619   4886    202    -55    336       O  
ATOM   2089  CB  VAL A 250      16.395  -4.621 105.855  1.00 30.81           C  
ANISOU 2089  CB  VAL A 250     4863   2313   4530    289    251    273       C  
ATOM   2090  CG1 VAL A 250      17.536  -3.720 105.421  1.00 27.72           C  
ANISOU 2090  CG1 VAL A 250     4518   1882   4131    295    408    244       C  
ATOM   2091  CG2 VAL A 250      16.813  -6.079 105.848  1.00 30.40           C  
ANISOU 2091  CG2 VAL A 250     4770   2231   4550    258    180    269       C  
ATOM   2092  N   ASP A 251      13.653  -5.181 107.425  1.00 19.00           N  
ANISOU 2092  N   ASP A 251     3238    924   3059    275     23    355       N  
ATOM   2093  CA  ASP A 251      12.605  -6.122 107.802  1.00 30.72           C  
ANISOU 2093  CA  ASP A 251     4652   2436   4586    254    -40    398       C  
ATOM   2094  C   ASP A 251      12.163  -6.875 106.555  1.00 31.46           C  
ANISOU 2094  C   ASP A 251     4820   2502   4630    271    -21    386       C  
ATOM   2095  O   ASP A 251      11.797  -6.254 105.551  1.00 28.92           O  
ANISOU 2095  O   ASP A 251     4607   2186   4195    331     11    376       O  
ATOM   2096  CB  ASP A 251      11.411  -5.385 108.424  1.00 31.81           C  
ANISOU 2096  CB  ASP A 251     4771   2637   4678    284    -51    434       C  
ATOM   2097  CG  ASP A 251      10.258  -6.311 108.773  1.00 45.27           C  
ANISOU 2097  CG  ASP A 251     6435   4384   6381    272    -61    481       C  
ATOM   2098  OD1 ASP A 251      10.274  -6.893 109.873  1.00 51.48           O  
ANISOU 2098  OD1 ASP A 251     7156   5215   7190    234    -29    500       O  
ATOM   2099  OD2 ASP A 251       9.334  -6.458 107.945  1.00 45.50           O1-
ANISOU 2099  OD2 ASP A 251     6573   4411   6303    315    -91    482       O1-
ATOM   2100  N   ILE A 252      12.198  -8.203 106.617  1.00 19.60           N  
ANISOU 2100  N   ILE A 252     3274    962   3211    222    -35    388       N  
ATOM   2101  CA  ILE A 252      11.783  -9.036 105.491  1.00 29.20           C  
ANISOU 2101  CA  ILE A 252     4573   2132   4391    218    -24    353       C  
ATOM   2102  C   ILE A 252      10.264  -8.993 105.396  1.00 34.54           C  
ANISOU 2102  C   ILE A 252     5361   2831   4929    244    -63    366       C  
ATOM   2103  O   ILE A 252       9.568  -9.157 106.404  1.00 50.67           O  
ANISOU 2103  O   ILE A 252     7364   4909   6978    220    -97    403       O  
ATOM   2104  CB  ILE A 252      12.289 -10.479 105.664  1.00 32.23           C  
ANISOU 2104  CB  ILE A 252     4905   2444   4897    156    -23    339       C  
ATOM   2105  CG1 ILE A 252      13.718 -10.631 105.138  1.00 29.17           C  
ANISOU 2105  CG1 ILE A 252     4551   1992   4540    162    -22    301       C  
ATOM   2106  CG2 ILE A 252      11.383 -11.464 104.929  1.00 32.06           C  
ANISOU 2106  CG2 ILE A 252     4981   2357   4845    120    -16    293       C  
ATOM   2107  CD1 ILE A 252      14.756  -9.776 105.834  1.00 25.81           C  
ANISOU 2107  CD1 ILE A 252     4097   1604   4106    180    -38    315       C  
ATOM   2108  N   ARG A 253       9.740  -8.756 104.192  1.00 35.56           N  
ANISOU 2108  N   ARG A 253     5698   2929   4883    307    -85    334       N  
ATOM   2109  CA  ARG A 253       8.293  -8.715 104.026  1.00 36.17           C  
ANISOU 2109  CA  ARG A 253     5951   3007   4784    356   -207    340       C  
ATOM   2110  C   ARG A 253       7.701 -10.115 104.112  1.00 46.15           C  
ANISOU 2110  C   ARG A 253     7283   4179   6071    235   -296    284       C  
ATOM   2111  O   ARG A 253       8.219 -11.064 103.515  1.00 40.12           O  
ANISOU 2111  O   ARG A 253     6555   3324   5363    159   -242    210       O  
ATOM   2112  CB  ARG A 253       7.904  -8.078 102.693  1.00 41.90           C  
ANISOU 2112  CB  ARG A 253     6907   3724   5290    498   -229    335       C  
ATOM   2113  CG  ARG A 253       6.419  -7.740 102.606  1.00 54.41           C  
ANISOU 2113  CG  ARG A 253     8629   5364   6680    628   -408    380       C  
ATOM   2114  CD  ARG A 253       6.028  -7.169 101.252  1.00 65.89           C  
ANISOU 2114  CD  ARG A 253    10195   6956   7884    784   -422    377       C  
ATOM   2115  NE  ARG A 253       5.741  -5.741 101.349  1.00 87.43           N  
ANISOU 2115  NE  ARG A 253    12937   9753  10529    992   -390    503       N  
ATOM   2116  CZ  ARG A 253       6.446  -4.796 100.736  1.00 97.86           C  
ANISOU 2116  CZ  ARG A 253    14281  11071  11829   1057   -226    525       C  
ATOM   2117  NH1 ARG A 253       7.476  -5.129  99.972  1.00107.62           N  
ANISOU 2117  NH1 ARG A 253    15611  12194  13084    998   -115    474       N  
ATOM   2118  NH2 ARG A 253       6.122  -3.519 100.886  1.00 91.77           N  
ANISOU 2118  NH2 ARG A 253    13443  10399  11027   1170   -170    594       N  
ATOM   2119  N   ASP A 254       6.601 -10.228 104.858  1.00 41.68           N  
ANISOU 2119  N   ASP A 254     6725   3630   5480    201   -437    312       N  
ATOM   2120  CA  ASP A 254       5.842 -11.463 105.017  1.00 45.45           C  
ANISOU 2120  CA  ASP A 254     7175   4104   5991     25   -522    235       C  
ATOM   2121  C   ASP A 254       6.758 -12.660 105.231  1.00 50.04           C  
ANISOU 2121  C   ASP A 254     7719   4536   6759    -93   -396    208       C  
ATOM   2122  O   ASP A 254       6.828 -13.557 104.386  1.00 45.50           O  
ANISOU 2122  O   ASP A 254     7240   3858   6189   -184   -373     96       O  
ATOM   2123  CB  ASP A 254       4.937 -11.689 103.808  1.00 40.94           C  
ANISOU 2123  CB  ASP A 254     6609   3724   5223      2   -598     98       C  
ATOM   2124  CG  ASP A 254       3.884 -12.740 104.071  1.00 63.04           C  
ANISOU 2124  CG  ASP A 254     9276   6642   8034   -200   -674    -12       C  
ATOM   2125  OD1 ASP A 254       3.643 -13.048 105.256  1.00 71.46           O  
ANISOU 2125  OD1 ASP A 254    10240   7682   9231   -287   -677     52       O  
ATOM   2126  OD2 ASP A 254       3.294 -13.256 103.102  1.00 73.86           O1-
ANISOU 2126  OD2 ASP A 254    10645   8141   9279   -283   -722   -168       O1-
ATOM   2127  N   ALA A 255       7.475 -12.668 106.356  1.00 41.02           N  
ANISOU 2127  N   ALA A 255     6373   3459   5752    -73   -281    293       N  
ATOM   2128  CA  ALA A 255       8.432 -13.732 106.634  1.00 38.98           C  
ANISOU 2128  CA  ALA A 255     5998   3144   5668   -114   -130    292       C  
ATOM   2129  C   ALA A 255       7.755 -15.098 106.623  1.00 43.42           C  
ANISOU 2129  C   ALA A 255     6613   3596   6287   -269   -148    231       C  
ATOM   2130  O   ALA A 255       8.129 -15.989 105.851  1.00 58.05           O  
ANISOU 2130  O   ALA A 255     8492   5342   8223   -317    -85    148       O  
ATOM   2131  CB  ALA A 255       9.115 -13.473 107.977  1.00 48.43           C  
ANISOU 2131  CB  ALA A 255     7044   4424   6934    -58    -28    392       C  
ATOM   2132  N   TYR A 256       6.735 -15.267 107.469  1.00 38.70           N  
ANISOU 2132  N   TYR A 256     6013   3025   5668   -365   -242    263       N  
ATOM   2133  CA  TYR A 256       6.030 -16.543 107.557  1.00 46.46           C  
ANISOU 2133  CA  TYR A 256     7013   3913   6728   -553   -239    199       C  
ATOM   2134  C   TYR A 256       5.426 -16.945 106.216  1.00 51.99           C  
ANISOU 2134  C   TYR A 256     7856   4540   7358   -691   -314     14       C  
ATOM   2135  O   TYR A 256       5.357 -18.138 105.895  1.00 52.68           O  
ANISOU 2135  O   TYR A 256     7943   4528   7543   -824   -224    -91       O  
ATOM   2136  CB  TYR A 256       4.932 -16.461 108.622  1.00 43.08           C  
ANISOU 2136  CB  TYR A 256     6532   3553   6283   -663   -352    264       C  
ATOM   2137  CG  TYR A 256       5.416 -16.576 110.053  1.00 38.95           C  
ANISOU 2137  CG  TYR A 256     5904   3079   5818   -589   -249    407       C  
ATOM   2138  CD1 TYR A 256       6.692 -16.175 110.417  1.00 34.06           C  
ANISOU 2138  CD1 TYR A 256     5252   2501   5189   -413   -129    470       C  
ATOM   2139  CD2 TYR A 256       4.590 -17.082 111.044  1.00 42.31           C  
ANISOU 2139  CD2 TYR A 256     6276   3519   6279   -719   -272    463       C  
ATOM   2140  CE1 TYR A 256       7.130 -16.278 111.724  1.00 28.32           C  
ANISOU 2140  CE1 TYR A 256     4486   1824   4450   -365    -73    571       C  
ATOM   2141  CE2 TYR A 256       5.022 -17.184 112.352  1.00 33.15           C  
ANISOU 2141  CE2 TYR A 256     5065   2403   5128   -650   -197    589       C  
ATOM   2142  CZ  TYR A 256       6.292 -16.782 112.687  1.00 33.94           C  
ANISOU 2142  CZ  TYR A 256     5168   2542   5186   -472   -116    636       C  
ATOM   2143  OH  TYR A 256       6.724 -16.886 113.986  1.00 29.35           O  
ANISOU 2143  OH  TYR A 256     4563   2010   4578   -422    -87    742       O  
ATOM   2144  N   GLY A 257       4.989 -15.966 105.420  1.00 43.22           N  
ANISOU 2144  N   GLY A 257     6823   3542   6057   -633   -447    -44       N  
ATOM   2145  CA  GLY A 257       4.357 -16.281 104.153  1.00 55.47           C  
ANISOU 2145  CA  GLY A 257     8397   5222   7457   -714   -483   -248       C  
ATOM   2146  C   GLY A 257       5.322 -16.672 103.055  1.00 42.82           C  
ANISOU 2146  C   GLY A 257     6969   3432   5868   -695   -379   -341       C  
ATOM   2147  O   GLY A 257       4.961 -17.444 102.162  1.00 42.58           O  
ANISOU 2147  O   GLY A 257     6978   3421   5782   -836   -362   -538       O  
ATOM   2148  N   ASN A 258       6.550 -16.155 103.095  1.00 38.07           N  
ANISOU 2148  N   ASN A 258     6421   2706   5337   -521   -289   -216       N  
ATOM   2149  CA  ASN A 258       7.532 -16.405 102.048  1.00 45.74           C  
ANISOU 2149  CA  ASN A 258     7443   3617   6320   -458   -165   -283       C  
ATOM   2150  C   ASN A 258       8.483 -17.546 102.389  1.00 46.66           C  
ANISOU 2150  C   ASN A 258     7380   3647   6699   -467    -29   -252       C  
ATOM   2151  O   ASN A 258       9.461 -17.760 101.666  1.00 64.77           O  
ANISOU 2151  O   ASN A 258     9677   5895   9039   -402     38   -280       O  
ATOM   2152  CB  ASN A 258       8.319 -15.128 101.743  1.00 38.98           C  
ANISOU 2152  CB  ASN A 258     6603   2826   5382   -251   -142   -176       C  
ATOM   2153  CG  ASN A 258       7.648 -14.270 100.682  1.00 49.46           C  
ANISOU 2153  CG  ASN A 258     8166   4202   6423   -189   -249   -255       C  
ATOM   2154  OD1 ASN A 258       6.969 -14.782  99.790  1.00 58.26           O  
ANISOU 2154  OD1 ASN A 258     9295   5450   7390   -284   -293   -424       O  
ATOM   2155  ND2 ASN A 258       7.836 -12.958 100.776  1.00 57.13           N  
ANISOU 2155  ND2 ASN A 258     9149   5248   7311     -3   -264   -122       N  
ATOM   2156  N   VAL A 259       8.227 -18.276 103.473  1.00 42.14           N  
ANISOU 2156  N   VAL A 259     6670   3047   6292   -532    -23   -185       N  
ATOM   2157  CA  VAL A 259       8.867 -19.571 103.656  1.00 42.88           C  
ANISOU 2157  CA  VAL A 259     6678   3020   6596   -555      7   -171       C  
ATOM   2158  C   VAL A 259       8.358 -20.515 102.577  1.00 50.62           C  
ANISOU 2158  C   VAL A 259     7807   3904   7522   -713     44   -382       C  
ATOM   2159  O   VAL A 259       7.147 -20.628 102.351  1.00 64.00           O  
ANISOU 2159  O   VAL A 259     9578   5630   9109   -889     22   -527       O  
ATOM   2160  CB  VAL A 259       8.582 -20.129 105.059  1.00 37.83           C  
ANISOU 2160  CB  VAL A 259     5910   2382   6080   -586    -24    -35       C  
ATOM   2161  CG1 VAL A 259       9.064 -21.575 105.160  1.00 34.83           C  
ANISOU 2161  CG1 VAL A 259     5591   1868   5773   -634    -56    -13       C  
ATOM   2162  CG2 VAL A 259       9.224 -19.253 106.131  1.00 29.07           C  
ANISOU 2162  CG2 VAL A 259     4633   1435   4976   -432    -21    140       C  
ATOM   2163  N   LYS A 260       9.278 -21.187 101.895  1.00 59.46           N  
ANISOU 2163  N   LYS A 260     8968   4930   8692   -672     95   -421       N  
ATOM   2164  CA  LYS A 260       8.936 -22.094 100.807  1.00 60.88           C  
ANISOU 2164  CA  LYS A 260     9281   5026   8826   -816    170   -639       C  
ATOM   2165  C   LYS A 260       8.821 -23.506 101.383  1.00 57.39           C  
ANISOU 2165  C   LYS A 260     8821   4451   8535   -912    204   -617       C  
ATOM   2166  O   LYS A 260       9.825 -24.122 101.745  1.00 52.34           O  
ANISOU 2166  O   LYS A 260     8169   3718   8001   -815    227   -495       O  
ATOM   2167  CB  LYS A 260       9.971 -22.006  99.689  1.00 58.11           C  
ANISOU 2167  CB  LYS A 260     9011   4643   8425   -721    245   -701       C  
ATOM   2168  CG  LYS A 260       9.736 -20.806  98.767  1.00 52.90           C  
ANISOU 2168  CG  LYS A 260     8466   4096   7540   -691    241   -793       C  
ATOM   2169  CD  LYS A 260      10.649 -19.642  99.138  1.00 66.92           C  
ANISOU 2169  CD  LYS A 260    10162   5944   9321   -489    220   -598       C  
ATOM   2170  CE  LYS A 260      10.412 -18.411  98.270  1.00 79.90           C  
ANISOU 2170  CE  LYS A 260    11973   7676  10711   -435    217   -648       C  
ATOM   2171  NZ  LYS A 260      11.181 -17.231  98.768  1.00 80.22           N  
ANISOU 2171  NZ  LYS A 260    11911   7800  10770   -260    204   -453       N  
ATOM   2172  N   ILE A 261       7.575 -23.995 101.466  1.00 57.34           N  
ANISOU 2172  N   ILE A 261     8826   4450   8510  -1117    209   -745       N  
ATOM   2173  CA  ILE A 261       7.343 -25.284 102.139  1.00 64.34           C  
ANISOU 2173  CA  ILE A 261     9702   5207   9538  -1219    263   -704       C  
ATOM   2174  C   ILE A 261       8.122 -26.419 101.504  1.00 65.02           C  
ANISOU 2174  C   ILE A 261     9879   5127   9698  -1214    389   -768       C  
ATOM   2175  O   ILE A 261       8.547 -27.325 102.236  1.00 65.86           O  
ANISOU 2175  O   ILE A 261     9990   5100   9932  -1186    440   -638       O  
ATOM   2176  CB  ILE A 261       5.821 -25.560 102.211  1.00 55.90           C  
ANISOU 2176  CB  ILE A 261     8609   4204   8426  -1471    259   -867       C  
ATOM   2177  CG1 ILE A 261       5.161 -24.613 103.211  1.00 45.88           C  
ANISOU 2177  CG1 ILE A 261     7235   3071   7125  -1461    152   -743       C  
ATOM   2178  CG2 ILE A 261       5.541 -27.003 102.605  1.00 60.77           C  
ANISOU 2178  CG2 ILE A 261     9244   4666   9181  -1607    366   -878       C  
ATOM   2179  CD1 ILE A 261       4.483 -23.453 102.555  1.00 60.22           C  
ANISOU 2179  CD1 ILE A 261     9063   5084   8734  -1515     67   -898       C  
ATOM   2180  N   PRO A 262       8.333 -26.475 100.169  1.00 72.40           N  
ANISOU 2180  N   PRO A 262    10902   6056  10552  -1247    458   -971       N  
ATOM   2181  CA  PRO A 262       9.283 -27.455  99.614  1.00 75.38           C  
ANISOU 2181  CA  PRO A 262    11358   6269  11012  -1206    592  -1006       C  
ATOM   2182  C   PRO A 262      10.610 -27.502 100.363  1.00 72.22           C  
ANISOU 2182  C   PRO A 262    10921   5804  10715   -990    580   -759       C  
ATOM   2183  O   PRO A 262      11.007 -28.540 100.922  1.00 86.69           O  
ANISOU 2183  O   PRO A 262    12776   7488  12675   -979    657   -674       O  
ATOM   2184  CB  PRO A 262       9.489 -26.963  98.173  1.00 84.72           C  
ANISOU 2184  CB  PRO A 262    12623   7520  12046  -1211    627  -1207       C  
ATOM   2185  CG  PRO A 262       8.339 -26.017  97.885  1.00 87.98           C  
ANISOU 2185  CG  PRO A 262    13025   8127  12276  -1322    521  -1340       C  
ATOM   2186  CD  PRO A 262       7.486 -25.899  99.112  1.00 80.75           C  
ANISOU 2186  CD  PRO A 262    12004   7256  11419  -1382    432  -1222       C  
ATOM   2187  N   VAL A 263      11.294 -26.353 100.377  1.00 46.21           N  
ANISOU 2187  N   VAL A 263     7573   2633   7353   -828    488   -655       N  
ATOM   2188  CA  VAL A 263      12.601 -26.247 101.021  1.00 51.83           C  
ANISOU 2188  CA  VAL A 263     8235   3337   8120   -644    457   -459       C  
ATOM   2189  C   VAL A 263      12.498 -26.582 102.501  1.00 57.13           C  
ANISOU 2189  C   VAL A 263     8858   3992   8859   -627    397   -269       C  
ATOM   2190  O   VAL A 263      13.385 -27.234 103.070  1.00 60.78           O  
ANISOU 2190  O   VAL A 263     9341   4348   9404   -545    494   -162       O  
ATOM   2191  CB  VAL A 263      13.179 -24.837 100.804  1.00 51.47           C  
ANISOU 2191  CB  VAL A 263     8125   3453   7978   -512    369   -406       C  
ATOM   2192  CG1 VAL A 263      14.639 -24.776 101.239  1.00 38.13           C  
ANISOU 2192  CG1 VAL A 263     6412   1748   6329   -359    419   -272       C  
ATOM   2193  CG2 VAL A 263      13.020 -24.415  99.352  1.00 54.55           C  
ANISOU 2193  CG2 VAL A 263     8593   3867   8264   -550    445   -600       C  
ATOM   2194  N   LEU A 264      11.418 -26.136 103.150  1.00 47.21           N  
ANISOU 2194  N   LEU A 264     7548   2823   7568   -707    300   -234       N  
ATOM   2195  CA  LEU A 264      11.263 -26.393 104.576  1.00 42.82           C  
ANISOU 2195  CA  LEU A 264     6959   2265   7047   -701    244    -52       C  
ATOM   2196  C   LEU A 264      11.158 -27.885 104.858  1.00 45.48           C  
ANISOU 2196  C   LEU A 264     7373   2402   7506   -781    387    -51       C  
ATOM   2197  O   LEU A 264      11.838 -28.402 105.750  1.00 49.06           O  
ANISOU 2197  O   LEU A 264     7845   2774   8022   -695    453     98       O  
ATOM   2198  CB  LEU A 264      10.039 -25.668 105.123  1.00 56.60           C  
ANISOU 2198  CB  LEU A 264     8634   4128   8742   -792    151    -36       C  
ATOM   2199  CG  LEU A 264       9.986 -25.752 106.648  1.00 54.46           C  
ANISOU 2199  CG  LEU A 264     8341   3883   8467   -771     88    166       C  
ATOM   2200  CD1 LEU A 264      11.309 -25.295 107.252  1.00 50.77           C  
ANISOU 2200  CD1 LEU A 264     7878   3466   7945   -590     71    302       C  
ATOM   2201  CD2 LEU A 264       8.838 -24.943 107.201  1.00 49.47           C  
ANISOU 2201  CD2 LEU A 264     7624   3388   7782   -848     11    186       C  
ATOM   2202  N   CYS A 265      10.285 -28.584 104.126  1.00 59.23           N  
ANISOU 2202  N   CYS A 265     9164   4052   9290   -953    483   -232       N  
ATOM   2203  CA  CYS A 265      10.141 -30.025 104.302  1.00 53.36           C  
ANISOU 2203  CA  CYS A 265     8497   3102   8675  -1045    639   -253       C  
ATOM   2204  C   CYS A 265      11.459 -30.738 104.051  1.00 65.62           C  
ANISOU 2204  C   CYS A 265    10117   4502  10315   -911    772   -218       C  
ATOM   2205  O   CYS A 265      11.797 -31.702 104.750  1.00 56.81           O  
ANISOU 2205  O   CYS A 265     9047   3220   9319   -881    898   -111       O  
ATOM   2206  CB  CYS A 265       9.058 -30.575 103.370  1.00 55.39           C  
ANISOU 2206  CB  CYS A 265     8801   3305   8942  -1274    744   -510       C  
ATOM   2207  SG  CYS A 265       7.390 -29.916 103.628  1.00 67.29           S  
ANISOU 2207  SG  CYS A 265    10223   4980  10365  -1475    649   -601       S  
ATOM   2208  N   LYS A 266      12.226 -30.274 103.058  1.00 78.19           N  
ANISOU 2208  N   LYS A 266    11716   6136  11857   -826    782   -307       N  
ATOM   2209  CA  LYS A 266      13.552 -30.848 102.848  1.00 81.06           C  
ANISOU 2209  CA  LYS A 266    12125   6364  12312   -689    935   -269       C  
ATOM   2210  C   LYS A 266      14.415 -30.697 104.095  1.00 71.29           C  
ANISOU 2210  C   LYS A 266    10833   5141  11113   -519    913    -31       C  
ATOM   2211  O   LYS A 266      15.012 -31.669 104.576  1.00 70.31           O  
ANISOU 2211  O   LYS A 266    10747   4845  11121   -450   1052     60       O  
ATOM   2212  CB  LYS A 266      14.248 -30.188 101.664  1.00 95.73           C  
ANISOU 2212  CB  LYS A 266    13983   8296  14093   -623    936   -384       C  
ATOM   2213  CG  LYS A 266      15.749 -30.427 101.700  1.00110.74           C  
ANISOU 2213  CG  LYS A 266    15882  10117  16076   -447   1054   -295       C  
ATOM   2214  CD  LYS A 266      16.515 -29.265 101.127  1.00118.98           C  
ANISOU 2214  CD  LYS A 266    16872  11317  17017   -343    990   -306       C  
ATOM   2215  CE  LYS A 266      18.015 -29.460 101.277  1.00117.19           C  
ANISOU 2215  CE  LYS A 266    16617  11028  16882   -174   1102   -211       C  
ATOM   2216  NZ  LYS A 266      18.544 -29.223 102.650  1.00109.88           N  
ANISOU 2216  NZ  LYS A 266    15604  10155  15991    -51   1037      1       N  
ATOM   2217  N   LEU A 267      14.510 -29.469 104.617  1.00 68.86           N  
ANISOU 2217  N   LEU A 267    10436   5037  10690   -446    747     64       N  
ATOM   2218  CA  LEU A 267      15.323 -29.223 105.805  1.00 64.89           C  
ANISOU 2218  CA  LEU A 267     9877   4580  10198   -295    715    266       C  
ATOM   2219  C   LEU A 267      14.890 -30.109 106.963  1.00 64.49           C  
ANISOU 2219  C   LEU A 267     9856   4418  10228   -323    757    401       C  
ATOM   2220  O   LEU A 267      15.730 -30.673 107.675  1.00 71.05           O  
ANISOU 2220  O   LEU A 267    10689   5158  11149   -195    836    543       O  
ATOM   2221  CB  LEU A 267      15.238 -27.751 106.211  1.00 60.76           C  
ANISOU 2221  CB  LEU A 267     9267   4294   9523   -256    536    317       C  
ATOM   2222  CG  LEU A 267      15.795 -26.718 105.232  1.00 71.26           C  
ANISOU 2222  CG  LEU A 267    10560   5744  10772   -203    498    223       C  
ATOM   2223  CD1 LEU A 267      15.397 -25.325 105.679  1.00 71.74           C  
ANISOU 2223  CD1 LEU A 267    10550   6014  10693   -197    333    265       C  
ATOM   2224  CD2 LEU A 267      17.309 -26.841 105.117  1.00 72.12           C  
ANISOU 2224  CD2 LEU A 267    10643   5810  10949    -51    600    266       C  
ATOM   2225  N   ILE A 268      13.576 -30.243 107.164  1.00 64.70           N  
ANISOU 2225  N   ILE A 268     9903   4451  10228   -488    709    364       N  
ATOM   2226  CA  ILE A 268      13.061 -31.117 108.216  1.00 51.66           C  
ANISOU 2226  CA  ILE A 268     8290   2683   8654   -539    767    488       C  
ATOM   2227  C   ILE A 268      13.546 -32.544 108.000  1.00 62.44           C  
ANISOU 2227  C   ILE A 268     9745   3782  10196   -517    983    484       C  
ATOM   2228  O   ILE A 268      13.995 -33.214 108.935  1.00 54.25           O  
ANISOU 2228  O   ILE A 268     8734   2633   9247   -421   1063    657       O  
ATOM   2229  CB  ILE A 268      11.523 -31.056 108.274  1.00 49.97           C  
ANISOU 2229  CB  ILE A 268     8073   2515   8398   -750    700    414       C  
ATOM   2230  CG1 ILE A 268      11.037 -29.613 108.394  1.00 50.96           C  
ANISOU 2230  CG1 ILE A 268     8109   2893   8361   -762    497    412       C  
ATOM   2231  CG2 ILE A 268      11.003 -31.883 109.441  1.00 50.46           C  
ANISOU 2231  CG2 ILE A 268     8172   2467   8533   -806    766    558       C  
ATOM   2232  CD1 ILE A 268      10.972 -29.105 109.805  1.00 54.10           C  
ANISOU 2232  CD1 ILE A 268     8471   3403   8682   -708    407    603       C  
ATOM   2233  N   GLN A 269      13.464 -33.031 106.759  1.00 70.69           N  
ANISOU 2233  N   GLN A 269    10848   4720  11293   -601   1091    288       N  
ATOM   2234  CA  GLN A 269      13.844 -34.416 106.498  1.00 68.02           C  
ANISOU 2234  CA  GLN A 269    10608   4110  11127   -597   1322    262       C  
ATOM   2235  C   GLN A 269      15.339 -34.627 106.710  1.00 64.18           C  
ANISOU 2235  C   GLN A 269    10111   3553  10722   -366   1403    393       C  
ATOM   2236  O   GLN A 269      15.773 -35.725 107.082  1.00 64.23           O  
ANISOU 2236  O   GLN A 269    10182   3339  10882   -298   1576    485       O  
ATOM   2237  CB  GLN A 269      13.447 -34.814 105.077  1.00 59.09           C  
ANISOU 2237  CB  GLN A 269     9541   2898  10012   -747   1421     -3       C  
ATOM   2238  CG  GLN A 269      11.993 -35.290 104.889  1.00 84.08           C  
ANISOU 2238  CG  GLN A 269    12746   6018  13181  -1000   1445   -150       C  
ATOM   2239  CD  GLN A 269      11.555 -36.421 105.819  1.00 98.42           C  
ANISOU 2239  CD  GLN A 269    14627   7629  15138  -1064   1590    -44       C  
ATOM   2240  OE1 GLN A 269      12.335 -36.948 106.611  1.00109.97           O  
ANISOU 2240  OE1 GLN A 269    16121   8961  16702   -908   1682    151       O  
ATOM   2241  NE2 GLN A 269      10.287 -36.794 105.718  1.00 98.66           N  
ANISOU 2241  NE2 GLN A 269    14676   7634  15175  -1297   1615   -173       N  
ATOM   2242  N   SER A 270      16.143 -33.583 106.484  1.00 55.97           N  
ANISOU 2242  N   SER A 270     8986   2694   9588   -243   1289    405       N  
ATOM   2243  CA  SER A 270      17.592 -33.715 106.578  1.00 73.79           C  
ANISOU 2243  CA  SER A 270    11209   4904  11924    -34   1364    506       C  
ATOM   2244  C   SER A 270      18.092 -33.851 108.011  1.00 57.22           C  
ANISOU 2244  C   SER A 270     9066   2809   9865    118   1334    757       C  
ATOM   2245  O   SER A 270      19.283 -34.114 108.202  1.00 58.45           O  
ANISOU 2245  O   SER A 270     9188   2909  10110    300   1405    860       O  
ATOM   2246  CB  SER A 270      18.262 -32.516 105.914  1.00 75.77           C  
ANISOU 2246  CB  SER A 270    11374   5352  12061     31   1259    435       C  
ATOM   2247  OG  SER A 270      17.523 -32.091 104.783  1.00 88.29           O  
ANISOU 2247  OG  SER A 270    12992   7002  13554   -120   1223    228       O  
ATOM   2248  N   ILE A 271      17.232 -33.690 109.008  1.00 56.45           N  
ANISOU 2248  N   ILE A 271     8965   2779   9703     51   1235    859       N  
ATOM   2249  CA  ILE A 271      17.694 -33.657 110.398  1.00 67.91           C  
ANISOU 2249  CA  ILE A 271    10370   4276  11155    198   1184   1099       C  
ATOM   2250  C   ILE A 271      18.055 -35.073 110.836  1.00 70.02           C  
ANISOU 2250  C   ILE A 271    10720   4277  11605    286   1377   1233       C  
ATOM   2251  O   ILE A 271      17.270 -36.006 110.598  1.00 63.00           O  
ANISOU 2251  O   ILE A 271     9939   3194  10804    153   1511   1174       O  
ATOM   2252  CB  ILE A 271      16.635 -33.054 111.312  1.00 77.83           C  
ANISOU 2252  CB  ILE A 271    11609   5685  12278     93   1034   1163       C  
ATOM   2253  CG1 ILE A 271      16.138 -31.723 110.749  1.00 80.79           C  
ANISOU 2253  CG1 ILE A 271    11919   6290  12486     -6    868   1015       C  
ATOM   2254  CG2 ILE A 271      17.189 -32.863 112.699  1.00 80.62           C  
ANISOU 2254  CG2 ILE A 271    11907   6124  12599    251    968   1396       C  
ATOM   2255  CD1 ILE A 271      14.839 -31.270 111.363  1.00 75.98           C  
ANISOU 2255  CD1 ILE A 271    11312   5793  11764   -156    753   1028       C  
ATOM   2256  N   PRO A 272      19.225 -35.269 111.444  1.00 61.98           N  
ANISOU 2256  N   PRO A 272     9655   3240  10654    508   1405   1409       N  
ATOM   2257  CA  PRO A 272      19.577 -36.591 111.977  1.00 76.93           C  
ANISOU 2257  CA  PRO A 272    11629   4881  12719    622   1587   1576       C  
ATOM   2258  C   PRO A 272      18.463 -37.167 112.841  1.00 79.02           C  
ANISOU 2258  C   PRO A 272    11984   5056  12985    509   1616   1678       C  
ATOM   2259  O   PRO A 272      17.769 -36.446 113.561  1.00 83.67           O  
ANISOU 2259  O   PRO A 272    12534   5828  13430    433   1457   1725       O  
ATOM   2260  CB  PRO A 272      20.839 -36.312 112.799  1.00 74.26           C  
ANISOU 2260  CB  PRO A 272    11185   4646  12385    879   1522   1783       C  
ATOM   2261  CG  PRO A 272      21.434 -35.077 112.207  1.00 62.99           C  
ANISOU 2261  CG  PRO A 272     9633   3448  10851    897   1383   1657       C  
ATOM   2262  CD  PRO A 272      20.347 -34.314 111.500  1.00 59.98           C  
ANISOU 2262  CD  PRO A 272     9269   3182  10337    666   1291   1444       C  
ATOM   2263  N   THR A 273      18.283 -38.485 112.749  1.00 72.98           N  
ANISOU 2263  N   THR A 273    11345   3996  12389    492   1840   1706       N  
ATOM   2264  CA  THR A 273      17.176 -39.141 113.432  1.00 78.38           C  
ANISOU 2264  CA  THR A 273    12129   4557  13097    356   1910   1780       C  
ATOM   2265  C   THR A 273      17.373 -39.209 114.940  1.00 74.18           C  
ANISOU 2265  C   THR A 273    11584   4072  12529    507   1855   2081       C  
ATOM   2266  O   THR A 273      16.390 -39.379 115.669  1.00 74.62           O  
ANISOU 2266  O   THR A 273    11694   4116  12543    384   1850   2155       O  
ATOM   2267  CB  THR A 273      16.965 -40.550 112.871  1.00 96.40           C  
ANISOU 2267  CB  THR A 273    14559   6488  15582    290   2195   1714       C  
ATOM   2268  OG1 THR A 273      17.238 -40.545 111.465  1.00 77.24           O  
ANISOU 2268  OG1 THR A 273    12135   4015  13198    230   2263   1463       O  
ATOM   2269  CG2 THR A 273      15.529 -41.010 113.094  1.00102.78           C  
ANISOU 2269  CG2 THR A 273    15459   7197  16396     42   2260   1659       C  
ATOM   2270  N   HIS A 274      18.611 -39.087 115.428  1.00 74.70           N  
ANISOU 2270  N   HIS A 274    11576   4200  12606    766   1817   2256       N  
ATOM   2271  CA  HIS A 274      18.805 -39.027 116.871  1.00 79.91           C  
ANISOU 2271  CA  HIS A 274    12210   4955  13197    914   1736   2538       C  
ATOM   2272  C   HIS A 274      18.344 -37.702 117.459  1.00 91.22           C  
ANISOU 2272  C   HIS A 274    13540   6715  14406    838   1484   2526       C  
ATOM   2273  O   HIS A 274      18.302 -37.571 118.687  1.00 93.35           O  
ANISOU 2273  O   HIS A 274    13794   7089  14586    920   1407   2739       O  
ATOM   2274  CB  HIS A 274      20.271 -39.288 117.236  1.00 84.15           C  
ANISOU 2274  CB  HIS A 274    12684   5482  13808   1223   1759   2731       C  
ATOM   2275  CG  HIS A 274      21.178 -38.109 117.042  1.00 86.93           C  
ANISOU 2275  CG  HIS A 274    12865   6110  14054   1326   1568   2672       C  
ATOM   2276  ND1 HIS A 274      21.719 -37.780 115.819  1.00 84.86           N  
ANISOU 2276  ND1 HIS A 274    12553   5853  13838   1308   1586   2461       N  
ATOM   2277  CD2 HIS A 274      21.660 -37.200 117.924  1.00 86.24           C  
ANISOU 2277  CD2 HIS A 274    12649   6298  13821   1445   1369   2795       C  
ATOM   2278  CE1 HIS A 274      22.485 -36.711 115.952  1.00 82.43           C  
ANISOU 2278  CE1 HIS A 274    12092   5802  13425   1407   1412   2458       C  
ATOM   2279  NE2 HIS A 274      22.466 -36.339 117.219  1.00 78.79           N  
ANISOU 2279  NE2 HIS A 274    11579   5509  12849   1489   1278   2652       N  
ATOM   2280  N   LEU A 275      17.981 -36.732 116.617  1.00 94.07           N  
ANISOU 2280  N   LEU A 275    13838   7234  14670    687   1367   2287       N  
ATOM   2281  CA  LEU A 275      17.467 -35.445 117.068  1.00 88.20           C  
ANISOU 2281  CA  LEU A 275    13009   6781  13721    602   1152   2251       C  
ATOM   2282  C   LEU A 275      15.988 -35.241 116.778  1.00 83.23           C  
ANISOU 2282  C   LEU A 275    12433   6165  13026    330   1128   2100       C  
ATOM   2283  O   LEU A 275      15.335 -34.484 117.495  1.00 78.73           O  
ANISOU 2283  O   LEU A 275    11828   5781  12303    256    993   2136       O  
ATOM   2284  CB  LEU A 275      18.262 -34.299 116.427  1.00 79.50           C  
ANISOU 2284  CB  LEU A 275    11779   5887  12541    665   1020   2118       C  
ATOM   2285  CG  LEU A 275      19.757 -34.282 116.754  1.00 80.19           C  
ANISOU 2285  CG  LEU A 275    11774   6018  12676    927   1010   2256       C  
ATOM   2286  CD1 LEU A 275      20.469 -33.108 116.091  1.00 79.09           C  
ANISOU 2286  CD1 LEU A 275    11508   6079  12464    958    894   2108       C  
ATOM   2287  CD2 LEU A 275      19.954 -34.258 118.262  1.00 71.63           C  
ANISOU 2287  CD2 LEU A 275    10657   5044  11516   1064    932   2515       C  
ATOM   2288  N   LEU A 276      15.449 -35.891 115.750  1.00 63.47           N  
ANISOU 2288  N   LEU A 276    10007   3475  10633    180   1258   1928       N  
ATOM   2289  CA  LEU A 276      14.025 -35.801 115.437  1.00 62.57           C  
ANISOU 2289  CA  LEU A 276     9930   3367  10475    -83   1243   1782       C  
ATOM   2290  C   LEU A 276      13.653 -37.064 114.675  1.00 79.51           C  
ANISOU 2290  C   LEU A 276    12190   5217  12803   -194   1467   1676       C  
ATOM   2291  O   LEU A 276      13.999 -37.200 113.498  1.00 82.14           O  
ANISOU 2291  O   LEU A 276    12529   5479  13201   -208   1532   1495       O  
ATOM   2292  CB  LEU A 276      13.720 -34.541 114.629  1.00 58.58           C  
ANISOU 2292  CB  LEU A 276     9336   3091   9831   -180   1074   1576       C  
ATOM   2293  CG  LEU A 276      12.278 -34.293 114.188  1.00 57.43           C  
ANISOU 2293  CG  LEU A 276     9198   2991   9630   -440   1029   1411       C  
ATOM   2294  CD1 LEU A 276      11.450 -33.867 115.381  1.00 70.67           C  
ANISOU 2294  CD1 LEU A 276    10858   4803  11192   -512    932   1543       C  
ATOM   2295  CD2 LEU A 276      12.236 -33.223 113.108  1.00 54.26           C  
ANISOU 2295  CD2 LEU A 276     8723   2766   9128   -487    900   1206       C  
ATOM   2296  N   ASP A 277      12.962 -37.987 115.340  1.00 87.08           N  
ANISOU 2296  N   ASP A 277    13243   6000  13842   -278   1600   1784       N  
ATOM   2297  CA  ASP A 277      12.773 -39.307 114.757  1.00 85.39           C  
ANISOU 2297  CA  ASP A 277    13153   5469  13823   -356   1855   1708       C  
ATOM   2298  C   ASP A 277      11.784 -39.258 113.593  1.00 81.49           C  
ANISOU 2298  C   ASP A 277    12663   4966  13332   -619   1874   1408       C  
ATOM   2299  O   ASP A 277      11.065 -38.270 113.387  1.00 78.80           O  
ANISOU 2299  O   ASP A 277    12236   4857  12847   -751   1691   1293       O  
ATOM   2300  CB  ASP A 277      12.319 -40.314 115.820  1.00 78.78           C  
ANISOU 2300  CB  ASP A 277    12424   4433  13075   -373   2014   1914       C  
ATOM   2301  CG  ASP A 277      10.994 -39.945 116.465  1.00 79.57           C  
ANISOU 2301  CG  ASP A 277    12507   4656  13070   -586   1928   1923       C  
ATOM   2302  OD1 ASP A 277       9.959 -39.950 115.766  1.00 77.85           O  
ANISOU 2302  OD1 ASP A 277    12286   4431  12861   -836   1947   1703       O  
ATOM   2303  OD2 ASP A 277      10.988 -39.663 117.683  1.00 86.54           O1-
ANISOU 2303  OD2 ASP A 277    13375   5649  13859   -505   1845   2151       O1-
ATOM   2304  N   SER A 278      11.753 -40.365 112.839  1.00 81.91           N  
ANISOU 2304  N   SER A 278    12822   4745  13555   -691   2110   1281       N  
ATOM   2305  CA  SER A 278      11.009 -40.422 111.584  1.00 87.46           C  
ANISOU 2305  CA  SER A 278    13533   5429  14268   -921   2151    971       C  
ATOM   2306  C   SER A 278       9.550 -40.021 111.772  1.00 94.41           C  
ANISOU 2306  C   SER A 278    14368   6447  15059  -1176   2051    880       C  
ATOM   2307  O   SER A 278       8.983 -39.302 110.938  1.00 94.85           O  
ANISOU 2307  O   SER A 278    14347   6677  15013  -1315   1922    667       O  
ATOM   2308  CB  SER A 278      11.105 -41.826 110.976  1.00 97.43           C  
ANISOU 2308  CB  SER A 278    14936   6346  15736   -978   2458    867       C  
ATOM   2309  OG  SER A 278      12.371 -42.421 111.203  1.00104.20           O  
ANISOU 2309  OG  SER A 278    15850   7030  16713   -724   2590   1035       O  
ATOM   2310  N   GLU A 279       8.916 -40.478 112.858  1.00112.70           N  
ANISOU 2310  N   GLU A 279    16724   8688  17408  -1241   2114   1044       N  
ATOM   2311  CA  GLU A 279       7.486 -40.220 112.998  1.00113.73           C  
ANISOU 2311  CA  GLU A 279    16804   8930  17478  -1505   2053    944       C  
ATOM   2312  C   GLU A 279       7.180 -38.739 113.130  1.00100.18           C  
ANISOU 2312  C   GLU A 279    14938   7566  15559  -1505   1758    940       C  
ATOM   2313  O   GLU A 279       6.276 -38.223 112.452  1.00101.94           O  
ANISOU 2313  O   GLU A 279    15083   7931  15720  -1694   1676    731       O  
ATOM   2314  CB  GLU A 279       6.885 -40.976 114.187  1.00127.04           C  
ANISOU 2314  CB  GLU A 279    18562  10472  19236  -1574   2189   1135       C  
ATOM   2315  CG  GLU A 279       5.508 -40.432 114.664  1.00131.22           C  
ANISOU 2315  CG  GLU A 279    19000  11187  19670  -1803   2087   1103       C  
ATOM   2316  CD  GLU A 279       4.470 -40.252 113.540  1.00130.79           C  
ANISOU 2316  CD  GLU A 279    18876  11204  19615  -2072   2099    765       C  
ATOM   2317  OE1 GLU A 279       4.665 -40.747 112.414  1.00127.60           O  
ANISOU 2317  OE1 GLU A 279    18519  10674  19289  -2125   2206    545       O  
ATOM   2318  OE2 GLU A 279       3.443 -39.584 113.785  1.00124.54           O1-
ANISOU 2318  OE2 GLU A 279    17973  10611  18736  -2232   2000    714       O1-
ATOM   2319  N   LYS A 280       7.928 -38.053 114.006  1.00 86.96           N  
ANISOU 2319  N   LYS A 280    13225   6031  13784  -1292   1619   1165       N  
ATOM   2320  CA  LYS A 280       7.674 -36.631 114.164  1.00 74.11           C  
ANISOU 2320  CA  LYS A 280    11468   4722  11966  -1289   1360   1161       C  
ATOM   2321  C   LYS A 280       8.149 -35.825 112.958  1.00 61.40           C  
ANISOU 2321  C   LYS A 280     9795   3244  10290  -1239   1243    971       C  
ATOM   2322  O   LYS A 280       7.549 -34.790 112.637  1.00 58.46           O  
ANISOU 2322  O   LYS A 280     9324   3095   9792  -1323   1070    868       O  
ATOM   2323  CB  LYS A 280       8.316 -36.102 115.435  1.00 74.01           C  
ANISOU 2323  CB  LYS A 280    11437   4832  11851  -1095   1256   1425       C  
ATOM   2324  CG  LYS A 280       9.606 -36.776 115.865  1.00 81.30           C  
ANISOU 2324  CG  LYS A 280    12434   5594  12861   -850   1366   1606       C  
ATOM   2325  CD  LYS A 280       9.750 -36.767 117.376  1.00 72.31           C  
ANISOU 2325  CD  LYS A 280    11313   4505  11658   -741   1339   1888       C  
ATOM   2326  CE  LYS A 280       8.713 -37.667 118.034  1.00 71.12           C  
ANISOU 2326  CE  LYS A 280    11244   4196  11582   -911   1488   1971       C  
ATOM   2327  NZ  LYS A 280       9.211 -38.166 119.341  1.00 70.85           N  
ANISOU 2327  NZ  LYS A 280    11278   4091  11550   -744   1554   2273       N  
ATOM   2328  N   LYS A 281       9.192 -36.284 112.256  1.00 74.29           N  
ANISOU 2328  N   LYS A 281    11482   4737  12008  -1105   1345    923       N  
ATOM   2329  CA  LYS A 281       9.533 -35.656 110.979  1.00 60.64           C  
ANISOU 2329  CA  LYS A 281     9708   3108  10226  -1092   1271    720       C  
ATOM   2330  C   LYS A 281       8.341 -35.685 110.028  1.00 66.24           C  
ANISOU 2330  C   LYS A 281    10399   3841  10926  -1345   1272    465       C  
ATOM   2331  O   LYS A 281       7.958 -34.662 109.438  1.00 67.47           O  
ANISOU 2331  O   LYS A 281    10468   4209  10960  -1393   1106    343       O  
ATOM   2332  CB  LYS A 281      10.743 -36.349 110.347  1.00 66.15           C  
ANISOU 2332  CB  LYS A 281    10476   3620  11040   -941   1426    697       C  
ATOM   2333  CG  LYS A 281      12.051 -36.129 111.084  1.00 87.93           C  
ANISOU 2333  CG  LYS A 281    13212   6404  13792   -673   1395    916       C  
ATOM   2334  CD  LYS A 281      13.243 -36.257 110.136  1.00 82.51           C  
ANISOU 2334  CD  LYS A 281    12533   5649  13167   -530   1472    835       C  
ATOM   2335  CE  LYS A 281      13.964 -37.598 110.281  1.00 93.70           C  
ANISOU 2335  CE  LYS A 281    14051   6773  14779   -421   1712    928       C  
ATOM   2336  NZ  LYS A 281      15.443 -37.422 110.412  1.00 89.25           N  
ANISOU 2336  NZ  LYS A 281    13440   6230  14243   -160   1709   1054       N  
ATOM   2337  N   ASN A 282       7.726 -36.862 109.895  1.00 75.61           N  
ANISOU 2337  N   ASN A 282    11668   4813  12248  -1509   1468    381       N  
ATOM   2338  CA  ASN A 282       6.598 -37.016 108.988  1.00 86.87           C  
ANISOU 2338  CA  ASN A 282    13077   6248  13681  -1768   1526    105       C  
ATOM   2339  C   ASN A 282       5.382 -36.242 109.480  1.00 84.34           C  
ANISOU 2339  C   ASN A 282    12645   6136  13266  -1921   1404     96       C  
ATOM   2340  O   ASN A 282       4.649 -35.655 108.674  1.00 72.90           O  
ANISOU 2340  O   ASN A 282    11120   4840  11740  -2063   1336   -121       O  
ATOM   2341  CB  ASN A 282       6.263 -38.499 108.815  1.00 90.97           C  
ANISOU 2341  CB  ASN A 282    13716   6474  14375  -1919   1803      8       C  
ATOM   2342  CG  ASN A 282       7.333 -39.258 108.041  1.00 95.87           C  
ANISOU 2342  CG  ASN A 282    14443   6889  15097  -1804   1951    -53       C  
ATOM   2343  OD1 ASN A 282       8.083 -40.053 108.606  1.00102.13           O  
ANISOU 2343  OD1 ASN A 282    15327   7464  16014  -1665   2109    116       O  
ATOM   2344  ND2 ASN A 282       7.401 -39.019 106.739  1.00 91.68           N  
ANISOU 2344  ND2 ASN A 282    13903   6415  14518  -1862   1943   -302       N  
ATOM   2345  N   PHE A 283       5.153 -36.222 110.798  1.00 86.35           N  
ANISOU 2345  N   PHE A 283    12885   6405  13519  -1894   1381    326       N  
ATOM   2346  CA  PHE A 283       4.037 -35.450 111.334  1.00 73.65           C  
ANISOU 2346  CA  PHE A 283    11160   5001  11823  -2029   1273    332       C  
ATOM   2347  C   PHE A 283       4.213 -33.970 111.036  1.00 68.23           C  
ANISOU 2347  C   PHE A 283    10362   4585  10977  -1928   1041    315       C  
ATOM   2348  O   PHE A 283       3.269 -33.298 110.618  1.00 77.08           O  
ANISOU 2348  O   PHE A 283    11381   5874  12033  -2073    971    158       O  
ATOM   2349  CB  PHE A 283       3.886 -35.657 112.841  1.00 80.36           C  
ANISOU 2349  CB  PHE A 283    12025   5824  12683  -1997   1294    602       C  
ATOM   2350  CG  PHE A 283       2.915 -34.694 113.474  1.00 89.37           C  
ANISOU 2350  CG  PHE A 283    13036   7204  13718  -2095   1167    640       C  
ATOM   2351  CD1 PHE A 283       1.554 -34.803 113.226  1.00 93.73           C  
ANISOU 2351  CD1 PHE A 283    13509   7806  14297  -2362   1233    456       C  
ATOM   2352  CD2 PHE A 283       3.360 -33.660 114.281  1.00 84.56           C  
ANISOU 2352  CD2 PHE A 283    12375   6780  12975  -1930    991    834       C  
ATOM   2353  CE1 PHE A 283       0.656 -33.913 113.788  1.00 86.22           C  
ANISOU 2353  CE1 PHE A 283    12421   7081  13258  -2449   1130    482       C  
ATOM   2354  CE2 PHE A 283       2.466 -32.764 114.844  1.00 77.21           C  
ANISOU 2354  CE2 PHE A 283    11323   6061  11951  -2021    894    862       C  
ATOM   2355  CZ  PHE A 283       1.114 -32.894 114.597  1.00 72.98           C  
ANISOU 2355  CZ  PHE A 283    10699   5569  11461  -2274    965    693       C  
ATOM   2356  N   ILE A 284       5.423 -33.445 111.239  1.00 64.30           N  
ANISOU 2356  N   ILE A 284     9881   4133  10416  -1683    930    466       N  
ATOM   2357  CA  ILE A 284       5.681 -32.029 110.996  1.00 52.83           C  
ANISOU 2357  CA  ILE A 284     8338   2919   8817  -1577    728    459       C  
ATOM   2358  C   ILE A 284       5.501 -31.694 109.519  1.00 65.59           C  
ANISOU 2358  C   ILE A 284     9928   4583  10411  -1643    715    197       C  
ATOM   2359  O   ILE A 284       4.923 -30.656 109.170  1.00 72.73           O  
ANISOU 2359  O   ILE A 284    10738   5676  11220  -1689    599    104       O  
ATOM   2360  CB  ILE A 284       7.092 -31.654 111.491  1.00 53.77           C  
ANISOU 2360  CB  ILE A 284     8489   3070   8873  -1317    642    645       C  
ATOM   2361  CG1 ILE A 284       7.129 -31.570 113.019  1.00 51.69           C  
ANISOU 2361  CG1 ILE A 284     8230   2851   8557  -1257    609    888       C  
ATOM   2362  CG2 ILE A 284       7.549 -30.335 110.890  1.00 53.73           C  
ANISOU 2362  CG2 ILE A 284     8417   3263   8737  -1209    477    584       C  
ATOM   2363  CD1 ILE A 284       8.531 -31.439 113.584  1.00 53.77           C  
ANISOU 2363  CD1 ILE A 284     8534   3119   8777  -1014    583   1047       C  
ATOM   2364  N   VAL A 285       6.000 -32.556 108.629  1.00 69.87           N  
ANISOU 2364  N   VAL A 285    10559   4953  11035  -1646    843     70       N  
ATOM   2365  CA  VAL A 285       5.908 -32.269 107.198  1.00 75.69           C  
ANISOU 2365  CA  VAL A 285    11291   5739  11727  -1706    841   -186       C  
ATOM   2366  C   VAL A 285       4.451 -32.297 106.742  1.00 82.70           C  
ANISOU 2366  C   VAL A 285    12125   6705  12594  -1977    872   -417       C  
ATOM   2367  O   VAL A 285       3.980 -31.385 106.047  1.00 87.00           O  
ANISOU 2367  O   VAL A 285    12598   7435  13021  -2028    769   -570       O  
ATOM   2368  CB  VAL A 285       6.779 -33.257 106.397  1.00 67.68           C  
ANISOU 2368  CB  VAL A 285    10392   4520  10806  -1658    995   -272       C  
ATOM   2369  CG1 VAL A 285       6.260 -33.408 104.972  1.00 69.75           C  
ANISOU 2369  CG1 VAL A 285    10674   4790  11037  -1828   1064   -590       C  
ATOM   2370  CG2 VAL A 285       8.237 -32.811 106.399  1.00 53.95           C  
ANISOU 2370  CG2 VAL A 285     8664   2799   9034  -1394    921   -129       C  
ATOM   2371  N   ASP A 286       3.722 -33.353 107.123  1.00 88.54           N  
ANISOU 2371  N   ASP A 286    12894   7310  13438  -2159   1023   -456       N  
ATOM   2372  CA  ASP A 286       2.281 -33.417 106.896  1.00 98.57           C  
ANISOU 2372  CA  ASP A 286    14086   8684  14684  -2438   1052   -670       C  
ATOM   2373  C   ASP A 286       1.582 -32.201 107.494  1.00 93.00           C  
ANISOU 2373  C   ASP A 286    13236   8230  13869  -2445    880   -599       C  
ATOM   2374  O   ASP A 286       0.635 -31.662 106.907  1.00101.89           O  
ANISOU 2374  O   ASP A 286    14262   9554  14898  -2608    817   -816       O  
ATOM   2375  CB  ASP A 286       1.757 -34.730 107.492  1.00107.32           C  
ANISOU 2375  CB  ASP A 286    15249   9588  15938  -2602   1253   -658       C  
ATOM   2376  CG  ASP A 286       0.248 -34.753 107.706  1.00112.48           C  
ANISOU 2376  CG  ASP A 286    15789  10373  16574  -2881   1274   -807       C  
ATOM   2377  OD1 ASP A 286      -0.496 -34.066 106.981  1.00112.05           O  
ANISOU 2377  OD1 ASP A 286    15624  10552  16398  -3010   1173  -1031       O  
ATOM   2378  OD2 ASP A 286      -0.200 -35.502 108.605  1.00118.52           O1-
ANISOU 2378  OD2 ASP A 286    16575  11014  17443  -2976   1401   -705       O1-
ATOM   2379  N   HIS A 287       2.073 -31.729 108.638  1.00 80.59           N  
ANISOU 2379  N   HIS A 287    11650   6674  12296  -2268    800   -308       N  
ATOM   2380  CA  HIS A 287       1.442 -30.635 109.362  1.00 77.48           C  
ANISOU 2380  CA  HIS A 287    11127   6496  11817  -2271    665   -218       C  
ATOM   2381  C   HIS A 287       1.575 -29.319 108.612  1.00 78.21           C  
ANISOU 2381  C   HIS A 287    11154   6786  11778  -2184    509   -313       C  
ATOM   2382  O   HIS A 287       0.615 -28.542 108.534  1.00 73.77           O  
ANISOU 2382  O   HIS A 287    10472   6427  11131  -2300    435   -427       O  
ATOM   2383  CB  HIS A 287       2.075 -30.541 110.752  1.00 71.00           C  
ANISOU 2383  CB  HIS A 287    10330   5635  11010  -2099    630    111       C  
ATOM   2384  CG  HIS A 287       1.520 -29.453 111.612  1.00 66.06           C  
ANISOU 2384  CG  HIS A 287     9583   5216  10301  -2091    513    225       C  
ATOM   2385  ND1 HIS A 287       0.478 -29.658 112.489  1.00 72.36           N  
ANISOU 2385  ND1 HIS A 287    10309   6059  11125  -2253    569    272       N  
ATOM   2386  CD2 HIS A 287       1.882 -28.157 111.754  1.00 63.24           C  
ANISOU 2386  CD2 HIS A 287     9163   5024   9840  -1940    360    304       C  
ATOM   2387  CE1 HIS A 287       0.211 -28.532 113.125  1.00 69.77           C  
ANISOU 2387  CE1 HIS A 287     9874   5923  10713  -2201    457    370       C  
ATOM   2388  NE2 HIS A 287       1.049 -27.605 112.697  1.00 63.03           N  
ANISOU 2388  NE2 HIS A 287     9028   5137   9783  -2012    332    390       N  
ATOM   2389  N   ILE A 288       2.756 -29.050 108.053  1.00 71.30           N  
ANISOU 2389  N   ILE A 288    10352   5861  10878  -1984    467   -276       N  
ATOM   2390  CA  ILE A 288       2.963 -27.782 107.364  1.00 56.38           C  
ANISOU 2390  CA  ILE A 288     8417   4136   8868  -1886    339   -348       C  
ATOM   2391  C   ILE A 288       2.523 -27.834 105.904  1.00 74.68           C  
ANISOU 2391  C   ILE A 288    10755   6509  11110  -2027    362   -664       C  
ATOM   2392  O   ILE A 288       2.345 -26.778 105.282  1.00 65.41           O  
ANISOU 2392  O   ILE A 288     9544   5506   9801  -2007    262   -773       O  
ATOM   2393  CB  ILE A 288       4.427 -27.318 107.446  1.00 51.78           C  
ANISOU 2393  CB  ILE A 288     7885   3517   8273  -1610    274   -169       C  
ATOM   2394  CG1 ILE A 288       5.373 -28.366 106.867  1.00 59.51           C  
ANISOU 2394  CG1 ILE A 288     8982   4307   9324  -1554    380   -198       C  
ATOM   2395  CG2 ILE A 288       4.796 -26.986 108.887  1.00 44.55           C  
ANISOU 2395  CG2 ILE A 288     6938   2634   7353  -1486    203    111       C  
ATOM   2396  CD1 ILE A 288       6.685 -27.783 106.399  1.00 51.00           C  
ANISOU 2396  CD1 ILE A 288     7932   3248   8198  -1332    319   -142       C  
ATOM   2397  N   SER A 289       2.342 -29.028 105.333  1.00 86.80           N  
ANISOU 2397  N   SER A 289    12357   7914  12710  -2175    496   -825       N  
ATOM   2398  CA  SER A 289       1.733 -29.102 104.009  1.00 77.52           C  
ANISOU 2398  CA  SER A 289    11181   6843  11428  -2354    507  -1155       C  
ATOM   2399  C   SER A 289       0.214 -29.058 104.088  1.00 69.19           C  
ANISOU 2399  C   SER A 289     9991   5993  10304  -2619    473  -1339       C  
ATOM   2400  O   SER A 289      -0.434 -28.584 103.151  1.00 79.05           O  
ANISOU 2400  O   SER A 289    11177   7473  11385  -2741    388  -1592       O  
ATOM   2401  CB  SER A 289       2.180 -30.377 103.287  1.00 80.69           C  
ANISOU 2401  CB  SER A 289    11702   7037  11918  -2413    674  -1281       C  
ATOM   2402  OG  SER A 289       3.589 -30.506 103.265  1.00 81.75           O  
ANISOU 2402  OG  SER A 289    11938   7003  12120  -2173    709  -1111       O  
ATOM   2403  N   ASN A 290      -0.359 -29.522 105.193  1.00 68.27           N  
ANISOU 2403  N   ASN A 290     9818   5829  10294  -2705    529  -1216       N  
ATOM   2404  CA  ASN A 290      -1.796 -29.781 105.325  1.00 74.38           C  
ANISOU 2404  CA  ASN A 290    10452   6773  11038  -2980    540  -1395       C  
ATOM   2405  C   ASN A 290      -2.490 -28.789 106.257  1.00 73.91           C  
ANISOU 2405  C   ASN A 290    10237   6927  10916  -2977    418  -1277       C  
ATOM   2406  O   ASN A 290      -3.195 -29.224 107.165  1.00 75.09           O  
ANISOU 2406  O   ASN A 290    10315   7068  11146  -3097    486  -1210       O  
ATOM   2407  CB  ASN A 290      -2.010 -31.202 105.848  1.00 76.82           C  
ANISOU 2407  CB  ASN A 290    10818   6848  11522  -3115    739  -1369       C  
ATOM   2408  CG  ASN A 290      -1.748 -32.281 104.808  1.00 79.00           C  
ANISOU 2408  CG  ASN A 290    11208   6965  11845  -3216    883  -1584       C  
ATOM   2409  OD1 ASN A 290      -1.183 -32.028 103.746  1.00 66.59           O  
ANISOU 2409  OD1 ASN A 290     9695   5421  10187  -3146    843  -1711       O  
ATOM   2410  ND2 ASN A 290      -2.132 -33.509 105.135  1.00 93.98           N  
ANISOU 2410  ND2 ASN A 290    13145   8680  13882  -3381   1071  -1623       N  
ATOM   2411  N   GLN A 291      -2.338 -27.473 106.105  1.00 73.28           N  
ANISOU 2411  N   GLN A 291    10107   7040  10698  -2849    256  -1250       N  
ATOM   2412  CA  GLN A 291      -2.872 -26.536 107.098  1.00 80.43           C  
ANISOU 2412  CA  GLN A 291    10878   8123  11558  -2826    162  -1112       C  
ATOM   2413  C   GLN A 291      -4.252 -26.022 106.692  1.00 78.08           C  
ANISOU 2413  C   GLN A 291    10365   8214  11087  -3024     39  -1360       C  
ATOM   2414  O   GLN A 291      -4.371 -25.153 105.825  1.00 68.92           O  
ANISOU 2414  O   GLN A 291     9152   7302   9732  -2993   -117  -1510       O  
ATOM   2415  CB  GLN A 291      -1.913 -25.375 107.352  1.00 74.32           C  
ANISOU 2415  CB  GLN A 291    10166   7335  10736  -2565     69   -914       C  
ATOM   2416  CG  GLN A 291      -1.032 -24.946 106.203  1.00 71.82           C  
ANISOU 2416  CG  GLN A 291     9968   6989  10330  -2428     20   -999       C  
ATOM   2417  CD  GLN A 291       0.108 -24.072 106.693  1.00 67.81           C  
ANISOU 2417  CD  GLN A 291     9539   6384   9842  -2149    -13   -745       C  
ATOM   2418  OE1 GLN A 291       0.460 -24.104 107.874  1.00 68.61           O  
ANISOU 2418  OE1 GLN A 291     9623   6388  10059  -2038     23   -495       O  
ATOM   2419  NE2 GLN A 291       0.667 -23.262 105.801  1.00 55.95           N  
ANISOU 2419  NE2 GLN A 291     8117   4934   8209  -2032    -83   -811       N  
ATOM   2420  N   PHE A 292      -5.287 -26.522 107.369  1.00 81.38           N  
ANISOU 2420  N   PHE A 292    10645   8713  11563  -3206     97  -1386       N  
ATOM   2421  CA  PHE A 292      -6.672 -26.157 107.106  1.00 77.99           C  
ANISOU 2421  CA  PHE A 292     9962   8687  10984  -3381    -17  -1606       C  
ATOM   2422  C   PHE A 292      -7.210 -25.260 108.214  1.00 75.42           C  
ANISOU 2422  C   PHE A 292     9477   8556  10624  -3340    -92  -1447       C  
ATOM   2423  O   PHE A 292      -6.964 -25.503 109.400  1.00 71.08           O  
ANISOU 2423  O   PHE A 292     8987   7802  10219  -3304     24  -1209       O  
ATOM   2424  CB  PHE A 292      -7.539 -27.408 106.994  1.00 76.53           C  
ANISOU 2424  CB  PHE A 292     9717   8476  10884  -3637    119  -1784       C  
ATOM   2425  CG  PHE A 292      -6.955 -28.462 106.107  1.00 74.24           C  
ANISOU 2425  CG  PHE A 292     9605   7936  10665  -3690    243  -1913       C  
ATOM   2426  CD1 PHE A 292      -6.837 -28.251 104.745  1.00 77.49           C  
ANISOU 2426  CD1 PHE A 292    10023   8503  10916  -3691    144  -2146       C  
ATOM   2427  CD2 PHE A 292      -6.498 -29.656 106.640  1.00 77.32           C  
ANISOU 2427  CD2 PHE A 292    10161   7949  11268  -3724    459  -1792       C  
ATOM   2428  CE1 PHE A 292      -6.294 -29.222 103.925  1.00 83.19           C  
ANISOU 2428  CE1 PHE A 292    10908   9002  11700  -3745    273  -2274       C  
ATOM   2429  CE2 PHE A 292      -5.952 -30.628 105.826  1.00 80.97           C  
ANISOU 2429  CE2 PHE A 292    10782   8189  11796  -3765    583  -1914       C  
ATOM   2430  CZ  PHE A 292      -5.852 -30.411 104.467  1.00 87.10           C  
ANISOU 2430  CZ  PHE A 292    11559   9115  12421  -3783    496  -2162       C  
ATOM   2431  N   VAL A 293      -7.946 -24.217 107.823  1.00 83.00           N  
ANISOU 2431  N   VAL A 293    10224   9939  11373  -3323   -292  -1571       N  
ATOM   2432  CA  VAL A 293      -8.591 -23.318 108.773  1.00 88.33           C  
ANISOU 2432  CA  VAL A 293    10707  10868  11988  -3280   -375  -1453       C  
ATOM   2433  C   VAL A 293     -10.007 -23.010 108.306  1.00 91.15           C  
ANISOU 2433  C   VAL A 293    10752  11703  12180  -3366   -517  -1676       C  
ATOM   2434  O   VAL A 293     -10.316 -23.033 107.108  1.00 91.00           O  
ANISOU 2434  O   VAL A 293    10667  11893  12015  -3383   -626  -1899       O  
ATOM   2435  CB  VAL A 293      -7.786 -22.013 108.984  1.00 83.46           C  
ANISOU 2435  CB  VAL A 293    10155  10293  11265  -3054   -505  -1272       C  
ATOM   2436  CG1 VAL A 293      -6.332 -22.337 109.147  1.00 86.46           C  
ANISOU 2436  CG1 VAL A 293    10845  10220  11785  -2941   -382  -1085       C  
ATOM   2437  CG2 VAL A 293      -7.988 -21.046 107.822  1.00 79.61           C  
ANISOU 2437  CG2 VAL A 293     9567  10162  10521  -2861   -734  -1397       C  
ATOM   2438  N   ALA A 294     -10.873 -22.726 109.275  1.00 84.97           N  
ANISOU 2438  N   ALA A 294     9772  11102  11411  -3400   -510  -1604       N  
ATOM   2439  CA  ALA A 294     -12.252 -22.345 109.006  1.00 83.02           C  
ANISOU 2439  CA  ALA A 294     9204  11320  11018  -3432   -638  -1772       C  
ATOM   2440  C   ALA A 294     -12.371 -20.825 108.967  1.00 73.63           C  
ANISOU 2440  C   ALA A 294     7858  10489   9627  -3164   -859  -1691       C  
ATOM   2441  O   ALA A 294     -11.831 -20.127 109.833  1.00 70.78           O  
ANISOU 2441  O   ALA A 294     7554  10049   9291  -3036   -856  -1471       O  
ATOM   2442  CB  ALA A 294     -13.196 -22.921 110.063  1.00 84.98           C  
ANISOU 2442  CB  ALA A 294     9319  11572  11398  -3610   -487  -1748       C  
ATOM   2443  N   PHE A 295     -13.078 -20.320 107.959  1.00 77.10           N  
ANISOU 2443  N   PHE A 295     8109  11327   9858  -3061  -1047  -1854       N  
ATOM   2444  CA  PHE A 295     -13.363 -18.899 107.824  1.00 77.77           C  
ANISOU 2444  CA  PHE A 295     8029  11782   9738  -2752  -1255  -1769       C  
ATOM   2445  C   PHE A 295     -14.773 -18.758 107.279  1.00 82.10           C  
ANISOU 2445  C   PHE A 295     8281  12767  10148  -2730  -1364  -1933       C  
ATOM   2446  O   PHE A 295     -15.136 -19.454 106.326  1.00 81.36           O  
ANISOU 2446  O   PHE A 295     8161  12751  10001  -2869  -1378  -2145       O  
ATOM   2447  CB  PHE A 295     -12.360 -18.207 106.900  1.00 74.22           C  
ANISOU 2447  CB  PHE A 295     7749  11322   9129  -2525  -1395  -1730       C  
ATOM   2448  CG  PHE A 295     -12.754 -16.811 106.530  1.00 71.41           C  
ANISOU 2448  CG  PHE A 295     7239  11353   8540  -2163  -1602  -1645       C  
ATOM   2449  CD1 PHE A 295     -12.758 -15.808 107.483  1.00 67.14           C  
ANISOU 2449  CD1 PHE A 295     6654  10844   8013  -1929  -1607  -1415       C  
ATOM   2450  CD2 PHE A 295     -13.125 -16.498 105.234  1.00 82.16           C  
ANISOU 2450  CD2 PHE A 295     8540  12996   9679  -2009  -1756  -1756       C  
ATOM   2451  CE1 PHE A 295     -13.117 -14.524 107.150  1.00 73.08           C  
ANISOU 2451  CE1 PHE A 295     7289  11905   8572  -1567  -1765  -1319       C  
ATOM   2452  CE2 PHE A 295     -13.490 -15.213 104.899  1.00 86.68           C  
ANISOU 2452  CE2 PHE A 295     9006  13876  10053  -1636  -1915  -1633       C  
ATOM   2453  CZ  PHE A 295     -13.480 -14.222 105.857  1.00 84.97           C  
ANISOU 2453  CZ  PHE A 295     8740  13680   9865  -1412  -1915  -1417       C  
ATOM   2454  N   ARG A 296     -15.555 -17.851 107.870  1.00 93.01           N  
ANISOU 2454  N   ARG A 296     9442  14430  11469  -2551  -1432  -1834       N  
ATOM   2455  CA  ARG A 296     -17.018 -17.867 107.754  1.00107.87           C  
ANISOU 2455  CA  ARG A 296    11022  16678  13288  -2585  -1472  -1969       C  
ATOM   2456  C   ARG A 296     -17.448 -19.277 108.148  1.00109.07           C  
ANISOU 2456  C   ARG A 296    11166  16650  13626  -2980  -1276  -2122       C  
ATOM   2457  O   ARG A 296     -17.220 -19.662 109.310  1.00107.90           O  
ANISOU 2457  O   ARG A 296    11096  16236  13664  -3117  -1103  -2007       O  
ATOM   2458  CB  ARG A 296     -17.438 -17.371 106.359  1.00108.18           C  
ANISOU 2458  CB  ARG A 296    10958  17066  13081  -2390  -1672  -2078       C  
ATOM   2459  CG  ARG A 296     -17.917 -15.911 106.341  1.00104.72           C  
ANISOU 2459  CG  ARG A 296    10363  16949  12476  -1991  -1823  -1924       C  
ATOM   2460  CD  ARG A 296     -16.843 -14.920 105.847  1.00 89.41           C  
ANISOU 2460  CD  ARG A 296     8633  14931  10408  -1657  -1932  -1743       C  
ATOM   2461  NE  ARG A 296     -17.188 -13.531 106.167  1.00 88.79           N  
ANISOU 2461  NE  ARG A 296     8455  15043  10238  -1276  -2007  -1545       N  
ATOM   2462  CZ  ARG A 296     -16.735 -12.461 105.516  1.00 88.70           C  
ANISOU 2462  CZ  ARG A 296     8553  15087  10063   -911  -2115  -1395       C  
ATOM   2463  NH1 ARG A 296     -15.903 -12.605 104.494  1.00 92.40           N  
ANISOU 2463  NH1 ARG A 296     9225  15462  10420   -878  -2177  -1420       N  
ATOM   2464  NH2 ARG A 296     -17.118 -11.244 105.888  1.00 89.30           N  
ANISOU 2464  NH2 ARG A 296     8548  15292  10090   -577  -2139  -1216       N  
ATOM   2465  N   ARG A 297     -18.030 -20.081 107.255  1.00107.22           N  
ANISOU 2465  N   ARG A 297    10856  16534  13350  -3167  -1281  -2365       N  
ATOM   2466  CA  ARG A 297     -18.210 -21.497 107.549  1.00112.95           C  
ANISOU 2466  CA  ARG A 297    11645  17005  14266  -3538  -1068  -2502       C  
ATOM   2467  C   ARG A 297     -17.462 -22.412 106.582  1.00125.38           C  
ANISOU 2467  C   ARG A 297    13444  18335  15860  -3687  -1020  -2647       C  
ATOM   2468  O   ARG A 297     -17.176 -23.566 106.932  1.00131.65           O  
ANISOU 2468  O   ARG A 297    14398  18772  16851  -3944   -808  -2686       O  
ATOM   2469  CB  ARG A 297     -19.705 -21.865 107.559  1.00119.80           C  
ANISOU 2469  CB  ARG A 297    12207  18197  15113  -3704  -1049  -2695       C  
ATOM   2470  CG  ARG A 297     -20.033 -23.366 107.583  1.00123.77           C  
ANISOU 2470  CG  ARG A 297    12754  18495  15779  -4092   -839  -2892       C  
ATOM   2471  CD  ARG A 297     -19.539 -24.038 108.887  1.00120.04           C  
ANISOU 2471  CD  ARG A 297    12479  17571  15561  -4249   -590  -2722       C  
ATOM   2472  NE  ARG A 297     -20.585 -24.402 109.848  1.00122.32           N  
ANISOU 2472  NE  ARG A 297    12588  17933  15954  -4426   -448  -2743       N  
ATOM   2473  CZ  ARG A 297     -20.460 -24.292 111.171  1.00122.68           C  
ANISOU 2473  CZ  ARG A 297    12688  17795  16131  -4418   -316  -2525       C  
ATOM   2474  NH1 ARG A 297     -19.337 -23.823 111.693  1.00115.79           N  
ANISOU 2474  NH1 ARG A 297    12034  16664  15299  -4245   -312  -2273       N  
ATOM   2475  NH2 ARG A 297     -21.454 -24.650 111.975  1.00125.36           N  
ANISOU 2475  NH2 ARG A 297    12861  18217  16551  -4588   -181  -2561       N  
ATOM   2476  N   LYS A 298     -17.093 -21.922 105.399  1.00128.23           N  
ANISOU 2476  N   LYS A 298    13840  18859  16024  -3515  -1196  -2708       N  
ATOM   2477  CA  LYS A 298     -16.351 -22.745 104.456  1.00124.10           C  
ANISOU 2477  CA  LYS A 298    13535  18109  15507  -3645  -1144  -2850       C  
ATOM   2478  C   LYS A 298     -14.909 -22.951 104.918  1.00119.47           C  
ANISOU 2478  C   LYS A 298    13285  17024  15083  -3623  -1020  -2670       C  
ATOM   2479  O   LYS A 298     -14.287 -22.068 105.522  1.00120.46           O  
ANISOU 2479  O   LYS A 298    13480  17081  15210  -3412  -1070  -2442       O  
ATOM   2480  CB  LYS A 298     -16.386 -22.121 103.065  1.00121.20           C  
ANISOU 2480  CB  LYS A 298    13111  18079  14860  -3454  -1366  -2956       C  
ATOM   2481  CG  LYS A 298     -17.593 -22.564 102.249  1.00121.89           C  
ANISOU 2481  CG  LYS A 298    12949  18543  14819  -3601  -1422  -3229       C  
ATOM   2482  CD  LYS A 298     -17.568 -24.068 102.053  1.00124.57           C  
ANISOU 2482  CD  LYS A 298    13394  18619  15319  -3972  -1215  -3453       C  
ATOM   2483  CE  LYS A 298     -16.290 -24.495 101.366  1.00119.71           C  
ANISOU 2483  CE  LYS A 298    13098  17666  14721  -3979  -1159  -3470       C  
ATOM   2484  NZ  LYS A 298     -15.739 -25.739 101.949  1.00117.50           N  
ANISOU 2484  NZ  LYS A 298    13041  16877  14725  -4236   -882  -3481       N  
ATOM   2485  N   ILE A 299     -14.388 -24.142 104.630  1.00118.87           N  
ANISOU 2485  N   ILE A 299    13415  16601  15149  -3837   -845  -2776       N  
ATOM   2486  CA  ILE A 299     -13.058 -24.567 105.057  1.00121.80           C  
ANISOU 2486  CA  ILE A 299    14112  16460  15707  -3831   -687  -2611       C  
ATOM   2487  C   ILE A 299     -12.067 -24.261 103.947  1.00121.12           C  
ANISOU 2487  C   ILE A 299    14208  16321  15490  -3685   -783  -2651       C  
ATOM   2488  O   ILE A 299     -12.399 -24.370 102.757  1.00129.75           O  
ANISOU 2488  O   ILE A 299    15236  17653  16410  -3714   -880  -2871       O  
ATOM   2489  CB  ILE A 299     -13.060 -26.067 105.409  1.00128.78           C  
ANISOU 2489  CB  ILE A 299    15126  16974  16830  -4106   -419  -2675       C  
ATOM   2490  CG1 ILE A 299     -13.816 -26.297 106.717  1.00131.44           C  
ANISOU 2490  CG1 ILE A 299    15340  17290  17310  -4219   -298  -2567       C  
ATOM   2491  CG2 ILE A 299     -11.644 -26.627 105.494  1.00129.42           C  
ANISOU 2491  CG2 ILE A 299    15553  16544  17077  -4060   -265  -2534       C  
ATOM   2492  CD1 ILE A 299     -13.441 -27.571 107.414  1.00132.93           C  
ANISOU 2492  CD1 ILE A 299    15738  17013  17757  -4391    -22  -2488       C  
ATOM   2493  N   TYR A 300     -10.845 -23.876 104.323  1.00104.25           N  
ANISOU 2493  N   TYR A 300    12302  13882  13428  -3530   -751  -2439       N  
ATOM   2494  CA  TYR A 300      -9.841 -23.495 103.345  1.00 93.22           C  
ANISOU 2494  CA  TYR A 300    11091  12423  11907  -3377   -830  -2459       C  
ATOM   2495  C   TYR A 300      -8.476 -24.038 103.743  1.00 90.84           C  
ANISOU 2495  C   TYR A 300    11109  11579  11826  -3360   -638  -2299       C  
ATOM   2496  O   TYR A 300      -8.099 -24.011 104.921  1.00 88.56           O  
ANISOU 2496  O   TYR A 300    10889  11047  11713  -3325   -536  -2067       O  
ATOM   2497  CB  TYR A 300      -9.764 -21.971 103.202  1.00 79.49           C  
ANISOU 2497  CB  TYR A 300     9262  11003   9936  -3094  -1065  -2348       C  
ATOM   2498  CG  TYR A 300     -11.007 -21.306 102.654  1.00 84.47           C  
ANISOU 2498  CG  TYR A 300     9590  12188  10319  -3005  -1275  -2459       C  
ATOM   2499  CD1 TYR A 300     -11.197 -21.171 101.286  1.00 93.67           C  
ANISOU 2499  CD1 TYR A 300    10725  13625  11242  -2936  -1411  -2629       C  
ATOM   2500  CD2 TYR A 300     -11.976 -20.783 103.502  1.00 84.39           C  
ANISOU 2500  CD2 TYR A 300     9327  12427  10310  -2960  -1331  -2373       C  
ATOM   2501  CE1 TYR A 300     -12.326 -20.550 100.776  1.00 99.93           C  
ANISOU 2501  CE1 TYR A 300    11244  14917  11807  -2814  -1599  -2694       C  
ATOM   2502  CE2 TYR A 300     -13.108 -20.160 103.000  1.00 92.37           C  
ANISOU 2502  CE2 TYR A 300    10062  13927  11107  -2836  -1509  -2447       C  
ATOM   2503  CZ  TYR A 300     -13.278 -20.048 101.633  1.00 99.46           C  
ANISOU 2503  CZ  TYR A 300    10937  15082  11772  -2758  -1645  -2599       C  
ATOM   2504  OH  TYR A 300     -14.398 -19.436 101.111  1.00100.70           O  
ANISOU 2504  OH  TYR A 300    10826  15718  11717  -2613  -1814  -2649       O  
ATOM   2505  N   LYS A 301      -7.733 -24.518 102.749  1.00 82.83           N  
ANISOU 2505  N   LYS A 301    10285  10393  10794  -3360   -587  -2411       N  
ATOM   2506  CA  LYS A 301      -6.327 -24.861 102.902  1.00 73.71           C  
ANISOU 2506  CA  LYS A 301     9427   8769   9810  -3262   -434  -2251       C  
ATOM   2507  C   LYS A 301      -5.474 -23.626 102.644  1.00 70.75           C  
ANISOU 2507  C   LYS A 301     9153   8439   9289  -3020   -567  -2134       C  
ATOM   2508  O   LYS A 301      -5.642 -22.946 101.622  1.00 59.49           O  
ANISOU 2508  O   LYS A 301     7676   7328   7600  -2944   -739  -2277       O  
ATOM   2509  CB  LYS A 301      -5.934 -25.983 101.937  1.00 73.35           C  
ANISOU 2509  CB  LYS A 301     9531   8522   9817  -3367   -299  -2431       C  
ATOM   2510  CG  LYS A 301      -4.434 -26.180 101.786  1.00 82.13           C  
ANISOU 2510  CG  LYS A 301    10925   9231  11049  -3201   -178  -2286       C  
ATOM   2511  CD  LYS A 301      -4.121 -27.329 100.831  1.00 90.28           C  
ANISOU 2511  CD  LYS A 301    12081  10092  12129  -3309    -36  -2477       C  
ATOM   2512  CE  LYS A 301      -2.673 -27.309 100.344  1.00 83.14           C  
ANISOU 2512  CE  LYS A 301    11416   8903  11269  -3109     37  -2379       C  
ATOM   2513  NZ  LYS A 301      -1.689 -27.460 101.450  1.00 84.20           N  
ANISOU 2513  NZ  LYS A 301    11674   8678  11641  -2930    153  -2047       N  
ATOM   2514  N   TRP A 302      -4.571 -23.339 103.580  1.00 77.02           N  
ANISOU 2514  N   TRP A 302    10093   8932  10239  -2886   -487  -1862       N  
ATOM   2515  CA  TRP A 302      -3.638 -22.230 103.468  1.00 71.89           C  
ANISOU 2515  CA  TRP A 302     9575   8254   9487  -2621   -572  -1694       C  
ATOM   2516  C   TRP A 302      -2.394 -22.697 102.722  1.00 80.03           C  
ANISOU 2516  C   TRP A 302    10872   8948  10587  -2569   -448  -1721       C  
ATOM   2517  O   TRP A 302      -1.741 -23.663 103.133  1.00 95.18           O  
