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***  HYDROLASE 12-JAN-16 5FT9  ***

elNémo ID: 2009011653371545

Job options:

ID        	=	 2009011653371545
JOBID     	=	 HYDROLASE 12-JAN-16 5FT9
USERID    	=	 unknown
PRIVAT    	=	 0

NMODES    	=	 5
DQMIN     	=	 -100
DQMAX     	=	 100
DQSTEP    	=	 10
DOGRAPHS  	=	 on

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


HEADER    HYDROLASE                               12-JAN-16   5FT9              
TITLE     ARABIDOPSIS THALIANA NUCLEAR PROTEIN-ONLY RNASE P 2 (PRORP2)          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEINACEOUS RNASE P 2;                                   
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: PROTEIN-ONLY RNASE P;                                       
COMPND   5 EC: 3.1.26.5;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;                           
SOURCE   3 ORGANISM_COMMON: THALE CRESS;                                        
SOURCE   4 ORGANISM_TAXID: 3702;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_VECTOR: PET-28B                                    
KEYWDS    HYDROLASE, PROTEINACEOUS RNASE P, PRORP, PPR, TRNA 5' MATURATION      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.FERNANDEZ-MILLAN,F.PINKER,C.SCHELCHER,A.GOBERT,P.GIEGE,C.SAUTER     
REVDAT   3   08-MAY-19 5FT9    1       REMARK                                   
REVDAT   2   06-MAR-19 5FT9    1       REMARK                                   
REVDAT   1   27-JAN-16 5FT9    0                                                
JRNL        AUTH   F.PINKER,C.SCHELCHER,P.FERNANDEZ-MILLAN,A.GOBERT,C.BIRCK,    
JRNL        AUTH 2 P.ROBLIN,P.GIEGE,C.SAUTER                                    
JRNL        TITL   STRUCTURES OF ARABIDOPSIS NUCLEAR RNASE P ALONE AND WITH     
JRNL        TITL 2 TRNA REVEAL PLASTICITIES                                     
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   F.PINKER,P.GIEGE,C.SAUTER                                    
REMARK   1  TITL   CRYSTALLIZATION AND CRYSTALLOGRAPHIC ANALYSIS OF AN          
REMARK   1  TITL 2 ARABIDOPSIS NUCLEAR PROTEINACEOUS RNASE P.                   
REMARK   1  REF    ACTA CRYSTALLOGR.,SECT.F      V.  71  1372 2015              
REMARK   1  REFN                   ESSN 2053-230X                               
REMARK   1  PMID   26527263                                                     
REMARK   1  DOI    10.1107/S2053230X15017033                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.05 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
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) : 3.05                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 34.71                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.910                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 92.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 23727                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.244                           
REMARK   3   R VALUE            (WORKING SET) : 0.242                           
REMARK   3   FREE R VALUE                     : 0.290                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1126                            
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 34.7095 -  6.0904    0.99     3012   168  0.1668 0.1985        
REMARK   3     2  6.0904 -  4.8383    0.99     3028   156  0.2126 0.2811        
REMARK   3     3  4.8383 -  4.2280    0.99     3025   148  0.1999 0.2637        
REMARK   3     4  4.2280 -  3.8419    0.79     2428   119  0.2740 0.3141        
REMARK   3     5  3.8419 -  3.5669    0.70     2168   102  0.3538 0.4782        
REMARK   3     6  3.5669 -  3.3567    0.95     2888   131  0.4158 0.4797        
REMARK   3     7  3.3567 -  3.1888    0.98     3047   145  0.3954 0.4433        
REMARK   3     8  3.1888 -  3.0500    0.98     3005   157  0.4094 0.4457        
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)     : 0.690            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 43.310           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 93.61                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 145.9                          
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           7598                                  
REMARK   3   ANGLE     :  1.148          10274                                  
REMARK   3   CHIRALITY :  0.051           1125                                  
REMARK   3   PLANARITY :  0.004           1315                                  
REMARK   3   DIHEDRAL  : 15.092           2746                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN A AND ((RESID 28 THROUGH 289 ) OR (RESID 479     
REMARK   3               THROUGH 515))                                          
REMARK   3    ORIGIN FOR THE GROUP (A):  34.2199  39.8225  26.0876              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0999 T22:   0.7343                                     
REMARK   3      T33:   0.4303 T12:   0.1057                                     
REMARK   3      T13:  -0.1202 T23:  -0.1135                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.5537 L22:   4.6760                                     
REMARK   3      L33:   3.1598 L12:   2.6632                                     
REMARK   3      L13:   0.6827 L23:  -0.1232                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0713 S12:  -0.1049 S13:   0.4066                       
REMARK   3      S21:   0.3065 S22:  -0.2930 S23:   0.1743                       
REMARK   3      S31:  -0.4557 S32:  -0.2954 S33:   0.1425                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN A AND (RESID 290 THROUGH 478 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  18.4925  17.6401  -4.9482              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.6104 T22:   1.0313                                     
REMARK   3      T33:   0.7716 T12:  -0.1727                                     
REMARK   3      T13:  -0.1610 T23:  -0.2309                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2870 L22:   3.8806                                     
REMARK   3      L33:   8.3254 L12:  -1.1105                                     
REMARK   3      L13:  -0.3694 L23:   1.6928                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3577 S12:  -0.4268 S13:   0.3445                       
REMARK   3      S21:   1.2752 S22:   0.0352 S23:  -0.1550                       
REMARK   3      S31:  -0.4312 S32:  -0.6640 S33:   0.2921                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN B AND ((RESID 28 THROUGH 289 ) OR (RESID 479     
REMARK   3               THROUGH 515))                                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.3585  33.4526  38.1753              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0939 T22:   0.8843                                     
REMARK   3      T33:   0.4747 T12:  -0.3491                                     
REMARK   3      T13:  -0.1304 T23:   0.1619                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3748 L22:   7.1738                                     
REMARK   3      L33:   2.2869 L12:  -1.2136                                     
REMARK   3      L13:   0.4914 L23:   0.5539                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0582 S12:  -0.0304 S13:   0.1801                       
REMARK   3      S21:   0.1350 S22:  -0.2218 S23:  -0.4716                       
REMARK   3      S31:   0.0193 S32:   0.0634 S33:   0.1432                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN A                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  -0.6380   6.7317  69.1332              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.6613 T22:   1.2112                                     
REMARK   3      T33:   0.7761 T12:  -0.4630                                     
REMARK   3      T13:  -0.0602 T23:   0.2521                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.6389 L22:   2.2017                                     
REMARK   3      L33:   4.8473 L12:   0.1983                                     
REMARK   3      L13:   0.5209 L23:   0.1745                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2293 S12:   0.4869 S13:   0.5213                       
REMARK   3      S21:  -0.6499 S22:   0.1751 S23:  -0.0050                       
REMARK   3      S31:   0.0884 S32:   0.7820 S33:   0.0566                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : 2                                           
REMARK   3   NCS GROUP : 1                                                      
REMARK   3   NCS GROUP : 2                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: NULL                                        
REMARK   3     SELECTION          : NULL                                        
REMARK   3     ATOM PAIRS NUMBER  : NULL                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5FT9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-JAN-16.                  
REMARK 100 THE DEPOSITION ID IS D_1290065971.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 23-FEB-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X06DA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 2M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 23923                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.050                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 35.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 92.4                               
REMARK 200  DATA REDUNDANCY                : 3.500                              
REMARK 200  R MERGE                    (I) : 0.12000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 8.7000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.05                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.23                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.50000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 0.800                              
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 4G26                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.40                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.90                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PRORP2 STOCK SOLUTION WAS PREPARED AT    
REMARK 280  2.5 MG/ML IN 50 MM HEPES-NA PH 7.5, 250 MM NACL, 5%(W/V)            
REMARK 280  GLYCEROL, 1 MM TCEP. PRORP2 WAS CRYSTALLIZED AT 277 K IN 2          
REMARK 280  MICROLITER MICROBATCH DROPS SET UP UNDER PARAFIN OIL BY MIXING 1    
REMARK 280  VOLUME OF PRORP2 SOLUTION WITH 1 VOLUME OF CRYSTALLANT SOLUTION     
REMARK 280  CONTAINING 200 MM SODIUM MALONATE PH 6, 20% (W/V) PEG 3350.         
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,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                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     0                                                      
REMARK 465     GLY A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     ALA A     3                                                      
REMARK 465     SER A     4                                                      
REMARK 465     ASP A     5                                                      
REMARK 465     GLN A     6                                                      
REMARK 465     HIS A     7                                                      
REMARK 465     ARG A     8                                                      
REMARK 465     SER A     9                                                      
REMARK 465     ARG A    10                                                      
REMARK 465     ARG A    11                                                      
REMARK 465     HIS A    12                                                      
REMARK 465     ASP A    13                                                      
REMARK 465     GLU A    14                                                      
REMARK 465     SER A    15                                                      
REMARK 465     SER A    16                                                      
REMARK 465     SER A    17                                                      
REMARK 465     ARG A    18                                                      
REMARK 465     PRO A    19                                                      
REMARK 465     ASN A    20                                                      
REMARK 465     LYS A    21                                                      
REMARK 465     LYS A    22                                                      
REMARK 465     LYS A    23                                                      
REMARK 465     LYS A    24                                                      
REMARK 465     VAL A    25                                                      
REMARK 465     SER A    26                                                      
REMARK 465     ARG A    27                                                      
REMARK 465     ARG A   312                                                      
REMARK 465     LYS A   313                                                      
REMARK 465     THR A   314                                                      
REMARK 465     LYS A   315                                                      
REMARK 465     MET A   316                                                      
REMARK 465     ASN A   317                                                      
REMARK 465     SER A   318                                                      
REMARK 465     CYS A   319                                                      
REMARK 465     GLU A   320                                                      
REMARK 465     THR A   321                                                      
REMARK 465     CYS A   499                                                      
REMARK 465     GLU A   500                                                      
REMARK 465     ASN A   501                                                      
REMARK 465     ASN A   502                                                      
REMARK 465     GLU A   503                                                      
REMARK 465     GLU A   504                                                      
REMARK 465     SER A   516                                                      
REMARK 465     ILE A   517                                                      
REMARK 465     LEU A   518                                                      
REMARK 465     ASP A   519                                                      
REMARK 465     SER A   520                                                      
REMARK 465     PRO A   521                                                      
REMARK 465     LYS A   522                                                      
REMARK 465     SER A   523                                                      
REMARK 465     ASN A   524                                                      
REMARK 465     GLY A   525                                                      
REMARK 465     LYS A   526                                                      
REMARK 465     ILE A   527                                                      
REMARK 465     PRO A   528                                                      
REMARK 465     LEU A   529                                                      
REMARK 465     GLU A   530                                                      
REMARK 465     HIS A   531                                                      
REMARK 465     HIS A   532                                                      
REMARK 465     HIS A   533                                                      
REMARK 465     HIS A   534                                                      
REMARK 465     HIS A   535                                                      
REMARK 465     HIS A   536                                                      
REMARK 465     MET B     0                                                      
REMARK 465     GLY B     1                                                      
REMARK 465     ALA B     2                                                      
REMARK 465     ALA B     3                                                      
REMARK 465     SER B     4                                                      
REMARK 465     ASP B     5                                                      
REMARK 465     GLN B     6                                                      
REMARK 465     HIS B     7                                                      
REMARK 465     ARG B     8                                                      
REMARK 465     SER B     9                                                      
REMARK 465     ARG B    10                                                      
REMARK 465     ARG B    11                                                      
REMARK 465     HIS B    12                                                      
REMARK 465     ASP B    13                                                      
REMARK 465     GLU B    14                                                      
REMARK 465     SER B    15                                                      
REMARK 465     SER B    16                                                      
REMARK 465     SER B    17                                                      
REMARK 465     ARG B    18                                                      
REMARK 465     PRO B    19                                                      
REMARK 465     ASN B    20                                                      
REMARK 465     LYS B    21                                                      
REMARK 465     LYS B    22                                                      
REMARK 465     LYS B    23                                                      
REMARK 465     LYS B    24                                                      
REMARK 465     VAL B    25                                                      
REMARK 465     SER B    26                                                      
REMARK 465     ARG B    27                                                      
REMARK 465     ARG B   312                                                      
REMARK 465     LYS B   313                                                      
REMARK 465     THR B   314                                                      
REMARK 465     LYS B   315                                                      
REMARK 465     MET B   316                                                      
REMARK 465     ASN B   317                                                      
REMARK 465     SER B   318                                                      
REMARK 465     CYS B   319                                                      
REMARK 465     GLU B   320                                                      
REMARK 465     THR B   321                                                      
REMARK 465     GLU B   500                                                      
REMARK 465     ASN B   501                                                      
REMARK 465     ASN B   502                                                      
REMARK 465     GLU B   503                                                      
REMARK 465     GLU B   504                                                      
REMARK 465     SER B   516                                                      
REMARK 465     ILE B   517                                                      
REMARK 465     LEU B   518                                                      
REMARK 465     ASP B   519                                                      
REMARK 465     SER B   520                                                      
REMARK 465     PRO B   521                                                      
REMARK 465     LYS B   522                                                      
REMARK 465     SER B   523                                                      
REMARK 465     ASN B   524                                                      
REMARK 465     GLY B   525                                                      
REMARK 465     LYS B   526                                                      
REMARK 465     ILE B   527                                                      
REMARK 465     PRO B   528                                                      
REMARK 465     LEU B   529                                                      
REMARK 465     GLU B   530                                                      
REMARK 465     HIS B   531                                                      
REMARK 465     HIS B   532                                                      
REMARK 465     HIS B   533                                                      
REMARK 465     HIS B   534                                                      
REMARK 465     HIS B   535                                                      
REMARK 465     HIS B   536                                                      
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  70   N   -  CA  -  C   ANGL. DEV. = -16.6 DEGREES          
REMARK 500    MET A 100   CB  -  CA  -  C   ANGL. DEV. = -13.9 DEGREES          
REMARK 500    VAL A 101   N   -  CA  -  CB  ANGL. DEV. =  13.5 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    ILE A 239     -126.22     43.52                                   
REMARK 500    ASN A 420     -161.25   -167.54                                   
REMARK 500    SER A 452     -141.51   -137.17                                   
REMARK 500    ARG A 514     -155.86   -111.19                                   
REMARK 500    SER B  60      -19.97     72.01                                   
REMARK 500    SER B  84       -5.42     73.03                                   
REMARK 500    ASP B 236     -119.72     41.48                                   
REMARK 500    GLN B 351       10.51     53.15                                   
REMARK 500    ASN B 377     -127.83     47.90                                   
REMARK 500    ASN B 378       49.57   -106.25                                   
REMARK 500    SER B 452      -65.69   -133.15                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 VAL A  355     ASP A  356                   32.92                    
REMARK 500 ASP A  421     ASP A  422                 -148.39                    
REMARK 500 GLY A  491     SER A  492                  -35.43                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 600                                                                      
REMARK 600 HETEROGEN                                                            
REMARK 600                                                                      
REMARK 600 ZINC ION (ZN): STRUCTURAL ZINC DOMAIN                                
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                              ZN A1001  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 284   SG                                                     
REMARK 620 2 CYS A 511   SG   97.6                                              
REMARK 620 3 HIS A 494   NE2 101.7 102.1                                        
REMARK 620 4 CYS A 281   SG  121.9 116.7 113.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B1001  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 281   SG                                                     
REMARK 620 2 CYS B 511   SG  104.9                                              
REMARK 620 3 HIS B 494   NE2 107.5  98.2                                        
REMARK 620 4 CYS B 284   SG  130.3 109.7 101.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 1001                 
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 ADDITION OF A GLY IN SECOND POSITION AND LEHHHHHH C-                 
REMARK 999 TERMINAL TAG FOR AFFINITY PURIFICATION                               
DBREF  5FT9 A    2   528  UNP    Q680B9   PRRP2_ARATH      2    528             
DBREF  5FT9 B    2   528  UNP    Q680B9   PRRP2_ARATH      2    528             
SEQADV 5FT9 MET A    0  UNP  Q680B9              EXPRESSION TAG                 
SEQADV 5FT9 GLY A    1  UNP  Q680B9              EXPRESSION TAG                 
SEQADV 5FT9 LEU A  529  UNP  Q680B9              EXPRESSION TAG                 
SEQADV 5FT9 GLU A  530  UNP  Q680B9              EXPRESSION TAG                 
SEQADV 5FT9 HIS A  531  UNP  Q680B9              EXPRESSION TAG                 
SEQADV 5FT9 HIS A  532  UNP  Q680B9              EXPRESSION TAG                 
SEQADV 5FT9 HIS A  533  UNP  Q680B9              EXPRESSION TAG                 
SEQADV 5FT9 HIS A  534  UNP  Q680B9              EXPRESSION TAG                 
SEQADV 5FT9 HIS A  535  UNP  Q680B9              EXPRESSION TAG                 
SEQADV 5FT9 HIS A  536  UNP  Q680B9              EXPRESSION TAG                 
SEQADV 5FT9 MET B    0  UNP  Q680B9              EXPRESSION TAG                 
SEQADV 5FT9 GLY B    1  UNP  Q680B9              EXPRESSION TAG                 
SEQADV 5FT9 LEU B  529  UNP  Q680B9              EXPRESSION TAG                 
SEQADV 5FT9 GLU B  530  UNP  Q680B9              EXPRESSION TAG                 
SEQADV 5FT9 HIS B  531  UNP  Q680B9              EXPRESSION TAG                 
SEQADV 5FT9 HIS B  532  UNP  Q680B9              EXPRESSION TAG                 
SEQADV 5FT9 HIS B  533  UNP  Q680B9              EXPRESSION TAG                 
SEQADV 5FT9 HIS B  534  UNP  Q680B9              EXPRESSION TAG                 
SEQADV 5FT9 HIS B  535  UNP  Q680B9              EXPRESSION TAG                 
SEQADV 5FT9 HIS B  536  UNP  Q680B9              EXPRESSION TAG                 
SEQRES   1 A  537  MET GLY ALA ALA SER ASP GLN HIS ARG SER ARG ARG HIS          
SEQRES   2 A  537  ASP GLU SER SER SER ARG PRO ASN LYS LYS LYS LYS VAL          
SEQRES   3 A  537  SER ARG ASN PRO GLU THR ASN LEU LEU PHE ASN LEU ASN          
SEQRES   4 A  537  SER CYS SER LYS SER LYS ASP LEU SER ALA ALA LEU ALA          
SEQRES   5 A  537  LEU TYR ASP ALA ALA ILE THR SER SER GLU VAL ARG LEU          
SEQRES   6 A  537  SER GLN GLN HIS PHE GLN THR LEU LEU TYR LEU CYS SER          
SEQRES   7 A  537  ALA SER ILE THR ASP ILE SER LEU GLN TYR LEU ALA ILE          
SEQRES   8 A  537  ASP ARG GLY PHE GLU ILE PHE ASP ARG MET VAL SER SER          
SEQRES   9 A  537  GLY ILE SER PRO ASN GLU ALA SER VAL THR SER VAL ALA          
SEQRES  10 A  537  ARG LEU ALA ALA ALA LYS GLY ASN GLY ASP TYR ALA PHE          
SEQRES  11 A  537  LYS VAL VAL LYS GLU PHE VAL SER VAL GLY GLY VAL SER          
SEQRES  12 A  537  ILE PRO ARG LEU ARG THR TYR ALA PRO ALA LEU LEU CYS          
SEQRES  13 A  537  PHE CYS GLU LYS LEU GLU ALA GLU LYS GLY TYR GLU VAL          
SEQRES  14 A  537  GLU GLU HIS MET GLU ALA ALA GLY ILE ALA LEU GLU GLU          
SEQRES  15 A  537  ALA GLU ILE SER ALA LEU LEU LYS VAL SER ALA ALA THR          
SEQRES  16 A  537  GLY ARG GLU ASN LYS VAL TYR ARG TYR LEU HIS LYS LEU          
SEQRES  17 A  537  ARG GLU TYR VAL GLY CYS VAL SER GLU GLU THR LEU LYS          
SEQRES  18 A  537  ILE ILE GLU GLU TRP PHE CYS GLY GLU LYS ALA GLY GLU          
SEQRES  19 A  537  VAL GLY ASP ASN GLY ILE GLY SER ASP VAL GLY MET LEU          
SEQRES  20 A  537  ARG GLU ALA VAL LEU ASN ASN GLY GLY GLY TRP HIS GLY          
SEQRES  21 A  537  HIS GLY TRP VAL GLY GLU GLY LYS TRP THR VAL LYS LYS          
SEQRES  22 A  537  GLY ASN VAL SER SER THR GLY ARG CYS LEU SER CYS SER          
SEQRES  23 A  537  GLU GLN LEU ALA CYS VAL ASP THR ASN GLU VAL GLU THR          
SEQRES  24 A  537  GLN LYS PHE VAL ASP SER LEU VAL ALA LEU ALA MET ASP          
SEQRES  25 A  537  ARG LYS THR LYS MET ASN SER CYS GLU THR ASN VAL VAL          
SEQRES  26 A  537  PHE SER GLU PHE GLN ASP TRP LEU GLU LYS HIS GLY ASP          
SEQRES  27 A  537  TYR GLU ALA ILE VAL ASP GLY ALA ASN ILE GLY LEU TYR          
SEQRES  28 A  537  GLN GLN ASN PHE VAL ASP GLY SER PHE SER LEU SER GLN          
SEQRES  29 A  537  LEU GLU SER VAL MET LYS GLU LEU TYR ARG GLU SER GLY          
SEQRES  30 A  537  ASN ASN LYS TRP PRO LEU ILE LEU LEU HIS LYS ARG ARG          
SEQRES  31 A  537  VAL LYS THR LEU LEU GLU ASN PRO THR HIS ARG ASN LEU          
SEQRES  32 A  537  VAL GLU GLU TRP ILE SER ASN GLY VAL LEU TYR ALA THR          
SEQRES  33 A  537  PRO PRO GLY SER ASN ASP ASP TRP TYR TRP LEU TYR ALA          
SEQRES  34 A  537  ALA ALA LYS LEU LYS CYS LEU LEU VAL THR ASN ASP GLU          
SEQRES  35 A  537  MET ARG ASP HIS ILE PHE GLU LEU LEU GLY SER THR PHE          
SEQRES  36 A  537  PHE GLN LYS TRP LYS GLU ARG HIS GLN VAL ARG TYR THR          
SEQRES  37 A  537  PHE VAL LYS GLY ASN LEU LYS LEU GLU MET PRO SER PRO          
SEQRES  38 A  537  PHE SER VAL VAL ILE GLN GLU SER GLU LYS GLY SER TRP          
SEQRES  39 A  537  HIS PHE PRO VAL SER CYS GLU ASN ASN GLU GLU SER SER          
SEQRES  40 A  537  ARG THR TRP MET CYS ILE SER ARG GLN SER ILE LEU ASP          
SEQRES  41 A  537  SER PRO LYS SER ASN GLY LYS ILE PRO LEU GLU HIS HIS          
SEQRES  42 A  537  HIS HIS HIS HIS                                              
SEQRES   1 B  537  MET GLY ALA ALA SER ASP GLN HIS ARG SER ARG ARG HIS          
SEQRES   2 B  537  ASP GLU SER SER SER ARG PRO ASN LYS LYS LYS LYS VAL          
SEQRES   3 B  537  SER ARG ASN PRO GLU THR ASN LEU LEU PHE ASN LEU ASN          
SEQRES   4 B  537  SER CYS SER LYS SER LYS ASP LEU SER ALA ALA LEU ALA          
SEQRES   5 B  537  LEU TYR ASP ALA ALA ILE THR SER SER GLU VAL ARG LEU          
SEQRES   6 B  537  SER GLN GLN HIS PHE GLN THR LEU LEU TYR LEU CYS SER          
SEQRES   7 B  537  ALA SER ILE THR ASP ILE SER LEU GLN TYR LEU ALA ILE          
SEQRES   8 B  537  ASP ARG GLY PHE GLU ILE PHE ASP ARG MET VAL SER SER          
SEQRES   9 B  537  GLY ILE SER PRO ASN GLU ALA SER VAL THR SER VAL ALA          
SEQRES  10 B  537  ARG LEU ALA ALA ALA LYS GLY ASN GLY ASP TYR ALA PHE          
SEQRES  11 B  537  LYS VAL VAL LYS GLU PHE VAL SER VAL GLY GLY VAL SER          
SEQRES  12 B  537  ILE PRO ARG LEU ARG THR TYR ALA PRO ALA LEU LEU CYS          
SEQRES  13 B  537  PHE CYS GLU LYS LEU GLU ALA GLU LYS GLY TYR GLU VAL          
SEQRES  14 B  537  GLU GLU HIS MET GLU ALA ALA GLY ILE ALA LEU GLU GLU          
SEQRES  15 B  537  ALA GLU ILE SER ALA LEU LEU LYS VAL SER ALA ALA THR          
SEQRES  16 B  537  GLY ARG GLU ASN LYS VAL TYR ARG TYR LEU HIS LYS LEU          
SEQRES  17 B  537  ARG GLU TYR VAL GLY CYS VAL SER GLU GLU THR LEU LYS          
SEQRES  18 B  537  ILE ILE GLU GLU TRP PHE CYS GLY GLU LYS ALA GLY GLU          
SEQRES  19 B  537  VAL GLY ASP ASN GLY ILE GLY SER ASP VAL GLY MET LEU          
SEQRES  20 B  537  ARG GLU ALA VAL LEU ASN ASN GLY GLY GLY TRP HIS GLY          
SEQRES  21 B  537  HIS GLY TRP VAL GLY GLU GLY LYS TRP THR VAL LYS LYS          
SEQRES  22 B  537  GLY ASN VAL SER SER THR GLY ARG CYS LEU SER CYS SER          
SEQRES  23 B  537  GLU GLN LEU ALA CYS VAL ASP THR ASN GLU VAL GLU THR          
SEQRES  24 B  537  GLN LYS PHE VAL ASP SER LEU VAL ALA LEU ALA MET ASP          
SEQRES  25 B  537  ARG LYS THR LYS MET ASN SER CYS GLU THR ASN VAL VAL          
SEQRES  26 B  537  PHE SER GLU PHE GLN ASP TRP LEU GLU LYS HIS GLY ASP          
SEQRES  27 B  537  TYR GLU ALA ILE VAL ASP GLY ALA ASN ILE GLY LEU TYR          
SEQRES  28 B  537  GLN GLN ASN PHE VAL ASP GLY SER PHE SER LEU SER GLN          
SEQRES  29 B  537  LEU GLU SER VAL MET LYS GLU LEU TYR ARG GLU SER GLY          
SEQRES  30 B  537  ASN ASN LYS TRP PRO LEU ILE LEU LEU HIS LYS ARG ARG          
SEQRES  31 B  537  VAL LYS THR LEU LEU GLU ASN PRO THR HIS ARG ASN LEU          
SEQRES  32 B  537  VAL GLU GLU TRP ILE SER ASN GLY VAL LEU TYR ALA THR          
SEQRES  33 B  537  PRO PRO GLY SER ASN ASP ASP TRP TYR TRP LEU TYR ALA          
SEQRES  34 B  537  ALA ALA LYS LEU LYS CYS LEU LEU VAL THR ASN ASP GLU          
SEQRES  35 B  537  MET ARG ASP HIS ILE PHE GLU LEU LEU GLY SER THR PHE          
SEQRES  36 B  537  PHE GLN LYS TRP LYS GLU ARG HIS GLN VAL ARG TYR THR          
SEQRES  37 B  537  PHE VAL LYS GLY ASN LEU LYS LEU GLU MET PRO SER PRO          
SEQRES  38 B  537  PHE SER VAL VAL ILE GLN GLU SER GLU LYS GLY SER TRP          
SEQRES  39 B  537  HIS PHE PRO VAL SER CYS GLU ASN ASN GLU GLU SER SER          
SEQRES  40 B  537  ARG THR TRP MET CYS ILE SER ARG GLN SER ILE LEU ASP          
SEQRES  41 B  537  SER PRO LYS SER ASN GLY LYS ILE PRO LEU GLU HIS HIS          
SEQRES  42 B  537  HIS HIS HIS HIS                                              
HET     ZN  A1001       1                                                       
HET     ZN  B1001       1                                                       
HETNAM      ZN ZINC ION                                                         
FORMUL   3   ZN    2(ZN 2+)                                                     
HELIX    1   1 ASN A   28  LYS A   44  1                                  17    
HELIX    2   2 ASP A   45  SER A   60  1                                  16    
HELIX    3   3 GLN A   66  ASP A   82  1                                  17    
HELIX    4   4 LEU A   85  SER A  102  1                                  18    
HELIX    5   5 ASN A  108  LYS A  122  1                                  15    
HELIX    6   6 ASN A  124  GLY A  139  1                                  16    
HELIX    7   7 ARG A  145  LYS A  159  1                                  15    
HELIX    8   8 GLU A  161  GLY A  176  1                                  16    
HELIX    9   9 GLU A  180  THR A  194  1                                  15    
HELIX   10  10 ARG A  196  VAL A  211  1                                  16    
HELIX   11  11 SER A  215  CYS A  227  1                                  13    
HELIX   12  12 GLY A  228  GLY A  235  1                                   8    
HELIX   13  13 ASP A  242  ASN A  253  1                                  12    
HELIX   14  14 ASN A  294  ASP A  311  1                                  18    
HELIX   15  15 ASN A  322  GLY A  336  1                                  15    
HELIX   16  16 GLY A  344  TYR A  350  1                                   7    
HELIX   17  17 SER A  360  GLY A  376  1                                  17    
HELIX   18  18 LYS A  387  ASN A  396  1                                  10    
HELIX   19  19 ASN A  396  GLY A  410  1                                  15    
HELIX   20  20 ASP A  422  LEU A  432  1                                  11    
HELIX   21  21 ASP A  444  GLY A  451  1                                   8    
HELIX   22  22 SER A  452  HIS A  462  1                                  11    
HELIX   23  23 ASN B   28  LYS B   44  1                                  17    
HELIX   24  24 ASP B   45  SER B   60  1                                  16    
HELIX   25  25 SER B   65  ASP B   82  1                                  18    
HELIX   26  26 LEU B   85  SER B  103  1                                  19    
HELIX   27  27 ASN B  108  LYS B  122  1                                  15    
HELIX   28  28 ASN B  124  GLY B  139  1                                  16    
HELIX   29  29 ARG B  145  LYS B  159  1                                  15    
HELIX   30  30 GLU B  161  ALA B  175  1                                  15    
HELIX   31  31 GLU B  180  THR B  194  1                                  15    
HELIX   32  32 ARG B  196  VAL B  211  1                                  16    
HELIX   33  33 SER B  215  CYS B  227  1                                  13    
HELIX   34  34 GLY B  228  GLY B  235  1                                   8    
HELIX   35  35 ASP B  242  ASN B  253  1                                  12    
HELIX   36  36 ASN B  294  ASP B  311  1                                  18    
HELIX   37  37 ASN B  322  HIS B  335  1                                  14    
HELIX   38  38 GLY B  344  TYR B  350  1                                   7    
HELIX   39  39 SER B  360  GLY B  376  1                                  17    
HELIX   40  40 LYS B  387  ASN B  396  1                                  10    
HELIX   41  41 ASN B  396  GLY B  410  1                                  15    
HELIX   42  42 TRP B  423  LYS B  433  1                                  11    
HELIX   43  43 ASP B  444  GLY B  451  1                                   8    
HELIX   44  44 SER B  452  HIS B  462  1                                  11    
SHEET    1  AA 4 THR A 269  GLY A 273  0                                        
SHEET    2  AA 4 TRP A 509  SER A 513 -1  O  TRP A 509   N  GLY A 273           
SHEET    3  AA 4 TRP A 493  PRO A 496 -1  O  TRP A 493   N  ILE A 512           
SHEET    4  AA 4 GLN A 486  GLU A 487 -1  O  GLN A 486   N  HIS A 494           
SHEET    1  AB 6 LEU A 412  THR A 415  0                                        
SHEET    2  AB 6 LEU A 382  HIS A 386  1  O  ILE A 383   N  TYR A 413           
SHEET    3  AB 6 ALA A 340  ASP A 343  1  O  ALA A 340   N  LEU A 382           
SHEET    4  AB 6 LEU A 435  VAL A 437  1  O  LEU A 435   N  ILE A 341           
SHEET    5  AB 6 GLN A 463  THR A 467  1  N  VAL A 464   O  LEU A 436           
SHEET    6  AB 6 LYS A 474  GLU A 476 -1  O  LYS A 474   N  THR A 467           
SHEET    1  BA 4 TRP B 268  GLY B 273  0                                        
SHEET    2  BA 4 TRP B 509  ARG B 514 -1  O  TRP B 509   N  GLY B 273           
SHEET    3  BA 4 TRP B 493  PRO B 496 -1  O  TRP B 493   N  ILE B 512           
SHEET    4  BA 4 GLN B 486  GLU B 487 -1  O  GLN B 486   N  HIS B 494           
SHEET    1  BB 2 ARG B 280  CYS B 281  0                                        
SHEET    2  BB 2 GLU B 286  GLN B 287 -1  O  GLU B 286   N  CYS B 281           
SHEET    1  BC 6 LEU B 412  THR B 415  0                                        
SHEET    2  BC 6 LEU B 382  HIS B 386  1  O  ILE B 383   N  TYR B 413           
SHEET    3  BC 6 ALA B 340  ASP B 343  1  O  ALA B 340   N  LEU B 382           
SHEET    4  BC 6 LEU B 435  VAL B 437  1  O  LEU B 435   N  ILE B 341           
SHEET    5  BC 6 GLN B 463  VAL B 469  1  N  VAL B 464   O  LEU B 436           
SHEET    6  BC 6 ASN B 472  GLU B 476 -1  O  ASN B 472   N  VAL B 469           
LINK        ZN    ZN A1001                 SG  CYS A 284     1555   1555  2.36  
LINK        ZN    ZN A1001                 SG  CYS A 511     1555   1555  2.49  
LINK        ZN    ZN A1001                 NE2 HIS A 494     1555   1555  2.27  
LINK        ZN    ZN A1001                 SG  CYS A 281     1555   1555  2.42  
LINK        ZN    ZN B1001                 SG  CYS B 281     1555   1555  2.80  
LINK        ZN    ZN B1001                 SG  CYS B 511     1555   1555  2.31  
LINK        ZN    ZN B1001                 NE2 HIS B 494     1555   1555  2.29  
LINK        ZN    ZN B1001                 SG  CYS B 284     1555   1555  2.22  
CISPEP   1 SER A   60    GLU A   61          0       -15.65                     
CISPEP   2 ALA A  175    GLY A  176          0         1.18                     
CISPEP   3 GLY A  238    ILE A  239          0        -3.52                     
CISPEP   4 SER A  241    ASP A  242          0         0.91                     
CISPEP   5 GLY A  336    ASP A  337          0         3.18                     
CISPEP   6 TYR A  350    GLN A  351          0        -0.36                     
CISPEP   7 SER A  358    PHE A  359          0        14.15                     
CISPEP   8 SER A  419    ASN A  420          0        -8.78                     
CISPEP   9 GLY B  123    ASN B  124          0         6.47                     
CISPEP  10 ASN B  237    GLY B  238          0        -7.88                     
CISPEP  11 ILE B  239    GLY B  240          0         5.56                     
CISPEP  12 GLY B  240    SER B  241          0         4.32                     
CISPEP  13 GLY B  336    ASP B  337          0         4.86                     
CISPEP  14 SER B  419    ASN B  420          0       -10.39                     
CISPEP  15 LYS B  470    GLY B  471          0        11.49                     
SITE     1 AC1  5 CYS A 281  SER A 283  CYS A 284  HIS A 494                    
SITE     2 AC1  5 CYS A 511                                                     
SITE     1 AC2  4 CYS B 281  CYS B 284  HIS B 494  CYS B 511                    
CRYST1   70.500   72.800   80.300  63.10  72.20  78.40 P 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      0.014184 -0.002912 -0.003672        0.00000                         
SCALE2      0.000000  0.014023 -0.006474        0.00000                         
SCALE3      0.000000  0.000000  0.014406        0.00000                         
MTRIX1   1 -0.913800  0.406200  0.007688       14.62000    1                    
MTRIX2   1  0.406200  0.913800 -0.005994       12.05000    1                    
MTRIX3   1 -0.009460 -0.002355 -1.000000       64.25000    1                    
ATOM      1  N   ASN A  28      53.375  71.856   1.496  1.00225.35           N  
ANISOU    1  N   ASN A  28    36251  25242  24129  -8381  -5314   8582       N  
ATOM      2  CA  ASN A  28      52.631  72.160   2.712  1.00226.20           C  
ANISOU    2  CA  ASN A  28    36421  24725  24799  -7820  -5578   8388       C  
ATOM      3  C   ASN A  28      53.283  71.468   3.906  1.00222.60           C  
ANISOU    3  C   ASN A  28    35799  24328  24450  -7671  -5261   8007       C  
ATOM      4  O   ASN A  28      53.539  70.266   3.865  1.00228.85           O  
ANISOU    4  O   ASN A  28    36391  25632  24930  -7657  -4871   7787       O  
ATOM      5  CB  ASN A  28      51.163  71.734   2.559  1.00227.27           C  
ANISOU    5  CB  ASN A  28    36572  24759  25021  -7316  -5767   8322       C  
ATOM      6  CG  ASN A  28      50.298  72.128   3.753  1.00224.16           C  
ANISOU    6  CG  ASN A  28    36239  23701  25230  -6727  -6041   8119       C  
ATOM      7  OD1 ASN A  28      50.656  71.899   4.908  1.00226.50           O  
ANISOU    7  OD1 ASN A  28    36482  23835  25743  -6534  -5897   7810       O  
ATOM      8  ND2 ASN A  28      49.147  72.727   3.471  1.00221.98           N  
ANISOU    8  ND2 ASN A  28    36068  23041  25234  -6448  -6437   8285       N  
ATOM      9  N   PRO A  29      53.569  72.236   4.971  1.00203.63           N  
ANISOU    9  N   PRO A  29    33482  21396  22493  -7577  -5437   7924       N  
ATOM     10  CA  PRO A  29      54.205  71.726   6.195  1.00187.84           C  
ANISOU   10  CA  PRO A  29    31350  19379  20639  -7469  -5208   7583       C  
ATOM     11  C   PRO A  29      53.364  70.670   6.914  1.00175.44           C  
ANISOU   11  C   PRO A  29    29694  17823  19142  -6912  -5102   7223       C  
ATOM     12  O   PRO A  29      53.911  69.683   7.407  1.00172.02           O  
ANISOU   12  O   PRO A  29    29072  17727  18561  -6911  -4769   6982       O  
ATOM     13  CB  PRO A  29      54.351  72.980   7.064  1.00197.41           C  
ANISOU   13  CB  PRO A  29    32749  19910  22346  -7441  -5534   7589       C  
ATOM     14  CG  PRO A  29      54.311  74.122   6.099  1.00201.12           C  
ANISOU   14  CG  PRO A  29    33398  20203  22815  -7747  -5825   8005       C  
ATOM     15  CD  PRO A  29      53.363  73.693   5.026  1.00200.61           C  
ANISOU   15  CD  PRO A  29    33335  20397  22491  -7621  -5873   8165       C  
ATOM     16  N   GLU A  30      52.053  70.889   6.975  1.00185.75           N  
ANISOU   16  N   GLU A  30    31122  18764  20692  -6451  -5389   7197       N  
ATOM     17  CA  GLU A  30      51.128  69.985   7.659  1.00189.21           C  
ANISOU   17  CA  GLU A  30    31490  19168  21231  -5898  -5328   6864       C  
ATOM     18  C   GLU A  30      51.027  68.627   6.967  1.00192.50           C  
ANISOU   18  C   GLU A  30    31718  20257  21164  -5906  -4999   6799       C  
ATOM     19  O   GLU A  30      50.925  67.595   7.629  1.00199.69           O  
ANISOU   19  O   GLU A  30    32505  21343  22024  -5639  -4777   6490       O  
ATOM     20  CB  GLU A  30      49.742  70.625   7.769  1.00193.45           C  
ANISOU   20  CB  GLU A  30    32164  19171  22168  -5433  -5712   6880       C  
ATOM     21  CG  GLU A  30      49.754  71.992   8.431  1.00202.20           C  
ANISOU   21  CG  GLU A  30    33462  19581  23784  -5389  -6027   6908       C  
ATOM     22  CD  GLU A  30      48.381  72.632   8.479  1.00212.29           C  
ANISOU   22  CD  GLU A  30    34831  20337  25494  -4924  -6379   6925       C  
ATOM     23  OE1 GLU A  30      47.485  72.182   7.734  1.00216.26           O  
ANISOU   23  OE1 GLU A  30    35256  21049  25865  -4744  -6439   7035       O  
ATOM     24  OE2 GLU A  30      48.199  73.595   9.254  1.00219.76           O  
ANISOU   24  OE2 GLU A  30    35910  20665  26923  -4747  -6591   6820       O  
ATOM     25  N   THR A  31      51.038  68.631   5.638  1.00213.42           N  
ANISOU   25  N   THR A  31    34360  23276  23454  -6219  -4971   7076       N  
ATOM     26  CA  THR A  31      50.929  67.396   4.868  1.00212.02           C  
ANISOU   26  CA  THR A  31    34023  23741  22796  -6264  -4651   6996       C  
ATOM     27  C   THR A  31      52.213  66.583   5.016  1.00228.44           C  
ANISOU   27  C   THR A  31    35904  26315  24579  -6582  -4177   6840       C  
ATOM     28  O   THR A  31      52.198  65.357   4.919  1.00222.31           O  
ANISOU   28  O   THR A  31    34958  25991  23518  -6486  -3846   6615       O  
ATOM     29  CB  THR A  31      50.658  67.668   3.375  1.00207.91           C  
ANISOU   29  CB  THR A  31    33567  23486  21943  -6576  -4746   7321       C  
ATOM     30  OG1 THR A  31      51.753  68.400   2.812  1.00216.98           O  
ANISOU   30  OG1 THR A  31    34764  24742  22936  -7150  -4699   7585       O  
ATOM     31  CG2 THR A  31      49.371  68.463   3.199  1.00210.40           C  
ANISOU   31  CG2 THR A  31    34042  23316  22585  -6267  -5236   7507       C  
ATOM     32  N   ASN A  32      53.321  67.280   5.247  1.00262.65           N  
ANISOU   32  N   ASN A  32    40239  30554  29002  -6964  -4148   6959       N  
ATOM     33  CA  ASN A  32      54.596  66.635   5.537  1.00271.78           C  
ANISOU   33  CA  ASN A  32    41164  32111  29988  -7266  -3727   6824       C  
ATOM     34  C   ASN A  32      54.540  65.956   6.899  1.00259.25           C  
ANISOU   34  C   ASN A  32    39488  30364  28651  -6884  -3654   6487       C  
ATOM     35  O   ASN A  32      55.126  64.893   7.104  1.00260.70           O  
ANISOU   35  O   ASN A  32    39413  30978  28661  -6915  -3268   6268       O  
ATOM     36  CB  ASN A  32      55.747  67.647   5.505  1.00286.68           C  
ANISOU   36  CB  ASN A  32    43064  33894  31968  -7769  -3765   7047       C  
ATOM     37  CG  ASN A  32      56.079  68.114   4.101  1.00301.38           C  
ANISOU   37  CG  ASN A  32    44966  36066  33479  -8252  -3726   7365       C  
ATOM     38  OD1 ASN A  32      55.278  67.967   3.178  1.00306.76           O  
ANISOU   38  OD1 ASN A  32    45740  36892  33922  -8189  -3802   7466       O  
ATOM     39  ND2 ASN A  32      57.269  68.683   3.934  1.00306.96           N  
ANISOU   39  ND2 ASN A  32    45600  36884  34147  -8758  -3617   7524       N  
ATOM     40  N   LEU A  33      53.836  66.594   7.828  1.00219.63           N  
ANISOU   40  N   LEU A  33    34659  24724  24066  -6510  -4018   6411       N  
ATOM     41  CA  LEU A  33      53.659  66.064   9.174  1.00178.21           C  
ANISOU   41  CA  LEU A  33    29328  19286  19098  -6091  -3986   6023       C  
ATOM     42  C   LEU A  33      52.805  64.802   9.197  1.00162.70           C  
ANISOU   42  C   LEU A  33    27167  17643  17009  -5602  -3789   5677       C  
ATOM     43  O   LEU A  33      53.063  63.895   9.981  1.00175.05           O  
ANISOU   43  O   LEU A  33    28429  19430  18652  -5339  -3530   5253       O  
ATOM     44  CB  LEU A  33      53.030  67.135  10.072  1.00168.46           C  
ANISOU   44  CB  LEU A  33    28387  17283  18338  -5835  -4414   6017       C  
ATOM     45  CG  LEU A  33      52.556  66.789  11.485  1.00151.17           C  
ANISOU   45  CG  LEU A  33    26094  14850  16495  -5290  -4414   5500       C  
ATOM     46  CD1 LEU A  33      52.755  67.993  12.386  1.00149.02           C  
ANISOU   46  CD1 LEU A  33    26065  13924  16631  -5349  -4710   5496       C  
ATOM     47  CD2 LEU A  33      51.091  66.372  11.495  1.00127.87           C  
ANISOU   47  CD2 LEU A  33    23189  11786  13610  -4740  -4516   5346       C  
ATOM     48  N   LEU A  34      51.790  64.748   8.340  1.00152.96           N  
ANISOU   48  N   LEU A  34    26106  16424  15588  -5500  -3940   5880       N  
ATOM     49  CA  LEU A  34      50.936  63.568   8.240  1.00152.28           C  
ANISOU   49  CA  LEU A  34    25851  16651  15355  -5087  -3773   5587       C  
ATOM     50  C   LEU A  34      51.703  62.388   7.650  1.00155.03           C  
ANISOU   50  C   LEU A  34    25893  17708  15304  -5297  -3281   5423       C  
ATOM     51  O   LEU A  34      51.448  61.235   7.996  1.00156.53           O  
ANISOU   51  O   LEU A  34    25830  18172  15472  -4953  -3031   5028       O  
ATOM     52  CB  LEU A  34      49.689  63.865   7.401  1.00163.79           C  
ANISOU   52  CB  LEU A  34    27538  17967  16728  -4966  -4085   5860       C  
ATOM     53  CG  LEU A  34      48.597  62.788   7.401  1.00161.55           C  
ANISOU   53  CG  LEU A  34    27143  17887  16353  -4516  -4018   5600       C  
ATOM     54  CD1 LEU A  34      47.215  63.423   7.453  1.00165.62           C  
ANISOU   54  CD1 LEU A  34    27798  17934  17194  -4134  -4437   5689       C  
ATOM     55  CD2 LEU A  34      48.718  61.874   6.184  1.00160.67           C  
ANISOU   55  CD2 LEU A  34    26926  18422  15700  -4775  -3733   5643       C  
ATOM     56  N   PHE A  35      52.627  62.684   6.742  1.00156.69           N  
ANISOU   56  N   PHE A  35    26127  18201  15208  -5871  -3136   5722       N  
ATOM     57  CA  PHE A  35      53.515  61.670   6.186  1.00164.63           C  
ANISOU   57  CA  PHE A  35    26816  19860  15876  -6116  -2622   5543       C  
ATOM     58  C   PHE A  35      54.422  61.099   7.274  1.00187.00           C  
ANISOU   58  C   PHE A  35    29263  22783  19007  -5955  -2350   5142       C  
ATOM     59  O   PHE A  35      54.601  59.884   7.364  1.00192.04           O  
ANISOU   59  O   PHE A  35    29577  23807  19581  -5756  -1991   4778       O  
ATOM     60  CB  PHE A  35      54.338  62.262   5.040  1.00163.80           C  
ANISOU   60  CB  PHE A  35    26829  20008  15399  -6810  -2524   5962       C  
ATOM     61  CG  PHE A  35      55.580  61.483   4.707  1.00160.67           C  
ANISOU   61  CG  PHE A  35    26052  20203  14793  -7119  -1965   5757       C  
ATOM     62  CD1 PHE A  35      55.518  60.368   3.885  1.00155.54           C  
ANISOU   62  CD1 PHE A  35    25241  20110  13747  -7148  -1563   5550       C  
ATOM     63  CD2 PHE A  35      56.818  61.890   5.182  1.00171.06           C  
ANISOU   63  CD2 PHE A  35    27162  21512  16322  -7401  -1839   5770       C  
ATOM     64  CE1 PHE A  35      56.661  59.658   3.567  1.00162.72           C  
ANISOU   64  CE1 PHE A  35    25773  21540  14514  -7411  -1019   5328       C  
ATOM     65  CE2 PHE A  35      57.965  61.185   4.868  1.00175.78           C  
ANISOU   65  CE2 PHE A  35    27355  22647  16784  -7670  -1318   5580       C  
ATOM     66  CZ  PHE A  35      57.888  60.068   4.059  1.00172.88           C  
ANISOU   66  CZ  PHE A  35    26815  22815  16056  -7661   -893   5348       C  
ATOM     67  N   ASN A  36      54.987  61.980   8.098  1.00200.38           N  
ANISOU   67  N   ASN A  36    31000  24100  21037  -6051  -2548   5219       N  
ATOM     68  CA  ASN A  36      55.847  61.568   9.207  1.00181.22           C  
ANISOU   68  CA  ASN A  36    28232  21712  18910  -5933  -2381   4892       C  
ATOM     69  C   ASN A  36      55.094  60.814  10.308  1.00162.34           C  
ANISOU   69  C   ASN A  36    25736  19176  16768  -5320  -2426   4473       C  
ATOM     70  O   ASN A  36      55.617  59.855  10.874  1.00165.19           O  
ANISOU   70  O   ASN A  36    25738  19799  17227  -5160  -2166   4150       O  
ATOM     71  CB  ASN A  36      56.558  62.785   9.805  1.00178.15           C  
ANISOU   71  CB  ASN A  36    27971  20926  18793  -6229  -2636   5097       C  
ATOM     72  CG  ASN A  36      57.746  63.233   8.971  1.00180.32           C  
ANISOU   72  CG  ASN A  36    28164  21480  18869  -6879  -2457   5409       C  
ATOM     73  OD1 ASN A  36      58.342  62.438   8.244  1.00179.18           O  
ANISOU   73  OD1 ASN A  36    27727  21893  18461  -7072  -2040   5343       O  
ATOM     74  ND2 ASN A  36      58.101  64.509   9.080  1.00181.56           N  
ANISOU   74  ND2 ASN A  36    28575  21246  19164  -7230  -2754   5735       N  
ATOM     75  N   LEU A  37      53.876  61.256  10.619  1.00145.63           N  
ANISOU   75  N   LEU A  37    23921  16637  14776  -4989  -2759   4490       N  
ATOM     76  CA  LEU A  37      53.035  60.568  11.599  1.00138.29           C  
ANISOU   76  CA  LEU A  37    22917  15585  14043  -4431  -2791   4106       C  
ATOM     77  C   LEU A  37      52.674  59.171  11.126  1.00139.10           C  
ANISOU   77  C   LEU A  37    22785  16157  13911  -4213  -2480   3877       C  
ATOM     78  O   LEU A  37      52.711  58.216  11.901  1.00117.49           O  
ANISOU   78  O   LEU A  37    19795  13550  11294  -3914  -2317   3524       O  
ATOM     79  CB  LEU A  37      51.756  61.355  11.888  1.00112.63           C  
ANISOU   79  CB  LEU A  37    20011  11807  10978  -4137  -3177   4176       C  
ATOM     80  CG  LEU A  37      51.839  62.471  12.926  1.00119.67           C  
ANISOU   80  CG  LEU A  37    21103  12127  12237  -4119  -3471   4167       C  
ATOM     81  CD1 LEU A  37      50.451  62.787  13.462  1.00119.16           C  
ANISOU   81  CD1 LEU A  37    21245  11620  12410  -3654  -3727   4032       C  
ATOM     82  CD2 LEU A  37      52.784  62.085  14.055  1.00111.96           C  
ANISOU   82  CD2 LEU A  37    19885  11242  11412  -4132  -3323   3872       C  
ATOM     83  N   ASN A  38      52.309  59.062   9.851  1.00151.14           N  
ANISOU   83  N   ASN A  38    24415  17919  15092  -4385  -2420   4087       N  
ATOM     84  CA  ASN A  38      51.992  57.771   9.252  1.00143.60           C  
ANISOU   84  CA  ASN A  38    23273  17418  13871  -4246  -2115   3874       C  
ATOM     85  C   ASN A  38      53.241  56.915   9.093  1.00143.00           C  
ANISOU   85  C   ASN A  38    22818  17802  13714  -4449  -1667   3686       C  
ATOM     86  O   ASN A  38      53.177  55.692   9.192  1.00141.99           O  
ANISOU   86  O   ASN A  38    22436  17950  13564  -4207  -1396   3358       O  
ATOM     87  CB  ASN A  38      51.311  57.961   7.894  1.00132.45           C  
ANISOU   87  CB  ASN A  38    22108  16146  12069  -4449  -2194   4169       C  
ATOM     88  CG  ASN A  38      49.898  58.500   8.018  1.00122.03           C  
ANISOU   88  CG  ASN A  38    21075  14420  10872  -4141  -2619   4299       C  
ATOM     89  OD1 ASN A  38      49.466  58.915   9.093  1.00118.69           O  
ANISOU   89  OD1 ASN A  38    20698  13569  10831  -3813  -2845   4183       O  
ATOM     90  ND2 ASN A  38      49.170  58.501   6.909  1.00131.19           N  
ANISOU   90  ND2 ASN A  38    22419  15716  11709  -4258  -2728   4535       N  
ATOM     91  N   SER A  39      54.378  57.563   8.853  1.00145.91           N  
ANISOU   91  N   SER A  39    23134  18234  14072  -4893  -1591   3893       N  
ATOM     92  CA  SER A  39      55.657  56.864   8.774  1.00144.25           C  
ANISOU   92  CA  SER A  39    22507  18429  13871  -5091  -1171   3722       C  
ATOM     93  C   SER A  39      56.038  56.241  10.113  1.00140.31           C  
ANISOU   93  C   SER A  39    21695  17840  13775  -4749  -1144   3393       C  
ATOM     94  O   SER A  39      56.625  55.162  10.158  1.00144.76           O  
ANISOU   94  O   SER A  39    21875  18729  14400  -4662   -805   3125       O  
ATOM     95  CB  SER A  39      56.763  57.807   8.310  1.00154.38           C  
ANISOU   95  CB  SER A  39    23794  19770  15093  -5659  -1131   4040       C  
ATOM     96  OG  SER A  39      58.038  57.283   8.635  1.00162.63           O  
ANISOU   96  OG  SER A  39    24381  21088  16322  -5779   -807   3856       O  
ATOM     97  N   CYS A  40      55.732  56.943  11.200  1.00139.11           N  
ANISOU   97  N   CYS A  40    21715  17237  13904  -4577  -1509   3418       N  
ATOM     98  CA  CYS A  40      55.966  56.421  12.544  1.00126.04           C  
ANISOU   98  CA  CYS A  40    19834  15472  12585  -4275  -1550   3133       C  
ATOM     99  C   CYS A  40      55.024  55.266  12.870  1.00117.72           C  
ANISOU   99  C   CYS A  40    18712  14485  11530  -3792  -1478   2821       C  
ATOM    100  O   CYS A  40      55.446  54.248  13.417  1.00117.37           O  
ANISOU  100  O   CYS A  40    18337  14618  11642  -3611  -1301   2567       O  
ATOM    101  CB  CYS A  40      55.815  57.523  13.595  1.00127.51           C  
ANISOU  101  CB  CYS A  40    20276  15158  13013  -4257  -1948   3216       C  
ATOM    102  SG  CYS A  40      57.329  58.441  13.947  1.00123.52           S  
ANISOU  102  SG  CYS A  40    19649  14587  12695  -4751  -2016   3417       S  
ATOM    103  N   SER A  41      53.749  55.431  12.524  1.00118.48           N  
ANISOU  103  N   SER A  41    19113  14432  11472  -3596  -1635   2861       N  
ATOM    104  CA  SER A  41      52.720  54.435  12.823  1.00106.58           C  
ANISOU  104  CA  SER A  41    17577  12961   9959  -3158  -1601   2590       C  
ATOM    105  C   SER A  41      53.028  53.105  12.131  1.00 96.12           C  
ANISOU  105  C   SER A  41    15953  12091   8477  -3138  -1207   2396       C  
ATOM    106  O   SER A  41      52.647  52.041  12.616  1.00114.20           O  
ANISOU  106  O   SER A  41    18084  14451  10855  -2810  -1113   2118       O  
ATOM    107  CB  SER A  41      51.339  54.947  12.416  1.00100.05           C  
ANISOU  107  CB  SER A  41    17100  11912   9004  -3006  -1847   2715       C  
ATOM    108  OG  SER A  41      50.326  54.021  12.764  1.00 92.97           O  
ANISOU  108  OG  SER A  41    16160  11046   8120  -2599  -1825   2454       O  
ATOM    109  N   LYS A  42      53.681  53.177  10.976  1.00 99.51           N  
ANISOU  109  N   LYS A  42    16325  12819   8667  -3505   -970   2538       N  
ATOM    110  CA  LYS A  42      54.153  51.982  10.280  1.00102.73           C  
ANISOU  110  CA  LYS A  42    16430  13658   8944  -3538   -538   2318       C  
ATOM    111  C   LYS A  42      55.106  51.175  11.168  1.00102.73           C  
ANISOU  111  C   LYS A  42    15999  13731   9305  -3393   -364   2071       C  
ATOM    112  O   LYS A  42      54.936  49.970  11.340  1.00103.70           O  
ANISOU  112  O   LYS A  42    15909  13981   9511  -3114   -181   1783       O  
ATOM    113  CB  LYS A  42      54.858  52.360   8.970  1.00121.07           C  
ANISOU  113  CB  LYS A  42    18760  16293  10949  -4031   -289   2514       C  
ATOM    114  CG  LYS A  42      53.955  52.937   7.884  1.00135.48           C  
ANISOU  114  CG  LYS A  42    20989  18135  12353  -4220   -430   2771       C  
ATOM    115  CD  LYS A  42      53.026  51.888   7.288  1.00141.18           C  
ANISOU  115  CD  LYS A  42    21749  19068  12824  -4011   -289   2551       C  
ATOM    116  CE  LYS A  42      51.564  52.194   7.583  1.00133.60           C  
ANISOU  116  CE  LYS A  42    21102  17792  11866  -3707   -702   2641       C  
ATOM    117  NZ  LYS A  42      51.144  53.527   7.064  1.00139.97           N  
ANISOU  117  NZ  LYS A  42    22283  18388  12513  -3962  -1052   3079       N  
ATOM    118  N   SER A  43      56.112  51.851  11.720  1.00114.59           N  
ANISOU  118  N   SER A  43    17371  15136  11032  -3601   -447   2204       N  
ATOM    119  CA  SER A  43      57.117  51.217  12.577  1.00130.46           C  
ANISOU  119  CA  SER A  43    18952  17203  13415  -3514   -347   2038       C  
ATOM    120  C   SER A  43      56.789  51.335  14.066  1.00145.68           C  
ANISOU  120  C   SER A  43    20950  18786  15618  -3239   -709   1985       C  
ATOM    121  O   SER A  43      57.608  50.974  14.909  1.00151.86           O  
ANISOU  121  O   SER A  43    21422  19568  16710  -3203   -730   1911       O  
ATOM    122  CB  SER A  43      58.501  51.816  12.307  1.00130.38           C  
ANISOU  122  CB  SER A  43    18701  17337  13500  -3941   -218   2210       C  
ATOM    123  OG  SER A  43      58.519  53.203  12.579  1.00132.55           O  
ANISOU  123  OG  SER A  43    19279  17331  13752  -4189   -549   2504       O  
ATOM    124  N   LYS A  44      55.614  51.889  14.365  1.00149.94           N  
ANISOU  124  N   LYS A  44    21892  19037  16040  -3077   -995   2034       N  
ATOM    125  CA  LYS A  44      55.057  52.001  15.721  1.00152.66           C  
ANISOU  125  CA  LYS A  44    22372  19063  16570  -2809  -1303   1939       C  
ATOM    126  C   LYS A  44      56.006  52.664  16.733  1.00157.74           C  
ANISOU  126  C   LYS A  44    22937  19536  17462  -2995  -1509   2024       C  
ATOM    127  O   LYS A  44      56.046  52.289  17.904  1.00173.24           O  
ANISOU  127  O   LYS A  44    24820  21389  19612  -2823  -1655   1889       O  
ATOM    128  CB  LYS A  44      54.581  50.623  16.240  1.00159.83           C  
ANISOU  128  CB  LYS A  44    23100  20063  17565  -2429  -1206   1657       C  
ATOM    129  CG  LYS A  44      55.648  49.587  16.610  1.00175.69           C  
ANISOU  129  CG  LYS A  44    24646  22275  19833  -2400  -1028   1528       C  
ATOM    130  CD  LYS A  44      55.033  48.283  17.093  1.00184.38           C  
ANISOU  130  CD  LYS A  44    25636  23406  21013  -2029   -977   1284       C  
ATOM    131  CE  LYS A  44      56.114  47.277  17.469  1.00185.35           C  
ANISOU  131  CE  LYS A  44    25287  23678  21460  -1988   -841   1187       C  
ATOM    132  NZ  LYS A  44      55.541  45.988  17.946  1.00180.77           N  
ANISOU  132  NZ  LYS A  44    24611  23092  20981  -1645   -815    978       N  
ATOM    133  N   ASP A  45      56.746  53.673  16.284  1.00143.58           N  
ANISOU  133  N   ASP A  45    21189  17718  15647  -3379  -1541   2262       N  
ATOM    134  CA  ASP A  45      57.607  54.443  17.177  1.00131.15           C  
ANISOU  134  CA  ASP A  45    19585  15960  14287  -3611  -1769   2364       C  
ATOM    135  C   ASP A  45      56.803  55.615  17.737  1.00118.27           C  
ANISOU  135  C   ASP A  45    18429  13884  12624  -3596  -2115   2430       C  
ATOM    136  O   ASP A  45      56.883  56.731  17.229  1.00113.18           O  
ANISOU  136  O   ASP A  45    18021  13070  11911  -3872  -2222   2659       O  
ATOM    137  CB  ASP A  45      58.855  54.936  16.432  1.00133.63           C  
ANISOU  137  CB  ASP A  45    19685  16470  14620  -4063  -1621   2584       C  
ATOM    138  CG  ASP A  45      59.912  55.522  17.361  1.00142.13           C  
ANISOU  138  CG  ASP A  45    20625  17423  15953  -4323  -1836   2673       C  
ATOM    139  OD1 ASP A  45      59.556  56.227  18.329  1.00143.60           O  
ANISOU  139  OD1 ASP A  45    21107  17253  16200  -4299  -2172   2668       O  
ATOM    140  OD2 ASP A  45      61.113  55.282  17.112  1.00145.83           O  
ANISOU  140  OD2 ASP A  45    20678  18160  16569  -4567  -1660   2738       O  
ATOM    141  N   LEU A  46      56.040  55.357  18.795  1.00115.21           N  
ANISOU  141  N   LEU A  46    18176  13298  12301  -3284  -2280   2223       N  
ATOM    142  CA  LEU A  46      55.170  56.367  19.394  1.00123.07           C  
ANISOU  142  CA  LEU A  46    19601  13862  13298  -3208  -2561   2203       C  
ATOM    143  C   LEU A  46      55.966  57.500  20.054  1.00143.21           C  
ANISOU  143  C   LEU A  46    22278  16147  15989  -3545  -2803   2315       C  
ATOM    144  O   LEU A  46      55.508  58.645  20.107  1.00148.80           O  
ANISOU  144  O   LEU A  46    23350  16477  16709  -3619  -3004   2390       O  
ATOM    145  CB  LEU A  46      54.222  55.708  20.406  1.00108.56           C  
ANISOU  145  CB  LEU A  46    17833  11937  11479  -2819  -2619   1915       C  
ATOM    146  CG  LEU A  46      53.199  56.586  21.137  1.00107.75           C  
ANISOU  146  CG  LEU A  46    18133  11407  11400  -2672  -2847   1800       C  
ATOM    147  CD1 LEU A  46      52.211  57.209  20.161  1.00107.66           C  
ANISOU  147  CD1 LEU A  46    18370  11223  11312  -2571  -2864   1920       C  
ATOM    148  CD2 LEU A  46      52.456  55.783  22.185  1.00107.20           C  
ANISOU  148  CD2 LEU A  46    18061  11345  11326  -2350  -2846   1505       C  
ATOM    149  N   SER A  47      57.156  57.176  20.553  1.00151.51           N  
ANISOU  149  N   SER A  47    23018  17378  17171  -3752  -2800   2328       N  
ATOM    150  CA  SER A  47      58.017  58.165  21.199  1.00155.45           C  
ANISOU  150  CA  SER A  47    23596  17666  17801  -4117  -3039   2435       C  
ATOM    151  C   SER A  47      58.413  59.263  20.215  1.00157.33           C  
ANISOU  151  C   SER A  47    23972  17800  18004  -4482  -3050   2728       C  
ATOM    152  O   SER A  47      58.390  60.448  20.550  1.00157.58           O  
ANISOU  152  O   SER A  47    24332  17450  18092  -4684  -3297   2806       O  
ATOM    153  CB  SER A  47      59.263  57.501  21.787  1.00155.28           C  
ANISOU  153  CB  SER A  47    23137  17915  17946  -4279  -3035   2434       C  
ATOM    154  OG  SER A  47      60.012  56.839  20.784  1.00162.64           O  
ANISOU  154  OG  SER A  47    23648  19239  18910  -4369  -2740   2552       O  
ATOM    155  N   ALA A  48      58.788  58.859  19.005  1.00149.08           N  
ANISOU  155  N   ALA A  48    22687  17094  16862  -4589  -2776   2884       N  
ATOM    156  CA  ALA A  48      59.130  59.808  17.953  1.00136.42           C  
ANISOU  156  CA  ALA A  48    21215  15451  15168  -4967  -2757   3194       C  
ATOM    157  C   ALA A  48      57.885  60.568  17.502  1.00128.39           C  
ANISOU  157  C   ALA A  48    20675  14081  14026  -4827  -2904   3274       C  
ATOM    158  O   ALA A  48      57.935  61.775  17.270  1.00132.65           O  
ANISOU  158  O   ALA A  48    21513  14300  14590  -5102  -3105   3502       O  
ATOM    159  CB  ALA A  48      59.777  59.094  16.779  1.00135.16           C  
ANISOU  159  CB  ALA A  48    20683  15784  14887  -5117  -2382   3297       C  
ATOM    160  N   ALA A  49      56.771  59.851  17.374  1.00121.16           N  
ANISOU  160  N   ALA A  49    19816  13214  13005  -4402  -2820   3100       N  
ATOM    161  CA  ALA A  49      55.495  60.464  17.020  1.00130.21           C  
ANISOU  161  CA  ALA A  49    21358  14030  14085  -4205  -2979   3156       C  
ATOM    162  C   ALA A  49      55.084  61.487  18.074  1.00139.09           C  
ANISOU  162  C   ALA A  49    22823  14607  15419  -4146  -3303   3067       C  
ATOM    163  O   ALA A  49      54.478  62.508  17.756  1.00151.53           O  
ANISOU  163  O   ALA A  49    24742  15788  17044  -4171  -3507   3223       O  
ATOM    164  CB  ALA A  49      54.418  59.405  16.861  1.00103.35           C  
ANISOU  164  CB  ALA A  49    17896  10805  10567  -3756  -2834   2946       C  
ATOM    165  N   LEU A  50      55.418  61.198  19.328  1.00139.77           N  
ANISOU  165  N   LEU A  50    22814  14661  15632  -4076  -3354   2811       N  
ATOM    166  CA  LEU A  50      55.165  62.117  20.430  1.00142.52           C  
ANISOU  166  CA  LEU A  50    23475  14524  16150  -4072  -3624   2664       C  
ATOM    167  C   LEU A  50      55.964  63.406  20.281  1.00157.58           C  
ANISOU  167  C   LEU A  50    25568  16139  18165  -4534  -3823   2918       C  
ATOM    168  O   LEU A  50      55.434  64.496  20.487  1.00168.97           O  
ANISOU  168  O   LEU A  50    27389  17072  19738  -4537  -4046   2927       O  
ATOM    169  CB  LEU A  50      55.499  61.455  21.765  1.00136.18           C  
ANISOU  169  CB  LEU A  50    22519  13831  15393  -3987  -3634   2366       C  
ATOM    170  CG  LEU A  50      54.335  60.853  22.549  1.00132.77           C  
ANISOU  170  CG  LEU A  50    22178  13335  14932  -3535  -3606   2025       C  
ATOM    171  CD1 LEU A  50      54.715  60.703  24.013  1.00135.54           C  
ANISOU  171  CD1 LEU A  50    22536  13644  15320  -3593  -3723   1775       C  
ATOM    172  CD2 LEU A  50      53.085  61.707  22.398  1.00133.91           C  
ANISOU  172  CD2 LEU A  50    22698  13035  15145  -3306  -3713   1969       C  
ATOM    173  N   ALA A  51      57.242  63.270  19.938  1.00158.18           N  
ANISOU  173  N   ALA A  51    25360  16525  18215  -4923  -3735   3114       N  
ATOM    174  CA  ALA A  51      58.126  64.418  19.751  1.00148.76           C  
ANISOU  174  CA  ALA A  51    24293  15115  17114  -5426  -3905   3382       C  
ATOM    175  C   ALA A  51      57.639  65.320  18.617  1.00158.28           C  
ANISOU  175  C   ALA A  51    25799  16068  18273  -5547  -3981   3703       C  
ATOM    176  O   ALA A  51      57.705  66.545  18.719  1.00162.33           O  
ANISOU  176  O   ALA A  51    26640  16111  18926  -5790  -4237   3848       O  
ATOM    177  CB  ALA A  51      59.550  63.951  19.485  1.00132.91           C  
ANISOU  177  CB  ALA A  51    21841  13569  15091  -5799  -3742   3532       C  
ATOM    178  N   LEU A  52      57.168  64.710  17.532  1.00159.51           N  
ANISOU  178  N   LEU A  52    25851  16527  18230  -5401  -3776   3824       N  
ATOM    179  CA  LEU A  52      56.579  65.464  16.429  1.00157.28           C  
ANISOU  179  CA  LEU A  52    25861  16032  17866  -5494  -3881   4153       C  
ATOM    180  C   LEU A  52      55.306  66.176  16.872  1.00148.74           C  
ANISOU  180  C   LEU A  52    25180  14359  16974  -5145  -4157   4046       C  
ATOM    181  O   LEU A  52      55.071  67.326  16.508  1.00162.52           O  
ANISOU  181  O   LEU A  52    27261  15651  18840  -5311  -4411   4305       O  
ATOM    182  CB  LEU A  52      56.285  64.551  15.236  1.00159.29           C  
ANISOU  182  CB  LEU A  52    25924  16775  17825  -5408  -3604   4262       C  
ATOM    183  CG  LEU A  52      57.461  63.752  14.673  1.00164.31           C  
ANISOU  183  CG  LEU A  52    26129  18019  18281  -5710  -3257   4321       C  
ATOM    184  CD1 LEU A  52      57.076  63.066  13.373  1.00153.33           C  
ANISOU  184  CD1 LEU A  52    24656  17038  16566  -5684  -3003   4438       C  
ATOM    185  CD2 LEU A  52      58.669  64.653  14.469  1.00176.04           C  
ANISOU  185  CD2 LEU A  52    27606  19462  19817  -6300  -3319   4616       C  
ATOM    186  N   TYR A  53      54.484  65.477  17.648  1.00132.85           N  
ANISOU  186  N   TYR A  53    23118  12349  15010  -4663  -4101   3666       N  
ATOM    187  CA  TYR A  53      53.265  66.052  18.212  1.00130.44           C  
ANISOU  187  CA  TYR A  53    23127  11513  14920  -4289  -4307   3478       C  
ATOM    188  C   TYR A  53      53.532  67.215  19.169  1.00135.83           C  
ANISOU  188  C   TYR A  53    24101  11630  15877  -4451  -4558   3375       C  
ATOM    189  O   TYR A  53      52.862  68.243  19.095  1.00137.85           O  
ANISOU  189  O   TYR A  53    24692  11327  16359  -4376  -4792   3447       O  
ATOM    190  CB  TYR A  53      52.462  64.959  18.922  1.00121.84           C  
ANISOU  190  CB  TYR A  53    21877  10625  13794  -3798  -4141   3069       C  
ATOM    191  CG  TYR A  53      51.309  65.460  19.761  1.00124.70           C  
ANISOU  191  CG  TYR A  53    22499  10488  14395  -3416  -4289   2774       C  
ATOM    192  CD1 TYR A  53      50.198  66.055  19.177  1.00117.79           C  
ANISOU  192  CD1 TYR A  53    21833   9253  13668  -3179  -4442   2897       C  
ATOM    193  CD2 TYR A  53      51.317  65.299  21.142  1.00127.90           C  
ANISOU  193  CD2 TYR A  53    22920  10799  14875  -3296  -4267   2363       C  
ATOM    194  CE1 TYR A  53      49.140  66.504  19.950  1.00119.74           C  
ANISOU  194  CE1 TYR A  53    22270   9042  14186  -2807  -4541   2593       C  
ATOM    195  CE2 TYR A  53      50.265  65.741  21.921  1.00125.87           C  
ANISOU  195  CE2 TYR A  53    22889  10113  14824  -2961  -4344   2045       C  
ATOM    196  CZ  TYR A  53      49.178  66.340  21.322  1.00126.85           C  
ANISOU  196  CZ  TYR A  53    23184   9870  15142  -2700  -4464   2145       C  
ATOM    197  OH  TYR A  53      48.132  66.776  22.104  1.00126.93           O  
ANISOU  197  OH  TYR A  53    23372   9449  15406  -2347  -4508   1796       O  
ATOM    198  N   ASP A  54      54.498  67.048  20.067  1.00139.98           N  
ANISOU  198  N   ASP A  54    24500  12285  16402  -4672  -4524   3201       N  
ATOM    199  CA  ASP A  54      54.881  68.112  20.996  1.00157.54           C  
ANISOU  199  CA  ASP A  54    27001  14014  18842  -4900  -4759   3085       C  
ATOM    200  C   ASP A  54      55.449  69.317  20.244  1.00169.77           C  
ANISOU  200  C   ASP A  54    28768  15239  20498  -5355  -4965   3503       C  
ATOM    201  O   ASP A  54      55.161  70.466  20.579  1.00180.54           O  
ANISOU  201  O   ASP A  54    30505  15979  22115  -5409  -5214   3481       O  
ATOM    202  CB  ASP A  54      55.899  67.599  22.019  1.00159.95           C  
ANISOU  202  CB  ASP A  54    27087  14606  19081  -5109  -4706   2874       C  
ATOM    203  CG  ASP A  54      55.332  66.512  22.916  1.00152.34           C  
ANISOU  203  CG  ASP A  54    25971  13887  18024  -4700  -4554   2468       C  
ATOM    204  OD1 ASP A  54      54.183  66.663  23.385  1.00147.76           O  
ANISOU  204  OD1 ASP A  54    25616  12999  17527  -4322  -4576   2191       O  
ATOM    205  OD2 ASP A  54      56.040  65.512  23.160  1.00145.77           O  
ANISOU  205  OD2 ASP A  54    24784  13545  17057  -4765  -4416   2432       O  
ATOM    206  N   ALA A  55      56.269  69.035  19.236  1.00169.85           N  
ANISOU  206  N   ALA A  55    28544  15675  20318  -5695  -4845   3870       N  
ATOM    207  CA  ALA A  55      56.848  70.061  18.372  1.00168.79           C  
ANISOU  207  CA  ALA A  55    28582  15331  20218  -6182  -5005   4327       C  
ATOM    208  C   ALA A  55      55.778  70.762  17.537  1.00168.69           C  
ANISOU  208  C   ALA A  55    28900  14897  20297  -6013  -5189   4578       C  
ATOM    209  O   ALA A  55      55.876  71.958  17.269  1.00175.29           O  
ANISOU  209  O   ALA A  55    30036  15251  21313  -6279  -5451   4838       O  
ATOM    210  CB  ALA A  55      57.913  69.460  17.467  1.00160.99           C  
ANISOU  210  CB  ALA A  55    27224  14978  18967  -6568  -4763   4621       C  
ATOM    211  N   ALA A  56      54.762  70.005  17.132  1.00163.59           N  
ANISOU  211  N   ALA A  56    28166  14451  19541  -5563  -5065   4498       N  
ATOM    212  CA  ALA A  56      53.709  70.511  16.254  1.00176.39           C  
ANISOU  212  CA  ALA A  56    30033  15755  21232  -5382  -5251   4770       C  
ATOM    213  C   ALA A  56      52.876  71.603  16.914  1.00189.28           C  
ANISOU  213  C   ALA A  56    32030  16595  23294  -5128  -5557   4620       C  
ATOM    214  O   ALA A  56      52.497  72.580  16.267  1.00204.97           O  
ANISOU  214  O   ALA A  56    34132  18302  25447  -5123  -5757   4848       O  
ATOM    215  CB  ALA A  56      52.806  69.371  15.806  1.00176.01           C  
ANISOU  215  CB  ALA A  56    29772  16126  20978  -4948  -5049   4659       C  
ATOM    216  N   ILE A  57      52.572  71.427  18.195  1.00185.77           N  
ANISOU  216  N   ILE A  57    31598  15970  23016  -4824  -5509   4113       N  
ATOM    217  CA  ILE A  57      51.773  72.404  18.927  1.00190.68           C  
ANISOU  217  CA  ILE A  57    32524  15871  24054  -4547  -5724   3858       C  
ATOM    218  C   ILE A  57      52.525  73.733  19.040  1.00216.46           C  
ANISOU  218  C   ILE A  57    35932  18798  27515  -4913  -5908   3962       C  
ATOM    219  O   ILE A  57      51.913  74.791  19.154  1.00240.66           O  
ANISOU  219  O   ILE A  57    39173  21338  30929  -4719  -6085   3893       O  
ATOM    220  CB  ILE A  57      51.407  71.904  20.339  1.00174.06           C  
ANISOU  220  CB  ILE A  57    30388  13734  22011  -4212  -5575   3244       C  
ATOM    221  CG1 ILE A  57      51.083  70.410  20.317  1.00159.20           C  
ANISOU  221  CG1 ILE A  57    28135  12536  19818  -3905  -5268   3068       C  
ATOM    222  CG2 ILE A  57      50.233  72.686  20.898  1.00177.71           C  
ANISOU  222  CG2 ILE A  57    31119  13510  22894  -3794  -5717   2948       C  
ATOM    223  CD1 ILE A  57      51.039  69.773  21.689  1.00157.90           C  
ANISOU  223  CD1 ILE A  57    27875  12517  19601  -3708  -5091   2521       C  
ATOM    224  N   THR A  58      53.853  73.657  19.063  1.00215.05           N  
ANISOU  224  N   THR A  58    35658  18917  27135  -5433  -5858   4107       N  
ATOM    225  CA  THR A  58      54.734  74.826  19.116  1.00206.72           C  
ANISOU  225  CA  THR A  58    34707  17627  26211  -5854  -6021   4244       C  
ATOM    226  C   THR A  58      55.095  75.481  17.766  1.00223.95           C  
ANISOU  226  C   THR A  58    36866  19900  28327  -6174  -6124   4786       C  
ATOM    227  O   THR A  58      55.342  76.682  17.705  1.00222.12           O  
ANISOU  227  O   THR A  58    36798  19289  28309  -6363  -6323   4902       O  
ATOM    228  CB  THR A  58      56.055  74.461  19.828  1.00172.10           C  
ANISOU  228  CB  THR A  58    30189  13542  21660  -6296  -5934   4142       C  
ATOM    229  OG1 THR A  58      56.834  73.599  18.989  1.00160.77           O  
ANISOU  229  OG1 THR A  58    28458  12727  19898  -6612  -5754   4480       O  
ATOM    230  CG2 THR A  58      55.772  73.756  21.142  1.00157.26           C  
ANISOU  230  CG2 THR A  58    28329  11637  19785  -6043  -5845   3626       C  
ATOM    231  N   SER A  59      55.120  74.686  16.699  1.00247.09           N  
ANISOU  231  N   SER A  59    39601  23338  30943  -6246  -5979   5099       N  
ATOM    232  CA  SER A  59      55.822  75.036  15.452  1.00253.73           C  
ANISOU  232  CA  SER A  59    40356  24475  31575  -6702  -5986   5592       C  
ATOM    233  C   SER A  59      55.404  76.206  14.523  1.00247.05           C  
ANISOU  233  C   SER A  59    39688  23304  30877  -6753  -6243   5943       C  
ATOM    234  O   SER A  59      56.265  77.018  14.187  1.00259.01           O  
ANISOU  234  O   SER A  59    41244  24783  32387  -7206  -6337   6195       O  
ATOM    235  CB  SER A  59      55.866  73.775  14.581  1.00249.04           C  
ANISOU  235  CB  SER A  59    39507  24548  30570  -6736  -5712   5766       C  
ATOM    236  OG  SER A  59      54.697  73.661  13.793  1.00246.83           O  
ANISOU  236  OG  SER A  59    39283  24237  30262  -6387  -5778   5893       O  
ATOM    237  N   SER A  60      54.143  76.335  14.101  1.00246.79           N  
ANISOU  237  N   SER A  60    39747  23035  30987  -6325  -6374   5983       N  
ATOM    238  CA  SER A  60      53.877  77.322  13.026  1.00244.76           C  
ANISOU  238  CA  SER A  60    39609  22583  30806  -6460  -6620   6406       C  
ATOM    239  C   SER A  60      53.026  78.607  13.234  1.00208.87           C  
ANISOU  239  C   SER A  60    35306  17285  26772  -6176  -6956   6392       C  
ATOM    240  O   SER A  60      53.273  79.585  12.527  1.00196.15           O  
ANISOU  240  O   SER A  60    33810  15492  25228  -6464  -7170   6755       O  
ATOM    241  CB  SER A  60      53.252  76.576  11.836  1.00227.62           C  
ANISOU  241  CB  SER A  60    37308  20854  28322  -6364  -6548   6669       C  
ATOM    242  OG  SER A  60      54.126  75.582  11.333  1.00213.87           O  
ANISOU  242  OG  SER A  60    35347  19818  26095  -6719  -6237   6774       O  
ATOM    243  N   GLU A  61      52.048  78.660  14.141  1.00204.09           N  
ANISOU  243  N   GLU A  61    34772  16236  26535  -5638  -6999   5995       N  
ATOM    244  CA  GLU A  61      51.432  77.518  14.800  1.00196.70           C  
ANISOU  244  CA  GLU A  61    33715  15485  25536  -5217  -6786   5607       C  
ATOM    245  C   GLU A  61      50.597  76.697  13.821  1.00187.48           C  
ANISOU  245  C   GLU A  61    32394  14690  24149  -4987  -6745   5817       C  
ATOM    246  O   GLU A  61      49.941  77.249  12.937  1.00180.59           O  
ANISOU  246  O   GLU A  61    31557  13666  23394  -4909  -6963   6128       O  
ATOM    247  CB  GLU A  61      50.557  77.988  15.965  1.00200.17           C  
ANISOU  247  CB  GLU A  61    34285  15307  26463  -4722  -6849   5130       C  
ATOM    248  CG  GLU A  61      51.323  78.662  17.106  1.00204.62           C  
ANISOU  248  CG  GLU A  61    35006  15533  27206  -4922  -6848   4813       C  
ATOM    249  CD  GLU A  61      52.246  77.715  17.856  1.00192.26           C  
ANISOU  249  CD  GLU A  61    33343  14400  25307  -5156  -6608   4567       C  
ATOM    250  OE1 GLU A  61      52.464  76.582  17.383  1.00178.61           O  
ANISOU  250  OE1 GLU A  61    31418  13247  23200  -5232  -6433   4701       O  
ATOM    251  OE2 GLU A  61      52.761  78.106  18.924  1.00188.33           O  
ANISOU  251  OE2 GLU A  61    32958  13670  24928  -5276  -6597   4237       O  
ATOM    252  N   VAL A  62      50.631  75.379  13.977  1.00187.09           N  
ANISOU  252  N   VAL A  62    32177  15131  23780  -4896  -6479   5651       N  
ATOM    253  CA  VAL A  62      49.881  74.487  13.100  1.00191.75           C  
ANISOU  253  CA  VAL A  62    32615  16124  24118  -4694  -6409   5808       C  
ATOM    254  C   VAL A  62      48.464  74.232  13.602  1.00193.03           C  
ANISOU  254  C   VAL A  62    32762  15995  24586  -4048  -6461   5508       C  
ATOM    255  O   VAL A  62      48.240  74.117  14.809  1.00186.18           O  
ANISOU  255  O   VAL A  62    31938  14853  23948  -3763  -6382   5059       O  
ATOM    256  CB  VAL A  62      50.603  73.125  12.952  1.00177.85           C  
ANISOU  256  CB  VAL A  62    30661  15062  21852  -4909  -6071   5782       C  
ATOM    257  CG1 VAL A  62      49.825  72.187  12.046  1.00165.54           C  
ANISOU  257  CG1 VAL A  62    28956  13934  20009  -4710  -5984   5912       C  
ATOM    258  CG2 VAL A  62      51.995  73.318  12.408  1.00183.39           C  
ANISOU  258  CG2 VAL A  62    31315  16102  22263  -5544  -5976   6068       C  
ATOM    259  N   ARG A  63      47.510  74.156  12.674  1.00196.31           N  
ANISOU  259  N   ARG A  63    33104  16484  25000  -3840  -6593   5747       N  
ATOM    260  CA  ARG A  63      46.213  73.578  12.990  1.00196.29           C  
ANISOU  260  CA  ARG A  63    32999  16401  25180  -3262  -6581   5492       C  
ATOM    261  C   ARG A  63      46.276  72.139  12.516  1.00195.15           C  
ANISOU  261  C   ARG A  63    32681  16944  24524  -3302  -6334   5521       C  