ANISOU 2517  O   TRP A 302    12899  10511  12753  -2552   -261  -1606       O  
ATOM   2518  CB  TRP A 302      -3.264 -21.709 104.856  1.00 64.33           C  
ANISOU 2518  CB  TRP A 302     8626   7156   8662  -2448   -541  -1358       C  
ATOM   2519  CG  TRP A 302      -2.351 -20.530 104.831  1.00 62.97           C  
ANISOU 2519  CG  TRP A 302     8552   6974   8400  -2092   -620  -1133       C  
ATOM   2520  CD1 TRP A 302      -0.985 -20.541 104.880  1.00 65.81           C  
ANISOU 2520  CD1 TRP A 302     9130   6998   8875  -1941   -518   -979       C  
ATOM   2521  CD2 TRP A 302      -2.739 -19.157 104.737  1.00 59.99           C  
ANISOU 2521  CD2 TRP A 302     8053   6933   7809  -1846   -800  -1044       C  
ATOM   2522  NE1 TRP A 302      -0.501 -19.255 104.829  1.00 63.94           N  
ANISOU 2522  NE1 TRP A 302     8913   6870   8512  -1642   -619   -815       N  
ATOM   2523  CE2 TRP A 302      -1.558 -18.387 104.740  1.00 60.25           C  
ANISOU 2523  CE2 TRP A 302     8253   6794   7844  -1574   -784   -845       C  
ATOM   2524  CE3 TRP A 302      -3.971 -18.504 104.654  1.00 56.46           C  
ANISOU 2524  CE3 TRP A 302     7365   6911   7176  -1822   -962  -1113       C  
ATOM   2525  CZ2 TRP A 302      -1.576 -16.997 104.662  1.00 59.24           C  
ANISOU 2525  CZ2 TRP A 302     8084   6875   7549  -1296   -905   -717       C  
ATOM   2526  CZ3 TRP A 302      -3.987 -17.128 104.576  1.00 55.01           C  
ANISOU 2526  CZ3 TRP A 302     7140   6938   6824  -1515  -1090   -969       C  
ATOM   2527  CH2 TRP A 302      -2.797 -16.388 104.582  1.00 54.51           C  
ANISOU 2527  CH2 TRP A 302     7271   6665   6775  -1262  -1052   -773       C  
ATOM   2528  N   ASN A 303      -2.074 -22.010 101.627  1.00 68.94           N  
ANISOU 2528  N   ASN A 303     9521   7715   8958  -2398   -560  -1786       N  
ATOM   2529  CA  ASN A 303      -0.973 -22.384 100.753  1.00 80.39           C  
ANISOU 2529  CA  ASN A 303    11208   8902  10433  -2357   -447  -1852       C  
ATOM   2530  C   ASN A 303       0.239 -21.468 100.876  1.00 72.89           C  
ANISOU 2530  C   ASN A 303    10406   7800   9487  -2020   -443  -1578       C  
ATOM   2531  O   ASN A 303       1.309 -21.814 100.363  1.00 89.54           O  
ANISOU 2531  O   ASN A 303    12716   9633  11674  -1973   -315  -1590       O  
ATOM   2532  CB  ASN A 303      -1.451 -22.401  99.291  1.00 90.93           C  
ANISOU 2532  CB  ASN A 303    12513  10542  11493  -2437   -547  -2158       C  
ATOM   2533  CG  ASN A 303      -0.800 -23.500  98.474  1.00 94.93           C  
ANISOU 2533  CG  ASN A 303    13167  10797  12106  -2496   -374  -2292       C  
ATOM   2534  OD1 ASN A 303       0.369 -23.833  98.661  1.00 90.43           O  
ANISOU 2534  OD1 ASN A 303    12766   9859  11734  -2367   -215  -2131       O  
ATOM   2535  ND2 ASN A 303      -1.567 -24.071  97.550  1.00105.34           N  
ANISOU 2535  ND2 ASN A 303    14392  12348  13284  -2664   -412  -2568       N  
ATOM   2536  N   HIS A 304       0.108 -20.319 101.539  1.00 63.94           N  
ANISOU 2536  N   HIS A 304     9176   6835   8281  -1797   -565  -1348       N  
ATOM   2537  CA  HIS A 304       1.119 -19.261 101.495  1.00 63.19           C  
ANISOU 2537  CA  HIS A 304     9198   6671   8142  -1487   -579  -1130       C  
ATOM   2538  C   HIS A 304       2.036 -19.369 102.710  1.00 60.75           C  
ANISOU 2538  C   HIS A 304     8960   6029   8093  -1416   -460   -886       C  
ATOM   2539  O   HIS A 304       1.770 -18.791 103.763  1.00 45.32           O  
ANISOU 2539  O   HIS A 304     6901   4149   6171  -1337   -514   -708       O  
ATOM   2540  CB  HIS A 304       0.444 -17.897 101.429  1.00 55.78           C  
ANISOU 2540  CB  HIS A 304     8124   6106   6965  -1280   -765  -1040       C  
ATOM   2541  CG  HIS A 304       1.394 -16.758 101.225  1.00 61.78           C  
ANISOU 2541  CG  HIS A 304     9010   6805   7658   -982   -763   -851       C  
ATOM   2542  ND1 HIS A 304       2.421 -16.798 100.307  1.00 67.67           N  
ANISOU 2542  ND1 HIS A 304     9952   7383   8378   -906   -673   -884       N  
ATOM   2543  CD2 HIS A 304       1.466 -15.542 101.815  1.00 65.24           C  
ANISOU 2543  CD2 HIS A 304     9409   7322   8058   -755   -819   -641       C  
ATOM   2544  CE1 HIS A 304       3.087 -15.658 100.342  1.00 70.01           C  
ANISOU 2544  CE1 HIS A 304    10321   7655   8626   -654   -672   -697       C  
ATOM   2545  NE2 HIS A 304       2.526 -14.877 101.247  1.00 68.24           N  
ANISOU 2545  NE2 HIS A 304     9961   7572   8397   -560   -758   -552       N  
ATOM   2546  N   GLY A 305       3.139 -20.101 102.548  1.00 62.60           N  
ANISOU 2546  N   GLY A 305     9370   5912   8503  -1432   -296   -881       N  
ATOM   2547  CA  GLY A 305       4.153 -20.193 103.583  1.00 52.61           C  
ANISOU 2547  CA  GLY A 305     8096   4427   7467  -1277   -188   -629       C  
ATOM   2548  C   GLY A 305       3.644 -20.833 104.866  1.00 55.56           C  
ANISOU 2548  C   GLY A 305     8326   4776   8006  -1368   -151   -523       C  
ATOM   2549  O   GLY A 305       2.620 -21.522 104.898  1.00 62.04           O  
ANISOU 2549  O   GLY A 305     9094   5647   8831  -1600   -155   -663       O  
ATOM   2550  N   LEU A 306       4.401 -20.607 105.938  1.00 55.73           N  
ANISOU 2550  N   LEU A 306     8266   4750   8161  -1179   -101   -281       N  
ATOM   2551  CA  LEU A 306       3.905 -20.893 107.276  1.00 45.23           C  
ANISOU 2551  CA  LEU A 306     6828   3431   6926  -1233    -77   -151       C  
ATOM   2552  C   LEU A 306       2.828 -19.885 107.643  1.00 48.47           C  
ANISOU 2552  C   LEU A 306     7237   4030   7148  -1329   -244   -148       C  
ATOM   2553  O   LEU A 306       2.903 -18.710 107.273  1.00 46.36           O  
ANISOU 2553  O   LEU A 306     7001   3886   6728  -1204   -380   -128       O  
ATOM   2554  CB  LEU A 306       5.026 -20.820 108.304  1.00 37.22           C  
ANISOU 2554  CB  LEU A 306     5723   2383   6036  -1005     28     76       C  
ATOM   2555  CG  LEU A 306       6.334 -21.559 108.042  1.00 34.52           C  
ANISOU 2555  CG  LEU A 306     5344   1965   5806   -862    -21    154       C  
ATOM   2556  CD1 LEU A 306       7.392 -20.973 108.933  1.00 52.41           C  
ANISOU 2556  CD1 LEU A 306     7470   4350   8095   -647     26    322       C  
ATOM   2557  CD2 LEU A 306       6.158 -23.028 108.340  1.00 44.41           C  
ANISOU 2557  CD2 LEU A 306     6716   3075   7085  -1005    -68    186       C  
ATOM   2558  N   LEU A 307       1.828 -20.340 108.384  1.00 41.09           N  
ANISOU 2558  N   LEU A 307     6211   3152   6250  -1517   -249   -153       N  
ATOM   2559  CA  LEU A 307       0.711 -19.483 108.741  1.00 55.98           C  
ANISOU 2559  CA  LEU A 307     7943   5348   7981  -1544   -402   -160       C  
ATOM   2560  C   LEU A 307       0.852 -19.024 110.185  1.00 52.80           C  
ANISOU 2560  C   LEU A 307     7486   4951   7625  -1450   -401     78       C  
ATOM   2561  O   LEU A 307       1.164 -19.815 111.080  1.00 55.94           O  
ANISOU 2561  O   LEU A 307     7910   5176   8167  -1494   -269    197       O  
ATOM   2562  CB  LEU A 307      -0.619 -20.199 108.491  1.00 72.25           C  
ANISOU 2562  CB  LEU A 307     9874   7563  10016  -1813   -404   -368       C  
ATOM   2563  CG  LEU A 307      -1.900 -19.514 108.934  1.00 75.00           C  
ANISOU 2563  CG  LEU A 307     9991   8278  10229  -1833   -526   -390       C  
ATOM   2564  CD1 LEU A 307      -1.970 -18.147 108.280  1.00 80.12           C  
ANISOU 2564  CD1 LEU A 307    10584   9196  10661  -1587   -690   -395       C  
ATOM   2565  CD2 LEU A 307      -3.055 -20.389 108.454  1.00 74.46           C  
ANISOU 2565  CD2 LEU A 307     9798   8341  10152  -2130   -511   -645       C  
ATOM   2566  N   GLN A 308       0.665 -17.726 110.386  1.00 48.97           N  
ANISOU 2566  N   GLN A 308     6912   4698   6996  -1272   -520    139       N  
ATOM   2567  CA  GLN A 308       0.881 -17.112 111.683  1.00 47.84           C  
ANISOU 2567  CA  GLN A 308     6723   4586   6867  -1166   -525    338       C  
ATOM   2568  C   GLN A 308      -0.168 -17.587 112.680  1.00 47.84           C  
ANISOU 2568  C   GLN A 308     6591   4692   6893  -1339   -497    363       C  
ATOM   2569  O   GLN A 308      -1.293 -17.942 112.315  1.00 53.17           O  
ANISOU 2569  O   GLN A 308     7152   5524   7528  -1504   -517    207       O  
ATOM   2570  CB  GLN A 308       0.834 -15.595 111.544  1.00 52.49           C  
ANISOU 2570  CB  GLN A 308     7255   5387   7300   -951   -634    359       C  
ATOM   2571  CG  GLN A 308       1.595 -15.089 110.340  1.00 50.55           C  
ANISOU 2571  CG  GLN A 308     7129   5080   6996   -805   -656    301       C  
ATOM   2572  CD  GLN A 308       1.739 -13.591 110.335  1.00 63.28           C  
ANISOU 2572  CD  GLN A 308     8725   6829   8490   -582   -717    361       C  
ATOM   2573  OE1 GLN A 308       1.421 -12.919 111.317  1.00 66.97           O  
ANISOU 2573  OE1 GLN A 308     9101   7409   8935   -528   -737    448       O  
ATOM   2574  NE2 GLN A 308       2.218 -13.051 109.223  1.00 85.38           N  
ANISOU 2574  NE2 GLN A 308    11623   9608  11211   -453   -729    311       N  
ATOM   2575  N   GLY A 309       0.218 -17.609 113.954  1.00 51.37           N  
ANISOU 2575  N   GLY A 309     7048   5068   7402  -1307   -446    557       N  
ATOM   2576  CA  GLY A 309      -0.632 -18.126 115.002  1.00 41.58           C  
ANISOU 2576  CA  GLY A 309     5712   3893   6192  -1467   -387    614       C  
ATOM   2577  C   GLY A 309      -0.535 -19.620 115.229  1.00 49.78           C  
ANISOU 2577  C   GLY A 309     6840   4684   7390  -1643   -222    639       C  
ATOM   2578  O   GLY A 309      -1.139 -20.122 116.183  1.00 52.84           O  
ANISOU 2578  O   GLY A 309     7170   5101   7804  -1757   -132    708       O  
ATOM   2579  N   ASP A 310       0.193 -20.351 114.384  1.00 54.04           N  
ANISOU 2579  N   ASP A 310     7493   5038   8003  -1592   -120    548       N  
ATOM   2580  CA  ASP A 310       0.335 -21.793 114.569  1.00 48.90           C  
ANISOU 2580  CA  ASP A 310     6896   4183   7500  -1658    108    534       C  
ATOM   2581  C   ASP A 310       1.526 -22.094 115.478  1.00 39.26           C  
ANISOU 2581  C   ASP A 310     5800   2859   6256  -1447    245    712       C  
ATOM   2582  O   ASP A 310       2.565 -21.437 115.373  1.00 38.45           O  
ANISOU 2582  O   ASP A 310     5747   2793   6069  -1237    187    761       O  
ATOM   2583  CB  ASP A 310       0.521 -22.492 113.226  1.00 51.08           C  
ANISOU 2583  CB  ASP A 310     7196   4312   7902  -1710    140    352       C  
ATOM   2584  CG  ASP A 310       0.769 -23.980 113.367  1.00 55.44           C  
ANISOU 2584  CG  ASP A 310     7750   4677   8637  -1732    155    444       C  
ATOM   2585  OD1 ASP A 310      -0.209 -24.744 113.412  1.00 58.43           O  
ANISOU 2585  OD1 ASP A 310     8119   5023   9058  -1983    180    375       O  
ATOM   2586  OD2 ASP A 310       1.943 -24.388 113.433  1.00 60.38           O1-
ANISOU 2586  OD2 ASP A 310     8509   5222   9212  -1583     75    584       O1-
ATOM   2587  N   PRO A 311       1.389 -23.080 116.372  1.00 41.34           N  
ANISOU 2587  N   PRO A 311     6132   3041   6533  -1505    395    796       N  
ATOM   2588  CA  PRO A 311       2.415 -23.285 117.413  1.00 45.37           C  
ANISOU 2588  CA  PRO A 311     6798   3526   6915  -1341    411    980       C  
ATOM   2589  C   PRO A 311       3.822 -23.568 116.900  1.00 62.65           C  
ANISOU 2589  C   PRO A 311     9146   5637   9019  -1178    359    978       C  
ATOM   2590  O   PRO A 311       4.793 -23.208 117.579  1.00 74.59           O  
ANISOU 2590  O   PRO A 311    10675   7189  10476   -991    325   1100       O  
ATOM   2591  CB  PRO A 311       1.858 -24.480 118.201  1.00 51.55           C  
ANISOU 2591  CB  PRO A 311     7687   4229   7671  -1517    472   1059       C  
ATOM   2592  CG  PRO A 311       0.383 -24.387 118.005  1.00 55.63           C  
ANISOU 2592  CG  PRO A 311     8009   4805   8323  -1721    566    931       C  
ATOM   2593  CD  PRO A 311       0.213 -23.941 116.587  1.00 43.92           C  
ANISOU 2593  CD  PRO A 311     6331   3328   7027  -1711    493    751       C  
ATOM   2594  N   LEU A 312       3.974 -24.212 115.743  1.00 60.69           N  
ANISOU 2594  N   LEU A 312     8984   5298   8778  -1267    263    872       N  
ATOM   2595  CA  LEU A 312       5.297 -24.563 115.234  1.00 45.82           C  
ANISOU 2595  CA  LEU A 312     7172   3332   6906  -1122    167    900       C  
ATOM   2596  C   LEU A 312       5.884 -23.506 114.308  1.00 49.21           C  
ANISOU 2596  C   LEU A 312     7591   3854   7252   -985    172    774       C  
ATOM   2597  O   LEU A 312       7.049 -23.633 113.906  1.00 61.40           O  
ANISOU 2597  O   LEU A 312     9176   5361   8792   -858    101    787       O  
ATOM   2598  CB  LEU A 312       5.250 -25.896 114.475  1.00 38.55           C  
ANISOU 2598  CB  LEU A 312     6228   2205   6213  -1232    116    892       C  
ATOM   2599  CG  LEU A 312       4.730 -27.160 115.163  1.00 57.63           C  
ANISOU 2599  CG  LEU A 312     8669   4454   8773  -1366    208    999       C  
ATOM   2600  CD1 LEU A 312       4.878 -28.364 114.240  1.00 63.38           C  
ANISOU 2600  CD1 LEU A 312     9444   4938   9700  -1436    284    919       C  
ATOM   2601  CD2 LEU A 312       5.452 -27.386 116.477  1.00 62.39           C  
ANISOU 2601  CD2 LEU A 312     9371   5044   9291  -1239    249   1194       C  
ATOM   2602  N   SER A 313       5.108 -22.477 113.963  1.00 32.17           N  
ANISOU 2602  N   SER A 313     5291   1796   5138   -991    284    669       N  
ATOM   2603  CA  SER A 313       5.525 -21.532 112.932  1.00 30.50           C  
ANISOU 2603  CA  SER A 313     4997   1642   4951   -877    267    575       C  
ATOM   2604  C   SER A 313       6.829 -20.835 113.294  1.00 38.30           C  
ANISOU 2604  C   SER A 313     6012   2711   5830   -664    222    658       C  
ATOM   2605  O   SER A 313       7.708 -20.675 112.443  1.00 47.68           O  
ANISOU 2605  O   SER A 313     7260   3900   6956   -577    217    591       O  
ATOM   2606  CB  SER A 313       4.421 -20.508 112.684  1.00 29.60           C  
ANISOU 2606  CB  SER A 313     4719   1613   4913   -965    135    538       C  
ATOM   2607  OG  SER A 313       3.375 -21.063 111.911  1.00 50.70           O  
ANISOU 2607  OG  SER A 313     7347   4227   7690  -1180    113    390       O  
ATOM   2608  N   GLY A 314       6.971 -20.400 114.544  1.00 32.96           N  
ANISOU 2608  N   GLY A 314     5284   2112   5127   -595    180    795       N  
ATOM   2609  CA  GLY A 314       8.181 -19.685 114.920  1.00 28.15           C  
ANISOU 2609  CA  GLY A 314     4662   1594   4441   -420    134    845       C  
ATOM   2610  C   GLY A 314       9.432 -20.530 114.774  1.00 30.51           C  
ANISOU 2610  C   GLY A 314     5084   1811   4699   -353    128    851       C  
ATOM   2611  O   GLY A 314      10.429 -20.097 114.184  1.00 31.29           O  
ANISOU 2611  O   GLY A 314     5180   1931   4777   -259     95    808       O  
ATOM   2612  N   CYS A 315       9.388 -21.760 115.287  1.00 29.78           N  
ANISOU 2612  N   CYS A 315     5078   1593   4643   -415    125    931       N  
ATOM   2613  CA  CYS A 315      10.549 -22.639 115.226  1.00 31.29           C  
ANISOU 2613  CA  CYS A 315     5328   1654   4907   -349     80    997       C  
ATOM   2614  C   CYS A 315      10.874 -23.047 113.793  1.00 43.13           C  
ANISOU 2614  C   CYS A 315     6863   3052   6474   -383     43    885       C  
ATOM   2615  O   CYS A 315      12.049 -23.074 113.401  1.00 57.58           O  
ANISOU 2615  O   CYS A 315     8677   4831   8369   -274     32    893       O  
ATOM   2616  CB  CYS A 315      10.310 -23.863 116.115  1.00 33.60           C  
ANISOU 2616  CB  CYS A 315     5683   1813   5270   -404     99   1137       C  
ATOM   2617  SG  CYS A 315       9.086 -25.069 115.543  1.00 43.39           S  
ANISOU 2617  SG  CYS A 315     6987   2897   6601   -635    110   1086       S  
ATOM   2618  N   LEU A 316       9.854 -23.349 112.986  1.00 38.66           N  
ANISOU 2618  N   LEU A 316     6319   2457   5911   -536     16    782       N  
ATOM   2619  CA  LEU A 316      10.135 -23.736 111.608  1.00 32.85           C  
ANISOU 2619  CA  LEU A 316     5572   1621   5287   -561    -34    684       C  
ATOM   2620  C   LEU A 316      10.614 -22.550 110.781  1.00 35.45           C  
ANISOU 2620  C   LEU A 316     5866   2079   5525   -474    -76    593       C  
ATOM   2621  O   LEU A 316      11.471 -22.717 109.903  1.00 37.10           O  
ANISOU 2621  O   LEU A 316     6059   2209   5831   -413    -78    551       O  
ATOM   2622  CB  LEU A 316       8.902 -24.381 110.983  1.00 34.13           C  
ANISOU 2622  CB  LEU A 316     5702   1701   5565   -743    -55    608       C  
ATOM   2623  CG  LEU A 316       8.463 -25.568 111.844  1.00 36.39           C  
ANISOU 2623  CG  LEU A 316     6032   1839   5954   -840     19    708       C  
ATOM   2624  CD1 LEU A 316       7.149 -26.157 111.384  1.00 47.32           C  
ANISOU 2624  CD1 LEU A 316     7371   3126   7481  -1049     58    620       C  
ATOM   2625  CD2 LEU A 316       9.561 -26.623 111.870  1.00 40.30           C  
ANISOU 2625  CD2 LEU A 316     6610   2129   6572   -754     98    777       C  
ATOM   2626  N   CYS A 317      10.100 -21.348 111.057  1.00 32.93           N  
ANISOU 2626  N   CYS A 317     5555   1938   5021   -454    -33    557       N  
ATOM   2627  CA  CYS A 317      10.594 -20.165 110.373  1.00 27.30           C  
ANISOU 2627  CA  CYS A 317     4821   1330   4222   -356    -15    489       C  
ATOM   2628  C   CYS A 317      12.042 -19.902 110.734  1.00 44.61           C  
ANISOU 2628  C   CYS A 317     6958   3519   6472   -221    -31    559       C  
ATOM   2629  O   CYS A 317      12.833 -19.526 109.870  1.00 41.77           O  
ANISOU 2629  O   CYS A 317     6572   3157   6142   -169    -83    511       O  
ATOM   2630  CB  CYS A 317       9.734 -18.950 110.710  1.00 25.61           C  
ANISOU 2630  CB  CYS A 317     4457   1251   4023   -308    214    474       C  
ATOM   2631  SG  CYS A 317      10.230 -17.425 109.859  1.00 29.56           S  
ANISOU 2631  SG  CYS A 317     4806   1870   4557   -183    257    432       S  
ATOM   2632  N   GLU A 318      12.423 -20.123 111.994  1.00 32.26           N  
ANISOU 2632  N   GLU A 318     5362   1951   4947   -166      4    676       N  
ATOM   2633  CA  GLU A 318      13.823 -19.912 112.346  1.00 49.73           C  
ANISOU 2633  CA  GLU A 318     7519   4158   7218    -43     -9    740       C  
ATOM   2634  C   GLU A 318      14.721 -20.979 111.725  1.00 42.78           C  
ANISOU 2634  C   GLU A 318     6673   3104   6477    -16     -7    750       C  
ATOM   2635  O   GLU A 318      15.853 -20.688 111.327  1.00 32.34           O  
ANISOU 2635  O   GLU A 318     5302   1781   5204     70      3    735       O  
ATOM   2636  CB  GLU A 318      14.011 -19.873 113.859  1.00 27.62           C  
ANISOU 2636  CB  GLU A 318     4667   1403   4425     17     -5    877       C  
ATOM   2637  CG  GLU A 318      15.410 -19.406 114.257  1.00 58.54           C  
ANISOU 2637  CG  GLU A 318     8475   5380   8386    140    -27    926       C  
ATOM   2638  CD  GLU A 318      15.694 -17.967 113.851  1.00 72.50           C  
ANISOU 2638  CD  GLU A 318    10184   7271  10093    161    -40    841       C  
ATOM   2639  OE1 GLU A 318      14.767 -17.278 113.370  1.00 88.22           O  
ANISOU 2639  OE1 GLU A 318    12207   9311  12001    103    -27    762       O  
ATOM   2640  OE2 GLU A 318      16.857 -17.531 113.981  1.00 85.49           O1-
ANISOU 2640  OE2 GLU A 318    11746   8953  11782    237    -53    854       O1-
ATOM   2641  N   LEU A 319      14.229 -22.216 111.607  1.00 40.65           N  
ANISOU 2641  N   LEU A 319     6468   2684   6293    -91     10    768       N  
ATOM   2642  CA  LEU A 319      14.981 -23.235 110.873  1.00 41.31           C  
ANISOU 2642  CA  LEU A 319     6564   2603   6530    -60     68    753       C  
ATOM   2643  C   LEU A 319      15.227 -22.796 109.429  1.00 43.97           C  
ANISOU 2643  C   LEU A 319     6895   2939   6873    -70     60    615       C  
ATOM   2644  O   LEU A 319      16.372 -22.786 108.949  1.00 52.96           O  
ANISOU 2644  O   LEU A 319     7997   4052   8074     23    118    597       O  
ATOM   2645  CB  LEU A 319      14.226 -24.562 110.930  1.00 42.57           C  
ANISOU 2645  CB  LEU A 319     6791   2597   6787   -160    113    775       C  
ATOM   2646  CG  LEU A 319      14.812 -25.770 110.202  1.00 50.65           C  
ANISOU 2646  CG  LEU A 319     7844   3423   7976   -139    229    745       C  
ATOM   2647  CD1 LEU A 319      16.000 -26.303 110.980  1.00 38.97           C  
ANISOU 2647  CD1 LEU A 319     6337   1887   6585     16    301    884       C  
ATOM   2648  CD2 LEU A 319      13.749 -26.842 110.026  1.00 39.37           C  
ANISOU 2648  CD2 LEU A 319     6486   1846   6628   -287    278    713       C  
ATOM   2649  N   TYR A 320      14.155 -22.401 108.735  1.00 31.57           N  
ANISOU 2649  N   TYR A 320     5337   1417   5242   -176     -5    519       N  
ATOM   2650  CA  TYR A 320      14.263 -21.919 107.360  1.00 48.05           C  
ANISOU 2650  CA  TYR A 320     7400   3517   7340   -179    -19    396       C  
ATOM   2651  C   TYR A 320      15.218 -20.730 107.252  1.00 45.89           C  
ANISOU 2651  C   TYR A 320     7073   3361   7001    -74    -28    398       C  
ATOM   2652  O   TYR A 320      16.053 -20.667 106.339  1.00 54.13           O  
ANISOU 2652  O   TYR A 320     8112   4355   8099    -24     29    340       O  
ATOM   2653  CB  TYR A 320      12.869 -21.548 106.854  1.00 53.03           C  
ANISOU 2653  CB  TYR A 320     7984   4229   7936   -286    -98    317       C  
ATOM   2654  CG  TYR A 320      12.812 -21.107 105.414  1.00 55.71           C  
ANISOU 2654  CG  TYR A 320     8285   4567   8315   -285    -89    187       C  
ATOM   2655  CD1 TYR A 320      13.039 -19.784 105.068  1.00 48.43           C  
ANISOU 2655  CD1 TYR A 320     7277   3783   7343   -213   -116    176       C  
ATOM   2656  CD2 TYR A 320      12.513 -22.006 104.403  1.00 58.85           C  
ANISOU 2656  CD2 TYR A 320     8752   4813   8795   -361    -28     65       C  
ATOM   2657  CE1 TYR A 320      12.984 -19.371 103.755  1.00 41.03           C  
ANISOU 2657  CE1 TYR A 320     6340   2828   6421   -205    -66     61       C  
ATOM   2658  CE2 TYR A 320      12.455 -21.603 103.084  1.00 59.20           C  
ANISOU 2658  CE2 TYR A 320     8810   4855   8830   -361     10    -75       C  
ATOM   2659  CZ  TYR A 320      12.693 -20.283 102.766  1.00 49.73           C  
ANISOU 2659  CZ  TYR A 320     7546   3782   7568   -278     -7    -69       C  
ATOM   2660  OH  TYR A 320      12.640 -19.870 101.456  1.00 53.06           O  
ANISOU 2660  OH  TYR A 320     8051   4203   7906   -278     91   -204       O  
ATOM   2661  N   MET A 321      15.107 -19.772 108.181  1.00 44.50           N  
ANISOU 2661  N   MET A 321     6861   3342   6705    -45    -69    452       N  
ATOM   2662  CA  MET A 321      15.910 -18.554 108.098  1.00 36.55           C  
ANISOU 2662  CA  MET A 321     5799   2440   5648     32    -71    442       C  
ATOM   2663  C   MET A 321      17.380 -18.833 108.379  1.00 50.93           C  
ANISOU 2663  C   MET A 321     7595   4194   7563    128      3    491       C  
ATOM   2664  O   MET A 321      18.256 -18.252 107.732  1.00 46.79           O  
ANISOU 2664  O   MET A 321     7026   3691   7063    175     40    447       O  
ATOM   2665  CB  MET A 321      15.395 -17.492 109.072  1.00 26.32           C  
ANISOU 2665  CB  MET A 321     4485   1306   4209     37    -92    474       C  
ATOM   2666  CG  MET A 321      13.979 -17.006 108.821  1.00 33.31           C  
ANISOU 2666  CG  MET A 321     5403   2280   4975    -35   -137    424       C  
ATOM   2667  SD  MET A 321      13.788 -16.099 107.273  1.00 46.61           S  
ANISOU 2667  SD  MET A 321     6872   4000   6837    -39   -256    354       S  
ATOM   2668  CE  MET A 321      14.515 -14.519 107.704  1.00 48.87           C  
ANISOU 2668  CE  MET A 321     7142   4403   7022     31   -251    365       C  
ATOM   2669  N   ALA A 322      17.673 -19.690 109.361  1.00 52.87           N  
ANISOU 2669  N   ALA A 322     7828   4392   7869    165     38    586       N  
ATOM   2670  CA  ALA A 322      19.053 -20.086 109.611  1.00 44.43           C  
ANISOU 2670  CA  ALA A 322     6687   3281   6914    270    107    641       C  
ATOM   2671  C   ALA A 322      19.645 -20.758 108.383  1.00 49.02           C  
ANISOU 2671  C   ALA A 322     7293   3736   7596    284    193    571       C  
ATOM   2672  O   ALA A 322      20.821 -20.547 108.047  1.00 47.18           O  
ANISOU 2672  O   ALA A 322     6999   3500   7426    359    257    559       O  
ATOM   2673  CB  ALA A 322      19.114 -21.019 110.819  1.00 53.36           C  
ANISOU 2673  CB  ALA A 322     7805   4364   8105    316    117    775       C  
ATOM   2674  N   PHE A 323      18.835 -21.566 107.691  1.00 55.19           N  
ANISOU 2674  N   PHE A 323     8159   4410   8399    206    208    515       N  
ATOM   2675  CA  PHE A 323      19.298 -22.150 106.437  1.00 55.56           C  
ANISOU 2675  CA  PHE A 323     8240   4341   8528    209    309    424       C  
ATOM   2676  C   PHE A 323      19.619 -21.070 105.411  1.00 57.56           C  
ANISOU 2676  C   PHE A 323     8474   4677   8719    211    313    329       C  
ATOM   2677  O   PHE A 323      20.652 -21.124 104.733  1.00 63.02           O  
ANISOU 2677  O   PHE A 323     9149   5327   9471    268    416    292       O  
ATOM   2678  CB  PHE A 323      18.255 -23.107 105.877  1.00 50.99           C  
ANISOU 2678  CB  PHE A 323     7753   3642   7979    105    326    360       C  
ATOM   2679  CG  PHE A 323      18.613 -23.636 104.528  1.00 67.94           C  
ANISOU 2679  CG  PHE A 323     9950   5678  10187     96    442    241       C  
ATOM   2680  CD1 PHE A 323      19.863 -24.186 104.309  1.00 73.72           C  
ANISOU 2680  CD1 PHE A 323    10668   6318  11026    191    572    254       C  
ATOM   2681  CD2 PHE A 323      17.724 -23.557 103.472  1.00 70.13           C  
ANISOU 2681  CD2 PHE A 323    10285   5947  10415     -3    426    111       C  
ATOM   2682  CE1 PHE A 323      20.217 -24.662 103.071  1.00 77.06           C  
ANISOU 2682  CE1 PHE A 323    11148   6638  11495    181    696    138       C  
ATOM   2683  CE2 PHE A 323      18.075 -24.038 102.227  1.00 79.15           C  
ANISOU 2683  CE2 PHE A 323    11488   6992  11593    -14    547    -11       C  
ATOM   2684  CZ  PHE A 323      19.324 -24.588 102.034  1.00 82.33           C  
ANISOU 2684  CZ  PHE A 323    11889   7300  12092     75    686      2       C  
ATOM   2685  N   MET A 324      18.729 -20.086 105.271  1.00 50.98           N  
ANISOU 2685  N   MET A 324     7644   3953   7774    153    212    296       N  
ATOM   2686  CA  MET A 324      18.963 -19.011 104.311  1.00 29.67           C  
ANISOU 2686  CA  MET A 324     4927   1325   5020    161    226    222       C  
ATOM   2687  C   MET A 324      20.204 -18.204 104.670  1.00 34.34           C  
ANISOU 2687  C   MET A 324     5443   1985   5618    239    270    259       C  
ATOM   2688  O   MET A 324      20.920 -17.723 103.784  1.00 47.12           O  
ANISOU 2688  O   MET A 324     7055   3606   7242    264    356    203       O  
ATOM   2689  CB  MET A 324      17.743 -18.101 104.241  1.00 28.13           C  
ANISOU 2689  CB  MET A 324     4725   1228   4734    104    111    202       C  
ATOM   2690  CG  MET A 324      16.469 -18.767 103.769  1.00 58.06           C  
ANISOU 2690  CG  MET A 324     8558   4959   8542     18     71    147       C  
ATOM   2691  SD  MET A 324      16.388 -18.947 101.974  1.00 37.85           S  
ANISOU 2691  SD  MET A 324     6067   2335   5978     -5    174     -3       S  
ATOM   2692  CE  MET A 324      16.875 -20.656 101.769  1.00 49.88           C  
ANISOU 2692  CE  MET A 324     7672   3677   7602    -28    282    -40       C  
ATOM   2693  N   ASP A 325      20.470 -18.047 105.970  1.00 28.70           N  
ANISOU 2693  N   ASP A 325     4672   1326   4905    274    226    348       N  
ATOM   2694  CA  ASP A 325      21.673 -17.351 106.417  1.00 28.42           C  
ANISOU 2694  CA  ASP A 325     4545   1348   4905    341    268    378       C  
ATOM   2695  C   ASP A 325      22.929 -18.122 106.034  1.00 38.10           C  
ANISOU 2695  C   ASP A 325     5736   2476   6266    412    388    380       C  
ATOM   2696  O   ASP A 325      23.898 -17.532 105.544  1.00 43.51           O  
ANISOU 2696  O   ASP A 325     6370   3175   6987    443    465    343       O  
ATOM   2697  CB  ASP A 325      21.627 -17.121 107.929  1.00 27.77           C  
ANISOU 2697  CB  ASP A 325     4405   1343   4804    364    198    472       C  
ATOM   2698  CG  ASP A 325      20.963 -15.804 108.299  1.00 55.79           C  
ANISOU 2698  CG  ASP A 325     7950   5015   8232    320    125    455       C  
ATOM   2699  OD1 ASP A 325      20.741 -14.972 107.396  1.00 59.36           O1-
ANISOU 2699  OD1 ASP A 325     8426   5493   8634    288    129    383       O1-
ATOM   2700  OD2 ASP A 325      20.686 -15.591 109.496  1.00 59.48           O  
ANISOU 2700  OD2 ASP A 325     8387   5551   8663    326     76    519       O  
ATOM   2701  N   ARG A 326      22.926 -19.442 106.241  1.00 42.12           N  
ANISOU 2701  N   ARG A 326     6271   2872   6859    438    417    423       N  
ATOM   2702  CA  ARG A 326      24.054 -20.258 105.792  1.00 39.78           C  
ANISOU 2702  CA  ARG A 326     5950   2462   6703    515    542    422       C  
ATOM   2703  C   ARG A 326      24.226 -20.175 104.277  1.00 35.30           C  
ANISOU 2703  C   ARG A 326     5441   1843   6127    482    645    302       C  
ATOM   2704  O   ARG A 326      25.356 -20.174 103.771  1.00 35.52           O  
ANISOU 2704  O   ARG A 326     5426   1833   6238    538    758    278       O  
ATOM   2705  CB  ARG A 326      23.853 -21.709 106.236  1.00 43.97           C  
ANISOU 2705  CB  ARG A 326     6521   2861   7326    546    567    491       C  
ATOM   2706  CG  ARG A 326      24.855 -22.725 105.693  1.00 59.56           C  
ANISOU 2706  CG  ARG A 326     8491   4685   9453    628    711    487       C  
ATOM   2707  CD  ARG A 326      26.289 -22.410 106.097  1.00 72.14           C  
ANISOU 2707  CD  ARG A 326     9953   6312  11145    749    749    546       C  
ATOM   2708  NE  ARG A 326      27.213 -22.527 104.972  1.00 88.85           N  
ANISOU 2708  NE  ARG A 326    12063   8355  13341    781    892    462       N  
ATOM   2709  CZ  ARG A 326      27.835 -23.653 104.632  1.00 90.97           C  
ANISOU 2709  CZ  ARG A 326    12345   8469  13749    858   1016    474       C  
ATOM   2710  NH1 ARG A 326      27.636 -24.765 105.329  1.00 90.36           N  
ANISOU 2710  NH1 ARG A 326    12292   8287  13752    915   1016    573       N  
ATOM   2711  NH2 ARG A 326      28.657 -23.673 103.593  1.00 88.25           N  
ANISOU 2711  NH2 ARG A 326    11997   8067  13469    879   1154    389       N  
ATOM   2712  N   LEU A 327      23.117 -20.099 103.539  1.00 38.15           N  
ANISOU 2712  N   LEU A 327     5899   2205   6391    393    610    227       N  
ATOM   2713  CA  LEU A 327      23.196 -20.140 102.082  1.00 34.19           C  
ANISOU 2713  CA  LEU A 327     5470   1649   5872    365    713    115       C  
ATOM   2714  C   LEU A 327      23.693 -18.821 101.493  1.00 57.07           C  
ANISOU 2714  C   LEU A 327     8340   4643   8699    369    748     77       C  
ATOM   2715  O   LEU A 327      24.505 -18.830 100.561  1.00 58.13           O  
ANISOU 2715  O   LEU A 327     8491   4730   8865    391    884     19       O  
ATOM   2716  CB  LEU A 327      21.830 -20.507 101.495  1.00 41.66           C  
ANISOU 2716  CB  LEU A 327     6520   2563   6744    273    660     44       C  
ATOM   2717  CG  LEU A 327      21.691 -20.842 100.000  1.00 48.19           C  
ANISOU 2717  CG  LEU A 327     7450   3315   7546    232    764    -86       C  
ATOM   2718  CD1 LEU A 327      22.916 -21.548  99.434  1.00 65.00           C  
ANISOU 2718  CD1 LEU A 327     9587   5329   9783    289    937   -118       C  
ATOM   2719  CD2 LEU A 327      20.432 -21.671  99.754  1.00 51.33           C  
ANISOU 2719  CD2 LEU A 327     7933   3641   7930    141    719   -151       C  
ATOM   2720  N   TYR A 328      23.233 -17.679 102.017  1.00 41.18           N  
ANISOU 2720  N   TYR A 328     6292   2758   6596    348    646    108       N  
ATOM   2721  CA  TYR A 328      23.467 -16.394 101.370  1.00 39.79           C  
ANISOU 2721  CA  TYR A 328     6117   2659   6343    339    691     70       C  
ATOM   2722  C   TYR A 328      24.247 -15.377 102.196  1.00 44.64           C  
ANISOU 2722  C   TYR A 328     6626   3356   6981    367    686    118       C  
ATOM   2723  O   TYR A 328      24.635 -14.342 101.643  1.00 52.62           O  
ANISOU 2723  O   TYR A 328     7637   4406   7950    359    762     87       O  
ATOM   2724  CB  TYR A 328      22.133 -15.741 100.973  1.00 29.30           C  
ANISOU 2724  CB  TYR A 328     4856   1395   4883    286    605     43       C  
ATOM   2725  CG  TYR A 328      21.312 -16.540  99.987  1.00 45.82           C  
ANISOU 2725  CG  TYR A 328     7053   3413   6943    246    616    -30       C  
ATOM   2726  CD1 TYR A 328      21.517 -16.409  98.621  1.00 40.00           C  
ANISOU 2726  CD1 TYR A 328     6408   2642   6150    243    734   -111       C  
ATOM   2727  CD2 TYR A 328      20.303 -17.390 100.418  1.00 55.54           C  
ANISOU 2727  CD2 TYR A 328     8301   4608   8194    202    516    -27       C  
ATOM   2728  CE1 TYR A 328      20.767 -17.127  97.712  1.00 42.08           C  
ANISOU 2728  CE1 TYR A 328     6777   2838   6375    199    746   -200       C  
ATOM   2729  CE2 TYR A 328      19.540 -18.106  99.517  1.00 51.57           C  
ANISOU 2729  CE2 TYR A 328     7891   4032   7671    150    533   -117       C  
ATOM   2730  CZ  TYR A 328      19.777 -17.972  98.162  1.00 47.53           C  
ANISOU 2730  CZ  TYR A 328     7469   3490   7099    149    643   -211       C  
ATOM   2731  OH  TYR A 328      19.031 -18.684  97.246  1.00 57.80           O  
ANISOU 2731  OH  TYR A 328     8872   4721   8368     89    661   -327       O  
ATOM   2732  N   PHE A 329      24.463 -15.606 103.491  1.00 29.33           N  
ANISOU 2732  N   PHE A 329     4604   1439   5100    395    611    190       N  
ATOM   2733  CA  PHE A 329      25.013 -14.585 104.381  1.00 54.25           C  
ANISOU 2733  CA  PHE A 329     7663   4680   8269    407    587    224       C  
ATOM   2734  C   PHE A 329      26.183 -15.138 105.181  1.00 47.20           C  
ANISOU 2734  C   PHE A 329     6659   3753   7520    480    616    277       C  
ATOM   2735  O   PHE A 329      26.387 -14.797 106.351  1.00 53.95           O  
ANISOU 2735  O   PHE A 329     7431   4668   8399    502    546    332       O  
ATOM   2736  CB  PHE A 329      23.922 -14.032 105.297  1.00 26.97           C  
ANISOU 2736  CB  PHE A 329     4218   1314   4715    370    446    261       C  
ATOM   2737  CG  PHE A 329      22.792 -13.380 104.552  1.00 26.14           C  
ANISOU 2737  CG  PHE A 329     4196   1247   4489    317    411    218       C  
ATOM   2738  CD1 PHE A 329      22.867 -12.046 104.189  1.00 41.59           C  
ANISOU 2738  CD1 PHE A 329     6151   3259   6392    302    457    189       C  
ATOM   2739  CD2 PHE A 329      21.673 -14.110 104.183  1.00 26.22           C  
ANISOU 2739  CD2 PHE A 329     4282   1226   4456    288    345    210       C  
ATOM   2740  CE1 PHE A 329      21.837 -11.442 103.490  1.00 39.38           C  
ANISOU 2740  CE1 PHE A 329     5942   3012   6011    278    438    167       C  
ATOM   2741  CE2 PHE A 329      20.638 -13.512 103.479  1.00 30.51           C  
ANISOU 2741  CE2 PHE A 329     4877   1805   4911    254    314    175       C  
ATOM   2742  CZ  PHE A 329      20.720 -12.177 103.132  1.00 24.97           C  
ANISOU 2742  CZ  PHE A 329     4173   1165   4149    259    363    161       C  
ATOM   2743  N   SER A 330      26.975 -16.000 104.545  1.00 55.32           N  
ANISOU 2743  N   SER A 330     7682   4684   8654    528    724    261       N  
ATOM   2744  CA  SER A 330      28.130 -16.614 105.178  1.00 66.37           C  
ANISOU 2744  CA  SER A 330     8968   6038  10211    624    758    317       C  
ATOM   2745  C   SER A 330      29.437 -15.886 104.891  1.00 67.15           C  
ANISOU 2745  C   SER A 330     8963   6144  10406    650    865    274       C  
ATOM   2746  O   SER A 330      30.395 -16.048 105.655  1.00 76.38           O  
ANISOU 2746  O   SER A 330     9994   7308  11720    736    873    326       O  
ATOM   2747  CB  SER A 330      28.262 -18.077 104.727  1.00 59.77           C  
ANISOU 2747  CB  SER A 330     8179   5071   9459    676    825    330       C  
ATOM   2748  OG  SER A 330      28.034 -18.207 103.333  1.00 57.12           O  
ANISOU 2748  OG  SER A 330     7948   4674   9079    624    926    235       O  
ATOM   2749  N   ASN A 331      29.498 -15.080 103.827  1.00 53.05           N  
ANISOU 2749  N   ASN A 331     7228   4364   8564    584    965    188       N  
ATOM   2750  CA  ASN A 331      30.751 -14.535 103.314  1.00 56.55           C  
ANISOU 2750  CA  ASN A 331     7592   4785   9109    595   1110    133       C  
ATOM   2751  C   ASN A 331      30.977 -13.073 103.695  1.00 55.51           C  
ANISOU 2751  C   ASN A 331     7394   4729   8969    537   1123    105       C  
ATOM   2752  O   ASN A 331      31.799 -12.398 103.067  1.00 54.79           O  
ANISOU 2752  O   ASN A 331     7256   4606   8955    507   1295     45       O  
ATOM   2753  CB  ASN A 331      30.804 -14.673 101.791  1.00 58.58           C  
ANISOU 2753  CB  ASN A 331     7957   4976   9327    561   1263     61       C  
ATOM   2754  CG  ASN A 331      31.004 -16.105 101.334  1.00 62.67           C  
ANISOU 2754  CG  ASN A 331     8509   5382   9920    622   1317     63       C  
ATOM   2755  OD1 ASN A 331      31.787 -16.852 101.919  1.00 56.14           O  
ANISOU 2755  OD1 ASN A 331     7581   4506   9243    714   1322    108       O  
ATOM   2756  ND2 ASN A 331      30.307 -16.489 100.270  1.00 64.43           N  
ANISOU 2756  ND2 ASN A 331     8877   5559  10044    580   1366     13       N  
ATOM   2757  N   LEU A 332      30.270 -12.565 104.697  1.00 52.40           N  
ANISOU 2757  N   LEU A 332     6988   4413   8509    512    987    144       N  
ATOM   2758  CA  LEU A 332      30.441 -11.171 105.077  1.00 49.41           C  
ANISOU 2758  CA  LEU A 332     6542   4078   8151    448   1034    109       C  
ATOM   2759  C   LEU A 332      31.610 -11.004 106.039  1.00 51.97           C  
ANISOU 2759  C   LEU A 332     6620   4360   8764    489   1123    119       C  
ATOM   2760  O   LEU A 332      31.980 -11.924 106.770  1.00 42.36           O  
ANISOU 2760  O   LEU A 332     5281   3118   7695    589   1073    198       O  
ATOM   2761  CB  LEU A 332      29.164 -10.606 105.703  1.00 36.79           C  
ANISOU 2761  CB  LEU A 332     5032   2574   6371    401    865    132       C  
ATOM   2762  CG  LEU A 332      27.854 -11.001 105.029  1.00 45.44           C  
ANISOU 2762  CG  LEU A 332     6283   3681   7300    382    802    146       C  
ATOM   2763  CD1 LEU A 332      26.660 -10.577 105.876  1.00 49.25           C  
ANISOU 2763  CD1 LEU A 332     6802   4241   7670    351    656    182       C  
ATOM   2764  CD2 LEU A 332      27.773 -10.410 103.637  1.00 58.23           C  
ANISOU 2764  CD2 LEU A 332     7997   5279   8849    344    936     90       C  
ATOM   2765  N   ASP A 333      32.180  -9.802 106.026  1.00 53.87           N  
ANISOU 2765  N   ASP A 333     6775   4591   9102    414   1256     37       N  
ATOM   2766  CA  ASP A 333      33.334  -9.418 106.831  1.00 49.33           C  
ANISOU 2766  CA  ASP A 333     5924   3964   8856    425   1359     -8       C  
ATOM   2767  C   ASP A 333      33.215  -9.916 108.264  1.00 59.64           C  
ANISOU 2767  C   ASP A 333     7060   5299  10300    521   1192     87       C  
ATOM   2768  O   ASP A 333      32.292  -9.539 108.992  1.00 52.65           O  
ANISOU 2768  O   ASP A 333     6233   4475   9296    484   1057    123       O  
ATOM   2769  CB  ASP A 333      33.468  -7.885 106.811  1.00 44.24           C  
ANISOU 2769  CB  ASP A 333     5262   3321   8226    284   1485   -133       C  
ATOM   2770  CG  ASP A 333      34.776  -7.385 107.410  1.00 57.89           C  
ANISOU 2770  CG  ASP A 333     6680   4978  10335    255   1638   -265       C  
ATOM   2771  OD1 ASP A 333      35.478  -8.159 108.093  1.00 67.02           O  
ANISOU 2771  OD1 ASP A 333     7588   6124  11755    390   1587   -238       O  
ATOM   2772  OD2 ASP A 333      35.104  -6.205 107.188  1.00 64.75           O1-
ANISOU 2772  OD2 ASP A 333     7537   5828  11239    112   1805   -407       O1-
ATOM   2773  N   LYS A 334      34.166 -10.759 108.673  1.00 56.47           N  
ANISOU 2773  N   LYS A 334     6436   4873  10147    665   1194    142       N  
ATOM   2774  CA  LYS A 334      34.181 -11.278 110.036  1.00 66.18           C  
ANISOU 2774  CA  LYS A 334     7459   6183  11503    810   1013    271       C  
ATOM   2775  C   LYS A 334      34.549 -10.218 111.065  1.00 59.94           C  
ANISOU 2775  C   LYS A 334     6371   5474  10931    803    983    178       C  
ATOM   2776  O   LYS A 334      34.420 -10.476 112.268  1.00 65.50           O  
ANISOU 2776  O   LYS A 334     6908   6418  11563    862    763    286       O  
ATOM   2777  CB  LYS A 334      35.143 -12.466 110.133  1.00 72.40           C  
ANISOU 2777  CB  LYS A 334     8069   6996  12442   1006   1007    371       C  
ATOM   2778  CG  LYS A 334      34.867 -13.560 109.107  1.00 90.34           C  
ANISOU 2778  CG  LYS A 334    10606   9173  14547   1014   1060    415       C  
ATOM   2779  CD  LYS A 334      36.111 -13.906 108.309  1.00 97.56           C  
ANISOU 2779  CD  LYS A 334    11407  10019  15641   1081   1238    351       C  
ATOM   2780  CE  LYS A 334      36.023 -15.299 107.709  1.00 93.45           C  
ANISOU 2780  CE  LYS A 334    11050   9425  15033   1165   1250    428       C  
ATOM   2781  NZ  LYS A 334      34.843 -15.452 106.821  1.00 95.05           N  
ANISOU 2781  NZ  LYS A 334    11583   9584  14949   1029   1237    383       N  
ATOM   2782  N   ASP A 335      35.016  -9.049 110.625  1.00 64.38           N  
ANISOU 2782  N   ASP A 335     6903   6034  11527    625   1150    -35       N  
ATOM   2783  CA  ASP A 335      35.228  -7.900 111.491  1.00 70.64           C  
ANISOU 2783  CA  ASP A 335     7507   7082  12250    445   1090   -184       C  
ATOM   2784  C   ASP A 335      34.081  -6.902 111.405  1.00 67.47           C  
ANISOU 2784  C   ASP A 335     7386   6563  11685    279   1118   -240       C  
ATOM   2785  O   ASP A 335      34.220  -5.768 111.875  1.00 74.28           O  
ANISOU 2785  O   ASP A 335     8160   7555  12509     96   1147   -406       O  
ATOM   2786  CB  ASP A 335      36.548  -7.210 111.144  1.00 83.08           C  
ANISOU 2786  CB  ASP A 335     8843   8737  13985    331   1280   -404       C  
ATOM   2787  CG  ASP A 335      37.707  -7.726 111.971  1.00 97.37           C  
ANISOU 2787  CG  ASP A 335    10215  10884  15898    436   1150   -401       C  
ATOM   2788  OD1 ASP A 335      37.471  -8.514 112.910  1.00 98.47           O  
ANISOU 2788  OD1 ASP A 335    10243  11209  15961    594    904   -220       O  
ATOM   2789  OD2 ASP A 335      38.858  -7.342 111.676  1.00104.23           O1-
ANISOU 2789  OD2 ASP A 335    10844  11841  16919    364   1300   -575       O1-
ATOM   2790  N   ALA A 336      32.960  -7.295 110.806  1.00 56.47           N  
ANISOU 2790  N   ALA A 336     6322   4933  10200    339   1119   -116       N  
ATOM   2791  CA  ALA A 336      31.765  -6.471 110.718  1.00 43.62           C  
ANISOU 2791  CA  ALA A 336     4950   3356   8266    204   1081   -123       C  
ATOM   2792  C   ALA A 336      30.672  -7.050 111.609  1.00 39.53           C  
ANISOU 2792  C   ALA A 336     4488   2908   7623    275    850     34       C  
ATOM   2793  O   ALA A 336      30.706  -8.223 111.990  1.00 52.51           O  
ANISOU 2793  O   ALA A 336     6059   4575   9318    421    726    185       O  
ATOM   2794  CB  ALA A 336      31.264  -6.371 109.273  1.00 38.67           C  
ANISOU 2794  CB  ALA A 336     4610   2765   7315    173   1151   -104       C  
ATOM   2795  N   PHE A 337      29.698  -6.210 111.944  1.00 31.30           N  
ANISOU 2795  N   PHE A 337     3577   1917   6400    176    803      4       N  
ATOM   2796  CA  PHE A 337      28.599  -6.603 112.818  1.00 42.44           C  
ANISOU 2796  CA  PHE A 337     5040   3395   7692    217    608    132       C  
ATOM   2797  C   PHE A 337      27.429  -7.098 111.977  1.00 43.68           C  
ANISOU 2797  C   PHE A 337     5482   3633   7484    238    543    204       C  
ATOM   2798  O   PHE A 337      26.967  -6.392 111.080  1.00 28.99           O  
ANISOU 2798  O   PHE A 337     3795   1797   5421    181    599    135       O  
ATOM   2799  CB  PHE A 337      28.156  -5.432 113.701  1.00 40.38           C  
ANISOU 2799  CB  PHE A 337     4746   3161   7436     90    590     32       C  
ATOM   2800  CG  PHE A 337      26.876  -5.685 114.464  1.00 35.73           C  
ANISOU 2800  CG  PHE A 337     4246   2649   6681    115    413    157       C  
ATOM   2801  CD1 PHE A 337      25.636  -5.450 113.883  1.00 38.09           C  
ANISOU 2801  CD1 PHE A 337     4806   3004   6663    101    404    175       C  
ATOM   2802  CD2 PHE A 337      26.918  -6.134 115.772  1.00 34.55           C  
ANISOU 2802  CD2 PHE A 337     3898   2771   6459    141    214    235       C  
ATOM   2803  CE1 PHE A 337      24.470  -5.687 114.586  1.00 40.74           C  
ANISOU 2803  CE1 PHE A 337     5205   3406   6870    115    266    268       C  
ATOM   2804  CE2 PHE A 337      25.754  -6.365 116.480  1.00 32.19           C  
ANISOU 2804  CE2 PHE A 337     3681   2543   6006    154     73    349       C  
ATOM   2805  CZ  PHE A 337      24.529  -6.141 115.887  1.00 36.12           C  
ANISOU 2805  CZ  PHE A 337     4437   2856   6433    141    120    375       C  
ATOM   2806  N   ILE A 338      26.944  -8.299 112.277  1.00 29.80           N  
ANISOU 2806  N   ILE A 338     3751   1911   5659    323    415    334       N  
ATOM   2807  CA  ILE A 338      25.700  -8.804 111.706  1.00 33.93           C  
ANISOU 2807  CA  ILE A 338     4509   2497   5885    318    333    357       C  
ATOM   2808  C   ILE A 338      24.901  -9.486 112.809  1.00 44.73           C  
ANISOU 2808  C   ILE A 338     5859   3919   7216    352    199    474       C  
ATOM   2809  O   ILE A 338      25.460 -10.218 113.634  1.00 48.57           O  
ANISOU 2809  O   ILE A 338     6184   4400   7870    431    148    589       O  
ATOM   2810  CB  ILE A 338      25.945  -9.770 110.523  1.00 28.78           C  
ANISOU 2810  CB  ILE A 338     3956   1811   5170    358    362    347       C  
ATOM   2811  CG1 ILE A 338      24.613 -10.268 109.958  1.00 30.41           C  
ANISOU 2811  CG1 ILE A 338     4359   2055   5142    337    262    347       C  
ATOM   2812  CG2 ILE A 338      26.804 -10.945 110.948  1.00 27.71           C  
ANISOU 2812  CG2 ILE A 338     3681   1625   5221    457    369    437       C  
ATOM   2813  CD1 ILE A 338      23.777  -9.186 109.310  1.00 42.07           C  
ANISOU 2813  CD1 ILE A 338     5917   3557   6510    275    275    288       C  
ATOM   2814  N   HIS A 339      23.596  -9.223 112.840  1.00 46.36           N  
ANISOU 2814  N   HIS A 339     6218   4187   7211    304    136    459       N  
ATOM   2815  CA  HIS A 339      22.707  -9.911 113.766  1.00 42.23           C  
ANISOU 2815  CA  HIS A 339     5700   3719   6627    323     37    559       C  
ATOM   2816  C   HIS A 339      21.315 -10.034 113.165  1.00 21.13           C  
ANISOU 2816  C   HIS A 339     3236   1082   3709    283      8    510       C  
ATOM   2817  O   HIS A 339      20.807  -9.099 112.541  1.00 25.06           O  
ANISOU 2817  O   HIS A 339     3822   1590   4111    239     20    431       O  
ATOM   2818  CB  HIS A 339      22.609  -9.204 115.121  1.00 46.14           C  
ANISOU 2818  CB  HIS A 339     6042   4254   7234    304    -28    624       C  
ATOM   2819  CG  HIS A 339      22.031 -10.065 116.202  1.00 40.72           C  
ANISOU 2819  CG  HIS A 339     5306   3639   6528    342   -145    775       C  
ATOM   2820  ND1 HIS A 339      20.689 -10.063 116.515  1.00 38.94           N  
ANISOU 2820  ND1 HIS A 339     5184   3475   6136    298   -181    781       N  
ATOM   2821  CD2 HIS A 339      22.609 -10.972 117.027  1.00 42.56           C  
ANISOU 2821  CD2 HIS A 339     5399   3906   6867    428   -228    935       C  
ATOM   2822  CE1 HIS A 339      20.467 -10.924 117.492  1.00 47.11           C  
ANISOU 2822  CE1 HIS A 339     6153   4569   7177    336   -271    928       C  
ATOM   2823  NE2 HIS A 339      21.615 -11.488 117.822  1.00 44.42           N  
ANISOU 2823  NE2 HIS A 339     5675   4223   6978    421   -305   1030       N  
ATOM   2824  N   ARG A 340      20.701 -11.193 113.378  1.00 37.68           N  
ANISOU 2824  N   ARG A 340     5381   3183   5753    304    -30    572       N  
ATOM   2825  CA  ARG A 340      19.327 -11.438 112.976  1.00 32.69           C  
ANISOU 2825  CA  ARG A 340     4853   2553   5016    264    -41    558       C  
ATOM   2826  C   ARG A 340      18.535 -11.947 114.173  1.00 48.89           C  
ANISOU 2826  C   ARG A 340     6875   4662   7041    265    -79    647       C  
ATOM   2827  O   ARG A 340      19.097 -12.514 115.115  1.00 62.05           O  
ANISOU 2827  O   ARG A 340     8451   6344   8782    309   -114    743       O  
ATOM   2828  CB  ARG A 340      19.250 -12.452 111.818  1.00 26.55           C  
ANISOU 2828  CB  ARG A 340     4152   1683   4252    264    -26    536       C  
ATOM   2829  CG  ARG A 340      17.840 -12.679 111.293  1.00 36.53           C  
ANISOU 2829  CG  ARG A 340     5523   2944   5413    216    -47    510       C  
ATOM   2830  CD  ARG A 340      17.779 -13.686 110.160  1.00 43.58           C  
ANISOU 2830  CD  ARG A 340     6475   3745   6339    200    -53    479       C  
ATOM   2831  NE  ARG A 340      18.304 -14.992 110.546  1.00 50.80           N  
ANISOU 2831  NE  ARG A 340     7382   4571   7350    231    -31    543       N  
ATOM   2832  CZ  ARG A 340      17.599 -15.912 111.197  1.00 47.77           C  
ANISOU 2832  CZ  ARG A 340     7028   4160   6961    213    -36    605       C  
ATOM   2833  NH1 ARG A 340      16.347 -15.658 111.548  1.00 42.75           N  
ANISOU 2833  NH1 ARG A 340     6422   3593   6230    162    -42    602       N  
ATOM   2834  NH2 ARG A 340      18.139 -17.087 111.502  1.00 51.77           N  
ANISOU 2834  NH2 ARG A 340     7518   4583   7569    249    -17    671       N  
ATOM   2835  N   THR A 341      17.224 -11.720 114.135  1.00 48.35           N  
ANISOU 2835  N   THR A 341     6861   4626   6883    224    -75    631       N  
ATOM   2836  CA  THR A 341      16.306 -12.363 115.063  1.00 60.83           C  
ANISOU 2836  CA  THR A 341     8417   6248   8448    210   -102    711       C  
ATOM   2837  C   THR A 341      15.365 -13.273 114.288  1.00 77.20           C  
ANISOU 2837  C   THR A 341    10582   8252  10497    176    -69    695       C  
ATOM   2838  O   THR A 341      15.555 -14.493 114.245  1.00 94.41           O  
ANISOU 2838  O   THR A 341    12796  10351  12723    179    -68    738       O  
ATOM   2839  CB  THR A 341      15.507 -11.324 115.850  1.00 39.26           C  
ANISOU 2839  CB  THR A 341     5639   3615   5662    184   -123    714       C  
ATOM   2840  OG1 THR A 341      14.601 -10.656 114.961  1.00 50.33           O  
ANISOU 2840  OG1 THR A 341     7103   5013   7005    164    -74    637       O  
ATOM   2841  CG2 THR A 341      16.436 -10.316 116.490  1.00 19.37           C  
ANISOU 2841  CG2 THR A 341     3010   1123   3225    191   -170    730       C  
ATOM   2842  N   VAL A 342      14.355 -12.673 113.660  1.00 42.01           N  
ANISOU 2842  N   VAL A 342     6162   3820   5979    146    -34    634       N  
ATOM   2843  CA  VAL A 342      13.377 -13.404 112.863  1.00 39.87           C  
ANISOU 2843  CA  VAL A 342     5943   3509   5698    104      7    605       C  
ATOM   2844  C   VAL A 342      13.435 -12.861 111.440  1.00 50.97           C  
ANISOU 2844  C   VAL A 342     7394   4912   7060    115     62    511       C  
ATOM   2845  O   VAL A 342      14.188 -13.367 110.602  1.00 51.24           O  
ANISOU 2845  O   VAL A 342     7517   4876   7076    113     30    468       O  
ATOM   2846  CB  VAL A 342      11.966 -13.291 113.476  1.00 30.74           C  
ANISOU 2846  CB  VAL A 342     4738   2404   4538     64     -4    644       C  
ATOM   2847  CG1 VAL A 342      10.917 -13.970 112.596  1.00 28.61           C  
ANISOU 2847  CG1 VAL A 342     4495   2081   4293      6     38    607       C  
ATOM   2848  CG2 VAL A 342      11.961 -13.890 114.876  1.00 20.31           C  
ANISOU 2848  CG2 VAL A 342     3378   1105   3233     49    -58    742       C  
ATOM   2849  N   ASP A 343      12.677 -11.810 111.164  1.00 40.50           N  
ANISOU 2849  N   ASP A 343     5993   3656   5738    129    106    496       N  
ATOM   2850  CA  ASP A 343      12.695 -11.179 109.853  1.00 40.40           C  
ANISOU 2850  CA  ASP A 343     5865   3647   5837    150    184    465       C  
ATOM   2851  C   ASP A 343      13.547  -9.925 109.812  1.00 28.69           C  
ANISOU 2851  C   ASP A 343     4222   2208   4472    171    168    467       C  
ATOM   2852  O   ASP A 343      13.557  -9.237 108.787  1.00 37.00           O  
ANISOU 2852  O   ASP A 343     5267   3224   5566    140    -87    423       O  
ATOM   2853  CB  ASP A 343      11.283 -10.808 109.442  1.00 40.30           C  
ANISOU 2853  CB  ASP A 343     5804   3652   5856    129     89    473       C  
ATOM   2854  CG  ASP A 343      10.508 -10.243 110.589  1.00 44.27           C  
ANISOU 2854  CG  ASP A 343     6331   4225   6265    136     52    509       C  
ATOM   2855  OD1 ASP A 343      10.887  -9.162 111.086  1.00 51.35           O  
ANISOU 2855  OD1 ASP A 343     7196   5176   7140    172     61    513       O  
ATOM   2856  OD2 ASP A 343       9.540 -10.896 111.009  1.00 77.72           O1-
ANISOU 2856  OD2 ASP A 343    10613   8430  10486     88    -16    539       O1-
ATOM   2857  N   ASP A 344      14.243  -9.610 110.895  1.00 31.52           N  
ANISOU 2857  N   ASP A 344     4942   2571   4462    183     57    409       N  
ATOM   2858  CA  ASP A 344      14.952  -8.351 111.044  1.00 44.25           C  
ANISOU 2858  CA  ASP A 344     6531   4194   6087    160   -129    371       C  
ATOM   2859  C   ASP A 344      16.450  -8.615 111.013  1.00 49.39           C  
ANISOU 2859  C   ASP A 344     7136   4778   6852    167   -109    376       C  
ATOM   2860  O   ASP A 344      16.977  -9.363 111.845  1.00 29.13           O  
ANISOU 2860  O   ASP A 344     4551   2194   4323    184    -54    425       O  
ATOM   2861  CB  ASP A 344      14.529  -7.648 112.335  1.00 28.98           C  
ANISOU 2861  CB  ASP A 344     4560   2321   4129    185     10    404       C  
ATOM   2862  CG  ASP A 344      13.111  -7.111 112.256  1.00 34.31           C  
ANISOU 2862  CG  ASP A 344     5095   3058   4882    218    156    449       C  
ATOM   2863  OD1 ASP A 344      12.756  -6.573 111.187  1.00 31.89           O  
ANISOU 2863  OD1 ASP A 344     4528   2736   4853    174    -22    468       O  
ATOM   2864  OD2 ASP A 344      12.353  -7.226 113.246  1.00 59.10           O1-
ANISOU 2864  OD2 ASP A 344     8212   6232   8012    201     83    489       O1-
ATOM   2865  N   TYR A 345      17.124  -7.999 110.047  1.00 40.61           N  
ANISOU 2865  N   TYR A 345     5970   3616   5845    169   -112    342       N  
ATOM   2866  CA  TYR A 345      18.570  -8.030 109.934  1.00 41.64           C  
ANISOU 2866  CA  TYR A 345     6096   3673   6053    187    -35    330       C  
ATOM   2867  C   TYR A 345      19.140  -6.679 110.342  1.00 48.27           C  
ANISOU 2867  C   TYR A 345     6893   4525   6923    177     23    296       C  
ATOM   2868  O   TYR A 345      18.562  -5.624 110.043  1.00 29.74           O  
ANISOU 2868  O   TYR A 345     4544   2193   4562    172     40    274       O  
ATOM   2869  CB  TYR A 345      19.011  -8.340 108.503  1.00 37.87           C  
ANISOU 2869  CB  TYR A 345     5621   3134   5634    202     26    300       C  
ATOM   2870  CG  TYR A 345      18.929  -9.795 108.092  1.00 38.95           C  
ANISOU 2870  CG  TYR A 345     5792   3219   5788    207     -1    317       C  
ATOM   2871  CD1 TYR A 345      19.994 -10.662 108.304  1.00 34.32           C  
ANISOU 2871  CD1 TYR A 345     5188   2589   5265    232     52    332       C  
ATOM   2872  CD2 TYR A 345      17.805 -10.291 107.454  1.00 35.56           C  
ANISOU 2872  CD2 TYR A 345     5377   2791   5343    187    -56    316       C  
ATOM   2873  CE1 TYR A 345      19.928 -11.992 107.909  1.00 30.69           C  
ANISOU 2873  CE1 TYR A 345     4763   2062   4838    240     49    346       C  
ATOM   2874  CE2 TYR A 345      17.731 -11.613 107.055  1.00 27.17           C  
ANISOU 2874  CE2 TYR A 345     4348   1665   4309    179    -64    318       C  
ATOM   2875  CZ  TYR A 345      18.797 -12.457 107.284  1.00 36.56           C  
ANISOU 2875  CZ  TYR A 345     5563   2781   5548    207    -13    333       C  
ATOM   2876  OH  TYR A 345      18.712 -13.774 106.889  1.00 42.56           O  
ANISOU 2876  OH  TYR A 345     6363   3455   6353    201     -4    334       O  
ATOM   2877  N   PHE A 346      20.306  -6.733 110.987  1.00 19.82           N  
ANISOU 2877  N   PHE A 346     3234    911   3386    176     75    292       N  
ATOM   2878  CA  PHE A 346      21.040  -5.567 111.460  1.00 34.83           C  
ANISOU 2878  CA  PHE A 346     5081   2809   5345    145    140    242       C  
ATOM   2879  C   PHE A 346      22.498  -5.749 111.066  1.00 27.41           C  
ANISOU 2879  C   PHE A 346     4073   1820   4522    151    232    212       C  
ATOM   2880  O   PHE A 346      23.158  -6.681 111.538  1.00 32.66           O  
ANISOU 2880  O   PHE A 346     4648   2460   5300    183    239    258       O  
ATOM   2881  CB  PHE A 346      20.910  -5.421 112.980  1.00 33.19           C  
ANISOU 2881  CB  PHE A 346     4805   2622   5183    126    121    274       C  
ATOM   2882  CG  PHE A 346      21.357  -4.083 113.514  1.00 27.79           C  
ANISOU 2882  CG  PHE A 346     4045   1903   4612     67    217    200       C  
ATOM   2883  CD1 PHE A 346      21.452  -2.979 112.681  1.00 27.06           C  
ANISOU 2883  CD1 PHE A 346     4011   1796   4477     46    297    123       C  
ATOM   2884  CD2 PHE A 346      21.675  -3.936 114.851  1.00 24.06           C  
ANISOU 2884  CD2 PHE A 346     3416   1405   4320     25    222    206       C  
ATOM   2885  CE1 PHE A 346      21.860  -1.754 113.177  1.00 34.55           C  
ANISOU 2885  CE1 PHE A 346     4906   2705   5516    -23    423     31       C  
ATOM   2886  CE2 PHE A 346      22.091  -2.716 115.354  1.00 32.98           C  
ANISOU 2886  CE2 PHE A 346     4476   2488   5567    -68    325     80       C  
ATOM   2887  CZ  PHE A 346      22.182  -1.623 114.519  1.00 23.93           C  
ANISOU 2887  CZ  PHE A 346     3429   1331   4330    -94    445    -15       C  
ATOM   2888  N   PHE A 347      22.999  -4.870 110.203  1.00 38.07           N  
ANISOU 2888  N   PHE A 347     5422   3135   5906    131    354    150       N  
ATOM   2889  CA  PHE A 347      24.354  -4.981 109.689  1.00 36.83           C  
ANISOU 2889  CA  PHE A 347     5204   2927   5865    129    469    110       C  
ATOM   2890  C   PHE A 347      25.090  -3.670 109.905  1.00 24.06           C  
ANISOU 2890  C   PHE A 347     3517   1268   4358     63    635     25       C  
ATOM   2891  O   PHE A 347      24.497  -2.595 109.802  1.00 22.80           O  
ANISOU 2891  O   PHE A 347     3425   1128   4110     34    658     -3       O  
ATOM   2892  CB  PHE A 347      24.351  -5.350 108.208  1.00 27.55           C  
ANISOU 2892  CB  PHE A 347     4092   1718   4659    160    549    114       C  
ATOM   2893  CG  PHE A 347      25.718  -5.542 107.633  1.00 41.08           C  
ANISOU 2893  CG  PHE A 347     5747   3375   6489    161    678     75       C  
ATOM   2894  CD1 PHE A 347      26.379  -6.749 107.783  1.00 47.31           C  
ANISOU 2894  CD1 PHE A 347     6475   4137   7362    205    643    102       C  
ATOM   2895  CD2 PHE A 347      26.353  -4.516 106.948  1.00 45.44           C  
ANISOU 2895  CD2 PHE A 347     6302   3891   7071    121    853     13       C  
ATOM   2896  CE1 PHE A 347      27.648  -6.933 107.257  1.00 39.69           C  
ANISOU 2896  CE1 PHE A 347     5430   3105   6547    214    794     65       C  
ATOM   2897  CE2 PHE A 347      27.620  -4.693 106.422  1.00 47.83           C  
ANISOU 2897  CE2 PHE A 347     6544   4139   7490    114    984    -29       C  
ATOM   2898  CZ  PHE A 347      28.264  -5.904 106.576  1.00 38.38           C  
ANISOU 2898  CZ  PHE A 347     5263   2907   6414    162    967     -6       C  
ATOM   2899  N   CYS A 348      26.384  -3.766 110.198  1.00 29.63           N  
ANISOU 2899  N   CYS A 348     4068   1907   5282     36    760    -28       N  
ATOM   2900  CA  CYS A 348      27.192  -2.598 110.506  1.00 40.04           C  
ANISOU 2900  CA  CYS A 348     5287   3177   6749    -63    936   -154       C  
ATOM   2901  C   CYS A 348      28.627  -2.832 110.060  1.00 54.61           C  
ANISOU 2901  C   CYS A 348     6993   4947   8807    -83   1098   -224       C  
ATOM   2902  O   CYS A 348      29.157  -3.942 110.177  1.00 60.92           O  
ANISOU 2902  O   CYS A 348     7683   5716   9749    -17   1056   -177       O  
ATOM   2903  CB  CYS A 348      27.157  -2.270 112.000  1.00 40.22           C  
ANISOU 2903  CB  CYS A 348     5169   3195   6919   -135    901   -216       C  
ATOM   2904  SG  CYS A 348      25.553  -1.710 112.612  1.00 42.28           S  
ANISOU 2904  SG  CYS A 348     5577   3528   6961   -134    772   -167       S  
ATOM   2905  N   SER A 349      29.246  -1.760 109.558  1.00 46.47           N  
ANISOU 2905  N   SER A 349     5962   3883   7811   -169   1297   -334       N  
ATOM   2906  CA  SER A 349      30.608  -1.738 109.055  1.00 38.82           C  
ANISOU 2906  CA  SER A 349     4863   2842   7046   -216   1497   -433       C  
ATOM   2907  C   SER A 349      31.114  -0.308 109.094  1.00 40.08           C  
ANISOU 2907  C   SER A 349     4991   2979   7260   -358   1708   -592       C  
ATOM   2908  O   SER A 349      30.337   0.617 108.813  1.00 40.94           O  
ANISOU 2908  O   SER A 349     5270   3113   7172   -365   1725   -559       O  
ATOM   2909  CB  SER A 349      30.677  -2.279 107.623  1.00 46.86           C  
ANISOU 2909  CB  SER A 349     6016   3849   7942   -135   1537   -345       C  
ATOM   2910  OG  SER A 349      31.991  -2.199 107.104  1.00 46.15           O  
ANISOU 2910  OG  SER A 349     5803   3681   8051   -186   1761   -443       O  
ATOM   2911  N   PRO A 350      32.375  -0.081 109.468  1.00 51.05           N  
ANISOU 2911  N   PRO A 350     6149   4322   8925   -476   1869   -780       N  
ATOM   2912  CA  PRO A 350      32.994   1.224 109.199  1.00 51.96           C  
ANISOU 2912  CA  PRO A 350     6254   4416   9072   -616   2118   -942       C  
ATOM   2913  C   PRO A 350      33.060   1.538 107.721  1.00 35.35           C  
ANISOU 2913  C   PRO A 350     4337   2263   6832   -566   2283   -851       C  
ATOM   2914  O   PRO A 350      33.230   2.707 107.356  1.00 55.04           O  
ANISOU 2914  O   PRO A 350     6902   4727   9285   -647   2483   -921       O  
ATOM   2915  CB  PRO A 350      34.398   1.084 109.804  1.00 38.20           C  
ANISOU 2915  CB  PRO A 350     4180   2665   7670   -755   2223  -1184       C  
ATOM   2916  CG  PRO A 350      34.628  -0.399 109.921  1.00 46.76           C  
ANISOU 2916  CG  PRO A 350     5127   3716   8925   -639   2072  -1091       C  
ATOM   2917  CD  PRO A 350      33.282  -0.994 110.181  1.00 52.66           C  
ANISOU 2917  CD  PRO A 350     6063   4495   9451   -491   1824   -869       C  
ATOM   2918  N   HIS A 351      32.901   0.530 106.862  1.00 40.79           N  
ANISOU 2918  N   HIS A 351     5111   2943   7443   -439   2206   -702       N  
ATOM   2919  CA  HIS A 351      33.006   0.714 105.425  1.00 45.30           C  
ANISOU 2919  CA  HIS A 351     5843   3476   7894   -404   2354   -634       C  
ATOM   2920  C   HIS A 351      31.623   0.942 104.823  1.00 33.07           C  
ANISOU 2920  C   HIS A 351     4544   1979   6042   -309   2212   -477       C  
ATOM   2921  O   HIS A 351      30.814  -0.010 104.743  1.00 44.01           O  
ANISOU 2921  O   HIS A 351     5996   3422   7302   -204   1981   -364       O  
ATOM   2922  CB  HIS A 351      33.703  -0.480 104.789  1.00 51.88           C  
ANISOU 2922  CB  HIS A 351     6608   4272   8831   -343   2375   -603       C  
ATOM   2923  CG  HIS A 351      35.086  -0.717 105.326  1.00 60.83           C  
ANISOU 2923  CG  HIS A 351     7454   5345  10314   -426   2524   -772       C  
ATOM   2924  ND1 HIS A 351      35.486  -1.919 105.873  1.00 56.85           N  
ANISOU 2924  ND1 HIS A 351     6764   4825  10011   -359   2405   -767       N  
ATOM   2925  CD2 HIS A 351      36.155   0.110 105.417  1.00 50.76           C  
ANISOU 2925  CD2 HIS A 351     6019   4019   9248   -572   2784   -973       C  
ATOM   2926  CE1 HIS A 351      36.746  -1.828 106.259  1.00 45.59           C  
ANISOU 2926  CE1 HIS A 351     5055   3339   8929   -455   2574   -964       C  
ATOM   2927  NE2 HIS A 351      37.175  -0.607 105.995  1.00 52.82           N  
ANISOU 2927  NE2 HIS A 351     5978   4244   9845   -599   2805  -1109       N  
ATOM   2928  N   PRO A 352      31.302   2.178 104.411  1.00 33.66           N  
ANISOU 2928  N   PRO A 352     4747   2028   6014   -343   2351   -480       N  
ATOM   2929  CA  PRO A 352      29.979   2.467 103.839  1.00 46.61           C  
ANISOU 2929  CA  PRO A 352     6591   3709   7411   -248   2232   -349       C  
ATOM   2930  C   PRO A 352      29.627   1.520 102.711  1.00 47.96           C  
ANISOU 2930  C   PRO A 352     6867   3884   7473   -151   2194   -249       C  
ATOM   2931  O   PRO A 352      28.517   0.986 102.669  1.00 56.11           O  
ANISOU 2931  O   PRO A 352     7974   4968   8376    -70   2021   -165       O  
ATOM   2932  CB  PRO A 352      30.108   3.907 103.318  1.00 34.14           C  
ANISOU 2932  CB  PRO A 352     5117   2048   5806   -302   2509   -379       C  
ATOM   2933  CG  PRO A 352      31.425   4.418 103.798  1.00 36.04           C  
ANISOU 2933  CG  PRO A 352     5202   2227   6266   -444   2735   -544       C  
ATOM   2934  CD  PRO A 352      32.198   3.348 104.454  1.00 35.91           C  
ANISOU 2934  CD  PRO A 352     4976   2238   6431   -474   2647   -620       C  
ATOM   2935  N   HIS A 353      30.579   1.318 101.799  1.00 54.71           N  
ANISOU 2935  N   HIS A 353     7721   4680   8385   -170   2368   -274       N  
ATOM   2936  CA  HIS A 353      30.349   0.456 100.649  1.00 55.76           C  
ANISOU 2936  CA  HIS A 353     7963   4805   8418    -92   2367   -200       C  
ATOM   2937  C   HIS A 353      29.948  -0.947 101.078  1.00 59.50           C  
ANISOU 2937  C   HIS A 353     8371   5343   8894    -29   2107   -166       C  
ATOM   2938  O   HIS A 353      29.145  -1.604 100.407  1.00 76.20           O  
ANISOU 2938  O   HIS A 353    10600   7477  10877     42   2027    -99       O  
ATOM   2939  CB  HIS A 353      31.607   0.423  99.787  1.00 46.17           C  
ANISOU 2939  CB  HIS A 353     6728   3514   7301   -137   2600   -251       C  
ATOM   2940  CG  HIS A 353      32.707  -0.417 100.352  1.00 64.80           C  
ANISOU 2940  CG  HIS A 353     8879   5854   9888   -177   2610   -331       C  
ATOM   2941  ND1 HIS A 353      33.800   0.124 100.993  1.00 78.33           N  
ANISOU 2941  ND1 HIS A 353    10416   7513  11833   -287   2801   -458       N  
ATOM   2942  CD2 HIS A 353      32.880  -1.760 100.382  1.00 70.76           C  
ANISOU 2942  CD2 HIS A 353     9563   6623  10698   -119   2478   -311       C  
ATOM   2943  CE1 HIS A 353      34.604  -0.849 101.382  1.00 81.89           C  
ANISOU 2943  CE1 HIS A 353    10681   7946  12488   -288   2784   -510       C  
ATOM   2944  NE2 HIS A 353      34.069  -2.002 101.023  1.00 74.09           N  
ANISOU 2944  NE2 HIS A 353     9766   6995  11392   -178   2591   -409       N  
ATOM   2945  N   LYS A 354      30.487  -1.419 102.204  1.00 42.62           N  
ANISOU 2945  N   LYS A 354     6057   3233   6905    -55   1979   -215       N  