ATOM    262  O   ARG A  63      46.676  71.864  11.383  1.00206.79           O  
ANISOU  262  O   ARG A  63    34092  18877  25602  -3650  -6303   5880       O  
ATOM    263  CB  ARG A  63      45.054  74.313  12.313  1.00205.11           C  
ANISOU  263  CB  ARG A  63    34102  17187  26645  -2983  -6887   5720       C  
ATOM    264  CG  ARG A  63      44.455  75.458  13.118  1.00209.64           C  
ANISOU  264  CG  ARG A  63    34781  17004  27868  -2649  -7070   5491       C  
ATOM    265  CD  ARG A  63      43.259  76.064  12.392  1.00219.08           C  
ANISOU  265  CD  ARG A  63    35905  17915  29422  -2351  -7369   5741       C  
ATOM    266  NE  ARG A  63      42.079  76.148  13.251  1.00215.83           N  
ANISOU  266  NE  ARG A  63    35398  17079  29530  -1734  -7360   5330       N  
ATOM    267  CZ  ARG A  63      40.875  76.541  12.842  1.00214.59           C  
ANISOU  267  CZ  ARG A  63    35111  16656  29769  -1363  -7581   5447       C  
ATOM    268  NH1 ARG A  63      40.676  76.888  11.577  1.00211.99           N  
ANISOU  268  NH1 ARG A  63    34759  16433  29355  -1557  -7865   5979       N  
ATOM    269  NH2 ARG A  63      39.864  76.586  13.700  1.00214.26           N  
ANISOU  269  NH2 ARG A  63    34948  16253  30207   -810  -7511   5022       N  
ATOM    270  N   LEU A  64      45.874  71.224  13.388  1.00181.79           N  
ANISOU  270  N   LEU A  64    30917  15323  22834  -2951  -6145   5121       N  
ATOM    271  CA  LEU A  64      46.022  69.799  13.127  1.00155.44           C  
ANISOU  271  CA  LEU A  64    27423  12613  19024  -2978  -5880   5087       C  
ATOM    272  C   LEU A  64      44.712  69.204  12.634  1.00166.90           C  
ANISOU  272  C   LEU A  64    28735  14204  20476  -2567  -5934   5094       C  
ATOM    273  O   LEU A  64      43.671  69.347  13.273  1.00176.88           O  
ANISOU  273  O   LEU A  64    29982  15094  22130  -2085  -6025   4834       O  
ATOM    274  CB  LEU A  64      46.520  69.070  14.378  1.00143.94           C  
ANISOU  274  CB  LEU A  64    25952  11225  17513  -2902  -5625   4653       C  
ATOM    275  CG  LEU A  64      47.972  69.318  14.820  1.00143.89           C  
ANISOU  275  CG  LEU A  64    25979  11298  17394  -3367  -5505   4628       C  
ATOM    276  CD1 LEU A  64      48.189  70.712  15.419  1.00157.44           C  
ANISOU  276  CD1 LEU A  64    27949  12340  19530  -3466  -5747   4600       C  
ATOM    277  CD2 LEU A  64      48.434  68.252  15.795  1.00126.38           C  
ANISOU  277  CD2 LEU A  64    23490   9523  15007  -3256  -5144   4140       C  
ATOM    278  N   SER A  65      44.772  68.533  11.490  1.00170.64           N  
ANISOU  278  N   SER A  65    29091  15233  20511  -2775  -5860   5371       N  
ATOM    279  CA  SER A  65      43.573  67.979  10.892  1.00167.87           C  
ANISOU  279  CA  SER A  65    28597  15064  20120  -2458  -5934   5416       C  
ATOM    280  C   SER A  65      43.203  66.764  11.725  1.00127.17           C  
ANISOU  280  C   SER A  65    23341  10102  14878  -2106  -5700   5017       C  
ATOM    281  O   SER A  65      44.040  66.229  12.446  1.00123.76           O  
ANISOU  281  O   SER A  65    22833   9897  14293  -2199  -5397   4718       O  
ATOM    282  CB  SER A  65      43.813  67.603   9.429  1.00167.33           C  
ANISOU  282  CB  SER A  65    28457  15558  19562  -2839  -5899   5785       C  
ATOM    283  OG  SER A  65      42.608  67.240   8.775  1.00171.19           O  
ANISOU  283  OG  SER A  65    28822  16177  20047  -2575  -6035   5865       O  
ATOM    284  N   GLN A  66      41.947  66.340  11.638  1.00126.21           N  
ANISOU  284  N   GLN A  66    23089   9985  14882  -1687  -5782   4926       N  
ATOM    285  CA  GLN A  66      41.457  65.234  12.453  1.00120.98           C  
ANISOU  285  CA  GLN A  66    22187   9590  14190  -1303  -5488   4425       C  
ATOM    286  C   GLN A  66      42.254  63.948  12.253  1.00116.51           C  
ANISOU  286  C   GLN A  66    21435   9746  13087  -1529  -5094   4282       C  
ATOM    287  O   GLN A  66      42.396  63.175  13.189  1.00128.99           O  
ANISOU  287  O   GLN A  66    22837  11526  14649  -1343  -4792   3832       O  
ATOM    288  CB  GLN A  66      39.972  64.990  12.177  1.00143.43           C  
ANISOU  288  CB  GLN A  66    24899  12370  17229   -879  -5666   4429       C  
ATOM    289  CG  GLN A  66      39.077  66.147  12.618  1.00165.21           C  
ANISOU  289  CG  GLN A  66    27753  14383  20637   -531  -5996   4438       C  
ATOM    290  CD  GLN A  66      39.022  67.284  11.606  1.00196.52           C  
ANISOU  290  CD  GLN A  66    31766  18144  24759   -755  -6309   4889       C  
ATOM    291  OE1 GLN A  66      39.573  67.181  10.510  1.00212.05           O  
ANISOU  291  OE1 GLN A  66    33758  20500  26313  -1180  -6328   5247       O  
ATOM    292  NE2 GLN A  66      38.350  68.373  11.971  1.00206.47           N  
ANISOU  292  NE2 GLN A  66    33026  18803  26619   -474  -6532   4846       N  
ATOM    293  N   GLN A  67      42.800  63.742  11.056  1.00117.83           N  
ANISOU  293  N   GLN A  67    21652  10287  12832  -1944  -5093   4660       N  
ATOM    294  CA  GLN A  67      43.657  62.583  10.780  1.00119.08           C  
ANISOU  294  CA  GLN A  67    21629  11101  12514  -2185  -4697   4524       C  
ATOM    295  C   GLN A  67      44.864  62.504  11.713  1.00130.39           C  
ANISOU  295  C   GLN A  67    22988  12579  13976  -2327  -4430   4252       C  
ATOM    296  O   GLN A  67      45.306  61.409  12.060  1.00128.81           O  
ANISOU  296  O   GLN A  67    22553  12805  13585  -2291  -4089   3944       O  
ATOM    297  CB  GLN A  67      44.136  62.577   9.324  1.00117.43           C  
ANISOU  297  CB  GLN A  67    21526  11242  11852  -2675  -4728   4978       C  
ATOM    298  CG  GLN A  67      43.124  62.024   8.324  1.00130.56           C  
ANISOU  298  CG  GLN A  67    23170  13168  13268  -2600  -4847   5148       C  
ATOM    299  CD  GLN A  67      42.210  63.083   7.745  1.00146.51           C  
ANISOU  299  CD  GLN A  67    25250  14823  15593  -2520  -5251   5444       C  
ATOM    300  OE1 GLN A  67      41.668  63.919   8.467  1.00156.34           O  
ANISOU  300  OE1 GLN A  67    26557  15499  17347  -2217  -5500   5409       O  
ATOM    301  NE2 GLN A  67      42.038  63.055   6.428  1.00149.91           N  
ANISOU  301  NE2 GLN A  67    25655  15579  15724  -2798  -5309   5717       N  
ATOM    302  N   HIS A  68      45.413  63.659  12.085  1.00139.24           N  
ANISOU  302  N   HIS A  68    24306  13255  15344  -2508  -4609   4388       N  
ATOM    303  CA  HIS A  68      46.592  63.717  12.952  1.00140.72           C  
ANISOU  303  CA  HIS A  68    24439  13455  15572  -2697  -4420   4179       C  
ATOM    304  C   HIS A  68      46.615  62.873  14.220  1.00138.47           C  
ANISOU  304  C   HIS A  68    23939  13302  15372  -2392  -4167   3652       C  
ATOM    305  O   HIS A  68      47.478  62.011  14.385  1.00152.87           O  
ANISOU  305  O   HIS A  68    25546  15558  16980  -2533  -3881   3501       O  
ATOM    306  CB  HIS A  68      47.003  65.165  13.223  1.00153.55           C  
ANISOU  306  CB  HIS A  68    26344  14501  17498  -2912  -4702   4386       C  
ATOM    307  CG  HIS A  68      47.288  65.962  11.988  1.00165.93           C  
ANISOU  307  CG  HIS A  68    28125  15991  18931  -3336  -4931   4953       C  
ATOM    308  ND1 HIS A  68      47.882  67.204  12.033  1.00171.58           N  
ANISOU  308  ND1 HIS A  68    29093  16254  19848  -3655  -5166   5217       N  
ATOM    309  CD2 HIS A  68      47.068  65.698  10.678  1.00175.51           C  
ANISOU  309  CD2 HIS A  68    29359  17524  19804  -3532  -4969   5317       C  
ATOM    310  CE1 HIS A  68      48.012  67.673  10.805  1.00184.89           C  
ANISOU  310  CE1 HIS A  68    30830  18068  21353  -3984  -5283   5640       C  
ATOM    311  NE2 HIS A  68      47.527  66.779   9.964  1.00185.31           N  
ANISOU  311  NE2 HIS A  68    30749  18593  21067  -3925  -5165   5704       N  
ATOM    312  N   PHE A  69      45.688  63.146  15.127  1.00133.38           N  
ANISOU  312  N   PHE A  69    23351  12272  15054  -1989  -4276   3378       N  
ATOM    313  CA  PHE A  69      45.575  62.323  16.333  1.00149.44           C  
ANISOU  313  CA  PHE A  69    25207  14445  17129  -1712  -4048   2891       C  
ATOM    314  C   PHE A  69      44.600  61.062  16.268  1.00152.71           C  
ANISOU  314  C   PHE A  69    25394  15219  17409  -1349  -3875   2671       C  
ATOM    315  O   PHE A  69      44.398  60.241  17.164  1.00154.52           O  
ANISOU  315  O   PHE A  69    25467  15610  17633  -1123  -3683   2301       O  
ATOM    316  CB  PHE A  69      44.899  63.112  17.434  1.00153.44           C  
ANISOU  316  CB  PHE A  69    25870  14401  18028  -1427  -4188   2618       C  
ATOM    317  CG  PHE A  69      43.535  63.582  17.064  1.00140.58           C  
ANISOU  317  CG  PHE A  69    24318  12438  16657  -1090  -4398   2692       C  
ATOM    318  CD1 PHE A  69      42.426  62.789  17.283  1.00138.01           C  
ANISOU  318  CD1 PHE A  69    23813  12270  16354   -688  -4291   2443       C  
ATOM    319  CD2 PHE A  69      43.364  64.825  16.476  1.00141.20           C  
ANISOU  319  CD2 PHE A  69    24634  12032  16982  -1187  -4723   3038       C  
ATOM    320  CE1 PHE A  69      41.163  63.231  16.929  1.00149.33           C  
ANISOU  320  CE1 PHE A  69    25269  13400  18071   -373  -4501   2524       C  
ATOM    321  CE2 PHE A  69      42.109  65.274  16.120  1.00158.46           C  
ANISOU  321  CE2 PHE A  69    26858  13884  19466   -861  -4956   3137       C  
ATOM    322  CZ  PHE A  69      41.005  64.477  16.345  1.00164.13           C  
ANISOU  322  CZ  PHE A  69    27360  14779  20222   -447  -4843   2876       C  
ATOM    323  N   GLN A  70      44.078  60.946  15.051  1.00138.35           N  
ANISOU  323  N   GLN A  70    23580  13545  15443  -1372  -3967   2968       N  
ATOM    324  CA  GLN A  70      43.347  59.746  14.681  1.00128.03           C  
ANISOU  324  CA  GLN A  70    22070  12641  13936  -1156  -3815   2847       C  
ATOM    325  C   GLN A  70      44.575  58.847  14.716  1.00111.16           C  
ANISOU  325  C   GLN A  70    19761  10962  11514  -1413  -3506   2750       C  
ATOM    326  O   GLN A  70      44.619  57.875  15.463  1.00117.85           O  
ANISOU  326  O   GLN A  70    20417  12029  12330  -1244  -3286   2418       O  
ATOM    327  CB  GLN A  70      42.649  59.638  13.319  1.00144.15           C  
ANISOU  327  CB  GLN A  70    24139  14840  15793  -1196  -3960   3176       C  
ATOM    328  CG  GLN A  70      41.347  60.422  13.175  1.00154.27           C  
ANISOU  328  CG  GLN A  70    25529  15693  17395   -911  -4301   3312       C  
ATOM    329  CD  GLN A  70      40.164  59.775  13.864  1.00169.11           C  
ANISOU  329  CD  GLN A  70    27223  17577  19455   -443  -4232   2955       C  
ATOM    330  OE1 GLN A  70      39.526  58.879  13.312  1.00176.50           O  
ANISOU  330  OE1 GLN A  70    28012  18855  20194   -348  -4177   2948       O  
ATOM    331  NE2 GLN A  70      39.855  60.237  15.072  1.00177.10           N  
ANISOU  331  NE2 GLN A  70    28246  18211  20831   -174  -4225   2646       N  
ATOM    332  N   THR A  71      45.592  59.222  13.944  1.00 99.41           N  
ANISOU  332  N   THR A  71    18332   9590   9848  -1833  -3499   3048       N  
ATOM    333  CA  THR A  71      46.840  58.467  13.855  1.00 98.07           C  
ANISOU  333  CA  THR A  71    17963   9844   9455  -2103  -3201   2986       C  
ATOM    334  C   THR A  71      47.463  58.288  15.228  1.00123.98           C  
ANISOU  334  C   THR A  71    21134  13049  12926  -2027  -3105   2677       C  
ATOM    335  O   THR A  71      48.005  57.232  15.553  1.00110.22           O  
ANISOU  335  O   THR A  71    19141  11647  11092  -2009  -2857   2469       O  
ATOM    336  CB  THR A  71      47.875  59.165  12.941  1.00101.89           C  
ANISOU  336  CB  THR A  71    18542  10392   9779  -2601  -3223   3361       C  
ATOM    337  OG1 THR A  71      47.365  59.263  11.607  1.00106.14           O  
ANISOU  337  OG1 THR A  71    19200  11064  10065  -2740  -3310   3675       O  
ATOM    338  CG2 THR A  71      49.197  58.402  12.929  1.00100.93           C  
ANISOU  338  CG2 THR A  71    18153  10697   9498  -2857  -2890   3260       C  
ATOM    339  N   LEU A  72      47.369  59.334  16.038  1.00126.02           N  
ANISOU  339  N   LEU A  72    21588  12837  13458  -1991  -3320   2649       N  
ATOM    340  CA  LEU A  72      47.964  59.320  17.359  1.00124.67           C  
ANISOU  340  CA  LEU A  72    21368  12564  13435  -1982  -3278   2378       C  
ATOM    341  C   LEU A  72      47.235  58.368  18.301  1.00120.85           C  
ANISOU  341  C   LEU A  72    20755  12181  12984  -1604  -3156   1994       C  
ATOM    342  O   LEU A  72      47.865  57.511  18.918  1.00135.82           O  
ANISOU  342  O   LEU A  72    22449  14340  14815  -1627  -2991   1813       O  
ATOM    343  CB  LEU A  72      47.979  60.737  17.934  1.00127.17           C  
ANISOU  343  CB  LEU A  72    21973  12326  14020  -2062  -3538   2422       C  
ATOM    344  CG  LEU A  72      49.364  61.232  18.346  1.00125.64           C  
ANISOU  344  CG  LEU A  72    21789  12094  13856  -2459  -3559   2491       C  
ATOM    345  CD1 LEU A  72      50.355  61.047  17.207  1.00120.50           C  
ANISOU  345  CD1 LEU A  72    20995  11801  12987  -2841  -3446   2818       C  
ATOM    346  CD2 LEU A  72      49.289  62.681  18.764  1.00136.29           C  
ANISOU  346  CD2 LEU A  72    23464  12853  15469  -2554  -3833   2549       C  
ATOM    347  N   LEU A  73      45.914  58.500  18.391  1.00109.60           N  
ANISOU  347  N   LEU A  73    19423  10550  11669  -1269  -3244   1889       N  
ATOM    348  CA  LEU A  73      45.121  57.621  19.253  1.00104.43           C  
ANISOU  348  CA  LEU A  73    18650   9997  11033   -929  -3118   1535       C  
ATOM    349  C   LEU A  73      45.191  56.167  18.806  1.00 99.59           C  
ANISOU  349  C   LEU A  73    17773   9886  10182   -883  -2890   1489       C  
ATOM    350  O   LEU A  73      45.210  55.250  19.628  1.00 92.63           O  
ANISOU  350  O   LEU A  73    16746   9182   9268   -762  -2747   1233       O  
ATOM    351  CB  LEU A  73      43.660  58.062  19.303  1.00102.15           C  
ANISOU  351  CB  LEU A  73    18466   9410  10935   -586  -3240   1449       C  
ATOM    352  CG  LEU A  73      43.252  59.094  20.350  1.00102.64           C  
ANISOU  352  CG  LEU A  73    18729   8975  11296   -456  -3362   1237       C  
ATOM    353  CD1 LEU A  73      44.024  60.392  20.213  1.00113.69           C  
ANISOU  353  CD1 LEU A  73    20359  10002  12835   -739  -3561   1451       C  
ATOM    354  CD2 LEU A  73      41.763  59.337  20.242  1.00101.07           C  
ANISOU  354  CD2 LEU A  73    18538   8549  11313    -80  -3440   1153       C  
ATOM    355  N   TYR A  74      45.216  55.963  17.495  1.00107.51           N  
ANISOU  355  N   TYR A  74    18732  11104  11011   -999  -2863   1739       N  
ATOM    356  CA  TYR A  74      45.322  54.623  16.949  1.00118.34           C  
ANISOU  356  CA  TYR A  74    19874  12932  12159   -984  -2632   1681       C  
ATOM    357  C   TYR A  74      46.664  54.027  17.358  1.00118.04           C  
ANISOU  357  C   TYR A  74    19644  13124  12084  -1182  -2451   1607       C  
ATOM    358  O   TYR A  74      46.750  52.857  17.727  1.00126.09           O  
ANISOU  358  O   TYR A  74    20456  14389  13063  -1062  -2275   1406       O  
ATOM    359  CB  TYR A  74      45.166  54.646  15.422  1.00120.16           C  
ANISOU  359  CB  TYR A  74    20140  13347  12170  -1141  -2639   1962       C  
ATOM    360  CG  TYR A  74      43.812  55.142  14.942  1.00128.08           C  
ANISOU  360  CG  TYR A  74    21292  14147  13224   -944  -2862   2079       C  
ATOM    361  CD1 TYR A  74      42.746  55.293  15.824  1.00130.84           C  
ANISOU  361  CD1 TYR A  74    21666  14231  13814   -592  -2965   1871       C  
ATOM    362  CD2 TYR A  74      43.619  55.518  13.617  1.00138.78           C  
ANISOU  362  CD2 TYR A  74    22760  15570  14400  -1133  -2982   2411       C  
ATOM    363  CE1 TYR A  74      41.518  55.760  15.393  1.00141.43           C  
ANISOU  363  CE1 TYR A  74    23090  15376  15270   -394  -3179   1981       C  
ATOM    364  CE2 TYR A  74      42.391  55.987  13.177  1.00150.71           C  
ANISOU  364  CE2 TYR A  74    24385  16883  15996   -956  -3240   2558       C  
ATOM    365  CZ  TYR A  74      41.346  56.105  14.072  1.00150.33           C  
ANISOU  365  CZ  TYR A  74    24311  16561  16245   -569  -3339   2340       C  
ATOM    366  OH  TYR A  74      40.124  56.567  13.640  1.00156.33           O  
ANISOU  366  OH  TYR A  74    25130  17117  17152   -372  -3600   2486       O  
ATOM    367  N   LEU A  75      47.704  54.851  17.322  1.00 85.83           N  
ANISOU  367  N   LEU A  75    15622   8939   8051  -1487  -2515   1782       N  
ATOM    368  CA  LEU A  75      49.034  54.420  17.728  1.00 85.63           C  
ANISOU  368  CA  LEU A  75    15382   9106   8047  -1693  -2382   1742       C  
ATOM    369  C   LEU A  75      49.115  54.149  19.228  1.00 87.43           C  
ANISOU  369  C   LEU A  75    15570   9222   8429  -1554  -2432   1489       C  
ATOM    370  O   LEU A  75      49.873  53.285  19.666  1.00 98.10           O  
ANISOU  370  O   LEU A  75    16675  10796   9801  -1590  -2314   1395       O  
ATOM    371  CB  LEU A  75      50.078  55.464  17.324  1.00 94.00           C  
ANISOU  371  CB  LEU A  75    16515  10070   9130  -2084  -2462   2010       C  
ATOM    372  CG  LEU A  75      51.532  54.988  17.295  1.00104.26           C  
ANISOU  372  CG  LEU A  75    17520  11659  10436  -2353  -2284   2040       C  
ATOM    373  CD1 LEU A  75      51.652  53.692  16.513  1.00105.03           C  
ANISOU  373  CD1 LEU A  75    17338  12184  10384  -2290  -1981   1962       C  
ATOM    374  CD2 LEU A  75      52.430  56.054  16.692  1.00 93.66           C  
ANISOU  374  CD2 LEU A  75    16255  10249   9082  -2771  -2347   2337       C  
ATOM    375  N   CYS A  76      48.339  54.893  20.012  1.00 88.25           N  
ANISOU  375  N   CYS A  76    15913   8974   8644  -1408  -2611   1380       N  
ATOM    376  CA  CYS A  76      48.330  54.722  21.464  1.00 93.34           C  
ANISOU  376  CA  CYS A  76    16576   9514   9376  -1319  -2659   1126       C  
ATOM    377  C   CYS A  76      47.799  53.354  21.887  1.00106.17           C  
ANISOU  377  C   CYS A  76    18019  11391  10929  -1067  -2510    913       C  
ATOM    378  O   CYS A  76      48.352  52.718  22.783  1.00 96.95           O  
ANISOU  378  O   CYS A  76    16726  10337   9773  -1106  -2492    799       O  
ATOM    379  CB  CYS A  76      47.503  55.825  22.126  1.00 84.51           C  
ANISOU  379  CB  CYS A  76    15762   7963   8383  -1208  -2830   1007       C  
ATOM    380  SG  CYS A  76      48.314  57.439  22.177  1.00 98.68           S  
ANISOU  380  SG  CYS A  76    17805   9368  10321  -1543  -3050   1186       S  
ATOM    381  N   SER A  77      46.721  52.911  21.246  1.00120.98           N  
ANISOU  381  N   SER A  77    19886  13344  12735   -829  -2431    879       N  
ATOM    382  CA  SER A  77      46.151  51.596  21.521  1.00111.47           C  
ANISOU  382  CA  SER A  77    18517  12374  11462   -607  -2289    695       C  
ATOM    383  C   SER A  77      47.037  50.484  20.993  1.00111.70           C  
ANISOU  383  C   SER A  77    18268  12742  11431   -703  -2121    753       C  
ATOM    384  O   SER A  77      47.183  49.441  21.627  1.00123.61           O  
ANISOU  384  O   SER A  77    19615  14398  12955   -623  -2047    619       O  
ATOM    385  CB  SER A  77      44.769  51.471  20.901  1.00107.06           C  
ANISOU  385  CB  SER A  77    18012  11807  10859   -358  -2269    659       C  
ATOM    386  OG  SER A  77      43.936  52.515  21.337  1.00109.01           O  
ANISOU  386  OG  SER A  77    18473  11717  11228   -237  -2413    597       O  
ATOM    387  N   ALA A  78      47.620  50.718  19.823  1.00 86.25           N  
ANISOU  387  N   ALA A  78    14991   9632   8149   -883  -2055    951       N  
ATOM    388  CA  ALA A  78      48.583  49.797  19.241  1.00 85.64           C  
ANISOU  388  CA  ALA A  78    14633   9861   8045  -1000  -1854    984       C  
ATOM    389  C   ALA A  78      49.761  49.615  20.188  1.00 99.02           C  
ANISOU  389  C   ALA A  78    16154  11566   9902  -1132  -1889    966       C  
ATOM    390  O   ALA A  78      50.393  48.561  20.216  1.00102.97           O  
ANISOU  390  O   ALA A  78    16374  12275  10477  -1116  -1751    908       O  
ATOM    391  CB  ALA A  78      49.051  50.304  17.890  1.00 96.00           C  
ANISOU  391  CB  ALA A  78    15955  11283   9239  -1235  -1772   1199       C  
ATOM    392  N   SER A  79      50.051  50.665  20.951  1.00110.30           N  
ANISOU  392  N   SER A  79    17752  12750  11407  -1268  -2092   1017       N  
ATOM    393  CA  SER A  79      51.130  50.655  21.934  1.00116.84           C  
ANISOU  393  CA  SER A  79    18454  13565  12375  -1436  -2195   1023       C  
ATOM    394  C   SER A  79      50.802  49.814  23.170  1.00103.02           C  
ANISOU  394  C   SER A  79    16666  11821  10655  -1267  -2257    839       C  
ATOM    395  O   SER A  79      51.704  49.268  23.811  1.00 92.01           O  
ANISOU  395  O   SER A  79    15060  10521   9378  -1363  -2310    858       O  
ATOM    396  CB  SER A  79      51.463  52.084  22.355  1.00114.92           C  
ANISOU  396  CB  SER A  79    18451  13040  12175  -1664  -2406   1119       C  
ATOM    397  OG  SER A  79      51.423  52.951  21.240  1.00101.85           O  
ANISOU  397  OG  SER A  79    16918  11315  10465  -1792  -2386   1301       O  
ATOM    398  N   ILE A  80      49.514  49.714  23.491  1.00 92.88           N  
ANISOU  398  N   ILE A  80    15576  10442   9273  -1034  -2262    679       N  
ATOM    399  CA  ILE A  80      49.055  49.052  24.711  1.00 86.29           C  
ANISOU  399  CA  ILE A  80    14768   9603   8417   -911  -2321    505       C  
ATOM    400  C   ILE A  80      49.588  47.634  24.823  1.00 88.04           C  
ANISOU  400  C   ILE A  80    14680  10059   8711   -864  -2243    510       C  
ATOM    401  O   ILE A  80      50.082  47.233  25.877  1.00 93.59           O  
ANISOU  401  O   ILE A  80    15322  10773   9467   -943  -2375    503       O  
ATOM    402  CB  ILE A  80      47.521  49.014  24.783  1.00 86.76           C  
ANISOU  402  CB  ILE A  80    15012   9583   8369   -653  -2266    331       C  
ATOM    403  CG1 ILE A  80      46.966  50.437  24.791  1.00106.81           C  
ANISOU  403  CG1 ILE A  80    17841  11831  10911   -665  -2363    307       C  
ATOM    404  CG2 ILE A  80      47.060  48.263  26.020  1.00 81.32           C  
ANISOU  404  CG2 ILE A  80    14345   8931   7623   -569  -2294    157       C  
ATOM    405  CD1 ILE A  80      45.486  50.514  25.056  1.00121.45           C  
ANISOU  405  CD1 ILE A  80    19846  13576  12723   -409  -2324    112       C  
ATOM    406  N   THR A  81      49.492  46.883  23.732  1.00 87.35           N  
ANISOU  406  N   THR A  81    14410  10146   8634   -748  -2043    526       N  
ATOM    407  CA  THR A  81      49.957  45.503  23.718  1.00100.72           C  
ANISOU  407  CA  THR A  81    15801  12021  10448   -671  -1944    506       C  
ATOM    408  C   THR A  81      51.466  45.436  23.987  1.00109.06           C  
ANISOU  408  C   THR A  81    16590  13127  11719   -870  -2017    644       C  
ATOM    409  O   THR A  81      51.950  44.494  24.619  1.00107.20           O  
ANISOU  409  O   THR A  81    16142  12945  11645   -838  -2079    651       O  
ATOM    410  CB  THR A  81      49.622  44.799  22.388  1.00112.28           C  
ANISOU  410  CB  THR A  81    17136  13651  11873   -542  -1687    462       C  
ATOM    411  OG1 THR A  81      50.227  43.502  22.369  1.00133.81           O  
ANISOU  411  OG1 THR A  81    19552  16509  14782   -475  -1581    425       O  
ATOM    412  CG2 THR A  81      50.127  45.599  21.198  1.00113.64           C  
ANISOU  412  CG2 THR A  81    17301  13879  11997   -707  -1579    582       C  
ATOM    413  N   ASP A  82      52.207  46.429  23.504  1.00120.26           N  
ANISOU  413  N   ASP A  82    18007  14524  13164  -1085  -2028    772       N  
ATOM    414  CA  ASP A  82      53.638  46.496  23.773  1.00126.20           C  
ANISOU  414  CA  ASP A  82    18487  15327  14136  -1302  -2113    912       C  
ATOM    415  C   ASP A  82      53.864  46.986  25.198  1.00129.45           C  
ANISOU  415  C   ASP A  82    19047  15585  14553  -1447  -2430    946       C  
ATOM    416  O   ASP A  82      53.000  47.637  25.780  1.00126.18           O  
ANISOU  416  O   ASP A  82    18988  15005  13950  -1430  -2541    855       O  
ATOM    417  CB  ASP A  82      54.349  47.411  22.777  1.00134.07           C  
ANISOU  417  CB  ASP A  82    19435  16366  15139  -1529  -2010   1047       C  
ATOM    418  CG  ASP A  82      55.862  47.303  22.867  1.00144.59           C  
ANISOU  418  CG  ASP A  82    20386  17808  16743  -1740  -2034   1182       C  
ATOM    419  OD1 ASP A  82      56.457  47.936  23.768  1.00142.51           O  
ANISOU  419  OD1 ASP A  82    20159  17435  16553  -1946  -2298   1282       O  
ATOM    420  OD2 ASP A  82      56.455  46.577  22.040  1.00152.51           O  
ANISOU  420  OD2 ASP A  82    21041  19010  17897  -1707  -1783   1173       O  
ATOM    421  N   ILE A  83      55.024  46.671  25.762  1.00142.21           N  
ANISOU  421  N   ILE A  83    20383  17259  16392  -1598  -2577   1067       N  
ATOM    422  CA  ILE A  83      55.340  47.111  27.115  1.00148.40           C  
ANISOU  422  CA  ILE A  83    21307  17926  17152  -1795  -2909   1116       C  
ATOM    423  C   ILE A  83      56.286  48.313  27.127  1.00142.07           C  
ANISOU  423  C   ILE A  83    20520  17054  16405  -2129  -3049   1254       C  
ATOM    424  O   ILE A  83      56.107  49.241  27.917  1.00146.53           O  
ANISOU  424  O   ILE A  83    21410  17445  16820  -2305  -3257   1224       O  
ATOM    425  CB  ILE A  83      55.960  45.962  27.953  1.00131.60           C  
ANISOU  425  CB  ILE A  83    18885  15886  15230  -1778  -3083   1199       C  
ATOM    426  CG1 ILE A  83      57.065  45.243  27.175  1.00135.14           C  
ANISOU  426  CG1 ILE A  83    18811  16492  16044  -1748  -2947   1314       C  
ATOM    427  CG2 ILE A  83      54.884  44.986  28.396  1.00127.86           C  
ANISOU  427  CG2 ILE A  83    18539  15412  14630  -1530  -3051   1067       C  
ATOM    428  CD1 ILE A  83      58.440  45.408  27.787  1.00140.02           C  
ANISOU  428  CD1 ILE A  83    19133  17137  16931  -2011  -3218   1522       C  
ATOM    429  N   SER A  84      57.270  48.320  26.234  1.00126.18           N  
ANISOU  429  N   SER A  84    18166  15174  14602  -2232  -2915   1387       N  
ATOM    430  CA  SER A  84      58.303  49.348  26.276  1.00123.98           C  
ANISOU  430  CA  SER A  84    17836  14856  14414  -2586  -3060   1548       C  
ATOM    431  C   SER A  84      57.769  50.736  25.907  1.00114.87           C  
ANISOU  431  C   SER A  84    17101  13503  13041  -2718  -3053   1529       C  
ATOM    432  O   SER A  84      58.463  51.741  26.076  1.00 98.33           O  
ANISOU  432  O   SER A  84    15069  11308  10982  -3037  -3213   1647       O  
ATOM    433  CB  SER A  84      59.455  48.968  25.340  1.00125.83           C  
ANISOU  433  CB  SER A  84    17564  15310  14935  -2664  -2862   1679       C  
ATOM    434  OG  SER A  84      60.538  49.875  25.456  1.00136.69           O  
ANISOU  434  OG  SER A  84    18831  16674  16432  -3034  -3017   1854       O  
ATOM    435  N   LEU A  85      56.529  50.791  25.430  1.00111.21           N  
ANISOU  435  N   LEU A  85    16918  12961  12377  -2478  -2895   1392       N  
ATOM    436  CA  LEU A  85      55.901  52.056  25.051  1.00110.41           C  
ANISOU  436  CA  LEU A  85    17207  12628  12116  -2550  -2908   1384       C  
ATOM    437  C   LEU A  85      54.551  52.325  25.721  1.00117.40           C  
ANISOU  437  C   LEU A  85    18497  13289  12818  -2346  -2981   1176       C  
ATOM    438  O   LEU A  85      54.002  53.418  25.604  1.00132.10           O  
ANISOU  438  O   LEU A  85    20689  14896  14605  -2385  -3034   1148       O  
ATOM    439  CB  LEU A  85      55.731  52.117  23.530  1.00115.49           C  
ANISOU  439  CB  LEU A  85    17784  13382  12715  -2501  -2638   1468       C  
ATOM    440  CG  LEU A  85      57.000  51.984  22.683  1.00117.84           C  
ANISOU  440  CG  LEU A  85    17697  13916  13161  -2729  -2486   1647       C  
ATOM    441  CD1 LEU A  85      56.620  52.022  21.222  1.00113.98           C  
ANISOU  441  CD1 LEU A  85    17227  13548  12533  -2691  -2210   1695       C  
ATOM    442  CD2 LEU A  85      58.020  53.071  23.000  1.00130.18           C  
ANISOU  442  CD2 LEU A  85    19272  15367  14825  -3126  -2685   1820       C  
ATOM    443  N   GLN A  86      54.010  51.324  26.405  1.00122.03           N  
ANISOU  443  N   GLN A  86    19045  13963  13358  -2131  -2973   1031       N  
ATOM    444  CA  GLN A  86      52.654  51.408  26.945  1.00125.08           C  
ANISOU  444  CA  GLN A  86    19754  14198  13573  -1913  -2970    810       C  
ATOM    445  C   GLN A  86      52.399  52.553  27.930  1.00111.69           C  
ANISOU  445  C   GLN A  86    18434  12211  11791  -2068  -3163    686       C  
ATOM    446  O   GLN A  86      51.385  53.245  27.824  1.00103.96           O  
ANISOU  446  O   GLN A  86    17739  11014  10746  -1931  -3116    547       O  
ATOM    447  CB  GLN A  86      52.287  50.095  27.644  1.00139.14           C  
ANISOU  447  CB  GLN A  86    21410  16143  15313  -1733  -2951    705       C  
ATOM    448  CG  GLN A  86      50.802  49.957  27.950  1.00134.64           C  
ANISOU  448  CG  GLN A  86    21089  15493  14574  -1476  -2862    479       C  
ATOM    449  CD  GLN A  86      50.488  48.705  28.744  1.00125.36           C  
ANISOU  449  CD  GLN A  86    19819  14472  13339  -1363  -2867    399       C  
ATOM    450  OE1 GLN A  86      50.569  48.705  29.970  1.00122.82           O  
ANISOU  450  OE1 GLN A  86    19629  14118  12917  -1504  -3035    335       O  
ATOM    451  NE2 GLN A  86      50.130  47.633  28.051  1.00121.99           N  
ANISOU  451  NE2 GLN A  86    19183  14211  12957  -1138  -2693    406       N  
ATOM    452  N   TYR A  87      53.312  52.754  28.876  1.00105.33           N  
ANISOU  452  N   TYR A  87    17624  11392  11005  -2356  -3384    728       N  
ATOM    453  CA  TYR A  87      53.066  53.680  29.977  1.00105.63           C  
ANISOU  453  CA  TYR A  87    18037  11178  10922  -2527  -3560    552       C  
ATOM    454  C   TYR A  87      52.840  55.126  29.554  1.00127.66           C  
ANISOU  454  C   TYR A  87    21118  13633  13755  -2609  -3577    522       C  
ATOM    455  O   TYR A  87      51.949  55.791  30.079  1.00138.35           O  
ANISOU  455  O   TYR A  87    22811  14728  15028  -2532  -3576    279       O  
ATOM    456  CB  TYR A  87      54.228  53.650  30.971  1.00105.51           C  
ANISOU  456  CB  TYR A  87    17948  11232  10910  -2884  -3832    645       C  
ATOM    457  CG  TYR A  87      55.565  54.072  30.406  1.00108.19           C  
ANISOU  457  CG  TYR A  87    18046  11612  11450  -3166  -3937    913       C  
ATOM    458  CD1 TYR A  87      56.303  53.218  29.601  1.00108.38           C  
ANISOU  458  CD1 TYR A  87    17612  11904  11664  -3111  -3836   1129       C  
ATOM    459  CD2 TYR A  87      56.076  55.340  30.659  1.00112.02           C  
ANISOU  459  CD2 TYR A  87    18755  11858  11948  -3496  -4115    931       C  
ATOM    460  CE1 TYR A  87      57.525  53.603  29.087  1.00113.90           C  
ANISOU  460  CE1 TYR A  87    18054  12666  12556  -3381  -3895   1359       C  
ATOM    461  CE2 TYR A  87      57.295  55.737  30.143  1.00114.44           C  
ANISOU  461  CE2 TYR A  87    18826  12216  12439  -3785  -4205   1186       C  
ATOM    462  CZ  TYR A  87      58.016  54.862  29.357  1.00110.01           C  
ANISOU  462  CZ  TYR A  87    17781  11956  12060  -3726  -4084   1401       C  
ATOM    463  OH  TYR A  87      59.233  55.241  28.838  1.00103.13           O  
ANISOU  463  OH  TYR A  87    16635  11166  11384  -4023  -4136   1642       O  
ATOM    464  N   LEU A  88      53.642  55.615  28.616  1.00137.09           N  
ANISOU  464  N   LEU A  88    22176  14820  15092  -2774  -3588    765       N  
ATOM    465  CA  LEU A  88      53.450  56.959  28.081  1.00135.85           C  
ANISOU  465  CA  LEU A  88    22288  14328  15001  -2863  -3623    799       C  
ATOM    466  C   LEU A  88      52.134  57.085  27.306  1.00122.21           C  
ANISOU  466  C   LEU A  88    20695  12473  13265  -2508  -3453    721       C  
ATOM    467  O   LEU A  88      51.474  58.126  27.355  1.00126.84           O  
ANISOU  467  O   LEU A  88    21599  12694  13903  -2465  -3506    614       O  
ATOM    468  CB  LEU A  88      54.644  57.361  27.212  1.00148.13           C  
ANISOU  468  CB  LEU A  88    23642  15954  16686  -3160  -3662   1113       C  
ATOM    469  CG  LEU A  88      55.004  56.540  25.980  1.00149.71           C  
ANISOU  469  CG  LEU A  88    23462  16489  16930  -3075  -3450   1325       C  
ATOM    470  CD1 LEU A  88      54.423  57.192  24.745  1.00166.36           C  
ANISOU  470  CD1 LEU A  88    25716  18462  19031  -2999  -3342   1444       C  
ATOM    471  CD2 LEU A  88      56.512  56.411  25.858  1.00138.46           C  
ANISOU  471  CD2 LEU A  88    21698  15278  15635  -3412  -3506   1547       C  
ATOM    472  N   ALA A  89      51.754  56.015  26.613  1.00111.06           N  
ANISOU  472  N   ALA A  89    19036  11349  11815  -2257  -3263    769       N  
ATOM    473  CA  ALA A  89      50.538  56.005  25.806  1.00109.50           C  
ANISOU  473  CA  ALA A  89    18915  11086  11602  -1939  -3124    730       C  
ATOM    474  C   ALA A  89      49.315  56.264  26.677  1.00113.20           C  
ANISOU  474  C   ALA A  89    19646  11322  12041  -1708  -3127    418       C  
ATOM    475  O   ALA A  89      48.371  56.921  26.241  1.00122.36           O  
ANISOU  475  O   ALA A  89    20979  12235  13278  -1521  -3112    372       O  
ATOM    476  CB  ALA A  89      50.388  54.679  25.071  1.00100.33           C  
ANISOU  476  CB  ALA A  89    17444  10299  10379  -1744  -2925    792       C  
ATOM    477  N   ILE A  90      49.333  55.729  27.897  1.00100.75           N  
ANISOU  477  N   ILE A  90    18083   9836  10360  -1731  -3146    212       N  
ATOM    478  CA  ILE A  90      48.247  55.921  28.856  1.00 98.45           C  
ANISOU  478  CA  ILE A  90    18030   9373  10005  -1562  -3106   -126       C  
ATOM    479  C   ILE A  90      48.228  57.396  29.242  1.00111.91           C  
ANISOU  479  C   ILE A  90    20070  10638  11812  -1703  -3231   -247       C  
ATOM    480  O   ILE A  90      47.176  58.023  29.215  1.00133.06           O  
ANISOU  480  O   ILE A  90    22931  13035  14590  -1480  -3171   -434       O  
ATOM    481  CB  ILE A  90      48.395  55.040  30.116  1.00104.08           C  
ANISOU  481  CB  ILE A  90    18711  10304  10529  -1644  -3116   -289       C  
ATOM    482  CG1 ILE A  90      48.331  53.556  29.761  1.00 98.98           C  
ANISOU  482  CG1 ILE A  90    17746  10034   9826  -1480  -3000   -181       C  
ATOM    483  CG2 ILE A  90      47.277  55.347  31.082  1.00 99.82           C  
ANISOU  483  CG2 ILE A  90    18436   9595   9895  -1515  -3033   -661       C  
ATOM    484  CD1 ILE A  90      49.445  52.755  30.428  1.00 91.52           C  
ANISOU  484  CD1 ILE A  90    16623   9331   8822  -1719  -3132    -58       C  
ATOM    485  N   ASP A  91      49.388  57.936  29.628  1.00115.23           N  
ANISOU  485  N   ASP A  91    20558  10987  12236  -2073  -3411   -151       N  
ATOM    486  CA  ASP A  91      49.493  59.336  30.061  1.00123.99           C  
ANISOU  486  CA  ASP A  91    22009  11657  13445  -2262  -3550   -278       C  
ATOM    487  C   ASP A  91      49.121  60.301  28.949  1.00126.27           C  
ANISOU  487  C   ASP A  91    22394  11618  13966  -2152  -3568   -123       C  
ATOM    488  O   ASP A  91      48.360  61.251  29.151  1.00124.69           O  
ANISOU  488  O   ASP A  91    22466  10998  13913  -2030  -3581   -328       O  
ATOM    489  CB  ASP A  91      50.911  59.661  30.524  1.00127.21           C  
ANISOU  489  CB  ASP A  91    22424  12090  13818  -2721  -3764   -140       C  
ATOM    490  CG  ASP A  91      51.007  59.827  32.025  1.00146.23           C  
ANISOU  490  CG  ASP A  91    25076  14432  16054  -2933  -3859   -449       C  
ATOM    491  OD1 ASP A  91      49.972  60.143  32.659  1.00155.45           O  
ANISOU  491  OD1 ASP A  91    26500  15391  17173  -2758  -3748   -812       O  
ATOM    492  OD2 ASP A  91      52.116  59.643  32.572  1.00155.56           O  
ANISOU  492  OD2 ASP A  91    26183  15778  17144  -3288  -4043   -334       O  
ATOM    493  N   ARG A  92      49.662  60.039  27.766  1.00121.42           N  
ANISOU  493  N   ARG A  92    21551  11195  13391  -2202  -3569    242       N  
ATOM    494  CA  ARG A  92      49.418  60.887  26.603  1.00116.83           C  
ANISOU  494  CA  ARG A  92    21053  10353  12984  -2162  -3619    474       C  
ATOM    495  C   ARG A  92      48.039  60.688  25.981  1.00112.63           C  
ANISOU  495  C   ARG A  92    20508   9770  12517  -1739  -3503    422       C  
ATOM    496  O   ARG A  92      47.408  61.650  25.555  1.00120.29           O  
ANISOU  496  O   ARG A  92    21670  10344  13689  -1627  -3590    456       O  
ATOM    497  CB  ARG A  92      50.518  60.676  25.567  1.00123.94           C  
ANISOU  497  CB  ARG A  92    21722  11518  13853  -2424  -3636    873       C  
ATOM    498  CG  ARG A  92      51.774  61.424  25.968  1.00132.50           C  
ANISOU  498  CG  ARG A  92    22885  12475  14983  -2872  -3816    978       C  
ATOM    499  CD  ARG A  92      51.594  62.905  25.611  1.00139.21           C  
ANISOU  499  CD  ARG A  92    24065  12798  16028  -2986  -3982   1070       C  
ATOM    500  NE  ARG A  92      52.053  63.783  26.681  1.00150.28           N  
ANISOU  500  NE  ARG A  92    25735  13866  17499  -3254  -4157    883       N  
ATOM    501  CZ  ARG A  92      53.301  64.230  26.792  1.00154.02           C  
ANISOU  501  CZ  ARG A  92    26196  14341  17985  -3703  -4308   1058       C  
ATOM    502  NH1 ARG A  92      54.228  63.821  25.942  1.00148.43           N  
ANISOU  502  NH1 ARG A  92    25183  13980  17234  -3916  -4272   1407       N  
ATOM    503  NH2 ARG A  92      53.633  65.056  27.774  1.00155.38           N  
ANISOU  503  NH2 ARG A  92    26646  14184  18207  -3955  -4481    863       N  
ATOM    504  N   GLY A  93      47.566  59.450  25.935  1.00108.80           N  
ANISOU  504  N   GLY A  93    19790   9663  11887  -1510  -3331    352       N  
ATOM    505  CA  GLY A  93      46.332  59.143  25.234  1.00102.88           C  
ANISOU  505  CA  GLY A  93    18976   8931  11183  -1144  -3234    347       C  
ATOM    506  C   GLY A  93      45.096  59.946  25.601  1.00 98.46           C  
ANISOU  506  C   GLY A  93    18627   7951  10833   -866  -3255    101       C  
ATOM    507  O   GLY A  93      44.334  60.353  24.726  1.00 94.85           O  
ANISOU  507  O   GLY A  93    18182   7318  10537   -669  -3309    241       O  
ATOM    508  N   PHE A  94      44.891  60.177  26.891  1.00119.08           N  
ANISOU  508  N   PHE A  94    21394  10402  13449   -858  -3215   -269       N  
ATOM    509  CA  PHE A  94      43.728  60.933  27.344  1.00135.46           C  
ANISOU  509  CA  PHE A  94    23644  12070  15754   -585  -3184   -576       C  
ATOM    510  C   PHE A  94      43.809  62.416  26.993  1.00142.68           C  
ANISOU  510  C   PHE A  94    24808  12425  16980   -651  -3381   -480       C  
ATOM    511  O   PHE A  94      42.848  62.989  26.482  1.00144.07           O  
ANISOU  511  O   PHE A  94    25015  12285  17442   -367  -3425   -467       O  
ATOM    512  CB  PHE A  94      43.546  60.758  28.851  1.00147.61           C  
ANISOU  512  CB  PHE A  94    25300  13622  17162   -611  -3049  -1031       C  
ATOM    513  CG  PHE A  94      43.274  59.343  29.257  1.00145.37           C  
ANISOU  513  CG  PHE A  94    24798  13831  16606   -523  -2868  -1131       C  
ATOM    514  CD1 PHE A  94      42.021  58.784  29.085  1.00146.95           C  
ANISOU  514  CD1 PHE A  94    24845  14139  16852   -163  -2701  -1262       C  
ATOM    515  CD2 PHE A  94      44.283  58.567  29.793  1.00145.14           C  
ANISOU  515  CD2 PHE A  94    24701  14145  16301   -809  -2889  -1068       C  
ATOM    516  CE1 PHE A  94      41.782  57.479  29.449  1.00151.94           C  
ANISOU  516  CE1 PHE A  94    25289  15203  17237   -111  -2547  -1335       C  
ATOM    517  CE2 PHE A  94      44.053  57.265  30.156  1.00151.13           C  
ANISOU  517  CE2 PHE A  94    25270  15314  16838   -737  -2753  -1126       C  
ATOM    518  CZ  PHE A  94      42.802  56.720  29.987  1.00151.72           C  
ANISOU  518  CZ  PHE A  94    25222  15485  16940   -397  -2577  -1263       C  
ATOM    519  N   GLU A  95      44.940  63.043  27.306  1.00151.94           N  
ANISOU  519  N   GLU A  95    26154  13453  18123  -1030  -3519   -409       N  
ATOM    520  CA  GLU A  95      45.137  64.461  27.011  1.00160.26           C  
ANISOU  520  CA  GLU A  95    27472  13949  19472  -1152  -3727   -300       C  
ATOM    521  C   GLU A  95      45.152  64.728  25.502  1.00148.19           C  
ANISOU  521  C   GLU A  95    25865  12377  18064  -1142  -3878    194       C  
ATOM    522  O   GLU A  95      44.551  65.694  25.033  1.00144.98           O  
ANISOU  522  O   GLU A  95    25608  11495  17983   -998  -4024    280       O  
ATOM    523  CB  GLU A  95      46.424  64.978  27.664  1.00180.64           C  
ANISOU  523  CB  GLU A  95    30236  16440  21959  -1617  -3851   -311       C  
ATOM    524  CG  GLU A  95      47.652  64.106  27.464  1.00193.07           C  
ANISOU  524  CG  GLU A  95    31583  18539  23236  -1939  -3857    -38       C  
ATOM    525  CD  GLU A  95      48.880  64.677  28.145  1.00210.15           C  
ANISOU  525  CD  GLU A  95    33906  20596  25346  -2405  -4012    -45       C  
ATOM    526  OE1 GLU A  95      48.723  65.543  29.029  1.00218.77           O  
ANISOU  526  OE1 GLU A  95    35305  21274  26544  -2477  -4073   -360       O  
ATOM    527  OE2 GLU A  95      50.003  64.262  27.801  1.00214.64           O  
ANISOU  527  OE2 GLU A  95    34283  21494  25778  -2707  -4068    248       O  
ATOM    528  N   ILE A  96      45.847  63.872  24.754  1.00144.64           N  
ANISOU  528  N   ILE A  96    25184  12418  17354  -1310  -3843    515       N  
ATOM    529  CA  ILE A  96      45.909  63.974  23.294  1.00136.06           C  
ANISOU  529  CA  ILE A  96    24020  11397  16280  -1358  -3948    981       C  
ATOM    530  C   ILE A  96      44.512  63.868  22.701  1.00130.55           C  
ANISOU  530  C   ILE A  96    23259  10610  15733   -938  -3946    991       C  
ATOM    531  O   ILE A  96      44.148  64.615  21.794  1.00132.84           O  
ANISOU  531  O   ILE A  96    23646  10607  16219   -905  -4142   1288       O  
ATOM    532  CB  ILE A  96      46.802  62.881  22.678  1.00130.39           C  
ANISOU  532  CB  ILE A  96    23026  11283  15233  -1572  -3826   1221       C  
ATOM    533  CG1 ILE A  96      48.271  63.136  23.016  1.00157.83           C  
ANISOU  533  CG1 ILE A  96    26521  14821  18624  -2025  -3879   1317       C  
ATOM    534  CG2 ILE A  96      46.624  62.827  21.171  1.00109.88           C  
ANISOU  534  CG2 ILE A  96    20350   8817  12581  -1586  -3876   1633       C  
ATOM    535  CD1 ILE A  96      49.214  62.125  22.405  1.00163.97           C  
ANISOU  535  CD1 ILE A  96    26990  16161  19150  -2230  -3741   1536       C  
ATOM    536  N   PHE A  97      43.738  62.928  23.231  1.00131.30           N  
ANISOU  536  N   PHE A  97    23183  10963  15740   -637  -3746    686       N  
ATOM    537  CA  PHE A  97      42.366  62.710  22.796  1.00127.45           C  
ANISOU  537  CA  PHE A  97    22585  10439  15400   -230  -3727    652       C  
ATOM    538  C   PHE A  97      41.561  63.983  22.989  1.00126.68           C  
ANISOU  538  C   PHE A  97    22688   9696  15750    -16  -3887    545       C  
ATOM    539  O   PHE A  97      40.910  64.465  22.072  1.00123.71           O  
ANISOU  539  O   PHE A  97    22311   9092  15601    138  -4074    814       O  
ATOM    540  CB  PHE A  97      41.741  61.558  23.588  1.00129.04           C  
ANISOU  540  CB  PHE A  97    22592  10992  15445      9  -3468    283       C  
ATOM    541  CG  PHE A  97      40.245  61.467  23.471  1.00120.73           C  
ANISOU  541  CG  PHE A  97    21427   9836  14609    438  -3430    138       C  
ATOM    542  CD1 PHE A  97      39.655  60.828  22.396  1.00103.37           C  
ANISOU  542  CD1 PHE A  97    19029   7904  12344    580  -3460    392       C  
ATOM    543  CD2 PHE A  97      39.427  62.011  24.450  1.00128.61           C  
ANISOU  543  CD2 PHE A  97    22506  10482  15879    685  -3353   -272       C  
ATOM    544  CE1 PHE A  97      38.283  60.735  22.293  1.00102.57           C  
ANISOU  544  CE1 PHE A  97    18789   7722  12462    960  -3449    275       C  
ATOM    545  CE2 PHE A  97      38.054  61.925  24.353  1.00128.23           C  
ANISOU  545  CE2 PHE A  97    22301  10349  16073   1085  -3304   -412       C  
ATOM    546  CZ  PHE A  97      37.480  61.282  23.272  1.00113.90           C  
ANISOU  546  CZ  PHE A  97    20264   8806  14207   1224  -3369   -122       C  
ATOM    547  N   ASP A  98      41.656  64.547  24.184  1.00141.37           N  
ANISOU  547  N   ASP A  98    24727  11245  17742    -30  -3827    157       N  
ATOM    548  CA  ASP A  98      40.879  65.721  24.549  1.00155.47           C  
ANISOU  548  CA  ASP A  98    26695  12383  19992    203  -3922    -57       C  
ATOM    549  C   ASP A  98      41.285  66.965  23.757  1.00161.17           C  
ANISOU  549  C   ASP A  98    27639  12603  20995     28  -4246    330       C  
ATOM    550  O   ASP A  98      40.496  67.902  23.613  1.00153.48           O  
ANISOU  550  O   ASP A  98    26762  11070  20483    279  -4399    310       O  
ATOM    551  CB  ASP A  98      41.003  65.977  26.051  1.00155.00           C  
ANISOU  551  CB  ASP A  98    26806  12153  19936    159  -3746   -604       C  
ATOM    552  CG  ASP A  98      40.015  65.156  26.857  1.00148.96           C  
ANISOU  552  CG  ASP A  98    25863  11637  19096    475  -3449  -1049       C  
ATOM    553  OD1 ASP A  98      38.981  64.748  26.284  1.00150.21           O  
ANISOU  553  OD1 ASP A  98    25790  11894  19388    818  -3415   -982       O  
ATOM    554  OD2 ASP A  98      40.271  64.905  28.054  1.00144.29           O  
ANISOU  554  OD2 ASP A  98    25363  11163  18297    350  -3259  -1448       O  
ATOM    555  N   ARG A  99      42.518  66.978  23.257  1.00170.27           N  
ANISOU  555  N   ARG A  99    28858  13942  21894   -408  -4352    684       N  
ATOM    556  CA  ARG A  99      42.987  68.076  22.418  1.00184.69           C  
ANISOU  556  CA  ARG A  99    30892  15358  23923   -647  -4660   1117       C  
ATOM    557  C   ARG A  99      42.251  68.487  21.139  1.00201.49           C  
ANISOU  557  C   ARG A  99    32998  17277  26282   -483  -4915   1561       C  
ATOM    558  O   ARG A  99      41.921  69.658  20.966  1.00225.17           O  
ANISOU  558  O   ARG A  99    36203  19638  29712   -419  -5168   1674       O  
ATOM    559  CB  ARG A  99      44.494  67.945  22.164  1.00180.45           C  
ANISOU  559  CB  ARG A  99    30391  15126  23045  -1181  -4683   1396       C  
ATOM    560  CG  ARG A  99      45.110  69.072  21.338  1.00181.82           C  
ANISOU  560  CG  ARG A  99    30793  14913  23378  -1517  -4986   1859       C  
ATOM    561  CD  ARG A  99      45.042  70.407  22.070  1.00181.31           C  
ANISOU  561  CD  ARG A  99    31057  14092  23740  -1527  -5153   1647       C  
ATOM    562  NE  ARG A  99      45.607  70.331  23.415  1.00184.47           N  
ANISOU  562  NE  ARG A  99    31539  14517  24035  -1665  -4987   1174       N  
ATOM    563  CZ  ARG A  99      46.890  70.531  23.704  1.00178.87           C  
ANISOU  563  CZ  ARG A  99    30928  13894  23141  -2148  -5029   1250       C  
ATOM    564  NH1 ARG A  99      47.754  70.821  22.740  1.00172.44           N  
ANISOU  564  NH1 ARG A  99    30128  13156  22236  -2536  -5194   1764       N  
ATOM    565  NH2 ARG A  99      47.311  70.441  24.958  1.00176.22           N  
ANISOU  565  NH2 ARG A  99    30670  13585  22699  -2268  -4911    818       N  
ATOM    566  N   MET A 100      42.010  67.533  20.241  1.00194.12           N  
ANISOU  566  N   MET A 100    31828  16862  25065   -437  -4868   1822       N  
ATOM    567  CA  MET A 100      41.096  67.803  19.099  1.00200.84           C  
ANISOU  567  CA  MET A 100    32636  17559  26117   -239  -5119   2207       C  
ATOM    568  C   MET A 100      39.494  67.493  19.169  1.00172.69           C  
ANISOU  568  C   MET A 100    28855  13915  22845    327  -5101   1997       C  
ATOM    569  O   MET A 100      38.609  67.830  18.382  1.00181.96           O  
ANISOU  569  O   MET A 100    29978  14871  24287    541  -5353   2276       O  
ATOM    570  CB  MET A 100      41.409  66.841  17.948  1.00200.00           C  
ANISOU  570  CB  MET A 100    32360  18091  25540   -446  -5085   2593       C  
ATOM    571  CG  MET A 100      40.624  67.011  16.668  1.00198.68           C  
ANISOU  571  CG  MET A 100    32304  18139  25047   -992  -5127   2975       C  
ATOM    572  SD  MET A 100      40.991  68.575  15.848  1.00406.58           S  
ANISOU  572  SD  MET A 100    58981  43801  51702  -1262  -5567   3484       S  
ATOM    573  CE  MET A 100      42.609  68.232  15.155  1.00173.35           C  
ANISOU  573  CE  MET A 100    29376  14248  22240  -1042  -5855   3925       C  
ATOM    574  N   VAL A 101      39.236  66.929  20.347  1.00155.27           N  
ANISOU  574  N   VAL A 101    26538  11850  20606    532  -4788   1444       N  
ATOM    575  CA  VAL A 101      37.861  66.712  20.785  1.00147.15           C  
ANISOU  575  CA  VAL A 101    25312  10720  19877   1031  -4686   1106       C  
ATOM    576  C   VAL A 101      37.494  68.182  20.988  1.00167.04           C  
ANISOU  576  C   VAL A 101    28041  12424  23004   1184  -4920   1070       C  
ATOM    577  O   VAL A 101      36.368  68.588  20.701  1.00178.58           O  
ANISOU  577  O   VAL A 101    29386  13544  24922   1564  -5072   1099       O  
ATOM    578  CB  VAL A 101      37.445  65.882  22.024  1.00136.73           C  
ANISOU  578  CB  VAL A 101    23833   9675  18441   1245  -4299    507       C  
ATOM    579  CG1 VAL A 101      35.964  66.033  22.300  1.00129.62           C  
ANISOU  579  CG1 VAL A 101    22745   8518  17987   1750  -4256    230       C  
ATOM    580  CG2 VAL A 101      37.762  64.420  21.803  1.00142.96           C  
ANISOU  580  CG2 VAL A 101    24414  11213  18691   1115  -4097    562       C  
ATOM    581  N   SER A 102      38.454  68.982  21.450  1.00178.48           N  
ANISOU  581  N   SER A 102    29786  13543  24486    882  -4967   1021       N  
ATOM    582  CA  SER A 102      38.236  70.411  21.680  1.00192.44           C  
ANISOU  582  CA  SER A 102    31796  14486  26836    981  -5188    967       C  
ATOM    583  C   SER A 102      37.815  71.119  20.390  1.00194.01           C  
ANISOU  583  C   SER A 102    31934  14447  27333   1024  -5561   1545       C  
ATOM    584  O   SER A 102      37.098  72.123  20.425  1.00184.36           O  
ANISOU  584  O   SER A 102    30629  12764  26657   1280  -5652   1484       O  
ATOM    585  CB  SER A 102      39.492  71.069  22.259  1.00196.88           C  
ANISOU  585  CB  SER A 102    32687  14824  27294    547  -5196    887       C  
ATOM    586  OG  SER A 102      39.316  72.461  22.446  1.00195.62           O  
ANISOU  586  OG  SER A 102    32636  14849  26844     86  -5409   1459       O  
ATOM    587  N   SER A 103      38.272  70.591  19.257  1.00198.68           N  
ANISOU  587  N   SER A 103    32515  15444  27530    744  -5726   2091       N  
ATOM    588  CA  SER A 103      37.929  71.130  17.940  1.00205.11           C  
ANISOU  588  CA  SER A 103    33226  16232  28475    695  -6045   2665       C  
ATOM    589  C   SER A 103      36.433  71.062  17.631  1.00208.56           C  
ANISOU  589  C   SER A 103    33356  16588  29297   1195  -6133   2651       C  
ATOM    590  O   SER A 103      35.947  71.741  16.725  1.00210.41           O  
ANISOU  590  O   SER A 103    33491  16666  29789   1226  -6417   3049       O  
ATOM    591  CB  SER A 103      38.699  70.381  16.852  1.00197.92           C  
ANISOU  591  CB  SER A 103    32345  15894  26961    272  -6115   3166       C  
ATOM    592  OG  SER A 103      40.092  70.421  17.091  1.00187.76           O  
ANISOU  592  OG  SER A 103    31286  14713  25341   -200  -6025   3202       O  
ATOM    593  N   GLY A 104      35.709  70.246  18.389  1.00206.10           N  
ANISOU  593  N   GLY A 104    32886  16396  29026   1566  -5892   2196       N  
ATOM    594  CA  GLY A 104      34.273  70.125  18.223  1.00199.91           C  
ANISOU  594  CA  GLY A 104    31766  15559  28633   2050  -5936   2124       C  
ATOM    595  C   GLY A 104      33.823  69.017  17.289  1.00183.41           C  
ANISOU  595  C   GLY A 104    29481  14013  26194   2070  -6034   2449       C  
ATOM    596  O   GLY A 104      32.628  68.874  17.034  1.00182.02           O  
ANISOU  596  O   GLY A 104    28996  13842  26321   2433  -6110   2450       O  
ATOM    597  N   ILE A 105      34.762  68.234  16.769  1.00173.96           N  
ANISOU  597  N   ILE A 105    28442  13290  24367   1670  -6019   2718       N  
ATOM    598  CA  ILE A 105      34.376  67.084  15.967  1.00182.35           C  
ANISOU  598  CA  ILE A 105    29272  14997  25017   1649  -5997   2921       C  
ATOM    599  C   ILE A 105      33.902  65.968  16.885  1.00181.84           C  
ANISOU  599  C   ILE A 105    28932  15355  24805   1907  -5563   2355       C  
ATOM    600  O   ILE A 105      34.591  65.615  17.846  1.00185.16           O  
ANISOU  600  O   ILE A 105    29413  15940  24998   1798  -5218   1955       O  
ATOM    601  CB  ILE A 105      35.528  66.563  15.063  1.00179.93           C  
ANISOU  601  CB  ILE A 105    29113  15213  24041   1103  -5996   3321       C  
ATOM    602  CG1 ILE A 105      35.156  65.190  14.482  1.00176.36           C  
ANISOU  602  CG1 ILE A 105    28411  15470  23127   1099  -5852   3354       C  
ATOM    603  CG2 ILE A 105      36.851  66.511  15.821  1.00158.98           C  
ANISOU  603  CG2 ILE A 105    26631  12669  21104    786  -5701   3072       C  
ATOM    604  CD1 ILE A 105      36.274  64.465  13.769  1.00157.27           C  
ANISOU  604  CD1 ILE A 105    26083  13633  20041    608  -5718   3585       C  
ATOM    605  N   SER A 106      32.716  65.431  16.605  1.00178.62           N  
ANISOU  605  N   SER A 106    28221  15112  24535   2231  -5605   2339       N  
ATOM    606  CA  SER A 106      32.217  64.313  17.388  1.00181.76           C  
ANISOU  606  CA  SER A 106    28351  15942  24769   2441  -5208   1850       C  
ATOM    607  C   SER A 106      33.226  63.214  17.140  1.00181.28           C  
ANISOU  607  C   SER A 106    28346  16534  23998   2047  -4989   1910       C  
ATOM    608  O   SER A 106      33.532  62.906  15.990  1.00181.45           O  
ANISOU  608  O   SER A 106    28408  16845  23688   1783  -5170   2354       O  
ATOM    609  CB  SER A 106      30.805  63.896  16.973  1.00182.31           C  
ANISOU  609  CB  SER A 106    28069  16115  25085   2799  -5326   1894       C  
ATOM    610  OG  SER A 106      30.303  62.871  17.817  1.00172.84           O  
ANISOU  610  OG  SER A 106    26617  15297  23757   2989  -4928   1403       O  
ATOM    611  N   PRO A 107      33.755  62.628  18.221  1.00174.18           N  
ANISOU  611  N   PRO A 107    27450  15859  22870   1996  -4600   1460       N  
ATOM    612  CA  PRO A 107      34.913  61.743  18.112  1.00164.84           C  
ANISOU  612  CA  PRO A 107    26337  15193  21102   1616  -4402   1504       C  
ATOM    613  C   PRO A 107      34.614  60.576  17.187  1.00165.98           C  
ANISOU  613  C   PRO A 107    26292  15899  20877   1558  -4386   1703       C  
ATOM    614  O   PRO A 107      33.450  60.223  16.995  1.00171.86           O  
ANISOU  614  O   PRO A 107    26812  16709  21778   1841  -4437   1665       O  
ATOM    615  CB  PRO A 107      35.134  61.289  19.560  1.00156.94           C  
ANISOU  615  CB  PRO A 107    25307  14287  20034   1683  -4031    954       C  
ATOM    616  CG  PRO A 107      33.773  61.394  20.183  1.00158.10           C  
ANISOU  616  CG  PRO A 107    25259  14227  20586   2125  -3959    617       C  
ATOM    617  CD  PRO A 107      33.203  62.637  19.587  1.00168.60           C  
ANISOU  617  CD  PRO A 107    26645  14989  22425   2297  -4315    880       C  
ATOM    618  N   ASN A 108      35.654  60.014  16.590  1.00159.59           N  
ANISOU  618  N   ASN A 108    25562  15476  19598   1184  -4318   1909       N  
ATOM    619  CA  ASN A 108      35.476  58.912  15.669  1.00141.34           C  
ANISOU  619  CA  ASN A 108    23107  13688  16906   1084  -4281   2071       C  
ATOM    620  C   ASN A 108      35.168  57.628  16.423  1.00134.22           C  
ANISOU  620  C   ASN A 108    21985  13167  15844   1240  -3945   1658       C  
ATOM    621  O   ASN A 108      35.611  57.451  17.554  1.00136.34           O  
ANISOU  621  O   ASN A 108    22263  13422  16118   1263  -3706   1315       O  
ATOM    622  CB  ASN A 108      36.730  58.753  14.807  1.00136.98           C  
ANISOU  622  CB  ASN A 108    22705  13414  15927    628  -4269   2378       C  
ATOM    623  CG  ASN A 108      36.589  57.672  13.767  1.00141.58           C  
ANISOU  623  CG  ASN A 108    23176  14520  16098    488  -4219   2529       C  
ATOM    624  OD1 ASN A 108      35.480  57.333  13.354  1.00150.39           O  
ANISOU  624  OD1 ASN A 108    24156  15717  17270    684  -4343   2571       O  
ATOM    625  ND2 ASN A 108      37.715  57.120  13.334  1.00138.13           N  
ANISOU  625  ND2 ASN A 108    22785  14442  15257    139  -4031   2596       N  
ATOM    626  N   GLU A 109      34.400  56.743  15.794  1.00137.19           N  
ANISOU  626  N   GLU A 109    22178  13879  16070   1319  -3952   1709       N  
ATOM    627  CA  GLU A 109      34.071  55.446  16.377  1.00127.92           C  
ANISOU  627  CA  GLU A 109    20798  13078  14727   1433  -3658   1366       C  
ATOM    628  C   GLU A 109      35.329  54.680  16.757  1.00113.70           C  
ANISOU  628  C   GLU A 109    19049  11572  12580   1179  -3378   1229       C  
ATOM    629  O   GLU A 109      35.419  54.098  17.837  1.00105.14           O  
ANISOU  629  O   GLU A 109    17889  10575  11485   1264  -3137    887       O  
ATOM    630  CB  GLU A 109      33.212  54.633  15.397  1.00142.25           C  
ANISOU  630  CB  GLU A 109    22447  15220  16381   1464  -3751   1515       C  
ATOM    631  CG  GLU A 109      32.795  53.237  15.872  1.00155.86           C  
ANISOU  631  CG  GLU A 109    23960  17326  17934   1559  -3475   1197       C  
ATOM    632  CD  GLU A 109      33.845  52.170  15.569  1.00157.12           C  
ANISOU  632  CD  GLU A 109    24160  17892  17647   1268  -3251   1176       C  
ATOM    633  OE1 GLU A 109      34.498  52.257  14.508  1.00169.19           O  
ANISOU  633  OE1 GLU A 109    25812  19548  18925    993  -3341   1463       O  
ATOM    634  OE2 GLU A 109      34.022  51.243  16.384  1.00140.68           O  
ANISOU  634  OE2 GLU A 109    21982  15997  15473   1306  -2983    875       O  
ATOM    635  N   ALA A 110      36.304  54.698  15.859  1.00107.25           N  
ANISOU  635  N   ALA A 110    18352  10909  11491    853  -3418   1510       N  
ATOM    636  CA  ALA A 110      37.581  54.046  16.099  1.00102.74           C  
ANISOU  636  CA  ALA A 110    17791  10599  10646    606  -3172   1418       C  
ATOM    637  C   ALA A 110      38.348  54.698  17.251  1.00108.22           C  
ANISOU  637  C   ALA A 110    18591  11020  11507    574  -3112   1252       C  
ATOM    638  O   ALA A 110      38.956  54.009  18.070  1.00102.36           O  
ANISOU  638  O   ALA A 110    17782  10442  10666    531  -2897   1018       O  
ATOM    639  CB  ALA A 110      38.415  54.057  14.830  1.00105.03           C  
ANISOU  639  CB  ALA A 110    18171  11098  10637    255  -3214   1751       C  
ATOM    640  N   SER A 111      38.310  56.027  17.316  1.00120.48           N  
ANISOU  640  N   SER A 111    20317  12139  13321    581  -3326   1383       N  
ATOM    641  CA  SER A 111      39.050  56.771  18.337  1.00123.50           C  
ANISOU  641  CA  SER A 111    20841  12227  13856    505  -3302   1236       C  
ATOM    642  C   SER A 111      38.482  56.525  19.732  1.00116.81           C  
ANISOU  642  C   SER A 111    19930  11291  13161    760  -3144    801       C  
ATOM    643  O   SER A 111      39.230  56.419  20.703  1.00124.97           O  
ANISOU  643  O   SER A 111    21012  12337  14135    646  -3014    597       O  
ATOM    644  CB  SER A 111      39.056  58.268  18.033  1.00135.12           C  
ANISOU  644  CB  SER A 111    22530  13206  15603    457  -3581   1473       C  
ATOM    645  OG  SER A 111      37.745  58.766  17.871  1.00153.17           O  
ANISOU  645  OG  SER A 111    24786  15208  18202    773  -3759   1486       O  
ATOM    646  N   VAL A 112      37.159  56.457  19.835  1.00102.43           N  
ANISOU  646  N   VAL A 112    17996   9390  11531   1082  -3162    667       N  
ATOM    647  CA  VAL A 112      36.512  56.215  21.118  1.00102.77           C  
ANISOU  647  CA  VAL A 112    17968   9380  11699   1309  -2978    241       C  
ATOM    648  C   VAL A 112      36.894  54.829  21.641  1.00114.54           C  
ANISOU  648  C   VAL A 112    19333  11320  12868   1220  -2730     62       C  
ATOM    649  O   VAL A 112      37.020  54.624  22.847  1.00126.78           O  
ANISOU  649  O   VAL A 112    20908  12873  14391   1223  -2570   -243       O  
ATOM    650  CB  VAL A 112      34.979  56.351  21.013  1.00 93.98           C  
ANISOU  650  CB  VAL A 112    16697   8135  10875   1669  -3029    149       C  
ATOM    651  CG1 VAL A 112      34.303  55.942  22.318  1.00 87.86           C  
ANISOU  651  CG1 VAL A 112    15818   7395  10169   1867  -2774   -312       C  
ATOM    652  CG2 VAL A 112      34.615  57.772  20.669  1.00 94.83           C  
ANISOU  652  CG2 VAL A 112    16923   7723  11385   1788  -3290    303       C  
ATOM    653  N   THR A 113      37.090  53.880  20.731  1.00110.87           N  
ANISOU  653  N   THR A 113    18747  11222  12158   1122  -2706    253       N  
ATOM    654  CA  THR A 113      37.587  52.566  21.122  1.00106.03           C  
ANISOU  654  CA  THR A 113    18017  10990  11281   1024  -2497    122       C  
ATOM    655  C   THR A 113      39.005  52.684  21.663  1.00107.37           C  
ANISOU  655  C   THR A 113    18289  11156  11349    759  -2457    128       C  
ATOM    656  O   THR A 113      39.368  52.023  22.635  1.00105.78           O  
ANISOU  656  O   THR A 113    18050  11088  11053    714  -2324    -70       O  
ATOM    657  CB  THR A 113      37.585  51.583  19.942  1.00 98.15           C  
ANISOU  657  CB  THR A 113    16884  10346  10062    957  -2472    310       C  
ATOM    658  OG1 THR A 113      36.299  51.598  19.315  1.00114.81           O  
ANISOU  658  OG1 THR A 113    18907  12448  12267   1161  -2572    362       O  
ATOM    659  CG2 THR A 113      37.900  50.172  20.410  1.00 81.71           C  
ANISOU  659  CG2 THR A 113    14662   8597   7786    917  -2259    139       C  
ATOM    660  N   SER A 114      39.796  53.541  21.026  1.00104.49           N  
ANISOU  660  N   SER A 114    18051  10641  11010    565  -2596    379       N  
ATOM    661  CA  SER A 114      41.192  53.735  21.394  1.00102.51           C  
ANISOU  661  CA  SER A 114    17869  10393  10689    283  -2586    430       C  
ATOM    662  C   SER A 114      41.390  54.268  22.816  1.00113.13           C  
ANISOU  662  C   SER A 114    19347  11498  12138    266  -2586    177       C  
ATOM    663  O   SER A 114      42.200  53.734  23.577  1.00121.11           O  
ANISOU  663  O   SER A 114    20321  12663  13034    115  -2513     82       O  
ATOM    664  CB  SER A 114      41.868  54.667  20.388  1.00 98.00           C  
ANISOU  664  CB  SER A 114    17415   9684  10136     61  -2741    763       C  
ATOM    665  OG  SER A 114      41.864  54.090  19.094  1.00 99.50           O  
ANISOU  665  OG  SER A 114    17499  10158  10147     -4  -2711    986       O  
ATOM    666  N   VAL A 115      40.656  55.319  23.170  1.00113.16           N  
ANISOU  666  N   VAL A 115    19505  11121  12368    414  -2678     65       N  
ATOM    667  CA  VAL A 115      40.726  55.872  24.520  1.00119.36           C  
ANISOU  667  CA  VAL A 115    20449  11667  13236    393  -2653   -234       C  
ATOM    668  C   VAL A 115      40.145  54.885  25.533  1.00130.36           C  
ANISOU  668  C   VAL A 115    21740  13289  14502    520  -2458   -551       C  
ATOM    669  O   VAL A 115      40.621  54.791  26.667  1.00137.97           O  
ANISOU  669  O   VAL A 115    22793  14270  15359    375  -2404   -751       O  
ATOM    670  CB  VAL A 115      39.996  57.236  24.615  1.00120.56           C  
ANISOU  670  CB  VAL A 115    20780  11317  13711    553  -2768   -322       C  
ATOM    671  CG1 VAL A 115      38.552  57.122  24.151  1.00118.09           C  
ANISOU  671  CG1 VAL A 115    20328  10967  13573    909  -2750   -365       C  
ATOM    672  CG2 VAL A 115      40.070  57.796  26.029  1.00135.21           C  
ANISOU  672  CG2 VAL A 115    22822  12929  15622    508  -2704   -691       C  
ATOM    673  N   ALA A 116      39.123  54.143  25.114  1.00127.37           N  
ANISOU  673  N   ALA A 116    21181  13097  14117    757  -2368   -578       N  
ATOM    674  CA  ALA A 116      38.523  53.118  25.961  1.00111.23           C  
ANISOU  674  CA  ALA A 116    19024  11298  11939    854  -2180   -838       C  
ATOM    675  C   ALA A 116      39.545  52.040  26.308  1.00 93.59           C  
ANISOU  675  C   ALA A 116    16724   9388   9450    628  -2131   -778       C  
ATOM    676  O   ALA A 116      39.639  51.618  27.460  1.00 90.26           O  
ANISOU  676  O   ALA A 116    16342   9053   8900    547  -2048   -982       O  
ATOM    677  CB  ALA A 116      37.309  52.502  25.282  1.00112.01           C  
ANISOU  677  CB  ALA A 116    18922  11549  12089   1114  -2121   -826       C  
ATOM    678  N   ARG A 117      40.312  51.605  25.311  1.00 90.37           N  
ANISOU  678  N   ARG A 117    16210   9152   8976    516  -2183   -496       N  
ATOM    679  CA  ARG A 117      41.370  50.626  25.541  1.00101.19           C  
ANISOU  679  CA  ARG A 117    17473  10788  10186    324  -2149   -421       C  
ATOM    680  C   ARG A 117      42.421  51.175  26.496  1.00106.83           C  
ANISOU  680  C   ARG A 117    18327  11379  10883     75  -2239   -453       C  
ATOM    681  O   ARG A 117      42.848  50.477  27.411  1.00112.46           O  
ANISOU  681  O   ARG A 117    19010  12240  11480    -38  -2222   -533       O  
ATOM    682  CB  ARG A 117      42.040  50.203  24.232  1.00113.22           C  
ANISOU  682  CB  ARG A 117    18851  12492  11676    244  -2153   -149       C  
ATOM    683  CG  ARG A 117      41.158  49.430  23.272  1.00110.42           C  
ANISOU  683  CG  ARG A 117    18354  12325  11276    425  -2069   -114       C  
ATOM    684  CD  ARG A 117      41.985  48.855  22.132  1.00117.57           C  
ANISOU  684  CD  ARG A 117    19123  13451  12095    292  -2023     93       C  
ATOM    685  NE  ARG A 117      41.160  48.127  21.174  1.00140.68           N  
ANISOU  685  NE  ARG A 117    21947  16562  14942    423  -1951    113       N  
ATOM    686  CZ  ARG A 117      40.869  46.834  21.272  1.00159.03           C  
ANISOU  686  CZ  ARG A 117    24123  19107  17195    501  -1826     -2       C  
ATOM    687  NH1 ARG A 117      41.337  46.122  22.289  1.00172.93           N  
ANISOU  687  NH1 ARG A 117    25819  20924  18964    469  -1772   -116       N  
ATOM    688  NH2 ARG A 117      40.109  46.253  20.353  1.00157.37           N  
ANISOU  688  NH2 ARG A 117    23841  19049  16904    590  -1779     13       N  
ATOM    689  N   LEU A 118      42.846  52.416  26.266  1.00109.73           N  
ANISOU  689  N   LEU A 118    18854  11473  11367    -33  -2363   -368       N  
ATOM    690  CA  LEU A 118      43.849  53.062  27.114  1.00111.95           C  
ANISOU  690  CA  LEU A 118    19286  11612  11639   -302  -2476   -393       C  
ATOM    691  C   LEU A 118      43.395  53.153  28.566  1.00105.93           C  
ANISOU  691  C   LEU A 118    18686  10766  10795   -310  -2439   -718       C  
ATOM    692  O   LEU A 118      44.165  52.880  29.490  1.00 79.57           O  
ANISOU  692  O   LEU A 118    15387   7521   7326   -541  -2498   -756       O  
ATOM    693  CB  LEU A 118      44.168  54.464  26.594  1.00104.73           C  
ANISOU  693  CB  LEU A 118    18546  10361  10887   -402  -2615   -267       C  
ATOM    694  CG  LEU A 118      44.937  54.572  25.278  1.00 96.53           C  
ANISOU  694  CG  LEU A 118    17397   9402   9877   -532  -2672     82       C  
ATOM    695  CD1 LEU A 118      44.856  55.988  24.749  1.00 96.47           C  
ANISOU  695  CD1 LEU A 118    17597   9014  10042   -579  -2817    204       C  
ATOM    696  CD2 LEU A 118      46.388  54.153  25.463  1.00 80.59           C  
ANISOU  696  CD2 LEU A 118    15248   7587   7786   -829  -2705    221       C  
ATOM    697  N   ALA A 119      42.133  53.523  28.751  1.00109.83           N  
ANISOU  697  N   ALA A 119    19262  11101  11367    -68  -2339   -950       N  
ATOM    698  CA  ALA A 119      41.541  53.610  30.075  1.00106.55           C  
ANISOU  698  CA  ALA A 119    18997  10629  10858    -65  -2237  -1308       C  
ATOM    699  C   ALA A 119      41.506  52.235  30.726  1.00111.94           C  
ANISOU  699  C   ALA A 119    19554  11681  11299   -115  -2145  -1353       C  
ATOM    700  O   ALA A 119      42.030  52.036  31.822  1.00105.32           O  
ANISOU  700  O   ALA A 119    18828  10920  10268   -355  -2182  -1451       O  
ATOM    701  CB  ALA A 119      40.146  54.208  29.987  1.00 82.26           C  
ANISOU  701  CB  ALA A 119    15956   7327   7972    244  -2115  -1543       C  
ATOM    702  N   ALA A 120      40.884  51.289  30.034  1.00114.82           N  
ANISOU  702  N   ALA A 120    19695  12262  11670     90  -2049  -1265       N  
ATOM    703  CA  ALA A 120      40.713  49.940  30.549  1.00105.93           C  
ANISOU  703  CA  ALA A 120    18443  11452  10353     68  -1963  -1292       C  
ATOM    704  C   ALA A 120      42.046  49.252  30.827  1.00104.26           C  
ANISOU  704  C   ALA A 120    18172  11412  10030   -194  -2103  -1083       C  
ATOM    705  O   ALA A 120      42.155  48.449  31.756  1.00102.78           O  
ANISOU  705  O   ALA A 120    17990  11398   9665   -324  -2105  -1130       O  
ATOM    706  CB  ALA A 120      39.895  49.114  29.569  1.00 98.71           C  
ANISOU  706  CB  ALA A 120    17301  10704   9501    317  -1862  -1209       C  
ATOM    707  N   ALA A 121      43.059  49.584  30.031  1.00105.85           N  
ANISOU  707  N   ALA A 121    18305  11562  10350   -283  -2226   -842       N  
ATOM    708  CA  ALA A 121      44.361  48.930  30.124  1.00112.79           C  
ANISOU  708  CA  ALA A 121    19048  12600  11206   -497  -2353   -624       C  
ATOM    709  C   ALA A 121      44.974  49.078  31.506  1.00122.24           C  
ANISOU  709  C   ALA A 121    20405  13784  12257   -779  -2494   -695       C  
ATOM    710  O   ALA A 121      45.586  48.149  32.028  1.00129.23           O  
ANISOU  710  O   ALA A 121    21179  14852  13072   -915  -2588   -581       O  
ATOM    711  CB  ALA A 121      45.312  49.482  29.071  1.00110.81           C  
ANISOU  711  CB  ALA A 121    18706  12283  11113   -573  -2430   -389       C  
ATOM    712  N   LYS A 122      44.807  50.253  32.096  1.00126.04           N  
ANISOU  712  N   LYS A 122    21156  14032  12700   -878  -2525   -883       N  
ATOM    713  CA  LYS A 122      45.329  50.498  33.431  1.00133.18           C  
ANISOU  713  CA  LYS A 122    22265  14921  13416  -1190  -2661   -986       C  
ATOM    714  C   LYS A 122      44.315  51.097  34.393  1.00121.72           C  
ANISOU  714  C   LYS A 122    21104  13341  11804  -1184  -2527  -1368       C  
ATOM    715  O   LYS A 122      44.251  52.312  34.576  1.00114.86           O  
ANISOU  715  O   LYS A 122    20460  12192  10989  -1238  -2533  -1546       O  
ATOM    716  CB  LYS A 122      46.573  51.385  33.361  1.00149.80           C  
ANISOU  716  CB  LYS A 122    24430  16874  15614  -1455  -2874   -836       C  
ATOM    717  CG  LYS A 122      47.746  50.726  32.657  1.00151.37           C  
ANISOU  717  CG  LYS A 122    24314  17243  15955  -1528  -2999   -483       C  
ATOM    718  CD  LYS A 122      48.397  49.669  33.532  1.00143.49           C  
ANISOU  718  CD  LYS A 122    23200  16478  14842  -1717  -3155   -365       C  
ATOM    719  CE  LYS A 122      49.208  48.677  32.718  1.00132.78           C  
ANISOU  719  CE  LYS A 122    21451  15308  13692  -1649  -3187    -69       C  
ATOM    720  NZ  LYS A 122      50.644  49.078  32.628  1.00114.49           N  
ANISOU  720  NZ  LYS A 122    18996  12977  11528  -1912  -3399    156       N  
ATOM    721  N   GLY A 123      43.495  50.222  34.966  1.00121.21           N  
ANISOU  721  N   GLY A 123    21021  13475  11560  -1116  -2386  -1502       N  
ATOM    722  CA  GLY A 123      42.580  50.592  36.028  1.00133.48           C  
ANISOU  722  CA  GLY A 123    22822  14984  12909  -1161  -2220  -1884       C  
ATOM    723  C   GLY A 123      41.262  51.226  35.660  1.00130.18           C  
ANISOU  723  C   GLY A 123    22426  14385  12650   -838  -1962  -2172       C  
ATOM    724  O   GLY A 123      40.198  50.669  35.928  1.00 99.55           O  
ANISOU  724  O   GLY A 123    18489  10648   8687   -695  -1748  -2350       O  
ATOM    725  N   ASN A 124      41.328  52.406  35.060  1.00152.98           N  
ANISOU  725  N   ASN A 124    25386  16946  15792   -733  -1995  -2207       N  
ATOM    726  CA  ASN A 124      40.129  53.202  34.841  1.00168.88           C  
ANISOU  726  CA  ASN A 124    27441  18712  18015   -438  -1792  -2498       C  
ATOM    727  C   ASN A 124      39.227  52.612  33.767  1.00169.55           C  
ANISOU  727  C   ASN A 124    27234  18897  18291    -75  -1687  -2372       C  
ATOM    728  O   ASN A 124      39.126  53.151  32.673  1.00171.30           O  
ANISOU  728  O   ASN A 124    27368  18927  18793    125  -1756  -2216       O  
ATOM    729  CB  ASN A 124      40.497  54.640  34.478  1.00170.75           C  
ANISOU  729  CB  ASN A 124    27848  18524  18507   -439  -1905  -2527       C  
ATOM    730  CG  ASN A 124      39.328  55.593  34.627  1.00168.61           C  
ANISOU  730  CG  ASN A 124    27673  17927  18463   -182  -1706  -2908       C  
ATOM    731  OD1 ASN A 124      38.171  55.175  34.679  1.00162.01           O  
ANISOU  731  OD1 ASN A 124    26694  17197  17664     67  -1482  -3093       O  
ATOM    732  ND2 ASN A 124      39.625  56.885  34.695  1.00175.53           N  
ANISOU  732  ND2 ASN A 124    28775  18389  19528   -241  -1789  -3030       N  
ATOM    733  N   GLY A 125      38.563  51.508  34.089  1.00163.18           N  
ANISOU  733  N   GLY A 125    26291  18393  17317    -21  -1537  -2429       N  
ATOM    734  CA  GLY A 125      37.558  50.961  33.200  1.00158.42           C  
ANISOU  734  CA  GLY A 125    25426  17888  16877    301  -1424  -2368       C  
ATOM    735  C   GLY A 125      36.357  51.862  33.004  1.00152.94           C  
ANISOU  735  C   GLY A 125    24711  16939  16458    600  -1268  -2634       C  
ATOM    736  O   GLY A 125      35.789  51.931  31.916  1.00176.61           O  
ANISOU  736  O   GLY A 125    27520  19874  19710    871  -1296  -2494       O  
ATOM    737  N   ASP A 126      35.979  52.557  34.070  1.00139.62           N  
ANISOU  737  N   ASP A 126    23218  15103  14728    540  -1109  -3025       N  
ATOM    738  CA  ASP A 126      34.785  53.395  34.066  1.00136.81           C  
ANISOU  738  CA  ASP A 126    22817  14488  14675    838   -918  -3348       C  
ATOM    739  C   ASP A 126      34.780  54.591  33.097  1.00156.97           C  
ANISOU  739  C   ASP A 126    25374  16608  17659   1064  -1079  -3239       C  
ATOM    740  O   ASP A 126      33.732  55.071  32.661  1.00166.68           O  
ANISOU  740  O   ASP A 126    26449  17641  19239   1395   -998  -3356       O  
ATOM    741  CB  ASP A 126      34.565  53.987  35.455  1.00141.49           C  
ANISOU  741  CB  ASP A 126    23660  14979  15122    680   -696  -3832       C  
ATOM    742  CG  ASP A 126      33.295  54.796  35.538  1.00168.68           C  
ANISOU  742  CG  ASP A 126    27017  18156  18920   1008   -447  -4225       C  
ATOM    743  OD1 ASP A 126      32.583  54.874  34.514  1.00181.38           O  
ANISOU  743  OD1 ASP A 126    28357  19663  20895   1358   -490  -4077       O  
ATOM    744  OD2 ASP A 126      33.002  55.344  36.620  1.00174.37           O1-
ANISOU  744  OD2 ASP A 126    27925  18769  19558    911   -209  -4686       O1-
ATOM    745  N   TYR A 127      35.981  55.038  32.748  1.00153.85           N  
ANISOU  745  N   TYR A 127    25138  16071  17246    867  -1330  -2982       N  
ATOM    746  CA  TYR A 127      36.145  56.112  31.777  1.00151.22           C  
ANISOU  746  CA  TYR A 127    24836  15344  17275   1006  -1527  -2794       C  
ATOM    747  C   TYR A 127      35.797  55.465  30.444  1.00150.51           C  
ANISOU  747  C   TYR A 127    24464  15431  17290   1209  -1628  -2426       C  
ATOM    748  O   TYR A 127      35.065  56.035  29.634  1.00156.50           O  
ANISOU  748  O   TYR A 127    25114  15958  18391   1485  -1693  -2352       O  
ATOM    749  CB  TYR A 127      37.556  56.701  31.705  1.00152.40           C  
ANISOU  749  CB  TYR A 127    25212  15335  17357    697  -1764  -2585       C  
ATOM    750  CG  TYR A 127      37.789  57.751  30.632  1.00157.74           C  
ANISOU  750  CG  TYR A 127    25930  15626  18377    789  -1988  -2326       C  
ATOM    751  CD1 TYR A 127      37.341  59.057  30.780  1.00164.60           C  
ANISOU  751  CD1 TYR A 127    26959  15986  19595    928  -2000  -2544       C  
ATOM    752  CD2 TYR A 127      38.461  57.422  29.462  1.00159.85           C  
ANISOU  752  CD2 TYR A 127    26082  16035  18619    720  -2183  -1861       C  
ATOM    753  CE1 TYR A 127      37.557  60.004  29.798  1.00172.94           C  
ANISOU  753  CE1 TYR A 127    28069  16670  20970    988  -2239  -2262       C  
ATOM    754  CE2 TYR A 127      38.684  58.361  28.475  1.00165.96           C  
ANISOU  754  CE2 TYR A 127    26914  16484  19659    751  -2393  -1591       C  
ATOM    755  CZ  TYR A 127      38.228  59.651  28.646  1.00172.77           C  
ANISOU  755  CZ  TYR A 127    27945  16828  20869    882  -2441  -1769       C  
ATOM    756  OH  TYR A 127      38.447  60.591  27.664  1.00181.79           O  
ANISOU  756  OH  TYR A 127    29163  17622  22286    892  -2685  -1458       O  
ATOM    757  N   ALA A 128      36.303  54.251  30.247  1.00139.75           N  
ANISOU  757  N   ALA A 128    22985  14476  15637   1063  -1647  -2205       N  
ATOM    758  CA  ALA A 128      36.087  53.509  29.013  1.00123.69           C  
ANISOU  758  CA  ALA A 128    20711  12653  13632   1194  -1724  -1882       C  
ATOM    759  C   ALA A 128      34.592  53.347  28.780  1.00121.05           C  
ANISOU  759  C   ALA A 128    20165  12336  13493   1522  -1596  -2027       C  
ATOM    760  O   ALA A 128      34.119  53.486  27.653  1.00130.97           O  
ANISOU  760  O   ALA A 128    21277  13534  14950   1708  -1720  -1806       O  
ATOM    761  CB  ALA A 128      36.770  52.149  29.035  1.00111.10           C  
ANISOU  761  CB  ALA A 128    19022  11472  11721   1002  -1713  -1716       C  
ATOM    762  N   PHE A 129      33.854  53.034  29.840  1.00109.09           N  
ANISOU  762  N   PHE A 129    18622  10922  11904   1565  -1355  -2385       N  
ATOM    763  CA  PHE A 129      32.404  52.917  29.742  1.00112.18           C  
ANISOU  763  CA  PHE A 129    18777  11336  12511   1867  -1203  -2563       C  
ATOM    764  C   PHE A 129      31.758  54.265  29.446  1.00120.93           C  
ANISOU  764  C   PHE A 129    19880  11988  14079   2139  -1257  -2670       C  
ATOM    765  O   PHE A 129      30.954  54.384  28.525  1.00130.79           O  
ANISOU  765  O   PHE A 129    20911  13169  15615   2399  -1357  -2520       O  
ATOM    766  CB  PHE A 129      31.817  52.344  31.035  1.00118.29           C  
ANISOU  766  CB  PHE A 129    19536  12327  13083   1804   -895  -2947       C  
ATOM    767  CG  PHE A 129      30.387  51.862  30.908  1.00131.35           C  
ANISOU  767  CG  PHE A 129    20879  14134  14893   2060   -717  -3087       C  
ATOM    768  CD1 PHE A 129      29.764  51.762  29.672  1.00131.04           C  
ANISOU  768  CD1 PHE A 129    20589  14088  15112   2302   -870  -2835       C  
ATOM    769  CD2 PHE A 129      29.660  51.532  32.041  1.00145.82           C  
ANISOU  769  CD2 PHE A 129    22671  16131  16602   2027   -397  -3472       C  
ATOM    770  CE1 PHE A 129      28.453  51.317  29.571  1.00133.60           C  
ANISOU  770  CE1 PHE A 129    20603  14565  15595   2517   -728  -2954       C  
ATOM    771  CE2 PHE A 129      28.351  51.096  31.946  1.00147.27           C  
ANISOU  771  CE2 PHE A 129    22540  16472  16946   2241   -220  -3604       C  
ATOM    772  CZ  PHE A 129      27.745  50.990  30.710  1.00141.03           C  
ANISOU  772  CZ  PHE A 129    21475  15666  16444   2495   -395  -3343       C  
ATOM    773  N   LYS A 130      32.137  55.285  30.209  1.00125.13           N  
ANISOU  773  N   LYS A 130    20659  12190  14694   2066  -1217  -2917       N  
ATOM    774  CA  LYS A 130      31.436  56.566  30.151  1.00138.29           C  
ANISOU  774  CA  LYS A 130    22324  13372  16847   2344  -1222  -3109       C  
ATOM    775  C   LYS A 130      31.571  57.258  28.796  1.00141.66           C  
ANISOU  775  C   LYS A 130    22721  13506  17598   2481  -1565  -2691       C  
ATOM    776  O   LYS A 130      30.605  57.826  28.290  1.00139.65           O  
ANISOU  776  O   LYS A 130    22285  12990  17784   2805  -1629  -2691       O  
ATOM    777  CB  LYS A 130      31.925  57.499  31.261  1.00129.82           C  