ATOM   2946  CA  LYS A 354      30.109  -2.739 102.692  1.00 40.71           C  
ANISOU 2946  CA  LYS A 354     5765   3037   6667     11   1750   -172       C  
ATOM   2947  C   LYS A 354      28.679  -2.744 103.210  1.00 43.30           C  
ANISOU 2947  C   LYS A 354     6165   3432   6856     50   1561   -108       C  
ATOM   2948  O   LYS A 354      27.932  -3.703 102.971  1.00 38.54           O  
ANISOU 2948  O   LYS A 354     5615   2855   6172    110   1429    -52       O  
ATOM   2949  CB  LYS A 354      31.076  -3.208 103.777  1.00 52.12           C  
ANISOU 2949  CB  LYS A 354     7000   4456   8345    -17   1751   -231       C  
ATOM   2950  CG  LYS A 354      32.345  -3.843 103.238  1.00 32.18           C  
ANISOU 2950  CG  LYS A 354     4370   1849   6008    -17   1926   -276       C  
ATOM   2951  CD  LYS A 354      33.211  -4.369 104.368  1.00 53.50           C  
ANISOU 2951  CD  LYS A 354     6822   4511   8996    -22   1926   -332       C  
ATOM   2952  CE  LYS A 354      34.491  -5.002 103.850  1.00 60.37           C  
ANISOU 2952  CE  LYS A 354     7555   5290  10094    -11   2107   -383       C  
ATOM   2953  NZ  LYS A 354      35.442  -4.008 103.290  1.00 58.65           N  
ANISOU 2953  NZ  LYS A 354     7283   5006   9996   -128   2403   -504       N  
ATOM   2954  N   VAL A 355      28.272  -1.686 103.920  1.00 39.08           N  
ANISOU 2954  N   VAL A 355     5630   2920   6299     10   1556   -125       N  
ATOM   2955  CA  VAL A 355      26.867  -1.625 104.338  1.00 42.31           C  
ANISOU 2955  CA  VAL A 355     6110   3388   6578     50   1396    -66       C  
ATOM   2956  C   VAL A 355      25.945  -1.565 103.117  1.00 34.91           C  
ANISOU 2956  C   VAL A 355     5342   2447   5477    108   1441     -5       C  
ATOM   2957  O   VAL A 355      24.894  -2.229 103.062  1.00 26.70           O  
ANISOU 2957  O   VAL A 355     4349   1451   4344    159   1285     45       O  
ATOM   2958  CB  VAL A 355      26.639  -0.435 105.286  1.00 53.22           C  
ANISOU 2958  CB  VAL A 355     7466   4781   7973     -4   1411   -104       C  
ATOM   2959  CG1 VAL A 355      25.188  -0.400 105.753  1.00 25.85           C  
ANISOU 2959  CG1 VAL A 355     4062   1374   4386     41   1250    -45       C  
ATOM   2960  CG2 VAL A 355      27.583  -0.518 106.475  1.00 27.02           C  
ANISOU 2960  CG2 VAL A 355     3986   1468   4813    -70   1363   -183       C  
ATOM   2961  N   TYR A 356      26.339  -0.774 102.117  1.00 36.93           N  
ANISOU 2961  N   TYR A 356     5692   2644   5696     99   1660    -11       N  
ATOM   2962  CA  TYR A 356      25.597  -0.668 100.863  1.00 36.88           C  
ANISOU 2962  CA  TYR A 356     5865   2623   5525    162   1725     48       C  
ATOM   2963  C   TYR A 356      25.451  -2.030 100.188  1.00 32.83           C  
ANISOU 2963  C   TYR A 356     5376   2119   4977    204   1632     65       C  
ATOM   2964  O   TYR A 356      24.356  -2.403  99.739  1.00 35.97           O  
ANISOU 2964  O   TYR A 356     5871   2548   5247    259   1529    107       O  
ATOM   2965  CB  TYR A 356      26.317   0.337  99.956  1.00 39.08           C  
ANISOU 2965  CB  TYR A 356     6241   2820   5790    140   2004     38       C  
ATOM   2966  CG  TYR A 356      25.903   0.342  98.506  1.00 46.77           C  
ANISOU 2966  CG  TYR A 356     7412   3760   6600    209   2108     95       C  
ATOM   2967  CD1 TYR A 356      24.894   1.177  98.062  1.00 46.58           C  
ANISOU 2967  CD1 TYR A 356     7550   3732   6415    278   2143    159       C  
ATOM   2968  CD2 TYR A 356      26.551  -0.456  97.575  1.00 49.48           C  
ANISOU 2968  CD2 TYR A 356     7786   4067   6948    211   2180     83       C  
ATOM   2969  CE1 TYR A 356      24.514   1.196  96.737  1.00 38.67           C  
ANISOU 2969  CE1 TYR A 356     6744   2699   5251    355   2231    213       C  
ATOM   2970  CE2 TYR A 356      26.186  -0.440  96.252  1.00 35.13           C  
ANISOU 2970  CE2 TYR A 356     6164   2215   4970    273   2277    130       C  
ATOM   2971  CZ  TYR A 356      25.168   0.387  95.833  1.00 36.77           C  
ANISOU 2971  CZ  TYR A 356     6538   2425   5007    348   2297    196       C  
ATOM   2972  OH  TYR A 356      24.800   0.396  94.505  1.00 45.56           O  
ANISOU 2972  OH  TYR A 356     7861   3504   5946    425   2383    245       O  
ATOM   2973  N   ASP A 357      26.547  -2.793 100.132  1.00 30.83           N  
ANISOU 2973  N   ASP A 357     5030   1833   4849    177   1670     24       N  
ATOM   2974  CA  ASP A 357      26.527  -4.119  99.524  1.00 47.09           C  
ANISOU 2974  CA  ASP A 357     7110   3882   6899    211   1607     27       C  
ATOM   2975  C   ASP A 357      25.626  -5.069 100.293  1.00 40.87           C  
ANISOU 2975  C   ASP A 357     6273   3151   6106    236   1364     49       C  
ATOM   2976  O   ASP A 357      24.936  -5.898  99.690  1.00 59.65           O  
ANISOU 2976  O   ASP A 357     8727   5528   8408    269   1293     62       O  
ATOM   2977  CB  ASP A 357      27.935  -4.700  99.457  1.00 44.83           C  
ANISOU 2977  CB  ASP A 357     6718   3543   6773    185   1706    -21       C  
ATOM   2978  CG  ASP A 357      28.798  -4.016  98.436  1.00 39.75           C  
ANISOU 2978  CG  ASP A 357     6141   2830   6131    157   1965    -44       C  
ATOM   2979  OD1 ASP A 357      28.268  -3.555  97.403  1.00 48.74           O  
ANISOU 2979  OD1 ASP A 357     7455   3949   7114    181   2063    -11       O  
ATOM   2980  OD2 ASP A 357      30.021  -3.964  98.663  1.00 51.23           O1-
ANISOU 2980  OD2 ASP A 357     7474   4245   7746    112   2075    -96       O1-
ATOM   2981  N   PHE A 358      25.661  -5.005 101.628  1.00 32.80           N  
ANISOU 2981  N   PHE A 358     5125   2168   5168    215   1245     47       N  
ATOM   2982  CA  PHE A 358      24.769  -5.859 102.405  1.00 29.70           C  
ANISOU 2982  CA  PHE A 358     4699   1823   4762    235   1031     77       C  
ATOM   2983  C   PHE A 358      23.320  -5.574 102.061  1.00 48.28           C  
ANISOU 2983  C   PHE A 358     7159   4217   6969    258    956    109       C  
ATOM   2984  O   PHE A 358      22.510  -6.498 101.925  1.00 54.83           O  
ANISOU 2984  O   PHE A 358     8014   5056   7761    276    837    124       O  
ATOM   2985  CB  PHE A 358      24.976  -5.684 103.906  1.00 30.56           C  
ANISOU 2985  CB  PHE A 358     4685   1969   4957    211    926     77       C  
ATOM   2986  CG  PHE A 358      23.999  -6.483 104.731  1.00 38.32           C  
ANISOU 2986  CG  PHE A 358     5653   2997   5910    227    724    119       C  
ATOM   2987  CD1 PHE A 358      24.192  -7.840 104.934  1.00 36.68           C  
ANISOU 2987  CD1 PHE A 358     5414   2766   5757    250    647    139       C  
ATOM   2988  CD2 PHE A 358      22.853  -5.892 105.245  1.00 29.43           C  
ANISOU 2988  CD2 PHE A 358     4555   1925   4701    221    631    141       C  
ATOM   2989  CE1 PHE A 358      23.286  -8.586 105.675  1.00 33.53           C  
ANISOU 2989  CE1 PHE A 358     5018   2397   5325    257    487    182       C  
ATOM   2990  CE2 PHE A 358      21.945  -6.631 105.986  1.00 34.79           C  
ANISOU 2990  CE2 PHE A 358     5222   2640   5356    226    461    179       C  
ATOM   2991  CZ  PHE A 358      22.163  -7.978 106.199  1.00 31.84           C  
ANISOU 2991  CZ  PHE A 358     4827   2242   5029    239    393    200       C  
ATOM   2992  N   GLU A 359      22.971  -4.291 101.929  1.00 40.91           N  
ANISOU 2992  N   GLU A 359     6286   3297   5962    260   1036    120       N  
ATOM   2993  CA  GLU A 359      21.595  -3.972 101.554  1.00 44.57           C  
ANISOU 2993  CA  GLU A 359     6852   3796   6287    301    976    157       C  
ATOM   2994  C   GLU A 359      21.256  -4.535 100.179  1.00 47.74           C  
ANISOU 2994  C   GLU A 359     7382   4168   6588    339   1015    162       C  
ATOM   2995  O   GLU A 359      20.174  -5.104  99.982  1.00 25.14           O  
ANISOU 2995  O   GLU A 359     4559   1331   3661    363    894    175       O  
ATOM   2996  CB  GLU A 359      21.343  -2.465 101.575  1.00 25.31           C  
ANISOU 2996  CB  GLU A 359     4475   1358   3783    314   1083    175       C  
ATOM   2997  CG  GLU A 359      19.935  -2.137 101.097  1.00 34.51           C  
ANISOU 2997  CG  GLU A 359     5755   2555   4803    381   1030    222       C  
ATOM   2998  CD  GLU A 359      19.517  -0.702 101.341  1.00 46.08           C  
ANISOU 2998  CD  GLU A 359     7275   4020   6214    410   1114    249       C  
ATOM   2999  OE1 GLU A 359      20.285   0.222 101.004  1.00 53.69           O  
ANISOU 2999  OE1 GLU A 359     8292   4926   7182    401   1306    244       O  
ATOM   3000  OE2 GLU A 359      18.408  -0.504 101.876  1.00 58.81           O1-
ANISOU 3000  OE2 GLU A 359     8877   5681   7786    441   1000    275       O1-
ATOM   3001  N   LEU A 360      22.164  -4.375  99.210  1.00 50.58           N  
ANISOU 3001  N   LEU A 360     7813   4469   6938    341   1191    146       N  
ATOM   3002  CA  LEU A 360      21.913  -4.931  97.881  1.00 41.49           C  
ANISOU 3002  CA  LEU A 360     6800   3282   5684    376   1236    143       C  
ATOM   3003  C   LEU A 360      21.715  -6.442  97.942  1.00 37.06           C  
ANISOU 3003  C   LEU A 360     6188   2712   5182    360   1105    110       C  
ATOM   3004  O   LEU A 360      20.798  -6.987  97.314  1.00 38.24           O  
ANISOU 3004  O   LEU A 360     6426   2860   5243    382   1035    104       O  
ATOM   3005  CB  LEU A 360      23.062  -4.581  96.939  1.00 53.96           C  
ANISOU 3005  CB  LEU A 360     8452   4791   7261    369   1460    129       C  
ATOM   3006  CG  LEU A 360      22.936  -3.222  96.251  1.00 51.33           C  
ANISOU 3006  CG  LEU A 360     8269   4437   6799    409   1624    173       C  
ATOM   3007  CD1 LEU A 360      24.135  -2.980  95.363  1.00 52.61           C  
ANISOU 3007  CD1 LEU A 360     8495   4520   6976    390   1860    157       C  
ATOM   3008  CD2 LEU A 360      21.639  -3.158  95.455  1.00 51.17           C  
ANISOU 3008  CD2 LEU A 360     8417   4438   6589    491   1556    216       C  
ATOM   3009  N   LEU A 361      22.564  -7.129  98.705  1.00 27.87           N  
ANISOU 3009  N   LEU A 361     4886   1533   4171    325   1076     86       N  
ATOM   3010  CA  LEU A 361      22.488  -8.581  98.828  1.00 31.29           C  
ANISOU 3010  CA  LEU A 361     5275   1936   4676    315    977     61       C  
ATOM   3011  C   LEU A 361      21.158  -9.006  99.434  1.00 35.09           C  
ANISOU 3011  C   LEU A 361     5738   2463   5132    311    790     80       C  
ATOM   3012  O   LEU A 361      20.500  -9.939  98.951  1.00 47.86           O  
ANISOU 3012  O   LEU A 361     7406   4050   6728    306    734     55       O  
ATOM   3013  CB  LEU A 361      23.657  -9.065  99.687  1.00 30.56           C  
ANISOU 3013  CB  LEU A 361     5044   1822   4747    301    984     54       C  
ATOM   3014  CG  LEU A 361      23.714 -10.514 100.161  1.00 28.82           C  
ANISOU 3014  CG  LEU A 361     4764   1564   4623    304    887     50       C  
ATOM   3015  CD1 LEU A 361      23.691 -11.446  98.968  1.00 28.52           C  
ANISOU 3015  CD1 LEU A 361     4824   1449   4563    310    956      3       C  
ATOM   3016  CD2 LEU A 361      24.959 -10.743 101.006  1.00 27.73           C  
ANISOU 3016  CD2 LEU A 361     4497   1406   4632    313    915     59       C  
ATOM   3017  N   ILE A 362      20.757  -8.331 100.511  1.00 37.40           N  
ANISOU 3017  N   ILE A 362     5955   2820   5434    305    704    117       N  
ATOM   3018  CA  ILE A 362      19.478  -8.615 101.151  1.00 28.80           C  
ANISOU 3018  CA  ILE A 362     4837   1776   4329    296    543    141       C  
ATOM   3019  C   ILE A 362      18.340  -8.420 100.162  1.00 40.98           C  
ANISOU 3019  C   ILE A 362     6501   3329   5742    323    541    138       C  
ATOM   3020  O   ILE A 362      17.455  -9.271 100.032  1.00 25.16           O  
ANISOU 3020  O   ILE A 362     4507   1314   3738    308    452    123       O  
ATOM   3021  CB  ILE A 362      19.299  -7.735 102.400  1.00 23.67           C  
ANISOU 3021  CB  ILE A 362     4102   1191   3699    288    480    176       C  
ATOM   3022  CG1 ILE A 362      20.157  -8.262 103.550  1.00 48.08           C  
ANISOU 3022  CG1 ILE A 362     7085   4275   6907    264    427    182       C  
ATOM   3023  CG2 ILE A 362      17.857  -7.686 102.819  1.00 34.29           C  
ANISOU 3023  CG2 ILE A 362     5439   2589   5002    288    358    204       C  
ATOM   3024  CD1 ILE A 362      19.455  -9.242 104.465  1.00 22.52           C  
ANISOU 3024  CD1 ILE A 362     3800   1050   3708    244    267    211       C  
ATOM   3025  N   LYS A 363      18.343  -7.292  99.451  1.00 41.76           N  
ANISOU 3025  N   LYS A 363     6702   3440   5726    366    647    154       N  
ATOM   3026  CA  LYS A 363      17.257  -7.011  98.521  1.00 31.81           C  
ANISOU 3026  CA  LYS A 363     5579   2192   4316    418    637    165       C  
ATOM   3027  C   LYS A 363      17.250  -7.977  97.348  1.00 32.18           C  
ANISOU 3027  C   LYS A 363     5730   2174   4321    416    663    111       C  
ATOM   3028  O   LYS A 363      16.207  -8.156  96.709  1.00 42.31           O  
ANISOU 3028  O   LYS A 363     7179   3439   5458    457    648    104       O  
ATOM   3029  CB  LYS A 363      17.343  -5.563  98.038  1.00 31.61           C  
ANISOU 3029  CB  LYS A 363     5660   2180   4171    482    757    210       C  
ATOM   3030  CG  LYS A 363      17.169  -4.560  99.172  1.00 34.18           C  
ANISOU 3030  CG  LYS A 363     5897   2556   4532    482    736    247       C  
ATOM   3031  CD  LYS A 363      16.411  -3.310  98.739  1.00 41.22           C  
ANISOU 3031  CD  LYS A 363     6910   3471   5281    573    787    303       C  
ATOM   3032  CE  LYS A 363      17.323  -2.305  98.048  1.00 59.67           C  
ANISOU 3032  CE  LYS A 363     9355   5754   7564    602    996    320       C  
ATOM   3033  NZ  LYS A 363      16.688  -1.716  96.840  1.00 79.76           N  
ANISOU 3033  NZ  LYS A 363    12094   8288   9925    718   1061    374       N  
ATOM   3034  N   GLY A 364      18.382  -8.606  97.061  1.00 38.69           N  
ANISOU 3034  N   GLY A 364     6539   2937   5223    384    751     69       N  
ATOM   3035  CA  GLY A 364      18.404  -9.690  96.103  1.00 35.11           C  
ANISOU 3035  CA  GLY A 364     6168   2412   4760    367    773     -4       C  
ATOM   3036  C   GLY A 364      17.792 -10.969  96.642  1.00 35.46           C  
ANISOU 3036  C   GLY A 364     6133   2434   4907    312    643    -48       C  
ATOM   3037  O   GLY A 364      17.050 -11.655  95.932  1.00 45.46           O  
ANISOU 3037  O   GLY A 364     7560   3635   6078    300    665   -114       O  
ATOM   3038  N   VAL A 365      18.092 -11.303  97.897  1.00 39.71           N  
ANISOU 3038  N   VAL A 365     6518   2986   5582    283    574    -14       N  
ATOM   3039  CA  VAL A 365      17.603 -12.563  98.459  1.00 40.73           C  
ANISOU 3039  CA  VAL A 365     6583   3076   5819    232    471    -40       C  
ATOM   3040  C   VAL A 365      16.117 -12.475  98.802  1.00 44.44           C  
ANISOU 3040  C   VAL A 365     7039   3594   6253    212    354    -30       C  
ATOM   3041  O   VAL A 365      15.318 -13.327  98.392  1.00 36.17           O  
ANISOU 3041  O   VAL A 365     6085   2481   5175    170    349    -98       O  
ATOM   3042  CB  VAL A 365      18.435 -12.970  99.688  1.00 45.03           C  
ANISOU 3042  CB  VAL A 365     6997   3613   6500    224    436      9       C  
ATOM   3043  CG1 VAL A 365      17.931 -14.298 100.248  1.00 30.40           C  
ANISOU 3043  CG1 VAL A 365     5108   1700   4742    178    345      1       C  
ATOM   3044  CG2 VAL A 365      19.914 -13.053  99.326  1.00 27.18           C  
ANISOU 3044  CG2 VAL A 365     4742   1303   4283    249    569     -6       C  
ATOM   3045  N   TYR A 366      15.727 -11.457  99.567  1.00 53.36           N  
ANISOU 3045  N   TYR A 366     8110   4812   7352    238    307     44       N  
ATOM   3046  CA  TYR A 366      14.364 -11.286 100.046  1.00 47.63           C  
ANISOU 3046  CA  TYR A 366     7379   4132   6585    231    223     69       C  
ATOM   3047  C   TYR A 366      13.721 -10.040  99.453  1.00 49.05           C  
ANISOU 3047  C   TYR A 366     7731   4354   6550    316    263    101       C  
ATOM   3048  O   TYR A 366      14.391  -9.151  98.918  1.00 46.01           O  
ANISOU 3048  O   TYR A 366     7391   3986   6103    369    346    121       O  
ATOM   3049  CB  TYR A 366      14.301 -11.147 101.570  1.00 25.35           C  
ANISOU 3049  CB  TYR A 366     4382   1370   3880    208    139    140       C  
ATOM   3050  CG  TYR A 366      14.971 -12.236 102.371  1.00 26.99           C  
ANISOU 3050  CG  TYR A 366     4500   1520   4234    161    100    147       C  
ATOM   3051  CD1 TYR A 366      14.410 -13.500 102.474  1.00 29.36           C  
ANISOU 3051  CD1 TYR A 366     4786   1753   4616    103     59    122       C  
ATOM   3052  CD2 TYR A 366      16.147 -11.986 103.060  1.00 31.36           C  
ANISOU 3052  CD2 TYR A 366     5006   2082   4828    179    101    180       C  
ATOM   3053  CE1 TYR A 366      15.017 -14.488 103.223  1.00 33.01           C  
ANISOU 3053  CE1 TYR A 366     5211   2153   5180     78     11    149       C  
ATOM   3054  CE2 TYR A 366      16.755 -12.965 103.813  1.00 23.45           C  
ANISOU 3054  CE2 TYR A 366     3973   1027   3908    160     52    201       C  
ATOM   3055  CZ  TYR A 366      16.184 -14.212 103.889  1.00 43.86           C  
ANISOU 3055  CZ  TYR A 366     6570   3542   6551    116      3    195       C  
ATOM   3056  OH  TYR A 366      16.795 -15.185 104.638  1.00 41.61           O  
ANISOU 3056  OH  TYR A 366     6307   3204   6298    112    -20    230       O  
ATOM   3057  N   GLN A 367      12.401  -9.982  99.599  1.00 41.65           N  
ANISOU 3057  N   GLN A 367     6907   3427   5491    338    192    111       N  
ATOM   3058  CA  GLN A 367      11.615  -8.787  99.310  1.00 37.53           C  
ANISOU 3058  CA  GLN A 367     6538   2958   4766    458    175    169       C  
ATOM   3059  C   GLN A 367      11.490  -8.006 100.617  1.00 53.33           C  
ANISOU 3059  C   GLN A 367     8322   5061   6881    451    129    244       C  
ATOM   3060  O   GLN A 367      10.709  -8.367 101.499  1.00 58.91           O  
ANISOU 3060  O   GLN A 367     8960   5791   7631    415     39    258       O  
ATOM   3061  CB  GLN A 367      10.266  -9.191  98.721  1.00 47.91           C  
ANISOU 3061  CB  GLN A 367     8127   4216   5859    511     67    127       C  
ATOM   3062  CG  GLN A 367       9.187  -8.126  98.683  1.00 73.74           C  
ANISOU 3062  CG  GLN A 367    11524   7565   8928    684    -28    216       C  
ATOM   3063  CD  GLN A 367       7.904  -8.649  98.067  1.00 93.06           C  
ANISOU 3063  CD  GLN A 367    14051  10155  11151    697   -199    137       C  
ATOM   3064  OE1 GLN A 367       7.540  -8.290  96.949  1.00103.20           O  
ANISOU 3064  OE1 GLN A 367    15429  11601  12180    806   -220    124       O  
ATOM   3065  NE2 GLN A 367       7.218  -9.519  98.795  1.00 82.34           N  
ANISOU 3065  NE2 GLN A 367    12531   8870   9884    537   -315     61       N  
ATOM   3066  N   VAL A 368      12.286  -6.942 100.756  1.00 55.71           N  
ANISOU 3066  N   VAL A 368     8532   5408   7227    474    197    277       N  
ATOM   3067  CA  VAL A 368      12.307  -6.172 101.998  1.00 45.39           C  
ANISOU 3067  CA  VAL A 368     7042   4176   6029    450    159    317       C  
ATOM   3068  C   VAL A 368      11.101  -5.234 102.062  1.00 50.89           C  
ANISOU 3068  C   VAL A 368     7833   4924   6579    553    136    371       C  
ATOM   3069  O   VAL A 368      10.419  -4.971 101.064  1.00 72.31           O  
ANISOU 3069  O   VAL A 368    10753   7628   9092    673    145    393       O  
ATOM   3070  CB  VAL A 368      13.634  -5.402 102.111  1.00 50.24           C  
ANISOU 3070  CB  VAL A 368     7646   4770   6675    443    264    306       C  
ATOM   3071  CG1 VAL A 368      13.801  -4.757 103.475  1.00 57.20           C  
ANISOU 3071  CG1 VAL A 368     8417   5685   7631    415    244    321       C  
ATOM   3072  CG2 VAL A 368      14.782  -6.334 101.844  1.00 66.87           C  
ANISOU 3072  CG2 VAL A 368     9732   6813   8862    388    302    261       C  
ATOM   3073  N   ASN A 369      10.822  -4.740 103.270  1.00 47.73           N  
ANISOU 3073  N   ASN A 369     7290   4579   6267    525     93    397       N  
ATOM   3074  CA  ASN A 369       9.724  -3.809 103.509  1.00 50.23           C  
ANISOU 3074  CA  ASN A 369     7659   4951   6477    626     70    449       C  
ATOM   3075  C   ASN A 369      10.281  -2.397 103.661  1.00 43.76           C  
ANISOU 3075  C   ASN A 369     6816   4134   5678    650    163    457       C  
ATOM   3076  O   ASN A 369      10.700  -2.011 104.767  1.00 47.24           O  
ANISOU 3076  O   ASN A 369     7167   4572   6210    593    176    438       O  
ATOM   3077  CB  ASN A 369       8.941  -4.219 104.758  1.00 59.24           C  
ANISOU 3077  CB  ASN A 369     8689   6135   7685    582    -23    467       C  
ATOM   3078  CG  ASN A 369       7.537  -3.652 104.777  1.00 75.69           C  
ANISOU 3078  CG  ASN A 369    10854   8284   9622    715    -86    521       C  
ATOM   3079  OD1 ASN A 369       6.923  -3.448 103.731  1.00 94.11           O  
ANISOU 3079  OD1 ASN A 369    13339  10641  11778    853   -109    547       O  
ATOM   3080  ND2 ASN A 369       7.018  -3.397 105.971  1.00 71.72           N  
ANISOU 3080  ND2 ASN A 369    10245   7827   9180    695   -123    543       N  
ATOM   3081  N   PRO A 370      10.274  -1.583 102.597  1.00 38.18           N  
ANISOU 3081  N   PRO A 370     6262   3410   4835    761    256    485       N  
ATOM   3082  CA  PRO A 370      11.027  -0.312 102.620  1.00 46.41           C  
ANISOU 3082  CA  PRO A 370     7343   4411   5880    780    400    485       C  
ATOM   3083  C   PRO A 370      10.725   0.569 103.819  1.00 46.53           C  
ANISOU 3083  C   PRO A 370     7291   4439   5951    777    410    489       C  
ATOM   3084  O   PRO A 370      11.648   1.097 104.453  1.00 46.81           O  
ANISOU 3084  O   PRO A 370     7300   4426   6058    714    500    451       O  
ATOM   3085  CB  PRO A 370      10.599   0.354 101.303  1.00 46.23           C  
ANISOU 3085  CB  PRO A 370     7493   4384   5687    931    476    546       C  
ATOM   3086  CG  PRO A 370      10.182  -0.779 100.424  1.00 58.03           C  
ANISOU 3086  CG  PRO A 370     9095   5889   7064    979    406    549       C  
ATOM   3087  CD  PRO A 370       9.502  -1.737 101.353  1.00 52.43           C  
ANISOU 3087  CD  PRO A 370     8266   5224   6431    910    251    527       C  
ATOM   3088  N   THR A 371       9.443   0.727 104.143  1.00 55.12           N  
ANISOU 3088  N   THR A 371     8347   5589   7006    846    321    531       N  
ATOM   3089  CA  THR A 371       8.958   1.476 105.295  1.00 41.60           C  
ANISOU 3089  CA  THR A 371     6571   3891   5343    853    320    534       C  
ATOM   3090  C   THR A 371       9.815   1.281 106.542  1.00 35.03           C  
ANISOU 3090  C   THR A 371     5638   3030   4643    718    319    470       C  
ATOM   3091  O   THR A 371      10.117   2.248 107.249  1.00 24.18           O  
ANISOU 3091  O   THR A 371     4268   1618   3303    710    405    447       O  
ATOM   3092  CB  THR A 371       7.505   1.075 105.585  1.00 54.65           C  
ANISOU 3092  CB  THR A 371     8194   5629   6943    931    198    582       C  
ATOM   3093  OG1 THR A 371       6.631   1.688 104.628  1.00 59.94           O  
ANISOU 3093  OG1 THR A 371     8985   6338   7450   1121    226    654       O  
ATOM   3094  CG2 THR A 371       7.087   1.481 107.006  1.00 49.65           C  
ANISOU 3094  CG2 THR A 371     7465   5009   6390    901    177    569       C  
ATOM   3095  N   LYS A 372      10.232   0.046 106.807  1.00 29.31           N  
ANISOU 3095  N   LYS A 372     4828   2318   3990    618    228    443       N  
ATOM   3096  CA  LYS A 372      10.881  -0.295 108.068  1.00 27.62           C  
ANISOU 3096  CA  LYS A 372     4505   2098   3892    512    189    402       C  
ATOM   3097  C   LYS A 372      12.400  -0.183 108.025  1.00 31.76           C  
ANISOU 3097  C   LYS A 372     5039   2566   4464    451    273    353       C  
ATOM   3098  O   LYS A 372      13.055  -0.488 109.030  1.00 37.08           O  
ANISOU 3098  O   LYS A 372     5629   3236   5223    375    229    321       O  
ATOM   3099  CB  LYS A 372      10.500  -1.719 108.488  1.00 39.50           C  
ANISOU 3099  CB  LYS A 372     5906   3644   5460    449     59    421       C  
ATOM   3100  CG  LYS A 372       9.042  -2.075 108.262  1.00 52.30           C  
ANISOU 3100  CG  LYS A 372     7516   5325   7032    502    -12    477       C  
ATOM   3101  CD  LYS A 372       8.622  -3.231 109.158  1.00 55.29           C  
ANISOU 3101  CD  LYS A 372     7809   5731   7468    438    -80    505       C  
ATOM   3102  CE  LYS A 372       7.113  -3.381 109.211  1.00 62.61           C  
ANISOU 3102  CE  LYS A 372     8804   6708   8276    521   -143    554       C  
ATOM   3103  NZ  LYS A 372       6.724  -4.682 109.822  1.00 56.54           N  
ANISOU 3103  NZ  LYS A 372     8011   5951   7522    451   -207    574       N  
ATOM   3104  N   THR A 373      12.976   0.242 106.904  1.00 22.38           N  
ANISOU 3104  N   THR A 373     3952   1334   3217    489    393    352       N  
ATOM   3105  CA  THR A 373      14.425   0.302 106.780  1.00 27.65           C  
ANISOU 3105  CA  THR A 373     4620   1949   3936    432    488    309       C  
ATOM   3106  C   THR A 373      14.971   1.496 107.554  1.00 34.26           C  
ANISOU 3106  C   THR A 373     5454   2745   4817    404    599    273       C  
ATOM   3107  O   THR A 373      14.429   2.603 107.473  1.00 48.88           O  
ANISOU 3107  O   THR A 373     7379   4574   6619    461    693    290       O  
ATOM   3108  CB  THR A 373      14.822   0.395 105.304  1.00 24.68           C  
ANISOU 3108  CB  THR A 373     4362   1534   3483    480    604    325       C  
ATOM   3109  OG1 THR A 373      14.614  -0.873 104.670  1.00 36.77           O  
ANISOU 3109  OG1 THR A 373     5885   3087   4999    477    508    333       O  
ATOM   3110  CG2 THR A 373      16.285   0.791 105.150  1.00 35.46           C  
ANISOU 3110  CG2 THR A 373     5735   2836   4903    428    753    285       C  
ATOM   3111  N   ARG A 374      16.042   1.267 108.318  1.00 34.34           N  
ANISOU 3111  N   ARG A 374     5383   2740   4924    320    592    220       N  
ATOM   3112  CA  ARG A 374      16.681   2.336 109.082  1.00 31.56           C  
ANISOU 3112  CA  ARG A 374     5019   2343   4629    271    703    164       C  
ATOM   3113  C   ARG A 374      18.187   2.281 108.868  1.00 33.13           C  
ANISOU 3113  C   ARG A 374     5190   2496   4903    205    802    113       C  
ATOM   3114  O   ARG A 374      18.809   1.246 109.120  1.00 34.97           O  
ANISOU 3114  O   ARG A 374     5345   2751   5190    170    703    103       O  
ATOM   3115  CB  ARG A 374      16.354   2.230 110.576  1.00 23.66           C  
ANISOU 3115  CB  ARG A 374     3934   1378   3680    226    580    133       C  
ATOM   3116  CG  ARG A 374      14.875   2.345 110.895  1.00 30.67           C  
ANISOU 3116  CG  ARG A 374     4835   2307   4512    286    499    176       C  
ATOM   3117  CD  ARG A 374      14.344   3.726 110.552  1.00 21.71           C  
ANISOU 3117  CD  ARG A 374     3796   1125   3328    348    654    182       C  
ATOM   3118  NE  ARG A 374      12.931   3.859 110.898  1.00 48.73           N  
ANISOU 3118  NE  ARG A 374     7222   4587   6706    418    579    222       N  
ATOM   3119  CZ  ARG A 374      11.926   3.509 110.104  1.00 32.48           C  
ANISOU 3119  CZ  ARG A 374     5198   2571   4572    506    524    293       C  
ATOM   3120  NH1 ARG A 374      12.171   3.008 108.901  1.00 29.65           N  
ANISOU 3120  NH1 ARG A 374     4887   2216   4163    533    534    326       N  
ATOM   3121  NH2 ARG A 374      10.676   3.665 110.515  1.00 48.47           N  
ANISOU 3121  NH2 ARG A 374     7209   4635   6572    569    461    324       N  
ATOM   3122  N   THR A 375      18.771   3.388 108.409  1.00 34.13           N  
ANISOU 3122  N   THR A 375     5379   2551   5038    192   1010     86       N  
ATOM   3123  CA  THR A 375      20.185   3.365 108.055  1.00 31.99           C  
ANISOU 3123  CA  THR A 375     5077   2233   4846    128   1130     36       C  
ATOM   3124  C   THR A 375      20.724   4.782 107.948  1.00 41.00           C  
ANISOU 3124  C   THR A 375     6270   3286   6021     84   1372    -14       C  
ATOM   3125  O   THR A 375      19.981   5.737 107.699  1.00 45.25           O  
ANISOU 3125  O   THR A 375     6914   3786   6493    135   1474     22       O  
ATOM   3126  CB  THR A 375      20.422   2.628 106.732  1.00 42.67           C  
ANISOU 3126  CB  THR A 375     6484   3582   6148    175   1153     84       C  
ATOM   3127  OG1 THR A 375      21.826   2.597 106.447  1.00 38.20           O  
ANISOU 3127  OG1 THR A 375     5875   2967   5674    113   1279     31       O  
ATOM   3128  CG2 THR A 375      19.694   3.332 105.600  1.00 45.65           C  
ANISOU 3128  CG2 THR A 375     7018   3926   6399    261   1274    149       C  
ATOM   3129  N   ASN A 376      22.039   4.899 108.146  1.00 42.83           N  
ANISOU 3129  N   ASN A 376     6425   3480   6367    -11   1471    -99       N  
ATOM   3130  CA  ASN A 376      22.798   6.100 107.819  1.00 41.33           C  
ANISOU 3130  CA  ASN A 376     6279   3195   6231    -74   1738   -158       C  
ATOM   3131  C   ASN A 376      23.594   5.930 106.527  1.00 50.81           C  
ANISOU 3131  C   ASN A 376     7531   4346   7427    -63   1889   -133       C  
ATOM   3132  O   ASN A 376      24.671   6.514 106.370  1.00 61.47           O  
ANISOU 3132  O   ASN A 376     8856   5627   8873   -149   2089   -211       O  
ATOM   3133  CB  ASN A 376      23.719   6.485 108.977  1.00 29.32           C  
ANISOU 3133  CB  ASN A 376     4624   1664   4852   -210   1771   -302       C  
ATOM   3134  CG  ASN A 376      24.768   5.433 109.266  1.00 50.10           C  
ANISOU 3134  CG  ASN A 376     7113   4342   7582   -262   1660   -355       C  
ATOM   3135  OD1 ASN A 376      24.626   4.278 108.871  1.00 41.98           O  
ANISOU 3135  OD1 ASN A 376     6077   3359   6516   -191   1514   -277       O  
ATOM   3136  ND2 ASN A 376      25.825   5.826 109.972  1.00 42.42           N  
ANISOU 3136  ND2 ASN A 376     6021   3339   6757   -396   1784   -506       N  
ATOM   3137  N   LEU A 377      23.082   5.127 105.602  1.00 41.92           N  
ANISOU 3137  N   LEU A 377     6476   3255   6197     33   1805    -39       N  
ATOM   3138  CA  LEU A 377      23.699   4.992 104.288  1.00 36.94           C  
ANISOU 3138  CA  LEU A 377     5925   2574   5535     55   1957    -10       C  
ATOM   3139  C   LEU A 377      23.475   6.272 103.489  1.00 48.88           C  
ANISOU 3139  C   LEU A 377     7610   3993   6971     92   2205     31       C  
ATOM   3140  O   LEU A 377      22.338   6.754 103.409  1.00 52.43           O  
ANISOU 3140  O   LEU A 377     8165   4445   7310    179   2180    100       O  
ATOM   3141  CB  LEU A 377      23.110   3.801 103.537  1.00 36.53           C  
ANISOU 3141  CB  LEU A 377     5916   2584   5381    143   1798     65       C  
ATOM   3142  CG  LEU A 377      23.794   2.442 103.710  1.00 41.98           C  
ANISOU 3142  CG  LEU A 377     6479   3318   6155    113   1661     34       C  
ATOM   3143  CD1 LEU A 377      22.847   1.318 103.321  1.00 42.67           C  
ANISOU 3143  CD1 LEU A 377     6601   3469   6143    190   1470     97       C  
ATOM   3144  CD2 LEU A 377      25.077   2.370 102.902  1.00 41.72           C  
ANISOU 3144  CD2 LEU A 377     6442   3220   6189     72   1846     -2       C  
ATOM   3145  N   PRO A 378      24.520   6.845 102.886  1.00 52.33           N  
ANISOU 3145  N   PRO A 378     8081   4338   7463     36   2457     -8       N  
ATOM   3146  CA  PRO A 378      24.322   8.067 102.090  1.00 52.92           C  
ANISOU 3146  CA  PRO A 378     8343   4304   7461     82   2718     42       C  
ATOM   3147  C   PRO A 378      23.381   7.870 100.919  1.00 48.58           C  
ANISOU 3147  C   PRO A 378     7977   3764   6717    236   2693    170       C  
ATOM   3148  O   PRO A 378      22.826   8.854 100.414  1.00 63.56           O  
ANISOU 3148  O   PRO A 378    10044   5587   8520    320   2849    238       O  
ATOM   3149  CB  PRO A 378      25.743   8.411 101.614  1.00 53.81           C  
ANISOU 3149  CB  PRO A 378     8437   4325   7682    -18   2977    -34       C  
ATOM   3150  CG  PRO A 378      26.649   7.650 102.542  1.00 54.96           C  
ANISOU 3150  CG  PRO A 378     8352   4535   7995   -134   2846   -150       C  
ATOM   3151  CD  PRO A 378      25.911   6.378 102.809  1.00 38.19           C  
ANISOU 3151  CD  PRO A 378     6171   2531   5807    -60   2528    -93       C  
ATOM   3152  N   THR A 379      23.185   6.624 100.478  1.00 49.58           N  
ANISOU 3152  N   THR A 379     8079   3974   6785    280   2506    199       N  
ATOM   3153  CA  THR A 379      22.298   6.330  99.361  1.00 46.61           C  
ANISOU 3153  CA  THR A 379     7868   3618   6224    419   2462    298       C  
ATOM   3154  C   THR A 379      20.837   6.611  99.685  1.00 51.60           C  
ANISOU 3154  C   THR A 379     8551   4300   6754    524   2319    362       C  
ATOM   3155  O   THR A 379      20.009   6.654  98.770  1.00 48.63           O  
ANISOU 3155  O   THR A 379     8327   3931   6219    657   2309    445       O  
ATOM   3156  CB  THR A 379      22.456   4.866  98.951  1.00 36.45           C  
ANISOU 3156  CB  THR A 379     6523   2405   4924    416   2292    287       C  
ATOM   3157  OG1 THR A 379      22.684   4.066 100.120  1.00 44.25           O  
ANISOU 3157  OG1 THR A 379     7303   3462   6046    331   2098    221       O  
ATOM   3158  CG2 THR A 379      23.627   4.700  97.997  1.00 41.14           C  
ANISOU 3158  CG2 THR A 379     7163   2930   5540    379   2487    266       C  
ATOM   3159  N   HIS A 380      20.499   6.791 100.959  1.00 58.44           N  
ANISOU 3159  N   HIS A 380     9294   5203   7708    472   2208    323       N  
ATOM   3160  CA  HIS A 380      19.115   6.939 101.388  1.00 43.28           C  
ANISOU 3160  CA  HIS A 380     7393   3338   5713    562   2057    374       C  
ATOM   3161  C   HIS A 380      18.782   8.404 101.641  1.00 41.22           C  
ANISOU 3161  C   HIS A 380     7226   2988   5448    601   2241    402       C  
ATOM   3162  O   HIS A 380      19.633   9.180 102.084  1.00 35.06           O  
ANISOU 3162  O   HIS A 380     6422   2121   4780    503   2426    342       O  
ATOM   3163  CB  HIS A 380      18.848   6.111 102.646  1.00 41.39           C  
ANISOU 3163  CB  HIS A 380     6967   3195   5563    491   1810    318       C  
ATOM   3164  CG  HIS A 380      18.525   4.677 102.360  1.00 63.37           C  
ANISOU 3164  CG  HIS A 380     9697   6071   8310    508   1595    326       C  
ATOM   3165  ND1 HIS A 380      17.233   4.202 102.284  1.00 69.88           N  
ANISOU 3165  ND1 HIS A 380    10539   6968   9043    593   1419    374       N  
ATOM   3166  CD2 HIS A 380      19.331   3.617 102.111  1.00 59.51           C  
ANISOU 3166  CD2 HIS A 380     9139   5600   7873    450   1544    289       C  
ATOM   3167  CE1 HIS A 380      17.259   2.909 102.013  1.00 65.00           C  
ANISOU 3167  CE1 HIS A 380     9868   6404   8426    574   1274    360       C  
ATOM   3168  NE2 HIS A 380      18.519   2.529 101.903  1.00 54.61           N  
ANISOU 3168  NE2 HIS A 380     8504   5054   7194    493   1347    313       N  
ATOM   3169  N   ARG A 381      17.526   8.770 101.368  1.00 46.40           N  
ANISOU 3169  N   ARG A 381     7983   3661   5984    746   2194    489       N  
ATOM   3170  CA  ARG A 381      17.138  10.178 101.366  1.00 51.05           C  
ANISOU 3170  CA  ARG A 381     8700   4147   6551    823   2396    541       C  
ATOM   3171  C   ARG A 381      17.194  10.789 102.762  1.00 60.73           C  
ANISOU 3171  C   ARG A 381     9820   5342   7914    719   2416    468       C  
ATOM   3172  O   ARG A 381      17.569  11.957 102.917  1.00 75.51           O  
ANISOU 3172  O   ARG A 381    11762   7086   9842    690   2660    455       O  
ATOM   3173  CB  ARG A 381      15.735  10.326 100.773  1.00 49.33           C  
ANISOU 3173  CB  ARG A 381     8596   3972   6176   1025   2315    656       C  
ATOM   3174  CG  ARG A 381      15.664  10.131  99.260  1.00 52.34           C  
ANISOU 3174  CG  ARG A 381     9138   4350   6401   1159   2369    737       C  
ATOM   3175  CD  ARG A 381      15.112  11.370  98.565  1.00 74.51           C  
ANISOU 3175  CD  ARG A 381    12144   7063   9103   1345   2571    852       C  
ATOM   3176  NE  ARG A 381      15.469  11.435  97.149  1.00 95.16           N  
ANISOU 3176  NE  ARG A 381    14935   9630  11593   1450   2712    916       N  
ATOM   3177  CZ  ARG A 381      14.997  10.620  96.209  1.00103.59           C  
ANISOU 3177  CZ  ARG A 381    16052  10788  12521   1558   2562    958       C  
ATOM   3178  NH1 ARG A 381      14.128   9.668  96.516  1.00103.52           N  
ANISOU 3178  NH1 ARG A 381    15923  10922  12486   1570   2273    944       N  
ATOM   3179  NH2 ARG A 381      15.392  10.766  94.953  1.00105.01           N  
ANISOU 3179  NH2 ARG A 381    16403  10909  12589   1653   2712   1011       N  
ATOM   3180  N   HIS A 382      16.829  10.024 103.787  1.00 52.54           N  
ANISOU 3180  N   HIS A 382     8620   4409   6932    659   2175    413       N  
ATOM   3181  CA  HIS A 382      16.640  10.548 105.141  1.00 61.12           C  
ANISOU 3181  CA  HIS A 382     9619   5482   8123    585   2161    346       C  
ATOM   3182  C   HIS A 382      17.447   9.723 106.135  1.00 58.29           C  
ANISOU 3182  C   HIS A 382     9072   5188   7888    427   2021    230       C  
ATOM   3183  O   HIS A 382      16.895   8.898 106.872  1.00 65.92           O  
ANISOU 3183  O   HIS A 382     9929   6257   8861    421   1787    213       O  
ATOM   3184  CB  HIS A 382      15.157  10.555 105.512  1.00 62.80           C  
ANISOU 3184  CB  HIS A 382     9838   5757   8267    705   2008    407       C  
ATOM   3185  CG  HIS A 382      14.334  11.467 104.661  1.00 68.17           C  
ANISOU 3185  CG  HIS A 382    10695   6373   8835    882   2146    524       C  
ATOM   3186  ND1 HIS A 382      13.453  11.010 103.704  1.00 67.78           N  
ANISOU 3186  ND1 HIS A 382    10714   6397   8641   1042   2037    623       N  
ATOM   3187  CD2 HIS A 382      14.272  12.818 104.615  1.00 71.91           C  
ANISOU 3187  CD2 HIS A 382    11292   6710   9319    932   2393    559       C  
ATOM   3188  CE1 HIS A 382      12.875  12.041 103.112  1.00 71.16           C  
ANISOU 3188  CE1 HIS A 382    11298   6748   8990   1200   2199    722       C  
ATOM   3189  NE2 HIS A 382      13.356  13.149 103.646  1.00 77.38           N  
ANISOU 3189  NE2 HIS A 382    12129   7401   9873   1139   2424    691       N  
ATOM   3190  N   PRO A 383      18.761   9.929 106.184  1.00 51.89           N  
ANISOU 3190  N   PRO A 383     8220   4318   7179    302   2167    147       N  
ATOM   3191  CA  PRO A 383      19.605   9.095 107.050  1.00 43.21           C  
ANISOU 3191  CA  PRO A 383     6940   3285   6193    173   2030     42       C  
ATOM   3192  C   PRO A 383      19.261   9.260 108.527  1.00 42.66           C  
ANISOU 3192  C   PRO A 383     6768   3248   6193    109   1923    -37       C  
ATOM   3193  O   PRO A 383      19.131  10.376 109.039  1.00 48.73           O  
ANISOU 3193  O   PRO A 383     7576   3939   7001     75   2072    -82       O  
ATOM   3194  CB  PRO A 383      21.025   9.584 106.735  1.00 39.06           C  
ANISOU 3194  CB  PRO A 383     6405   2671   5767     63   2262    -36       C  
ATOM   3195  CG  PRO A 383      20.925  10.245 105.411  1.00 49.30           C  
ANISOU 3195  CG  PRO A 383     7886   3875   6971    152   2478     55       C  
ATOM   3196  CD  PRO A 383      19.555  10.837 105.339  1.00 35.14           C  
ANISOU 3196  CD  PRO A 383     6215   2067   5069    286   2466    152       C  
ATOM   3197  N   GLN A 384      19.098   8.124 109.203  1.00 54.51           N  
ANISOU 3197  N   GLN A 384     8149   4859   7705     95   1671    -54       N  
ATOM   3198  CA  GLN A 384      19.015   8.053 110.654  1.00 46.40           C  
ANISOU 3198  CA  GLN A 384     7012   3874   6745     20   1552   -143       C  
ATOM   3199  C   GLN A 384      20.354   7.577 111.199  1.00 41.93           C  
ANISOU 3199  C   GLN A 384     6314   3327   6290   -107   1526   -253       C  
ATOM   3200  O   GLN A 384      21.081   6.852 110.518  1.00 48.02           O  
ANISOU 3200  O   GLN A 384     7056   4111   7077   -107   1510   -231       O  
ATOM   3201  CB  GLN A 384      17.936   7.074 111.090  1.00 49.88           C  
ANISOU 3201  CB  GLN A 384     7414   4416   7123     92   1296    -82       C  
ATOM   3202  CG  GLN A 384      16.564   7.319 110.517  1.00 61.29           C  
ANISOU 3202  CG  GLN A 384     8961   5867   8460    226   1282     23       C  
ATOM   3203  CD  GLN A 384      15.474   7.200 111.543  1.00 75.87           C  
ANISOU 3203  CD  GLN A 384    10766   7767  10294    253   1137     20       C  
ATOM   3204  OE1 GLN A 384      15.710   6.775 112.666  1.00 89.84           O  
ANISOU 3204  OE1 GLN A 384    12438   9576  12119    175   1024    -51       O  
ATOM   3205  NE2 GLN A 384      14.256   7.551 111.150  1.00 78.12           N  
ANISOU 3205  NE2 GLN A 384    11127   8055  10500    371   1138     99       N  
ATOM   3206  N   ASP A 385      20.675   7.969 112.429  1.00 37.95           N  
ANISOU 3206  N   ASP A 385     5728   2828   5861   -214   1522   -379       N  
ATOM   3207  CA  ASP A 385      21.783   7.355 113.143  1.00 47.11           C  
ANISOU 3207  CA  ASP A 385     6750   4015   7135   -335   1506   -495       C  
ATOM   3208  C   ASP A 385      21.323   6.528 114.330  1.00 45.72           C  
ANISOU 3208  C   ASP A 385     6496   3910   6965   -353   1322   -518       C  
ATOM   3209  O   ASP A 385      22.047   5.617 114.748  1.00 52.98           O  
ANISOU 3209  O   ASP A 385     7302   4865   7963   -411   1243   -561       O  
ATOM   3210  CB  ASP A 385      22.770   8.424 113.608  1.00 57.67           C  
ANISOU 3210  CB  ASP A 385     8031   5289   8592   -499   1749   -679       C  
ATOM   3211  CG  ASP A 385      23.575   9.010 112.466  1.00 95.86           C  
ANISOU 3211  CG  ASP A 385    12917  10046  13459   -511   1954   -672       C  
ATOM   3212  OD1 ASP A 385      22.971   9.453 111.466  1.00110.53           O  
ANISOU 3212  OD1 ASP A 385    14917  11856  15223   -400   2006   -543       O  
ATOM   3213  OD2 ASP A 385      24.823   8.957 112.552  1.00100.82           O1-
ANISOU 3213  OD2 ASP A 385    13433  10665  14209   -633   2066   -801       O1-
ATOM   3214  N   GLU A 386      20.133   6.803 114.857  1.00 48.32           N  
ANISOU 3214  N   GLU A 386     6882   4253   7224   -303   1265   -487       N  
ATOM   3215  CA  GLU A 386      19.503   5.924 115.831  1.00 45.70           C  
ANISOU 3215  CA  GLU A 386     6502   3983   6879   -299   1090   -475       C  
ATOM   3216  C   GLU A 386      18.678   4.890 115.073  1.00 41.54           C  
ANISOU 3216  C   GLU A 386     6025   3504   6253   -151    898   -292       C  
ATOM   3217  O   GLU A 386      17.700   5.249 114.399  1.00 37.23           O  
ANISOU 3217  O   GLU A 386     5565   2963   5618    -46    884   -206       O  
ATOM   3218  CB  GLU A 386      18.612   6.717 116.786  1.00 53.13           C  
ANISOU 3218  CB  GLU A 386     7474   4917   7797   -326   1144   -549       C  
ATOM   3219  CG  GLU A 386      19.338   7.736 117.634  1.00 76.10           C  
ANISOU 3219  CG  GLU A 386    10319   7804  10790   -501   1327   -770       C  
ATOM   3220  CD  GLU A 386      18.581   8.074 118.898  1.00 85.21           C  
ANISOU 3220  CD  GLU A 386    11459   8994  11924   -567   1329   -886       C  
ATOM   3221  OE1 GLU A 386      19.231   8.356 119.924  1.00 82.90           O  
ANISOU 3221  OE1 GLU A 386    11048   8766  11684   -756   1385  -1111       O  
ATOM   3222  OE2 GLU A 386      17.336   8.062 118.870  1.00 83.85           O1-
ANISOU 3222  OE2 GLU A 386    11378   8809  11674   -441   1273   -774       O1-
ATOM   3223  N   ILE A 387      19.062   3.621 115.181  1.00 30.12           N  
ANISOU 3223  N   ILE A 387     4514   2095   4833   -154    761   -246       N  
ATOM   3224  CA  ILE A 387      18.365   2.536 114.500  1.00 37.14           C  
ANISOU 3224  CA  ILE A 387     5436   3040   5635    -46    582   -101       C  
ATOM   3225  C   ILE A 387      17.741   1.628 115.571  1.00 39.93           C  
ANISOU 3225  C   ILE A 387     5752   3426   5992    -54    448    -57       C  
ATOM   3226  O   ILE A 387      18.434   1.211 116.506  1.00 32.35           O  
ANISOU 3226  O   ILE A 387     4701   2448   5141   -142    454   -105       O  
ATOM   3227  CB  ILE A 387      19.284   1.752 113.547  1.00 46.87           C  
ANISOU 3227  CB  ILE A 387     6650   4277   6883    -31    554    -65       C  
ATOM   3228  CG1 ILE A 387      19.624   2.635 112.344  1.00 46.23           C  
ANISOU 3228  CG1 ILE A 387     6626   4161   6778    -10    693    -80       C  
ATOM   3229  CG2 ILE A 387      18.604   0.498 113.050  1.00 56.13           C  
ANISOU 3229  CG2 ILE A 387     7840   5509   7977     42    368     44       C  
ATOM   3230  CD1 ILE A 387      20.927   3.322 112.410  1.00 60.00           C  
ANISOU 3230  CD1 ILE A 387     8329   5842   8627   -102    881   -184       C  
ATOM   3231  N   PRO A 388      16.435   1.364 115.495  1.00 36.35           N  
ANISOU 3231  N   PRO A 388     5343   3016   5451     21    344     27       N  
ATOM   3232  CA  PRO A 388      15.819   0.467 116.484  1.00 33.63           C  
ANISOU 3232  CA  PRO A 388     4971   2698   5108     10    237     92       C  
ATOM   3233  C   PRO A 388      15.929  -0.989 116.074  1.00 34.18           C  
ANISOU 3233  C   PRO A 388     5039   2813   5136     39     98    196       C  
ATOM   3234  O   PRO A 388      15.563  -1.346 114.954  1.00 32.09           O  
ANISOU 3234  O   PRO A 388     4806   2583   4805     91     21    228       O  
ATOM   3235  CB  PRO A 388      14.357   0.924 116.516  1.00 35.99           C  
ANISOU 3235  CB  PRO A 388     5315   3021   5337     75    221    122       C  
ATOM   3236  CG  PRO A 388      14.132   1.556 115.159  1.00 29.89           C  
ANISOU 3236  CG  PRO A 388     4580   2258   4518    147    256    122       C  
ATOM   3237  CD  PRO A 388      15.464   1.853 114.506  1.00 32.52           C  
ANISOU 3237  CD  PRO A 388     4914   2556   4888    111    338     69       C  
ATOM   3238  N   TYR A 389      16.439  -1.834 116.965  1.00 30.85           N  
ANISOU 3238  N   TYR A 389     4536   2391   4794      0     80    246       N  
ATOM   3239  CA  TYR A 389      16.555  -3.262 116.709  1.00 27.59           C  
ANISOU 3239  CA  TYR A 389     4109   2031   4342     42      6    347       C  
ATOM   3240  C   TYR A 389      16.449  -3.985 118.043  1.00 27.01           C  
ANISOU 3240  C   TYR A 389     3879   2002   4383     13   -120    469       C  
ATOM   3241  O   TYR A 389      17.078  -3.580 119.027  1.00 24.56           O  
ANISOU 3241  O   TYR A 389     3432   1764   4135    -56   -158    430       O  
ATOM   3242  CB  TYR A 389      17.876  -3.584 115.999  1.00 18.73           C  
ANISOU 3242  CB  TYR A 389     2963    873   3280     45     41    315       C  
ATOM   3243  CG  TYR A 389      18.149  -5.052 115.799  1.00 18.71           C  
ANISOU 3243  CG  TYR A 389     2934    905   3271     91    -10    402       C  
ATOM   3244  CD1 TYR A 389      17.418  -5.801 114.882  1.00 20.46           C  
ANISOU 3244  CD1 TYR A 389     3294   1158   3321    132    -22    408       C  
ATOM   3245  CD2 TYR A 389      19.153  -5.687 116.520  1.00 25.50           C  
ANISOU 3245  CD2 TYR A 389     3620   1750   4320     93    -60    475       C  
ATOM   3246  CE1 TYR A 389      17.683  -7.147 114.694  1.00 18.32           C  
ANISOU 3246  CE1 TYR A 389     3008    895   3056    162    -38    461       C  
ATOM   3247  CE2 TYR A 389      19.427  -7.028 116.339  1.00 23.00           C  
ANISOU 3247  CE2 TYR A 389     3285   1456   3998    150   -101    560       C  
ATOM   3248  CZ  TYR A 389      18.687  -7.753 115.428  1.00 32.95           C  
ANISOU 3248  CZ  TYR A 389     4705   2737   5078    176    -73    537       C  
ATOM   3249  OH  TYR A 389      18.962  -9.087 115.249  1.00 48.79           O  
ANISOU 3249  OH  TYR A 389     6710   4734   7093    218    -89    595       O  
ATOM   3250  N   CYS A 390      15.629  -5.033 118.077  1.00 27.21           N  
ANISOU 3250  N   CYS A 390     3919   2113   4306     50   -187    568       N  
ATOM   3251  CA  CYS A 390      15.438  -5.840 119.281  1.00 40.39           C  
ANISOU 3251  CA  CYS A 390     5479   3864   6004     27   -345    723       C  
ATOM   3252  C   CYS A 390      14.988  -4.989 120.464  1.00 41.67           C  
ANISOU 3252  C   CYS A 390     5571   4179   6083    -42   -388    683       C  
ATOM   3253  O   CYS A 390      15.514  -5.100 121.572  1.00 36.70           O  
ANISOU 3253  O   CYS A 390     4804   3749   5393    -80   -459    693       O  
ATOM   3254  CB  CYS A 390      16.710  -6.611 119.635  1.00 36.51           C  
ANISOU 3254  CB  CYS A 390     4871   3375   5625     48   -415    819       C  
ATOM   3255  SG  CYS A 390      16.727  -8.323 119.099  1.00 60.69           S  
ANISOU 3255  SG  CYS A 390     7971   6471   8617    120   -384    874       S  
ATOM   3256  N   GLY A 391      14.019  -4.117 120.217  1.00 28.25           N  
ANISOU 3256  N   GLY A 391     3959   2442   4333    -45   -321    606       N  
ATOM   3257  CA  GLY A 391      13.486  -3.276 121.268  1.00 23.74           C  
ANISOU 3257  CA  GLY A 391     3332   2041   3647   -103   -315    520       C  
ATOM   3258  C   GLY A 391      14.501  -2.326 121.865  1.00 35.93           C  
ANISOU 3258  C   GLY A 391     4788   3669   5196   -180   -257    354       C  
ATOM   3259  O   GLY A 391      14.228  -1.662 122.870  1.00 43.85           O  
ANISOU 3259  O   GLY A 391     5728   4836   6095   -248   -250    258       O  
ATOM   3260  N   LYS A 392      15.680  -2.259 121.263  1.00 33.22           N  
ANISOU 3260  N   LYS A 392     4431   3223   4970   -182   -207    302       N  
ATOM   3261  CA  LYS A 392      16.692  -1.297 121.661  1.00 34.59           C  
ANISOU 3261  CA  LYS A 392     4515   3456   5172   -278   -127    111       C  
ATOM   3262  C   LYS A 392      16.885  -0.278 120.547  1.00 36.86           C  
ANISOU 3262  C   LYS A 392     4943   3486   5576   -273     69    -10       C  
ATOM   3263  O   LYS A 392      16.438  -0.460 119.417  1.00 40.79           O  
ANISOU 3263  O   LYS A 392     5592   3781   6125   -177    117     75       O  
ATOM   3264  CB  LYS A 392      18.021  -1.987 121.990  1.00 32.55           C  
ANISOU 3264  CB  LYS A 392     4086   3326   4957   -297   -216    134       C  
ATOM   3265  CG  LYS A 392      17.892  -3.177 122.944  1.00 36.94           C  
ANISOU 3265  CG  LYS A 392     4528   4105   5404   -258   -403    315       C  
ATOM   3266  CD  LYS A 392      17.213  -2.788 124.253  1.00 40.89           C  
ANISOU 3266  CD  LYS A 392     4966   4852   5720   -329   -460    273       C  
ATOM   3267  CE  LYS A 392      17.459  -3.833 125.329  1.00 52.25           C  
ANISOU 3267  CE  LYS A 392     6262   6555   7036   -300   -633    437       C  
ATOM   3268  NZ  LYS A 392      16.319  -3.944 126.270  1.00 58.16           N  
ANISOU 3268  NZ  LYS A 392     7031   7460   7608   -321   -685    505       N  
ATOM   3269  N   ILE A 393      17.559   0.809 120.887  1.00 34.44           N  
ANISOU 3269  N   ILE A 393     4590   3194   5302   -383    190   -215       N  
ATOM   3270  CA  ILE A 393      17.857   1.896 119.964  1.00 40.59           C  
ANISOU 3270  CA  ILE A 393     5505   3720   6198   -399    414   -342       C  
ATOM   3271  C   ILE A 393      19.368   2.047 119.986  1.00 48.42           C  
ANISOU 3271  C   ILE A 393     6359   4741   7295   -511    468   -479       C  
ATOM   3272  O   ILE A 393      19.934   2.549 120.966  1.00 55.49           O  
ANISOU 3272  O   ILE A 393     7100   5823   8161   -653    469   -655       O  
ATOM   3273  CB  ILE A 393      17.159   3.205 120.352  1.00 46.59           C  
ANISOU 3273  CB  ILE A 393     6352   4428   6920   -443    564   -487       C  
ATOM   3274  CG1 ILE A 393      15.642   3.003 120.402  1.00 53.77           C  
ANISOU 3274  CG1 ILE A 393     7357   5352   7723   -321    496   -350       C  
ATOM   3275  CG2 ILE A 393      17.548   4.324 119.387  1.00 51.08           C  
ANISOU 3275  CG2 ILE A 393     7051   4794   7564   -429    783   -568       C  
ATOM   3276  CD1 ILE A 393      14.828   4.258 120.161  1.00 55.47           C  
ANISOU 3276  CD1 ILE A 393     7730   5399   7946   -273    687   -429       C  
ATOM   3277  N   PHE A 394      20.024   1.571 118.933  1.00 43.39           N  
ANISOU 3277  N   PHE A 394     5763   3951   6774   -454    508   -410       N  
ATOM   3278  CA  PHE A 394      21.469   1.653 118.816  1.00 46.54           C  
ANISOU 3278  CA  PHE A 394     6020   4371   7293   -548    572   -533       C  
ATOM   3279  C   PHE A 394      21.826   2.952 118.108  1.00 49.10           C  
ANISOU 3279  C   PHE A 394     6458   4538   7660   -600    815   -672       C  
ATOM   3280  O   PHE A 394      21.311   3.236 117.020  1.00 54.24           O  
ANISOU 3280  O   PHE A 394     7275   5144   8190   -454    849   -535       O  
ATOM   3281  CB  PHE A 394      22.014   0.454 118.036  1.00 34.17           C  
ANISOU 3281  CB  PHE A 394     4430   2751   5802   -439    496   -373       C  
ATOM   3282  CG  PHE A 394      21.801  -0.872 118.721  1.00 26.64           C  
ANISOU 3282  CG  PHE A 394     3354   2004   4763   -356    252   -195       C  
ATOM   3283  CD1 PHE A 394      20.589  -1.530 118.614  1.00 27.64           C  
ANISOU 3283  CD1 PHE A 394     3608   2092   4801   -251    156    -18       C  
ATOM   3284  CD2 PHE A 394      22.822  -1.473 119.441  1.00 34.67           C  
ANISOU 3284  CD2 PHE A 394     4126   3253   5792   -378    131   -198       C  
ATOM   3285  CE1 PHE A 394      20.385  -2.743 119.235  1.00 32.56           C  
ANISOU 3285  CE1 PHE A 394     4140   2871   5359   -186    -34    152       C  
ATOM   3286  CE2 PHE A 394      22.623  -2.686 120.067  1.00 30.33           C  
ANISOU 3286  CE2 PHE A 394     3487   2870   5165   -281    -71     -5       C  
ATOM   3287  CZ  PHE A 394      21.404  -3.324 119.963  1.00 24.88           C  
ANISOU 3287  CZ  PHE A 394     2950   2104   4399   -192   -141    171       C  
ATOM   3288  N   ASN A 395      22.690   3.747 118.733  1.00 36.18           N  
ANISOU 3288  N   ASN A 395     4687   2959   6101   -788    926   -916       N  
ATOM   3289  CA  ASN A 395      23.202   4.957 118.105  1.00 46.00           C  
ANISOU 3289  CA  ASN A 395     5994   4150   7333   -810   1138   -999       C  
ATOM   3290  C   ASN A 395      24.459   4.601 117.327  1.00 41.71           C  
ANISOU 3290  C   ASN A 395     5367   3579   6903   -822   1198  -1009       C  
ATOM   3291  O   ASN A 395      25.430   4.098 117.901  1.00 33.72           O  
ANISOU 3291  O   ASN A 395     4128   2655   6029   -958   1149  -1149       O  
ATOM   3292  CB  ASN A 395      23.494   6.051 119.131  1.00 39.42           C  
ANISOU 3292  CB  ASN A 395     5063   3402   6511  -1008   1252  -1266       C  
ATOM   3293  CG  ASN A 395      23.692   7.408 118.484  1.00 50.80           C  
ANISOU 3293  CG  ASN A 395     6614   4743   7945  -1008   1498  -1305       C  
ATOM   3294  OD1 ASN A 395      24.490   7.556 117.553  1.00 50.02           O  
ANISOU 3294  OD1 ASN A 395     6522   4577   7904   -991   1613  -1279       O  
ATOM   3295  ND2 ASN A 395      22.959   8.405 118.965  1.00 75.59           N  
ANISOU 3295  ND2 ASN A 395     9835   7866  11022  -1031   1593  -1365       N  
ATOM   3296  N   LEU A 396      24.441   4.861 116.022  1.00 39.95           N  
ANISOU 3296  N   LEU A 396     5292   3267   6620   -695   1291   -871       N  
ATOM   3297  CA  LEU A 396      25.605   4.516 115.221  1.00 47.65           C  
ANISOU 3297  CA  LEU A 396     6197   4210   7696   -703   1368   -882       C  
ATOM   3298  C   LEU A 396      26.776   5.438 115.507  1.00 54.42           C  
ANISOU 3298  C   LEU A 396     6918   5078   8682   -890   1571  -1127       C  
ATOM   3299  O   LEU A 396      27.921   4.990 115.476  1.00 56.82           O  
ANISOU 3299  O   LEU A 396     7047   5408   9135   -970   1598  -1232       O  
ATOM   3300  CB  LEU A 396      25.268   4.533 113.736  1.00 46.92           C  
ANISOU 3300  CB  LEU A 396     6283   4060   7483   -546   1401   -694       C  
ATOM   3301  CG  LEU A 396      24.284   3.449 113.326  1.00 44.72           C  
ANISOU 3301  CG  LEU A 396     6100   3817   7076   -385   1183   -492       C  
ATOM   3302  CD1 LEU A 396      24.397   3.221 111.833  1.00 36.11           C  
ANISOU 3302  CD1 LEU A 396     5105   2710   5906   -287   1206   -381       C  
ATOM   3303  CD2 LEU A 396      24.489   2.153 114.103  1.00 46.88           C  
ANISOU 3303  CD2 LEU A 396     6246   4121   7443   -390   1025   -475       C  
ATOM   3304  N   THR A 397      26.522   6.708 115.818  1.00 60.16           N  
ANISOU 3304  N   THR A 397     7701   5793   9364   -967   1718  -1232       N  
ATOM   3305  CA  THR A 397      27.627   7.640 116.016  1.00 53.43           C  
ANISOU 3305  CA  THR A 397     6728   4953   8621  -1151   1934  -1474       C  
ATOM   3306  C   THR A 397      28.220   7.515 117.415  1.00 43.76           C  
ANISOU 3306  C   THR A 397     5246   3916   7466  -1355   1847  -1740       C  
ATOM   3307  O   THR A 397      29.439   7.401 117.573  1.00 47.84           O  
ANISOU 3307  O   THR A 397     5547   4531   8100  -1490   1883  -1923       O  
ATOM   3308  CB  THR A 397      27.166   9.077 115.760  1.00 61.60           C  
ANISOU 3308  CB  THR A 397     7922   5893   9592  -1160   2150  -1482       C  
ATOM   3309  OG1 THR A 397      26.488   9.151 114.496  1.00 61.53           O  
ANISOU 3309  OG1 THR A 397     8125   5773   9482   -973   2174  -1230       O  
ATOM   3310  CG2 THR A 397      28.362  10.008 115.737  1.00 39.74           C  
ANISOU 3310  CG2 THR A 397     5051   3108   6942  -1339   2410  -1714       C  
ATOM   3311  N   THR A 398      27.375   7.545 118.443  1.00 54.82           N  
ANISOU 3311  N   THR A 398     6643   5411   8774  -1386   1717  -1773       N  
ATOM   3312  CA  THR A 398      27.846   7.501 119.820  1.00 53.33           C  
ANISOU 3312  CA  THR A 398     6192   5488   8581  -1591   1600  -2025       C  
ATOM   3313  C   THR A 398      28.034   6.085 120.350  1.00 50.66           C  
ANISOU 3313  C   THR A 398     5628   5356   8265  -1599   1308  -1976       C  
ATOM   3314  O   THR A 398      28.690   5.913 121.382  1.00 39.23           O  
ANISOU 3314  O   THR A 398     3877   4244   6784  -1751   1164  -2153       O  
ATOM   3315  CB  THR A 398      26.866   8.242 120.733  1.00 42.41           C  
ANISOU 3315  CB  THR A 398     4891   4155   7069  -1636   1606  -2097       C  
ATOM   3316  OG1 THR A 398      25.681   7.455 120.903  1.00 48.99           O  
ANISOU 3316  OG1 THR A 398     5827   4966   7820  -1504   1418  -1903       O  
ATOM   3317  CG2 THR A 398      26.484   9.582 120.125  1.00 42.96           C  
ANISOU 3317  CG2 THR A 398     5181   4007   7133  -1593   1887  -2075       C  
ATOM   3318  N   ARG A 399      27.467   5.081 119.677  1.00 50.73           N  
ANISOU 3318  N   ARG A 399     5755   5213   8307  -1422   1207  -1719       N  
ATOM   3319  CA  ARG A 399      27.491   3.677 120.082  1.00 54.16           C  
ANISOU 3319  CA  ARG A 399     6017   5874   8687  -1300    913  -1535       C  
ATOM   3320  C   ARG A 399      26.701   3.432 121.358  1.00 57.01           C  
ANISOU 3320  C   ARG A 399     6310   6517   8833  -1281    688  -1489       C  
ATOM   3321  O   ARG A 399      26.952   2.449 122.064  1.00 46.25           O  
ANISOU 3321  O   ARG A 399     4743   5462   7369  -1200    436  -1369       O  
ATOM   3322  CB  ARG A 399      28.925   3.151 120.228  1.00 56.77           C  
ANISOU 3322  CB  ARG A 399     6020   6447   9101  -1346    835  -1610       C  
ATOM   3323  CG  ARG A 399      29.740   3.307 118.964  1.00 61.22           C  
ANISOU 3323  CG  ARG A 399     6636   6745   9879  -1362   1065  -1650       C  
ATOM   3324  CD  ARG A 399      30.787   4.394 119.127  1.00 63.63           C  
ANISOU 3324  CD  ARG A 399     6789   7117  10270  -1602   1261  -1972       C  
ATOM   3325  NE  ARG A 399      31.704   4.420 117.999  1.00 70.18           N  
ANISOU 3325  NE  ARG A 399     7643   7775  11246  -1568   1451  -1973       N  
ATOM   3326  CZ  ARG A 399      32.693   3.552 117.816  1.00 74.42           C  
ANISOU 3326  CZ  ARG A 399     7907   8440  11929  -1560   1377  -1967       C  
ATOM   3327  NH1 ARG A 399      32.906   2.585 118.699  1.00 72.55           N  
ANISOU 3327  NH1 ARG A 399     7390   8564  11610  -1474   1077  -1881       N  
ATOM   3328  NH2 ARG A 399      33.473   3.650 116.747  1.00 73.14           N  
ANISOU 3328  NH2 ARG A 399     7796   8099  11895  -1534   1580  -1981       N  
ATOM   3329  N   GLN A 400      25.734   4.298 121.659  1.00 57.19           N  
ANISOU 3329  N   GLN A 400     6511   6436   8784  -1339    786  -1568       N  
ATOM   3330  CA  GLN A 400      24.886   4.137 122.830  1.00 44.40           C  
ANISOU 3330  CA  GLN A 400     4852   5061   6955  -1325    605  -1532       C  
ATOM   3331  C   GLN A 400      23.647   3.307 122.493  1.00 45.41           C  
ANISOU 3331  C   GLN A 400     5176   5073   7004  -1102    489  -1220       C  
ATOM   3332  O   GLN A 400      23.187   3.255 121.349  1.00 39.41           O  
ANISOU 3332  O   GLN A 400     4639   3997   6337   -985    599  -1090       O  
ATOM   3333  CB  GLN A 400      24.469   5.493 123.406  1.00 42.72           C  
ANISOU 3333  CB  GLN A 400     4712   4811   6707  -1507    781  -1798       C  
ATOM   3334  CG  GLN A 400      25.631   6.403 123.762  1.00 45.69           C  
ANISOU 3334  CG  GLN A 400     4902   5291   7167  -1771    926  -2153       C  
ATOM   3335  CD  GLN A 400      26.542   5.809 124.812  1.00 57.70           C  
ANISOU 3335  CD  GLN A 400     6059   7297   8569  -1850    681  -2234       C  
ATOM   3336  OE1 GLN A 400      26.175   5.708 125.978  1.00 77.80           O  
ANISOU 3336  OE1 GLN A 400     8496  10157  10908  -1884    515  -2270       O  
ATOM   3337  NE2 GLN A 400      27.736   5.407 124.401  1.00 57.10           N  
ANISOU 3337  NE2 GLN A 400     5787   7298   8612  -1868    659  -2256       N  
ATOM   3338  N   VAL A 401      23.112   2.645 123.518  1.00 43.15           N  
ANISOU 3338  N   VAL A 401     4797   5064   6534  -1050    267  -1108       N  
ATOM   3339  CA  VAL A 401      21.955   1.764 123.381  1.00 38.15           C  
ANISOU 3339  CA  VAL A 401     4307   4372   5816   -868    144   -828       C  
ATOM   3340  C   VAL A 401      20.913   2.191 124.404  1.00 44.97           C  
ANISOU 3340  C   VAL A 401     5202   5380   6503   -913    107   -873       C  
ATOM   3341  O   VAL A 401      21.142   2.077 125.615  1.00 48.75           O  
ANISOU 3341  O   VAL A 401     5497   6196   6828   -990    -27   -938       O  
ATOM   3342  CB  VAL A 401      22.316   0.285 123.574  1.00 56.30           C  
ANISOU 3342  CB  VAL A 401     6471   6846   8076   -736    -82   -591       C  
ATOM   3343  CG1 VAL A 401      21.053  -0.575 123.527  1.00 52.19           C  
ANISOU 3343  CG1 VAL A 401     6098   6262   7468   -589   -185   -333       C  
ATOM   3344  CG2 VAL A 401      23.321  -0.161 122.533  1.00 65.23           C  
ANISOU 3344  CG2 VAL A 401     7571   7822   9390   -679    -29   -550       C  
ATOM   3345  N   ARG A 402      19.752   2.600 123.934  1.00 56.13           N  
ANISOU 3345  N   ARG A 402     6841   6560   7927   -854    224   -836       N  
ATOM   3346  CA  ARG A 402      18.653   2.991 124.777  1.00 46.80           C  
ANISOU 3346  CA  ARG A 402     5703   5487   6593   -870    209   -864       C  
ATOM   3347  C   ARG A 402      17.492   2.059 124.635  1.00 48.22           C  
ANISOU 3347  C   ARG A 402     5968   5656   6696   -707     73   -586       C  
ATOM   3348  O   ARG A 402      17.318   1.462 123.624  1.00 59.94           O  
ANISOU 3348  O   ARG A 402     7539   6965   8271   -586     49   -409       O  
ATOM   3349  CB  ARG A 402      18.176   4.354 124.363  1.00 34.47           C  
ANISOU 3349  CB  ARG A 402     4314   3681   5101   -920    462  -1046       C  
ATOM   3350  CG  ARG A 402      19.101   5.449 124.807  1.00 42.13           C  
ANISOU 3350  CG  ARG A 402     5209   4652   6146  -1123    633  -1361       C  
ATOM   3351  CD  ARG A 402      19.189   5.548 126.304  1.00 46.29           C  
ANISOU 3351  CD  ARG A 402     5547   5540   6502  -1284    544  -1549       C  
ATOM   3352  NE  ARG A 402      19.140   6.943 126.626  1.00 63.15           N  
ANISOU 3352  NE  ARG A 402     7792   7583   8619  -1375    745  -1765       N  
ATOM   3353  CZ  ARG A 402      18.041   7.585 126.970  1.00 83.56           C  
ANISOU 3353  CZ  ARG A 402    10473  10184  11093  -1291    734  -1690       C  
ATOM   3354  NH1 ARG A 402      16.900   6.938 127.094  1.00 76.93           N  
ANISOU 3354  NH1 ARG A 402     9628   9457  10146  -1135    532  -1413       N  
ATOM   3355  NH2 ARG A 402      18.092   8.877 127.196  1.00 91.68           N  
ANISOU 3355  NH2 ARG A 402    11600  11106  12126  -1366    944  -1902       N  
ATOM   3356  N   THR A 403      16.667   1.949 125.651  1.00 46.01           N  
ANISOU 3356  N   THR A 403     5661   5572   6250   -718     -5   -562       N  
ATOM   3357  CA  THR A 403      15.500   1.085 125.525  1.00 48.74           C  
ANISOU 3357  CA  THR A 403     6087   5898   6533   -589   -100   -326       C  
ATOM   3358  C   THR A 403      14.497   1.734 124.584  1.00 38.94           C  
ANISOU 3358  C   THR A 403     5043   4381   5372   -505     49   -325       C  
ATOM   3359  O   THR A 403      14.221   2.932 124.688  1.00 34.90           O  
ANISOU 3359  O   THR A 403     4596   3790   4874   -549    212   -502       O  
ATOM   3360  CB  THR A 403      14.858   0.824 126.885  1.00 48.57           C  
ANISOU 3360  CB  THR A 403     5976   6174   6306   -631   -208   -299       C  
ATOM   3361  OG1 THR A 403      15.842   0.306 127.784  1.00 45.32           O  
ANISOU 3361  OG1 THR A 403     5377   6048   5793   -694   -349   -297       O  
ATOM   3362  CG2 THR A 403      13.721  -0.181 126.748  1.00 24.52           C  
ANISOU 3362  CG2 THR A 403     2996   3108   3211   -520   -298    -52       C  
ATOM   3363  N   LEU A 404      13.968   0.955 123.650  1.00 31.61           N  
ANISOU 3363  N   LEU A 404     4209   3308   4496   -379      2   -131       N  
ATOM   3364  CA  LEU A 404      12.941   1.469 122.758  1.00 35.66           C  
ANISOU 3364  CA  LEU A 404     4886   3612   5051   -274    110   -105       C  
ATOM   3365  C   LEU A 404      11.566   1.240 123.369  1.00 28.52           C  
ANISOU 3365  C   LEU A 404     3971   2842   4022   -236     49    -29       C  
ATOM   3366  O   LEU A 404      11.244   0.132 123.805  1.00 35.51           O  
ANISOU 3366  O   LEU A 404     4785   3875   4833   -237   -100    117       O  
ATOM   3367  CB  LEU A 404      13.038   0.807 121.386  1.00 32.17           C  
ANISOU 3367  CB  LEU A 404     4543   2971   4708   -168     95     35       C  
ATOM   3368  CG  LEU A 404      11.791   0.846 120.502  1.00 39.43           C  
ANISOU 3368  CG  LEU A 404     5595   3767   5619    -35    121    130       C  
ATOM   3369  CD1 LEU A 404      11.483   2.259 120.005  1.00 55.30           C  
ANISOU 3369  CD1 LEU A 404     7737   5607   7670     25    318     21       C  
ATOM   3370  CD2 LEU A 404      11.989  -0.099 119.334  1.00 51.70           C  
ANISOU 3370  CD2 LEU A 404     7213   5196   7236     36     64    262       C  
ATOM   3371  N   TYR A 405      10.759   2.293 123.400  1.00 35.47           N  
ANISOU 3371  N   TYR A 405     4924   3661   4890   -200    181   -126       N  
ATOM   3372  CA  TYR A 405       9.419   2.245 123.970  1.00 39.41           C  
ANISOU 3372  CA  TYR A 405     5402   4289   5283   -161    154    -81       C  
ATOM   3373  C   TYR A 405       8.406   2.509 122.868  1.00 35.72           C  
ANISOU 3373  C   TYR A 405     5052   3655   4866      1    214     -5       C  
ATOM   3374  O   TYR A 405       8.467   3.549 122.208  1.00 43.24           O  
ANISOU 3374  O   TYR A 405     6120   4412   5897     75    373    -82       O  
ATOM   3375  CB  TYR A 405       9.278   3.257 125.108  1.00 40.63           C  
ANISOU 3375  CB  TYR A 405     5515   4560   5363   -247    259   -273       C  
ATOM   3376  CG  TYR A 405      10.069   2.888 126.344  1.00 37.55           C  
ANISOU 3376  CG  TYR A 405     4981   4424   4863   -403    163   -338       C  
ATOM   3377  CD1 TYR A 405       9.550   2.003 127.283  1.00 31.93           C  
ANISOU 3377  CD1 TYR A 405     4169   3964   3999   -434     24   -226       C  
ATOM   3378  CD2 TYR A 405      11.335   3.418 126.568  1.00 27.67           C  
ANISOU 3378  CD2 TYR A 405     3687   3176   3649   -518    214   -508       C  
ATOM   3379  CE1 TYR A 405      10.270   1.661 128.416  1.00 44.61           C  
ANISOU 3379  CE1 TYR A 405     5647   5829   5474   -553    -71   -262       C  
ATOM   3380  CE2 TYR A 405      12.061   3.081 127.695  1.00 30.99           C  
ANISOU 3380  CE2 TYR A 405     3954   3876   3945   -648    106   -568       C  
ATOM   3381  CZ  TYR A 405      11.520   2.207 128.615  1.00 44.90           C  
ANISOU 3381  CZ  TYR A 405     5629   5895   5537   -653    -41   -434       C  
ATOM   3382  OH  TYR A 405      12.232   1.866 129.741  1.00 49.18           O  
ANISOU 3382  OH  TYR A 405     6023   6741   5924   -759   -156   -470       O  
ATOM   3383  N   LYS A 406       7.492   1.559 122.662  1.00 62.52           N  
ANISOU 3383  N   LYS A 406     8413   7131   8212     55     91    148       N  
ATOM   3384  CA  LYS A 406       6.437   1.691 121.655  1.00 71.98           C  
ANISOU 3384  CA  LYS A 406     9683   8241   9427    208    112    222       C  
ATOM   3385  C   LYS A 406       5.260   2.427 122.276  1.00 55.07           C  
ANISOU 3385  C   LYS A 406     7504   6201   7220    264    185    166       C  
ATOM   3386  O   LYS A 406       4.389   1.830 122.909  1.00 62.07           O  
ANISOU 3386  O   LYS A 406     8285   7274   8023    232    103    217       O  
ATOM   3387  CB  LYS A 406       6.019   0.323 121.130  1.00 87.82           C  
ANISOU 3387  CB  LYS A 406    11653  10297  11417    213    -44    376       C  
ATOM   3388  CG  LYS A 406       7.114  -0.724 121.186  1.00 95.44           C  
ANISOU 3388  CG  LYS A 406    12594  11251  12418    113   -139    437       C  
ATOM   3389  CD  LYS A 406       7.531  -1.152 119.796  1.00105.93           C  
ANISOU 3389  CD  LYS A 406    14020  12400  13830    179   -151    496       C  
ATOM   3390  CE  LYS A 406       8.885  -1.773 119.872  1.00109.54           C  
ANISOU 3390  CE  LYS A 406    14462  12807  14352    102   -187    513       C  
ATOM   3391  NZ  LYS A 406       9.397  -2.287 118.587  1.00103.62           N  
ANISOU 3391  NZ  LYS A 406    13802  11883  13684    152   -188    562       N  
ATOM   3392  N   LEU A 407       5.219   3.740 122.067  1.00 37.84           N  
ANISOU 3392  N   LEU A 407     5414   3878   5086    353    361     62       N  
ATOM   3393  CA  LEU A 407       4.166   4.589 122.615  1.00 33.35           C  
ANISOU 3393  CA  LEU A 407     4823   3370   4479    432    468     -5       C  
ATOM   3394  C   LEU A 407       3.716   5.584 121.555  1.00 35.49           C  
ANISOU 3394  C   LEU A 407     5226   3439   4820    648    610     15       C  
ATOM   3395  O   LEU A 407       4.207   6.719 121.509  1.00 49.10           O  
ANISOU 3395  O   LEU A 407     7066   4972   6619    677    805    -94       O  
ATOM   3396  CB  LEU A 407       4.651   5.309 123.868  1.00 40.59           C  
ANISOU 3396  CB  LEU A 407     5711   4339   5371    295    579   -191       C  
ATOM   3397  CG  LEU A 407       4.815   4.487 125.143  1.00 43.91           C  
ANISOU 3397  CG  LEU A 407     5989   5024   5672    114    452   -206       C  
ATOM   3398  CD1 LEU A 407       5.259   5.387 126.279  1.00 49.76           C  
ANISOU 3398  CD1 LEU A 407     6713   5825   6371     -9    580   -422       C  
ATOM   3399  CD2 LEU A 407       3.527   3.771 125.493  1.00 35.90           C  
ANISOU 3399  CD2 LEU A 407     4870   4206   4566    149    356    -96       C  
ATOM   3400  N   PRO A 408       2.769   5.199 120.704  1.00 32.50           N  
ANISOU 3400  N   PRO A 408     4832   3103   4412    805    526    151       N  
ATOM   3401  CA  PRO A 408       2.296   6.090 119.635  1.00 32.94           C  
ANISOU 3401  CA  PRO A 408     5010   3000   4507   1049    642    207       C  
ATOM   3402  C   PRO A 408       1.686   7.367 120.185  1.00 52.01           C  
ANISOU 3402  C   PRO A 408     7453   5363   6947   1167    842    118       C  
ATOM   3403  O   PRO A 408       1.489   7.503 121.403  1.00 59.88           O  
ANISOU 3403  O   PRO A 408     8356   6479   7917   1052    877      1       O  
ATOM   3404  CB  PRO A 408       1.235   5.236 118.927  1.00 24.48           C  
ANISOU 3404  CB  PRO A 408     3843   2100   3358   1156    465    347       C  
ATOM   3405  CG  PRO A 408       1.708   3.852 119.110  1.00 44.45           C  
ANISOU 3405  CG  PRO A 408     6292   4737   5862    953    285    376       C  
ATOM   3406  CD  PRO A 408       2.349   3.806 120.481  1.00 31.14           C  
ANISOU 3406  CD  PRO A 408     4550   3102   4179    751    313    269       C  
ATOM   3407  N   PRO A 409       1.387   8.337 119.318  1.00 71.03           N  
ANISOU 3407  N   PRO A 409     9998   7588   9404   1406    990    173       N  
ATOM   3408  CA  PRO A 409       0.661   9.534 119.767  1.00 80.26           C  
ANISOU 3408  CA  PRO A 409    11168   8733  10594   1520   1164    108       C  
ATOM   3409  C   PRO A 409      -0.703   9.192 120.351  1.00 74.09           C  
ANISOU 3409  C   PRO A 409    10215   8190   9744   1630   1098    131       C  
ATOM   3410  O   PRO A 409      -1.503   8.485 119.734  1.00 64.82           O  
ANISOU 3410  O   PRO A 409     8935   7195   8499   1733    924    263       O  
ATOM   3411  CB  PRO A 409       0.531  10.373 118.487  1.00 79.45           C  
ANISOU 3411  CB  PRO A 409    11134   8574  10479   1620   1180    218       C  
ATOM   3412  CG  PRO A 409       0.923   9.459 117.350  1.00 68.91           C  
ANISOU 3412  CG  PRO A 409     9800   7294   9089   1587   1001    331       C  
ATOM   3413  CD  PRO A 409       1.888   8.488 117.941  1.00 66.46           C  
ANISOU 3413  CD  PRO A 409     9477   6966   8808   1389    930    262       C  
ATOM   3414  N   ASN A 410      -0.963   9.718 121.551  1.00 83.38           N  
ANISOU 3414  N   ASN A 410    11337   9414  10930   1559   1222    -18       N  
ATOM   3415  CA  ASN A 410      -2.255   9.581 122.225  1.00 89.52           C  
ANISOU 3415  CA  ASN A 410    11930  10441  11643   1623   1187    -24       C  
ATOM   3416  C   ASN A 410      -2.587   8.122 122.530  1.00 77.07           C  
ANISOU 3416  C   ASN A 410    10160   9161   9960   1450    929     34       C  
ATOM   3417  O   ASN A 410      -3.753   7.716 122.509  1.00 64.82           O  
ANISOU 3417  O   ASN A 410     8445   7830   8355   1539    839     99       O  
ATOM   3418  CB  ASN A 410      -3.375  10.240 121.415  1.00 88.59           C  
ANISOU 3418  CB  ASN A 410    11810  10307  11545   1973   1253     95       C  
ATOM   3419  CG  ASN A 410      -3.109  11.712 121.160  1.00 89.95           C  
ANISOU 3419  CG  ASN A 410    12160  10207  11811   2072   1480     57       C  
ATOM   3420  OD1 ASN A 410      -3.537  12.573 121.929  1.00 98.55           O  
ANISOU 3420  OD1 ASN A 410    13238  11267  12940   2098   1647    -54       O  
ATOM   3421  ND2 ASN A 410      -2.393  12.008 120.081  1.00 84.52           N  
ANISOU 3421  ND2 ASN A 410    11605   9373  11136   2034   1443    146       N  
ATOM   3422  N   TYR A 411      -1.560   7.325 122.810  1.00 69.26           N  
ANISOU 3422  N   TYR A 411     9187   8179   8951   1205    822     11       N  
ATOM   3423  CA  TYR A 411      -1.745   5.959 123.275  1.00 54.78           C  
ANISOU 3423  CA  TYR A 411     7198   6586   7029   1019    618     61       C  
ATOM   3424  C   TYR A 411      -1.987   5.969 124.779  1.00 43.67           C  
ANISOU 3424  C   TYR A 411     5688   5353   5553    864    670    -56       C  
ATOM   3425  O   TYR A 411      -1.207   6.556 125.537  1.00 42.92           O  
ANISOU 3425  O   TYR A 411     5663   5185   5462    754    785   -196       O  
ATOM   3426  CB  TYR A 411      -0.515   5.116 122.935  1.00 53.53           C  
ANISOU 3426  CB  TYR A 411     7107   6349   6882    855    496    105       C  
ATOM   3427  CG  TYR A 411      -0.525   3.717 123.503  1.00 48.21           C  
ANISOU 3427  CG  TYR A 411     6308   5876   6134    658    319    163       C  
ATOM   3428  CD1 TYR A 411      -1.233   2.696 122.882  1.00 49.99           C  
ANISOU 3428  CD1 TYR A 411     6445   6214   6335    672    169    283       C  
ATOM   3429  CD2 TYR A 411       0.194   3.415 124.652  1.00 50.27           C  
ANISOU 3429  CD2 TYR A 411     6543   6213   6344    456    311     98       C  
ATOM   3430  CE1 TYR A 411      -1.234   1.417 123.399  1.00 40.09           C  
ANISOU 3430  CE1 TYR A 411     5098   5102   5031    487     42    342       C  
ATOM   3431  CE2 TYR A 411       0.197   2.144 125.180  1.00 35.60           C  
ANISOU 3431  CE2 TYR A 411     4591   4519   4417    299    169    181       C  
ATOM   3432  CZ  TYR A 411      -0.516   1.147 124.548  1.00 27.90           C  
ANISOU 3432  CZ  TYR A 411     3548   3610   3441    314     47    306       C  
ATOM   3433  OH  TYR A 411      -0.511  -0.121 125.076  1.00 44.03           O  
ANISOU 3433  OH  TYR A 411     5518   5778   5433    154    -61    394       O  
ATOM   3434  N   GLU A 412      -3.068   5.325 125.208  1.00 45.30           N  
ANISOU 3434  N   GLU A 412     5723   5802   5686    845    593    -12       N  
ATOM   3435  CA  GLU A 412      -3.416   5.274 126.624  1.00 51.98           C  
ANISOU 3435  CA  GLU A 412     6467   6839   6445    704    647   -108       C  
ATOM   3436  C   GLU A 412      -2.505   4.267 127.318  1.00 44.77           C  
ANISOU 3436  C   GLU A 412     5548   6010   5452    450    527    -88       C  
ATOM   3437  O   GLU A 412      -2.648   3.055 127.123  1.00 46.38           O  
ANISOU 3437  O   GLU A 412     5683   6313   5626    366    370     42       O  
ATOM   3438  CB  GLU A 412      -4.886   4.906 126.803  1.00 47.87           C  
ANISOU 3438  CB  GLU A 412     5759   6550   5881    766    621    -62       C  
ATOM   3439  CG  GLU A 412      -5.865   5.930 126.248  1.00 51.26           C  
ANISOU 3439  CG  GLU A 412     6160   6941   6376   1047    742    -77       C  
ATOM   3440  CD  GLU A 412      -7.309   5.507 126.411  1.00 66.83           C  
ANISOU 3440  CD  GLU A 412     7907   9178   8308   1101    704    -40       C  
ATOM   3441  OE1 GLU A 412      -7.831   5.578 127.541  1.00 67.04           O  
ANISOU 3441  OE1 GLU A 412     7832   9365   8275   1016    795   -126       O  
ATOM   3442  OE2 GLU A 412      -7.920   5.101 125.404  1.00 71.75           O1-
ANISOU 3442  OE2 GLU A 412     8446   9865   8951   1220    585     66       O1-
ATOM   3443  N   ILE A 413      -1.584   4.767 128.149  1.00 33.72           N  
ANISOU 3443  N   ILE A 413     4216   4578   4017    331    608   -220       N  
ATOM   3444  CA  ILE A 413      -0.519   3.933 128.705  1.00 42.08           C  
ANISOU 3444  CA  ILE A 413     5279   5707   5002    128    489   -192       C  
ATOM   3445  C   ILE A 413      -1.082   2.761 129.503  1.00 51.26           C  
ANISOU 3445  C   ILE A 413     6314   7123   6039      2    382    -86       C  
ATOM   3446  O   ILE A 413      -0.469   1.686 129.561  1.00 39.99           O  
ANISOU 3446  O   ILE A 413     4882   5736   4576   -110    243     35       O  
ATOM   3447  CB  ILE A 413       0.432   4.804 129.554  1.00 36.99           C  
ANISOU 3447  CB  ILE A 413     4694   5042   4318     22    604   -389       C  
ATOM   3448  CG1 ILE A 413       1.592   3.973 130.109  1.00 43.23           C  
ANISOU 3448  CG1 ILE A 413     5465   5938   5020   -162    465   -354       C  
ATOM   3449  CG2 ILE A 413      -0.335   5.520 130.668  1.00 38.69           C  
ANISOU 3449  CG2 ILE A 413     4854   5405   4442      3    757   -543       C  
ATOM   3450  CD1 ILE A 413       2.654   3.642 129.079  1.00 46.63           C  
ANISOU 3450  CD1 ILE A 413     5973   6177   5565   -146    377   -278       C  
ATOM   3451  N   ARG A 414      -2.265   2.930 130.097  1.00 68.22           N  
ANISOU 3451  N   ARG A 414     8361   9433   8127     25    460   -118       N  
ATOM   3452  CA  ARG A 414      -2.899   1.865 130.867  1.00 63.25           C  
ANISOU 3452  CA  ARG A 414     7615   9036   7382   -100    395    -18       C  
ATOM   3453  C   ARG A 414      -3.066   0.579 130.069  1.00 56.49           C  
ANISOU 3453  C   ARG A 414     6727   8156   6578   -125    241    172       C  
ATOM   3454  O   ARG A 414      -3.323  -0.474 130.665  1.00 43.05           O  
ANISOU 3454  O   ARG A 414     4963   6600   4795   -258    186    280       O  
ATOM   3455  CB  ARG A 414      -4.266   2.333 131.372  1.00 53.01           C  
ANISOU 3455  CB  ARG A 414     6202   7892   6049    -41    524    -89       C  
ATOM   3456  CG  ARG A 414      -5.223   2.707 130.261  1.00 40.22           C  
ANISOU 3456  CG  ARG A 414     4530   6193   4559    161    544    -69       C  
ATOM   3457  CD  ARG A 414      -6.554   3.175 130.804  1.00 33.63           C  
ANISOU 3457  CD  ARG A 414     3555   5529   3695    233    676   -143       C  
ATOM   3458  NE  ARG A 414      -7.499   3.443 129.725  1.00 33.97           N  
ANISOU 3458  NE  ARG A 414     3515   5542   3848    444    669   -104       N  
ATOM   3459  CZ  ARG A 414      -8.218   2.511 129.106  1.00 39.15           C  
ANISOU 3459  CZ  ARG A 414     4044   6303   4526    434    545     10       C  
ATOM   3460  NH1 ARG A 414      -8.112   1.237 129.462  1.00 37.91           N  
ANISOU 3460  NH1 ARG A 414     3847   6247   4309    218    443    103       N  
ATOM   3461  NH2 ARG A 414      -9.050   2.855 128.131  1.00 34.41           N  
ANISOU 3461  NH2 ARG A 414     3356   5713   4005    641    531     30       N  
ATOM   3462  N   HIS A 415      -2.929   0.638 128.743  1.00 51.15           N  
ANISOU 3462  N   HIS A 415     6106   7297   6033     -4    186    212       N  
ATOM   3463  CA  HIS A 415      -3.101  -0.536 127.900  1.00 36.84           C  
ANISOU 3463  CA  HIS A 415     4270   5454   4275    -33     52    357       C  
ATOM   3464  C   HIS A 415      -1.881  -1.448 127.891  1.00 37.15           C  
ANISOU 3464  C   HIS A 415     4395   5406   4315   -150    -53    455       C  
ATOM   3465  O   HIS A 415      -1.960  -2.546 127.330  1.00 30.45           O  
ANISOU 3465  O   HIS A 415     3538   4522   3511   -201   -147    573       O  
ATOM   3466  CB  HIS A 415      -3.433  -0.114 126.465  1.00 40.30           C  
ANISOU 3466  CB  HIS A 415     4732   5757   4822    147     31    355       C  
ATOM   3467  CG  HIS A 415      -4.876   0.233 126.254  1.00 52.20           C  
ANISOU 3467  CG  HIS A 415     6100   7401   6333    264     75    326       C  
ATOM   3468  ND1 HIS A 415      -5.882  -0.238 127.071  1.00 57.51           N  
ANISOU 3468  ND1 HIS A 415     6616   8295   6940    168    101    329       N  
ATOM   3469  CD2 HIS A 415      -5.481   1.003 125.318  1.00 57.63           C  
ANISOU 3469  CD2 HIS A 415     6771   8050   7077    479    101    302       C  
ATOM   3470  CE1 HIS A 415      -7.044   0.230 126.648  1.00 60.56           C  
ANISOU 3470  CE1 HIS A 415     6876   8783   7352    315    136    292       C  
ATOM   3471  NE2 HIS A 415      -6.829   0.984 125.586  1.00 60.65           N  
ANISOU 3471  NE2 HIS A 415     6968   8645   7431    517    130    283       N  
ATOM   3472  N   LYS A 416      -0.759  -1.036 128.485  1.00 44.37           N  
ANISOU 3472  N   LYS A 416     5382   6290   5187   -193    -35    401       N  
ATOM   3473  CA  LYS A 416       0.408  -1.909 128.535  1.00 45.66           C  
ANISOU 3473  CA  LYS A 416     5600   6399   5349   -281   -137    504       C  
ATOM   3474  C   LYS A 416       0.398  -2.855 129.729  1.00 45.07           C  
ANISOU 3474  C   LYS A 416     5471   6512   5140   -421   -173    613       C  
ATOM   3475  O   LYS A 416       1.144  -3.843 129.725  1.00 52.64           O  
ANISOU 3475  O   LYS A 416     6463   7432   6105   -475   -262    749       O  
ATOM   3476  CB  LYS A 416       1.698  -1.076 128.565  1.00 48.98           C  
ANISOU 3476  CB  LYS A 416     6099   6724   5787   -266   -113    394       C  
ATOM   3477  CG  LYS A 416       2.112  -0.542 127.202  1.00 55.09           C  
ANISOU 3477  CG  LYS A 416     6967   7254   6710   -146    -98    356       C  
ATOM   3478  CD  LYS A 416       3.353  -1.231 126.667  1.00 60.42           C  
ANISOU 3478  CD  LYS A 416     7701   7804   7452   -177   -190    435       C  
ATOM   3479  CE  LYS A 416       3.527  -0.946 125.189  1.00 67.68           C  
ANISOU 3479  CE  LYS A 416     8714   8495   8506    -59   -177    432       C  
ATOM   3480  NZ  LYS A 416       4.859  -1.386 124.694  1.00 66.75           N  
ANISOU 3480  NZ  LYS A 416     8655   8245   8462    -85   -231    471       N  
ATOM   3481  N   PHE A 417      -0.428  -2.590 130.735  1.00 42.09           N  
ANISOU 3481  N   PHE A 417     5018   6332   4641   -468    -94    567       N  
ATOM   3482  CA  PHE A 417      -0.327  -3.242 132.032  1.00 46.89           C  
ANISOU 3482  CA  PHE A 417     5593   7142   5080   -592   -102    655       C  
ATOM   3483  C   PHE A 417      -1.553  -4.102 132.308  1.00 50.80           C  
ANISOU 3483  C   PHE A 417     6013   7743   5546   -661    -69    767       C  
ATOM   3484  O   PHE A 417      -2.689  -3.619 132.241  1.00 60.64           O  
ANISOU 3484  O   PHE A 417     7180   9052   6809   -631     17    679       O  
ATOM   3485  CB  PHE A 417      -0.130  -2.188 133.119  1.00 53.00           C  
ANISOU 3485  CB  PHE A 417     6349   8082   5705   -617    -17    486       C  
ATOM   3486  CG  PHE A 417       0.923  -1.172 132.771  1.00 58.38           C  
ANISOU 3486  CG  PHE A 417     7094   8644   6444   -566    -10    326       C  
ATOM   3487  CD1 PHE A 417       2.212  -1.580 132.463  1.00 53.11           C  
ANISOU 3487  CD1 PHE A 417     6474   7893   5814   -578   -119    389       C  
ATOM   3488  CD2 PHE A 417       0.620   0.179 132.713  1.00 56.60           C  
ANISOU 3488  CD2 PHE A 417     6879   8374   6254   -504    122    113       C  
ATOM   3489  CE1 PHE A 417       3.188  -0.660 132.128  1.00 49.37           C  
ANISOU 3489  CE1 PHE A 417     6046   7310   5404   -553    -96    230       C  
ATOM   3490  CE2 PHE A 417       1.596   1.106 132.378  1.00 62.15           C  
ANISOU 3490  CE2 PHE A 417     7650   8938   7025   -478    158    -40       C  
ATOM   3491  CZ  PHE A 417       2.878   0.684 132.089  1.00 54.56           C  
ANISOU 3491  CZ  PHE A 417     6725   7910   6095   -514     48     13       C  
ATOM   3492  N   LYS A 418      -1.307  -5.374 132.630  1.00 41.19           N  
ANISOU 3492  N   LYS A 418     4818   6541   4292   -751   -124    963       N  
ATOM   3493  CA  LYS A 418      -2.357  -6.365 132.864  1.00 31.95           C  
ANISOU 3493  CA  LYS A 418     3593   5435   3113   -850    -76   1087       C  
ATOM   3494  C   LYS A 418      -2.610  -6.451 134.367  1.00 39.39           C  
ANISOU 3494  C   LYS A 418     4505   6623   3838   -941      1   1134       C  
ATOM   3495  O   LYS A 418      -2.140  -7.356 135.056  1.00 56.09           O  
ANISOU 3495  O   LYS A 418     6671   8790   5851  -1008    -21   1318       O  
ATOM   3496  CB  LYS A 418      -1.950  -7.718 132.286  1.00 31.28           C  
ANISOU 3496  CB  LYS A 418     3575   5177   3131   -894   -147   1277       C  
ATOM   3497  CG  LYS A 418      -3.100  -8.671 132.004  1.00 41.14           C  
ANISOU 3497  CG  LYS A 418     4770   6406   4456  -1000    -89   1351       C  
ATOM   3498  CD  LYS A 418      -2.585 -10.091 131.811  1.00 51.52           C  
ANISOU 3498  CD  LYS A 418     6178   7555   5842  -1069   -118   1557       C  
ATOM   3499  CE  LYS A 418      -3.227 -11.053 132.787  1.00 52.24           C  
ANISOU 3499  CE  LYS A 418     6261   7741   5846  -1213     -9   1719       C  
ATOM   3500  NZ  LYS A 418      -3.010 -12.481 132.441  1.00 54.57           N  
ANISOU 3500  NZ  LYS A 418     6649   7828   6257  -1291      7   1906       N  
ATOM   3501  N   LEU A 419      -3.383  -5.490 134.875  1.00 40.83           N  
ANISOU 3501  N   LEU A 419     4608   6962   3943   -931    105    970       N  
ATOM   3502  CA  LEU A 419      -3.566  -5.381 136.320  1.00 43.10           C  
ANISOU 3502  CA  LEU A 419     4873   7504   3999  -1012    190    974       C  
ATOM   3503  C   LEU A 419      -4.296  -6.591 136.893  1.00 51.03           C  
ANISOU 3503  C   LEU A 419     5855   8596   4937  -1140    253   1172       C  
ATOM   3504  O   LEU A 419      -4.015  -7.005 138.023  1.00 49.97           O  
ANISOU 3504  O   LEU A 419     5758   8629   4598  -1210    279   1291       O  
ATOM   3505  CB  LEU A 419      -4.314  -4.089 136.658  1.00 47.27           C  
ANISOU 3505  CB  LEU A 419     5322   8155   4485   -970    313    739       C  
ATOM   3506  CG  LEU A 419      -3.812  -2.781 136.031  1.00 55.70           C  
ANISOU 3506  CG  LEU A 419     6418   9097   5648   -841    305    528       C  
ATOM   3507  CD1 LEU A 419      -4.296  -1.570 136.816  1.00 55.57           C  
ANISOU 3507  CD1 LEU A 419     6356   9231   5527   -823    456    309       C  
ATOM   3508  CD2 LEU A 419      -2.293  -2.751 135.931  1.00 66.53           C  
ANISOU 3508  CD2 LEU A 419     7891  10384   7004   -830    187    544       C  
ATOM   3509  N   TRP A 420      -5.202  -7.191 136.127  1.00 63.78           N  
ANISOU 3509  N   TRP A 420     7411  10105   6716  -1177    282   1211       N  
ATOM   3510  CA  TRP A 420      -6.041  -8.279 136.605  1.00 64.06           C  
ANISOU 3510  CA  TRP A 420     7414  10204   6720  -1323    381   1365       C  
ATOM   3511  C   TRP A 420      -5.639  -9.601 135.966  1.00 77.91           C  
ANISOU 3511  C   TRP A 420     9256  11740   8607  -1376    321   1565       C  
ATOM   3512  O   TRP A 420      -5.201  -9.645 134.815  1.00 95.58           O  
ANISOU 3512  O   TRP A 420    11524  13774  11017  -1307    217   1531       O  
ATOM   3513  CB  TRP A 420      -7.517  -8.007 136.298  1.00 60.21           C  
ANISOU 3513  CB  TRP A 420     6762   9794   6322  -1359    490   1232       C  
ATOM   3514  CG  TRP A 420      -7.930  -6.587 136.513  1.00 58.44           C  
ANISOU 3514  CG  TRP A 420     6448   9709   6048  -1253    545   1005       C  
ATOM   3515  CD1 TRP A 420      -7.700  -5.528 135.683  1.00 58.01           C  
ANISOU 3515  CD1 TRP A 420     6383   9558   6099  -1092    483    838       C  
ATOM   3516  CD2 TRP A 420      -8.664  -6.071 137.627  1.00 58.51           C  
ANISOU 3516  CD2 TRP A 420     6376   9961   5895  -1296    699    922       C  
ATOM   3517  NE1 TRP A 420      -8.239  -4.383 136.216  1.00 48.18           N  
ANISOU 3517  NE1 TRP A 420     5062   8463   4783  -1025    595    659       N  
ATOM   3518  CE2 TRP A 420      -8.837  -4.691 137.411  1.00 57.32           C  
ANISOU 3518  CE2 TRP A 420     6168   9835   5774  -1150    726    696       C  
ATOM   3519  CE3 TRP A 420      -9.191  -6.643 138.789  1.00 54.51           C  
ANISOU 3519  CE3 TRP A 420     5848   9644   5219  -1442    834   1020       C  
ATOM   3520  CZ2 TRP A 420      -9.513  -3.874 138.314  1.00 46.33           C  
ANISOU 3520  CZ2 TRP A 420     4696   8649   4259  -1144    883    550       C  
ATOM   3521  CZ3 TRP A 420      -9.860  -5.832 139.684  1.00 52.42           C  
ANISOU 3521  CZ3 TRP A 420     5498   9604   4815  -1443    982    876       C  
ATOM   3522  CH2 TRP A 420     -10.016  -4.462 139.442  1.00 49.88           C  
ANISOU 3522  CH2 TRP A 420     5115   9299   4536  -1295   1006    635       C  
ATOM   3523  N   ASN A 421      -5.806 -10.682 136.724  1.00 88.25           N  
ANISOU 3523  N   ASN A 421    10616  13082   9834  -1500    407   1775       N  
ATOM   3524  CA  ASN A 421      -5.679 -12.032 136.189  1.00 86.61           C  
ANISOU 3524  CA  ASN A 421    10489  12647   9771  -1577    409   1961       C  
ATOM   3525  C   ASN A 421      -6.790 -12.893 136.766  1.00 71.93           C  
ANISOU 3525  C   ASN A 421     8591  10848   7893  -1762    593   2064       C  
ATOM   3526  O   ASN A 421      -6.956 -12.961 137.986  1.00 76.26           O  
ANISOU 3526  O   ASN A 421     9158  11582   8235  -1813    696   2168       O  
ATOM   3527  CB  ASN A 421      -4.313 -12.651 136.508  1.00 90.89           C  
ANISOU 3527  CB  ASN A 421    11193  13091  10248  -1508    326   2182       C  
ATOM   3528  CG  ASN A 421      -4.207 -14.091 136.038  1.00 91.01           C  
ANISOU 3528  CG  ASN A 421    11312  12847  10422  -1582    368   2388       C  
ATOM   3529  OD1 ASN A 421      -4.734 -14.454 134.985  1.00 89.05           O  
ANISOU 3529  OD1 ASN A 421    11029  12422  10386  -1648    381   2302       O  
ATOM   3530  ND2 ASN A 421      -3.526 -14.920 136.819  1.00 90.69           N  
ANISOU 3530  ND2 ASN A 421    11402  12747  10309  -1520    382   2578       N  
ATOM   3531  N   PHE A 422      -7.541 -13.551 135.881  1.00 71.92           N  
ANISOU 3531  N   PHE A 422     8531  10697   8097  -1874    639   2026       N  
ATOM   3532  CA  PHE A 422      -8.706 -14.321 136.307  1.00 72.85           C  
ANISOU 3532  CA  PHE A 422     8582  10865   8232  -2080    833   2078       C  
ATOM   3533  C   PHE A 422      -8.307 -15.537 137.138  1.00 75.75           C  
ANISOU 3533  C   PHE A 422     9135  11096   8550  -2123    932   2330       C  
ATOM   3534  O   PHE A 422      -9.026 -15.921 138.068  1.00 87.13           O  
ANISOU 3534  O   PHE A 422    10574  12620   9912  -2209   1095   2373       O  
ATOM   3535  CB  PHE A 422      -9.512 -14.750 135.079  1.00 65.39           C  
ANISOU 3535  CB  PHE A 422     7525   9790   7532  -2190    839   1937       C  
ATOM   3536  CG  PHE A 422     -10.980 -14.912 135.340  1.00 73.00           C  
ANISOU 3536  CG  PHE A 422     8302  10916   8519  -2376   1009   1840       C  
ATOM   3537  CD1 PHE A 422     -11.820 -13.810 135.355  1.00 63.54           C  
ANISOU 3537  CD1 PHE A 422     6896   9969   7279  -2317   1006   1623       C  
ATOM   3538  CD2 PHE A 422     -11.527 -16.168 135.547  1.00 84.47           C  
ANISOU 3538  CD2 PHE A 422     9799  12232  10064  -2565   1173   1928       C  
ATOM   3539  CE1 PHE A 422     -13.172 -13.956 135.586  1.00 60.72           C  
ANISOU 3539  CE1 PHE A 422     6339   9782   6950  -2482   1163   1527       C  
ATOM   3540  CE2 PHE A 422     -12.880 -16.320 135.781  1.00 74.82           C  
ANISOU 3540  CE2 PHE A 422     8401  11142   8884  -2718   1327   1803       C  
ATOM   3541  CZ  PHE A 422     -13.704 -15.212 135.799  1.00 63.59           C  
ANISOU 3541  CZ  PHE A 422     6735  10026   7400  -2696   1321   1613       C  
ATOM   3542  N   ASN A 423      -7.168 -16.158 136.823  1.00 74.33           N  
ANISOU 3542  N   ASN A 423     9128  10678   8438  -2013    837   2463       N  
ATOM   3543  CA  ASN A 423      -6.799 -17.399 137.499  1.00 79.04           C  
ANISOU 3543  CA  ASN A 423     9911  11087   9033  -1992    938   2664       C  
ATOM   3544  C   ASN A 423      -6.422 -17.151 138.957  1.00 72.99           C  
ANISOU 3544  C   ASN A 423     9211  10529   7995  -1898    957   2787       C  
ATOM   3545  O   ASN A 423      -6.665 -18.006 139.820  1.00 82.12           O  
ANISOU 3545  O   ASN A 423    10475  11635   9092  -1931   1111   2934       O  
ATOM   3546  CB  ASN A 423      -5.655 -18.085 136.752  1.00 90.07           C  
ANISOU 3546  CB  ASN A 423    11458  12188  10578  -1870    839   2748       C  
ATOM   3547  CG  ASN A 423      -6.098 -18.704 135.433  1.00 80.33           C  
ANISOU 3547  CG  ASN A 423    10204  10704   9615  -1987    873   2642       C  
ATOM   3548  OD1 ASN A 423      -6.110 -18.046 134.393  1.00 54.15           O  
ANISOU 3548  OD1 ASN A 423     6782   7403   6388  -1994    749   2492       O  
ATOM   3549  ND2 ASN A 423      -6.451 -19.984 135.473  1.00 92.55           N  
ANISOU 3549  ND2 ASN A 423    11860  12016  11288  -2083   1053   2714       N  
ATOM   3550  N   ASN A 424      -5.831 -15.993 139.252  1.00 72.47           N  
ANISOU 3550  N   ASN A 424     9086  10694   7753  -1787    814   2719       N  
ATOM   3551  CA  ASN A 424      -5.449 -15.601 140.611  1.00 76.88           C  
ANISOU 3551  CA  ASN A 424     9683  11498   8032  -1705    810   2785       C  
ATOM   3552  C   ASN A 424      -6.201 -14.302 140.885  1.00 71.42           C  
ANISOU 3552  C   ASN A 424     8821  11109   7205  -1768    834   2578       C  
ATOM   3553  O   ASN A 424      -5.772 -13.218 140.476  1.00 80.14           O  
ANISOU 3553  O   ASN A 424     9851  12327   8272  -1703    712   2434       O  
ATOM   3554  CB  ASN A 424      -3.889 -15.453 140.745  1.00 92.24           C  
ANISOU 3554  CB  ASN A 424    11714  13439   9893  -1508    620   2863       C  
ATOM   3555  CG  ASN A 424      -3.439 -14.860 142.085  1.00108.65           C  
ANISOU 3555  CG  ASN A 424    13795  15823  11664  -1432    582   2877       C  
ATOM   3556  OD1 ASN A 424      -4.060 -13.954 142.636  1.00114.80           O  
ANISOU 3556  OD1 ASN A 424    14476  16860  12284  -1498    631   2735       O  
ATOM   3557  ND2 ASN A 424      -2.354 -15.404 142.624  1.00115.50           N  
ANISOU 3557  ND2 ASN A 424    14771  16667  12446  -1290    501   3038       N  
ATOM   3558  N   GLN A 425      -7.346 -14.421 141.551  1.00 70.90           N  
ANISOU 3558  N   GLN A 425     8699  11160   7079  -1891   1015   2553       N  
ATOM   3559  CA  GLN A 425      -8.151 -13.258 141.881  1.00 76.86           C  
ANISOU 3559  CA  GLN A 425     9291  12196   7717  -1939   1074   2343       C  
ATOM   3560  C   GLN A 425      -7.741 -12.690 143.237  1.00 78.77           C  
ANISOU 3560  C   GLN A 425     9579  12694   7658  -1866   1072   2344       C  
ATOM   3561  O   GLN A 425      -7.056 -13.339 144.034  1.00 71.44           O  
ANISOU 3561  O   GLN A 425     8794  11747   6603  -1802   1052   2529       O  
ATOM   3562  CB  GLN A 425      -9.638 -13.613 141.897  1.00 79.37           C  
ANISOU 3562  CB  GLN A 425     9494  12528   8136  -2105   1274   2279       C  
ATOM   3563  CG  GLN A 425     -10.142 -14.232 140.602  1.00 81.20           C  
ANISOU 3563  CG  GLN A 425     9658  12533   8660  -2205   1283   2246       C  
ATOM   3564  CD  GLN A 425     -11.596 -13.900 140.326  1.00 76.51           C  
ANISOU 3564  CD  GLN A 425     8839  12068   8163  -2337   1412   2049       C  
ATOM   3565  OE1 GLN A 425     -12.188 -13.061 141.003  1.00 85.55           O  
ANISOU 3565  OE1 GLN A 425     9872  13463   9169  -2327   1488   1922       O  
ATOM   3566  NE2 GLN A 425     -12.179 -14.559 139.332  1.00 65.56           N  
ANISOU 3566  NE2 GLN A 425     7376  10515   7017  -2453   1436   2002       N  
ATOM   3567  N   ILE A 426      -8.167 -11.454 143.494  1.00 81.97           N  
ANISOU 3567  N   ILE A 426     9855  13340   7948  -1868   1100   2119       N  
ATOM   3568  CA  ILE A 426      -7.856 -10.759 144.740  1.00 74.06           C  
ANISOU 3568  CA  ILE A 426     8879  12599   6663  -1818   1106   2054       C  
ATOM   3569  C   ILE A 426      -9.114 -10.036 145.198  1.00 76.75           C  
ANISOU 3569  C   ILE A 426     9082  13132   6949  -1897   1283   1854       C  
ATOM   3570  O   ILE A 426      -9.640  -9.184 144.474  1.00 67.40           O  
ANISOU 3570  O   ILE A 426     7753  11979   5877  -1896   1306   1645       O  
ATOM   3571  CB  ILE A 426      -6.693  -9.763 144.583  1.00 63.85           C  
ANISOU 3571  CB  ILE A 426     7591  11394   5273  -1702    929   1929       C  
ATOM   3572  CG1 ILE A 426      -5.453 -10.466 144.024  1.00 65.69           C  
ANISOU 3572  CG1 ILE A 426     7936  11427   5595  -1611    751   2113       C  
ATOM   3573  CG2 ILE A 426      -6.379  -9.109 145.910  1.00 54.85           C  
ANISOU 3573  CG2 ILE A 426     6473  10527   3842  -1674    938   1837       C  
ATOM   3574  CD1 ILE A 426      -4.430  -9.527 143.457  1.00 58.48           C  
ANISOU 3574  CD1 ILE A 426     7003  10540   4677  -1520    588   1972       C  
ATOM   3575  N   SER A 427      -9.590 -10.367 146.397  1.00 83.23           N  
ANISOU 3575  N   SER A 427     9946  14077   7602  -1948   1418   1918       N  
ATOM   3576  CA  SER A 427     -10.859  -9.843 146.879  1.00 91.89           C  
ANISOU 3576  CA  SER A 427    10913  15333   8667  -2025   1610   1747       C  
ATOM   3577  C   SER A 427     -10.808  -8.323 147.032  1.00 83.76           C  
ANISOU 3577  C   SER A 427     9789  14499   7536  -1955   1595   1456       C  
ATOM   3578  O   SER A 427      -9.740  -7.711 147.140  1.00 91.62           O  
ANISOU 3578  O   SER A 427    10847  15553   8413  -1869   1455   1395       O  
ATOM   3579  CB  SER A 427     -11.232 -10.496 148.209  1.00105.10           C  
ANISOU 3579  CB  SER A 427    12680  17099  10153  -2083   1757   1889       C  
ATOM   3580  OG  SER A 427     -10.310 -10.139 149.222  1.00111.38           O  
ANISOU 3580  OG  SER A 427    13585  18066  10669  -2002   1672   1908       O  
ATOM   3581  N   ASP A 428     -12.000  -7.718 147.052  1.00 77.40           N  
ANISOU 3581  N   ASP A 428     8828  13787   6794  -1991   1756   1261       N  
ATOM   3582  CA  ASP A 428     -12.138  -6.266 147.026  1.00 60.87           C  
ANISOU 3582  CA  ASP A 428     6635  11823   4672  -1910   1784    963       C  
ATOM   3583  C   ASP A 428     -11.574  -5.583 148.266  1.00 66.81           C  
ANISOU 3583  C   ASP A 428     7478  12764   5144  -1881   1788    860       C  
ATOM   3584  O   ASP A 428     -11.310  -4.377 148.225  1.00 60.73           O  
ANISOU 3584  O   ASP A 428     6674  12056   4343  -1807   1780    612       O  
ATOM   3585  CB  ASP A 428     -13.614  -5.889 146.871  1.00 69.92           C  
ANISOU 3585  CB  ASP A 428     7587  13021   5958  -1934   1969    799       C  
ATOM   3586  CG  ASP A 428     -14.535  -6.748 147.725  1.00 97.63           C  
ANISOU 3586  CG  ASP A 428    11093  16587   9417  -2058   2136    920       C  
ATOM   3587  OD1 ASP A 428     -14.413  -7.990 147.674  1.00107.39           O  
ANISOU 3587  OD1 ASP A 428    12415  17700  10687  -2144   2118   1166       O  
ATOM   3588  OD2 ASP A 428     -15.380  -6.179 148.450  1.00110.11           O1-
ANISOU 3588  OD2 ASP A 428    12590  18315  10930  -2064   2301    768       O1-
ATOM   3589  N   ASP A 429     -11.378  -6.308 149.365  1.00 85.02           N  
ANISOU 3589  N   ASP A 429     9902  15156   7247  -1934   1809   1034       N  
ATOM   3590  CA  ASP A 429     -10.954  -5.684 150.610  1.00 93.47           C  
ANISOU 3590  CA  ASP A 429    11039  16439   8036  -1921   1821    926       C  
ATOM   3591  C   ASP A 429      -9.464  -5.868 150.887  1.00 92.48           C  
ANISOU 3591  C   ASP A 429    11043  16346   7748  -1868   1611   1033       C  
ATOM   3592  O   ASP A 429      -9.049  -5.829 152.051  1.00 83.46           O  
ANISOU 3592  O   ASP A 429     9976  15389   6347  -1873   1602   1046       O  
ATOM   3593  CB  ASP A 429     -11.784  -6.223 151.774  1.00106.72           C  
ANISOU 3593  CB  ASP A 429    12746  18240   9563  -2002   2002   1020       C  
ATOM   3594  CG  ASP A 429     -11.576  -7.705 151.997  1.00116.86           C  
ANISOU 3594  CG  ASP A 429    14156  19429  10818  -2042   1983   1371       C  
ATOM   3595  OD1 ASP A 429     -10.865  -8.332 151.184  1.00110.85           O1-
ANISOU 3595  OD1 ASP A 429    13446  18489  10182  -2006   1834   1534       O1-
ATOM   3596  OD2 ASP A 429     -12.129  -8.242 152.979  1.00120.68           O  
ANISOU 3596  OD2 ASP A 429    14695  19999  11159  -2102   2135   1483       O  
ATOM   3597  N   ASN A 430      -8.650  -6.046 149.847  1.00 85.76           N  
ANISOU 3597  N   ASN A 430    10208  15333   7044  -1813   1442   1102       N  
ATOM   3598  CA  ASN A 430      -7.196  -6.152 149.989  1.00 82.50           C  
ANISOU 3598  CA  ASN A 430     9887  14947   6512  -1748   1233   1182       C  
ATOM   3599  C   ASN A 430      -6.516  -5.422 148.839  1.00 74.19           C  
ANISOU 3599  C   ASN A 430     8792  13779   5619  -1688   1108   1030       C  
ATOM   3600  O   ASN A 430      -6.028  -6.040 147.886  1.00 63.16           O  
ANISOU 3600  O   ASN A 430     7422  12191   4384  -1650    991   1192       O  
ATOM   3601  CB  ASN A 430      -6.757  -7.616 150.043  1.00 80.62           C  
ANISOU 3601  CB  ASN A 430     9761  14592   6281  -1728   1156   1544       C  
ATOM   3602  CG  ASN A 430      -5.286  -7.767 150.389  1.00 79.09           C  
ANISOU 3602  CG  ASN A 430     9642  14466   5942  -1638    949   1635       C  
ATOM   3603  OD1 ASN A 430      -4.664  -6.849 150.923  1.00 83.79           O  
ANISOU 3603  OD1 ASN A 430    10208  15258   6370  -1623    880   1433       O  
ATOM   3604  ND2 ASN A 430      -4.720  -8.927 150.078  1.00 71.35           N  
ANISOU 3604  ND2 ASN A 430     8750  13317   5042  -1578    857   1925       N  
ATOM   3605  N   PRO A 431      -6.461  -4.088 148.901  1.00 82.10           N  
ANISOU 3605  N   PRO A 431     9737  14873   6584  -1678   1146    709       N  
ATOM   3606  CA  PRO A 431      -5.748  -3.343 147.851  1.00 86.43           C  
ANISOU 3606  CA  PRO A 431    10266  15302   7270  -1620   1048    554       C  
ATOM   3607  C   PRO A 431      -4.238  -3.489 147.927  1.00 85.77           C  
ANISOU 3607  C   PRO A 431    10248  15247   7093  -1583    834    617       C  
ATOM   3608  O   PRO A 431      -3.551  -3.268 146.919  1.00 87.63           O  
ANISOU 3608  O   PRO A 431    10487  15342   7467  -1536    728    586       O  
ATOM   3609  CB  PRO A 431      -6.180  -1.888 148.092  1.00 91.42           C  
ANISOU 3609  CB  PRO A 431    10839  16009   7886  -1619   1192    184       C  
ATOM   3610  CG  PRO A 431      -7.370  -1.958 149.009  1.00 83.96           C  
ANISOU 3610  CG  PRO A 431     9856  15188   6856  -1671   1377    166       C  
ATOM   3611  CD  PRO A 431      -7.166  -3.192 149.832  1.00 83.74           C  
ANISOU 3611  CD  PRO A 431     9902  15255   6661  -1717   1313    464       C  
ATOM   3612  N   ALA A 432      -3.704  -3.856 149.095  1.00 78.84           N  
ANISOU 3612  N   ALA A 432     9413  14557   5984  -1597    770    704       N  
ATOM   3613  CA  ALA A 432      -2.258  -3.902 149.275  1.00 75.88           C  
ANISOU 3613  CA  ALA A 432     9063  14255   5514  -1553    568    732       C  
ATOM   3614  C   ALA A 432      -1.626  -4.976 148.400  1.00 69.30           C  
ANISOU 3614  C   ALA A 432     8273  13218   4838  -1476    420   1025       C  
ATOM   3615  O   ALA A 432      -0.655  -4.713 147.681  1.00 73.20           O  
ANISOU 3615  O   ALA A 432     8757  13632   5425  -1429    283    973       O  
ATOM   3616  CB  ALA A 432      -1.925  -4.138 150.749  1.00 82.33           C  
ANISOU 3616  CB  ALA A 432     9900  15339   6041  -1570    542    783       C  
ATOM   3617  N   ARG A 433      -2.160  -6.200 148.457  1.00 68.56           N  
ANISOU 3617  N   ARG A 433     8235  13023   4791  -1465    461   1324       N  
ATOM   3618  CA  ARG A 433      -1.604  -7.274 147.644  1.00 76.48           C  
ANISOU 3618  CA  ARG A 433     9295  13795   5970  -1389    345   1596       C  
ATOM   3619  C   ARG A 433      -1.794  -6.997 146.160  1.00 76.57           C  
ANISOU 3619  C   ARG A 433     9277  13570   6248  -1389    339   1527       C  
ATOM   3620  O   ARG A 433      -0.946  -7.376 145.345  1.00 69.96           O  
ANISOU 3620  O   ARG A 433     8465  12563   5551  -1317    201   1630       O  
ATOM   3621  CB  ARG A 433      -2.238  -8.613 148.019  1.00 81.14           C  
ANISOU 3621  CB  ARG A 433     9966  14289   6573  -1394    434   1899       C  
ATOM   3622  CG  ARG A 433      -1.576  -9.796 147.334  1.00 90.64           C  
ANISOU 3622  CG  ARG A 433    11248  15237   7952  -1304    331   2175       C  
ATOM   3623  CD  ARG A 433      -2.420 -11.060 147.375  1.00 95.44           C  
ANISOU 3623  CD  ARG A 433    11945  15662   8655  -1338    471   2426       C  
ATOM   3624  NE  ARG A 433      -1.944 -12.025 146.387  1.00106.12           N  
ANISOU 3624  NE  ARG A 433    13365  16703  10253  -1272    404   2615       N  
ATOM   3625  CZ  ARG A 433      -1.402 -13.201 146.684  1.00110.56           C  
ANISOU 3625  CZ  ARG A 433    14046  17139  10820  -1181    384   2877       C  
ATOM   3626  NH1 ARG A 433      -1.266 -13.570 147.950  1.00110.80           N  
ANISOU 3626  NH1 ARG A 433    14145  17345  10608  -1142    418   3005       N  
ATOM   3627  NH2 ARG A 433      -0.993 -14.008 145.714  1.00112.33           N  
ANISOU 3627  NH2 ARG A 433    14332  17060  11290  -1122    341   3006       N  
ATOM   3628  N   PHE A 434      -2.889  -6.331 145.792  1.00 78.53           N  
ANISOU 3628  N   PHE A 434     9464  13805   6568  -1455    490   1351       N  
ATOM   3629  CA  PHE A 434      -3.082  -5.964 144.394  1.00 77.87           C  
ANISOU 3629  CA  PHE A 434     9345  13529   6714  -1442    491   1272       C  
ATOM   3630  C   PHE A 434      -1.990  -5.009 143.923  1.00 72.88           C  
ANISOU 3630  C   PHE A 434     8709  12853   6129  -1372    362   1061       C  
ATOM   3631  O   PHE A 434      -1.334  -5.256 142.901  1.00 46.56           O  
ANISOU 3631  O   PHE A 434     5401   9274   3015  -1298    236   1117       O  
ATOM   3632  CB  PHE A 434      -4.462  -5.342 144.203  1.00 84.24           C  
ANISOU 3632  CB  PHE A 434    10061  14324   7621  -1483    678   1086       C  
ATOM   3633  CG  PHE A 434      -4.785  -5.035 142.777  1.00 89.11           C  
ANISOU 3633  CG  PHE A 434    10633  14635   8590  -1404    650    982       C  
ATOM   3634  CD1 PHE A 434      -4.601  -5.992 141.795  1.00 88.14           C  
ANISOU 3634  CD1 PHE A 434    10545  14264   8680  -1379    552   1177       C  
ATOM   3635  CD2 PHE A 434      -5.272  -3.793 142.416  1.00 88.18           C  
ANISOU 3635  CD2 PHE A 434    10445  14479   8582  -1346    730    693       C  
ATOM   3636  CE1 PHE A 434      -4.897  -5.715 140.483  1.00 89.94           C  
ANISOU 3636  CE1 PHE A 434    10731  14244   9198  -1307    520   1079       C  
ATOM   3637  CE2 PHE A 434      -5.569  -3.508 141.098  1.00 77.49           C  
ANISOU 3637  CE2 PHE A 434     9053  12864   7524  -1251    699    622       C  
ATOM   3638  CZ  PHE A 434      -5.379  -4.470 140.130  1.00 70.62           C  
ANISOU 3638  CZ  PHE A 434     8212  11781   6839  -1235    586    812       C  
ATOM   3639  N   LEU A 435      -1.777  -3.915 144.661  1.00 77.21           N  
ANISOU 3639  N   LEU A 435     9228  13620   6490  -1404    405    798       N  
ATOM   3640  CA  LEU A 435      -0.692  -2.994 144.331  1.00 65.41           C  
ANISOU 3640  CA  LEU A 435     7728  12084   5039  -1366    304    572       C  
ATOM   3641  C   LEU A 435       0.643  -3.722 144.254  1.00 64.84           C  
ANISOU 3641  C   LEU A 435     7688  12033   4917  -1324     96    766       C  
ATOM   3642  O   LEU A 435       1.429  -3.512 143.322  1.00 71.40           O  
ANISOU 3642  O   LEU A 435     8522  12651   5955  -1260     -8    712       O  
ATOM   3643  CB  LEU A 435      -0.626  -1.870 145.365  1.00 69.07           C  
ANISOU 3643  CB  LEU A 435     8161  12826   5254  -1443    395    269       C  
ATOM   3644  CG  LEU A 435      -0.894  -0.457 144.849  1.00 66.95           C  
ANISOU 3644  CG  LEU A 435     7872  12393   5172  -1424    519    -92       C  
ATOM   3645  CD1 LEU A 435      -0.408   0.577 145.848  1.00 76.40           C  
ANISOU 3645  CD1 LEU A 435     9054  13852   6120  -1519    576   -403       C  
ATOM   3646  CD2 LEU A 435      -0.229  -0.252 143.493  1.00 59.48           C  
ANISOU 3646  CD2 LEU A 435     6948  11108   4541  -1331    417   -113       C  
ATOM   3647  N   GLN A 436       0.909  -4.590 145.231  1.00 77.97           N  
ANISOU 3647  N   GLN A 436     9365  13847   6412  -1316     39    978       N  
ATOM   3648  CA  GLN A 436       2.161  -5.335 145.259  1.00 82.48           C  
ANISOU 3648  CA  GLN A 436     9949  14402   6989  -1231   -147   1165       C  
ATOM   3649  C   GLN A 436       2.349  -6.136 143.978  1.00 83.29           C  
ANISOU 3649  C   GLN A 436    10099  14197   7352  -1158   -215   1374       C  
ATOM   3650  O   GLN A 436       3.345  -5.973 143.267  1.00 83.24           O  
ANISOU 3650  O   GLN A 436    10078  14098   7450  -1104   -341   1340       O  
ATOM   3651  CB  GLN A 436       2.191  -6.257 146.481  1.00 80.75           C  
ANISOU 3651  CB  GLN A 436     9754  14335   6590  -1202   -158   1386       C  
ATOM   3652  CG  GLN A 436       3.496  -7.007 146.650  1.00 94.29           C  
ANISOU 3652  CG  GLN A 436    11472  16065   8291  -1086   -333   1572       C  
ATOM   3653  CD  GLN A 436       4.677  -6.072 146.777  1.00114.06           C  
ANISOU 3653  CD  GLN A 436    13880  18742  10715  -1090   -455   1329       C  
ATOM   3654  OE1 GLN A 436       4.754  -5.277 147.712  1.00118.08           O  
ANISOU 3654  OE1 GLN A 436    14332  19516  11015  -1163   -433   1113       O  
ATOM   3655  NE2 GLN A 436       5.601  -6.154 145.827  1.00118.02           N  
ANISOU 3655  NE2 GLN A 436    14361  19087  11394  -1022   -575   1346       N  
ATOM   3656  N   LYS A 437       1.383  -7.002 143.660  1.00 68.45           N  
ANISOU 3656  N   LYS A 437     8270  12149   5590  -1168   -123   1576       N  
ATOM   3657  CA  LYS A 437       1.491  -7.838 142.470  1.00 58.09           C  
ANISOU 3657  CA  LYS A 437     7007  10524   4539  -1113   -171   1766       C  
ATOM   3658  C   LYS A 437       1.542  -7.015 141.190  1.00 59.62           C  
ANISOU 3658  C   LYS A 437     7176  10503   4974  -1094   -190   1553       C  
ATOM   3659  O   LYS A 437       2.032  -7.506 140.168  1.00 46.06           O  
ANISOU 3659  O   LYS A 437     5493   8525   3484  -1026   -270   1644       O  
ATOM   3660  CB  LYS A 437       0.328  -8.831 142.410  1.00 59.74           C  
ANISOU 3660  CB  LYS A 437     7262  10590   4845  -1161    -39   1959       C  
ATOM   3661  CG  LYS A 437       0.436  -9.965 143.424  1.00 81.74           C  
ANISOU 3661  CG  LYS A 437    10114  13411   7532  -1125    -22   2197       C  
ATOM   3662  CD  LYS A 437       1.867 -10.481 143.530  1.00 85.51           C  
ANISOU 3662  CD  LYS A 437    10623  13859   8008   -988   -183   2322       C  
ATOM   3663  CE  LYS A 437       2.354 -10.469 144.968  1.00 92.41           C  
ANISOU 3663  CE  LYS A 437    11488  15027   8597   -951   -217   2351       C  
ATOM   3664  NZ  LYS A 437       3.835 -10.449 145.068  1.00 89.49           N  
ANISOU 3664  NZ  LYS A 437    11083  14732   8188   -831   -392   2361       N  
ATOM   3665  N   ALA A 438       1.051  -5.776 141.220  1.00 63.46           N  
ANISOU 3665  N   ALA A 438     7610  11040   5462  -1130   -103   1249       N  
ATOM   3666  CA  ALA A 438       1.256  -4.885 140.084  1.00 55.50           C  
ANISOU 3666  CA  ALA A 438     6590   9794   4705  -1075   -115   1024       C  
ATOM   3667  C   ALA A 438       2.667  -4.309 140.048  1.00 48.03           C  
ANISOU 3667  C   ALA A 438     5633   8887   3728  -1044   -235    898       C  
ATOM   3668  O   ALA A 438       3.166  -3.983 138.966  1.00 43.98           O  
ANISOU 3668  O   ALA A 438     5136   8130   3444   -984   -278    816       O  
ATOM   3669  CB  ALA A 438       0.236  -3.744 140.107  1.00 39.68           C  
ANISOU 3669  CB  ALA A 438     4543   7802   2731  -1099     42    758       C  
ATOM   3670  N   MET A 439       3.320  -4.188 141.201  1.00 50.44           N  
ANISOU 3670  N   MET A 439     5905   9511   3749  -1091   -287    876       N  
ATOM   3671  CA  MET A 439       4.674  -3.657 141.280  1.00 53.84           C  
ANISOU 3671  CA  MET A 439     6292  10038   4127  -1086   -404    736       C  
ATOM   3672  C   MET A 439       5.744  -4.741 141.208  1.00 63.06           C  
ANISOU 3672  C   MET A 439     7455  11229   5275  -1008   -579   1008       C  
ATOM   3673  O   MET A 439       6.917  -4.457 141.474  1.00 56.78           O  
ANISOU 3673  O   MET A 439     6592  10597   4385  -1004   -695    924       O  
ATOM   3674  CB  MET A 439       4.842  -2.842 142.562  1.00 46.84           C  
ANISOU 3674  CB  MET A 439     5347   9523   2927  -1187   -372    516       C  
ATOM   3675  CG  MET A 439       4.144  -1.490 142.554  1.00 60.24           C  
ANISOU 3675  CG  MET A 439     7043  11169   4677  -1254   -195    166       C  
ATOM   3676  SD  MET A 439       4.877  -0.315 141.398  1.00 68.88           S  
ANISOU 3676  SD  MET A 439     8142  11961   6066  -1236   -172   -131       S  
ATOM   3677  CE  MET A 439       3.794  -0.526 140.002  1.00 61.74           C  
ANISOU 3677  CE  MET A 439     7311  10638   5508  -1121    -84    -14       C  
ATOM   3678  N   ASP A 440       5.369  -5.970 140.865  1.00 66.28           N  
ANISOU 3678  N   ASP A 440     7927  11481   5776   -947   -589   1322       N  
ATOM   3679  CA  ASP A 440       6.352  -7.032 140.705  1.00 60.93           C  
ANISOU 3679  CA  ASP A 440     7259  10747   5144   -840   -722   1581       C  
ATOM   3680  C   ASP A 440       7.206  -6.775 139.465  1.00 68.70           C  
ANISOU 3680  C   ASP A 440     8231  11488   6383   -783   -799   1494       C  
ATOM   3681  O   ASP A 440       6.696  -6.426 138.398  1.00 78.99           O  
ANISOU 3681  O   ASP A 440     9578  12496   7939   -786   -723   1380       O  
ATOM   3682  CB  ASP A 440       5.653  -8.389 140.618  1.00 62.01           C  
ANISOU 3682  CB  ASP A 440     7486  10681   5395   -794   -657   1880       C  
ATOM   3683  CG  ASP A 440       5.049  -8.823 141.948  1.00 65.70           C  
ANISOU 3683  CG  ASP A 440     7968  11345   5652   -822   -578   1979       C  
ATOM   3684  OD1 ASP A 440       5.093  -8.031 142.913  1.00 67.53           O  
ANISOU 3684  OD1 ASP A 440     8138  11871   5649   -879   -573   1810       O  
ATOM   3685  OD2 ASP A 440       4.525  -9.952 142.028  1.00 68.18           O1-
ANISOU 3685  OD2 ASP A 440     8360  11508   6036   -796   -511   2211       O1-
ATOM   3686  N   PHE A 441       8.512  -6.971 139.614  1.00 56.12           N  
ANISOU 3686  N   PHE A 441     6573  10005   4745   -714   -937   1539       N  
ATOM   3687  CA  PHE A 441       9.576  -6.525 138.715  1.00 61.36           C  
ANISOU 3687  CA  PHE A 441     7186  10534   5593   -677  -1013   1399       C  
ATOM   3688  C   PHE A 441       9.635  -7.153 137.311  1.00 72.88           C  
ANISOU 3688  C   PHE A 441     8723  11584   7383   -592  -1002   1518       C  
ATOM   3689  O   PHE A 441      10.246  -6.552 136.404  1.00 77.10           O  
ANISOU 3689  O   PHE A 441     9239  11946   8108   -582  -1008   1341       O  
ATOM   3690  CB  PHE A 441      10.905  -6.746 139.444  1.00 63.94           C  
ANISOU 3690  CB  PHE A 441     7399  11112   5785   -614  -1146   1431       C  
ATOM   3691  CG  PHE A 441      12.109  -6.434 138.622  1.00 65.78           C  
ANISOU 3691  CG  PHE A 441     7550  11275   6168   -579  -1242   1328       C  
ATOM   3692  CD1 PHE A 441      12.474  -5.122 138.380  1.00 68.09           C  
ANISOU 3692  CD1 PHE A 441     7775  11599   6496   -691  -1212    971       C  
ATOM   3693  CD2 PHE A 441      12.879  -7.451 138.094  1.00 53.65           C  
ANISOU 3693  CD2 PHE A 441     6019   9561   4804   -430  -1303   1545       C  
ATOM   3694  CE1 PHE A 441      13.586  -4.831 137.617  1.00 61.79           C  
ANISOU 3694  CE1 PHE A 441     6904  10694   5880   -668  -1260    854       C  
ATOM   3695  CE2 PHE A 441      13.990  -7.168 137.332  1.00 60.45           C  
ANISOU 3695  CE2 PHE A 441     6792  10368   5810   -399  -1381   1450       C  
ATOM   3696  CZ  PHE A 441      14.345  -5.856 137.094  1.00 63.55           C  
ANISOU 3696  CZ  PHE A 441     7107  10814   6227   -524  -1359   1101       C  
ATOM   3697  N   PRO A 442       9.071  -8.352 137.081  1.00 72.17           N  
ANISOU 3697  N   PRO A 442     8726  11329   7368   -538   -975   1804       N  
ATOM   3698  CA  PRO A 442       9.050  -8.894 135.710  1.00 57.94           C  
ANISOU 3698  CA  PRO A 442     7003   9139   5874   -480   -950   1871       C  
ATOM   3699  C   PRO A 442       8.579  -7.936 134.619  1.00 56.97           C  
ANISOU 3699  C   PRO A 442     6908   8786   5952   -525   -869   1610       C  
ATOM   3700  O   PRO A 442       9.157  -7.939 133.522  1.00 69.05           O  
ANISOU 3700  O   PRO A 442     8462  10082   7694   -471   -887   1570       O  
ATOM   3701  CB  PRO A 442       8.107 -10.088 135.837  1.00 42.68           C  
ANISOU 3701  CB  PRO A 442     5167   7080   3971   -478   -869   2115       C  
ATOM   3702  CG  PRO A 442       8.303 -10.573 137.222  1.00 55.32           C  
ANISOU 3702  CG  PRO A 442     6741   8917   5361   -446   -874   2222       C  
ATOM   3703  CD  PRO A 442       8.801  -9.414 138.060  1.00 64.32           C  
ANISOU 3703  CD  PRO A 442     7765  10417   6256   -494   -947   2032       C  
ATOM   3704  N   PHE A 443       7.550  -7.125 134.873  1.00 47.14           N  
ANISOU 3704  N   PHE A 443     5664   7601   4644   -608   -773   1441       N  
ATOM   3705  CA  PHE A 443       6.981  -6.313 133.801  1.00 45.53           C  
ANISOU 3705  CA  PHE A 443     5498   7168   4631   -615   -689   1242       C  
ATOM   3706  C   PHE A 443       7.965  -5.279 133.266  1.00 57.08           C  
ANISOU 3706  C   PHE A 443     6937   8569   6184   -599   -701   1019       C  
ATOM   3707  O   PHE A 443       7.756  -4.754 132.167  1.00 59.00           O  
ANISOU 3707  O   PHE A 443     7232   8573   6612   -569   -641    904       O  
ATOM   3708  CB  PHE A 443       5.692  -5.617 134.273  1.00 35.05           C  
ANISOU 3708  CB  PHE A 443     4162   5941   3214   -683   -574   1113       C  
ATOM   3709  CG  PHE A 443       5.924  -4.340 135.030  1.00 41.57           C  
ANISOU 3709  CG  PHE A 443     4932   6968   3895   -736   -533    861       C  
ATOM   3710  CD1 PHE A 443       6.113  -4.360 136.399  1.00 42.63           C  
ANISOU 3710  CD1 PHE A 443     5009   7428   3762   -798   -560    873       C  
ATOM   3711  CD2 PHE A 443       5.927  -3.118 134.378  1.00 45.57           C  
ANISOU 3711  CD2 PHE A 443     5454   7335   4526   -727   -453    610       C  
ATOM   3712  CE1 PHE A 443       6.318  -3.193 137.105  1.00 45.29           C  
ANISOU 3712  CE1 PHE A 443     5295   7955   3959   -869   -511    610       C  
ATOM   3713  CE2 PHE A 443       6.137  -1.945 135.075  1.00 38.54           C  
ANISOU 3713  CE2 PHE A 443     4525   6599   3521   -792   -386    359       C  
ATOM   3714  CZ  PHE A 443       6.335  -1.981 136.441  1.00 35.67           C  
ANISOU 3714  CZ  PHE A 443     4095   6567   2891   -873   -417    343       C  
ATOM   3715  N   ILE A 444       9.030  -4.980 134.007  1.00 49.44           N  
ANISOU 3715  N   ILE A 444     5884   7817   5083   -620   -773    954       N  
ATOM   3716  CA  ILE A 444      10.027  -4.002 133.594  1.00 50.70           C  
ANISOU 3716  CA  ILE A 444     6003   7935   5325   -636   -769    723       C  
ATOM   3717  C   ILE A 444      11.411  -4.610 133.427  1.00 51.59           C  
ANISOU 3717  C   ILE A 444     6048   8073   5479   -578   -892    824       C  
ATOM   3718  O   ILE A 444      12.324  -3.919 132.961  1.00 45.34           O  
ANISOU 3718  O   ILE A 444     5214   7226   4788   -596   -885    645       O  
ATOM   3719  CB  ILE A 444      10.079  -2.813 134.576  1.00 50.65           C  
ANISOU 3719  CB  ILE A 444     5928   8177   5139   -745   -718    457       C  
ATOM   3720  CG1 ILE A 444      10.667  -1.569 133.901  1.00 43.77           C  
ANISOU 3720  CG1 ILE A 444     5062   7149   4418   -786   -628    170       C  
ATOM   3721  CG2 ILE A 444      10.888  -3.176 135.810  1.00 46.66           C  
ANISOU 3721  CG2 ILE A 444     5302   8046   4382   -779   -845    510       C  
ATOM   3722  CD1 ILE A 444       9.844  -1.048 132.743  1.00 31.07           C  
ANISOU 3722  CD1 ILE A 444     3579   5203   3023   -733   -493    113       C  
ATOM   3723  N   CYS A 445      11.596  -5.885 133.787  1.00 51.00           N  
ANISOU 3723  N   CYS A 445     5963   8073   5343   -505   -990   1109       N  
ATOM   3724  CA  CYS A 445      12.920  -6.503 133.690  1.00 43.03           C  
ANISOU 3724  CA  CYS A 445     4873   7107   4370   -419  -1106   1224       C  
ATOM   3725  C   CYS A 445      13.567  -6.356 132.310  1.00 47.07           C  
ANISOU 3725  C   CYS A 445     5414   7312   5156   -374  -1075   1146       C  
ATOM   3726  O   CYS A 445      14.799  -6.304 132.213  1.00 53.74           O  
ANISOU 3726  O   CYS A 445     6154   8225   6041   -342  -1142   1104       O  
ATOM   3727  CB  CYS A 445      12.829  -7.983 134.065  1.00 34.58           C  
ANISOU 3727  CB  CYS A 445     3834   6061   3245   -315  -1173   1581       C  
ATOM   3728  SG  CYS A 445      12.138  -9.026 132.773  1.00 45.64           S  
ANISOU 3728  SG  CYS A 445     5399   7021   4919   -251  -1093   1768       S  
ATOM   3729  N   ASN A 446      12.773  -6.281 131.237  1.00 40.05           N  
ANISOU 3729  N   ASN A 446     4657   6110   4449   -371   -974   1122       N  
ATOM   3730  CA  ASN A 446      13.350  -6.256 129.891  1.00 42.15           C  
ANISOU 3730  CA  ASN A 446     4972   6088   4956   -319   -938   1076       C  
ATOM   3731  C   ASN A 446      14.023  -4.932 129.544  1.00 51.40           C  
ANISOU 3731  C   ASN A 446     6100   7240   6188   -382   -876    790       C  
ATOM   3732  O   ASN A 446      14.717  -4.861 128.522  1.00 39.27           O  
ANISOU 3732  O   ASN A 446     4587   5502   4834   -344   -843    746       O  
ATOM   3733  CB  ASN A 446      12.285  -6.571 128.840  1.00 46.11           C  
ANISOU 3733  CB  ASN A 446     5622   6295   5601   -295   -857   1131       C  
ATOM   3734  CG  ASN A 446      11.931  -8.043 128.789  1.00 62.89           C  
ANISOU 3734  CG  ASN A 446     7801   8337   7757   -238   -895   1404       C  
ATOM   3735  OD1 ASN A 446      12.769  -8.887 128.469  1.00 66.91           O  
ANISOU 3735  OD1 ASN A 446     8303   8760   8359   -157   -940   1541       O  
ATOM   3736  ND2 ASN A 446      10.678  -8.359 129.092  1.00 66.69           N  
ANISOU 3736  ND2 ASN A 446     8336   8831   8172   -281   -858   1477       N  
ATOM   3737  N   SER A 447      13.819  -3.885 130.340  1.00 55.06           N  
ANISOU 3737  N   SER A 447     6515   7893   6513   -484   -836    588       N  
ATOM   3738  CA  SER A 447      14.637  -2.681 130.269  1.00 38.09           C  
ANISOU 3738  CA  SER A 447     4302   5768   4402   -571   -771    307       C  
ATOM   3739  C   SER A 447      15.608  -2.588 131.441  1.00 50.56           C  
ANISOU 3739  C   SER A 447     5693   7718   5800   -638   -879    231       C  
ATOM   3740  O   SER A 447      16.159  -1.512 131.701  1.00 42.97           O  
ANISOU 3740  O   SER A 447     4656   6851   4817   -758   -820    -46       O  
ATOM   3741  CB  SER A 447      13.750  -1.437 130.192  1.00 28.29           C  
ANISOU 3741  CB  SER A 447     3153   4430   3165   -644   -613     90       C  
ATOM   3742  OG  SER A 447      13.186  -1.130 131.450  1.00 59.30           O  
ANISOU 3742  OG  SER A 447     7029   8629   6873   -721   -622     24       O  
ATOM   3743  N   PHE A 448      15.818  -3.693 132.152  1.00 57.69           N  
ANISOU 3743  N   PHE A 448     6518   8837   6565   -564  -1029    469       N  
ATOM   3744  CA  PHE A 448      16.867  -3.824 133.161  1.00 57.34           C  
ANISOU 3744  CA  PHE A 448     6275   9173   6341   -581  -1169    453       C  
ATOM   3745  C   PHE A 448      17.864  -4.888 132.710  1.00 59.55           C  
ANISOU 3745  C   PHE A 448     6480   9416   6730   -435  -1277    671       C  
ATOM   3746  O   PHE A 448      17.931  -5.982 133.274  1.00 58.58           O  
ANISOU 3746  O   PHE A 448     6323   9441   6495   -317  -1394    949       O  
ATOM   3747  CB  PHE A 448      16.272  -4.219 134.534  1.00 54.65           C  
ANISOU 3747  CB  PHE A 448     5900   9166   5697   -588  -1253    579       C  
ATOM   3748  CG  PHE A 448      15.669  -3.083 135.316  1.00 60.26           C  
ANISOU 3748  CG  PHE A 448     6610  10049   6239   -748  -1170    311       C  
ATOM   3749  CD1 PHE A 448      14.500  -2.464 134.895  1.00 59.20           C  
ANISOU 3749  CD1 PHE A 448     6631   9671   6192   -795  -1008    210       C  
ATOM   3750  CD2 PHE A 448      16.235  -2.680 136.514  1.00 58.88           C  
ANISOU 3750  CD2 PHE A 448     6272  10300   5800   -840  -1256    165       C  
ATOM   3751  CE1 PHE A 448      13.936  -1.435 135.639  1.00 52.66           C  
ANISOU 3751  CE1 PHE A 448     5804   8988   5217   -927   -913    -36       C  
ATOM   3752  CE2 PHE A 448      15.674  -1.656 137.263  1.00 57.22           C  
ANISOU 3752  CE2 PHE A 448     6067  10245   5428   -995  -1164    -99       C  
ATOM   3753  CZ  PHE A 448      14.525  -1.033 136.826  1.00 56.99           C  
ANISOU 3753  CZ  PHE A 448     6203   9937   5512  -1034   -983   -198       C  
ATOM   3754  N   THR A 449      18.636  -4.588 131.670  1.00 63.35           N  
ANISOU 3754  N   THR A 449     6946   9684   7440   -431  -1219    556       N  
ATOM   3755  CA  THR A 449      19.572  -5.579 131.155  1.00 52.04           C  
ANISOU 3755  CA  THR A 449     5445   8189   6139   -283  -1297    749       C  
ATOM   3756  C   THR A 449      20.957  -4.967 130.979  1.00 56.99           C  
ANISOU 3756  C   THR A 449     5877   8936   6842   -337  -1311    530       C  
ATOM   3757  O   THR A 449      21.164  -3.757 131.136  1.00 57.39           O  
ANISOU 3757  O   THR A 449     5870   9068   6870   -507  -1239    218       O  
ATOM   3758  CB  THR A 449      19.103  -6.190 129.820  1.00 35.74           C  
ANISOU 3758  CB  THR A 449     3575   5687   4319   -192  -1201    890       C  
ATOM   3759  OG1 THR A 449      19.469  -5.331 128.735  1.00 50.16           O  
ANISOU 3759  OG1 THR A 449     5441   7273   6343   -258  -1071    665       O  
ATOM   3760  CG2 THR A 449      17.599  -6.409 129.800  1.00 30.65           C  
ANISOU 3760  CG2 THR A 449     3121   4893   3632   -203  -1141    993       C  
ATOM   3761  N   LYS A 450      21.909  -5.846 130.651  1.00 57.88           N  
ANISOU 3761  N   LYS A 450     5885   9052   7055   -191  -1391    697       N  
ATOM   3762  CA  LYS A 450      23.265  -5.419 130.327  1.00 56.29           C  
ANISOU 3762  CA  LYS A 450     5483   8940   6966   -224  -1396    512       C  
ATOM   3763  C   LYS A 450      23.259  -4.350 129.248  1.00 57.57           C  
ANISOU 3763  C   LYS A 450     5751   8787   7337   -365  -1196    239       C  
ATOM   3764  O   LYS A 450      24.081  -3.426 129.279  1.00 62.73           O  
ANISOU 3764  O   LYS A 450     6255   9557   8024   -506  -1148    -42       O  
ATOM   3765  CB  LYS A 450      24.103  -6.626 129.885  1.00 48.67           C  
ANISOU 3765  CB  LYS A 450     4437   7924   6133    -10  -1471    766       C  
ATOM   3766  CG  LYS A 450      23.436  -7.521 128.828  1.00 50.46           C  
ANISOU 3766  CG  LYS A 450     4911   7711   6552    117  -1378    993       C  
ATOM   3767  CD  LYS A 450      24.086  -8.904 128.765  1.00 45.60           C  
ANISOU 3767  CD  LYS A 450     4227   7091   6006    352  -1465   1298       C  
ATOM   3768  CE  LYS A 450      23.359  -9.826 127.793  1.00 53.10           C  
ANISOU 3768  CE  LYS A 450     5431   7610   7133    451  -1362   1500       C  
ATOM   3769  NZ  LYS A 450      22.140 -10.438 128.400  1.00 69.59           N  
ANISOU 3769  NZ  LYS A 450     7680   9682   9079    471  -1386   1711       N  
ATOM   3770  N   PHE A 451      22.315  -4.445 128.308  1.00 44.91           N  
ANISOU 3770  N   PHE A 451     4404   6795   5866   -333  -1071    317       N  
ATOM   3771  CA  PHE A 451      22.177  -3.453 127.250  1.00 47.81           C  
ANISOU 3771  CA  PHE A 451     4907   6848   6409   -434   -873    102       C  
ATOM   3772  C   PHE A 451      21.936  -2.056 127.803  1.00 47.82           C  
ANISOU 3772  C   PHE A 451     4896   6955   6318   -631   -782   -200       C  
ATOM   3773  O   PHE A 451      22.375  -1.068 127.204  1.00 44.80           O  
ANISOU 3773  O   PHE A 451     4530   6421   6070   -746   -622   -438       O  
ATOM   3774  CB  PHE A 451      21.025  -3.847 126.331  1.00 49.41           C  
ANISOU 3774  CB  PHE A 451     5376   6696   6703   -352   -790    258       C  
ATOM   3775  CG  PHE A 451      21.456  -4.608 125.120  1.00 53.65           C  
ANISOU 3775  CG  PHE A 451     5982   6960   7444   -231   -748    387       C  
ATOM   3776  CD1 PHE A 451      22.213  -3.992 124.141  1.00 47.79           C  
ANISOU 3776  CD1 PHE A 451     5245   6034   6878   -275   -611    222       C  
ATOM   3777  CD2 PHE A 451      21.105  -5.939 124.958  1.00 54.15           C  
ANISOU 3777  CD2 PHE A 451     6111   6937   7525    -84   -825    665       C  
ATOM   3778  CE1 PHE A 451      22.611  -4.683 123.020  1.00 47.09           C  
ANISOU 3778  CE1 PHE A 451     5224   5703   6965   -168   -560    328       C  
ATOM   3779  CE2 PHE A 451      21.505  -6.638 123.836  1.00 53.28           C  
ANISOU 3779  CE2 PHE A 451     6071   6569   7603     18   -770    759       C  
ATOM   3780  CZ  PHE A 451      22.258  -6.005 122.871  1.00 46.11           C  
ANISOU 3780  CZ  PHE A 451     5164   5502   6854    -21   -642    588       C  
ATOM   3781  N   GLU A 452      21.226  -1.948 128.923  1.00 55.29           N  
ANISOU 3781  N   GLU A 452     5827   8138   7040   -675   -856   -197       N  
ATOM   3782  CA  GLU A 452      20.917  -0.651 129.509  1.00 48.06           C  
ANISOU 3782  CA  GLU A 452     4913   7316   6031   -861   -755   -492       C  
ATOM   3783  C   GLU A 452      21.928  -0.206 130.550  1.00 56.23           C  
ANISOU 3783  C   GLU A 452     5684   8759   6920   -999   -840   -710       C  
ATOM   3784  O   GLU A 452      22.172   0.998 130.685  1.00 37.82           O  
ANISOU 3784  O   GLU A 452     3323   6439   4607  -1189   -706  -1037       O  
ATOM   3785  CB  GLU A 452      19.530  -0.672 130.162  1.00 36.72           C  
ANISOU 3785  CB  GLU A 452     3606   5921   4425   -850   -763   -408       C  
ATOM   3786  CG  GLU A 452      18.381  -0.727 129.187  1.00 36.23           C  
ANISOU 3786  CG  GLU A 452     3791   5482   4492   -765   -646   -290       C  
ATOM   3787  CD  GLU A 452      18.094  -2.132 128.706  1.00 40.72           C  
ANISOU 3787  CD  GLU A 452     4421   5942   5109   -593   -749     41       C  
ATOM   3788  OE1 GLU A 452      18.810  -3.063 129.128  1.00 50.22           O  
ANISOU 3788  OE1 GLU A 452     5489   7332   6258   -521   -897    199       O  
ATOM   3789  OE2 GLU A 452      17.153  -2.310 127.908  1.00 48.82           O1-
ANISOU 3789  OE2 GLU A 452     5627   6698   6225   -526   -677    142       O1-
ATOM   3790  N   PHE A 453      22.519  -1.138 131.294  1.00 49.57           N  
ANISOU 3790  N   PHE A 453     4648   8258   5929   -908  -1054   -542       N  
ATOM   3791  CA  PHE A 453      23.312  -0.768 132.456  1.00 51.46           C  
ANISOU 3791  CA  PHE A 453     4623   8972   5959  -1030  -1172   -736       C  
ATOM   3792  C   PHE A 453      24.802  -1.022 132.294  1.00 57.29           C  
ANISOU 3792  C   PHE A 453     5096   9895   6777  -1012  -1263   -784       C  
ATOM   3793  O   PHE A 453      25.563  -0.760 133.232  1.00 63.32           O  
ANISOU 3793  O   PHE A 453     5598  11099   7360  -1110  -1384   -953       O  
ATOM   3794  CB  PHE A 453      22.781  -1.493 133.694  1.00 58.75           C  
ANISOU 3794  CB  PHE A 453     5503  10245   6572   -946  -1357   -526       C  
ATOM   3795  CG  PHE A 453      21.352  -1.164 134.001  1.00 59.00           C  
ANISOU 3795  CG  PHE A 453     5754  10157   6505   -990  -1262   -519       C  
ATOM   3796  CD1 PHE A 453      20.880   0.125 133.818  1.00 61.33           C  
ANISOU 3796  CD1 PHE A 453     6158  10281   6865  -1169  -1062   -832       C  
ATOM   3797  CD2 PHE A 453      20.478  -2.134 134.453  1.00 41.62           C  
ANISOU 3797  CD2 PHE A 453     3651   8001   4161   -848  -1352   -200       C  
ATOM   3798  CE1 PHE A 453      19.565   0.443 134.093  1.00 60.39           C  
ANISOU 3798  CE1 PHE A 453     6221  10059   6665  -1190   -968   -827       C  
ATOM   3799  CE2 PHE A 453      19.162  -1.819 134.736  1.00 41.31           C  
ANISOU 3799  CE2 PHE A 453     3789   7870   4038   -894  -1256   -207       C  
ATOM   3800  CZ  PHE A 453      18.705  -0.531 134.551  1.00 50.07           C  
ANISOU 3800  CZ  PHE A 453     4986   8827   5210  -1056  -1070   -520       C  
ATOM   3801  N   ASN A 454      25.243  -1.502 131.134  1.00 47.14           N  
ANISOU 3801  N   ASN A 454     3855   8307   5748   -895  -1206   -659       N  
ATOM   3802  CA  ASN A 454      26.671  -1.626 130.898  1.00 46.75           C  
ANISOU 3802  CA  ASN A 454     3543   8413   5806   -890  -1258   -741       C  