ANISOU  777  CB  LYS A 130    21570  11988  15767   2190  -1110  -3479       C  
ATOM    778  CG  LYS A 130      30.976  58.656  31.535  1.00126.36           C  
ANISOU  778  CG  LYS A 130    21098  11070  15842   2507   -988  -3847       C  
ATOM    779  CD  LYS A 130      31.573  59.661  32.501  1.00131.75           C  
ANISOU  779  CD  LYS A 130    22144  11392  16524   2326   -911  -4200       C  
ATOM    780  CE  LYS A 130      30.672  60.876  32.649  1.00139.14           C  
ANISOU  780  CE  LYS A 130    23041  11771  18054   2673   -807  -4560       C  
ATOM    781  NZ  LYS A 130      31.206  61.846  33.645  1.00141.20           N1+
ANISOU  781  NZ  LYS A 130    23679  11665  18307   2482   -698  -4973       N1+
ATOM    782  N   VAL A 131      32.755  57.187  28.197  1.00135.08           N  
ANISOU  782  N   VAL A 131    22045  12731  16548   2221  -1792  -2319       N  
ATOM    783  CA  VAL A 131      32.982  57.823  26.905  1.00132.08           C  
ANISOU  783  CA  VAL A 131    21674  12113  16396   2272  -2115  -1892       C  
ATOM    784  C   VAL A 131      32.153  57.162  25.793  1.00130.38           C  
ANISOU  784  C   VAL A 131    21162  12129  16248   2468  -2218  -1614       C  
ATOM    785  O   VAL A 131      31.667  57.846  24.889  1.00144.69           O  
ANISOU  785  O   VAL A 131    22907  13670  18400   2651  -2452  -1378       O  
ATOM    786  CB  VAL A 131      34.490  57.807  26.536  1.00171.81           C  
ANISOU  786  CB  VAL A 131    26919  17223  21137   1903  -2286  -1572       C  
ATOM    787  CG1 VAL A 131      35.035  56.386  26.488  1.00157.95           C  
ANISOU  787  CG1 VAL A 131    25061  16017  18937   1703  -2195  -1454       C  
ATOM    788  CG2 VAL A 131      34.742  58.534  25.218  1.00180.08           C  
ANISOU  788  CG2 VAL A 131    28007  18028  22385   1902  -2605  -1126       C  
ATOM    789  N   VAL A 132      31.983  55.843  25.865  1.00114.50           N  
ANISOU  789  N   VAL A 132    18983  10603  13917   2412  -2066  -1632       N  
ATOM    790  CA  VAL A 132      31.189  55.103  24.881  1.00114.12           C  
ANISOU  790  CA  VAL A 132    18663  10812  13885   2557  -2148  -1409       C  
ATOM    791  C   VAL A 132      29.694  55.420  24.999  1.00109.75           C  
ANISOU  791  C   VAL A 132    17851  10104  13745   2923  -2090  -1613       C  
ATOM    792  O   VAL A 132      28.997  55.561  23.991  1.00100.32           O  
ANISOU  792  O   VAL A 132    16474   8856  12787   3100  -2308  -1358       O  
ATOM    793  CB  VAL A 132      31.408  53.584  25.001  1.00113.08           C  
ANISOU  793  CB  VAL A 132    18433  11205  13328   2390  -1990  -1408       C  
ATOM    794  CG1 VAL A 132      30.537  52.858  24.011  1.00102.06           C  
ANISOU  794  CG1 VAL A 132    16774  10052  11953   2522  -2074  -1214       C  
ATOM    795  CG2 VAL A 132      32.857  53.246  24.729  1.00126.38           C  
ANISOU  795  CG2 VAL A 132    20302  13035  14680   2067  -2065  -1176       C  
ATOM    796  N   LYS A 133      29.200  55.519  26.231  1.00112.92           N  
ANISOU  796  N   LYS A 133    18224  10450  14231   3020  -1796  -2075       N  
ATOM    797  CA  LYS A 133      27.797  55.871  26.461  1.00123.51           C  
ANISOU  797  CA  LYS A 133    19284  11634  16011   3376  -1683  -2334       C  
ATOM    798  C   LYS A 133      27.464  57.259  25.912  1.00142.17           C  
ANISOU  798  C   LYS A 133    21647  13436  18936   3632  -1934  -2224       C  
ATOM    799  O   LYS A 133      26.430  57.458  25.281  1.00145.82           O  
ANISOU  799  O   LYS A 133    21819  13791  19796   3923  -2073  -2115       O  
ATOM    800  CB  LYS A 133      27.466  55.832  27.956  1.00126.27           C  
ANISOU  800  CB  LYS A 133    19651  12014  16312   3380  -1274  -2892       C  
ATOM    801  CG  LYS A 133      27.852  54.562  28.687  1.00121.33           C  
ANISOU  801  CG  LYS A 133    19077  11887  15136   3093  -1039  -3007       C  
ATOM    802  CD  LYS A 133      27.253  54.533  30.097  1.00126.42           C  
ANISOU  802  CD  LYS A 133    19699  12589  15746   3104   -629  -3554       C  
ATOM    803  CE  LYS A 133      25.772  54.889  30.098  1.00133.46           C  
ANISOU  803  CE  LYS A 133    20226  13353  17128   3484   -475  -3805       C  
ATOM    804  NZ  LYS A 133      25.293  55.239  31.469  1.00129.16           N1+
ANISOU  804  NZ  LYS A 133    19708  12747  16618   3500    -51  -4398       N1+
ATOM    805  N   GLU A 134      28.346  58.215  26.175  1.00158.81           N  
ANISOU  805  N   GLU A 134    24076  15171  21093   3511  -2011  -2244       N  
ATOM    806  CA  GLU A 134      28.233  59.570  25.652  1.00158.59           C  
ANISOU  806  CA  GLU A 134    24118  14555  21583   3697  -2287  -2095       C  
ATOM    807  C   GLU A 134      28.312  59.552  24.116  1.00144.39           C  
ANISOU  807  C   GLU A 134    22263  12784  19814   3675  -2711  -1482       C  
ATOM    808  O   GLU A 134      27.684  60.355  23.416  1.00132.77           O  
ANISOU  808  O   GLU A 134    20679  10937  18829   3919  -2993  -1269       O  
ATOM    809  CB  GLU A 134      29.336  60.427  26.275  1.00157.55           C  
ANISOU  809  CB  GLU A 134    24387  14087  21387   3473  -2277  -2225       C  
ATOM    810  CG  GLU A 134      29.012  60.897  27.689  1.00156.73           C  
ANISOU  810  CG  GLU A 134    24353  13763  21433   3565  -1918  -2856       C  
ATOM    811  CD  GLU A 134      30.020  61.892  28.228  1.00156.87           C  
ANISOU  811  CD  GLU A 134    24777  13374  21452   3350  -1959  -2982       C  
ATOM    812  OE1 GLU A 134      31.204  61.811  27.837  1.00152.07           O  
ANISOU  812  OE1 GLU A 134    24404  12863  20513   3015  -2158  -2643       O  
ATOM    813  OE2 GLU A 134      29.623  62.770  29.023  1.00167.97           O1-
ANISOU  813  OE2 GLU A 134    26257  14355  23208   3510  -1786  -3432       O1-
ATOM    814  N   PHE A 135      29.084  58.601  23.605  1.00147.86           N  
ANISOU  814  N   PHE A 135    22778  13678  19724   3368  -2753  -1204       N  
ATOM    815  CA  PHE A 135      29.250  58.424  22.170  1.00150.08           C  
ANISOU  815  CA  PHE A 135    23038  14085  19901   3267  -3097   -658       C  
ATOM    816  C   PHE A 135      28.017  57.894  21.457  1.00156.52           C  
ANISOU  816  C   PHE A 135    23498  15095  20876   3497  -3211   -519       C  
ATOM    817  O   PHE A 135      27.612  58.432  20.429  1.00165.11           O  
ANISOU  817  O   PHE A 135    24524  15985  22227   3593  -3570   -143       O  
ATOM    818  CB  PHE A 135      30.420  57.485  21.898  1.00150.14           C  
ANISOU  818  CB  PHE A 135    23200  14540  19306   2880  -3041   -481       C  
ATOM    819  CG  PHE A 135      30.773  57.376  20.451  1.00159.69           C  
ANISOU  819  CG  PHE A 135    24449  15882  20345   2706  -3347     43       C  
ATOM    820  CD1 PHE A 135      31.399  58.418  19.795  1.00171.47           C  
ANISOU  820  CD1 PHE A 135    26166  17033  21953   2574  -3632    379       C  
ATOM    821  CD2 PHE A 135      30.473  56.226  19.741  1.00159.14           C  
ANISOU  821  CD2 PHE A 135    24205  16281  19979   2644  -3345    193       C  
ATOM    822  CE1 PHE A 135      31.721  58.311  18.460  1.00171.09           C  
ANISOU  822  CE1 PHE A 135    26171  17143  21694   2367  -3895    861       C  
ATOM    823  CE2 PHE A 135      30.794  56.116  18.407  1.00158.21           C  
ANISOU  823  CE2 PHE A 135    24147  16312  19655   2447  -3601    642       C  
ATOM    824  CZ  PHE A 135      31.417  57.160  17.765  1.00163.98           C  
ANISOU  824  CZ  PHE A 135    25103  16731  20469   2300  -3870    979       C  
ATOM    825  N   VAL A 136      27.430  56.832  21.998  1.00157.69           N  
ANISOU  825  N   VAL A 136    23421  15636  20857   3555  -2928   -799       N  
ATOM    826  CA  VAL A 136      26.262  56.211  21.384  1.00164.33           C  
ANISOU  826  CA  VAL A 136    23906  16713  21818   3736  -3018   -691       C  
ATOM    827  C   VAL A 136      25.077  57.178  21.433  1.00168.47           C  
ANISOU  827  C   VAL A 136    24173  16807  23030   4143  -3139   -776       C  
ATOM    828  O   VAL A 136      24.124  57.052  20.662  1.00166.44           O  
ANISOU  828  O   VAL A 136    23623  16603  23012   4314  -3370   -555       O  
ATOM    829  CB  VAL A 136      25.900  54.874  22.071  1.00155.58           C  
ANISOU  829  CB  VAL A 136    22620  16096  20397   3687  -2665   -998       C  
ATOM    830  CG1 VAL A 136      25.348  55.115  23.471  1.00157.29           C  
ANISOU  830  CG1 VAL A 136    22735  16182  20844   3876  -2299  -1535       C  
ATOM    831  CG2 VAL A 136      24.912  54.086  21.229  1.00152.65           C  
ANISOU  831  CG2 VAL A 136    21927  16034  20040   3767  -2806   -803       C  
ATOM    832  N   SER A 137      25.156  58.152  22.336  1.00166.87           N  
ANISOU  832  N   SER A 137    24076  16164  23162   4291  -2991  -1103       N  
ATOM    833  CA  SER A 137      24.131  59.179  22.472  1.00173.50           C  
ANISOU  833  CA  SER A 137    24682  16510  24730   4702  -3074  -1240       C  
ATOM    834  C   SER A 137      24.010  60.022  21.205  1.00179.94           C  
ANISOU  834  C   SER A 137    25503  16963  25902   4789  -3616   -693       C  
ATOM    835  O   SER A 137      22.908  60.405  20.816  1.00189.21           O  
ANISOU  835  O   SER A 137    26339  17923  27627   5121  -3821   -601       O  
ATOM    836  CB  SER A 137      24.434  60.075  23.674  1.00185.03           C  
ANISOU  836  CB  SER A 137    26336  17547  26421   4783  -2795  -1720       C  
ATOM    837  OG  SER A 137      24.878  59.307  24.778  1.00179.76           O  
ANISOU  837  OG  SER A 137    25789  17242  25271   4569  -2356  -2131       O  
ATOM    838  N   VAL A 138      25.144  60.316  20.573  1.00188.25           N  
ANISOU  838  N   VAL A 138    26927  17950  26648   4476  -3856   -316       N  
ATOM    839  CA  VAL A 138      25.160  61.140  19.366  1.00202.68           C  
ANISOU  839  CA  VAL A 138    28831  19444  28736   4476  -4384    249       C  
ATOM    840  C   VAL A 138      24.348  60.500  18.240  1.00217.09           C  
ANISOU  840  C   VAL A 138    30370  21594  30520   4506  -4688    648       C  
ATOM    841  O   VAL A 138      23.370  61.077  17.763  1.00242.20           O  
ANISOU  841  O   VAL A 138    33289  24472  34262   4801  -5008    844       O  
ATOM    842  CB  VAL A 138      26.600  61.392  18.873  1.00195.56           C  
ANISOU  842  CB  VAL A 138    28378  18533  27393   4050  -4532    582       C  
ATOM    843  CG1 VAL A 138      26.583  62.162  17.561  1.00203.00           C  
ANISOU  843  CG1 VAL A 138    29409  19189  28532   3990  -5086   1213       C  
ATOM    844  CG2 VAL A 138      27.398  62.141  19.926  1.00187.93           C  
ANISOU  844  CG2 VAL A 138    27700  17198  26506   3998  -4304    230       C  
ATOM    845  N   GLY A 139      24.759  59.308  17.817  1.00210.03           N  
ANISOU  845  N   GLY A 139    29522  21301  28978   4195  -4601    766       N  
ATOM    846  CA  GLY A 139      23.974  58.520  16.885  1.00199.49           C  
ANISOU  846  CA  GLY A 139    27923  20347  27526   4185  -4819   1048       C  
ATOM    847  C   GLY A 139      23.977  58.972  15.436  1.00196.00           C  
ANISOU  847  C   GLY A 139    27574  19814  27083   4039  -5379   1696       C  
ATOM    848  O   GLY A 139      23.493  58.249  14.563  1.00183.81           O  
ANISOU  848  O   GLY A 139    25882  18646  25311   3930  -5578   1963       O  
ATOM    849  N   GLY A 140      24.521  60.155  15.168  1.00200.93           N  
ANISOU  849  N   GLY A 140    28461  19946  27938   4001  -5645   1961       N  
ATOM    850  CA  GLY A 140      24.538  60.672  13.812  1.00201.48           C  
ANISOU  850  CA  GLY A 140    28651  19900  28002   3827  -6202   2615       C  
ATOM    851  C   GLY A 140      25.438  59.828  12.936  1.00194.32           C  
ANISOU  851  C   GLY A 140    28005  19540  26290   3321  -6203   2893       C  
ATOM    852  O   GLY A 140      25.015  59.319  11.900  1.00197.47           O  
ANISOU  852  O   GLY A 140    28325  20261  26446   3167  -6480   3243       O  
ATOM    853  N   VAL A 141      26.686  59.670  13.359  1.00186.91           N  
ANISOU  853  N   VAL A 141    27367  18711  24940   3053  -5886   2721       N  
ATOM    854  CA  VAL A 141      27.597  58.739  12.706  1.00180.31           C  
ANISOU  854  CA  VAL A 141    26730  18421  23360   2604  -5764   2860       C  
ATOM    855  C   VAL A 141      28.300  57.959  13.812  1.00168.00           C  
ANISOU  855  C   VAL A 141    25199  17111  21524   2564  -5220   2340       C  
ATOM    856  O   VAL A 141      29.520  57.794  13.805  1.00160.27           O  
ANISOU  856  O   VAL A 141    24473  16279  20142   2247  -5049   2348       O  
ATOM    857  CB  VAL A 141      28.631  59.450  11.798  1.00179.38           C  
ANISOU  857  CB  VAL A 141    26986  18184  22985   2209  -6026   3340       C  
ATOM    858  CG1 VAL A 141      29.289  58.447  10.857  1.00172.66           C  
ANISOU  858  CG1 VAL A 141    26266  17936  21398   1762  -5948   3524       C  
ATOM    859  CG2 VAL A 141      27.973  60.554  10.981  1.00178.61           C  
ANISOU  859  CG2 VAL A 141    26902  17651  23313   2292  -6602   3852       C  
ATOM    860  N   SER A 142      27.513  57.495  14.776  1.00167.33           N  
ANISOU  860  N   SER A 142    24835  17069  21672   2880  -4959   1901       N  
ATOM    861  CA  SER A 142      28.046  56.760  15.913  1.00177.44           C  
ANISOU  861  CA  SER A 142    26130  18567  22721   2853  -4476   1419       C  
ATOM    862  C   SER A 142      28.637  55.432  15.455  1.00181.23           C  
ANISOU  862  C   SER A 142    26655  19629  22575   2536  -4303   1447       C  
ATOM    863  O   SER A 142      29.805  55.136  15.723  1.00171.79           O  
ANISOU  863  O   SER A 142    25661  18573  21040   2289  -4085   1363       O  
ATOM    864  CB  SER A 142      26.954  56.532  16.963  1.00176.82           C  
ANISOU  864  CB  SER A 142    25736  18441  23007   3228  -4246    974       C  
ATOM    865  OG  SER A 142      25.870  55.796  16.422  1.00169.98           O  
ANISOU  865  OG  SER A 142    24561  17865  22159   3334  -4351   1054       O  
ATOM    866  N   ILE A 143      27.820  54.654  14.749  1.00193.24           N  
ANISOU  866  N   ILE A 143    27974  21469  23978   2546  -4414   1563       N  
ATOM    867  CA  ILE A 143      28.204  53.334  14.257  1.00187.00           C  
ANISOU  867  CA  ILE A 143    27200  21210  22640   2272  -4255   1556       C  
ATOM    868  C   ILE A 143      28.794  52.491  15.396  1.00176.25           C  
ANISOU  868  C   ILE A 143    25840  20036  21090   2253  -3803   1122       C  
ATOM    869  O   ILE A 143      29.914  51.990  15.285  1.00176.50           O  
ANISOU  869  O   ILE A 143    26048  20275  20740   1981  -3637   1121       O  
ATOM    870  CB  ILE A 143      29.224  53.442  13.089  1.00180.50           C  
ANISOU  870  CB  ILE A 143    26660  20522  21399   1875  -4409   1940       C  
ATOM    871  CG1 ILE A 143      28.868  54.607  12.159  1.00189.88           C  
ANISOU  871  CG1 ILE A 143    27934  21401  22811   1862  -4885   2410       C  
ATOM    872  CG2 ILE A 143      29.331  52.124  12.317  1.00175.28           C  
ANISOU  872  CG2 ILE A 143    25980  20390  20229   1619  -4308   1958       C  
ATOM    873  CD1 ILE A 143      27.624  54.376  11.317  1.00193.67           C  
ANISOU  873  CD1 ILE A 143    28206  22008  23372   1942  -5217   2643       C  
ATOM    874  N   PRO A 144      28.057  52.365  16.514  1.00166.09           N  
ANISOU  874  N   PRO A 144    24351  18670  20087   2531  -3606    759       N  
ATOM    875  CA  PRO A 144      28.647  51.752  17.707  1.00147.93           C  
ANISOU  875  CA  PRO A 144    22093  16486  17628   2493  -3219    380       C  
ATOM    876  C   PRO A 144      29.033  50.289  17.510  1.00132.20           C  
ANISOU  876  C   PRO A 144    20082  14959  15189   2277  -3030    320       C  
ATOM    877  O   PRO A 144      28.164  49.435  17.345  1.00134.72           O  
ANISOU  877  O   PRO A 144    20193  15525  15470   2336  -3003    254       O  
ATOM    878  CB  PRO A 144      27.530  51.883  18.741  1.00145.93           C  
ANISOU  878  CB  PRO A 144    21597  16101  17749   2814  -3075     41       C  
ATOM    879  CG  PRO A 144      26.279  51.844  17.927  1.00155.20           C  
ANISOU  879  CG  PRO A 144    22503  17322  19143   2978  -3325    222       C  
ATOM    880  CD  PRO A 144      26.624  52.659  16.714  1.00162.84           C  
ANISOU  880  CD  PRO A 144    23636  18111  20127   2868  -3714    679       C  
ATOM    881  N   ARG A 145      30.330  50.005  17.526  1.00124.83           N  
ANISOU  881  N   ARG A 145    19351  14125  13953   2029  -2904    340       N  
ATOM    882  CA  ARG A 145      30.801  48.645  17.304  1.00121.33           C  
ANISOU  882  CA  ARG A 145    18892  14071  13138   1835  -2725    280       C  
ATOM    883  C   ARG A 145      31.033  47.976  18.656  1.00124.23           C  
ANISOU  883  C   ARG A 145    19220  14502  13480   1871  -2429    -61       C  
ATOM    884  O   ARG A 145      31.308  48.647  19.649  1.00119.24           O  
ANISOU  884  O   ARG A 145    18664  13638  13003   1939  -2354   -211       O  
ATOM    885  CB  ARG A 145      32.076  48.615  16.458  1.00114.30           C  
ANISOU  885  CB  ARG A 145    18195  13282  11951   1539  -2746    499       C  
ATOM    886  CG  ARG A 145      32.423  47.221  15.958  1.00106.70           C  
ANISOU  886  CG  ARG A 145    17191  12702  10650   1359  -2584    448       C  
ATOM    887  CD  ARG A 145      33.719  47.174  15.171  1.00110.05           C  
ANISOU  887  CD  ARG A 145    17771  13240  10803   1070  -2540    610       C  
ATOM    888  NE  ARG A 145      33.620  47.829  13.870  1.00132.97           N  
ANISOU  888  NE  ARG A 145    20781  16146  13594    924  -2781    938       N  
ATOM    889  CZ  ARG A 145      34.624  47.914  13.001  1.00139.85           C  
ANISOU  889  CZ  ARG A 145    21795  17140  14203    635  -2755   1115       C  
ATOM    890  NH1 ARG A 145      35.804  47.383  13.296  1.00131.46           N  
ANISOU  890  NH1 ARG A 145    20743  16190  13016    498  -2494    980       N  
ATOM    891  NH2 ARG A 145      34.448  48.527  11.837  1.00144.47           N  
ANISOU  891  NH2 ARG A 145    22499  17739  14655    471  -2995   1436       N  
ATOM    892  N   LEU A 146      30.878  46.658  18.701  1.00131.09           N  
ANISOU  892  N   LEU A 146    19982  15675  14151   1808  -2277   -179       N  
ATOM    893  CA  LEU A 146      31.138  45.890  19.914  1.00124.74           C  
ANISOU  893  CA  LEU A 146    19154  14957  13283   1793  -2029   -446       C  
ATOM    894  C   LEU A 146      32.539  46.118  20.481  1.00118.82           C  
ANISOU  894  C   LEU A 146    18585  14117  12443   1642  -1947   -458       C  
ATOM    895  O   LEU A 146      32.716  46.183  21.695  1.00121.19           O  
ANISOU  895  O   LEU A 146    18923  14338  12785   1659  -1824   -653       O  
ATOM    896  CB  LEU A 146      30.932  44.399  19.644  1.00130.99           C  
ANISOU  896  CB  LEU A 146    19836  16065  13869   1703  -1921   -503       C  
ATOM    897  CG  LEU A 146      31.163  43.456  20.826  1.00121.89           C  
ANISOU  897  CG  LEU A 146    18660  15011  12640   1659  -1701   -726       C  
ATOM    898  CD1 LEU A 146      29.982  42.514  21.000  1.00123.32           C  
ANISOU  898  CD1 LEU A 146    18653  15377  12826   1720  -1630   -856       C  
ATOM    899  CD2 LEU A 146      32.456  42.671  20.648  1.00103.11           C  
ANISOU  899  CD2 LEU A 146    16372  12739  10067   1463  -1625   -676       C  
ATOM    900  N   ARG A 147      33.529  46.247  19.603  1.00118.50           N  
ANISOU  900  N   ARG A 147    18652  14105  12268   1469  -2017   -249       N  
ATOM    901  CA  ARG A 147      34.913  46.435  20.032  1.00114.30           C  
ANISOU  901  CA  ARG A 147    18247  13511  11669   1305  -1955   -233       C  
ATOM    902  C   ARG A 147      35.096  47.709  20.862  1.00114.28           C  
ANISOU  902  C   ARG A 147    18376  13191  11856   1354  -2016   -280       C  
ATOM    903  O   ARG A 147      36.028  47.794  21.657  1.00105.75           O  
ANISOU  903  O   ARG A 147    17383  12056  10744   1238  -1953   -348       O  
ATOM    904  CB  ARG A 147      35.854  46.450  18.831  1.00118.22           C  
ANISOU  904  CB  ARG A 147    18806  14105  12008   1103  -2001      0       C  
ATOM    905  CG  ARG A 147      35.795  47.716  18.009  1.00132.25           C  
ANISOU  905  CG  ARG A 147    20700  15695  13854   1076  -2210    244       C  
ATOM    906  CD  ARG A 147      36.796  47.667  16.876  1.00139.58           C  
ANISOU  906  CD  ARG A 147    21697  16768  14569    818  -2210    461       C  
ATOM    907  NE  ARG A 147      36.569  48.762  15.941  1.00140.23           N  
ANISOU  907  NE  ARG A 147    21900  16706  14673    759  -2441    743       N  
ATOM    908  CZ  ARG A 147      37.188  49.935  16.002  1.00133.18           C  
ANISOU  908  CZ  ARG A 147    21157  15559  13887    669  -2558    900       C  
ATOM    909  NH1 ARG A 147      38.086  50.161  16.949  1.00150.64           N  
ANISOU  909  NH1 ARG A 147    23408  17653  16177    618  -2459    784       N  
ATOM    910  NH2 ARG A 147      36.913  50.878  15.112  1.00114.53           N  
ANISOU  910  NH2 ARG A 147    18912  13054  11551    606  -2799   1192       N  
ATOM    911  N   THR A 148      34.245  48.711  20.641  1.00117.36           N  
ANISOU  911  N   THR A 148    18779  13355  12458   1516  -2158   -238       N  
ATOM    912  CA  THR A 148      34.242  49.917  21.472  1.00122.51           C  
ANISOU  912  CA  THR A 148    19552  13659  13336   1598  -2197   -344       C  
ATOM    913  C   THR A 148      33.765  49.590  22.887  1.00125.53           C  
ANISOU  913  C   THR A 148    19890  14049  13755   1695  -2003   -691       C  
ATOM    914  O   THR A 148      34.386  49.985  23.872  1.00134.52           O  
ANISOU  914  O   THR A 148    21170  15058  14885   1606  -1938   -836       O  
ATOM    915  CB  THR A 148      33.342  51.031  20.892  1.00126.57           C  
ANISOU  915  CB  THR A 148    20059  13888  14143   1788  -2402   -226       C  
ATOM    916  OG1 THR A 148      32.013  50.902  21.413  1.00129.23           O  
ANISOU  916  OG1 THR A 148    20216  14206  14679   2048  -2330   -451       O  
ATOM    917  CG2 THR A 148      33.303  50.964  19.380  1.00132.54           C  
ANISOU  917  CG2 THR A 148    20796  14760  14802   1707  -2598    120       C  
ATOM    918  N   TYR A 149      32.629  48.900  22.968  1.00111.42           N  
ANISOU  918  N   TYR A 149    17914  12425  11996   1849  -1917   -819       N  
ATOM    919  CA  TYR A 149      32.058  48.426  24.229  1.00 99.89           C  
ANISOU  919  CA  TYR A 149    16389  11044  10521   1907  -1703  -1137       C  
ATOM    920  C   TYR A 149      32.976  47.455  24.973  1.00106.33           C  
ANISOU  920  C   TYR A 149    17276  12067  11057   1684  -1576  -1197       C  
ATOM    921  O   TYR A 149      32.873  47.295  26.190  1.00 98.93           O  
ANISOU  921  O   TYR A 149    16383  11149  10055   1642  -1427  -1432       O  
ATOM    922  CB  TYR A 149      30.720  47.735  23.969  1.00102.42           C  
ANISOU  922  CB  TYR A 149    16460  11550  10906   2071  -1648  -1204       C  
ATOM    923  CG  TYR A 149      29.515  48.643  23.891  1.00109.09           C  
ANISOU  923  CG  TYR A 149    17166  12180  12105   2342  -1699  -1289       C  
ATOM    924  CD1 TYR A 149      29.353  49.705  24.766  1.00108.61           C  
ANISOU  924  CD1 TYR A 149    17180  11816  12269   2457  -1624  -1517       C  
ATOM    925  CD2 TYR A 149      28.529  48.427  22.935  1.00108.25           C  
ANISOU  925  CD2 TYR A 149    16839  12163  12128   2482  -1831  -1148       C  
ATOM    926  CE1 TYR A 149      28.233  50.528  24.687  1.00102.17           C  
ANISOU  926  CE1 TYR A 149    16197  10771  11852   2741  -1661  -1613       C  
ATOM    927  CE2 TYR A 149      27.417  49.241  22.849  1.00100.74           C  
ANISOU  927  CE2 TYR A 149    15710  11004  11562   2750  -1906  -1203       C  
ATOM    928  CZ  TYR A 149      27.275  50.291  23.724  1.00 98.63           C  
ANISOU  928  CZ  TYR A 149    15495  10414  11566   2896  -1812  -1439       C  
ATOM    929  OH  TYR A 149      26.166  51.098  23.633  1.00107.66           O  
ANISOU  929  OH  TYR A 149    16427  11317  13163   3195  -1878  -1511       O  
ATOM    930  N   ALA A 150      33.856  46.792  24.228  1.00119.16           N  
ANISOU  930  N   ALA A 150    18905  13848  12521   1533  -1637   -983       N  
ATOM    931  CA  ALA A 150      34.643  45.674  24.752  1.00114.76           C  
ANISOU  931  CA  ALA A 150    18351  13494  11760   1356  -1546  -1000       C  
ATOM    932  C   ALA A 150      35.575  46.026  25.919  1.00112.49           C  
ANISOU  932  C   ALA A 150    18226  13104  11413   1197  -1531  -1084       C  
ATOM    933  O   ALA A 150      35.480  45.391  26.968  1.00114.23           O  
ANISOU  933  O   ALA A 150    18455  13429  11518   1124  -1432  -1230       O  
ATOM    934  CB  ALA A 150      35.449  45.021  23.621  1.00122.27           C  
ANISOU  934  CB  ALA A 150    19253  14591  12613   1248  -1599   -777       C  
ATOM    935  N   PRO A 151      36.468  47.030  25.760  1.00114.11           N  
ANISOU  935  N   PRO A 151    18568  13110  11677   1109  -1644   -979       N  
ATOM    936  CA  PRO A 151      37.423  47.268  26.850  1.00103.44           C  
ANISOU  936  CA  PRO A 151    17364  11690  10246    914  -1659  -1043       C  
ATOM    937  C   PRO A 151      36.732  47.686  28.138  1.00 99.86           C  
ANISOU  937  C   PRO A 151    17022  11141   9779    940  -1559  -1337       C  
ATOM    938  O   PRO A 151      37.222  47.380  29.223  1.00116.60           O  
ANISOU  938  O   PRO A 151    19238  13325  11739    756  -1535  -1428       O  
ATOM    939  CB  PRO A 151      38.305  48.403  26.313  1.00106.49           C  
ANISOU  939  CB  PRO A 151    17870  11858  10734    826  -1803   -881       C  
ATOM    940  CG  PRO A 151      38.058  48.438  24.845  1.00115.01           C  
ANISOU  940  CG  PRO A 151    18849  12969  11880    924  -1857   -675       C  
ATOM    941  CD  PRO A 151      36.640  48.020  24.683  1.00117.14           C  
ANISOU  941  CD  PRO A 151    18998  13318  12192   1147  -1782   -792       C  
ATOM    942  N   ALA A 152      35.600  48.368  28.009  1.00 88.18           N  
ANISOU  942  N   ALA A 152    15520   9517   8469   1156  -1503  -1485       N  
ATOM    943  CA  ALA A 152      34.826  48.783  29.172  1.00105.15           C  
ANISOU  943  CA  ALA A 152    17743  11580  10628   1202  -1347  -1820       C  
ATOM    944  C   ALA A 152      34.383  47.572  29.986  1.00113.61           C  
ANISOU  944  C   ALA A 152    18738  12949  11478   1123  -1185  -1950       C  
ATOM    945  O   ALA A 152      34.562  47.531  31.204  1.00112.61           O  
ANISOU  945  O   ALA A 152    18757  12861  11169    946  -1097  -2136       O  
ATOM    946  CB  ALA A 152      33.620  49.606  28.745  1.00104.94           C  
ANISOU  946  CB  ALA A 152    17623  11352  10898   1494  -1309  -1942       C  
ATOM    947  N   LEU A 153      33.814  46.583  29.307  1.00115.97           N  
ANISOU  947  N   LEU A 153    18829  13459  11774   1221  -1159  -1842       N  
ATOM    948  CA  LEU A 153      33.361  45.371  29.976  1.00111.27           C  
ANISOU  948  CA  LEU A 153    18155  13134  10987   1134  -1023  -1926       C  
ATOM    949  C   LEU A 153      34.507  44.522  30.531  1.00109.35           C  
ANISOU  949  C   LEU A 153    18010  13023  10516    864  -1101  -1787       C  
ATOM    950  O   LEU A 153      34.432  44.057  31.666  1.00116.94           O  
ANISOU  950  O   LEU A 153    19054  14103  11277    691  -1018  -1905       O  
ATOM    951  CB  LEU A 153      32.495  44.542  29.022  1.00105.81           C  
ANISOU  951  CB  LEU A 153    17223  12608  10373   1290  -1003  -1833       C  
ATOM    952  CG  LEU A 153      31.959  43.207  29.543  1.00 91.45           C  
ANISOU  952  CG  LEU A 153    15304  11058   8385   1196   -880  -1885       C  
ATOM    953  CD1 LEU A 153      30.519  42.998  29.117  1.00 69.80           C  
ANISOU  953  CD1 LEU A 153    12334   8412   5775   1386   -774  -1984       C  
ATOM    954  CD2 LEU A 153      32.827  42.074  29.020  1.00 95.18           C  
ANISOU  954  CD2 LEU A 153    15752  11653   8761   1073   -995  -1640       C  
ATOM    955  N   LEU A 154      35.566  44.328  29.749  1.00 98.44           N  
ANISOU  955  N   LEU A 154    16608  11622   9171    815  -1262  -1532       N  
ATOM    956  CA  LEU A 154      36.676  43.473  30.177  1.00 98.21           C  
ANISOU  956  CA  LEU A 154    16607  11699   9009    595  -1358  -1376       C  
ATOM    957  C   LEU A 154      37.355  43.986  31.440  1.00107.73           C  
ANISOU  957  C   LEU A 154    18024  12836  10071    364  -1415  -1451       C  
ATOM    958  O   LEU A 154      37.690  43.209  32.336  1.00114.51           O  
ANISOU  958  O   LEU A 154    18931  13823  10755    164  -1452  -1417       O  
ATOM    959  CB  LEU A 154      37.723  43.327  29.070  1.00 92.86           C  
ANISOU  959  CB  LEU A 154    15839  10999   8444    597  -1485  -1126       C  
ATOM    960  CG  LEU A 154      37.544  42.158  28.099  1.00 96.20           C  
ANISOU  960  CG  LEU A 154    16068  11576   8908    685  -1451  -1012       C  
ATOM    961  CD1 LEU A 154      36.245  42.270  27.323  1.00103.36           C  
ANISOU  961  CD1 LEU A 154    16886  12513   9872    889  -1363  -1095       C  
ATOM    962  CD2 LEU A 154      38.742  42.048  27.160  1.00 85.19           C  
ANISOU  962  CD2 LEU A 154    14596  10171   7603    641  -1534   -811       C  
ATOM    963  N   CYS A 155      37.562  45.294  31.504  1.00102.75           N  
ANISOU  963  N   CYS A 155    17535  11993   9512    370  -1446  -1541       N  
ATOM    964  CA  CYS A 155      38.191  45.897  32.663  1.00103.46           C  
ANISOU  964  CA  CYS A 155    17855  12002   9454    127  -1508  -1642       C  
ATOM    965  C   CYS A 155      37.289  45.742  33.887  1.00100.84           C  
ANISOU  965  C   CYS A 155    17638  11771   8907     41  -1331  -1926       C  
ATOM    966  O   CYS A 155      37.764  45.401  34.966  1.00100.07           O  
ANISOU  966  O   CYS A 155    17687  11777   8560   -240  -1387  -1935       O  
ATOM    967  CB  CYS A 155      38.509  47.366  32.394  1.00115.24           C  
ANISOU  967  CB  CYS A 155    19482  13205  11097    159  -1568  -1701       C  
ATOM    968  SG  CYS A 155      39.523  48.150  33.656  1.00 98.80           S  
ANISOU  968  SG  CYS A 155    17696  11003   8841   -190  -1695  -1794       S  
ATOM    969  N   PHE A 156      35.993  45.995  33.719  1.00101.25           N  
ANISOU  969  N   PHE A 156    17614  11806   9052    264  -1121  -2150       N  
ATOM    970  CA  PHE A 156      35.024  45.798  34.800  1.00117.81           C  
ANISOU  970  CA  PHE A 156    19772  14035  10955    191   -890  -2445       C  
ATOM    971  C   PHE A 156      34.953  44.345  35.260  1.00109.47           C  
ANISOU  971  C   PHE A 156    18654  13275   9666     18   -884  -2316       C  
ATOM    972  O   PHE A 156      34.676  44.057  36.424  1.00105.33           O  
ANISOU  972  O   PHE A 156    18266  12899   8857   -214   -773  -2470       O  
ATOM    973  CB  PHE A 156      33.634  46.262  34.366  1.00126.56           C  
ANISOU  973  CB  PHE A 156    20721  15076  12290    502   -671  -2679       C  
ATOM    974  CG  PHE A 156      33.477  47.749  34.345  1.00140.28           C  
ANISOU  974  CG  PHE A 156    22564  16493  14244    642   -629  -2902       C  
ATOM    975  CD1 PHE A 156      34.384  48.559  35.010  1.00157.05           C  
ANISOU  975  CD1 PHE A 156    24964  18444  16262    429   -717  -2980       C  
ATOM    976  CD2 PHE A 156      32.424  48.341  33.666  1.00148.62           C  
ANISOU  976  CD2 PHE A 156    23439  17398  15631    978   -527  -3026       C  
ATOM    977  CE1 PHE A 156      34.249  49.933  34.996  1.00176.30           C  
ANISOU  977  CE1 PHE A 156    27519  20542  18926    550   -684  -3196       C  
ATOM    978  CE2 PHE A 156      32.282  49.715  33.649  1.00164.35           C  
ANISOU  978  CE2 PHE A 156    25526  19041  17879   1122   -509  -3222       C  
ATOM    979  CZ  PHE A 156      33.194  50.511  34.315  1.00172.30           C  
ANISOU  979  CZ  PHE A 156    26830  19855  18781    909   -577  -3317       C  
ATOM    980  N   CYS A 157      35.189  43.434  34.326  1.00105.21           N  
ANISOU  980  N   CYS A 157    17919  12811   9244    117   -999  -2039       N  
ATOM    981  CA  CYS A 157      35.192  42.011  34.621  1.00107.63           C  
ANISOU  981  CA  CYS A 157    18157  13339   9400    -25  -1029  -1880       C  
ATOM    982  C   CYS A 157      36.415  41.599  35.439  1.00105.03           C  
ANISOU  982  C   CYS A 157    17981  13043   8881   -341  -1247  -1688       C  
ATOM    983  O   CYS A 157      36.315  40.823  36.394  1.00 88.87           O  
ANISOU  983  O   CYS A 157    16020  11158   6589   -582  -1254  -1658       O  
ATOM    984  CB  CYS A 157      35.122  41.205  33.327  1.00106.53           C  
ANISOU  984  CB  CYS A 157    17774  13231   9471    178  -1083  -1676       C  
ATOM    985  SG  CYS A 157      33.428  40.934  32.761  1.00138.50           S  
ANISOU  985  SG  CYS A 157    21614  17387  13622    418   -853  -1847       S  
ATOM    986  N   GLU A 158      37.577  42.099  35.034  1.00114.96           N  
ANISOU  986  N   GLU A 158    19260  14154  10267   -353  -1446  -1529       N  
ATOM    987  CA  GLU A 158      38.823  41.794  35.720  1.00121.25           C  
ANISOU  987  CA  GLU A 158    20154  14965  10949   -637  -1696  -1318       C  
ATOM    988  C   GLU A 158      38.829  42.352  37.152  1.00139.22           C  
ANISOU  988  C   GLU A 158    22724  17275  12897   -949  -1696  -1495       C  
ATOM    989  O   GLU A 158      39.407  41.751  38.059  1.00153.48           O  
ANISOU  989  O   GLU A 158    24609  19191  14515  -1245  -1865  -1332       O  
ATOM    990  CB  GLU A 158      40.002  42.342  34.911  1.00116.54           C  
ANISOU  990  CB  GLU A 158    19482  14210  10588   -579  -1874  -1139       C  
ATOM    991  CG  GLU A 158      41.376  42.033  35.481  1.00135.36           C  
ANISOU  991  CG  GLU A 158    21891  16602  12938   -845  -2162   -890       C  
ATOM    992  CD  GLU A 158      41.834  40.611  35.199  1.00151.56           C  
ANISOU  992  CD  GLU A 158    23724  18743  15120   -830  -2286   -614       C  
ATOM    993  OE1 GLU A 158      40.979  39.711  35.051  1.00149.64           O  
ANISOU  993  OE1 GLU A 158    23403  18595  14858   -726  -2159   -641       O  
ATOM    994  OE2 GLU A 158      43.061  40.393  35.123  1.00167.18           O  
ANISOU  994  OE2 GLU A 158    25592  20680  17248   -921  -2514   -376       O  
ATOM    995  N   LYS A 159      38.190  43.504  37.344  1.00132.13           N  
ANISOU  995  N   LYS A 159    21962  16276  11966   -884  -1503  -1820       N  
ATOM    996  CA  LYS A 159      38.084  44.144  38.659  1.00110.10           C  
ANISOU  996  CA  LYS A 159    19371  13520   8941  -1153  -1411  -2044       C  
ATOM    997  C   LYS A 159      36.933  43.575  39.495  1.00 99.45           C  
ANISOU  997  C   LYS A 159    17963  12406   7416  -1231  -1139  -2215       C  
ATOM    998  O   LYS A 159      36.700  44.017  40.622  1.00118.36           O  
ANISOU  998  O   LYS A 159    20469  14880   9622  -1447  -1004  -2419       O  
ATOM    999  CB  LYS A 159      37.928  45.662  38.502  1.00106.74           C  
ANISOU  999  CB  LYS A 159    19108  12839   8611  -1040  -1309  -2349       C  
ATOM   1000  CG  LYS A 159      39.244  46.405  38.292  1.00100.70           C  
ANISOU 1000  CG  LYS A 159    18482  11870   7909  -1159  -1593  -2204       C  
ATOM   1001  CD  LYS A 159      39.025  47.813  37.748  1.00 97.50           C  
ANISOU 1001  CD  LYS A 159    18145  11156   7743   -954  -1504  -2426       C  
ATOM   1002  CE  LYS A 159      38.088  48.625  38.628  1.00 98.16           C  
ANISOU 1002  CE  LYS A 159    18419  11169   7710   -982  -1223  -2888       C  
ATOM   1003  NZ  LYS A 159      37.852  49.990  38.073  1.00 97.98           N  
ANISOU 1003  NZ  LYS A 159    18466  10780   7983   -753  -1159  -3101       N  
ATOM   1004  N   LEU A 160      36.203  42.624  38.915  1.00 87.88           N  
ANISOU 1004  N   LEU A 160    16327  11055   6009  -1062  -1053  -2147       N  
ATOM   1005  CA  LEU A 160      35.123  41.898  39.591  1.00 85.73           C  
ANISOU 1005  CA  LEU A 160    15974  11026   5574  -1152   -819  -2257       C  
ATOM   1006  C   LEU A 160      33.902  42.764  39.901  1.00 86.52           C  
ANISOU 1006  C   LEU A 160    16081  11133   5658  -1037   -453  -2704       C  
ATOM   1007  O   LEU A 160      33.113  42.434  40.787  1.00 88.83           O  
ANISOU 1007  O   LEU A 160    16345  11642   5764  -1191   -232  -2856       O  
ATOM   1008  CB  LEU A 160      35.628  41.233  40.880  1.00 81.87           C  
ANISOU 1008  CB  LEU A 160    15562  10719   4826  -1552   -936  -2073       C  
ATOM   1009  CG  LEU A 160      36.379  39.898  40.778  1.00 83.54           C  
ANISOU 1009  CG  LEU A 160    15708  10987   5048  -1677  -1233  -1640       C  
ATOM   1010  CD1 LEU A 160      37.699  40.040  40.047  1.00 78.17           C  
ANISOU 1010  CD1 LEU A 160    15029  10113   4560  -1607  -1556  -1391       C  
ATOM   1011  CD2 LEU A 160      36.596  39.294  42.157  1.00 97.69           C  
ANISOU 1011  CD2 LEU A 160    17597  12950   6571  -2075  -1313  -1490       C  
ATOM   1012  N   GLU A 161      33.740  43.862  39.171  1.00 93.33           N  
ANISOU 1012  N   GLU A 161    16982  11745   6735   -762   -392  -2913       N  
ATOM   1013  CA  GLU A 161      32.528  44.667  39.300  1.00111.87           C  
ANISOU 1013  CA  GLU A 161    19302  14041   9163   -577    -47  -3349       C  
ATOM   1014  C   GLU A 161      31.422  44.026  38.470  1.00123.89           C  
ANISOU 1014  C   GLU A 161    20599  15644  10831   -300     97  -3367       C  
ATOM   1015  O   GLU A 161      31.307  44.282  37.271  1.00127.18           O  
ANISOU 1015  O   GLU A 161    20810  15899  11615     34      9  -3252       O  
ATOM   1016  CB  GLU A 161      32.775  46.109  38.847  1.00124.97           C  
ANISOU 1016  CB  GLU A 161    21099  15334  11048   -372    -67  -3550       C  
ATOM   1017  CG  GLU A 161      34.189  46.621  39.114  1.00137.10           C  
ANISOU 1017  CG  GLU A 161    22835  16734  12525   -596   -350  -3376       C  
ATOM   1018  CD  GLU A 161      34.209  47.825  40.040  1.00154.75           C  
ANISOU 1018  CD  GLU A 161    25242  18836  14721   -730   -209  -3723       C  
ATOM   1019  OE1 GLU A 161      33.119  48.287  40.441  1.00154.21           O  
ANISOU 1019  OE1 GLU A 161    25121  18768  14705   -617    123  -4119       O  
ATOM   1020  OE2 GLU A 161      35.314  48.306  40.373  1.00165.75           O  
ANISOU 1020  OE2 GLU A 161    26810  20124  16045   -949   -427  -3613       O  
ATOM   1021  N   ALA A 162      30.607  43.195  39.116  1.00132.74           N  
ANISOU 1021  N   ALA A 162    21624  17054  11757   -454    303  -3439       N  
ATOM   1022  CA  ALA A 162      29.634  42.363  38.411  1.00130.18           C  
ANISOU 1022  CA  ALA A 162    21023  16864  11574   -264    401  -3377       C  
ATOM   1023  C   ALA A 162      28.478  43.164  37.821  1.00123.30           C  
ANISOU 1023  C   ALA A 162    19894  15882  11073    115    636  -3663       C  
ATOM   1024  O   ALA A 162      28.190  43.060  36.632  1.00101.32           O  
ANISOU 1024  O   ALA A 162    16861  13016   8618    414    524  -3500       O  
ATOM   1025  CB  ALA A 162      29.101  41.286  39.347  1.00130.98           C  
ANISOU 1025  CB  ALA A 162    21124  17300  11342   -583    554  -3374       C  
ATOM   1026  N   GLU A 163      27.821  43.958  38.661  1.00124.72           N  
ANISOU 1026  N   GLU A 163    20130  16057  11202     90    956  -4091       N  
ATOM   1027  CA  GLU A 163      26.660  44.751  38.255  1.00135.36           C  
ANISOU 1027  CA  GLU A 163    21202  17283  12947    456   1203  -4402       C  
ATOM   1028  C   GLU A 163      27.026  45.776  37.189  1.00129.05           C  
ANISOU 1028  C   GLU A 163    20352  16102  12581    810    980  -4312       C  
ATOM   1029  O   GLU A 163      26.189  46.164  36.374  1.00120.02           O  
ANISOU 1029  O   GLU A 163    18911  14839  11854   1167   1015  -4359       O  
ATOM   1030  CB  GLU A 163      26.028  45.445  39.467  1.00152.11           C  
ANISOU 1030  CB  GLU A 163    23421  19447  14926    337   1618  -4927       C  
ATOM   1031  CG  GLU A 163      24.946  44.626  40.168  1.00156.15           C  
ANISOU 1031  CG  GLU A 163    23770  20339  15221    157   1974  -5113       C  
ATOM   1032  CD  GLU A 163      25.464  43.311  40.725  1.00156.75           C  
ANISOU 1032  CD  GLU A 163    23980  20731  14845   -261   1813  -4759       C  
ATOM   1033  OE1 GLU A 163      26.650  43.252  41.115  1.00151.58           O  
ANISOU 1033  OE1 GLU A 163    23567  20035  13990   -487   1522  -4504       O  
ATOM   1034  OE2 GLU A 163      24.681  42.337  40.780  1.00160.88           O  
ANISOU 1034  OE2 GLU A 163    24315  21534  15277   -356   1952  -4704       O  
ATOM   1035  N   LYS A 164      28.266  46.251  37.239  1.00142.84           N  
ANISOU 1035  N   LYS A 164    22388  17658  14228    687    743  -4178       N  
ATOM   1036  CA  LYS A 164      28.782  47.165  36.228  1.00145.71           C  
ANISOU 1036  CA  LYS A 164    22746  17669  14947    949    497  -4030       C  
ATOM   1037  C   LYS A 164      28.852  46.472  34.866  1.00142.57           C  
ANISOU 1037  C   LYS A 164    22120  17317  14734   1126    244  -3617       C  
ATOM   1038  O   LYS A 164      28.456  47.035  33.846  1.00150.90           O  
ANISOU 1038  O   LYS A 164    22993  18179  16164   1439    151  -3548       O  
ATOM   1039  CB  LYS A 164      30.167  47.679  36.636  1.00144.33           C  
ANISOU 1039  CB  LYS A 164    22926  17333  14579    706    294  -3948       C  
ATOM   1040  CG  LYS A 164      30.137  48.693  37.762  1.00140.96           C  
ANISOU 1040  CG  LYS A 164    22755  16759  14046    573    508  -4385       C  
ATOM   1041  CD  LYS A 164      29.195  49.836  37.439  1.00141.69           C  
ANISOU 1041  CD  LYS A 164    22693  16545  14598    948    694  -4710       C  
ATOM   1042  CE  LYS A 164      29.033  50.769  38.620  1.00147.88           C  
ANISOU 1042  CE  LYS A 164    23719  17188  15283    819    980  -5229       C  
ATOM   1043  NZ  LYS A 164      28.485  50.054  39.804  1.00151.80           N  
ANISOU 1043  NZ  LYS A 164    24262  18065  15352    529   1316  -5505       N  
ATOM   1044  N   GLY A 165      29.370  45.246  34.874  1.00126.55           N  
ANISOU 1044  N   GLY A 165    20116  15534  12433    906    124  -3346       N  
ATOM   1045  CA  GLY A 165      29.480  44.424  33.682  1.00114.98           C  
ANISOU 1045  CA  GLY A 165    18464  14144  11081   1017    -78  -2998       C  
ATOM   1046  C   GLY A 165      28.130  44.056  33.085  1.00105.39           C  
ANISOU 1046  C   GLY A 165    16920  13046  10076   1243     45  -3052       C  
ATOM   1047  O   GLY A 165      27.972  43.983  31.868  1.00109.23           O  
ANISOU 1047  O   GLY A 165    17235  13483  10786   1444   -118  -2849       O  
ATOM   1048  N   TYR A 166      27.163  43.783  33.950  1.00 97.41           N  
ANISOU 1048  N   TYR A 166    15820  12221   8970   1176    331  -3321       N  
ATOM   1049  CA  TYR A 166      25.827  43.436  33.510  1.00106.88           C  
ANISOU 1049  CA  TYR A 166    16674  13556  10378   1363    467  -3396       C  
ATOM   1050  C   TYR A 166      25.193  44.656  32.846  1.00117.61           C  
ANISOU 1050  C   TYR A 166    17849  14650  12188   1735    461  -3522       C  
ATOM   1051  O   TYR A 166      24.471  44.537  31.855  1.00120.69           O  
ANISOU 1051  O   TYR A 166    17955  15049  12853   1959    364  -3400       O  
ATOM   1052  CB  TYR A 166      24.978  42.940  34.689  1.00114.02           C  
ANISOU 1052  CB  TYR A 166    17523  14730  11067   1169    813  -3677       C  
ATOM   1053  CG  TYR A 166      25.457  41.632  35.294  1.00128.48           C  
ANISOU 1053  CG  TYR A 166    19513  16823  12479    792    783  -3498       C  
ATOM   1054  CD1 TYR A 166      26.628  41.019  34.855  1.00127.02           C  
ANISOU 1054  CD1 TYR A 166    19495  16595  12174    676    473  -3144       C  
ATOM   1055  CD2 TYR A 166      24.761  41.034  36.336  1.00140.50           C  
ANISOU 1055  CD2 TYR A 166    21018  18624  13741    541   1067  -3683       C  
ATOM   1056  CE1 TYR A 166      27.075  39.837  35.416  1.00125.95           C  
ANISOU 1056  CE1 TYR A 166    19490  16648  11719    353    414  -2963       C  
ATOM   1057  CE2 TYR A 166      25.203  39.851  36.905  1.00146.55           C  
ANISOU 1057  CE2 TYR A 166    21947  19599  14137    178   1000  -3479       C  
ATOM   1058  CZ  TYR A 166      26.364  39.260  36.440  1.00136.55           C  
ANISOU 1058  CZ  TYR A 166    20835  18243  12805    101    657  -3112       C  
ATOM   1059  OH  TYR A 166      26.816  38.085  36.993  1.00135.90           O  
ANISOU 1059  OH  TYR A 166    20898  18318  12420   -235    557  -2887       O  
ATOM   1060  N   GLU A 167      25.473  45.830  33.407  1.00127.63           N  
ANISOU 1060  N   GLU A 167    19289  15666  13539   1784    544  -3760       N  
ATOM   1061  CA  GLU A 167      24.952  47.101  32.902  1.00126.44           C  
ANISOU 1061  CA  GLU A 167    18998  15185  13857   2136    527  -3893       C  
ATOM   1062  C   GLU A 167      25.474  47.450  31.508  1.00132.64           C  
ANISOU 1062  C   GLU A 167    19774  15756  14868   2309    145  -3513       C  
ATOM   1063  O   GLU A 167      24.709  47.925  30.669  1.00148.30           O  
ANISOU 1063  O   GLU A 167    21502  17599  17246   2605     48  -3458       O  
ATOM   1064  CB  GLU A 167      25.279  48.234  33.879  1.00125.47           C  
ANISOU 1064  CB  GLU A 167    19123  14809  13739   2100    697  -4246       C  
ATOM   1065  CG  GLU A 167      24.760  49.595  33.445  1.00130.46           C  
ANISOU 1065  CG  GLU A 167    19629  15033  14909   2472    682  -4406       C  
ATOM   1066  CD  GLU A 167      24.956  50.661  34.504  1.00135.04           C  
ANISOU 1066  CD  GLU A 167    20449  15356  15503   2428    909  -4837       C  
ATOM   1067  OE1 GLU A 167      24.847  50.338  35.707  1.00135.88           O  
ANISOU 1067  OE1 GLU A 167    20677  15683  15268   2175   1228  -5159       O  
ATOM   1068  OE2 GLU A 167      25.213  51.826  34.134  1.00132.50           O  
ANISOU 1068  OE2 GLU A 167    20212  14607  15524   2624    766  -4857       O  
ATOM   1069  N   VAL A 168      26.769  47.254  31.262  1.00119.86           N  
ANISOU 1069  N   VAL A 168    18421  14110  13010   2114    -74  -3248       N  
ATOM   1070  CA  VAL A 168      27.304  47.519  29.928  1.00123.08           C  
ANISOU 1070  CA  VAL A 168    18827  14362  13573   2224   -402  -2888       C  
ATOM   1071  C   VAL A 168      26.707  46.528  28.924  1.00124.35           C  
ANISOU 1071  C   VAL A 168    18729  14763  13755   2287   -507  -2654       C  
ATOM   1072  O   VAL A 168      26.359  46.917  27.815  1.00129.05           O  
ANISOU 1072  O   VAL A 168    19183  15243  14606   2482   -706  -2466       O  
ATOM   1073  CB  VAL A 168      28.864  47.488  29.885  1.00102.80           C  
ANISOU 1073  CB  VAL A 168    16565  11742  10754   1983   -582  -2669       C  
ATOM   1074  CG1 VAL A 168      29.414  46.167  30.350  1.00104.86           C  
ANISOU 1074  CG1 VAL A 168    16891  12314  10638   1706   -543  -2581       C  
ATOM   1075  CG2 VAL A 168      29.373  47.811  28.487  1.00 76.60           C  
ANISOU 1075  CG2 VAL A 168    13238   8285   7580   2072   -877  -2319       C  
ATOM   1076  N   GLU A 169      26.545  45.269  29.332  1.00122.72           N  
ANISOU 1076  N   GLU A 169    18470  14878  13281   2105   -384  -2666       N  
ATOM   1077  CA  GLU A 169      25.945  44.241  28.475  1.00127.95           C  
ANISOU 1077  CA  GLU A 169    18902  15771  13941   2126   -463  -2486       C  
ATOM   1078  C   GLU A 169      24.538  44.665  28.057  1.00129.08           C  
ANISOU 1078  C   GLU A 169    18710  15890  14443   2399   -434  -2582       C  
ATOM   1079  O   GLU A 169      24.153  44.527  26.894  1.00129.16           O  
ANISOU 1079  O   GLU A 169    18554  15924  14598   2511   -644  -2362       O  
ATOM   1080  CB  GLU A 169      25.894  42.879  29.186  1.00130.84           C  
ANISOU 1080  CB  GLU A 169    19273  16445  13996   1876   -308  -2526       C  
ATOM   1081  CG  GLU A 169      24.859  41.905  28.599  1.00133.70           C  
ANISOU 1081  CG  GLU A 169    19349  17043  14407   1906   -304  -2463       C  
ATOM   1082  CD  GLU A 169      24.665  40.631  29.423  1.00129.41           C  
ANISOU 1082  CD  GLU A 169    18808  16772  13590   1648   -133  -2523       C  
ATOM   1083  OE1 GLU A 169      25.656  39.921  29.684  1.00118.55           O  
ANISOU 1083  OE1 GLU A 169    17649  15435  11961   1430   -195  -2390       O  
ATOM   1084  OE2 GLU A 169      23.513  40.336  29.807  1.00129.78           O  
ANISOU 1084  OE2 GLU A 169    18625  16989  13698   1658     55  -2688       O  
ATOM   1085  N   GLU A 170      23.779  45.175  29.024  1.00131.91           N  
ANISOU 1085  N   GLU A 170    18964  16212  14944   2489   -169  -2921       N  
ATOM   1086  CA  GLU A 170      22.418  45.652  28.796  1.00154.71           C  
ANISOU 1086  CA  GLU A 170    21482  19057  18243   2772   -103  -3063       C  
ATOM   1087  C   GLU A 170      22.402  46.750  27.727  1.00165.70           C  
ANISOU 1087  C   GLU A 170    22819  20117  20022   3047   -403  -2872       C  
ATOM   1088  O   GLU A 170      21.503  46.795  26.886  1.00190.19           O  
ANISOU 1088  O   GLU A 170    25613  23229  23421   3241   -559  -2745       O  
ATOM   1089  CB  GLU A 170      21.807  46.152  30.113  1.00171.38           C  
ANISOU 1089  CB  GLU A 170    23532  21145  20441   2811    283  -3516       C  
ATOM   1090  CG  GLU A 170      20.298  46.383  30.079  1.00183.92           C  
ANISOU 1090  CG  GLU A 170    24660  22772  22451   3074    441  -3720       C  
ATOM   1091  CD  GLU A 170      19.621  45.998  31.385  1.00191.21           C  
ANISOU 1091  CD  GLU A 170    25476  23941  23232   2937    899  -4124       C  
ATOM   1092  OE1 GLU A 170      20.148  45.111  32.090  1.00186.81           O  
ANISOU 1092  OE1 GLU A 170    25154  23636  22191   2589   1025  -4128       O  
ATOM   1093  OE2 GLU A 170      18.558  46.572  31.703  1.00198.35           O  
ANISOU 1093  OE2 GLU A 170    26053  24791  24518   3167   1134  -4431       O  
ATOM   1094  N   HIS A 171      23.382  47.648  27.779  1.00149.75           N  
ANISOU 1094  N   HIS A 171    21095  17799  18002   3043   -503  -2836       N  
ATOM   1095  CA  HIS A 171      23.513  48.694  26.766  1.00136.93           C  
ANISOU 1095  CA  HIS A 171    19480  15840  16708   3249   -817  -2604       C  
ATOM   1096  C   HIS A 171      23.973  48.113  25.431  1.00123.85           C  
ANISOU 1096  C   HIS A 171    17862  14314  14881   3142  -1143  -2168       C  
ATOM   1097  O   HIS A 171      23.539  48.550  24.367  1.00137.88           O  
ANISOU 1097  O   HIS A 171    19498  15974  16916   3301  -1419  -1926       O  
ATOM   1098  CB  HIS A 171      24.494  49.776  27.218  1.00136.55           C  
ANISOU 1098  CB  HIS A 171    19763  15440  16679   3221   -831  -2682       C  
ATOM   1099  CG  HIS A 171      23.833  51.037  27.681  1.00146.51           C  
ANISOU 1099  CG  HIS A 171    20927  16328  18411   3504   -730  -2970       C  
ATOM   1100  ND1 HIS A 171      23.386  51.212  28.972  1.00154.45           N  
ANISOU 1100  ND1 HIS A 171    21904  17333  19445   3523   -346  -3443       N  
ATOM   1101  CD2 HIS A 171      23.540  52.182  27.022  1.00152.35           C  
ANISOU 1101  CD2 HIS A 171    21592  16665  19628   3776   -959  -2860       C  
ATOM   1102  CE1 HIS A 171      22.847  52.413  29.090  1.00163.47           C  
ANISOU 1102  CE1 HIS A 171    22947  18078  21088   3817   -316  -3651       C  
ATOM   1103  NE2 HIS A 171      22.928  53.022  27.920  1.00163.51           N  
ANISOU 1103  NE2 HIS A 171    22918  17814  21395   3985   -704  -3287       N  
ATOM   1104  N   MET A 172      24.858  47.125  25.505  1.00118.32           N  
ANISOU 1104  N   MET A 172    17354  13853  13747   2860  -1108  -2074       N  
ATOM   1105  CA  MET A 172      25.354  46.427  24.325  1.00112.10           C  
ANISOU 1105  CA  MET A 172    16615  13225  12753   2723  -1341  -1731       C  
ATOM   1106  C   MET A 172      24.242  45.755  23.534  1.00141.67           C  
ANISOU 1106  C   MET A 172    20056  17187  16585   2795  -1439  -1628       C  
ATOM   1107  O   MET A 172      24.234  45.800  22.309  1.00141.98           O  
ANISOU 1107  O   MET A 172    20074  17232  16641   2798  -1712  -1341       O  
ATOM   1108  CB  MET A 172      26.396  45.391  24.726  1.00107.23           C  
ANISOU 1108  CB  MET A 172    16203  12815  11723   2438  -1233  -1719       C  
ATOM   1109  CG  MET A 172      27.656  45.995  25.309  1.00 98.53           C  
ANISOU 1109  CG  MET A 172    15401  11525  10510   2320  -1212  -1742       C  
ATOM   1110  SD  MET A 172      28.898  44.761  25.692  1.00135.03           S  
ANISOU 1110  SD  MET A 172    20207  16372  14725   2007  -1146  -1675       S  
ATOM   1111  CE  MET A 172      29.534  44.427  24.057  1.00 70.49           C  
ANISOU 1111  CE  MET A 172    12048   8258   6477   1948  -1381  -1326       C  
ATOM   1112  N   GLU A 173      23.339  45.081  24.234  1.00167.61           N  
ANISOU 1112  N   GLU A 173    23121  20676  19886   2807  -1217  -1853       N  
ATOM   1113  CA  GLU A 173      22.205  44.427  23.593  1.00169.65           C  
ANISOU 1113  CA  GLU A 173    23060  21153  20247   2856  -1300  -1780       C  
ATOM   1114  C   GLU A 173      21.259  45.468  22.984  1.00156.46           C  
ANISOU 1114  C   GLU A 173    21125  19278  19044   3151  -1505  -1702       C  
ATOM   1115  O   GLU A 173      20.722  45.278  21.894  1.00160.29           O  
ANISOU 1115  O   GLU A 173    21445  19850  19608   3176  -1777  -1458       O  
ATOM   1116  CB  GLU A 173      21.481  43.518  24.602  1.00181.95           C  
ANISOU 1116  CB  GLU A 173    24441  22970  21721   2772   -988  -2049       C  
ATOM   1117  CG  GLU A 173      20.204  44.082  25.220  1.00196.46           C  
ANISOU 1117  CG  GLU A 173    25931  24771  23943   3003   -809  -2311       C  
ATOM   1118  CD  GLU A 173      20.011  43.641  26.656  1.00203.07           C  
ANISOU 1118  CD  GLU A 173    26769  25765  24623   2875   -402  -2654       C  
ATOM   1119  OE1 GLU A 173      20.778  42.768  27.117  1.00202.80           O  
ANISOU 1119  OE1 GLU A 173    26986  25885  24183   2597   -311  -2638       O  
ATOM   1120  OE2 GLU A 173      19.091  44.164  27.321  1.00204.67           O  
ANISOU 1120  OE2 GLU A 173    26715  25936  25113   3044   -175  -2937       O  
ATOM   1121  N   ALA A 174      21.097  46.580  23.693  1.00137.63           N  
ANISOU 1121  N   ALA A 174    18716  16603  16975   3363  -1391  -1908       N  
ATOM   1122  CA  ALA A 174      20.190  47.660  23.311  1.00145.69           C  
ANISOU 1122  CA  ALA A 174    19462  17356  18538   3690  -1560  -1879       C  
ATOM   1123  C   ALA A 174      20.529  48.419  22.027  1.00159.62           C  
ANISOU 1123  C   ALA A 174    21328  18883  20437   3753  -2003  -1473       C  
ATOM   1124  O   ALA A 174      19.632  48.759  21.256  1.00162.38           O  
ANISOU 1124  O   ALA A 174    21393  19170  21134   3935  -2275  -1287       O  
ATOM   1125  CB  ALA A 174      20.084  48.650  24.460  1.00146.94           C  
ANISOU 1125  CB  ALA A 174    19623  17222  18984   3881  -1287  -2250       C  
ATOM   1126  N   ALA A 175      21.811  48.689  21.799  1.00166.57           N  
ANISOU 1126  N   ALA A 175    22602  19642  21046   3585  -2090  -1319       N  
ATOM   1127  CA  ALA A 175      22.231  49.511  20.654  1.00168.74           C  
ANISOU 1127  CA  ALA A 175    23018  19677  21416   3600  -2487   -933       C  
ATOM   1128  C   ALA A 175      21.981  48.941  19.234  1.00166.59           C  
ANISOU 1128  C   ALA A 175    22679  19639  20980   3468  -2828   -543       C  
ATOM   1129  O   ALA A 175      21.397  49.652  18.415  1.00176.37           O  
ANISOU 1129  O   ALA A 175    23780  20700  22532   3614  -3174   -278       O  
ATOM   1130  CB  ALA A 175      23.720  49.885  20.810  1.00164.31           C  
ANISOU 1130  CB  ALA A 175    22885  18968  20578   3407  -2456   -880       C  
ATOM   1131  N   GLY A 176      22.387  47.709  18.909  1.00140.66           N  
ANISOU 1131  N   GLY A 176    19492  16725  17229   3192  -2758   -500       N  
ATOM   1132  CA  GLY A 176      23.055  46.790  19.806  1.00133.24           C  
ANISOU 1132  CA  GLY A 176    18696  15983  15946   3015  -2405   -759       C  
ATOM   1133  C   GLY A 176      23.680  45.581  19.142  1.00134.73           C  
ANISOU 1133  C   GLY A 176    19031  16491  15671   2716  -2414   -630       C  
ATOM   1134  O   GLY A 176      23.011  44.833  18.435  1.00133.27           O  
ANISOU 1134  O   GLY A 176    18686  16544  15406   2647  -2531   -532       O  
ATOM   1135  N   ILE A 177      24.977  45.401  19.358  1.00135.61           N  
ANISOU 1135  N   ILE A 177    19436  16594  15495   2535  -2295   -640       N  
ATOM   1136  CA  ILE A 177      25.694  44.254  18.812  1.00148.82           C  
ANISOU 1136  CA  ILE A 177    21244  18530  16771   2270  -2255   -566       C  
ATOM   1137  C   ILE A 177      25.648  43.132  19.840  1.00140.86           C  
ANISOU 1137  C   ILE A 177    20183  17704  15633   2200  -1963   -832       C  
ATOM   1138  O   ILE A 177      25.833  43.365  21.036  1.00129.71           O  
ANISOU 1138  O   ILE A 177    18806  16190  14287   2254  -1764  -1038       O  
ATOM   1139  CB  ILE A 177      27.151  44.582  18.430  1.00166.52           C  
ANISOU 1139  CB  ILE A 177    23785  20682  18803   2104  -2283   -420       C  
ATOM   1140  CG1 ILE A 177      27.180  45.667  17.350  1.00180.36           C  
ANISOU 1140  CG1 ILE A 177    25611  22268  20648   2121  -2591   -114       C  
ATOM   1141  CG2 ILE A 177      27.867  43.331  17.926  1.00167.44           C  
ANISOU 1141  CG2 ILE A 177    23996  21062  18561   1857  -2191   -404       C  
ATOM   1142  CD1 ILE A 177      28.497  45.770  16.598  1.00183.52           C  
ANISOU 1142  CD1 ILE A 177    26274  22686  20768   1882  -2633     81       C  
ATOM   1143  N   ALA A 178      25.400  41.913  19.373  1.00146.67           N  
ANISOU 1143  N   ALA A 178    20855  18702  16172   2054  -1949   -823       N  
ATOM   1144  CA  ALA A 178      25.413  40.759  20.258  1.00142.00           C  
ANISOU 1144  CA  ALA A 178    20238  18267  15448   1950  -1707  -1025       C  
ATOM   1145  C   ALA A 178      26.847  40.332  20.523  1.00123.83           C  
ANISOU 1145  C   ALA A 178    18186  15941  12922   1787  -1597  -1027       C  
ATOM   1146  O   ALA A 178      27.757  40.651  19.757  1.00118.23           O  
ANISOU 1146  O   ALA A 178    17636  15174  12114   1717  -1695   -872       O  
ATOM   1147  CB  ALA A 178      24.612  39.608  19.655  1.00158.81           C  
ANISOU 1147  CB  ALA A 178    22212  20647  17483   1843  -1748  -1016       C  
ATOM   1148  N   LEU A 179      27.025  39.565  21.592  1.00114.76           N  
ANISOU 1148  N   LEU A 179    17053  14850  11699   1710  -1399  -1188       N  
ATOM   1149  CA  LEU A 179      28.342  39.302  22.152  1.00 98.43           C  
ANISOU 1149  CA  LEU A 179    15183  12719   9496   1589  -1308  -1195       C  
ATOM   1150  C   LEU A 179      29.101  38.184  21.456  1.00 97.88           C  
ANISOU 1150  C   LEU A 179    15180  12752   9256   1426  -1311  -1122       C  
ATOM   1151  O   LEU A 179      28.542  37.137  21.139  1.00120.24           O  
ANISOU 1151  O   LEU A 179    17923  15732  12031   1357  -1291  -1157       O  
ATOM   1152  CB  LEU A 179      28.198  38.946  23.630  1.00 98.21           C  
ANISOU 1152  CB  LEU A 179    15155  12708   9450   1546  -1129  -1371       C  
ATOM   1153  CG  LEU A 179      27.501  39.965  24.531  1.00108.90           C  
ANISOU 1153  CG  LEU A 179    16454  13967  10955   1683  -1044  -1528       C  
ATOM   1154  CD1 LEU A 179      27.109  39.313  25.844  1.00114.82           C  
ANISOU 1154  CD1 LEU A 179    17180  14832  11613   1576   -841  -1708       C  
ATOM   1155  CD2 LEU A 179      28.376  41.177  24.771  1.00113.67           C  
ANISOU 1155  CD2 LEU A 179    17236  14339  11613   1731  -1090  -1508       C  
ATOM   1156  N   GLU A 180      30.381  38.429  21.203  1.00 96.87           N  
ANISOU 1156  N   GLU A 180    15200  12536   9070   1363  -1327  -1033       N  
ATOM   1157  CA  GLU A 180      31.270  37.387  20.716  1.00111.71           C  
ANISOU 1157  CA  GLU A 180    17127  14480  10839   1226  -1278  -1009       C  
ATOM   1158  C   GLU A 180      31.736  36.580  21.928  1.00101.65           C  
ANISOU 1158  C   GLU A 180    15871  13178   9572   1158  -1173  -1088       C  
ATOM   1159  O   GLU A 180      31.415  36.934  23.058  1.00 94.66           O  
ANISOU 1159  O   GLU A 180    14995  12250   8722   1187  -1139  -1152       O  
ATOM   1160  CB  GLU A 180      32.441  37.981  19.930  1.00130.31           C  
ANISOU 1160  CB  GLU A 180    19589  16772  13150   1176  -1318   -884       C  
ATOM   1161  CG  GLU A 180      32.132  38.153  18.438  1.00140.42           C  
ANISOU 1161  CG  GLU A 180    20874  18154  14326   1136  -1410   -788       C  
ATOM   1162  CD  GLU A 180      33.258  38.817  17.663  1.00150.75           C  
ANISOU 1162  CD  GLU A 180    22295  19423  15561   1047  -1430   -654       C  
ATOM   1163  OE1 GLU A 180      34.437  38.630  18.039  1.00166.29           O  
ANISOU 1163  OE1 GLU A 180    24296  21336  17550    988  -1327   -670       O  
ATOM   1164  OE2 GLU A 180      32.961  39.510  16.664  1.00151.44           O  
ANISOU 1164  OE2 GLU A 180    22428  19543  15571   1018  -1559   -517       O  
ATOM   1165  N   GLU A 181      32.459  35.488  21.698  1.00108.18           N  
ANISOU 1165  N   GLU A 181    16706  14024  10372   1060  -1125  -1086       N  
ATOM   1166  CA  GLU A 181      32.808  34.544  22.768  1.00109.05           C  
ANISOU 1166  CA  GLU A 181    16822  14098  10513    982  -1074  -1118       C  
ATOM   1167  C   GLU A 181      33.580  35.180  23.922  1.00105.77           C  
ANISOU 1167  C   GLU A 181    16493  13575  10122    960  -1096  -1075       C  
ATOM   1168  O   GLU A 181      33.237  34.979  25.086  1.00116.16           O  
ANISOU 1168  O   GLU A 181    17834  14895  11406    905  -1078  -1112       O  
ATOM   1169  CB  GLU A 181      33.616  33.373  22.199  1.00119.55           C  
ANISOU 1169  CB  GLU A 181    18132  15407  11884    911  -1037  -1116       C  
ATOM   1170  CG  GLU A 181      34.131  32.402  23.253  1.00114.51           C  
ANISOU 1170  CG  GLU A 181    17498  14681  11331    834  -1036  -1094       C  
ATOM   1171  CD  GLU A 181      35.495  31.838  22.919  1.00115.16           C  
ANISOU 1171  CD  GLU A 181    17552  14653  11551    816  -1023  -1053       C  
ATOM   1172  OE1 GLU A 181      36.000  32.093  21.804  1.00107.40           O  
ANISOU 1172  OE1 GLU A 181    16546  13692  10568    845   -966  -1078       O  
ATOM   1173  OE2 GLU A 181      36.068  31.145  23.782  1.00127.12           O  
ANISOU 1173  OE2 GLU A 181    19056  16061  13181    764  -1071   -990       O  
ATOM   1174  N   ALA A 182      34.629  35.926  23.590  1.00101.24           N  
ANISOU 1174  N   ALA A 182    15970  12917   9579    968  -1135   -996       N  
ATOM   1175  CA  ALA A 182      35.491  36.565  24.585  1.00 98.51           C  
ANISOU 1175  CA  ALA A 182    15712  12465   9254    916  -1184   -946       C  
ATOM   1176  C   ALA A 182      34.719  37.357  25.637  1.00 81.00           C  
ANISOU 1176  C   ALA A 182    13570  10229   6979    932  -1178  -1033       C  
ATOM   1177  O   ALA A 182      35.044  37.312  26.823  1.00 73.10           O  
ANISOU 1177  O   ALA A 182    12648   9198   5930    827  -1194  -1040       O  
ATOM   1178  CB  ALA A 182      36.492  37.469  23.894  1.00 99.17           C  
ANISOU 1178  CB  ALA A 182    15826  12475   9378    920  -1225   -853       C  
ATOM   1179  N   GLU A 183      33.709  38.096  25.194  1.00 80.39           N  
ANISOU 1179  N   GLU A 183    13463  10167   6913   1054  -1157  -1101       N  
ATOM   1180  CA  GLU A 183      32.916  38.918  26.100  1.00 91.00           C  
ANISOU 1180  CA  GLU A 183    14847  11477   8253   1102  -1110  -1233       C  
ATOM   1181  C   GLU A 183      32.044  38.058  27.010  1.00100.36           C  
ANISOU 1181  C   GLU A 183    15983  12791   9358   1034  -1004  -1347       C  
ATOM   1182  O   GLU A 183      31.918  38.344  28.199  1.00111.64           O  
ANISOU 1182  O   GLU A 183    17496  14214  10707    956   -938  -1451       O  
ATOM   1183  CB  GLU A 183      32.058  39.913  25.315  1.00 94.24           C  
ANISOU 1183  CB  GLU A 183    15195  11839   8772   1279  -1137  -1260       C  
ATOM   1184  CG  GLU A 183      32.846  41.045  24.643  1.00113.64           C  
ANISOU 1184  CG  GLU A 183    17746  14134  11299   1316  -1250  -1140       C  
ATOM   1185  CD  GLU A 183      33.501  40.614  23.337  1.00129.93           C  
ANISOU 1185  CD  GLU A 183    19783  16258  13325   1269  -1315   -973       C  
ATOM   1186  OE1 GLU A 183      32.892  39.796  22.621  1.00153.77           O  
ANISOU 1186  OE1 GLU A 183    22698  19420  16308   1282  -1301   -971       O  
ATOM   1187  OE2 GLU A 183      34.609  41.102  23.013  1.00116.82           O  
ANISOU 1187  OE2 GLU A 183    18207  14513  11664   1198  -1368   -859       O  
ATOM   1188  N   ILE A 184      31.439  37.009  26.461  1.00 94.96           N  
ANISOU 1188  N   ILE A 184    15176  12231   8673   1031   -981  -1334       N  
ATOM   1189  CA  ILE A 184      30.596  36.138  27.278  1.00100.98           C  
ANISOU 1189  CA  ILE A 184    15887  13123   9359    932   -883  -1419       C  
ATOM   1190  C   ILE A 184      31.398  35.358  28.314  1.00107.12           C  
ANISOU 1190  C   ILE A 184    16784  13889  10028    730   -904  -1348       C  
ATOM   1191  O   ILE A 184      30.985  35.239  29.465  1.00119.86           O  
ANISOU 1191  O   ILE A 184    18452  15572  11517    600   -825  -1420       O  
ATOM   1192  CB  ILE A 184      29.813  35.130  26.416  1.00115.30           C  
ANISOU 1192  CB  ILE A 184    17551  15055  11203    942   -879  -1408       C  
ATOM   1193  CG1 ILE A 184      29.296  35.800  25.141  1.00119.22           C  
ANISOU 1193  CG1 ILE A 184    17945  15558  11796   1110   -938  -1401       C  
ATOM   1194  CG2 ILE A 184      28.675  34.506  27.221  1.00123.53           C  
ANISOU 1194  CG2 ILE A 184    18507  16242  12184    848   -761  -1511       C  
ATOM   1195  CD1 ILE A 184      28.254  34.985  24.395  1.00113.73           C  
ANISOU 1195  CD1 ILE A 184    17091  15007  11113   1102   -944  -1420       C  
ATOM   1196  N   SER A 185      32.555  34.847  27.906  1.00100.94           N  
ANISOU 1196  N   SER A 185    16034  13019   9300    693  -1012  -1203       N  
ATOM   1197  CA  SER A 185      33.405  34.064  28.799  1.00 97.86           C  
ANISOU 1197  CA  SER A 185    15727  12585   8870    516  -1091  -1086       C  
ATOM   1198  C   SER A 185      33.893  34.917  29.970  1.00102.86           C  
ANISOU 1198  C   SER A 185    16515  13183   9385    406  -1125  -1093       C  
ATOM   1199  O   SER A 185      33.933  34.453  31.111  1.00104.94           O  
ANISOU 1199  O   SER A 185    16874  13488   9510    209  -1152  -1053       O  
ATOM   1200  CB  SER A 185      34.582  33.455  28.025  1.00 94.16           C  
ANISOU 1200  CB  SER A 185    15209  12008   8560    543  -1189   -951       C  
ATOM   1201  OG  SER A 185      35.599  34.404  27.760  1.00105.33           O  
ANISOU 1201  OG  SER A 185    16656  13333  10030    591  -1247   -901       O  
ATOM   1202  N   ALA A 186      34.253  36.166  29.682  1.00 95.55           N  
ANISOU 1202  N   ALA A 186    15631  12176   8496    506  -1135  -1137       N  
ATOM   1203  CA  ALA A 186      34.676  37.107  30.712  1.00 81.94           C  
ANISOU 1203  CA  ALA A 186    14073  10400   6661    398  -1161  -1183       C  
ATOM   1204  C   ALA A 186      33.527  37.390  31.678  1.00 92.62           C  
ANISOU 1204  C   ALA A 186    15487  11858   7846    335   -999  -1388       C  
ATOM   1205  O   ALA A 186      33.727  37.502  32.888  1.00113.90           O  
ANISOU 1205  O   ALA A 186    18342  14586  10349    127  -1000  -1425       O  
ATOM   1206  CB  ALA A 186      35.178  38.402  30.080  1.00 70.10           C  
ANISOU 1206  CB  ALA A 186    12604   8765   5268    524  -1199  -1199       C  
ATOM   1207  N   LEU A 187      32.328  37.521  31.120  1.00 83.15           N  
ANISOU 1207  N   LEU A 187    14150  10723   6721    501   -858  -1526       N  
ATOM   1208  CA  LEU A 187      31.104  37.701  31.893  1.00 86.70           C  
ANISOU 1208  CA  LEU A 187    14579  11295   7067    471   -657  -1746       C  
ATOM   1209  C   LEU A 187      30.782  36.472  32.729  1.00 90.12           C  
ANISOU 1209  C   LEU A 187    15034  11898   7311    229   -611  -1702       C  
ATOM   1210  O   LEU A 187      30.254  36.582  33.836  1.00103.45           O  
ANISOU 1210  O   LEU A 187    16804  13702   8800     61   -462  -1850       O  
ATOM   1211  CB  LEU A 187      29.941  38.017  30.960  1.00101.65           C  
ANISOU 1211  CB  LEU A 187    16258  13216   9149    717   -562  -1856       C  
ATOM   1212  CG  LEU A 187      29.864  39.472  30.513  1.00109.76           C  
ANISOU 1212  CG  LEU A 187    17281  14073  10350    935   -564  -1958       C  
ATOM   1213  CD1 LEU A 187      28.736  39.666  29.517  1.00110.21           C  
ANISOU 1213  CD1 LEU A 187    17099  14155  10620   1169   -537  -2000       C  
ATOM   1214  CD2 LEU A 187      29.668  40.359  31.732  1.00118.11           C  
ANISOU 1214  CD2 LEU A 187    18470  15090  11318    869   -410  -2202       C  
ATOM   1215  N   LEU A 188      31.066  35.299  32.175  1.00 89.79           N  
ANISOU 1215  N   LEU A 188    14920  11866   7332    200   -727  -1508       N  
ATOM   1216  CA  LEU A 188      30.876  34.049  32.899  1.00102.72           C  
ANISOU 1216  CA  LEU A 188    16591  13612   8825    -43   -736  -1408       C  
ATOM   1217  C   LEU A 188      31.819  33.962  34.093  1.00115.67           C  
ANISOU 1217  C   LEU A 188    18452  15228  10268   -309   -860  -1285       C  
ATOM   1218  O   LEU A 188      31.411  33.571  35.186  1.00124.38           O  
ANISOU 1218  O   LEU A 188    19663  16468  11128   -570   -796  -1297       O  
ATOM   1219  CB  LEU A 188      31.091  32.852  31.971  1.00 93.23           C  
ANISOU 1219  CB  LEU A 188    15276  12358   7790      3   -852  -1237       C  
ATOM   1220  CG  LEU A 188      30.940  31.467  32.603  1.00 79.02           C  
ANISOU 1220  CG  LEU A 188    13512  10610   5903   -240   -902  -1096       C  
ATOM   1221  CD1 LEU A 188      29.489  31.036  32.551  1.00 78.84           C  
ANISOU 1221  CD1 LEU A 188    13361  10762   5832   -276   -723  -1223       C  
ATOM   1222  CD2 LEU A 188      31.833  30.448  31.915  1.00 62.80           C  
ANISOU 1222  CD2 LEU A 188    11420   8386   4055   -206  -1087   -898       C  
ATOM   1223  N   LYS A 189      33.072  34.355  33.876  1.00113.54           N  
ANISOU 1223  N   LYS A 189    18246  14801  10092   -266  -1043  -1159       N  
ATOM   1224  CA  LYS A 189      34.110  34.307  34.909  1.00103.48           C  
ANISOU 1224  CA  LYS A 189    17159  13489   8668   -517  -1227  -1001       C  
ATOM   1225  C   LYS A 189      33.709  35.072  36.168  1.00103.45           C  
ANISOU 1225  C   LYS A 189    17358  13605   8345   -734  -1106  -1182       C  
ATOM   1226  O   LYS A 189      33.860  34.572  37.281  1.00112.87           O  
ANISOU 1226  O   LYS A 189    18714  14892   9280  -1052  -1182  -1079       O  
ATOM   1227  CB  LYS A 189      35.425  34.871  34.361  1.00 85.95           C  
ANISOU 1227  CB  LYS A 189    14927  11094   6635   -407  -1408   -886       C  
ATOM   1228  CG  LYS A 189      36.506  35.073  35.397  1.00 75.56           C  
ANISOU 1228  CG  LYS A 189    13787   9741   5182   -660  -1621   -738       C  
ATOM   1229  CD  LYS A 189      37.727  35.764  34.803  1.00 92.05           C  
ANISOU 1229  CD  LYS A 189    15827  11672   7475   -550  -1769   -650       C  
ATOM   1230  CE  LYS A 189      38.769  34.762  34.326  1.00 97.14           C  
ANISOU 1230  CE  LYS A 189    16311  12213   8385   -519  -1979   -376       C  
ATOM   1231  NZ  LYS A 189      40.088  35.416  34.075  1.00 94.43           N  
ANISOU 1231  NZ  LYS A 189    15924  11754   8202   -504  -2141   -266       N  
ATOM   1232  N   VAL A 190      33.163  36.267  35.978  1.00100.89           N  
ANISOU 1232  N   VAL A 190    17026  13270   8038   -570   -915  -1455       N  
ATOM   1233  CA  VAL A 190      32.801  37.134  37.090  1.00101.00           C  
ANISOU 1233  CA  VAL A 190    17229  13364   7784   -743   -755  -1702       C  
ATOM   1234  C   VAL A 190      31.654  36.553  37.904  1.00109.59           C  
ANISOU 1234  C   VAL A 190    18328  14688   8623   -941   -527  -1834       C  
ATOM   1235  O   VAL A 190      31.697  36.546  39.136  1.00124.54           O  
ANISOU 1235  O   VAL A 190    20327  16709  10284  -1240   -480  -1849       O  
ATOM   1236  CB  VAL A 190      32.412  38.529  36.589  1.00 91.78           C  
ANISOU 1236  CB  VAL A 190    16015  12075   6783   -472   -596  -1978       C  
ATOM   1237  CG1 VAL A 190      31.940  39.404  37.747  1.00 84.65           C  
ANISOU 1237  CG1 VAL A 190    15299  11235   5628   -637   -376  -2303       C  
ATOM   1238  CG2 VAL A 190      33.591  39.156  35.895  1.00 92.86           C  
ANISOU 1238  CG2 VAL A 190    16175  11993   7115   -346   -819  -1833       C  
ATOM   1239  N   SER A 191      30.630  36.065  37.212  1.00102.50           N  
ANISOU 1239  N   SER A 191    17195  13863   7885   -764   -378  -1889       N  
ATOM   1240  CA  SER A 191      29.482  35.464  37.877  1.00105.93           C  
ANISOU 1240  CA  SER A 191    17591  14539   8120   -953   -144  -2006       C  
ATOM   1241  C   SER A 191      29.935  34.275  38.717  1.00101.71           C  
ANISOU 1241  C   SER A 191    17223  14101   7319  -1339   -314  -1725       C  
ATOM   1242  O   SER A 191      29.400  34.025  39.798  1.00 79.09           O  
ANISOU 1242  O   SER A 191    14393  11434   4224  -1620   -159  -1773       O  
ATOM   1243  CB  SER A 191      28.425  35.037  36.857  1.00 97.04           C  
ANISOU 1243  CB  SER A 191    16156  13458   7255   -705    -26  -2053       C  
ATOM   1244  OG  SER A 191      27.719  36.157  36.354  1.00 96.26           O  
ANISOU 1244  OG  SER A 191    15897  13316   7360   -405    163  -2334       O  
ATOM   1245  N   ALA A 192      30.938  33.559  38.215  1.00 93.55           N  
ANISOU 1245  N   ALA A 192    16188  12906   6450  -1310   -632  -1398       N  
ATOM   1246  CA  ALA A 192      31.532  32.438  38.932  1.00 89.79           C  
ANISOU 1246  CA  ALA A 192    15852  12446   5816  -1638   -871  -1072       C  
ATOM   1247  C   ALA A 192      32.267  32.892  40.180  1.00 91.60           C  
ANISOU 1247  C   ALA A 192    16226  12702   5877  -1904   -963   -995       C  
ATOM   1248  O   ALA A 192      32.097  32.308  41.249  1.00101.69           O  
ANISOU 1248  O   ALA A 192    17588  14112   6938  -2241   -971   -869       O  
ATOM   1249  CB  ALA A 192      32.480  31.674  38.019  1.00 89.88           C  
ANISOU 1249  CB  ALA A 192    15754  12230   6167  -1469  -1169   -778       C  
ATOM   1250  N   ALA A 193      33.086  33.930  40.034  1.00 91.75           N  
ANISOU 1250  N   ALA A 193    16284  12589   5986  -1776  -1043  -1060       N  
ATOM   1251  CA  ALA A 193      33.878  34.466  41.140  1.00 97.75           C  
ANISOU 1251  CA  ALA A 193    17191  13356   6596  -2029  -1156   -999       C  
ATOM   1252  C   ALA A 193      33.004  35.117  42.213  1.00 89.78           C  
ANISOU 1252  C   ALA A 193    16246  12543   5322  -2208   -839  -1294       C  
ATOM   1253  O   ALA A 193      33.260  34.965  43.409  1.00104.85           O  
ANISOU 1253  O   ALA A 193    18291  14548   6997  -2554   -895  -1192       O  
ATOM   1254  CB  ALA A 193      34.902  35.457  40.622  1.00 78.07           C  
ANISOU 1254  CB  ALA A 193    14722  10671   4272  -1852  -1304  -1019       C  
ATOM   1255  N   THR A 194      31.976  35.844  41.782  1.00 82.75           N  
ANISOU 1255  N   THR A 194    15259  11704   4479  -1976   -510  -1663       N  
ATOM   1256  CA  THR A 194      31.029  36.454  42.712  1.00 94.22           C  
ANISOU 1256  CA  THR A 194    16741  13337   5721  -2101   -162  -1997       C  
ATOM   1257  C   THR A 194      30.013  35.428  43.220  1.00 96.53           C  
ANISOU 1257  C   THR A 194    16979  13865   5832  -2318     13  -1963       C  
ATOM   1258  O   THR A 194      29.146  35.760  44.026  1.00116.35           O  
ANISOU 1258  O   THR A 194    19495  16558   8155  -2457    328  -2225       O  
ATOM   1259  CB  THR A 194      30.278  37.645  42.079  1.00102.21           C  
ANISOU 1259  CB  THR A 194    17652  14286   6897  -1758    125  -2421       C  
ATOM   1260  OG1 THR A 194      29.595  37.213  40.898  1.00113.97           O  
ANISOU 1260  OG1 THR A 194    18960  15757   8585  -1483    185  -2438       O  
ATOM   1261  CG2 THR A 194      31.247  38.758  41.724  1.00 85.01           C  
ANISOU 1261  CG2 THR A 194    15568  11867   4865  -1606    -31  -2468       C  
ATOM   1262  N   GLY A 195      30.129  34.188  42.747  1.00 86.33           N  
ANISOU 1262  N   GLY A 195    15640  12558   4603  -2359   -187  -1646       N  
ATOM   1263  CA  GLY A 195      29.248  33.113  43.170  1.00 99.53           C  
ANISOU 1263  CA  GLY A 195    17277  14427   6111  -2603    -68  -1560       C  
ATOM   1264  C   GLY A 195      27.778  33.313  42.842  1.00118.88           C  
ANISOU 1264  C   GLY A 195    19543  17053   8575  -2463    336  -1906       C  
ATOM   1265  O   GLY A 195      26.906  32.950  43.633  1.00133.84           O  
ANISOU 1265  O   GLY A 195    21422  19177  10255  -2727    575  -1986       O  
ATOM   1266  N   ARG A 196      27.495  33.875  41.669  1.00122.20           N  
ANISOU 1266  N   ARG A 196    19812  17368   9250  -2068    409  -2104       N  
ATOM   1267  CA  ARG A 196      26.113  34.006  41.212  1.00120.96           C  
ANISOU 1267  CA  ARG A 196    19438  17363   9159  -1915    757  -2412       C  
ATOM   1268  C   ARG A 196      25.676  32.765  40.438  1.00119.66           C  
ANISOU 1268  C   ARG A 196    19162  17249   9053  -1936    669  -2215       C  
ATOM   1269  O   ARG A 196      26.111  32.543  39.310  1.00119.40           O  
ANISOU 1269  O   ARG A 196    19030  17013   9323  -1660    439  -2056       O  
ATOM   1270  CB  ARG A 196      25.960  35.239  40.316  1.00113.32           C  
ANISOU 1270  CB  ARG A 196    18370  16241   8445  -1498    867  -2722       C  
ATOM   1271  CG  ARG A 196      26.278  36.568  40.988  1.00106.33           C  
ANISOU 1271  CG  ARG A 196    17591  15273   7538  -1451    980  -2976       C  
ATOM   1272  CD  ARG A 196      25.324  36.886  42.119  1.00126.00           C  
ANISOU 1272  CD  ARG A 196    20038  17988   9848  -1635   1368  -3279       C  
ATOM   1273  NE  ARG A 196      23.942  36.995  41.665  1.00133.48           N  
ANISOU 1273  NE  ARG A 196    20703  19068  10945  -1451   1723  -3592       N  
ATOM   1274  CZ  ARG A 196      23.420  38.086  41.110  1.00139.43           C  
ANISOU 1274  CZ  ARG A 196    21301  19704  11973  -1097   1931  -3960       C  
ATOM   1275  NH1 ARG A 196      24.164  39.172  40.937  1.00135.88           N  
ANISOU 1275  NH1 ARG A 196    20996  18983  11651   -902   1817  -4056       N  
ATOM   1276  NH2 ARG A 196      22.151  38.093  40.726  1.00145.94           N  
ANISOU 1276  NH2 ARG A 196    21785  20665  13002   -929   2231  -4210       N  
ATOM   1277  N   GLU A 197      24.824  31.951  41.056  1.00125.87           N  
ANISOU 1277  N   GLU A 197    19895  18275   9653  -2235    840  -2190       N  
ATOM   1278  CA  GLU A 197      24.443  30.666  40.474  1.00134.36           C  
ANISOU 1278  CA  GLU A 197    20868  19384  10800  -2314    726  -1958       C  
ATOM   1279  C   GLU A 197      23.616  30.850  39.195  1.00141.74           C  
ANISOU 1279  C   GLU A 197    21420  20272  12161  -1898    822  -2110       C  
ATOM   1280  O   GLU A 197      23.935  30.273  38.157  1.00146.59           O  
ANISOU 1280  O   GLU A 197    21940  20703  13054  -1705    573  -1905       O  
ATOM   1281  CB  GLU A 197      23.695  29.767  41.477  1.00145.75           C  
ANISOU 1281  CB  GLU A 197    22353  21102  11921  -2783    889  -1883       C  
ATOM   1282  CG  GLU A 197      22.415  30.350  42.094  1.00155.82           C  
ANISOU 1282  CG  GLU A 197    23441  22677  13087  -2858   1375  -2268       C  
ATOM   1283  CD  GLU A 197      22.672  31.349  43.216  1.00159.37           C  
ANISOU 1283  CD  GLU A 197    24014  23151  13388  -2936   1534  -2452       C  
ATOM   1284  OE1 GLU A 197      23.660  32.110  43.145  1.00156.29           O  
ANISOU 1284  OE1 GLU A 197    23763  22539  13080  -2749   1346  -2443       O  
ATOM   1285  OE2 GLU A 197      21.868  31.378  44.172  1.00165.18           O  
ANISOU 1285  OE2 GLU A 197    24705  24136  13920  -3204   1859  -2619       O  
ATOM   1286  N   ASN A 198      22.558  31.653  39.275  1.00137.12           N  
ANISOU 1286  N   ASN A 198    20612  19853  11633  -1769   1179  -2473       N  
ATOM   1287  CA  ASN A 198      21.634  31.829  38.160  1.00125.44           C  
ANISOU 1287  CA  ASN A 198    18744  18368  10551  -1416   1259  -2601       C  
ATOM   1288  C   ASN A 198      22.276  32.510  36.961  1.00130.29           C  
ANISOU 1288  C   ASN A 198    19302  18690  11512   -978   1020  -2561       C  
ATOM   1289  O   ASN A 198      21.956  32.204  35.814  1.00145.23           O  
ANISOU 1289  O   ASN A 198    20973  20514  13694   -755    892  -2477       O  
ATOM   1290  CB  ASN A 198      20.409  32.623  38.607  1.00134.06           C  
ANISOU 1290  CB  ASN A 198    19584  19681  11670  -1363   1693  -3006       C  
ATOM   1291  CG  ASN A 198      19.486  31.813  39.492  1.00160.55           C  
ANISOU 1291  CG  ASN A 198    22875  23376  14749  -1779   1969  -3049       C  
ATOM   1292  OD1 ASN A 198      19.788  30.672  39.845  1.00164.42           O  
ANISOU 1292  OD1 ASN A 198    23553  23921  14998  -2135   1812  -2752       O  
ATOM   1293  ND2 ASN A 198      18.354  32.400  39.859  1.00179.32           N  
ANISOU 1293  ND2 ASN A 198    24976  25975  17183  -1742   2385  -3417       N  
ATOM   1294  N   LYS A 199      23.175  33.447  37.233  1.00120.31           N  
ANISOU 1294  N   LYS A 199    18251  17266  10195   -889    961  -2622       N  
ATOM   1295  CA  LYS A 199      23.876  34.145  36.167  1.00113.26           C  
ANISOU 1295  CA  LYS A 199    17338  16100   9594   -523    739  -2565       C  
ATOM   1296  C   LYS A 199      24.836  33.239  35.395  1.00104.60           C  
ANISOU 1296  C   LYS A 199    16331  14842   8571   -520    390  -2215       C  
ATOM   1297  O   LYS A 199      24.945  33.354  34.177  1.00110.88           O  
ANISOU 1297  O   LYS A 199    16989  15501   9640   -242    245  -2150       O  
ATOM   1298  CB  LYS A 199      24.626  35.351  36.728  1.00114.52           C  
ANISOU 1298  CB  LYS A 199    17719  16126   9667   -479    763  -2714       C  
ATOM   1299  CG  LYS A 199      24.215  36.664  36.086  1.00111.74           C  
ANISOU 1299  CG  LYS A 199    17187  15631   9639    -89    856  -2956       C  
ATOM   1300  CD  LYS A 199      22.722  36.923  36.202  1.00113.72           C  
ANISOU 1300  CD  LYS A 199    17120  16057  10033     11   1185  -3250       C  
ATOM   1301  CE  LYS A 199      22.342  38.181  35.431  1.00111.19           C  
ANISOU 1301  CE  LYS A 199    16592  15537  10120    437   1204  -3429       C  
ATOM   1302  NZ  LYS A 199      20.920  38.578  35.628  1.00112.52           N  
ANISOU 1302  NZ  LYS A 199    16413  15845  10496    569   1534  -3748       N  
ATOM   1303  N   VAL A 200      25.526  32.341  36.092  1.00 94.35           N  
ANISOU 1303  N   VAL A 200    15258  13554   7038   -834    255  -1993       N  
ATOM   1304  CA  VAL A 200      26.394  31.379  35.416  1.00 93.21           C  
ANISOU 1304  CA  VAL A 200    15165  13236   7014   -827    -50  -1685       C  
ATOM   1305  C   VAL A 200      25.562  30.477  34.508  1.00 94.47           C  
ANISOU 1305  C   VAL A 200    15094  13441   7358   -762    -49  -1643       C  
ATOM   1306  O   VAL A 200      25.983  30.132  33.402  1.00 85.12           O  
ANISOU 1306  O   VAL A 200    13847  12099   6396   -580   -227  -1531       O  
ATOM   1307  CB  VAL A 200      27.194  30.511  36.419  1.00 87.03           C  
ANISOU 1307  CB  VAL A 200    14641  12438   5988  -1190   -219  -1429       C  
ATOM   1308  CG1 VAL A 200      27.984  29.436  35.696  1.00 81.13           C  
ANISOU 1308  CG1 VAL A 200    13895  11483   5449  -1151   -508  -1139       C  
ATOM   1309  CG2 VAL A 200      28.121  31.370  37.250  1.00 74.09           C  
ANISOU 1309  CG2 VAL A 200    13241  10750   4159  -1281   -278  -1443       C  
ATOM   1310  N   TYR A 201      24.366  30.128  34.970  1.00102.96           N  
ANISOU 1310  N   TYR A 201    16041  14747   8333   -930    167  -1753       N  
ATOM   1311  CA  TYR A 201      23.455  29.299  34.190  1.00106.99           C  
ANISOU 1311  CA  TYR A 201    16319  15328   9003   -912    174  -1730       C  
ATOM   1312  C   TYR A 201      23.077  30.025  32.905  1.00115.25           C  
ANISOU 1312  C   TYR A 201    17129  16320  10342   -534    158  -1856       C  
ATOM   1313  O   TYR A 201      23.190  29.462  31.817  1.00129.79           O  
ANISOU 1313  O   TYR A 201    18902  18060  12352   -430    -13  -1749       O  
ATOM   1314  CB  TYR A 201      22.207  28.954  35.008  1.00105.78           C  
ANISOU 1314  CB  TYR A 201    16041  15466   8686  -1179    442  -1847       C  
ATOM   1315  CG  TYR A 201      21.219  28.033  34.319  1.00111.38           C  
ANISOU 1315  CG  TYR A 201    16507  16269   9542  -1227    444  -1811       C  
ATOM   1316  CD1 TYR A 201      21.522  26.695  34.088  1.00100.48           C  
ANISOU 1316  CD1 TYR A 201    15231  14780   8167  -1423    239  -1563       C  
ATOM   1317  CD2 TYR A 201      19.969  28.498  33.924  1.00124.46           C  
ANISOU 1317  CD2 TYR A 201    17820  18111  11357  -1086    639  -2027       C  
ATOM   1318  CE1 TYR A 201      20.612  25.851  33.464  1.00103.20           C  
ANISOU 1318  CE1 TYR A 201    15372  15200   8638  -1498    233  -1545       C  
ATOM   1319  CE2 TYR A 201      19.055  27.662  33.301  1.00119.94           C  
ANISOU 1319  CE2 TYR A 201    17016  17642  10915  -1161    618  -1987       C  
ATOM   1320  CZ  TYR A 201      19.381  26.341  33.074  1.00112.19           C  
ANISOU 1320  CZ  TYR A 201    16173  16554   9901  -1381    418  -1753       C  
ATOM   1321  OH  TYR A 201      18.467  25.515  32.457  1.00111.47           O  
ANISOU 1321  OH  TYR A 201    15869  16554   9932  -1483    390  -1728       O  
ATOM   1322  N   ARG A 202      22.668  31.286  33.031  1.00105.06           N  
ANISOU 1322  N   ARG A 202    15730  15078   9108   -339    324  -2083       N  
ATOM   1323  CA  ARG A 202      22.268  32.086  31.874  1.00 96.66           C  
ANISOU 1323  CA  ARG A 202    14443  13950   8333     12    279  -2172       C  
ATOM   1324  C   ARG A 202      23.393  32.228  30.855  1.00 87.26           C  
ANISOU 1324  C   ARG A 202    13383  12522   7249    192     12  -2008       C  
ATOM   1325  O   ARG A 202      23.183  32.048  29.655  1.00103.42           O  
ANISOU 1325  O   ARG A 202    15296  14534   9462    335   -121  -1948       O  
ATOM   1326  CB  ARG A 202      21.816  33.478  32.318  1.00 97.24           C  
ANISOU 1326  CB  ARG A 202    14420  14043   8483    195    484  -2432       C  
ATOM   1327  CG  ARG A 202      21.524  34.433  31.173  1.00 99.57           C  
ANISOU 1327  CG  ARG A 202    14515  14218   9100    565    384  -2478       C  
ATOM   1328  CD  ARG A 202      21.082  35.795  31.683  1.00114.60           C  
ANISOU 1328  CD  ARG A 202    16323  16084  11136    756    587  -2747       C  
ATOM   1329  NE  ARG A 202      19.925  35.708  32.570  1.00142.06           N  
ANISOU 1329  NE  ARG A 202    19589  19799  14589    642    914  -2987       N  
ATOM   1330  CZ  ARG A 202      18.683  36.029  32.216  1.00151.34           C  
ANISOU 1330  CZ  ARG A 202    20372  21075  16057    823   1031  -3133       C  
ATOM   1331  NH1 ARG A 202      18.434  36.468  30.989  1.00154.40           N  
ANISOU 1331  NH1 ARG A 202    20561  21336  16766   1118    805  -3035       N  
ATOM   1332  NH2 ARG A 202      17.691  35.918  33.090  1.00144.63           N  
ANISOU 1332  NH2 ARG A 202    19317  20460  15175    693   1369  -3368       N  
ATOM   1333  N   TYR A 203      24.586  32.551  31.342  1.00 74.07           N  
ANISOU 1333  N   TYR A 203    11969  10707   5467    156    -61  -1940       N  
ATOM   1334  CA  TYR A 203      25.732  32.790  30.470  1.00 80.67           C  
ANISOU 1334  CA  TYR A 203    12915  11333   6405    310   -276  -1803       C  
ATOM   1335  C   TYR A 203      26.295  31.505  29.865  1.00 80.79           C  
ANISOU 1335  C   TYR A 203    12978  11278   6442    214   -442  -1609       C  
ATOM   1336  O   TYR A 203      26.921  31.543  28.806  1.00101.98           O  
ANISOU 1336  O   TYR A 203    15666  13837   9245    357   -577  -1535       O  
ATOM   1337  CB  TYR A 203      26.827  33.567  31.207  1.00 95.80           C  
ANISOU 1337  CB  TYR A 203    15060  13122   8218    287   -306  -1794       C  
ATOM   1338  CG  TYR A 203      26.423  34.999  31.490  1.00104.42           C  
ANISOU 1338  CG  TYR A 203    16118  14197   9359    448   -168  -2010       C  
ATOM   1339  CD1 TYR A 203      25.273  35.536  30.920  1.00116.00           C  
ANISOU 1339  CD1 TYR A 203    17334  15723  11018    655    -69  -2157       C  
ATOM   1340  CD2 TYR A 203      27.199  35.821  32.294  1.00 94.76           C  
ANISOU 1340  CD2 TYR A 203    15104  12877   8024    396   -157  -2065       C  
ATOM   1341  CE1 TYR A 203      24.891  36.836  31.168  1.00115.97           C  
ANISOU 1341  CE1 TYR A 203    17281  15655  11129    831     53  -2362       C  
ATOM   1342  CE2 TYR A 203      26.827  37.126  32.541  1.00107.04           C  
ANISOU 1342  CE2 TYR A 203    16641  14374   9656    548    -24  -2291       C  
ATOM   1343  CZ  TYR A 203      25.671  37.626  31.973  1.00120.93           C  
ANISOU 1343  CZ  TYR A 203    18140  16163  11645    780     87  -2443       C  
ATOM   1344  OH  TYR A 203      25.286  38.924  32.209  1.00145.00           O  
ANISOU 1344  OH  TYR A 203    21150  19105  14838    960    215  -2676       O  
ATOM   1345  N   LEU A 204      26.121  30.377  30.544  1.00 69.17           N  
ANISOU 1345  N   LEU A 204    11554   9869   4857    -41   -427  -1531       N  
ATOM   1346  CA  LEU A 204      26.486  29.104  29.927  1.00 82.97           C  
ANISOU 1346  CA  LEU A 204    13322  11517   6685   -116   -571  -1381       C  
ATOM   1347  C   LEU A 204      25.567  28.815  28.742  1.00 90.02           C  
ANISOU 1347  C   LEU A 204    14014  12483   7706    -17   -567  -1454       C  
ATOM   1348  O   LEU A 204      26.007  28.301  27.716  1.00 87.24           O  
ANISOU 1348  O   LEU A 204    13669  12018   7461     46   -684  -1403       O  
ATOM   1349  CB  LEU A 204      26.435  27.953  30.929  1.00 87.03           C  
ANISOU 1349  CB  LEU A 204    13940  12052   7074   -428   -584  -1254       C  
ATOM   1350  CG  LEU A 204      27.617  27.832  31.890  1.00 94.16           C  
ANISOU 1350  CG  LEU A 204    15069  12828   7879   -570   -705  -1085       C  
ATOM   1351  CD1 LEU A 204      27.371  26.705  32.881  1.00 97.26           C  
ANISOU 1351  CD1 LEU A 204    15563  13260   8132   -913   -736   -929       C  
ATOM   1352  CD2 LEU A 204      28.924  27.626  31.128  1.00 85.33           C  
ANISOU 1352  CD2 LEU A 204    13999  11460   6963   -417   -897   -964       C  
ATOM   1353  N   HIS A 205      24.287  29.142  28.895  1.00 95.04           N  
ANISOU 1353  N   HIS A 205    14462  13319   8331    -19   -428  -1584       N  
ATOM   1354  CA  HIS A 205      23.326  29.018  27.803  1.00 91.53           C  
ANISOU 1354  CA  HIS A 205    13795  12969   8012     69   -455  -1643       C  
ATOM   1355  C   HIS A 205      23.605  30.039  26.719  1.00104.37           C  
ANISOU 1355  C   HIS A 205    15378  14523   9753    344   -551  -1665       C  
ATOM   1356  O   HIS A 205      23.419  29.769  25.534  1.00122.98           O  
ANISOU 1356  O   HIS A 205    17666  16883  12179    395   -668  -1641       O  
ATOM   1357  CB  HIS A 205      21.895  29.184  28.303  1.00 91.99           C  
ANISOU 1357  CB  HIS A 205    13612  13265   8076      7   -283  -1769       C  
ATOM   1358  CG  HIS A 205      21.308  27.932  28.868  1.00 99.73           C  
ANISOU 1358  CG  HIS A 205    14570  14356   8965   -302   -223  -1725       C  
ATOM   1359  ND1 HIS A 205      21.957  26.717  28.812  1.00 91.42           N  
ANISOU 1359  ND1 HIS A 205    13704  13162   7871   -485   -350  -1575       N  
ATOM   1360  CD2 HIS A 205      20.124  27.698  29.481  1.00114.76           C  
ANISOU 1360  CD2 HIS A 205    16280  16490  10834   -469    -49  -1807       C  
ATOM   1361  CE1 HIS A 205      21.203  25.792  29.379  1.00106.75           C  
ANISOU 1361  CE1 HIS A 205    15592  15224   9743   -766   -280  -1545       C  
ATOM   1362  NE2 HIS A 205      20.085  26.361  29.792  1.00120.17           N  
ANISOU 1362  NE2 HIS A 205    17061  17171  11429   -775    -87  -1684       N  
ATOM   1363  N   LYS A 206      24.051  31.217  27.138  1.00102.90           N  
ANISOU 1363  N   LYS A 206    15253  14273   9569    489   -508  -1706       N  
ATOM   1364  CA  LYS A 206      24.421  32.261  26.200  1.00 96.67           C  
ANISOU 1364  CA  LYS A 206    14459  13387   8885    725   -614  -1692       C  
ATOM   1365  C   LYS A 206      25.557  31.746  25.327  1.00 89.14           C  
ANISOU 1365  C   LYS A 206    13661  12299   7910    710   -756  -1569       C  
ATOM   1366  O   LYS A 206      25.562  31.942  24.115  1.00104.67           O  
ANISOU 1366  O   LYS A 206    15589  14257   9923    802   -864  -1535       O  
ATOM   1367  CB  LYS A 206      24.842  33.531  26.943  1.00101.49           C  
ANISOU 1367  CB  LYS A 206    15153  13907   9501    842   -543  -1758       C  
ATOM   1368  CG  LYS A 206      24.250  34.816  26.398  1.00109.71           C  
ANISOU 1368  CG  LYS A 206    16045  14921  10720   1089   -567  -1823       C  
ATOM   1369  CD  LYS A 206      22.761  34.897  26.686  1.00116.48           C  
ANISOU 1369  CD  LYS A 206    16617  15945  11694   1127   -439  -1965       C  
ATOM   1370  CE  LYS A 206      22.200  36.248  26.282  1.00127.89           C  
ANISOU 1370  CE  LYS A 206    17895  17311  13386   1402   -474  -2029       C  
ATOM   1371  NZ  LYS A 206      20.740  36.348  26.552  1.00133.75           N  
ANISOU 1371  NZ  LYS A 206    18298  18211  14309   1467   -342  -2178       N  
ATOM   1372  N   LEU A 207      26.495  31.043  25.951  1.00 72.49           N  
ANISOU 1372  N   LEU A 207    11718  10091   5732    577   -754  -1503       N  
ATOM   1373  CA  LEU A 207      27.612  30.439  25.239  1.00 76.87           C  
ANISOU 1373  CA  LEU A 207    12385  10505   6316    565   -850  -1416       C  
ATOM   1374  C   LEU A 207      27.163  29.384  24.244  1.00 91.40           C  
ANISOU 1374  C   LEU A 207    14161  12383   8184    496   -890  -1436       C  
ATOM   1375  O   LEU A 207      27.710  29.287  23.148  1.00105.78           O  
ANISOU 1375  O   LEU A 207    16017  14148  10028    546   -945  -1434       O  
ATOM   1376  CB  LEU A 207      28.604  29.812  26.220  1.00 87.27           C  
ANISOU 1376  CB  LEU A 207    13848  11697   7615    435   -864  -1324       C  
ATOM   1377  CG  LEU A 207      29.657  30.717  26.853  1.00 85.85           C  
ANISOU 1377  CG  LEU A 207    13787  11418   7414    484   -890  -1270       C  
ATOM   1378  CD1 LEU A 207      30.607  29.876  27.687  1.00 94.12           C  
ANISOU 1378  CD1 LEU A 207    14949  12343   8470    332   -965  -1137       C  
ATOM   1379  CD2 LEU A 207      30.414  31.482  25.783  1.00 84.50           C  
ANISOU 1379  CD2 LEU A 207    13622  11169   7316    648   -941  -1257       C  
ATOM   1380  N   ARG A 208      26.182  28.580  24.636  1.00101.07           N  
ANISOU 1380  N   ARG A 208    15302  13708   9391    352   -852  -1468       N  
ATOM   1381  CA  ARG A 208      25.684  27.517  23.772  1.00107.41           C  
ANISOU 1381  CA  ARG A 208    16056  14538  10216    246   -897  -1501       C  
ATOM   1382  C   ARG A 208      25.096  28.092  22.495  1.00125.06           C  
ANISOU 1382  C   ARG A 208    18182  16889  12444    347   -967  -1550       C  
ATOM   1383  O   ARG A 208      25.341  27.589  21.398  1.00157.22           O  
ANISOU 1383  O   ARG A 208    22304  20933  16499    311  -1028  -1578       O  
ATOM   1384  CB  ARG A 208      24.603  26.700  24.474  1.00 96.68           C  
ANISOU 1384  CB  ARG A 208    14605  13292   8839     50   -847  -1515       C  
ATOM   1385  CG  ARG A 208      24.061  25.578  23.615  1.00 93.68           C  
ANISOU 1385  CG  ARG A 208    14185  12924   8486    -91   -908  -1556       C  
ATOM   1386  CD  ARG A 208      22.694  25.088  24.065  1.00 99.22           C  
ANISOU 1386  CD  ARG A 208    14720  13806   9172   -272   -866  -1578       C  
ATOM   1387  NE  ARG A 208      21.646  26.063  23.768  1.00100.47           N  
ANISOU 1387  NE  ARG A 208    14642  14187   9343   -158   -854  -1635       N  
ATOM   1388  CZ  ARG A 208      21.155  26.944  24.630  1.00107.37           C  
ANISOU 1388  CZ  ARG A 208    15388  15183  10225    -80   -736  -1661       C  
ATOM   1389  NH1 ARG A 208      21.614  26.990  25.869  1.00118.16           N  
ANISOU 1389  NH1 ARG A 208    16872  16503  11521   -141   -617  -1637       N  
ATOM   1390  NH2 ARG A 208      20.198  27.780  24.248  1.00108.03           N  
ANISOU 1390  NH2 ARG A 208    15223  15429  10395     52   -744  -1717       N  
ATOM   1391  N   GLU A 209      24.330  29.167  22.659  1.00110.28           N  
ANISOU 1391  N   GLU A 209    16167  15142  10592    466   -960  -1561       N  
ATOM   1392  CA  GLU A 209      23.593  29.786  21.566  1.00 97.42           C  
ANISOU 1392  CA  GLU A 209    14399  13629   8986    556  -1073  -1560       C  
ATOM   1393  C   GLU A 209      24.496  30.435  20.515  1.00106.57           C  
ANISOU 1393  C   GLU A 209    15688  14705  10099    659  -1170  -1502       C  
ATOM   1394  O   GLU A 209      24.155  30.468  19.329  1.00118.96           O  
ANISOU 1394  O   GLU A 209    17226  16357  11615    634  -1297  -1479       O  
ATOM   1395  CB  GLU A 209      22.625  30.831  22.123  1.00 84.69           C  
ANISOU 1395  CB  GLU A 209    12578  12119   7482    694  -1039  -1585       C  
ATOM   1396  CG  GLU A 209      21.427  31.102  21.234  1.00111.26           C  
ANISOU 1396  CG  GLU A 209    15704  15640  10931    733  -1177  -1570       C  
ATOM   1397  CD  GLU A 209      20.289  31.753  21.987  1.00127.05           C  
ANISOU 1397  CD  GLU A 209    17422  17747  13103    839  -1093  -1637       C  
ATOM   1398  OE1 GLU A 209      20.459  32.015  23.196  1.00118.37           O  
ANISOU 1398  OE1 GLU A 209    16352  16610  12013    863   -900  -1719       O  
ATOM   1399  OE2 GLU A 209      19.226  31.995  21.374  1.00138.31           O  
ANISOU 1399  OE2 GLU A 209    18591  19302  14659    886  -1217  -1614       O  
ATOM   1400  N   TYR A 210      25.639  30.959  20.950  1.00107.15           N  
ANISOU 1400  N   TYR A 210    15907  14632  10173    741  -1117  -1467       N  
ATOM   1401  CA  TYR A 210      26.490  31.745  20.062  1.00105.94           C  
ANISOU 1401  CA  TYR A 210    15860  14413   9978    827  -1187  -1399       C  
ATOM   1402  C   TYR A 210      27.866  31.122  19.814  1.00102.30           C  
ANISOU 1402  C   TYR A 210    15566  13828   9474    760  -1128  -1405       C  
ATOM   1403  O   TYR A 210      28.653  31.655  19.035  1.00 97.06           O  
ANISOU 1403  O   TYR A 210    14987  13131   8759    791  -1152  -1359       O  
ATOM   1404  CB  TYR A 210      26.660  33.161  20.624  1.00107.34           C  
ANISOU 1404  CB  TYR A 210    16036  14516  10232    996  -1193  -1348       C  
ATOM   1405  CG  TYR A 210      25.355  33.923  20.748  1.00118.73           C  
ANISOU 1405  CG  TYR A 210    17282  16044  11786   1111  -1246  -1359       C  
ATOM   1406  CD1 TYR A 210      24.570  33.807  21.888  1.00123.12           C  
ANISOU 1406  CD1 TYR A 210    17708  16652  12419   1117  -1125  -1460       C  
ATOM   1407  CD2 TYR A 210      24.907  34.753  19.728  1.00125.95           C  
ANISOU 1407  CD2 TYR A 210    18127  16986  12743   1203  -1417  -1263       C  
ATOM   1408  CE1 TYR A 210      23.378  34.493  22.010  1.00123.16           C  
ANISOU 1408  CE1 TYR A 210    17484  16732  12579   1242  -1140  -1500       C  
ATOM   1409  CE2 TYR A 210      23.714  35.445  19.843  1.00132.73           C  
ANISOU 1409  CE2 TYR A 210    18761  17893  13778   1337  -1485  -1265       C  
ATOM   1410  CZ  TYR A 210      22.955  35.310  20.987  1.00131.50           C  
ANISOU 1410  CZ  TYR A 210    18443  17784  13737   1371  -1329  -1402       C  
ATOM   1411  OH  TYR A 210      21.767  35.994  21.113  1.00139.75           O  
ANISOU 1411  OH  TYR A 210    19217  18874  15007   1523  -1363  -1435       O  
ATOM   1412  N   VAL A 211      28.169  30.019  20.497  1.00110.73           N  
ANISOU 1412  N   VAL A 211    16666  14820  10585    665  -1050  -1451       N  
ATOM   1413  CA  VAL A 211      29.384  29.237  20.228  1.00112.18           C  
ANISOU 1413  CA  VAL A 211    16955  14863  10805    616   -996  -1475       C  
ATOM   1414  C   VAL A 211      29.099  27.738  20.333  1.00116.77           C  
ANISOU 1414  C   VAL A 211    17535  15394  11439    476   -968  -1552       C  
ATOM   1415  O   VAL A 211      28.261  27.314  21.132  1.00114.97           O  
ANISOU 1415  O   VAL A 211    17252  15206  11227    402   -977  -1541       O  
ATOM   1416  CB  VAL A 211      30.549  29.580  21.202  1.00135.21           C  
ANISOU 1416  CB  VAL A 211    19935  17629  13810    673   -967  -1396       C  
ATOM   1417  CG1 VAL A 211      31.867  29.004  20.687  1.00123.32           C  
ANISOU 1417  CG1 VAL A 211    18479  15985  12392    665   -916  -1417       C  
ATOM   1418  CG2 VAL A 211      30.679  31.085  21.424  1.00138.07           C  
ANISOU 1418  CG2 VAL A 211    20309  18014  14138    789  -1000  -1324       C  
ATOM   1419  N   GLY A 212      29.805  26.937  19.542  1.00121.31           N  
ANISOU 1419  N   GLY A 212    18171  15870  12051    429   -921  -1641       N  
ATOM   1420  CA  GLY A 212      29.660  25.495  19.616  1.00123.42           C  
ANISOU 1420  CA  GLY A 212    18457  16021  12417    306   -898  -1726       C  
ATOM   1421  C   GLY A 212      30.831  24.866  20.343  1.00119.76           C  
ANISOU 1421  C   GLY A 212    18030  15306  12167    337   -867  -1682       C  
ATOM   1422  O   GLY A 212      30.753  24.590  21.539  1.00108.07           O  
ANISOU 1422  O   GLY A 212    16548  13750  10764    299   -920  -1563       O  
ATOM   1423  N   CYS A 213      31.925  24.647  19.622  1.00130.67           N  
ANISOU 1423  N   CYS A 213    19435  16567  13649    392   -785  -1770       N  
ATOM   1424  CA  CYS A 213      33.160  24.201  20.249  1.00132.62           C  
ANISOU 1424  CA  CYS A 213    19666  16569  14156    459   -775  -1710       C  
ATOM   1425  C   CYS A 213      33.827  25.419  20.871  1.00139.95           C  
ANISOU 1425  C   CYS A 213    20574  17546  15054    558   -815  -1550       C  
ATOM   1426  O   CYS A 213      33.969  26.456  20.226  1.00146.71           O  
ANISOU 1426  O   CYS A 213    21433  18544  15765    612   -774  -1564       O  
ATOM   1427  CB  CYS A 213      34.083  23.513  19.240  1.00128.52           C  
ANISOU 1427  CB  CYS A 213    19132  15900  13798    492   -636  -1899       C  
ATOM   1428  SG  CYS A 213      34.354  24.438  17.712  1.00309.50           S  
ANISOU 1428  SG  CYS A 213    42076  39046  36474    505   -490  -2047       S  
ATOM   1429  N   VAL A 214      34.220  25.293  22.133  1.00137.20           N  
ANISOU 1429  N   VAL A 214    20224  17076  14830    552   -914  -1385       N  
ATOM   1430  CA  VAL A 214      34.721  26.432  22.891  1.00118.94           C  
ANISOU 1430  CA  VAL A 214    17919  14813  12460    601   -975  -1238       C  
ATOM   1431  C   VAL A 214      36.240  26.448  22.955  1.00116.82           C  
ANISOU 1431  C   VAL A 214    17588  14380  12418    676   -986  -1173       C  
ATOM   1432  O   VAL A 214      36.894  25.424  22.759  1.00115.09           O  
ANISOU 1432  O   VAL A 214    17304  13966  12461    697   -969  -1209       O  
ATOM   1433  CB  VAL A 214      34.165  26.435  24.324  1.00106.01           C  
ANISOU 1433  CB  VAL A 214    16336  13195  10749    500  -1084  -1095       C  
ATOM   1434  CG1 VAL A 214      34.046  27.854  24.835  1.00104.55           C  
ANISOU 1434  CG1 VAL A 214    16190  13152  10384    532  -1097  -1044       C  
ATOM   1435  CG2 VAL A 214      32.811  25.744  24.364  1.00113.71           C  
ANISOU 1435  CG2 VAL A 214    17323  14255  11626    387  -1067  -1156       C  
ATOM   1436  N   SER A 215      36.793  27.625  23.218  1.00122.38           N  
ANISOU 1436  N   SER A 215    18297  15151  13052    717  -1015  -1085       N  
ATOM   1437  CA  SER A 215      38.234  27.794  23.330  1.00121.16           C  
ANISOU 1437  CA  SER A 215    18054  14872  13109    769  -1041  -1002       C  
ATOM   1438  C   SER A 215      38.757  27.202  24.628  1.00117.16           C  
ANISOU 1438  C   SER A 215    17532  14196  12787    713  -1224   -813       C  
ATOM   1439  O   SER A 215      37.986  26.880  25.529  1.00121.06           O  
ANISOU 1439  O   SER A 215    18122  14702  13172    608  -1322   -733       O  
ATOM   1440  CB  SER A 215      38.610  29.272  23.251  1.00114.38           C  
ANISOU 1440  CB  SER A 215    17222  14131  12105    792  -1040   -951       C  
ATOM   1441  OG  SER A 215      38.084  29.986  24.354  1.00106.99           O  
ANISOU 1441  OG  SER A 215    16396  13254  11003    732  -1156   -849       O  
ATOM   1442  N   GLU A 216      40.076  27.057  24.703  1.00125.06           N  
ANISOU 1442  N   GLU A 216    18401  15050  14068    765  -1274   -730       N  
ATOM   1443  CA  GLU A 216      40.750  26.499  25.874  1.00145.99           C  
ANISOU 1443  CA  GLU A 216    21011  17521  16939    708  -1502   -505       C  
ATOM   1444  C   GLU A 216      40.649  27.399  27.104  1.00150.52           C  
ANISOU 1444  C   GLU A 216    21719  18199  17271    572  -1675   -324       C  
ATOM   1445  O   GLU A 216      40.481  26.917  28.223  1.00138.16           O  
ANISOU 1445  O   GLU A 216    20236  16574  15684    436  -1863   -150       O  
ATOM   1446  CB  GLU A 216      42.225  26.248  25.558  1.00157.35           C  
ANISOU 1446  CB  GLU A 216    22221  18791  18776    814  -1514   -465       C  
ATOM   1447  CG  GLU A 216      42.477  25.195  24.497  1.00169.41           C  
ANISOU 1447  CG  GLU A 216    23598  20162  20606    943  -1332   -667       C  
ATOM   1448  CD  GLU A 216      42.683  23.819  25.090  1.00180.83           C  
ANISOU 1448  CD  GLU A 216    24975  21308  22424    954  -1497   -555       C  
ATOM   1449  OE1 GLU A 216      42.108  23.543  26.165  1.00190.72           O  
ANISOU 1449  OE1 GLU A 216    26371  22531  23561    818  -1716   -355       O  
ATOM   1450  OE2 GLU A 216      43.430  23.018  24.489  1.00180.10           O  
ANISOU 1450  OE2 GLU A 216    24683  21001  22748   1090  -1404   -668       O  
ATOM   1451  N   GLU A 217      40.776  28.707  26.890  1.00156.60           N  
ANISOU 1451  N   GLU A 217    22529  19117  17856    587  -1613   -368       N  
ATOM   1452  CA  GLU A 217      40.716  29.676  27.979  1.00149.39           C  
ANISOU 1452  CA  GLU A 217    21760  18291  16711    458  -1746   -255       C  
ATOM   1453  C   GLU A 217      39.367  29.650  28.687  1.00136.70           C  
ANISOU 1453  C   GLU A 217    20331  16800  14808    347  -1732   -294       C  
ATOM   1454  O   GLU A 217      39.300  29.612  29.916  1.00140.76           O  
ANISOU 1454  O   GLU A 217    20962  17325  15195    175  -1881   -161       O  
ATOM   1455  CB  GLU A 217      40.997  31.090  27.456  1.00155.75           C  
ANISOU 1455  CB  GLU A 217    22582  19197  17398    507  -1659   -328       C  
ATOM   1456  CG  GLU A 217      42.376  31.283  26.832  1.00155.44           C  
ANISOU 1456  CG  GLU A 217    22359  19085  17617    571  -1655   -281       C  
ATOM   1457  CD  GLU A 217      42.426  30.891  25.366  1.00150.33           C  
ANISOU 1457  CD  GLU A 217    21580  18449  17090    707  -1430   -447       C  
ATOM   1458  OE1 GLU A 217      41.358  30.586  24.793  1.00153.12           O  
ANISOU 1458  OE1 GLU A 217    22007  18873  17299    745  -1305   -591       O  
ATOM   1459  OE2 GLU A 217      43.533  30.891  24.786  1.00145.03           O  
ANISOU 1459  OE2 GLU A 217    20727  17731  16648    754  -1373   -442       O  
ATOM   1460  N   THR A 218      38.296  29.654  27.901  1.00123.68           N  
ANISOU 1460  N   THR A 218    18694  15254  13046    424  -1552   -475       N  
ATOM   1461  CA  THR A 218      36.943  29.534  28.433  1.00116.90           C  
ANISOU 1461  CA  THR A 218    17943  14519  11956    333  -1503   -537       C  
ATOM   1462  C   THR A 218      36.731  28.194  29.128  1.00110.61           C  
ANISOU 1462  C   THR A 218    17167  13637  11224    194  -1604   -418       C  
ATOM   1463  O   THR A 218      36.057  28.113  30.154  1.00114.86           O  
ANISOU 1463  O   THR A 218    17821  14263  11558     20  -1639   -366       O  
ATOM   1464  CB  THR A 218      35.887  29.706  27.328  1.00123.12           C  
ANISOU 1464  CB  THR A 218    18688  15424  12667    447  -1326   -731       C  
ATOM   1465  OG1 THR A 218      36.187  30.882  26.566  1.00133.28           O  
ANISOU 1465  OG1 THR A 218    19959  16755  13925    567  -1266   -796       O  
ATOM   1466  CG2 THR A 218      34.499  29.856  27.935  1.00119.19           C  
ANISOU 1466  CG2 THR A 218    18256  15081  11949    364  -1261   -804       C  
ATOM   1467  N   LEU A 219      37.312  27.148  28.555  1.00106.02           N  
ANISOU 1467  N   LEU A 219    16473  12876  10933    261  -1641   -382       N  
ATOM   1468  CA  LEU A 219      37.153  25.794  29.067  1.00110.61           C  
ANISOU 1468  CA  LEU A 219    17068  13312  11646    145  -1757   -258       C  
ATOM   1469  C   LEU A 219      37.647  25.706  30.509  1.00120.95           C  
ANISOU 1469  C   LEU A 219    18476  14572  12907    -53  -1999     10       C  
ATOM   1470  O   LEU A 219      37.033  25.039  31.344  1.00120.02           O  
ANISOU 1470  O   LEU A 219    18468  14462  12672   -254  -2084    130       O  
ATOM   1471  CB  LEU A 219      37.908  24.804  28.184  1.00114.47           C  
ANISOU 1471  CB  LEU A 219    17406  13560  12529    285  -1755   -288       C  
ATOM   1472  CG  LEU A 219      37.640  23.323  28.435  1.00122.55           C  
ANISOU 1472  CG  LEU A 219    18437  14373  13753    200  -1854   -203       C  
ATOM   1473  CD1 LEU A 219      36.231  22.983  27.965  1.00113.79           C  
ANISOU 1473  CD1 LEU A 219    17394  13393  12448    140  -1698   -379       C  
ATOM   1474  CD2 LEU A 219      38.677  22.458  27.743  1.00130.60           C  
ANISOU 1474  CD2 LEU A 219    19286  15094  15241    362  -1871   -229       C  
ATOM   1475  N   LYS A 220      38.760  26.384  30.790  1.00124.83           N  
ANISOU 1475  N   LYS A 220    18933  15025  13470    -27  -2119    116       N  
ATOM   1476  CA  LYS A 220      39.326  26.440  32.139  1.00103.96           C  
ANISOU 1476  CA  LYS A 220    16394  12359  10748   -243  -2384    381       C  
ATOM   1477  C   LYS A 220      38.401  27.202  33.086  1.00 81.45           C  
ANISOU 1477  C   LYS A 220    13763   9752   7430   -455  -2326    335       C  
ATOM   1478  O   LYS A 220      38.237  26.818  34.239  1.00 81.99           O  
ANISOU 1478  O   LYS A 220    13981   9851   7320   -720  -2486    519       O  
ATOM   1479  CB  LYS A 220      40.717  27.087  32.127  1.00101.79           C  
ANISOU 1479  CB  LYS A 220    16008  12008  10659   -174  -2521    483       C  
ATOM   1480  CG  LYS A 220      41.777  26.296  31.365  1.00122.40           C  
ANISOU 1480  CG  LYS A 220    18360  14370  13777     18  -2580    540       C  
ATOM   1481  CD  LYS A 220      43.171  26.890  31.557  1.00135.65           C  
ANISOU 1481  CD  LYS A 220    19898  15991  15651     37  -2751    686       C  
ATOM   1482  CE  LYS A 220      44.232  26.120  30.770  1.00142.82           C  
ANISOU 1482  CE  LYS A 220    20495  16659  17111    248  -2763    706       C  
ATOM   1483  NZ  LYS A 220      44.032  26.211  29.295  1.00138.20           N  
ANISOU 1483  NZ  LYS A 220    19796  16108  16604    470  -2410    388       N  
ATOM   1484  N   ILE A 221      37.806  28.285  32.593  1.00 70.66           N  
ANISOU 1484  N   ILE A 221    12417   8554   5878   -347  -2096     86       N  
ATOM   1485  CA  ILE A 221      36.839  29.059  33.369  1.00 75.44           C  
ANISOU 1485  CA  ILE A 221    13194   9377   6094   -498  -1976    -33       C  
ATOM   1486  C   ILE A 221      35.620  28.223  33.761  1.00 86.66           C  
ANISOU 1486  C   ILE A 221    14671  10899   7358   -651  -1888    -52       C  
ATOM   1487  O   ILE A 221      35.173  28.256  34.910  1.00 82.07           O  
ANISOU 1487  O   ILE A 221    14253  10451   6481   -917  -1903     -2       O  
ATOM   1488  CB  ILE A 221      36.374  30.308  32.588  1.00 66.14           C  
ANISOU 1488  CB  ILE A 221    11979   8303   4847   -298  -1752   -298       C  
ATOM   1489  CG1 ILE A 221      37.514  31.325  32.501  1.00 63.61           C  
ANISOU 1489  CG1 ILE A 221    11662   7913   4595   -236  -1843   -265       C  
ATOM   1490  CG2 ILE A 221      35.175  30.955  33.264  1.00 63.77           C  
ANISOU 1490  CG2 ILE A 221    11799   8202   4228   -404  -1576   -475       C  
ATOM   1491  CD1 ILE A 221      37.293  32.420  31.475  1.00 61.29           C  
ANISOU 1491  CD1 ILE A 221    11309   7648   4329    -17  -1673   -462       C  
ATOM   1492  N   ILE A 222      35.090  27.476  32.797  1.00 97.55           N  
ANISOU 1492  N   ILE A 222    15920  12227   8918   -512  -1789   -132       N  
ATOM   1493  CA  ILE A 222      33.982  26.555  33.038  1.00 85.58           C  
ANISOU 1493  CA  ILE A 222    14427  10781   7307   -663  -1721   -134       C  
ATOM   1494  C   ILE A 222      34.361  25.469  34.041  1.00 73.05           C  
ANISOU 1494  C   ILE A 222    12948   9075   5731   -931  -1961    165       C  
ATOM   1495  O   ILE A 222      33.575  25.126  34.922  1.00 74.02           O  
ANISOU 1495  O   ILE A 222    13192   9335   5597  -1203  -1938    224       O  
ATOM   1496  CB  ILE A 222      33.509  25.898  31.725  1.00 96.10           C  
ANISOU 1496  CB  ILE A 222    15606  12043   8865   -478  -1614   -267       C  
ATOM   1497  CG1 ILE A 222      33.115  26.973  30.711  1.00102.74           C  
ANISOU 1497  CG1 ILE A 222    16351  13008   9676   -243  -1423   -514       C  
ATOM   1498  CG2 ILE A 222      32.329  24.976  31.982  1.00 95.68           C  
ANISOU 1498  CG2 ILE A 222    15571  12068   8715   -663  -1552   -268       C  
ATOM   1499  CD1 ILE A 222      33.261  26.535  29.270  1.00112.38           C  
ANISOU 1499  CD1 ILE A 222    17442  14124  11135    -46  -1377   -615       C  
ATOM   1500  N   GLU A 223      35.568  24.931  33.897  1.00 75.49           N  
ANISOU 1500  N   GLU A 223    13201   9128   6354   -862  -2193    362       N  
ATOM   1501  CA  GLU A 223      36.052  23.868  34.771  1.00 86.46           C  
ANISOU 1501  CA  GLU A 223    14670  10343   7839  -1088  -2486    697       C  
ATOM   1502  C   GLU A 223      36.164  24.329  36.229  1.00111.20           C  
ANISOU 1502  C   GLU A 223    18018  13635  10599  -1420  -2634    882       C  
ATOM   1503  O   GLU A 223      35.765  23.611  37.149  1.00107.93           O  
ANISOU 1503  O   GLU A 223    17754  13250  10006  -1736  -2758   1091       O  
ATOM   1504  CB  GLU A 223      37.406  23.361  34.265  1.00 79.04           C  
ANISOU 1504  CB  GLU A 223    13568   9083   7380   -892  -2699    846       C  
ATOM   1505  CG  GLU A 223      37.865  22.052  34.883  1.00109.17           C  
ANISOU 1505  CG  GLU A 223    17407  12626  11449  -1050  -3020   1192       C  
ATOM   1506  CD  GLU A 223      39.225  21.617  34.373  1.00129.16           C  
ANISOU 1506  CD  GLU A 223    19722  14828  14525   -816  -3209   1309       C  
ATOM   1507  OE1 GLU A 223      39.823  22.365  33.570  1.00129.55           O  
ANISOU 1507  OE1 GLU A 223    19615  14903  14705   -565  -3070   1118       O  
ATOM   1508  OE2 GLU A 223      39.692  20.527  34.767  1.00136.39           O  
ANISOU 1508  OE2 GLU A 223    20612  15454  15758   -886  -3494   1594       O  
ATOM   1509  N   GLU A 224      36.681  25.541  36.428  1.00130.62           N  
ANISOU 1509  N   GLU A 224    20510  16204  12913  -1378  -2616    798       N  
ATOM   1510  CA  GLU A 224      36.898  26.090  37.769  1.00127.57           C  
ANISOU 1510  CA  GLU A 224    20348  15971  12151  -1705  -2755    933       C  
ATOM   1511  C   GLU A 224      35.592  26.358  38.504  1.00113.64           C  
ANISOU 1511  C   GLU A 224    18763  14503   9911  -1963  -2513    773       C  
ATOM   1512  O   GLU A 224      35.539  26.248  39.727  1.00124.78           O  
ANISOU 1512  O   GLU A 224    20393  16038  10977  -2344  -2636    942       O  
ATOM   1513  CB  GLU A 224      37.725  27.376  37.711  1.00143.11           C  
ANISOU 1513  CB  GLU A 224    22310  17969  14095  -1595  -2769    834       C  
ATOM   1514  CG  GLU A 224      39.205  27.160  37.428  1.00162.57           C  
ANISOU 1514  CG  GLU A 224    24621  20187  16960  -1469  -3071   1069       C  
ATOM   1515  CD  GLU A 224      40.000  28.453  37.480  1.00180.56           C  
ANISOU 1515  CD  GLU A 224    26910  22517  19178  -1428  -3099    991       C  
ATOM   1516  OE1 GLU A 224      39.377  29.529  37.600  1.00185.88           O  
ANISOU 1516  OE1 GLU A 224    27711  23378  19537  -1449  -2865    725       O  
ATOM   1517  OE2 GLU A 224      41.245  28.394  37.399  1.00189.52           O  
ANISOU 1517  OE2 GLU A 224    27911  23489  20608  -1374  -3356   1192       O  
ATOM   1518  N   TRP A 225      34.558  26.760  37.771  1.00 87.57           N  
ANISOU 1518  N   TRP A 225    15358  11329   6584  -1770  -2169    445       N  
ATOM   1519  CA  TRP A 225      33.250  26.978  38.381  1.00 89.17           C  
ANISOU 1519  CA  TRP A 225    15661  11815   6406  -1980  -1898    261       C  
ATOM   1520  C   TRP A 225      32.610  25.697  38.925  1.00102.27           C  
ANISOU 1520  C   TRP A 225    17388  13507   7963  -2285  -1955    464       C  
ATOM   1521  O   TRP A 225      32.130  25.682  40.058  1.00118.48           O  
ANISOU 1521  O   TRP A 225    19632  15772   9611  -2662  -1908    511       O  
ATOM   1522  CB  TRP A 225      32.282  27.616  37.392  1.00 86.50           C  
ANISOU 1522  CB  TRP A 225    15141  11579   6148  -1680  -1560   -101       C  
ATOM   1523  CG  TRP A 225      30.852  27.392  37.796  1.00100.90           C  
ANISOU 1523  CG  TRP A 225    16962  13650   7726  -1863  -1296   -250       C  
ATOM   1524  CD1 TRP A 225      29.987  26.477  37.266  1.00104.14           C  
ANISOU 1524  CD1 TRP A 225    17236  14073   8257  -1855  -1213   -254       C  
ATOM   1525  CD2 TRP A 225      30.122  28.084  38.819  1.00115.46           C  
ANISOU 1525  CD2 TRP A 225    18930  15772   9169  -2101  -1061   -435       C  
ATOM   1526  NE1 TRP A 225      28.768  26.557  37.893  1.00102.13           N  
ANISOU 1526  NE1 TRP A 225    16988  14099   7717  -2072   -950   -408       N  
ATOM   1527  CE2 TRP A 225      28.821  27.542  38.849  1.00110.34           C  
ANISOU 1527  CE2 TRP A 225    18180  15308   8435  -2218   -831   -537       C  
ATOM   1528  CE3 TRP A 225      30.439  29.117  39.711  1.00126.96           C  
ANISOU 1528  CE3 TRP A 225    20571  17337  10330  -2240  -1007   -551       C  
ATOM   1529  CZ2 TRP A 225      27.838  27.989  39.732  1.00107.72           C  
ANISOU 1529  CZ2 TRP A 225    17898  15280   7752  -2453   -524   -754       C  
ATOM   1530  CZ3 TRP A 225      29.460  29.562  40.590  1.00131.14           C  
ANISOU 1530  CZ3 TRP A 225    21126  18137  10566  -2443   -690   -781       C  
ATOM   1531  CH2 TRP A 225      28.177  28.997  40.593  1.00118.93           C  
ANISOU 1531  CH2 TRP A 225    19486  16793   8911  -2562   -445   -889       C  
ATOM   1532  N   PHE A 226      32.584  24.634  38.121  1.00 92.86           N  
ANISOU 1532  N   PHE A 226    16055  12107   7120  -2148  -2041    571       N  
ATOM   1533  CA  PHE A 226      31.934  23.393  38.549  1.00109.50           C  
ANISOU 1533  CA  PHE A 226    18226  14209   9171  -2437  -2100    765       C  
ATOM   1534  C   PHE A 226      32.655  22.746  39.728  1.00119.28           C  
ANISOU 1534  C   PHE A 226    19684  15357  10281  -2809  -2457   1184       C  
ATOM   1535  O   PHE A 226      32.025  22.173  40.617  1.00127.00           O  
ANISOU 1535  O   PHE A 226    20824  16473  10957  -3209  -2468   1341       O  
ATOM   1536  CB  PHE A 226      31.830  22.393  37.390  1.00107.81           C  
ANISOU 1536  CB  PHE A 226    17830  13741   9392  -2207  -2134    770       C  
ATOM   1537  CG  PHE A 226      30.716  22.696  36.425  1.00110.03           C  
ANISOU 1537  CG  PHE A 226    17935  14175   9696  -2004  -1803    422       C  
ATOM   1538  CD1 PHE A 226      29.391  22.635  36.835  1.00109.54           C  
ANISOU 1538  CD1 PHE A 226    17878  14390   9353  -2229  -1570    306       C  
ATOM   1539  CD2 PHE A 226      30.989  23.033  35.111  1.00109.04           C  
ANISOU 1539  CD2 PHE A 226    17627  13932   9869  -1612  -1734    224       C  
ATOM   1540  CE1 PHE A 226      28.359  22.916  35.955  1.00 98.02           C  
ANISOU 1540  CE1 PHE A 226    16221  13073   7949  -2045  -1306     12       C  
ATOM   1541  CE2 PHE A 226      29.961  23.314  34.225  1.00105.00           C  
ANISOU 1541  CE2 PHE A 226    16960  13568   9368  -1453  -1483    -57       C  
ATOM   1542  CZ  PHE A 226      28.644  23.255  34.650  1.00100.71           C  
ANISOU 1542  CZ  PHE A 226    16399  13285   8581  -1659  -1285   -156       C  
ATOM   1543  N   CYS A 227      33.978  22.840  39.734  1.00116.12           N  
ANISOU 1543  N   CYS A 227    19280  14732  10109  -2698  -2763   1382       N  
ATOM   1544  CA  CYS A 227      34.764  22.377  40.870  1.00133.00           C  
ANISOU 1544  CA  CYS A 227    21614  16788  12133  -3046  -3160   1807       C  
ATOM   1545  C   CYS A 227      34.647  23.333  42.058  1.00139.75           C  
ANISOU 1545  C   CYS A 227    22718  17976  12406  -3394  -3103   1766       C  
ATOM   1546  O   CYS A 227      35.046  23.002  43.178  1.00148.75           O  
ANISOU 1546  O   CYS A 227    24014  19127  13377  -3765  -3355   2078       O  
ATOM   1547  CB  CYS A 227      36.226  22.198  40.464  1.00143.26           C  
ANISOU 1547  CB  CYS A 227    22773  17743  13915  -2800  -3508   2024       C  
ATOM   1548  SG  CYS A 227      36.458  20.946  39.192  1.00111.12           S  
ANISOU 1548  SG  CYS A 227    18437  13249  10536  -2439  -3577   2065       S  
ATOM   1549  N   GLY A 228      34.107  24.522  41.802  1.00133.91           N  
ANISOU 1549  N   GLY A 228    21945  17471  11466  -3241  -2729   1344       N  
ATOM   1550  CA  GLY A 228      33.930  25.503  42.851  1.00129.95           C  
ANISOU 1550  CA  GLY A 228    21533  17225  10617  -3461  -2532   1178       C  
ATOM   1551  C   GLY A 228      32.936  24.993  43.871  1.00137.79           C  
ANISOU 1551  C   GLY A 228    22622  18441  11290  -3874  -2362   1214       C  
ATOM   1552  O   GLY A 228      31.863  24.496  43.526  1.00140.79           O  
ANISOU 1552  O   GLY A 228    22965  18927  11599  -3899  -2149   1109       O  
ATOM   1553  N   GLU A 229      33.303  25.125  45.140  1.00145.65           N  
ANISOU 1553  N   GLU A 229    23744  19517  12080  -4226  -2460   1362       N  
ATOM   1554  CA  GLU A 229      32.476  24.650  46.234  1.00157.04           C  
ANISOU 1554  CA  GLU A 229    25304  21175  13190  -4679  -2324   1424       C  
ATOM   1555  C   GLU A 229      31.116  25.332  46.215  1.00149.87           C  
ANISOU 1555  C   GLU A 229    24322  20579  12043  -4643  -1779    963       C  
ATOM   1556  O   GLU A 229      30.100  24.692  46.480  1.00151.81           O  
ANISOU 1556  O   GLU A 229    24575  20988  12119  -4882  -1598    962       O  
ATOM   1557  CB  GLU A 229      33.181  24.874  47.577  1.00169.16           C  
ANISOU 1557  CB  GLU A 229    26998  22752  14523  -5055  -2514   1611       C  
ATOM   1558  CG  GLU A 229      34.382  23.950  47.802  1.00173.36           C  
ANISOU 1558  CG  GLU A 229    27583  22988  15298  -5187  -3087   2135       C  
ATOM   1559  CD  GLU A 229      35.060  24.177  49.142  1.00173.63           C  
ANISOU 1559  CD  GLU A 229    27772  23078  15120  -5593  -3295   2323       C  
ATOM   1560  OE1 GLU A 229      34.578  25.033  49.914  1.00172.50           O  
ANISOU 1560  OE1 GLU A 229    27726  23207  14610  -5791  -2980   2039       O  
ATOM   1561  OE2 GLU A 229      36.071  23.496  49.426  1.00171.56           O  
ANISOU 1561  OE2 GLU A 229    27529  22582  15072  -5717  -3780   2751       O  
ATOM   1562  N   LYS A 230      31.099  26.615  45.859  1.00140.69           N  
ANISOU 1562  N   LYS A 230    23070  19480  10904  -4337  -1531    581       N  
ATOM   1563  CA  LYS A 230      29.852  27.368  45.777  1.00145.80           C  
ANISOU 1563  CA  LYS A 230    23607  20385  11406  -4237  -1028    124       C  
ATOM   1564  C   LYS A 230      28.887  26.697  44.818  1.00143.99           C  
ANISOU 1564  C   LYS A 230    23227  20190  11291  -4090   -881     55       C  
ATOM   1565  O   LYS A 230      27.707  26.556  45.116  1.00136.31           O  
ANISOU 1565  O   LYS A 230    22192  19462  10136  -4255   -556   -119       O  
ATOM   1566  CB  LYS A 230      30.112  28.808  45.330  1.00146.96           C  
ANISOU 1566  CB  LYS A 230    23674  20503  11662  -3867   -866   -233       C  
ATOM   1567  CG  LYS A 230      28.859  29.679  45.269  1.00157.60           C  
ANISOU 1567  CG  LYS A 230    24890  22076  12916  -3731   -367   -715       C  
ATOM   1568  CD  LYS A 230      28.231  29.849  46.647  1.00174.83           C  
ANISOU 1568  CD  LYS A 230    27174  24517  14736  -4136   -110   -836       C  
ATOM   1569  CE  LYS A 230      27.122  30.895  46.636  1.00173.29           C  
ANISOU 1569  CE  LYS A 230    26835  24511  14498  -3962    385  -1352       C  
ATOM   1570  NZ  LYS A 230      26.065  30.584  45.633  1.00162.15           N  
ANISOU 1570  NZ  LYS A 230    25183  23170  13257  -3722    601  -1511       N  
ATOM   1571  N   ALA A 231      29.398  26.277  43.667  1.00144.01           N  
ANISOU 1571  N   ALA A 231    23171  19953  11594  -3797  -1121    186       N  
ATOM   1572  CA  ALA A 231      28.573  25.622  42.663  1.00143.00           C  
ANISOU 1572  CA  ALA A 231    22922  19832  11581  -3661  -1024    125       C  
ATOM   1573  C   ALA A 231      28.024  24.291  43.158  1.00147.57           C  
ANISOU 1573  C   ALA A 231    23585  20468  12016  -4068  -1102    408       C  
ATOM   1574  O   ALA A 231      26.853  23.979  42.958  1.00147.87           O  
ANISOU 1574  O   ALA A 231    23522  20700  11960  -4151   -834    256       O  
ATOM   1575  CB  ALA A 231      29.367  25.408  41.396  1.00141.82           C  
ANISOU 1575  CB  ALA A 231    22698  19371  11816  -3279  -1289    219       C  
ATOM   1576  N   GLY A 232      28.885  23.508  43.799  1.00148.69           N  
ANISOU 1576  N   GLY A 232    23902  20431  12161  -4331  -1488    837       N  
ATOM   1577  CA  GLY A 232      28.500  22.200  44.293  1.00140.66           C  
ANISOU 1577  CA  GLY A 232    22995  19405  11043  -4737  -1635   1175       C  
ATOM   1578  C   GLY A 232      27.471  22.206  45.405  1.00135.87           C  
ANISOU 1578  C   GLY A 232    22417  19142  10064  -5165  -1315   1077       C  
ATOM   1579  O   GLY A 232      26.496  21.456  45.361  1.00118.00           O  
ANISOU 1579  O   GLY A 232    20125  17006   7702  -5386  -1177   1107       O  
ATOM   1580  N   GLU A 233      27.694  23.043  46.413  1.00155.18           N  
ANISOU 1580  N   GLU A 233    24926  21738  12298  -5308  -1198    959       N  
ATOM   1581  CA  GLU A 233      26.804  23.086  47.565  1.00171.77           C  
ANISOU 1581  CA  GLU A 233    27076  24164  14026  -5744   -896    855       C  
ATOM   1582  C   GLU A 233      25.432  23.664  47.228  1.00176.59           C  
ANISOU 1582  C   GLU A 233    27470  25081  14546  -5619   -352    385       C  
ATOM   1583  O   GLU A 233      24.408  23.074  47.567  1.00176.71           O  
ANISOU 1583  O   GLU A 233    27446  25317  14379  -5936   -138    378       O  
ATOM   1584  CB  GLU A 233      27.448  23.908  48.687  1.00177.16           C  
ANISOU 1584  CB  GLU A 233    27898  24912  14501  -5918   -915    814       C  
ATOM   1585  CG  GLU A 233      28.824  23.410  49.111  1.00182.95           C  
ANISOU 1585  CG  GLU A 233    28814  25368  15332  -6066  -1461   1275       C  
ATOM   1586  CD  GLU A 233      29.580  24.413  49.962  1.00184.88           C  
ANISOU 1586  CD  GLU A 233    29169  25654  15422  -6146  -1492   1185       C  
ATOM   1587  OE1 GLU A 233      28.997  25.459  50.317  1.00194.85           O  
ANISOU 1587  OE1 GLU A 233    30401  27156  16476  -6122  -1080    766       O  
ATOM   1588  OE2 GLU A 233      30.761  24.154  50.277  1.00178.18           O  
ANISOU 1588  OE2 GLU A 233    28433  24588  14678  -6237  -1936   1532       O  
ATOM   1589  N   VAL A 234      25.414  24.817  46.562  1.00183.90           N  
ANISOU 1589  N   VAL A 234    28242  26013  15620  -5167   -141      1       N  
ATOM   1590  CA  VAL A 234      24.167  25.557  46.371  1.00191.85           C  
ANISOU 1590  CA  VAL A 234    29021  27300  16573  -5029    374   -474       C  
ATOM   1591  C   VAL A 234      23.466  25.050  45.113  1.00188.16           C  
ANISOU 1591  C   VAL A 234    28349  26826  16318  -4800    436   -536       C  
ATOM   1592  O   VAL A 234      22.270  25.278  44.927  1.00200.18           O  
ANISOU 1592  O   VAL A 234    29649  28605  17807  -4776    830   -846       O  
ATOM   1593  CB  VAL A 234      24.388  27.087  46.283  1.00197.24           C  
ANISOU 1593  CB  VAL A 234    29632  27978  17333  -4664    575   -870       C  
ATOM   1594  CG1 VAL A 234      24.826  27.491  44.889  1.00199.85           C  
ANISOU 1594  CG1 VAL A 234    29840  28078  18017  -4137    440   -953       C  
ATOM   1595  CG2 VAL A 234      23.108  27.818  46.646  1.00195.84           C  
ANISOU 1595  CG2 VAL A 234    29269  28113  17030  -4679   1116  -1329       C  
ATOM   1596  N   GLY A 235      24.237  24.390  44.247  1.00180.85           N  
ANISOU 1596  N   GLY A 235    27489  25604  15621  -4633     44   -253       N  
ATOM   1597  CA  GLY A 235      23.798  23.993  42.917  1.00169.70           C  
ANISOU 1597  CA  GLY A 235    25920  24129  14429  -4374     37   -319       C  
ATOM   1598  C   GLY A 235      22.431  23.351  42.866  1.00181.59           C  
ANISOU 1598  C   GLY A 235    27220  25870  15906  -4575    310   -398       C  
ATOM   1599  O   GLY A 235      21.669  23.570  41.931  1.00154.91           O  
ANISOU 1599  O   GLY A 235    23509  22518  12833  -4251    496   -647       O  
ATOM   1600  N   ASP A 236      22.135  22.536  43.873  1.00213.38           N  
ANISOU 1600  N   ASP A 236    31426  30055  19593  -5124    305   -156       N  
ATOM   1601  CA  ASP A 236      20.803  21.973  44.044  1.00232.67           C  
ANISOU 1601  CA  ASP A 236    33710  32801  21894  -5435    610   -231       C  
ATOM   1602  C   ASP A 236      19.744  23.068  44.045  1.00234.92           C  
ANISOU 1602  C   ASP A 236    33692  33432  22134  -5270   1144   -755       C  
ATOM   1603  O   ASP A 236      19.836  24.044  44.786  1.00243.72           O  
ANISOU 1603  O   ASP A 236    34810  34639  23155  -5224   1348   -981       O  
ATOM   1604  CB  ASP A 236      20.721  21.153  45.339  1.00238.82           C  
ANISOU 1604  CB  ASP A 236    34697  33676  22366  -6038    546     92       C  
ATOM   1605  CG  ASP A 236      20.774  22.016  46.588  1.00237.01           C  
ANISOU 1605  CG  ASP A 236    34523  33632  21896  -6197    770    -84       C  
ATOM   1606  OD1 ASP A 236      21.857  22.544  46.906  1.00236.28           O  
ANISOU 1606  OD1 ASP A 236    34599  33346  21833  -6064    544    -12       O  
ATOM   1607  OD2 ASP A 236      19.729  22.168  47.253  1.00234.36           O  
ANISOU 1607  OD2 ASP A 236    34059  33644  21344  -6469   1176   -305       O  
ATOM   1608  N   ASN A 237      18.743  22.909  43.191  1.00226.58           N  
ANISOU 1608  N   ASN A 237    32255  32443  21390  -5067   1321   -930       N  
ATOM   1609  CA  ASN A 237      17.626  23.837  43.164  1.00218.31           C  
ANISOU 1609  CA  ASN A 237    30857  31719  20372  -4913   1815  -1402       C  
ATOM   1610  C   ASN A 237      16.336  23.100  42.850  1.00213.21           C  
ANISOU 1610  C   ASN A 237    29873  31281  19857  -5077   2006  -1427       C  
ATOM   1611  O   ASN A 237      16.343  22.076  42.165  1.00199.11           O  
ANISOU 1611  O   ASN A 237    28056  29292  18305  -5094   1714  -1151       O  
ATOM   1612  CB  ASN A 237      17.873  24.953  42.147  1.00216.77           C  
ANISOU 1612  CB  ASN A 237    30446  31330  20588  -4261   1802  -1683       C  
ATOM   1613  CG  ASN A 237      17.005  26.169  42.399  1.00217.89           C  
ANISOU 1613  CG  ASN A 237    30311  31748  20728  -4093   2291  -2178       C  
ATOM   1614  OD1 ASN A 237      15.792  26.054  42.575  1.00221.98           O  
ANISOU 1614  OD1 ASN A 237    30523  32574  21244  -4241   2643  -2369       O  
ATOM   1615  ND2 ASN A 237      17.624  27.344  42.426  1.00211.33           N  
ANISOU 1615  ND2 ASN A 237    29572  30796  19926  -3786   2317  -2395       N  
ATOM   1616  N   GLY A 238      15.227  23.622  43.357  1.00220.64           N  
ANISOU 1616  N   GLY A 238    30549  32622  20660  -5206   2506  -1775       N  
ATOM   1617  CA  GLY A 238      13.951  22.960  43.193  1.00222.84           C  
ANISOU 1617  CA  GLY A 238    30477  33156  21035  -5421   2724  -1808       C  
ATOM   1618  C   GLY A 238      12.864  23.835  42.593  1.00235.52           C  
ANISOU 1618  C   GLY A 238    31532  34952  23002  -5031   3083  -2250       C  
ATOM   1619  O   GLY A 238      12.511  24.835  43.217  1.00231.82           O  
ANISOU 1619  O   GLY A 238    30956  34721  22405  -4985   3499  -2629       O  
ATOM   1620  N   ILE A 239      12.320  23.520  41.408  1.00251.61           N  
ANISOU 1620  N   ILE A 239    33214  36885  25501  -4750   2930  -2226       N  
ATOM   1621  CA  ILE A 239      12.678  22.414  40.492  1.00270.65           C  
ANISOU 1621  CA  ILE A 239    35716  38988  28132  -4741   2460  -1859       C  
ATOM   1622  C   ILE A 239      12.930  21.042  41.142  1.00290.06           C  
ANISOU 1622  C   ILE A 239    38517  41413  30278  -5330   2276  -1449       C  
ATOM   1623  O   ILE A 239      12.082  20.541  41.883  1.00297.59           O  
ANISOU 1623  O   ILE A 239    39387  42698  30986  -5815   2546  -1432       O  
ATOM   1624  CB  ILE A 239      13.908  22.794  39.628  1.00190.39           C  
ANISOU 1624  CB  ILE A 239    25759  28381  18199  -4259   2058  -1768       C  
ATOM   1625  CG1 ILE A 239      13.979  24.311  39.445  1.00188.24           C  
ANISOU 1625  CG1 ILE A 239    25325  28124  18074  -3781   2246  -2130       C  
ATOM   1626  CG2 ILE A 239      13.832  22.117  38.259  1.00182.45           C  
ANISOU 1626  CG2 ILE A 239    24601  27129  17592  -4040   1723  -1623       C  
ATOM   1627  CD1 ILE A 239      15.081  24.773  38.525  1.00182.47           C  
ANISOU 1627  CD1 ILE A 239    24746  27001  17584  -3315   1888  -2060       C  
ATOM   1628  N   GLY A 240      14.088  20.442  40.868  1.00299.02           N  
ANISOU 1628  N   GLY A 240    40024  42144  31444  -5293   1820  -1115       N  
ATOM   1629  CA  GLY A 240      14.387  19.095  41.331  1.00298.44           C  
ANISOU 1629  CA  GLY A 240    40267  41939  31186  -5789   1562   -686       C  
ATOM   1630  C   GLY A 240      13.589  18.055  40.563  1.00296.00           C  
ANISOU 1630  C   GLY A 240    39730  41582  31153  -5910   1457   -575       C  
ATOM   1631  O   GLY A 240      13.995  16.899  40.432  1.00298.73           O  
ANISOU 1631  O   GLY A 240    40313  41635  31556  -6135   1116   -225       O  
ATOM   1632  N   SER A 241      12.443  18.494  40.055  1.00258.83           N  
ANISOU 1632  N   SER A 241    34550  37151  26644  -5757   1743   -883       N  
ATOM   1633  CA  SER A 241      11.505  17.683  39.305  1.00228.46           C  
ANISOU 1633  CA  SER A 241    30407  33337  23061  -5872   1691   -845       C  
ATOM   1634  C   SER A 241      10.951  18.568  38.185  1.00192.10           C  
ANISOU 1634  C   SER A 241    25347  28792  18850  -5334   1767  -1180       C  
ATOM   1635  O   SER A 241      10.962  19.794  38.310  1.00180.58           O  
ANISOU 1635  O   SER A 241    23743  27467  17403  -5001   1994  -1464       O  
ATOM   1636  CB  SER A 241      10.394  17.152  40.225  1.00223.18           C  
ANISOU 1636  CB  SER A 241    29592  33088  22119  -6476   2024   -814       C  
ATOM   1637  OG  SER A 241       9.744  18.205  40.913  1.00207.96           O  
ANISOU 1637  OG  SER A 241    27398  31598  20018  -6460   2524  -1163       O  
ATOM   1638  N   ASP A 242      10.494  17.975  37.084  1.00161.93           N  
ANISOU 1638  N   ASP A 242    21318  24854  15355  -5254   1555  -1142       N  
ATOM   1639  CA  ASP A 242      10.469  16.531  36.882  1.00142.06           C  
ANISOU 1639  CA  ASP A 242    18977  22135  12862  -5638   1285   -839       C  
ATOM   1640  C   ASP A 242      11.002  16.173  35.502  1.00151.64           C  
ANISOU 1640  C   ASP A 242    20256  22942  14419  -5299    885   -797       C  
ATOM   1641  O   ASP A 242      10.843  16.939  34.553  1.00163.51           O  
ANISOU 1641  O   ASP A 242    21500  24460  16165  -4861    864  -1018       O  
ATOM   1642  CB  ASP A 242       9.049  15.998  37.074  1.00139.00           C  
ANISOU 1642  CB  ASP A 242    18223  22116  12473  -6060   1514   -868       C  
ATOM   1643  CG  ASP A 242       7.999  16.932  36.517  1.00128.94           C  
ANISOU 1643  CG  ASP A 242    16367  21172  11451  -5754   1763  -1212       C  
ATOM   1644  OD1 ASP A 242       8.253  18.153  36.479  1.00120.93           O  
ANISOU 1644  OD1 ASP A 242    15248  20207  10491  -5315   1901  -1451       O  
ATOM   1645  OD2 ASP A 242       6.903  16.456  36.162  1.00132.59           O  
ANISOU 1645  OD2 ASP A 242    16463  21842  12073  -5969   1814  -1236       O  
ATOM   1646  N   VAL A 243      11.641  15.011  35.402  1.00149.27           N  
ANISOU 1646  N   VAL A 243    20309  22270  14139  -5516    571   -514       N  
ATOM   1647  CA  VAL A 243      12.219  14.548  34.143  1.00143.59           C  
ANISOU 1647  CA  VAL A 243    19696  21138  13723  -5244    219   -496       C  
ATOM   1648  C   VAL A 243      11.195  14.467  33.010  1.00155.99           C  
ANISOU 1648  C   VAL A 243    20886  22842  15542  -5172    196   -676       C  
ATOM   1649  O   VAL A 243      11.546  14.669  31.852  1.00170.91           O  
ANISOU 1649  O   VAL A 243    22758  24534  17647  -4815      2   -791       O  
ATOM   1650  CB  VAL A 243      12.902  13.175  34.308  1.00134.57           C  
ANISOU 1650  CB  VAL A 243    18956  19566  12607  -5550    -83   -177       C  
ATOM   1651  CG1 VAL A 243      14.162  13.298  35.152  1.00141.30           C  
ANISOU 1651  CG1 VAL A 243    20195  20195  13299  -5511   -180     23       C  
ATOM   1652  CG2 VAL A 243      11.927  12.164  34.912  1.00134.68           C  
ANISOU 1652  CG2 VAL A 243    18924  19738  12510  -6157    -15      1       C  
ATOM   1653  N   GLY A 244       9.939  14.170  33.338  1.00149.52           N  
ANISOU 1653  N   GLY A 244    19759  22370  14680  -5538    387   -693       N  
ATOM   1654  CA  GLY A 244       8.876  14.127  32.344  1.00147.40           C  
ANISOU 1654  CA  GLY A 244    19081  22278  14647  -5510    356   -846       C  
ATOM   1655  C   GLY A 244       8.665  15.453  31.629  1.00145.17           C  
ANISOU 1655  C   GLY A 244    18459  22173  14525  -4990    426  -1113       C  
ATOM   1656  O   GLY A 244       8.612  15.505  30.398  1.00139.26           O  
ANISOU 1656  O   GLY A 244    17611  21312  13990  -4755    196  -1197       O  
ATOM   1657  N   MET A 245       8.534  16.524  32.407  1.00143.34           N  
ANISOU 1657  N   MET A 245    18063  22213  14187  -4833    740  -1247       N  
ATOM   1658  CA  MET A 245       8.400  17.875  31.866  1.00132.83           C  
ANISOU 1658  CA  MET A 245    16432  21007  13031  -4321    813  -1485       C  
ATOM   1659  C   MET A 245       9.672  18.287  31.139  1.00113.17           C  
ANISOU 1659  C   MET A 245    14270  18139  10589  -3897    551  -1476       C  
ATOM   1660  O   MET A 245       9.625  18.925  30.089  1.00114.00           O  
ANISOU 1660  O   MET A 245    14204  18212  10900  -3533    406  -1588       O  
ATOM   1661  CB  MET A 245       8.092  18.882  32.974  1.00141.26           C  
ANISOU 1661  CB  MET A 245    17314  22387  13970  -4266   1231  -1653       C  
ATOM   1662  CG  MET A 245       8.178  20.336  32.523  1.00141.41           C  
ANISOU 1662  CG  MET A 245    17109  22434  14186  -3704   1288  -1885       C  
ATOM   1663  SD  MET A 245       7.988  21.533  33.861  1.00272.19           S  
ANISOU 1663  SD  MET A 245    33536  39283  30601  -3621   1793  -2135       S  
ATOM   1664  CE  MET A 245       9.391  21.127  34.900  1.00126.82           C  
ANISOU 1664  CE  MET A 245    15803  20636  11746  -3851   1764  -1942       C  
ATOM   1665  N   LEU A 246      10.809  17.925  31.723  1.00100.23           N  
ANISOU 1665  N   LEU A 246    13094  16228   8760  -3967    485  -1324       N  
ATOM   1666  CA  LEU A 246      12.118  18.246  31.164  1.00103.27           C  
ANISOU 1666  CA  LEU A 246    13797  16255   9184  -3605    264  -1302       C  
ATOM   1667  C   LEU A 246      12.368  17.628  29.791  1.00 99.53           C  
ANISOU 1667  C   LEU A 246    13398  15513   8906  -3505    -58  -1283       C  
ATOM   1668  O   LEU A 246      12.860  18.306  28.896  1.00 91.62           O  
ANISOU 1668  O   LEU A 246    12400  14399   8012  -3123   -180  -1381       O  
ATOM   1669  CB  LEU A 246      13.227  17.825  32.128  1.00108.65           C  
ANISOU 1669  CB  LEU A 246    14924  16704   9654  -3761    231  -1107       C  
ATOM   1670  CG  LEU A 246      13.736  18.872  33.124  1.00106.13           C  
ANISOU 1670  CG  LEU A 246    14696  16495   9135  -3626    441  -1165       C  
ATOM   1671  CD1 LEU A 246      12.609  19.570  33.878  1.00 99.90           C  
ANISOU 1671  CD1 LEU A 246    13563  16152   8242  -3734    824  -1350       C  
ATOM   1672  CD2 LEU A 246      14.718  18.234  34.092  1.00116.93           C  
ANISOU 1672  CD2 LEU A 246    16496  17651  10282  -3887    346   -911       C  
ATOM   1673  N   ARG A 247      12.073  16.342  29.627  1.00116.37           N  
ANISOU 1673  N   ARG A 247    15618  17529  11066  -3868   -193  -1163       N  
ATOM   1674  CA  ARG A 247      12.290  15.694  28.334  1.00120.98           C  
ANISOU 1674  CA  ARG A 247    16299  17854  11816  -3814   -474  -1190       C  
ATOM   1675  C   ARG A 247      11.387  16.310  27.264  1.00114.48           C  
ANISOU 1675  C   ARG A 247    15094  17278  11127  -3640   -520  -1361       C  
ATOM   1676  O   ARG A 247      11.794  16.477  26.115  1.00105.46           O  
ANISOU 1676  O   ARG A 247    14019  15985  10068  -3405   -715  -1443       O  
ATOM   1677  CB  ARG A 247      12.045  14.182  28.422  1.00120.34           C  
ANISOU 1677  CB  ARG A 247    16379  17587  11759  -4272   -600  -1046       C  
ATOM   1678  CG  ARG A 247      13.141  13.408  29.141  1.00118.19           C  
ANISOU 1678  CG  ARG A 247    16540  16930  11438  -4401   -685   -840       C  
ATOM   1679  CD  ARG A 247      12.818  11.924  29.215  1.00122.77           C  
ANISOU 1679  CD  ARG A 247    17268  17294  12085  -4861   -827   -688       C  
ATOM   1680  NE  ARG A 247      12.762  11.306  27.893  1.00138.90           N  
ANISOU 1680  NE  ARG A 247    19342  19111  14322  -4830  -1037   -823       N  
ATOM   1681  CZ  ARG A 247      12.337  10.066  27.660  1.00153.93           C  
ANISOU 1681  CZ  ARG A 247    21335  20822  16327  -5209  -1177   -764       C  
ATOM   1682  NH1 ARG A 247      11.923   9.305  28.664  1.00156.03           N  
ANISOU 1682  NH1 ARG A 247    21661  21094  16528  -5652  -1141   -536       N  
ATOM   1683  NH2 ARG A 247      12.321   9.586  26.422  1.00159.45           N  
ANISOU 1683  NH2 ARG A 247    22082  21324  17176  -5174  -1354   -935       N  
ATOM   1684  N   GLU A 248      10.169  16.668  27.657  1.00114.56           N  
ANISOU 1684  N   GLU A 248    14691  17678  11159  -3765   -341  -1410       N  
ATOM   1685  CA  GLU A 248       9.251  17.359  26.762  1.00108.18           C  
ANISOU 1685  CA  GLU A 248    13457  17126  10520  -3586   -399  -1541       C  
ATOM   1686  C   GLU A 248       9.740  18.764  26.429  1.00115.21           C  
ANISOU 1686  C   GLU A 248    14289  18022  11464  -3078   -384  -1644       C  
ATOM   1687  O   GLU A 248       9.635  19.215  25.287  1.00129.96           O  
ANISOU 1687  O   GLU A 248    16041  19890  13449  -2854   -590  -1698       O  
ATOM   1688  CB  GLU A 248       7.852  17.419  27.383  1.00113.29           C  
ANISOU 1688  CB  GLU A 248    13629  18188  11229  -3830   -178  -1571       C  
ATOM   1689  CG  GLU A 248       6.860  18.290  26.624  1.00128.15           C  
ANISOU 1689  CG  GLU A 248    14990  20355  13347  -3603   -227  -1690       C  
ATOM   1690  CD  GLU A 248       6.558  19.595  27.336  1.00140.80           C  
ANISOU 1690  CD  GLU A 248    16276  22191  15030  -3303     73  -1817       C  
ATOM   1691  OE1 GLU A 248       6.264  19.556  28.548  1.00153.62           O  
ANISOU 1691  OE1 GLU A 248    17826  23993  16549  -3501    409  -1845       O  
ATOM   1692  OE2 GLU A 248       6.602  20.658  26.682  1.00140.28           O  
ANISOU 1692  OE2 GLU A 248    16043  22125  15132  -2887    -24  -1896       O  
ATOM   1693  N   ALA A 249      10.289  19.448  27.429  1.00112.17           N  
ANISOU 1693  N   ALA A 249    14008  17636  10977  -2928   -157  -1659       N  
ATOM   1694  CA  ALA A 249      10.810  20.796  27.236  1.00 93.21           C  
ANISOU 1694  CA  ALA A 249    11582  15204   8627  -2468   -130  -1754       C  
ATOM   1695  C   ALA A 249      12.153  20.805  26.510  1.00 95.38           C  
ANISOU 1695  C   ALA A 249    12260  15125   8853  -2249   -351  -1708       C  
ATOM   1696  O   ALA A 249      12.421  21.712  25.722  1.00107.12           O  
ANISOU 1696  O   ALA A 249    13698  16575  10427  -1910   -462  -1764       O  
ATOM   1697  CB  ALA A 249      10.932  21.511  28.574  1.00 93.68           C  
ANISOU 1697  CB  ALA A 249    11634  15382   8578  -2421    198  -1816       C  
ATOM   1698  N   VAL A 250      13.000  19.811  26.775  1.00102.97           N  
ANISOU 1698  N   VAL A 250    13605  15823   9697  -2445   -417  -1599       N  
ATOM   1699  CA  VAL A 250      14.284  19.726  26.079  1.00 94.24           C  
ANISOU 1699  CA  VAL A 250    12845  14379   8582  -2249   -599  -1576       C  
ATOM   1700  C   VAL A 250      14.050  19.459  24.599  1.00102.79           C  
ANISOU 1700  C   VAL A 250    13879  15422   9755  -2214   -832  -1638       C  
ATOM   1701  O   VAL A 250      14.754  20.000  23.759  1.00109.04           O  
ANISOU 1701  O   VAL A 250    14784  16092  10554  -1948   -944  -1683       O  
ATOM   1702  CB  VAL A 250      15.247  18.648  26.673  1.00120.68           C  
ANISOU 1702  CB  VAL A 250    16582  17414  11857  -2454   -639  -1441       C  
ATOM   1703  CG1 VAL A 250      14.769  17.238  26.398  1.00136.74           C  
ANISOU 1703  CG1 VAL A 250    18667  19350  13939  -2821   -756  -1387       C  
ATOM   1704  CG2 VAL A 250      16.650  18.826  26.105  1.00 97.22           C  
ANISOU 1704  CG2 VAL A 250    13901  14124   8915  -2181   -764  -1444       C  
ATOM   1705  N   LEU A 251      13.060  18.628  24.288  1.00108.00           N  
ANISOU 1705  N   LEU A 251    14377  16199  10458  -2516   -904  -1640       N  
ATOM   1706  CA  LEU A 251      12.747  18.279  22.910  1.00111.89           C  
ANISOU 1706  CA  LEU A 251    14839  16679  10996  -2562  -1140  -1705       C  
ATOM   1707  C   LEU A 251      12.303  19.490  22.102  1.00108.81           C  
ANISOU 1707  C   LEU A 251    14173  16506  10665  -2277  -1231  -1757       C  
ATOM   1708  O   LEU A 251      12.734  19.678  20.965  1.00104.69           O  
ANISOU 1708  O   LEU A 251    13777  15894  10106  -2153  -1416  -1798       O  
ATOM   1709  CB  LEU A 251      11.658  17.205  22.869  1.00124.69           C  
ANISOU 1709  CB  LEU A 251    16306  18416  12655  -2982  -1198  -1688       C  
ATOM   1710  CG  LEU A 251      11.295  16.637  21.496  1.00 93.57           C  
ANISOU 1710  CG  LEU A 251    12374  14452   8725  -3128  -1460  -1764       C  
ATOM   1711  CD1 LEU A 251      12.454  15.831  20.922  1.00 92.08           C  
ANISOU 1711  CD1 LEU A 251    12644  13861   8482  -3148  -1554  -1828       C  
ATOM   1712  CD2 LEU A 251      10.040  15.791  21.590  1.00 97.45           C  
ANISOU 1712  CD2 LEU A 251    12623  15128   9274  -3546  -1506  -1737       C  
ATOM   1713  N   ASN A 252      11.472  20.328  22.713  1.00101.05           N  
ANISOU 1713  N   ASN A 252    12818  15796   9779  -2177  -1092  -1755       N  
ATOM   1714  CA  ASN A 252      10.822  21.428  22.008  1.00102.34           C  
ANISOU 1714  CA  ASN A 252    12641  16164  10078  -1928  -1208  -1777       C  
ATOM   1715  C   ASN A 252      11.845  22.463  21.523  1.00107.94           C  
ANISOU 1715  C   ASN A 252    13549  16709  10752  -1549  -1273  -1778       C  
ATOM   1716  O   ASN A 252      11.625  23.151  20.529  1.00110.82           O  
ANISOU 1716  O   ASN A 252    13788  17141  11178  -1383  -1481  -1757       O  
ATOM   1717  CB  ASN A 252       9.784  22.080  22.927  1.00103.21           C  
ANISOU 1717  CB  ASN A 252    12300  16559  10356  -1880   -988  -1807       C  
ATOM   1718  CG  ASN A 252       8.825  23.003  22.193  1.00109.64           C  
ANISOU 1718  CG  ASN A 252    12660  17591  11406  -1678  -1146  -1808       C  
ATOM   1719  OD1 ASN A 252       9.076  23.432  21.071  1.00111.30           O  
ANISOU 1719  OD1 ASN A 252    12933  17734  11623  -1516  -1422  -1761       O  
ATOM   1720  ND2 ASN A 252       7.711  23.319  22.843  1.00116.62           N  
ANISOU 1720  ND2 ASN A 252    13072  18743  12496  -1696   -971  -1855       N  
ATOM   1721  N   ASN A 253      12.981  22.543  22.207  1.00127.85           N  
ANISOU 1721  N   ASN A 253    16391  19016  13172  -1444  -1119  -1780       N  
ATOM   1722  CA  ASN A 253      13.998  23.541  21.889  1.00139.58           C  
ANISOU 1722  CA  ASN A 253    18059  20347  14627  -1109  -1150  -1777       C  
ATOM   1723  C   ASN A 253      15.101  22.985  20.987  1.00133.39           C  
ANISOU 1723  C   ASN A 253    17655  19318  13709  -1134  -1295  -1776       C  
ATOM   1724  O   ASN A 253      16.190  23.558  20.892  1.00132.62           O  
ANISOU 1724  O   ASN A 253    17778  19053  13561   -918  -1277  -1769       O  
ATOM   1725  CB  ASN A 253      14.610  24.092  23.176  1.00143.57           C  
ANISOU 1725  CB  ASN A 253    18662  20780  15108   -973   -901  -1788       C  
ATOM   1726  CG  ASN A 253      13.617  24.884  23.997  1.00148.70           C  
ANISOU 1726  CG  ASN A 253    18941  21667  15893   -891   -711  -1848       C  
ATOM   1727  OD1 ASN A 253      12.709  25.513  23.455  1.00150.33           O  
ANISOU 1727  OD1 ASN A 253    18800  22040  16278   -764   -798  -1868       O  
ATOM   1728  ND2 ASN A 253      13.780  24.854  25.314  1.00149.45           N  
ANISOU 1728  ND2 ASN A 253    19100  21777  15908   -971   -451  -1882       N  
ATOM   1729  N   GLY A 254      14.808  21.885  20.301  1.00137.80           N  
ANISOU 1729  N   GLY A 254    18280  19858  14220  -1405  -1426  -1803       N  
ATOM   1730  CA  GLY A 254      15.832  21.183  19.552  1.00117.58           C  
ANISOU 1730  CA  GLY A 254    16079  17047  11550  -1463  -1502  -1857       C  
ATOM   1731  C   GLY A 254      16.382  20.084  20.434  1.00117.18           C  
ANISOU 1731  C   GLY A 254    16246  16764  11513  -1636  -1375  -1853       C  
ATOM   1732  O   GLY A 254      15.784  19.749  21.443  1.00115.21           O  
ANISOU 1732  O   GLY A 254    15872  16595  11308  -1792  -1270  -1795       O  
ATOM   1733  N   GLY A 255      17.488  19.477  20.030  1.00127.16           N  
ANISOU 1733  N   GLY A 255    17825  17740  12750  -1632  -1389  -1910       N  
ATOM   1734  CA  GLY A 255      18.119  18.455  20.844  1.00129.39           C  
ANISOU 1734  CA  GLY A 255    18317  17744  13101  -1764  -1311  -1874       C  
ATOM   1735  C   GLY A 255      18.768  19.003  22.103  1.00129.92           C  
ANISOU 1735  C   GLY A 255    18424  17755  13184  -1610  -1176  -1752       C  
ATOM   1736  O   GLY A 255      18.814  18.334  23.135  1.00132.85           O  
ANISOU 1736  O   GLY A 255    18865  18024  13589  -1780  -1121  -1649       O  
ATOM   1737  N   GLY A 256      19.256  20.235  22.008  1.00132.72           N  
ANISOU 1737  N   GLY A 256    18747  18179  13499  -1316  -1140  -1751       N  
ATOM   1738  CA  GLY A 256      20.231  20.789  22.937  1.00129.29           C  
ANISOU 1738  CA  GLY A 256    18429  17630  13067  -1147  -1044  -1667       C  
ATOM   1739  C   GLY A 256      19.929  21.108  24.393  1.00116.42           C  
ANISOU 1739  C   GLY A 256    16728  16111  11396  -1204   -914  -1566       C  
ATOM   1740  O   GLY A 256      20.766  20.838  25.252  1.00116.14           O  
ANISOU 1740  O   GLY A 256    16875  15898  11354  -1234   -886  -1466       O  
ATOM   1741  N   TRP A 257      18.779  21.702  24.692  1.00110.11           N  
ANISOU 1741  N   TRP A 257    15663  15604  10569  -1225   -832  -1596       N  
ATOM   1742  CA  TRP A 257      18.634  22.329  26.002  1.00104.73           C  
ANISOU 1742  CA  TRP A 257    14924  15050   9820  -1222   -657  -1560       C  
ATOM   1743  C   TRP A 257      17.204  22.496  26.511  1.00112.88           C  
ANISOU 1743  C   TRP A 257    15642  16399  10850  -1362   -516  -1611       C  
ATOM   1744  O   TRP A 257      16.249  22.493  25.735  1.00111.17           O  
ANISOU 1744  O   TRP A 257    15176  16341  10723  -1373   -579  -1672       O  
ATOM   1745  CB  TRP A 257      19.300  23.699  25.967  1.00112.28           C  
ANISOU 1745  CB  TRP A 257    15902  15988  10772   -892   -625  -1600       C  
ATOM   1746  CG  TRP A 257      18.701  24.591  24.928  1.00127.93           C  
ANISOU 1746  CG  TRP A 257    17661  18106  12842   -676   -691  -1685       C  
ATOM   1747  CD1 TRP A 257      18.961  24.580  23.588  1.00129.89           C  
ANISOU 1747  CD1 TRP A 257    17949  18282  13121   -581   -866  -1697       C  
ATOM   1748  CD2 TRP A 257      17.729  25.619  25.139  1.00136.68           C  
ANISOU 1748  CD2 TRP A 257    18468  19439  14027   -543   -597  -1760       C  
ATOM   1749  NE1 TRP A 257      18.216  25.541  22.954  1.00133.06           N  
ANISOU 1749  NE1 TRP A 257    18108  18851  13598   -412   -927  -1731       N  
ATOM   1750  CE2 TRP A 257      17.450  26.195  23.885  1.00139.99           C  
ANISOU 1750  CE2 TRP A 257    18755  19893  14543   -362   -769  -1772       C  
ATOM   1751  CE3 TRP A 257      17.070  26.113  26.268  1.00144.52           C  
ANISOU 1751  CE3 TRP A 257    19286  20603  15023   -564   -374  -1829       C  
ATOM   1752  CZ2 TRP A 257      16.543  27.237  23.727  1.00151.59           C  
ANISOU 1752  CZ2 TRP A 257    19905  21525  16165   -176   -764  -1819       C  
ATOM   1753  CZ3 TRP A 257      16.169  27.148  26.111  1.00147.54           C  
ANISOU 1753  CZ3 TRP A 257    19340  21152  15568   -365   -319  -1927       C  
ATOM   1754  CH2 TRP A 257      15.913  27.700  24.850  1.00149.50           C  
ANISOU 1754  CH2 TRP A 257    19444  21396  15965   -159   -532  -1907       C  
ATOM   1755  N   HIS A 258      17.082  22.666  27.828  1.00120.59           N  
ANISOU 1755  N   HIS A 258    16622  17479  11718  -1481   -322  -1590       N  
ATOM   1756  CA  HIS A 258      15.826  23.050  28.466  1.00123.97           C  
ANISOU 1756  CA  HIS A 258    16730  18229  12143  -1578   -107  -1682       C  
ATOM   1757  C   HIS A 258      16.040  24.339  29.261  1.00115.95           C  
ANISOU 1757  C   HIS A 258    15688  17292  11075  -1369     92  -1787       C  
ATOM   1758  O   HIS A 258      17.067  24.511  29.917  1.00107.72           O  
ANISOU 1758  O   HIS A 258    14934  16100   9894  -1356    108  -1730       O  
ATOM   1759  CB  HIS A 258      15.308  21.932  29.377  1.00132.01           C  
ANISOU 1759  CB  HIS A 258    17775  19344  13038  -2014     -4  -1590       C  
ATOM   1760  CG  HIS A 258      16.146  21.707  30.598  1.00134.81           C  
ANISOU 1760  CG  HIS A 258    18445  19595  13182  -2182     71  -1471       C  
ATOM   1761  ND1 HIS A 258      16.078  22.524  31.707  1.00135.00           N  
ANISOU 1761  ND1 HIS A 258    18453  19796  13045  -2190    317  -1549       N  
ATOM   1762  CD2 HIS A 258      17.077  20.766  30.880  1.00126.79           C  
ANISOU 1762  CD2 HIS A 258    17769  18309  12098  -2357    -87  -1276       C  
ATOM   1763  CE1 HIS A 258      16.924  22.090  32.623  1.00128.60           C  
ANISOU 1763  CE1 HIS A 258    17974  18856  12033  -2394    288  -1387       C  
ATOM   1764  NE2 HIS A 258      17.545  21.026  32.146  1.00123.15           N  
ANISOU 1764  NE2 HIS A 258    17489  17884  11419  -2485     31  -1203       N  
ATOM   1765  N   GLY A 259      15.068  25.240  29.197  1.00120.14           N  
ANISOU 1765  N   GLY A 259    15863  18044  11741  -1208    233  -1945       N  
ATOM   1766  CA  GLY A 259      15.213  26.562  29.776  1.00134.05           C  
ANISOU 1766  CA  GLY A 259    17578  19839  13516   -961    417  -2092       C  
ATOM   1767  C   GLY A 259      15.037  26.665  31.281  1.00145.53           C  
ANISOU 1767  C   GLY A 259    19075  21456  14765  -1179    738  -2183       C  
ATOM   1768  O   GLY A 259      15.556  27.589  31.905  1.00146.39           O  
ANISOU 1768  O   GLY A 259    19307  21517  14798  -1039    867  -2289       O  
ATOM   1769  N   HIS A 260      14.308  25.716  31.860  1.00153.71           N  
ANISOU 1769  N   HIS A 260    20026  22689  15687  -1554    866  -2145       N  
ATOM   1770  CA  HIS A 260      13.740  25.873  33.201  1.00154.64           C  
ANISOU 1770  CA  HIS A 260    20071  23070  15617  -1798   1234  -2278       C  
ATOM   1771  C   HIS A 260      14.733  26.142  34.339  1.00134.61           C  
ANISOU 1771  C   HIS A 260    17927  20458  12761  -1916   1336  -2262       C  
ATOM   1772  O   HIS A 260      14.416  26.897  35.256  1.00133.78           O  
ANISOU 1772  O   HIS A 260    17757  20533  12540  -1941   1657  -2478       O  
ATOM   1773  CB  HIS A 260      12.899  24.641  33.538  1.00163.37           C  
ANISOU 1773  CB  HIS A 260    21066  24381  16626  -2245   1308  -2177       C  
ATOM   1774  CG  HIS A 260      11.605  24.575  32.784  1.00170.68           C  
ANISOU 1774  CG  HIS A 260    21502  25507  17841  -2194   1328  -2266       C  
ATOM   1775  ND1 HIS A 260      11.071  23.393  32.319  1.00174.05           N  
ANISOU 1775  ND1 HIS A 260    21848  25976  18307  -2480   1177  -2114       N  
ATOM   1776  CD2 HIS A 260      10.738  25.549  32.418  1.00173.84           C  
ANISOU 1776  CD2 HIS A 260    21456  26064  18534  -1897   1456  -2481       C  
ATOM   1777  CE1 HIS A 260       9.932  23.641  31.697  1.00176.07           C  
ANISOU 1777  CE1 HIS A 260    21625  26433  18841  -2378   1205  -2226       C  
ATOM   1778  NE2 HIS A 260       9.706  24.941  31.743  1.00176.47           N  
ANISOU 1778  NE2 HIS A 260    21432  26554  19066  -2014   1367  -2439       N  
ATOM   1779  N   GLY A 261      15.916  25.537  34.304  1.00123.38           N  
ANISOU 1779  N   GLY A 261    16899  18774  11205  -1998   1070  -2023       N  
ATOM   1780  CA  GLY A 261      16.898  25.823  35.338  1.00119.55           C  
ANISOU 1780  CA  GLY A 261    16775  18214  10433  -2113   1107  -1978       C  
ATOM   1781  C   GLY A 261      17.847  24.699  35.709  1.00124.37           C  
ANISOU 1781  C   GLY A 261    17764  18634  10856  -2410    858  -1656       C  
ATOM   1782  O   GLY A 261      18.269  23.917  34.858  1.00122.12           O  
ANISOU 1782  O   GLY A 261    17543  18116  10742  -2356    575  -1476       O  
ATOM   1783  N   TRP A 262      18.211  24.656  36.989  1.00129.98           N  
ANISOU 1783  N   TRP A 262    18733  19432  11223  -2724    959  -1590       N  
ATOM   1784  CA  TRP A 262      19.106  23.638  37.535  1.00132.01           C  
ANISOU 1784  CA  TRP A 262    19351  19510  11297  -3041    704  -1248       C  
ATOM   1785  C   TRP A 262      18.363  22.357  37.896  1.00143.43           C  
ANISOU 1785  C   TRP A 262    20783  21074  12639  -3489    720  -1066       C  
ATOM   1786  O   TRP A 262      17.168  22.380  38.198  1.00148.56           O  
ANISOU 1786  O   TRP A 262    21189  22046  13210  -3670   1020  -1224       O  
ATOM   1787  CB  TRP A 262      19.821  24.155  38.781  1.00132.12           C  
ANISOU 1787  CB  TRP A 262    19670  19579  10949  -3236    761  -1220       C  
ATOM   1788  CG  TRP A 262      20.646  25.376  38.569  1.00127.24           C  
ANISOU 1788  CG  TRP A 262    19116  18826  10403  -2865    726  -1372       C  
ATOM   1789  CD1 TRP A 262      20.263  26.671  38.765  1.00132.29           C  
ANISOU 1789  CD1 TRP A 262    19627  19621  11016  -2668   1015  -1716       C  
ATOM   1790  CD2 TRP A 262      22.009  25.420  38.132  1.00118.07           C  
ANISOU 1790  CD2 TRP A 262    18156  17329   9376  -2655    386  -1188       C  
ATOM   1791  NE1 TRP A 262      21.306  27.520  38.472  1.00129.07           N  
ANISOU 1791  NE1 TRP A 262    19355  18986  10700  -2368    856  -1740       N  
ATOM   1792  CE2 TRP A 262      22.388  26.777  38.081  1.00125.59           C  
ANISOU 1792  CE2 TRP A 262    19105  18263  10350  -2362    478  -1418       C  
ATOM   1793  CE3 TRP A 262      22.945  24.444  37.776  1.00107.83           C  
ANISOU 1793  CE3 TRP A 262    17023  15733   8216  -2684     22   -863       C  
ATOM   1794  CZ2 TRP A 262      23.664  27.180  37.687  1.00115.22           C  
ANISOU 1794  CZ2 TRP A 262    17944  16674   9159  -2128    219  -1315       C  
ATOM   1795  CZ3 TRP A 262      24.210  24.847  37.385  1.00104.20           C  
ANISOU 1795  CZ3 TRP A 262    16686  15004   7903  -2425   -214   -783       C  
ATOM   1796  CH2 TRP A 262      24.558  26.203  37.343  1.00105.34           C  
ANISOU 1796  CH2 TRP A 262    16821  15169   8035  -2165   -115   -999       C  
ATOM   1797  N   VAL A 263      19.077  21.237  37.870  1.00150.30           N  
ANISOU 1797  N   VAL A 263    21901  21670  13537  -3670    395   -730       N  
ATOM   1798  CA  VAL A 263      18.469  19.952  38.184  1.00162.29           C  
ANISOU 1798  CA  VAL A 263    23448  23231  14984  -4112    356   -512       C  
ATOM   1799  C   VAL A 263      19.259  19.184  39.247  1.00162.73           C  
ANISOU 1799  C   VAL A 263    23897  23153  14781  -4522    140   -139       C  
ATOM   1800  O   VAL A 263      20.491  19.229  39.283  1.00151.25           O  
ANISOU 1800  O   VAL A 263    22679  21410  13381  -4383   -138     31       O  
ATOM   1801  CB  VAL A 263      18.328  19.084  36.915  1.00170.98           C  
ANISOU 1801  CB  VAL A 263    24423  24074  16465  -3962    133   -452       C  
ATOM   1802  CG1 VAL A 263      19.689  18.754  36.341  1.00172.78           C  
ANISOU 1802  CG1 VAL A 263    24877  23852  16919  -3718   -228   -279       C  
ATOM   1803  CG2 VAL A 263      17.543  17.813  37.213  1.00178.12           C  
ANISOU 1803  CG2 VAL A 263    25328  25034  17317  -4435    118   -261       C  
ATOM   1804  N   GLY A 264      18.532  18.505  40.129  1.00175.23           N  
ANISOU 1804  N   GLY A 264    25535  24961  16081  -5045    263      2       N  
ATOM   1805  CA  GLY A 264      19.124  17.548  41.042  1.00173.67           C  
ANISOU 1805  CA  GLY A 264    25702  24616  15667  -5500      0    429       C  
ATOM   1806  C   GLY A 264      19.774  18.159  42.261  1.00162.39           C  
ANISOU 1806  C   GLY A 264    24561  23330  13809  -5715     24    510       C  
ATOM   1807  O   GLY A 264      19.663  19.356  42.511  1.00145.98           O  
ANISOU 1807  O   GLY A 264    22403  21502  11560  -5550    309    189       O  
ATOM   1808  N   GLU A 265      20.452  17.313  43.027  1.00165.84           N  
ANISOU 1808  N   GLU A 265    25342  23591  14079  -6102   -301    951       N  