ATOM   3803  C   ASN A 454      27.322  -0.250 130.898  1.00 62.09           C  
ANISOU 3803  C   ASN A 454     5363  10418   7810  -1168  -1114  -1183       C  
ATOM   3804  O   ASN A 454      26.733   0.745 130.468  1.00 61.10           O  
ANISOU 3804  O   ASN A 454     5439   9998   7780  -1320   -898  -1383       O  
ATOM   3805  CB  ASN A 454      26.935  -2.340 129.570  1.00 66.30           C  
ANISOU 3805  CB  ASN A 454     6124  10506   8559   -722  -1182   -543       C  
ATOM   3806  CG  ASN A 454      26.800  -1.419 128.366  1.00 68.55           C  
ANISOU 3806  CG  ASN A 454     6599  10358   9089   -849   -917   -746       C  
ATOM   3807  OD1 ASN A 454      27.730  -0.691 128.014  1.00 70.41           O  
ANISOU 3807  OD1 ASN A 454     6701  10596   9456   -993   -807  -1006       O  
ATOM   3808  ND2 ASN A 454      25.635  -1.446 127.733  1.00 51.34           N  
ANISOU 3808  ND2 ASN A 454     4727   7813   6965   -796   -808   -623       N  
ATOM   3809  N   THR A 455      28.538  -0.195 131.420  1.00 71.86           N  
ANISOU 3809  N   THR A 455     6263  12052   8989  -1233  -1231  -1337       N  
ATOM   3810  CA  THR A 455      29.439   0.921 131.180  1.00 62.66           C  
ANISOU 3810  CA  THR A 455     5023  10830   7954  -1450  -1049  -1698       C  
ATOM   3811  C   THR A 455      30.637   0.428 130.381  1.00 61.57           C  
ANISOU 3811  C   THR A 455     4699  10664   8033  -1362  -1057  -1651       C  
ATOM   3812  O   THR A 455      31.791   0.729 130.689  1.00 63.49           O  
ANISOU 3812  O   THR A 455     4745  11110   8268  -1427  -1064  -1809       O  
ATOM   3813  CB  THR A 455      29.862   1.591 132.486  1.00 66.12           C  
ANISOU 3813  CB  THR A 455     5356  11619   8146  -1578  -1088  -1911       C  
ATOM   3814  OG1 THR A 455      30.321   0.597 133.410  1.00 79.34           O  
ANISOU 3814  OG1 THR A 455     6856  13684   9607  -1388  -1348  -1677       O  
ATOM   3815  CG2 THR A 455      28.684   2.337 133.100  1.00 66.50           C  
ANISOU 3815  CG2 THR A 455     5606  11622   8037  -1704   -997  -2034       C  
ATOM   3816  N   VAL A 456      30.354  -0.377 129.358  1.00 65.13           N  
ANISOU 3816  N   VAL A 456     5261  10816   8669  -1181  -1036  -1398       N  
ATOM   3817  CA  VAL A 456      31.365  -0.879 128.437  1.00 49.73           C  
ANISOU 3817  CA  VAL A 456     3186   8753   6955  -1075   -998  -1333       C  
ATOM   3818  C   VAL A 456      31.334  -0.023 127.177  1.00 48.60           C  
ANISOU 3818  C   VAL A 456     3253   8130   7082  -1219   -686  -1519       C  
ATOM   3819  O   VAL A 456      32.325   0.638 126.846  1.00 69.51           O  
ANISOU 3819  O   VAL A 456     5724  10809   9877  -1391   -557  -1794       O  
ATOM   3820  CB  VAL A 456      31.146  -2.371 128.125  1.00 49.49           C  
ANISOU 3820  CB  VAL A 456     3236   8619   6948   -739  -1132   -891       C  
ATOM   3821  CG1 VAL A 456      32.270  -2.904 127.250  1.00 55.58           C  
ANISOU 3821  CG1 VAL A 456     3850   9309   7958   -621  -1091   -841       C  
ATOM   3822  CG2 VAL A 456      31.054  -3.175 129.421  1.00 54.64           C  
ANISOU 3822  CG2 VAL A 456     3727   9721   7313   -588  -1416   -676       C  
ATOM   3823  N   PHE A 457      30.203  -0.018 126.466  1.00 43.64           N  
ANISOU 3823  N   PHE A 457     2998   7069   6516  -1152   -556  -1371       N  
ATOM   3824  CA  PHE A 457      30.026   0.950 125.393  1.00 55.54           C  
ANISOU 3824  CA  PHE A 457     4733   8144   8226  -1291   -255  -1547       C  
ATOM   3825  C   PHE A 457      29.183   2.151 125.799  1.00 55.59           C  
ANISOU 3825  C   PHE A 457     4910   8063   8147  -1489   -117  -1768       C  
ATOM   3826  O   PHE A 457      29.333   3.222 125.195  1.00 54.58           O  
ANISOU 3826  O   PHE A 457     4888   7675   8172  -1665    147  -2006       O  
ATOM   3827  CB  PHE A 457      29.414   0.306 124.136  1.00 52.31           C  
ANISOU 3827  CB  PHE A 457     4624   7291   7962  -1092   -164  -1273       C  
ATOM   3828  CG  PHE A 457      28.316  -0.713 124.395  1.00 44.55           C  
ANISOU 3828  CG  PHE A 457     3802   6284   6840   -879   -334   -941       C  
ATOM   3829  CD1 PHE A 457      28.618  -2.044 124.640  1.00 44.36           C  
ANISOU 3829  CD1 PHE A 457     3652   6426   6778   -667   -537   -671       C  
ATOM   3830  CD2 PHE A 457      26.979  -0.342 124.324  1.00 49.96           C  
ANISOU 3830  CD2 PHE A 457     4772   6757   7454   -887   -267   -895       C  
ATOM   3831  CE1 PHE A 457      27.609  -2.979 124.845  1.00 39.86           C  
ANISOU 3831  CE1 PHE A 457     3244   5799   6101   -494   -658   -374       C  
ATOM   3832  CE2 PHE A 457      25.968  -1.273 124.527  1.00 45.45           C  
ANISOU 3832  CE2 PHE A 457     4336   6162   6770   -716   -404   -609       C  
ATOM   3833  CZ  PHE A 457      26.283  -2.590 124.787  1.00 37.86           C  
ANISOU 3833  CZ  PHE A 457     3259   5353   5775   -533   -592   -354       C  
ATOM   3834  N   ASN A 458      28.337   2.029 126.824  1.00 61.95           N  
ANISOU 3834  N   ASN A 458     5744   9077   8718  -1467   -268  -1702       N  
ATOM   3835  CA  ASN A 458      27.414   3.106 127.155  1.00 65.53           C  
ANISOU 3835  CA  ASN A 458     6388   9410   9102  -1621   -121  -1886       C  
ATOM   3836  C   ASN A 458      27.962   4.036 128.233  1.00 58.18           C  
ANISOU 3836  C   ASN A 458     5231   8826   8051  -1889   -114  -2260       C  
ATOM   3837  O   ASN A 458      28.545   3.597 129.226  1.00 50.92           O  
ANISOU 3837  O   ASN A 458     4043   8361   6944  -1884   -336  -2265       O  
ATOM   3838  CB  ASN A 458      26.051   2.541 127.580  1.00 64.50           C  
ANISOU 3838  CB  ASN A 458     6446   9266   8796  -1462   -243  -1626       C  
ATOM   3839  CG  ASN A 458      25.198   2.174 126.397  1.00 68.87           C  
ANISOU 3839  CG  ASN A 458     7303   9377   9487  -1288   -143  -1382       C  
ATOM   3840  OD1 ASN A 458      25.405   2.707 125.308  1.00 78.29           O  
ANISOU 3840  OD1 ASN A 458     8630  10233  10882  -1319     70  -1458       O  
ATOM   3841  ND2 ASN A 458      24.202   1.340 126.608  1.00 66.12           N  
ANISOU 3841  ND2 ASN A 458     7071   9031   9021  -1121   -278  -1107       N  
ATOM   3842  N   ASP A 459      27.748   5.335 128.028  1.00 53.21           N  
ANISOU 3842  N   ASP A 459     4774   7941   7502  -2065    162  -2518       N  
ATOM   3843  CA  ASP A 459      28.181   6.352 128.974  1.00 57.01           C  
ANISOU 3843  CA  ASP A 459     5185   8630   7847  -2230    242  -2800       C  
ATOM   3844  C   ASP A 459      27.364   6.280 130.262  1.00 71.57           C  
ANISOU 3844  C   ASP A 459     7014  10773   9407  -2234     86  -2794       C  
ATOM   3845  O   ASP A 459      26.271   5.707 130.312  1.00 72.43           O  
ANISOU 3845  O   ASP A 459     7235  10840   9444  -2130    -18  -2598       O  
ATOM   3846  CB  ASP A 459      28.041   7.755 128.370  1.00 69.39           C  
ANISOU 3846  CB  ASP A 459     6995   9797   9573  -2348    614  -3009       C  
ATOM   3847  CG  ASP A 459      29.030   8.016 127.246  1.00 85.63           C  
ANISOU 3847  CG  ASP A 459     9056  11611  11867  -2366    801  -3054       C  
ATOM   3848  OD1 ASP A 459      30.019   7.255 127.117  1.00 96.10           O  
ANISOU 3848  OD1 ASP A 459    10148  13138  13229  -2334    650  -3004       O  
ATOM   3849  OD2 ASP A 459      28.814   8.979 126.486  1.00 88.72           O1-
ANISOU 3849  OD2 ASP A 459     9684  11623  12402  -2390   1106  -3117       O1-
ATOM   3850  N   GLN A 460      27.917   6.887 131.316  1.00 76.39           N  
ANISOU 3850  N   GLN A 460     7482  11694   9850  -2363     84  -3020       N  
ATOM   3851  CA  GLN A 460      27.192   7.017 132.578  1.00 81.10           C  
ANISOU 3851  CA  GLN A 460     8079  12563  10172  -2391     -8  -3059       C  
ATOM   3852  C   GLN A 460      25.878   7.764 132.371  1.00 77.02           C  
ANISOU 3852  C   GLN A 460     7853  11707   9705  -2425    203  -3109       C  
ATOM   3853  O   GLN A 460      24.828   7.376 132.912  1.00 65.11           O  
ANISOU 3853  O   GLN A 460     6418  10288   8031  -2357     92  -2981       O  
ATOM   3854  CB  GLN A 460      28.070   7.747 133.590  1.00 93.61           C  
ANISOU 3854  CB  GLN A 460     9478  14477  11612  -2554     24  -3348       C  
ATOM   3855  CG  GLN A 460      27.749   7.465 135.041  1.00100.13           C  
ANISOU 3855  CG  GLN A 460    10198  15744  12104  -2544   -168  -3331       C  
ATOM   3856  CD  GLN A 460      29.003   7.218 135.856  1.00113.69           C  
ANISOU 3856  CD  GLN A 460    11616  17922  13660  -2572   -334  -3411       C  
ATOM   3857  OE1 GLN A 460      29.561   6.122 135.839  1.00115.43           O  
ANISOU 3857  OE1 GLN A 460    11677  18346  13834  -2408   -576  -3172       O  
ATOM   3858  NE2 GLN A 460      29.460   8.244 136.566  1.00123.78           N  
ANISOU 3858  NE2 GLN A 460    12812  19362  14858  -2773   -193  -3747       N  
ATOM   3859  N   ARG A 461      25.949   8.880 131.633  1.00 92.11           N  
ANISOU 3859  N   ARG A 461     9928  13237  11833  -2519    524  -3288       N  
ATOM   3860  CA  ARG A 461      24.790   9.566 131.076  1.00 89.84           C  
ANISOU 3860  CA  ARG A 461     9943  12527  11664  -2490    759  -3272       C  
ATOM   3861  C   ARG A 461      23.718   8.579 130.638  1.00 76.81           C  
ANISOU 3861  C   ARG A 461     8422  10756  10006  -2319    605  -2980       C  
ATOM   3862  O   ARG A 461      22.567   8.629 131.094  1.00 73.42           O  
ANISOU 3862  O   ARG A 461     8114  10320   9460  -2287    595  -2943       O  
ATOM   3863  CB  ARG A 461      25.267  10.413 129.888  1.00103.74           C  
ANISOU 3863  CB  ARG A 461    11847  13869  13702  -2511   1066  -3337       C  
ATOM   3864  CG  ARG A 461      24.293  11.443 129.354  1.00111.05           C  
ANISOU 3864  CG  ARG A 461    13069  14372  14751  -2470   1367  -3330       C  
ATOM   3865  CD  ARG A 461      23.279  11.879 130.377  1.00116.72           C  
ANISOU 3865  CD  ARG A 461    13842  15198  15308  -2509   1382  -3415       C  
ATOM   3866  NE  ARG A 461      22.345  12.858 129.837  1.00125.80           N  
ANISOU 3866  NE  ARG A 461    15259  15949  16590  -2439   1663  -3372       N  
ATOM   3867  CZ  ARG A 461      21.201  12.538 129.243  1.00116.63           C  
ANISOU 3867  CZ  ARG A 461    14308  14543  15464  -2250   1650  -3137       C  
ATOM   3868  NH1 ARG A 461      20.857  11.264 129.111  1.00117.94           N  
ANISOU 3868  NH1 ARG A 461    14453  14802  15555  -2143   1389  -2954       N  
ATOM   3869  NH2 ARG A 461      20.403  13.490 128.781  1.00105.56           N  
ANISOU 3869  NH2 ARG A 461    13124  12817  14169  -2165   1893  -3075       N  
ATOM   3870  N   THR A 462      24.103   7.661 129.752  1.00 61.05           N  
ANISOU 3870  N   THR A 462     6387   8672   8137  -2214    492  -2781       N  
ATOM   3871  CA  THR A 462      23.141   6.770 129.120  1.00 59.29           C  
ANISOU 3871  CA  THR A 462     6328   8259   7942  -2000    396  -2449       C  
ATOM   3872  C   THR A 462      22.593   5.752 130.109  1.00 59.83           C  
ANISOU 3872  C   THR A 462     6300   8690   7743  -1877    109  -2228       C  
ATOM   3873  O   THR A 462      21.396   5.445 130.084  1.00 64.05           O  
ANISOU 3873  O   THR A 462     7016   9107   8215  -1731     90  -2021       O  
ATOM   3874  CB  THR A 462      23.795   6.078 127.924  1.00 58.18           C  
ANISOU 3874  CB  THR A 462     6191   7920   7994  -1866    381  -2248       C  
ATOM   3875  OG1 THR A 462      24.439   7.064 127.101  1.00 71.07           O  
ANISOU 3875  OG1 THR A 462     7890   9255   9859  -2010    661  -2476       O  
ATOM   3876  CG2 THR A 462      22.765   5.350 127.097  1.00 45.88           C  
ANISOU 3876  CG2 THR A 462     4871   6085   6476  -1610    349  -1893       C  
ATOM   3877  N   VAL A 463      23.448   5.210 130.981  1.00 54.13           N  
ANISOU 3877  N   VAL A 463     5290   8419   6857  -1928   -112  -2260       N  
ATOM   3878  CA  VAL A 463      22.972   4.249 131.978  1.00 54.38           C  
ANISOU 3878  CA  VAL A 463     5240   8807   6616  -1807   -372  -2034       C  
ATOM   3879  C   VAL A 463      21.899   4.882 132.858  1.00 65.22           C  
ANISOU 3879  C   VAL A 463     6721  10255   7805  -1891   -306  -2158       C  
ATOM   3880  O   VAL A 463      20.845   4.282 133.130  1.00 66.98           O  
ANISOU 3880  O   VAL A 463     7062  10481   7905  -1745   -386  -1911       O  
ATOM   3881  CB  VAL A 463      24.142   3.713 132.822  1.00 61.77           C  
ANISOU 3881  CB  VAL A 463     5834  10250   7385  -1847   -608  -2072       C  
ATOM   3882  CG1 VAL A 463      23.672   2.565 133.681  1.00 64.86           C  
ANISOU 3882  CG1 VAL A 463     6176  10956   7514  -1670   -865  -1755       C  
ATOM   3883  CG2 VAL A 463      25.280   3.261 131.929  1.00 62.11           C  
ANISOU 3883  CG2 VAL A 463     5749  10209   7641  -1784   -631  -2007       C  
ATOM   3884  N   PHE A 464      22.149   6.110 133.315  1.00 64.41           N  
ANISOU 3884  N   PHE A 464     6581  10202   7689  -2133   -139  -2554       N  
ATOM   3885  CA  PHE A 464      21.192   6.750 134.212  1.00 62.72           C  
ANISOU 3885  CA  PHE A 464     6471  10059   7302  -2198    -51  -2681       C  
ATOM   3886  C   PHE A 464      19.907   7.124 133.483  1.00 52.38           C  
ANISOU 3886  C   PHE A 464     5458   8310   6136  -2106    142  -2599       C  
ATOM   3887  O   PHE A 464      18.807   7.000 134.043  1.00 48.39           O  
ANISOU 3887  O   PHE A 464     5047   7863   5477  -2036    122  -2502       O  
ATOM   3888  CB  PHE A 464      21.824   7.974 134.868  1.00 63.23           C  
ANISOU 3888  CB  PHE A 464     6475  10203   7346  -2376    137  -3018       C  
ATOM   3889  CG  PHE A 464      22.768   7.636 135.982  1.00 72.03           C  
ANISOU 3889  CG  PHE A 464     7329  11812   8227  -2414    -53  -3056       C  
ATOM   3890  CD1 PHE A 464      22.540   6.529 136.780  1.00 83.40           C  
ANISOU 3890  CD1 PHE A 464     8667  13617   9405  -2286   -331  -2807       C  
ATOM   3891  CD2 PHE A 464      23.879   8.421 136.234  1.00 66.19           C  
ANISOU 3891  CD2 PHE A 464     6452  11171   7526  -2565     59  -3327       C  
ATOM   3892  CE1 PHE A 464      23.400   6.209 137.813  1.00 85.66           C  
ANISOU 3892  CE1 PHE A 464     8731  14346   9471  -2290   -496  -2815       C  
ATOM   3893  CE2 PHE A 464      24.747   8.107 137.267  1.00 67.12           C  
ANISOU 3893  CE2 PHE A 464     6324  11759   7418  -2593   -120  -3368       C  
ATOM   3894  CZ  PHE A 464      24.505   6.997 138.057  1.00 78.33           C  
ANISOU 3894  CZ  PHE A 464     7654  13530   8576  -2446   -400  -3104       C  
ATOM   3895  N   ALA A 465      20.025   7.587 132.235  1.00 49.67           N  
ANISOU 3895  N   ALA A 465     5270   7523   6080  -2073    342  -2605       N  
ATOM   3896  CA  ALA A 465      18.831   7.844 131.441  1.00 49.50           C  
ANISOU 3896  CA  ALA A 465     5529   7089   6189  -1915    506  -2453       C  
ATOM   3897  C   ALA A 465      18.005   6.578 131.251  1.00 45.61           C  
ANISOU 3897  C   ALA A 465     5088   6623   5617  -1672    303  -2045       C  
ATOM   3898  O   ALA A 465      16.771   6.630 131.306  1.00 50.28           O  
ANISOU 3898  O   ALA A 465     5827   7113   6166  -1570    351  -1940       O  
ATOM   3899  CB  ALA A 465      19.220   8.441 130.091  1.00 51.23           C  
ANISOU 3899  CB  ALA A 465     5897   6864   6704  -1902    732  -2491       C  
ATOM   3900  N   ASN A 466      18.666   5.434 131.053  1.00 40.78           N  
ANISOU 3900  N   ASN A 466     4350   6153   4993  -1582     89  -1823       N  
ATOM   3901  CA  ASN A 466      17.950   4.168 130.926  1.00 35.25           C  
ANISOU 3901  CA  ASN A 466     3694   5475   4223  -1375    -91  -1450       C  
ATOM   3902  C   ASN A 466      17.203   3.830 132.211  1.00 52.71           C  
ANISOU 3902  C   ASN A 466     5850   8017   6159  -1383   -212  -1396       C  
ATOM   3903  O   ASN A 466      16.034   3.423 132.178  1.00 60.14           O  
ANISOU 3903  O   ASN A 466     6915   8878   7059  -1265   -221  -1202       O  
ATOM   3904  CB  ASN A 466      18.931   3.049 130.570  1.00 44.56           C  
ANISOU 3904  CB  ASN A 466     4739   6747   5446  -1287   -274  -1250       C  
ATOM   3905  CG  ASN A 466      19.213   2.963 129.082  1.00 52.48           C  
ANISOU 3905  CG  ASN A 466     5863   7364   6713  -1194   -171  -1162       C  
ATOM   3906  OD1 ASN A 466      18.368   3.299 128.252  1.00 61.57           O  
ANISOU 3906  OD1 ASN A 466     7227   8189   7979  -1119    -29  -1110       O  
ATOM   3907  ND2 ASN A 466      20.406   2.501 128.738  1.00 51.84           N  
ANISOU 3907  ND2 ASN A 466     5640   7337   6719  -1190   -243  -1141       N  
ATOM   3908  N   PHE A 467      17.870   3.988 133.359  1.00 59.57           N  
ANISOU 3908  N   PHE A 467     6525   9282   6828  -1527   -306  -1573       N  
ATOM   3909  CA  PHE A 467      17.211   3.687 134.632  1.00 64.36           C  
ANISOU 3909  CA  PHE A 467     7081  10232   7141  -1541   -414  -1528       C  
ATOM   3910  C   PHE A 467      15.984   4.569 134.844  1.00 65.64           C  
ANISOU 3910  C   PHE A 467     7407  10246   7286  -1582   -217  -1667       C  
ATOM   3911  O   PHE A 467      14.899   4.080 135.195  1.00 59.37           O  
ANISOU 3911  O   PHE A 467     6687   9494   6377  -1487   -253  -1479       O  
ATOM   3912  CB  PHE A 467      18.186   3.854 135.797  1.00 43.09           C  
ANISOU 3912  CB  PHE A 467     4145   8012   4215  -1702   -537  -1737       C  
ATOM   3913  CG  PHE A 467      17.594   3.492 137.130  1.00 67.83           C  
ANISOU 3913  CG  PHE A 467     7224  11536   7010  -1711   -656  -1675       C  
ATOM   3914  CD1 PHE A 467      16.958   2.276 137.308  1.00 65.60           C  
ANISOU 3914  CD1 PHE A 467     6987  11317   6620  -1528   -801  -1287       C  
ATOM   3915  CD2 PHE A 467      17.659   4.370 138.200  1.00 72.86           C  
ANISOU 3915  CD2 PHE A 467     7778  12467   7437  -1912   -603  -2010       C  
ATOM   3916  CE1 PHE A 467      16.400   1.936 138.529  1.00 69.48           C  
ANISOU 3916  CE1 PHE A 467     7443  12160   6794  -1536   -889  -1213       C  
ATOM   3917  CE2 PHE A 467      17.101   4.037 139.424  1.00 71.92           C  
ANISOU 3917  CE2 PHE A 467     7642  12657   7028  -1881   -673  -1908       C  
ATOM   3918  CZ  PHE A 467      16.473   2.821 139.588  1.00 71.32           C  
ANISOU 3918  CZ  PHE A 467     7601  12678   6819  -1713   -831  -1527       C  
ATOM   3919  N   TYR A 468      16.143   5.879 134.639  1.00 59.73           N  
ANISOU 3919  N   TYR A 468     6716   9318   6661  -1724      9  -2000       N  
ATOM   3920  CA  TYR A 468      15.033   6.811 134.815  1.00 56.25           C  
ANISOU 3920  CA  TYR A 468     6433   8711   6228  -1746    226  -2150       C  
ATOM   3921  C   TYR A 468      13.895   6.507 133.841  1.00 61.74           C  
ANISOU 3921  C   TYR A 468     7321   9059   7079  -1531    287  -1881       C  
ATOM   3922  O   TYR A 468      12.713   6.577 134.207  1.00 62.79           O  
ANISOU 3922  O   TYR A 468     7530   9197   7129  -1468    340  -1830       O  
ATOM   3923  CB  TYR A 468      15.561   8.238 134.647  1.00 66.00           C  
ANISOU 3923  CB  TYR A 468     7707   9761   7610  -1930    482  -2545       C  
ATOM   3924  CG  TYR A 468      14.579   9.380 134.845  1.00 66.72           C  
ANISOU 3924  CG  TYR A 468     7962   9652   7738  -1963    753  -2753       C  
ATOM   3925  CD1 TYR A 468      14.209   9.805 136.116  1.00 61.30           C  
ANISOU 3925  CD1 TYR A 468     7219   9251   6822  -2098    787  -2974       C  
ATOM   3926  CD2 TYR A 468      14.076  10.075 133.755  1.00 64.57           C  
ANISOU 3926  CD2 TYR A 468     7899   8906   7727  -1855    988  -2737       C  
ATOM   3927  CE1 TYR A 468      13.329  10.869 136.288  1.00 57.16           C  
ANISOU 3927  CE1 TYR A 468     6844   8524   6349  -2119   1058  -3176       C  
ATOM   3928  CE2 TYR A 468      13.199  11.136 133.917  1.00 69.98           C  
ANISOU 3928  CE2 TYR A 468     8734   9393   8463  -1855   1250  -2914       C  
ATOM   3929  CZ  TYR A 468      12.827  11.530 135.183  1.00 63.17           C  
ANISOU 3929  CZ  TYR A 468     7812   8798   7391  -1988   1291  -3138       C  
ATOM   3930  OH  TYR A 468      11.954  12.586 135.343  1.00 57.88           O  
ANISOU 3930  OH  TYR A 468     7268   7912   6813  -1939   1544  -3224       O  
ATOM   3931  N   ASP A 469      14.233   6.129 132.604  1.00 62.12           N  
ANISOU 3931  N   ASP A 469     7433   8832   7339  -1415    275  -1711       N  
ATOM   3932  CA  ASP A 469      13.207   5.816 131.614  1.00 50.92           C  
ANISOU 3932  CA  ASP A 469     6180   7115   6051  -1216    316  -1469       C  
ATOM   3933  C   ASP A 469      12.431   4.563 131.996  1.00 49.09           C  
ANISOU 3933  C   ASP A 469     5912   7070   5670  -1105    121  -1171       C  
ATOM   3934  O   ASP A 469      11.226   4.463 131.731  1.00 40.32           O  
ANISOU 3934  O   ASP A 469     4901   5843   4576   -991    167  -1046       O  
ATOM   3935  CB  ASP A 469      13.846   5.654 130.235  1.00 36.48           C  
ANISOU 3935  CB  ASP A 469     4421   4987   4453  -1135    340  -1370       C  
ATOM   3936  CG  ASP A 469      14.326   6.970 129.662  1.00 48.10           C  
ANISOU 3936  CG  ASP A 469     6033   6123   6120  -1170    612  -1582       C  
ATOM   3937  OD1 ASP A 469      13.920   8.026 130.185  1.00 50.77           O  
ANISOU 3937  OD1 ASP A 469     6437   6418   6437  -1225    790  -1780       O  
ATOM   3938  OD2 ASP A 469      15.111   6.949 128.689  1.00 68.35           O1-
ANISOU 3938  OD2 ASP A 469     8652   8456   8861  -1138    665  -1548       O1-
ATOM   3939  N   ALA A 470      13.108   3.588 132.606  1.00 41.51           N  
ANISOU 3939  N   ALA A 470     4805   6398   4567  -1132    -87  -1050       N  
ATOM   3940  CA  ALA A 470      12.412   2.404 133.101  1.00 42.51           C  
ANISOU 3940  CA  ALA A 470     4906   6703   4541  -1045   -245   -770       C  
ATOM   3941  C   ALA A 470      11.484   2.762 134.257  1.00 52.17           C  
ANISOU 3941  C   ALA A 470     6120   8149   5553  -1109   -196   -859       C  
ATOM   3942  O   ALA A 470      10.314   2.349 134.291  1.00 42.26           O  
ANISOU 3942  O   ALA A 470     4929   6864   4264  -1027   -184   -700       O  
ATOM   3943  CB  ALA A 470      13.425   1.347 133.534  1.00 43.52           C  
ANISOU 3943  CB  ALA A 470     4888   7085   4564  -1040   -458   -613       C  
ATOM   3944  N   MET A 471      11.990   3.538 135.215  1.00 57.62           N  
ANISOU 3944  N   MET A 471     6723   9076   6095  -1266   -157  -1133       N  
ATOM   3945  CA  MET A 471      11.164   3.913 136.356  1.00 51.19           C  
ANISOU 3945  CA  MET A 471     5899   8489   5061  -1338    -96  -1245       C  
ATOM   3946  C   MET A 471       9.980   4.790 135.955  1.00 48.24           C  
ANISOU 3946  C   MET A 471     5669   7845   4815  -1290    129  -1348       C  
ATOM   3947  O   MET A 471       8.999   4.849 136.700  1.00 54.90           O  
ANISOU 3947  O   MET A 471     6522   8827   5511  -1294    181  -1355       O  
ATOM   3948  CB  MET A 471      12.015   4.607 137.422  1.00 52.07           C  
ANISOU 3948  CB  MET A 471     5883   8919   4983  -1534    -95  -1556       C  
ATOM   3949  CG  MET A 471      13.131   3.734 137.990  1.00 45.69           C  
ANISOU 3949  CG  MET A 471     4898   8464   3997  -1561   -339  -1447       C  
ATOM   3950  SD  MET A 471      12.613   2.040 138.332  1.00 48.73           S  
ANISOU 3950  SD  MET A 471     5272   9022   4220  -1392   -550   -973       S  
ATOM   3951  CE  MET A 471      11.542   2.279 139.749  1.00 63.80           C  
ANISOU 3951  CE  MET A 471     7188  11245   5805  -1472   -490  -1048       C  
ATOM   3952  N   ILE A 472      10.027   5.445 134.790  1.00 38.73           N  
ANISOU 3952  N   ILE A 472     4575   6265   3875  -1229    268  -1411       N  
ATOM   3953  CA  ILE A 472       8.838   6.161 134.318  1.00 38.03           C  
ANISOU 3953  CA  ILE A 472     4621   5920   3909  -1127    465  -1446       C  
ATOM   3954  C   ILE A 472       7.725   5.180 133.956  1.00 55.34           C  
ANISOU 3954  C   ILE A 472     6837   8089   6101   -968    373  -1136       C  
ATOM   3955  O   ILE A 472       6.565   5.352 134.353  1.00 60.78           O  
ANISOU 3955  O   ILE A 472     7542   8826   6727   -925    455  -1133       O  
ATOM   3956  CB  ILE A 472       9.177   7.074 133.128  1.00 40.49           C  
ANISOU 3956  CB  ILE A 472     5058   5838   4488  -1077    639  -1555       C  
ATOM   3957  CG1 ILE A 472      10.148   8.176 133.546  1.00 46.61           C  
ANISOU 3957  CG1 ILE A 472     5817   6613   5281  -1266    785  -1908       C  
ATOM   3958  CG2 ILE A 472       7.899   7.673 132.568  1.00 37.15           C  
ANISOU 3958  CG2 ILE A 472     4766   5167   4183   -916    815  -1525       C  
ATOM   3959  CD1 ILE A 472       9.505   9.278 134.346  1.00 42.14           C  
ANISOU 3959  CD1 ILE A 472     5294   6065   4652  -1341   1003  -2181       C  
ATOM   3960  N   CYS A 473       8.057   4.162 133.158  1.00 63.45           N  
ANISOU 3960  N   CYS A 473     7863   9033   7213   -886    220   -888       N  
ATOM   3961  CA  CYS A 473       7.124   3.074 132.877  1.00 54.29           C  
ANISOU 3961  CA  CYS A 473     6707   7878   6042   -776    119   -605       C  
ATOM   3962  C   CYS A 473       6.570   2.489 134.171  1.00 46.07           C  
ANISOU 3962  C   CYS A 473     5582   7167   4757   -842     54   -537       C  
ATOM   3963  O   CYS A 473       5.362   2.223 134.294  1.00 58.23           O  
ANISOU 3963  O   CYS A 473     7128   8731   6264   -790     90   -441       O  
ATOM   3964  CB  CYS A 473       7.853   1.998 132.064  1.00 63.54           C  
ANISOU 3964  CB  CYS A 473     7876   8957   7309   -723    -40   -387       C  
ATOM   3965  SG  CYS A 473       6.821   0.966 131.006  1.00 62.02           S  
ANISOU 3965  SG  CYS A 473     7744   8587   7232   -579    -98   -107       S  
ATOM   3966  N   VAL A 474       7.447   2.315 135.160  1.00 43.13           N  
ANISOU 3966  N   VAL A 474     5120   7068   4200   -959    -36   -593       N  
ATOM   3967  CA  VAL A 474       7.045   1.736 136.440  1.00 54.15           C  
ANISOU 3967  CA  VAL A 474     6443   8803   5328  -1020   -101   -512       C  
ATOM   3968  C   VAL A 474       6.017   2.625 137.140  1.00 61.95           C  
ANISOU 3968  C   VAL A 474     7447   9873   6220  -1064     74   -705       C  
ATOM   3969  O   VAL A 474       4.948   2.159 137.558  1.00 59.26           O  
ANISOU 3969  O   VAL A 474     7100   9630   5787  -1039     95   -579       O  
ATOM   3970  CB  VAL A 474       8.288   1.500 137.317  1.00 47.65           C  
ANISOU 3970  CB  VAL A 474     5512   8283   4308  -1121   -238   -553       C  
ATOM   3971  CG1 VAL A 474       7.887   1.254 138.759  1.00 52.27           C  
ANISOU 3971  CG1 VAL A 474     6037   9251   4575  -1198   -264   -540       C  
ATOM   3972  CG2 VAL A 474       9.096   0.334 136.777  1.00 53.58           C  
ANISOU 3972  CG2 VAL A 474     6236   8993   5129  -1042   -418   -287       C  
ATOM   3973  N   ALA A 475       6.332   3.915 137.290  1.00 56.57           N  
ANISOU 3973  N   ALA A 475     6783   9144   5566  -1138    221  -1024       N  
ATOM   3974  CA  ALA A 475       5.418   4.844 137.948  1.00 52.34           C  
ANISOU 3974  CA  ALA A 475     6269   8661   4957  -1174    415  -1237       C  
ATOM   3975  C   ALA A 475       4.093   4.953 137.208  1.00 48.94           C  
ANISOU 3975  C   ALA A 475     5904   7996   4695  -1019    531  -1138       C  
ATOM   3976  O   ALA A 475       3.040   5.126 137.835  1.00 50.98           O  
ANISOU 3976  O   ALA A 475     6145   8369   4855  -1012    635  -1173       O  
ATOM   3977  CB  ALA A 475       6.077   6.218 138.067  1.00 44.85           C  
ANISOU 3977  CB  ALA A 475     5350   7632   4061  -1280    578  -1605       C  
ATOM   3978  N   TYR A 476       4.125   4.856 135.879  1.00 63.29           N  
ANISOU 3978  N   TYR A 476     7786   9507   6754   -891    514  -1019       N  
ATOM   3979  CA  TYR A 476       2.890   4.885 135.104  1.00 63.38           C  
ANISOU 3979  CA  TYR A 476     7836   9335   6909   -729    590   -909       C  
ATOM   3980  C   TYR A 476       2.008   3.685 135.422  1.00 54.38           C  
ANISOU 3980  C   TYR A 476     6624   8375   5663   -715    482   -666       C  
ATOM   3981  O   TYR A 476       0.787   3.821 135.572  1.00 46.42           O  
ANISOU 3981  O   TYR A 476     5587   7402   4648   -656    580   -660       O  
ATOM   3982  CB  TYR A 476       3.214   4.927 133.611  1.00 48.69           C  
ANISOU 3982  CB  TYR A 476     6058   7151   5290   -602    569   -820       C  
ATOM   3983  CG  TYR A 476       3.190   6.318 133.033  1.00 58.03           C  
ANISOU 3983  CG  TYR A 476     7344   8067   6638   -523    779  -1020       C  
ATOM   3984  CD1 TYR A 476       2.070   7.122 133.174  1.00 55.35           C  
ANISOU 3984  CD1 TYR A 476     7023   7679   6326   -424    962  -1114       C  
ATOM   3985  CD2 TYR A 476       4.283   6.826 132.341  1.00 71.98           C  
ANISOU 3985  CD2 TYR A 476     9192   9618   8541   -540    815  -1107       C  
ATOM   3986  CE1 TYR A 476       2.033   8.393 132.650  1.00 63.25           C  
ANISOU 3986  CE1 TYR A 476     8135   8409   7486   -328   1177  -1274       C  
ATOM   3987  CE2 TYR A 476       4.257   8.104 131.811  1.00 71.71           C  
ANISOU 3987  CE2 TYR A 476     9274   9307   8664   -466   1038  -1274       C  
ATOM   3988  CZ  TYR A 476       3.127   8.882 131.970  1.00 66.04           C  
ANISOU 3988  CZ  TYR A 476     8589   8531   7972   -353   1220  -1350       C  
ATOM   3989  OH  TYR A 476       3.083  10.154 131.448  1.00 63.18           O  
ANISOU 3989  OH  TYR A 476     8360   7869   7775   -255   1464  -1494       O  
ATOM   3990  N   LYS A 477       2.604   2.497 135.529  1.00 35.12           N  
ANISOU 3990  N   LYS A 477     4151   6044   3148   -767    297   -463       N  
ATOM   3991  CA  LYS A 477       1.771   1.347 135.869  1.00 55.69           C  
ANISOU 3991  CA  LYS A 477     6704   8794   5661   -772    227   -233       C  
ATOM   3992  C   LYS A 477       1.315   1.400 137.328  1.00 59.40           C  
ANISOU 3992  C   LYS A 477     7115   9578   5874   -877    290   -296       C  
ATOM   3993  O   LYS A 477       0.238   0.890 137.659  1.00 59.59           O  
ANISOU 3993  O   LYS A 477     7099   9704   5840   -877    329   -185       O  
ATOM   3994  CB  LYS A 477       2.510   0.044 135.555  1.00 62.41           C  
ANISOU 3994  CB  LYS A 477     7558   9635   6522   -782     41     17       C  
ATOM   3995  CG  LYS A 477       3.122  -0.659 136.726  1.00 76.22           C  
ANISOU 3995  CG  LYS A 477     9262  11667   8031   -881    -57    114       C  
ATOM   3996  CD  LYS A 477       3.158  -2.163 136.506  1.00 74.82           C  
ANISOU 3996  CD  LYS A 477     9092  11469   7868   -861   -183    430       C  
ATOM   3997  CE  LYS A 477       1.777  -2.761 136.321  1.00 53.47           C  
ANISOU 3997  CE  LYS A 477     6383   8723   5211   -850   -118    561       C  
ATOM   3998  NZ  LYS A 477       1.881  -4.241 136.186  1.00 50.67           N  
ANISOU 3998  NZ  LYS A 477     6050   8331   4872   -856   -213    854       N  
ATOM   3999  N   PHE A 478       2.099   2.046 138.195  1.00 61.75           N  
ANISOU 3999  N   PHE A 478     7404  10043   6014   -977    311   -492       N  
ATOM   4000  CA  PHE A 478       1.662   2.313 139.565  1.00 60.38           C  
ANISOU 4000  CA  PHE A 478     7186  10174   5582  -1079    398   -607       C  
ATOM   4001  C   PHE A 478       0.414   3.192 139.576  1.00 51.01           C  
ANISOU 4001  C   PHE A 478     6001   8917   4463  -1027    612   -768       C  
ATOM   4002  O   PHE A 478      -0.546   2.933 140.314  1.00 64.54           O  
ANISOU 4002  O   PHE A 478     7668  10815   6039  -1054    686   -727       O  
ATOM   4003  CB  PHE A 478       2.818   2.965 140.331  1.00 66.32           C  
ANISOU 4003  CB  PHE A 478     7923  11105   6171  -1201    381   -838       C  
ATOM   4004  CG  PHE A 478       2.499   3.359 141.755  1.00 59.15           C  
ANISOU 4004  CG  PHE A 478     6975  10531   4967  -1322    474  -1007       C  
ATOM   4005  CD1 PHE A 478       2.590   2.434 142.787  1.00 61.20           C  
ANISOU 4005  CD1 PHE A 478     7187  11135   4933  -1389    362   -833       C  
ATOM   4006  CD2 PHE A 478       2.189   4.675 142.073  1.00 54.33           C  
ANISOU 4006  CD2 PHE A 478     6386   9891   4365  -1367    683  -1346       C  
ATOM   4007  CE1 PHE A 478       2.329   2.802 144.098  1.00 64.92           C  
ANISOU 4007  CE1 PHE A 478     7627  11938   5103  -1503    449   -993       C  
ATOM   4008  CE2 PHE A 478       1.928   5.048 143.383  1.00 59.84           C  
ANISOU 4008  CE2 PHE A 478     7051  10904   4781  -1489    778  -1527       C  
ATOM   4009  CZ  PHE A 478       2.004   4.111 144.395  1.00 59.38           C  
ANISOU 4009  CZ  PHE A 478     6940  11212   4409  -1560    654  -1353       C  
ATOM   4010  N   ASP A 479       0.409   4.231 138.739  1.00 50.28           N  
ANISOU 4010  N   ASP A 479     5964   8549   4590   -938    727   -939       N  
ATOM   4011  CA  ASP A 479      -0.751   5.115 138.630  1.00 49.61           C  
ANISOU 4011  CA  ASP A 479     5882   8366   4602   -842    937  -1076       C  
ATOM   4012  C   ASP A 479      -1.955   4.390 138.030  1.00 52.03           C  
ANISOU 4012  C   ASP A 479     6132   8627   5008   -724    913   -851       C  
ATOM   4013  O   ASP A 479      -3.104   4.635 138.426  1.00 63.83           O  
ANISOU 4013  O   ASP A 479     7566  10213   6475   -686   1050   -896       O  
ATOM   4014  CB  ASP A 479      -0.373   6.343 137.800  1.00 40.03           C  
ANISOU 4014  CB  ASP A 479     4761   6840   3609   -753   1066  -1273       C  
ATOM   4015  CG  ASP A 479      -1.576   7.054 137.219  1.00 58.44           C  
ANISOU 4015  CG  ASP A 479     7102   8989   6113   -568   1244  -1309       C  
ATOM   4016  OD1 ASP A 479      -2.376   7.606 138.004  1.00 76.23           O  
ANISOU 4016  OD1 ASP A 479     9320  11360   8285   -571   1415  -1455       O  
ATOM   4017  OD2 ASP A 479      -1.705   7.083 135.974  1.00 62.95           O1-
ANISOU 4017  OD2 ASP A 479     7715   9310   6893   -409   1216  -1193       O1-
ATOM   4018  N   ALA A 480      -1.709   3.499 137.068  1.00 45.46           N  
ANISOU 4018  N   ALA A 480     5309   7665   4298   -672    749   -625       N  
ATOM   4019  CA  ALA A 480      -2.771   2.643 136.541  1.00 44.63           C  
ANISOU 4019  CA  ALA A 480     5136   7554   4267   -605    705   -419       C  
ATOM   4020  C   ALA A 480      -3.403   1.808 137.649  1.00 44.89           C  
ANISOU 4020  C   ALA A 480     5088   7873   4095   -725    710   -315       C  
ATOM   4021  O   ALA A 480      -4.637   1.717 137.765  1.00 61.77           O  
ANISOU 4021  O   ALA A 480     7137  10089   6243   -696    804   -296       O  
ATOM   4022  CB  ALA A 480      -2.210   1.734 135.444  1.00 34.49           C  
ANISOU 4022  CB  ALA A 480     3889   6100   3116   -571    526   -215       C  
ATOM   4023  N   ALA A 481      -2.559   1.170 138.461  1.00 39.72           N  
ANISOU 4023  N   ALA A 481     4456   7386   3249   -855    612   -237       N  
ATOM   4024  CA  ALA A 481      -3.036   0.453 139.636  1.00 46.39           C  
ANISOU 4024  CA  ALA A 481     5252   8515   3861   -971    636   -135       C  
ATOM   4025  C   ALA A 481      -3.907   1.346 140.509  1.00 57.28           C  
ANISOU 4025  C   ALA A 481     6581  10059   5126   -991    839   -346       C  
ATOM   4026  O   ALA A 481      -5.005   0.953 140.911  1.00 52.16           O  
ANISOU 4026  O   ALA A 481     5856   9538   4424  -1016    929   -277       O  
ATOM   4027  CB  ALA A 481      -1.849  -0.087 140.433  1.00 40.95           C  
ANISOU 4027  CB  ALA A 481     4603   8000   2954  -1074    508    -52       C  
ATOM   4028  N   MET A 482      -3.424   2.552 140.821  1.00 65.31           N  
ANISOU 4028  N   MET A 482     7637  11068   6110   -992    931   -617       N  
ATOM   4029  CA  MET A 482      -4.187   3.445 141.696  1.00 69.41           C  
ANISOU 4029  CA  MET A 482     8120  11733   6518  -1014   1146   -845       C  
ATOM   4030  C   MET A 482      -5.552   3.781 141.112  1.00 67.00           C  
ANISOU 4030  C   MET A 482     7741  11312   6404   -874   1287   -860       C  
ATOM   4031  O   MET A 482      -6.537   3.924 141.849  1.00 79.79           O  
ANISOU 4031  O   MET A 482     9285  13106   7925   -895   1443   -924       O  
ATOM   4032  CB  MET A 482      -3.407   4.727 141.977  1.00 80.77           C  
ANISOU 4032  CB  MET A 482     9627  13127   7935  -1041   1240  -1160       C  
ATOM   4033  CG  MET A 482      -3.620   5.277 143.376  1.00 89.12           C  
ANISOU 4033  CG  MET A 482    10668  14466   8727  -1164   1397  -1383       C  
ATOM   4034  SD  MET A 482      -3.041   4.124 144.620  1.00 91.02           S  
ANISOU 4034  SD  MET A 482    10888  15113   8582  -1344   1237  -1210       S  
ATOM   4035  CE  MET A 482      -1.302   4.135 144.249  1.00 81.84           C  
ANISOU 4035  CE  MET A 482     9780  13887   7430  -1390   1027  -1234       C  
ATOM   4036  N   MET A 483      -5.627   3.923 139.790  1.00 62.05           N  
ANISOU 4036  N   MET A 483     7126  10410   6042   -723   1237   -804       N  
ATOM   4037  CA  MET A 483      -6.924   4.125 139.150  1.00 68.75           C  
ANISOU 4037  CA  MET A 483     7876  11184   7061   -569   1333   -785       C  
ATOM   4038  C   MET A 483      -7.843   2.934 139.392  1.00 70.90           C  
ANISOU 4038  C   MET A 483     8026  11641   7270   -642   1293   -583       C  
ATOM   4039  O   MET A 483      -9.016   3.097 139.773  1.00 77.49           O  
ANISOU 4039  O   MET A 483     8741  12609   8092   -615   1441   -633       O  
ATOM   4040  CB  MET A 483      -6.738   4.364 137.652  1.00 57.31           C  
ANISOU 4040  CB  MET A 483     6468   9438   5870   -396   1253   -729       C  
ATOM   4041  CG  MET A 483      -6.158   5.724 137.299  1.00 48.45           C  
ANISOU 4041  CG  MET A 483     5460   8090   4860   -288   1366   -938       C  
ATOM   4042  SD  MET A 483      -6.935   7.121 138.145  1.00 49.53           S  
ANISOU 4042  SD  MET A 483     5578   8272   4970   -220   1675  -1228       S  
ATOM   4043  CE  MET A 483      -5.745   7.462 139.447  1.00 45.73           C  
ANISOU 4043  CE  MET A 483     5194   7928   4252   -460   1714  -1444       C  
ATOM   4044  N   ALA A 484      -7.323   1.724 139.160  1.00 61.83           N  
ANISOU 4044  N   ALA A 484     6905  10491   6095   -735   1110   -357       N  
ATOM   4045  CA  ALA A 484      -8.101   0.517 139.440  1.00 64.54           C  
ANISOU 4045  CA  ALA A 484     7156  10985   6381   -837   1093   -161       C  
ATOM   4046  C   ALA A 484      -8.559   0.477 140.894  1.00 66.59           C  
ANISOU 4046  C   ALA A 484     7378  11533   6392   -966   1239   -207       C  
ATOM   4047  O   ALA A 484      -9.669   0.024 141.193  1.00 61.87           O  
ANISOU 4047  O   ALA A 484     6661  11070   5775  -1012   1340   -151       O  
ATOM   4048  CB  ALA A 484      -7.286  -0.733 139.104  1.00 43.25           C  
ANISOU 4048  CB  ALA A 484     4534   8218   3682   -922    902     80       C  
ATOM   4049  N   LEU A 485      -7.709   0.940 141.809  1.00 48.81           N  
ANISOU 4049  N   LEU A 485     5217   9392   3935  -1035   1257   -318       N  
ATOM   4050  CA  LEU A 485      -8.063   0.987 143.224  1.00 59.66           C  
ANISOU 4050  CA  LEU A 485     6570  11063   5035  -1156   1398   -383       C  
ATOM   4051  C   LEU A 485      -9.239   1.925 143.458  1.00 68.92           C  
ANISOU 4051  C   LEU A 485     7639  12291   6256  -1085   1630   -597       C  
ATOM   4052  O   LEU A 485     -10.271   1.534 144.016  1.00 73.42           O  
ANISOU 4052  O   LEU A 485     8106  13040   6751  -1143   1757   -551       O  
ATOM   4053  CB  LEU A 485      -6.856   1.438 144.056  1.00 62.13           C  
ANISOU 4053  CB  LEU A 485     6991  11498   5118  -1235   1357   -506       C  
ATOM   4054  CG  LEU A 485      -5.661   0.504 144.222  1.00 57.20           C  
ANISOU 4054  CG  LEU A 485     6449  10926   4358  -1313   1146   -298       C  
ATOM   4055  CD1 LEU A 485      -4.670   1.077 145.229  1.00 60.09           C  
ANISOU 4055  CD1 LEU A 485     6872  11507   4452  -1400   1131   -470       C  
ATOM   4056  CD2 LEU A 485      -6.134  -0.863 144.658  1.00 76.88           C  
ANISOU 4056  CD2 LEU A 485     8923  13556   6732  -1397   1124      3       C  
ATOM   4057  N   ARG A 486      -9.093   3.180 143.032  1.00 70.99           N  
ANISOU 4057  N   ARG A 486     7928  12390   6655   -954   1705   -830       N  
ATOM   4058  CA  ARG A 486     -10.115   4.182 143.299  1.00 76.64           C  
ANISOU 4058  CA  ARG A 486     8559  13139   7420   -858   1946  -1048       C  
ATOM   4059  C   ARG A 486     -11.438   3.870 142.613  1.00 80.48           C  
ANISOU 4059  C   ARG A 486     8875  13603   8099   -744   1991   -947       C  
ATOM   4060  O   ARG A 486     -12.480   4.346 143.076  1.00103.60           O  
ANISOU 4060  O   ARG A 486    11687  16654  11021   -697   2195  -1071       O  
ATOM   4061  CB  ARG A 486      -9.613   5.572 142.885  1.00 77.64           C  
ANISOU 4061  CB  ARG A 486     8775  13040   7684   -726   2029  -1298       C  
ATOM   4062  CG  ARG A 486      -8.629   6.163 143.888  1.00 81.99           C  
ANISOU 4062  CG  ARG A 486     9446  13694   8014   -867   2080  -1512       C  
ATOM   4063  CD  ARG A 486      -8.119   7.564 143.551  1.00 77.54           C  
ANISOU 4063  CD  ARG A 486     8983  12887   7593   -773   2204  -1790       C  
ATOM   4064  NE  ARG A 486      -9.078   8.403 142.840  1.00 77.00           N  
ANISOU 4064  NE  ARG A 486     8866  12610   7782   -542   2379  -1869       N  
ATOM   4065  CZ  ARG A 486      -9.055   9.733 142.880  1.00 82.32           C  
ANISOU 4065  CZ  ARG A 486     9615  13103   8559   -449   2593  -2135       C  
ATOM   4066  NH1 ARG A 486      -8.143  10.350 143.617  1.00 87.60           N  
ANISOU 4066  NH1 ARG A 486    10416  13735   9132   -588   2606  -2326       N  
ATOM   4067  NH2 ARG A 486      -9.947  10.447 142.207  1.00 79.41           N  
ANISOU 4067  NH2 ARG A 486     9203  12541   8428   -202   2746  -2163       N  
ATOM   4068  N   THR A 487     -11.438   3.073 141.539  1.00 80.10           N  
ANISOU 4068  N   THR A 487     8795  13422   8216   -703   1811   -740       N  
ATOM   4069  CA  THR A 487     -12.688   2.806 140.834  1.00 74.97           C  
ANISOU 4069  CA  THR A 487     7960  12780   7745   -602   1840   -672       C  
ATOM   4070  C   THR A 487     -13.188   1.369 140.919  1.00 78.26           C  
ANISOU 4070  C   THR A 487     8283  13334   8119   -766   1769   -450       C  
ATOM   4071  O   THR A 487     -14.243   1.070 140.348  1.00 90.77           O  
ANISOU 4071  O   THR A 487     9687  14955   9845   -716   1789   -410       O  
ATOM   4072  CB  THR A 487     -12.563   3.204 139.358  1.00 65.08           C  
ANISOU 4072  CB  THR A 487     6712  11267   6748   -393   1726   -654       C  
ATOM   4073  OG1 THR A 487     -11.367   2.641 138.807  1.00 58.98           O  
ANISOU 4073  OG1 THR A 487     6089  10333   5987   -453   1517   -524       O  
ATOM   4074  CG2 THR A 487     -12.527   4.720 139.220  1.00 49.22           C  
ANISOU 4074  CG2 THR A 487     4754   9117   4830   -190   1874   -875       C  
ATOM   4075  N   SER A 488     -12.487   0.473 141.608  1.00 83.58           N  
ANISOU 4075  N   SER A 488     9065  14087   8604   -958   1698   -306       N  
ATOM   4076  CA  SER A 488     -13.009  -0.875 141.796  1.00 87.17           C  
ANISOU 4076  CA  SER A 488     9450  14651   9019  -1123   1683    -95       C  
ATOM   4077  C   SER A 488     -12.880  -1.274 143.257  1.00 87.89           C  
ANISOU 4077  C   SER A 488     9606  14976   8813  -1301   1791    -44       C  
ATOM   4078  O   SER A 488     -13.844  -1.740 143.871  1.00 91.61           O  
ANISOU 4078  O   SER A 488     9966  15630   9211  -1410   1944     -3       O  
ATOM   4079  CB  SER A 488     -12.283  -1.879 140.899  1.00 80.74           C  
ANISOU 4079  CB  SER A 488     8721  13644   8312  -1160   1465    114       C  
ATOM   4080  OG  SER A 488     -12.898  -3.153 140.967  1.00 79.12           O  
ANISOU 4080  OG  SER A 488     8446  13502   8113  -1318   1481    300       O  
ATOM   4081  N   PHE A 489     -11.683  -1.094 143.819  1.00 93.02           N  
ANISOU 4081  N   PHE A 489    10426  15639   9278  -1334   1715    -48       N  
ATOM   4082  CA  PHE A 489     -11.494  -1.317 145.246  1.00 91.61           C  
ANISOU 4082  CA  PHE A 489    10318  15706   8785  -1473   1802    -21       C  
ATOM   4083  C   PHE A 489     -12.181  -0.238 146.077  1.00 83.64           C  
ANISOU 4083  C   PHE A 489     9263  14797   7719  -1427   1987   -281       C  
ATOM   4084  O   PHE A 489     -12.582  -0.501 147.216  1.00 94.40           O  
ANISOU 4084  O   PHE A 489    10648  16302   8920  -1514   2072   -258       O  
ATOM   4085  CB  PHE A 489     -10.003  -1.360 145.580  1.00103.46           C  
ANISOU 4085  CB  PHE A 489    11990  17209  10110  -1500   1639     26       C  
ATOM   4086  CG  PHE A 489      -9.343  -2.684 145.295  1.00112.36           C  
ANISOU 4086  CG  PHE A 489    13199  18268  11226  -1564   1471    340       C  
ATOM   4087  CD1 PHE A 489      -9.110  -3.102 143.995  1.00109.73           C  
ANISOU 4087  CD1 PHE A 489    12867  17657  11169  -1491   1321    441       C  
ATOM   4088  CD2 PHE A 489      -8.946  -3.507 146.335  1.00114.48           C  
ANISOU 4088  CD2 PHE A 489    13570  18634  11293  -1643   1419    523       C  
ATOM   4089  CE1 PHE A 489      -8.490  -4.317 143.742  1.00 97.66           C  
ANISOU 4089  CE1 PHE A 489    11425  16031   9652  -1541   1182    718       C  
ATOM   4090  CE2 PHE A 489      -8.333  -4.724 146.085  1.00106.85           C  
ANISOU 4090  CE2 PHE A 489    12690  17566  10343  -1670   1280    818       C  
ATOM   4091  CZ  PHE A 489      -8.102  -5.127 144.789  1.00 95.77           C  
ANISOU 4091  CZ  PHE A 489    11273  15964   9151  -1642   1187    922       C  
ATOM   4092  N   LEU A 490     -12.328   0.970 145.520  1.00 78.22           N  
ANISOU 4092  N   LEU A 490     8523  14023   7174  -1282   2063   -522       N  
ATOM   4093  CA  LEU A 490     -12.869   2.134 146.221  1.00 92.09           C  
ANISOU 4093  CA  LEU A 490    10260  15818   8911  -1213   2246   -787       C  
ATOM   4094  C   LEU A 490     -12.257   2.261 147.609  1.00101.45           C  
ANISOU 4094  C   LEU A 490    11583  17144   9821  -1330   2250   -849       C  
ATOM   4095  O   LEU A 490     -12.906   1.947 148.618  1.00109.53           O  
ANISOU 4095  O   LEU A 490    12588  18317  10710  -1410   2348   -818       O  
ATOM   4096  CB  LEU A 490     -14.394   2.060 146.325  1.00102.09           C  
ANISOU 4096  CB  LEU A 490    11351  17148  10288  -1177   2410   -797       C  
ATOM   4097  CG  LEU A 490     -15.232   2.207 145.060  1.00 98.47           C  
ANISOU 4097  CG  LEU A 490    10706  16594  10112  -1024   2432   -801       C  
ATOM   4098  CD1 LEU A 490     -16.357   1.184 145.067  1.00 85.62           C  
ANISOU 4098  CD1 LEU A 490     8917  15073   8544  -1112   2465   -642       C  
ATOM   4099  CD2 LEU A 490     -15.782   3.624 144.933  1.00100.43           C  
ANISOU 4099  CD2 LEU A 490    10897  16761  10501   -815   2596  -1057       C  
ATOM   4100  N   VAL A 491     -10.970   2.587 147.618  1.00 94.19           N  
ANISOU 4100  N   VAL A 491    10789  16183   8816  -1340   2147   -949       N  
ATOM   4101  CA  VAL A 491     -10.149   2.629 148.822  1.00 93.34           C  
ANISOU 4101  CA  VAL A 491    10796  16239   8429  -1466   2064   -940       C  
ATOM   4102  C   VAL A 491     -10.481   3.599 149.939  1.00103.54           C  
ANISOU 4102  C   VAL A 491    12106  17624   9611  -1482   2232  -1206       C  
ATOM   4103  O   VAL A 491     -10.798   4.766 149.708  1.00107.25           O  
ANISOU 4103  O   VAL A 491    12560  17961  10230  -1384   2372  -1460       O  
ATOM   4104  CB  VAL A 491      -8.661   2.828 148.457  1.00 74.81           C  
ANISOU 4104  CB  VAL A 491     8547  13832   6047  -1478   1874   -949       C  
ATOM   4105  CG1 VAL A 491      -7.786   2.651 149.688  1.00 73.19           C  
ANISOU 4105  CG1 VAL A 491     8426  13805   5578  -1580   1811  -1056       C  
ATOM   4106  CG2 VAL A 491      -8.251   1.860 147.358  1.00 69.60           C  
ANISOU 4106  CG2 VAL A 491     7895  13138   5411  -1498   1692   -623       C  
ATOM   4107  N   ASN A 492     -10.382   3.090 151.163  1.00100.02           N  
ANISOU 4107  N   ASN A 492    11703  17397   8903  -1598   2224  -1137       N  
ATOM   4108  CA  ASN A 492     -10.600   3.914 152.347  1.00117.15           C  
ANISOU 4108  CA  ASN A 492    13903  19703  10907  -1646   2359  -1367       C  
ATOM   4109  C   ASN A 492      -9.392   4.628 152.959  1.00116.02           C  
ANISOU 4109  C   ASN A 492    13850  19598  10635  -1702   2249  -1555       C  
ATOM   4110  O   ASN A 492      -9.274   5.848 152.854  1.00108.51           O  
ANISOU 4110  O   ASN A 492    12917  18482   9832  -1650   2310  -1815       O  
ATOM   4111  CB  ASN A 492     -11.142   3.072 153.501  1.00131.05           C  
ANISOU 4111  CB  ASN A 492    15670  21692  12429  -1744   2390  -1185       C  
ATOM   4112  CG  ASN A 492     -10.534   1.684 153.546  1.00133.78           C  
ANISOU 4112  CG  ASN A 492    16064  22101  12666  -1798   2189   -846       C  
ATOM   4113  OD1 ASN A 492      -9.464   1.444 152.987  1.00132.51           O  
ANISOU 4113  OD1 ASN A 492    15942  21868  12536  -1782   2003   -788       O  
ATOM   4114  ND2 ASN A 492     -11.216   0.761 154.214  1.00139.51           N  
ANISOU 4114  ND2 ASN A 492    16795  22945  13268  -1856   2238   -618       N  
ATOM   4115  N   ASP A 493      -8.484   3.870 153.565  1.00124.88           N  
ANISOU 4115  N   ASP A 493    15024  20932  11493  -1804   2093  -1424       N  
ATOM   4116  CA  ASP A 493      -7.181   4.386 153.979  1.00122.71           C  
ANISOU 4116  CA  ASP A 493    14800  20740  11085  -1871   1962  -1584       C  
ATOM   4117  C   ASP A 493      -6.073   3.994 152.998  1.00116.89           C  
ANISOU 4117  C   ASP A 493    14074  19882  10455  -1838   1753  -1461       C  
ATOM   4118  O   ASP A 493      -5.957   2.830 152.614  1.00116.54           O  
ANISOU 4118  O   ASP A 493    14027  19817  10437  -1806   1637  -1147       O  
ATOM   4119  CB  ASP A 493      -6.834   3.896 155.387  1.00115.43           C  
ANISOU 4119  CB  ASP A 493    13906  20133   9818  -1972   1885  -1495       C  
ATOM   4120  CG  ASP A 493      -6.363   2.456 155.402  1.00103.66           C  
ANISOU 4120  CG  ASP A 493    12436  18732   8219  -1964   1689  -1105       C  
ATOM   4121  OD1 ASP A 493      -5.169   2.217 155.124  1.00 94.80           O  
ANISOU 4121  OD1 ASP A 493    11324  17625   7071  -1961   1483  -1036       O  
ATOM   4122  OD2 ASP A 493      -7.186   1.562 155.693  1.00104.09           O1-
ANISOU 4122  OD2 ASP A 493    12496  18829   8225  -1957   1754   -864       O1-
ATOM   4123  N   PHE A 494      -5.262   4.971 152.598  1.00114.76           N  
ANISOU 4123  N   PHE A 494    13823  19513  10267  -1851   1722  -1715       N  
ATOM   4124  CA  PHE A 494      -4.163   4.736 151.670  1.00106.01           C  
ANISOU 4124  CA  PHE A 494    12727  18297   9256  -1829   1535  -1639       C  
ATOM   4125  C   PHE A 494      -2.833   4.536 152.395  1.00100.23           C  
ANISOU 4125  C   PHE A 494    11992  17790   8300  -1923   1338  -1640       C  
ATOM   4126  O   PHE A 494      -1.774   4.909 151.875  1.00101.81           O  
ANISOU 4126  O   PHE A 494    12190  17914   8579  -1939   1231  -1748       O  
ATOM   4127  CB  PHE A 494      -4.057   5.888 150.672  1.00101.47           C  
ANISOU 4127  CB  PHE A 494    12171  17427   8956  -1771   1640  -1903       C  
ATOM   4128  CG  PHE A 494      -5.116   5.871 149.601  1.00 95.12           C  
ANISOU 4128  CG  PHE A 494    11349  16387   8405  -1632   1768  -1826       C  
ATOM   4129  CD1 PHE A 494      -5.014   5.026 148.507  1.00 86.89           C  
ANISOU 4129  CD1 PHE A 494    10293  15241   7479  -1563   1650  -1575       C  
ATOM   4130  CD2 PHE A 494      -6.229   6.692 149.703  1.00104.73           C  
ANISOU 4130  CD2 PHE A 494    12549  17498   9745  -1563   2006  -2000       C  
ATOM   4131  CE1 PHE A 494      -5.998   5.009 147.527  1.00 90.94           C  
ANISOU 4131  CE1 PHE A 494    10763  15572   8220  -1437   1762  -1510       C  
ATOM   4132  CE2 PHE A 494      -7.208   6.682 148.732  1.00 99.70           C  
ANISOU 4132  CE2 PHE A 494    11864  16675   9344  -1416   2114  -1925       C  
ATOM   4133  CZ  PHE A 494      -7.095   5.844 147.643  1.00 94.88           C  
ANISOU 4133  CZ  PHE A 494    11225  15985   8840  -1358   1989  -1686       C  
ATOM   4134  N   GLY A 495      -2.865   3.948 153.594  1.00 90.77           N  
ANISOU 4134  N   GLY A 495    10787  16874   6827  -1978   1293  -1517       N  
ATOM   4135  CA  GLY A 495      -1.653   3.839 154.391  1.00 97.01           C  
ANISOU 4135  CA  GLY A 495    11552  17915   7392  -2051   1117  -1535       C  
ATOM   4136  C   GLY A 495      -0.646   2.850 153.841  1.00101.18           C  
ANISOU 4136  C   GLY A 495    12068  18449   7927  -1993    875  -1251       C  
ATOM   4137  O   GLY A 495       0.558   2.990 154.077  1.00 97.15           O  
ANISOU 4137  O   GLY A 495    11511  18070   7330  -2031    722  -1321       O  
ATOM   4138  N   PHE A 496      -1.112   1.848 153.100  1.00110.23           N  
ANISOU 4138  N   PHE A 496    13246  19448   9188  -1900    843   -934       N  
ATOM   4139  CA  PHE A 496      -0.221   0.828 152.567  1.00115.22           C  
ANISOU 4139  CA  PHE A 496    13879  20052   9847  -1829    627   -638       C  
ATOM   4140  C   PHE A 496       0.555   1.302 151.345  1.00117.65           C  
ANISOU 4140  C   PHE A 496    14171  20149  10380  -1805    550   -757       C  
ATOM   4141  O   PHE A 496       1.604   0.722 151.031  1.00125.13           O  
ANISOU 4141  O   PHE A 496    15100  21109  11334  -1760    357   -598       O  
ATOM   4142  CB  PHE A 496      -1.017  -0.432 152.208  1.00111.11           C  
ANISOU 4142  CB  PHE A 496    13408  19419   9389  -1754    639   -261       C  
ATOM   4143  CG  PHE A 496      -2.274  -0.154 151.430  1.00110.76           C  
ANISOU 4143  CG  PHE A 496    13370  19158   9554  -1743    827   -318       C  
ATOM   4144  CD1 PHE A 496      -3.468   0.124 152.081  1.00122.20           C  
ANISOU 4144  CD1 PHE A 496    14815  20671  10945  -1782   1028   -405       C  
ATOM   4145  CD2 PHE A 496      -2.257  -0.160 150.045  1.00105.56           C  
ANISOU 4145  CD2 PHE A 496    12713  18245   9151  -1685    804   -287       C  
ATOM   4146  CE1 PHE A 496      -4.618   0.384 151.364  1.00117.76           C  
ANISOU 4146  CE1 PHE A 496    14229  19926  10588  -1753   1199   -459       C  
ATOM   4147  CE2 PHE A 496      -3.404   0.100 149.326  1.00102.42           C  
ANISOU 4147  CE2 PHE A 496    12298  17673   8943  -1659    973   -338       C  
ATOM   4148  CZ  PHE A 496      -4.582   0.376 149.986  1.00104.82           C  
ANISOU 4148  CZ  PHE A 496    12578  18048   9200  -1688   1168   -425       C  
ATOM   4149  N   ILE A 497       0.066   2.330 150.646  1.00107.77           N  
ANISOU 4149  N   ILE A 497    12932  18693   9321  -1819    708  -1026       N  
ATOM   4150  CA  ILE A 497       0.715   2.717 149.401  1.00 94.69           C  
ANISOU 4150  CA  ILE A 497    11284  16807   7888  -1785    657  -1115       C  
ATOM   4151  C   ILE A 497       2.060   3.378 149.678  1.00100.11           C  
ANISOU 4151  C   ILE A 497    11922  17590   8524  -1863    554  -1344       C  
ATOM   4152  O   ILE A 497       3.000   3.220 148.896  1.00 95.47           O  
ANISOU 4152  O   ILE A 497    11322  16909   8044  -1836    420  -1302       O  
ATOM   4153  CB  ILE A 497      -0.197   3.627 148.559  1.00 82.25           C  
ANISOU 4153  CB  ILE A 497     9744  14962   6544  -1750    874  -1324       C  
ATOM   4154  CG1 ILE A 497      -0.276   5.037 149.144  1.00 89.85           C  
ANISOU 4154  CG1 ILE A 497    10707  15919   7513  -1827   1047  -1726       C  
ATOM   4155  CG2 ILE A 497      -1.582   3.014 148.439  1.00 80.15           C  
ANISOU 4155  CG2 ILE A 497     9483  14654   6315  -1687    988  -1122       C  
ATOM   4156  CD1 ILE A 497      -1.177   5.970 148.368  1.00 79.61           C  
ANISOU 4156  CD1 ILE A 497     9451  14327   6470  -1752   1279  -1917       C  
ATOM   4157  N   TRP A 498       2.195   4.109 150.792  1.00105.71           N  
ANISOU 4157  N   TRP A 498    12593  18497   9074  -1968    617  -1590       N  
ATOM   4158  CA  TRP A 498       3.488   4.694 151.134  1.00106.77           C  
ANISOU 4158  CA  TRP A 498    12654  18759   9155  -2063    522  -1809       C  
ATOM   4159  C   TRP A 498       4.545   3.607 151.295  1.00 93.66           C  
ANISOU 4159  C   TRP A 498    10928  17290   7368  -2011    265  -1525       C  
ATOM   4160  O   TRP A 498       5.648   3.709 150.740  1.00101.14           O  
ANISOU 4160  O   TRP A 498    11823  18195   8410  -2014    146  -1573       O  
ATOM   4161  CB  TRP A 498       3.348   5.533 152.407  1.00125.59           C  
ANISOU 4161  CB  TRP A 498    15004  21354  11360  -2190    634  -2091       C  
ATOM   4162  CG  TRP A 498       4.598   6.243 152.868  1.00131.93           C  
ANISOU 4162  CG  TRP A 498    15712  22315  12102  -2318    567  -2360       C  
ATOM   4163  CD1 TRP A 498       5.047   6.345 154.154  1.00138.42           C  
ANISOU 4163  CD1 TRP A 498    16451  23488  12656  -2414    515  -2454       C  
ATOM   4164  CD2 TRP A 498       5.539   6.963 152.058  1.00133.20           C  
ANISOU 4164  CD2 TRP A 498    15841  22294  12474  -2371    560  -2576       C  
ATOM   4165  NE1 TRP A 498       6.212   7.072 154.194  1.00144.73           N  
ANISOU 4165  NE1 TRP A 498    17153  24350  13487  -2530    472  -2719       N  
ATOM   4166  CE2 TRP A 498       6.535   7.463 152.921  1.00144.73           C  
ANISOU 4166  CE2 TRP A 498    17186  24018  13789  -2510    505  -2797       C  
ATOM   4167  CE3 TRP A 498       5.639   7.227 150.689  1.00127.97           C  
ANISOU 4167  CE3 TRP A 498    15239  21276  12107  -2318    603  -2604       C  
ATOM   4168  CZ2 TRP A 498       7.615   8.211 152.458  1.00148.71           C  
ANISOU 4168  CZ2 TRP A 498    17623  24433  14448  -2607    502  -3045       C  
ATOM   4169  CZ3 TRP A 498       6.712   7.967 150.233  1.00131.58           C  
ANISOU 4169  CZ3 TRP A 498    15648  21630  12715  -2406    600  -2842       C  
ATOM   4170  CH2 TRP A 498       7.685   8.452 151.115  1.00137.82           C  
ANISOU 4170  CH2 TRP A 498    16314  22680  13370  -2554    555  -3059       C  
ATOM   4171  N   LEU A 499       4.203   2.535 152.014  1.00 88.18           N  
ANISOU 4171  N   LEU A 499    10243  16783   6479  -1947    191  -1213       N  
ATOM   4172  CA  LEU A 499       5.123   1.424 152.225  1.00 92.10           C  
ANISOU 4172  CA  LEU A 499    10693  17434   6865  -1860    -32   -905       C  
ATOM   4173  C   LEU A 499       5.424   0.691 150.923  1.00 84.29           C  
ANISOU 4173  C   LEU A 499     9738  16186   6104  -1744   -135   -662       C  
ATOM   4174  O   LEU A 499       6.590   0.400 150.627  1.00 96.43           O  
ANISOU 4174  O   LEU A 499    11211  17751   7676  -1699   -301   -597       O  
ATOM   4175  CB  LEU A 499       4.544   0.461 153.262  1.00106.18           C  
ANISOU 4175  CB  LEU A 499    12513  19417   8413  -1809    -42   -621       C  
ATOM   4176  CG  LEU A 499       5.479  -0.603 153.833  1.00111.92           C  
ANISOU 4176  CG  LEU A 499    13198  20354   8970  -1709   -245   -325       C  
ATOM   4177  CD1 LEU A 499       6.080  -0.120 155.140  1.00110.98           C  
ANISOU 4177  CD1 LEU A 499    12989  20612   8566  -1790   -288   -511       C  
ATOM   4178  CD2 LEU A 499       4.732  -1.911 154.037  1.00117.83           C  
ANISOU 4178  CD2 LEU A 499    14049  21054   9667  -1598   -234     84       C  
ATOM   4179  N   VAL A 500       4.385   0.382 150.136  1.00 64.91           N  
ANISOU 4179  N   VAL A 500     7374  13484   3806  -1694    -35   -530       N  
ATOM   4180  CA  VAL A 500       4.592  -0.296 148.854  1.00 66.44           C  
ANISOU 4180  CA  VAL A 500     7605  13419   4218  -1594   -121   -309       C  
ATOM   4181  C   VAL A 500       5.522   0.523 147.969  1.00 65.15           C  
ANISOU 4181  C   VAL A 500     7405  13127   4222  -1626   -165   -554       C  
ATOM   4182  O   VAL A 500       6.452  -0.005 147.345  1.00 77.24           O  
ANISOU 4182  O   VAL A 500     8910  14588   5849  -1555   -322   -409       O  
ATOM   4183  CB  VAL A 500       3.245  -0.557 148.155  1.00 66.01           C  
ANISOU 4183  CB  VAL A 500     7637  13140   4304  -1563     22   -194       C  
ATOM   4184  CG1 VAL A 500       3.471  -1.054 146.732  1.00 53.11           C  
ANISOU 4184  CG1 VAL A 500     6041  11232   2908  -1480    -55    -27       C  
ATOM   4185  CG2 VAL A 500       2.416  -1.558 148.942  1.00 67.51           C  
ANISOU 4185  CG2 VAL A 500     7863  13428   4361  -1534     60     90       C  
ATOM   4186  N   LEU A 501       5.292   1.834 147.923  1.00 65.37           N  
ANISOU 4186  N   LEU A 501     7434  13102   4301  -1730     -9   -935       N  
ATOM   4187  CA  LEU A 501       6.050   2.713 147.043  1.00 69.17           C  
ANISOU 4187  CA  LEU A 501     7904  13407   4970  -1774      1  -1199       C  
ATOM   4188  C   LEU A 501       7.511   2.802 147.469  1.00 74.96           C  
ANISOU 4188  C   LEU A 501     8518  14329   5633  -1822   -154  -1282       C  
ATOM   4189  O   LEU A 501       8.421   2.696 146.633  1.00 84.14           O  
ANISOU 4189  O   LEU A 501     9652  15376   6943  -1792   -260  -1264       O  
ATOM   4190  CB  LEU A 501       5.393   4.093 147.039  1.00 75.78           C  
ANISOU 4190  CB  LEU A 501     8787  14112   5894  -1864    246  -1581       C  
ATOM   4191  CG  LEU A 501       5.885   5.133 146.049  1.00 75.06           C  
ANISOU 4191  CG  LEU A 501     8729  13743   6048  -1904    340  -1873       C  
ATOM   4192  CD1 LEU A 501       5.753   4.571 144.663  1.00 74.81           C  
ANISOU 4192  CD1 LEU A 501     8769  13460   6194  -1789    291  -1675       C  
ATOM   4193  CD2 LEU A 501       5.066   6.398 146.190  1.00 75.40           C  
ANISOU 4193  CD2 LEU A 501     8836  13623   6191  -1955    614  -2195       C  
ATOM   4194  N   SER A 502       7.756   3.017 148.767  1.00 81.87           N  
ANISOU 4194  N   SER A 502     9315  15509   6285  -1897   -163  -1384       N  
ATOM   4195  CA  SER A 502       9.126   3.021 149.273  1.00 88.47           C  
ANISOU 4195  CA  SER A 502    10013  16579   7023  -1933   -314  -1446       C  
ATOM   4196  C   SER A 502       9.832   1.710 148.943  1.00 87.98           C  
ANISOU 4196  C   SER A 502     9918  16546   6964  -1775   -531  -1062       C  
ATOM   4197  O   SER A 502      10.979   1.701 148.466  1.00 98.03           O  
ANISOU 4197  O   SER A 502    11106  17808   8333  -1759   -645  -1092       O  
ATOM   4198  CB  SER A 502       9.123   3.269 150.786  1.00 99.73           C  
ANISOU 4198  CB  SER A 502    11366  18361   8164  -2019   -299  -1558       C  
ATOM   4199  OG  SER A 502       8.622   4.556 151.107  1.00106.17           O  
ANISOU 4199  OG  SER A 502    12202  19136   9002  -2173    -93  -1943       O  
ATOM   4200  N   SER A 503       9.138   0.588 149.172  1.00 83.19           N  
ANISOU 4200  N   SER A 503     9383  15950   6276  -1655   -569   -700       N  
ATOM   4201  CA  SER A 503       9.719  -0.728 148.930  1.00 85.45           C  
ANISOU 4201  CA  SER A 503     9661  16224   6581  -1489   -744   -314       C  
ATOM   4202  C   SER A 503      10.124  -0.893 147.473  1.00 91.59           C  
ANISOU 4202  C   SER A 503    10465  16695   7642  -1426   -795   -254       C  
ATOM   4203  O   SER A 503      11.227  -1.363 147.173  1.00106.83           O  
ANISOU 4203  O   SER A 503    12321  18637   9632  -1343   -942   -145       O  
ATOM   4204  CB  SER A 503       8.720  -1.813 149.327  1.00 97.02           C  
ANISOU 4204  CB  SER A 503    11230  17673   7959  -1394   -717     36       C  
ATOM   4205  OG  SER A 503       7.973  -1.420 150.463  1.00108.82           O  
ANISOU 4205  OG  SER A 503    12735  19378   9233  -1482   -607    -79       O  
ATOM   4206  N   THR A 504       9.238  -0.513 146.550  1.00 83.34           N  
ANISOU 4206  N   THR A 504     9521  15376   6767  -1456   -671   -324       N  
ATOM   4207  CA  THR A 504       9.533  -0.702 145.132  1.00 76.49           C  
ANISOU 4207  CA  THR A 504     8692  14214   6155  -1395   -718   -254       C  
ATOM   4208  C   THR A 504      10.676   0.197 144.685  1.00 72.79           C  
ANISOU 4208  C   THR A 504     8132  13728   5794  -1473   -749   -556       C  
ATOM   4209  O   THR A 504      11.567  -0.238 143.947  1.00 70.60           O  
ANISOU 4209  O   THR A 504     7814  13350   5660  -1398   -871   -447       O  
ATOM   4210  CB  THR A 504       8.291  -0.442 144.281  1.00 76.02           C  
ANISOU 4210  CB  THR A 504     8759  13899   6228  -1409   -572   -277       C  
ATOM   4211  OG1 THR A 504       7.901   0.929 144.409  1.00 88.34           O  
ANISOU 4211  OG1 THR A 504    10331  15454   7782  -1541   -399   -675       O  
ATOM   4212  CG2 THR A 504       7.157  -1.344 144.716  1.00 59.81           C  
ANISOU 4212  CG2 THR A 504     6778  11859   4089  -1350   -523     13       C  
ATOM   4213  N   VAL A 505      10.666   1.462 145.110  1.00 63.93           N  
ANISOU 4213  N   VAL A 505     6980  12681   4629  -1628   -619   -945       N  
ATOM   4214  CA  VAL A 505      11.765   2.356 144.751  1.00 61.81           C  
ANISOU 4214  CA  VAL A 505     6624  12379   4481  -1727   -615  -1253       C  
ATOM   4215  C   VAL A 505      13.092   1.734 145.165  1.00 69.45           C  
ANISOU 4215  C   VAL A 505     7440  13577   5372  -1669   -809  -1126       C  
ATOM   4216  O   VAL A 505      14.026   1.617 144.357  1.00 60.20           O  
ANISOU 4216  O   VAL A 505     6212  12293   4368  -1635   -892  -1118       O  
ATOM   4217  CB  VAL A 505      11.562   3.748 145.376  1.00 62.22           C  
ANISOU 4217  CB  VAL A 505     6666  12486   4490  -1908   -423  -1676       C  
ATOM   4218  CG1 VAL A 505      12.820   4.576 145.233  1.00 66.26           C  
ANISOU 4218  CG1 VAL A 505     7063  13006   5105  -2025   -415  -1974       C  
ATOM   4219  CG2 VAL A 505      10.392   4.464 144.705  1.00 54.18           C  
ANISOU 4219  CG2 VAL A 505     5805  11161   3619  -1935   -208  -1827       C  
ATOM   4220  N   ARG A 506      13.166   1.262 146.416  1.00 98.03           N  
ANISOU 4220  N   ARG A 506    10993  17517   8735  -1641   -880  -1006       N  
ATOM   4221  CA  ARG A 506      14.436   0.769 146.949  1.00 98.18           C  
ANISOU 4221  CA  ARG A 506    10857  17797   8649  -1581  -1052   -918       C  
ATOM   4222  C   ARG A 506      14.857  -0.541 146.270  1.00 85.39           C  
ANISOU 4222  C   ARG A 506     9252  16051   7140  -1375  -1206   -524       C  
ATOM   4223  O   ARG A 506      16.043  -0.752 145.976  1.00 91.79           O  
ANISOU 4223  O   ARG A 506     9946  16907   8022  -1321  -1323   -509       O  
ATOM   4224  CB  ARG A 506      14.330   0.576 148.457  1.00110.98           C  
ANISOU 4224  CB  ARG A 506    12420  19792   9955  -1591  -1084   -879       C  
ATOM   4225  CG  ARG A 506      13.719  -0.732 148.930  1.00116.12           C  
ANISOU 4225  CG  ARG A 506    13154  20493  10474  -1422  -1153   -455       C  
ATOM   4226  CD  ARG A 506      14.246  -1.146 150.296  1.00121.19           C  
ANISOU 4226  CD  ARG A 506    13691  21537  10817  -1382  -1259   -366       C  
ATOM   4227  NE  ARG A 506      15.455  -1.956 150.184  1.00122.06           N  
ANISOU 4227  NE  ARG A 506    13698  21738  10940  -1229  -1441   -161       N  
ATOM   4228  CZ  ARG A 506      15.943  -2.723 151.154  1.00128.16           C  
ANISOU 4228  CZ  ARG A 506    14404  22803  11486  -1111  -1565     50       C  
ATOM   4229  NH1 ARG A 506      15.330  -2.792 152.328  1.00128.19           N  
ANISOU 4229  NH1 ARG A 506    14440  23047  11222  -1137  -1531     87       N  
ATOM   4230  NH2 ARG A 506      17.057  -3.413 150.955  1.00135.64           N  
ANISOU 4230  NH2 ARG A 506    15255  23809  12472   -961  -1719    222       N  
ATOM   4231  N   ALA A 507      13.880  -1.415 145.957  1.00 71.53           N  