ATOM   1809  CA  GLU A 265      21.113  17.739  44.251  1.00170.58           C  
ANISOU 1809  CA  GLU A 265    26265  24323  14224  -6401   -354   1102       C  
ATOM   1810  C   GLU A 265      22.544  17.218  44.311  1.00158.30           C  
ANISOU 1810  C   GLU A 265    24987  22312  12846  -6350   -902   1525       C  
ATOM   1811  O   GLU A 265      22.889  16.238  43.646  1.00151.06           O  
ANISOU 1811  O   GLU A 265    24056  20990  12349  -6234  -1225   1767       O  
ATOM   1812  CB  GLU A 265      20.327  17.254  45.468  1.00179.03           C  
ANISOU 1812  CB  GLU A 265    27497  25763  14762  -7107   -167   1262       C  
ATOM   1813  CG  GLU A 265      18.893  17.750  45.510  1.00170.77           C  
ANISOU 1813  CG  GLU A 265    26138  25198  13549  -7193    410    837       C  
ATOM   1814  CD  GLU A 265      18.038  16.956  46.466  1.00168.56           C  
ANISOU 1814  CD  GLU A 265    25899  25176  12972  -7837    557   1017       C  
ATOM   1815  OE1 GLU A 265      18.575  16.034  47.113  1.00172.63           O  
ANISOU 1815  OE1 GLU A 265    26694  25468  13428  -8206    183   1477       O  
ATOM   1816  OE2 GLU A 265      16.827  17.244  46.555  1.00170.72           O  
ANISOU 1816  OE2 GLU A 265    25888  25853  13126  -7957   1033    696       O  
ATOM   1817  N   GLY A 266      23.367  17.867  45.125  1.00148.12           N  
ANISOU 1817  N   GLY A 266    23936  21085  11257  -6445  -1005   1601       N  
ATOM   1818  CA  GLY A 266      24.703  17.377  45.397  1.00142.85           C  
ANISOU 1818  CA  GLY A 266    23488  20016  10772  -6452  -1534   2032       C  
ATOM   1819  C   GLY A 266      25.801  18.077  44.630  1.00131.40           C  
ANISOU 1819  C   GLY A 266    21983  18303   9640  -5905  -1716   1925       C  
ATOM   1820  O   GLY A 266      25.566  19.078  43.958  1.00140.71           O  
ANISOU 1820  O   GLY A 266    22940  19600  10925  -5492  -1418   1488       O  
ATOM   1821  N   LYS A 267      27.008  17.532  44.730  1.00122.47           N  
ANISOU 1821  N   LYS A 267    21006  16787   8740  -5885  -2214   2330       N  
ATOM   1822  CA  LYS A 267      28.186  18.123  44.107  1.00113.65           C  
ANISOU 1822  CA  LYS A 267    19805  15397   7982  -5394  -2413   2269       C  
ATOM   1823  C   LYS A 267      28.420  17.610  42.691  1.00106.16           C  
ANISOU 1823  C   LYS A 267    18595  14051   7690  -4890  -2498   2188       C  
ATOM   1824  O   LYS A 267      27.898  16.563  42.309  1.00 99.57           O  
ANISOU 1824  O   LYS A 267    17707  13050   7074  -4967  -2540   2294       O  
ATOM   1825  CB  LYS A 267      29.417  17.853  44.970  1.00121.46           C  
ANISOU 1825  CB  LYS A 267    20989  16167   8993  -5589  -2882   2706       C  
ATOM   1826  CG  LYS A 267      29.327  18.470  46.363  1.00149.19           C  
ANISOU 1826  CG  LYS A 267    24565  19983  12136  -5946  -2725   2644       C  
ATOM   1827  CD  LYS A 267      30.462  18.021  47.278  1.00161.62           C  
ANISOU 1827  CD  LYS A 267    26272  21327  13811  -6183  -3208   3085       C  
ATOM   1828  CE  LYS A 267      31.813  18.558  46.827  1.00154.79           C  
ANISOU 1828  CE  LYS A 267    25337  20201  13274  -5787  -3489   3127       C  
ATOM   1829  NZ  LYS A 267      32.469  17.696  45.801  1.00156.92           N  
ANISOU 1829  NZ  LYS A 267    25548  20021  14055  -5477  -3865   3397       N  
ATOM   1830  N   TRP A 268      29.195  18.373  41.918  1.00117.93           N  
ANISOU 1830  N   TRP A 268    19936  15402   9469  -4403  -2507   1981       N  
ATOM   1831  CA  TRP A 268      29.503  18.044  40.524  1.00116.87           C  
ANISOU 1831  CA  TRP A 268    19562  14931   9913  -3916  -2544   1846       C  
ATOM   1832  C   TRP A 268      30.685  17.098  40.357  1.00115.54           C  
ANISOU 1832  C   TRP A 268    19421  14266  10213  -3821  -2998   2212       C  
ATOM   1833  O   TRP A 268      31.644  17.146  41.125  1.00125.81           O  
ANISOU 1833  O   TRP A 268    20864  15469  11469  -3955  -3317   2522       O  
ATOM   1834  CB  TRP A 268      29.806  19.312  39.727  1.00113.69           C  
ANISOU 1834  CB  TRP A 268    18982  14613   9602  -3456  -2333   1464       C  
ATOM   1835  CG  TRP A 268      28.655  20.244  39.571  1.00124.22           C  
ANISOU 1835  CG  TRP A 268    20206  16340  10651  -3412  -1891   1058       C  
ATOM   1836  CD1 TRP A 268      28.511  21.473  40.144  1.00131.59           C  
ANISOU 1836  CD1 TRP A 268    21192  17580  11227  -3446  -1676    848       C  
ATOM   1837  CD2 TRP A 268      27.462  20.010  38.809  1.00131.63           C  
ANISOU 1837  CD2 TRP A 268    20949  17394  11671  -3329  -1620    812       C  
ATOM   1838  NE1 TRP A 268      27.310  22.028  39.770  1.00132.96           N  
ANISOU 1838  NE1 TRP A 268    21188  18030  11299  -3354  -1282    483       N  
ATOM   1839  CE2 TRP A 268      26.651  21.152  38.960  1.00137.33           C  
ANISOU 1839  CE2 TRP A 268    21581  18489  12111  -3290  -1255    472       C  
ATOM   1840  CE3 TRP A 268      27.011  18.951  38.021  1.00123.64           C  
ANISOU 1840  CE3 TRP A 268    19828  16194  10958  -3294  -1663    842       C  
ATOM   1841  CZ2 TRP A 268      25.407  21.260  38.331  1.00134.08           C  
ANISOU 1841  CZ2 TRP A 268    20936  18274  11734  -3200   -956    191       C  
ATOM   1842  CZ3 TRP A 268      25.774  19.063  37.410  1.00119.32           C  
ANISOU 1842  CZ3 TRP A 268    19079  15864  10392  -3242  -1368    559       C  
ATOM   1843  CH2 TRP A 268      24.988  20.208  37.568  1.00122.78           C  
ANISOU 1843  CH2 TRP A 268    19397  16682  10571  -3191  -1029    252       C  
ATOM   1844  N   THR A 269      30.608  16.248  39.339  1.00119.13           N  
ANISOU 1844  N   THR A 269    19726  14404  11133  -3590  -3027   2159       N  
ATOM   1845  CA  THR A 269      31.732  15.412  38.931  1.00138.19           C  
ANISOU 1845  CA  THR A 269    22092  16302  14110  -3383  -3388   2395       C  
ATOM   1846  C   THR A 269      32.130  15.790  37.505  1.00137.48           C  
ANISOU 1846  C   THR A 269    21750  16067  14420  -2844  -3218   2026       C  
ATOM   1847  O   THR A 269      31.296  15.772  36.600  1.00137.69           O  
ANISOU 1847  O   THR A 269    21657  16179  14479  -2707  -2937   1704       O  
ATOM   1848  CB  THR A 269      31.399  13.906  39.013  1.00141.55           C  
ANISOU 1848  CB  THR A 269    22599  16399  14786  -3619  -3600   2675       C  
ATOM   1849  OG1 THR A 269      30.359  13.590  38.082  1.00146.94           O  
ANISOU 1849  OG1 THR A 269    23160  17126  15543  -3530  -3304   2352       O  
ATOM   1850  CG2 THR A 269      30.943  13.527  40.417  1.00136.21           C  
ANISOU 1850  CG2 THR A 269    22193  15899  13663  -4210  -3759   3064       C  
ATOM   1851  N   VAL A 270      33.402  16.122  37.302  1.00136.61           N  
ANISOU 1851  N   VAL A 270    21552  15752  14600  -2569  -3396   2083       N  
ATOM   1852  CA  VAL A 270      33.872  16.614  36.004  1.00142.30           C  
ANISOU 1852  CA  VAL A 270    22046  16386  15637  -2095  -3214   1736       C  
ATOM   1853  C   VAL A 270      34.750  15.594  35.271  1.00159.23           C  
ANISOU 1853  C   VAL A 270    24054  18018  18429  -1843  -3405   1804       C  
ATOM   1854  O   VAL A 270      35.721  15.081  35.823  1.00175.75           O  
ANISOU 1854  O   VAL A 270    26155  19808  20814  -1875  -3758   2146       O  
ATOM   1855  CB  VAL A 270      34.659  17.943  36.157  1.00102.23           C  
ANISOU 1855  CB  VAL A 270    16928  11501  10415  -1936  -3187   1663       C  
ATOM   1856  CG1 VAL A 270      35.648  17.861  37.316  1.00125.46           C  
ANISOU 1856  CG1 VAL A 270    19984  14332  13351  -2143  -3580   2085       C  
ATOM   1857  CG2 VAL A 270      35.368  18.308  34.861  1.00 92.02           C  
ANISOU 1857  CG2 VAL A 270    15403  10062   9497  -1484  -3060   1389       C  
ATOM   1858  N   LYS A 271      34.396  15.301  34.022  1.00160.81           N  
ANISOU 1858  N   LYS A 271    24122  18119  18859  -1600  -3173   1468       N  
ATOM   1859  CA  LYS A 271      35.174  14.377  33.200  1.00157.24           C  
ANISOU 1859  CA  LYS A 271    23532  17189  19024  -1339  -3271   1427       C  
ATOM   1860  C   LYS A 271      35.460  14.961  31.809  1.00158.86           C  
ANISOU 1860  C   LYS A 271    23544  17442  19374   -955  -2970    993       C  
ATOM   1861  O   LYS A 271      34.573  15.525  31.170  1.00161.79           O  
ANISOU 1861  O   LYS A 271    23912  18121  19439   -931  -2680    691       O  
ATOM   1862  CB  LYS A 271      34.426  13.044  33.063  1.00147.62           C  
ANISOU 1862  CB  LYS A 271    22399  15704  17985  -1514  -3323   1470       C  
ATOM   1863  CG  LYS A 271      34.424  12.178  34.321  1.00150.98           C  
ANISOU 1863  CG  LYS A 271    23005  15929  18432  -1878  -3694   1965       C  
ATOM   1864  CD  LYS A 271      33.409  11.039  34.210  1.00148.92           C  
ANISOU 1864  CD  LYS A 271    22859  15503  18220  -2123  -3690   1981       C  
ATOM   1865  CE  LYS A 271      33.335  10.209  35.487  1.00142.84           C  
ANISOU 1865  CE  LYS A 271    22298  14559  17417  -2542  -4064   2509       C  
ATOM   1866  NZ  LYS A 271      32.308   9.129  35.412  1.00129.32           N  
ANISOU 1866  NZ  LYS A 271    20707  12698  15732  -2825  -4059   2542       N  
ATOM   1867  N   LYS A 272      36.705  14.834  31.353  1.00156.98           N  
ANISOU 1867  N   LYS A 272    23134  16909  19603   -670  -3048    977       N  
ATOM   1868  CA  LYS A 272      37.095  15.258  30.005  1.00148.47           C  
ANISOU 1868  CA  LYS A 272    21878  15848  18688   -336  -2761    578       C  
ATOM   1869  C   LYS A 272      37.384  14.038  29.124  1.00154.75           C  
ANISOU 1869  C   LYS A 272    22578  16195  20023   -173  -2726    404       C  
ATOM   1870  O   LYS A 272      38.345  13.307  29.370  1.00153.80           O  
ANISOU 1870  O   LYS A 272    22353  15660  20423    -68  -2947    584       O  
ATOM   1871  CB  LYS A 272      38.318  16.185  30.053  1.00136.12           C  
ANISOU 1871  CB  LYS A 272    20157  14340  17223   -136  -2798    622       C  
ATOM   1872  CG  LYS A 272      38.154  17.395  30.971  1.00126.79           C  
ANISOU 1872  CG  LYS A 272    19085  13548  15542   -302  -2850    780       C  
ATOM   1873  CD  LYS A 272      39.446  18.207  31.096  1.00127.74           C  
ANISOU 1873  CD  LYS A 272    19055  13674  15805   -143  -2942    864       C  
ATOM   1874  CE  LYS A 272      40.625  17.360  31.585  1.00136.37           C  
ANISOU 1874  CE  LYS A 272    20013  14355  17447    -90  -3286   1177       C  
ATOM   1875  NZ  LYS A 272      40.473  16.834  32.976  1.00134.52           N  
ANISOU 1875  NZ  LYS A 272    19958  14040  17114   -410  -3667   1621       N  
ATOM   1876  N   GLY A 273      36.559  13.819  28.102  1.00160.43           N  
ANISOU 1876  N   GLY A 273    23329  16988  20638   -156  -2459     49       N  
ATOM   1877  CA  GLY A 273      36.645  12.603  27.310  1.00166.51           C  
ANISOU 1877  CA  GLY A 273    24065  17339  21861    -64  -2408   -155       C  
ATOM   1878  C   GLY A 273      36.252  12.745  25.850  1.00166.48           C  
ANISOU 1878  C   GLY A 273    24030  17468  21759     57  -2052   -646       C  
ATOM   1879  O   GLY A 273      35.568  13.691  25.472  1.00165.21           O  
ANISOU 1879  O   GLY A 273    23906  17746  21121     11  -1871   -794       O  
ATOM   1880  N   ASN A 274      36.699  11.802  25.026  1.00173.16           N  
ANISOU 1880  N   ASN A 274    24809  17919  23065    205  -1959   -900       N  
ATOM   1881  CA  ASN A 274      36.238  11.703  23.645  1.00170.57           C  
ANISOU 1881  CA  ASN A 274    24504  17679  22628    244  -1642  -1374       C  
ATOM   1882  C   ASN A 274      34.816  11.148  23.583  1.00174.96           C  
ANISOU 1882  C   ASN A 274    25254  18313  22911    -46  -1657  -1422       C  
ATOM   1883  O   ASN A 274      34.241  10.787  24.608  1.00173.40           O  
ANISOU 1883  O   ASN A 274    25161  18078  22646   -270  -1890  -1094       O  
ATOM   1884  CB  ASN A 274      37.180  10.819  22.823  1.00161.98           C  
ANISOU 1884  CB  ASN A 274    23291  16125  22128    474  -1510  -1673       C  
ATOM   1885  CG  ASN A 274      38.438  11.547  22.390  1.00160.04           C  
ANISOU 1885  CG  ASN A 274    22816  15939  22053    759  -1345  -1794       C  
ATOM   1886  OD1 ASN A 274      38.593  11.906  21.220  1.00157.62           O  
ANISOU 1886  OD1 ASN A 274    22464  15800  21624    853  -1020  -2190       O  
ATOM   1887  ND2 ASN A 274      39.340  11.781  23.336  1.00163.46           N  
ANISOU 1887  ND2 ASN A 274    23104  16255  22747    865  -1578  -1439       N  
ATOM   1888  N   VAL A 275      34.256  11.066  22.379  1.00173.49           N  
ANISOU 1888  N   VAL A 275    25115  18246  22558    -72  -1414  -1824       N  
ATOM   1889  CA  VAL A 275      32.919  10.508  22.202  1.00172.69           C  
ANISOU 1889  CA  VAL A 275    25171  18218  22225   -358  -1430  -1898       C  
ATOM   1890  C   VAL A 275      32.895   9.454  21.101  1.00189.05           C  
ANISOU 1890  C   VAL A 275    27307  19959  24566   -363  -1284  -2306       C  
ATOM   1891  O   VAL A 275      33.742   9.453  20.204  1.00199.71           O  
ANISOU 1891  O   VAL A 275    28580  21183  26119   -147  -1072  -2629       O  
ATOM   1892  CB  VAL A 275      31.881  11.599  21.865  1.00162.07           C  
ANISOU 1892  CB  VAL A 275    23844  17464  20271   -480  -1319  -1962       C  
ATOM   1893  CG1 VAL A 275      31.604  12.473  23.076  1.00155.23           C  
ANISOU 1893  CG1 VAL A 275    22954  16898  19130   -547  -1462  -1583       C  
ATOM   1894  CG2 VAL A 275      32.351  12.434  20.684  1.00162.93           C  
ANISOU 1894  CG2 VAL A 275    23881  17803  20223   -288  -1070  -2281       C  
ATOM   1895  N   SER A 276      31.908   8.567  21.174  1.00208.02           N  
ANISOU 1895  N   SER A 276    29854  22230  26952   -634  -1382  -2307       N  
ATOM   1896  CA  SER A 276      31.788   7.457  20.233  1.00216.36           C  
ANISOU 1896  CA  SER A 276    31011  22926  28268   -693  -1274  -2692       C  
ATOM   1897  C   SER A 276      31.360   7.910  18.844  1.00209.44           C  
ANISOU 1897  C   SER A 276    30173  22395  27012   -732  -1003  -3139       C  
ATOM   1898  O   SER A 276      30.975   9.062  18.638  1.00211.20           O  
ANISOU 1898  O   SER A 276    30346  23142  26757   -741   -938  -3105       O  
ATOM   1899  CB  SER A 276      30.795   6.415  20.753  1.00222.72           C  
ANISOU 1899  CB  SER A 276    31973  23510  29139  -1022  -1482  -2534       C  
ATOM   1900  OG  SER A 276      29.460   6.867  20.615  1.00223.29           O  
ANISOU 1900  OG  SER A 276    32099  24071  28670  -1303  -1474  -2526       O  
ATOM   1901  N   SER A 277      31.449   6.989  17.892  1.00200.87           N  
ANISOU 1901  N   SER A 277    29184  20989  26148   -764   -857  -3557       N  
ATOM   1902  CA  SER A 277      30.908   7.194  16.557  1.00187.40           C  
ANISOU 1902  CA  SER A 277    27573  19578  24053   -898   -639  -3987       C  
ATOM   1903  C   SER A 277      29.394   7.389  16.617  1.00179.12           C  
ANISOU 1903  C   SER A 277    26610  18921  22526  -1242   -786  -3858       C  
ATOM   1904  O   SER A 277      28.838   8.204  15.883  1.00170.75           O  
ANISOU 1904  O   SER A 277    25550  18343  20985  -1329   -702  -3980       O  
ATOM   1905  CB  SER A 277      31.265   6.014  15.653  1.00190.98           C  
ANISOU 1905  CB  SER A 277    28144  19553  24865   -910   -465  -4473       C  
ATOM   1906  OG  SER A 277      32.668   5.814  15.603  1.00194.02           O  
ANISOU 1906  OG  SER A 277    28398  19563  25756   -571   -309  -4611       O  
ATOM   1907  N   THR A 278      28.736   6.641  17.501  1.00179.07           N  
ANISOU 1907  N   THR A 278    26661  18707  22672  -1446  -1016  -3591       N  
ATOM   1908  CA  THR A 278      27.303   6.805  17.742  1.00167.73           C  
ANISOU 1908  CA  THR A 278    25250  17641  20839  -1776  -1159  -3420       C  
ATOM   1909  C   THR A 278      27.040   8.103  18.501  1.00163.61           C  
ANISOU 1909  C   THR A 278    24570  17617  19976  -1704  -1217  -3064       C  
ATOM   1910  O   THR A 278      25.901   8.552  18.619  1.00147.54           O  
ANISOU 1910  O   THR A 278    22489  15989  17580  -1913  -1285  -2948       O  
ATOM   1911  CB  THR A 278      26.722   5.621  18.549  1.00161.47           C  
ANISOU 1911  CB  THR A 278    24559  16478  20315  -2045  -1374  -3211       C  
ATOM   1912  OG1 THR A 278      27.311   4.396  18.099  1.00170.82           O  
ANISOU 1912  OG1 THR A 278    25879  17046  21981  -2018  -1337  -3491       O  
ATOM   1913  CG2 THR A 278      25.206   5.540  18.394  1.00159.33           C  
ANISOU 1913  CG2 THR A 278    24318  16547  19673  -2437  -1462  -3194       C  
ATOM   1914  N   GLY A 279      28.113   8.703  19.005  1.00186.38           N  
ANISOU 1914  N   GLY A 279    27358  20454  23004  -1406  -1187  -2908       N  
ATOM   1915  CA  GLY A 279      28.038   9.963  19.721  1.00198.42           C  
ANISOU 1915  CA  GLY A 279    28753  22397  24241  -1311  -1223  -2611       C  
ATOM   1916  C   GLY A 279      27.711   9.769  21.185  1.00197.57           C  
ANISOU 1916  C   GLY A 279    28639  22241  24190  -1447  -1425  -2184       C  
ATOM   1917  O   GLY A 279      27.227  10.681  21.852  1.00190.69           O  
ANISOU 1917  O   GLY A 279    27683  21756  23013  -1481  -1455  -1959       O  
ATOM   1918  N   ARG A 280      27.999   8.574  21.687  1.00189.53           N  
ANISOU 1918  N   ARG A 280    27716  20731  23568  -1532  -1561  -2076       N  
ATOM   1919  CA  ARG A 280      27.819   8.258  23.096  1.00176.84           C  
ANISOU 1919  CA  ARG A 280    26138  19024  22029  -1699  -1776  -1639       C  
ATOM   1920  C   ARG A 280      29.032   8.736  23.884  1.00162.72           C  
ANISOU 1920  C   ARG A 280    24284  17119  20421  -1447  -1853  -1387       C  
ATOM   1921  O   ARG A 280      30.166   8.404  23.540  1.00160.84           O  
ANISOU 1921  O   ARG A 280    24018  16508  20586  -1195  -1836  -1498       O  
ATOM   1922  CB  ARG A 280      27.613   6.749  23.283  1.00182.89           C  
ANISOU 1922  CB  ARG A 280    27051  19276  23163  -1926  -1934  -1589       C  
ATOM   1923  CG  ARG A 280      27.094   6.325  24.652  1.00178.16           C  
ANISOU 1923  CG  ARG A 280    26521  18638  22535  -2230  -2164  -1128       C  
ATOM   1924  CD  ARG A 280      27.285   4.825  24.867  1.00174.42           C  
ANISOU 1924  CD  ARG A 280    26201  17519  22552  -2381  -2361  -1031       C  
ATOM   1925  NE  ARG A 280      28.699   4.477  24.984  1.00175.05           N  
ANISOU 1925  NE  ARG A 280    26265  17092  23155  -2065  -2454   -980       N  
ATOM   1926  CZ  ARG A 280      29.251   3.933  26.063  1.00173.80           C  
ANISOU 1926  CZ  ARG A 280    26161  16566  23311  -2111  -2735   -553       C  
ATOM   1927  NH1 ARG A 280      28.505   3.652  27.121  1.00176.28           N  
ANISOU 1927  NH1 ARG A 280    26584  16971  23424  -2493  -2933   -147       N  
ATOM   1928  NH2 ARG A 280      30.548   3.657  26.081  1.00170.57           N  
ANISOU 1928  NH2 ARG A 280    25685  15701  23424  -1793  -2824   -524       N  
ATOM   1929  N   CYS A 281      28.805   9.529  24.927  1.00152.53           N  
ANISOU 1929  N   CYS A 281    22958  16157  18842  -1520  -1927  -1069       N  
ATOM   1930  CA  CYS A 281      29.917  10.004  25.741  1.00143.11           C  
ANISOU 1930  CA  CYS A 281    21718  14879  17779  -1331  -2034   -808       C  
ATOM   1931  C   CYS A 281      30.452   8.841  26.561  1.00136.76           C  
ANISOU 1931  C   CYS A 281    21004  13548  17409  -1426  -2306   -503       C  
ATOM   1932  O   CYS A 281      29.719   8.236  27.344  1.00132.43           O  
ANISOU 1932  O   CYS A 281    20574  12962  16783  -1755  -2463   -242       O  
ATOM   1933  CB  CYS A 281      29.496  11.157  26.652  1.00151.22           C  
ANISOU 1933  CB  CYS A 281    22713  16393  18353  -1420  -2032   -582       C  
ATOM   1934  SG  CYS A 281      30.822  11.784  27.725  1.00138.88           S  
ANISOU 1934  SG  CYS A 281    21120  14760  16889  -1255  -2198   -249       S  
ATOM   1935  N   LEU A 282      31.728   8.530  26.365  1.00146.88           N  
ANISOU 1935  N   LEU A 282    22219  14421  19167  -1145  -2365   -526       N  
ATOM   1936  CA  LEU A 282      32.351   7.371  26.992  1.00171.38           C  
ANISOU 1936  CA  LEU A 282    25377  16937  22801  -1176  -2649   -252       C  
ATOM   1937  C   LEU A 282      32.272   7.418  28.516  1.00189.99           C  
ANISOU 1937  C   LEU A 282    27824  19358  25005  -1431  -2952    297       C  
ATOM   1938  O   LEU A 282      32.120   6.383  29.170  1.00216.56           O  
ANISOU 1938  O   LEU A 282    31318  22360  28606  -1661  -3214    595       O  
ATOM   1939  CB  LEU A 282      33.810   7.261  26.552  1.00169.11           C  
ANISOU 1939  CB  LEU A 282    24926  16268  23059   -780  -2641   -372       C  
ATOM   1940  CG  LEU A 282      34.037   7.191  25.043  1.00161.67           C  
ANISOU 1940  CG  LEU A 282    23902  15253  22272   -540  -2310   -938       C  
ATOM   1941  CD1 LEU A 282      35.516   7.035  24.742  1.00161.83           C  
ANISOU 1941  CD1 LEU A 282    23726  14888  22875   -164  -2288  -1036       C  
ATOM   1942  CD2 LEU A 282      33.233   6.052  24.426  1.00166.58           C  
ANISOU 1942  CD2 LEU A 282    24674  15591  23029   -727  -2265  -1183       C  
ATOM   1943  N   SER A 283      32.370   8.622  29.070  1.00169.79           N  
ANISOU 1943  N   SER A 283    25218  17258  22038  -1413  -2916    426       N  
ATOM   1944  CA  SER A 283      32.384   8.808  30.516  1.00157.31           C  
ANISOU 1944  CA  SER A 283    23735  15793  20240  -1667  -3175    913       C  
ATOM   1945  C   SER A 283      31.054   8.481  31.204  1.00166.67           C  
ANISOU 1945  C   SER A 283    25092  17207  21029  -2127  -3204   1095       C  
ATOM   1946  O   SER A 283      31.038   7.760  32.200  1.00176.70           O  
ANISOU 1946  O   SER A 283    26506  18264  22367  -2417  -3493   1509       O  
ATOM   1947  CB  SER A 283      32.795  10.242  30.847  1.00131.91           C  
ANISOU 1947  CB  SER A 283    20435  13018  16666  -1537  -3085    927       C  
ATOM   1948  OG  SER A 283      31.822  11.162  30.395  1.00127.78           O  
ANISOU 1948  OG  SER A 283    19887  13012  15650  -1569  -2779    643       O  
ATOM   1949  N   CYS A 284      29.944   9.002  30.682  1.00150.96           N  
ANISOU 1949  N   CYS A 284    23073  15649  18634  -2211  -2918    805       N  
ATOM   1950  CA  CYS A 284      28.656   8.841  31.361  1.00137.61           C  
ANISOU 1950  CA  CYS A 284    21488  14255  16543  -2647  -2899    957       C  
ATOM   1951  C   CYS A 284      27.670   7.954  30.596  1.00151.02           C  
ANISOU 1951  C   CYS A 284    23210  15842  18331  -2814  -2813    744       C  
ATOM   1952  O   CYS A 284      26.533   7.771  31.031  1.00155.98           O  
ANISOU 1952  O   CYS A 284    23887  16722  18655  -3183  -2772    835       O  
ATOM   1953  CB  CYS A 284      28.011  10.205  31.633  1.00115.97           C  
ANISOU 1953  CB  CYS A 284    18669  12156  13240  -2677  -2659    852       C  
ATOM   1954  SG  CYS A 284      27.492  11.131  30.170  1.00136.32           S  
ANISOU 1954  SG  CYS A 284    21049  15072  15676  -2373  -2308    317       S  
ATOM   1955  N   SER A 285      28.104   7.425  29.454  1.00159.54           N  
ANISOU 1955  N   SER A 285    24247  16558  19813  -2559  -2770    442       N  
ATOM   1956  CA  SER A 285      27.317   6.469  28.673  1.00170.18           C  
ANISOU 1956  CA  SER A 285    25646  17713  21301  -2721  -2724    220       C  
ATOM   1957  C   SER A 285      26.012   7.038  28.121  1.00159.56           C  
ANISOU 1957  C   SER A 285    24215  16898  19511  -2866  -2480    -42       C  
ATOM   1958  O   SER A 285      25.066   6.293  27.864  1.00169.30           O  
ANISOU 1958  O   SER A 285    25500  18093  20732  -3154  -2483   -105       O  
ATOM   1959  CB  SER A 285      27.011   5.226  29.513  1.00193.10           C  
ANISOU 1959  CB  SER A 285    28729  20245  24395  -3104  -2996    590       C  
ATOM   1960  OG  SER A 285      28.205   4.597  29.943  1.00205.71           O  
ANISOU 1960  OG  SER A 285    30389  21283  26487  -2960  -3269    846       O  
ATOM   1961  N   GLU A 286      25.960   8.353  27.945  1.00137.47           N  
ANISOU 1961  N   GLU A 286    21277  14579  16378  -2672  -2290   -180       N  
ATOM   1962  CA  GLU A 286      24.800   8.988  27.333  1.00136.30           C  
ANISOU 1962  CA  GLU A 286    21003  14915  15870  -2747  -2081   -430       C  
ATOM   1963  C   GLU A 286      25.204   9.567  25.992  1.00137.11           C  
ANISOU 1963  C   GLU A 286    21013  15072  16011  -2400  -1923   -819       C  
ATOM   1964  O   GLU A 286      26.288  10.138  25.863  1.00135.94           O  
ANISOU 1964  O   GLU A 286    20837  14847  15967  -2082  -1897   -853       O  
ATOM   1965  CB  GLU A 286      24.216  10.081  28.227  1.00139.00           C  
ANISOU 1965  CB  GLU A 286    21248  15788  15777  -2842  -1983   -276       C  
ATOM   1966  CG  GLU A 286      23.096   9.607  29.138  1.00139.57           C  
ANISOU 1966  CG  GLU A 286    21348  16041  15642  -3300  -2010    -49       C  
ATOM   1967  CD  GLU A 286      23.596   9.195  30.506  1.00146.62           C  
ANISOU 1967  CD  GLU A 286    22409  16756  16546  -3512  -2197    373       C  
ATOM   1968  OE1 GLU A 286      24.592   9.786  30.974  1.00160.77           O  
ANISOU 1968  OE1 GLU A 286    24233  18509  18343  -3301  -2255    494       O  
ATOM   1969  OE2 GLU A 286      22.988   8.291  31.118  1.00139.34           O  
ANISOU 1969  OE2 GLU A 286    21590  15743  15610  -3918  -2303    602       O  
ATOM   1970  N   GLN A 287      24.361   9.391  24.981  1.00140.73           N  
ANISOU 1970  N   GLN A 287    21431  15660  16380  -2489  -1830  -1103       N  
ATOM   1971  CA  GLN A 287      24.691   9.942  23.676  1.00140.97           C  
ANISOU 1971  CA  GLN A 287    21401  15778  16382  -2219  -1687  -1460       C  
ATOM   1972  C   GLN A 287      24.140  11.344  23.434  1.00148.08           C  
ANISOU 1972  C   GLN A 287    22132  17233  16897  -2114  -1558  -1527       C  
ATOM   1973  O   GLN A 287      23.039  11.692  23.873  1.00 84.88           O  
ANISOU 1973  O   GLN A 287    14021   9583   8645  -2310  -1544  -1429       O  
ATOM   1974  CB  GLN A 287      24.232   9.016  22.548  1.00135.82           C  
ANISOU 1974  CB  GLN A 287    20824  14939  15840  -2362  -1675  -1765       C  
ATOM   1975  CG  GLN A 287      22.741   8.839  22.423  1.00144.42           C  
ANISOU 1975  CG  GLN A 287    21855  16332  16686  -2706  -1694  -1783       C  
ATOM   1976  CD  GLN A 287      22.379   8.069  21.176  1.00164.25           C  
ANISOU 1976  CD  GLN A 287    24453  18691  19264  -2838  -1685  -2126       C  
ATOM   1977  OE1 GLN A 287      23.184   7.293  20.659  1.00169.53           O  
ANISOU 1977  OE1 GLN A 287    25273  18905  20237  -2747  -1679  -2317       O  
ATOM   1978  NE2 GLN A 287      21.164   8.276  20.684  1.00176.16           N  
ANISOU 1978  NE2 GLN A 287    25856  20574  20500  -3061  -1686  -2218       N  
ATOM   1979  N   LEU A 288      24.945  12.152  22.756  1.00137.12           N  
ANISOU 1979  N   LEU A 288    20707  15900  15491  -1800  -1462  -1687       N  
ATOM   1980  CA  LEU A 288      24.585  13.533  22.481  1.00140.07           C  
ANISOU 1980  CA  LEU A 288    20937  16730  15554  -1662  -1364  -1735       C  
ATOM   1981  C   LEU A 288      23.446  13.652  21.481  1.00149.35           C  
ANISOU 1981  C   LEU A 288    22030  18192  16524  -1796  -1338  -1936       C  
ATOM   1982  O   LEU A 288      23.373  12.882  20.522  1.00171.42           O  
ANISOU 1982  O   LEU A 288    24912  20823  19396  -1890  -1346  -2159       O  
ATOM   1983  CB  LEU A 288      25.807  14.276  21.952  1.00140.39           C  
ANISOU 1983  CB  LEU A 288    20981  16716  15646  -1329  -1283  -1839       C  
ATOM   1984  CG  LEU A 288      26.922  14.351  22.997  1.00134.03           C  
ANISOU 1984  CG  LEU A 288    20211  15687  15028  -1191  -1338  -1607       C  
ATOM   1985  CD1 LEU A 288      28.197  14.960  22.433  1.00139.07           C  
ANISOU 1985  CD1 LEU A 288    20829  16241  15770   -882  -1256  -1718       C  
ATOM   1986  CD2 LEU A 288      26.438  15.133  24.189  1.00141.07           C  
ANISOU 1986  CD2 LEU A 288    21041  16866  15692  -1263  -1365  -1355       C  
ATOM   1987  N   ALA A 289      22.563  14.617  21.701  1.00130.12           N  
ANISOU 1987  N   ALA A 289    19421  16175  13844  -1810  -1313  -1866       N  
ATOM   1988  CA  ALA A 289      21.397  14.786  20.849  1.00114.29           C  
ANISOU 1988  CA  ALA A 289    17289  14468  11668  -1946  -1335  -2002       C  
ATOM   1989  C   ALA A 289      21.876  15.338  19.511  1.00116.60           C  
ANISOU 1989  C   ALA A 289    17618  14813  11871  -1761  -1309  -2218       C  
ATOM   1990  O   ALA A 289      22.975  15.882  19.407  1.00115.98           O  
ANISOU 1990  O   ALA A 289    17603  14636  11827  -1507  -1241  -2234       O  
ATOM   1991  CB  ALA A 289      20.328  15.687  21.444  1.00103.91           C  
ANISOU 1991  CB  ALA A 289    15733  13565  10183  -1981  -1313  -1873       C  
ATOM   1992  N   CYS A 290      21.057  15.156  18.482  1.00212.25           N  
ANISOU 1992  N   CYS A 290    38833  25913  15898   1614  -2728  -2695       N  
ATOM   1993  CA  CYS A 290      21.349  15.694  17.161  1.00152.37           C  
ANISOU 1993  CA  CYS A 290    30748  18245   8900   1382  -2922  -2836       C  
ATOM   1994  C   CYS A 290      21.150  17.205  17.182  1.00179.89           C  
ANISOU 1994  C   CYS A 290    33987  21777  12585   1390  -3063  -3219       C  
ATOM   1995  O   CYS A 290      20.214  17.699  17.810  1.00154.91           O  
ANISOU 1995  O   CYS A 290    30968  18736   9154   1486  -2747  -3334       O  
ATOM   1996  CB  CYS A 290      20.456  15.046  16.096  1.00148.06           C  
ANISOU 1996  CB  CYS A 290    30071  17667   8519   1083  -2419  -2638       C  
ATOM   1997  SG  CYS A 290      20.995  15.320  14.384  1.00180.38           S  
ANISOU 1997  SG  CYS A 290    33611  21629  13298    805  -2675  -2710       S  
ATOM   1998  N   VAL A 291      22.028  17.937  16.507  1.00175.33           N  
ANISOU 1998  N   VAL A 291    33054  21097  12468   1289  -3519  -3415       N  
ATOM   1999  CA  VAL A 291      21.849  19.377  16.366  1.00199.56           C  
ANISOU 1999  CA  VAL A 291    35921  24121  15780   1254  -3634  -3756       C  
ATOM   2000  C   VAL A 291      20.540  19.639  15.637  1.00217.70           C  
ANISOU 2000  C   VAL A 291    38089  26440  18188   1141  -3131  -3759       C  
ATOM   2001  O   VAL A 291      20.237  18.990  14.643  1.00241.93           O  
ANISOU 2001  O   VAL A 291    40977  29492  21453    943  -2905  -3570       O  
ATOM   2002  CB  VAL A 291      23.028  20.040  15.599  1.00198.79           C  
ANISOU 2002  CB  VAL A 291    35446  23882  16204   1072  -4156  -3926       C  
ATOM   2003  CG1 VAL A 291      23.343  19.288  14.310  1.00190.92           C  
ANISOU 2003  CG1 VAL A 291    34149  22822  15571    838  -4144  -3710       C  
ATOM   2004  CG2 VAL A 291      22.745  21.515  15.323  1.00196.44           C  
ANISOU 2004  CG2 VAL A 291    35004  23455  16181    996  -4206  -4240       C  
ATOM   2005  N   ASP A 292      19.745  20.565  16.156  1.00209.74           N  
ANISOU 2005  N   ASP A 292    37176  25494  17022   1292  -2953  -3987       N  
ATOM   2006  CA  ASP A 292      18.548  20.993  15.452  1.00200.73           C  
ANISOU 2006  CA  ASP A 292    35859  24410  15998   1251  -2535  -4055       C  
ATOM   2007  C   ASP A 292      18.694  22.470  15.151  1.00192.33           C  
ANISOU 2007  C   ASP A 292    34666  23159  15251   1296  -2800  -4376       C  
ATOM   2008  O   ASP A 292      18.818  23.301  16.051  1.00200.21           O  
ANISOU 2008  O   ASP A 292    35870  24121  16079   1488  -2972  -4611       O  
ATOM   2009  CB  ASP A 292      17.284  20.718  16.268  1.00206.43           C  
ANISOU 2009  CB  ASP A 292    36801  25414  16219   1423  -1990  -4032       C  
ATOM   2010  CG  ASP A 292      16.907  19.247  16.290  1.00202.79           C  
ANISOU 2010  CG  ASP A 292    36450  25102  15500   1280  -1593  -3682       C  
ATOM   2011  OD1 ASP A 292      17.382  18.494  15.413  1.00195.66           O  
ANISOU 2011  OD1 ASP A 292    35406  24077  14860   1050  -1670  -3474       O  
ATOM   2012  OD2 ASP A 292      16.130  18.842  17.181  1.00206.94           O  
ANISOU 2012  OD2 ASP A 292    37218  25854  15557   1382  -1185  -3613       O  
ATOM   2013  N   THR A 293      18.686  22.781  13.862  1.00177.97           N  
ANISOU 2013  N   THR A 293    32539  21196  13886   1110  -2827  -4376       N  
ATOM   2014  CA  THR A 293      18.983  24.119  13.390  1.00164.43           C  
ANISOU 2014  CA  THR A 293    30727  19216  12533   1094  -3103  -4624       C  
ATOM   2015  C   THR A 293      17.856  25.085  13.776  1.00160.34           C  
ANISOU 2015  C   THR A 293    30362  18738  11823   1393  -2837  -4861       C  
ATOM   2016  O   THR A 293      16.683  24.709  13.795  1.00155.18           O  
ANISOU 2016  O   THR A 293    29689  18352  10920   1535  -2368  -4813       O  
ATOM   2017  CB  THR A 293      19.219  24.080  11.860  1.00150.32           C  
ANISOU 2017  CB  THR A 293    28593  17274  11246    820  -3156  -4514       C  
ATOM   2018  OG1 THR A 293      20.336  23.232  11.557  1.00135.52           O  
ANISOU 2018  OG1 THR A 293    26568  15380   9544    577  -3428  -4325       O  
ATOM   2019  CG2 THR A 293      19.457  25.446  11.306  1.00150.23           C  
ANISOU 2019  CG2 THR A 293    28536  16950  11596    785  -3386  -4729       C  
ATOM   2020  N   ASN A 294      18.220  26.329  14.077  1.00162.97           N  
ANISOU 2020  N   ASN A 294    30839  18816  12266   1483  -3128  -5128       N  
ATOM   2021  CA  ASN A 294      17.271  27.299  14.620  1.00168.03           C  
ANISOU 2021  CA  ASN A 294    31695  19466  12684   1830  -2933  -5382       C  
ATOM   2022  C   ASN A 294      16.206  27.706  13.611  1.00169.64           C  
ANISOU 2022  C   ASN A 294    31731  19676  13048   1961  -2620  -5407       C  
ATOM   2023  O   ASN A 294      16.515  28.047  12.473  1.00170.40           O  
ANISOU 2023  O   ASN A 294    31658  19522  13566   1788  -2766  -5366       O  
ATOM   2024  CB  ASN A 294      18.014  28.535  15.132  1.00181.57           C  
ANISOU 2024  CB  ASN A 294    33649  20842  14500   1859  -3349  -5663       C  
ATOM   2025  CG  ASN A 294      17.129  29.448  15.966  1.00196.00           C  
ANISOU 2025  CG  ASN A 294    35778  22685  16008   2263  -3178  -5936       C  
ATOM   2026  OD1 ASN A 294      16.207  28.993  16.641  1.00201.76           O  
ANISOU 2026  OD1 ASN A 294    36574  23767  16318   2518  -2804  -5922       O  
ATOM   2027  ND2 ASN A 294      17.406  30.747  15.918  1.00199.38           N  
ANISOU 2027  ND2 ASN A 294    36400  22727  16627   2312  -3433  -6188       N  
ATOM   2028  N   GLU A 295      14.950  27.656  14.044  1.00176.42           N  
ANISOU 2028  N   GLU A 295    32623  20859  13549   2278  -2181  -5480       N  
ATOM   2029  CA  GLU A 295      13.806  27.950  13.182  1.00175.60           C  
ANISOU 2029  CA  GLU A 295    32315  20889  13518   2481  -1843  -5528       C  
ATOM   2030  C   GLU A 295      13.896  29.330  12.538  1.00167.21           C  
ANISOU 2030  C   GLU A 295    31353  19400  12780   2638  -2089  -5719       C  
ATOM   2031  O   GLU A 295      13.746  29.458  11.324  1.00164.99           O  
ANISOU 2031  O   GLU A 295    30873  19007  12807   2582  -2078  -5647       O  
ATOM   2032  CB  GLU A 295      12.501  27.823  13.968  1.00186.60           C  
ANISOU 2032  CB  GLU A 295    33718  22750  14434   2831  -1350  -5641       C  
ATOM   2033  CG  GLU A 295      12.245  26.423  14.502  1.00194.46           C  
ANISOU 2033  CG  GLU A 295    34632  24169  15084   2646  -1007  -5420       C  
ATOM   2034  CD  GLU A 295      12.260  25.369  13.410  1.00191.57           C  
ANISOU 2034  CD  GLU A 295    33950  23908  14931   2304   -866  -5150       C  
ATOM   2035  OE1 GLU A 295      11.753  25.647  12.303  1.00199.54           O  
ANISOU 2035  OE1 GLU A 295    34689  24938  16189   2346   -768  -5185       O  
ATOM   2036  OE2 GLU A 295      12.787  24.263  13.658  1.00185.30           O  
ANISOU 2036  OE2 GLU A 295    33202  23163  14042   2014   -862  -4903       O  
ATOM   2037  N   VAL A 296      14.127  30.359  13.349  1.00164.23           N  
ANISOU 2037  N   VAL A 296    31322  18769  12311   2837  -2302  -5959       N  
ATOM   2038  CA  VAL A 296      14.234  31.723  12.833  1.00163.60           C  
ANISOU 2038  CA  VAL A 296    31443  18211  12506   2982  -2531  -6137       C  
ATOM   2039  C   VAL A 296      15.387  31.799  11.838  1.00174.26           C  
ANISOU 2039  C   VAL A 296    32706  19159  14347   2528  -2894  -5991       C  
ATOM   2040  O   VAL A 296      15.342  32.563  10.876  1.00182.79           O  
ANISOU 2040  O   VAL A 296    33827  19901  15724   2557  -2973  -6006       O  
ATOM   2041  CB  VAL A 296      14.428  32.765  13.963  1.00170.34           C  
ANISOU 2041  CB  VAL A 296    32732  18825  13166   3205  -2727  -6425       C  
ATOM   2042  CG1 VAL A 296      15.726  32.525  14.721  1.00169.95           C  
ANISOU 2042  CG1 VAL A 296    32801  18653  13120   2841  -3102  -6423       C  
ATOM   2043  CG2 VAL A 296      14.392  34.178  13.401  1.00168.79           C  
ANISOU 2043  CG2 VAL A 296    32806  18107  13221   3386  -2904  -6596       C  
ATOM   2044  N   GLU A 297      16.421  31.000  12.079  1.00153.77           N  
ANISOU 2044  N   GLU A 297    29993  16615  11817   2127  -3105  -5846       N  
ATOM   2045  CA  GLU A 297      17.543  30.912  11.159  1.00162.72           C  
ANISOU 2045  CA  GLU A 297    30953  17473  13402   1671  -3414  -5699       C  
ATOM   2046  C   GLU A 297      17.142  30.194   9.865  1.00173.19           C  
ANISOU 2046  C   GLU A 297    31934  18938  14933   1560  -3200  -5459       C  
ATOM   2047  O   GLU A 297      17.575  30.585   8.782  1.00172.92           O  
ANISOU 2047  O   GLU A 297    31814  18603  15284   1346  -3349  -5387       O  
ATOM   2048  CB  GLU A 297      18.729  30.210  11.826  1.00153.17           C  
ANISOU 2048  CB  GLU A 297    29674  16358  12167   1350  -3698  -5632       C  
ATOM   2049  CG  GLU A 297      19.360  30.989  12.980  1.00155.91           C  
ANISOU 2049  CG  GLU A 297    30333  16538  12368   1382  -3999  -5895       C  
ATOM   2050  CD  GLU A 297      19.833  32.375  12.579  1.00160.12           C  
ANISOU 2050  CD  GLU A 297    31057  16563  13220   1258  -4257  -6089       C  
ATOM   2051  OE1 GLU A 297      19.029  33.331  12.651  1.00161.74           O  
ANISOU 2051  OE1 GLU A 297    31554  16565  13336   1586  -4127  -6259       O  
ATOM   2052  OE2 GLU A 297      21.015  32.512  12.201  1.00158.18           O  
ANISOU 2052  OE2 GLU A 297    30677  16124  13301    832  -4580  -6075       O  
ATOM   2053  N   THR A 298      16.306  29.160   9.976  1.00173.98           N  
ANISOU 2053  N   THR A 298    31850  19494  14760   1685  -2835  -5341       N  
ATOM   2054  CA  THR A 298      15.848  28.430   8.793  1.00169.15           C  
ANISOU 2054  CA  THR A 298    30908  19062  14298   1578  -2609  -5144       C  
ATOM   2055  C   THR A 298      15.145  29.337   7.800  1.00175.67           C  
ANISOU 2055  C   THR A 298    31735  19716  15298   1822  -2527  -5232       C  
ATOM   2056  O   THR A 298      15.487  29.360   6.619  1.00179.89           O  
ANISOU 2056  O   THR A 298    32120  20059  16171   1611  -2633  -5105       O  
ATOM   2057  CB  THR A 298      14.846  27.298   9.138  1.00176.69           C  
ANISOU 2057  CB  THR A 298    31698  20560  14876   1694  -2153  -5054       C  
ATOM   2058  OG1 THR A 298      13.712  27.848   9.820  1.00184.99           O  
ANISOU 2058  OG1 THR A 298    32873  21831  15584   2145  -1863  -5268       O  
ATOM   2059  CG2 THR A 298      15.471  26.242   9.995  1.00166.77           C  
ANISOU 2059  CG2 THR A 298    30483  19463  13420   1472  -2193  -4904       C  
ATOM   2060  N   GLN A 299      14.168  30.092   8.291  1.00172.39           N  
ANISOU 2060  N   GLN A 299    31499  19373  14629   2301  -2340  -5448       N  
ATOM   2061  CA  GLN A 299      13.388  30.980   7.441  1.00173.37           C  
ANISOU 2061  CA  GLN A 299    31657  19365  14849   2666  -2253  -5546       C  
ATOM   2062  C   GLN A 299      14.258  32.058   6.805  1.00182.63           C  
ANISOU 2062  C   GLN A 299    33104  19884  16403   2514  -2632  -5553       C  
ATOM   2063  O   GLN A 299      14.079  32.395   5.636  1.00188.49           O  
ANISOU 2063  O   GLN A 299    33807  20445  17366   2566  -2639  -5481       O  
ATOM   2064  CB  GLN A 299      12.242  31.621   8.226  1.00168.34           C  
ANISOU 2064  CB  GLN A 299    31168  18943  13851   3256  -2003  -5795       C  
ATOM   2065  CG  GLN A 299      11.302  32.475   7.374  1.00174.18           C  
ANISOU 2065  CG  GLN A 299    31911  19634  14638   3757  -1890  -5900       C  
ATOM   2066  CD  GLN A 299      10.458  31.660   6.401  1.00175.66           C  
ANISOU 2066  CD  GLN A 299    31609  20328  14806   3834  -1577  -5794       C  
ATOM   2067  OE1 GLN A 299      10.956  31.156   5.393  1.00175.90           O  
ANISOU 2067  OE1 GLN A 299    31465  20266  15103   3482  -1679  -5599       O  
ATOM   2068  NE2 GLN A 299       9.170  31.536   6.700  1.00180.63           N  
ANISOU 2068  NE2 GLN A 299    31982  21534  15114   4288  -1187  -5937       N  
ATOM   2069  N   LYS A 300      15.206  32.592   7.568  1.00177.44           N  
ANISOU 2069  N   LYS A 300    32727  18885  15805   2309  -2936  -5641       N  
ATOM   2070  CA  LYS A 300      16.070  33.649   7.053  1.00184.91           C  
ANISOU 2070  CA  LYS A 300    33945  19212  17098   2088  -3264  -5660       C  
ATOM   2071  C   LYS A 300      16.995  33.140   5.953  1.00190.32           C  
ANISOU 2071  C   LYS A 300    34360  19775  18179   1555  -3418  -5414       C  
ATOM   2072  O   LYS A 300      17.351  33.885   5.039  1.00201.04           O  
ANISOU 2072  O   LYS A 300    35859  20695  19833   1417  -3549  -5359       O  
ATOM   2073  CB  LYS A 300      16.894  34.273   8.181  1.00190.69           C  
ANISOU 2073  CB  LYS A 300    34983  19689  17784   1943  -3543  -5844       C  
ATOM   2074  CG  LYS A 300      17.621  35.543   7.769  1.00199.66           C  
ANISOU 2074  CG  LYS A 300    36463  20176  19223   1744  -3825  -5917       C  
ATOM   2075  CD  LYS A 300      16.666  36.521   7.096  1.00208.44           C  
ANISOU 2075  CD  LYS A 300    37883  20988  20327   2215  -3683  -5965       C  
ATOM   2076  CE  LYS A 300      15.594  37.004   8.063  1.00216.49           C  
ANISOU 2076  CE  LYS A 300    39161  22155  20942   2850  -3509  -6210       C  
ATOM   2077  NZ  LYS A 300      14.534  37.792   7.376  1.00215.42           N  
ANISOU 2077  NZ  LYS A 300    39243  21851  20757   3424  -3344  -6245       N  
ATOM   2078  N   PHE A 301      17.387  31.874   6.046  1.00194.58           N  
ANISOU 2078  N   PHE A 301    34535  20690  18708   1261  -3389  -5256       N  
ATOM   2079  CA  PHE A 301      18.175  31.254   4.991  1.00174.03           C  
ANISOU 2079  CA  PHE A 301    31619  18054  16451    800  -3496  -5020       C  
ATOM   2080  C   PHE A 301      17.304  31.044   3.751  1.00152.05           C  
ANISOU 2080  C   PHE A 301    28681  15368  13723    970  -3258  -4901       C  
ATOM   2081  O   PHE A 301      17.727  31.314   2.626  1.00138.25           O  
ANISOU 2081  O   PHE A 301    26893  13345  12290    741  -3359  -4774       O  
ATOM   2082  CB  PHE A 301      18.762  29.927   5.469  1.00168.28           C  
ANISOU 2082  CB  PHE A 301    30582  17703  15653    524  -3524  -4888       C  
ATOM   2083  CG  PHE A 301      19.812  29.362   4.558  1.00162.40           C  
ANISOU 2083  CG  PHE A 301    29518  16909  15276     38  -3698  -4678       C  
ATOM   2084  CD1 PHE A 301      19.468  28.634   3.429  1.00147.04           C  
ANISOU 2084  CD1 PHE A 301    27295  15120  13451    -47  -3524  -4480       C  
ATOM   2085  CD2 PHE A 301      21.155  29.556   4.840  1.00163.49           C  
ANISOU 2085  CD2 PHE A 301    29605  16887  15627   -330  -4034  -4701       C  
ATOM   2086  CE1 PHE A 301      20.444  28.120   2.597  1.00140.76           C  
ANISOU 2086  CE1 PHE A 301    26199  14295  12987   -477  -3676  -4294       C  
ATOM   2087  CE2 PHE A 301      22.135  29.042   4.011  1.00158.94           C  
ANISOU 2087  CE2 PHE A 301    28686  16324  15382   -753  -4177  -4525       C  
ATOM   2088  CZ  PHE A 301      21.778  28.324   2.889  1.00147.83           C  
ANISOU 2088  CZ  PHE A 301    27024  15048  14097   -819  -3994  -4312       C  
ATOM   2089  N   VAL A 302      16.085  30.559   3.976  1.00154.73           N  
ANISOU 2089  N   VAL A 302    28920  16137  13734   1368  -2930  -4953       N  
ATOM   2090  CA  VAL A 302      15.100  30.380   2.912  1.00160.77           C  
ANISOU 2090  CA  VAL A 302    29366  17153  14565   1598  -2644  -4824       C  
ATOM   2091  C   VAL A 302      14.779  31.695   2.212  1.00169.74           C  
ANISOU 2091  C   VAL A 302    30808  17868  15816   1919  -2719  -4903       C  
ATOM   2092  O   VAL A 302      14.812  31.776   0.987  1.00169.31           O  
ANISOU 2092  O   VAL A 302    30530  17736  16064   1826  -2699  -4681       O  
ATOM   2093  CB  VAL A 302      13.790  29.763   3.451  1.00159.73           C  
ANISOU 2093  CB  VAL A 302    28982  17637  14070   1974  -2236  -4889       C  
ATOM   2094  CG1 VAL A 302      12.710  29.762   2.375  1.00154.65           C  
ANISOU 2094  CG1 VAL A 302    27913  17314  13533   2256  -1956  -4782       C  
ATOM   2095  CG2 VAL A 302      14.039  28.356   3.973  1.00161.84           C  
ANISOU 2095  CG2 VAL A 302    28964  18294  14234   1629  -2103  -4739       C  
ATOM   2096  N   ASP A 303      14.482  32.724   2.997  1.00170.72           N  
ANISOU 2096  N   ASP A 303    31451  17714  15701   2307  -2796  -5193       N  
ATOM   2097  CA  ASP A 303      14.159  34.038   2.452  1.00177.94           C  
ANISOU 2097  CA  ASP A 303    32761  18160  16688   2675  -2868  -5270       C  
ATOM   2098  C   ASP A 303      15.307  34.591   1.615  1.00192.65           C  
ANISOU 2098  C   ASP A 303    34835  19408  18956   2194  -3151  -5109       C  
ATOM   2099  O   ASP A 303      15.081  35.214   0.576  1.00188.96           O  
ANISOU 2099  O   ASP A 303    34547  18632  18616   2362  -3154  -5022       O  
ATOM   2100  CB  ASP A 303      13.811  35.020   3.578  1.00191.19           C  
ANISOU 2100  CB  ASP A 303    34840  19663  18142   3076  -2890  -5517       C  
ATOM   2101  CG  ASP A 303      12.492  34.692   4.255  1.00182.77           C  
ANISOU 2101  CG  ASP A 303    33577  19202  16666   3649  -2556  -5686       C  
ATOM   2102  OD1 ASP A 303      12.021  33.542   4.123  1.00177.51           O  
ANISOU 2102  OD1 ASP A 303    32441  19130  15876   3596  -2311  -5612       O  
ATOM   2103  OD2 ASP A 303      11.928  35.584   4.923  1.00153.63           O  
ANISOU 2103  OD2 ASP A 303    30193  15407  12772   4133  -2524  -5893       O  
ATOM   2104  N   SER A 304      16.535  34.355   2.066  1.00203.30           N  
ANISOU 2104  N   SER A 304    36125  20622  20499   1604  -3370  -5055       N  
ATOM   2105  CA  SER A 304      17.713  34.867   1.375  1.00208.11           C  
ANISOU 2105  CA  SER A 304    36853  20724  21497   1070  -3610  -4916       C  
ATOM   2106  C   SER A 304      17.862  34.279  -0.029  1.00190.88           C  
ANISOU 2106  C   SER A 304    34391  18594  19543    825  -3556  -4666       C  
ATOM   2107  O   SER A 304      18.054  35.014  -0.997  1.00192.60           O  
ANISOU 2107  O   SER A 304    34828  18379  19973    750  -3593  -4537       O  
ATOM   2108  CB  SER A 304      18.973  34.583   2.196  1.00223.05           C  
ANISOU 2108  CB  SER A 304    38595  22636  23518    526  -3839  -4944       C  
ATOM   2109  OG  SER A 304      20.117  35.168   1.598  1.00235.84           O  
ANISOU 2109  OG  SER A 304    40285  23820  25504     -6  -4043  -4848       O  
ATOM   2110  N   LEU A 305      17.768  32.958  -0.140  1.00185.43           N  
ANISOU 2110  N   LEU A 305    33083  18504  18869    691  -3399  -4492       N  
ATOM   2111  CA  LEU A 305      17.896  32.300  -1.439  1.00153.84           C  
ANISOU 2111  CA  LEU A 305    28560  14725  15166    452  -3265  -4142       C  
ATOM   2112  C   LEU A 305      16.721  32.614  -2.368  1.00147.09           C  
ANISOU 2112  C   LEU A 305    27622  13994  14273    946  -3024  -4026       C  
ATOM   2113  O   LEU A 305      16.909  32.842  -3.563  1.00124.43           O  
ANISOU 2113  O   LEU A 305    24675  10965  11639    831  -3009  -3794       O  
ATOM   2114  CB  LEU A 305      18.065  30.784  -1.248  1.00148.56           C  
ANISOU 2114  CB  LEU A 305    27306  14637  14503    208  -3156  -4008       C  
ATOM   2115  CG  LEU A 305      17.024  29.923  -0.521  1.00134.77           C  
ANISOU 2115  CG  LEU A 305    25324  13453  12431    539  -2892  -4077       C  
ATOM   2116  CD1 LEU A 305      15.858  29.526  -1.411  1.00127.58           C  
ANISOU 2116  CD1 LEU A 305    23995  12962  11518    832  -2565  -3929       C  
ATOM   2117  CD2 LEU A 305      17.685  28.675   0.061  1.00127.28           C  
ANISOU 2117  CD2 LEU A 305    24102  12798  11459    184  -2924  -4006       C  
ATOM   2118  N   VAL A 306      15.519  32.662  -1.803  1.00159.99           N  
ANISOU 2118  N   VAL A 306    29275  15931  15581   1518  -2842  -4203       N  
ATOM   2119  CA  VAL A 306      14.311  32.976  -2.559  1.00166.04           C  
ANISOU 2119  CA  VAL A 306    29922  16910  16254   2081  -2637  -4156       C  
ATOM   2120  C   VAL A 306      14.367  34.360  -3.208  1.00185.37           C  
ANISOU 2120  C   VAL A 306    32954  18708  18770   2330  -2779  -4143       C  
ATOM   2121  O   VAL A 306      13.941  34.535  -4.349  1.00193.29           O  
ANISOU 2121  O   VAL A 306    33827  19756  19859   2540  -2696  -3944       O  
ATOM   2122  CB  VAL A 306      13.050  32.880  -1.657  1.00141.05           C  
ANISOU 2122  CB  VAL A 306    26689  14210  12694   2665  -2421  -4416       C  
ATOM   2123  CG1 VAL A 306      11.849  33.544  -2.312  1.00140.65           C  
ANISOU 2123  CG1 VAL A 306    26635  14296  12509   3362  -2286  -4455       C  
ATOM   2124  CG2 VAL A 306      12.744  31.430  -1.316  1.00126.83           C  
ANISOU 2124  CG2 VAL A 306    24258  13110  10821   2443  -2183  -4355       C  
ATOM   2125  N   ALA A 307      14.903  35.338  -2.484  1.00200.46           N  
ANISOU 2125  N   ALA A 307    35545  19996  20624   2300  -2997  -4357       N  
ATOM   2126  CA  ALA A 307      14.989  36.708  -2.990  1.00219.59           C  
ANISOU 2126  CA  ALA A 307    38660  21685  23087   2510  -3128  -4362       C  
ATOM   2127  C   ALA A 307      15.848  36.811  -4.248  1.00226.75           C  
ANISOU 2127  C   ALA A 307    39542  22262  24351   2004  -3188  -4019       C  
ATOM   2128  O   ALA A 307      15.512  37.541  -5.183  1.00230.93           O  
ANISOU 2128  O   ALA A 307    40368  22478  24898   2301  -3156  -3862       O  
ATOM   2129  CB  ALA A 307      15.529  37.627  -1.911  1.00229.93           C  
ANISOU 2129  CB  ALA A 307    40703  22373  24287   2439  -3360  -4685       C  
ATOM   2130  N   LEU A 308      16.961  36.085  -4.261  1.00230.14           N  
ANISOU 2130  N   LEU A 308    39631  22775  25036   1271  -3271  -3905       N  
ATOM   2131  CA  LEU A 308      17.856  36.068  -5.414  1.00228.45           C  
ANISOU 2131  CA  LEU A 308    39307  22338  25157    734  -3296  -3590       C  
ATOM   2132  C   LEU A 308      17.231  35.314  -6.583  1.00217.86           C  
ANISOU 2132  C   LEU A 308    37382  21529  23864    921  -3073  -3292       C  
ATOM   2133  O   LEU A 308      17.635  35.476  -7.735  1.00219.33           O  
ANISOU 2133  O   LEU A 308    37557  21536  24242    696  -3042  -3010       O  
ATOM   2134  CB  LEU A 308      19.201  35.441  -5.049  1.00230.07           C  
ANISOU 2134  CB  LEU A 308    39232  22586  25598    -43  -3450  -3592       C  
ATOM   2135  CG  LEU A 308      20.333  35.702  -6.046  1.00230.59           C  
ANISOU 2135  CG  LEU A 308    39310  22301  26003   -675  -3505  -3346       C  
ATOM   2136  CD1 LEU A 308      20.563  37.198  -6.190  1.00233.16           C  
ANISOU 2136  CD1 LEU A 308    40473  21776  26343   -709  -3607  -3403       C  
ATOM   2137  CD2 LEU A 308      21.611  34.997  -5.622  1.00230.10           C  
ANISOU 2137  CD2 LEU A 308    38862  22417  26150  -1366  -3664  -3392       C  
ATOM   2138  N   ALA A 309      16.242  34.484  -6.274  1.00194.59           N  
ANISOU 2138  N   ALA A 309    33957  19253  20726   1311  -2909  -3367       N  
ATOM   2139  CA  ALA A 309      15.587  33.658  -7.276  1.00170.64           C  
ANISOU 2139  CA  ALA A 309    30314  16804  17719   1463  -2707  -3149       C  
ATOM   2140  C   ALA A 309      14.627  34.446  -8.159  1.00160.99           C  
ANISOU 2140  C   ALA A 309    29309  15505  16356   2098  -2639  -3068       C  
ATOM   2141  O   ALA A 309      14.659  34.315  -9.379  1.00169.38           O  
ANISOU 2141  O   ALA A 309    30181  16643  17533   2048  -2584  -2799       O  
ATOM   2142  CB  ALA A 309      14.849  32.524  -6.598  1.00169.30           C  
ANISOU 2142  CB  ALA A 309    29582  17358  17386   1602  -2540  -3283       C  
ATOM   2143  N   MET A 310      13.786  35.272  -7.545  1.00151.16           N  
ANISOU 2143  N   MET A 310    28480  14117  14837   2734  -2653  -3306       N  
ATOM   2144  CA  MET A 310      12.840  36.102  -8.289  1.00177.74           C  
ANISOU 2144  CA  MET A 310    32114  17397  18021   3460  -2623  -3261       C  
ATOM   2145  C   MET A 310      13.517  37.072  -9.272  1.00186.67           C  
ANISOU 2145  C   MET A 310    33857  17775  19292   3323  -2736  -2997       C  
ATOM   2146  O   MET A 310      12.887  37.539 -10.228  1.00185.27           O  
ANISOU 2146  O   MET A 310    33815  17580  18998   3833  -2706  -2840       O  
ATOM   2147  CB  MET A 310      11.950  36.875  -7.311  1.00189.34           C  
ANISOU 2147  CB  MET A 310    33993  18783  19163   4173  -2635  -3604       C  
ATOM   2148  CG  MET A 310      11.068  35.981  -6.444  1.00187.84           C  
ANISOU 2148  CG  MET A 310    33192  19410  18771   4404  -2457  -3852       C  
ATOM   2149  SD  MET A 310       9.930  34.970  -7.421  1.00193.49           S  
ANISOU 2149  SD  MET A 310    32966  21122  19430   4697  -2227  -3735       S  
ATOM   2150  CE  MET A 310       9.040  34.104  -6.132  1.00136.02           C  
ANISOU 2150  CE  MET A 310    25146  14633  11902   4842  -1993  -4067       C  
ATOM   2151  N   ASP A 311      14.790  37.380  -9.035  1.00185.46           N  
ANISOU 2151  N   ASP A 311    34077  17022  19369   2638  -2863  -2952       N  
ATOM   2152  CA  ASP A 311      15.541  38.243  -9.945  1.00185.22           C  
ANISOU 2152  CA  ASP A 311    34616  16271  19489   2358  -2926  -2687       C  
ATOM   2153  C   ASP A 311      16.455  37.445 -10.874  1.00176.60           C  
ANISOU 2153  C   ASP A 311    33021  15388  18692   1651  -2860  -2372       C  
ATOM   2154  O   ASP A 311      16.891  36.343 -10.541  1.00173.97           O  
ANISOU 2154  O   ASP A 311    32047  15548  18506   1207  -2836  -2409       O  
ATOM   2155  CB  ASP A 311      16.365  39.264  -9.165  1.00195.08           C  
ANISOU 2155  CB  ASP A 311    36662  16663  20797   2025  -3098  -2862       C  
ATOM   2156  CG  ASP A 311      16.493  40.584  -9.899  1.00206.44           C  
ANISOU 2156  CG  ASP A 311    38994  17238  22204   2168  -3132  -2686       C  
ATOM   2157  OD1 ASP A 311      16.556  40.564 -11.148  1.00205.43           O  
ANISOU 2157  OD1 ASP A 311    38806  17110  22138   2128  -3032  -2328       O  
ATOM   2158  OD2 ASP A 311      16.522  41.640  -9.230  1.00211.94           O  
ANISOU 2158  OD2 ASP A 311    40498  17237  22792   2329  -3253  -2905       O  
ATOM   2159  N   ASN A 322      11.765  33.746 -10.501  1.00183.40           N  
ANISOU 2159  N   ASN A 322    31084  19749  18851   3410  -2280  -2855       N  
ATOM   2160  CA  ASN A 322      10.774  34.178 -11.478  1.00189.56           C  
ANISOU 2160  CA  ASN A 322    31819  20760  19445   4085  -2260  -2788       C  
ATOM   2161  C   ASN A 322       9.424  33.507 -11.251  1.00213.32           C  
ANISOU 2161  C   ASN A 322    34152  24668  22232   4553  -2101  -3021       C  
ATOM   2162  O   ASN A 322       9.198  32.885 -10.213  1.00213.05           O  
ANISOU 2162  O   ASN A 322    33819  24977  22151   4408  -1985  -3242       O  
ATOM   2163  CB  ASN A 322      11.271  33.895 -12.898  1.00167.96           C  
ANISOU 2163  CB  ASN A 322    28922  18018  16878   3787  -2267  -2441       C  
ATOM   2164  CG  ASN A 322      12.442  34.776 -13.294  1.00157.27           C  
ANISOU 2164  CG  ASN A 322    28283  15782  15690   3428  -2389  -2198       C  
ATOM   2165  OD1 ASN A 322      12.261  35.824 -13.917  1.00166.43           O  
ANISOU 2165  OD1 ASN A 322    30021  16492  16723   3851  -2460  -2066       O  
ATOM   2166  ND2 ASN A 322      13.650  34.357 -12.933  1.00136.98           N  
ANISOU 2166  ND2 ASN A 322    25684  12968  13393   2645  -2409  -2141       N  
ATOM   2167  N   VAL A 323       8.526  33.649 -12.223  1.00232.59           N  
ANISOU 2167  N   VAL A 323    36354  27504  24515   5109  -2093  -2976       N  
ATOM   2168  CA  VAL A 323       7.212  33.015 -12.160  1.00229.52           C  
ANISOU 2168  CA  VAL A 323    35230  28054  23922   5528  -1944  -3213       C  
ATOM   2169  C   VAL A 323       7.370  31.495 -12.207  1.00218.08           C  
ANISOU 2169  C   VAL A 323    33018  27188  22654   4833  -1776  -3193       C  
ATOM   2170  O   VAL A 323       6.528  30.755 -11.695  1.00226.98           O  
ANISOU 2170  O   VAL A 323    33557  29019  23668   4880  -1592  -3429       O  
ATOM   2171  CB  VAL A 323       6.287  33.502 -13.304  1.00230.62           C  
ANISOU 2171  CB  VAL A 323    35259  28519  23848   6278  -2023  -3169       C  
ATOM   2172  CG1 VAL A 323       6.831  33.080 -14.664  1.00225.61           C  
ANISOU 2172  CG1 VAL A 323    34470  27876  23376   5912  -2077  -2840       C  
ATOM   2173  CG2 VAL A 323       4.861  32.998 -13.104  1.00232.75           C  
ANISOU 2173  CG2 VAL A 323    34756  29798  23879   6768  -1883  -3491       C  
ATOM   2174  N   VAL A 324       8.461  31.038 -12.815  1.00199.57           N  
ANISOU 2174  N   VAL A 324    30710  24537  20582   4184  -1822  -2917       N  
ATOM   2175  CA  VAL A 324       8.787  29.619 -12.852  1.00174.74           C  
ANISOU 2175  CA  VAL A 324    26970  21800  17622   3511  -1683  -2880       C  
ATOM   2176  C   VAL A 324       9.100  29.121 -11.441  1.00168.66           C  
ANISOU 2176  C   VAL A 324    26215  20983  16885   3141  -1583  -3039       C  
ATOM   2177  O   VAL A 324       8.771  27.990 -11.077  1.00160.71           O  
ANISOU 2177  O   VAL A 324    24685  20497  15880   2841  -1397  -3140       O  
ATOM   2178  CB  VAL A 324       9.977  29.335 -13.797  1.00159.29           C  
ANISOU 2178  CB  VAL A 324    25107  19482  15935   2958  -1764  -2556       C  
ATOM   2179  CG1 VAL A 324       9.543  29.485 -15.245  1.00155.07           C  
ANISOU 2179  CG1 VAL A 324    24406  19188  15325   3272  -1811  -2406       C  
ATOM   2180  CG2 VAL A 324      11.150  30.262 -13.492  1.00153.48           C  
ANISOU 2180  CG2 VAL A 324    25107  17874  15334   2744  -1918  -2410       C  
ATOM   2181  N   PHE A 325       9.757  29.973 -10.661  1.00172.12           N  
ANISOU 2181  N   PHE A 325    27296  20770  17331   3147  -1711  -3058       N  
ATOM   2182  CA  PHE A 325      10.062  29.664  -9.275  1.00167.46           C  
ANISOU 2182  CA  PHE A 325    26816  20099  16711   2885  -1659  -3223       C  
ATOM   2183  C   PHE A 325       8.823  29.812  -8.393  1.00168.72           C  
ANISOU 2183  C   PHE A 325    26839  20713  16555   3419  -1502  -3536       C  
ATOM   2184  O   PHE A 325       8.651  29.076  -7.422  1.00161.97           O  
ANISOU 2184  O   PHE A 325    25767  20161  15614   3201  -1336  -3678       O  
ATOM   2185  CB  PHE A 325      11.189  30.553  -8.763  1.00168.51           C  
ANISOU 2185  CB  PHE A 325    27670  19411  16947   2697  -1876  -3178       C  
ATOM   2186  CG  PHE A 325      11.514  30.327  -7.324  1.00167.57           C  
ANISOU 2186  CG  PHE A 325    27714  19205  16751   2489  -1868  -3367       C  
ATOM   2187  CD1 PHE A 325      12.127  29.152  -6.919  1.00155.42           C  
ANISOU 2187  CD1 PHE A 325    25866  17856  15332   1912  -1807  -3309       C  
ATOM   2188  CD2 PHE A 325      11.213  31.286  -6.376  1.00180.76           C  
ANISOU 2188  CD2 PHE A 325    29888  20594  18200   2906  -1931  -3607       C  
ATOM   2189  CE1 PHE A 325      12.425  28.934  -5.598  1.00159.89           C  
ANISOU 2189  CE1 PHE A 325    26615  18355  15780   1761  -1814  -3468       C  
ATOM   2190  CE2 PHE A 325      11.509  31.074  -5.054  1.00186.53           C  
ANISOU 2190  CE2 PHE A 325    30785  21270  18817   2733  -1932  -3788       C  
ATOM   2191  CZ  PHE A 325      12.119  29.895  -4.662  1.00179.62           C  
ANISOU 2191  CZ  PHE A 325    29596  20607  18047   2160  -1878  -3709       C  
ATOM   2192  N   SER A 326       7.973  30.779  -8.729  1.00175.80           N  
ANISOU 2192  N   SER A 326    27886  21656  17256   4142  -1547  -3641       N  
ATOM   2193  CA  SER A 326       6.683  30.940  -8.065  1.00192.61           C  
ANISOU 2193  CA  SER A 326    29780  24337  19067   4742  -1382  -3957       C  
ATOM   2194  C   SER A 326       5.848  29.675  -8.244  1.00199.63           C  
ANISOU 2194  C   SER A 326    29789  26141  19920   4549  -1115  -4039       C  
ATOM   2195  O   SER A 326       5.114  29.271  -7.341  1.00200.42           O  
ANISOU 2195  O   SER A 326    29589  26740  19822   4625   -883  -4280       O  
ATOM   2196  CB  SER A 326       5.936  32.160  -8.614  1.00198.27           C  
ANISOU 2196  CB  SER A 326    30773  24976  19585   5615  -1507  -4031       C  
ATOM   2197  OG  SER A 326       4.579  32.164  -8.205  1.00195.48           O  
ANISOU 2197  OG  SER A 326    29989  25357  18929   6227  -1330  -4344       O  
ATOM   2198  N   GLU A 327       5.966  29.059  -9.418  1.00207.05           N  
ANISOU 2198  N   GLU A 327    30338  27292  21040   4273  -1137  -3846       N  
ATOM   2199  CA  GLU A 327       5.326  27.775  -9.679  1.00200.89           C  
ANISOU 2199  CA  GLU A 327    28762  27296  20272   3949   -901  -3915       C  
ATOM   2200  C   GLU A 327       5.892  26.709  -8.750  1.00187.19           C  
ANISOU 2200  C   GLU A 327    26967  25526  18631   3244   -726  -3895       C  
ATOM   2201  O   GLU A 327       5.149  25.905  -8.192  1.00184.27           O  
ANISOU 2201  O   GLU A 327    26139  25743  18133   3098   -446  -4071       O  
ATOM   2202  CB  GLU A 327       5.506  27.351 -11.142  1.00204.64           C  
ANISOU 2202  CB  GLU A 327    28931  27900  20923   3761   -996  -3709       C  
ATOM   2203  CG  GLU A 327       4.648  28.124 -12.136  1.00206.10           C  
ANISOU 2203  CG  GLU A 327    28986  28382  20940   4490  -1125  -3760       C  
ATOM   2204  CD  GLU A 327       4.691  27.531 -13.534  1.00200.38           C  
ANISOU 2204  CD  GLU A 327    27866  27936  20334   4287  -1187  -3601       C  
ATOM   2205  OE1 GLU A 327       5.602  26.722 -13.817  1.00191.52           O  
ANISOU 2205  OE1 GLU A 327    26724  26588  19458   3602  -1169  -3404       O  
ATOM   2206  OE2 GLU A 327       3.811  27.877 -14.350  1.00204.45           O  
ANISOU 2206  OE2 GLU A 327    28093  28917  20672   4850  -1266  -3689       O  
ATOM   2207  N   PHE A 328       7.210  26.729  -8.569  1.00176.25           N  
ANISOU 2207  N   PHE A 328    26063  23454  17450   2819   -887  -3684       N  
ATOM   2208  CA  PHE A 328       7.891  25.752  -7.726  1.00162.94           C  
ANISOU 2208  CA  PHE A 328    24399  21669  15842   2204   -780  -3635       C  
ATOM   2209  C   PHE A 328       7.467  25.846  -6.262  1.00162.12           C  
ANISOU 2209  C   PHE A 328    24458  21670  15470   2350   -620  -3861       C  
ATOM   2210  O   PHE A 328       7.236  24.823  -5.616  1.00158.21           O  
ANISOU 2210  O   PHE A 328    23706  21513  14893   2003   -371  -3909       O  
ATOM   2211  CB  PHE A 328       9.402  25.926  -7.829  1.00150.57           C  
ANISOU 2211  CB  PHE A 328    23305  19380  14526   1820  -1032  -3400       C  
ATOM   2212  CG  PHE A 328      10.179  24.808  -7.208  1.00146.68           C  
ANISOU 2212  CG  PHE A 328    22780  18823  14129   1218   -966  -3315       C  
ATOM   2213  CD1 PHE A 328       9.659  23.524  -7.163  1.00145.91           C  
ANISOU 2213  CD1 PHE A 328    22207  19236  13996    918   -699  -3337       C  
ATOM   2214  CD2 PHE A 328      11.417  25.041  -6.647  1.00146.75           C  
ANISOU 2214  CD2 PHE A 328    23250  18262  14245    960  -1176  -3227       C  
ATOM   2215  CE1 PHE A 328      10.371  22.491  -6.585  1.00137.35           C  
ANISOU 2215  CE1 PHE A 328    21176  18042  12970    419   -641  -3241       C  
ATOM   2216  CE2 PHE A 328      12.134  24.013  -6.068  1.00144.21           C  
ANISOU 2216  CE2 PHE A 328    22912  17903  13978    490  -1144  -3151       C  
ATOM   2217  CZ  PHE A 328      11.609  22.735  -6.037  1.00134.65           C  
ANISOU 2217  CZ  PHE A 328    21292  17154  12716    245   -875  -3143       C  
ATOM   2218  N   GLN A 329       7.381  27.067  -5.739  1.00165.95           N  
ANISOU 2218  N   GLN A 329    25417  21837  15798   2859   -753  -3995       N  
ATOM   2219  CA  GLN A 329       6.941  27.281  -4.362  1.00178.40           C  
ANISOU 2219  CA  GLN A 329    27188  23520  17074   3084   -608  -4238       C  
ATOM   2220  C   GLN A 329       5.554  26.691  -4.154  1.00192.34           C  
ANISOU 2220  C   GLN A 329    28323  26152  18604   3261   -241  -4449       C  
ATOM   2221  O   GLN A 329       5.313  25.947  -3.200  1.00193.74           O  
ANISOU 2221  O   GLN A 329    28377  26621  18614   2999     26  -4534       O  
ATOM   2222  CB  GLN A 329       6.928  28.771  -4.013  1.00183.31           C  
ANISOU 2222  CB  GLN A 329    28414  23683  17553   3697   -815  -4387       C  
ATOM   2223  CG  GLN A 329       8.290  29.442  -3.923  1.00171.04           C  
ANISOU 2223  CG  GLN A 329    27550  21252  16187   3468  -1150  -4249       C  
ATOM   2224  CD  GLN A 329       8.177  30.951  -3.800  1.00171.17           C  
ANISOU 2224  CD  GLN A 329    28184  20775  16076   4079  -1346  -4394       C  
ATOM   2225  OE1 GLN A 329       7.258  31.560  -4.346  1.00163.30           O  
ANISOU 2225  OE1 GLN A 329    27097  19995  14954   4696  -1315  -4482       O  
ATOM   2226  NE2 GLN A 329       9.081  31.555  -3.039  1.00183.81           N  
ANISOU 2226  NE2 GLN A 329    30431  21726  17684   3935  -1554  -4447       N  
ATOM   2227  N   ASP A 330       4.649  27.040  -5.061  1.00207.27           N  
ANISOU 2227  N   ASP A 330    29819  28468  20466   3706   -228  -4533       N  
ATOM   2228  CA  ASP A 330       3.283  26.541  -5.037  1.00205.81           C  
ANISOU 2228  CA  ASP A 330    28924  29198  20078   3884     99  -4767       C  
ATOM   2229  C   ASP A 330       3.279  25.029  -5.231  1.00198.40           C  
ANISOU 2229  C   ASP A 330    27465  28646  19272   3130    345  -4666       C  
ATOM   2230  O   ASP A 330       2.508  24.314  -4.595  1.00197.78           O  
ANISOU 2230  O   ASP A 330    26985  29152  19011   2947    705  -4831       O  
ATOM   2231  CB  ASP A 330       2.439  27.222  -6.115  1.00210.90           C  
ANISOU 2231  CB  ASP A 330    29243  30209  20682   4526    -16  -4865       C  
ATOM   2232  CG  ASP A 330       2.409  28.733  -5.971  1.00213.97           C  
ANISOU 2232  CG  ASP A 330    30225  30153  20919   5324   -257  -4956       C  
ATOM   2233  OD1 ASP A 330       2.649  29.238  -4.853  1.00213.13           O  
ANISOU 2233  OD1 ASP A 330    30625  29696  20658   5467   -245  -5067       O  
ATOM   2234  OD2 ASP A 330       2.143  29.418  -6.982  1.00214.80           O  
ANISOU 2234  OD2 ASP A 330    30332  30242  21040   5824   -463  -4919       O  
ATOM   2235  N   TRP A 331       4.148  24.555  -6.120  1.00190.62           N  
ANISOU 2235  N   TRP A 331    26517  27315  18593   2689    165  -4398       N  
ATOM   2236  CA  TRP A 331       4.216  23.139  -6.469  1.00179.33           C  
ANISOU 2236  CA  TRP A 331    24661  26163  17312   2000    357  -4296       C  
ATOM   2237  C   TRP A 331       4.582  22.243  -5.296  1.00163.59           C  
ANISOU 2237  C   TRP A 331    22854  24062  15240   1480    591  -4255       C  
ATOM   2238  O   TRP A 331       3.952  21.211  -5.071  1.00154.93           O  
ANISOU 2238  O   TRP A 331    21343  23460  14063   1099    933  -4331       O  
ATOM   2239  CB  TRP A 331       5.248  22.923  -7.581  1.00173.60           C  
ANISOU 2239  CB  TRP A 331    24059  24987  16914   1694     87  -4013       C  
ATOM   2240  CG  TRP A 331       5.307  21.515  -8.078  1.00176.19           C  
ANISOU 2240  CG  TRP A 331    23981  25570  17395   1055    256  -3928       C  
ATOM   2241  CD1 TRP A 331       4.560  20.960  -9.079  1.00184.26           C  
ANISOU 2241  CD1 TRP A 331    24394  27157  18460    966    349  -4013       C  
ATOM   2242  CD2 TRP A 331       6.116  20.463  -7.558  1.00169.91           C  
ANISOU 2242  CD2 TRP A 331    23383  24477  16698    436    352  -3769       C  
ATOM   2243  NE1 TRP A 331       4.883  19.634  -9.232  1.00186.70           N  
ANISOU 2243  NE1 TRP A 331    24545  27484  18908    295    503  -3919       N  
ATOM   2244  CE2 TRP A 331       5.844  19.299  -8.294  1.00174.98           C  
ANISOU 2244  CE2 TRP A 331    23570  25458  17455    -18    512  -3755       C  
ATOM   2245  CE3 TRP A 331       7.070  20.387  -6.531  1.00162.63           C  
ANISOU 2245  CE3 TRP A 331    23005  23027  15761    244    297  -3647       C  
ATOM   2246  CZ2 TRP A 331       6.466  18.083  -8.057  1.00168.27           C  
ANISOU 2246  CZ2 TRP A 331    22831  24398  16705   -622    634  -3611       C  
ATOM   2247  CZ3 TRP A 331       7.692  19.183  -6.289  1.00159.07           C  
ANISOU 2247  CZ3 TRP A 331    22629  22413  15395   -322    400  -3496       C  
ATOM   2248  CH2 TRP A 331       7.390  18.047  -7.047  1.00159.15           C  
ANISOU 2248  CH2 TRP A 331    22223  22724  15520   -738    574  -3471       C  
ATOM   2249  N   LEU A 332       5.593  22.652  -4.541  1.00156.36           N  
ANISOU 2249  N   LEU A 332    22582  22499  14327   1463    405  -4142       N  
ATOM   2250  CA  LEU A 332       6.116  21.826  -3.465  1.00149.48           C  
ANISOU 2250  CA  LEU A 332    21981  21449  13366   1011    556  -4063       C  
ATOM   2251  C   LEU A 332       5.071  21.695  -2.346  1.00156.33           C  
ANISOU 2251  C   LEU A 332    22716  22825  13859   1142    941  -4296       C  
ATOM   2252  O   LEU A 332       4.874  20.610  -1.796  1.00154.85           O  
ANISOU 2252  O   LEU A 332    22414  22862  13559    685   1260  -4262       O  
ATOM   2253  CB  LEU A 332       7.438  22.426  -2.952  1.00142.68           C  
ANISOU 2253  CB  LEU A 332    21808  19829  12576   1027    210  -3932       C  
ATOM   2254  CG  LEU A 332       8.369  21.730  -1.939  1.00134.21           C  
ANISOU 2254  CG  LEU A 332    21144  18411  11440    625    200  -3805       C  
ATOM   2255  CD1 LEU A 332       9.819  22.087  -2.237  1.00118.72           C  
ANISOU 2255  CD1 LEU A 332    19578  15790   9742    495   -220  -3624       C  
ATOM   2256  CD2 LEU A 332       8.051  22.000  -0.469  1.00142.76           C  
ANISOU 2256  CD2 LEU A 332    22559  19549  12134    830    349  -3975       C  
ATOM   2257  N   GLU A 333       4.391  22.795  -2.030  1.00162.61           N  
ANISOU 2257  N   GLU A 333    23543  23798  14443   1775    928  -4531       N  
ATOM   2258  CA  GLU A 333       3.366  22.793  -0.988  1.00168.10           C  
ANISOU 2258  CA  GLU A 333    24086  25030  14756   1978   1305  -4784       C  
ATOM   2259  C   GLU A 333       2.255  21.799  -1.318  1.00179.97           C  
ANISOU 2259  C   GLU A 333    24825  27345  16212   1662   1729  -4887       C  
ATOM   2260  O   GLU A 333       1.774  21.086  -0.435  1.00188.75           O  
ANISOU 2260  O   GLU A 333    25834  28804  17080   1363   2136  -4953       O  
ATOM   2261  CB  GLU A 333       2.791  24.198  -0.783  1.00168.75           C  
ANISOU 2261  CB  GLU A 333    24293  25187  14638   2802   1192  -5043       C  
ATOM   2262  CG  GLU A 333       3.606  25.078   0.171  1.00172.34           C  
ANISOU 2262  CG  GLU A 333    25553  24968  14960   3067    945  -5059       C  
ATOM   2263  CD  GLU A 333       3.569  24.588   1.616  1.00178.64           C  
ANISOU 2263  CD  GLU A 333    26592  25867  15416   2870   1232  -5127       C  
ATOM   2264  OE1 GLU A 333       4.269  23.599   1.933  1.00174.05           O  
ANISOU 2264  OE1 GLU A 333    26158  25077  14894   2264   1283  -4907       O  
ATOM   2265  OE2 GLU A 333       2.850  25.202   2.436  1.00184.03           O  
ANISOU 2265  OE2 GLU A 333    27348  26831  15744   3358   1405  -5398       O  
ATOM   2266  N   LYS A 334       1.839  21.776  -2.581  1.00184.48           N  
ANISOU 2266  N   LYS A 334    24877  28225  16994   1719   1639  -4912       N  
ATOM   2267  CA  LYS A 334       0.838  20.830  -3.048  1.00190.77           C  
ANISOU 2267  CA  LYS A 334    24905  29791  17787   1362   1986  -5038       C  
ATOM   2268  C   LYS A 334       1.357  19.401  -2.891  1.00190.88           C  
ANISOU 2268  C   LYS A 334    24992  29618  17915    501   2192  -4821       C  
ATOM   2269  O   LYS A 334       0.645  18.523  -2.414  1.00197.59           O  
ANISOU 2269  O   LYS A 334    25519  30951  18605     78   2636  -4917       O  
ATOM   2270  CB  LYS A 334       0.460  21.118  -4.509  1.00191.78           C  
ANISOU 2270  CB  LYS A 334    24537  30210  18120   1611   1757  -5094       C  
ATOM   2271  CG  LYS A 334      -0.057  22.527  -4.752  1.00191.92           C  
ANISOU 2271  CG  LYS A 334    24537  30375  18008   2528   1532  -5285       C  
ATOM   2272  CD  LYS A 334      -0.368  22.753  -6.231  1.00185.56           C  
ANISOU 2272  CD  LYS A 334    23299  29833  17372   2780   1284  -5301       C  
ATOM   2273  CE  LYS A 334      -1.630  22.018  -6.661  1.00185.22           C  
ANISOU 2273  CE  LYS A 334    22313  30813  17251   2607   1581  -5572       C  
ATOM   2274  NZ  LYS A 334      -2.839  22.510  -5.939  1.00193.56           N  
ANISOU 2274  NZ  LYS A 334    22965  32614  17967   3127   1844  -5935       N  
ATOM   2275  N   HIS A 335       2.594  19.168  -3.315  1.00187.80           N  
ANISOU 2275  N   HIS A 335    25034  28528  17794    247   1879  -4532       N  
ATOM   2276  CA  HIS A 335       3.123  17.806  -3.377  1.00188.28           C  
ANISOU 2276  CA  HIS A 335    25166  28382  17991   -496   2020  -4323       C  
ATOM   2277  C   HIS A 335       3.792  17.318  -2.086  1.00197.18           C  
ANISOU 2277  C   HIS A 335    26903  29080  18935   -770   2148  -4163       C  
ATOM   2278  O   HIS A 335       4.351  16.220  -2.059  1.00194.88           O  
ANISOU 2278  O   HIS A 335    26799  28516  18731  -1317   2231  -3961       O  
ATOM   2279  CB  HIS A 335       4.116  17.689  -4.540  1.00180.81           C  
ANISOU 2279  CB  HIS A 335    24323  26965  17411   -624   1639  -4104       C  
ATOM   2280  CG  HIS A 335       3.472  17.723  -5.892  1.00181.53           C  
ANISOU 2280  CG  HIS A 335    23799  27509  17664   -544   1575  -4221       C  
ATOM   2281  ND1 HIS A 335       2.808  18.827  -6.374  1.00189.67           N  
ANISOU 2281  ND1 HIS A 335    24554  28875  18636     89   1426  -4405       N  
ATOM   2282  CD2 HIS A 335       3.396  16.780  -6.860  1.00176.40           C  
ANISOU 2282  CD2 HIS A 335    22788  27029  17205   -992   1625  -4191       C  
ATOM   2283  CE1 HIS A 335       2.351  18.568  -7.588  1.00188.97           C  
ANISOU 2283  CE1 HIS A 335    23940  29177  18684     40   1372  -4476       C  
ATOM   2284  NE2 HIS A 335       2.695  17.330  -7.904  1.00182.13           N  
ANISOU 2284  NE2 HIS A 335    23004  28223  17975   -632   1493  -4360       N  
ATOM   2285  N   GLY A 336       3.717  18.114  -1.021  1.00208.42           N  
ANISOU 2285  N   GLY A 336    28660  30452  20077   -363   2160  -4262       N  
ATOM   2286  CA  GLY A 336       4.400  17.781   0.218  1.00214.56           C  
ANISOU 2286  CA  GLY A 336    30065  30822  20637   -532   2218  -4120       C  
ATOM   2287  C   GLY A 336       3.923  16.490   0.856  1.00223.44           C  
ANISOU 2287  C   GLY A 336    31138  32209  21549  -1106   2722  -4064       C  
ATOM   2288  O   GLY A 336       2.758  16.114   0.715  1.00238.98           O  
ANISOU 2288  O   GLY A 336    32550  34831  23421  -1282   3129  -4241       O  
ATOM   2289  N   ASP A 337       4.808  15.824   1.593  1.00201.33           N  
ANISOU 2289  N   ASP A 337    28932  28914  18650  -1393   2705  -3825       N  
ATOM   2290  CA  ASP A 337       6.154  16.315   1.854  1.00179.77           C  
ANISOU 2290  CA  ASP A 337    26799  25505  16000  -1167   2218  -3668       C  
ATOM   2291  C   ASP A 337       7.203  15.225   1.611  1.00162.22           C  
ANISOU 2291  C   ASP A 337    24876  22800  13960  -1618   2088  -3369       C  
ATOM   2292  O   ASP A 337       6.916  14.034   1.749  1.00154.45           O  
ANISOU 2292  O   ASP A 337    23888  21905  12890  -2094   2442  -3258       O  
ATOM   2293  CB  ASP A 337       6.243  16.843   3.283  1.00195.85           C  
ANISOU 2293  CB  ASP A 337    29346  27449  17617   -864   2254  -3737       C  
ATOM   2294  CG  ASP A 337       5.120  17.808   3.615  1.00199.96           C  
ANISOU 2294  CG  ASP A 337    29584  28491  17902   -401   2452  -4054       C  
ATOM   2295  OD1 ASP A 337       4.025  17.345   3.994  1.00200.64           O  
ANISOU 2295  OD1 ASP A 337    29348  29150  17735   -561   2964  -4171       O  
ATOM   2296  OD2 ASP A 337       5.331  19.033   3.490  1.00194.52           O  
ANISOU 2296  OD2 ASP A 337    28998  27636  17273    123   2107  -4195       O  
ATOM   2297  N   TYR A 338       8.422  15.633   1.271  1.00159.06           N  
ANISOU 2297  N   TYR A 338    24751  21885  13798  -1466   1593  -3248       N  
ATOM   2298  CA  TYR A 338       9.486  14.671   0.989  1.00157.33           C  
ANISOU 2298  CA  TYR A 338    24783  21236  13761  -1801   1426  -2988       C  
ATOM   2299  C   TYR A 338      10.507  14.586   2.110  1.00155.55           C  
ANISOU 2299  C   TYR A 338    25212  20583  13307  -1713   1215  -2856       C  
ATOM   2300  O   TYR A 338      11.036  15.596   2.576  1.00162.30           O  
ANISOU 2300  O   TYR A 338    26314  21248  14104  -1354    887  -2943       O  
ATOM   2301  CB  TYR A 338      10.212  15.018  -0.316  1.00158.30           C  
ANISOU 2301  CB  TYR A 338    24675  21141  14330  -1753   1033  -2934       C  
ATOM   2302  CG  TYR A 338       9.361  14.962  -1.561  1.00164.31           C  
ANISOU 2302  CG  TYR A 338    24817  22293  15321  -1849   1179  -3033       C  
ATOM   2303  CD1 TYR A 338       8.471  15.982  -1.869  1.00169.10           C  
ANISOU 2303  CD1 TYR A 338    25066  23275  15909  -1497   1205  -3255       C  
ATOM   2304  CD2 TYR A 338       9.463  13.891  -2.439  1.00159.67           C  
ANISOU 2304  CD2 TYR A 338    24022  21698  14949  -2254   1267  -2921       C  
ATOM   2305  CE1 TYR A 338       7.698  15.928  -3.012  1.00170.38           C  
ANISOU 2305  CE1 TYR A 338    24650  23838  16247  -1541   1300  -3357       C  
ATOM   2306  CE2 TYR A 338       8.700  13.830  -3.580  1.00162.68           C  
ANISOU 2306  CE2 TYR A 338    23837  22461  15513  -2341   1370  -3038       C  
ATOM   2307  CZ  TYR A 338       7.818  14.850  -3.863  1.00170.79           C  
ANISOU 2307  CZ  TYR A 338    24485  23901  16505  -1981   1377  -3254       C  
ATOM   2308  OH  TYR A 338       7.053  14.792  -5.004  1.00176.75           O  
ANISOU 2308  OH  TYR A 338    24662  25085  17411  -2023   1445  -3383       O  
ATOM   2309  N   GLU A 339      10.766  13.354   2.534  1.00139.85           N  
ANISOU 2309  N   GLU A 339    23524  18440  11173  -2042   1400  -2656       N  
ATOM   2310  CA  GLU A 339      11.733  13.060   3.581  1.00136.90           C  
ANISOU 2310  CA  GLU A 339    23786  17689  10540  -1957   1205  -2504       C  
ATOM   2311  C   GLU A 339      13.179  13.306   3.149  1.00129.59           C  
ANISOU 2311  C   GLU A 339    22989  16347   9905  -1819    635  -2414       C  
ATOM   2312  O   GLU A 339      14.024  13.639   3.973  1.00128.79           O  
ANISOU 2312  O   GLU A 339    23302  16007   9625  -1593    321  -2402       O  
ATOM   2313  CB  GLU A 339      11.576  11.616   4.064  1.00137.81           C  
ANISOU 2313  CB  GLU A 339    24229  17725  10408  -2329   1577  -2288       C  
ATOM   2314  CG  GLU A 339      10.293  11.328   4.827  1.00151.30           C  
ANISOU 2314  CG  GLU A 339    25947  19817  11723  -2505   2168  -2354       C  
ATOM   2315  CD  GLU A 339      10.460  11.537   6.316  1.00168.22           C  
ANISOU 2315  CD  GLU A 339    28683  21887  13345  -2261   2195  -2328       C  
ATOM   2316  OE1 GLU A 339      11.499  11.104   6.851  1.00174.36           O  
ANISOU 2316  OE1 GLU A 339    30012  22256  13982  -2176   1924  -2135       O  
ATOM   2317  OE2 GLU A 339       9.549  12.106   6.956  1.00176.55           O  
ANISOU 2317  OE2 GLU A 339    29654  23321  14107  -2130   2487  -2510       O  
ATOM   2318  N   ALA A 340      13.474  13.115   1.868  1.00124.22           N  
ANISOU 2318  N   ALA A 340    21937  15612   9650  -1967    509  -2364       N  
ATOM   2319  CA  ALA A 340      14.811  13.403   1.356  1.00124.27           C  
ANISOU 2319  CA  ALA A 340    21972  15295   9952  -1860      7  -2299       C  
ATOM   2320  C   ALA A 340      14.744  14.021  -0.035  1.00118.41           C  
ANISOU 2320  C   ALA A 340    20716  14640   9636  -1865   -116  -2370       C  
ATOM   2321  O   ALA A 340      13.743  13.879  -0.732  1.00129.31           O  
ANISOU 2321  O   ALA A 340    21714  16315  11103  -1995    178  -2431       O  
ATOM   2322  CB  ALA A 340      15.652  12.145   1.335  1.00128.43           C  
ANISOU 2322  CB  ALA A 340    22749  15555  10492  -2035    -53  -2073       C  
ATOM   2323  N   ILE A 341      15.817  14.697  -0.439  1.00108.65           N  
ANISOU 2323  N   ILE A 341    19469  13168   8646  -1736   -549  -2367       N  
ATOM   2324  CA  ILE A 341      15.874  15.314  -1.761  1.00115.57           C  