ANISOU 4231  N   ALA A 507     7641  14112   5425  -1261  -1190   -213       N  
ATOM   4232  CA  ALA A 507      14.205  -2.698 145.342  1.00 68.87           C  
ANISOU 4232  CA  ALA A 507     7337  13617   5213  -1067  -1305    164       C  
ATOM   4233  C   ALA A 507      14.672  -2.526 143.906  1.00 70.22           C  
ANISOU 4233  C   ALA A 507     7512  13496   5673  -1054  -1321    109       C  
ATOM   4234  O   ALA A 507      15.648  -3.161 143.493  1.00 73.56           O  
ANISOU 4234  O   ALA A 507     7867  13884   6198   -935  -1439    257       O  
ATOM   4235  CB  ALA A 507      12.993  -3.607 145.406  1.00 78.01           C  
ANISOU 4235  CB  ALA A 507     8650  14637   6354   -981  -1249    476       C  
ATOM   4236  N   TYR A 508      13.982  -1.687 143.124  1.00 63.00           N  
ANISOU 4236  N   TYR A 508     6678  12366   4891  -1167  -1197   -100       N  
ATOM   4237  CA  TYR A 508      14.410  -1.455 141.748  1.00 62.27           C  
ANISOU 4237  CA  TYR A 508     6594  11999   5068  -1167  -1205   -171       C  
ATOM   4238  C   TYR A 508      15.759  -0.743 141.713  1.00 62.35           C  
ANISOU 4238  C   TYR A 508     6444  12117   5128  -1248  -1244   -446       C  
ATOM   4239  O   TYR A 508      16.609  -1.048 140.864  1.00 58.50           O  
ANISOU 4239  O   TYR A 508     5900  11502   4825  -1182  -1321   -386       O  
ATOM   4240  CB  TYR A 508      13.347  -0.661 140.984  1.00 66.28           C  
ANISOU 4240  CB  TYR A 508     7230  12267   5687  -1268  -1054   -350       C  
ATOM   4241  CG  TYR A 508      12.078  -1.432 140.675  1.00 72.92           C  
ANISOU 4241  CG  TYR A 508     8227  12894   6587  -1164   -996    -58       C  
ATOM   4242  CD1 TYR A 508      11.368  -2.074 141.679  1.00 69.81           C  
ANISOU 4242  CD1 TYR A 508     7859  12709   5956  -1136  -1005    139       C  
ATOM   4243  CD2 TYR A 508      11.586  -1.507 139.380  1.00 74.07           C  
ANISOU 4243  CD2 TYR A 508     8494  12585   7063  -1089   -901     10       C  
ATOM   4244  CE1 TYR A 508      10.215  -2.770 141.410  1.00 60.91           C  
ANISOU 4244  CE1 TYR A 508     6856  11413   4874  -1073   -943    385       C  
ATOM   4245  CE2 TYR A 508      10.424  -2.206 139.097  1.00 65.74           C  
ANISOU 4245  CE2 TYR A 508     7558  11345   6074  -1011   -843    248       C  
ATOM   4246  CZ  TYR A 508       9.743  -2.835 140.120  1.00 57.40           C  
ANISOU 4246  CZ  TYR A 508     6512  10533   4766  -1012   -859    428       C  
ATOM   4247  OH  TYR A 508       8.586  -3.538 139.872  1.00 57.26           O  
ANISOU 4247  OH  TYR A 508     6596  10342   4817   -961   -787    646       O  
ATOM   4248  N   ALA A 509      15.984   0.192 142.646  1.00 65.78           N  
ANISOU 4248  N   ALA A 509     6799  12788   5408  -1396  -1180   -751       N  
ATOM   4249  CA  ALA A 509      17.298   0.815 142.758  1.00 58.06           C  
ANISOU 4249  CA  ALA A 509     5653  11948   4460  -1484  -1208  -1006       C  
ATOM   4250  C   ALA A 509      18.374  -0.221 143.057  1.00 67.78           C  
ANISOU 4250  C   ALA A 509     6749  13374   5630  -1323  -1402   -751       C  
ATOM   4251  O   ALA A 509      19.486  -0.143 142.524  1.00 73.85           O  
ANISOU 4251  O   ALA A 509     7398  14124   6537  -1318  -1459   -828       O  
ATOM   4252  CB  ALA A 509      17.277   1.891 143.843  1.00 61.01           C  
ANISOU 4252  CB  ALA A 509     5965  12562   4655  -1668  -1100  -1348       C  
ATOM   4253  N   SER A 510      18.062  -1.200 143.910  1.00 78.09           N  
ANISOU 4253  N   SER A 510     8075  14858   6737  -1186  -1490   -447       N  
ATOM   4254  CA  SER A 510      19.045  -2.226 144.246  1.00 84.78           C  
ANISOU 4254  CA  SER A 510     8811  15877   7524  -1009  -1659   -189       C  
ATOM   4255  C   SER A 510      19.376  -3.085 143.031  1.00 78.50           C  
ANISOU 4255  C   SER A 510     8055  14783   6987   -847  -1720     60       C  
ATOM   4256  O   SER A 510      20.551  -3.339 142.739  1.00 85.77           O  
ANISOU 4256  O   SER A 510     8840  15755   7993   -774  -1818     75       O  
ATOM   4257  CB  SER A 510      18.530  -3.088 145.399  1.00 92.09           C  
ANISOU 4257  CB  SER A 510     9783  17010   8198   -897  -1706     88       C  
ATOM   4258  OG  SER A 510      17.255  -3.627 145.096  1.00106.49           O  
ANISOU 4258  OG  SER A 510    11802  18587  10072   -844  -1627    311       O  
ATOM   4259  N   ARG A 511      18.348  -3.543 142.310  1.00 78.93           N  
ANISOU 4259  N   ARG A 511     8289  14530   7171   -791  -1657    252       N  
ATOM   4260  CA  ARG A 511      18.596  -4.297 141.080  1.00 74.32           C  
ANISOU 4260  CA  ARG A 511     7752  13637   6848   -654  -1694    465       C  
ATOM   4261  C   ARG A 511      19.439  -3.503 140.094  1.00 73.25           C  
ANISOU 4261  C   ARG A 511     7514  13394   6923   -747  -1685    198       C  
ATOM   4262  O   ARG A 511      20.342  -4.057 139.453  1.00 62.60           O  
ANISOU 4262  O   ARG A 511     6090  11962   5734   -629  -1763    313       O  
ATOM   4263  CB  ARG A 511      17.291  -4.708 140.410  1.00 58.67           C  
ANISOU 4263  CB  ARG A 511     5973  11344   4976   -625  -1606    650       C  
ATOM   4264  CG  ARG A 511      16.263  -5.305 141.317  1.00 69.39           C  
ANISOU 4264  CG  ARG A 511     7443  12771   6150   -585  -1565    855       C  
ATOM   4265  CD  ARG A 511      15.406  -6.252 140.516  1.00 64.91           C  
ANISOU 4265  CD  ARG A 511     7046  11860   5755   -483  -1514   1149       C  
ATOM   4266  NE  ARG A 511      14.983  -7.394 141.309  1.00 74.36           N  
ANISOU 4266  NE  ARG A 511     8322  13088   6842   -365  -1508   1455       N  
ATOM   4267  CZ  ARG A 511      13.865  -7.408 142.024  1.00 77.24           C  
ANISOU 4267  CZ  ARG A 511     8774  13519   7055   -426  -1421   1496       C  
ATOM   4268  NH1 ARG A 511      13.080  -6.342 142.031  1.00 70.95           N  
ANISOU 4268  NH1 ARG A 511     7993  12766   6198   -591  -1336   1249       N  
ATOM   4269  NH2 ARG A 511      13.529  -8.478 142.728  1.00 88.81           N  
ANISOU 4269  NH2 ARG A 511    10312  14999   8431   -324  -1406   1773       N  
ATOM   4270  N   ALA A 512      19.146  -2.209 139.941  1.00 69.59           N  
ANISOU 4270  N   ALA A 512     7055  12906   6480   -958  -1569   -165       N  
ATOM   4271  CA  ALA A 512      19.910  -1.395 139.004  1.00 66.68           C  
ANISOU 4271  CA  ALA A 512     6605  12399   6331  -1070  -1521   -442       C  
ATOM   4272  C   ALA A 512      21.368  -1.292 139.433  1.00 78.02           C  
ANISOU 4272  C   ALA A 512     7825  14086   7734  -1074  -1606   -561       C  
ATOM   4273  O   ALA A 512      22.277  -1.457 138.613  1.00 87.03           O  
ANISOU 4273  O   ALA A 512     8872  15123   9073  -1030  -1643   -561       O  
ATOM   4274  CB  ALA A 512      19.285  -0.007 138.875  1.00 57.32           C  
ANISOU 4274  CB  ALA A 512     5492  11109   5178  -1296  -1338   -821       C  
ATOM   4275  N   PHE A 513      21.609  -1.013 140.718  1.00 81.78           N  
ANISOU 4275  N   PHE A 513     8210  14907   7956  -1131  -1633   -669       N  
ATOM   4276  CA  PHE A 513      22.976  -0.949 141.229  1.00 82.19           C  
ANISOU 4276  CA  PHE A 513     8039  15248   7940  -1134  -1728   -775       C  
ATOM   4277  C   PHE A 513      23.728  -2.245 140.952  1.00 82.04           C  
ANISOU 4277  C   PHE A 513     7948  15241   7984   -887  -1890   -428       C  
ATOM   4278  O   PHE A 513      24.887  -2.227 140.515  1.00 60.44           O  
ANISOU 4278  O   PHE A 513     5050  12539   5376   -870  -1941   -504       O  
ATOM   4279  CB  PHE A 513      22.950  -0.646 142.728  1.00 62.71           C  
ANISOU 4279  CB  PHE A 513     5499  13174   5154  -1204  -1750   -879       C  
ATOM   4280  CG  PHE A 513      24.160   0.092 143.226  1.00 79.03           C  
ANISOU 4280  CG  PHE A 513     7343  15530   7155  -1336  -1766  -1187       C  
ATOM   4281  CD1 PHE A 513      25.434  -0.294 142.846  1.00 79.44           C  
ANISOU 4281  CD1 PHE A 513     7219  15655   7310  -1250  -1877  -1147       C  
ATOM   4282  CD2 PHE A 513      24.025   1.167 144.088  1.00 85.76           C  
ANISOU 4282  CD2 PHE A 513     8153  16587   7843  -1547  -1662  -1523       C  
ATOM   4283  CE1 PHE A 513      26.547   0.378 143.307  1.00 71.04           C  
ANISOU 4283  CE1 PHE A 513     5937  14875   6181  -1379  -1889  -1436       C  
ATOM   4284  CE2 PHE A 513      25.142   1.841 144.554  1.00 90.45           C  
ANISOU 4284  CE2 PHE A 513     8535  17455   8375  -1681  -1668  -1816       C  
ATOM   4285  CZ  PHE A 513      26.401   1.445 144.162  1.00 82.55           C  
ANISOU 4285  CZ  PHE A 513     7356  16538   7471  -1599  -1785  -1773       C  
ATOM   4286  N   LYS A 514      23.074  -3.387 141.186  1.00 81.44           N  
ANISOU 4286  N   LYS A 514     7995  15114   7834   -693  -1950    -47       N  
ATOM   4287  CA  LYS A 514      23.752  -4.668 141.003  1.00 84.85           C  
ANISOU 4287  CA  LYS A 514     8382  15529   8328   -443  -2075    292       C  
ATOM   4288  C   LYS A 514      24.039  -4.950 139.533  1.00 80.36           C  
ANISOU 4288  C   LYS A 514     7837  14611   8086   -376  -2053    357       C  
ATOM   4289  O   LYS A 514      25.129  -5.419 139.193  1.00 87.58           O  
ANISOU 4289  O   LYS A 514     8612  15553   9111   -256  -2133    426       O  
ATOM   4290  CB  LYS A 514      22.931  -5.798 141.623  1.00 94.40           C  
ANISOU 4290  CB  LYS A 514     9747  16722   9401   -271  -2099    668       C  
ATOM   4291  CG  LYS A 514      22.505  -5.510 143.052  1.00103.33           C  
ANISOU 4291  CG  LYS A 514    10868  18185  10208   -345  -2103    610       C  
ATOM   4292  CD  LYS A 514      21.916  -6.719 143.756  1.00105.06           C  
ANISOU 4292  CD  LYS A 514    11211  18418  10286   -162  -2130    993       C  
ATOM   4293  CE  LYS A 514      22.915  -7.324 144.727  1.00116.14           C  
ANISOU 4293  CE  LYS A 514    12463  20167  11499    -15  -2270   1127       C  
ATOM   4294  NZ  LYS A 514      22.323  -7.525 146.084  1.00120.61           N  
ANISOU 4294  NZ  LYS A 514    13073  21000  11754    -10  -2274   1227       N  
ATOM   4295  N   LYS A 515      23.078  -4.671 138.649  1.00 74.65           N  
ANISOU 4295  N   LYS A 515     7278  13571   7516   -447  -1943    335       N  
ATOM   4296  CA  LYS A 515      23.321  -4.833 137.217  1.00 72.63           C  
ANISOU 4296  CA  LYS A 515     7038  12995   7565   -404  -1912    370       C  
ATOM   4297  C   LYS A 515      24.480  -3.959 136.753  1.00 74.83           C  
ANISOU 4297  C   LYS A 515     7118  13337   7979   -535  -1895     45       C  
ATOM   4298  O   LYS A 515      25.362  -4.416 136.009  1.00 76.77           O  
ANISOU 4298  O   LYS A 515     7260  13493   8416   -427  -1934    121       O  
ATOM   4299  CB  LYS A 515      22.055  -4.483 136.437  1.00 76.12           C  
ANISOU 4299  CB  LYS A 515     7673  13136   8112   -494  -1795    353       C  
ATOM   4300  CG  LYS A 515      21.107  -5.643 136.157  1.00 74.87           C  
ANISOU 4300  CG  LYS A 515     7714  12740   7992   -323  -1791    738       C  
ATOM   4301  CD  LYS A 515      21.770  -6.747 135.354  1.00 61.55           C  
ANISOU 4301  CD  LYS A 515     6020  10848   6517   -114  -1833   1003       C  
ATOM   4302  CE  LYS A 515      21.079  -8.073 135.606  1.00 55.21           C  
ANISOU 4302  CE  LYS A 515     5401   9886   5690     65  -1819   1373       C  
ATOM   4303  NZ  LYS A 515      20.958  -8.350 137.060  1.00 66.50           N  
ANISOU 4303  NZ  LYS A 515     6819  11609   6840     92  -1864   1445       N  
ATOM   4304  N   ILE A 516      24.493  -2.695 137.187  1.00 78.57           N  
ANISOU 4304  N   ILE A 516     7541  13944   8366   -772  -1813   -328       N  
ATOM   4305  CA  ILE A 516      25.547  -1.767 136.785  1.00 79.20           C  
ANISOU 4305  CA  ILE A 516     7457  14049   8587   -933  -1749   -671       C  
ATOM   4306  C   ILE A 516      26.903  -2.260 137.273  1.00 75.82           C  
ANISOU 4306  C   ILE A 516     6798  13909   8101   -824  -1888   -617       C  
ATOM   4307  O   ILE A 516      27.894  -2.239 136.533  1.00 76.76           O  
ANISOU 4307  O   ILE A 516     6776  13965   8422   -817  -1884   -690       O  
ATOM   4308  CB  ILE A 516      25.240  -0.351 137.307  1.00 79.39           C  
ANISOU 4308  CB  ILE A 516     7506  14142   8519  -1203  -1601  -1072       C  
ATOM   4309  CG1 ILE A 516      23.914   0.162 136.740  1.00 56.69           C  
ANISOU 4309  CG1 ILE A 516     4857  10955   5725  -1298  -1449  -1134       C  
ATOM   4310  CG2 ILE A 516      26.377   0.605 136.965  1.00 90.76           C  
ANISOU 4310  CG2 ILE A 516     8790  15589  10105  -1379  -1502  -1426       C  
ATOM   4311  CD1 ILE A 516      23.612   1.600 137.094  1.00 59.43           C  
ANISOU 4311  CD1 ILE A 516     5256  11283   6041  -1550  -1257  -1536       C  
ATOM   4312  N   VAL A 517      26.966  -2.715 138.527  1.00 74.25           N  
ANISOU 4312  N   VAL A 517     6551  14035   7625   -737  -2006   -488       N  
ATOM   4313  CA  VAL A 517      28.211  -3.274 139.046  1.00 79.63           C  
ANISOU 4313  CA  VAL A 517     7013  15013   8231   -606  -2152   -405       C  
ATOM   4314  C   VAL A 517      28.621  -4.498 138.238  1.00 78.89           C  
ANISOU 4314  C   VAL A 517     6914  14727   8332   -346  -2227    -70       C  
ATOM   4315  O   VAL A 517      29.808  -4.716 137.966  1.00 88.03           O  
ANISOU 4315  O   VAL A 517     7874  15976   9597   -275  -2290    -87       O  
ATOM   4316  CB  VAL A 517      28.071  -3.600 140.545  1.00 76.12           C  
ANISOU 4316  CB  VAL A 517     6541  14941   7440   -545  -2255   -297       C  
ATOM   4317  CG1 VAL A 517      29.236  -4.456 141.025  1.00 70.25           C  
ANISOU 4317  CG1 VAL A 517     5598  14474   6619   -344  -2423   -115       C  
ATOM   4318  CG2 VAL A 517      27.987  -2.317 141.357  1.00 69.73           C  
ANISOU 4318  CG2 VAL A 517     5675  14371   6449   -811  -2178   -684       C  
ATOM   4319  N   THR A 518      27.641  -5.299 137.818  1.00 71.39           N  
ANISOU 4319  N   THR A 518     6181  13499   7444   -206  -2205    228       N  
ATOM   4320  CA  THR A 518      27.938  -6.521 137.081  1.00 70.67           C  
ANISOU 4320  CA  THR A 518     6120  13190   7540     49  -2246    555       C  
ATOM   4321  C   THR A 518      28.545  -6.220 135.716  1.00 79.55           C  
ANISOU 4321  C   THR A 518     7160  14082   8982      9  -2178    421       C  
ATOM   4322  O   THR A 518      29.458  -6.926 135.271  1.00 79.69           O  
ANISOU 4322  O   THR A 518     7062  14068   9148    182  -2228    555       O  
ATOM   4323  CB  THR A 518      26.668  -7.359 136.932  1.00 68.52           C  
ANISOU 4323  CB  THR A 518     6121  12644   7268    169  -2199    869       C  
ATOM   4324  OG1 THR A 518      26.126  -7.642 138.228  1.00 77.72           O  
ANISOU 4324  OG1 THR A 518     7356  14031   8144    197  -2243    988       O  
ATOM   4325  CG2 THR A 518      26.967  -8.666 136.213  1.00 55.73           C  
ANISOU 4325  CG2 THR A 518     4561  10766   5846    428  -2209   1197       C  
ATOM   4326  N   TYR A 519      28.057  -5.184 135.031  1.00 83.34           N  
ANISOU 4326  N   TYR A 519     7697  14391   9578   -213  -2049    157       N  
ATOM   4327  CA  TYR A 519      28.584  -4.888 133.702  1.00 72.28           C  
ANISOU 4327  CA  TYR A 519     6223  12756   8485   -262  -1957     29       C  
ATOM   4328  C   TYR A 519      29.399  -3.603 133.693  1.00 73.29           C  
ANISOU 4328  C   TYR A 519     6179  13010   8659   -519  -1873   -403       C  
ATOM   4329  O   TYR A 519      29.159  -2.702 132.882  1.00 74.44           O  
ANISOU 4329  O   TYR A 519     6380  12930   8975   -714  -1706   -654       O  
ATOM   4330  CB  TYR A 519      27.457  -4.823 132.678  1.00 72.85           C  
ANISOU 4330  CB  TYR A 519     6504  12464   8711   -298  -1840     92       C  
ATOM   4331  CG  TYR A 519      26.668  -6.099 132.638  1.00 72.95           C  
ANISOU 4331  CG  TYR A 519     6709  12306   8702    -60  -1893    520       C  
ATOM   4332  CD1 TYR A 519      27.117  -7.189 131.905  1.00 68.41           C  
ANISOU 4332  CD1 TYR A 519     6140  11531   8321    171  -1906    793       C  
ATOM   4333  CD2 TYR A 519      25.487  -6.222 133.349  1.00 80.21           C  
ANISOU 4333  CD2 TYR A 519     7820  13235   9422    -72  -1899    636       C  
ATOM   4334  CE1 TYR A 519      26.403  -8.365 131.876  1.00 76.15           C  
ANISOU 4334  CE1 TYR A 519     7340  12288   9305    368  -1905   1151       C  
ATOM   4335  CE2 TYR A 519      24.767  -7.384 133.326  1.00 84.07           C  
ANISOU 4335  CE2 TYR A 519     8505  13527   9910    118  -1906    999       C  
ATOM   4336  CZ  TYR A 519      25.226  -8.455 132.589  1.00 86.89           C  
ANISOU 4336  CZ  TYR A 519     8891  13652  10470    330  -1901   1247       C  
ATOM   4337  OH  TYR A 519      24.500  -9.621 132.568  1.00 95.73           O  
ANISOU 4337  OH  TYR A 519    10239  14526  11608    491  -1862   1564       O  
ATOM   4338  N   LYS A 520      30.371  -3.533 134.596  1.00 75.33           N  
ANISOU 4338  N   LYS A 520     6239  13613   8768   -520  -1971   -489       N  
ATOM   4339  CA  LYS A 520      31.325  -2.440 134.636  1.00 70.53           C  
ANISOU 4339  CA  LYS A 520     5450  13143   8206   -747  -1892   -877       C  
ATOM   4340  C   LYS A 520      32.310  -2.569 133.480  1.00 66.23           C  
ANISOU 4340  C   LYS A 520     4763  12435   7967   -715  -1831   -916       C  
ATOM   4341  O   LYS A 520      32.605  -3.670 133.008  1.00 59.00           O  
ANISOU 4341  O   LYS A 520     3806  11446   7166   -467  -1914   -622       O  
ATOM   4342  CB  LYS A 520      32.046  -2.448 135.984  1.00 64.20           C  
ANISOU 4342  CB  LYS A 520     4464  12798   7129   -736  -2033   -925       C  
ATOM   4343  CG  LYS A 520      31.673  -1.283 136.874  1.00 65.56           C  
ANISOU 4343  CG  LYS A 520     4670  13146   7094   -991  -1955  -1245       C  
ATOM   4344  CD  LYS A 520      32.112  -1.442 138.302  1.00 75.89           C  
ANISOU 4344  CD  LYS A 520     5830  14923   8083   -952  -2106  -1236       C  
ATOM   4345  CE  LYS A 520      31.123  -0.754 139.204  1.00 88.21           C  
ANISOU 4345  CE  LYS A 520     7530  16577   9407  -1107  -2042  -1377       C  
ATOM   4346  NZ  LYS A 520      31.836  -0.093 140.320  1.00102.43           N  
ANISOU 4346  NZ  LYS A 520     9136  18806  10977  -1250  -2074  -1645       N  
ATOM   4347  N   GLY A 521      32.769  -1.432 132.983  1.00 72.77           N  
ANISOU 4347  N   GLY A 521     5540  13168   8940   -967  -1654  -1279       N  
ATOM   4348  CA  GLY A 521      33.731  -1.404 131.896  1.00 81.93           C  
ANISOU 4348  CA  GLY A 521     6568  14170  10391   -977  -1554  -1361       C  
ATOM   4349  C   GLY A 521      34.574  -0.153 131.936  1.00 97.43           C  
ANISOU 4349  C   GLY A 521     8419  16200  12400  -1255  -1399  -1774       C  
ATOM   4350  O   GLY A 521      34.836   0.407 133.005  1.00104.01           O  
ANISOU 4350  O   GLY A 521     9167  17340  13012  -1375  -1445  -1958       O  
ATOM   4351  N   GLY A 522      34.996   0.293 130.754  1.00100.88           N  
ANISOU 4351  N   GLY A 522     8866  16339  13126  -1359  -1192  -1925       N  
ATOM   4352  CA  GLY A 522      35.931   1.396 130.652  1.00 93.14           C  
ANISOU 4352  CA  GLY A 522     7783  15383  12223  -1605  -1017  -2295       C  
ATOM   4353  C   GLY A 522      35.331   2.769 130.863  1.00 83.51           C  
ANISOU 4353  C   GLY A 522     6763  14011  10957  -1878   -800  -2615       C  
ATOM   4354  O   GLY A 522      36.089   3.726 131.056  1.00 67.17           O  
ANISOU 4354  O   GLY A 522     4605  12023   8894  -2085   -664  -2935       O  
ATOM   4355  N   LYS A 523      34.005   2.900 130.827  1.00 88.02           N  
ANISOU 4355  N   LYS A 523     7598  14359  11487  -1879   -749  -2540       N  
ATOM   4356  CA  LYS A 523      33.367   4.194 131.027  1.00 83.36           C  
ANISOU 4356  CA  LYS A 523     7213  13596  10864  -2108   -525  -2822       C  
ATOM   4357  C   LYS A 523      32.611   4.301 132.346  1.00 90.99           C  
ANISOU 4357  C   LYS A 523     8214  14836  11522  -2122   -650  -2827       C  
ATOM   4358  O   LYS A 523      31.898   5.286 132.556  1.00 89.72           O  
ANISOU 4358  O   LYS A 523     8238  14523  11327  -2279   -467  -3025       O  
ATOM   4359  CB  LYS A 523      32.441   4.523 129.847  1.00 79.19           C  
ANISOU 4359  CB  LYS A 523     6989  12537  10563  -2127   -295  -2788       C  
ATOM   4360  CG  LYS A 523      31.918   3.313 129.110  1.00 90.74           C  
ANISOU 4360  CG  LYS A 523     8499  13851  12129  -1903   -419  -2442       C  
ATOM   4361  CD  LYS A 523      31.362   3.684 127.752  1.00 89.25           C  
ANISOU 4361  CD  LYS A 523     8574  13128  12210  -1935   -157  -2446       C  
ATOM   4362  CE  LYS A 523      32.441   4.186 126.811  1.00 87.50           C  
ANISOU 4362  CE  LYS A 523     8318  12704  12223  -2023     63  -2604       C  
ATOM   4363  NZ  LYS A 523      31.951   4.205 125.402  1.00 86.29           N  
ANISOU 4363  NZ  LYS A 523     8422  12042  12322  -1978    281  -2507       N  
ATOM   4364  N   TYR A 524      32.749   3.321 133.235  1.00 96.30           N  
ANISOU 4364  N   TYR A 524     8725  15894  11970  -1948   -936  -2603       N  
ATOM   4365  CA  TYR A 524      32.312   3.479 134.615  1.00 90.40           C  
ANISOU 4365  CA  TYR A 524     7966  15478  10903  -1978  -1044  -2643       C  
ATOM   4366  C   TYR A 524      33.098   4.614 135.266  1.00 92.24           C  
ANISOU 4366  C   TYR A 524     8067  15923  11056  -2220   -924  -3041       C  
ATOM   4367  O   TYR A 524      34.313   4.727 135.080  1.00 99.43           O  
ANISOU 4367  O   TYR A 524     8768  16961  12051  -2270   -918  -3173       O  
ATOM   4368  CB  TYR A 524      32.547   2.190 135.400  1.00 94.15           C  
ANISOU 4368  CB  TYR A 524     8284  16323  11165  -1729  -1352  -2316       C  
ATOM   4369  CG  TYR A 524      32.146   2.315 136.859  1.00105.27           C  
ANISOU 4369  CG  TYR A 524     9679  18092  12228  -1754  -1454  -2346       C  
ATOM   4370  CD1 TYR A 524      30.876   2.714 137.227  1.00113.30           C  
ANISOU 4370  CD1 TYR A 524    10918  18999  13132  -1820  -1373  -2369       C  
ATOM   4371  CD2 TYR A 524      33.018   1.970 137.864  1.00111.36           C  
ANISOU 4371  CD2 TYR A 524    10212  19320  12781  -1695  -1632  -2333       C  
ATOM   4372  CE1 TYR A 524      30.511   2.819 138.555  1.00118.37           C  
ANISOU 4372  CE1 TYR A 524    11543  19972  13461  -1845  -1449  -2398       C  
ATOM   4373  CE2 TYR A 524      32.664   2.098 139.196  1.00117.76           C  
ANISOU 4373  CE2 TYR A 524    11006  20468  13268  -1723  -1710  -2368       C  
ATOM   4374  CZ  TYR A 524      31.411   2.493 139.534  1.00118.24           C  
ANISOU 4374  CZ  TYR A 524    11290  20409  13228  -1796  -1617  -2392       C  
ATOM   4375  OH  TYR A 524      31.060   2.601 140.858  1.00121.80           O  
ANISOU 4375  OH  TYR A 524    11720  21201  13359  -1824  -1683  -2424       O  
ATOM   4376  N   ARG A 525      32.403   5.472 136.011  1.00 86.10           N  
ANISOU 4376  N   ARG A 525     7405  15182  10125  -2374   -812  -3243       N  
ATOM   4377  CA  ARG A 525      33.058   6.505 136.804  1.00 88.51           C  
ANISOU 4377  CA  ARG A 525     7576  15737  10317  -2601   -704  -3619       C  
ATOM   4378  C   ARG A 525      32.699   6.364 138.277  1.00 90.79           C  
ANISOU 4378  C   ARG A 525     7796  16452  10250  -2588   -861  -3608       C  
ATOM   4379  O   ARG A 525      33.600   6.181 139.093  1.00106.81           O  
ANISOU 4379  O   ARG A 525     9573  18914  12097  -2591  -1009  -3672       O  
ATOM   4380  CB  ARG A 525      32.712   7.894 136.254  1.00 89.23           C  
ANISOU 4380  CB  ARG A 525     7864  15441  10600  -2833   -343  -3939       C  
ATOM   4381  CG  ARG A 525      33.427   8.236 134.946  1.00 91.71           C  
ANISOU 4381  CG  ARG A 525     8197  15411  11240  -2890   -150  -4029       C  
ATOM   4382  CD  ARG A 525      34.909   7.831 134.943  1.00 99.00           C  
ANISOU 4382  CD  ARG A 525     8808  16630  12178  -2880   -280  -4071       C  
ATOM   4383  NE  ARG A 525      35.242   6.785 133.971  1.00104.32           N  
ANISOU 4383  NE  ARG A 525     9441  17169  13029  -2679   -402  -3776       N  
ATOM   4384  CZ  ARG A 525      35.475   7.015 132.682  1.00106.78           C  
ANISOU 4384  CZ  ARG A 525     9852  17080  13639  -2706   -203  -3797       C  
ATOM   4385  NH1 ARG A 525      35.406   8.253 132.207  1.00111.82           N  
ANISOU 4385  NH1 ARG A 525    10656  17402  14428  -2909    130  -4076       N  
ATOM   4386  NH2 ARG A 525      35.779   6.015 131.865  1.00112.56           N  
ANISOU 4386  NH2 ARG A 525    10526  17722  14521  -2521   -316  -3531       N  
ATOM   4387  N   LYS A 526      31.420   6.427 138.632  1.00 83.30           N  
ANISOU 4387  N   LYS A 526     7057  15399   9195  -2569   -831  -3525       N  
ATOM   4388  CA  LYS A 526      30.920   6.010 139.936  1.00 90.09           C  
ANISOU 4388  CA  LYS A 526     7881  16631   9717  -2498  -1002  -3411       C  
ATOM   4389  C   LYS A 526      29.402   6.124 139.928  1.00 85.26           C  
ANISOU 4389  C   LYS A 526     7546  15765   9084  -2480   -913  -3314       C  
ATOM   4390  O   LYS A 526      28.851   7.106 139.421  1.00 79.22           O  
ANISOU 4390  O   LYS A 526     6956  14658   8486  -2632   -654  -3526       O  
ATOM   4391  CB  LYS A 526      31.485   6.846 141.089  1.00 94.57           C  
ANISOU 4391  CB  LYS A 526     8273  17587  10071  -2700   -956  -3754       C  
ATOM   4392  CG  LYS A 526      31.064   6.374 142.477  1.00 97.23           C  
ANISOU 4392  CG  LYS A 526     8555  18347  10043  -2622  -1137  -3630       C  
ATOM   4393  CD  LYS A 526      31.824   5.116 142.893  1.00103.62           C  
ANISOU 4393  CD  LYS A 526     9160  19521  10692  -2387  -1444  -3325       C  
ATOM   4394  CE  LYS A 526      31.492   4.689 144.323  1.00106.02           C  
ANISOU 4394  CE  LYS A 526     9404  20260  10618  -2312  -1606  -3207       C  
ATOM   4395  NZ  LYS A 526      30.410   3.664 144.400  1.00100.74           N  
ANISOU 4395  NZ  LYS A 526     8928  19481   9868  -2079  -1720  -2790       N  
ATOM   4396  N   VAL A 527      28.733   5.108 140.477  1.00 95.72           N  
ANISOU 4396  N   VAL A 527     8912  17247  10209  -2283  -1114  -2982       N  
ATOM   4397  CA  VAL A 527      27.283   5.100 140.629  1.00103.73           C  
ANISOU 4397  CA  VAL A 527    10161  18094  11158  -2255  -1058  -2871       C  
ATOM   4398  C   VAL A 527      26.952   4.839 142.092  1.00107.32           C  
ANISOU 4398  C   VAL A 527    10556  18965  11256  -2227  -1180  -2812       C  
ATOM   4399  O   VAL A 527      27.670   4.118 142.794  1.00116.61           O  
ANISOU 4399  O   VAL A 527    11550  20514  12244  -2113  -1384  -2668       O  
ATOM   4400  CB  VAL A 527      26.623   4.055 139.701  1.00108.28           C  
ANISOU 4400  CB  VAL A 527    10886  18386  11871  -2038  -1151  -2492       C  
ATOM   4401  CG1 VAL A 527      27.020   4.311 138.249  1.00107.20           C  
ANISOU 4401  CG1 VAL A 527    10791  17856  12085  -2071  -1026  -2559       C  
ATOM   4402  CG2 VAL A 527      27.008   2.645 140.118  1.00114.94           C  
ANISOU 4402  CG2 VAL A 527    11611  19499  12563  -1788  -1425  -2114       C  
ATOM   4403  N   THR A 528      25.857   5.440 142.555  1.00102.72           N  
ANISOU 4403  N   THR A 528    10129  18315  10584  -2326  -1043  -2923       N  
ATOM   4404  CA  THR A 528      25.535   5.444 143.974  1.00 98.48           C  
ANISOU 4404  CA  THR A 528     9536  18163   9718  -2352  -1103  -2944       C  
ATOM   4405  C   THR A 528      24.069   5.100 144.201  1.00 90.05           C  
ANISOU 4405  C   THR A 528     8680  16977   8557  -2269  -1087  -2741       C  
ATOM   4406  O   THR A 528      23.202   5.439 143.386  1.00 86.60           O  
ANISOU 4406  O   THR A 528     8439  16152   8312  -2294   -938  -2758       O  
ATOM   4407  CB  THR A 528      25.853   6.803 144.611  1.00 98.78           C  
ANISOU 4407  CB  THR A 528     9490  18336   9707  -2626   -912  -3402       C  
ATOM   4408  OG1 THR A 528      25.359   7.850 143.768  1.00 96.71           O  
ANISOU 4408  OG1 THR A 528     9398  17633   9715  -2777   -633  -3639       O  
ATOM   4409  CG2 THR A 528      27.358   6.972 144.783  1.00105.22           C  
ANISOU 4409  CG2 THR A 528    10041  19432  10507  -2700   -978  -3582       C  
ATOM   4410  N   PHE A 529      23.803   4.428 145.328  1.00 86.46           N  
ANISOU 4410  N   PHE A 529     8181  16867   7801  -2170  -1234  -2548       N  
ATOM   4411  CA  PHE A 529      22.440   4.032 145.664  1.00 84.48           C  
ANISOU 4411  CA  PHE A 529     8115  16547   7435  -2091  -1220  -2342       C  
ATOM   4412  C   PHE A 529      21.592   5.245 146.012  1.00 86.04           C  
ANISOU 4412  C   PHE A 529     8414  16654   7622  -2301   -985  -2670       C  
ATOM   4413  O   PHE A 529      20.395   5.272 145.716  1.00 89.72           O  
ANISOU 4413  O   PHE A 529     9073  16873   8143  -2278   -888  -2593       O  
ATOM   4414  CB  PHE A 529      22.452   3.023 146.814  1.00 94.80           C  
ANISOU 4414  CB  PHE A 529     9349  18243   8429  -1935  -1414  -2055       C  
ATOM   4415  CG  PHE A 529      21.124   2.349 147.056  1.00 92.84           C  
ANISOU 4415  CG  PHE A 529     9290  17904   8082  -1816  -1416  -1764       C  
ATOM   4416  CD1 PHE A 529      20.798   1.171 146.400  1.00 93.32           C  
ANISOU 4416  CD1 PHE A 529     9457  17764   8238  -1596  -1516  -1361       C  
ATOM   4417  CD2 PHE A 529      20.208   2.883 147.951  1.00 90.82           C  
ANISOU 4417  CD2 PHE A 529     9101  17763   7643  -1929  -1305  -1897       C  
ATOM   4418  CE1 PHE A 529      19.580   0.543 146.625  1.00 89.97           C  
ANISOU 4418  CE1 PHE A 529     9201  17253   7729  -1500  -1499  -1098       C  
ATOM   4419  CE2 PHE A 529      18.990   2.260 148.179  1.00 88.25           C  
ANISOU 4419  CE2 PHE A 529     8941  17362   7230  -1826  -1295  -1634       C  
ATOM   4420  CZ  PHE A 529      18.675   1.091 147.514  1.00 88.89           C  
ANISOU 4420  CZ  PHE A 529     9125  17242   7407  -1616  -1389  -1235       C  
ATOM   4421  N   GLN A 530      22.193   6.263 146.632  1.00 91.89           N  
ANISOU 4421  N   GLN A 530     9024  17587   8302  -2507   -882  -3042       N  
ATOM   4422  CA  GLN A 530      21.471   7.512 146.853  1.00 89.15           C  
ANISOU 4422  CA  GLN A 530     8776  17094   8003  -2713   -623  -3379       C  
ATOM   4423  C   GLN A 530      20.994   8.099 145.527  1.00 92.79           C  
ANISOU 4423  C   GLN A 530     9422  17025   8809  -2748   -422  -3465       C  
ATOM   4424  O   GLN A 530      19.832   8.509 145.389  1.00 83.83           O  
ANISOU 4424  O   GLN A 530     8471  15647   7736  -2770   -265  -3499       O  
ATOM   4425  CB  GLN A 530      22.360   8.511 147.602  1.00 83.03           C  
ANISOU 4425  CB  GLN A 530     7815  16585   7148  -2939   -532  -3775       C  
ATOM   4426  CG  GLN A 530      23.395   7.890 148.541  1.00102.90           C  
ANISOU 4426  CG  GLN A 530    10087  19621   9389  -2891   -765  -3705       C  
ATOM   4427  CD  GLN A 530      23.998   8.913 149.483  1.00124.50           C  
ANISOU 4427  CD  GLN A 530    12650  22666  11989  -3135   -662  -4115       C  
ATOM   4428  OE1 GLN A 530      23.633  10.086 149.452  1.00132.38           O  
ANISOU 4428  OE1 GLN A 530    13717  23470  13110  -3342   -405  -4447       O  
ATOM   4429  NE2 GLN A 530      24.929   8.475 150.322  1.00124.06           N  
ANISOU 4429  NE2 GLN A 530    12365  23089  11683  -3108   -857  -4094       N  
ATOM   4430  N   CYS A 531      21.879   8.113 144.527  1.00 99.21           N  
ANISOU 4430  N   CYS A 531    10189  17654   9852  -2741   -425  -3488       N  
ATOM   4431  CA  CYS A 531      21.535   8.678 143.226  1.00 97.61           C  
ANISOU 4431  CA  CYS A 531    10160  16943   9983  -2769   -228  -3565       C  
ATOM   4432  C   CYS A 531      20.461   7.853 142.532  1.00 82.82           C  
ANISOU 4432  C   CYS A 531     8474  14825   8168  -2582   -297  -3239       C  
ATOM   4433  O   CYS A 531      19.514   8.407 141.966  1.00 72.63           O  
ANISOU 4433  O   CYS A 531     7378  13184   7035  -2606   -108  -3305       O  
ATOM   4434  CB  CYS A 531      22.781   8.778 142.349  1.00101.87           C  
ANISOU 4434  CB  CYS A 531    10597  17370  10739  -2796   -226  -3640       C  
ATOM   4435  SG  CYS A 531      22.650   9.960 140.993  1.00107.62           S  
ANISOU 4435  SG  CYS A 531    11510  17506  11875  -2912    112  -3870       S  
ATOM   4436  N   LEU A 532      20.605   6.526 142.544  1.00 72.24           N  
ANISOU 4436  N   LEU A 532     7079  13656   6713  -2389   -556  -2879       N  
ATOM   4437  CA  LEU A 532      19.583   5.663 141.957  1.00 67.37           C  
ANISOU 4437  CA  LEU A 532     6625  12843   6131  -2218   -627  -2555       C  
ATOM   4438  C   LEU A 532      18.235   5.885 142.624  1.00 72.33           C  
ANISOU 4438  C   LEU A 532     7388  13488   6606  -2237   -533  -2561       C  
ATOM   4439  O   LEU A 532      17.197   6.012 141.952  1.00 68.76           O  
ANISOU 4439  O   LEU A 532     7118  12731   6276  -2208   -423  -2524       O  
ATOM   4440  CB  LEU A 532      20.016   4.202 142.081  1.00 68.18           C  
ANISOU 4440  CB  LEU A 532     6634  13158   6115  -2008   -901  -2160       C  
ATOM   4441  CG  LEU A 532      21.095   3.700 141.125  1.00 78.15           C  
ANISOU 4441  CG  LEU A 532     7801  14315   7577  -1924  -1005  -2056       C  
ATOM   4442  CD1 LEU A 532      21.062   2.198 141.056  1.00 85.27           C  
ANISOU 4442  CD1 LEU A 532     8695  15290   8414  -1679  -1225  -1607       C  
ATOM   4443  CD2 LEU A 532      20.935   4.288 139.732  1.00 62.76           C  
ANISOU 4443  CD2 LEU A 532     5974  11919   5954  -1988   -842  -2188       C  
ATOM   4444  N   LYS A 533      18.239   5.934 143.956  1.00 77.63           N  
ANISOU 4444  N   LYS A 533     7965  14526   7005  -2286   -571  -2612       N  
ATOM   4445  CA  LYS A 533      17.005   6.088 144.710  1.00 71.96           C  
ANISOU 4445  CA  LYS A 533     7353  13867   6123  -2303   -487  -2610       C  
ATOM   4446  C   LYS A 533      16.307   7.388 144.347  1.00 72.43           C  
ANISOU 4446  C   LYS A 533     7549  13609   6361  -2447   -201  -2933       C  
ATOM   4447  O   LYS A 533      15.092   7.413 144.096  1.00 72.95           O  
ANISOU 4447  O   LYS A 533     7782  13475   6459  -2397   -103  -2868       O  
ATOM   4448  CB  LYS A 533      17.301   6.048 146.207  1.00 82.98           C  
ANISOU 4448  CB  LYS A 533     8605  15716   7208  -2356   -561  -2659       C  
ATOM   4449  CG  LYS A 533      16.059   5.997 147.043  1.00 94.74           C  
ANISOU 4449  CG  LYS A 533    10193  17299   8506  -2351   -500  -2601       C  
ATOM   4450  CD  LYS A 533      16.330   5.519 148.434  1.00 94.05           C  
ANISOU 4450  CD  LYS A 533     9977  17669   8089  -2335   -635  -2512       C  
ATOM   4451  CE  LYS A 533      15.024   5.444 149.190  1.00 93.13           C  
ANISOU 4451  CE  LYS A 533     9973  17612   7801  -2328   -557  -2443       C  
ATOM   4452  NZ  LYS A 533      15.262   5.100 150.615  1.00 88.83           N  
ANISOU 4452  NZ  LYS A 533     9311  17516   6923  -2333   -664  -2392       N  
ATOM   4453  N   SER A 534      17.069   8.482 144.305  1.00 68.16           N  
ANISOU 4453  N   SER A 534     6942  13005   5950  -2619    -48  -3275       N  
ATOM   4454  CA  SER A 534      16.491   9.788 144.000  1.00 83.52           C  
ANISOU 4454  CA  SER A 534     9023  14614   8096  -2747    256  -3574       C  
ATOM   4455  C   SER A 534      16.090   9.910 142.524  1.00 79.25           C  
ANISOU 4455  C   SER A 534     8666  13579   7865  -2663    369  -3510       C  
ATOM   4456  O   SER A 534      15.127  10.605 142.192  1.00 77.53           O  
ANISOU 4456  O   SER A 534     8624  13047   7786  -2662    587  -3603       O  
ATOM   4457  CB  SER A 534      17.473  10.891 144.360  1.00102.38           C  
ANISOU 4457  CB  SER A 534    11288  17061  10549  -2956    403  -3935       C  
ATOM   4458  OG  SER A 534      18.046  10.698 145.648  1.00112.36           O  
ANISOU 4458  OG  SER A 534    12356  18817  11520  -3029    268  -3994       O  
ATOM   4459  N   ILE A 535      16.805   9.234 141.621  1.00 75.11           N  
ANISOU 4459  N   ILE A 535     8106  12975   7458  -2577    228  -3343       N  
ATOM   4460  CA  ILE A 535      16.366   9.128 140.231  1.00 55.51           C  
ANISOU 4460  CA  ILE A 535     5797  10061   5234  -2476    296  -3232       C  
ATOM   4461  C   ILE A 535      14.969   8.522 140.190  1.00 60.69           C  
ANISOU 4461  C   ILE A 535     6599  10670   5792  -2340    258  -3017       C  
ATOM   4462  O   ILE A 535      14.066   9.032 139.518  1.00 64.43           O  
ANISOU 4462  O   ILE A 535     7262  10788   6430  -2298    451  -3065       O  
ATOM   4463  CB  ILE A 535      17.371   8.285 139.423  1.00 59.25           C  
ANISOU 4463  CB  ILE A 535     6175  10532   5804  -2399    106  -3050       C  
ATOM   4464  CG1 ILE A 535      18.574   9.107 139.023  1.00 68.52           C  
ANISOU 4464  CG1 ILE A 535     7269  11586   7177  -2528    237  -3292       C  
ATOM   4465  CG2 ILE A 535      16.691   7.713 138.197  1.00 56.79           C  
ANISOU 4465  CG2 ILE A 535     6026   9891   5659  -2259     84  -2833       C  
ATOM   4466  CD1 ILE A 535      19.822   8.289 138.728  1.00 71.82           C  
ANISOU 4466  CD1 ILE A 535     7507  12177   7604  -2477     22  -3156       C  
ATOM   4467  N   ALA A 536      14.769   7.430 140.938  1.00 64.47           N  
ANISOU 4467  N   ALA A 536     6992  11507   5999  -2255     27  -2761       N  
ATOM   4468  CA  ALA A 536      13.475   6.750 140.922  1.00 62.13           C  
ANISOU 4468  CA  ALA A 536     6816  11196   5594  -2129    -12  -2525       C  
ATOM   4469  C   ALA A 536      12.383   7.626 141.527  1.00 73.24           C  
ANISOU 4469  C   ALA A 536     8328  12550   6949  -2184    216  -2719       C  
ATOM   4470  O   ALA A 536      11.261   7.695 141.002  1.00 77.48           O  
ANISOU 4470  O   ALA A 536     9025  12844   7572  -2091    338  -2658       O  
ATOM   4471  CB  ALA A 536      13.587   5.419 141.661  1.00 61.29           C  
ANISOU 4471  CB  ALA A 536     6598  11459   5228  -2021   -276  -2181       C  
ATOM   4472  N   TRP A 537      12.695   8.296 142.640  1.00 66.57           N  
ANISOU 4472  N   TRP A 537     7386  11926   5982  -2318    283  -2938       N  
ATOM   4473  CA  TRP A 537      11.738   9.210 143.256  1.00 69.78           C  
ANISOU 4473  CA  TRP A 537     7876  12269   6366  -2380    510  -3141       C  
ATOM   4474  C   TRP A 537      11.328  10.318 142.292  1.00 71.75           C  
ANISOU 4474  C   TRP A 537     8294  12028   6939  -2379    792  -3334       C  
ATOM   4475  O   TRP A 537      10.139  10.648 142.178  1.00 68.00           O  
ANISOU 4475  O   TRP A 537     7958  11362   6517  -2297    956  -3334       O  
ATOM   4476  CB  TRP A 537      12.338   9.824 144.518  1.00 81.67           C  
ANISOU 4476  CB  TRP A 537     9237  14077   7717  -2550    536  -3376       C  
ATOM   4477  CG  TRP A 537      12.524   8.915 145.702  1.00 86.42           C  
ANISOU 4477  CG  TRP A 537     9696  15161   7978  -2535    314  -3202       C  
ATOM   4478  CD1 TRP A 537      13.679   8.722 146.404  1.00 91.73           C  
ANISOU 4478  CD1 TRP A 537    10181  16175   8498  -2606    166  -3238       C  
ATOM   4479  CD2 TRP A 537      11.528   8.108 146.343  1.00 85.10           C  
ANISOU 4479  CD2 TRP A 537     9568  15180   7586  -2433    237  -2958       C  
ATOM   4480  NE1 TRP A 537      13.468   7.839 147.431  1.00 92.40           N  
ANISOU 4480  NE1 TRP A 537    10197  16631   8279  -2539     -1  -3019       N  
ATOM   4481  CE2 TRP A 537      12.157   7.444 147.416  1.00 87.01           C  
ANISOU 4481  CE2 TRP A 537     9656  15852   7553  -2440     44  -2840       C  
ATOM   4482  CE3 TRP A 537      10.169   7.871 146.107  1.00 86.00           C  
ANISOU 4482  CE3 TRP A 537     9829  15138   7709  -2330    323  -2820       C  
ATOM   4483  CZ2 TRP A 537      11.476   6.564 148.253  1.00 90.57           C  
ANISOU 4483  CZ2 TRP A 537    10112  16550   7751  -2351    -54  -2580       C  
ATOM   4484  CZ3 TRP A 537       9.492   6.995 146.942  1.00 87.53           C  
ANISOU 4484  CZ3 TRP A 537    10012  15597   7651  -2258    226  -2574       C  
ATOM   4485  CH2 TRP A 537      10.147   6.352 148.000  1.00 87.82           C  
ANISOU 4485  CH2 TRP A 537     9911  16030   7428  -2270     44  -2451       C  
ATOM   4486  N   ARG A 538      12.306  10.932 141.621  1.00 77.60           N  
ANISOU 4486  N   ARG A 538     9022  12555   7908  -2454    868  -3484       N  
ATOM   4487  CA  ARG A 538      12.006  11.958 140.629  1.00 70.04           C  
ANISOU 4487  CA  ARG A 538     8237  11091   7282  -2423   1143  -3605       C  
ATOM   4488  C   ARG A 538      11.137  11.398 139.514  1.00 65.22           C  
ANISOU 4488  C   ARG A 538     7793  10203   6787  -2214   1144  -3376       C  
ATOM   4489  O   ARG A 538      10.239  12.084 139.010  1.00 50.46           O  
ANISOU 4489  O   ARG A 538     6088   7986   5100  -2107   1370  -3395       O  
ATOM   4490  CB  ARG A 538      13.308  12.524 140.061  1.00 62.61           C  
ANISOU 4490  CB  ARG A 538     7240   9997   6550  -2533   1204  -3746       C  
ATOM   4491  CG  ARG A 538      14.154  13.293 141.062  1.00 65.15           C  
ANISOU 4491  CG  ARG A 538     7403  10552   6799  -2752   1267  -4021       C  
ATOM   4492  CD  ARG A 538      14.333  14.738 140.646  1.00 70.85           C  
ANISOU 4492  CD  ARG A 538     8220  10888   7813  -2848   1589  -4247       C  
ATOM   4493  NE  ARG A 538      15.125  15.487 141.616  1.00 88.73           N  
ANISOU 4493  NE  ARG A 538    10324  13387  10000  -3080   1665  -4536       N  
ATOM   4494  CZ  ARG A 538      15.542  16.733 141.425  1.00 95.48           C  
ANISOU 4494  CZ  ARG A 538    11212  13989  11076  -3217   1935  -4760       C  
ATOM   4495  NH1 ARG A 538      15.234  17.366 140.304  1.00101.59           N  
ANISOU 4495  NH1 ARG A 538    12181  14263  12156  -3124   2149  -4692       N  
ATOM   4496  NH2 ARG A 538      16.260  17.349 142.351  1.00 94.74           N  
ANISOU 4496  NH2 ARG A 538    10959  14149  10891  -3443   1998  -5039       N  
ATOM   4497  N   ALA A 539      11.400  10.156 139.106  1.00 68.62           N  
ANISOU 4497  N   ALA A 539     8174  10782   7115  -2142    893  -3143       N  
ATOM   4498  CA  ALA A 539      10.564   9.525 138.092  1.00 69.72           C  
ANISOU 4498  CA  ALA A 539     8427  10637   7427  -1887    862  -2774       C  
ATOM   4499  C   ALA A 539       9.122   9.401 138.566  1.00 72.81           C  
ANISOU 4499  C   ALA A 539     8876  11077   7710  -1778    922  -2667       C  
ATOM   4500  O   ALA A 539       8.184   9.601 137.786  1.00 64.07           O  
ANISOU 4500  O   ALA A 539     7895   9656   6792  -1603   1048  -2543       O  
ATOM   4501  CB  ALA A 539      11.132   8.154 137.721  1.00 68.72           C  
ANISOU 4501  CB  ALA A 539     8203  10640   7267  -1795    568  -2430       C  
ATOM   4502  N   PHE A 540       8.924   9.078 139.843  1.00 79.55           N  
ANISOU 4502  N   PHE A 540     9630  12342   8253  -1875    837  -2712       N  
ATOM   4503  CA  PHE A 540       7.555   8.959 140.340  1.00 76.78           C  
ANISOU 4503  CA  PHE A 540     9323  12054   7795  -1786    913  -2622       C  
ATOM   4504  C   PHE A 540       6.874  10.323 140.426  1.00 64.98           C  
ANISOU 4504  C   PHE A 540     7940  10337   6412  -1807   1237  -2932       C  
ATOM   4505  O   PHE A 540       5.693  10.456 140.077  1.00 53.36           O  
ANISOU 4505  O   PHE A 540     6551   8674   5050  -1641   1362  -2822       O  
ATOM   4506  CB  PHE A 540       7.537   8.244 141.691  1.00 78.19           C  
ANISOU 4506  CB  PHE A 540     9380  12735   7594  -1883    753  -2575       C  
ATOM   4507  CG  PHE A 540       7.446   6.747 141.573  1.00 68.44           C  
ANISOU 4507  CG  PHE A 540     8091  11638   6274  -1760    499  -2146       C  
ATOM   4508  CD1 PHE A 540       6.214   6.119 141.481  1.00 70.59           C  
ANISOU 4508  CD1 PHE A 540     8409  11861   6550  -1622    512  -1886       C  
ATOM   4509  CD2 PHE A 540       8.592   5.970 141.532  1.00 69.45           C  
ANISOU 4509  CD2 PHE A 540     8120  11933   6335  -1782    264  -2008       C  
ATOM   4510  CE1 PHE A 540       6.128   4.742 141.356  1.00 56.75           C  
ANISOU 4510  CE1 PHE A 540     6624  10199   4741  -1528    310  -1505       C  
ATOM   4511  CE2 PHE A 540       8.511   4.594 141.413  1.00 64.78           C  
ANISOU 4511  CE2 PHE A 540     7500  11428   5686  -1659     60  -1611       C  
ATOM   4512  CZ  PHE A 540       7.277   3.980 141.328  1.00 53.09           C  
ANISOU 4512  CZ  PHE A 540     6084   9873   4214  -1542     91  -1363       C  
ATOM   4513  N   LEU A 541       7.605  11.350 140.866  1.00 62.35           N  
ANISOU 4513  N   LEU A 541     7588   9976   6126  -1976   1357  -3241       N  
ATOM   4514  CA  LEU A 541       7.021  12.690 140.914  1.00 71.65           C  
ANISOU 4514  CA  LEU A 541     8869  10850   7507  -1959   1647  -3431       C  
ATOM   4515  C   LEU A 541       6.654  13.187 139.520  1.00 73.69           C  
ANISOU 4515  C   LEU A 541     9292  10614   8094  -1772   1817  -3354       C  
ATOM   4516  O   LEU A 541       5.608  13.828 139.339  1.00 65.04           O  
ANISOU 4516  O   LEU A 541     8298   9284   7130  -1625   2010  -3343       O  
ATOM   4517  CB  LEU A 541       7.976  13.674 141.590  1.00 71.42           C  
ANISOU 4517  CB  LEU A 541     8770  10854   7511  -2179   1727  -3713       C  
ATOM   4518  CG  LEU A 541       8.483  13.367 142.999  1.00 75.23           C  
ANISOU 4518  CG  LEU A 541     9076  11826   7684  -2366   1576  -3816       C  
ATOM   4519  CD1 LEU A 541       9.823  14.064 143.231  1.00 69.00           C  
ANISOU 4519  CD1 LEU A 541     8183  11074   6961  -2575   1603  -4053       C  
ATOM   4520  CD2 LEU A 541       7.464  13.783 144.045  1.00 86.72           C  
ANISOU 4520  CD2 LEU A 541    10545  13396   9009  -2380   1697  -3911       C  
ATOM   4521  N   ALA A 542       7.509  12.911 138.529  1.00 82.12           N  
ANISOU 4521  N   ALA A 542    10381  11522   9298  -1760   1744  -3283       N  
ATOM   4522  CA  ALA A 542       7.241  13.346 137.162  1.00 73.72           C  
ANISOU 4522  CA  ALA A 542     9477   9993   8539  -1570   1892  -3171       C  
ATOM   4523  C   ALA A 542       5.890  12.838 136.683  1.00 58.96           C  
ANISOU 4523  C   ALA A 542     7669   8057   6676  -1321   1903  -2943       C  
ATOM   4524  O   ALA A 542       5.112  13.584 136.078  1.00 59.53           O  
ANISOU 4524  O   ALA A 542     7864   7807   6948  -1138   2102  -2908       O  
ATOM   4525  CB  ALA A 542       8.357  12.867 136.233  1.00 68.78           C  
ANISOU 4525  CB  ALA A 542     8848   9271   8014  -1598   1773  -3099       C  
ATOM   4526  N   VAL A 543       5.587  11.569 136.958  1.00 58.51           N  
ANISOU 4526  N   VAL A 543     7494   8293   6443  -1280   1635  -2671       N  
ATOM   4527  CA  VAL A 543       4.303  11.013 136.548  1.00 63.19           C  
ANISOU 4527  CA  VAL A 543     8095   8847   7068  -1056   1593  -2388       C  
ATOM   4528  C   VAL A 543       3.173  11.598 137.387  1.00 68.78           C  
ANISOU 4528  C   VAL A 543     8803   9643   7688  -1031   1784  -2533       C  
ATOM   4529  O   VAL A 543       2.145  12.031 136.853  1.00 67.71           O  
ANISOU 4529  O   VAL A 543     8732   9295   7700   -828   1934  -2469       O  
ATOM   4530  CB  VAL A 543       4.327   9.476 136.628  1.00 56.65           C  
ANISOU 4530  CB  VAL A 543     7150   8283   6091  -1046   1283  -2072       C  
ATOM   4531  CG1 VAL A 543       3.015   8.904 136.118  1.00 39.76           C  
ANISOU 4531  CG1 VAL A 543     5008   6091   4007   -841   1252  -1804       C  
ATOM   4532  CG2 VAL A 543       5.493   8.928 135.825  1.00 42.20           C  
ANISOU 4532  CG2 VAL A 543     5317   6361   4356  -1066   1114  -1949       C  
ATOM   4533  N   LEU A 544       3.345  11.631 138.713  1.00 65.48           N  
ANISOU 4533  N   LEU A 544     8306   9556   7018  -1228   1785  -2733       N  
ATOM   4534  CA  LEU A 544       2.228  12.004 139.575  1.00 63.03           C  
ANISOU 4534  CA  LEU A 544     7980   9376   6591  -1207   1949  -2846       C  
ATOM   4535  C   LEU A 544       1.825  13.468 139.426  1.00 78.06           C  
ANISOU 4535  C   LEU A 544     9998  10931   8730  -1125   2231  -3031       C  
ATOM   4536  O   LEU A 544       0.675  13.808 139.726  1.00 88.45           O  
ANISOU 4536  O   LEU A 544    11316  12230  10061  -1001   2363  -3022       O  
ATOM   4537  CB  LEU A 544       2.554  11.699 141.039  1.00 67.91           C  
ANISOU 4537  CB  LEU A 544     8491  10430   6883  -1431   1856  -2976       C  
ATOM   4538  CG  LEU A 544       2.936  10.259 141.404  1.00 65.71           C  
ANISOU 4538  CG  LEU A 544     8095  10511   6359  -1494   1547  -2721       C  
ATOM   4539  CD1 LEU A 544       3.438  10.179 142.840  1.00 74.11           C  
ANISOU 4539  CD1 LEU A 544     9067  11985   7105  -1708   1473  -2878       C  
ATOM   4540  CD2 LEU A 544       1.781   9.296 141.172  1.00 60.50           C  
ANISOU 4540  CD2 LEU A 544     7399   9892   5696  -1326   1460  -2377       C  
ATOM   4541  N   LYS A 545       2.726  14.342 138.966  1.00 74.18           N  
ANISOU 4541  N   LYS A 545     9594  10152   8440  -1180   2309  -3150       N  
ATOM   4542  CA  LYS A 545       2.353  15.749 138.820  1.00 72.59           C  
ANISOU 4542  CA  LYS A 545     9508   9603   8470  -1094   2555  -3254       C  
ATOM   4543  C   LYS A 545       1.370  15.986 137.671  1.00 75.06           C  
ANISOU 4543  C   LYS A 545     9920   9601   8999   -773   2662  -3047       C  
ATOM   4544  O   LYS A 545       0.755  17.056 137.612  1.00 94.85           O  
ANISOU 4544  O   LYS A 545    12510  11871  11658   -646   2856  -3083       O  
ATOM   4545  CB  LYS A 545       3.616  16.612 138.645  1.00 73.61           C  
ANISOU 4545  CB  LYS A 545     9690   9530   8747  -1264   2618  -3414       C  
ATOM   4546  CG  LYS A 545       3.373  18.135 138.551  1.00 90.04           C  
ANISOU 4546  CG  LYS A 545    11903  11236  11071  -1199   2884  -3505       C  
ATOM   4547  CD  LYS A 545       4.658  18.962 138.426  1.00106.56           C  
ANISOU 4547  CD  LYS A 545    13957  13427  13104  -1453   3001  -3807       C  
ATOM   4548  CE  LYS A 545       4.335  20.456 138.314  1.00116.97           C  
ANISOU 4548  CE  LYS A 545    15419  14349  14674  -1389   3283  -3880       C  
ATOM   4549  NZ  LYS A 545       5.550  21.322 138.189  1.00126.88           N  
ANISOU 4549  NZ  LYS A 545    16650  15691  15867  -1575   3440  -4165       N  
ATOM   4550  N   ARG A 546       1.176  15.019 136.772  1.00 64.98           N  
ANISOU 4550  N   ARG A 546     8626   8334   7729   -631   2540  -2827       N  
ATOM   4551  CA  ARG A 546       0.130  15.182 135.769  1.00 74.44           C  
ANISOU 4551  CA  ARG A 546     9881   9302   9099   -315   2623  -2625       C  
ATOM   4552  C   ARG A 546      -1.267  15.086 136.365  1.00 90.89           C  
ANISOU 4552  C   ARG A 546    11876  11565  11095   -188   2691  -2601       C  
ATOM   4553  O   ARG A 546      -2.232  15.533 135.733  1.00102.86           O  
ANISOU 4553  O   ARG A 546    13422  12901  12760     83   2794  -2478       O  
ATOM   4554  CB  ARG A 546       0.282  14.151 134.657  1.00 69.30           C  
ANISOU 4554  CB  ARG A 546     9221   8628   8482   -208   2471  -2398       C  
ATOM   4555  CG  ARG A 546       1.713  13.814 134.339  1.00 63.72           C  
ANISOU 4555  CG  ARG A 546     8540   7888   7780   -388   2328  -2410       C  
ATOM   4556  CD  ARG A 546       1.763  12.887 133.146  1.00 60.36           C  
ANISOU 4556  CD  ARG A 546     8105   7398   7431   -243   2100  -2073       C  
ATOM   4557  NE  ARG A 546       0.839  13.327 132.106  1.00 52.06           N  
ANISOU 4557  NE  ARG A 546     7137   6088   6554     60   2214  -1917       N  
ATOM   4558  CZ  ARG A 546       0.594  12.650 130.992  1.00 57.54           C  
ANISOU 4558  CZ  ARG A 546     7827   6723   7313    230   2049  -1633       C  
ATOM   4559  NH1 ARG A 546       1.209  11.493 130.777  1.00 53.64           N  
ANISOU 4559  NH1 ARG A 546     7261   6376   6743    121   1782  -1481       N  
ATOM   4560  NH2 ARG A 546      -0.265  13.130 130.100  1.00 57.85           N  
ANISOU 4560  NH2 ARG A 546     7931   6565   7485    516   2154  -1506       N  
ATOM   4561  N   ARG A 547      -1.398  14.500 137.553  1.00 93.04           N  
ANISOU 4561  N   ARG A 547    12027  12209  11116   -371   2625  -2699       N  
ATOM   4562  CA  ARG A 547      -2.633  14.607 138.317  1.00 92.86           C  
ANISOU 4562  CA  ARG A 547    11922  12352  11008   -295   2720  -2718       C  
ATOM   4563  C   ARG A 547      -2.286  15.071 139.728  1.00100.04           C  
ANISOU 4563  C   ARG A 547    12819  13437  11755   -534   2762  -2958       C  
ATOM   4564  O   ARG A 547      -2.564  14.380 140.717  1.00101.37           O  
ANISOU 4564  O   ARG A 547    12875  13967  11675   -663   2683  -2974       O  
ATOM   4565  CB  ARG A 547      -3.405  13.285 138.303  1.00 83.95           C  
ANISOU 4565  CB  ARG A 547    10635  11532   9728   -251   2579  -2517       C  
ATOM   4566  CG  ARG A 547      -3.910  12.914 136.903  1.00 77.79           C  
ANISOU 4566  CG  ARG A 547     9848  10561   9148     12   2470  -2212       C  
ATOM   4567  CD  ARG A 547      -5.003  11.853 136.906  1.00 70.88           C  
ANISOU 4567  CD  ARG A 547     8800   9937   8193     91   2311  -1966       C  
ATOM   4568  NE  ARG A 547      -4.674  10.759 135.993  1.00 71.18           N  
ANISOU 4568  NE  ARG A 547     8808   9975   8261    106   2032  -1684       N  
ATOM   4569  CZ  ARG A 547      -3.989   9.678 136.352  1.00 76.29           C  
ANISOU 4569  CZ  ARG A 547     9415  10820   8753    -94   1809  -1581       C  
ATOM   4570  NH1 ARG A 547      -3.576   9.548 137.605  1.00 63.31           N  
ANISOU 4570  NH1 ARG A 547     7746   9417   6891   -314   1815  -1722       N  
ATOM   4571  NH2 ARG A 547      -3.717   8.725 135.469  1.00 85.02           N  
ANISOU 4571  NH2 ARG A 547    10505  11888   9912    -66   1585  -1337       N  
ATOM   4572  N   THR A 548      -1.725  16.280 139.853  1.00103.92           N  
ANISOU 4572  N   THR A 548    13424  13679  12382   -606   2883  -3136       N  
ATOM   4573  CA  THR A 548      -1.356  16.867 141.164  1.00114.28           C  
ANISOU 4573  CA  THR A 548    14730  15100  13589   -804   2977  -3391       C  
ATOM   4574  C   THR A 548      -2.524  17.575 141.889  1.00124.75           C  
ANISOU 4574  C   THR A 548    15994  16591  14816   -713   3078  -3404       C  
ATOM   4575  O   THR A 548      -2.341  18.339 142.837  1.00100.52           O  
ANISOU 4575  O   THR A 548    12835  13860  11499   -885   3020  -3492       O  
ATOM   4576  CB  THR A 548      -0.179  17.852 141.028  1.00111.42           C  
ANISOU 4576  CB  THR A 548    14506  14367  13463   -817   3167  -3544       C  
ATOM   4577  OG1 THR A 548       0.281  18.233 142.331  1.00125.36           O  
ANISOU 4577  OG1 THR A 548    16364  15802  15464   -506   3309  -3393       O  
ATOM   4578  CG2 THR A 548      -0.610  19.094 140.264  1.00 84.65           C  
ANISOU 4578  CG2 THR A 548    11151  10874  10140   -989   3081  -3587       C  
ATOM   4579  N   GLU A 549      -3.714  17.277 141.393  1.00150.06           N  
ANISOU 4579  N   GLU A 549    19238  19570  18207   -428   3226  -3302       N  
ATOM   4580  CA  GLU A 549      -5.030  17.718 141.792  1.00155.59           C  
ANISOU 4580  CA  GLU A 549    19876  20377  18864   -295   3356  -3311       C  
ATOM   4581  C   GLU A 549      -5.660  16.427 142.393  1.00140.20           C  
ANISOU 4581  C   GLU A 549    17763  18836  16670   -350   3220  -3197       C  
ATOM   4582  O   GLU A 549      -6.859  16.378 142.665  1.00155.21           O  
ANISOU 4582  O   GLU A 549    19579  20845  18548   -210   3307  -3143       O  
ATOM   4583  CB  GLU A 549      -5.833  18.202 140.589  1.00167.98           C  
ANISOU 4583  CB  GLU A 549    21485  21661  20680     57   3487  -3166       C  
ATOM   4584  CG  GLU A 549      -5.291  19.470 139.950  1.00167.57           C  
ANISOU 4584  CG  GLU A 549    21429  21500  20742    224   3353  -2918       C  
ATOM   4585  CD  GLU A 549      -6.070  19.881 138.716  1.00168.79           C  
ANISOU 4585  CD  GLU A 549    21740  21321  21070    197   3344  -2919       C  
ATOM   4586  OE1 GLU A 549      -6.908  19.082 138.248  1.00170.48           O  
ANISOU 4586  OE1 GLU A 549    22050  21224  21501    432   3445  -2825       O  
ATOM   4587  OE2 GLU A 549      -5.844  21.002 138.214  1.00170.81           O1-
ANISOU 4587  OE2 GLU A 549    22015  21643  21240    -60   3232  -3004       O1-
ATOM   4588  N   ILE A 550      -4.805  15.425 142.593  1.00101.39           N  
ANISOU 4588  N   ILE A 550    12798  14158  11568   -558   3009  -3155       N  
ATOM   4589  CA  ILE A 550      -5.196  14.139 143.156  1.00 81.53           C  
ANISOU 4589  CA  ILE A 550    10141  12038   8799   -647   2855  -3015       C  
ATOM   4590  C   ILE A 550      -4.023  13.893 144.110  1.00 91.54           C  
ANISOU 4590  C   ILE A 550    11395  13574   9813   -941   2690  -3108       C  
ATOM   4591  O   ILE A 550      -4.209  13.833 145.326  1.00106.71           O  
ANISOU 4591  O   ILE A 550    13242  15816  11485  -1071   2645  -3122       O  
ATOM   4592  CB  ILE A 550      -5.620  13.147 142.057  1.00 73.63           C  
ANISOU 4592  CB  ILE A 550     9071  11054   7852   -516   2725  -2750       C  
ATOM   4593  CG1 ILE A 550      -6.830  13.685 141.290  1.00 76.67           C  
ANISOU 4593  CG1 ILE A 550     9407  11281   8442   -219   2860  -2637       C  
ATOM   4594  CG2 ILE A 550      -5.927  11.784 142.658  1.00 58.75           C  
ANISOU 4594  CG2 ILE A 550     7061   9577   5683   -678   2524  -2589       C  
ATOM   4595  CD1 ILE A 550      -6.495  14.211 139.912  1.00 85.26           C  
ANISOU 4595  CD1 ILE A 550    10615  11958   9823     -2   2942  -2617       C  
ATOM   4596  N   TYR A 551      -2.859  13.641 143.513  1.00 94.16           N  
ANISOU 4596  N   TYR A 551    11790  13783  10203  -1038   2599  -3161       N  
ATOM   4597  CA  TYR A 551      -1.636  13.266 144.224  1.00100.27           C  
ANISOU 4597  CA  TYR A 551    12520  14834  10743  -1289   2406  -3216       C  
ATOM   4598  C   TYR A 551      -0.861  14.357 144.940  1.00108.60           C  
ANISOU 4598  C   TYR A 551    13607  15886  11769  -1477   2490  -3513       C  
ATOM   4599  O   TYR A 551       0.340  14.217 145.168  1.00106.22           O  
ANISOU 4599  O   TYR A 551    13248  15822  11288  -1682   2332  -3580       O  
ATOM   4600  CB  TYR A 551      -0.694  12.514 143.277  1.00 91.84           C  
ANISOU 4600  CB  TYR A 551    11469  13684   9741  -1301   2242  -3104       C  
ATOM   4601  CG  TYR A 551      -1.292  11.257 142.687  1.00 78.67           C  
ANISOU 4601  CG  TYR A 551     9740  12140   8011  -1196   2099  -2806       C  
ATOM   4602  CD1 TYR A 551      -1.303  10.068 143.404  1.00 66.40           C  
ANISOU 4602  CD1 TYR A 551     8088  10976   6164  -1304   1901  -2637       C  
ATOM   4603  CD2 TYR A 551      -1.845  11.259 141.414  1.00 83.66           C  
ANISOU 4603  CD2 TYR A 551    10411  12487   8890   -981   2145  -2660       C  
ATOM   4604  CE1 TYR A 551      -1.848   8.916 142.869  1.00 68.19           C  
ANISOU 4604  CE1 TYR A 551     8262  11231   6416  -1202   1720  -2281       C  
ATOM   4605  CE2 TYR A 551      -2.393  10.112 140.871  1.00 78.64           C  
ANISOU 4605  CE2 TYR A 551     9707  11891   8282   -877   1927  -2298       C  
ATOM   4606  CZ  TYR A 551      -2.392   8.944 141.602  1.00 70.30           C  
ANISOU 4606  CZ  TYR A 551     8559  11170   6981   -996   1725  -2119       C  
ATOM   4607  OH  TYR A 551      -2.936   7.800 141.066  1.00 51.46           O  
ANISOU 4607  OH  TYR A 551     6117   8788   4646   -907   1537  -1778       O  
ATOM   4608  N   LYS A 552      -1.534  15.436 145.305  1.00115.28           N  
ANISOU 4608  N   LYS A 552    14530  16489  12784  -1410   2731  -3686       N  
ATOM   4609  CA  LYS A 552      -0.843  16.506 146.024  1.00118.88           C  
ANISOU 4609  CA  LYS A 552    15022  16892  13254  -1600   2839  -3984       C  
ATOM   4610  C   LYS A 552      -0.282  16.017 147.356  1.00106.52           C  
ANISOU 4610  C   LYS A 552    13345  15773  11355  -1852   2693  -4089       C  
ATOM   4611  O   LYS A 552       0.867  16.318 147.704  1.00118.67           O  
ANISOU 4611  O   LYS A 552    14851  17389  12847  -2059   2633  -4261       O  
ATOM   4612  CB  LYS A 552      -1.788  17.695 146.231  1.00125.25           C  
ANISOU 4612  CB  LYS A 552    15913  17454  14225  -1484   3120  -4123       C  
ATOM   4613  CG  LYS A 552      -1.160  18.857 146.997  1.00129.46           C  
ANISOU 4613  CG  LYS A 552    16537  17714  14937  -1606   3292  -4385       C  
ATOM   4614  CD  LYS A 552       0.037  19.455 146.261  1.00128.82           C  
ANISOU 4614  CD  LYS A 552    16552  17363  15032  -1458   3578  -4490       C  
ATOM   4615  CE  LYS A 552       0.554  20.719 146.942  1.00121.76           C  
ANISOU 4615  CE  LYS A 552    15794  15989  14482  -1248   3722  -4403       C  
ATOM   4616  NZ  LYS A 552       1.845  21.182 146.355  1.00115.61           N  
ANISOU 4616  NZ  LYS A 552    15109  14946  13869  -1112   4003  -4512       N  
ATOM   4617  N   GLY A 553      -1.057  15.216 148.085  1.00 85.81           N  
ANISOU 4617  N   GLY A 553    10648  13461   8494  -1831   2628  -3966       N  
ATOM   4618  CA  GLY A 553      -0.558  14.561 149.278  1.00 90.36           C  
ANISOU 4618  CA  GLY A 553    11119  14484   8728  -2030   2458  -3986       C  
ATOM   4619  C   GLY A 553       0.726  13.780 149.063  1.00 79.43           C  
ANISOU 4619  C   GLY A 553     9664  13283   7232  -2141   2197  -3888       C  
ATOM   4620  O   GLY A 553       1.729  14.046 149.731  1.00 77.33           O  
ANISOU 4620  O   GLY A 553     9336  13198   6848  -2336   2127  -4064       O  
ATOM   4621  N   LEU A 554       0.713  12.826 148.127  1.00 84.06           N  
ANISOU 4621  N   LEU A 554    10248  13832   7859  -2015   2056  -3613       N  
ATOM   4622  CA  LEU A 554       1.877  11.969 147.902  1.00 88.53           C  
ANISOU 4622  CA  LEU A 554    10745  14581   8313  -2092   1799  -3482       C  
ATOM   4623  C   LEU A 554       3.069  12.770 147.391  1.00 91.89           C  
ANISOU 4623  C   LEU A 554    11185  14802   8925  -2192   1819  -3689       C  
ATOM   4624  O   LEU A 554       4.208  12.582 147.847  1.00 89.25           O  
ANISOU 4624  O   LEU A 554    10753  14704   8454  -2347   1663  -3752       O  
ATOM   4625  CB  LEU A 554       1.511  10.863 146.912  1.00 72.44           C  
ANISOU 4625  CB  LEU A 554     8718  12495   6311  -1928   1680  -3153       C  
ATOM   4626  CG  LEU A 554       2.393   9.618 146.926  1.00 68.33           C  
ANISOU 4626  CG  LEU A 554     8117  12250   5596  -1974   1390  -2917       C  
ATOM   4627  CD1 LEU A 554       2.801   9.300 148.355  1.00 62.66           C  
ANISOU 4627  CD1 LEU A 554     7301  11942   4567  -2114   1269  -2933       C  
ATOM   4628  CD2 LEU A 554       1.678   8.440 146.279  1.00 58.46           C  
ANISOU 4628  CD2 LEU A 554     6875  11012   4327  -1827   1303  -2568       C  
ATOM   4629  N   ILE A 555       2.820  13.640 146.412  1.00 86.13           N  
ANISOU 4629  N   ILE A 555    10573  13636   8518  -2089   2012  -3772       N  
ATOM   4630  CA  ILE A 555       3.808  14.552 145.855  1.00 84.65           C  
ANISOU 4630  CA  ILE A 555    10425  13178   8560  -2175   2092  -3963       C  
ATOM   4631  C   ILE A 555       4.542  15.218 147.010  1.00104.49           C  
ANISOU 4631  C   ILE A 555    12852  15903  10945  -2421   2118  -4246       C  
ATOM   4632  O   ILE A 555       5.746  14.998 147.210  1.00100.95           O  
ANISOU 4632  O   ILE A 555    12295  15656  10407  -2576   1968  -4305       O  
ATOM   4633  CB  ILE A 555       3.132  15.582 144.927  1.00 83.15           C  
ANISOU 4633  CB  ILE A 555    10393  12486   8715  -2008   2353  -4003       C  
ATOM   4634  CG1 ILE A 555       2.553  14.872 143.697  1.00 86.14           C  
ANISOU 4634  CG1 ILE A 555    10834  12646   9249  -1792   2296  -3740       C  
ATOM   4635  CG2 ILE A 555       4.100  16.697 144.526  1.00 91.78           C  
ANISOU 4635  CG2 ILE A 555    11535  13314  10021  -2144   2518  -4258       C  
ATOM   4636  CD1 ILE A 555       1.642  15.744 142.852  1.00 82.09           C  
ANISOU 4636  CD1 ILE A 555    10471  11645   9075  -1592   2525  -3727       C  
ATOM   4637  N   ASP A 556       3.796  15.974 147.821  1.00121.90           N  
ANISOU 4637  N   ASP A 556    15091  18102  13123  -2452   2303  -4418       N  
ATOM   4638  CA  ASP A 556       4.415  16.751 148.885  1.00122.36           C  
ANISOU 4638  CA  ASP A 556    15079  18329  13083  -2692   2370  -4722       C  
ATOM   4639  C   ASP A 556       5.057  15.864 149.945  1.00113.40           C  
ANISOU 4639  C   ASP A 556    13773  17735  11581  -2836   2122  -4692       C  
ATOM   4640  O   ASP A 556       6.079  16.247 150.523  1.00120.96           O  
ANISOU 4640  O   ASP A 556    14621  18878  12459  -3042   2089  -4901       O  
ATOM   4641  CB  ASP A 556       3.377  17.691 149.495  1.00121.60           C  
ANISOU 4641  CB  ASP A 556    15068  18102  13034  -2673   2627  -4896       C  
ATOM   4642  CG  ASP A 556       2.942  18.782 148.526  1.00120.00           C  
ANISOU 4642  CG  ASP A 556    15028  17359  13208  -2539   2889  -4948       C  
ATOM   4643  OD1 ASP A 556       2.431  18.455 147.433  1.00118.11           O  
ANISOU 4643  OD1 ASP A 556    14871  16870  13137  -2307   2886  -4716       O  
ATOM   4644  OD2 ASP A 556       3.125  19.973 148.852  1.00127.34           O1-
ANISOU 4644  OD2 ASP A 556    16003  18117  14263  -2661   3102  -5214       O1-
ATOM   4645  N   ARG A 557       4.507  14.671 150.191  1.00101.24           N  
ANISOU 4645  N   ARG A 557    12198  16452   9815  -2725   1949  -4417       N  
ATOM   4646  CA  ARG A 557       5.126  13.758 151.148  1.00 97.95           C  
ANISOU 4646  CA  ARG A 557    11633  16534   9051  -2821   1704  -4322       C  
ATOM   4647  C   ARG A 557       6.537  13.394 150.717  1.00103.63           C  
ANISOU 4647  C   ARG A 557    12245  17349   9779  -2888   1510  -4287       C  
ATOM   4648  O   ARG A 557       7.485  13.456 151.519  1.00108.64           O  
ANISOU 4648  O   ARG A 557    12739  18301  10238  -3047   1411  -4418       O  
ATOM   4649  CB  ARG A 557       4.291  12.487 151.295  1.00 95.67           C  
ANISOU 4649  CB  ARG A 557    11348  16436   8566  -2667   1566  -3974       C  
ATOM   4650  CG  ARG A 557       4.883  11.487 152.293  1.00101.19           C  
ANISOU 4650  CG  ARG A 557    11913  17627   8908  -2728   1318  -3816       C  
ATOM   4651  CD  ARG A 557       4.118  10.178 152.303  1.00108.09           C  
ANISOU 4651  CD  ARG A 557    12807  18632   9629  -2572   1193  -3429       C  
ATOM   4652  NE  ARG A 557       3.969   9.648 153.655  1.00108.13           N  
ANISOU 4652  NE  ARG A 557    12748  19044   9293  -2621   1111  -3349       N  
ATOM   4653  CZ  ARG A 557       2.917   9.887 154.431  1.00102.89           C  
ANISOU 4653  CZ  ARG A 557    12129  18441   8522  -2630   1264  -3410       C  
ATOM   4654  NH1 ARG A 557       1.926  10.645 153.984  1.00 93.26           N  
ANISOU 4654  NH1 ARG A 557    11009  16906   7521  -2579   1502  -3546       N  
ATOM   4655  NH2 ARG A 557       2.850   9.372 155.650  1.00109.63           N  
ANISOU 4655  NH2 ARG A 557    12931  19669   9055  -2674   1187  -3327       N  
ATOM   4656  N   ILE A 558       6.692  12.992 149.451  1.00 99.08           N  
ANISOU 4656  N   ILE A 558    11727  16516   9403  -2759   1455  -4108       N  
ATOM   4657  CA  ILE A 558       8.004  12.546 148.987  1.00 95.41           C  
ANISOU 4657  CA  ILE A 558    11160  16141   8951  -2801   1265  -4048       C  
ATOM   4658  C   ILE A 558       8.975  13.726 148.898  1.00 93.96           C  
ANISOU 4658  C   ILE A 558    10934  15818   8947  -2981   1402  -4382       C  
ATOM   4659  O   ILE A 558      10.155  13.602 149.256  1.00 84.95           O  
ANISOU 4659  O   ILE A 558     9636  14940   7701  -3103   1269  -4454       O  