ANISOU 2324  CA  ILE A 341    19933  14079   9899  -1736   -676  -2399       C  
ATOM   2325  C   ILE A 341      17.253  15.139  -2.402  1.00118.39           C  
ANISOU 2325  C   ILE A 341    20260  14175  10548  -1815  -1024  -2275       C  
ATOM   2326  O   ILE A 341      18.276  15.236  -1.724  1.00110.43           O  
ANISOU 2326  O   ILE A 341    19529  12950   9480  -1742  -1320  -2256       O  
ATOM   2327  CB  ILE A 341      15.501  16.817  -1.667  1.00 97.39           C  
ANISOU 2327  CB  ILE A 341    17613  11808   7585  -1446   -796  -2584       C  
ATOM   2328  CG1 ILE A 341      13.980  16.978  -1.687  1.00 99.24           C  
ANISOU 2328  CG1 ILE A 341    17615  12435   7658  -1354   -418  -2719       C  
ATOM   2329  CG2 ILE A 341      16.125  17.623  -2.792  1.00 95.09           C  
ANISOU 2329  CG2 ILE A 341    17116  11361   7652  -1415  -1079  -2568       C  
ATOM   2330  CD1 ILE A 341      13.472  18.100  -0.836  1.00102.18           C  
ANISOU 2330  CD1 ILE A 341    18189  12852   7784  -1007   -432  -2919       C  
ATOM   2331  N   VAL A 342      17.272  14.878  -3.710  1.00122.02           N  
ANISOU 2331  N   VAL A 342    20357  14701  11306  -1955   -988  -2211       N  
ATOM   2332  CA  VAL A 342      18.512  14.552  -4.411  1.00107.56           C  
ANISOU 2332  CA  VAL A 342    18438  12690   9739  -2045  -1246  -2094       C  
ATOM   2333  C   VAL A 342      18.897  15.597  -5.448  1.00105.73           C  
ANISOU 2333  C   VAL A 342    17945  12424   9804  -2009  -1444  -2116       C  
ATOM   2334  O   VAL A 342      18.049  16.111  -6.179  1.00 87.32           O  
ANISOU 2334  O   VAL A 342    15383  10254   7539  -1967  -1303  -2166       O  
ATOM   2335  CB  VAL A 342      18.421  13.183  -5.128  1.00102.23           C  
ANISOU 2335  CB  VAL A 342    17620  12075   9149  -2260  -1039  -1978       C  
ATOM   2336  CG1 VAL A 342      19.813  12.614  -5.379  1.00 87.31           C  
ANISOU 2336  CG1 VAL A 342    15776   9988   7412  -2275  -1302  -1864       C  
ATOM   2337  CG2 VAL A 342      17.567  12.204  -4.330  1.00 95.62           C  
ANISOU 2337  CG2 VAL A 342    17011  11306   8014  -2371   -698  -1962       C  
ATOM   2338  N   ASP A 343      20.193  15.881  -5.517  1.00118.29           N  
ANISOU 2338  N   ASP A 343    19570  13822  11554  -2027  -1768  -2077       N  
ATOM   2339  CA  ASP A 343      20.740  16.764  -6.536  1.00113.22           C  
ANISOU 2339  CA  ASP A 343    18710  13111  11197  -2068  -1935  -2061       C  
ATOM   2340  C   ASP A 343      20.990  15.949  -7.795  1.00102.45           C  
ANISOU 2340  C   ASP A 343    17024  11857  10046  -2214  -1839  -1938       C  
ATOM   2341  O   ASP A 343      22.001  15.254  -7.905  1.00103.43           O  
ANISOU 2341  O   ASP A 343    17101  11934  10263  -2290  -1965  -1867       O  
ATOM   2342  CB  ASP A 343      22.024  17.446  -6.043  1.00111.55           C  
ANISOU 2342  CB  ASP A 343    18635  12686  11062  -2089  -2302  -2104       C  
ATOM   2343  CG  ASP A 343      22.702  18.280  -7.119  1.00115.23           C  
ANISOU 2343  CG  ASP A 343    18889  13065  11827  -2217  -2437  -2065       C  
ATOM   2344  OD1 ASP A 343      22.067  18.578  -8.150  1.00130.63           O  
ANISOU 2344  OD1 ASP A 343    20669  15084  13880  -2213  -2266  -2008       O  
ATOM   2345  OD2 ASP A 343      23.869  18.669  -6.920  1.00109.37           O  
ANISOU 2345  OD2 ASP A 343    18155  12202  11201  -2327  -2713  -2097       O  
ATOM   2346  N   GLY A 344      20.047  16.025  -8.728  1.00 93.57           N  
ANISOU 2346  N   GLY A 344    15676  10907   8970  -2216  -1623  -1935       N  
ATOM   2347  CA  GLY A 344      20.094  15.217  -9.929  1.00102.27           C  
ANISOU 2347  CA  GLY A 344    16490  12146  10224  -2343  -1504  -1852       C  
ATOM   2348  C   GLY A 344      21.384  15.318 -10.716  1.00 98.62           C  
ANISOU 2348  C   GLY A 344    15879  11592  10002  -2428  -1698  -1758       C  
ATOM   2349  O   GLY A 344      21.977  14.301 -11.074  1.00 79.74           O  
ANISOU 2349  O   GLY A 344    13390   9229   7680  -2508  -1687  -1700       O  
ATOM   2350  N   ALA A 345      21.839  16.545 -10.946  1.00 99.34           N  
ANISOU 2350  N   ALA A 345    15977  11564  10206  -2414  -1865  -1751       N  
ATOM   2351  CA  ALA A 345      23.041  16.781 -11.742  1.00112.86           C  
ANISOU 2351  CA  ALA A 345    17514  13224  12145  -2546  -2010  -1665       C  
ATOM   2352  C   ALA A 345      24.247  16.071 -11.141  1.00120.44           C  
ANISOU 2352  C   ALA A 345    18473  14148  13141  -2603  -2192  -1669       C  
ATOM   2353  O   ALA A 345      24.947  15.326 -11.826  1.00109.58           O  
ANISOU 2353  O   ALA A 345    16876  12874  11884  -2661  -2186  -1607       O  
ATOM   2354  CB  ALA A 345      23.313  18.279 -11.864  1.00127.13           C  
ANISOU 2354  CB  ALA A 345    19425  14842  14036  -2574  -2146  -1666       C  
ATOM   2355  N   ASN A 346      24.458  16.291  -9.848  1.00133.56           N  
ANISOU 2355  N   ASN A 346    20389  15686  14669  -2542  -2361  -1757       N  
ATOM   2356  CA  ASN A 346      25.610  15.762  -9.127  1.00130.10           C  
ANISOU 2356  CA  ASN A 346    19976  15234  14220  -2531  -2598  -1785       C  
ATOM   2357  C   ASN A 346      25.792  14.248  -9.261  1.00109.31           C  
ANISOU 2357  C   ASN A 346    17292  12704  11539  -2454  -2507  -1718       C  
ATOM   2358  O   ASN A 346      26.902  13.769  -9.490  1.00104.31           O  
ANISOU 2358  O   ASN A 346    16481  12141  11011  -2442  -2658  -1701       O  
ATOM   2359  CB  ASN A 346      25.506  16.146  -7.651  1.00143.06           C  
ANISOU 2359  CB  ASN A 346    21966  16752  15638  -2426  -2761  -1902       C  
ATOM   2360  CG  ASN A 346      26.680  15.656  -6.842  1.00154.65           C  
ANISOU 2360  CG  ASN A 346    23471  18240  17048  -2363  -3054  -1949       C  
ATOM   2361  OD1 ASN A 346      26.524  14.832  -5.943  1.00183.72           O  
ANISOU 2361  OD1 ASN A 346    27404  21915  20486  -2194  -3059  -1946       O  
ATOM   2362  ND2 ASN A 346      27.870  16.145  -7.168  1.00137.93           N  
ANISOU 2362  ND2 ASN A 346    21099  16170  15139  -2497  -3294  -1995       N  
ATOM   2363  N   ILE A 347      24.699  13.507  -9.113  1.00102.60           N  
ANISOU 2363  N   ILE A 347    16601  11860  10521  -2402  -2254  -1694       N  
ATOM   2364  CA  ILE A 347      24.725  12.048  -9.185  1.00108.26           C  
ANISOU 2364  CA  ILE A 347    17383  12589  11163  -2353  -2131  -1634       C  
ATOM   2365  C   ILE A 347      25.198  11.521 -10.534  1.00 95.65           C  
ANISOU 2365  C   ILE A 347    15467  11100   9777  -2410  -2067  -1582       C  
ATOM   2366  O   ILE A 347      26.151  10.743 -10.617  1.00 82.23           O  
ANISOU 2366  O   ILE A 347    13725   9405   8114  -2311  -2180  -1558       O  
ATOM   2367  CB  ILE A 347      23.329  11.459  -8.904  1.00102.87           C  
ANISOU 2367  CB  ILE A 347    16905  11900  10282  -2394  -1813  -1635       C  
ATOM   2368  CG1 ILE A 347      22.664  12.160  -7.711  1.00109.26           C  
ANISOU 2368  CG1 ILE A 347    17981  12663  10871  -2337  -1812  -1702       C  
ATOM   2369  CG2 ILE A 347      23.429   9.942  -8.696  1.00 83.32           C  
ANISOU 2369  CG2 ILE A 347    14648   9328   7682  -2365  -1701  -1572       C  
ATOM   2370  CD1 ILE A 347      23.323  11.884  -6.404  1.00110.52           C  
ANISOU 2370  CD1 ILE A 347    18483  12689  10820  -2191  -2013  -1700       C  
ATOM   2371  N   GLY A 348      24.524  11.974 -11.585  1.00 93.84           N  
ANISOU 2371  N   GLY A 348    15020  10976   9658  -2526  -1894  -1576       N  
ATOM   2372  CA  GLY A 348      24.760  11.496 -12.931  1.00 87.39           C  
ANISOU 2372  CA  GLY A 348    13924  10287   8992  -2580  -1790  -1538       C  
ATOM   2373  C   GLY A 348      26.140  11.700 -13.521  1.00 98.51           C  
ANISOU 2373  C   GLY A 348    15069  11772  10590  -2574  -1966  -1506       C  
ATOM   2374  O   GLY A 348      26.614  10.840 -14.264  1.00102.97           O  
ANISOU 2374  O   GLY A 348    15487  12423  11215  -2533  -1911  -1492       O  
ATOM   2375  N   LEU A 349      26.792  12.818 -13.214  1.00106.73           N  
ANISOU 2375  N   LEU A 349    16041  12791  11718  -2630  -2165  -1514       N  
ATOM   2376  CA  LEU A 349      28.104  13.064 -13.798  1.00104.94           C  
ANISOU 2376  CA  LEU A 349    15503  12691  11679  -2692  -2301  -1499       C  
ATOM   2377  C   LEU A 349      29.201  12.422 -12.958  1.00 98.37           C  
ANISOU 2377  C   LEU A 349    14668  11893  10816  -2542  -2542  -1559       C  
ATOM   2378  O   LEU A 349      30.283  12.124 -13.460  1.00 84.65           O  
ANISOU 2378  O   LEU A 349    12628  10337   9199  -2514  -2622  -1569       O  
ATOM   2379  CB  LEU A 349      28.335  14.564 -13.960  1.00 97.43           C  
ANISOU 2379  CB  LEU A 349    14477  11693  10847  -2889  -2382  -1488       C  
ATOM   2380  CG  LEU A 349      27.392  15.195 -14.992  1.00108.65           C  
ANISOU 2380  CG  LEU A 349    15889  13106  12287  -2965  -2160  -1404       C  
ATOM   2381  CD1 LEU A 349      26.451  16.204 -14.358  1.00103.79           C  
ANISOU 2381  CD1 LEU A 349    15565  12298  11573  -2950  -2173  -1433       C  
ATOM   2382  CD2 LEU A 349      28.181  15.835 -16.126  1.00131.64           C  
ANISOU 2382  CD2 LEU A 349    18532  16115  15372  -3147  -2124  -1317       C  
ATOM   2383  N   TYR A 350      28.901  12.193 -11.683  1.00 97.86           N  
ANISOU 2383  N   TYR A 350    14938  11683  10561  -2415  -2652  -1602       N  
ATOM   2384  CA  TYR A 350      29.760  11.405 -10.808  1.00107.76           C  
ANISOU 2384  CA  TYR A 350    16284  12956  11703  -2184  -2880  -1645       C  
ATOM   2385  C   TYR A 350      29.638   9.983 -11.321  1.00126.54           C  
ANISOU 2385  C   TYR A 350    18728  15327  14026  -2010  -2708  -1589       C  
ATOM   2386  O   TYR A 350      28.521   9.532 -11.546  1.00145.71           O  
ANISOU 2386  O   TYR A 350    21364  17631  16369  -2066  -2445  -1544       O  
ATOM   2387  CB  TYR A 350      29.315  11.511  -9.347  1.00113.20           C  
ANISOU 2387  CB  TYR A 350    17393  13474  12144  -2082  -3000  -1684       C  
ATOM   2388  CG  TYR A 350      30.273  10.926  -8.328  1.00128.76           C  
ANISOU 2388  CG  TYR A 350    19488  15479  13958  -1810  -3306  -1734       C  
ATOM   2389  CD1 TYR A 350      30.364   9.552  -8.132  1.00124.92           C  
ANISOU 2389  CD1 TYR A 350    19232  14927  13307  -1531  -3267  -1668       C  
ATOM   2390  CD2 TYR A 350      31.063  11.751  -7.534  1.00139.31           C  
ANISOU 2390  CD2 TYR A 350    20749  16897  15284  -1818  -3648  -1859       C  
ATOM   2391  CE1 TYR A 350      31.230   9.017  -7.192  1.00122.02           C  
ANISOU 2391  CE1 TYR A 350    19017  14592  12752  -1206  -3571  -1703       C  
ATOM   2392  CE2 TYR A 350      31.931  11.224  -6.590  1.00133.40           C  
ANISOU 2392  CE2 TYR A 350    20096  16233  14357  -1525  -3968  -1924       C  
ATOM   2393  CZ  TYR A 350      32.011   9.859  -6.423  1.00124.79           C  
ANISOU 2393  CZ  TYR A 350    19237  15090  13086  -1188  -3932  -1834       C  
ATOM   2394  OH  TYR A 350      32.875   9.341  -5.484  1.00112.19           O  
ANISOU 2394  OH  TYR A 350    17770  13581  11274   -825  -4273  -1888       O  
ATOM   2395  N   GLN A 351      30.736   9.268 -11.539  1.00129.29           N  
ANISOU 2395  N   GLN A 351    18896  15813  14417  -1803  -2845  -1612       N  
ATOM   2396  CA  GLN A 351      32.103   9.720 -11.338  1.00121.85           C  
ANISOU 2396  CA  GLN A 351    17609  15108  13579  -1741  -3154  -1699       C  
ATOM   2397  C   GLN A 351      32.885   9.661 -12.642  1.00128.95           C  
ANISOU 2397  C   GLN A 351    18014  16282  14699  -1790  -3077  -1709       C  
ATOM   2398  O   GLN A 351      34.108   9.796 -12.663  1.00134.48           O  
ANISOU 2398  O   GLN A 351    18337  17262  15496  -1722  -3288  -1796       O  
ATOM   2399  CB  GLN A 351      32.849   8.765 -10.402  1.00123.13           C  
ANISOU 2399  CB  GLN A 351    17951  15283  13550  -1337  -3410  -1739       C  
ATOM   2400  CG  GLN A 351      34.086   9.337  -9.732  1.00134.87           C  
ANISOU 2400  CG  GLN A 351    19150  17030  15066  -1260  -3808  -1874       C  
ATOM   2401  CD  GLN A 351      34.660   8.402  -8.678  1.00134.67           C  
ANISOU 2401  CD  GLN A 351    19388  17005  14776   -785  -4088  -1907       C  
ATOM   2402  OE1 GLN A 351      34.104   7.336  -8.409  1.00128.49           O  
ANISOU 2402  OE1 GLN A 351    19081  15961  13780   -532  -3959  -1801       O  
ATOM   2403  NE2 GLN A 351      35.776   8.799  -8.076  1.00132.63           N  
ANISOU 2403  NE2 GLN A 351    18839  17039  14514   -669  -4477  -2058       N  
ATOM   2404  N   GLN A 352      32.154   9.442 -13.731  1.00134.69           N  
ANISOU 2404  N   GLN A 352    18726  16966  15483  -1906  -2767  -1637       N  
ATOM   2405  CA  GLN A 352      32.825   9.349 -15.047  1.00133.76           C  
ANISOU 2405  CA  GLN A 352    18171  17117  15533  -1941  -2650  -1640       C  
ATOM   2406  C   GLN A 352      33.247  10.668 -15.633  1.00133.16           C  
ANISOU 2406  C   GLN A 352    17722  17221  15651  -2280  -2641  -1627       C  
ATOM   2407  O   GLN A 352      32.672  11.701 -15.288  1.00118.61           O  
ANISOU 2407  O   GLN A 352    16025  15219  13822  -2520  -2650  -1595       O  
ATOM   2408  CB  GLN A 352      31.874   8.642 -16.003  1.00126.65           C  
ANISOU 2408  CB  GLN A 352    17418  16114  14589  -1943  -2338  -1587       C  
ATOM   2409  CG  GLN A 352      30.651   9.432 -16.356  1.00109.39           C  
ANISOU 2409  CG  GLN A 352    15346  13810  12408  -2225  -2149  -1520       C  
ATOM   2410  CD  GLN A 352      29.666   9.444 -15.213  1.00 96.61           C  
ANISOU 2410  CD  GLN A 352    14150  11925  10632  -2229  -2171  -1516       C  
ATOM   2411  OE1 GLN A 352      29.911   8.856 -14.160  1.00113.83           O  
ANISOU 2411  OE1 GLN A 352    16578  13985  12685  -2039  -2320  -1542       O  
ATOM   2412  NE2 GLN A 352      28.530  10.100 -15.421  1.00 86.39           N  
ANISOU 2412  NE2 GLN A 352    12947  10559   9317  -2415  -2016  -1484       N  
ATOM   2413  N   ASN A 353      34.280  10.636 -16.466  1.00149.37           N  
ANISOU 2413  N   ASN A 353    19321  19596  17836  -2292  -2619  -1657       N  
ATOM   2414  CA  ASN A 353      34.893  11.821 -17.048  1.00154.88           C  
ANISOU 2414  CA  ASN A 353    19643  20488  18715  -2653  -2588  -1639       C  
ATOM   2415  C   ASN A 353      34.110  12.629 -18.074  1.00156.09           C  
ANISOU 2415  C   ASN A 353    19852  20538  18915  -2947  -2310  -1498       C  
ATOM   2416  O   ASN A 353      33.137  12.136 -18.636  1.00142.68           O  
ANISOU 2416  O   ASN A 353    18368  18724  17120  -2846  -2112  -1433       O  
ATOM   2417  CB  ASN A 353      36.133  11.196 -17.688  1.00163.64           C  
ANISOU 2417  CB  ASN A 353    20264  22014  19897  -2495  -2587  -1717       C  
ATOM   2418  CG  ASN A 353      37.268  12.183 -17.848  1.00171.16           C  
ANISOU 2418  CG  ASN A 353    20719  23284  21031  -2824  -2662  -1773       C  
ATOM   2419  OD1 ASN A 353      37.057  13.346 -18.187  1.00176.06           O  
ANISOU 2419  OD1 ASN A 353    21342  23805  21749  -3247  -2551  -1688       O  
ATOM   2420  ND2 ASN A 353      38.485  11.724 -17.584  1.00173.13           N  
ANISOU 2420  ND2 ASN A 353    20547  23918  21317  -2631  -2852  -1928       N  
ATOM   2421  N   PHE A 354      34.528  13.872 -18.308  1.00172.81           N  
ANISOU 2421  N   PHE A 354    21801  22693  21165  -3312  -2303  -1458       N  
ATOM   2422  CA  PHE A 354      33.828  14.759 -19.236  1.00164.94           C  
ANISOU 2422  CA  PHE A 354    20926  21562  20181  -3560  -2062  -1300       C  
ATOM   2423  C   PHE A 354      34.072  14.369 -20.693  1.00166.25           C  
ANISOU 2423  C   PHE A 354    20824  21993  20349  -3550  -1788  -1218       C  
ATOM   2424  O   PHE A 354      34.542  15.164 -21.507  1.00149.82           O  
ANISOU 2424  O   PHE A 354    18554  20026  18344  -3839  -1635  -1119       O  
ATOM   2425  CB  PHE A 354      34.246  16.212 -19.009  1.00180.33           C  
ANISOU 2425  CB  PHE A 354    22867  23397  22254  -3968  -2129  -1273       C  
ATOM   2426  CG  PHE A 354      33.429  16.920 -17.964  1.00199.94           C  
ANISOU 2426  CG  PHE A 354    25792  25500  24679  -3995  -2285  -1298       C  
ATOM   2427  CD1 PHE A 354      32.249  16.362 -17.495  1.00204.63           C  
ANISOU 2427  CD1 PHE A 354    26731  25910  25109  -3701  -2283  -1302       C  
ATOM   2428  CD2 PHE A 354      33.834  18.148 -17.458  1.00204.09           C  
ANISOU 2428  CD2 PHE A 354    26390  25854  25302  -4332  -2416  -1335       C  
ATOM   2429  CE1 PHE A 354      31.491  17.012 -16.535  1.00201.80           C  
ANISOU 2429  CE1 PHE A 354    26756  25247  24673  -3697  -2401  -1339       C  
ATOM   2430  CE2 PHE A 354      33.079  18.804 -16.498  1.00205.25           C  
ANISOU 2430  CE2 PHE A 354    26969  25646  25371  -4315  -2556  -1382       C  
ATOM   2431  CZ  PHE A 354      31.906  18.234 -16.037  1.00203.99           C  
ANISOU 2431  CZ  PHE A 354    27124  25348  25034  -3974  -2544  -1382       C  
ATOM   2432  N   VAL A 355      33.729  13.122 -20.995  1.00183.33           N  
ANISOU 2432  N   VAL A 355    23019  24231  22405  -3223  -1717  -1262       N  
ATOM   2433  CA  VAL A 355      33.880  12.519 -22.316  1.00190.84           C  
ANISOU 2433  CA  VAL A 355    23766  25433  23312  -3129  -1475  -1231       C  
ATOM   2434  C   VAL A 355      32.906  12.986 -23.429  1.00152.78           C  
ANISOU 2434  C   VAL A 355    19113  20544  18392  -3233  -1229  -1084       C  
ATOM   2435  O   VAL A 355      33.377  13.281 -24.530  1.00158.74           O  
ANISOU 2435  O   VAL A 355    19643  21525  19145  -3352  -1032   -999       O  
ATOM   2436  CB  VAL A 355      33.784  10.973 -22.218  1.00159.89           C  
ANISOU 2436  CB  VAL A 355    19909  21549  19293  -2732  -1498  -1358       C  
ATOM   2437  CG1 VAL A 355      34.177  10.326 -23.535  1.00162.63           C  
ANISOU 2437  CG1 VAL A 355    20008  22191  19593  -2608  -1274  -1375       C  
ATOM   2438  CG2 VAL A 355      34.663  10.452 -21.086  1.00160.71           C  
ANISOU 2438  CG2 VAL A 355    19921  21703  19439  -2531  -1768  -1489       C  
ATOM   2439  N   ASP A 356      31.586  13.076 -23.192  1.00129.78           N  
ANISOU 2439  N   ASP A 356    16567  17370  15374  -3177  -1231  -1058       N  
ATOM   2440  CA  ASP A 356      30.960  13.438 -21.907  1.00136.41           C  
ANISOU 2440  CA  ASP A 356    17704  17912  16215  -3184  -1419  -1092       C  
ATOM   2441  C   ASP A 356      30.831  12.360 -20.834  1.00148.02           C  
ANISOU 2441  C   ASP A 356    19315  19286  17640  -2956  -1571  -1230       C  
ATOM   2442  O   ASP A 356      30.725  12.698 -19.653  1.00153.16           O  
ANISOU 2442  O   ASP A 356    20148  19750  18296  -2974  -1751  -1266       O  
ATOM   2443  CB  ASP A 356      29.558  13.999 -22.144  1.00131.40           C  
ANISOU 2443  CB  ASP A 356    17364  17101  15461  -3191  -1330  -1018       C  
ATOM   2444  CG  ASP A 356      28.701  13.082 -22.977  1.00141.92           C  
ANISOU 2444  CG  ASP A 356    18720  18551  16652  -3022  -1172  -1059       C  
ATOM   2445  OD1 ASP A 356      29.067  12.838 -24.144  1.00140.24           O  
ANISOU 2445  OD1 ASP A 356    18316  18560  16410  -3012  -1022  -1023       O  
ATOM   2446  OD2 ASP A 356      27.691  12.566 -22.455  1.00151.83           O  
ANISOU 2446  OD2 ASP A 356    20177  19696  17816  -2918  -1190  -1146       O  
ATOM   2447  N   GLY A 357      30.802  11.087 -21.219  1.00142.14           N  
ANISOU 2447  N   GLY A 357    18548  18634  16825  -2740  -1492  -1306       N  
ATOM   2448  CA  GLY A 357      30.667  10.002 -20.256  1.00135.44           C  
ANISOU 2448  CA  GLY A 357    17922  17635  15902  -2520  -1605  -1409       C  
ATOM   2449  C   GLY A 357      29.364   9.976 -19.473  1.00125.63           C  
ANISOU 2449  C   GLY A 357    17062  16126  14546  -2543  -1600  -1416       C  
ATOM   2450  O   GLY A 357      29.026   8.972 -18.843  1.00125.31           O  
ANISOU 2450  O   GLY A 357    17274  15933  14404  -2399  -1613  -1480       O  
ATOM   2451  N   SER A 358      28.629  11.081 -19.520  1.00120.27           N  
ANISOU 2451  N   SER A 358    16442  15389  13868  -2714  -1565  -1348       N  
ATOM   2452  CA  SER A 358      27.326  11.175 -18.892  1.00121.25           C  
ANISOU 2452  CA  SER A 358    16855  15340  13874  -2728  -1527  -1370       C  
ATOM   2453  C   SER A 358      26.390  10.317 -19.736  1.00148.39           C  
ANISOU 2453  C   SER A 358    20313  18855  17212  -2702  -1322  -1424       C  
ATOM   2454  O   SER A 358      26.660  10.097 -20.918  1.00166.87           O  
ANISOU 2454  O   SER A 358    22456  21374  19574  -2694  -1219  -1417       O  
ATOM   2455  CB  SER A 358      26.875  12.638 -18.820  1.00126.14           C  
ANISOU 2455  CB  SER A 358    17517  15898  14514  -2853  -1554  -1299       C  
ATOM   2456  OG  SER A 358      26.931  13.254 -20.095  1.00144.20           O  
ANISOU 2456  OG  SER A 358    19625  18325  16839  -2929  -1440  -1207       O  
ATOM   2457  N   PHE A 359      25.294   9.828 -19.167  1.00140.27           N  
ANISOU 2457  N   PHE A 359    19512  17720  16065  -2712  -1249  -1495       N  
ATOM   2458  CA  PHE A 359      24.747  10.268 -17.892  1.00118.71           C  
ANISOU 2458  CA  PHE A 359    17010  14826  13266  -2729  -1319  -1500       C  
ATOM   2459  C   PHE A 359      24.249   9.047 -17.138  1.00125.41           C  
ANISOU 2459  C   PHE A 359    18130  15530  13988  -2715  -1238  -1574       C  
ATOM   2460  O   PHE A 359      23.464   8.265 -17.676  1.00143.97           O  
ANISOU 2460  O   PHE A 359    20499  17930  16274  -2791  -1056  -1652       O  
ATOM   2461  CB  PHE A 359      23.630  11.281 -18.152  1.00102.81           C  
ANISOU 2461  CB  PHE A 359    14966  12895  11202  -2782  -1246  -1495       C  
ATOM   2462  CG  PHE A 359      22.945  11.778 -16.922  1.00 86.92           C  
ANISOU 2462  CG  PHE A 359    13174  10756   9094  -2770  -1284  -1525       C  
ATOM   2463  CD1 PHE A 359      23.440  12.863 -16.229  1.00 94.10           C  
ANISOU 2463  CD1 PHE A 359    14170  11535  10047  -2745  -1457  -1477       C  
ATOM   2464  CD2 PHE A 359      21.782  11.178 -16.479  1.00 86.87           C  
ANISOU 2464  CD2 PHE A 359    13285  10778   8944  -2805  -1129  -1619       C  
ATOM   2465  CE1 PHE A 359      22.794  13.332 -15.105  1.00 98.12           C  
ANISOU 2465  CE1 PHE A 359    14903  11938  10441  -2702  -1487  -1527       C  
ATOM   2466  CE2 PHE A 359      21.134  11.638 -15.356  1.00 90.54           C  
ANISOU 2466  CE2 PHE A 359    13937  11170   9293  -2779  -1131  -1655       C  
ATOM   2467  CZ  PHE A 359      21.641  12.717 -14.666  1.00 93.80           C  
ANISOU 2467  CZ  PHE A 359    14459  11448   9734  -2700  -1316  -1610       C  
ATOM   2468  N   SER A 360      24.707   8.863 -15.904  1.00109.96           N  
ANISOU 2468  N   SER A 360    16410  13392  11979  -2633  -1369  -1555       N  
ATOM   2469  CA  SER A 360      24.421   7.616 -15.206  1.00102.10           C  
ANISOU 2469  CA  SER A 360    15748  12207  10839  -2605  -1284  -1587       C  
ATOM   2470  C   SER A 360      23.116   7.648 -14.433  1.00 89.91           C  
ANISOU 2470  C   SER A 360    14425  10602   9134  -2741  -1124  -1622       C  
ATOM   2471  O   SER A 360      23.084   7.998 -13.256  1.00 90.44           O  
ANISOU 2471  O   SER A 360    14709  10559   9094  -2691  -1206  -1593       O  
ATOM   2472  CB  SER A 360      25.565   7.261 -14.256  1.00 80.16           C  
ANISOU 2472  CB  SER A 360    13158   9275   8024  -2394  -1506  -1542       C  
ATOM   2473  OG  SER A 360      26.598   6.583 -14.951  1.00102.77           O  
ANISOU 2473  OG  SER A 360    15886  12186  10976  -2236  -1571  -1549       O  
ATOM   2474  N   LEU A 361      22.044   7.251 -15.115  1.00 94.09           N  
ANISOU 2474  N   LEU A 361    14877  11242   9632  -2916   -891  -1705       N  
ATOM   2475  CA  LEU A 361      20.761   7.005 -14.473  1.00 99.66           C  
ANISOU 2475  CA  LEU A 361    15745  11944  10176  -3090   -679  -1771       C  
ATOM   2476  C   LEU A 361      20.913   5.764 -13.605  1.00108.20           C  
ANISOU 2476  C   LEU A 361    17273  12722  11114  -3121   -594  -1739       C  
ATOM   2477  O   LEU A 361      20.145   5.541 -12.671  1.00115.43           O  
ANISOU 2477  O   LEU A 361    18441  13560  11856  -3246   -436  -1745       O  
ATOM   2478  CB  LEU A 361      19.641   6.835 -15.504  1.00102.16           C  
ANISOU 2478  CB  LEU A 361    15801  12517  10500  -3289   -472  -1906       C  
ATOM   2479  CG  LEU A 361      18.222   6.688 -14.945  1.00113.12           C  
ANISOU 2479  CG  LEU A 361    17226  14022  11733  -3508   -231  -2015       C  
ATOM   2480  CD1 LEU A 361      17.234   7.435 -15.813  1.00108.83           C  
ANISOU 2480  CD1 LEU A 361    16264  13879  11209  -3541   -177  -2138       C  
ATOM   2481  CD2 LEU A 361      17.823   5.220 -14.850  1.00132.55           C  
ANISOU 2481  CD2 LEU A 361    19943  16315  14106  -3779      4  -2088       C  
ATOM   2482  N   SER A 362      21.904   4.947 -13.946  1.00105.50           N  
ANISOU 2482  N   SER A 362    17046  12212  10826  -2987   -684  -1703       N  
ATOM   2483  CA  SER A 362      22.227   3.765 -13.164  1.00112.30           C  
ANISOU 2483  CA  SER A 362    18406  12728  11535  -2924   -645  -1646       C  
ATOM   2484  C   SER A 362      22.569   4.180 -11.742  1.00127.42           C  
ANISOU 2484  C   SER A 362    20593  14520  13300  -2758   -796  -1540       C  
ATOM   2485  O   SER A 362      22.129   3.558 -10.775  1.00139.68           O  
ANISOU 2485  O   SER A 362    22591  15847  14632  -2821   -658  -1488       O  
ATOM   2486  CB  SER A 362      23.399   3.004 -13.785  1.00100.95           C  
ANISOU 2486  CB  SER A 362    17005  11170  10181  -2683   -779  -1633       C  
ATOM   2487  OG  SER A 362      24.476   3.875 -14.088  1.00 83.67           O  
ANISOU 2487  OG  SER A 362    14459   9186   8148  -2452  -1051  -1601       O  
ATOM   2488  N   GLN A 363      23.351   5.248 -11.626  1.00120.76           N  
ANISOU 2488  N   GLN A 363    19496  13826  12560  -2570  -1073  -1514       N  
ATOM   2489  CA  GLN A 363      23.726   5.789 -10.325  1.00112.97           C  
ANISOU 2489  CA  GLN A 363    18721  12769  11433  -2409  -1267  -1455       C  
ATOM   2490  C   GLN A 363      22.585   6.544  -9.649  1.00 84.70           C  
ANISOU 2490  C   GLN A 363    15187   9267   7727  -2575  -1121  -1487       C  
ATOM   2491  O   GLN A 363      22.472   6.540  -8.428  1.00 93.39           O  
ANISOU 2491  O   GLN A 363    16635  10246   8601  -2506  -1140  -1445       O  
ATOM   2492  CB  GLN A 363      24.947   6.688 -10.473  1.00 84.26           C  
ANISOU 2492  CB  GLN A 363    14775   9276   7964  -2217  -1609  -1458       C  
ATOM   2493  CG  GLN A 363      26.235   5.906 -10.654  1.00 85.49           C  
ANISOU 2493  CG  GLN A 363    14893   9400   8190  -1974  -1781  -1438       C  
ATOM   2494  CD  GLN A 363      27.427   6.804 -10.870  1.00 94.66           C  
ANISOU 2494  CD  GLN A 363    15658  10778   9532  -1859  -2085  -1468       C  
ATOM   2495  OE1 GLN A 363      28.404   6.423 -11.518  1.00 93.37           O  
ANISOU 2495  OE1 GLN A 363    15286  10713   9477  -1689  -2204  -1483       O  
ATOM   2496  NE2 GLN A 363      27.362   8.006 -10.314  1.00 94.85           N  
ANISOU 2496  NE2 GLN A 363    15579  10881   9581  -1960  -2202  -1492       N  
ATOM   2497  N   LEU A 364      21.763   7.220 -10.443  1.00 82.91           N  
ANISOU 2497  N   LEU A 364    14609   9270   7623  -2749   -987  -1568       N  
ATOM   2498  CA  LEU A 364      20.543   7.849  -9.941  1.00 91.69           C  
ANISOU 2498  CA  LEU A 364    15715  10513   8610  -2873   -809  -1631       C  
ATOM   2499  C   LEU A 364      19.540   6.830  -9.405  1.00108.63           C  
ANISOU 2499  C   LEU A 364    18154  12583  10539  -3089   -474  -1643       C  
ATOM   2500  O   LEU A 364      18.912   7.043  -8.369  1.00 92.75           O  
ANISOU 2500  O   LEU A 364    16350  10577   8313  -3118   -355  -1647       O  
ATOM   2501  CB  LEU A 364      19.874   8.677 -11.035  1.00 94.51           C  
ANISOU 2501  CB  LEU A 364    15628  11157   9126  -2953   -747  -1720       C  
ATOM   2502  CG  LEU A 364      20.175  10.173 -11.019  1.00107.63           C  
ANISOU 2502  CG  LEU A 364    17120  12897  10877  -2796   -968  -1723       C  
ATOM   2503  CD1 LEU A 364      21.421  10.472 -11.836  1.00121.74           C  
ANISOU 2503  CD1 LEU A 364    18714  14656  12887  -2718  -1203  -1661       C  
ATOM   2504  CD2 LEU A 364      18.978  10.958 -11.528  1.00106.50           C  
ANISOU 2504  CD2 LEU A 364    16721  13015  10729  -2827   -824  -1819       C  
ATOM   2505  N   GLU A 365      19.369   5.738 -10.144  1.00128.74           N  
ANISOU 2505  N   GLU A 365    20718  15061  13135  -3266   -301  -1662       N  
ATOM   2506  CA  GLU A 365      18.408   4.706  -9.779  1.00133.77           C  
ANISOU 2506  CA  GLU A 365    21633  15600  13591  -3568     53  -1688       C  
ATOM   2507  C   GLU A 365      18.852   4.037  -8.486  1.00142.72           C  
ANISOU 2507  C   GLU A 365    23376  16379  14472  -3468     56  -1538       C  
ATOM   2508  O   GLU A 365      18.023   3.658  -7.657  1.00157.39           O  
ANISOU 2508  O   GLU A 365    25527  18181  16094  -3676    339  -1520       O  
ATOM   2509  CB  GLU A 365      18.256   3.672 -10.901  1.00137.81           C  
ANISOU 2509  CB  GLU A 365    22081  16061  14221  -3787    201  -1764       C  
ATOM   2510  CG  GLU A 365      16.911   2.952 -10.904  1.00141.31           C  
ANISOU 2510  CG  GLU A 365    22569  16572  14551  -4238    603  -1883       C  
ATOM   2511  CD  GLU A 365      16.827   1.861 -11.954  1.00135.61           C  
ANISOU 2511  CD  GLU A 365    21860  15739  13928  -4476    728  -1986       C  
ATOM   2512  OE1 GLU A 365      17.816   1.665 -12.693  1.00133.22           O  
ANISOU 2512  OE1 GLU A 365    21533  15317  13769  -4242    509  -1959       O  
ATOM   2513  OE2 GLU A 365      15.768   1.206 -12.040  1.00135.79           O  
ANISOU 2513  OE2 GLU A 365    21904  15813  13877  -4910   1052  -2116       O  
ATOM   2514  N   SER A 366      20.165   3.901  -8.322  1.00117.31           N  
ANISOU 2514  N   SER A 366    20336  12954  11281  -3137   -256  -1433       N  
ATOM   2515  CA  SER A 366      20.734   3.287  -7.128  1.00110.76           C  
ANISOU 2515  CA  SER A 366    20099  11801  10184  -2937   -328  -1283       C  
ATOM   2516  C   SER A 366      20.392   4.063  -5.859  1.00123.12           C  
ANISOU 2516  C   SER A 366    21823  13444  11511  -2872   -343  -1255       C  
ATOM   2517  O   SER A 366      19.921   3.471  -4.889  1.00139.92           O  
ANISOU 2517  O   SER A 366    24443  15388  13332  -2958   -124  -1165       O  
ATOM   2518  CB  SER A 366      22.252   3.155  -7.260  1.00 93.43           C  
ANISOU 2518  CB  SER A 366    17933   9490   8077  -2531   -719  -1220       C  
ATOM   2519  OG  SER A 366      22.605   2.331  -8.355  1.00 93.20           O  
ANISOU 2519  OG  SER A 366    17826   9366   8219  -2540   -687  -1249       O  
ATOM   2520  N   VAL A 367      20.607   5.380  -5.868  1.00114.57           N  
ANISOU 2520  N   VAL A 367    20366  12616  10551  -2733   -580  -1335       N  
ATOM   2521  CA  VAL A 367      20.354   6.196  -4.676  1.00112.34           C  
ANISOU 2521  CA  VAL A 367    20246  12401  10038  -2628   -631  -1344       C  
ATOM   2522  C   VAL A 367      18.884   6.105  -4.279  1.00112.11           C  
ANISOU 2522  C   VAL A 367    20286  12493   9816  -2922   -196  -1390       C  
ATOM   2523  O   VAL A 367      18.556   6.124  -3.095  1.00131.32           O  
ANISOU 2523  O   VAL A 367    23089  14880  11928  -2885    -91  -1345       O  
ATOM   2524  CB  VAL A 367      20.773   7.698  -4.854  1.00 97.10           C  
ANISOU 2524  CB  VAL A 367    17917  10683   8294  -2468   -945  -1453       C  
ATOM   2525  CG1 VAL A 367      22.208   7.821  -5.349  1.00 90.04           C  
ANISOU 2525  CG1 VAL A 367    16854   9741   7618  -2259  -1335  -1432       C  
ATOM   2526  CG2 VAL A 367      19.826   8.448  -5.768  1.00101.32           C  
ANISOU 2526  CG2 VAL A 367    17984  11488   9023  -2650   -774  -1575       C  
ATOM   2527  N   MET A 368      18.005   5.993  -5.268  1.00 97.16           N  
ANISOU 2527  N   MET A 368    18021  10796   8099  -3209     58  -1492       N  
ATOM   2528  CA  MET A 368      16.587   5.818  -5.004  1.00109.88           C  
ANISOU 2528  CA  MET A 368    19599  12601   9548  -3529    489  -1572       C  
ATOM   2529  C   MET A 368      16.327   4.490  -4.298  1.00121.54           C  
ANISOU 2529  C   MET A 368    21645  13785  10750  -3762    803  -1443       C  
ATOM   2530  O   MET A 368      15.506   4.415  -3.384  1.00119.77           O  
ANISOU 2530  O   MET A 368    21639  13630  10240  -3922   1108  -1435       O  
ATOM   2531  CB  MET A 368      15.797   5.893  -6.307  1.00125.67           C  
ANISOU 2531  CB  MET A 368    21046  14905  11798  -3775    643  -1733       C  
ATOM   2532  CG  MET A 368      15.851   7.248  -6.989  1.00123.50           C  
ANISOU 2532  CG  MET A 368    20267  14919  11740  -3551    395  -1842       C  
ATOM   2533  SD  MET A 368      14.423   8.263  -6.558  1.00134.31           S  
ANISOU 2533  SD  MET A 368    21338  16735  12960  -3560    620  -2020       S  
ATOM   2534  CE  MET A 368      13.098   7.147  -7.013  1.00139.86           C  
ANISOU 2534  CE  MET A 368    21845  17682  13612  -4067   1103  -2142       C  
ATOM   2535  N   LYS A 369      17.040   3.450  -4.722  1.00137.87           N  
ANISOU 2535  N   LYS A 369    23984  15512  12887  -3768    740  -1339       N  
ATOM   2536  CA  LYS A 369      16.873   2.118  -4.149  1.00159.78           C  
ANISOU 2536  CA  LYS A 369    27398  17907  15405  -3978   1030  -1195       C  
ATOM   2537  C   LYS A 369      17.320   2.050  -2.687  1.00175.46           C  
ANISOU 2537  C   LYS A 369    30005  19656  17005  -3711    959  -1008       C  
ATOM   2538  O   LYS A 369      16.587   1.545  -1.835  1.00199.62           O  
ANISOU 2538  O   LYS A 369    33489  22616  19743  -3955   1330   -924       O  
ATOM   2539  CB  LYS A 369      17.637   1.080  -4.976  1.00166.39           C  
ANISOU 2539  CB  LYS A 369    28421  18398  16401  -3944    927  -1141       C  
ATOM   2540  CG  LYS A 369      16.983   0.723  -6.306  1.00165.65           C  
ANISOU 2540  CG  LYS A 369    27908  18454  16578  -4324   1123  -1321       C  
ATOM   2541  CD  LYS A 369      17.720  -0.429  -6.980  1.00166.37           C  
ANISOU 2541  CD  LYS A 369    28317  18137  16759  -4276   1059  -1272       C  
ATOM   2542  CE  LYS A 369      18.170  -0.062  -8.386  1.00166.54           C  
ANISOU 2542  CE  LYS A 369    27755  18387  17135  -4158    820  -1420       C  
ATOM   2543  NZ  LYS A 369      19.612  -0.374  -8.600  1.00160.91           N  
ANISOU 2543  NZ  LYS A 369    27228  17419  16491  -3688    466  -1320       N  
ATOM   2544  N   GLU A 370      18.515   2.553  -2.396  1.00165.35           N  
ANISOU 2544  N   GLU A 370    28774  18312  15738  -3228    491   -952       N  
ATOM   2545  CA  GLU A 370      19.047   2.498  -1.036  1.00156.54           C  
ANISOU 2545  CA  GLU A 370    28240  17002  14236  -2913    348   -795       C  
ATOM   2546  C   GLU A 370      18.261   3.397  -0.090  1.00146.16           C  
ANISOU 2546  C   GLU A 370    26894  15960  12680  -2959    494   -859       C  
ATOM   2547  O   GLU A 370      18.037   3.049   1.070  1.00165.75           O  
ANISOU 2547  O   GLU A 370    29940  18298  14737  -2933    664   -727       O  
ATOM   2548  CB  GLU A 370      20.525   2.891  -1.015  1.00150.52           C  
ANISOU 2548  CB  GLU A 370    27424  16198  13569  -2401   -226   -779       C  
ATOM   2549  CG  GLU A 370      21.167   2.901   0.373  1.00154.52           C  
ANISOU 2549  CG  GLU A 370    28486  16562  13661  -2015   -461   -652       C  
ATOM   2550  CD  GLU A 370      21.099   1.555   1.076  1.00154.04           C  
ANISOU 2550  CD  GLU A 370    29250  16074  13206  -1999   -226   -413       C  
ATOM   2551  OE1 GLU A 370      21.508   0.545   0.468  1.00150.03           O  
ANISOU 2551  OE1 GLU A 370    28941  15269  12795  -1969   -215   -327       O  
ATOM   2552  OE2 GLU A 370      20.660   1.509   2.246  1.00154.83           O  
ANISOU 2552  OE2 GLU A 370    29842  16112  12875  -1994    -51   -307       O  
ATOM   2553  N   LEU A 371      17.850   4.557  -0.586  1.00115.45           N  
ANISOU 2553  N   LEU A 371    22379  12455   9032  -2995    431  -1060       N  
ATOM   2554  CA  LEU A 371      17.158   5.524   0.253  1.00128.78           C  
ANISOU 2554  CA  LEU A 371    24007  14417  10506  -2958    529  -1159       C  
ATOM   2555  C   LEU A 371      15.806   5.001   0.716  1.00144.09           C  
ANISOU 2555  C   LEU A 371    26105  16464  12180  -3352   1112  -1150       C  
ATOM   2556  O   LEU A 371      15.438   5.187   1.875  1.00157.50           O  
ANISOU 2556  O   LEU A 371    28142  18210  13490  -3292   1268  -1115       O  
ATOM   2557  CB  LEU A 371      16.980   6.853  -0.478  1.00125.59           C  
ANISOU 2557  CB  LEU A 371    22938  14357  10424  -2884    345  -1375       C  
ATOM   2558  CG  LEU A 371      16.456   8.033   0.345  1.00125.17           C  
ANISOU 2558  CG  LEU A 371    22829  14554  10175  -2724    345  -1512       C  
ATOM   2559  CD1 LEU A 371      17.042   9.315  -0.213  1.00120.41           C  
ANISOU 2559  CD1 LEU A 371    21824  14054   9874  -2480    -72  -1653       C  
ATOM   2560  CD2 LEU A 371      14.926   8.116   0.369  1.00129.27           C  
ANISOU 2560  CD2 LEU A 371    23114  15415  10587  -3005    844  -1631       C  
ATOM   2561  N   TYR A 372      15.072   4.357  -0.186  1.00144.29           N  
ANISOU 2561  N   TYR A 372    25871  16554  12398  -3771   1439  -1201       N  
ATOM   2562  CA  TYR A 372      13.738   3.862   0.135  1.00163.92           C  
ANISOU 2562  CA  TYR A 372    28396  19212  14675  -4237   2021  -1234       C  
ATOM   2563  C   TYR A 372      13.782   2.916   1.343  1.00184.17           C  
ANISOU 2563  C   TYR A 372    31788  21414  16772  -4322   2282   -992       C  
ATOM   2564  O   TYR A 372      12.960   3.034   2.249  1.00192.97           O  
ANISOU 2564  O   TYR A 372    33058  22716  17547  -4471   2644   -993       O  
ATOM   2565  CB  TYR A 372      13.103   3.167  -1.074  1.00168.13           C  
ANISOU 2565  CB  TYR A 372    28561  19824  15497  -4705   2278  -1340       C  
ATOM   2566  CG  TYR A 372      11.667   2.735  -0.843  1.00177.07           C  
ANISOU 2566  CG  TYR A 372    29590  21232  16456  -5258   2881  -1435       C  
ATOM   2567  CD1 TYR A 372      10.628   3.646  -0.996  1.00180.98           C  
ANISOU 2567  CD1 TYR A 372    29432  22334  16998  -5323   3038  -1683       C  
ATOM   2568  CD2 TYR A 372      11.347   1.437  -0.464  1.00185.18           C  
ANISOU 2568  CD2 TYR A 372    31171  21926  17262  -5712   3300  -1288       C  
ATOM   2569  CE1 TYR A 372       9.311   3.280  -0.787  1.00191.69           C  
ANISOU 2569  CE1 TYR A 372    30597  24039  18198  -5830   3592  -1806       C  
ATOM   2570  CE2 TYR A 372      10.025   1.060  -0.249  1.00191.53           C  
ANISOU 2570  CE2 TYR A 372    31835  23025  17913  -6293   3883  -1394       C  
ATOM   2571  CZ  TYR A 372       9.013   1.988  -0.413  1.00191.15           C  
ANISOU 2571  CZ  TYR A 372    31041  23661  17927  -6352   4025  -1666       C  
ATOM   2572  OH  TYR A 372       7.700   1.629  -0.204  1.00189.52           O  
ANISOU 2572  OH  TYR A 372    30605  23835  17569  -6930   4607  -1804       O  
ATOM   2573  N   ARG A 373      14.733   1.983   1.361  1.00189.06           N  
ANISOU 2573  N   ARG A 373    32960  21526  17348  -4196   2109   -781       N  
ATOM   2574  CA  ARG A 373      14.830   1.051   2.485  1.00198.08           C  
ANISOU 2574  CA  ARG A 373    34984  22266  18013  -4220   2336   -515       C  
ATOM   2575  C   ARG A 373      15.308   1.767   3.753  1.00194.04           C  
ANISOU 2575  C   ARG A 373    34800  21804  17123  -3744   2087   -442       C  
ATOM   2576  O   ARG A 373      14.885   1.426   4.856  1.00207.35           O  
ANISOU 2576  O   ARG A 373    37049  23402  18332  -3824   2406   -293       O  
ATOM   2577  CB  ARG A 373      15.759  -0.129   2.157  1.00203.88           C  
ANISOU 2577  CB  ARG A 373    36264  22423  18776  -4113   2178   -313       C  
ATOM   2578  CG  ARG A 373      17.245   0.200   2.122  1.00203.20           C  
ANISOU 2578  CG  ARG A 373    36224  22198  18785  -3459   1523   -266       C  
ATOM   2579  CD  ARG A 373      18.094  -0.965   2.618  1.00214.31           C  
ANISOU 2579  CD  ARG A 373    38502  23027  19899  -3186   1423     12       C  
ATOM   2580  NE  ARG A 373      17.751  -1.348   3.986  1.00222.46           N  
ANISOU 2580  NE  ARG A 373    40308  23864  20354  -3190   1698    233       N  
ATOM   2581  CZ  ARG A 373      18.423  -2.243   4.704  1.00228.00           C  
ANISOU 2581  CZ  ARG A 373    41890  24075  20665  -2872   1614    510       C  
ATOM   2582  NH1 ARG A 373      19.483  -2.849   4.188  1.00226.32           N  
ANISOU 2582  NH1 ARG A 373    41860  23536  20594  -2496   1249    579       N  
ATOM   2583  NH2 ARG A 373      18.037  -2.531   5.941  1.00234.82           N  
ANISOU 2583  NH2 ARG A 373    43464  24787  20969  -2894   1899    721       N  
ATOM   2584  N   GLU A 374      16.190   2.752   3.596  1.00176.83           N  
ANISOU 2584  N   GLU A 374    32285  19764  15138  -3274   1528   -555       N  
ATOM   2585  CA  GLU A 374      16.654   3.549   4.729  1.00172.90           C  
ANISOU 2585  CA  GLU A 374    32028  19353  14314  -2837   1239   -555       C  
ATOM   2586  C   GLU A 374      15.528   4.433   5.267  1.00183.50           C  
ANISOU 2586  C   GLU A 374    33114  21124  15485  -2979   1554   -724       C  
ATOM   2587  O   GLU A 374      15.282   4.479   6.472  1.00199.00           O  
ANISOU 2587  O   GLU A 374    35548  23101  16960  -2878   1713   -648       O  
ATOM   2588  CB  GLU A 374      17.866   4.402   4.336  1.00157.90           C  
ANISOU 2588  CB  GLU A 374    29778  17505  12710  -2388    575   -674       C  
ATOM   2589  CG  GLU A 374      19.206   3.834   4.790  1.00151.00           C  
ANISOU 2589  CG  GLU A 374    29419  16295  11660  -1956    143   -499       C  
ATOM   2590  CD  GLU A 374      19.389   3.901   6.297  1.00155.71           C  
ANISOU 2590  CD  GLU A 374    30658  16832  11671  -1650     70   -394       C  
ATOM   2591  OE1 GLU A 374      18.750   4.764   6.935  1.00153.34           O  
ANISOU 2591  OE1 GLU A 374    30270  16809  11183  -1674    191   -526       O  
ATOM   2592  OE2 GLU A 374      20.173   3.096   6.846  1.00160.85           O  
ANISOU 2592  OE2 GLU A 374    31922  17169  12024  -1345   -118   -187       O  
ATOM   2593  N   SER A 375      14.847   5.123   4.357  1.00176.58           N  
ANISOU 2593  N   SER A 375    31497  20609  14986  -3174   1643   -958       N  
ATOM   2594  CA  SER A 375      13.670   5.932   4.677  1.00179.98           C  
ANISOU 2594  CA  SER A 375    31583  21501  15300  -3292   1968  -1156       C  
ATOM   2595  C   SER A 375      12.503   5.075   5.154  1.00192.12           C  
ANISOU 2595  C   SER A 375    33353  23126  16519  -3773   2652  -1075       C  
ATOM   2596  O   SER A 375      11.669   5.523   5.944  1.00184.08           O  
ANISOU 2596  O   SER A 375    32328  22431  15182  -3801   2969  -1164       O  
ATOM   2597  CB  SER A 375      13.235   6.767   3.467  1.00173.36           C  
ANISOU 2597  CB  SER A 375    29911  21016  14941  -3350   1884  -1410       C  
ATOM   2598  OG  SER A 375      12.727   5.945   2.430  1.00166.53           O  
ANISOU 2598  OG  SER A 375    28759  20170  14345  -3791   2159  -1410       O  
ATOM   2599  N   GLY A 376      12.459   3.838   4.672  1.00202.97           N  
ANISOU 2599  N   GLY A 376    34943  24204  17971  -4162   2891   -918       N  
ATOM   2600  CA  GLY A 376      11.350   2.937   4.920  1.00191.79           C  
ANISOU 2600  CA  GLY A 376    33703  22839  16330  -4751   3567   -855       C  
ATOM   2601  C   GLY A 376      10.265   3.015   3.861  1.00183.24           C  
ANISOU 2601  C   GLY A 376    31826  22195  15600  -5217   3873  -1111       C  
ATOM   2602  O   GLY A 376      10.380   3.745   2.880  1.00172.58           O  
ANISOU 2602  O   GLY A 376    29824  21084  14665  -5047   3551  -1314       O  
ATOM   2603  N   ASN A 377       9.190   2.270   4.086  1.00207.18           N  
ANISOU 2603  N   ASN A 377    34920  25358  18441  -5816   4507  -1106       N  
ATOM   2604  CA  ASN A 377       8.134   2.068   3.093  1.00226.38           C  
ANISOU 2604  CA  ASN A 377    36646  28195  21172  -6362   4840  -1351       C  
ATOM   2605  C   ASN A 377       7.181   3.223   2.785  1.00230.88           C  
ANISOU 2605  C   ASN A 377    36310  29540  21874  -6276   4896  -1699       C  
ATOM   2606  O   ASN A 377       6.176   3.017   2.101  1.00236.95           O  
ANISOU 2606  O   ASN A 377    36482  30736  22812  -6743   5221  -1921       O  
ATOM   2607  CB  ASN A 377       7.287   0.869   3.526  1.00242.95           C  
ANISOU 2607  CB  ASN A 377    39127  30191  22993  -7099   5535  -1246       C  
ATOM   2608  CG  ASN A 377       8.072  -0.429   3.523  1.00250.44           C  
ANISOU 2608  CG  ASN A 377    40937  30339  23881  -7272   5525   -936       C  
ATOM   2609  OD1 ASN A 377       8.221  -1.078   2.488  1.00253.05           O  
ANISOU 2609  OD1 ASN A 377    41155  30443  24549  -7540   5457   -985       O  
ATOM   2610  ND2 ASN A 377       8.581  -0.813   4.686  1.00252.25           N  
ANISOU 2610  ND2 ASN A 377    42061  30132  23649  -7076   5583   -620       N  
ATOM   2611  N   ASN A 378       7.468   4.429   3.262  1.00228.98           N  
ANISOU 2611  N   ASN A 378    35960  29494  21549  -5676   4575  -1770       N  
ATOM   2612  CA  ASN A 378       6.471   5.495   3.147  1.00232.15           C  
ANISOU 2612  CA  ASN A 378    35612  30612  21982  -5547   4691  -2090       C  
ATOM   2613  C   ASN A 378       6.738   6.565   2.080  1.00212.37           C  
ANISOU 2613  C   ASN A 378    32476  28311  19904  -5117   4180  -2296       C  
ATOM   2614  O   ASN A 378       5.826   6.945   1.346  1.00209.98           O  
ANISOU 2614  O   ASN A 378    31441  28555  19785  -5219   4306  -2562       O  
ATOM   2615  CB  ASN A 378       6.287   6.173   4.511  1.00249.38           C  
ANISOU 2615  CB  ASN A 378    38094  32961  23696  -5209   4814  -2085       C  
ATOM   2616  CG  ASN A 378       7.584   6.724   5.068  1.00254.07           C  
ANISOU 2616  CG  ASN A 378    39239  33095  24203  -4606   4253  -1929       C  
ATOM   2617  OD1 ASN A 378       8.671   6.367   4.611  1.00256.34           O  
ANISOU 2617  OD1 ASN A 378    39798  32886  24713  -4501   3844  -1762       O  
ATOM   2618  ND2 ASN A 378       7.477   7.595   6.065  1.00253.63           N  
ANISOU 2618  ND2 ASN A 378    39331  33229  23809  -4204   4229  -2008       N  
ATOM   2619  N   LYS A 379       7.979   7.035   1.984  1.00196.24           N  
ANISOU 2619  N   LYS A 379    30714  25846  18002  -4648   3613  -2176       N  
ATOM   2620  CA  LYS A 379       8.307   8.184   1.134  1.00176.43           C  
ANISOU 2620  CA  LYS A 379    27721  23477  15836  -4212   3139  -2339       C  
ATOM   2621  C   LYS A 379       9.429   7.948   0.122  1.00169.78           C  
ANISOU 2621  C   LYS A 379    26908  22221  15380  -4143   2689  -2222       C  
ATOM   2622  O   LYS A 379      10.360   7.178   0.358  1.00164.25           O  
ANISOU 2622  O   LYS A 379    26743  21022  14642  -4186   2559  -1992       O  
ATOM   2623  CB  LYS A 379       8.642   9.402   2.001  1.00166.91           C  
ANISOU 2623  CB  LYS A 379    26702  22285  14431  -3647   2870  -2394       C  
ATOM   2624  CG  LYS A 379       7.444   9.945   2.770  1.00163.39           C  
ANISOU 2624  CG  LYS A 379    26050  22375  13655  -3586   3268  -2596       C  
ATOM   2625  CD  LYS A 379       6.355  10.420   1.812  1.00150.71           C  
ANISOU 2625  CD  LYS A 379    23619  21370  12275  -3623   3411  -2879       C  
ATOM   2626  CE  LYS A 379       5.126  10.932   2.552  1.00147.76           C  
ANISOU 2626  CE  LYS A 379    22968  21608  11566  -3528   3827  -3110       C  
ATOM   2627  NZ  LYS A 379       4.411   9.854   3.295  1.00145.91           N  
ANISOU 2627  NZ  LYS A 379    22894  21544  11001  -4082   4448  -3042       N  
ATOM   2628  N   TRP A 380       9.309   8.631  -1.012  1.00169.31           N  
ANISOU 2628  N   TRP A 380    26266  22400  15665  -4003   2462  -2386       N  
ATOM   2629  CA  TRP A 380      10.263   8.539  -2.107  1.00164.34           C  
ANISOU 2629  CA  TRP A 380    25553  21482  15405  -3932   2069  -2310       C  
ATOM   2630  C   TRP A 380      10.984   9.879  -2.241  1.00143.27           C  
ANISOU 2630  C   TRP A 380    22808  18751  12877  -3410   1589  -2348       C  
ATOM   2631  O   TRP A 380      10.393  10.933  -1.995  1.00144.11           O  
ANISOU 2631  O   TRP A 380    22692  19163  12900  -3142   1590  -2514       O  
ATOM   2632  CB  TRP A 380       9.545   8.197  -3.412  1.00183.01           C  
ANISOU 2632  CB  TRP A 380    27333  24167  18035  -4232   2209  -2463       C  
ATOM   2633  CG  TRP A 380       9.205   6.752  -3.587  1.00201.93           C  
ANISOU 2633  CG  TRP A 380    29862  26457  20405  -4804   2568  -2413       C  
ATOM   2634  CD1 TRP A 380       7.980   6.174  -3.432  1.00212.88           C  
ANISOU 2634  CD1 TRP A 380    31033  28205  21646  -5273   3067  -2551       C  
ATOM   2635  CD2 TRP A 380      10.096   5.706  -3.981  1.00202.62           C  
ANISOU 2635  CD2 TRP A 380    30333  26036  20618  -4979   2462  -2233       C  
ATOM   2636  NE1 TRP A 380       8.055   4.828  -3.691  1.00212.74           N  
ANISOU 2636  NE1 TRP A 380    31293  27880  21658  -5776   3284  -2460       N  
ATOM   2637  CE2 TRP A 380       9.343   4.516  -4.032  1.00206.94           C  
ANISOU 2637  CE2 TRP A 380    30950  26595  21082  -5569   2913  -2264       C  
ATOM   2638  CE3 TRP A 380      11.457   5.659  -4.289  1.00197.66           C  
ANISOU 2638  CE3 TRP A 380    29988  24959  20155  -4692   2038  -2065       C  
ATOM   2639  CZ2 TRP A 380       9.910   3.293  -4.380  1.00207.73           C  
ANISOU 2639  CZ2 TRP A 380    31466  26209  21253  -5843   2940  -2125       C  
ATOM   2640  CZ3 TRP A 380      12.016   4.447  -4.634  1.00195.25           C  
ANISOU 2640  CZ3 TRP A 380    30034  24239  19914  -4920   2064  -1934       C  
ATOM   2641  CH2 TRP A 380      11.245   3.279  -4.676  1.00202.03           C  
ANISOU 2641  CH2 TRP A 380    31027  25055  20680  -5473   2506  -1961       C  
ATOM   2642  N   PRO A 381      12.266   9.848  -2.638  1.00122.72           N  
ANISOU 2642  N   PRO A 381    20394  15752  10483  -3270   1188  -2206       N  
ATOM   2643  CA  PRO A 381      13.055  11.082  -2.688  1.00115.03           C  
ANISOU 2643  CA  PRO A 381    19406  14664   9635  -2857    746  -2232       C  
ATOM   2644  C   PRO A 381      12.921  11.826  -4.013  1.00125.28           C  
ANISOU 2644  C   PRO A 381    20190  16150  11262  -2757    580  -2336       C  
ATOM   2645  O   PRO A 381      13.073  11.234  -5.081  1.00144.89           O  
ANISOU 2645  O   PRO A 381    22445  18629  13978  -2949    574  -2297       O  
ATOM   2646  CB  PRO A 381      14.485  10.579  -2.492  1.00101.42           C  
ANISOU 2646  CB  PRO A 381    18083  12488   7965  -2804    431  -2040       C  
ATOM   2647  CG  PRO A 381      14.479   9.201  -3.088  1.00 98.00           C  
ANISOU 2647  CG  PRO A 381    17670  11947   7617  -3144    631  -1932       C  
ATOM   2648  CD  PRO A 381      13.063   8.665  -3.009  1.00108.50           C  
ANISOU 2648  CD  PRO A 381    18847  13587   8792  -3484   1137  -2027       C  
ATOM   2649  N   LEU A 382      12.633  13.120  -3.934  1.00112.81           N  
ANISOU 2649  N   LEU A 382    18478  14716   9671  -2434    449  -2468       N  
ATOM   2650  CA  LEU A 382      12.499  13.945  -5.128  1.00112.10           C  
ANISOU 2650  CA  LEU A 382    17986  14769   9838  -2274    282  -2544       C  
ATOM   2651  C   LEU A 382      13.854  14.199  -5.786  1.00115.23           C  
ANISOU 2651  C   LEU A 382    18469  14802  10509  -2220   -106  -2406       C  
ATOM   2652  O   LEU A 382      14.857  14.387  -5.099  1.00123.10           O  
ANISOU 2652  O   LEU A 382    19818  15478  11478  -2139   -346  -2328       O  
ATOM   2653  CB  LEU A 382      11.812  15.267  -4.776  1.00103.53           C  
ANISOU 2653  CB  LEU A 382    16833  13880   8623  -1895    257  -2718       C  
ATOM   2654  CG  LEU A 382      11.636  16.316  -5.871  1.00 98.17           C  
ANISOU 2654  CG  LEU A 382    15856  13301   8141  -1624     68  -2785       C  
ATOM   2655  CD1 LEU A 382      10.336  17.042  -5.653  1.00 98.86           C  
ANISOU 2655  CD1 LEU A 382    15718  13811   8033  -1324    252  -3004       C  
ATOM   2656  CD2 LEU A 382      12.783  17.305  -5.857  1.00101.28           C  
ANISOU 2656  CD2 LEU A 382    16562  13252   8670  -1418   -327  -2707       C  
ATOM   2657  N   ILE A 383      13.875  14.212  -7.117  1.00103.55           N  
ANISOU 2657  N   ILE A 383    16647  13418   9278  -2268   -165  -2391       N  
ATOM   2658  CA  ILE A 383      15.103  14.476  -7.859  1.00 98.81           C  
ANISOU 2658  CA  ILE A 383    16067  12540   8937  -2241   -482  -2265       C  
ATOM   2659  C   ILE A 383      14.951  15.695  -8.758  1.00112.24           C  
ANISOU 2659  C   ILE A 383    17558  14313  10775  -2012   -632  -2305       C  
ATOM   2660  O   ILE A 383      13.994  15.794  -9.528  1.00122.20           O  
ANISOU 2660  O   ILE A 383    18492  15901  12038  -1960   -491  -2390       O  
ATOM   2661  CB  ILE A 383      15.525  13.280  -8.729  1.00 91.36           C  
ANISOU 2661  CB  ILE A 383    14987  11571   8154  -2509   -430  -2169       C  
ATOM   2662  CG1 ILE A 383      15.430  11.973  -7.947  1.00 88.56           C  
ANISOU 2662  CG1 ILE A 383    14876  11140   7634  -2741   -215  -2130       C  
ATOM   2663  CG2 ILE A 383      16.940  13.468  -9.230  1.00101.38           C  
ANISOU 2663  CG2 ILE A 383    16311  12562   9645  -2476   -739  -2040       C  
ATOM   2664  CD1 ILE A 383      15.385  10.751  -8.832  1.00 86.26           C  
ANISOU 2664  CD1 ILE A 383    14444  10878   7454  -3018    -65  -2101       C  
ATOM   2665  N   LEU A 384      15.905  16.616  -8.667  1.00115.88           N  
ANISOU 2665  N   LEU A 384    18223  14467  11339  -1881   -924  -2247       N  
ATOM   2666  CA  LEU A 384      15.896  17.799  -9.520  1.00113.83           C  
ANISOU 2666  CA  LEU A 384    17878  14171  11202  -1684  -1067  -2244       C  
ATOM   2667  C   LEU A 384      16.983  17.765 -10.582  1.00104.77           C  
ANISOU 2667  C   LEU A 384    16636  12857  10314  -1829  -1235  -2089       C  
ATOM   2668  O   LEU A 384      18.180  17.748 -10.281  1.00 83.39           O  
ANISOU 2668  O   LEU A 384    14088   9882   7713  -1951  -1427  -2013       O  
ATOM   2669  CB  LEU A 384      16.017  19.066  -8.676  1.00129.26           C  
ANISOU 2669  CB  LEU A 384    20168  15886  13061  -1441  -1234  -2321       C  
ATOM   2670  CG  LEU A 384      14.682  19.424  -8.023  1.00132.32           C  
ANISOU 2670  CG  LEU A 384    20557  16532  13186  -1174  -1042  -2500       C  
ATOM   2671  CD1 LEU A 384      14.884  20.124  -6.705  1.00124.89           C  
ANISOU 2671  CD1 LEU A 384    20027  15357  12068  -1013  -1154  -2604       C  
ATOM   2672  CD2 LEU A 384      13.854  20.287  -8.960  1.00128.51           C  
ANISOU 2672  CD2 LEU A 384    19883  16229  12715   -873  -1023  -2552       C  
ATOM   2673  N   LEU A 385      16.531  17.757 -11.832  1.00115.40           N  
ANISOU 2673  N   LEU A 385    17695  14414  11737  -1802  -1159  -2060       N  
ATOM   2674  CA  LEU A 385      17.404  17.705 -12.991  1.00122.51           C  
ANISOU 2674  CA  LEU A 385    18471  15232  12846  -1923  -1260  -1916       C  
ATOM   2675  C   LEU A 385      16.918  18.717 -14.017  1.00126.41           C  
ANISOU 2675  C   LEU A 385    18886  15800  13344  -1700  -1285  -1885       C  
ATOM   2676  O   LEU A 385      15.724  19.024 -14.082  1.00102.45           O  
ANISOU 2676  O   LEU A 385    15750  13020  10155  -1461  -1185  -1996       O  
ATOM   2677  CB  LEU A 385      17.415  16.300 -13.596  1.00108.15           C  
ANISOU 2677  CB  LEU A 385    16402  13614  11078  -2143  -1117  -1899       C  
ATOM   2678  CG  LEU A 385      18.643  15.427 -13.350  1.00 87.83           C  
ANISOU 2678  CG  LEU A 385    13910  10844   8618  -2352  -1197  -1813       C  
ATOM   2679  CD1 LEU A 385      18.405  14.020 -13.869  1.00 83.16           C  
ANISOU 2679  CD1 LEU A 385    13147  10423   8029  -2523  -1021  -1834       C  
ATOM   2680  CD2 LEU A 385      19.867  16.040 -13.996  1.00 79.02           C  
ANISOU 2680  CD2 LEU A 385    12781   9549   7694  -2384  -1391  -1687       C  
ATOM   2681  N   HIS A 386      17.843  19.246 -14.807  1.00136.61           N  
ANISOU 2681  N   HIS A 386    20228  16887  14792  -1762  -1414  -1733       N  
ATOM   2682  CA  HIS A 386      17.490  20.234 -15.813  1.00148.77           C  
ANISOU 2682  CA  HIS A 386    21787  18432  16308  -1543  -1440  -1656       C  
ATOM   2683  C   HIS A 386      16.633  19.591 -16.895  1.00139.36           C  
ANISOU 2683  C   HIS A 386    20240  17668  15041  -1465  -1303  -1685       C  
ATOM   2684  O   HIS A 386      16.690  18.379 -17.097  1.00145.96           O  
ANISOU 2684  O   HIS A 386    20834  18706  15918  -1683  -1202  -1724       O  
ATOM   2685  CB  HIS A 386      18.738  20.861 -16.421  1.00164.19           C  
ANISOU 2685  CB  HIS A 386    23886  20065  18431  -1707  -1562  -1469       C  
ATOM   2686  CG  HIS A 386      18.484  22.179 -17.080  1.00187.64           C  
ANISOU 2686  CG  HIS A 386    27092  22857  21343  -1471  -1611  -1367       C  
ATOM   2687  ND1 HIS A 386      18.105  22.291 -18.401  1.00202.83           N  
ANISOU 2687  ND1 HIS A 386    28893  24971  23205  -1326  -1547  -1256       N  
ATOM   2688  CD2 HIS A 386      18.549  23.442 -16.599  1.00195.58           C  
ANISOU 2688  CD2 HIS A 386    28509  23485  22319  -1335  -1720  -1359       C  
ATOM   2689  CE1 HIS A 386      17.949  23.567 -18.705  1.00209.79           C  
ANISOU 2689  CE1 HIS A 386    30117  25585  24009  -1091  -1610  -1158       C  
ATOM   2690  NE2 HIS A 386      18.214  24.287 -17.629  1.00207.99           N  
ANISOU 2690  NE2 HIS A 386    30230  24988  23811  -1102  -1710  -1222       N  
ATOM   2691  N   LYS A 387      15.838  20.399 -17.588  1.00124.81           N  
ANISOU 2691  N   LYS A 387    18391  15957  13072  -1136  -1312  -1680       N  
ATOM   2692  CA  LYS A 387      15.069  19.895 -18.719  1.00107.05           C  
ANISOU 2692  CA  LYS A 387    15796  14149  10731  -1037  -1229  -1721       C  
ATOM   2693  C   LYS A 387      15.981  19.323 -19.788  1.00114.45           C  
ANISOU 2693  C   LYS A 387    16622  15071  11795  -1289  -1224  -1572       C  
ATOM   2694  O   LYS A 387      15.642  18.320 -20.412  1.00130.97           O  
ANISOU 2694  O   LYS A 387    18400  17500  13861  -1397  -1133  -1657       O  
ATOM   2695  CB  LYS A 387      14.192  20.987 -19.325  1.00 98.23           C  
ANISOU 2695  CB  LYS A 387    14741  13155   9428   -565  -1291  -1716       C  
ATOM   2696  CG  LYS A 387      13.098  21.473 -18.407  1.00102.59           C  
ANISOU 2696  CG  LYS A 387    15314  13852   9815   -231  -1274  -1912       C  
ATOM   2697  CD  LYS A 387      12.203  22.458 -19.125  1.00118.33           C  
ANISOU 2697  CD  LYS A 387    17337  16025  11600    317  -1352  -1919       C  
ATOM   2698  CE  LYS A 387      11.390  21.756 -20.189  1.00112.39           C  
ANISOU 2698  CE  LYS A 387    16097  15874  10731    395  -1304  -2021       C  
ATOM   2699  NZ  LYS A 387      10.508  20.738 -19.562  1.00108.85           N  
ANISOU 2699  NZ  LYS A 387    15205  15910  10244    233  -1148  -2304       N  
ATOM   2700  N   ARG A 388      17.130  19.959 -20.001  1.00105.36           N  
ANISOU 2700  N   ARG A 388    15721  13543  10770  -1397  -1309  -1371       N  
ATOM   2701  CA  ARG A 388      18.116  19.428 -20.935  1.00112.40           C  
ANISOU 2701  CA  ARG A 388    16493  14435  11780  -1643  -1280  -1234       C  
ATOM   2702  C   ARG A 388      18.467  17.982 -20.605  1.00103.28           C  
ANISOU 2702  C   ARG A 388    15109  13409  10724  -1922  -1208  -1342       C  
ATOM   2703  O   ARG A 388      18.446  17.119 -21.478  1.00108.08           O  
ANISOU 2703  O   ARG A 388    15481  14265  11319  -2000  -1128  -1368       O  
ATOM   2704  CB  ARG A 388      19.381  20.274 -20.971  1.00127.02           C  
ANISOU 2704  CB  ARG A 388    18611  15877  13773  -1805  -1356  -1034       C  
ATOM   2705  CG  ARG A 388      20.213  19.934 -22.194  1.00147.90           C  
ANISOU 2705  CG  ARG A 388    21108  18610  16478  -1976  -1288   -880       C  
ATOM   2706  CD  ARG A 388      21.424  20.829 -22.331  1.00165.09           C  
ANISOU 2706  CD  ARG A 388    23508  20433  18785  -2186  -1321   -682       C  
ATOM   2707  NE  ARG A 388      21.045  22.237 -22.283  1.00174.76           N  
ANISOU 2707  NE  ARG A 388    25130  21354  19916  -1995  -1378   -581       N  
ATOM   2708  CZ  ARG A 388      21.004  23.036 -23.345  1.00178.80           C  
ANISOU 2708  CZ  ARG A 388    25841  21786  20310  -1878  -1327   -377       C  
ATOM   2709  NH1 ARG A 388      21.333  22.568 -24.545  1.00175.41           N  
ANISOU 2709  NH1 ARG A 388    25213  21600  19835  -1948  -1213   -258       N  
ATOM   2710  NH2 ARG A 388      20.645  24.307 -23.209  1.00183.84           N  
ANISOU 2710  NH2 ARG A 388    26922  22081  20850  -1671  -1386   -288       N  
ATOM   2711  N   ARG A 389      18.809  17.724 -19.350  1.00103.35           N  
ANISOU 2711  N   ARG A 389    15233  13227  10808  -2050  -1242  -1407       N  
ATOM   2712  CA  ARG A 389      19.115  16.366 -18.920  1.00109.89           C  
ANISOU 2712  CA  ARG A 389    15941  14116  11696  -2264  -1179  -1493       C  
ATOM   2713  C   ARG A 389      17.892  15.460 -19.016  1.00106.31           C  
ANISOU 2713  C   ARG A 389    15286  13996  11112  -2254  -1028  -1670       C  
ATOM   2714  O   ARG A 389      17.994  14.306 -19.432  1.00111.80           O  
ANISOU 2714  O   ARG A 389    15836  14812  11831  -2419   -939  -1726       O  
ATOM   2715  CB  ARG A 389      19.620  16.369 -17.481  1.00120.04           C  
ANISOU 2715  CB  ARG A 389    17447  15138  13026  -2342  -1263  -1521       C  
ATOM   2716  CG  ARG A 389      21.047  16.822 -17.273  1.00126.28           C  
ANISOU 2716  CG  ARG A 389    18353  15651  13976  -2466  -1420  -1405       C  
ATOM   2717  CD  ARG A 389      22.010  15.773 -17.792  1.00114.49           C  
ANISOU 2717  CD  ARG A 389    16676  14228  12598  -2625  -1401  -1365       C  
ATOM   2718  NE  ARG A 389      23.396  16.127 -17.513  1.00114.82           N  
ANISOU 2718  NE  ARG A 389    16745  14091  12790  -2750  -1553  -1293       N  
ATOM   2719  CZ  ARG A 389      24.160  16.831 -18.335  1.00117.19           C  
ANISOU 2719  CZ  ARG A 389    16964  14362  13199  -2847  -1576  -1172       C  
ATOM   2720  NH1 ARG A 389      23.664  17.248 -19.488  1.00125.33           N  
ANISOU 2720  NH1 ARG A 389    17941  15499  14178  -2787  -1462  -1085       N  
ATOM   2721  NH2 ARG A 389      25.412  17.115 -18.003  1.00108.99           N  
ANISOU 2721  NH2 ARG A 389    15895  13213  12302  -3009  -1708  -1144       N  
ATOM   2722  N   VAL A 390      16.737  15.994 -18.635  1.00 98.26           N  
ANISOU 2722  N   VAL A 390    14256  13131   9948  -2066   -996  -1778       N  
ATOM   2723  CA  VAL A 390      15.498  15.232 -18.660  1.00103.44           C  
ANISOU 2723  CA  VAL A 390    14663  14164  10474  -2094   -840  -1980       C  
ATOM   2724  C   VAL A 390      15.072  14.890 -20.091  1.00119.39           C  
ANISOU 2724  C   VAL A 390    16390  16527  12446  -2070   -808  -2029       C  
ATOM   2725  O   VAL A 390      14.664  13.761 -20.370  1.00124.53           O  
ANISOU 2725  O   VAL A 390    16841  17399  13077  -2281   -687  -2176       O  
ATOM   2726  CB  VAL A 390      14.371  16.003 -17.938  1.00 97.66           C  
ANISOU 2726  CB  VAL A 390    13933  13589   9584  -1846   -814  -2102       C  
ATOM   2727  CG1 VAL A 390      12.999  15.470 -18.318  1.00100.59           C  
ANISOU 2727  CG1 VAL A 390    13927  14483   9811  -1834   -667  -2327       C  
ATOM   2728  CG2 VAL A 390      14.578  15.939 -16.429  1.00 89.48           C  
ANISOU 2728  CG2 VAL A 390    13153  12306   8541  -1930   -786  -2123       C  
ATOM   2729  N   LYS A 391      15.200  15.851 -21.001  1.00121.73           N  
ANISOU 2729  N   LYS A 391    16703  16842  12706  -1825   -918  -1905       N  
ATOM   2730  CA  LYS A 391      14.797  15.641 -22.390  1.00110.65           C  
ANISOU 2730  CA  LYS A 391    15053  15785  11203  -1742   -915  -1943       C  
ATOM   2731  C   LYS A 391      15.674  14.605 -23.086  1.00103.33           C  
ANISOU 2731  C   LYS A 391    14066  14814  10381  -2013   -867  -1909       C  
ATOM   2732  O   LYS A 391      15.164  13.738 -23.791  1.00129.43           O  
ANISOU 2732  O   LYS A 391    17131  18432  13616  -2109   -802  -2073       O  
ATOM   2733  CB  LYS A 391      14.824  16.958 -23.169  1.00107.47           C  
ANISOU 2733  CB  LYS A 391    14783  15349  10701  -1390  -1038  -1770       C  
ATOM   2734  CG  LYS A 391      13.591  17.820 -22.953  1.00110.14           C  
ANISOU 2734  CG  LYS A 391    15081  15919  10849   -995  -1090  -1875       C  
ATOM   2735  CD  LYS A 391      13.507  18.941 -23.975  1.00113.76           C  
ANISOU 2735  CD  LYS A 391    15689  16384  11151   -600  -1209  -1706       C  
ATOM   2736  CE  LYS A 391      12.367  19.890 -23.639  1.00122.76           C  
ANISOU 2736  CE  LYS A 391    16853  17695  12096   -118  -1284  -1805       C  
ATOM   2737  NZ  LYS A 391      11.076  19.168 -23.468  1.00124.96           N  
ANISOU 2737  NZ  LYS A 391    16654  18571  12254    -74  -1223  -2134       N  
ATOM   2738  N   THR A 392      16.988  14.699 -22.891  1.00 78.72           N  
ANISOU 2738  N   THR A 392    11155  11331   7424  -2129   -905  -1723       N  
ATOM   2739  CA  THR A 392      17.928  13.733 -23.463  1.00 77.65           C  
ANISOU 2739  CA  THR A 392    10967  11150   7387  -2331   -859  -1697       C  
ATOM   2740  C   THR A 392      17.655  12.339 -22.916  1.00105.22           C  
ANISOU 2740  C   THR A 392    14406  14667  10905  -2561   -753  -1889       C  
ATOM   2741  O   THR A 392      17.803  11.337 -23.616  1.00 91.47           O  
ANISOU 2741  O   THR A 392    12565  13029   9160  -2683   -686  -1981       O  
ATOM   2742  CB  THR A 392      19.387  14.118 -23.182  1.00 98.11           C  
ANISOU 2742  CB  THR A 392    13734  13397  10148  -2405   -924  -1494       C  
ATOM   2743  OG1 THR A 392      19.677  15.373 -23.808  1.00102.91           O  
ANISOU 2743  OG1 THR A 392    14430  13944  10726  -2265   -983  -1304       O  
ATOM   2744  CG2 THR A 392      20.337  13.063 -23.729  1.00 89.62           C  
ANISOU 2744  CG2 THR A 392    12567  12326   9157  -2553   -870  -1498       C  
ATOM   2745  N   LEU A 393      17.270  12.282 -21.647  1.00112.38           N  
ANISOU 2745  N   LEU A 393    15431  15450  11820  -2620   -728  -1948       N  
ATOM   2746  CA  LEU A 393      16.870  11.025 -21.030  1.00110.28           C  
ANISOU 2746  CA  LEU A 393    15185  15174  11541  -2857   -592  -2110       C  
ATOM   2747  C   LEU A 393      15.567  10.497 -21.638  1.00 98.27           C  
ANISOU 2747  C   LEU A 393    13393  14057   9889  -2950   -474  -2347       C  
ATOM   2748  O   LEU A 393      15.425   9.297 -21.859  1.00 97.09           O  
ANISOU 2748  O   LEU A 393    13220  13933   9737  -3196   -359  -2490       O  
ATOM   2749  CB  LEU A 393      16.724  11.207 -19.520  1.00116.82           C  
ANISOU 2749  CB  LEU A 393    16226  15800  12359  -2882   -575  -2097       C  
ATOM   2750  CG  LEU A 393      17.895  10.650 -18.710  1.00121.02           C  
ANISOU 2750  CG  LEU A 393    17038  15952  12991  -2967   -621  -1989       C  
ATOM   2751  CD1 LEU A 393      17.963   9.153 -18.871  1.00128.73           C  
ANISOU 2751  CD1 LEU A 393    18074  16872  13968  -3179   -490  -2081       C  
ATOM   2752  CD2 LEU A 393      19.213  11.288 -19.149  1.00122.07           C  
ANISOU 2752  CD2 LEU A 393    17193  15929  13260  -2848   -794  -1812       C  
ATOM   2753  N   LEU A 394      14.627  11.399 -21.910  1.00 80.24           N  
ANISOU 2753  N   LEU A 394    10911  12090   7486  -2743   -514  -2404       N  
ATOM   2754  CA  LEU A 394      13.377  11.058 -22.585  1.00 89.87           C  
ANISOU 2754  CA  LEU A 394    11786  13798   8564  -2782   -449  -2656       C  
ATOM   2755  C   LEU A 394      13.623  10.521 -23.995  1.00116.53           C  
ANISOU 2755  C   LEU A 394    15022  17340  11912  -2818   -485  -2711       C  
ATOM   2756  O   LEU A 394      12.911   9.637 -24.474  1.00109.54           O  
ANISOU 2756  O   LEU A 394    13920  16743  10956  -3031   -404  -2963       O  
ATOM   2757  CB  LEU A 394      12.456  12.277 -22.659  1.00100.13           C  
ANISOU 2757  CB  LEU A 394    12909  15418   9721  -2425   -536  -2685       C  
ATOM   2758  CG  LEU A 394      11.653  12.648 -21.410  1.00 96.84           C  
ANISOU 2758  CG  LEU A 394    12481  15068   9248  -2381   -454  -2774       C  
ATOM   2759  CD1 LEU A 394      10.581  13.682 -21.744  1.00105.14           C  
ANISOU 2759  CD1 LEU A 394    13276  16554  10119  -1972   -541  -2875       C  
ATOM   2760  CD2 LEU A 394      11.041  11.416 -20.755  1.00 88.24           C  
ANISOU 2760  CD2 LEU A 394    11283  14091   8153  -2806   -227  -2991       C  
ATOM   2761  N   GLU A 395      14.630  11.082 -24.657  1.00135.29           N  
ANISOU 2761  N   GLU A 395    17528  19546  14332  -2630   -596  -2487       N  
ATOM   2762  CA  GLU A 395      14.977  10.703 -26.021  1.00132.30           C  
ANISOU 2762  CA  GLU A 395    17051  19325  13894  -2611   -624  -2507       C  
ATOM   2763  C   GLU A 395      15.480   9.266 -26.082  1.00136.71           C  
ANISOU 2763  C   GLU A 395    17683  19722  14540  -2920   -516  -2629       C  
ATOM   2764  O   GLU A 395      15.244   8.565 -27.061  1.00150.80           O  
ANISOU 2764  O   GLU A 395    19330  21733  16234  -3000   -494  -2807       O  
ATOM   2765  CB  GLU A 395      16.039  11.649 -26.581  1.00125.19           C  
ANISOU 2765  CB  GLU A 395    16304  18243  13019  -2382   -717  -2210       C  
ATOM   2766  CG  GLU A 395      15.492  12.911 -27.230  1.00118.35           C  
ANISOU 2766  CG  GLU A 395    15388  17604  11976  -2032   -826  -2112       C  
ATOM   2767  CD  GLU A 395      16.596  13.869 -27.631  1.00123.78           C  
ANISOU 2767  CD  GLU A 395    16308  18022  12702  -1892   -871  -1788       C  
ATOM   2768  OE1 GLU A 395      17.727  13.401 -27.891  1.00126.04           O  
ANISOU 2768  OE1 GLU A 395    16657  18127  13103  -2055   -815  -1692       O  
ATOM   2769  OE2 GLU A 395      16.336  15.089 -27.681  1.00125.79           O  
ANISOU 2769  OE2 GLU A 395    16690  18243  12864  -1623   -952  -1637       O  
ATOM   2770  N   ASN A 396      16.178   8.828 -25.038  1.00125.90           N  
ANISOU 2770  N   ASN A 396    16561  17951  13323  -3063   -461  -2542       N  
ATOM   2771  CA  ASN A 396      16.639   7.448 -24.979  1.00117.57           C  
ANISOU 2771  CA  ASN A 396    15659  16680  12332  -3303   -360  -2647       C  
ATOM   2772  C   ASN A 396      15.451   6.518 -24.767  1.00116.40           C  
ANISOU 2772  C   ASN A 396    15432  16686  12109  -3613   -221  -2939       C  
ATOM   2773  O   ASN A 396      14.666   6.712 -23.840  1.00111.85           O  
ANISOU 2773  O   ASN A 396    14832  16157  11511  -3714   -152  -2986       O  
ATOM   2774  CB  ASN A 396      17.675   7.257 -23.869  1.00114.26           C  
ANISOU 2774  CB  ASN A 396    15548  15810  12058  -3312   -365  -2472       C  
ATOM   2775  CG  ASN A 396      18.444   5.948 -24.005  1.00107.91           C  
ANISOU 2775  CG  ASN A 396    14948  14749  11305  -3417   -303  -2530       C  
ATOM   2776  OD1 ASN A 396      17.859   4.866 -24.058  1.00106.38           O  
ANISOU 2776  OD1 ASN A 396    14833  14528  11060  -3653   -179  -2737       O  
ATOM   2777  ND2 ASN A 396      19.765   6.047 -24.060  1.00101.33           N  
ANISOU 2777  ND2 ASN A 396    14205  13727  10568  -3242   -386  -2361       N  
ATOM   2778  N   PRO A 397      15.311   5.511 -25.642  1.00125.53           N  
ANISOU 2778  N   PRO A 397    16546  17935  13214  -3786   -165  -3153       N  
ATOM   2779  CA  PRO A 397      14.183   4.573 -25.629  1.00132.93           C  
ANISOU 2779  CA  PRO A 397    17386  19041  14078  -4161    -25  -3475       C  
ATOM   2780  C   PRO A 397      14.183   3.687 -24.389  1.00125.04           C  
ANISOU 2780  C   PRO A 397    16728  17631  13152  -4473    153  -3480       C  
ATOM   2781  O   PRO A 397      13.117   3.383 -23.847  1.00133.36           O  
ANISOU 2781  O   PRO A 397    17690  18828  14153  -4786    302  -3657       O  
ATOM   2782  CB  PRO A 397      14.405   3.741 -26.893  1.00148.99           C  
ANISOU 2782  CB  PRO A 397    19403  21153  16054  -4228    -38  -3667       C  
ATOM   2783  CG  PRO A 397      15.873   3.843 -27.161  1.00143.42           C  
ANISOU 2783  CG  PRO A 397    18923  20141  15431  -3945   -112  -3419       C  
ATOM   2784  CD  PRO A 397      16.251   5.229 -26.741  1.00128.16           C  
ANISOU 2784  CD  PRO A 397    16919  18232  13546  -3643   -223  -3118       C  
ATOM   2785  N   THR A 398      15.375   3.287 -23.954  1.00123.18           N  
ANISOU 2785  N   THR A 398    16876  16912  13013  -4374    142  -3286       N  
ATOM   2786  CA  THR A 398      15.550   2.444 -22.775  1.00133.03           C  
ANISOU 2786  CA  THR A 398    18546  17705  14293  -4583    286  -3238       C  
ATOM   2787  C   THR A 398      14.940   3.083 -21.528  1.00125.81           C  
ANISOU 2787  C   THR A 398    17623  16827  13350  -4634    350  -3145       C  
ATOM   2788  O   THR A 398      14.108   2.486 -20.839  1.00118.75           O  
ANISOU 2788  O   THR A 398    16834  15894  12392  -4986    558  -3266       O  
ATOM   2789  CB  THR A 398      17.053   2.175 -22.494  1.00 87.39           C  
ANISOU 2789  CB  THR A 398    13124  11477   8601  -4313    189  -3013       C  
ATOM   2790  OG1 THR A 398      17.716   1.734 -23.686  1.00 85.57           O  
ANISOU 2790  OG1 THR A 398    12862  11265   8386  -4183    127  -3087       O  
ATOM   2791  CG2 THR A 398      17.228   1.153 -21.380  1.00 98.60           C  
ANISOU 2791  CG2 THR A 398    15055  12405  10003  -4483    325  -2971       C  
ATOM   2792  N   HIS A 399      15.366   4.314 -21.261  1.00117.75           N  
ANISOU 2792  N   HIS A 399    16490  15881  12367  -4293    186  -2939       N  
ATOM   2793  CA  HIS A 399      15.035   5.016 -20.028  1.00110.41           C  
ANISOU 2793  CA  HIS A 399    15618  14926  11404  -4247    211  -2829       C  
ATOM   2794  C   HIS A 399      13.653   5.676 -19.996  1.00118.31           C  
ANISOU 2794  C   HIS A 399    16242  16406  12305  -4311    285  -2991       C  
ATOM   2795  O   HIS A 399      13.115   5.916 -18.917  1.00132.18           O  
ANISOU 2795  O   HIS A 399    18058  18169  13994  -4375    395  -2980       O  
ATOM   2796  CB  HIS A 399      16.102   6.082 -19.762  1.00103.43           C  
ANISOU 2796  CB  HIS A 399    14799  13896  10603  -3871    -10  -2572       C  
ATOM   2797  CG  HIS A 399      17.508   5.582 -19.915  1.00107.43           C  
ANISOU 2797  CG  HIS A 399    15549  14061  11209  -3747   -114  -2436       C  
ATOM   2798  ND1 HIS A 399      17.893   4.319 -19.529  1.00119.82           N  
ANISOU 2798  ND1 HIS A 399    17470  15289  12768  -3883    -20  -2456       N  
ATOM   2799  CD2 HIS A 399      18.616   6.181 -20.416  1.00 93.93           C  
ANISOU 2799  CD2 HIS A 399    13771  12319   9598  -3489   -295  -2286       C  
ATOM   2800  CE1 HIS A 399      19.184   4.158 -19.780  1.00115.40           C  
ANISOU 2800  CE1 HIS A 399    17019  14534  12294  -3656   -160  -2338       C  
ATOM   2801  NE2 HIS A 399      19.643   5.272 -20.317  1.00 95.26           N  
ANISOU 2801  NE2 HIS A 399    14186  12190   9817  -3446   -317  -2240       N  
ATOM   2802  N   ARG A 400      13.085   5.958 -21.167  1.00113.01           N  
ANISOU 2802  N   ARG A 400    15181  16162  11597  -4260    221  -3151       N  
ATOM   2803  CA  ARG A 400      11.912   6.835 -21.267  1.00119.35           C  
ANISOU 2803  CA  ARG A 400    15573  17483  12292  -4150    211  -3285       C  
ATOM   2804  C   ARG A 400      10.723   6.446 -20.382  1.00138.44           C  
ANISOU 2804  C   ARG A 400    17872  20112  14618  -4474    454  -3482       C  
ATOM   2805  O   ARG A 400      10.106   7.313 -19.757  1.00144.36           O  
ANISOU 2805  O   ARG A 400    18463  21096  15292  -4295    465  -3482       O  
ATOM   2806  CB  ARG A 400      11.440   6.926 -22.720  1.00120.23           C  
ANISOU 2806  CB  ARG A 400    15301  18046  12335  -4073    106  -3468       C  
ATOM   2807  CG  ARG A 400      10.268   7.878 -22.904  1.00120.37           C  
ANISOU 2807  CG  ARG A 400    14882  18640  12214  -3852     48  -3609       C  
ATOM   2808  CD  ARG A 400      10.063   8.289 -24.350  1.00114.57           C  
ANISOU 2808  CD  ARG A 400    13847  18307  11376  -3594   -141  -3694       C  
ATOM   2809  NE  ARG A 400       9.042   9.327 -24.492  1.00119.97           N  
ANISOU 2809  NE  ARG A 400    14164  19516  11903  -3251   -241  -3790       N  
ATOM   2810  CZ  ARG A 400       7.743   9.138 -24.274  1.00131.72           C  
ANISOU 2810  CZ  ARG A 400    15237  21526  13283  -3397   -144  -4100       C  
ATOM   2811  NH1 ARG A 400       7.287   7.940 -23.933  1.00124.07           N  
ANISOU 2811  NH1 ARG A 400    14187  20601  12352  -3958     78  -4341       N  
ATOM   2812  NH2 ARG A 400       6.893  10.145 -24.417  1.00146.47           N  
ANISOU 2812  NH2 ARG A 400    16776  23883  14995  -2980   -263  -4179       N  
ATOM   2813  N   ASN A 401      10.399   5.158 -20.324  1.00155.79           N  
ANISOU 2813  N   ASN A 401    20162  22221  16810  -4956    666  -3655       N  
ATOM   2814  CA  ASN A 401       9.271   4.709 -19.509  1.00169.06           C  
ANISOU 2814  CA  ASN A 401    21728  24110  18396  -5357    951  -3845       C  
ATOM   2815  C   ASN A 401       9.500   4.973 -18.023  1.00167.23           C  
ANISOU 2815  C   ASN A 401    21847  23565  18128  -5306   1067  -3632       C  
ATOM   2816  O   ASN A 401       8.582   5.370 -17.306  1.00170.57           O  
ANISOU 2816  O   ASN A 401    22060  24310  18440  -5357   1223  -3725       O  
ATOM   2817  CB  ASN A 401       8.986   3.221 -19.742  1.00178.86           C  
ANISOU 2817  CB  ASN A 401    23105  25210  19642  -5948   1175  -4054       C  
ATOM   2818  CG  ASN A 401      10.185   2.340 -19.450  1.00180.15           C  
ANISOU 2818  CG  ASN A 401    23919  24644  19885  -6010   1192  -3842       C  
ATOM   2819  OD1 ASN A 401      11.324   2.701 -19.744  1.00184.19           O  
ANISOU 2819  OD1 ASN A 401    24618  24886  20480  -5611    962  -3624       O  
ATOM   2820  ND2 ASN A 401       9.932   1.173 -18.868  1.00176.21           N  
ANISOU 2820  ND2 ASN A 401    23773  23831  19349  -6509   1475  -3910       N  
ATOM   2821  N   LEU A 402      10.730   4.754 -17.569  1.00155.91           N  
ANISOU 2821  N   LEU A 402    20930  21542  16765  -5178    984  -3363       N  
ATOM   2822  CA  LEU A 402      11.069   4.918 -16.161  1.00134.07           C  
ANISOU 2822  CA  LEU A 402    18557  18447  13935  -5113   1059  -3160       C  
ATOM   2823  C   LEU A 402      11.045   6.381 -15.712  1.00118.90           C  
ANISOU 2823  C   LEU A 402    16482  16713  11982  -4667    893  -3062       C  
ATOM   2824  O   LEU A 402      10.443   6.712 -14.688  1.00119.62           O  
ANISOU 2824  O   LEU A 402    16593  16915  11941  -4681   1044  -3077       O  
ATOM   2825  CB  LEU A 402      12.448   4.311 -15.889  1.00128.60           C  
ANISOU 2825  CB  LEU A 402    18417  17131  13315  -5029    954  -2925       C  
ATOM   2826  CG  LEU A 402      13.058   4.501 -14.500  1.00127.24           C  
ANISOU 2826  CG  LEU A 402    18696  16589  13062  -4872    942  -2694       C  
ATOM   2827  CD1 LEU A 402      12.114   3.974 -13.426  1.00137.32           C  
ANISOU 2827  CD1 LEU A 402    20144  17882  14149  -5232   1290  -2752       C  
ATOM   2828  CD2 LEU A 402      14.411   3.814 -14.411  1.00117.57           C  
ANISOU 2828  CD2 LEU A 402    17942  14830  11900  -4748    803  -2505       C  
ATOM   2829  N   VAL A 403      11.684   7.255 -16.485  1.00107.43           N  
ANISOU 2829  N   VAL A 403    14904  15283  10631  -4282    603  -2967       N  
ATOM   2830  CA  VAL A 403      11.776   8.669 -16.123  1.00106.64           C  
ANISOU 2830  CA  VAL A 403    14751  15258  10510  -3859    427  -2864       C  
ATOM   2831  C   VAL A 403      10.409   9.338 -16.143  1.00122.68           C  
ANISOU 2831  C   VAL A 403    16355  17848  12410  -3765    517  -3072       C  
ATOM   2832  O   VAL A 403      10.093  10.152 -15.274  1.00125.59           O  
ANISOU 2832  O   VAL A 403    16765  18274  12682  -3545    529  -3054       O  
ATOM   2833  CB  VAL A 403      12.731   9.439 -17.056  1.00 96.18           C  
ANISOU 2833  CB  VAL A 403    13406  13824   9316  -3529    133  -2714       C  
ATOM   2834  CG1 VAL A 403      12.785  10.914 -16.677  1.00 83.61           C  
ANISOU 2834  CG1 VAL A 403    11830  12243   7696  -3133    -33  -2617       C  
ATOM   2835  CG2 VAL A 403      14.118   8.824 -17.020  1.00 82.32           C  
ANISOU 2835  CG2 VAL A 403    11999  11592   7685  -3580     39  -2532       C  
ATOM   2836  N   GLU A 404       9.595   8.985 -17.132  1.00135.64           N  
ANISOU 2836  N   GLU A 404    17576  19930  14032  -3907    571  -3296       N  
ATOM   2837  CA  GLU A 404       8.248   9.529 -17.225  1.00162.87           C  
ANISOU 2837  CA  GLU A 404    20535  24007  17342  -3799    644  -3538       C  
ATOM   2838  C   GLU A 404       7.431   9.077 -16.019  1.00165.47           C  
ANISOU 2838  C   GLU A 404    20854  24470  17546  -4109    971  -3662       C  
ATOM   2839  O   GLU A 404       6.610   9.833 -15.496  1.00166.52           O  
ANISOU 2839  O   GLU A 404    20749  24977  17545  -3884   1034  -3770       O  