ATOM   4660  CB  ILE A 558       7.884  11.809 147.643  1.00 90.94           C  
ANISOU 4660  CB  ILE A 558    10676  15330   8549  -2621   1181  -3777       C  
ATOM   4661  CG1 ILE A 558       6.646  10.904 147.636  1.00 86.95           C  
ANISOU 4661  CG1 ILE A 558    10240  14870   7929  -2452   1139  -3490       C  
ATOM   4662  CG2 ILE A 558       9.121  10.979 147.338  1.00 85.38           C  
ANISOU 4662  CG2 ILE A 558     9850  14809   7781  -2627    928  -3628       C  
ATOM   4663  CD1 ILE A 558       6.508  10.106 146.365  1.00 60.64           C  
ANISOU 4663  CD1 ILE A 558     6974  11338   4727  -2288   1049  -3223       C  
ATOM   4664  N   LYS A 559       8.495  14.900 148.450  1.00100.79           N  
ANISOU 4664  N   LYS A 559    11933  16273  10089  -2995   1682  -4581       N  
ATOM   4665  CA  LYS A 559       9.388  16.064 148.434  1.00110.40           C  
ANISOU 4665  CA  LYS A 559    13115  17351  11482  -3186   1843  -4894       C  
ATOM   4666  C   LYS A 559       9.800  16.482 149.841  1.00130.62           C  
ANISOU 4666  C   LYS A 559    15531  20291  13805  -3404   1850  -5151       C  
ATOM   4667  O   LYS A 559      10.906  16.995 150.030  1.00139.36           O  
ANISOU 4667  O   LYS A 559    16517  21495  14937  -3590   1869  -5368       O  
ATOM   4668  CB  LYS A 559       8.751  17.243 147.702  1.00114.79           C  
ANISOU 4668  CB  LYS A 559    13861  17370  12384  -3136   2154  -5014       C  
ATOM   4669  CG  LYS A 559       7.887  16.880 146.509  1.00118.27           C  
ANISOU 4669  CG  LYS A 559    14468  17454  13015  -2874   2181  -4750       C  
ATOM   4670  CD  LYS A 559       7.724  18.032 145.532  1.00118.66           C  
ANISOU 4670  CD  LYS A 559    14684  16958  13442  -2814   2454  -4827       C  
ATOM   4671  CE  LYS A 559       7.399  19.339 146.242  1.00128.60           C  
ANISOU 4671  CE  LYS A 559    15993  18092  14778  -2935   2722  -5109       C  
ATOM   4672  NZ  LYS A 559       6.087  19.339 146.948  1.00127.62           N  
ANISOU 4672  NZ  LYS A 559    15923  18037  14529  -2832   2791  -5094       N  
ATOM   4673  N   SER A 560       8.951  16.238 150.844  1.00136.11           N  
ANISOU 4673  N   SER A 560    16228  21227  14259  -3388   1835  -5131       N  
ATOM   4674  CA  SER A 560       9.280  16.660 152.200  1.00140.88           C  
ANISOU 4674  CA  SER A 560    16707  22195  14627  -3593   1852  -5384       C  
ATOM   4675  C   SER A 560      10.216  15.678 152.891  1.00127.42           C  
ANISOU 4675  C   SER A 560    14799  21019  12596  -3637   1555  -5270       C  
ATOM   4676  O   SER A 560      11.152  16.089 153.587  1.00133.97           O  
ANISOU 4676  O   SER A 560    15473  22120  13311  -3830   1538  -5504       O  
ATOM   4677  CB  SER A 560       8.000  16.824 153.015  1.00154.89           C  
ANISOU 4677  CB  SER A 560    18570  24012  16270  -3554   1970  -5411       C  
ATOM   4678  OG  SER A 560       7.762  15.672 153.806  1.00160.91           O  
ANISOU 4678  OG  SER A 560    19254  25205  16681  -3488   1743  -5182       O  
ATOM   4679  N   ARG A 561       9.982  14.381 152.719  1.00111.72           N  
ANISOU 4679  N   ARG A 561    12807  19185  10457  -3453   1325  -4904       N  
ATOM   4680  CA  ARG A 561      10.675  13.379 153.514  1.00112.36           C  
ANISOU 4680  CA  ARG A 561    12719  19770  10202  -3449   1049  -4738       C  
ATOM   4681  C   ARG A 561      11.667  12.548 152.718  1.00113.16           C  
ANISOU 4681  C   ARG A 561    12739  19904  10353  -3354    830  -4514       C  
ATOM   4682  O   ARG A 561      12.185  11.562 153.246  1.00109.47           O  
ANISOU 4682  O   ARG A 561    12152  19813   9630  -3290    587  -4299       O  
ATOM   4683  CB  ARG A 561       9.665  12.458 154.195  1.00113.40           C  
ANISOU 4683  CB  ARG A 561    12901  20113  10072  -3316    954  -4467       C  
ATOM   4684  CG  ARG A 561       8.849  13.126 155.282  1.00113.43           C  
ANISOU 4684  CG  ARG A 561    12943  20222   9934  -3420   1126  -4682       C  
ATOM   4685  CD  ARG A 561       8.386  12.115 156.308  1.00107.20           C  
ANISOU 4685  CD  ARG A 561    12123  19826   8781  -3341    971  -4434       C  
ATOM   4686  NE  ARG A 561       6.980  12.290 156.646  1.00111.05           N  
ANISOU 4686  NE  ARG A 561    12747  20198   9248  -3293   1145  -4430       N  
ATOM   4687  CZ  ARG A 561       6.010  11.506 156.186  1.00120.43           C  
ANISOU 4687  CZ  ARG A 561    14044  21248  10468  -3109   1130  -4121       C  
ATOM   4688  NH1 ARG A 561       6.302  10.499 155.372  1.00122.14           N  
ANISOU 4688  NH1 ARG A 561    14258  21415  10737  -2964    949  -3796       N  
ATOM   4689  NH2 ARG A 561       4.751  11.725 156.537  1.00125.90           N  
ANISOU 4689  NH2 ARG A 561    14841  21852  11142  -3071   1305  -4142       N  
ATOM   4690  N   GLU A 562      11.955  12.908 151.474  1.00119.32           N  
ANISOU 4690  N   GLU A 562    13586  20294  11456  -3331    914  -4547       N  
ATOM   4691  CA  GLU A 562      12.906  12.127 150.702  1.00108.26           C  
ANISOU 4691  CA  GLU A 562    12110  18917  10108  -3241    714  -4344       C  
ATOM   4692  C   GLU A 562      14.029  12.995 150.144  1.00 97.83           C  
ANISOU 4692  C   GLU A 562    10714  17442   9015  -3388    815  -4614       C  
ATOM   4693  O   GLU A 562      13.916  14.216 150.015  1.00109.92           O  
ANISOU 4693  O   GLU A 562    12306  18710  10748  -3530   1076  -4916       O  
ATOM   4694  CB  GLU A 562      12.214  11.365 149.565  1.00107.55           C  
ANISOU 4694  CB  GLU A 562    12172  18522  10169  -3029    665  -4028       C  
ATOM   4695  CG  GLU A 562      11.209  10.296 150.032  1.00107.19           C  
ANISOU 4695  CG  GLU A 562    12182  18648   9896  -2874    543  -3704       C  
ATOM   4696  CD  GLU A 562      11.783   9.296 151.023  1.00104.11           C  
ANISOU 4696  CD  GLU A 562    11642  18740   9174  -2840    292  -3500       C  
ATOM   4697  OE1 GLU A 562      12.828   8.688 150.720  1.00 97.53           O  
ANISOU 4697  OE1 GLU A 562    10702  18024   8333  -2788    105  -3364       O  
ATOM   4698  OE2 GLU A 562      11.164   9.088 152.092  1.00110.78           O1-
ANISOU 4698  OE2 GLU A 562    12484  19836   9772  -2846    287  -3457       O1-
ATOM   4699  N   LYS A 563      15.122  12.319 149.821  1.00 83.77           N  
ANISOU 4699  N   LYS A 563     8802  15824   7204  -3343    613  -4483       N  
ATOM   4700  CA  LYS A 563      16.324  12.906 149.237  1.00 91.47           C  
ANISOU 4700  CA  LYS A 563     9680  16698   8375  -3459    671  -4685       C  
ATOM   4701  C   LYS A 563      16.207  12.799 147.718  1.00100.79           C  
ANISOU 4701  C   LYS A 563    11009  17410   9876  -3337    724  -4545       C  
ATOM   4702  O   LYS A 563      16.163  11.694 147.159  1.00 73.15           O  
ANISOU 4702  O   LYS A 563     7533  13910   6352  -3152    525  -4219       O  
ATOM   4703  CB  LYS A 563      17.591  12.196 149.740  1.00 89.65           C  
ANISOU 4703  CB  LYS A 563     9216  16920   7927  -3456    417  -4616       C  
ATOM   4704  CG  LYS A 563      17.678  10.623 149.543  1.00101.36           C  
ANISOU 4704  CG  LYS A 563    10677  18571   9263  -3207    107  -4163       C  
ATOM   4705  CD  LYS A 563      16.668   9.940 150.447  1.00106.17           C  
ANISOU 4705  CD  LYS A 563    11342  19398   9598  -3107     17  -3945       C  
ATOM   4706  CE  LYS A 563      16.641   8.450 150.462  1.00107.01           C  
ANISOU 4706  CE  LYS A 563    11440  19673   9544  -2876   -248  -3499       C  
ATOM   4707  NZ  LYS A 563      15.270   8.116 151.010  1.00108.20           N  
ANISOU 4707  NZ  LYS A 563    11730  19835   9548  -2807   -210  -3340       N  
ATOM   4708  N   LEU A 564      16.138  13.947 147.049  1.00104.76           N  
ANISOU 4708  N   LEU A 564    11619  17503  10683  -3438   1001  -4778       N  
ATOM   4709  CA  LEU A 564      16.098  13.997 145.600  1.00 90.72           C  
ANISOU 4709  CA  LEU A 564     9985  15263   9221  -3336   1084  -4672       C  
ATOM   4710  C   LEU A 564      17.294  14.721 145.004  1.00 95.39           C  
ANISOU 4710  C   LEU A 564    10503  15704  10037  -3470   1208  -4878       C  
ATOM   4711  O   LEU A 564      17.455  14.702 143.777  1.00 76.89           O  
ANISOU 4711  O   LEU A 564     8262  13004   7949  -3386   1261  -4778       O  
ATOM   4712  CB  LEU A 564      14.814  14.683 145.129  1.00 70.94           C  
ANISOU 4712  CB  LEU A 564     7719  12317   6919  -3276   1329  -4691       C  
ATOM   4713  CG  LEU A 564      13.569  14.324 145.936  1.00 72.89           C  
ANISOU 4713  CG  LEU A 564     8028  12716   6949  -3198   1292  -4592       C  
ATOM   4714  CD1 LEU A 564      12.404  15.232 145.581  1.00 74.57           C  
ANISOU 4714  CD1 LEU A 564     8454  12501   7377  -3152   1572  -4670       C  
ATOM   4715  CD2 LEU A 564      13.238  12.876 145.687  1.00 67.78           C  
ANISOU 4715  CD2 LEU A 564     7386  12224   6143  -3000   1025  -4224       C  
ATOM   4716  N   THR A 565      18.128  15.357 145.836  1.00110.43           N  
ANISOU 4716  N   THR A 565    12234  17877  11849  -3679   1264  -5164       N  
ATOM   4717  CA  THR A 565      19.308  16.062 145.348  1.00116.41           C  
ANISOU 4717  CA  THR A 565    12900  18528  12801  -3826   1398  -5380       C  
ATOM   4718  C   THR A 565      20.090  15.179 144.388  1.00121.13           C  
ANISOU 4718  C   THR A 565    13452  19096  13476  -3691   1211  -5159       C  
ATOM   4719  O   THR A 565      20.401  14.022 144.692  1.00105.32           O  
ANISOU 4719  O   THR A 565    11330  17437  11251  -3573    909  -4943       O  
ATOM   4720  CB  THR A 565      20.200  16.485 146.511  1.00126.75           C  
ANISOU 4720  CB  THR A 565    13972  20280  13907  -4046   1387  -5675       C  
ATOM   4721  OG1 THR A 565      19.537  17.490 147.283  1.00136.66           O  
ANISOU 4721  OG1 THR A 565    15282  21494  15148  -4204   1614  -5927       O  
ATOM   4722  CG2 THR A 565      21.513  17.056 145.980  1.00125.47           C  
ANISOU 4722  CG2 THR A 565    13690  20058  13926  -4190   1500  -5882       C  
ATOM   4723  N   MET A 566      20.378  15.723 143.220  1.00140.41           N  
ANISOU 4723  N   MET A 566    15999  21111  16241  -3697   1400  -5192       N  
ATOM   4724  CA  MET A 566      20.976  14.962 142.137  1.00151.39           C  
ANISOU 4724  CA  MET A 566    17388  22380  17754  -3560   1263  -4979       C  
ATOM   4725  C   MET A 566      22.435  15.370 141.989  1.00153.88           C  
ANISOU 4725  C   MET A 566    17522  22796  18148  -3710   1315  -5188       C  
ATOM   4726  O   MET A 566      22.750  16.377 141.345  1.00154.52           O  
ANISOU 4726  O   MET A 566    17673  22542  18494  -3821   1599  -5363       O  
ATOM   4727  CB  MET A 566      20.202  15.163 140.848  1.00156.95           C  
ANISOU 4727  CB  MET A 566    18353  22528  18752  -3427   1425  -4823       C  
ATOM   4728  CG  MET A 566      20.063  13.869 140.141  1.00153.58           C  
ANISOU 4728  CG  MET A 566    17962  22091  18302  -3213   1170  -4488       C  
ATOM   4729  SD  MET A 566      18.734  13.800 138.966  1.00152.77           S  
ANISOU 4729  SD  MET A 566    18165  21462  18417  -3014   1283  -4257       S  
ATOM   4730  CE  MET A 566      19.235  12.258 138.244  1.00157.61           C  
ANISOU 4730  CE  MET A 566    18708  22188  18988  -2848    955  -3946       C  
ATOM   4731  N   LYS A 567      23.318  14.577 142.590  1.00152.72           N  
ANISOU 4731  N   LYS A 567    17143  23117  17768  -3703   1044  -5154       N  
ATOM   4732  CA  LYS A 567      24.757  14.761 142.475  1.00154.94           C  
ANISOU 4732  CA  LYS A 567    17221  23560  18090  -3818   1039  -5328       C  
ATOM   4733  C   LYS A 567      25.342  13.524 141.817  1.00149.34           C  
ANISOU 4733  C   LYS A 567    16441  22923  17376  -3624    760  -5034       C  
ATOM   4734  O   LYS A 567      25.131  12.404 142.294  1.00145.03           O  
ANISOU 4734  O   LYS A 567    15834  22669  16601  -3465    466  -4776       O  
ATOM   4735  CB  LYS A 567      25.399  15.000 143.841  1.00154.89           C  
ANISOU 4735  CB  LYS A 567    16968  24076  17807  -3987    972  -5576       C  
ATOM   4736  CG  LYS A 567      24.822  14.154 144.955  1.00145.42           C  
ANISOU 4736  CG  LYS A 567    15709  23285  16257  -3883    710  -5401       C  
ATOM   4737  CD  LYS A 567      25.343  14.603 146.303  1.00141.44           C  
ANISOU 4737  CD  LYS A 567    14989  23258  15495  -4073    700  -5685       C  
ATOM   4738  CE  LYS A 567      24.468  14.056 147.414  1.00141.84           C  
ANISOU 4738  CE  LYS A 567    15048  23615  15229  -3994    538  -5541       C  
ATOM   4739  NZ  LYS A 567      23.022  14.278 147.119  1.00136.54           N  
ANISOU 4739  NZ  LYS A 567    14646  22561  14672  -3931    686  -5439       N  
ATOM   4740  N   PHE A 568      26.045  13.725 140.712  1.00144.66           N  
ANISOU 4740  N   PHE A 568    15868  22049  17047  -3632    867  -5057       N  
ATOM   4741  CA  PHE A 568      26.829  12.678 140.084  1.00152.89           C  
ANISOU 4741  CA  PHE A 568    16805  23169  18115  -3485    630  -4835       C  
ATOM   4742  C   PHE A 568      28.305  12.948 140.330  1.00169.06           C  
ANISOU 4742  C   PHE A 568    18595  25498  20143  -3626    620  -5070       C  
ATOM   4743  O   PHE A 568      28.715  14.080 140.600  1.00178.83           O  
ANISOU 4743  O   PHE A 568    19783  26726  21438  -3850    867  -5414       O  
ATOM   4744  CB  PHE A 568      26.564  12.608 138.578  1.00142.67           C  
ANISOU 4744  CB  PHE A 568    15716  21354  17136  -3376    746  -4670       C  
ATOM   4745  CG  PHE A 568      25.115  12.709 138.211  1.00131.24           C  
ANISOU 4745  CG  PHE A 568    14543  19556  15766  -3280    850  -4523       C  
ATOM   4746  CD1 PHE A 568      24.302  11.590 138.236  1.00124.37           C  
ANISOU 4746  CD1 PHE A 568    13737  18750  14769  -3086    608  -4207       C  
ATOM   4747  CD2 PHE A 568      24.566  13.925 137.841  1.00128.96           C  
ANISOU 4747  CD2 PHE A 568    14445  18875  15678  -3377   1196  -4688       C  
ATOM   4748  CE1 PHE A 568      22.971  11.681 137.893  1.00123.99           C  
ANISOU 4748  CE1 PHE A 568    13928  18396  14785  -3001    703  -4090       C  
ATOM   4749  CE2 PHE A 568      23.238  14.022 137.494  1.00127.37           C  
ANISOU 4749  CE2 PHE A 568    14488  18357  15550  -3268   1287  -4544       C  
ATOM   4750  CZ  PHE A 568      22.441  12.899 137.520  1.00126.78           C  
ANISOU 4750  CZ  PHE A 568    14466  18365  15339  -3086   1038  -4260       C  
ATOM   4751  N   HIS A 569      29.101  11.891 140.247  1.00169.30           N  
ANISOU 4751  N   HIS A 569    18450  25783  20093  -3494    338  -4879       N  
ATOM   4752  CA  HIS A 569      30.551  12.035 140.164  1.00167.20           C  
ANISOU 4752  CA  HIS A 569    17945  25715  19867  -3593    324  -5062       C  
ATOM   4753  C   HIS A 569      30.970  12.055 138.697  1.00153.47           C  
ANISOU 4753  C   HIS A 569    16297  23554  18461  -3552    448  -5001       C  
ATOM   4754  O   HIS A 569      31.748  11.235 138.210  1.00144.89           O  
ANISOU 4754  O   HIS A 569    15080  22550  17423  -3435    267  -4839       O  
ATOM   4755  CB  HIS A 569      31.238  10.924 140.949  1.00169.12           C  
ANISOU 4755  CB  HIS A 569    17929  26489  19838  -3463    -40  -4891       C  
ATOM   4756  CG  HIS A 569      31.043  11.040 142.428  1.00166.04           C  
ANISOU 4756  CG  HIS A 569    17422  26553  19113  -3533   -131  -5001       C  
ATOM   4757  ND1 HIS A 569      29.912  10.579 143.068  1.00162.70           N  
ANISOU 4757  ND1 HIS A 569    17122  26203  18495  -3419   -236  -4795       N  
ATOM   4758  CD2 HIS A 569      31.822  11.586 143.391  1.00169.22           C  
ANISOU 4758  CD2 HIS A 569    17595  27364  19337  -3714   -119  -5305       C  
ATOM   4759  CE1 HIS A 569      30.008  10.826 144.362  1.00164.11           C  
ANISOU 4759  CE1 HIS A 569    17157  26810  18390  -3521   -285  -4956       C  
ATOM   4760  NE2 HIS A 569      31.158  11.436 144.584  1.00169.83           N  
ANISOU 4760  NE2 HIS A 569    17662  27750  19114  -3701   -221  -5270       N  
ATOM   4761  N   ASP A 570      30.369  12.997 137.990  1.00148.58           N  
ANISOU 4761  N   ASP A 570    15911  22465  18078  -3644    780  -5123       N  
ATOM   4762  CA  ASP A 570      30.597  13.183 136.578  1.00142.33           C  
ANISOU 4762  CA  ASP A 570    15282  21194  17603  -3582    940  -5022       C  
ATOM   4763  C   ASP A 570      30.104  14.579 136.289  1.00140.09           C  
ANISOU 4763  C   ASP A 570    15237  20456  17536  -3705   1346  -5196       C  
ATOM   4764  O   ASP A 570      29.260  15.111 137.011  1.00139.98           O  
ANISOU 4764  O   ASP A 570    15421  20258  17507  -3661   1425  -5119       O  
ATOM   4765  CB  ASP A 570      29.810  12.159 135.762  1.00139.38           C  
ANISOU 4765  CB  ASP A 570    15041  20663  17253  -3328    729  -4620       C  
ATOM   4766  CG  ASP A 570      30.138  12.215 134.283  1.00134.73           C  
ANISOU 4766  CG  ASP A 570    14626  19588  16979  -3255    890  -4501       C  
ATOM   4767  OD1 ASP A 570      30.881  13.131 133.872  1.00136.18           O  
ANISOU 4767  OD1 ASP A 570    14741  19673  17329  -3357   1054  -4666       O  
ATOM   4768  OD2 ASP A 570      29.654  11.343 133.532  1.00130.04           O1-
ANISOU 4768  OD2 ASP A 570    14236  18716  16459  -3099    862  -4247       O1-
ATOM   4769  N   GLY A 571      30.633  15.177 135.238  1.00136.05           N  
ANISOU 4769  N   GLY A 571    14706  19760  17225  -3850   1614  -5414       N  
ATOM   4770  CA  GLY A 571      30.248  16.527 134.886  1.00138.38           C  
ANISOU 4770  CA  GLY A 571    15235  19594  17748  -3937   2017  -5522       C  
ATOM   4771  C   GLY A 571      29.602  16.384 133.529  1.00136.93           C  
ANISOU 4771  C   GLY A 571    15326  18903  17798  -3751   2126  -5236       C  
ATOM   4772  O   GLY A 571      29.229  17.388 132.917  1.00130.32           O  
ANISOU 4772  O   GLY A 571    14691  17665  17160  -3787   2463  -5269       O  
ATOM   4773  N   GLU A 572      29.444  15.155 133.042  1.00140.18           N  
ANISOU 4773  N   GLU A 572    15747  19328  18186  -3547   1850  -4938       N  
ATOM   4774  CA  GLU A 572      28.972  14.903 131.686  1.00142.56           C  
ANISOU 4774  CA  GLU A 572    16283  19183  18700  -3368   1931  -4666       C  
ATOM   4775  C   GLU A 572      27.459  14.785 131.584  1.00142.97           C  
ANISOU 4775  C   GLU A 572    16581  19004  18736  -3216   1924  -4443       C  
ATOM   4776  O   GLU A 572      26.896  15.048 130.515  1.00143.54           O  
ANISOU 4776  O   GLU A 572    16894  18652  18994  -3096   2099  -4265       O  
ATOM   4777  CB  GLU A 572      29.591  13.608 131.152  1.00144.78           C  
ANISOU 4777  CB  GLU A 572    16441  19584  18986  -3233   1649  -4463       C  
ATOM   4778  CG  GLU A 572      31.095  13.647 130.962  1.00151.11           C  
ANISOU 4778  CG  GLU A 572    17018  20546  19852  -3344   1664  -4635       C  
ATOM   4779  CD  GLU A 572      31.498  14.060 129.566  1.00156.62           C  
ANISOU 4779  CD  GLU A 572    17861  20823  20825  -3319   1930  -4594       C  
ATOM   4780  OE1 GLU A 572      30.608  14.415 128.770  1.00156.44           O  
ANISOU 4780  OE1 GLU A 572    18119  20389  20931  -3214   2116  -4428       O  
ATOM   4781  OE2 GLU A 572      32.704  14.000 129.254  1.00161.28           O1-
ANISOU 4781  OE2 GLU A 572    18280  21508  21490  -3392   1945  -4710       O1-
ATOM   4782  N   VAL A 573      26.790  14.388 132.659  1.00138.55           N  
ANISOU 4782  N   VAL A 573    15965  18730  17949  -3209   1725  -4437       N  
ATOM   4783  CA  VAL A 573      25.416  13.902 132.602  1.00116.21           C  
ANISOU 4783  CA  VAL A 573    13322  15765  15068  -3043   1628  -4198       C  
ATOM   4784  C   VAL A 573      24.466  15.053 132.916  1.00115.51           C  
ANISOU 4784  C   VAL A 573    13409  15462  15016  -3099   1897  -4303       C  
ATOM   4785  O   VAL A 573      24.476  15.602 134.022  1.00109.13           O  
ANISOU 4785  O   VAL A 573    12497  14896  14071  -3255   1939  -4532       O  
ATOM   4786  CB  VAL A 573      25.214  12.709 133.548  1.00108.86           C  
ANISOU 4786  CB  VAL A 573    12229  15274  13858  -2982   1252  -4090       C  
ATOM   4787  CG1 VAL A 573      25.821  13.001 134.911  1.00107.99           C  
ANISOU 4787  CG1 VAL A 573    11884  15626  13523  -3153   1185  -4344       C  
ATOM   4788  CG2 VAL A 573      23.738  12.364 133.676  1.00113.38           C  
ANISOU 4788  CG2 VAL A 573    12986  15741  14353  -2851   1189  -3904       C  
ATOM   4789  N   ASP A 574      23.646  15.419 131.931  1.00125.18           N  
ANISOU 4789  N   ASP A 574    14897  16239  16426  -2962   2078  -4120       N  
ATOM   4790  CA  ASP A 574      22.667  16.483 132.109  1.00122.73           C  
ANISOU 4790  CA  ASP A 574    14767  15689  16174  -2974   2326  -4160       C  
ATOM   4791  C   ASP A 574      21.570  16.032 133.064  1.00111.91           C  
ANISOU 4791  C   ASP A 574    13408  14514  14597  -2926   2153  -4126       C  
ATOM   4792  O   ASP A 574      20.926  15.002 132.845  1.00120.43           O  
ANISOU 4792  O   ASP A 574    14543  15616  15600  -2758   1934  -3902       O  
ATOM   4793  CB  ASP A 574      22.068  16.877 130.757  1.00126.75           C  
ANISOU 4793  CB  ASP A 574    15547  15709  16904  -2792   2518  -3910       C  
ATOM   4794  CG  ASP A 574      21.107  18.054 130.855  1.00131.01           C  
ANISOU 4794  CG  ASP A 574    16272  15982  17522  -2784   2781  -3922       C  
ATOM   4795  OD1 ASP A 574      20.969  18.637 131.950  1.00134.19           O  
ANISOU 4795  OD1 ASP A 574    16597  16549  17840  -2946   2849  -4156       O  
ATOM   4796  OD2 ASP A 574      20.489  18.404 129.827  1.00131.58           O1-
ANISOU 4796  OD2 ASP A 574    16566  15691  17736  -2607   2914  -3688       O1-
ATOM   4797  N   ALA A 575      21.350  16.813 134.123  1.00100.63           N  
ANISOU 4797  N   ALA A 575    11928  13228  13079  -3081   2266  -4356       N  
ATOM   4798  CA  ALA A 575      20.333  16.491 135.114  1.00 90.49           C  
ANISOU 4798  CA  ALA A 575    10647  12149  11585  -3053   2132  -4351       C  
ATOM   4799  C   ALA A 575      18.981  17.129 134.826  1.00 86.30           C  
ANISOU 4799  C   ALA A 575    10369  11256  11166  -2930   2319  -4243       C  
ATOM   4800  O   ALA A 575      17.979  16.700 135.410  1.00 58.71           O  
ANISOU 4800  O   ALA A 575     6914   7878   7517  -2850   2200  -4180       O  
ATOM   4801  CB  ALA A 575      20.799  16.913 136.512  1.00 85.89           C  
ANISOU 4801  CB  ALA A 575     9858  11964  10812  -3280   2128  -4656       C  
ATOM   4802  N   SER A 576      18.928  18.136 133.947  1.00 80.29           N  
ANISOU 4802  N   SER A 576     9776  10075  10656  -2901   2607  -4207       N  
ATOM   4803  CA  SER A 576      17.649  18.735 133.576  1.00 79.27           C  
ANISOU 4803  CA  SER A 576     9888   9597  10632  -2740   2768  -4060       C  
ATOM   4804  C   SER A 576      16.689  17.696 133.012  1.00 91.92           C  
ANISOU 4804  C   SER A 576    11609  11131  12185  -2476   2569  -3762       C  
ATOM   4805  O   SER A 576      15.469  17.832 133.156  1.00 88.63           O  
ANISOU 4805  O   SER A 576    11325  10605  11746  -2341   2599  -3673       O  
ATOM   4806  CB  SER A 576      17.876  19.859 132.563  1.00 83.45           C  
ANISOU 4806  CB  SER A 576    10574   9714  11420  -2720   3076  -4005       C  
ATOM   4807  OG  SER A 576      16.652  20.388 132.083  1.00 84.88           O  
ANISOU 4807  OG  SER A 576    10990   9567  11694  -2520   3206  -3814       O  
ATOM   4808  N   TYR A 577      17.222  16.646 132.385  1.00102.80           N  
ANISOU 4808  N   TYR A 577    12933  12579  13546  -2403   2369  -3617       N  
ATOM   4809  CA  TYR A 577      16.389  15.588 131.827  1.00 92.42           C  
ANISOU 4809  CA  TYR A 577    11718  11210  12186  -2175   2182  -3352       C  
ATOM   4810  C   TYR A 577      15.750  14.721 132.905  1.00 82.75           C  
ANISOU 4810  C   TYR A 577    10400  10338  10704  -2187   1958  -3392       C  
ATOM   4811  O   TYR A 577      14.719  14.092 132.646  1.00 85.11           O  
ANISOU 4811  O   TYR A 577    10807  10578  10955  -2007   1869  -3212       O  
ATOM   4812  CB  TYR A 577      17.230  14.726 130.883  1.00 91.75           C  
ANISOU 4812  CB  TYR A 577    11594  11102  12166  -2120   2044  -3206       C  
ATOM   4813  CG  TYR A 577      16.557  13.462 130.398  1.00 80.58           C  
ANISOU 4813  CG  TYR A 577    10241   9685  10689  -1930   1822  -2967       C  
ATOM   4814  CD1 TYR A 577      15.510  13.511 129.486  1.00 80.35           C  
ANISOU 4814  CD1 TYR A 577    10426   9346  10757  -1691   1894  -2727       C  
ATOM   4815  CD2 TYR A 577      16.980  12.217 130.844  1.00 68.27           C  
ANISOU 4815  CD2 TYR A 577     8515   8456   8969  -1989   1534  -2968       C  
ATOM   4816  CE1 TYR A 577      14.899  12.353 129.041  1.00 71.87           C  
ANISOU 4816  CE1 TYR A 577     9402   8272   9633  -1532   1708  -2528       C  
ATOM   4817  CE2 TYR A 577      16.376  11.056 130.408  1.00 66.39           C  
ANISOU 4817  CE2 TYR A 577     8331   8211   8684  -1845   1342  -2758       C  
ATOM   4818  CZ  TYR A 577      15.336  11.129 129.506  1.00 57.63           C  
ANISOU 4818  CZ  TYR A 577     7444   6767   7687  -1625   1445  -2558       C  
ATOM   4819  OH  TYR A 577      14.734   9.974 129.064  1.00 37.36           O  
ANISOU 4819  OH  TYR A 577     4881   4247   5065  -1413   1226  -2205       O  
ATOM   4820  N   PHE A 578      16.330  14.675 134.103  1.00 79.18           N  
ANISOU 4820  N   PHE A 578     9745  10274  10066  -2390   1866  -3614       N  
ATOM   4821  CA  PHE A 578      15.823  13.840 135.181  1.00 85.00           C  
ANISOU 4821  CA  PHE A 578    10374  11408  10512  -2406   1638  -3623       C  
ATOM   4822  C   PHE A 578      14.811  14.564 136.056  1.00 96.63           C  
ANISOU 4822  C   PHE A 578    11910  12899  11907  -2428   1779  -3739       C  
ATOM   4823  O   PHE A 578      14.637  14.200 137.225  1.00104.53           O  
ANISOU 4823  O   PHE A 578    12783  14286  12648  -2510   1643  -3822       O  
ATOM   4824  CB  PHE A 578      16.982  13.343 136.036  1.00 80.97           C  
ANISOU 4824  CB  PHE A 578     9599  11359   9805  -2576   1434  -3748       C  
ATOM   4825  CG  PHE A 578      17.963  12.481 135.295  1.00 89.53           C  
ANISOU 4825  CG  PHE A 578    10591  12484  10943  -2540   1254  -3619       C  
ATOM   4826  CD1 PHE A 578      19.052  13.045 134.648  1.00100.43           C  
ANISOU 4826  CD1 PHE A 578    11936  13699  12525  -2616   1392  -3712       C  
ATOM   4827  CD2 PHE A 578      17.811  11.104 135.265  1.00 85.94           C  
ANISOU 4827  CD2 PHE A 578    10075  12243  10336  -2434    952  -3395       C  
ATOM   4828  CE1 PHE A 578      19.962  12.252 133.972  1.00106.40           C  
ANISOU 4828  CE1 PHE A 578    12598  14492  13337  -2578   1234  -3596       C  
ATOM   4829  CE2 PHE A 578      18.720  10.306 134.591  1.00 97.38           C  
ANISOU 4829  CE2 PHE A 578    11424  13721  11854  -2397    785  -3264       C  
ATOM   4830  CZ  PHE A 578      19.795  10.883 133.943  1.00108.06           C  
ANISOU 4830  CZ  PHE A 578    12744  14899  13415  -2466    928  -3372       C  
ATOM   4831  N   CYS A 579      14.142  15.576 135.517  1.00 95.23           N  
ANISOU 4831  N   CYS A 579    11921  12319  11941  -2341   2043  -3721       N  
ATOM   4832  CA  CYS A 579      13.299  16.450 136.314  1.00 90.47           C  
ANISOU 4832  CA  CYS A 579    11374  11691  11311  -2373   2212  -3854       C  
ATOM   4833  C   CYS A 579      11.991  16.695 135.580  1.00 88.71           C  
ANISOU 4833  C   CYS A 579    11373  11114  11221  -2117   2333  -3653       C  
ATOM   4834  O   CYS A 579      10.934  16.869 136.195  1.00 95.14           O  
ANISOU 4834  O   CYS A 579    12231  11970  11948  -2053   2379  -3673       O  
ATOM   4835  CB  CYS A 579      14.035  17.759 136.562  1.00 96.55           C  
ANISOU 4835  CB  CYS A 579    12115  12352  12219  -2573   2455  -4094       C  
ATOM   4836  SG  CYS A 579      15.342  17.667 137.786  1.00113.74           S  
ANISOU 4836  SG  CYS A 579    14000  15026  14190  -2881   2343  -4392       S  
ATOM   4837  N   LYS A 580      12.069  16.729 134.256  1.00 84.95           N  
ANISOU 4837  N   LYS A 580    11025  10305  10948  -1958   2387  -3450       N  
ATOM   4838  CA  LYS A 580      10.889  16.732 133.413  1.00 83.30           C  
ANISOU 4838  CA  LYS A 580    10999   9814  10838  -1673   2442  -3206       C  
ATOM   4839  C   LYS A 580      10.479  15.298 133.104  1.00 72.70           C  
ANISOU 4839  C   LYS A 580     9635   8621   9367  -1533   2204  -3024       C  
ATOM   4840  O   LYS A 580      11.174  14.337 133.441  1.00 58.98           O  
ANISOU 4840  O   LYS A 580     7760   7171   7480  -1654   1997  -3067       O  
ATOM   4841  CB  LYS A 580      11.146  17.508 132.118  1.00 81.29           C  
ANISOU 4841  CB  LYS A 580    10892   9159  10835  -1559   2612  -3051       C  
ATOM   4842  CG  LYS A 580      12.590  17.500 131.637  1.00 74.16           C  
ANISOU 4842  CG  LYS A 580     9916   8247  10015  -1712   2607  -3095       C  
ATOM   4843  CD  LYS A 580      12.897  18.790 130.891  1.00 71.78           C  
ANISOU 4843  CD  LYS A 580     9738   7610   9926  -1707   2875  -3066       C  
ATOM   4844  CE  LYS A 580      14.286  18.804 130.269  1.00 79.30           C  
ANISOU 4844  CE  LYS A 580    10624   8537  10970  -1834   2901  -3088       C  
ATOM   4845  NZ  LYS A 580      14.481  17.774 129.221  1.00 71.10           N  
ANISOU 4845  NZ  LYS A 580     9607   7467   9939  -1674   2722  -2843       N  
ATOM   4846  N   LEU A 581       9.323  15.159 132.480  1.00 72.52           N  
ANISOU 4846  N   LEU A 581     9739   8422   9394  -1277   2233  -2819       N  
ATOM   4847  CA  LEU A 581       8.973  13.887 131.874  1.00 70.17           C  
ANISOU 4847  CA  LEU A 581     9447   8182   9033  -1129   2052  -2622       C  
ATOM   4848  C   LEU A 581       9.758  13.746 130.575  1.00 55.01           C  
ANISOU 4848  C   LEU A 581     7593   6021   7289  -1065   2029  -2459       C  
ATOM   4849  O   LEU A 581       9.855  14.714 129.814  1.00 60.80           O  
ANISOU 4849  O   LEU A 581     8435   6464   8204   -985   2189  -2377       O  
ATOM   4850  CB  LEU A 581       7.474  13.805 131.602  1.00 61.45           C  
ANISOU 4850  CB  LEU A 581     8428   6991   7928   -869   2103  -2460       C  
ATOM   4851  CG  LEU A 581       6.603  13.098 132.641  1.00 60.20           C  
ANISOU 4851  CG  LEU A 581     8154   7186   7534   -880   1989  -2468       C  
ATOM   4852  CD1 LEU A 581       5.158  13.523 132.479  1.00 64.73           C  
ANISOU 4852  CD1 LEU A 581     8803   7634   8159   -644   2135  -2384       C  
ATOM   4853  CD2 LEU A 581       6.741  11.592 132.513  1.00 59.34           C  
ANISOU 4853  CD2 LEU A 581     7913   7333   7302   -858   1644  -2178       C  
ATOM   4854  N   PRO A 582      10.375  12.598 130.312  1.00 45.22           N  
ANISOU 4854  N   PRO A 582     6285   4908   5987  -1110   1833  -2409       N  
ATOM   4855  CA  PRO A 582      11.048  12.411 129.023  1.00 47.46           C  
ANISOU 4855  CA  PRO A 582     6634   4957   6440  -1028   1812  -2230       C  
ATOM   4856  C   PRO A 582      10.087  12.613 127.861  1.00 50.86           C  
ANISOU 4856  C   PRO A 582     7228   5106   6989   -736   1881  -1956       C  
ATOM   4857  O   PRO A 582       8.881  12.392 127.978  1.00 50.76           O  
ANISOU 4857  O   PRO A 582     7254   5114   6918   -578   1879  -1881       O  
ATOM   4858  CB  PRO A 582      11.564  10.967 129.099  1.00 45.84           C  
ANISOU 4858  CB  PRO A 582     6270   5032   6114  -1062   1492  -2069       C  
ATOM   4859  CG  PRO A 582      10.905  10.371 130.321  1.00 54.68           C  
ANISOU 4859  CG  PRO A 582     7252   6525   6998  -1096   1323  -2049       C  
ATOM   4860  CD  PRO A 582      10.695  11.513 131.248  1.00 54.81           C  
ANISOU 4860  CD  PRO A 582     7292   6561   6974  -1230   1543  -2371       C  
ATOM   4861  N   GLU A 583      10.646  13.043 126.729  1.00 65.83           N  
ANISOU 4861  N   GLU A 583     9199   6783   9029   -667   1936  -1805       N  
ATOM   4862  CA  GLU A 583       9.865  13.449 125.570  1.00 68.30           C  
ANISOU 4862  CA  GLU A 583     9649   6883   9418   -408   1991  -1548       C  
ATOM   4863  C   GLU A 583       8.977  12.338 125.032  1.00 62.57           C  
ANISOU 4863  C   GLU A 583     8948   6185   8642   -206   1830  -1341       C  
ATOM   4864  O   GLU A 583       8.048  12.634 124.277  1.00 67.81           O  
ANISOU 4864  O   GLU A 583     9692   6748   9324     19   1851  -1152       O  
ATOM   4865  CB  GLU A 583      10.790  13.946 124.481  1.00 80.53           C  
ANISOU 4865  CB  GLU A 583    11249   8279  11070   -411   2053  -1442       C  
ATOM   4866  CG  GLU A 583      11.968  14.704 125.024  1.00 92.29           C  
ANISOU 4866  CG  GLU A 583    12674   9776  12614   -659   2191  -1667       C  
ATOM   4867  CD  GLU A 583      12.826  15.247 123.924  1.00 95.96           C  
ANISOU 4867  CD  GLU A 583    13193  10092  13177   -656   2292  -1568       C  
ATOM   4868  OE1 GLU A 583      13.219  14.469 123.031  1.00102.32           O  
ANISOU 4868  OE1 GLU A 583    13996  10902  13979   -582   2165  -1411       O  
ATOM   4869  OE2 GLU A 583      13.111  16.461 123.923  1.00 98.72           O1-
ANISOU 4869  OE2 GLU A 583    13590  10316  13603   -729   2512  -1648       O1-
ATOM   4870  N   LYS A 584       9.241  11.082 125.386  1.00 61.72           N  
ANISOU 4870  N   LYS A 584     8762   6225   8465   -286   1665  -1372       N  
ATOM   4871  CA  LYS A 584       8.473   9.941 124.906  1.00 63.62           C  
ANISOU 4871  CA  LYS A 584     8952   6594   8628   -124   1429  -1089       C  
ATOM   4872  C   LYS A 584       7.282   9.612 125.792  1.00 70.83           C  
ANISOU 4872  C   LYS A 584     9760   7753   9397    -82   1336  -1053       C  
ATOM   4873  O   LYS A 584       6.421   8.828 125.378  1.00 76.68           O  
ANISOU 4873  O   LYS A 584    10468   8578  10090     61   1186   -840       O  
ATOM   4874  CB  LYS A 584       9.391   8.723 124.803  1.00 49.09           C  
ANISOU 4874  CB  LYS A 584     6995   4911   6746   -232   1191   -993       C  
ATOM   4875  CG  LYS A 584      10.675   8.916 125.586  1.00 55.34           C  
ANISOU 4875  CG  LYS A 584     7690   5807   7531   -478   1208  -1217       C  
ATOM   4876  CD  LYS A 584      11.545   7.686 125.607  1.00 54.46           C  
ANISOU 4876  CD  LYS A 584     7439   5882   7371   -556    968  -1109       C  
ATOM   4877  CE  LYS A 584      12.865   8.009 126.283  1.00 63.58           C  
ANISOU 4877  CE  LYS A 584     8480   7148   8528   -784    996  -1345       C  
ATOM   4878  NZ  LYS A 584      13.451   6.828 126.966  1.00 69.49           N  
ANISOU 4878  NZ  LYS A 584     9033   8226   9146   -863    733  -1265       N  
ATOM   4879  N   PHE A 585       7.203  10.198 126.988  1.00 55.46           N  
ANISOU 4879  N   PHE A 585     7760   5929   7382   -213   1434  -1272       N  
ATOM   4880  CA  PHE A 585       6.171   9.846 127.951  1.00 58.31           C  
ANISOU 4880  CA  PHE A 585     8011   6554   7591   -204   1354  -1255       C  
ATOM   4881  C   PHE A 585       5.171  10.956 128.237  1.00 49.72           C  
ANISOU 4881  C   PHE A 585     6996   5359   6538    -91   1591  -1371       C  
ATOM   4882  O   PHE A 585       4.086  10.663 128.745  1.00 56.09           O  
ANISOU 4882  O   PHE A 585     7721   6347   7245    -20   1541  -1309       O  
ATOM   4883  CB  PHE A 585       6.815   9.416 129.278  1.00 59.51           C  
ANISOU 4883  CB  PHE A 585     8012   7023   7577   -447   1240  -1396       C  
ATOM   4884  CG  PHE A 585       7.443   8.051 129.234  1.00 48.80           C  
ANISOU 4884  CG  PHE A 585     6544   5856   6143   -510    966  -1217       C  
ATOM   4885  CD1 PHE A 585       6.654   6.913 129.159  1.00 45.46           C  
ANISOU 4885  CD1 PHE A 585     6056   5578   5639   -419    780   -971       C  
ATOM   4886  CD2 PHE A 585       8.821   7.904 129.263  1.00 48.37           C  
ANISOU 4886  CD2 PHE A 585     6443   5828   6106   -658    910  -1300       C  
ATOM   4887  CE1 PHE A 585       7.225   5.661 129.119  1.00 28.44           C  
ANISOU 4887  CE1 PHE A 585     3818   3558   3429   -466    559   -803       C  
ATOM   4888  CE2 PHE A 585       9.399   6.644 129.225  1.00 54.57           C  
ANISOU 4888  CE2 PHE A 585     7126   6776   6830   -686    671  -1122       C  
ATOM   4889  CZ  PHE A 585       8.596   5.526 129.149  1.00 33.42           C  
ANISOU 4889  CZ  PHE A 585     4410   4207   4079   -585    504   -869       C  
ATOM   4890  N   ARG A 586       5.496  12.210 127.929  1.00 49.31           N  
ANISOU 4890  N   ARG A 586     7096   5008   6631    -72   1865  -1536       N  
ATOM   4891  CA  ARG A 586       4.683  13.327 128.396  1.00 44.13           C  
ANISOU 4891  CA  ARG A 586     6507   4249   6012      9   2117  -1683       C  
ATOM   4892  C   ARG A 586       3.401  13.540 127.592  1.00 44.86           C  
ANISOU 4892  C   ARG A 586     6651   4229   6164    329   2146  -1455       C  
ATOM   4893  O   ARG A 586       2.615  14.422 127.954  1.00 83.43           O  
ANISOU 4893  O   ARG A 586    11546   9084  11069    419   2275  -1495       O  
ATOM   4894  CB  ARG A 586       5.518  14.616 128.401  1.00 56.54           C  
ANISOU 4894  CB  ARG A 586     8142   5644   7697   -117   2255  -1788       C  
ATOM   4895  CG  ARG A 586       5.912  15.115 127.023  1.00 69.46           C  
ANISOU 4895  CG  ARG A 586     9891   7022   9478      3   2280  -1583       C  
ATOM   4896  CD  ARG A 586       6.746  16.387 127.088  1.00 78.44           C  
ANISOU 4896  CD  ARG A 586    11082   8004  10717   -147   2460  -1701       C  
ATOM   4897  NE  ARG A 586       7.804  16.312 128.091  1.00 83.67           N  
ANISOU 4897  NE  ARG A 586    11643   8812  11336   -451   2461  -1964       N  
ATOM   4898  CZ  ARG A 586       9.014  16.840 127.938  1.00 81.05           C  
ANISOU 4898  CZ  ARG A 586    11305   8406  11084   -632   2540  -2054       C  
ATOM   4899  NH1 ARG A 586       9.329  17.475 126.818  1.00 72.87           N  
ANISOU 4899  NH1 ARG A 586    10374   7146  10168   -546   2639  -1896       N  
ATOM   4900  NH2 ARG A 586       9.914  16.730 128.906  1.00 84.45           N  
ANISOU 4900  NH2 ARG A 586    11609   9021  11456   -904   2523  -2306       N  
ATOM   4901  N   PHE A 587       3.143  12.764 126.532  1.00 45.49           N  
ANISOU 4901  N   PHE A 587     6741   4283   6259    498   1999  -1207       N  
ATOM   4902  CA  PHE A 587       1.881  12.888 125.803  1.00 59.90           C  
ANISOU 4902  CA  PHE A 587     8585   6062   8113    807   2011  -1011       C  
ATOM   4903  C   PHE A 587       1.069  11.595 125.752  1.00 60.20           C  
ANISOU 4903  C   PHE A 587     8446   6405   8024    853   1726   -813       C  
ATOM   4904  O   PHE A 587       0.117  11.513 124.968  1.00 72.08           O  
ANISOU 4904  O   PHE A 587     9938   7907   9543   1097   1687   -635       O  
ATOM   4905  CB  PHE A 587       2.078  13.375 124.364  1.00 62.71           C  
ANISOU 4905  CB  PHE A 587     9043   6228   8556    945   1970   -796       C  
ATOM   4906  CG  PHE A 587       3.259  14.265 124.153  1.00 65.34           C  
ANISOU 4906  CG  PHE A 587     9466   6392   8967    778   2062   -868       C  
ATOM   4907  CD1 PHE A 587       3.225  15.594 124.539  1.00 62.13           C  
ANISOU 4907  CD1 PHE A 587     9117   5867   8622    748   2256   -974       C  
ATOM   4908  CD2 PHE A 587       4.385  13.788 123.500  1.00 70.01           C  
ANISOU 4908  CD2 PHE A 587    10082   6942   9575    664   1969   -816       C  
ATOM   4909  CE1 PHE A 587       4.309  16.423 124.312  1.00 67.55           C  
ANISOU 4909  CE1 PHE A 587     9881   6401   9386    594   2369  -1033       C  
ATOM   4910  CE2 PHE A 587       5.471  14.610 123.271  1.00 64.13           C  
ANISOU 4910  CE2 PHE A 587     9397   6068   8902    518   2074   -877       C  
ATOM   4911  CZ  PHE A 587       5.433  15.929 123.677  1.00 71.18           C  
ANISOU 4911  CZ  PHE A 587    10345   6844   9856    480   2281   -985       C  
ATOM   4912  N   VAL A 588       1.405  10.583 126.540  1.00 53.62           N  
ANISOU 4912  N   VAL A 588     7471   5837   7064    629   1529   -832       N  
ATOM   4913  CA  VAL A 588       0.575   9.383 126.555  1.00 61.15           C  
ANISOU 4913  CA  VAL A 588     8267   7058   7912    655   1296   -654       C  
ATOM   4914  C   VAL A 588      -0.701   9.680 127.332  1.00 53.04           C  
ANISOU 4914  C   VAL A 588     7134   6195   6825    732   1376   -703       C  
ATOM   4915  O   VAL A 588      -0.672  10.324 128.389  1.00 40.00           O  
ANISOU 4915  O   VAL A 588     5478   4584   5136    634   1528   -901       O  
ATOM   4916  CB  VAL A 588       1.338   8.181 127.142  1.00 53.81           C  
ANISOU 4916  CB  VAL A 588     7238   6335   6872    411   1082   -629       C  
ATOM   4917  CG1 VAL A 588       2.441   7.737 126.182  1.00 53.38           C  
ANISOU 4917  CG1 VAL A 588     7265   6128   6890    380    985   -541       C  
ATOM   4918  CG2 VAL A 588       1.899   8.502 128.520  1.00 35.73           C  
ANISOU 4918  CG2 VAL A 588     4910   4176   4491    195   1152   -844       C  
ATOM   4919  N   LYS A 589      -1.832   9.230 126.794  1.00 48.23           N  
ANISOU 4919  N   LYS A 589     6429   5692   6203    907   1283   -538       N  
ATOM   4920  CA  LYS A 589      -3.133   9.580 127.347  1.00 62.82           C  
ANISOU 4920  CA  LYS A 589     8164   7686   8020   1025   1375   -571       C  
ATOM   4921  C   LYS A 589      -3.374   8.840 128.657  1.00 59.01           C  
ANISOU 4921  C   LYS A 589     7529   7503   7387    804   1299   -634       C  
ATOM   4922  O   LYS A 589      -3.216   7.618 128.731  1.00 65.88           O  
ANISOU 4922  O   LYS A 589     8316   8541   8176    662   1091   -520       O  
ATOM   4923  CB  LYS A 589      -4.234   9.255 126.340  1.00 72.95           C  
ANISOU 4923  CB  LYS A 589     9358   9033   9326   1266   1277   -381       C  
ATOM   4924  CG  LYS A 589      -5.539  10.002 126.577  1.00 83.17           C  
ANISOU 4924  CG  LYS A 589    10561  10396  10643   1487   1428   -412       C  
ATOM   4925  CD  LYS A 589      -5.323  11.507 126.661  1.00 90.44           C  
ANISOU 4925  CD  LYS A 589    11652  11035  11676   1633   1722   -545       C  
ATOM   4926  CE  LYS A 589      -6.137  12.126 127.785  1.00 89.02           C  
ANISOU 4926  CE  LYS A 589    11385  10961  11478   1655   1912   -704       C  
ATOM   4927  NZ  LYS A 589      -5.471  11.975 129.102  1.00 76.52           N  
ANISOU 4927  NZ  LYS A 589     9801   9474   9798   1337   1947   -904       N  
ATOM   4928  N   ILE A 590      -3.770   9.583 129.688  1.00 36.49           N  
ANISOU 4928  N   ILE A 590     4654   4710   4499    781   1484   -811       N  
ATOM   4929  CA  ILE A 590      -3.983   9.032 131.020  1.00 52.18           C  
ANISOU 4929  CA  ILE A 590     6519   6986   6323    575   1450   -887       C  
ATOM   4930  C   ILE A 590      -5.434   9.122 131.467  1.00 50.76           C  
ANISOU 4930  C   ILE A 590     6188   6989   6109    687   1532   -889       C  
ATOM   4931  O   ILE A 590      -5.753   8.687 132.577  1.00 46.57           O  
ANISOU 4931  O   ILE A 590     5554   6707   5434    529   1529   -944       O  
ATOM   4932  CB  ILE A 590      -3.065   9.711 132.056  1.00 56.32           C  
ANISOU 4932  CB  ILE A 590     7128   7488   6783    384   1588  -1133       C  
ATOM   4933  CG1 ILE A 590      -3.114  11.233 131.895  1.00 63.56           C  
ANISOU 4933  CG1 ILE A 590     8177   8132   7840    528   1876  -1315       C  
ATOM   4934  CG2 ILE A 590      -1.642   9.205 131.914  1.00 41.19           C  
ANISOU 4934  CG2 ILE A 590     5279   5529   4843    203   1442  -1118       C  
ATOM   4935  CD1 ILE A 590      -3.105  11.993 133.200  1.00 73.44           C  
ANISOU 4935  CD1 ILE A 590     9435   9460   9008    393   2083  -1595       C  
ATOM   4936  N   ASN A 591      -6.320   9.672 130.645  1.00 51.41           N  
ANISOU 4936  N   ASN A 591     6250   6973   6312    963   1608   -825       N  
ATOM   4937  CA  ASN A 591      -7.734   9.789 130.967  1.00 60.74           C  
ANISOU 4937  CA  ASN A 591     7260   8337   7481   1101   1687   -824       C  
ATOM   4938  C   ASN A 591      -8.526   8.775 130.150  1.00 67.22           C  
ANISOU 4938  C   ASN A 591     7918   9320   8303   1179   1476   -612       C  
ATOM   4939  O   ASN A 591      -8.297   8.615 128.947  1.00 60.77           O  
ANISOU 4939  O   ASN A 591     7155   8375   7561   1301   1360   -477       O  
ATOM   4940  CB  ASN A 591      -8.237  11.210 130.705  1.00 51.66           C  
ANISOU 4940  CB  ASN A 591     6179   6983   6467   1383   1945   -915       C  
ATOM   4941  CG  ASN A 591      -7.645  12.223 131.672  1.00 58.27           C  
ANISOU 4941  CG  ASN A 591     7155   7683   7303   1278   2195  -1172       C  
ATOM   4942  OD1 ASN A 591      -7.440  11.925 132.850  1.00 46.11           O  
ANISOU 4942  OD1 ASN A 591     5570   6329   5620   1033   2205  -1308       O  
ATOM   4943  ND2 ASN A 591      -7.362  13.423 131.178  1.00 66.74           N  
ANISOU 4943  ND2 ASN A 591     8402   8428   8527   1457   2407  -1245       N  
ATOM   4944  N   ARG A 592      -9.457   8.092 130.811  1.00 71.85           N  
ANISOU 4944  N   ARG A 592     8304  10195   8800   1095   1439   -597       N  
ATOM   4945  CA  ARG A 592     -10.134   6.912 130.275  1.00 68.64           C  
ANISOU 4945  CA  ARG A 592     7723   9983   8372   1066   1238   -432       C  
ATOM   4946  C   ARG A 592     -11.593   7.262 129.996  1.00 71.53           C  
ANISOU 4946  C   ARG A 592     7883  10501   8792   1301   1304   -420       C  
ATOM   4947  O   ARG A 592     -12.495   6.934 130.770  1.00 87.32           O  
ANISOU 4947  O   ARG A 592     9697  12749  10732   1227   1354   -460       O  
ATOM   4948  CB  ARG A 592     -10.009   5.762 131.273  1.00 61.81           C  
ANISOU 4948  CB  ARG A 592     6789   9331   7366    757   1154   -415       C  
ATOM   4949  CG  ARG A 592     -10.771   4.524 130.878  1.00 46.81           C  
ANISOU 4949  CG  ARG A 592     4707   7625   5452    685    992   -275       C  
ATOM   4950  CD  ARG A 592     -10.473   3.380 131.797  1.00 38.66           C  
ANISOU 4950  CD  ARG A 592     3659   6736   4292    387    928   -227       C  
ATOM   4951  NE  ARG A 592     -11.038   2.144 131.281  1.00 45.96           N  
ANISOU 4951  NE  ARG A 592     4449   7781   5232    294    781    -93       N  
ATOM   4952  CZ  ARG A 592     -10.812   0.953 131.814  1.00 48.89           C  
ANISOU 4952  CZ  ARG A 592     4816   8237   5521     49    712     -3       C  
ATOM   4953  NH1 ARG A 592     -10.030   0.846 132.879  1.00 37.72           N  
ANISOU 4953  NH1 ARG A 592     3516   6833   3983   -105    754    -15       N  
ATOM   4954  NH2 ARG A 592     -11.363  -0.127 131.282  1.00 37.78           N  
ANISOU 4954  NH2 ARG A 592     3294   6908   4153    -40    606     97       N  
ATOM   4955  N   LYS A 593     -11.825   7.948 128.879  1.00 58.10           N  
ANISOU 4955  N   LYS A 593     6212   8663   7200   1596   1312   -359       N  
ATOM   4956  CA  LYS A 593     -13.137   8.495 128.547  1.00 68.38           C  
ANISOU 4956  CA  LYS A 593     7325  10095   8561   1886   1388   -344       C  
ATOM   4957  C   LYS A 593     -13.656   7.826 127.278  1.00 59.82           C  
ANISOU 4957  C   LYS A 593     6103   9134   7490   2003   1166   -184       C  
ATOM   4958  O   LYS A 593     -12.932   7.741 126.281  1.00 59.94           O  
ANISOU 4958  O   LYS A 593     6269   8977   7528   2053   1049    -89       O  
ATOM   4959  CB  LYS A 593     -13.069  10.031 128.375  1.00 85.59           C  
ANISOU 4959  CB  LYS A 593     9654  12018  10850   2188   1623   -407       C  
ATOM   4960  CG  LYS A 593     -12.357  10.856 129.500  1.00 94.61           C  
ANISOU 4960  CG  LYS A 593    10981  12975  11991   2066   1866   -605       C  
ATOM   4961  CD  LYS A 593     -12.324  10.129 130.854  1.00 97.39           C  
ANISOU 4961  CD  LYS A 593    11248  13552  12205   1728   1862   -716       C  
ATOM   4962  CE  LYS A 593     -11.667  10.953 131.953  1.00 97.26           C  
ANISOU 4962  CE  LYS A 593    11394  13401  12158   1606   2090   -934       C  
ATOM   4963  NZ  LYS A 593     -11.988  10.364 133.290  1.00 86.73           N  
ANISOU 4963  NZ  LYS A 593     9936  12350  10668   1350   2116  -1033       N  
ATOM   4964  N   ALA A 594     -14.875   7.305 127.355  1.00 80.04           N  
ANISOU 4964  N   ALA A 594     8372  12010  10031   2030   1111   -171       N  
ATOM   4965  CA  ALA A 594     -15.498   6.581 126.253  1.00 84.02           C  
ANISOU 4965  CA  ALA A 594     8699  12702  10521   2066    884    -58       C  
ATOM   4966  C   ALA A 594     -15.448   7.301 124.915  1.00 95.36           C  
ANISOU 4966  C   ALA A 594    10194  14030  12006   2422    832     48       C  
ATOM   4967  O   ALA A 594     -16.129   8.307 124.717  1.00 95.63           O  
ANISOU 4967  O   ALA A 594    10135  14110  12089   2752    944     57       O  
ATOM   4968  CB  ALA A 594     -16.935   6.224 126.606  1.00 72.36           C  
ANISOU 4968  CB  ALA A 594     6868  11598   9026   2048    876    -97       C  
ATOM   4969  N   SER A 595     -14.647   6.778 123.990  1.00104.88           N  
ANISOU 4969  N   SER A 595    11554  15101  13193   2369    669    140       N  
ATOM   4970  CA  SER A 595     -14.548   7.385 122.682  1.00111.09           C  
ANISOU 4970  CA  SER A 595    12434  15775  13999   2694    622    257       C  
ATOM   4971  C   SER A 595     -15.696   7.085 121.687  1.00114.60           C  
ANISOU 4971  C   SER A 595    12588  16559  14396   2869    450    324       C  
ATOM   4972  O   SER A 595     -16.547   7.934 121.424  1.00112.11           O  
ANISOU 4972  O   SER A 595    12129  16365  14103   3147    521    339       O  
ATOM   4973  CB  SER A 595     -13.258   6.989 121.978  1.00112.61           C  
ANISOU 4973  CB  SER A 595    12893  15715  14179   2568    520    320       C  
ATOM   4974  OG  SER A 595     -12.152   7.158 122.847  1.00113.20           O  
ANISOU 4974  OG  SER A 595    13187  15539  14285   2353    646    239       O  
ATOM   4975  N   ILE A 596     -15.680   5.868 121.165  1.00125.75           N  
ANISOU 4975  N   ILE A 596    13927  18109  15743   2672    224    352       N  
ATOM   4976  CA  ILE A 596     -16.748   5.420 120.279  1.00130.55           C  
ANISOU 4976  CA  ILE A 596    14250  19066  16287   2794     37    388       C  
ATOM   4977  C   ILE A 596     -17.436   4.161 120.802  1.00107.30           C  
ANISOU 4977  C   ILE A 596    11041  16405  13324   2444    -45    282       C  
ATOM   4978  O   ILE A 596     -17.036   3.043 120.346  1.00 93.29           O  
ANISOU 4978  O   ILE A 596     9221  14716  11509   2183   -209    265       O  
ATOM   4979  CB  ILE A 596     -16.241   5.147 118.843  1.00144.88           C  
ANISOU 4979  CB  ILE A 596    16227  20787  18034   2847   -139    488       C  
ATOM   4980  CG1 ILE A 596     -15.686   6.431 118.223  1.00141.35           C  
ANISOU 4980  CG1 ILE A 596    16086  20013  17607   3121    -16    588       C  
ATOM   4981  CG2 ILE A 596     -17.343   4.562 117.972  1.00156.20           C  
ANISOU 4981  CG2 ILE A 596    17457  22516  19376   2849   -333    485       C  
ATOM   4982  CD1 ILE A 596     -16.734   7.493 117.977  1.00137.27           C  
ANISOU 4982  CD1 ILE A 596    15485  19587  17083   3379     39    625       C  
ATOM   4983  OXT ILE A 596     -18.352   4.307 121.671  1.00 91.19           O1-
ANISOU 4983  OXT ILE A 596     8824  14507  11318   2415     85    204       O1-
TER    4984      ILE A 596                                                      
ATOM   4985  O5' VAL E   1      -5.601 -21.797 123.975  1.00223.59           O  
ANISOU 4985  O5' VAL E   1    28391  27275  29287  -2396    539   1398       O  
ATOM   4986VAL5' VAL E   1      -6.473 -21.118 123.077  1.00228.68         VAL  
ANISOU 4986VAL5' VAL E   1    28840  28138  29909  -2532    406   1185     VAL  
ATOM   4987VAL4' VAL E   1      -5.720 -20.532 121.909  1.00232.19         VAL  
ANISOU 4987VAL4' VAL E   1    29328  28542  30352  -2407    227   1103     VAL  
ATOM   4988  O4' VAL E   1      -6.669 -19.982 120.953  1.00241.66           O  
ANISOU 4988  O4' VAL E   1    30329  29985  31506  -2464    115    838       O  
ATOM   4989VAL3' VAL E   1      -4.762 -19.402 122.269  1.00223.97         VAL  
ANISOU 4989VAL3' VAL E   1    28332  27577  29191  -2120     90   1228     VAL  
ATOM   4990  O3' VAL E   1      -3.575 -19.496 121.478  1.00204.61           O  
ANISOU 4990  O3' VAL E   1    26035  24905  26803  -1983     30   1244       O  
ATOM   4991VAL2' VAL E   1      -5.556 -18.143 121.917  1.00232.23         VAL  
ANISOU 4991VAL2' VAL E   1    29175  28953  30110  -2036    -45   1051     VAL  
ATOM   4992  O2' VAL E   1      -4.760 -17.026 121.578  1.00228.60           O  
ANISOU 4992  O2' VAL E   1    28750  28537  29569  -1781   -185   1050       O  
ATOM   4993VAL1' VAL E   1      -6.396 -18.613 120.728  1.00239.48         VAL  
ANISOU 4993VAL1' VAL E   1    29992  29905  31094  -2205    -59    813     VAL  
ATOM   4994  N1  VAL E   1      -7.690 -17.920 120.566  1.00243.51           N  
ANISOU 4994  N1  VAL E   1    30248  30761  31513  -2238   -123    640       N  
ATOM   4995VAL2  VAL E   1      -7.764 -16.536 120.341  1.00242.38         VAL  
ANISOU 4995VAL2  VAL E   1    30008  30846  31240  -1999   -269    592     VAL  
ATOM   4996  O2  VAL E   1      -6.729 -15.852 120.304  1.00240.93           O  
ANISOU 4996  O2  VAL E   1    29956  30570  31017  -1779   -337    684       O  
ATOM   4997  N3  VAL E   1      -8.979 -15.956 120.187  1.00238.85           N  
ANISOU 4997  N3  VAL E   1    29318  30716  30719  -2009   -319    446       N  
ATOM   4998VAL4  VAL E   1     -10.092 -16.690 120.229  1.00237.69         VAL  
ANISOU 4998VAL4  VAL E   1    29003  30688  30620  -2262   -242    329     VAL  
ATOM   4999  N4  VAL E   1     -11.262 -16.067 120.067  1.00234.14           N  
ANISOU 4999  N4  VAL E   1    28286  30580  30094  -2247   -303    185       N  
ATOM   5000VAL5  VAL E   1     -10.051 -18.097 120.439  1.00242.73         VAL  
ANISOU 5000VAL5  VAL E   1    29738  31094  31395  -2540    -85    354     VAL  
ATOM   5001VAL6  VAL E   1      -8.845 -18.658 120.594  1.00246.04         VAL  
ANISOU 5001VAL6  VAL E   1    30419  31176  31888  -2507    -28    517     VAL  
ATOM   5002  P   VAL E   2      -2.147 -19.568 122.217  1.00144.55           P  
ANISOU 5002  P   VAL E   2    18593  17163  19167  -1726     59   1431       P  
ATOM   5003  OP1 VAL E   2      -2.390 -20.101 123.581  1.00146.12           O  
ANISOU 5003  OP1 VAL E   2    18810  17386  19323  -1760    193   1586       O  
ATOM   5004  OP2 VAL E   2      -1.495 -18.246 122.073  1.00134.70           O1-
ANISOU 5004  OP2 VAL E   2    17319  16031  17832  -1550   -110   1453       O1-
ATOM   5005  O5' VAL E   2      -1.305 -20.664 121.415  1.00127.60           O  
ANISOU 5005  O5' VAL E   2    16611  14727  17143  -1661    164   1365       O  
ATOM   5006VAL5' VAL E   2      -1.301 -20.708 119.995  1.00112.78         VAL  
ANISOU 5006VAL5' VAL E   2    14741  12771  15341  -1703    115   1182     VAL  
ATOM   5007VAL4' VAL E   2       0.089 -20.526 119.428  1.00 94.81         VAL  
ANISOU 5007VAL4' VAL E   2    12582  10383  13059  -1468     81   1178     VAL  
ATOM   5008  O4' VAL E   2       0.108 -19.346 118.581  1.00 89.14           O  
ANISOU 5008  O4' VAL E   2    11799   9780  12290  -1416   -102   1092       O  
ATOM   5009VAL3' VAL E   2       1.205 -20.284 120.436  1.00 71.46         VAL  
ANISOU 5009VAL3' VAL E   2     9685   7449  10018  -1246     82   1342     VAL  
ATOM   5010  O3' VAL E   2       1.718 -21.480 120.995  1.00 40.11           O  
ANISOU 5010  O3' VAL E   2     5856   3313   6071  -1219    243   1429       O  
ATOM   5011VAL2' VAL E   2       2.231 -19.510 119.620  1.00 77.12         VAL  
ANISOU 5011VAL2' VAL E   2    10423   8174  10707  -1063    -18   1270     VAL  
ATOM   5012  O2' VAL E   2       2.983 -20.386 118.793  1.00 93.00           O  
ANISOU 5012  O2' VAL E   2    12562   9994  12782  -1017     89   1191       O  
ATOM   5013VAL1' VAL E   2       1.330 -18.658 118.730  1.00 83.33         VAL  
ANISOU 5013VAL1' VAL E   2    11112   9057  11492  -1171   -152   1154     VAL  
ATOM   5014  N1  VAL E   2       1.039 -17.336 119.331  1.00 93.73           N  
ANISOU 5014  N1  VAL E   2    12328  10576  12708  -1132   -288   1224       N  
ATOM   5015VAL2  VAL E   2       1.956 -16.313 119.189  1.00 99.66         VAL  
ANISOU 5015VAL2  VAL E   2    13093  11372  13400   -937   -365   1220     VAL  
ATOM   5016  O2  VAL E   2       3.012 -16.445 118.592  1.00 86.28           O  
ANISOU 5016  O2  VAL E   2    11473   9585  11724   -802   -329   1159       O  
ATOM   5017  N3  VAL E   2       1.583 -15.127 119.780  1.00110.97           N  
ANISOU 5017  N3  VAL E   2    14444  12971  14747   -921   -460   1279       N  
ATOM   5018VAL4  VAL E   2       0.423 -14.857 120.477  1.00106.95         VAL  
ANISOU 5018VAL4  VAL E   2    13810  12675  14152  -1002   -452   1260     VAL  
ATOM   5019  O4  VAL E   2       0.235 -13.734 120.949  1.00104.81           O  
ANISOU 5019  O4  VAL E   2    13463  12589  13772   -909   -494   1235       O  
ATOM   5020VAL5  VAL E   2      -0.471 -15.964 120.576  1.00 96.45         VAL  
ANISOU 5020VAL5  VAL E   2    12453  11314  12881  -1202   -372   1259     VAL  
ATOM   5021VAL6  VAL E   2      -0.136 -17.125 120.008  1.00 90.79         VAL  
ANISOU 5021VAL6  VAL E   2    11843  10356  12298  -1293   -306   1271     VAL  
ATOM   5022  P   VAL E   3       2.558 -21.439 122.366  1.00 58.78           P  
ANISOU 5022  P   VAL E   3     8263   5741   8330  -1056    235   1625       P  
ATOM   5023  OP1 VAL E   3       2.434 -22.768 123.015  1.00 49.10           O  
ANISOU 5023  OP1 VAL E   3     7182   4356   7118  -1130    395   1729       O  
ATOM   5024  OP2 VAL E   3       2.176 -20.214 123.114  1.00 73.34           O1-
ANISOU 5024  OP2 VAL E   3     9955   7832  10077  -1040    104   1689       O1-
ATOM   5025  O5' VAL E   3       4.069 -21.263 121.894  1.00 68.23           O  
ANISOU 5025  O5' VAL E   3     9528   6893   9505   -843    180   1596       O  
ATOM   5026VAL5' VAL E   3       4.646 -22.143 120.941  1.00 60.91         VAL  
ANISOU 5026VAL5' VAL E   3     8747   5764   8633   -835    256   1506     VAL  
ATOM   5027VAL4' VAL E   3       5.850 -21.518 120.284  1.00 57.98         VAL  
ANISOU 5027VAL4' VAL E   3     8369   5427   8235   -661    176   1435     VAL  
ATOM   5028  O4' VAL E   3       5.450 -20.320 119.570  1.00 58.33           O  
ANISOU 5028  O4' VAL E   3     8283   5597   8281   -667     87   1319       O  
ATOM   5029VAL3' VAL E   3       6.939 -21.037 121.228  1.00 49.30         VAL  
ANISOU 5029VAL3' VAL E   3     7224   4444   7062   -486     96   1554     VAL  
ATOM   5030  O3' VAL E   3       7.796 -22.080 121.652  1.00 53.44           O  
ANISOU 5030  O3' VAL E   3     7869   4847   7587   -415    132   1660       O  
ATOM   5031VAL2' VAL E   3       7.640 -19.960 120.411  1.00 45.90         VAL  
ANISOU 5031VAL2' VAL E   3     6724   4100   6617   -386     17   1429     VAL  
ATOM   5032  O2' VAL E   3       8.515 -20.541 119.454  1.00 60.05           O  
ANISOU 5032  O2' VAL E   3     8628   5752   8435   -334     61   1348       O  
ATOM   5033VAL1' VAL E   3       6.463 -19.340 119.662  1.00 49.85         VAL  
ANISOU 5033VAL1' VAL E   3     7155   4642   7145   -504     -4   1317     VAL  
ATOM   5034  N9  VAL E   3       5.914 -18.145 120.337  1.00 59.12           N  
ANISOU 5034  N9  VAL E   3     8193   6009   8261   -515   -119   1356       N  
ATOM   5035VAL8  VAL E   3       4.725 -18.043 121.016  1.00 53.28         VAL  
ANISOU 5035VAL8  VAL E   3     7390   5349   7506   -643   -142   1425     VAL  
ATOM   5036  N7  VAL E   3       4.490 -16.851 121.490  1.00 46.87           N  
ANISOU 5036  N7  VAL E   3     6481   4709   6620   -629   -250   1445       N  
ATOM   5037VAL5  VAL E   3       5.595 -16.112 121.103  1.00 55.45         VAL  
ANISOU 5037VAL5  VAL E   3     7566   5817   7683   -486   -293   1377     VAL  
ATOM   5038VAL6  VAL E   3       5.905 -14.751 121.338  1.00 69.16         VAL  
ANISOU 5038VAL6  VAL E   3     9236   7687   9353   -420   -382   1352     VAL  
ATOM   5039  O6  VAL E   3       5.245 -13.901 121.950  1.00 67.78           O  
ANISOU 5039  O6  VAL E   3     8997   7643   9115   -465   -448   1393       O  
ATOM   5040  N1  VAL E   3       7.128 -14.414 120.771  1.00 73.66           N  
ANISOU 5040  N1  VAL E   3     9832   8221   9936   -302   -371   1270       N  
ATOM   5041VAL2  VAL E   3       7.948 -15.264 120.070  1.00 70.58         VAL  
ANISOU 5041VAL2  VAL E   3     9517   7703   9598   -247   -293   1227     VAL  
ATOM   5042  N2  VAL E   3       9.093 -14.748 119.597  1.00 83.05           N  
ANISOU 5042  N2  VAL E   3    11102   9280  11174   -150   -287   1157       N  
ATOM   5043  N3  VAL E   3       7.666 -16.539 119.847  1.00 47.57           N  
ANISOU 5043  N3  VAL E   3     6678   4662   6734   -298   -213   1252       N  
ATOM   5044VAL4  VAL E   3       6.483 -16.893 120.389  1.00 54.97         VAL  
ANISOU 5044VAL4  VAL E   3     7594   5614   7676   -417   -214   1323     VAL  
ATOM   5045  P   VAL E   4       8.442 -22.043 123.121  1.00 59.56           P  
ANISOU 5045  P   VAL E   4     8597   5735   8297   -296     78   1862       P  
ATOM   5046  OP1 VAL E   4       9.016 -23.384 123.397  1.00 60.83           O  
ANISOU 5046  OP1 VAL E   4     8897   5722   8494   -257    127   1982       O  
ATOM   5047  OP2 VAL E   4       7.444 -21.458 124.050  1.00 73.50           O1-
ANISOU 5047  OP2 VAL E   4    10266   7659  10000   -373     61   1936       O1-
ATOM   5048  O5' VAL E   4       9.665 -21.037 122.969  1.00 51.17           O  
ANISOU 5048  O5' VAL E   4     7427   4806   7210   -143    -30   1816       O  
ATOM   5049VAL5' VAL E   4      10.725 -21.335 122.076  1.00 49.70         VAL  
ANISOU 5049VAL5' VAL E   4     7294   4514   7074    -60    -29   1738     VAL  
ATOM   5050VAL4' VAL E   4      11.555 -20.118 121.762  1.00 49.26         VAL  
ANISOU 5050VAL4' VAL E   4     7120   4596   7001     26   -110   1652     VAL  
ATOM   5051  O4' VAL E   4      10.730 -19.097 121.143  1.00 59.38           O  
ANISOU 5051  O4' VAL E   4     8346   5953   8263    -55   -121   1513       O  
ATOM   5052VAL3' VAL E   4      12.179 -19.414 122.954  1.00 52.81         VAL  
ANISOU 5052VAL3' VAL E   4     7434   5234   7396    112   -208   1777     VAL  
ATOM   5053  O3' VAL E   4      13.367 -20.043 123.399  1.00 56.10           O  
ANISOU 5053  O3' VAL E   4     7849   5629   7838    240   -231   1901       O  
ATOM   5054VAL2' VAL E   4      12.395 -18.003 122.424  1.00 55.51         VAL  
ANISOU 5054VAL2' VAL E   4     7674   5689   7726    109   -268   1639     VAL  
ATOM   5055  O2' VAL E   4      13.520 -17.968 121.556  1.00 53.76           O  
ANISOU 5055  O2' VAL E   4     7464   5401   7561    184   -258   1556       O  
ATOM   5056VAL1' VAL E   4      11.143 -17.815 121.573  1.00 47.55         VAL  
ANISOU 5056VAL1' VAL E   4     6715   4629   6722     -8   -215   1508     VAL  
ATOM   5057  N9  VAL E   4      10.023 -17.208 122.323  1.00 43.08           N  
ANISOU 5057  N9  VAL E   4     6078   4189   6102    -93   -259   1553       N  
ATOM   5058VAL8  VAL E   4       8.879 -17.877 122.672  1.00 48.44         VAL  
ANISOU 5058VAL8  VAL E   4     6796   4829   6779   -194   -210   1616     VAL  
ATOM   5059  N7  VAL E   4       8.007 -17.153 123.317  1.00 48.84           N  
ANISOU 5059  N7  VAL E   4     6766   5020   6772   -266   -265   1651       N  
ATOM   5060VAL5  VAL E   4       8.605 -15.910 123.403  1.00 47.72         VAL  
ANISOU 5060VAL5  VAL E   4     6540   5006   6587   -209   -356   1604     VAL  
ATOM   5061VAL6  VAL E   4       8.158 -14.716 123.987  1.00 47.88         VAL  
ANISOU 5061VAL6  VAL E   4     6471   5193   6528   -249   -440   1610     VAL  
ATOM   5062  N6  VAL E   4       6.979 -14.583 124.606  1.00 44.95           N  
ANISOU 5062  N6  VAL E   4     6070   4911   6096   -351   -449   1672       N  
ATOM   5063  N1  VAL E   4       8.973 -13.651 123.911  1.00 56.44           N  
ANISOU 5063  N1  VAL E   4     7506   6344   7595   -190   -502   1550       N  
ATOM   5064VAL2  VAL E   4      10.156 -13.782 123.290  1.00 54.42         VAL  
ANISOU 5064VAL2  VAL E   4     7268   6005   7402   -102   -484   1494     VAL  
ATOM   5065  N3  VAL E   4      10.686 -14.860 122.703  1.00 44.41           N  
ANISOU 5065  N3  VAL E   4     6073   4599   6201    -52   -412   1486       N  
ATOM   5066VAL4  VAL E   4       9.851 -15.915 122.792  1.00 43.02         VAL  
ANISOU 5066VAL4  VAL E   4     5964   4347   6036   -108   -350   1542     VAL  
ATOM   5067  P   VAL E   5      13.757 -20.034 124.959  1.00 66.28           P  
ANISOU 5067  P   VAL E   5     9048   7088   9048    323   -309   2117       P  
ATOM   5068  OP1 VAL E   5      15.036 -20.771 125.129  1.00 71.50           O  
ANISOU 5068  OP1 VAL E   5     9703   7704   9760    474   -326   2231       O  
ATOM   5069  OP2 VAL E   5      12.561 -20.442 125.737  1.00 60.71           O1-
ANISOU 5069  OP2 VAL E   5     8399   6393   8274    233   -267   2214       O1-
ATOM   5070  O5' VAL E   5      14.062 -18.504 125.268  1.00 47.36           O  
ANISOU 5070  O5' VAL E   5     6483   4920   6591    322   -421   2068       O  
ATOM   5071VAL5' VAL E   5      15.119 -17.835 124.598  1.00 52.20         VAL  
ANISOU 5071VAL5' VAL E   5     7019   5548   7267    379   -462   1972     VAL  
ATOM   5072VAL4' VAL E   5      15.081 -16.355 124.861  1.00 52.95         VAL  
ANISOU 5072VAL4' VAL E   5     6987   5824   7307    329   -553   1914     VAL  
ATOM   5073  O4' VAL E   5      13.834 -15.797 124.376  1.00 51.71           O  
ANISOU 5073  O4' VAL E   5     6881   5635   7132    204   -515   1788       O  
ATOM   5074VAL3' VAL E   5      15.123 -15.946 126.323  1.00 56.83         VAL  
ANISOU 5074VAL3' VAL E   5     7367   6566   7661    343   -660   2065     VAL  
ATOM   5075  O3' VAL E   5      16.434 -15.961 126.857  1.00 66.58           O  
ANISOU 5075  O3' VAL E   5     8483   7935   8882    465   -746   2166       O  
ATOM   5076VAL2' VAL E   5      14.492 -14.564 126.295  1.00 56.80         VAL  
ANISOU 5076VAL2' VAL E   5     7307   6668   7604    230   -710   1957     VAL  
ATOM   5077  O2' VAL E   5      15.421 -13.599 125.823  1.00 53.57           O  
ANISOU 5077  O2' VAL E   5     6809   6291   7256    250   -770   1873       O  
ATOM   5078VAL1' VAL E   5      13.418 -14.748 125.225  1.00 46.96         VAL  
ANISOU 5078VAL1' VAL E   5     6186   5226   6430    147   -603   1818     VAL  
ATOM   5079  N1  VAL E   5      12.092 -15.096 125.783  1.00 51.27           N  
ANISOU 5079  N1  VAL E   5     6779   5798   6901     62   -571   1874       N  
ATOM   5080VAL2  VAL E   5      11.330 -14.124 126.435  1.00 49.77         VAL  
ANISOU 5080VAL2  VAL E   5     6529   5776   6604    -22   -629   1877     VAL  
ATOM   5081  O2  VAL E   5      11.802 -12.990 126.564  1.00 64.30           O  
ANISOU 5081  O2  VAL E   5     8289   7736   8407    -25   -711   1833       O  
ATOM   5082  N3  VAL E   5      10.113 -14.460 126.921  1.00 41.45           N  
ANISOU 5082  N3  VAL E   5     5509   4752   5489   -106   -591   1933       N  
ATOM   5083VAL4  VAL E   5       9.647 -15.700 126.765  1.00 63.29         VAL  
ANISOU 5083VAL4  VAL E   5     8367   7372   8310   -116   -497   1985     VAL  
ATOM   5084  N4  VAL E   5       8.436 -15.976 127.261  1.00 58.94           N  
ANISOU 5084  N4  VAL E   5     7835   6852   7705   -217   -454   2046       N  
ATOM   5085VAL5  VAL E   5      10.402 -16.703 126.092  1.00 70.75         VAL  
ANISOU 5085VAL5  VAL E   5     9392   8130   9361    -35   -435   1977     VAL  
ATOM   5086VAL6  VAL E   5      11.603 -16.359 125.618  1.00 59.19         VAL  
ANISOU 5086VAL6  VAL E   5     7890   6654   7945     56   -476   1920     VAL  
ATOM   5087  P   VAL E   6      16.662 -16.267 128.416  1.00 78.86           P  
ANISOU 5087  P   VAL E   6     9958   9742  10262    537   -833   2364       P  
ATOM   5088  OP1 VAL E   6      18.125 -16.351 128.656  1.00 89.36           O  
ANISOU 5088  OP1 VAL E   6    11152  11197  11603    684   -919   2434       O  