ATOM   2840  CB  GLU A 404       7.574   9.101 -18.533  1.00176.91           C  
ANISOU 2840  CB  GLU A 404    21845  26265  19108  -3933    619  -3787       C  
ATOM   2841  CG  GLU A 404       6.102   9.501 -18.646  1.00194.47           C  
ANISOU 2841  CG  GLU A 404    23474  29244  21172  -3851    696  -4096       C  
ATOM   2842  CD  GLU A 404       5.850  10.955 -18.273  1.00199.55           C  
ANISOU 2842  CD  GLU A 404    24058  30047  21715  -3239    552  -4025       C  
ATOM   2843  OE1 GLU A 404       6.602  11.833 -18.746  1.00204.47           O  
ANISOU 2843  OE1 GLU A 404    24900  30408  22383  -2803    283  -3808       O  
ATOM   2844  OE2 GLU A 404       4.902  11.221 -17.501  1.00195.71           O  
ANISOU 2844  OE2 GLU A 404    23327  29939  21095  -3200    724  -4193       O  
ATOM   2845  N   GLU A 405       7.679   7.849 -15.572  1.00156.90           N  
ANISOU 2845  N   GLU A 405    20066  23064  16485  -4605   1191  -3636       N  
ATOM   2846  CA  GLU A 405       6.999   7.313 -14.401  1.00161.19           C  
ANISOU 2846  CA  GLU A 405    20697  23660  16886  -4965   1548  -3708       C  
ATOM   2847  C   GLU A 405       7.291   8.187 -13.186  1.00158.43           C  
ANISOU 2847  C   GLU A 405    20645  23117  16433  -4612   1521  -3530       C  
ATOM   2848  O   GLU A 405       6.406   8.468 -12.382  1.00178.11           O  
ANISOU 2848  O   GLU A 405    22975  25945  18756  -4628   1744  -3650       O  
ATOM   2849  CB  GLU A 405       7.426   5.868 -14.138  1.00174.38           C  
ANISOU 2849  CB  GLU A 405    22808  24860  18589  -5505   1759  -3640       C  
ATOM   2850  CG  GLU A 405       6.642   5.177 -13.029  1.00198.13           C  
ANISOU 2850  CG  GLU A 405    25936  27920  21424  -5978   2190  -3712       C  
ATOM   2851  CD  GLU A 405       5.252   4.754 -13.473  1.00208.76           C  
ANISOU 2851  CD  GLU A 405    26685  29918  22718  -6432   2458  -4079       C  
ATOM   2852  OE1 GLU A 405       5.147   4.045 -14.496  1.00207.73           O  
ANISOU 2852  OE1 GLU A 405    26384  29851  22694  -6735   2431  -4245       O  
ATOM   2853  OE2 GLU A 405       4.267   5.124 -12.798  1.00213.12           O  
ANISOU 2853  OE2 GLU A 405    26918  30946  23111  -6487   2697  -4224       O  
ATOM   2854  N   TRP A 406       8.538   8.624 -13.064  1.00144.06           N  
ANISOU 2854  N   TRP A 406    19241  20788  14708  -4299   1248  -3267       N  
ATOM   2855  CA  TRP A 406       8.931   9.519 -11.982  1.00124.17           C  
ANISOU 2855  CA  TRP A 406    17027  18055  12097  -3951   1159  -3119       C  
ATOM   2856  C   TRP A 406       8.244  10.871 -12.092  1.00116.87           C  
ANISOU 2856  C   TRP A 406    15756  17549  11102  -3494   1048  -3241       C  
ATOM   2857  O   TRP A 406       7.713  11.383 -11.110  1.00117.53           O  
ANISOU 2857  O   TRP A 406    15870  17777  11009  -3347   1175  -3299       O  
ATOM   2858  CB  TRP A 406      10.448   9.694 -11.966  1.00108.07           C  
ANISOU 2858  CB  TRP A 406    15432  15434  10195  -3750    859  -2854       C  
ATOM   2859  CG  TRP A 406      11.152   8.452 -11.548  1.00103.05           C  
ANISOU 2859  CG  TRP A 406    15228  14358   9568  -4074    958  -2721       C  
ATOM   2860  CD1 TRP A 406      10.576   7.304 -11.085  1.00113.82           C  
ANISOU 2860  CD1 TRP A 406    16720  15714  10813  -4519   1299  -2782       C  
ATOM   2861  CD2 TRP A 406      12.565   8.216 -11.564  1.00 95.67           C  
ANISOU 2861  CD2 TRP A 406    14673  12926   8751  -3964    721  -2508       C  
ATOM   2862  NE1 TRP A 406      11.544   6.371 -10.802  1.00116.23           N  
ANISOU 2862  NE1 TRP A 406    17530  15494  11140  -4646   1276  -2602       N  
ATOM   2863  CE2 TRP A 406      12.770   6.904 -11.088  1.00100.87           C  
ANISOU 2863  CE2 TRP A 406    15710  13278   9339  -4286    913  -2444       C  
ATOM   2864  CE3 TRP A 406      13.672   8.985 -11.929  1.00 91.47           C  
ANISOU 2864  CE3 TRP A 406    14194  12192   8370  -3634    377  -2372       C  
ATOM   2865  CZ2 TRP A 406      14.046   6.347 -10.970  1.00 90.44           C  
ANISOU 2865  CZ2 TRP A 406    14797  11484   8080  -4204    739  -2259       C  
ATOM   2866  CZ3 TRP A 406      14.937   8.426 -11.812  1.00 89.96           C  
ANISOU 2866  CZ3 TRP A 406    14340  11583   8258  -3615    223  -2206       C  
ATOM   2867  CH2 TRP A 406      15.112   7.120 -11.335  1.00 86.64           C  
ANISOU 2867  CH2 TRP A 406    14273  10892   7752  -3858    390  -2156       C  
ATOM   2868  N   ILE A 407       8.242  11.436 -13.295  1.00112.74           N  
ANISOU 2868  N   ILE A 407    14934  17215  10688  -3242    819  -3281       N  
ATOM   2869  CA  ILE A 407       7.640  12.745 -13.529  1.00114.12           C  
ANISOU 2869  CA  ILE A 407    14843  17735  10783  -2732    677  -3376       C  
ATOM   2870  C   ILE A 407       6.140  12.733 -13.230  1.00122.06           C  
ANISOU 2870  C   ILE A 407    15365  19414  11597  -2758    939  -3673       C  
ATOM   2871  O   ILE A 407       5.608  13.681 -12.651  1.00124.39           O  
ANISOU 2871  O   ILE A 407    15600  19917  11745  -2360    941  -3752       O  
ATOM   2872  CB  ILE A 407       7.864  13.215 -14.981  1.00108.44           C  
ANISOU 2872  CB  ILE A 407    13916  17111  10175  -2481    406  -3350       C  
ATOM   2873  CG1 ILE A 407       9.358  13.240 -15.306  1.00 90.95           C  
ANISOU 2873  CG1 ILE A 407    12120  14291   8145  -2480    182  -3069       C  
ATOM   2874  CG2 ILE A 407       7.213  14.575 -15.217  1.00 96.70           C  
ANISOU 2874  CG2 ILE A 407    12231  15941   8569  -1896    256  -3431       C  
ATOM   2875  CD1 ILE A 407       9.706  14.026 -16.549  1.00 89.76           C  
ANISOU 2875  CD1 ILE A 407    11885  14156   8064  -2152    -80  -2982       C  
ATOM   2876  N   SER A 408       5.461  11.665 -13.636  1.00133.61           N  
ANISOU 2876  N   SER A 408    16474  21231  13059  -3229   1163  -3861       N  
ATOM   2877  CA  SER A 408       4.027  11.542 -13.393  1.00150.73           C  
ANISOU 2877  CA  SER A 408    18096  24118  15057  -3348   1441  -4180       C  
ATOM   2878  C   SER A 408       3.752  11.329 -11.907  1.00151.31           C  
ANISOU 2878  C   SER A 408    18395  24129  14966  -3543   1772  -4172       C  
ATOM   2879  O   SER A 408       2.805  11.892 -11.357  1.00146.01           O  
ANISOU 2879  O   SER A 408    17412  23957  14109  -3323   1927  -4362       O  
ATOM   2880  CB  SER A 408       3.429  10.397 -14.214  1.00169.89           C  
ANISOU 2880  CB  SER A 408    20102  26913  17536  -3901   1598  -4405       C  
ATOM   2881  OG  SER A 408       4.015   9.155 -13.870  1.00174.96           O  
ANISOU 2881  OG  SER A 408    21157  27059  18258  -4498   1793  -4281       O  
ATOM   2882  N   ASN A 409       4.580  10.506 -11.267  1.00161.54           N  
ANISOU 2882  N   ASN A 409    20243  24831  16303  -3920   1882  -3954       N  
ATOM   2883  CA  ASN A 409       4.468  10.258  -9.831  1.00169.01           C  
ANISOU 2883  CA  ASN A 409    21527  25633  17056  -4095   2184  -3892       C  
ATOM   2884  C   ASN A 409       4.763  11.503  -8.997  1.00172.00           C  
ANISOU 2884  C   ASN A 409    22174  25866  17314  -3506   2020  -3801       C  
ATOM   2885  O   ASN A 409       4.097  11.762  -7.993  1.00181.23           O  
ANISOU 2885  O   ASN A 409    23315  27294  18249  -3443   2271  -3902       O  
ATOM   2886  CB  ASN A 409       5.411   9.127  -9.403  1.00156.45           C  
ANISOU 2886  CB  ASN A 409    20550  23380  15516  -4534   2272  -3648       C  
ATOM   2887  CG  ASN A 409       4.889   7.748  -9.774  1.00144.73           C  
ANISOU 2887  CG  ASN A 409    18921  22011  14058  -5230   2589  -3770       C  
ATOM   2888  OD1 ASN A 409       3.680   7.526  -9.855  1.00141.05           O  
ANISOU 2888  OD1 ASN A 409    17936  22156  13501  -5520   2881  -4047       O  
ATOM   2889  ND2 ASN A 409       5.805   6.810  -9.992  1.00134.05           N  
ANISOU 2889  ND2 ASN A 409    18032  20075  12826  -5504   2536  -3584       N  
ATOM   2890  N   GLY A 410       5.767  12.268  -9.415  1.00156.58           N  
ANISOU 2890  N   GLY A 410    20489  23494  15509  -3099   1613  -3623       N  
ATOM   2891  CA  GLY A 410       6.190  13.438  -8.669  1.00141.05           C  
ANISOU 2891  CA  GLY A 410    18857  21283  13453  -2589   1420  -3540       C  
ATOM   2892  C   GLY A 410       7.543  13.202  -8.028  1.00128.12           C  
ANISOU 2892  C   GLY A 410    17871  18940  11869  -2671   1265  -3266       C  
ATOM   2893  O   GLY A 410       7.948  13.920  -7.116  1.00135.74           O  
ANISOU 2893  O   GLY A 410    19204  19654  12718  -2384   1158  -3206       O  
ATOM   2894  N   VAL A 411       8.237  12.175  -8.503  1.00112.73           N  
ANISOU 2894  N   VAL A 411    16060  16691  10080  -3045   1244  -3126       N  
ATOM   2895  CA  VAL A 411       9.540  11.809  -7.966  1.00109.87           C  
ANISOU 2895  CA  VAL A 411    16264  15716   9765  -3110   1085  -2882       C  
ATOM   2896  C   VAL A 411      10.645  12.495  -8.772  1.00103.78           C  
ANISOU 2896  C   VAL A 411    15564  14634   9235  -2837    668  -2751       C  
ATOM   2897  O   VAL A 411      11.823  12.445  -8.414  1.00 95.21           O  
ANISOU 2897  O   VAL A 411    14870  13094   8211  -2804    460  -2575       O  
ATOM   2898  CB  VAL A 411       9.741  10.282  -7.974  1.00122.80           C  
ANISOU 2898  CB  VAL A 411    18078  17161  11418  -3620   1298  -2798       C  
ATOM   2899  CG1 VAL A 411      10.868   9.893  -7.041  1.00122.71           C  
ANISOU 2899  CG1 VAL A 411    18689  16600  11337  -3614   1192  -2571       C  
ATOM   2900  CG2 VAL A 411       8.465   9.587  -7.540  1.00131.86           C  
ANISOU 2900  CG2 VAL A 411    19026  18706  12369  -3998   1760  -2963       C  
ATOM   2901  N   LEU A 412      10.263  13.107  -9.888  1.00109.33           N  
ANISOU 2901  N   LEU A 412    15873  15611  10057  -2651    553  -2840       N  
ATOM   2902  CA  LEU A 412      11.202  13.895 -10.675  1.00104.11           C  
ANISOU 2902  CA  LEU A 412    15280  14687   9592  -2396    203  -2712       C  
ATOM   2903  C   LEU A 412      10.629  15.278 -10.999  1.00100.96           C  
ANISOU 2903  C   LEU A 412    14709  14504   9146  -1942     76  -2808       C  
ATOM   2904  O   LEU A 412       9.425  15.426 -11.222  1.00101.37           O  
ANISOU 2904  O   LEU A 412    14387  15050   9079  -1830    231  -3000       O  
ATOM   2905  CB  LEU A 412      11.584  13.161 -11.960  1.00106.56           C  
ANISOU 2905  CB  LEU A 412    15392  15000  10096  -2611    153  -2660       C  
ATOM   2906  CG  LEU A 412      12.852  13.710 -12.614  1.00107.86           C  
ANISOU 2906  CG  LEU A 412    15714  14810  10458  -2458   -162  -2475       C  
ATOM   2907  CD1 LEU A 412      14.075  12.981 -12.110  1.00108.05           C  
ANISOU 2907  CD1 LEU A 412    16084  14407  10561  -2649   -236  -2318       C  
ATOM   2908  CD2 LEU A 412      12.762  13.619 -14.125  1.00118.69           C  
ANISOU 2908  CD2 LEU A 412    16758  16389  11948  -2461   -218  -2488       C  
ATOM   2909  N   TYR A 413      11.492  16.290 -10.988  1.00101.19           N  
ANISOU 2909  N   TYR A 413    15027  14161   9258  -1679   -205  -2685       N  
ATOM   2910  CA  TYR A 413      11.105  17.640 -11.386  1.00108.98           C  
ANISOU 2910  CA  TYR A 413    15976  15221  10209  -1227   -354  -2735       C  
ATOM   2911  C   TYR A 413      12.152  18.230 -12.328  1.00113.42           C  
ANISOU 2911  C   TYR A 413    16684  15433  10977  -1163   -626  -2545       C  
ATOM   2912  O   TYR A 413      13.354  18.054 -12.128  1.00102.95           O  
ANISOU 2912  O   TYR A 413    15618  13707   9791  -1363   -758  -2395       O  
ATOM   2913  CB  TYR A 413      10.922  18.530 -10.154  1.00125.97           C  
ANISOU 2913  CB  TYR A 413    18440  17237  12185   -941   -374  -2817       C  
ATOM   2914  CG  TYR A 413      10.266  19.875 -10.406  1.00129.44           C  
ANISOU 2914  CG  TYR A 413    18875  17782  12525   -411   -475  -2918       C  
ATOM   2915  CD1 TYR A 413      11.001  20.958 -10.880  1.00125.98           C  
ANISOU 2915  CD1 TYR A 413    18743  16924  12198   -185   -750  -2790       C  
ATOM   2916  CD2 TYR A 413       8.918  20.071 -10.134  1.00132.69           C  
ANISOU 2916  CD2 TYR A 413    18997  18704  12714   -129   -285  -3147       C  
ATOM   2917  CE1 TYR A 413      10.405  22.192 -11.096  1.00126.48           C  
ANISOU 2917  CE1 TYR A 413    18902  17010  12146    337   -844  -2868       C  
ATOM   2918  CE2 TYR A 413       8.313  21.302 -10.347  1.00138.20           C  
ANISOU 2918  CE2 TYR A 413    19722  19494  13294    442   -393  -3248       C  
ATOM   2919  CZ  TYR A 413       9.061  22.359 -10.828  1.00127.03           C  
ANISOU 2919  CZ  TYR A 413    18694  17588  11984    689   -678  -3099       C  
ATOM   2920  OH  TYR A 413       8.465  23.583 -11.040  1.00115.53           O  
ANISOU 2920  OH  TYR A 413    17356  16151  10389   1291   -786  -3184       O  
ATOM   2921  N   ALA A 414      11.687  18.946 -13.343  1.00133.33           N  
ANISOU 2921  N   ALA A 414    19036  18132  13493   -869   -705  -2555       N  
ATOM   2922  CA  ALA A 414      12.574  19.509 -14.348  1.00134.03           C  
ANISOU 2922  CA  ALA A 414    19260  17928  13739   -824   -911  -2361       C  
ATOM   2923  C   ALA A 414      12.807  20.993 -14.097  1.00135.21           C  
ANISOU 2923  C   ALA A 414    19802  17719  13853   -469  -1092  -2308       C  
ATOM   2924  O   ALA A 414      11.898  21.808 -14.254  1.00139.94           O  
ANISOU 2924  O   ALA A 414    20384  18495  14293    -36  -1102  -2404       O  
ATOM   2925  CB  ALA A 414      12.007  19.288 -15.739  1.00137.45           C  
ANISOU 2925  CB  ALA A 414    19321  18744  14160   -742   -889  -2372       C  
ATOM   2926  N   THR A 415      14.023  21.341 -13.693  1.00123.30           N  
ANISOU 2926  N   THR A 415    18656  15710  12484   -646  -1240  -2176       N  
ATOM   2927  CA  THR A 415      14.377  22.741 -13.522  1.00118.65           C  
ANISOU 2927  CA  THR A 415    18497  14697  11888   -402  -1416  -2125       C  
ATOM   2928  C   THR A 415      14.438  23.409 -14.894  1.00125.93           C  
ANISOU 2928  C   THR A 415    19439  15559  12849   -235  -1489  -1965       C  
ATOM   2929  O   THR A 415      15.051  22.879 -15.819  1.00123.33           O  
ANISOU 2929  O   THR A 415    18939  15264  12658   -493  -1483  -1816       O  
ATOM   2930  CB  THR A 415      15.722  22.899 -12.787  1.00 99.71           C  
ANISOU 2930  CB  THR A 415    16430  11817   9639   -711  -1567  -2053       C  
ATOM   2931  OG1 THR A 415      16.777  22.351 -13.584  1.00 96.41           O  
ANISOU 2931  OG1 THR A 415    15875  11322   9435  -1065  -1608  -1876       O  
ATOM   2932  CG2 THR A 415      15.687  22.165 -11.464  1.00101.10           C  
ANISOU 2932  CG2 THR A 415    16618  12067   9729   -846  -1505  -2188       C  
ATOM   2933  N   PRO A 416      13.805  24.584 -15.026  1.00136.78           N  
ANISOU 2933  N   PRO A 416    21062  16833  14074    230  -1554  -1992       N  
ATOM   2934  CA  PRO A 416      13.734  25.291 -16.312  1.00146.62           C  
ANISOU 2934  CA  PRO A 416    22406  18014  15287    475  -1619  -1823       C  
ATOM   2935  C   PRO A 416      15.079  25.889 -16.743  1.00151.07           C  
ANISOU 2935  C   PRO A 416    23352  18010  16036    178  -1726  -1576       C  
ATOM   2936  O   PRO A 416      16.005  25.925 -15.934  1.00152.85           O  
ANISOU 2936  O   PRO A 416    23777  17891  16409   -159  -1787  -1581       O  
ATOM   2937  CB  PRO A 416      12.706  26.398 -16.031  1.00151.99           C  
ANISOU 2937  CB  PRO A 416    23339  18680  15730   1104  -1667  -1946       C  
ATOM   2938  CG  PRO A 416      11.928  25.910 -14.847  1.00145.15           C  
ANISOU 2938  CG  PRO A 416    22249  18151  14752   1182  -1557  -2221       C  
ATOM   2939  CD  PRO A 416      12.952  25.219 -14.010  1.00138.35           C  
ANISOU 2939  CD  PRO A 416    21439  17054  14075    625  -1544  -2200       C  
ATOM   2940  N   PRO A 417      15.190  26.336 -18.009  1.00146.00           N  
ANISOU 2940  N   PRO A 417    22797  17307  15367    289  -1743  -1370       N  
ATOM   2941  CA  PRO A 417      16.450  26.879 -18.531  1.00148.56           C  
ANISOU 2941  CA  PRO A 417    23451  17141  15856    -47  -1789  -1121       C  
ATOM   2942  C   PRO A 417      16.853  28.217 -17.894  1.00168.86           C  
ANISOU 2942  C   PRO A 417    26664  19060  18435      4  -1902  -1096       C  
ATOM   2943  O   PRO A 417      16.026  28.891 -17.272  1.00172.01           O  
ANISOU 2943  O   PRO A 417    27323  19369  18664    447  -1954  -1245       O  
ATOM   2944  CB  PRO A 417      16.155  27.044 -20.027  1.00139.82           C  
ANISOU 2944  CB  PRO A 417    22300  16204  14622    172  -1749   -923       C  
ATOM   2945  CG  PRO A 417      14.679  27.220 -20.090  1.00143.68           C  
ANISOU 2945  CG  PRO A 417    22676  17072  14842    795  -1766  -1081       C  
ATOM   2946  CD  PRO A 417      14.179  26.237 -19.076  1.00140.95           C  
ANISOU 2946  CD  PRO A 417    21900  17121  14531    691  -1706  -1361       C  
ATOM   2947  N   GLY A 418      18.122  28.584 -18.050  1.00174.93           N  
ANISOU 2947  N   GLY A 418    27676  19393  19398   -460  -1931   -932       N  
ATOM   2948  CA  GLY A 418      18.625  29.853 -17.555  1.00173.51           C  
ANISOU 2948  CA  GLY A 418    28132  18545  19249   -525  -2032   -909       C  
ATOM   2949  C   GLY A 418      19.020  29.813 -16.090  1.00181.45           C  
ANISOU 2949  C   GLY A 418    29212  19379  20350   -741  -2143  -1150       C  
ATOM   2950  O   GLY A 418      19.562  30.784 -15.559  1.00185.38           O  
ANISOU 2950  O   GLY A 418    30216  19322  20900   -889  -2249  -1184       O  
ATOM   2951  N   SER A 419      18.751  28.687 -15.438  1.00191.26           N  
ANISOU 2951  N   SER A 419    29986  21086  21599   -770  -2119  -1323       N  
ATOM   2952  CA  SER A 419      19.018  28.541 -14.014  1.00198.74           C  
ANISOU 2952  CA  SER A 419    30997  21944  22571   -906  -2222  -1552       C  
ATOM   2953  C   SER A 419      18.943  27.077 -13.584  1.00205.56           C  
ANISOU 2953  C   SER A 419    31320  23325  23458  -1044  -2153  -1647       C  
ATOM   2954  O   SER A 419      18.066  26.359 -14.062  1.00212.89           O  
ANISOU 2954  O   SER A 419    31896  24707  24287   -825  -2014  -1646       O  
ATOM   2955  CB  SER A 419      18.020  29.370 -13.199  1.00197.78           C  
ANISOU 2955  CB  SER A 419    31264  21665  22219   -398  -2267  -1750       C  
ATOM   2956  OG  SER A 419      16.715  28.825 -13.273  1.00196.40           O  
ANISOU 2956  OG  SER A 419    30759  22018  21845     52  -2139  -1843       O  
ATOM   2957  N   ASN A 420      19.828  26.604 -12.697  1.00200.08           N  
ANISOU 2957  N   ASN A 420    30570  22575  22876  -1396  -2252  -1736       N  
ATOM   2958  CA  ASN A 420      21.023  27.285 -12.181  1.00182.24           C  
ANISOU 2958  CA  ASN A 420    28609  19871  20762  -1754  -2440  -1766       C  
ATOM   2959  C   ASN A 420      21.819  26.189 -11.465  1.00183.65           C  
ANISOU 2959  C   ASN A 420    28470  20279  21029  -2060  -2515  -1845       C  
ATOM   2960  O   ASN A 420      21.591  25.001 -11.706  1.00184.53           O  
ANISOU 2960  O   ASN A 420    28184  20796  21133  -2047  -2396  -1802       O  
ATOM   2961  CB  ASN A 420      20.665  28.414 -11.201  1.00161.53           C  
ANISOU 2961  CB  ASN A 420    26532  16848  17995  -1527  -2564  -1957       C  
ATOM   2962  CG  ASN A 420      21.843  29.309 -10.869  1.00157.34           C  
ANISOU 2962  CG  ASN A 420    26362  15803  17618  -1931  -2758  -1997       C  
ATOM   2963  OD1 ASN A 420      22.981  28.854 -10.782  1.00153.27           O  
ANISOU 2963  OD1 ASN A 420    25605  15341  17289  -2388  -2851  -1986       O  
ATOM   2964  ND2 ASN A 420      21.569  30.596 -10.678  1.00166.42           N  
ANISOU 2964  ND2 ASN A 420    28094  16456  18683  -1757  -2824  -2066       N  
ATOM   2965  N   ASP A 421      22.745  26.567 -10.584  1.00183.78           N  
ANISOU 2965  N   ASP A 421    28678  20035  21113  -2322  -2725  -1973       N  
ATOM   2966  CA  ASP A 421      23.395  25.598  -9.702  1.00170.87           C  
ANISOU 2966  CA  ASP A 421    26816  18619  19488  -2491  -2841  -2081       C  
ATOM   2967  C   ASP A 421      22.350  25.424  -8.612  1.00161.74           C  
ANISOU 2967  C   ASP A 421    25841  17560  18053  -2124  -2807  -2252       C  
ATOM   2968  O   ASP A 421      22.572  25.755  -7.446  1.00141.42           O  
ANISOU 2968  O   ASP A 421    23538  14829  15365  -2113  -2980  -2445       O  
ATOM   2969  CB  ASP A 421      24.731  26.095  -9.150  1.00159.72           C  
ANISOU 2969  CB  ASP A 421    25508  16961  18218  -2878  -3106  -2189       C  
ATOM   2970  CG  ASP A 421      25.519  25.002  -8.440  1.00145.52           C  
ANISOU 2970  CG  ASP A 421    23411  15453  16427  -3011  -3249  -2268       C  
ATOM   2971  OD1 ASP A 421      24.906  24.174  -7.733  1.00132.77           O  
ANISOU 2971  OD1 ASP A 421    21775  14058  14612  -2752  -3201  -2323       O  
ATOM   2972  OD2 ASP A 421      26.759  24.971  -8.593  1.00149.31           O  
ANISOU 2972  OD2 ASP A 421    23680  15952  17100  -3367  -3402  -2273       O  
ATOM   2973  N   ASP A 422      21.212  24.878  -9.029  1.00169.96           N  
ANISOU 2973  N   ASP A 422    26702  18900  18975  -1840  -2573  -2194       N  
ATOM   2974  CA  ASP A 422      19.913  25.189  -8.450  1.00167.14           C  
ANISOU 2974  CA  ASP A 422    26533  18615  18357  -1426  -2460  -2331       C  
ATOM   2975  C   ASP A 422      19.796  25.124  -6.943  1.00162.81           C  
ANISOU 2975  C   ASP A 422    26221  18048  17590  -1325  -2540  -2543       C  
ATOM   2976  O   ASP A 422      20.263  24.195  -6.284  1.00147.74           O  
ANISOU 2976  O   ASP A 422    24195  16294  15644  -1483  -2580  -2562       O  
ATOM   2977  CB  ASP A 422      18.855  24.260  -9.048  1.00167.77           C  
ANISOU 2977  CB  ASP A 422    26233  19155  18357  -1250  -2195  -2264       C  
ATOM   2978  CG  ASP A 422      18.659  24.478 -10.532  1.00162.07           C  
ANISOU 2978  CG  ASP A 422    25331  18490  17760  -1216  -2109  -2091       C  
ATOM   2979  OD1 ASP A 422      18.427  25.638 -10.936  1.00156.02           O  
ANISOU 2979  OD1 ASP A 422    24845  17460  16975  -1016  -2156  -2070       O  
ATOM   2980  OD2 ASP A 422      18.744  23.488 -11.291  1.00161.36           O  
ANISOU 2980  OD2 ASP A 422    24862  18687  17762  -1371  -1998  -1976       O  
ATOM   2981  N   TRP A 423      19.143  26.150  -6.420  1.00175.66           N  
ANISOU 2981  N   TRP A 423    28223  19476  19045  -1015  -2561  -2702       N  
ATOM   2982  CA  TRP A 423      18.750  26.190  -5.035  1.00190.50           C  
ANISOU 2982  CA  TRP A 423    30353  21382  20645   -817  -2584  -2923       C  
ATOM   2983  C   TRP A 423      17.448  25.415  -4.932  1.00176.93           C  
ANISOU 2983  C   TRP A 423    28370  20143  18715   -541  -2275  -2939       C  
ATOM   2984  O   TRP A 423      16.928  25.201  -3.840  1.00179.93           O  
ANISOU 2984  O   TRP A 423    28873  20672  18822   -372  -2194  -3095       O  
ATOM   2985  CB  TRP A 423      18.570  27.632  -4.572  1.00216.52           C  
ANISOU 2985  CB  TRP A 423    34176  24259  23833   -573  -2720  -3111       C  
ATOM   2986  CG  TRP A 423      17.630  28.390  -5.459  1.00240.22           C  
ANISOU 2986  CG  TRP A 423    37239  27214  26819   -207  -2585  -3062       C  
ATOM   2987  CD1 TRP A 423      16.286  28.546  -5.284  1.00250.99           C  
ANISOU 2987  CD1 TRP A 423    38591  28841  27933    298  -2391  -3176       C  
ATOM   2988  CD2 TRP A 423      17.957  29.071  -6.690  1.00251.31           C  
ANISOU 2988  CD2 TRP A 423    38715  28329  28443   -289  -2629  -2881       C  
ATOM   2989  NE1 TRP A 423      15.759  29.291  -6.316  1.00255.24           N  
ANISOU 2989  NE1 TRP A 423    39191  29273  28515    586  -2350  -3088       N  
ATOM   2990  CE2 TRP A 423      16.754  29.618  -7.179  1.00258.50           C  
ANISOU 2990  CE2 TRP A 423    39693  29326  29200    234  -2486  -2892       C  
ATOM   2991  CE3 TRP A 423      19.142  29.264  -7.397  1.00254.14           C  
ANISOU 2991  CE3 TRP A 423    39083  28394  29087   -744  -2762  -2716       C  
ATOM   2992  CZ2 TRP A 423      16.719  30.358  -8.372  1.00265.20           C  
ANISOU 2992  CZ2 TRP A 423    40684  29926  30154    337  -2491  -2715       C  
ATOM   2993  CZ3 TRP A 423      19.092  30.000  -8.574  1.00262.42           C  
ANISOU 2993  CZ3 TRP A 423    40268  29196  30245   -693  -2725  -2536       C  
ATOM   2994  CH2 TRP A 423      17.890  30.537  -9.047  1.00268.25           C  
ANISOU 2994  CH2 TRP A 423    41136  29979  30805   -142  -2599  -2526       C  
ATOM   2995  N   TYR A 424      16.931  25.007  -6.092  1.00161.91           N  
ANISOU 2995  N   TYR A 424    26095  18497  16925   -520  -2097  -2789       N  
ATOM   2996  CA  TYR A 424      15.700  24.229  -6.181  1.00149.93           C  
ANISOU 2996  CA  TYR A 424    24236  17484  15246   -339  -1797  -2816       C  
ATOM   2997  C   TYR A 424      15.693  23.080  -5.181  1.00139.37           C  
ANISOU 2997  C   TYR A 424    22830  16375  13751   -511  -1675  -2854       C  
ATOM   2998  O   TYR A 424      14.707  22.867  -4.484  1.00139.82           O  
ANISOU 2998  O   TYR A 424    22863  16718  13545   -314  -1459  -2986       O  
ATOM   2999  CB  TYR A 424      15.492  23.706  -7.617  1.00145.57           C  
ANISOU 2999  CB  TYR A 424    23257  17173  14879   -436  -1682  -2642       C  
ATOM   3000  CG  TYR A 424      14.973  24.752  -8.594  1.00133.64           C  
ANISOU 3000  CG  TYR A 424    21789  15593  13395   -113  -1708  -2616       C  
ATOM   3001  CD1 TYR A 424      15.792  25.778  -9.051  1.00127.26           C  
ANISOU 3001  CD1 TYR A 424    21316  14297  12740   -153  -1921  -2520       C  
ATOM   3002  CD2 TYR A 424      13.664  24.703  -9.067  1.00121.10           C  
ANISOU 3002  CD2 TYR A 424    19912  14438  11662    230  -1519  -2688       C  
ATOM   3003  CE1 TYR A 424      15.319  26.732  -9.943  1.00122.98           C  
ANISOU 3003  CE1 TYR A 424    20902  13640  12183    172  -1937  -2464       C  
ATOM   3004  CE2 TYR A 424      13.184  25.653  -9.957  1.00118.40           C  
ANISOU 3004  CE2 TYR A 424    19640  14044  11302    603  -1570  -2657       C  
ATOM   3005  CZ  TYR A 424      14.017  26.662 -10.392  1.00119.29           C  
ANISOU 3005  CZ  TYR A 424    20170  13610  11548    587  -1776  -2527       C  
ATOM   3006  OH  TYR A 424      13.551  27.609 -11.275  1.00114.82           O  
ANISOU 3006  OH  TYR A 424    19762  12937  10928    983  -1821  -2464       O  
ATOM   3007  N   TRP A 425      16.801  22.353  -5.097  1.00138.54           N  
ANISOU 3007  N   TRP A 425    22708  16147  13784   -860  -1806  -2736       N  
ATOM   3008  CA  TRP A 425      16.934  21.313  -4.082  1.00143.11           C  
ANISOU 3008  CA  TRP A 425    23343  16852  14181   -988  -1732  -2746       C  
ATOM   3009  C   TRP A 425      17.357  21.875  -2.725  1.00144.93           C  
ANISOU 3009  C   TRP A 425    24017  16855  14196   -884  -1927  -2902       C  
ATOM   3010  O   TRP A 425      16.906  21.391  -1.688  1.00145.93           O  
ANISOU 3010  O   TRP A 425    24287  17137  14023   -803  -1785  -2975       O  
ATOM   3011  CB  TRP A 425      17.910  20.222  -4.552  1.00136.78           C  
ANISOU 3011  CB  TRP A 425    22351  16040  13578  -1321  -1798  -2564       C  
ATOM   3012  CG  TRP A 425      19.271  20.711  -4.947  1.00138.80           C  
ANISOU 3012  CG  TRP A 425    22652  15995  14091  -1491  -2125  -2505       C  
ATOM   3013  CD1 TRP A 425      20.299  21.052  -4.122  1.00141.51           C  
ANISOU 3013  CD1 TRP A 425    23251  16102  14413  -1561  -2422  -2579       C  
ATOM   3014  CD2 TRP A 425      19.748  20.898  -6.283  1.00145.37           C  
ANISOU 3014  CD2 TRP A 425    23233  16776  15227  -1637  -2172  -2372       C  
ATOM   3015  NE1 TRP A 425      21.390  21.446  -4.861  1.00133.83           N  
ANISOU 3015  NE1 TRP A 425    22163  14952  13733  -1777  -2640  -2512       N  
ATOM   3016  CE2 TRP A 425      21.077  21.357  -6.190  1.00141.73           C  
ANISOU 3016  CE2 TRP A 425    22870  16051  14929  -1826  -2474  -2370       C  
ATOM   3017  CE3 TRP A 425      19.180  20.720  -7.547  1.00166.76           C  
ANISOU 3017  CE3 TRP A 425    25636  19665  18061  -1631  -1988  -2267       C  
ATOM   3018  CZ2 TRP A 425      21.844  21.646  -7.316  1.00163.42           C  
ANISOU 3018  CZ2 TRP A 425    25423  18707  17963  -2029  -2554  -2248       C  
ATOM   3019  CZ3 TRP A 425      19.943  21.005  -8.663  1.00182.88           C  
ANISOU 3019  CZ3 TRP A 425    27528  21595  20363  -1792  -2088  -2137       C  
ATOM   3020  CH2 TRP A 425      21.260  21.466  -8.541  1.00188.86           C  
ANISOU 3020  CH2 TRP A 425    28393  22085  21282  -1999  -2348  -2120       C  
ATOM   3021  N   LEU A 426      18.207  22.897  -2.731  1.00133.66           N  
ANISOU 3021  N   LEU A 426    22822  15062  12902   -906  -2239  -2962       N  
ATOM   3022  CA  LEU A 426      18.613  23.546  -1.489  1.00113.08           C  
ANISOU 3022  CA  LEU A 426    20651  12225  10090   -813  -2463  -3158       C  
ATOM   3023  C   LEU A 426      17.401  24.160  -0.789  1.00119.98           C  
ANISOU 3023  C   LEU A 426    21751  13191  10644   -419  -2281  -3354       C  
ATOM   3024  O   LEU A 426      17.226  23.992   0.416  1.00134.97           O  
ANISOU 3024  O   LEU A 426    23901  15161  12222   -300  -2258  -3486       O  
ATOM   3025  CB  LEU A 426      19.672  24.618  -1.748  1.00110.78           C  
ANISOU 3025  CB  LEU A 426    20553  11512  10028   -968  -2810  -3215       C  
ATOM   3026  CG  LEU A 426      21.123  24.153  -1.918  1.00114.99           C  
ANISOU 3026  CG  LEU A 426    20938  11965  10789  -1347  -3076  -3124       C  
ATOM   3027  CD1 LEU A 426      22.056  25.333  -2.183  1.00105.13           C  
ANISOU 3027  CD1 LEU A 426    19864  10320   9762  -1557  -3372  -3212       C  
ATOM   3028  CD2 LEU A 426      21.610  23.352  -0.716  1.00124.62           C  
ANISOU 3028  CD2 LEU A 426    22271  13311  11767  -1360  -3206  -3190       C  
ATOM   3029  N   TYR A 427      16.567  24.866  -1.550  1.00106.13           N  
ANISOU 3029  N   TYR A 427    19911  11461   8953   -181  -2150  -3376       N  
ATOM   3030  CA  TYR A 427      15.325  25.430  -1.025  1.00117.28           C  
ANISOU 3030  CA  TYR A 427    21455  13040  10067    262  -1951  -3572       C  
ATOM   3031  C   TYR A 427      14.421  24.330  -0.507  1.00140.69           C  
ANISOU 3031  C   TYR A 427    24166  16513  12777    290  -1595  -3570       C  
ATOM   3032  O   TYR A 427      13.902  24.416   0.602  1.00175.56           O  
ANISOU 3032  O   TYR A 427    28801  21057  16848    503  -1478  -3742       O  
ATOM   3033  CB  TYR A 427      14.590  26.238  -2.101  1.00112.89           C  
ANISOU 3033  CB  TYR A 427    20781  12482   9630    552  -1880  -3565       C  
ATOM   3034  CG  TYR A 427      13.137  26.558  -1.782  1.00120.04           C  
ANISOU 3034  CG  TYR A 427    21627  13743  10238   1052  -1614  -3752       C  
ATOM   3035  CD1 TYR A 427      12.800  27.663  -1.009  1.00125.98           C  
ANISOU 3035  CD1 TYR A 427    22828  14284  10754   1472  -1689  -4001       C  
ATOM   3036  CD2 TYR A 427      12.103  25.759  -2.263  1.00122.92           C  
ANISOU 3036  CD2 TYR A 427    21470  14680  10555   1106  -1289  -3708       C  
ATOM   3037  CE1 TYR A 427      11.474  27.964  -0.721  1.00130.83           C  
ANISOU 3037  CE1 TYR A 427    23349  15277  11083   1983  -1439  -4193       C  
ATOM   3038  CE2 TYR A 427      10.774  26.051  -1.977  1.00124.92           C  
ANISOU 3038  CE2 TYR A 427    21584  15344  10534   1562  -1040  -3908       C  
ATOM   3039  CZ  TYR A 427      10.466  27.155  -1.207  1.00128.02           C  
ANISOU 3039  CZ  TYR A 427    22406  15548  10688   2025  -1112  -4147       C  
ATOM   3040  OH  TYR A 427       9.149  27.448  -0.922  1.00128.73           O  
ANISOU 3040  OH  TYR A 427    22323  16098  10492   2529   -857  -4366       O  
ATOM   3041  N   ALA A 428      14.244  23.291  -1.315  1.00125.52           N  
ANISOU 3041  N   ALA A 428    21805  14874  11015     47  -1408  -3381       N  
ATOM   3042  CA  ALA A 428      13.344  22.205  -0.965  1.00121.54           C  
ANISOU 3042  CA  ALA A 428    21043  14836  10300    -14  -1031  -3370       C  
ATOM   3043  C   ALA A 428      13.861  21.435   0.251  1.00130.47           C  
ANISOU 3043  C   ALA A 428    22464  15915  11194   -192  -1027  -3344       C  
ATOM   3044  O   ALA A 428      13.084  21.039   1.120  1.00130.31           O  
ANISOU 3044  O   ALA A 428    22500  16176  10837   -112   -737  -3424       O  
ATOM   3045  CB  ALA A 428      13.151  21.282  -2.150  1.00111.86           C  
ANISOU 3045  CB  ALA A 428    19335  13851   9317   -280   -872  -3193       C  
ATOM   3046  N   ALA A 429      15.173  21.237   0.325  1.00105.24           N  
ANISOU 3046  N   ALA A 429    19453  12387   8148   -414  -1345  -3235       N  
ATOM   3047  CA  ALA A 429      15.753  20.555   1.476  1.00106.38           C  
ANISOU 3047  CA  ALA A 429    19912  12469   8038   -513  -1407  -3208       C  
ATOM   3048  C   ALA A 429      15.552  21.385   2.746  1.00132.30           C  
ANISOU 3048  C   ALA A 429    23631  15682  10955   -214  -1479  -3442       C  
ATOM   3049  O   ALA A 429      15.133  20.861   3.779  1.00125.45           O  
ANISOU 3049  O   ALA A 429    22966  14994   9705   -154  -1273  -3471       O  
ATOM   3050  CB  ALA A 429      17.234  20.276   1.246  1.00104.45           C  
ANISOU 3050  CB  ALA A 429    19719  11935   8031   -747  -1783  -3083       C  
ATOM   3051  N   ALA A 430      15.843  22.680   2.655  1.00129.04           N  
ANISOU 3051  N   ALA A 430    23397  14989  10643    -35  -1756  -3611       N  
ATOM   3052  CA  ALA A 430      15.724  23.594   3.789  1.00126.52           C  
ANISOU 3052  CA  ALA A 430    23534  14541   9996    263  -1872  -3877       C  
ATOM   3053  C   ALA A 430      14.272  23.836   4.188  1.00131.67           C  
ANISOU 3053  C   ALA A 430    24161  15535  10333    618  -1481  -4030       C  
ATOM   3054  O   ALA A 430      13.953  23.894   5.377  1.00130.48           O  
ANISOU 3054  O   ALA A 430    24325  15487   9764    813  -1388  -4186       O  
ATOM   3055  CB  ALA A 430      16.403  24.914   3.470  1.00116.55           C  
ANISOU 3055  CB  ALA A 430    22494  12833   8956    316  -2254  -4021       C  
ATOM   3056  N   LYS A 431      13.402  23.995   3.193  1.00117.35           N  
ANISOU 3056  N   LYS A 431    21958  13934   8697    723  -1258  -4002       N  
ATOM   3057  CA  LYS A 431      11.986  24.263   3.437  1.00133.45           C  
ANISOU 3057  CA  LYS A 431    23859  16381  10464   1092   -891  -4174       C  
ATOM   3058  C   LYS A 431      11.334  23.087   4.156  1.00144.41           C  
ANISOU 3058  C   LYS A 431    25110  18225  11536    944   -475  -4118       C  
ATOM   3059  O   LYS A 431      10.463  23.267   5.009  1.00156.29           O  
ANISOU 3059  O   LYS A 431    26702  20028  12654   1218   -202  -4302       O  
ATOM   3060  CB  LYS A 431      11.252  24.550   2.126  1.00124.35           C  
ANISOU 3060  CB  LYS A 431    22252  15421   9575   1222   -774  -4143       C  
ATOM   3061  CG  LYS A 431       9.850  25.115   2.296  1.00135.98           C  
ANISOU 3061  CG  LYS A 431    23568  17310  10788   1718   -483  -4378       C  
ATOM   3062  CD  LYS A 431       9.891  26.539   2.831  1.00153.84           C  
ANISOU 3062  CD  LYS A 431    26338  19220  12893   2208   -711  -4633       C  
ATOM   3063  CE  LYS A 431       8.500  27.150   2.896  1.00165.71           C  
ANISOU 3063  CE  LYS A 431    27662  21154  14146   2795   -441  -4880       C  
ATOM   3064  NZ  LYS A 431       8.540  28.565   3.361  1.00172.25           N  
ANISOU 3064  NZ  LYS A 431    29052  21574  14820   3320   -673  -5139       N  
ATOM   3065  N   LEU A 432      11.771  21.881   3.809  1.00139.88           N  
ANISOU 3065  N   LEU A 432    24349  17687  11113    508   -411  -3862       N  
ATOM   3066  CA  LEU A 432      11.251  20.669   4.429  1.00144.06           C  
ANISOU 3066  CA  LEU A 432    24822  18555  11361    283     -8  -3762       C  
ATOM   3067  C   LEU A 432      12.101  20.278   5.627  1.00140.52           C  
ANISOU 3067  C   LEU A 432    24910  17865  10617    211   -161  -3704       C  
ATOM   3068  O   LEU A 432      11.764  19.341   6.355  1.00126.34           O  
ANISOU 3068  O   LEU A 432    23233  16270   8500     60    158  -3609       O  
ATOM   3069  CB  LEU A 432      11.212  19.514   3.423  1.00146.59           C  
ANISOU 3069  CB  LEU A 432    24719  19008  11969   -137    163  -3526       C  
ATOM   3070  CG  LEU A 432      10.021  19.430   2.466  1.00134.01           C  
ANISOU 3070  CG  LEU A 432    22531  17874  10514   -142    486  -3587       C  
ATOM   3071  CD1 LEU A 432       8.702  19.390   3.213  1.00140.03           C  
ANISOU 3071  CD1 LEU A 432    23160  19159  10887      4    952  -3769       C  
ATOM   3072  CD2 LEU A 432      10.053  20.597   1.523  1.00121.06           C  
ANISOU 3072  CD2 LEU A 432    20728  16115   9155    166    204  -3688       C  
ATOM   3073  N   LYS A 433      13.215  20.988   5.804  1.00150.34           N  
ANISOU 3073  N   LYS A 433    26480  18681  11961    301   -653  -3762       N  
ATOM   3074  CA  LYS A 433      14.168  20.712   6.875  1.00147.84           C  
ANISOU 3074  CA  LYS A 433    26651  18141  11382    270   -908  -3738       C  
ATOM   3075  C   LYS A 433      14.624  19.261   6.803  1.00147.99           C  
ANISOU 3075  C   LYS A 433    26636  18176  11418    -72   -816  -3437       C  
ATOM   3076  O   LYS A 433      14.965  18.640   7.813  1.00153.81           O  
ANISOU 3076  O   LYS A 433    27764  18887  11789    -77   -817  -3363       O  
ATOM   3077  CB  LYS A 433      13.550  21.039   8.234  1.00146.24           C  
ANISOU 3077  CB  LYS A 433    26839  18107  10620    570   -725  -3938       C  
ATOM   3078  CG  LYS A 433      13.446  22.531   8.486  1.00150.47           C  
ANISOU 3078  CG  LYS A 433    27582  18485  11104    953   -952  -4266       C  
ATOM   3079  CD  LYS A 433      12.668  22.840   9.747  1.00156.07           C  
ANISOU 3079  CD  LYS A 433    28603  19434  11261   1289   -699  -4479       C  
ATOM   3080  CE  LYS A 433      11.222  22.398   9.604  1.00158.58           C  
ANISOU 3080  CE  LYS A 433    28557  20286  11409   1339    -87  -4472       C  
ATOM   3081  NZ  LYS A 433      10.372  22.929  10.702  1.00161.50           N  
ANISOU 3081  NZ  LYS A 433    29153  20935  11274   1732    179  -4731       N  
ATOM   3082  N   CYS A 434      14.609  18.730   5.585  1.00133.96           N  
ANISOU 3082  N   CYS A 434    24425  16430  10044   -328   -736  -3268       N  
ATOM   3083  CA  CYS A 434      14.899  17.327   5.345  1.00130.39           C  
ANISOU 3083  CA  CYS A 434    23921  15980   9640   -645   -597  -2995       C  
ATOM   3084  C   CYS A 434      16.338  17.105   4.900  1.00121.98           C  
ANISOU 3084  C   CYS A 434    22885  14592   8871   -757  -1058  -2870       C  
ATOM   3085  O   CYS A 434      17.175  18.003   4.994  1.00111.93           O  
ANISOU 3085  O   CYS A 434    21718  13104   7707   -629  -1488  -3000       O  
ATOM   3086  CB  CYS A 434      13.928  16.763   4.302  1.00137.25           C  
ANISOU 3086  CB  CYS A 434    24290  17126  10731   -872   -192  -2917       C  
ATOM   3087  SG  CYS A 434      14.174  17.383   2.627  1.00125.53           S  
ANISOU 3087  SG  CYS A 434    22290  15570   9834   -913   -424  -2929       S  
ATOM   3088  N   LEU A 435      16.606  15.908   4.388  1.00123.71           N  
ANISOU 3088  N   LEU A 435    22994  14787   9222  -1007   -954  -2637       N  
ATOM   3089  CA  LEU A 435      17.950  15.537   3.967  1.00125.12           C  
ANISOU 3089  CA  LEU A 435    23164  14723   9653  -1083  -1349  -2514       C  
ATOM   3090  C   LEU A 435      18.265  16.077   2.580  1.00118.43           C  
ANISOU 3090  C   LEU A 435    21849  13829   9319  -1188  -1513  -2534       C  
ATOM   3091  O   LEU A 435      17.368  16.305   1.773  1.00114.60           O  
ANISOU 3091  O   LEU A 435    21031  13508   9003  -1251  -1253  -2563       O  
ATOM   3092  CB  LEU A 435      18.123  14.012   3.984  1.00126.08           C  
ANISOU 3092  CB  LEU A 435    23423  14802   9680  -1252  -1168  -2261       C  
ATOM   3093  CG  LEU A 435      18.273  13.269   5.317  1.00131.55           C  
ANISOU 3093  CG  LEU A 435    24692  15429   9861  -1143  -1115  -2156       C  
ATOM   3094  CD1 LEU A 435      16.979  13.244   6.121  1.00138.47           C  
ANISOU 3094  CD1 LEU A 435    25766  16517  10328  -1150   -632  -2198       C  
ATOM   3095  CD2 LEU A 435      18.772  11.850   5.067  1.00125.80           C  
ANISOU 3095  CD2 LEU A 435    24110  14540   9147  -1273  -1063  -1893       C  
ATOM   3096  N   LEU A 436      19.549  16.297   2.320  1.00115.97           N  
ANISOU 3096  N   LEU A 436    21506  13325   9232  -1199  -1945  -2526       N  
ATOM   3097  CA  LEU A 436      20.020  16.668   0.991  1.00119.89           C  
ANISOU 3097  CA  LEU A 436    21590  13766  10198  -1337  -2089  -2500       C  
ATOM   3098  C   LEU A 436      21.087  15.684   0.536  1.00132.77           C  
ANISOU 3098  C   LEU A 436    23111  15331  12003  -1457  -2257  -2333       C  
ATOM   3099  O   LEU A 436      21.957  15.302   1.319  1.00160.16           O  
ANISOU 3099  O   LEU A 436    26830  18725  15299  -1363  -2516  -2318       O  
ATOM   3100  CB  LEU A 436      20.576  18.091   0.979  1.00118.69           C  
ANISOU 3100  CB  LEU A 436    21452  13452  10192  -1270  -2437  -2687       C  
ATOM   3101  CG  LEU A 436      21.002  18.610  -0.396  1.00111.00           C  
ANISOU 3101  CG  LEU A 436    20100  12404   9670  -1429  -2543  -2647       C  
ATOM   3102  CD1 LEU A 436      19.822  19.231  -1.120  1.00106.75           C  
ANISOU 3102  CD1 LEU A 436    19396  11952   9214  -1365  -2265  -2681       C  
ATOM   3103  CD2 LEU A 436      22.147  19.604  -0.280  1.00115.76           C  
ANISOU 3103  CD2 LEU A 436    20770  12789  10427  -1485  -2974  -2779       C  
ATOM   3104  N   VAL A 437      21.024  15.272  -0.726  1.00106.65           N  
ANISOU 3104  N   VAL A 437    19435  12073   9012  -1624  -2123  -2222       N  
ATOM   3105  CA  VAL A 437      22.027  14.362  -1.262  1.00 94.81           C  
ANISOU 3105  CA  VAL A 437    17809  10525   7690  -1700  -2268  -2084       C  
ATOM   3106  C   VAL A 437      22.812  15.036  -2.371  1.00110.04           C  
ANISOU 3106  C   VAL A 437    19352  12435  10023  -1805  -2491  -2108       C  
ATOM   3107  O   VAL A 437      22.285  15.301  -3.450  1.00117.64           O  
ANISOU 3107  O   VAL A 437    20025  13463  11210  -1915  -2312  -2083       O  
ATOM   3108  CB  VAL A 437      21.409  13.078  -1.811  1.00 93.67           C  
ANISOU 3108  CB  VAL A 437    17605  10440   7544  -1826  -1907  -1928       C  
ATOM   3109  CG1 VAL A 437      22.484  12.012  -1.955  1.00 93.79           C  
ANISOU 3109  CG1 VAL A 437    17672  10355   7609  -1794  -2075  -1798       C  
ATOM   3110  CG2 VAL A 437      20.295  12.589  -0.899  1.00 96.60           C  
ANISOU 3110  CG2 VAL A 437    18299  10864   7540  -1824  -1556  -1912       C  
ATOM   3111  N   THR A 438      24.076  15.324  -2.094  1.00110.34           N  
ANISOU 3111  N   THR A 438    19383  12410  10132  -1775  -2881  -2162       N  
ATOM   3112  CA  THR A 438      24.922  16.047  -3.032  1.00115.31           C  
ANISOU 3112  CA  THR A 438    19662  13028  11124  -1925  -3089  -2196       C  
ATOM   3113  C   THR A 438      26.363  15.791  -2.652  1.00120.47           C  
ANISOU 3113  C   THR A 438    20257  13713  11805  -1892  -3475  -2236       C  
ATOM   3114  O   THR A 438      26.664  15.499  -1.497  1.00119.50           O  
ANISOU 3114  O   THR A 438    20427  13586  11394  -1716  -3661  -2293       O  
ATOM   3115  CB  THR A 438      24.651  17.567  -3.027  1.00120.45           C  
ANISOU 3115  CB  THR A 438    20356  13560  11849  -1982  -3166  -2344       C  
ATOM   3116  OG1 THR A 438      23.243  17.817  -3.071  1.00144.83           O  
ANISOU 3116  OG1 THR A 438    23550  16665  14812  -1899  -2841  -2348       O  
ATOM   3117  CG2 THR A 438      25.307  18.233  -4.217  1.00107.51           C  
ANISOU 3117  CG2 THR A 438    18378  11886  10585  -2197  -3256  -2321       C  
ATOM   3118  N   ASN A 439      27.254  15.866  -3.629  1.00124.68           N  
ANISOU 3118  N   ASN A 439    20396  14317  12659  -2040  -3590  -2211       N  
ATOM   3119  CA  ASN A 439      28.661  15.695  -3.352  1.00129.24           C  
ANISOU 3119  CA  ASN A 439    20809  15009  13289  -2011  -3964  -2285       C  
ATOM   3120  C   ASN A 439      29.351  17.062  -3.352  1.00114.71           C  
ANISOU 3120  C   ASN A 439    18819  13133  11633  -2244  -4235  -2468       C  
ATOM   3121  O   ASN A 439      30.573  17.154  -3.215  1.00102.29           O  
ANISOU 3121  O   ASN A 439    17007  11705  10154  -2306  -4562  -2580       O  
ATOM   3122  CB  ASN A 439      29.276  14.769  -4.404  1.00135.27           C  
ANISOU 3122  CB  ASN A 439    21207  15924  14266  -2016  -3898  -2156       C  
ATOM   3123  CG  ASN A 439      30.222  13.756  -3.810  1.00130.88           C  
ANISOU 3123  CG  ASN A 439    20672  15499  13556  -1749  -4151  -2159       C  
ATOM   3124  OD1 ASN A 439      29.937  13.166  -2.769  1.00118.20           O  
ANISOU 3124  OD1 ASN A 439    19476  13822  11611  -1504  -4188  -2137       O  
ATOM   3125  ND2 ASN A 439      31.349  13.537  -4.474  1.00142.28           N  
ANISOU 3125  ND2 ASN A 439    21686  17151  15224  -1766  -4316  -2181       N  
ATOM   3126  N   ASP A 440      28.560  18.126  -3.485  1.00110.89           N  
ANISOU 3126  N   ASP A 440    18487  12458  11188  -2370  -4099  -2513       N  
ATOM   3127  CA  ASP A 440      29.122  19.470  -3.565  1.00137.10           C  
ANISOU 3127  CA  ASP A 440    21752  15649  14688  -2634  -4309  -2675       C  
ATOM   3128  C   ASP A 440      29.550  19.995  -2.206  1.00160.89           C  
ANISOU 3128  C   ASP A 440    25046  18607  17479  -2584  -4664  -2922       C  
ATOM   3129  O   ASP A 440      28.719  20.213  -1.323  1.00162.50           O  
ANISOU 3129  O   ASP A 440    25666  18684  17393  -2392  -4616  -2994       O  
ATOM   3130  CB  ASP A 440      28.113  20.444  -4.187  1.00149.10           C  
ANISOU 3130  CB  ASP A 440    23418  16936  16298  -2721  -4050  -2635       C  
ATOM   3131  CG  ASP A 440      28.418  20.760  -5.638  1.00143.43           C  
ANISOU 3131  CG  ASP A 440    22361  16218  15920  -2977  -3912  -2500       C  
ATOM   3132  OD1 ASP A 440      29.614  20.826  -5.997  1.00133.48           O  
ANISOU 3132  OD1 ASP A 440    20784  15064  14868  -3218  -4092  -2530       O  
ATOM   3133  OD2 ASP A 440      27.460  20.953  -6.418  1.00140.01           O  
ANISOU 3133  OD2 ASP A 440    21964  15709  15523  -2928  -3621  -2373       O  
ATOM   3134  N   GLU A 441      30.849  20.216  -2.049  1.00176.74           N  
ANISOU 3134  N   GLU A 441    26799  20745  19608  -2762  -5021  -3075       N  
ATOM   3135  CA  GLU A 441      31.358  20.931  -0.892  1.00194.58           C  
ANISOU 3135  CA  GLU A 441    29276  22956  21700  -2800  -5405  -3364       C  
ATOM   3136  C   GLU A 441      30.846  22.361  -0.988  1.00190.28           C  
ANISOU 3136  C   GLU A 441    29006  22048  21245  -3033  -5343  -3485       C  
ATOM   3137  O   GLU A 441      30.627  23.021   0.028  1.00200.88           O  
ANISOU 3137  O   GLU A 441    30679  23255  22391  -2935  -5456  -3670       O  
ATOM   3138  CB  GLU A 441      32.890  20.872  -0.831  1.00216.96           C  
ANISOU 3138  CB  GLU A 441    31678  26077  24681  -2986  -5803  -3530       C  
ATOM   3139  CG  GLU A 441      33.619  21.656  -1.924  1.00234.11           C  
ANISOU 3139  CG  GLU A 441    33431  28240  27280  -3480  -5786  -3556       C  
ATOM   3140  CD  GLU A 441      33.401  21.103  -3.321  1.00236.44           C  
ANISOU 3140  CD  GLU A 441    33411  28603  27821  -3518  -5409  -3260       C  
ATOM   3141  OE1 GLU A 441      32.925  19.955  -3.448  1.00237.94           O  
ANISOU 3141  OE1 GLU A 441    33613  28911  27884  -3174  -5227  -3068       O  
ATOM   3142  OE2 GLU A 441      33.705  21.821  -4.296  1.00236.73           O  
ANISOU 3142  OE2 GLU A 441    33224  28560  28163  -3906  -5289  -3223       O  
ATOM   3143  N   MET A 442      30.688  22.815  -2.235  1.00177.21           N  
ANISOU 3143  N   MET A 442    27164  20263  19904  -3280  -5095  -3337       N  
ATOM   3144  CA  MET A 442      30.177  24.140  -2.601  1.00154.79           C  
ANISOU 3144  CA  MET A 442    24603  17031  17178  -3476  -4982  -3383       C  
ATOM   3145  C   MET A 442      30.927  25.289  -1.909  1.00134.27           C  
ANISOU 3145  C   MET A 442    22103  14270  14643  -3720  -5247  -3653       C  
ATOM   3146  O   MET A 442      30.343  26.330  -1.610  1.00137.75           O  
ANISOU 3146  O   MET A 442    22932  14369  15035  -3687  -5173  -3740       O  
ATOM   3147  CB  MET A 442      28.651  24.236  -2.386  1.00150.00           C  
ANISOU 3147  CB  MET A 442    24410  16248  16334  -3114  -4694  -3310       C  
ATOM   3148  CG  MET A 442      28.108  24.146  -0.969  1.00147.33           C  
ANISOU 3148  CG  MET A 442    24483  15902  15594  -2789  -4800  -3487       C  
ATOM   3149  SD  MET A 442      26.314  23.902  -0.935  1.00206.41           S  
ANISOU 3149  SD  MET A 442    32240  23364  22822  -2369  -4362  -3353       S  
ATOM   3150  CE  MET A 442      26.159  22.251  -1.597  1.00103.51           C  
ANISOU 3150  CE  MET A 442    18802  10696   9832  -2284  -4104  -3054       C  
ATOM   3151  N   ARG A 443      32.229  25.108  -1.686  1.00145.86           N  
ANISOU 3151  N   ARG A 443    23171  16016  16234  -3940  -5521  -3785       N  
ATOM   3152  CA  ARG A 443      33.040  26.150  -1.063  1.00162.74           C  
ANISOU 3152  CA  ARG A 443    25290  18079  18465  -4212  -5737  -4058       C  
ATOM   3153  C   ARG A 443      33.473  27.136  -2.148  1.00185.46           C  
ANISOU 3153  C   ARG A 443    28037  20713  21716  -4727  -5604  -4017       C  
ATOM   3154  O   ARG A 443      34.638  27.221  -2.535  1.00187.66           O  
ANISOU 3154  O   ARG A 443    27852  21208  22244  -5127  -5721  -4097       O  
ATOM   3155  CB  ARG A 443      34.254  25.556  -0.327  1.00157.18           C  
ANISOU 3155  CB  ARG A 443    24181  17836  17704  -4223  -6104  -4261       C  
ATOM   3156  CG  ARG A 443      35.163  24.656  -1.163  1.00153.04           C  
ANISOU 3156  CG  ARG A 443    23066  17710  17373  -4375  -6183  -4165       C  
ATOM   3157  CD  ARG A 443      36.532  24.473  -0.517  1.00157.93           C  
ANISOU 3157  CD  ARG A 443    23229  18783  17995  -4476  -6579  -4444       C  
ATOM   3158  NE  ARG A 443      37.138  25.750  -0.143  1.00165.37           N  
ANISOU 3158  NE  ARG A 443    24135  19610  19088  -4887  -6687  -4736       N  
ATOM   3159  CZ  ARG A 443      38.437  26.024  -0.230  1.00166.79           C  
ANISOU 3159  CZ  ARG A 443    23766  20125  19482  -5283  -6900  -4976       C  
ATOM   3160  NH1 ARG A 443      39.285  25.112  -0.688  1.00167.05           N  
ANISOU 3160  NH1 ARG A 443    23210  20664  19598  -5286  -7044  -4954       N  
ATOM   3161  NH2 ARG A 443      38.890  27.216   0.136  1.00171.23           N  
ANISOU 3161  NH2 ARG A 443    24357  20528  20175  -5677  -6970  -5260       N  
ATOM   3162  N   ASP A 444      32.498  27.905  -2.619  1.00194.94           N  
ANISOU 3162  N   ASP A 444    29676  21464  22930  -4698  -5348  -3893       N  
ATOM   3163  CA  ASP A 444      32.719  28.888  -3.667  1.00195.56           C  
ANISOU 3163  CA  ASP A 444    29788  21214  23301  -5130  -5176  -3799       C  
ATOM   3164  C   ASP A 444      32.147  30.236  -3.243  1.00213.19           C  
ANISOU 3164  C   ASP A 444    32615  22914  25475  -5109  -5130  -3916       C  
ATOM   3165  O   ASP A 444      31.258  30.308  -2.397  1.00215.76           O  
ANISOU 3165  O   ASP A 444    33339  23122  25519  -4684  -5146  -4001       O  
ATOM   3166  CB  ASP A 444      32.080  28.415  -4.978  1.00182.86           C  
ANISOU 3166  CB  ASP A 444    28151  19567  21759  -5090  -4894  -3472       C  
ATOM   3167  CG  ASP A 444      32.211  29.431  -6.097  1.00181.75           C  
ANISOU 3167  CG  ASP A 444    28140  19052  21864  -5497  -4687  -3327       C  
ATOM   3168  OD1 ASP A 444      31.423  30.400  -6.115  1.00181.44           O  
ANISOU 3168  OD1 ASP A 444    28661  18525  21752  -5388  -4574  -3308       O  
ATOM   3169  OD2 ASP A 444      33.095  29.256  -6.961  1.00181.71           O  
ANISOU 3169  OD2 ASP A 444    27699  19242  22102  -5903  -4629  -3225       O  
ATOM   3170  N   HIS A 445      32.660  31.294  -3.863  1.00231.57           N  
ANISOU 3170  N   HIS A 445    35012  24916  28056  -5569  -5051  -3911       N  
ATOM   3171  CA  HIS A 445      32.393  32.675  -3.472  1.00244.39           C  
ANISOU 3171  CA  HIS A 445    37193  26000  29664  -5638  -5041  -4053       C  
ATOM   3172  C   HIS A 445      30.906  33.011  -3.463  1.00237.45           C  
ANISOU 3172  C   HIS A 445    36943  24740  28539  -5129  -4877  -3945       C  
ATOM   3173  O   HIS A 445      30.415  33.664  -2.540  1.00242.24           O  
ANISOU 3173  O   HIS A 445    37989  25096  28954  -4876  -4954  -4142       O  
ATOM   3174  CB  HIS A 445      33.136  33.620  -4.418  1.00255.15           C  
ANISOU 3174  CB  HIS A 445    38540  27057  31347  -6238  -4909  -3976       C  
ATOM   3175  CG  HIS A 445      34.557  33.219  -4.671  1.00263.82           C  
ANISOU 3175  CG  HIS A 445    38932  28597  32709  -6748  -5011  -4056       C  
ATOM   3176  ND1 HIS A 445      35.500  33.135  -3.669  1.00268.10           N  
ANISOU 3176  ND1 HIS A 445    39126  29468  33271  -6902  -5313  -4407       N  
ATOM   3177  CD2 HIS A 445      35.188  32.853  -5.812  1.00266.52           C  
ANISOU 3177  CD2 HIS A 445    38824  29155  33285  -7110  -4854  -3849       C  
ATOM   3178  CE1 HIS A 445      36.655  32.752  -4.184  1.00270.02           C  
ANISOU 3178  CE1 HIS A 445    38716  30115  33763  -7327  -5349  -4428       C  
ATOM   3179  NE2 HIS A 445      36.492  32.573  -5.483  1.00270.97           N  
ANISOU 3179  NE2 HIS A 445    38761  30178  34019  -7466  -5059  -4085       N  
ATOM   3180  N   ILE A 446      30.201  32.580  -4.504  1.00221.73           N  
ANISOU 3180  N   ILE A 446    34979  22726  26543  -4974  -4655  -3656       N  
ATOM   3181  CA  ILE A 446      28.764  32.808  -4.609  1.00215.62           C  
ANISOU 3181  CA  ILE A 446    34731  21666  25529  -4459  -4500  -3571       C  
ATOM   3182  C   ILE A 446      28.048  32.138  -3.442  1.00213.63           C  
ANISOU 3182  C   ILE A 446    34520  21694  24955  -3945  -4589  -3733       C  
ATOM   3183  O   ILE A 446      27.198  32.739  -2.785  1.00204.01           O  
ANISOU 3183  O   ILE A 446    33777  20229  23509  -3566  -4574  -3865       O  
ATOM   3184  CB  ILE A 446      28.183  32.273  -5.943  1.00133.84           C  
ANISOU 3184  CB  ILE A 446    24304  11343  15206  -4385  -4274  -3266       C  
ATOM   3185  CG1 ILE A 446      28.577  33.164  -7.132  1.00137.28           C  
ANISOU 3185  CG1 ILE A 446    24918  11370  15873  -4792  -4121  -3066       C  
ATOM   3186  CG2 ILE A 446      26.666  32.252  -5.884  1.00123.88           C  
ANISOU 3186  CG2 ILE A 446    23452   9965  13651  -3763  -4146  -3248       C  
ATOM   3187  CD1 ILE A 446      30.053  33.184  -7.499  1.00138.68           C  
ANISOU 3187  CD1 ILE A 446    24613  11714  16365  -5454  -4156  -3043       C  
ATOM   3188  N   PHE A 447      28.411  30.885  -3.191  1.00220.89           N  
ANISOU 3188  N   PHE A 447    34954  23131  25841  -3926  -4667  -3715       N  
ATOM   3189  CA  PHE A 447      27.871  30.118  -2.075  1.00223.64           C  
ANISOU 3189  CA  PHE A 447    35319  23781  25873  -3496  -4731  -3833       C  
ATOM   3190  C   PHE A 447      28.340  30.632  -0.714  1.00262.41           C  
ANISOU 3190  C   PHE A 447    40372  28671  30661  -3483  -4963  -4126       C  
ATOM   3191  O   PHE A 447      27.539  30.796   0.206  1.00265.57           O  
ANISOU 3191  O   PHE A 447    41120  29022  30763  -3084  -4950  -4256       O  
ATOM   3192  CB  PHE A 447      28.250  28.644  -2.218  1.00220.08           C  
ANISOU 3192  CB  PHE A 447    34364  23837  25418  -3501  -4759  -3713       C  
ATOM   3193  CG  PHE A 447      27.673  27.986  -3.439  1.00207.28           C  
ANISOU 3193  CG  PHE A 447    32605  22293  23859  -3463  -4529  -3455       C  
ATOM   3194  CD1 PHE A 447      26.357  27.554  -3.455  1.00200.09           C  
ANISOU 3194  CD1 PHE A 447    31790  21494  22740  -2994  -4254  -3338       C  
ATOM   3195  CD2 PHE A 447      28.451  27.793  -4.570  1.00201.11           C  
ANISOU 3195  CD2 PHE A 447    31405  21615  23393  -3823  -4462  -3265       C  
ATOM   3196  CE1 PHE A 447      25.825  26.948  -4.578  1.00194.72           C  
ANISOU 3196  CE1 PHE A 447    30804  21011  22168  -2895  -3951  -3055       C  
ATOM   3197  CE2 PHE A 447      27.927  27.188  -5.692  1.00194.41           C  
ANISOU 3197  CE2 PHE A 447    30286  20948  22634  -3693  -4149  -2968       C  
ATOM   3198  CZ  PHE A 447      26.612  26.764  -5.697  1.00192.58           C  
ANISOU 3198  CZ  PHE A 447    30161  20813  22196  -3233  -3909  -2871       C  
ATOM   3199  N   GLU A 448      29.641  30.886  -0.600  1.00301.87           N  
ANISOU 3199  N   GLU A 448    45081  33737  35878  -3925  -5170  -4249       N  
ATOM   3200  CA  GLU A 448      30.252  31.273   0.671  1.00334.24           C  
ANISOU 3200  CA  GLU A 448    49233  37896  39867  -3965  -5434  -4562       C  
ATOM   3201  C   GLU A 448      29.843  32.667   1.155  1.00360.33           C  
ANISOU 3201  C   GLU A 448    53102  40700  43108  -3927  -5430  -4753       C  
ATOM   3202  O   GLU A 448      29.893  32.938   2.351  1.00384.66           O  
ANISOU 3202  O   GLU A 448    56367  43809  45977  -3778  -5602  -5013       O  
ATOM   3203  CB  GLU A 448      31.779  31.180   0.583  1.00340.45           C  
ANISOU 3203  CB  GLU A 448    49499  38942  40915  -4471  -5661  -4685       C  
ATOM   3204  CG  GLU A 448      32.462  31.189   1.942  1.00343.59           C  
ANISOU 3204  CG  GLU A 448    49827  39583  41140  -4450  -5982  -5021       C  
ATOM   3205  CD  GLU A 448      31.878  30.154   2.888  1.00339.34           C  
ANISOU 3205  CD  GLU A 448    49364  39364  40204  -3910  -6039  -5003       C  
ATOM   3206  OE1 GLU A 448      31.712  28.988   2.469  1.00331.90           O  
ANISOU 3206  OE1 GLU A 448    48174  38712  39220  -3735  -5961  -4776       O  
ATOM   3207  OE2 GLU A 448      31.577  30.509   4.047  1.00342.28           O  
ANISOU 3207  OE2 GLU A 448    50071  39683  40295  -3668  -6148  -5213       O  
ATOM   3208  N   LEU A 449      29.508  33.571   0.239  1.00316.82           N  
ANISOU 3208  N   LEU A 449    47887  34720  37769  -4065  -5250  -4632       N  
ATOM   3209  CA  LEU A 449      28.998  34.873   0.659  1.00278.36           C  
ANISOU 3209  CA  LEU A 449    43633  29327  32804  -3944  -5233  -4793       C  
ATOM   3210  C   LEU A 449      27.723  34.640   1.467  1.00252.59           C  
ANISOU 3210  C   LEU A 449    40711  26118  29144  -3281  -5162  -4849       C  
ATOM   3211  O   LEU A 449      27.540  35.222   2.538  1.00251.16           O  
ANISOU 3211  O   LEU A 449    40859  25813  28757  -3091  -5270  -5105       O  
ATOM   3212  CB  LEU A 449      28.740  35.792  -0.537  1.00267.21           C  
ANISOU 3212  CB  LEU A 449    42550  27385  31593  -4115  -5030  -4599       C  
ATOM   3213  CG  LEU A 449      29.755  36.926  -0.719  1.00255.32           C  
ANISOU 3213  CG  LEU A 449    41149  25498  30362  -4705  -5101  -4719       C  
ATOM   3214  CD1 LEU A 449      29.704  37.897   0.455  1.00252.53           C  
ANISOU 3214  CD1 LEU A 449    41249  24849  29853  -4612  -5259  -5062       C  
ATOM   3215  CD2 LEU A 449      31.161  36.372  -0.889  1.00249.10           C  
ANISOU 3215  CD2 LEU A 449    39674  25127  29846  -5277  -5237  -4765       C  
ATOM   3216  N   LEU A 450      26.851  33.777   0.954  1.00231.41           N  
ANISOU 3216  N   LEU A 450    37931  23646  26347  -2947  -4968  -4627       N  
ATOM   3217  CA  LEU A 450      25.693  33.324   1.718  1.00209.58           C  
ANISOU 3217  CA  LEU A 450    35360  21071  23199  -2358  -4866  -4680       C  
ATOM   3218  C   LEU A 450      26.139  32.395   2.840  1.00205.96           C  
ANISOU 3218  C   LEU A 450    34623  21084  22547  -2306  -5029  -4795       C  
ATOM   3219  O   LEU A 450      25.582  32.420   3.939  1.00202.66           O  
ANISOU 3219  O   LEU A 450    34453  20750  21800  -1941  -5036  -4958       O  
ATOM   3220  CB  LEU A 450      24.678  32.616   0.822  1.00187.41           C  
ANISOU 3220  CB  LEU A 450    32477  18402  20327  -2071  -4605  -4442       C  
ATOM   3221  CG  LEU A 450      23.466  33.449   0.404  1.00179.63           C  
ANISOU 3221  CG  LEU A 450    31977  17059  19216  -1658  -4412  -4440       C  
ATOM   3222  CD1 LEU A 450      23.875  34.525  -0.592  1.00185.89           C  
ANISOU 3222  CD1 LEU A 450    33015  17320  20296  -1958  -4418  -4347       C  
ATOM   3223  CD2 LEU A 450      22.353  32.565  -0.156  1.00156.78           C  
ANISOU 3223  CD2 LEU A 450    28949  14468  16153  -1287  -4168  -4299       C  
ATOM   3224  N   GLY A 451      27.141  31.569   2.542  1.00212.13           N  
ANISOU 3224  N   GLY A 451    34906  22179  23514  -2643  -5153  -4703       N  
ATOM   3225  CA  GLY A 451      27.634  30.576   3.477  1.00217.36           C  
ANISOU 3225  CA  GLY A 451    35308  23294  23987  -2565  -5324  -4772       C  
ATOM   3226  C   GLY A 451      28.134  31.230   4.744  1.00228.61           C  
ANISOU 3226  C   GLY A 451    36926  24678  25257  -2576  -5574  -5091       C  
ATOM   3227  O   GLY A 451      28.858  32.220   4.706  1.00246.17           O  
ANISOU 3227  O   GLY A 451    39199  26644  27691  -2930  -5724  -5268       O  
ATOM   3228  N   SER A 452      27.747  30.676   5.881  1.00221.57           N  
ANISOU 3228  N   SER A 452    36161  24042  23983  -2205  -5609  -5172       N  
ATOM   3229  CA  SER A 452      28.034  31.324   7.148  1.00214.96           C  
ANISOU 3229  CA  SER A 452    35581  23164  22932  -2142  -5824  -5485       C  
ATOM   3230  C   SER A 452      28.510  30.347   8.211  1.00190.78           C  
ANISOU 3230  C   SER A 452    32363  20556  19569  -1984  -6024  -5545       C  
ATOM   3231  O   SER A 452      29.280  29.426   7.943  1.00182.63           O  
ANISOU 3231  O   SER A 452    30922  19842  18629  -2127  -6152  -5433       O  
ATOM   3232  CB  SER A 452      26.787  32.054   7.647  1.00231.19           C  
ANISOU 3232  CB  SER A 452    38173  24948  24722  -1732  -5627  -5577       C  
ATOM   3233  OG  SER A 452      25.611  31.302   7.378  1.00226.62           O  
ANISOU 3233  OG  SER A 452    37635  24520  23951  -1349  -5312  -5355       O  
ATOM   3234  N   THR A 453      28.053  30.590   9.432  1.00182.65           N  
ANISOU 3234  N   THR A 453    31696  19545  18159  -1662  -6055  -5726       N  
ATOM   3235  CA  THR A 453      28.266  29.689  10.549  1.00175.45           C  
ANISOU 3235  CA  THR A 453    30772  19028  16861  -1409  -6196  -5755       C  
ATOM   3236  C   THR A 453      27.068  28.745  10.581  1.00164.78           C  
ANISOU 3236  C   THR A 453    29562  17824  15223   -997  -5847  -5490       C  
ATOM   3237  O   THR A 453      27.179  27.566  10.926  1.00165.69           O  
ANISOU 3237  O   THR A 453    29572  18266  15117   -840  -5853  -5332       O  
ATOM   3238  CB  THR A 453      28.400  30.453  11.864  1.00180.13           C  
ANISOU 3238  CB  THR A 453    31698  19577  17166  -1293  -6397  -6094       C  
ATOM   3239  OG1 THR A 453      27.186  31.170  12.129  1.00178.65           O  
ANISOU 3239  OG1 THR A 453    31968  19113  16799   -988  -6134  -6150       O  
ATOM   3240  CG2 THR A 453      29.559  31.441  11.776  1.00186.04           C  
ANISOU 3240  CG2 THR A 453    32303  20168  18214  -1770  -6716  -6390       C  
ATOM   3241  N   PHE A 454      25.923  29.293  10.184  1.00173.10           N  
ANISOU 3241  N   PHE A 454    30862  18630  16278   -830  -5535  -5452       N  
ATOM   3242  CA  PHE A 454      24.675  28.553  10.043  1.00171.46           C  
ANISOU 3242  CA  PHE A 454    30746  18563  15839   -497  -5148  -5240       C  
ATOM   3243  C   PHE A 454      24.822  27.494   8.950  1.00163.62           C  
ANISOU 3243  C   PHE A 454    29381  17722  15066   -666  -5043  -4941       C  
ATOM   3244  O   PHE A 454      24.316  26.380   9.084  1.00170.03           O  
ANISOU 3244  O   PHE A 454    30170  18792  15640   -484  -4841  -4752       O  
ATOM   3245  CB  PHE A 454      23.520  29.517   9.733  1.00177.13           C  
ANISOU 3245  CB  PHE A 454    31749  19000  16551   -288  -4881  -5316       C  
ATOM   3246  CG  PHE A 454      22.201  28.840   9.458  1.00177.24           C  
ANISOU 3246  CG  PHE A 454    31783  19207  16354     21  -4462  -5142       C  
ATOM   3247  CD1 PHE A 454      21.863  27.642  10.064  1.00176.66           C  
ANISOU 3247  CD1 PHE A 454    31678  19507  15939    186  -4298  -5005       C  
ATOM   3248  CD2 PHE A 454      21.293  29.414   8.587  1.00177.63           C  
ANISOU 3248  CD2 PHE A 454    31893  19070  16527    143  -4224  -5123       C  
ATOM   3249  CE1 PHE A 454      20.661  27.031   9.795  1.00174.96           C  
ANISOU 3249  CE1 PHE A 454    31451  19493  15531    399  -3883  -4869       C  
ATOM   3250  CE2 PHE A 454      20.082  28.806   8.325  1.00168.20           C  
ANISOU 3250  CE2 PHE A 454    30658  18120  15129    413  -3838  -5009       C  
ATOM   3251  CZ  PHE A 454      19.764  27.616   8.927  1.00164.31           C  
ANISOU 3251  CZ  PHE A 454    30095  18020  14316    509  -3654  -4890       C  
ATOM   3252  N   PHE A 455      25.517  27.841   7.871  1.00156.46           N  
ANISOU 3252  N   PHE A 455    28202  16647  14600  -1030  -5164  -4900       N  
ATOM   3253  CA  PHE A 455      25.637  26.935   6.730  1.00156.90           C  
ANISOU 3253  CA  PHE A 455    27906  16822  14885  -1195  -5057  -4632       C  
ATOM   3254  C   PHE A 455      26.328  25.614   7.058  1.00129.91           C  
ANISOU 3254  C   PHE A 455    24262  13755  11342  -1189  -5195  -4505       C  
ATOM   3255  O   PHE A 455      25.846  24.549   6.667  1.00132.49           O  
ANISOU 3255  O   PHE A 455    24515  14243  11580  -1089  -4980  -4277       O  
ATOM   3256  CB  PHE A 455      26.387  27.625   5.600  1.00158.51           C  
ANISOU 3256  CB  PHE A 455    27867  16793  15567  -1611  -5177  -4629       C  
ATOM   3257  CG  PHE A 455      26.107  27.046   4.249  1.00159.00           C  
ANISOU 3257  CG  PHE A 455    27676  16877  15861  -1729  -4971  -4368       C  
ATOM   3258  CD1 PHE A 455      24.806  26.867   3.826  1.00148.16           C  
ANISOU 3258  CD1 PHE A 455    26458  15478  14358  -1476  -4633  -4252       C  
ATOM   3259  CD2 PHE A 455      27.148  26.725   3.378  1.00154.67           C  
ANISOU 3259  CD2 PHE A 455    26713  16399  15654  -2097  -5113  -4267       C  
ATOM   3260  CE1 PHE A 455      24.537  26.333   2.580  1.00132.68           C  
ANISOU 3260  CE1 PHE A 455    24266  13557  12589  -1589  -4455  -4037       C  
ATOM   3261  CE2 PHE A 455      26.880  26.202   2.127  1.00125.59           C  
ANISOU 3261  CE2 PHE A 455    22811  12739  12168  -2201  -4920  -4034       C  
ATOM   3262  CZ  PHE A 455      25.566  26.007   1.734  1.00116.73           C  
ANISOU 3262  CZ  PHE A 455    21873  11579  10902  -1949  -4599  -3921       C  
ATOM   3263  N   GLN A 456      27.427  25.689   7.801  1.00133.68           N  
ANISOU 3263  N   GLN A 456    24660  14349  11784  -1273  -5554  -4667       N  
ATOM   3264  CA  GLN A 456      28.141  24.507   8.260  1.00140.29           C  
ANISOU 3264  CA  GLN A 456    25344  15518  12443  -1179  -5743  -4578       C  
ATOM   3265  C   GLN A 456      27.296  23.689   9.232  1.00145.95           C  
ANISOU 3265  C   GLN A 456    26420  16381  12654   -770  -5548  -4471       C  
ATOM   3266  O   GLN A 456      27.417  22.470   9.291  1.00142.18           O  
ANISOU 3266  O   GLN A 456    25913  16102  12007   -639  -5525  -4270       O  
ATOM   3267  CB  GLN A 456      29.476  24.904   8.892  1.00166.96           C  
ANISOU 3267  CB  GLN A 456    28550  19023  15862  -1334  -6193  -4830       C  
ATOM   3268  CG  GLN A 456      30.638  24.987   7.907  1.00186.80           C  
ANISOU 3268  CG  GLN A 456    30552  21603  18822  -1744  -6405  -4852       C  
ATOM   3269  CD  GLN A 456      30.280  25.706   6.612  1.00185.12           C  
ANISOU 3269  CD  GLN A 456    30235  21080  19021  -2054  -6175  -4775       C  
ATOM   3270  OE1 GLN A 456      29.614  26.744   6.621  1.00191.96           O  
ANISOU 3270  OE1 GLN A 456    31393  21623  19919  -2074  -6027  -4869       O  
ATOM   3271  NE2 GLN A 456      30.732  25.157   5.490  1.00166.54           N  
ANISOU 3271  NE2 GLN A 456    27491  18823  16965  -2267  -6149  -4602       N  
ATOM   3272  N   LYS A 457      26.461  24.368  10.013  1.00160.04           N  
ANISOU 3272  N   LYS A 457    28568  18060  14180   -567  -5399  -4608       N  
ATOM   3273  CA  LYS A 457      25.558  23.681  10.932  1.00165.33           C  
ANISOU 3273  CA  LYS A 457    29586  18879  14355   -210  -5144  -4510       C  
ATOM   3274  C   LYS A 457      24.526  22.890  10.143  1.00157.36           C  
ANISOU 3274  C   LYS A 457    28556  17902  13333   -175  -4711  -4249       C  
ATOM   3275  O   LYS A 457      24.283  21.712  10.415  1.00162.11           O  
ANISOU 3275  O   LYS A 457    29263  18676  13657    -44  -4550  -4040       O  
ATOM   3276  CB  LYS A 457      24.848  24.676  11.852  1.00165.81           C  
ANISOU 3276  CB  LYS A 457    30001  18839  14161     -4  -5053  -4741       C  
ATOM   3277  CG  LYS A 457      25.743  25.378  12.854  1.00167.72           C  
ANISOU 3277  CG  LYS A 457    30344  19077  14304     -6  -5454  -5024       C  
ATOM   3278  CD  LYS A 457      25.039  26.594  13.439  1.00174.48           C  
ANISOU 3278  CD  LYS A 457    31526  19739  15028    137  -5360  -5281       C  
ATOM   3279  CE  LYS A 457      23.653  26.240  13.964  1.00173.21           C  
ANISOU 3279  CE  LYS A 457    31666  19692  14453    499  -4924  -5189       C  
ATOM   3280  NZ  LYS A 457      22.885  27.455  14.364  1.00181.37           N  
ANISOU 3280  NZ  LYS A 457    32985  20538  15389    679  -4805  -5442       N  
ATOM   3281  N   TRP A 458      23.941  23.547   9.150  1.00143.61           N  
ANISOU 3281  N   TRP A 458    26698  15984  11884   -304  -4526  -4265       N  
ATOM   3282  CA  TRP A 458      22.931  22.928   8.313  1.00135.30           C  
ANISOU 3282  CA  TRP A 458    25582  14987  10841   -297  -4124  -4068       C  
ATOM   3283  C   TRP A 458      23.499  21.796   7.466  1.00132.54           C  
ANISOU 3283  C   TRP A 458    24958  14727  10675   -494  -4160  -3830       C  
ATOM   3284  O   TRP A 458      22.834  20.781   7.258  1.00135.00           O  
ANISOU 3284  O   TRP A 458    25315  15168  10813   -452  -3853  -3638       O  
ATOM   3285  CB  TRP A 458      22.292  23.973   7.405  1.00137.93           C  
ANISOU 3285  CB  TRP A 458    25851  15110  11446   -354  -3985  -4161       C  
ATOM   3286  CG  TRP A 458      21.007  23.525   6.795  1.00138.38           C  
ANISOU 3286  CG  TRP A 458    25889  15288  11400   -256  -3545  -4045       C  
ATOM   3287  CD1 TRP A 458      19.776  23.496   7.384  1.00123.05           C  
ANISOU 3287  CD1 TRP A 458    24155  13513   9086     23  -3189  -4102       C  
ATOM   3288  CD2 TRP A 458      20.834  22.999   5.474  1.00127.90           C  
ANISOU 3288  CD2 TRP A 458    24286  13981  10328   -452  -3404  -3873       C  
ATOM   3289  NE1 TRP A 458      18.843  23.007   6.500  1.00120.01           N  
ANISOU 3289  NE1 TRP A 458    23615  13271   8712      0  -2835  -3994       N  
ATOM   3290  CE2 TRP A 458      19.469  22.691   5.325  1.00126.74           C  
ANISOU 3290  CE2 TRP A 458    24116  14041   9997   -286  -2945  -3818       C  
ATOM   3291  CE3 TRP A 458      21.703  22.768   4.403  1.00130.37           C  
ANISOU 3291  CE3 TRP A 458    24284  14207  11043   -754  -3589  -3746       C  
ATOM   3292  CZ2 TRP A 458      18.954  22.158   4.145  1.00127.17           C  
ANISOU 3292  CZ2 TRP A 458    23739  14240  10341   -413  -2650  -3598       C  
ATOM   3293  CZ3 TRP A 458      21.190  22.242   3.237  1.00110.51           C  
ANISOU 3293  CZ3 TRP A 458    21380  11813   8797   -852  -3279  -3512       C  
ATOM   3294  CH2 TRP A 458      19.828  21.943   3.116  1.00115.23           C  
ANISOU 3294  CH2 TRP A 458    21917  12621   9246   -685  -2830  -3447       C  
ATOM   3295  N   LYS A 459      24.725  21.967   6.976  1.00121.88           N  
ANISOU 3295  N   LYS A 459    23323  13319   9668   -722  -4518  -3857       N  
ATOM   3296  CA  LYS A 459      25.355  20.931   6.156  1.00118.90           C  
ANISOU 3296  CA  LYS A 459    22664  13039   9472   -878  -4584  -3657       C  
ATOM   3297  C   LYS A 459      25.613  19.643   6.939  1.00140.28           C  
ANISOU 3297  C   LYS A 459    25553  15935  11813   -670  -4621  -3513       C  
ATOM   3298  O   LYS A 459      25.285  18.563   6.463  1.00142.39           O  
ANISOU 3298  O   LYS A 459    25834  16256  12011   -671  -4408  -3296       O  
ATOM   3299  CB  LYS A 459      26.659  21.451   5.532  1.00119.29           C  
ANISOU 3299  CB  LYS A 459    22334  13043   9946  -1162  -4954  -3749       C  
ATOM   3300  CG  LYS A 459      26.442  22.348   4.311  1.00117.04           C  
ANISOU 3300  CG  LYS A 459    21852  12547  10073  -1433  -4846  -3764       C  
ATOM   3301  CD  LYS A 459      27.748  22.843   3.695  1.00118.04           C  
ANISOU 3301  CD  LYS A 459    21600  12644  10604  -1775  -5157  -3841       C  
ATOM   3302  CE  LYS A 459      28.748  21.717   3.482  1.00117.37           C  
ANISOU 3302  CE  LYS A 459    21202  12827  10567  -1815  -5363  -3738       C  
ATOM   3303  NZ  LYS A 459      30.109  22.255   3.183  1.00119.89           N  
ANISOU 3303  NZ  LYS A 459    21126  13215  11211  -2129  -5697  -3886       N  
ATOM   3304  N   GLU A 460      26.167  19.754   8.142  1.00153.80           N  
ANISOU 3304  N   GLU A 460    27447  17728  13263   -483  -4881  -3631       N  
ATOM   3305  CA  GLU A 460      26.379  18.583   8.987  1.00171.43           C  
ANISOU 3305  CA  GLU A 460    29941  20110  15087   -222  -4919  -3479       C  
ATOM   3306  C   GLU A 460      25.021  18.006   9.356  1.00172.68           C  
ANISOU 3306  C   GLU A 460    30479  20263  14866    -82  -4420  -3315       C  
ATOM   3307  O   GLU A 460      24.856  16.794   9.472  1.00186.14           O  
ANISOU 3307  O   GLU A 460    32394  22013  16319     14  -4251  -3079       O  
ATOM   3308  CB  GLU A 460      27.191  18.939  10.236  1.00188.34           C  
ANISOU 3308  CB  GLU A 460    32205  22357  16998    -33  -5301  -3663       C  
ATOM   3309  CG  GLU A 460      28.453  19.734   9.954  1.00197.74           C  
ANISOU 3309  CG  GLU A 460    32987  23588  18556   -242  -5759  -3898       C  
ATOM   3310  CD  GLU A 460      29.544  18.967   9.205  1.00202.35           C  
ANISOU 3310  CD  GLU A 460    33191  24319  19374   -324  -6021  -3805       C  
ATOM   3311  OE1 GLU A 460      29.323  17.829   8.741  1.00201.61           O  
ANISOU 3311  OE1 GLU A 460    33156  24240  19207   -226  -5853  -3549       O  
ATOM   3312  OE2 GLU A 460      30.630  19.552   9.021  1.00204.41           O  
ANISOU 3312  OE2 GLU A 460    33073  24684  19911   -515  -6383  -4009       O  
ATOM   3313  N   ARG A 461      24.047  18.892   9.514  1.00150.12           N  
ANISOU 3313  N   ARG A 461    27713  17355  11971    -77  -4170  -3449       N  
ATOM   3314  CA  ARG A 461      22.687  18.499   9.851  1.00142.05           C  
ANISOU 3314  CA  ARG A 461    26974  16400  10600     28  -3661  -3348       C  
ATOM   3315  C   ARG A 461      21.985  17.710   8.733  1.00135.43           C  
ANISOU 3315  C   ARG A 461    26003  15571   9883   -169  -3286  -3149       C  
ATOM   3316  O   ARG A 461      21.239  16.774   9.018  1.00126.71           O  
ANISOU 3316  O   ARG A 461    25141  14555   8450   -144  -2901  -2971       O  
ATOM   3317  CB  ARG A 461      21.870  19.741  10.220  1.00146.93           C  
ANISOU 3317  CB  ARG A 461    27661  16996  11168    124  -3522  -3588       C  
ATOM   3318  CG  ARG A 461      20.400  19.496  10.531  1.00150.16           C  
ANISOU 3318  CG  ARG A 461    28270  17553  11230    237  -2973  -3543       C  
ATOM   3319  CD  ARG A 461      20.207  18.535  11.686  1.00157.01           C  
ANISOU 3319  CD  ARG A 461    29513  18563  11580    397  -2790  -3383       C  
ATOM   3320  NE  ARG A 461      18.795  18.219  11.893  1.00170.58           N  
ANISOU 3320  NE  ARG A 461    31360  20469  12982    425  -2202  -3327       N  
ATOM   3321  CZ  ARG A 461      18.165  17.175  11.361  1.00178.88           C  
ANISOU 3321  CZ  ARG A 461    32396  21606  13963    233  -1790  -3104       C  
ATOM   3322  NH1 ARG A 461      18.819  16.319  10.587  1.00178.58           N  
ANISOU 3322  NH1 ARG A 461    32269  21445  14140     37  -1915  -2906       N  
ATOM   3323  NH2 ARG A 461      16.876  16.986  11.606  1.00182.98           N  
ANISOU 3323  NH2 ARG A 461    32977  22354  14194    223  -1238  -3095       N  
ATOM   3324  N   HIS A 462      22.198  18.087   7.472  1.00138.14           N  
ANISOU 3324  N   HIS A 462    25979  15827  10682   -391  -3372  -3181       N  
ATOM   3325  CA  HIS A 462      21.330  17.587   6.400  1.00128.61           C  
ANISOU 3325  CA  HIS A 462    24449  14686   9731   -563  -2922  -2989       C  
ATOM   3326  C   HIS A 462      21.997  16.939   5.176  1.00132.65           C  
ANISOU 3326  C   HIS A 462    24541  15166  10694   -778  -2988  -2799       C  
ATOM   3327  O   HIS A 462      21.340  16.212   4.427  1.00129.95           O  
ANISOU 3327  O   HIS A 462    23991  14896  10487   -911  -2617  -2617       O  
ATOM   3328  CB  HIS A 462      20.442  18.736   5.929  1.00113.83           C  
ANISOU 3328  CB  HIS A 462    22416  12811   8025   -559  -2747  -3160       C  
ATOM   3329  CG  HIS A 462      19.302  19.018   6.854  1.00117.45           C  
ANISOU 3329  CG  HIS A 462    23177  13403   8046   -345  -2433  -3281       C  
ATOM   3330  ND1 HIS A 462      18.618  20.214   6.854  1.00122.76           N  
ANISOU 3330  ND1 HIS A 462    23864  14059   8720   -193  -2374  -3514       N  
ATOM   3331  CD2 HIS A 462      18.717  18.252   7.804  1.00119.80           C  
ANISOU 3331  CD2 HIS A 462    23788  13861   7871   -246  -2137  -3198       C  
ATOM   3332  CE1 HIS A 462      17.670  20.179   7.772  1.00121.37           C  
ANISOU 3332  CE1 HIS A 462    23950  14072   8094     11  -2062  -3593       C  
ATOM   3333  NE2 HIS A 462      17.706  18.997   8.361  1.00125.01           N  
ANISOU 3333  NE2 HIS A 462    24591  14648   8259    -46  -1897  -3397       N  
ATOM   3334  N   GLN A 463      23.285  17.190   4.967  1.00131.88           N  
ANISOU 3334  N   GLN A 463    24300  14991  10818   -823  -3449  -2863       N  
ATOM   3335  CA  GLN A 463      23.946  16.729   3.743  1.00125.27           C  
ANISOU 3335  CA  GLN A 463    23023  14154  10421  -1013  -3509  -2719       C  
ATOM   3336  C   GLN A 463      24.350  15.256   3.774  1.00132.33           C  
ANISOU 3336  C   GLN A 463    23977  15094  11207   -948  -3466  -2488       C  
ATOM   3337  O   GLN A 463      24.913  14.765   4.757  1.00134.21           O  
ANISOU 3337  O   GLN A 463    24544  15342  11106   -739  -3688  -2480       O  
ATOM   3338  CB  GLN A 463      25.174  17.585   3.440  1.00122.09           C  
ANISOU 3338  CB  GLN A 463    22382  13693  10312  -1124  -3980  -2889       C  
ATOM   3339  CG  GLN A 463      25.360  17.868   1.959  1.00111.32           C  
ANISOU 3339  CG  GLN A 463    20535  12305   9458  -1380  -3910  -2818       C  
ATOM   3340  CD  GLN A 463      26.679  18.543   1.661  1.00125.83           C  
ANISOU 3340  CD  GLN A 463    22116  14118  11577  -1553  -4339  -2960       C  
ATOM   3341  OE1 GLN A 463      27.531  18.681   2.539  1.00135.83           O  
ANISOU 3341  OE1 GLN A 463    23508  15425  12676  -1482  -4724  -3122       O  
ATOM   3342  NE2 GLN A 463      26.860  18.964   0.416  1.00129.24           N  
ANISOU 3342  NE2 GLN A 463    22175  14511  12421  -1796  -4270  -2907       N  
ATOM   3343  N   VAL A 464      24.064  14.572   2.669  1.00125.98           N  
ANISOU 3343  N   VAL A 464    22883  14305  10679  -1105  -3192  -2310       N  
ATOM   3344  CA  VAL A 464      24.401  13.166   2.486  1.00121.39           C  
ANISOU 3344  CA  VAL A 464    22362  13708  10051  -1059  -3115  -2092       C  
ATOM   3345  C   VAL A 464      25.508  13.051   1.445  1.00102.90           C  
ANISOU 3345  C   VAL A 464    19578  11398   8119  -1130  -3373  -2075       C  
ATOM   3346  O   VAL A 464      25.561  13.839   0.506  1.00128.56           O  
ANISOU 3346  O   VAL A 464    22432  14680  11736  -1322  -3387  -2150       O  
ATOM   3347  CB  VAL A 464      23.176  12.355   2.035  1.00103.10           C  
ANISOU 3347  CB  VAL A 464    20082  11386   7706  -1211  -2572  -1927       C  
ATOM   3348  CG1 VAL A 464      23.522  10.882   1.894  1.00103.64           C  
ANISOU 3348  CG1 VAL A 464    20321  11355   7702  -1170  -2486  -1710       C  
ATOM   3349  CG2 VAL A 464      22.035  12.530   3.019  1.00105.25           C  
ANISOU 3349  CG2 VAL A 464    20713  11697   7581  -1175  -2267  -1962       C  
ATOM   3350  N   ARG A 465      26.411  12.095   1.626  1.00111.23           N  
ANISOU 3350  N   ARG A 465    20720  12455   9088   -946  -3576  -1979       N  
ATOM   3351  CA  ARG A 465      27.550  11.964   0.729  1.00124.53           C  
ANISOU 3351  CA  ARG A 465    21961  14233  11123   -963  -3833  -1990       C  
ATOM   3352  C   ARG A 465      27.611  10.537   0.196  1.00133.21           C  
ANISOU 3352  C   ARG A 465    23117  15269  12229   -869  -3643  -1781       C  
ATOM   3353  O   ARG A 465      27.174   9.605   0.870  1.00141.66           O  
ANISOU 3353  O   ARG A 465    24672  16200  12953   -716  -3471  -1638       O  
ATOM   3354  CB  ARG A 465      28.842  12.299   1.461  1.00139.65           C  
ANISOU 3354  CB  ARG A 465    23843  16275  12941   -764  -4374  -2149       C  
ATOM   3355  CG  ARG A 465      28.834  13.652   2.137  1.00138.26           C  