ATOM   5089  OP2 VAL E   6      15.799 -17.416 128.794  1.00 75.72           O1-
ANISOU 5089  OP2 VAL E   6     9706   9227   9837    529   -741   2473       O1-
ATOM   5090  O5' VAL E   6      16.135 -14.950 129.141  1.00 68.23           O  
ANISOU 5090  O5' VAL E   6     8511   8660   8752    426   -927   2316       O  
ATOM   5091VAL5' VAL E   6      16.747 -13.695 128.878  1.00 64.85         VAL  
ANISOU 5091VAL5' VAL E   6     7949   8360   8329    393  -1020   2201     VAL  
ATOM   5092VAL4' VAL E   6      15.969 -12.553 129.480  1.00 59.47         VAL  
ANISOU 5092VAL4' VAL E   6     7221   7888   7486    261  -1080   2134     VAL  
ATOM   5093  O4' VAL E   6      14.649 -12.480 128.888  1.00 59.27           O  
ANISOU 5093  O4' VAL E   6     7336   7665   7519    156   -981   2068       O  
ATOM   5094VAL3' VAL E   6      15.702 -12.643 130.973  1.00 44.81         VAL  
ANISOU 5094VAL3' VAL E   6     5310   6336   5379    255  -1137   2233     VAL  
ATOM   5095  O3' VAL E   6      16.807 -12.207 131.738  1.00 37.31           O  
ANISOU 5095  O3' VAL E   6     4179   5705   4291    308  -1266   2223       O  
ATOM   5096VAL2' VAL E   6      14.470 -11.767 131.152  1.00 58.10         VAL  
ANISOU 5096VAL2' VAL E   6     7030   8086   6961    101  -1120   2143     VAL  
ATOM   5097  O2' VAL E   6      14.837 -10.396 131.187  1.00 63.19           O  
ANISOU 5097  O2' VAL E   6     7553   8930   7527     23  -1210   1975       O  
ATOM   5098VAL1' VAL E   6      13.719 -12.021 129.845  1.00 59.50         VAL  
ANISOU 5098VAL1' VAL E   6     7352   7899   7356     64  -1005   2086     VAL  
ATOM   5099  N1  VAL E   6      12.618 -13.007 129.953  1.00 55.24           N  
ANISOU 5099  N1  VAL E   6     6937   7223   6830     38   -896   2164       N  
ATOM   5100VAL2  VAL E   6      11.421 -12.620 130.564  1.00 51.88         VAL  
ANISOU 5100VAL2  VAL E   6     6524   6917   6269    -72   -878   2165     VAL  
ATOM   5101  O2  VAL E   6      11.334 -11.478 131.033  1.00 60.81           O  
ANISOU 5101  O2  VAL E   6     7576   8273   7255   -138   -948   2092       O  
ATOM   5102  N3  VAL E   6      10.404 -13.505 130.627  1.00 43.08           N  
ANISOU 5102  N3  VAL E   6     5504   5682   5181   -111   -778   2235       N  
ATOM   5103VAL4  VAL E   6      10.537 -14.722 130.101  1.00 47.42         VAL  
ANISOU 5103VAL4  VAL E   6     6146   5998   5874    -52   -698   2287     VAL  
ATOM   5104  N4  VAL E   6       9.510 -15.569 130.189  1.00 47.95           N  
ANISOU 5104  N4  VAL E   6     6303   5957   5961   -111   -598   2349       N  
ATOM   5105VAL5  VAL E   6      11.741 -15.140 129.468  1.00 45.35         VAL  
ANISOU 5105VAL5  VAL E   6     5888   5609   5735     64   -710   2275     VAL  
ATOM   5106VAL6  VAL E   6      12.741 -14.254 129.407  1.00 50.44         VAL  
ANISOU 5106VAL6  VAL E   6     6425   6376   6363    107   -808   2218     VAL  
ATOM   5107  P   VAL E   7      17.322 -13.074 132.985  1.00 60.03           P  
ANISOU 5107  P   VAL E   7     7010   8799   7002    431  -1313   2389       P  
ATOM   5108  OP1 VAL E   7      18.687 -12.590 133.324  1.00 60.35           O  
ANISOU 5108  OP1 VAL E   7     6840   9120   6973    494  -1446   2322       O  
ATOM   5109  OP2 VAL E   7      17.104 -14.510 132.658  1.00 73.92           O1-
ANISOU 5109  OP2 VAL E   7     8928  10258   8900    533  -1203   2556       O1-
ATOM   5110  O5' VAL E   7      16.348 -12.641 134.168  1.00 39.90           O  
ANISOU 5110  O5' VAL E   7     4468   6498   4193    322  -1321   2383       O  
ATOM   5111VAL5' VAL E   7      16.226 -11.275 134.540  1.00 44.61         VAL  
ANISOU 5111VAL5' VAL E   7     4953   7366   4630    185  -1388   2184     VAL  
ATOM   5112VAL4' VAL E   7      14.959 -11.022 135.318  1.00 64.82         VAL  
ANISOU 5112VAL4' VAL E   7     7583  10034   7010     71  -1333   2180     VAL  
ATOM   5113  O4' VAL E   7      13.808 -11.200 134.455  1.00 69.89           O  
ANISOU 5113  O4' VAL E   7     8378  10364   7813      8  -1220   2199       O  
ATOM   5114VAL3' VAL E   7      14.693 -11.952 136.492  1.00 66.73         VAL  
ANISOU 5114VAL3' VAL E   7     7872  10393   7091    139  -1312   2372     VAL  
ATOM   5115  O3' VAL E   7      15.405 -11.572 137.660  1.00 68.13           O  
ANISOU 5115  O3' VAL E   7     7908  10957   7022    157  -1415   2327       O  
ATOM   5116VAL2' VAL E   7      13.178 -11.870 136.650  1.00 75.19         VAL  
ANISOU 5116VAL2' VAL E   7     9060  11395   8116     17  -1203   2379     VAL  
ATOM   5117  O2' VAL E   7      12.810 -10.717 137.392  1.00 92.41           O  
ANISOU 5117  O2' VAL E   7    11161  13882  10070   -112  -1231   2204       O  
ATOM   5118VAL1' VAL E   7      12.717 -11.691 135.202  1.00 70.68         VAL  
ANISOU 5118VAL1' VAL E   7     8566  10490   7800    -33  -1141   2305     VAL  
ATOM   5119  N1  VAL E   7      12.240 -12.958 134.599  1.00 65.83           N  
ANISOU 5119  N1  VAL E   7     8098   9534   7382     22  -1032   2457       N  
ATOM   5120VAL2  VAL E   7      10.925 -13.302 134.833  1.00 60.55         VAL  
ANISOU 5120VAL2  VAL E   7     7524   8795   6686    -64   -929   2512     VAL  
ATOM   5121  O2  VAL E   7      10.172 -12.614 135.499  1.00 63.28           O  
ANISOU 5121  O2  VAL E   7     7841   9346   6858   -168   -921   2456       O  
ATOM   5122  N3  VAL E   7      10.516 -14.481 134.258  1.00 53.63           N  
ANISOU 5122  N3  VAL E   7     6774   7612   5989    -34   -823   2614       N  
ATOM   5123VAL4  VAL E   7      11.274 -15.335 133.485  1.00 54.90         VAL  
ANISOU 5123VAL4  VAL E   7     6989   7530   6342     76   -804   2656     VAL  
ATOM   5124  O4  VAL E   7      10.773 -16.364 133.028  1.00 70.06           O  
ANISOU 5124  O4  VAL E   7     9032   9192   8394     75   -694   2716       O  
ATOM   5125VAL5  VAL E   7      12.626 -14.911 133.288  1.00 57.44         VAL  
ANISOU 5125VAL5  VAL E   7     7207   7939   6680    173   -911   2609     VAL  
ATOM   5126VAL6  VAL E   7      13.053 -13.767 133.837  1.00 61.90         VAL  
ANISOU 5126VAL6  VAL E   7     7634   8805   7081    141  -1023   2518     VAL  
ATOM   5127  P   VAL E   8      15.290 -12.438 139.011  1.00 74.91           P  
ANISOU 5127  P   VAL E   8     8797  11994   7671    241  -1415   2533       P  
ATOM   5128  OP1 VAL E   8      16.273 -11.922 139.993  1.00 85.11           O  
ANISOU 5128  OP1 VAL E   8     9914  13689   8736    264  -1544   2443       O  
ATOM   5129  OP2 VAL E   8      15.292 -13.876 138.653  1.00 87.20           O1-
ANISOU 5129  OP2 VAL E   8    10488  13249   9396    384  -1347   2784       O1-
ATOM   5130  O5' VAL E   8      13.841 -12.101 139.577  1.00 63.84           O  
ANISOU 5130  O5' VAL E   8     7482  10646   6127     96  -1318   2505       O  
ATOM   5131VAL5' VAL E   8      13.175 -13.018 140.428  1.00 77.88         VAL  
ANISOU 5131VAL5' VAL E   8     9366  12429   7797    135  -1247   2718     VAL  
ATOM   5132VAL4' VAL E   8      11.684 -12.997 140.221  1.00 77.71         VAL  
ANISOU 5132VAL4' VAL E   8     9464  12247   7815      6  -1110   2716     VAL  
ATOM   5133  O4' VAL E   8      11.368 -13.294 138.842  1.00 62.95           O  
ANISOU 5133  O4' VAL E   8     7678  10000   6239     -4  -1045   2712       O  
ATOM   5134VAL3' VAL E   8      10.907 -14.034 141.010  1.00104.93         VAL  
ANISOU 5134VAL3' VAL E   8    13036  15656  11178     32  -1010   2942     VAL  
ATOM   5135  O3' VAL E   8      10.682 -13.624 142.345  1.00117.76           O  
ANISOU 5135  O3' VAL E   8    14612  17631  12501    -12  -1027   2927       O  
ATOM   5136VAL2' VAL E   8       9.628 -14.212 140.195  1.00 95.16         VAL  
ANISOU 5136VAL2' VAL E   8    11910  14126  10120    -81   -871   2932     VAL  
ATOM   5137  O2' VAL E   8       8.675 -13.212 140.526  1.00 90.39           O  
ANISOU 5137  O2' VAL E   8    11267  13698   9379   -238   -831   2775       O  
ATOM   5138VAL1' VAL E   8      10.122 -13.951 138.769  1.00 68.81         VAL  
ANISOU 5138VAL1' VAL E   8     8552  10548   7043    -66   -907   2816     VAL  
ATOM   5139  N9  VAL E   8      10.234 -15.146 137.907  1.00 52.70           N  
ANISOU 5139  N9  VAL E   8     6628   8140   5254     18   -840   2948       N  
ATOM   5140VAL8  VAL E   8      11.345 -15.537 137.203  1.00 55.26         VAL  
ANISOU 5140VAL8  VAL E   8     6940   8317   5740    143   -894   2963     VAL  
ATOM   5141  N7  VAL E   8      11.139 -16.595 136.471  1.00 48.93           N  
ANISOU 5141  N7  VAL E   8     6267   7181   5145    180   -795   3049       N  
ATOM   5142VAL5  VAL E   8       9.809 -16.914 136.685  1.00 62.91         VAL  
ANISOU 5142VAL5  VAL E   8     8133   8874   6898     65   -674   3092     VAL  
ATOM   5143VAL6  VAL E   8       9.022 -17.970 136.161  1.00 78.22         VAL  
ANISOU 5143VAL6  VAL E   8    10221  10500   8999     24   -527   3162     VAL  
ATOM   5144  O6  VAL E   8       9.313 -18.874 135.366  1.00 82.07           O  
ANISOU 5144  O6  VAL E   8    10804  10698   9680     80   -469   3191       O  
ATOM   5145  N1  VAL E   8       7.723 -17.902 136.647  1.00 69.66           N  
ANISOU 5145  N1  VAL E   8     9170   9469   7828   -116   -433   3180       N  
ATOM   5146VAL2  VAL E   8       7.232 -16.966 137.520  1.00 75.78         VAL  
ANISOU 5146VAL2  VAL E   8     9857  10553   8383   -197   -467   3136     VAL  
ATOM   5147  N2  VAL E   8       5.942 -17.084 137.871  1.00 66.67           N  
ANISOU 5147  N2  VAL E   8     8747   9407   7179   -331   -347   3161       N  
ATOM   5148  N3  VAL E   8       7.960 -15.985 138.017  1.00 81.28           N  
ANISOU 5148  N3  VAL E   8    10427  11538   8916   -159   -599   3055       N  
ATOM   5149VAL4  VAL E   8       9.230 -16.019 137.560  1.00 62.05         VAL  
ANISOU 5149VAL4  VAL E   8     7950   9060   6567    -32   -699   3038     VAL  
ATOM   5150  P   VAL E   9      10.854 -14.682 143.535  1.00115.60           P  
ANISOU 5150  P   VAL E   9    14403  17471  12048    110  -1018   3189       P  
ATOM   5151  OP1 VAL E   9      10.801 -13.953 144.829  1.00110.29           O  
ANISOU 5151  OP1 VAL E   9    13643  17213  11048     52  -1063   3101       O  
ATOM   5152  OP2 VAL E   9      12.038 -15.518 143.210  1.00115.95           O1-
ANISOU 5152  OP2 VAL E   9    14444  17398  12212    297  -1094   3336       O1-
ATOM   5153  O5' VAL E   9       9.556 -15.594 143.406  1.00107.59           O  
ANISOU 5153  O5' VAL E   9    13572  16176  11134     57   -837   3354       O  
ATOM   5154VAL5' VAL E   9       8.261 -15.012 143.352  1.00100.70         VAL  
ANISOU 5154VAL5' VAL E   9    12718  15303  10241   -120   -729   3235     VAL  
ATOM   5155VAL4' VAL E   9       7.203 -16.058 143.123  1.00106.46         VAL  
ANISOU 5155VAL4' VAL E   9    13609  15738  11102   -160   -558   3402     VAL  
ATOM   5156  O4' VAL E   9       7.108 -16.379 141.715  1.00102.71           O  
ANISOU 5156  O4' VAL E   9    13179  14905  10942   -173   -521   3364       O  
ATOM   5157VAL3' VAL E   9       7.461 -17.397 143.786  1.00120.34         VAL  
ANISOU 5157VAL3' VAL E   9    15501  17410  12813    -32   -507   3685     VAL  
ATOM   5158  O3' VAL E   9       7.117 -17.392 145.157  1.00121.53           O  
ANISOU 5158  O3' VAL E   9    15670  17836  12670    -44   -476   3777       O  
ATOM   5159VAL2' VAL E   9       6.629 -18.362 142.947  1.00124.50         VAL  
ANISOU 5159VAL2' VAL E   9    16180  17531  13594    -89   -342   3771     VAL  
ATOM   5160  O2' VAL E   9       5.264 -18.310 143.340  1.00130.83           O  
ANISOU 5160  O2' VAL E   9    17030  18352  14326   -249   -190   3767       O  
ATOM   5161VAL1' VAL E   9       6.734 -17.734 141.559  1.00106.54         VAL  
ANISOU 5161VAL1' VAL E   9    13826  15094  11559   -140   -391   3562     VAL  
ATOM   5162  N9  VAL E   9       7.676 -18.392 140.630  1.00 88.23           N  
ANISOU 5162  N9  VAL E   9    11546  12513   9466    -14   -434   3601       N  
ATOM   5163VAL8  VAL E   9       8.990 -18.093 140.357  1.00 72.96         VAL  
ANISOU 5163VAL8  VAL E   9     9516  10649   7556    116   -583   3554     VAL  
ATOM   5164  N7  VAL E   9       9.514 -18.843 139.414  1.00 67.65           N  
ANISOU 5164  N7  VAL E   9     8910   9677   7118    199   -565   3589       N  
ATOM   5165VAL5  VAL E   9       8.471 -19.679 139.028  1.00 79.39         VAL  
ANISOU 5165VAL5  VAL E   9    10549  10874   8740    108   -396   3648     VAL  
ATOM   5166VAL6  VAL E   9       8.367 -20.706 138.069  1.00 98.23         VAL  
ANISOU 5166VAL6  VAL E   9    13070  12878  11373    113   -289   3677     VAL  
ATOM   5167  N6  VAL E   9       9.376 -21.095 137.284  1.00102.23           N  
ANISOU 5167  N6  VAL E   9    13584  13217  12043    233   -337   3661       N  
ATOM   5168  N1  VAL E   9       7.170 -21.332 137.943  1.00 92.83           N  
ANISOU 5168  N1  VAL E   9    12513  12000  10759    -24   -119   3710       N  
ATOM   5169VAL2  VAL E   9       6.161 -20.950 138.734  1.00 86.44         VAL  
ANISOU 5169VAL2  VAL E   9    11688  11368   9789   -146    -59   3726     VAL  
ATOM   5170  N3  VAL E   9       6.135 -19.999 139.661  1.00 88.95           N  
ANISOU 5170  N3  VAL E   9    11888  12040   9869   -155   -143   3703       N  
ATOM   5171VAL4  VAL E   9       7.333 -19.399 139.763  1.00 83.08         VAL  
ANISOU 5171VAL4  VAL E   9    11029  11483   9056    -26   -315   3659     VAL  
ATOM   5172  P   VAL E  10       7.942 -18.302 146.187  1.00127.70           P  
ANISOU 5172  P   VAL E  10    16517  18730  13275    138   -523   4036       P  
ATOM   5173  OP1 VAL E  10       7.974 -17.603 147.497  1.00128.82           O  
ANISOU 5173  OP1 VAL E  10    16575  19303  13069    119   -584   3993       O  
ATOM   5174  OP2 VAL E  10       9.210 -18.687 145.519  1.00124.70           O1-
ANISOU 5174  OP2 VAL E  10    16098  18225  13056    302   -641   4078       O1-
ATOM   5175  O5' VAL E  10       7.052 -19.614 146.326  1.00145.09           O  
ANISOU 5175  O5' VAL E  10    18943  20636  15549    121   -318   4279       O  
ATOM   5176VAL5' VAL E  10       5.639 -19.544 146.178  1.00150.96         VAL  
ANISOU 5176VAL5' VAL E  10    19751  21263  16342    -69   -142   4221     VAL  
ATOM   5177VAL4' VAL E  10       5.065 -20.816 145.600  1.00159.46         VAL  
ANISOU 5177VAL4' VAL E  10    21020  21921  17647    -98     38   4376     VAL  
ATOM   5178  O4' VAL E  10       5.565 -21.022 144.246  1.00147.33           O  
ANISOU 5178  O4' VAL E  10    19471  20096  16413    -61     -6   4294       O  
ATOM   5179VAL3' VAL E  10       5.386 -22.092 146.380  1.00181.12         VAL  
ANISOU 5179VAL3' VAL E  10    23943  24571  20301     27    107   4683     VAL  
ATOM   5180  O3' VAL E  10       4.238 -22.937 146.398  1.00210.62           O  
ANISOU 5180  O3' VAL E  10    27861  28051  24115   -111    344   4788       O  
ATOM   5181VAL2' VAL E  10       6.487 -22.740 145.542  1.00162.32         VAL  
ANISOU 5181VAL2' VAL E  10    21584  21953  18137    186     23   4741     VAL  
ATOM   5182  O2' VAL E  10       6.587 -24.142 145.684  1.00154.43           O  
ANISOU 5182  O2' VAL E  10    20787  20681  17207    264    139   4997       O  
ATOM   5183VAL1' VAL E  10       6.080 -22.333 144.128  1.00149.36         VAL  
ANISOU 5183VAL1' VAL E  10    19886  20082  16781     61     46   4507     VAL  
ATOM   5184  N1  VAL E  10       7.200 -22.328 143.170  1.00138.42           N  
ANISOU 5184  N1  VAL E  10    18433  18576  15584    187    -85   4436       N  
ATOM   5185VAL2  VAL E  10       7.142 -23.093 141.989  1.00132.64         VAL  
ANISOU 5185VAL2  VAL E  10    17802  17444  15150    166      1   4413     VAL  
ATOM   5186  O2  VAL E  10       6.123 -23.757 141.732  1.00135.44           O  
ANISOU 5186  O2  VAL E  10    18297  17550  15613     26    185   4441       O  
ATOM   5187  N3  VAL E  10       8.205 -23.079 141.144  1.00116.91           N  
ANISOU 5187  N3  VAL E  10    15747  15356  13318    287   -111   4345       N  
ATOM   5188VAL4  VAL E  10       9.289 -22.359 141.440  1.00105.10         VAL  
ANISOU 5188VAL4  VAL E  10    14089  14139  11704    418   -298   4306     VAL  
ATOM   5189  N4  VAL E  10      10.316 -22.364 140.587  1.00 96.53           N  
ANISOU 5189  N4  VAL E  10    12941  12952  10785    526   -390   4237       N  
ATOM   5190VAL5  VAL E  10       9.376 -21.586 142.632  1.00113.60         VAL  
ANISOU 5190VAL5  VAL E  10    15056  15626  12480    430   -393   4320     VAL  
ATOM   5191VAL6  VAL E  10       8.323 -21.603 143.457  1.00128.39         VAL  
ANISOU 5191VAL6  VAL E  10    17000  17592  14190    318   -284   4383     VAL  
ATOM   5192  P   VAL E  11       3.336 -23.038 147.724  1.00241.85           P  
ANISOU 5192  P   VAL E  11    31905  32193  27793   -199    489   4913       P  
ATOM   5193  OP1 VAL E  11       1.919 -22.976 147.305  1.00244.22           O  
ANISOU 5193  OP1 VAL E  11    32234  32341  28220   -435    692   4796       O  
ATOM   5194  OP2 VAL E  11       3.856 -22.055 148.702  1.00244.35           O1-
ANISOU 5194  OP2 VAL E  11    32074  32966  27800   -122    323   4858       O1-
ATOM   5195  O5' VAL E  11       3.641 -24.505 148.288  1.00252.63           O  
ANISOU 5195  O5' VAL E  11    33504  33358  29127    -91    590   5246       O  
ATOM   5196VAL5' VAL E  11       4.971 -24.873 148.636  1.00257.57         VAL  
ANISOU 5196VAL5' VAL E  11    34124  34070  29671    152    427   5413     VAL  
ATOM   5197VAL4' VAL E  11       5.035 -26.330 149.054  1.00264.03         VAL  
ANISOU 5197VAL4' VAL E  11    35180  34641  30500    226    563   5734     VAL  
ATOM   5198  O4' VAL E  11       3.977 -26.602 150.004  1.00266.94           O  
ANISOU 5198  O4' VAL E  11    35688  35056  30679     88    757   5854       O  
ATOM   5199VAL3' VAL E  11       4.865 -27.336 147.911  1.00262.17         VAL  
ANISOU 5199VAL3' VAL E  11    35079  33917  30617    165    693   5753     VAL  
ATOM   5200  O3' VAL E  11       5.922 -28.290 147.935  1.00259.93           O  
ANISOU 5200  O3' VAL E  11    34873  33498  30390    382    637   5981       O  
ATOM   5201VAL2' VAL E  11       3.506 -27.987 148.181  1.00264.33         VAL  
ANISOU 5201VAL2' VAL E  11    35543  33988  30903    -66    968   5829     VAL  
ATOM   5202VAL1' VAL E  11       3.359 -27.823 149.686  1.00266.01         VAL  
ANISOU 5202VAL1' VAL E  11    35792  34530  30748    -21    982   6002     VAL  
ATOM   5203  N1  VAL E  11       1.942 -27.754 150.135  1.00261.57           N  
ANISOU 5203  N1  VAL E  11    35313  33969  30102   -270   1210   5966       N  
ATOM   5204VAL2  VAL E  11       1.394 -28.821 150.805  1.00265.24         VAL  
ANISOU 5204VAL2  VAL E  11    36007  34269  30502   -348   1423   6219     VAL  
ATOM   5205  O2  VAL E  11       2.012 -29.840 151.056  1.00269.99           O  
ANISOU 5205  O2  VAL E  11    36750  34719  31114   -209   1431   6487       O  
ATOM   5206  N3  VAL E  11       0.086 -28.653 151.174  1.00262.53           N  
ANISOU 5206  N3  VAL E  11    35713  33949  30087   -595   1637   6150       N  
ATOM   5207VAL4  VAL E  11      -0.711 -27.546 150.945  1.00255.06         VAL  
ANISOU 5207VAL4  VAL E  11    34600  33176  29135   -747   1658   5864     VAL  
ATOM   5208  O4  VAL E  11      -1.877 -27.490 151.317  1.00253.09           O  
ANISOU 5208  O4  VAL E  11    34394  32942  28829   -958   1872   5819       O  
ATOM   5209VAL5  VAL E  11      -0.074 -26.461 150.237  1.00250.10         VAL  
ANISOU 5209VAL5  VAL E  11    33733  32714  28581   -642   1418   5624     VAL  
ATOM   5210VAL7  VAL E  11      -0.837 -25.207 149.929  1.00243.12         VAL  
ANISOU 5210VAL7  VAL E  11    32639  32028  27706   -781   1412   5322     VAL  
ATOM   5211VAL6  VAL E  11       1.206 -26.616 149.871  1.00253.46         VAL  
ANISOU 5211VAL6  VAL E  11    34121  33112  29069   -422   1210   5684     VAL  
ATOM   5212  P   VAL E  12       7.104 -28.207 146.849  1.00235.80           P  
ANISOU 5212  P   VAL E  12    31691  30339  27564    540    466   5871       P  
ATOM   5213  OP1 VAL E  12       7.071 -26.858 146.245  1.00228.16           O  
ANISOU 5213  OP1 VAL E  12    30511  29558  26622    462    336   5550       O  
ATOM   5214  OP2 VAL E  12       7.008 -29.402 145.984  1.00237.76           O1-
ANISOU 5214  OP2 VAL E  12    32104  30123  28112    506    613   5943       O1-
ATOM   5215  O5' VAL E  12       8.435 -28.349 147.722  1.00230.56           O  
ANISOU 5215  O5' VAL E  12    30959  29948  26695    836    290   6089       O  
ATOM   5216VAL5' VAL E  12       9.669 -27.861 147.220  1.00223.64         VAL  
ANISOU 5216VAL5' VAL E  12    29891  29200  25881   1006     78   5984     VAL  
ATOM   5217VAL4' VAL E  12      10.797 -28.817 147.550  1.00229.92         VAL  
ANISOU 5217VAL4' VAL E  12    30724  29963  26672   1278     26   6264     VAL  
ATOM   5218  O4' VAL E  12      10.598 -29.364 148.880  1.00232.09           O  
ANISOU 5218  O4' VAL E  12    31121  30386  26676   1353     87   6559       O  
ATOM   5219VAL3' VAL E  12      10.920 -30.014 146.615  1.00239.67         VAL  
ANISOU 5219VAL3' VAL E  12    32111  30721  28234   1310    161   6354     VAL  
ATOM   5220  O3' VAL E  12      12.283 -30.312 146.408  1.00255.09           O  
ANISOU 5220  O3' VAL E  12    33964  32706  30252   1570     29   6445       O  
ATOM   5221VAL2' VAL E  12      10.216 -31.127 147.382  1.00236.81         VAL  
ANISOU 5221VAL2' VAL E  12    31991  30182  27803   1282    367   6649     VAL  
ATOM   5222VAL1' VAL E  12      10.555 -30.774 148.820  1.00237.94         VAL  
ANISOU 5222VAL1' VAL E  12    32076  30766  27564   1424    256   6829     VAL  
ATOM   5223  N1  VAL E  12       9.542 -31.247 149.797  1.00243.00           N  
ANISOU 5223  N1  VAL E  12    32912  31396  28020   1312    437   7025       N  
ATOM   5224VAL2  VAL E  12       9.962 -31.809 150.977  1.00245.96         VAL  
ANISOU 5224VAL2  VAL E  12    33359  31949  28146   1509    429   7355     VAL  
ATOM   5225  O2  VAL E  12      11.137 -31.943 151.270  1.00245.30           O  
ANISOU 5225  O2  VAL E  12    33174  32046  27984   1780    272   7496       O  
ATOM   5226  N3  VAL E  12       8.953 -32.209 151.810  1.00249.75           N  
ANISOU 5226  N3  VAL E  12    34030  32400  28464   1376    615   7519       N  
ATOM   5227VAL4  VAL E  12       7.592 -32.108 151.583  1.00248.70         VAL  
ANISOU 5227VAL4  VAL E  12    34008  32087  28401   1064    809   7378     VAL  
ATOM   5228  O4  VAL E  12       6.758 -32.497 152.395  1.00249.50           O  
ANISOU 5228  O4  VAL E  12    34275  32180  28344    953    981   7541       O  
ATOM   5229VAL5  VAL E  12       7.219 -31.509 150.324  1.00245.49         VAL  
ANISOU 5229VAL5  VAL E  12    33501  31514  28260    878    799   7029     VAL  
ATOM   5230VAL7  VAL E  12       5.772 -31.344 149.969  1.00244.51         VAL  
ANISOU 5230VAL7  VAL E  12    33459  31215  28228    544    997   6850     VAL  
ATOM   5231VAL6  VAL E  12       8.200 -31.112 149.501  1.00242.30         VAL  
ANISOU 5231VAL6  VAL E  12    32925  31131  28009   1013    615   6875     VAL  
ATOM   5232  P   VAL E  13      13.140 -29.444 145.365  1.00272.43           P  
ANISOU 5232  P   VAL E  13    35937  34972  32603   1605   -146   6160       P  
ATOM   5233  OP1 VAL E  13      14.226 -28.775 146.116  1.00278.86           O  
ANISOU 5233  OP1 VAL E  13    36537  36241  33178   1797   -371   6195       O  
ATOM   5234  OP2 VAL E  13      12.182 -28.638 144.576  1.00269.98           O1-
ANISOU 5234  OP2 VAL E  13    35608  34571  32402   1337   -100   5851       O1-
ATOM   5235  O5' VAL E  13      13.769 -30.543 144.394  1.00275.17           O  
ANISOU 5235  O5' VAL E  13    36367  34919  33267   1727    -68   6239       O  
ATOM   5236VAL5' VAL E  13      13.072 -31.761 144.174  1.00277.73         VAL  
ANISOU 5236VAL5' VAL E  13    36933  34831  33759   1655    160   6386     VAL  
ATOM   5237VAL4' VAL E  13      13.171 -32.175 142.722  1.00278.23         VAL  
ANISOU 5237VAL4' VAL E  13    37033  34508  34173   1593    235   6214     VAL  
ATOM   5238  O4' VAL E  13      11.860 -32.538 142.225  1.00273.22           O  
ANISOU 5238  O4' VAL E  13    36570  33564  33679   1316    431   6115       O  
ATOM   5239VAL3' VAL E  13      13.661 -31.089 141.790  1.00282.20         VAL  
ANISOU 5239VAL3' VAL E  13    37336  35125  34762   1560     79   5899     VAL  
ATOM   5240  O3' VAL E  13      14.306 -31.680 140.675  1.00294.41           O  
ANISOU 5240  O3' VAL E  13    38895  36379  36589   1634    113   5839       O  
ATOM   5241VAL2' VAL E  13      12.364 -30.373 141.401  1.00271.45         VAL  
ANISOU 5241VAL2' VAL E  13    36003  33726  33410   1258    143   5650     VAL  
ATOM   5242VAL1' VAL E  13      11.347 -31.514 141.386  1.00267.95         VAL  
ANISOU 5242VAL1' VAL E  13    35802  32929  33077   1113    380   5775     VAL  
ATOM   5243  N1  VAL E  13       9.997 -31.143 141.911  1.00263.21           N  
ANISOU 5243  N1  VAL E  13    35271  32400  32338    875    476   5732       N  
ATOM   5244VAL2  VAL E  13       8.854 -31.696 141.325  1.00259.95         VAL  
ANISOU 5244VAL2  VAL E  13    35008  31667  32094    625    671   5652     VAL  
ATOM   5245  O2  VAL E  13       8.981 -32.458 140.360  1.00260.64           O  
ANISOU 5245  O2  VAL E  13    35169  31423  32439    600    752   5604       O  
ATOM   5246  N3  VAL E  13       7.636 -31.374 141.827  1.00256.34           N  
ANISOU 5246  N3  VAL E  13    34600  31287  31511    409    769   5619       N  
ATOM   5247VAL4  VAL E  13       7.540 -30.548 142.870  1.00255.05         VAL  
ANISOU 5247VAL4  VAL E  13    34352  31492  31062    444    685   5662     VAL  
ATOM   5248  N4  VAL E  13       6.317 -30.260 143.328  1.00251.23           N  
ANISOU 5248  N4  VAL E  13    33916  31073  30466    228    804   5623       N  
ATOM   5249VAL5  VAL E  13       8.693 -29.981 143.489  1.00258.69         VAL  
ANISOU 5249VAL5  VAL E  13    34663  32287  31339    693    480   5737     VAL  
ATOM   5250VAL6  VAL E  13       9.889 -30.307 142.985  1.00261.72         VAL  
ANISOU 5250VAL6  VAL E  13    34990  32598  31854    898    380   5772     VAL  
ATOM   5251  P   VAL E  14      15.089 -30.765 139.615  1.00302.30           P  
ANISOU 5251  P   VAL E  14    39697  37454  37709   1650    -36   5553       P  
ATOM   5252  OP1 VAL E  14      16.124 -31.609 138.978  1.00309.03           O  
ANISOU 5252  OP1 VAL E  14    40553  38096  38768   1842    -13   5631       O  
ATOM   5253  OP2 VAL E  14      15.476 -29.508 140.292  1.00305.42           O1-
ANISOU 5253  OP2 VAL E  14    39883  38303  37860   1690   -234   5483       O1-
ATOM   5254  O5' VAL E  14      13.968 -30.447 138.526  1.00298.41           O  
ANISOU 5254  O5' VAL E  14    39278  36721  37382   1357     65   5264       O  
ATOM   5255VAL5' VAL E  14      13.213 -31.521 138.011  1.00295.15         VAL  
ANISOU 5255VAL5' VAL E  14    39071  35917  37157   1230    266   5292     VAL  
ATOM   5256VAL4' VAL E  14      11.974 -31.058 137.274  1.00286.63         VAL  
ANISOU 5256VAL4' VAL E  14    38036  34719  36150    932    340   5032     VAL  
ATOM   5257  O4' VAL E  14      11.075 -30.408 138.201  1.00283.71           O  
ANISOU 5257  O4' VAL E  14    37657  34581  35557    812    338   5053       O  
ATOM   5258VAL3' VAL E  14      12.206 -30.060 136.145  1.00279.67         VAL  
ANISOU 5258VAL3' VAL E  14    37016  33882  35365    870    236   4717     VAL  
ATOM   5259  O3' VAL E  14      11.213 -30.261 135.143  1.00275.40           O  
ANISOU 5259  O3' VAL E  14    36573  33080  34987    633    357   4520       O  
ATOM   5260VAL2' VAL E  14      12.019 -28.727 136.856  1.00274.87         VAL  
ANISOU 5260VAL2' VAL E  14    36255  33658  34526    846    104   4650     VAL  
ATOM   5261VAL1' VAL E  14      10.888 -29.066 137.819  1.00276.64         VAL  
ANISOU 5261VAL1' VAL E  14    36605  33896  34609    720    224   4797     VAL  
ATOM   5262  N9  VAL E  14      10.877 -28.252 139.024  1.00273.67           N  
ANISOU 5262  N9  VAL E  14    36124  33905  33953    768    122   4878       N  
ATOM   5263VAL8  VAL E  14      11.936 -27.579 139.585  1.00272.79         VAL  
ANISOU 5263VAL8  VAL E  14    35838  34123  33686    953    -62   4916     VAL  
ATOM   5264  N7  VAL E  14      11.618 -26.930 140.671  1.00272.21           N  
ANISOU 5264  N7  VAL E  14    35701  34372  33353    935   -118   4969       N  
ATOM   5265VAL5  VAL E  14      10.262 -27.196 140.840  1.00273.27         VAL  
ANISOU 5265VAL5  VAL E  14    35981  34374  33477    734     49   4976     VAL  
ATOM   5266VAL6  VAL E  14       9.364 -26.766 141.845  1.00271.21         VAL  
ANISOU 5266VAL6  VAL E  14    35730  34330  32986    624     91   5019     VAL  
ATOM   5267  O6  VAL E  14       9.596 -26.039 142.821  1.00268.25           O  
ANISOU 5267  O6  VAL E  14    35242  34327  32355    684    -23   5054       O  
ATOM   5268  N1  VAL E  14       8.078 -27.267 141.637  1.00272.02           N  
ANISOU 5268  N1  VAL E  14    35991  34190  33175    412    291   5006       N  
ATOM   5269VAL2  VAL E  14       7.711 -28.080 140.590  1.00272.79         VAL  
ANISOU 5269VAL2  VAL E  14    36214  33895  33540    307    424   4947     VAL  
ATOM   5270  N2  VAL E  14       6.426 -28.465 140.552  1.00272.92           N  
ANISOU 5270  N2  VAL E  14    36355  33744  33599     78    610   4929       N  
ATOM   5271  N3  VAL E  14       8.544 -28.487 139.645  1.00273.57           N  
ANISOU 5271  N3  VAL E  14    36308  33792  33845    406    380   4897       N  
ATOM   5272VAL4  VAL E  14       9.797 -28.008 139.833  1.00273.43         VAL  
ANISOU 5272VAL4  VAL E  14    36142  33995  33753    624    196   4920     VAL  
ATOM   5273  P   VAL E  15      11.279 -29.487 133.736  1.00220.02           P  
ANISOU 5273  P   VAL E  15    29467  26020  28109    542    296   4191       P  
ATOM   5274  OP1 VAL E  15      11.886 -30.403 132.744  1.00218.34           O  
ANISOU 5274  OP1 VAL E  15    29323  25517  28119    596    354   4159       O  
ATOM   5275  OP2 VAL E  15      11.876 -28.153 133.962  1.00210.93           O1-
ANISOU 5275  OP2 VAL E  15    28118  25200  26825    635    122   4103       O1-
ATOM   5276  O5' VAL E  15       9.738 -29.275 133.357  1.00202.55           O  
ANISOU 5276  O5' VAL E  15    27322  23722  25914    251    403   4027       O  
ATOM   5277VAL5' VAL E  15       8.842 -30.391 133.354  1.00193.46         VAL  
ANISOU 5277VAL5' VAL E  15    26342  22311  24851     90    578   4104     VAL  
ATOM   5278VAL4' VAL E  15       7.431 -29.981 133.765  1.00188.34         VAL  
ANISOU 5278VAL4' VAL E  15    25713  21748  24102   -141    656   4056     VAL  
ATOM   5279  O4' VAL E  15       7.469 -29.254 135.020  1.00186.79           O  
ANISOU 5279  O4' VAL E  15    25439  21863  23669    -51    587   4188       O  
ATOM   5280VAL3' VAL E  15       6.700 -29.067 132.795  1.00187.37         VAL  
ANISOU 5280VAL3' VAL E  15    25504  21664  24025   -316    635   3760     VAL  
ATOM   5281  O3' VAL E  15       5.297 -29.283 132.906  1.00196.94           O  
ANISOU 5281  O3' VAL E  15    26777  22816  25236   -573    774   3728       O  
ATOM   5282VAL2' VAL E  15       7.092 -27.682 133.299  1.00181.02         VAL  
ANISOU 5282VAL2' VAL E  15    24524  21201  23053   -192    486   3724     VAL  
ATOM   5283VAL1' VAL E  15       7.119 -27.894 134.812  1.00183.16         VAL  
ANISOU 5283VAL1' VAL E  15    24825  21635  23132   -110    499   3988     VAL  
ATOM   5284  N9  VAL E  15       8.111 -27.075 135.507  1.00185.14           N  
ANISOU 5284  N9  VAL E  15    24929  22190  23224     98    329   4056       N  
ATOM   5285VAL8  VAL E  15       9.427 -26.910 135.151  1.00183.73         VAL  
ANISOU 5285VAL8  VAL E  15    24664  22053  23093    291    197   4040     VAL  
ATOM   5286  N7  VAL E  15      10.096 -26.145 135.965  1.00183.77           N  
ANISOU 5286  N7  VAL E  15    24528  22374  22921    427     56   4105       N  
ATOM   5287VAL5  VAL E  15       9.168 -25.779 136.933  1.00185.53         VAL  
ANISOU 5287VAL5  VAL E  15    24752  22781  22960    325     94   4168     VAL  
ATOM   5288VAL6  VAL E  15       9.321 -24.953 138.073  1.00186.02         VAL  
ANISOU 5288VAL6  VAL E  15    24691  23216  22770    383    -13   4235     VAL  
ATOM   5289  O6  VAL E  15      10.341 -24.367 138.459  1.00178.33           O  
ANISOU 5289  O6  VAL E  15    23576  22496  21687    532   -174   4249       O  
ATOM   5290  N1  VAL E  15       8.133 -24.837 138.795  1.00194.50           N  
ANISOU 5290  N1  VAL E  15    25815  24376  23711    234     87   4276       N  
ATOM   5291VAL2  VAL E  15       6.945 -25.443 138.455  1.00195.42         VAL  
ANISOU 5291VAL2  VAL E  15    26071  24245  23934     45    273   4257     VAL  
ATOM   5292  N2  VAL E  15       5.901 -25.215 139.272  1.00195.68           N  
ANISOU 5292  N2  VAL E  15    26120  24416  23812    -86    362   4300       N  
ATOM   5293  N3  VAL E  15       6.788 -26.223 137.385  1.00192.99           N  
ANISOU 5293  N3  VAL E  15    25872  23592  23862    -25    370   4187       N  
ATOM   5294VAL4  VAL E  15       7.939 -26.346 136.672  1.00188.81         VAL  
ANISOU 5294VAL4  VAL E  15    25307  22977  23457    126    269   4144     VAL  
ATOM   5295  P   VAL E  16       4.319 -28.932 131.680  1.00200.07           P  
ANISOU 5295  P   VAL E  16    27132  23133  25752   -812    815   3442       P  
ATOM   5296  OP1 VAL E  16       3.392 -30.072 131.504  1.00205.54           O  
ANISOU 5296  OP1 VAL E  16    27939  23593  26562  -1053    970   3470       O  
ATOM   5297  OP2 VAL E  16       5.156 -28.475 130.550  1.00196.68           O1-
ANISOU 5297  OP2 VAL E  16    26634  22680  25415   -701    697   3262       O1-
ATOM   5298  O5' VAL E  16       3.473 -27.682 132.207  1.00192.82           O  
ANISOU 5298  O5' VAL E  16    26079  22498  24687   -880    809   3373       O  
ATOM   5299VAL5' VAL E  16       2.420 -27.884 133.144  1.00185.06         VAL  
ANISOU 5299VAL5' VAL E  16    25132  21574  23608  -1035    940   3481     VAL  
ATOM   5300VAL4' VAL E  16       2.155 -26.615 133.928  1.00174.78         VAL  
ANISOU 5300VAL4' VAL E  16    23670  20608  22133   -977    880   3483     VAL  
ATOM   5301  O4' VAL E  16       3.371 -26.220 134.614  1.00169.09           O  
ANISOU 5301  O4' VAL E  16    22902  20062  21280   -719    725   3616       O  
ATOM   5302VAL3' VAL E  16       1.738 -25.412 133.070  1.00170.14         VAL  
ANISOU 5302VAL3' VAL E  16    22888  20153  21603  -1028    805   3244     VAL  
ATOM   5303  O3' VAL E  16       0.425 -24.960 133.416  1.00178.15           O  
ANISOU 5303  O3' VAL E  16    23806  21306  22578  -1213    902   3198       O  
ATOM   5304VAL2' VAL E  16       2.792 -24.348 133.373  1.00160.72         VAL  
ANISOU 5304VAL2' VAL E  16    21558  19208  20298   -804    599   3260     VAL  
ATOM   5305VAL1' VAL E  16       3.401 -24.825 134.682  1.00161.45         VAL  
ANISOU 5305VAL1' VAL E  16    21736  19385  20224   -670    593   3509     VAL  
ATOM   5306  N1  VAL E  16       4.804 -24.349 134.838  1.00156.46           N  
ANISOU 5306  N1  VAL E  16    21028  18892  19528   -436    407   3547       N  
ATOM   5307VAL2  VAL E  16       5.169 -23.665 135.976  1.00144.42         VAL  
ANISOU 5307VAL2  VAL E  16    19407  17681  17785   -334    304   3653     VAL  
ATOM   5308  O2  VAL E  16       4.412 -23.469 136.911  1.00129.18           O  
ANISOU 5308  O2  VAL E  16    17468  15916  15699   -413    362   3731       O  
ATOM   5309  N3  VAL E  16       6.468 -23.227 135.984  1.00148.81           N  
ANISOU 5309  N3  VAL E  16    19875  18363  18305   -147    136   3655       N  
ATOM   5310VAL4  VAL E  16       7.413 -23.389 134.984  1.00148.71         VAL  
ANISOU 5310VAL4  VAL E  16    19858  18191  18454    -48     73   3568     VAL  
ATOM   5311  O4  VAL E  16       8.560 -22.962 135.085  1.00139.12           O  
ANISOU 5311  O4  VAL E  16    18546  17116  17196    108    -68   3575       O  
ATOM   5312VAL5  VAL E  16       6.956 -24.096 133.812  1.00154.59         VAL  
ANISOU 5312VAL5  VAL E  16    20715  18610  19413   -154    188   3458     VAL  
ATOM   5313VAL7  VAL E  16       7.889 -24.330 132.658  1.00152.01         VAL  
ANISOU 5313VAL7  VAL E  16    20400  18102  19255    -66    141   3346     VAL  
ATOM   5314VAL6  VAL E  16       5.688 -24.525 133.792  1.00158.23         VAL  
ANISOU 5314VAL6  VAL E  16    21260  18953  19905   -345    341   3448     VAL  
ATOM   5315  P   VAL E  17      -0.395 -24.012 132.403  1.00181.22           P  
ANISOU 5315  P   VAL E  17    23995  21783  23077  -1342    862   2957       P  
ATOM   5316  OP1 VAL E  17      -1.732 -24.606 132.192  1.00184.25           O  
ANISOU 5316  OP1 VAL E  17    24388  22057  23561  -1605   1063   2883       O  
ATOM   5317  OP2 VAL E  17       0.479 -23.714 131.245  1.00175.04           O1-
ANISOU 5317  OP2 VAL E  17    23191  20914  22404  -1226    723   2823       O1-
ATOM   5318  O5' VAL E  17      -0.593 -22.647 133.210  1.00171.37           O  
ANISOU 5318  O5' VAL E  17    22557  20909  21648  -1296    733   2979       O  
ATOM   5319VAL5' VAL E  17       0.521 -21.823 133.488  1.00155.87         VAL  
ANISOU 5319VAL5' VAL E  17    20535  19119  19568  -1093    539   3010     VAL  
ATOM   5320VAL4' VAL E  17       0.563 -21.468 134.961  1.00138.93         VAL  
ANISOU 5320VAL4' VAL E  17    18368  17238  17180  -1040    522   3166     VAL  
ATOM   5321  O4' VAL E  17       1.792 -21.964 135.538  1.00126.93           O  
ANISOU 5321  O4' VAL E  17    16954  15694  15580   -843    467   3322       O  
ATOM   5322VAL3' VAL E  17       0.499 -19.972 135.249  1.00129.41         VAL  
ANISOU 5322VAL3' VAL E  17    16979  16365  15827  -1031    372   3076     VAL  
ATOM   5323  O3' VAL E  17      -0.809 -19.638 135.705  1.00127.73           O  
ANISOU 5323  O3' VAL E  17    16686  16308  15539  -1209    471   3047       O  
ATOM   5324VAL2' VAL E  17       1.539 -19.742 136.345  1.00121.83         VAL  
ANISOU 5324VAL2' VAL E  17    16032  15602  14658   -858    272   3207     VAL  
ATOM   5325VAL1' VAL E  17       2.481 -20.935 136.212  1.00120.57         VAL  
ANISOU 5325VAL1' VAL E  17    16030  15191  14589   -722    300   3334     VAL  
ATOM   5326  N1  VAL E  17       3.750 -20.654 135.473  1.00110.18           N  
ANISOU 5326  N1  VAL E  17    14681  13823  13359   -566    148   3261       N  
ATOM   5327VAL2  VAL E  17       4.690 -19.770 136.012  1.00 84.29         VAL  
ANISOU 5327VAL2  VAL E  17    11294  10805   9927   -440    -17   3260     VAL  
ATOM   5328  O2  VAL E  17       4.449 -19.205 137.082  1.00 84.80           O  
ANISOU 5328  O2  VAL E  17    11296  11151   9774   -459    -43   3307       O  
ATOM   5329  N3  VAL E  17       5.838 -19.548 135.336  1.00 73.60           N  
ANISOU 5329  N3  VAL E  17     9903   9399   8663   -314   -134   3190       N  
ATOM   5330VAL4  VAL E  17       6.068 -20.172 134.181  1.00 93.88         VAL  
ANISOU 5330VAL4  VAL E  17    12546  11674  11450   -299    -92   3124     VAL  
ATOM   5331  N4  VAL E  17       7.225 -19.921 133.565  1.00 99.87           N  
ANISOU 5331  N4  VAL E  17    13263  12401  12284   -175   -197   3054       N  
ATOM   5332VAL5  VAL E  17       5.132 -21.087 133.620  1.00112.05         VAL  
ANISOU 5332VAL5  VAL E  17    14968  13713  13895   -423     69   3115     VAL  
ATOM   5333VAL6  VAL E  17       3.997 -21.292 134.291  1.00118.35         VAL  
ANISOU 5333VAL6  VAL E  17    15792  14562  14615   -559    184   3184     VAL  
ATOM   5334  P   VAL E  18      -1.544 -18.323 135.151  1.00119.45           P  
ANISOU 5334  P   VAL E  18    15449  15452  14483  -1319    390   2852       P  
ATOM   5335  OP1 VAL E  18      -2.680 -18.003 136.039  1.00123.30           O  
ANISOU 5335  OP1 VAL E  18    15858  16169  14824  -1459    500   2855       O  
ATOM   5336  OP2 VAL E  18      -1.774 -18.503 133.703  1.00111.77           O1-
ANISOU 5336  OP2 VAL E  18    14459  14261  13747  -1385    378   2715       O1-
ATOM   5337  O5' VAL E  18      -0.453 -17.180 135.331  1.00103.15           O  
ANISOU 5337  O5' VAL E  18    13325  13585  12284  -1159    196   2811       O  
ATOM   5338VAL5' VAL E  18      -0.147 -16.681 136.621  1.00 98.35         VAL  
ANISOU 5338VAL5' VAL E  18    12693  13254  11421  -1100    164   2880     VAL  
ATOM   5339VAL4' VAL E  18       0.739 -15.471 136.483  1.00 93.88         VAL  
ANISOU 5339VAL4' VAL E  18    12044  12855  10770  -1001     -8   2769     VAL  
ATOM   5340  O4' VAL E  18       2.107 -15.898 136.383  1.00 96.94           O  
ANISOU 5340  O4' VAL E  18    12495  13136  11203   -833   -104   2838       O  
ATOM   5341VAL3' VAL E  18       0.470 -14.683 135.213  1.00 88.67         VAL  
ANISOU 5341VAL3' VAL E  18    11313  12122  10254  -1051    -65   2595     VAL  
ATOM   5342  O3' VAL E  18      -0.375 -13.579 135.498  1.00 88.89           O  
ANISOU 5342  O3' VAL E  18    11234  12400  10142  -1150    -41   2482       O  
ATOM   5343VAL2' VAL E  18       1.854 -14.241 134.722  1.00 85.25         VAL  
ANISOU 5343VAL2' VAL E  18    10888  11641   9863   -900   -217   2546     VAL  
ATOM   5344VAL1' VAL E  18       2.835 -14.944 135.655  1.00 90.19         VAL  
ANISOU 5344VAL1' VAL E  18    11572  12304  10393   -774   -239   2696     VAL  
ATOM   5345  N9  VAL E  18       3.903 -15.635 134.950  1.00 77.40           N  
ANISOU 5345  N9  VAL E  18    10018  10448   8945   -645   -287   2729       N  
ATOM   5346VAL8  VAL E  18       3.806 -16.812 134.264  1.00 72.51         VAL  
ANISOU 5346VAL8  VAL E  18     9502   9526   8522   -639   -201   2782     VAL  
ATOM   5347  N7  VAL E  18       4.935 -17.207 133.732  1.00 76.63           N  
ANISOU 5347  N7  VAL E  18    10065   9897   9153   -506   -255   2786       N  
ATOM   5348VAL5  VAL E  18       5.834 -16.220 134.096  1.00 68.02         VAL  
ANISOU 5348VAL5  VAL E  18     8878   9027   7939   -425   -391   2739     VAL  
ATOM   5349VAL6  VAL E  18       7.203 -16.050 133.843  1.00 50.80         VAL  
ANISOU 5349VAL6  VAL E  18     6665   6846   5790   -288   -496   2716     VAL  
ATOM   5350  N6  VAL E  18       7.924 -16.915 133.132  1.00 49.95           N  
ANISOU 5350  N6  VAL E  18     6630   6498   5852   -190   -475   2740       N  
ATOM   5351  N1  VAL E  18       7.802 -14.952 134.348  1.00 56.04           N  
ANISOU 5351  N1  VAL E  18     7217   7778   6300   -265   -612   2651       N  
ATOM   5352VAL2  VAL E  18       7.072 -14.089 135.063  1.00 70.73         VAL  
ANISOU 5352VAL2  VAL E  18     9017   9885   7974   -367   -617   2602     VAL  
ATOM   5353  N3  VAL E  18       5.776 -14.141 135.366  1.00 75.75           N  
ANISOU 5353  N3  VAL E  18     9676  10550   8556   -489   -519   2620       N  
ATOM   5354VAL4  VAL E  18       5.212 -15.242 134.847  1.00 72.98         VAL  
ANISOU 5354VAL4  VAL E  18     9423   9933   8374   -514   -412   2697     VAL  
ATOM   5355  P   VAL E  19      -0.358 -12.276 134.561  1.00 78.02           P  
ANISOU 5355  P   VAL E  19     9773  11021   8849  -1099   -125   2200       P  
ATOM   5356  OP1 VAL E  19      -1.572 -11.496 134.870  1.00 66.96           O  
ANISOU 5356  OP1 VAL E  19     8265   9798   7381  -1172    -38   2026       O  
ATOM   5357  OP2 VAL E  19      -0.082 -12.702 133.172  1.00 62.44           O1-
ANISOU 5357  OP2 VAL E  19     7844   8759   7122  -1069   -174   2173       O1-
ATOM   5358  O5' VAL E  19       0.916 -11.467 135.072  1.00 92.85           O  
ANISOU 5358  O5' VAL E  19    11650  13047  10582   -980   -244   2158       O  
ATOM   5359VAL5' VAL E  19       0.830 -10.093 135.336  1.00 83.69         VAL  
ANISOU 5359VAL5' VAL E  19    10411  12064   9322   -960   -255   1920     VAL  
ATOM   5360VAL4' VAL E  19       2.115  -9.409 134.932  1.00 57.42         VAL  
ANISOU 5360VAL4' VAL E  19     7090   8699   6028   -854   -374   1814     VAL  
ATOM   5361  O4' VAL E  19       3.157 -10.405 134.763  1.00 53.08           O  
ANISOU 5361  O4' VAL E  19     6607   8031   5530   -793   -455   2026       O  
ATOM   5362VAL3' VAL E  19       2.031  -8.634 133.622  1.00 52.07         VAL  
ANISOU 5362VAL3' VAL E  19     6404   7827   5554   -805   -387   1607     VAL  
ATOM   5363  O3' VAL E  19       2.383  -7.282 133.846  1.00 60.13           O  
ANISOU 5363  O3' VAL E  19     7382   8961   6503   -772   -392   1384       O  
ATOM   5364VAL2' VAL E  19       3.020  -9.334 132.683  1.00 44.03         VAL  
ANISOU 5364VAL2' VAL E  19     5454   6572   4704   -736   -472   1710     VAL  
ATOM   5365VAL1' VAL E  19       3.937 -10.088 133.638  1.00 52.14         VAL  
ANISOU 5365VAL1' VAL E  19     6502   7714   5593   -714   -528   1923     VAL  
ATOM   5366  N9  VAL E  19       4.439 -11.325 133.055  1.00 62.76           N  
ANISOU 5366  N9  VAL E  19     7925   8836   7085   -672   -553   2129       N  
ATOM   5367VAL8  VAL E  19       3.709 -12.446 132.763  1.00 62.14         VAL  
ANISOU 5367VAL8  VAL E  19     7909   8588   7114   -729   -473   2269     VAL  
ATOM   5368  N7  VAL E  19       4.411 -13.401 132.227  1.00 65.75           N  
ANISOU 5368  N7  VAL E  19     8431   8814   7737   -645   -476   2319       N  
ATOM   5369VAL5  VAL E  19       5.689 -12.876 132.144  1.00 59.27         VAL  
ANISOU 5369VAL5  VAL E  19     7581   8034   6903   -535   -579   2272     VAL  
ATOM   5370VAL6  VAL E  19       6.873 -13.456 131.644  1.00 46.82         VAL  
ANISOU 5370VAL6  VAL E  19     6037   6294   5458   -413   -614   2289     VAL  
ATOM   5371  O6  VAL E  19       7.026 -14.585 131.162  1.00 45.25           O  
ANISOU 5371  O6  VAL E  19     5917   5871   5405   -368   -552   2342       O  
ATOM   5372  N1  VAL E  19       7.952 -12.587 131.743  1.00 53.88           N  
ANISOU 5372  N1  VAL E  19     6860   7323   6290   -348   -720   2225       N  
ATOM   5373VAL2  VAL E  19       7.893 -11.314 132.259  1.00 57.96         VAL  
ANISOU 5373VAL2  VAL E  19     7297   8095   6631   -403   -783   2137     VAL  
ATOM   5374  N2  VAL E  19       9.041 -10.622 132.274  1.00 63.96           N  
ANISOU 5374  N2  VAL E  19     7985   8961   7355   -348   -879   2056       N  
ATOM   5375  N3  VAL E  19       6.786 -10.757 132.734  1.00 53.45           N  
ANISOU 5375  N3  VAL E  19     6709   7663   5937   -503   -729   2068       N  
ATOM   5376VAL4  VAL E  19       5.726 -11.594 132.645  1.00 57.63         VAL  
ANISOU 5376VAL4  VAL E  19     7298   8082   6518   -567   -641   2185     VAL  
ATOM   5377  P   VAL E  20       2.188  -6.195 132.678  1.00 59.12           P  
ANISOU 5377  P   VAL E  20     7254   8664   6546   -705   -367   1159       P  
ATOM   5378  OP1 VAL E  20       1.895  -4.906 133.341  1.00 42.48           O  
ANISOU 5378  OP1 VAL E  20     5098   6719   4323   -714   -290    949       O  
ATOM   5379  OP2 VAL E  20       1.253  -6.756 131.673  1.00 47.46           O1-
ANISOU 5379  OP2 VAL E  20     5784   7020   5229   -704   -343   1205       O1-
ATOM   5380  O5' VAL E  20       3.637  -6.083 132.020  1.00 61.27           O  
ANISOU 5380  O5' VAL E  20     7573   8791   6916   -636   -459   1142       O  
ATOM   5381VAL5' VAL E  20       3.840  -6.307 130.631  1.00 26.29         VAL  
ANISOU 5381VAL5' VAL E  20     3198   4098   2692   -573   -486   1148     VAL  
ATOM   5382VAL4' VAL E  20       5.329  -6.326 130.336  1.00 46.47         VAL  
ANISOU 5382VAL4' VAL E  20     5781   6574   5302   -524   -563   1156     VAL  
ATOM   5383  O4' VAL E  20       5.901  -7.527 130.900  1.00 55.46           O  
ANISOU 5383  O4' VAL E  20     6920   7765   6386   -532   -631   1378       O  
ATOM   5384VAL3' VAL E  20       5.709  -6.337 128.861  1.00 46.92         VAL  
ANISOU 5384VAL3' VAL E  20     5904   6360   5564   -453   -574   1124     VAL  
ATOM   5385  O3' VAL E  20       5.870  -5.001 128.399  1.00 46.01           O  
ANISOU 5385  O3' VAL E  20     5800   6192   5491   -413   -519    916       O  
ATOM   5386VAL2' VAL E  20       7.042  -7.073 128.866  1.00 38.42         VAL  
ANISOU 5386VAL2' VAL E  20     4835   5240   4522   -424   -655   1245     VAL  
ATOM   5387VAL1' VAL E  20       6.895  -8.041 130.037  1.00 49.50         VAL  
ANISOU 5387VAL1' VAL E  20     6208   6817   5782   -465   -688   1443     VAL  
ATOM   5388  N9  VAL E  20       6.522  -9.384 129.622  1.00 56.78           N  
ANISOU 5388  N9  VAL E  20     7192   7583   6801   -468   -683   1641       N  
ATOM   5389VAL8  VAL E  20       5.284  -9.977 129.700  1.00 59.40         VAL  
ANISOU 5389VAL8  VAL E  20     7540   7900   7128   -540   -621   1713     VAL  
ATOM   5390  N7  VAL E  20       5.268 -11.198 129.233  1.00 54.29           N  
ANISOU 5390  N7  VAL E  20     6958   7072   6596   -547   -611   1872       N  
ATOM   5391VAL5  VAL E  20       6.579 -11.416 128.821  1.00 60.08         VAL  
ANISOU 5391VAL5  VAL E  20     7719   7694   7413   -454   -671   1915     VAL  
ATOM   5392VAL6  VAL E  20       7.184 -12.554 128.229  1.00 74.71         VAL  
ANISOU 5392VAL6  VAL E  20     9630   9337   9419   -383   -632   1933     VAL  
ATOM   5393  O6  VAL E  20       6.672 -13.643 127.945  1.00 85.80           O  
ANISOU 5393  O6  VAL E  20    11095  10599  10906   -408   -553   1971       O  
ATOM   5394  N1  VAL E  20       8.542 -12.340 127.974  1.00 80.96           N  
ANISOU 5394  N1  VAL E  20    10404  10101  10256   -282   -684   1900       N  
ATOM   5395VAL2  VAL E  20       9.218 -11.176 128.250  1.00 79.04         VAL  
ANISOU 5395VAL2  VAL E  20    10092  10008   9934   -267   -773   1857     VAL  
ATOM   5396  N2  VAL E  20      10.520 -11.139 127.938  1.00 78.80           N  
ANISOU 5396  N2  VAL E  20    10031   9935   9972   -181   -816   1838       N  
ATOM   5397  N3  VAL E  20       8.660 -10.114 128.797  1.00 66.60           N  
ANISOU 5397  N3  VAL E  20     8466   8618   8222   -331   -779   1751       N  
ATOM   5398VAL4  VAL E  20       7.351 -10.303 129.053  1.00 56.22         VAL  
ANISOU 5398VAL4  VAL E  20     7170   7336   6856   -409   -721   1774     VAL  
ATOM   5399  P   VAL E  21       5.798  -4.656 126.830  1.00 47.36           P  
ANISOU 5399  P   VAL E  21     6050   6107   5837   -329   -489    850       P  
ATOM   5400  OP1 VAL E  21       5.984  -3.194 126.712  1.00 56.66           O  
ANISOU 5400  OP1 VAL E  21     7245   7260   7024   -292   -402    653       O  
ATOM   5401  OP2 VAL E  21       4.593  -5.288 126.257  1.00 39.99           O1-
ANISOU 5401  OP2 VAL E  21     5125   5127   4944   -325   -487    923       O1-
ATOM   5402  O5' VAL E  21       7.085  -5.370 126.203  1.00 47.41           O  
ANISOU 5402  O5' VAL E  21     6097   5965   5951   -303   -553    934       O  
ATOM   5403VAL5' VAL E  21       8.377  -4.859 126.479  1.00 46.79         VAL  
ANISOU 5403VAL5' VAL E  21     5992   5913   5871   -303   -563    858     VAL  
ATOM   5404VAL4' VAL E  21       9.457  -5.712 125.836  1.00 42.01         VAL  
ANISOU 5404VAL4' VAL E  21     5409   5170   5381   -263   -620    961     VAL  
ATOM   5405  O4' VAL E  21       9.512  -7.013 126.463  1.00 26.97           O  
ANISOU 5405  O4' VAL E  21     3475   3341   3432   -275   -694   1166       O  
ATOM   5406VAL3' VAL E  21       9.238  -6.024 124.374  1.00 47.91         VAL  
ANISOU 5406VAL3' VAL E  21     6257   5668   6280   -206   -592    977     VAL  
ATOM   5407  O3' VAL E  21       9.670  -4.955 123.612  1.00 47.37           O  
ANISOU 5407  O3' VAL E  21     6236   5483   6280   -168   -521    825       O  
ATOM   5408VAL2' VAL E  21      10.141  -7.234 124.191  1.00 50.33         VAL  
ANISOU 5408VAL2' VAL E  21     6565   5893   6665   -183   -651   1126     VAL  
ATOM   5409VAL1' VAL E  21       9.892  -7.979 125.493  1.00 39.57         VAL  
ANISOU 5409VAL1' VAL E  21     5135   4723   5177   -224   -709   1274     VAL  
ATOM   5410  N1  VAL E  21       8.832  -8.991 125.393  1.00 52.76           N  
ANISOU 5410  N1  VAL E  21     6852   6336   6857   -256   -701   1405       N  
ATOM   5411VAL2  VAL E  21       9.153 -10.224 124.894  1.00 56.58         VAL  
ANISOU 5411VAL2  VAL E  21     7383   6672   7445   -225   -685   1495     VAL  
ATOM   5412  O2  VAL E  21      10.276 -10.527 124.534  1.00 52.47           O  
ANISOU 5412  O2  VAL E  21     6861   6078   6998   -156   -679   1477       O  
ATOM   5413  N3  VAL E  21       8.120 -11.105 124.835  1.00 46.89           N  
ANISOU 5413  N3  VAL E  21     6186   5410   6221   -274   -634   1529       N  
ATOM   5414VAL4  VAL E  21       6.808 -10.877 125.211  1.00 38.48         VAL  
ANISOU 5414VAL4  VAL E  21     5106   4431   5083   -364   -636   1565     VAL  
ATOM   5415  O4  VAL E  21       5.949 -11.746 125.118  1.00 47.44           O  
ANISOU 5415  O4  VAL E  21     6259   5522   6243   -426   -590   1604       O  
ATOM   5416VAL5  VAL E  21       6.530  -9.552 125.723  1.00 49.62         VAL  
ANISOU 5416VAL5  VAL E  21     6459   6013   6380   -371   -649   1462     VAL  
ATOM   5417VAL7  VAL E  21       5.144  -9.188 126.163  1.00 60.58         VAL  
ANISOU 5417VAL7  VAL E  21     7800   7543   7675   -436   -607   1410     VAL  
ATOM   5418VAL6  VAL E  21       7.546  -8.679 125.785  1.00 48.09         VAL  
ANISOU 5418VAL6  VAL E  21     6244   5853   6175   -316   -668   1367     VAL  
ATOM   5419  P   VAL E  22       9.314  -4.873 122.054  1.00 58.11           P  
ANISOU 5419  P   VAL E  22     7713   6616   7752    -94   -471    803       P  
ATOM   5420  OP1 VAL E  22      10.138  -3.742 121.602  1.00 65.02           O  
ANISOU 5420  OP1 VAL E  22     8627   7395   8683    -65   -382    663       O  
ATOM   5421  OP2 VAL E  22       7.849  -4.882 121.847  1.00 52.93           O1-
ANISOU 5421  OP2 VAL E  22     7071   5993   7045    -81   -467    815       O1-
ATOM   5422  O5' VAL E  22       9.966  -6.179 121.404  1.00 58.50           O  
ANISOU 5422  O5' VAL E  22     7794   6532   7902    -80   -522    927       O  
ATOM   5423VAL5' VAL E  22      11.325  -6.158 121.049  1.00 73.84         VAL  
ANISOU 5423VAL5' VAL E  22     9738   8381   9936    -55   -506    904     VAL  
ATOM   5424VAL4' VAL E  22      11.742  -7.435 120.357  1.00 66.57         VAL  
ANISOU 5424VAL4' VAL E  22     8829   7421   9043    -17   -469    918     VAL  
ATOM   5425  O4' VAL E  22      11.407  -8.568 121.190  1.00 58.76           O  
ANISOU 5425  O4' VAL E  22     7794   6517   8017    -46   -529   1049       O  
ATOM   5426VAL3' VAL E  22      11.049  -7.698 119.039  1.00 69.16         VAL  
ANISOU 5426VAL3' VAL E  22     9239   7698   9341     21   -371    821     VAL  
ATOM   5427  O3' VAL E  22      11.733  -7.030 117.973  1.00 72.47           O  
ANISOU 5427  O3' VAL E  22     9719   8043   9773     73   -267    710       O  
ATOM   5428VAL2' VAL E  22      11.161  -9.221 118.926  1.00 67.07         VAL  
ANISOU 5428VAL2' VAL E  22     8974   7426   9085     16   -363    872     VAL  
ATOM   5429VAL1' VAL E  22      10.998  -9.660 120.381  1.00 61.15         VAL  
ANISOU 5429VAL1' VAL E  22     8149   6763   8322    -31   -460   1017     VAL  
ATOM   5430  N1  VAL E  22       9.597 -10.024 120.766  1.00 60.87           N  
ANISOU 5430  N1  VAL E  22     8111   6777   8239    -93   -488   1073       N  
ATOM   5431VAL2  VAL E  22       9.178 -11.355 120.686  1.00 60.70         VAL  
ANISOU 5431VAL2  VAL E  22     8113   6718   8232   -121   -459   1122     VAL  
ATOM   5432  O2  VAL E  22       9.971 -12.213 120.279  1.00 77.44           O  
ANISOU 5432  O2  VAL E  22    10269   8760  10395    -79   -405   1115       O  
ATOM   5433  N3  VAL E  22       7.910 -11.664 121.054  1.00 45.26           N  
ANISOU 5433  N3  VAL E  22     6146   4799   6250   -202   -483   1182       N  
ATOM   5434VAL4  VAL E  22       7.087 -10.707 121.491  1.00 45.40         VAL  
ANISOU 5434VAL4  VAL E  22     6128   4908   6214   -242   -539   1199     VAL  
ATOM   5435  N4  VAL E  22       5.846 -11.059 121.842  1.00 35.79           N  
ANISOU 5435  N4  VAL E  22     4889   3737   4970   -335   -559   1272       N  
ATOM   5436VAL5  VAL E  22       7.498  -9.346 121.584  1.00 44.08         VAL  
ANISOU 5436VAL5  VAL E  22     5950   4777   6021   -196   -566   1150     VAL  
ATOM   5437VAL6  VAL E  22       8.749  -9.056 121.223  1.00 49.25         VAL  
ANISOU 5437VAL6  VAL E  22     6620   5375   6718   -130   -537   1086     VAL  
ATOM   5438  P   VAL E  23      10.966  -5.954 117.053  1.00 87.70           P  
ANISOU 5438  P   VAL E  23    11721   9941  11659    120   -183    628       P  
ATOM   5439  OP1 VAL E  23      11.217  -6.319 115.639  1.00 92.29           O  
ANISOU 5439  OP1 VAL E  23    12364  10483  12220    167    -70    577       O  
ATOM   5440  OP2 VAL E  23      11.354  -4.602 117.518  1.00101.02           O1-
ANISOU 5440  OP2 VAL E  23    13420  11584  13378    120   -161    587       O1-
ATOM   5441  O5' VAL E  23       9.412  -6.155 117.415  1.00 90.83           O  
ANISOU 5441  O5' VAL E  23    12095  10397  12019     97   -272    687       O  
ATOM   5442VAL5' VAL E  23       8.534  -6.864 116.519  1.00100.24         VAL  
ANISOU 5442VAL5' VAL E  23    13307  11590  13190    103   -275    688     VAL  
ATOM   5443VAL4' VAL E  23       8.961  -8.316 116.395  1.00113.62         VAL  
ANISOU 5443VAL4' VAL E  23    14994  13267  14912     60   -271    711     VAL  
ATOM   5444  O4' VAL E  23       8.181  -9.147 117.268  1.00106.31           O  
ANISOU 5444  O4' VAL E  23    14022  12379  13992    -18   -360    799       O  
ATOM   5445VAL3' VAL E  23       8.795  -8.960 115.032  1.00105.58         VAL  
ANISOU 5445VAL3' VAL E  23    14025  12189  13901     73   -218    667     VAL  
ATOM   5446  O3' VAL E  23       9.934  -8.680 114.221  1.00 86.44           O  
ANISOU 5446  O3' VAL E  23    11637   9722  11483    131    -96    609       O  
ATOM   5447VAL2' VAL E  23       8.703 -10.461 115.378  1.00101.88         VAL  
ANISOU 5447VAL2' VAL E  23    13549  11691  13470      2   -244    717     VAL  
ATOM   5448VAL1' VAL E  23       8.454 -10.474 116.899  1.00 94.68         VAL  
ANISOU 5448VAL1' VAL E  23    12571  10849  12554    -44   -324    808     VAL  
ATOM   5449  N9  VAL E  23       7.355 -11.354 117.308  1.00 81.44           N  
ANISOU 5449  N9  VAL E  23    10875   9173  10895   -138   -382    882       N  
ATOM   5450VAL8  VAL E  23       7.322 -12.716 117.178  1.00 77.97         VAL  
ANISOU 5450VAL8  VAL E  23    10463   8657  10503   -191   -343    910     VAL  
ATOM   5451  N7  VAL E  23       6.221 -13.266 117.618  1.00 77.15           N  
ANISOU 5451  N7  VAL E  23    10338   8557  10417   -299   -389    979       N  
ATOM   5452VAL5  VAL E  23       5.472 -12.193 118.070  1.00 82.39         VAL  
ANISOU 5452VAL5  VAL E  23    10950   9324  11033   -313   -476   1007     VAL  
ATOM   5453VAL6  VAL E  23       4.196 -12.115 118.655  1.00 81.97         VAL  
ANISOU 5453VAL6  VAL E  23    10845   9336  10962   -424   -549   1091     VAL  
ATOM   5454  N6  VAL E  23       3.434 -13.180 118.888  1.00 69.46           N  
ANISOU 5454  N6  VAL E  23     9249   7724   9420   -566   -536   1152       N  
ATOM   5455  N1  VAL E  23       3.734 -10.895 118.993  1.00 82.10           N  
ANISOU 5455  N1  VAL E  23    10822   9457  10916   -390   -609   1105       N  
ATOM   5456VAL2  VAL E  23       4.504  -9.826 118.756  1.00 84.86         VAL  
ANISOU 5456VAL2  VAL E  23    11199   9805  11241   -262   -594   1036     VAL  
ATOM   5457  N3  VAL E  23       5.720  -9.773 118.210  1.00 80.44           N  
ANISOU 5457  N3  VAL E  23    10682   9183  10699   -176   -519    948       N  
ATOM   5458VAL4  VAL E  23       6.152 -11.003 117.886  1.00 79.13         VAL  
ANISOU 5458VAL4  VAL E  23    10540   8945  10580   -205   -469    944     VAL  
TER    5459      VAL E  23                                                      
ATOM   5460 MG    MG A 601       8.801  -8.561 108.483  1.00 39.35          MG  
ANISOU 5460 MG    MG A 601     5820   3587   5545    217   -119    485      MG  
ATOM   5461 MG    MG A 602      10.144  -6.852 112.364  1.00 44.95          MG  
ANISOU 5461 MG    MG A 602     6329   4475   6276    222     29    536      MG  
ATOM   5462  O4  VAL A 603      -1.318 -14.170 118.097  1.00 74.38           O  
ANISOU 5462  O4  VAL A 603     9539   8755   9968  -1025   -564    879       O  
ATOM   5463  C10 VAL A 603       2.714 -13.076 115.358  1.00 55.63           C  
ANISOU 5463  C10 VAL A 603     7609   5829   7700   -564   -616    861       C  
ATOM   5464  C11 VAL A 603       2.187 -11.835 115.721  1.00 57.96           C  
ANISOU 5464  C11 VAL A 603     7818   6322   7883   -467   -657    843       C  
ATOM   5465  C12 VAL A 603       0.988 -11.858 116.422  1.00 70.72           C  
ANISOU 5465  C12 VAL A 603     9299   8130   9444   -550   -670    835       C  
ATOM   5466  C13 VAL A 603       3.903 -14.773 114.583  1.00 66.98           C  
ANISOU 5466  C13 VAL A 603     9166   7025   9259   -591   -462    805       C  
ATOM   5467  C14 VAL A 603       2.835 -15.362 115.179  1.00 61.73           C  
ANISOU 5467  C14 VAL A 603     8451   6372   8631   -772   -490    855       C  
ATOM   5468  C15 VAL A 603      -2.540 -11.637 116.397  1.00 96.11           C  
ANISOU 5468  C15 VAL A 603    12118  11916  12485   -700   -749    630       C  
ATOM   5469  C2' VAL A 603       4.832 -13.189 112.719  1.00 59.85           C  
ANISOU 5469  C2' VAL A 603     8357   6122   8261   -357   -489    673       C  
ATOM   5470  C3' VAL A 603       5.359 -12.172 111.738  1.00 66.18           C  
ANISOU 5470  C3' VAL A 603     9213   6938   8996   -215   -477    614       C  
ATOM   5471  C4' VAL A 603       6.593 -11.899 112.559  1.00 62.30           C  
ANISOU 5471  C4' VAL A 603     8659   6504   8510   -124   -339    637       C  
ATOM   5472  C5  VAL A 603       4.788 -12.435 114.180  1.00 50.85           C  
ANISOU 5472  C5  VAL A 603     7127   5107   7085   -315   -508    769       C  
ATOM   5473  C5' VAL A 603       7.203 -10.604 112.129  1.00 68.90           C  
ANISOU 5473  C5' VAL A 603     9497   7389   9294      0   -284    604       C  
ATOM   5474  C6  VAL A 603      -0.989 -13.147 117.516  1.00 73.33           C  
ANISOU 5474  C6  VAL A 603     9422   8665   9774   -856   -629    830       C  
ATOM   5475  C7  VAL A 603       0.312 -13.051 116.763  1.00 61.27           C  
ANISOU 5475  C7  VAL A 603     8052   6931   8297   -742   -637    845       C  
ATOM   5476  C8  VAL A 603       0.866 -14.272 116.390  1.00 43.82           C  
ANISOU 5476  C8  VAL A 603     5946   4499   6205   -844   -586    865       C  
ATOM   5477  C9  VAL A 603       2.058 -14.298 115.682  1.00 57.15           C  
ANISOU 5477  C9  VAL A 603     7768   5993   7952   -748   -577    872       C  
ATOM   5478  N1  VAL A 603       3.849 -13.400 114.671  1.00 57.28           N  
ANISOU 5478  N1  VAL A 603     7913   5897   7955   -488   -548    823       N  
ATOM   5479  O1A VAL A 603       7.597  -8.156 110.162  1.00 69.99           O1-
ANISOU 5479  O1A VAL A 603     9685   7554   9353    211   -211    544       O1-
ATOM   5480  O1B VAL A 603       4.882 -11.120 108.500  1.00 61.63           O1-
ANISOU 5480  O1B VAL A 603     8899   6299   8218    -64   -605    454       O1-
ATOM   5481  O1G VAL A 603       6.848  -7.309 107.462  1.00 73.01           O  
ANISOU 5481  O1G VAL A 603    10311   7893   9537    368   -299    497       O  
ATOM   5482  O2A VAL A 603       6.062  -7.076 111.877  1.00110.98           O  
ANISOU 5482  O2A VAL A 603    14850  12858  14461    242   -349    617       O  
ATOM   5483  O2B VAL A 603       7.013  -9.878 108.321  1.00 73.26           O  
ANISOU 5483  O2B VAL A 603    10286   7816   9733    126   -325    468       O  
ATOM   5484  O2G VAL A 603       5.148  -7.686 105.744  1.00 61.27           O1-
ANISOU 5484  O2G VAL A 603     9128   6385   7765    491   -547    475       O1-
ATOM   5485  O3' VAL A 603       5.670 -12.627 110.391  1.00 70.58           O  
ANISOU 5485  O3' VAL A 603     9860   7397   9560   -217   -445    527       O  
ATOM   5486  O3A VAL A 603       5.174  -8.899 110.035  1.00 66.68           O  
ANISOU 5486  O3A VAL A 603     9399   7116   8819    145   -528    575       O  
ATOM   5487  O3B VAL A 603       4.959  -8.847 107.636  1.00 62.38           O  
ANISOU 5487  O3B VAL A 603     9082   6503   8117    253   -591    493       O  
ATOM   5488  O3G VAL A 603       4.544  -6.412 108.026  1.00 69.72           O  
ANISOU 5488  O3G VAL A 603     9953   7612   8926    523   -528    577       O  
ATOM   5489  O4' VAL A 603       6.217 -11.969 114.000  1.00 70.87           O  
ANISOU 5489  O4' VAL A 603     9675   7654   9598   -174   -385    721       O  
ATOM   5490  O5' VAL A 603       6.384  -9.444 112.208  1.00 87.39           O  
ANISOU 5490  O5' VAL A 603    11843   9792  11570     51   -372    621       O  
ATOM   5491  O8  VAL A 603      -1.835 -12.100 117.545  1.00 88.59           O  
ANISOU 5491  O8  VAL A 603    11230  10829  11600   -768   -676    764       O  
ATOM   5492  PA  VAL A 603       6.363  -8.320 111.010  1.00 91.03           P  
ANISOU 5492  PA  VAL A 603    12365  10255  11968    173   -352    584       P  
ATOM   5493  PB  VAL A 603       5.578  -9.755 108.728  1.00 66.90           P  
ANISOU 5493  PB  VAL A 603     9533   7034   8852    106   -511    503       P  
ATOM   5494  PG  VAL A 603       5.395  -7.436 107.208  1.00 61.60           P  
ANISOU 5494  PG  VAL A 603     8992   6464   7947    424   -483    515       P  
CONECT 2098 5460 5461                                                           
CONECT 2099 5460                                                                
CONECT 2103 5460                                                                
CONECT 2855 5461                                                                
CONECT 2863 5461                                                                
CONECT 2864 5461                                                                
CONECT 5446 5461                                                                
CONECT 5460 2098 2099 2103 5479                                                 
CONECT 5460 5481 5483                                                           
CONECT 5461 2098 2855 2863 2864                                                 
CONECT 5461 5446                                                                
CONECT 5462 5474                                                                
CONECT 5463 5464 5477 5478                                                      
CONECT 5464 5463 5465                                                           
CONECT 5465 5464 5475                                                           
CONECT 5466 5467 5478                                                           
CONECT 5467 5466 5477                                                           
CONECT 5468 5491                                                                
CONECT 5469 5470 5472                                                           
CONECT 5470 5469 5471 5485                                                      
CONECT 5471 5470 5473 5489                                                      
CONECT 5472 5469 5478 5489                                                      
CONECT 5473 5471 5490                                                           
CONECT 5474 5462 5475 5491                                                      
CONECT 5475 5465 5474 5476                                                      
CONECT 5476 5475 5477                                                           
CONECT 5477 5463 5467 5476                                                      
CONECT 5478 5463 5466 5472                                                      
CONECT 5479 5460 5492                                                           
CONECT 5480 5493                                                                
CONECT 5481 5460 5494                                                           
CONECT 5482 5492                                                                
CONECT 5483 5460 5493                                                           
CONECT 5484 5494                                                                
CONECT 5485 5470                                                                
CONECT 5486 5492 5493                                                           
CONECT 5487 5493 5494                                                           
CONECT 5488 5494                                                                
CONECT 5489 5471 5472                                                           
CONECT 5490 5473 5492                                                           
CONECT 5491 5468 5474                                                           
CONECT 5492 5479 5482 5486 5490                                                 
CONECT 5493 5480 5483 5486 5487                                                 
CONECT 5494 5481 5484 5487 5488                                                 
MASTER      333    0    3   26   16    0    8    6 5492    2   44   48          
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.