ANISOU 3355  CG  ARG A 465    23710  16116  12705   -857  -4595  -2389       C  
ATOM   3356  CD  ARG A 465      30.234  14.091   2.499  1.00151.90           C  
ANISOU 3356  CD  ARG A 465    25211  18028  14477   -787  -5148  -2599       C  
ATOM   3357  NE  ARG A 465      30.216  15.324   3.281  1.00174.63           N  
ANISOU 3357  NE  ARG A 465    28228  20879  17244   -877  -5377  -2857       N  
ATOM   3358  CZ  ARG A 465      30.045  16.542   2.779  1.00179.85           C  
ANISOU 3358  CZ  ARG A 465    28686  21454  18197  -1201  -5350  -3003       C  
ATOM   3359  NH1 ARG A 465      29.870  16.714   1.475  1.00182.41           N  
ANISOU 3359  NH1 ARG A 465    28638  21737  18932  -1460  -5103  -2899       N  
ATOM   3360  NH2 ARG A 465      30.046  17.593   3.589  1.00176.90           N  
ANISOU 3360  NH2 ARG A 465    28528  21009  17675  -1247  -5574  -3257       N  
ATOM   3361  N   TYR A 466      28.141  10.353  -1.009  1.00129.51           N  
ANISOU 3361  N   TYR A 466    22198  14878  12131   -964  -3654  -1761       N  
ATOM   3362  CA  TYR A 466      28.221   9.011  -1.570  1.00121.21           C  
ANISOU 3362  CA  TYR A 466    21222  13740  11092   -858  -3481  -1594       C  
ATOM   3363  C   TYR A 466      29.582   8.738  -2.199  1.00119.68           C  
ANISOU 3363  C   TYR A 466    20636  13713  11123   -691  -3793  -1636       C  
ATOM   3364  O   TYR A 466      30.287   9.663  -2.604  1.00119.69           O  
ANISOU 3364  O   TYR A 466    20166  13922  11389   -810  -4028  -1782       O  
ATOM   3365  CB  TYR A 466      27.111   8.792  -2.601  1.00120.97           C  
ANISOU 3365  CB  TYR A 466    21071  13640  11254  -1160  -3015  -1517       C  
ATOM   3366  CG  TYR A 466      27.115   9.764  -3.759  1.00132.93           C  
ANISOU 3366  CG  TYR A 466    22028  15308  13170  -1417  -2996  -1609       C  
ATOM   3367  CD1 TYR A 466      27.885   9.520  -4.890  1.00144.39           C  
ANISOU 3367  CD1 TYR A 466    23071  16870  14921  -1434  -3062  -1603       C  
ATOM   3368  CD2 TYR A 466      26.357  10.925  -3.722  1.00131.89           C  
ANISOU 3368  CD2 TYR A 466    21815  15208  13090  -1610  -2904  -1698       C  
ATOM   3369  CE1 TYR A 466      27.895  10.398  -5.952  1.00141.27           C  
ANISOU 3369  CE1 TYR A 466    22221  16603  14851  -1670  -3021  -1658       C  
ATOM   3370  CE2 TYR A 466      26.363  11.813  -4.780  1.00138.42           C  
ANISOU 3370  CE2 TYR A 466    22215  16131  14246  -1812  -2885  -1753       C  
ATOM   3371  CZ  TYR A 466      27.133  11.544  -5.894  1.00142.48           C  
ANISOU 3371  CZ  TYR A 466    22351  16746  15041  -1859  -2936  -1721       C  
ATOM   3372  OH  TYR A 466      27.143  12.424  -6.954  1.00147.17           O  
ANISOU 3372  OH  TYR A 466    22571  17424  15925  -2064  -2894  -1747       O  
ATOM   3373  N   THR A 467      29.951   7.462  -2.254  1.00123.53           N  
ANISOU 3373  N   THR A 467    21342  14106  11488   -412  -3782  -1514       N  
ATOM   3374  CA  THR A 467      31.116   7.029  -3.016  1.00136.14           C  
ANISOU 3374  CA  THR A 467    22548  15879  13299   -216  -3995  -1550       C  
ATOM   3375  C   THR A 467      30.744   5.827  -3.884  1.00143.80           C  
ANISOU 3375  C   THR A 467    23656  16654  14326   -190  -3664  -1408       C  
ATOM   3376  O   THR A 467      29.991   4.954  -3.454  1.00155.97           O  
ANISOU 3376  O   THR A 467    25767  17889  15605   -144  -3413  -1263       O  
ATOM   3377  CB  THR A 467      32.300   6.661  -2.101  1.00142.72           C  
ANISOU 3377  CB  THR A 467    23498  16846  13882    266  -4461  -1602       C  
ATOM   3378  OG1 THR A 467      32.587   7.758  -1.230  1.00156.25           O  
ANISOU 3378  OG1 THR A 467    25126  18731  15511    212  -4778  -1767       O  
ATOM   3379  CG2 THR A 467      33.543   6.336  -2.923  1.00138.59           C  
ANISOU 3379  CG2 THR A 467    22452  16604  13601    480  -4689  -1684       C  
ATOM   3380  N   PHE A 468      31.271   5.791  -5.103  1.00138.60           N  
ANISOU 3380  N   PHE A 468    22496  16168  13997   -245  -3648  -1460       N  
ATOM   3381  CA  PHE A 468      30.943   4.747  -6.060  1.00128.97           C  
ANISOU 3381  CA  PHE A 468    21360  14784  12860   -247  -3346  -1373       C  
ATOM   3382  C   PHE A 468      32.222   4.085  -6.562  1.00147.16           C  
ANISOU 3382  C   PHE A 468    23417  17254  15245    147  -3577  -1420       C  
ATOM   3383  O   PHE A 468      33.066   4.749  -7.160  1.00154.96           O  
ANISOU 3383  O   PHE A 468    23788  18599  16489    113  -3760  -1545       O  
ATOM   3384  CB  PHE A 468      30.173   5.341  -7.233  1.00120.82           C  
ANISOU 3384  CB  PHE A 468    19951  13825  12132   -697  -3038  -1403       C  
ATOM   3385  CG  PHE A 468      28.683   5.320  -7.066  1.00113.45           C  
ANISOU 3385  CG  PHE A 468    19345  12671  11089  -1009  -2668  -1335       C  
ATOM   3386  CD1 PHE A 468      27.972   4.143  -7.190  1.00117.86           C  
ANISOU 3386  CD1 PHE A 468    20325  12947  11510  -1041  -2362  -1244       C  
ATOM   3387  CD2 PHE A 468      27.991   6.485  -6.789  1.00105.62           C  
ANISOU 3387  CD2 PHE A 468    18235  11766  10130  -1276  -2619  -1384       C  
ATOM   3388  CE1 PHE A 468      26.597   4.134  -7.042  1.00110.72           C  
ANISOU 3388  CE1 PHE A 468    19644  11913  10512  -1375  -2008  -1212       C  
ATOM   3389  CE2 PHE A 468      26.619   6.479  -6.638  1.00 92.83           C  
ANISOU 3389  CE2 PHE A 468    16844  10024   8402  -1530  -2277  -1349       C  
ATOM   3390  CZ  PHE A 468      25.923   5.306  -6.768  1.00 92.16           C  
ANISOU 3390  CZ  PHE A 468    17103   9723   8191  -1600  -1967  -1269       C  
ATOM   3391  N   VAL A 469      32.377   2.788  -6.322  1.00155.02           N  
ANISOU 3391  N   VAL A 469    24899  17991  16010    527  -3558  -1326       N  
ATOM   3392  CA  VAL A 469      33.508   2.052  -6.888  1.00160.24           C  
ANISOU 3392  CA  VAL A 469    25353  18798  16733    967  -3740  -1382       C  
ATOM   3393  C   VAL A 469      33.083   0.692  -7.435  1.00172.12           C  
ANISOU 3393  C   VAL A 469    27336  19908  18155   1097  -3443  -1284       C  
ATOM   3394  O   VAL A 469      32.718  -0.197  -6.670  1.00169.98           O  
ANISOU 3394  O   VAL A 469    27798  19224  17561   1301  -3376  -1146       O  
ATOM   3395  CB  VAL A 469      34.628   1.854  -5.847  1.00151.33           C  
ANISOU 3395  CB  VAL A 469    24321  17828  15351   1539  -4212  -1419       C  
ATOM   3396  CG1 VAL A 469      35.531   3.076  -5.792  1.00144.85           C  
ANISOU 3396  CG1 VAL A 469    22764  17542  14731   1452  -4563  -1611       C  
ATOM   3397  CG2 VAL A 469      34.034   1.569  -4.481  1.00142.48           C  
ANISOU 3397  CG2 VAL A 469    23960  16362  13814   1653  -4231  -1274       C  
ATOM   3398  N   LYS A 470      33.111   0.561  -8.764  1.00193.10           N  
ANISOU 3398  N   LYS A 470    29609  22673  21088    952  -3253  -1359       N  
ATOM   3399  CA  LYS A 470      32.952  -0.710  -9.486  1.00192.52           C  
ANISOU 3399  CA  LYS A 470    29885  22286  20979   1113  -3022  -1336       C  
ATOM   3400  C   LYS A 470      31.803  -1.541  -8.916  1.00184.25           C  
ANISOU 3400  C   LYS A 470    29674  20660  19673    946  -2723  -1184       C  
ATOM   3401  O   LYS A 470      31.818  -2.771  -8.943  1.00198.27           O  
ANISOU 3401  O   LYS A 470    32026  22033  21274   1216  -2624  -1126       O  
ATOM   3402  CB  LYS A 470      34.274  -1.494  -9.450  1.00192.13           C  
ANISOU 3402  CB  LYS A 470    29844  22332  20825   1822  -3325  -1388       C  
ATOM   3403  CG  LYS A 470      34.374  -2.732 -10.367  1.00192.24           C  
ANISOU 3403  CG  LYS A 470    30121  22084  20837   2081  -3137  -1420       C  
ATOM   3404  CD  LYS A 470      33.977  -2.463 -11.813  1.00180.30           C  
ANISOU 3404  CD  LYS A 470    28130  20740  19637   1657  -2844  -1531       C  
ATOM   3405  CE  LYS A 470      34.053  -3.748 -12.632  1.00175.36           C  
ANISOU 3405  CE  LYS A 470    27854  19810  18964   1934  -2670  -1589       C  
ATOM   3406  NZ  LYS A 470      33.537  -3.573 -14.014  1.00171.77           N  
ANISOU 3406  NZ  LYS A 470    27027  19483  18754   1512  -2372  -1702       N  
ATOM   3407  N   GLY A 471      30.807  -0.840  -8.387  1.00164.66           N  
ANISOU 3407  N   GLY A 471    27263  18142  17160    490  -2567  -1127       N  
ATOM   3408  CA  GLY A 471      29.651  -1.468  -7.783  1.00162.89           C  
ANISOU 3408  CA  GLY A 471    27745  17455  16691    234  -2246   -993       C  
ATOM   3409  C   GLY A 471      28.531  -0.480  -7.539  1.00162.13           C  
ANISOU 3409  C   GLY A 471    27466  17486  16650   -312  -2042   -997       C  
ATOM   3410  O   GLY A 471      28.145   0.289  -8.421  1.00100.55           O  
ANISOU 3410  O   GLY A 471    19102   9967   9135   -655  -1936  -1106       O  
ATOM   3411  N   ASN A 472      28.028  -0.506  -6.310  1.00154.99           N  
ANISOU 3411  N   ASN A 472    27069  16381  15437   -342  -1993   -875       N  
ATOM   3412  CA  ASN A 472      26.959   0.374  -5.870  1.00151.69           C  
ANISOU 3412  CA  ASN A 472    26558  16079  14999   -777  -1799   -881       C  
ATOM   3413  C   ASN A 472      27.347   1.181  -4.641  1.00131.99           C  
ANISOU 3413  C   ASN A 472    24117  13733  12301   -564  -2096   -856       C  
ATOM   3414  O   ASN A 472      28.374   0.931  -4.024  1.00136.92           O  
ANISOU 3414  O   ASN A 472    24927  14343  12752    -89  -2443   -818       O  
ATOM   3415  CB  ASN A 472      25.671  -0.413  -5.630  1.00180.02           C  
ANISOU 3415  CB  ASN A 472    30692  19314  18395  -1158  -1331   -790       C  
ATOM   3416  CG  ASN A 472      24.951  -0.755  -6.929  1.00199.05           C  
ANISOU 3416  CG  ASN A 472    32839  21724  21066  -1562  -1013   -899       C  
ATOM   3417  OD1 ASN A 472      24.074  -0.011  -7.379  1.00204.63           O  
ANISOU 3417  OD1 ASN A 472    33115  22697  21938  -1960   -833  -1002       O  
ATOM   3418  ND2 ASN A 472      25.319  -1.878  -7.538  1.00206.31           N  
ANISOU 3418  ND2 ASN A 472    34031  22354  22002  -1427   -962   -894       N  
ATOM   3419  N   LEU A 473      26.508   2.153  -4.310  1.00119.09           N  
ANISOU 3419  N   LEU A 473    22313  12262  10675   -895  -1970   -902       N  
ATOM   3420  CA  LEU A 473      26.802   3.174  -3.316  1.00113.55           C  
ANISOU 3420  CA  LEU A 473    21550  11754   9840   -763  -2251   -943       C  
ATOM   3421  C   LEU A 473      26.819   2.742  -1.856  1.00117.15           C  
ANISOU 3421  C   LEU A 473    22695  11997   9819   -506  -2316   -811       C  
ATOM   3422  O   LEU A 473      25.973   1.979  -1.397  1.00109.35           O  
ANISOU 3422  O   LEU A 473    22270  10714   8563   -649  -1965   -671       O  
ATOM   3423  CB  LEU A 473      25.794   4.316  -3.456  1.00102.11           C  
ANISOU 3423  CB  LEU A 473    19763  10509   8526  -1165  -2057  -1043       C  
ATOM   3424  CG  LEU A 473      24.320   3.901  -3.417  1.00 99.94           C  
ANISOU 3424  CG  LEU A 473    19749  10096   8129  -1545  -1552   -990       C  
ATOM   3425  CD1 LEU A 473      23.730   3.966  -2.022  1.00102.70           C  
ANISOU 3425  CD1 LEU A 473    20604  10351   8067  -1536  -1436   -916       C  
ATOM   3426  CD2 LEU A 473      23.538   4.779  -4.340  1.00 96.25           C  
ANISOU 3426  CD2 LEU A 473    18718   9891   7961  -1884  -1381  -1125       C  
ATOM   3427  N   LYS A 474      27.833   3.236  -1.154  1.00131.57           N  
ANISOU 3427  N   LYS A 474    24464  13994  11532   -134  -2776   -867       N  
ATOM   3428  CA  LYS A 474      27.896   3.218   0.301  1.00143.82           C  
ANISOU 3428  CA  LYS A 474    26567  15461  12617    126  -2925   -791       C  
ATOM   3429  C   LYS A 474      27.544   4.649   0.713  1.00127.17           C  
ANISOU 3429  C   LYS A 474    24137  13624  10558    -88  -3009   -955       C  
ATOM   3430  O   LYS A 474      28.159   5.601   0.228  1.00108.92           O  
ANISOU 3430  O   LYS A 474    21231  11595   8560   -125  -3290  -1135       O  
ATOM   3431  CB  LYS A 474      29.286   2.808   0.811  1.00154.62           C  
ANISOU 3431  CB  LYS A 474    28071  16881  13798    725  -3431   -785       C  
ATOM   3432  CG  LYS A 474      29.349   2.338   2.276  1.00155.42           C  
ANISOU 3432  CG  LYS A 474    28945  16795  13312   1096  -3551   -638       C  
ATOM   3433  CD  LYS A 474      29.231   0.819   2.426  1.00160.81           C  
ANISOU 3433  CD  LYS A 474    30395  17013  13692   1334  -3332   -378       C  
ATOM   3434  CE  LYS A 474      29.219   0.390   3.896  1.00175.75           C  
ANISOU 3434  CE  LYS A 474    33128  18699  14950   1691  -3413   -196       C  
ATOM   3435  NZ  LYS A 474      28.047   0.887   4.665  1.00177.75           N  
ANISOU 3435  NZ  LYS A 474    33666  18912  14959   1298  -3058   -149       N  
ATOM   3436  N   LEU A 475      26.520   4.805   1.548  1.00143.25           N  
ANISOU 3436  N   LEU A 475    26570  15565  12292   -255  -2729   -899       N  
ATOM   3437  CA  LEU A 475      26.014   6.131   1.912  1.00143.86           C  
ANISOU 3437  CA  LEU A 475    26402  15861  12396   -447  -2743  -1065       C  
ATOM   3438  C   LEU A 475      26.566   6.683   3.228  1.00149.79           C  
ANISOU 3438  C   LEU A 475    27425  16704  12782   -133  -3125  -1142       C  
ATOM   3439  O   LEU A 475      26.417   6.070   4.287  1.00151.62           O  
ANISOU 3439  O   LEU A 475    28295  16780  12533     80  -3076  -1003       O  
ATOM   3440  CB  LEU A 475      24.484   6.120   1.994  1.00127.98           C  
ANISOU 3440  CB  LEU A 475    24560  13786  10282   -819  -2191  -1015       C  
ATOM   3441  CG  LEU A 475      23.720   6.408   0.706  1.00105.34           C  
ANISOU 3441  CG  LEU A 475    21162  11024   7838  -1214  -1888  -1089       C  
ATOM   3442  CD1 LEU A 475      22.260   6.691   1.004  1.00105.33           C  
ANISOU 3442  CD1 LEU A 475    21236  11092   7693  -1517  -1432  -1113       C  
ATOM   3443  CD2 LEU A 475      24.360   7.582  -0.005  1.00102.32           C  
ANISOU 3443  CD2 LEU A 475    20157  10873   7845  -1211  -2220  -1274       C  
ATOM   3444  N   GLU A 476      27.220   7.839   3.146  1.00138.39           N  
ANISOU 3444  N   GLU A 476    25522  15505  11556   -121  -3507  -1369       N  
ATOM   3445  CA  GLU A 476      27.627   8.564   4.341  1.00123.80           C  
ANISOU 3445  CA  GLU A 476    23873  13773   9392     97  -3869  -1513       C  
ATOM   3446  C   GLU A 476      26.447   9.428   4.773  1.00120.70           C  
ANISOU 3446  C   GLU A 476    23590  13387   8885   -146  -3573  -1598       C  
ATOM   3447  O   GLU A 476      25.709   9.945   3.941  1.00116.85           O  
ANISOU 3447  O   GLU A 476    22750  12928   8721   -469  -3290  -1647       O  
ATOM   3448  CB  GLU A 476      28.869   9.417   4.069  1.00122.39           C  
ANISOU 3448  CB  GLU A 476    23158  13844   9499    162  -4406  -1752       C  
ATOM   3449  CG  GLU A 476      29.335  10.275   5.246  1.00143.84           C  
ANISOU 3449  CG  GLU A 476    26025  16703  11923    333  -4828  -1968       C  
ATOM   3450  CD  GLU A 476      30.040   9.472   6.331  1.00160.38           C  
ANISOU 3450  CD  GLU A 476    28596  18820  13520    828  -5155  -1899       C  
ATOM   3451  OE1 GLU A 476      30.922   8.658   5.990  1.00172.49           O  
ANISOU 3451  OE1 GLU A 476    30018  20408  15112   1094  -5365  -1821       O  
ATOM   3452  OE2 GLU A 476      29.715   9.655   7.525  1.00152.79           O  
ANISOU 3452  OE2 GLU A 476    28136  17836  12083    991  -5205  -1926       O  
ATOM   3453  N   MET A 477      26.281   9.593   6.078  1.00127.46           N  
ANISOU 3453  N   MET A 477    24935  14240   9252     53  -3652  -1626       N  
ATOM   3454  CA  MET A 477      25.095  10.238   6.628  1.00124.84           C  
ANISOU 3454  CA  MET A 477    24797  13924   8714   -105  -3318  -1693       C  
ATOM   3455  C   MET A 477      25.459  11.425   7.504  1.00127.52           C  
ANISOU 3455  C   MET A 477    25183  14394   8875     39  -3703  -1965       C  
ATOM   3456  O   MET A 477      26.583  11.513   7.996  1.00134.74           O  
ANISOU 3456  O   MET A 477    26137  15383   9675    295  -4216  -2067       O  
ATOM   3457  CB  MET A 477      24.279   9.227   7.437  1.00128.85           C  
ANISOU 3457  CB  MET A 477    25956  14286   8715    -48  -2900  -1454       C  
ATOM   3458  CG  MET A 477      23.615   8.151   6.604  1.00119.82           C  
ANISOU 3458  CG  MET A 477    24809  12982   7735   -308  -2414  -1223       C  
ATOM   3459  SD  MET A 477      22.529   8.863   5.356  1.00146.01           S  
ANISOU 3459  SD  MET A 477    27471  16443  11563   -768  -2027  -1352       S  
ATOM   3460  CE  MET A 477      21.027   9.111   6.298  1.00117.21           C  
ANISOU 3460  CE  MET A 477    24155  12895   7486   -904  -1508  -1368       C  
ATOM   3461  N   PRO A 478      24.512  12.356   7.688  1.00128.97           N  
ANISOU 3461  N   PRO A 478    25350  14622   9032   -112  -3470  -2113       N  
ATOM   3462  CA  PRO A 478      24.715  13.402   8.689  1.00140.83           C  
ANISOU 3462  CA  PRO A 478    27047  16199  10264     49  -3784  -2380       C  
ATOM   3463  C   PRO A 478      24.930  12.789  10.067  1.00160.04           C  
ANISOU 3463  C   PRO A 478    30019  18645  12145    388  -3861  -2274       C  
ATOM   3464  O   PRO A 478      24.281  11.795  10.394  1.00173.94           O  
ANISOU 3464  O   PRO A 478    32210  20323  13558    423  -3476  -2025       O  
ATOM   3465  CB  PRO A 478      23.407  14.199   8.622  1.00136.05           C  
ANISOU 3465  CB  PRO A 478    26401  15618   9674   -117  -3367  -2486       C  
ATOM   3466  CG  PRO A 478      22.406  13.233   8.061  1.00131.75           C  
ANISOU 3466  CG  PRO A 478    25831  15057   9172   -304  -2785  -2224       C  
ATOM   3467  CD  PRO A 478      23.194  12.473   7.044  1.00122.04           C  
ANISOU 3467  CD  PRO A 478    24292  13750   8326   -395  -2919  -2066       C  
ATOM   3468  N   SER A 479      25.837  13.364  10.851  1.00124.15           N  
ANISOU 3468  N   SER A 479    19667  15174  12330  -1899   -610  -4390       N  
ATOM   3469  CA  SER A 479      26.184  12.803  12.153  1.00129.57           C  
ANISOU 3469  CA  SER A 479    20271  15495  13466  -1735   -627  -4211       C  
ATOM   3470  C   SER A 479      24.956  12.735  13.058  1.00134.74           C  
ANISOU 3470  C   SER A 479    20810  16268  14119  -1878   -868  -3909       C  
ATOM   3471  O   SER A 479      24.182  13.690  13.132  1.00146.27           O  
ANISOU 3471  O   SER A 479    22135  18122  15318  -1899   -997  -3697       O  
ATOM   3472  CB  SER A 479      27.290  13.632  12.815  1.00120.60           C  
ANISOU 3472  CB  SER A 479    19013  14322  12489  -1386   -532  -4016       C  
ATOM   3473  OG  SER A 479      27.752  13.028  14.010  1.00110.28           O  
ANISOU 3473  OG  SER A 479    17649  12642  11610  -1250   -565  -3847       O  
ATOM   3474  N   PRO A 480      24.768  11.596  13.743  1.00117.62           N  
ANISOU 3474  N   PRO A 480    18683  13747  12261  -1985   -923  -3889       N  
ATOM   3475  CA  PRO A 480      23.610  11.439  14.628  1.00115.81           C  
ANISOU 3475  CA  PRO A 480    18343  13632  12028  -2167  -1119  -3612       C  
ATOM   3476  C   PRO A 480      23.639  12.410  15.809  1.00115.63           C  
ANISOU 3476  C   PRO A 480    18131  13791  12011  -1965  -1164  -3235       C  
ATOM   3477  O   PRO A 480      22.585  12.687  16.385  1.00 92.45           O  
ANISOU 3477  O   PRO A 480    15054  11110   8962  -2097  -1284  -3024       O  
ATOM   3478  CB  PRO A 480      23.729   9.986  15.100  1.00113.19           C  
ANISOU 3478  CB  PRO A 480    18136  12801  12068  -2302  -1143  -3671       C  
ATOM   3479  CG  PRO A 480      25.186   9.671  14.975  1.00103.22           C  
ANISOU 3479  CG  PRO A 480    16965  11138  11116  -2037   -970  -3842       C  
ATOM   3480  CD  PRO A 480      25.615  10.391  13.729  1.00 98.26           C  
ANISOU 3480  CD  PRO A 480    16373  10759  10202  -1950   -805  -4120       C  
ATOM   3481  N   PHE A 481      24.823  12.924  16.146  1.00128.73           N  
ANISOU 3481  N   PHE A 481    19781  15331  13801  -1664  -1056  -3174       N  
ATOM   3482  CA  PHE A 481      24.990  13.816  17.293  1.00115.04           C  
ANISOU 3482  CA  PHE A 481    17906  13729  12075  -1483  -1090  -2847       C  
ATOM   3483  C   PHE A 481      25.584  15.168  16.905  1.00114.23           C  
ANISOU 3483  C   PHE A 481    17737  13875  11789  -1236  -1009  -2834       C  
ATOM   3484  O   PHE A 481      26.389  15.271  15.980  1.00121.97           O  
ANISOU 3484  O   PHE A 481    18795  14798  12749  -1136   -886  -3049       O  
ATOM   3485  CB  PHE A 481      25.879  13.158  18.353  1.00 99.64           C  
ANISOU 3485  CB  PHE A 481    15999  11369  10489  -1384  -1099  -2696       C  
ATOM   3486  CG  PHE A 481      27.338  13.076  17.967  1.00 92.14           C  
ANISOU 3486  CG  PHE A 481    15103  10132   9776  -1134   -969  -2846       C  
ATOM   3487  CD1 PHE A 481      27.789  12.092  17.102  1.00105.27           C  
ANISOU 3487  CD1 PHE A 481    16884  11473  11639  -1165   -871  -3168       C  
ATOM   3488  CD2 PHE A 481      28.261  13.971  18.484  1.00 80.07           C  
ANISOU 3488  CD2 PHE A 481    13490   8647   8286   -878   -934  -2682       C  
ATOM   3489  CE1 PHE A 481      29.133  12.008  16.756  1.00103.17           C  
ANISOU 3489  CE1 PHE A 481    16620  10947  11631   -926   -716  -3331       C  
ATOM   3490  CE2 PHE A 481      29.604  13.891  18.139  1.00 83.01           C  
ANISOU 3490  CE2 PHE A 481    13864   8770   8905   -657   -810  -2815       C  
ATOM   3491  CZ  PHE A 481      30.039  12.910  17.276  1.00 88.29           C  
ANISOU 3491  CZ  PHE A 481    14619   9131   9796   -671   -689  -3142       C  
ATOM   3492  N   SER A 482      25.176  16.200  17.631  1.00119.34           N  
ANISOU 3492  N   SER A 482    18243  14793  12306  -1154  -1065  -2590       N  
ATOM   3493  CA  SER A 482      25.705  17.547  17.457  1.00143.25           C  
ANISOU 3493  CA  SER A 482    21209  18026  15193   -923  -1014  -2528       C  
ATOM   3494  C   SER A 482      27.132  17.706  17.970  1.00145.50           C  
ANISOU 3494  C   SER A 482    21528  18068  15686   -695   -928  -2469       C  
ATOM   3495  O   SER A 482      27.530  17.059  18.937  1.00156.86           O  
ANISOU 3495  O   SER A 482    22986  19246  17368   -690   -960  -2348       O  
ATOM   3496  CB  SER A 482      24.813  18.553  18.179  1.00174.90           C  
ANISOU 3496  CB  SER A 482    25052  22344  19057   -900  -1092  -2310       C  
ATOM   3497  OG  SER A 482      24.856  18.353  19.581  1.00193.94           O  
ANISOU 3497  OG  SER A 482    27433  24649  21607   -902  -1104  -2114       O  
ATOM   3498  N   VAL A 483      27.896  18.579  17.326  1.00142.51           N  
ANISOU 3498  N   VAL A 483    21150  17784  15213   -528   -841  -2530       N  
ATOM   3499  CA  VAL A 483      29.141  19.049  17.913  1.00128.29           C  
ANISOU 3499  CA  VAL A 483    19326  15842  13578   -310   -784  -2420       C  
ATOM   3500  C   VAL A 483      28.896  20.466  18.410  1.00119.27           C  
ANISOU 3500  C   VAL A 483    18097  14972  12250   -206   -837  -2219       C  
ATOM   3501  O   VAL A 483      29.182  21.444  17.720  1.00117.84           O  
ANISOU 3501  O   VAL A 483    17907  14958  11908   -113   -795  -2246       O  
ATOM   3502  CB  VAL A 483      30.313  19.021  16.921  1.00116.80           C  
ANISOU 3502  CB  VAL A 483    17915  14274  12190   -203   -619  -2634       C  
ATOM   3503  CG1 VAL A 483      31.583  19.515  17.591  1.00108.50           C  
ANISOU 3503  CG1 VAL A 483    16797  13088  11341      9   -583  -2494       C  
ATOM   3504  CG2 VAL A 483      30.513  17.617  16.378  1.00123.14           C  
ANISOU 3504  CG2 VAL A 483    18803  14784  13201   -298   -536  -2895       C  
ATOM   3505  N   VAL A 484      28.328  20.561  19.605  1.00119.24           N  
ANISOU 3505  N   VAL A 484    18039  15005  12261   -243   -924  -2024       N  
ATOM   3506  CA  VAL A 484      27.946  21.841  20.185  1.00125.59           C  
ANISOU 3506  CA  VAL A 484    18760  16046  12912   -157   -955  -1873       C  
ATOM   3507  C   VAL A 484      27.716  21.636  21.687  1.00127.41           C  
ANISOU 3507  C   VAL A 484    18974  16228  13207   -223  -1001  -1690       C  
ATOM   3508  O   VAL A 484      27.609  20.496  22.145  1.00129.37           O  
ANISOU 3508  O   VAL A 484    19269  16300  13585   -370  -1039  -1658       O  
ATOM   3509  CB  VAL A 484      26.673  22.407  19.498  1.00115.36           C  
ANISOU 3509  CB  VAL A 484    17376  15052  11405   -219   -999  -1920       C  
ATOM   3510  CG1 VAL A 484      25.455  21.591  19.876  1.00113.92           C  
ANISOU 3510  CG1 VAL A 484    17131  14930  11223   -427  -1051  -1916       C  
ATOM   3511  CG2 VAL A 484      26.460  23.876  19.836  1.00122.12           C  
ANISOU 3511  CG2 VAL A 484    18141  16102  12157    -69  -1016  -1806       C  
ATOM   3512  N   ILE A 485      27.663  22.723  22.454  1.00116.66           N  
ANISOU 3512  N   ILE A 485    17565  15010  11750   -138   -998  -1572       N  
ATOM   3513  CA  ILE A 485      27.290  22.644  23.861  1.00107.40           C  
ANISOU 3513  CA  ILE A 485    16389  13863  10553   -248  -1016  -1425       C  
ATOM   3514  C   ILE A 485      25.885  22.051  23.988  1.00116.40           C  
ANISOU 3514  C   ILE A 485    17449  15153  11625   -453  -1012  -1451       C  
ATOM   3515  O   ILE A 485      24.936  22.534  23.368  1.00112.58           O  
ANISOU 3515  O   ILE A 485    16839  14891  11047   -440   -994  -1541       O  
ATOM   3516  CB  ILE A 485      27.335  24.029  24.543  1.00105.33           C  
ANISOU 3516  CB  ILE A 485    16092  13759  10169   -131   -979  -1363       C  
ATOM   3517  CG1 ILE A 485      28.769  24.565  24.579  1.00104.11           C  
ANISOU 3517  CG1 ILE A 485    16018  13450  10089     26  -1001  -1307       C  
ATOM   3518  CG2 ILE A 485      26.787  23.952  25.956  1.00109.40           C  
ANISOU 3518  CG2 ILE A 485    16613  14359  10596   -293   -957  -1258       C  
ATOM   3519  CD1 ILE A 485      28.882  26.003  25.064  1.00 93.59           C  
ANISOU 3519  CD1 ILE A 485    14675  12242   8644    143   -973  -1276       C  
ATOM   3520  N   GLN A 486      25.761  20.993  24.783  1.00130.58           N  
ANISOU 3520  N   GLN A 486    19308  16822  13486   -658  -1050  -1351       N  
ATOM   3521  CA  GLN A 486      24.484  20.313  24.952  1.00131.89           C  
ANISOU 3521  CA  GLN A 486    19399  17115  13600   -899  -1044  -1359       C  
ATOM   3522  C   GLN A 486      24.115  20.255  26.439  1.00116.36           C  
ANISOU 3522  C   GLN A 486    17442  15233  11534  -1088  -1013  -1193       C  
ATOM   3523  O   GLN A 486      24.994  20.127  27.293  1.00 91.31           O  
ANISOU 3523  O   GLN A 486    14406  11898   8388  -1107  -1064  -1040       O  
ATOM   3524  CB  GLN A 486      24.546  18.908  24.335  1.00147.72           C  
ANISOU 3524  CB  GLN A 486    21489  18872  15764  -1043  -1118  -1412       C  
ATOM   3525  CG  GLN A 486      23.197  18.220  24.180  1.00158.72           C  
ANISOU 3525  CG  GLN A 486    22795  20404  17109  -1302  -1128  -1454       C  
ATOM   3526  CD  GLN A 486      22.948  17.151  25.223  1.00162.30           C  
ANISOU 3526  CD  GLN A 486    23327  20720  17618  -1589  -1175  -1285       C  
ATOM   3527  OE1 GLN A 486      23.871  16.460  25.655  1.00172.61           O  
ANISOU 3527  OE1 GLN A 486    24795  21704  19085  -1606  -1256  -1167       O  
ATOM   3528  NE2 GLN A 486      21.692  17.007  25.633  1.00158.83           N  
ANISOU 3528  NE2 GLN A 486    22760  20525  17063  -1827  -1133  -1255       N  
ATOM   3529  N   GLU A 487      22.824  20.398  26.740  1.00129.33           N  
ANISOU 3529  N   GLU A 487    18932  17153  13056  -1237   -927  -1225       N  
ATOM   3530  CA  GLU A 487      22.309  20.303  28.110  1.00135.77           C  
ANISOU 3530  CA  GLU A 487    19746  18107  13731  -1475   -848  -1102       C  
ATOM   3531  C   GLU A 487      21.303  19.160  28.251  1.00133.69           C  
ANISOU 3531  C   GLU A 487    19435  17890  13473  -1808   -855  -1059       C  
ATOM   3532  O   GLU A 487      20.470  18.953  27.367  1.00158.29           O  
ANISOU 3532  O   GLU A 487    22396  21107  16640  -1831   -859  -1183       O  
ATOM   3533  CB  GLU A 487      21.651  21.621  28.534  1.00142.31           C  
ANISOU 3533  CB  GLU A 487    20401  19255  14413  -1369   -675  -1201       C  
ATOM   3534  CG  GLU A 487      21.500  21.801  30.047  1.00141.73           C  
ANISOU 3534  CG  GLU A 487    20387  19319  14145  -1575   -551  -1110       C  
ATOM   3535  CD  GLU A 487      20.144  22.372  30.443  1.00135.76           C  
ANISOU 3535  CD  GLU A 487    19375  18921  13285  -1653   -327  -1247       C  
ATOM   3536  OE1 GLU A 487      19.514  23.065  29.618  1.00130.12           O  
ANISOU 3536  OE1 GLU A 487    18426  18338  12675  -1438   -285  -1407       O  
ATOM   3537  OE2 GLU A 487      19.714  22.141  31.591  1.00133.20           O  
ANISOU 3537  OE2 GLU A 487    19076  18751  12782  -1938   -193  -1190       O  
ATOM   3538  N   SER A 488      21.372  18.428  29.360  1.00103.72           N  
ANISOU 3538  N   SER A 488    15774  14022   9611  -2095   -878   -866       N  
ATOM   3539  CA  SER A 488      20.545  17.238  29.540  1.00124.64           C  
ANISOU 3539  CA  SER A 488    18418  16662  12279  -2453   -909   -784       C  
ATOM   3540  C   SER A 488      19.603  17.405  30.730  1.00128.45           C  
ANISOU 3540  C   SER A 488    18810  17472  12522  -2751   -736   -712       C  
ATOM   3541  O   SER A 488      19.846  18.240  31.600  1.00114.95           O  
ANISOU 3541  O   SER A 488    17129  15913  10631  -2713   -620   -692       O  
ATOM   3542  CB  SER A 488      21.422  16.001  29.726  1.00 81.31           C  
ANISOU 3542  CB  SER A 488    13185  10750   6958  -2589  -1116   -587       C  
ATOM   3543  OG  SER A 488      20.657  14.811  29.637  1.00 99.07           O  
ANISOU 3543  OG  SER A 488    15441  12923   9278  -2913  -1175   -532       O  
ATOM   3544  N   GLU A 489      18.515  16.638  30.760  1.00140.85           N  
ANISOU 3544  N   GLU A 489    20267  19168  14081  -3066   -699   -696       N  
ATOM   3545  CA  GLU A 489      17.562  16.754  31.862  1.00144.40           C  
ANISOU 3545  CA  GLU A 489    20603  19964  14300  -3385   -491   -648       C  
ATOM   3546  C   GLU A 489      18.135  16.177  33.156  1.00137.29           C  
ANISOU 3546  C   GLU A 489    19992  18947  13226  -3703   -548   -365       C  
ATOM   3547  O   GLU A 489      17.812  16.640  34.246  1.00141.60           O  
ANISOU 3547  O   GLU A 489    20531  19773  13497  -3896   -355   -334       O  
ATOM   3548  CB  GLU A 489      16.240  16.055  31.511  1.00150.84           C  
ANISOU 3548  CB  GLU A 489    21193  20956  15165  -3667   -443   -693       C  
ATOM   3549  CG  GLU A 489      16.350  14.570  31.181  1.00157.70           C  
ANISOU 3549  CG  GLU A 489    22245  21491  16185  -3935   -671   -535       C  
ATOM   3550  CD  GLU A 489      16.748  14.306  29.740  1.00160.88           C  
ANISOU 3550  CD  GLU A 489    22669  21618  16841  -3670   -855   -680       C  
ATOM   3551  OE1 GLU A 489      17.006  15.279  29.002  1.00156.36           O  
ANISOU 3551  OE1 GLU A 489    21988  21119  16304  -3290   -825   -864       O  
ATOM   3552  OE2 GLU A 489      16.799  13.121  29.345  1.00172.92           O  
ANISOU 3552  OE2 GLU A 489    24333  22847  18522  -3864  -1025   -615       O  
ATOM   3553  N   LYS A 490      18.984  15.163  33.025  1.00127.06           N  
ANISOU 3553  N   LYS A 490    18950  17231  12096  -3767   -816   -161       N  
ATOM   3554  CA  LYS A 490      19.773  14.656  34.136  1.00127.36           C  
ANISOU 3554  CA  LYS A 490    19284  17079  12029  -4006   -964    158       C  
ATOM   3555  C   LYS A 490      21.107  15.372  34.030  1.00142.00           C  
ANISOU 3555  C   LYS A 490    21255  18738  13959  -3628  -1073    151       C  
ATOM   3556  O   LYS A 490      21.809  15.173  33.050  1.00149.51           O  
ANISOU 3556  O   LYS A 490    22221  19380  15205  -3332  -1219     81       O  
ATOM   3557  CB  LYS A 490      19.927  13.131  34.071  1.00136.48           C  
ANISOU 3557  CB  LYS A 490    20620  17842  13394  -4279  -1222    403       C  
ATOM   3558  CG  LYS A 490      20.223  12.578  32.679  1.00142.43           C  
ANISOU 3558  CG  LYS A 490    21342  18243  14530  -4015  -1367    248       C  
ATOM   3559  CD  LYS A 490      20.620  11.104  32.713  1.00149.29           C  
ANISOU 3559  CD  LYS A 490    22433  18624  15665  -4241  -1641    489       C  
ATOM   3560  CE  LYS A 490      19.433  10.193  33.011  1.00151.83           C  
ANISOU 3560  CE  LYS A 490    22734  19045  15909  -4729  -1619    596       C  
ATOM   3561  NZ  LYS A 490      19.800   8.749  32.914  1.00147.37           N  
ANISOU 3561  NZ  LYS A 490    22390  17942  15660  -4927  -1902    808       N  
ATOM   3562  N   GLY A 491      21.472  16.192  35.014  1.00150.28           N  
ANISOU 3562  N   GLY A 491    22390  19970  14740  -3657   -993    209       N  
ATOM   3563  CA  GLY A 491      22.648  17.038  34.865  1.00139.42           C  
ANISOU 3563  CA  GLY A 491    21083  18462  13428  -3296  -1072    168       C  
ATOM   3564  C   GLY A 491      22.294  17.944  33.702  1.00119.34           C  
ANISOU 3564  C   GLY A 491    18290  16050  11003  -2901   -909   -176       C  
ATOM   3565  O   GLY A 491      21.478  18.848  33.861  1.00104.54           O  
ANISOU 3565  O   GLY A 491    16241  14528   8953  -2870   -660   -372       O  
ATOM   3566  N   SER A 492      22.914  17.749  32.541  1.00117.80           N  
ANISOU 3566  N   SER A 492    18075  15577  11108  -2601  -1045   -253       N  
ATOM   3567  CA  SER A 492      24.302  17.331  32.375  1.00110.76           C  
ANISOU 3567  CA  SER A 492    17354  14284  10446  -2452  -1284   -104       C  
ATOM   3568  C   SER A 492      24.879  18.312  31.376  1.00 95.35           C  
ANISOU 3568  C   SER A 492    15298  12321   8607  -2024  -1234   -328       C  
ATOM   3569  O   SER A 492      24.162  18.759  30.480  1.00 99.70           O  
ANISOU 3569  O   SER A 492    15674  13045   9162  -1880  -1101   -561       O  
ATOM   3570  CB  SER A 492      24.448  15.897  31.858  1.00131.46           C  
ANISOU 3570  CB  SER A 492    20048  16534  13366  -2553  -1471     -5       C  
ATOM   3571  OG  SER A 492      24.089  14.944  32.839  1.00140.83           O  
ANISOU 3571  OG  SER A 492    21337  17717  14456  -2980  -1534    226       O  
ATOM   3572  N   TRP A 493      26.151  18.657  31.499  1.00 89.31           N  
ANISOU 3572  N   TRP A 493    14631  11364   7937  -1840  -1353   -242       N  
ATOM   3573  CA  TRP A 493      26.724  19.608  30.554  1.00 96.11           C  
ANISOU 3573  CA  TRP A 493    15401  12226   8890  -1469  -1297   -438       C  
ATOM   3574  C   TRP A 493      27.882  19.017  29.763  1.00 98.85           C  
ANISOU 3574  C   TRP A 493    15784  12201   9572  -1274  -1443   -423       C  
ATOM   3575  O   TRP A 493      28.832  18.471  30.329  1.00114.49           O  
ANISOU 3575  O   TRP A 493    17873  13917  11711  -1318  -1625   -208       O  
ATOM   3576  CB  TRP A 493      27.152  20.878  31.283  1.00 96.39           C  
ANISOU 3576  CB  TRP A 493    15468  12431   8723  -1387  -1241   -427       C  
ATOM   3577  CG  TRP A 493      25.975  21.717  31.645  1.00 99.61           C  
ANISOU 3577  CG  TRP A 493    15772  13208   8866  -1454  -1018   -578       C  
ATOM   3578  CD1 TRP A 493      25.065  21.484  32.639  1.00109.72           C  
ANISOU 3578  CD1 TRP A 493    17067  14704   9918  -1768   -914   -526       C  
ATOM   3579  CD2 TRP A 493      25.569  22.928  31.004  1.00 89.97           C  
ANISOU 3579  CD2 TRP A 493    14395  12175   7613  -1198   -863   -812       C  
ATOM   3580  NE1 TRP A 493      24.116  22.480  32.652  1.00 99.23           N  
ANISOU 3580  NE1 TRP A 493    15572  13687   8445  -1699   -677   -747       N  
ATOM   3581  CE2 TRP A 493      24.405  23.378  31.659  1.00 95.78           C  
ANISOU 3581  CE2 TRP A 493    15030  13218   8145  -1340   -663   -912       C  
ATOM   3582  CE3 TRP A 493      26.079  23.676  29.941  1.00 71.17           C  
ANISOU 3582  CE3 TRP A 493    11948   9729   5365   -876   -875   -937       C  
ATOM   3583  CZ2 TRP A 493      23.746  24.545  31.282  1.00 96.18           C  
ANISOU 3583  CZ2 TRP A 493    14896  13470   8176  -1132   -497  -1131       C  
ATOM   3584  CZ3 TRP A 493      25.425  24.829  29.571  1.00 76.20           C  
ANISOU 3584  CZ3 TRP A 493    12437  10570   5943   -703   -736  -1118       C  
ATOM   3585  CH2 TRP A 493      24.273  25.255  30.239  1.00 86.49           C  
ANISOU 3585  CH2 TRP A 493    13625  12140   7098   -812   -559  -1214       C  
ATOM   3586  N   HIS A 494      27.784  19.129  28.442  1.00 76.68           N  
ANISOU 3586  N   HIS A 494    12874   9382   6877  -1070  -1363   -656       N  
ATOM   3587  CA  HIS A 494      28.808  18.599  27.558  1.00 70.65           C  
ANISOU 3587  CA  HIS A 494    12124   8300   6422   -885  -1430   -719       C  
ATOM   3588  C   HIS A 494      29.394  19.696  26.678  1.00 82.58           C  
ANISOU 3588  C   HIS A 494    13558   9905   7916   -596  -1332   -889       C  
ATOM   3589  O   HIS A 494      28.658  20.455  26.050  1.00 92.84           O  
ANISOU 3589  O   HIS A 494    14775  11461   9038   -532  -1215  -1050       O  
ATOM   3590  CB  HIS A 494      28.229  17.476  26.709  1.00 72.18           C  
ANISOU 3590  CB  HIS A 494    12313   8350   6762   -977  -1424   -854       C  
ATOM   3591  CG  HIS A 494      27.919  16.231  27.485  1.00 82.48           C  
ANISOU 3591  CG  HIS A 494    13716   9450   8172  -1259  -1558   -658       C  
ATOM   3592  ND1 HIS A 494      26.684  15.991  28.048  1.00 81.76           N  
ANISOU 3592  ND1 HIS A 494    13623   9572   7871  -1548  -1531   -592       N  
ATOM   3593  CD2 HIS A 494      28.683  15.153  27.780  1.00 91.44           C  
ANISOU 3593  CD2 HIS A 494    14946  10172   9624  -1303  -1729   -502       C  
ATOM   3594  CE1 HIS A 494      26.701  14.820  28.660  1.00 93.62           C  
ANISOU 3594  CE1 HIS A 494    15242  10810   9519  -1787  -1682   -388       C  
ATOM   3595  NE2 HIS A 494      27.902  14.291  28.512  1.00 98.32           N  
ANISOU 3595  NE2 HIS A 494    15901  11005  10449  -1634  -1820   -322       N  
ATOM   3596  N   PHE A 495      30.720  19.801  26.667  1.00 74.28           N  
ANISOU 3596  N   PHE A 495    12519   8644   7061   -434  -1397   -829       N  
ATOM   3597  CA  PHE A 495      31.388  20.862  25.923  1.00 81.70           C  
ANISOU 3597  CA  PHE A 495    13393   9669   7979   -196  -1307   -955       C  
ATOM   3598  C   PHE A 495      32.421  20.295  24.964  1.00100.35           C  
ANISOU 3598  C   PHE A 495    15716  11766  10645    -39  -1284  -1073       C  
ATOM   3599  O   PHE A 495      33.368  19.649  25.395  1.00103.73           O  
ANISOU 3599  O   PHE A 495    16143  11909  11361    -12  -1396   -946       O  
ATOM   3600  CB  PHE A 495      32.061  21.855  26.880  1.00 87.84           C  
ANISOU 3600  CB  PHE A 495    14194  10518   8662   -155  -1368   -790       C  
ATOM   3601  CG  PHE A 495      31.147  22.382  27.946  1.00101.55           C  
ANISOU 3601  CG  PHE A 495    15982  12496  10105   -325  -1357   -705       C  
ATOM   3602  CD1 PHE A 495      31.007  21.710  29.155  1.00113.63           C  
ANISOU 3602  CD1 PHE A 495    17609  13970  11594   -565  -1476   -494       C  
ATOM   3603  CD2 PHE A 495      30.416  23.541  27.738  1.00 97.48           C  
ANISOU 3603  CD2 PHE A 495    15417  12260   9363   -257  -1224   -840       C  
ATOM   3604  CE1 PHE A 495      30.159  22.187  30.139  1.00114.85           C  
ANISOU 3604  CE1 PHE A 495    17814  14378  11447   -752  -1417   -452       C  
ATOM   3605  CE2 PHE A 495      29.564  24.022  28.715  1.00108.93           C  
ANISOU 3605  CE2 PHE A 495    16889  13926  10574   -400  -1168   -812       C  
ATOM   3606  CZ  PHE A 495      29.437  23.343  29.919  1.00119.57           C  
ANISOU 3606  CZ  PHE A 495    18338  15251  11844   -658  -1243   -635       C  
ATOM   3607  N   PRO A 496      32.242  20.535  23.658  1.00105.04           N  
ANISOU 3607  N   PRO A 496    16270  12457  11182     55  -1140  -1317       N  
ATOM   3608  CA  PRO A 496      33.266  20.174  22.673  1.00104.52           C  
ANISOU 3608  CA  PRO A 496    16162  12194  11358    200  -1051  -1483       C  
ATOM   3609  C   PRO A 496      34.408  21.187  22.690  1.00107.76           C  
ANISOU 3609  C   PRO A 496    16504  12640  11799    369  -1024  -1426       C  
ATOM   3610  O   PRO A 496      34.223  22.281  23.217  1.00109.13           O  
ANISOU 3610  O   PRO A 496    16690  13023  11753    373  -1060  -1308       O  
ATOM   3611  CB  PRO A 496      32.504  20.214  21.349  1.00 96.76           C  
ANISOU 3611  CB  PRO A 496    15195  11384  10185    168   -914  -1745       C  
ATOM   3612  CG  PRO A 496      31.429  21.223  21.578  1.00 91.98           C  
ANISOU 3612  CG  PRO A 496    14587  11116   9247    112   -939  -1675       C  
ATOM   3613  CD  PRO A 496      31.031  21.084  23.022  1.00 97.36           C  
ANISOU 3613  CD  PRO A 496    15286  11786   9922      4  -1059  -1450       C  
ATOM   3614  N   VAL A 497      35.563  20.839  22.135  1.00116.20           N  
ANISOU 3614  N   VAL A 497    17492  13504  13153    499   -951  -1522       N  
ATOM   3615  CA  VAL A 497      36.693  21.764  22.142  1.00129.56           C  
ANISOU 3615  CA  VAL A 497    19094  15234  14900    636   -925  -1460       C  
ATOM   3616  C   VAL A 497      37.207  22.038  20.723  1.00138.18           C  
ANISOU 3616  C   VAL A 497    20128  16396  15979    726   -694  -1721       C  
ATOM   3617  O   VAL A 497      37.166  21.169  19.851  1.00144.27           O  
ANISOU 3617  O   VAL A 497    20899  17054  16862    720   -557  -1960       O  
ATOM   3618  CB  VAL A 497      37.847  21.233  23.030  1.00133.23           C  
ANISOU 3618  CB  VAL A 497    19459  15401  15761    700  -1075  -1265       C  
ATOM   3619  CG1 VAL A 497      38.562  20.075  22.359  1.00140.49           C  
ANISOU 3619  CG1 VAL A 497    20268  16002  17108    802   -980  -1442       C  
ATOM   3620  CG2 VAL A 497      38.833  22.346  23.358  1.00130.60           C  
ANISOU 3620  CG2 VAL A 497    19041  15159  15422    782  -1112  -1130       C  
ATOM   3621  N   SER A 498      37.674  23.264  20.498  1.00138.54           N  
ANISOU 3621  N   SER A 498    20143  16632  15866    781   -645  -1679       N  
ATOM   3622  CA  SER A 498      38.220  23.663  19.205  1.00123.14           C  
ANISOU 3622  CA  SER A 498    18149  14789  13850    823   -425  -1886       C  
ATOM   3623  C   SER A 498      39.551  22.968  18.930  1.00109.90           C  
ANISOU 3623  C   SER A 498    16303  12869  12585    934   -297  -1998       C  
ATOM   3624  O   SER A 498      39.605  21.964  18.218  1.00106.17           O  
ANISOU 3624  O   SER A 498    15812  12252  12277    940   -144  -2248       O  
ATOM   3625  CB  SER A 498      38.395  25.183  19.143  1.00114.77           C  
ANISOU 3625  CB  SER A 498    17105  13966  12535    831   -437  -1765       C  
ATOM   3626  OG  SER A 498      37.166  25.848  19.387  1.00116.08           O  
ANISOU 3626  OG  SER A 498    17393  14326  12385    762   -546  -1680       O  
ATOM   3627  N   SER A 505      37.626  12.600  14.248  1.00172.69           N  
ANISOU 3627  N   SER A 505    24733  18741  22140    576    653  -4476       N  
ATOM   3628  CA  SER A 505      38.479  13.769  14.429  1.00176.69           C  
ANISOU 3628  CA  SER A 505    25061  19499  22576    732    701  -4288       C  
ATOM   3629  C   SER A 505      39.128  13.761  15.808  1.00190.80           C  
ANISOU 3629  C   SER A 505    26659  21029  24807    927    435  -3869       C  
ATOM   3630  O   SER A 505      39.899  14.661  16.149  1.00191.04           O  
ANISOU 3630  O   SER A 505    26526  21212  24850   1055    422  -3670       O  
ATOM   3631  CB  SER A 505      37.671  15.055  14.233  1.00171.79           C  
ANISOU 3631  CB  SER A 505    24559  19428  21284    568    624  -4108       C  
ATOM   3632  OG  SER A 505      36.743  15.246  15.288  1.00163.90           O  
ANISOU 3632  OG  SER A 505    23625  18496  20153    489    288  -3721       O  
ATOM   3633  N   SER A 506      38.817  12.720  16.578  1.00215.14           N  
ANISOU 3633  N   SER A 506    29779  23717  28245    917    207  -3731       N  
ATOM   3634  CA  SER A 506      39.272  12.555  17.957  1.00211.70           C  
ANISOU 3634  CA  SER A 506    29217  23019  28199   1032   -115  -3290       C  
ATOM   3635  C   SER A 506      39.053  13.828  18.767  1.00208.80           C  
ANISOU 3635  C   SER A 506    28854  23054  27427    981   -311  -2884       C  
ATOM   3636  O   SER A 506      39.964  14.320  19.433  1.00221.91           O  
ANISOU 3636  O   SER A 506    30338  24686  29291   1126   -418  -2636       O  
ATOM   3637  CB  SER A 506      40.755  12.171  17.989  1.00211.30           C  
ANISOU 3637  CB  SER A 506    28879  22596  28810   1319    -24  -3362       C  
ATOM   3638  OG  SER A 506      40.980  10.926  17.353  1.00211.68           O  
ANISOU 3638  OG  SER A 506    28910  22198  29322   1393    155  -3748       O  
ATOM   3639  N   ARG A 507      37.831  14.346  18.717  1.00192.81           N  
ANISOU 3639  N   ARG A 507    27021  21391  24849    770   -363  -2828       N  
ATOM   3640  CA  ARG A 507      37.495  15.581  19.412  1.00168.42           C  
ANISOU 3640  CA  ARG A 507    23948  18680  21363    719   -512  -2506       C  
ATOM   3641  C   ARG A 507      37.437  15.361  20.915  1.00154.36           C  
ANISOU 3641  C   ARG A 507    22169  16741  19739    679   -841  -2081       C  
ATOM   3642  O   ARG A 507      37.018  14.300  21.374  1.00158.78           O  
ANISOU 3642  O   ARG A 507    22806  17014  20511    581   -989  -2003       O  
ATOM   3643  CB  ARG A 507      36.172  16.137  18.893  1.00155.96           C  
ANISOU 3643  CB  ARG A 507    22538  17502  19220    523   -470  -2587       C  
ATOM   3644  CG  ARG A 507      35.802  17.487  19.467  1.00152.75           C  
ANISOU 3644  CG  ARG A 507    22136  17474  18427    497   -577  -2322       C  
ATOM   3645  CD  ARG A 507      34.500  17.968  18.883  1.00154.49           C  
ANISOU 3645  CD  ARG A 507    22475  18047  18178    332   -547  -2411       C  
ATOM   3646  NE  ARG A 507      34.632  18.216  17.450  1.00159.23           N  
ANISOU 3646  NE  ARG A 507    23100  18801  18600    329   -322  -2725       N  
ATOM   3647  CZ  ARG A 507      35.065  19.359  16.928  1.00167.43           C  
ANISOU 3647  CZ  ARG A 507    24102  20094  19418    396   -222  -2733       C  
ATOM   3648  NH1 ARG A 507      35.397  20.371  17.719  1.00164.39           N  
ANISOU 3648  NH1 ARG A 507    23651  19821  18990    487   -326  -2464       N  
ATOM   3649  NH2 ARG A 507      35.159  19.494  15.612  1.00177.40           N  
ANISOU 3649  NH2 ARG A 507    25415  21504  20485    340    -22  -3008       N  
ATOM   3650  N   THR A 508      37.832  16.372  21.681  1.00135.52           N  
ANISOU 3650  N   THR A 508    19723  14548  17222    719   -960  -1802       N  
ATOM   3651  CA  THR A 508      37.780  16.277  23.134  1.00132.72           C  
ANISOU 3651  CA  THR A 508    19400  14104  16925    632  -1272  -1394       C  
ATOM   3652  C   THR A 508      36.562  16.999  23.700  1.00120.77           C  
ANISOU 3652  C   THR A 508    18042  12962  14885    429  -1342  -1247       C  
ATOM   3653  O   THR A 508      36.236  18.112  23.290  1.00117.39           O  
ANISOU 3653  O   THR A 508    17624  12888  14089    441  -1216  -1335       O  
ATOM   3654  CB  THR A 508      39.053  16.854  23.781  1.00135.11           C  
ANISOU 3654  CB  THR A 508    19539  14351  17447    775  -1395  -1164       C  
ATOM   3655  OG1 THR A 508      40.209  16.324  23.122  1.00137.58           O  
ANISOU 3655  OG1 THR A 508    19644  14365  18265    993  -1273  -1346       O  
ATOM   3656  CG2 THR A 508      39.115  16.503  25.258  1.00139.07           C  
ANISOU 3656  CG2 THR A 508    20087  14692  18060    653  -1750   -739       C  
ATOM   3657  N   TRP A 509      35.911  16.365  24.668  1.00115.01           N  
ANISOU 3657  N   TRP A 509    17421  12136  14142    239  -1545  -1015       N  
ATOM   3658  CA  TRP A 509      34.689  16.902  25.248  1.00113.14           C  
ANISOU 3658  CA  TRP A 509    17305  12237  13446     29  -1578   -906       C  
ATOM   3659  C   TRP A 509      34.849  17.068  26.758  1.00115.85           C  
ANISOU 3659  C   TRP A 509    17704  12585  13729   -107  -1819   -524       C  
ATOM   3660  O   TRP A 509      35.812  16.573  27.346  1.00124.81           O  
ANISOU 3660  O   TRP A 509    18799  13423  15201    -67  -2015   -309       O  
ATOM   3661  CB  TRP A 509      33.495  15.987  24.948  1.00112.34           C  
ANISOU 3661  CB  TRP A 509    17301  12104  13280   -162  -1551  -1017       C  
ATOM   3662  CG  TRP A 509      32.957  16.047  23.535  1.00109.20           C  
ANISOU 3662  CG  TRP A 509    16895  11843  12753   -123  -1328  -1384       C  
ATOM   3663  CD1 TRP A 509      33.513  15.495  22.415  1.00112.52           C  
ANISOU 3663  CD1 TRP A 509    17281  12051  13420      2  -1187  -1674       C  
ATOM   3664  CD2 TRP A 509      31.736  16.668  23.109  1.00 98.56           C  
ANISOU 3664  CD2 TRP A 509    15573  10879  10997   -235  -1234  -1497       C  
ATOM   3665  NE1 TRP A 509      32.722  15.746  21.319  1.00103.70           N  
ANISOU 3665  NE1 TRP A 509    16201  11182  12017    -58  -1024  -1949       N  
ATOM   3666  CE2 TRP A 509      31.624  16.463  21.719  1.00 98.76           C  
ANISOU 3666  CE2 TRP A 509    15599  10915  11009   -194  -1074  -1825       C  
ATOM   3667  CE3 TRP A 509      30.730  17.382  23.768  1.00 90.56           C  
ANISOU 3667  CE3 TRP A 509    14568  10200   9642   -367  -1266  -1362       C  
ATOM   3668  CZ2 TRP A 509      30.548  16.949  20.976  1.00 99.75           C  
ANISOU 3668  CZ2 TRP A 509    15735  11373  10792   -290   -999  -1973       C  
ATOM   3669  CZ3 TRP A 509      29.664  17.862  23.031  1.00 89.58           C  
ANISOU 3669  CZ3 TRP A 509    14416  10384   9237   -423  -1169  -1527       C  
ATOM   3670  CH2 TRP A 509      29.581  17.645  21.650  1.00 96.07           C  
ANISOU 3670  CH2 TRP A 509    15241  11209  10053   -388  -1063  -1807       C  
ATOM   3671  N   MET A 510      33.906  17.773  27.378  1.00110.23           N  
ANISOU 3671  N   MET A 510    17078  12214  12591   -276  -1806   -445       N  
ATOM   3672  CA  MET A 510      33.833  17.867  28.835  1.00109.73           C  
ANISOU 3672  CA  MET A 510    17114  12205  12373   -487  -2001   -117       C  
ATOM   3673  C   MET A 510      32.501  17.298  29.311  1.00 89.51           C  
ANISOU 3673  C   MET A 510    14664   9759   9588   -778  -2000    -62       C  
ATOM   3674  O   MET A 510      31.461  17.590  28.735  1.00 91.25           O  
ANISOU 3674  O   MET A 510    14859  10225   9585   -805  -1815   -276       O  
ATOM   3675  CB  MET A 510      33.987  19.319  29.305  1.00118.90           C  
ANISOU 3675  CB  MET A 510    18279  13684  13214   -453  -1954    -90       C  
ATOM   3676  CG  MET A 510      35.353  19.664  29.890  1.00121.18           C  
ANISOU 3676  CG  MET A 510    18534  13835  13673   -373  -2137    117       C  
ATOM   3677  SD  MET A 510      35.351  21.209  30.833  1.00150.34           S  
ANISOU 3677  SD  MET A 510    22310  17877  16933   -460  -2135    196       S  
ATOM   3678  CE  MET A 510      34.229  20.804  32.167  1.00 75.36           C  
ANISOU 3678  CE  MET A 510    13008   8539   7086   -849  -2209    387       C  
ATOM   3679  N   CYS A 511      32.528  16.509  30.376  1.00 76.83           N  
ANISOU 3679  N   CYS A 511    13168   7987   8037  -1017  -2222    247       N  
ATOM   3680  CA  CYS A 511      31.311  15.881  30.873  1.00 98.35           C  
ANISOU 3680  CA  CYS A 511    15996  10811  10560  -1339  -2222    327       C  
ATOM   3681  C   CYS A 511      30.974  16.378  32.270  1.00110.98           C  
ANISOU 3681  C   CYS A 511    17717  12679  11773  -1623  -2286    574       C  
ATOM   3682  O   CYS A 511      31.847  16.513  33.127  1.00106.53           O  
ANISOU 3682  O   CYS A 511    17225  12024  11226  -1673  -2493    837       O  
ATOM   3683  CB  CYS A 511      31.452  14.358  30.881  1.00110.11           C  
ANISOU 3683  CB  CYS A 511    17549  11861  12427  -1454  -2416    478       C  
ATOM   3684  SG  CYS A 511      29.985  13.468  31.460  1.00180.05           S  
ANISOU 3684  SG  CYS A 511    26537  20809  21065  -1901  -2431    604       S  
ATOM   3685  N   ILE A 512      29.703  16.694  32.480  1.00115.46           N  
ANISOU 3685  N   ILE A 512    18294  13596  11981  -1816  -2099    471       N  
ATOM   3686  CA  ILE A 512      29.251  17.166  33.776  1.00118.74           C  
ANISOU 3686  CA  ILE A 512    18823  14306  11988  -2116  -2086    638       C  
ATOM   3687  C   ILE A 512      28.118  16.280  34.301  1.00137.08           C  
ANISOU 3687  C   ILE A 512    21219  16710  14155  -2507  -2069    754       C  
ATOM   3688  O   ILE A 512      27.080  16.115  33.661  1.00146.13           O  
ANISOU 3688  O   ILE A 512    22256  17993  15274  -2527  -1886    543       O  
ATOM   3689  CB  ILE A 512      28.835  18.647  33.696  1.00111.00           C  
ANISOU 3689  CB  ILE A 512    17755  13720  10699  -1977  -1825    380       C  
ATOM   3690  CG1 ILE A 512      30.032  19.529  34.049  1.00101.20           C  
ANISOU 3690  CG1 ILE A 512    16559  12443   9451  -1818  -1927    449       C  
ATOM   3691  CG2 ILE A 512      27.703  18.956  34.643  1.00126.55           C  
ANISOU 3691  CG2 ILE A 512    19771  16060  12252  -2298  -1656    377       C  
ATOM   3692  CD1 ILE A 512      31.036  19.667  32.945  1.00 74.06           C  
ANISOU 3692  CD1 ILE A 512    13003   8763   6374  -1443  -1973    339       C  
ATOM   3693  N   SER A 513      28.346  15.693  35.470  1.00145.32           N  
ANISOU 3693  N   SER A 513    22447  17669  15098  -2845  -2285   1114       N  
ATOM   3694  CA  SER A 513      27.414  14.745  36.062  1.00162.77           C  
ANISOU 3694  CA  SER A 513    24759  19917  17171  -3273  -2310   1296       C  
ATOM   3695  C   SER A 513      27.112  15.102  37.512  1.00171.65           C  
ANISOU 3695  C   SER A 513    26052  21362  17805  -3686  -2297   1512       C  
ATOM   3696  O   SER A 513      28.005  15.495  38.261  1.00182.60           O  
ANISOU 3696  O   SER A 513    27570  22724  19087  -3722  -2473   1711       O  
ATOM   3697  CB  SER A 513      27.968  13.320  35.979  1.00172.05           C  
ANISOU 3697  CB  SER A 513    26033  20574  18766  -3352  -2640   1581       C  
ATOM   3698  OG  SER A 513      27.154  12.424  36.715  1.00180.50           O  
ANISOU 3698  OG  SER A 513    27240  21667  19674  -3826  -2708   1829       O  
ATOM   3699  N   ARG A 514      25.849  14.973  37.898  1.00165.58           N  
ANISOU 3699  N   ARG A 514    25273  20912  16727  -4016  -2077   1458       N  
ATOM   3700  CA  ARG A 514      25.458  15.176  39.283  1.00152.04           C  
ANISOU 3700  CA  ARG A 514    23732  19523  14512  -4480  -2021   1644       C  
ATOM   3701  C   ARG A 514      25.041  13.802  39.854  1.00158.69           C  
ANISOU 3701  C   ARG A 514    24737  20215  15341  -4964  -2213   2012       C  
ATOM   3702  O   ARG A 514      25.485  12.772  39.345  1.00156.69           O  
ANISOU 3702  O   ARG A 514    24512  19503  15518  -4888  -2492   2190       O  
ATOM   3703  CB  ARG A 514      24.350  16.244  39.363  1.00135.09           C  
ANISOU 3703  CB  ARG A 514    21422  17901  12007  -4489  -1568   1267       C  
ATOM   3704  CG  ARG A 514      24.008  16.727  40.770  1.00134.53           C  
ANISOU 3704  CG  ARG A 514    21518  18222  11375  -4923  -1416   1346       C  
ATOM   3705  CD  ARG A 514      22.882  17.752  40.827  1.00130.12           C  
ANISOU 3705  CD  ARG A 514    20754  18148  10538  -4901   -933    930       C  
ATOM   3706  NE  ARG A 514      23.304  19.109  40.499  1.00121.47           N  
ANISOU 3706  NE  ARG A 514    19562  17131   9459  -4482   -794    620       N  
ATOM   3707  CZ  ARG A 514      23.548  20.035  41.421  1.00120.68           C  
ANISOU 3707  CZ  ARG A 514    19601  17262   8990  -4599   -669    544       C  
ATOM   3708  NH1 ARG A 514      23.427  19.733  42.705  1.00136.74           N  
ANISOU 3708  NH1 ARG A 514    21882  19495  10580  -5131   -666    754       N  
ATOM   3709  NH2 ARG A 514      23.914  21.256  41.071  1.00109.69           N  
ANISOU 3709  NH2 ARG A 514    18124  15901   7652  -4217   -554    260       N  
ATOM   3710  N   GLN A 515      24.208  13.782  40.892  1.00161.08           N  
ANISOU 3710  N   GLN A 515    25148  20887  15168  -5464  -2057   2117       N  
ATOM   3711  CA  GLN A 515      23.753  12.547  41.530  1.00151.11           C  
ANISOU 3711  CA  GLN A 515    24061  19529  13823  -5997  -2225   2494       C  
ATOM   3712  C   GLN A 515      22.468  12.774  42.312  1.00148.21           C  
ANISOU 3712  C   GLN A 515    23681  19709  12923  -6471  -1855   2407       C  
ATOM   3713  O   GLN A 515      21.504  12.027  42.152  1.00149.59           O  
ANISOU 3713  O   GLN A 515    23780  19934  13123  -6734  -1755   2424       O  
ATOM   3714  CB  GLN A 515      24.826  11.990  42.474  1.00148.17           C  
ANISOU 3714  CB  GLN A 515    24005  18868  13426  -6258  -2687   3022       C  
ATOM   3715  CG  GLN A 515      25.221  10.535  42.222  1.00147.65           C  
ANISOU 3715  CG  GLN A 515    24043  18223  13836  -6340  -3109   3403       C  
ATOM   3716  CD  GLN A 515      25.858  10.325  40.867  1.00139.60           C  
ANISOU 3716  CD  GLN A 515    22828  16744  13469  -5745  -3209   3189       C  
ATOM   3717  OE1 GLN A 515      25.193   9.918  39.912  1.00139.43           O  
ANISOU 3717  OE1 GLN A 515    22644  16637  13696  -5608  -3051   2935       O  
ATOM   3718  NE2 GLN A 515      27.149  10.623  40.767  1.00134.04           N  
ANISOU 3718  NE2 GLN A 515    22133  15766  13032  -5407  -3460   3275       N  
TER    3719      GLN A 515                                                      
ATOM   3720  N   ASN B  28     -11.233  71.081  61.719  1.00185.11           N  
ANISOU 3720  N   ASN B  28    33588  17326  19417   -553  -6606  -5539       N  
ATOM   3721  CA  ASN B  28     -10.209  70.913  60.696  1.00170.62           C  
ANISOU 3721  CA  ASN B  28    31249  15440  18138   -939  -6924  -5203       C  
ATOM   3722  C   ASN B  28     -10.833  70.455  59.384  1.00181.64           C  
ANISOU 3722  C   ASN B  28    32306  16988  19720  -1077  -6592  -4980       C  
ATOM   3723  O   ASN B  28     -11.589  69.486  59.363  1.00188.39           O  
ANISOU 3723  O   ASN B  28    33220  18180  20180   -995  -6163  -4950       O  
ATOM   3724  CB  ASN B  28      -9.149  69.911  61.168  1.00183.58           C  
ANISOU 3724  CB  ASN B  28    32823  17283  19646  -1097  -7142  -5025       C  
ATOM   3725  CG  ASN B  28      -8.003  69.756  60.185  1.00151.03           C  
ANISOU 3725  CG  ASN B  28    28162  13092  16130  -1482  -7455  -4694       C  
ATOM   3726  OD1 ASN B  28      -7.613  70.707  59.512  1.00151.77           O  
ANISOU 3726  OD1 ASN B  28    28011  12869  16785  -1634  -7691  -4642       O  
ATOM   3727  ND2 ASN B  28      -7.451  68.551  60.106  1.00148.09           N  
ANISOU 3727  ND2 ASN B  28    27605  13007  15657  -1636  -7432  -4462       N  
ATOM   3728  N   PRO B  29     -10.534  71.168  58.286  1.00191.28           N  
ANISOU 3728  N   PRO B  29    33189  17943  21544  -1283  -6782  -4817       N  
ATOM   3729  CA  PRO B  29     -11.074  70.841  56.959  1.00190.55           C  
ANISOU 3729  CA  PRO B  29    32725  17984  21691  -1404  -6477  -4541       C  
ATOM   3730  C   PRO B  29     -10.672  69.458  56.432  1.00184.67           C  
ANISOU 3730  C   PRO B  29    31606  17670  20890  -1630  -6279  -4164       C  
ATOM   3731  O   PRO B  29     -11.507  68.790  55.827  1.00172.19           O  
ANISOU 3731  O   PRO B  29    29760  16451  19213  -1562  -5782  -3963       O  
ATOM   3732  CB  PRO B  29     -10.500  71.948  56.061  1.00190.72           C  
ANISOU 3732  CB  PRO B  29    32497  17580  22386  -1606  -6801  -4401       C  
ATOM   3733  CG  PRO B  29      -9.410  72.600  56.864  1.00195.89           C  
ANISOU 3733  CG  PRO B  29    33263  17958  23209  -1673  -7281  -4529       C  
ATOM   3734  CD  PRO B  29      -9.834  72.462  58.286  1.00196.42           C  
ANISOU 3734  CD  PRO B  29    33793  18154  22682  -1351  -7215  -4875       C  
ATOM   3735  N   GLU B  30      -9.422  69.048  56.635  1.00186.97           N  
ANISOU 3735  N   GLU B  30    31857  17903  21278  -1889  -6680  -4080       N  
ATOM   3736  CA  GLU B  30      -8.946  67.762  56.122  1.00190.59           C  
ANISOU 3736  CA  GLU B  30    31957  18734  21726  -2103  -6525  -3728       C  
ATOM   3737  C   GLU B  30      -9.564  66.523  56.785  1.00205.83           C  
ANISOU 3737  C   GLU B  30    34079  21101  23027  -1937  -6156  -3765       C  
ATOM   3738  O   GLU B  30      -9.899  65.556  56.103  1.00207.76           O  
ANISOU 3738  O   GLU B  30    33989  21717  23232  -1999  -5762  -3473       O  
ATOM   3739  CB  GLU B  30      -7.423  67.677  56.255  1.00195.88           C  
ANISOU 3739  CB  GLU B  30    32451  19250  22726  -2370  -7007  -3615       C  
ATOM   3740  CG  GLU B  30      -6.673  68.821  55.612  1.00204.26           C  
ANISOU 3740  CG  GLU B  30    33244  19896  24471  -2567  -7317  -3519       C  
ATOM   3741  CD  GLU B  30      -5.176  68.715  55.806  1.00211.62           C  
ANISOU 3741  CD  GLU B  30    33889  20732  25783  -2784  -7697  -3386       C  
ATOM   3742  OE1 GLU B  30      -4.743  67.950  56.693  1.00218.12           O  
ANISOU 3742  OE1 GLU B  30    34825  21753  26300  -2710  -7811  -3449       O  
ATOM   3743  OE2 GLU B  30      -4.431  69.401  55.075  1.00211.25           O  
ANISOU 3743  OE2 GLU B  30    33508  20398  26359  -3020  -7871  -3214       O  
ATOM   3744  N   THR B  31      -9.690  66.541  58.110  1.00216.08           N  
ANISOU 3744  N   THR B  31    35902  22355  23845  -1720  -6257  -4093       N  
ATOM   3745  CA  THR B  31     -10.218  65.387  58.841  1.00198.34           C  
ANISOU 3745  CA  THR B  31    33907  20475  20977  -1566  -5902  -4123       C  
ATOM   3746  C   THR B  31     -11.729  65.176  58.744  1.00206.78           C  
ANISOU 3746  C   THR B  31    35007  21793  21767  -1324  -5246  -4173       C  
ATOM   3747  O   THR B  31     -12.195  64.041  58.829  1.00211.82           O  
ANISOU 3747  O   THR B  31    35597  22800  22086  -1295  -4832  -4034       O  
ATOM   3748  CB  THR B  31      -9.856  65.460  60.337  1.00196.23           C  
ANISOU 3748  CB  THR B  31    34061  20161  20336  -1353  -6072  -4331       C  
ATOM   3749  OG1 THR B  31     -10.435  66.636  60.913  1.00200.00           O  
ANISOU 3749  OG1 THR B  31    34874  20375  20741  -1096  -6080  -4662       O  
ATOM   3750  CG2 THR B  31      -8.347  65.491  60.524  1.00193.95           C  
ANISOU 3750  CG2 THR B  31    33584  19725  20385  -1543  -6629  -4205       C  
ATOM   3751  N   ASN B  32     -12.502  66.249  58.598  1.00229.20           N  
ANISOU 3751  N   ASN B  32    37883  24434  24769  -1136  -5128  -4357       N  
ATOM   3752  CA  ASN B  32     -13.943  66.083  58.419  1.00245.41           C  
ANISOU 3752  CA  ASN B  32    39828  26726  26691   -898  -4490  -4379       C  
ATOM   3753  C   ASN B  32     -14.291  65.508  57.045  1.00259.63           C  
ANISOU 3753  C   ASN B  32    40984  28803  28859  -1053  -4192  -3987       C  
ATOM   3754  O   ASN B  32     -15.202  64.690  56.927  1.00281.50           O  
ANISOU 3754  O   ASN B  32    43593  31907  31457   -961  -3682  -3901       O  
ATOM   3755  CB  ASN B  32     -14.693  67.403  58.653  1.00245.95           C  
ANISOU 3755  CB  ASN B  32    40105  26487  26857   -621  -4461  -4705       C  
ATOM   3756  CG  ASN B  32     -14.186  68.537  57.787  1.00246.01           C  
ANISOU 3756  CG  ASN B  32    39873  26135  27466   -758  -4874  -4635       C  
ATOM   3757  OD1 ASN B  32     -14.255  68.479  56.560  1.00244.71           O  
ANISOU 3757  OD1 ASN B  32    39205  26054  27719   -908  -4787  -4317       O  
ATOM   3758  ND2 ASN B  32     -13.707  69.596  58.427  1.00247.33           N  
ANISOU 3758  ND2 ASN B  32    40433  25874  27667   -694  -5320  -4937       N  
ATOM   3759  N   LEU B  33     -13.571  65.932  56.010  1.00222.29           N  
ANISOU 3759  N   LEU B  33    35904  23920  24637  -1288  -4504  -3752       N  
ATOM   3760  CA  LEU B  33     -13.793  65.390  54.670  1.00184.73           C  
ANISOU 3760  CA  LEU B  33    30601  19400  20188  -1433  -4269  -3375       C  
ATOM   3761  C   LEU B  33     -13.327  63.936  54.610  1.00164.62           C  
ANISOU 3761  C   LEU B  33    27902  17207  17438  -1619  -4152  -3129       C  
ATOM   3762  O   LEU B  33     -13.883  63.133  53.866  1.00169.52           O  
ANISOU 3762  O   LEU B  33    28184  18132  18093  -1647  -3801  -2900       O  
ATOM   3763  CB  LEU B  33     -13.105  66.244  53.598  1.00168.78           C  
ANISOU 3763  CB  LEU B  33    28313  17093  18723  -1628  -4596  -3175       C  
ATOM   3764  CG  LEU B  33     -11.611  66.157  53.301  1.00151.36           C  
ANISOU 3764  CG  LEU B  33    25985  14744  16781  -1960  -5010  -2972       C  
ATOM   3765  CD1 LEU B  33     -11.325  65.085  52.265  1.00121.35           C  
ANISOU 3765  CD1 LEU B  33    21755  11260  13095  -2168  -4810  -2568       C  
ATOM   3766  CD2 LEU B  33     -11.112  67.507  52.816  1.00163.23           C  
ANISOU 3766  CD2 LEU B  33    27459  15788  18771  -2050  -5355  -2972       C  
ATOM   3767  N   LEU B  34     -12.292  63.608  55.378  1.00146.32           N  
ANISOU 3767  N   LEU B  34    25838  14826  14932  -1740  -4485  -3184       N  
ATOM   3768  CA  LEU B  34     -11.811  62.231  55.468  1.00141.28           C  
ANISOU 3768  CA  LEU B  34    25117  14490  14072  -1888  -4412  -2981       C  
ATOM   3769  C   LEU B  34     -12.862  61.354  56.135  1.00127.57           C  
ANISOU 3769  C   LEU B  34    23572  13061  11839  -1689  -3914  -3067       C  
ATOM   3770  O   LEU B  34     -13.017  60.182  55.803  1.00124.59           O  
ANISOU 3770  O   LEU B  34    22976  13000  11362  -1774  -3636  -2841       O  
ATOM   3771  CB  LEU B  34     -10.507  62.161  56.257  1.00159.00           C  
ANISOU 3771  CB  LEU B  34    27633  16553  16228  -2017  -4937  -3066       C  
ATOM   3772  CG  LEU B  34      -9.202  62.218  55.471  1.00163.10           C  
ANISOU 3772  CG  LEU B  34    27786  16935  17249  -2326  -5331  -2822       C  
ATOM   3773  CD1 LEU B  34      -8.022  62.174  56.433  1.00168.21           C  
ANISOU 3773  CD1 LEU B  34    28724  17378  17811  -2407  -5886  -2977       C  
ATOM   3774  CD2 LEU B  34      -9.140  61.068  54.480  1.00151.94           C  
ANISOU 3774  CD2 LEU B  34    25923  15866  15942  -2487  -5033  -2445       C  
ATOM   3775  N   PHE B  35     -13.562  61.937  57.100  1.00126.45           N  
ANISOU 3775  N   PHE B  35    23853  12799  11393  -1424  -3790  -3402       N  
ATOM   3776  CA  PHE B  35     -14.716  61.311  57.729  1.00135.50           C  
ANISOU 3776  CA  PHE B  35    25176  14186  12122  -1207  -3226  -3509       C  
ATOM   3777  C   PHE B  35     -15.821  61.167  56.692  1.00149.29           C  
ANISOU 3777  C   PHE B  35    26411  16133  14181  -1167  -2775  -3355       C  
ATOM   3778  O   PHE B  35     -16.467  60.126  56.593  1.00154.44           O  
ANISOU 3778  O   PHE B  35    26891  17090  14699  -1166  -2340  -3223       O  
ATOM   3779  CB  PHE B  35     -15.178  62.138  58.931  1.00139.25           C  
ANISOU 3779  CB  PHE B  35    26225  14439  12245   -915  -3192  -3919       C  
ATOM   3780  CG  PHE B  35     -16.599  61.884  59.345  1.00130.11           C  
ANISOU 3780  CG  PHE B  35    25138  13462  10835   -654  -2517  -4052       C  
ATOM   3781  CD1 PHE B  35     -16.918  60.812  60.155  1.00131.03           C  
ANISOU 3781  CD1 PHE B  35    25532  13809  10445   -596  -2127  -4040       C  
ATOM   3782  CD2 PHE B  35     -17.612  62.747  58.952  1.00131.26           C  
ANISOU 3782  CD2 PHE B  35    25078  13519  11274   -459  -2269  -4192       C  
ATOM   3783  CE1 PHE B  35     -18.222  60.591  60.544  1.00138.22           C  
ANISOU 3783  CE1 PHE B  35    26478  14864  11175   -370  -1456  -4156       C  
ATOM   3784  CE2 PHE B  35     -18.916  62.532  59.338  1.00133.27           C  
ANISOU 3784  CE2 PHE B  35    25341  13923  11372   -216  -1634  -4327       C  
ATOM   3785  CZ  PHE B  35     -19.223  61.454  60.136  1.00137.25           C  
ANISOU 3785  CZ  PHE B  35    26092  14660  11396   -181  -1205  -4308       C  
ATOM   3786  N   ASN B  36     -16.020  62.230  55.918  1.00156.07           N  
ANISOU 3786  N   ASN B  36    27038  16790  15473  -1133  -2916  -3375       N  
ATOM   3787  CA  ASN B  36     -17.012  62.251  54.848  1.00155.23           C  
ANISOU 3787  CA  ASN B  36    26458  16813  15711  -1076  -2608  -3242       C  
ATOM   3788  C   ASN B  36     -16.659  61.278  53.721  1.00138.92           C  
ANISOU 3788  C   ASN B  36    23944  14992  13847  -1325  -2595  -2856       C  
ATOM   3789  O   ASN B  36     -17.542  60.649  53.137  1.00133.78           O  
ANISOU 3789  O   ASN B  36    22966  14579  13285  -1287  -2240  -2739       O  
ATOM   3790  CB  ASN B  36     -17.162  63.668  54.291  1.00164.56           C  
ANISOU 3790  CB  ASN B  36    27567  17668  17290   -979  -2845  -3339       C  
ATOM   3791  CG  ASN B  36     -18.012  64.560  55.176  1.00170.76           C  
ANISOU 3791  CG  ASN B  36    28673  18265  17942   -654  -2687  -3730       C  
ATOM   3792  OD1 ASN B  36     -17.589  65.647  55.571  1.00178.47           O  
ANISOU 3792  OD1 ASN B  36    29949  18895  18967   -588  -3026  -3937       O  
ATOM   3793  ND2 ASN B  36     -19.223  64.108  55.485  1.00168.48           N  
ANISOU 3793  ND2 ASN B  36    28312  18189  17516   -445  -2157  -3838       N  
ATOM   3794  N   LEU B  37     -15.370  61.176  53.402  1.00126.09           N  
ANISOU 3794  N   LEU B  37    22296  13289  12324  -1574  -2989  -2670       N  
ATOM   3795  CA  LEU B  37     -14.910  60.219  52.400  1.00123.67           C  
ANISOU 3795  CA  LEU B  37    21617  13202  12171  -1803  -2974  -2316       C  
ATOM   3796  C   LEU B  37     -15.180  58.791  52.863  1.00123.95           C  
ANISOU 3796  C   LEU B  37    21668  13570  11857  -1825  -2654  -2250       C  
ATOM   3797  O   LEU B  37     -15.643  57.956  52.087  1.00112.39           O  
ANISOU 3797  O   LEU B  37    19869  12350  10483  -1880  -2401  -2047       O  
ATOM   3798  CB  LEU B  37     -13.420  60.397  52.100  1.00106.68           C  
ANISOU 3798  CB  LEU B  37    19442  10879  10213  -2055  -3425  -2156       C  
ATOM   3799  CG  LEU B  37     -13.027  61.483  51.096  1.00116.14           C  
ANISOU 3799  CG  LEU B  37    20450  11800  11877  -2138  -3673  -2041       C  
ATOM   3800  CD1 LEU B  37     -11.647  61.199  50.509  1.00107.83           C  
ANISOU 3800  CD1 LEU B  37    19212  10694  11063  -2431  -3945  -1773       C  
ATOM   3801  CD2 LEU B  37     -14.074  61.636  50.001  1.00105.16           C  
ANISOU 3801  CD2 LEU B  37    18771  10497  10688  -2029  -3408  -1921       C  
ATOM   3802  N   ASN B  38     -14.884  58.516  54.130  1.00130.02           N  
ANISOU 3802  N   ASN B  38    22858  14325  12219  -1778  -2684  -2421       N  
ATOM   3803  CA  ASN B  38     -15.163  57.210  54.717  1.00131.00           C  
ANISOU 3803  CA  ASN B  38    23087  14723  11966  -1780  -2363  -2368       C  
ATOM   3804  C   ASN B  38     -16.662  57.005  54.882  1.00129.59           C  
ANISOU 3804  C   ASN B  38    22836  14699  11703  -1581  -1802  -2477       C  
ATOM   3805  O   ASN B  38     -17.153  55.880  54.826  1.00135.44           O  
ANISOU 3805  O   ASN B  38    23433  15695  12334  -1622  -1447  -2346       O  
ATOM   3806  CB  ASN B  38     -14.454  57.050  56.063  1.00144.19           C  
ANISOU 3806  CB  ASN B  38    25307  16295  13183  -1752  -2571  -2528       C  
ATOM   3807  CG  ASN B  38     -12.953  56.894  55.916  1.00158.44           C  
ANISOU 3807  CG  ASN B  38    27102  17998  15101  -1974  -3104  -2387       C  
ATOM   3808  OD1 ASN B  38     -12.460  55.808  55.615  1.00145.52           O  
ANISOU 3808  OD1 ASN B  38    25299  16547  13445  -2132  -3101  -2152       O  
ATOM   3809  ND2 ASN B  38     -12.218  57.979  56.133  1.00182.46           N  
ANISOU 3809  ND2 ASN B  38    30304  20724  18297  -1984  -3567  -2540       N  
ATOM   3810  N   SER B  39     -17.385  58.101  55.095  1.00127.29           N  
ANISOU 3810  N   SER B  39    22630  14234  11503  -1366  -1723  -2725       N  
ATOM   3811  CA  SER B  39     -18.842  58.059  55.177  1.00137.08           C  
ANISOU 3811  CA  SER B  39    23722  15584  12778  -1159  -1195  -2850       C  
ATOM   3812  C   SER B  39     -19.434  57.605  53.846  1.00141.45           C  
ANISOU 3812  C   SER B  39    23682  16315  13749  -1239  -1058  -2623       C  
ATOM   3813  O   SER B  39     -20.441  56.896  53.811  1.00141.68           O  
ANISOU 3813  O   SER B  39    23486  16541  13806  -1181   -613  -2611       O  
ATOM   3814  CB  SER B  39     -19.404  59.425  55.575  1.00149.14           C  
ANISOU 3814  CB  SER B  39    25432  16852  14384   -899  -1198  -3168       C  
ATOM   3815  OG  SER B  39     -20.779  59.528  55.249  1.00153.03           O  
ANISOU 3815  OG  SER B  39    25598  17426  15122   -714   -767  -3250       O  
ATOM   3816  N   CYS B  40     -18.811  58.032  52.752  1.00142.73           N  
ANISOU 3816  N   CYS B  40    23605  16385  14241  -1369  -1441  -2448       N  
ATOM   3817  CA  CYS B  40     -19.225  57.597  51.424  1.00134.94           C  
ANISOU 3817  CA  CYS B  40    22130  15544  13597  -1444  -1390  -2219       C  
ATOM   3818  C   CYS B  40     -18.914  56.126  51.209  1.00132.05           C  
ANISOU 3818  C   CYS B  40    21627  15451  13095  -1643  -1264  -1981       C  
ATOM   3819  O   CYS B  40     -19.763  55.365  50.754  1.00135.93           O  
ANISOU 3819  O   CYS B  40    21811  16135  13701  -1634   -975  -1908       O  
ATOM   3820  CB  CYS B  40     -18.523  58.414  50.336  1.00134.99           C  
ANISOU 3820  CB  CYS B  40    22006  15361  13925  -1535  -1812  -2067       C  
ATOM   3821  SG  CYS B  40     -19.342  59.939  49.837  1.00108.09           S  
ANISOU 3821  SG  CYS B  40    18514  11678  10879  -1292  -1909  -2235       S  
ATOM   3822  N   SER B  41     -17.697  55.731  51.573  1.00132.81           N  
ANISOU 3822  N   SER B  41    21950  15540  12971  -1816  -1502  -1876       N  
ATOM   3823  CA  SER B  41     -17.219  54.373  51.338  1.00119.22           C  
ANISOU 3823  CA  SER B  41    20121  14042  11135  -2007  -1449  -1639       C  
ATOM   3824  C   SER B  41     -18.045  53.337  52.098  1.00112.29           C  
ANISOU 3824  C   SER B  41    19309  13364   9992  -1955   -992  -1690       C  
ATOM   3825  O   SER B  41     -18.303  52.244  51.587  1.00 95.94           O  
ANISOU 3825  O   SER B  41    16984  11495   7975  -2059   -810  -1514       O  
ATOM   3826  CB  SER B  41     -15.741  54.269  51.723  1.00116.47           C  
ANISOU 3826  CB  SER B  41    20018  13604  10629  -2168  -1824  -1560       C  
ATOM   3827  OG  SER B  41     -15.220  52.983  51.448  1.00117.99           O  
ANISOU 3827  OG  SER B  41    20096  13992  10743  -2339  -1798  -1330       O  
ATOM   3828  N   LYS B  42     -18.483  53.697  53.301  1.00117.48           N  
ANISOU 3828  N   LYS B  42    20320  13947  10370  -1790   -788  -1932       N  
ATOM   3829  CA  LYS B  42     -19.380  52.843  54.071  1.00123.29           C  
ANISOU 3829  CA  LYS B  42    21143  14837  10866  -1721   -267  -1988       C  
ATOM   3830  C   LYS B  42     -20.645  52.586  53.273  1.00122.14           C  
ANISOU 3830  C   LYS B  42    20491  14816  11099  -1673     74  -1964       C  
ATOM   3831  O   LYS B  42     -21.089  51.450  53.133  1.00115.80           O  
ANISOU 3831  O   LYS B  42    19491  14197  10310  -1765    368  -1834       O  
ATOM   3832  CB  LYS B  42     -19.738  53.467  55.423  1.00135.71           C  
ANISOU 3832  CB  LYS B  42    23199  16275  12089  -1507    -61  -2277       C  
ATOM   3833  CG  LYS B  42     -18.615  53.522  56.447  1.00136.80           C  
ANISOU 3833  CG  LYS B  42    23923  16292  11764  -1528   -368  -2333       C  
ATOM   3834  CD  LYS B  42     -19.163  53.228  57.838  1.00134.85           C  
ANISOU 3834  CD  LYS B  42    24179  16047  11009  -1363     67  -2503       C  
ATOM   3835  CE  LYS B  42     -20.367  54.108  58.159  1.00127.89           C  
ANISOU 3835  CE  LYS B  42    23291  15082  10218  -1105    466  -2777       C  
ATOM   3836  NZ  LYS B  42     -21.131  53.603  59.334  1.00122.37           N  
ANISOU 3836  NZ  LYS B  42    22973  14435   9087   -958   1076  -2890       N  
ATOM   3837  N   SER B  43     -21.227  53.663  52.762  1.00125.82           N  
ANISOU 3837  N   SER B  43    20751  15158  11895  -1522      5  -2101       N  
ATOM   3838  CA  SER B  43     -22.463  53.571  52.004  1.00131.57           C  
ANISOU 3838  CA  SER B  43    20990  15965  13036  -1438    253  -2118       C  
ATOM   3839  C   SER B  43     -22.209  53.470  50.511  1.00145.86           C  
ANISOU 3839  C   SER B  43    22420  17811  15191  -1556    -89  -1904       C  
ATOM   3840  O   SER B  43     -23.151  53.480  49.725  1.00149.76           O  
ANISOU 3840  O   SER B  43    22511  18338  16053  -1478    -12  -1916       O  
ATOM   3841  CB  SER B  43     -23.361  54.772  52.299  1.00132.27           C  
ANISOU 3841  CB  SER B  43    21064  15886  13308  -1166    385  -2403       C  
ATOM   3842  OG  SER B  43     -24.618  54.624  51.664  1.00131.15           O  
ANISOU 3842  OG  SER B  43    20421  15812  13597  -1068    630  -2442       O  
ATOM   3843  N   LYS B  44     -20.935  53.387  50.134  1.00158.07           N  
ANISOU 3843  N   LYS B  44    24106  19333  16619  -1729   -469  -1717       N  
ATOM   3844  CA  LYS B  44     -20.532  53.160  48.745  1.00174.32           C  
ANISOU 3844  CA  LYS B  44    25882  21431  18921  -1855   -751  -1481       C  
ATOM   3845  C   LYS B  44     -21.116  54.168  47.762  1.00182.55           C  
ANISOU 3845  C   LYS B  44    26690  22335  20335  -1710   -927  -1524       C  
ATOM   3846  O   LYS B  44     -21.484  53.806  46.646  1.00196.99           O  
ANISOU 3846  O   LYS B  44    28213  24235  22398  -1729   -996  -1393       O  
ATOM   3847  CB  LYS B  44     -20.919  51.749  48.298  1.00181.27           C  
ANISOU 3847  CB  LYS B  44    26493  22541  19840  -1973   -545  -1327       C  
ATOM   3848  CG  LYS B  44     -19.813  50.708  48.445  1.00189.62           C  
ANISOU 3848  CG  LYS B  44    27706  23711  20629  -2189   -623  -1125       C  
ATOM   3849  CD  LYS B  44     -20.102  49.468  47.599  1.00192.99           C  
ANISOU 3849  CD  LYS B  44    27827  24319  21181  -2305   -533   -948       C  
ATOM   3850  CE  LYS B  44     -19.143  48.332  47.921  1.00191.20           C  
ANISOU 3850  CE  LYS B  44    27765  24201  20684  -2491   -544   -775       C  
ATOM   3851  NZ  LYS B  44     -19.366  47.767  49.279  1.00185.73           N  
ANISOU 3851  NZ  LYS B  44    27329  23554  19687  -2488   -227   -861       N  
ATOM   3852  N   ASP B  45     -21.204  55.426  48.174  1.00158.39           N  
ANISOU 3852  N   ASP B  45    23805  19059  17318  -1552  -1023  -1711       N  
ATOM   3853  CA  ASP B  45     -21.671  56.487  47.291  1.00131.83           C  
ANISOU 3853  CA  ASP B  45    20280  15517  14293  -1399  -1233  -1746       C  
ATOM   3854  C   ASP B  45     -20.483  57.096  46.548  1.00118.25           C  
ANISOU 3854  C   ASP B  45    18693  13631  12604  -1526  -1643  -1551       C  
ATOM   3855  O   ASP B  45     -19.949  58.119  46.965  1.00118.97           O  
ANISOU 3855  O   ASP B  45    19036  13492  12674  -1495  -1828  -1643       O  
ATOM   3856  CB  ASP B  45     -22.418  57.558  48.094  1.00131.10           C  
ANISOU 3856  CB  ASP B  45    20303  15246  14265  -1146  -1111  -2057       C  
ATOM   3857  CG  ASP B  45     -23.154  58.561  47.215  1.00128.08           C  
ANISOU 3857  CG  ASP B  45    19711  14682  14272   -943  -1291  -2116       C  
ATOM   3858  OD1 ASP B  45     -22.622  58.954  46.156  1.00132.57           O  
ANISOU 3858  OD1 ASP B  45    20259  15140  14972  -1007  -1636  -1921       O  
ATOM   3859  OD2 ASP B  45     -24.262  58.987  47.607  1.00120.80           O  
ANISOU 3859  OD2 ASP B  45    18664  13708  13526   -705  -1076  -2361       O  
ATOM   3860  N   LEU B  46     -20.087  56.485  45.436  1.00123.10           N  
ANISOU 3860  N   LEU B  46    19143  14343  13288  -1667  -1769  -1288       N  
ATOM   3861  CA  LEU B  46     -18.933  56.960  44.678  1.00125.58           C  
ANISOU 3861  CA  LEU B  46    19565  14506  13643  -1804  -2080  -1069       C  
ATOM   3862  C   LEU B  46     -19.199  58.339  44.088  1.00134.51           C  
ANISOU 3862  C   LEU B  46    20734  15352  15021  -1650  -2297  -1103       C  
ATOM   3863  O   LEU B  46     -18.285  59.154  43.938  1.00138.42           O  
ANISOU 3863  O   LEU B  46    21409  15621  15564  -1733  -2522  -1017       O  
ATOM   3864  CB  LEU B  46     -18.581  55.981  43.555  1.00125.97           C  
ANISOU 3864  CB  LEU B  46    19445  14721  13697  -1948  -2109   -790       C  
ATOM   3865  CG  LEU B  46     -17.384  56.375  42.682  1.00130.17           C  
ANISOU 3865  CG  LEU B  46    20071  15107  14280  -2095  -2346   -533       C  
ATOM   3866  CD1 LEU B  46     -16.093  56.401  43.497  1.00121.65           C  
ANISOU 3866  CD1 LEU B  46    19175  13968  13080  -2281  -2419   -511       C  
ATOM   3867  CD2 LEU B  46     -17.257  55.478  41.460  1.00134.20           C  
ANISOU 3867  CD2 LEU B  46    20435  15768  14787  -2171  -2339   -285       C  
ATOM   3868  N   SER B  47     -20.463  58.595  43.769  1.00136.39           N  
ANISOU 3868  N   SER B  47    20790  15583  15449  -1426  -2235  -1231       N  
ATOM   3869  CA  SER B  47     -20.873  59.870  43.195  1.00136.29           C  
ANISOU 3869  CA  SER B  47    20810  15290  15683  -1237  -2451  -1275       C  
ATOM   3870  C   SER B  47     -20.622  61.047  44.146  1.00135.09           C  
ANISOU 3870  C   SER B  47    20918  14876  15534  -1159  -2519  -1484       C  
ATOM   3871  O   SER B  47     -20.072  62.073  43.742  1.00128.44           O  
ANISOU 3871  O   SER B  47    20242  13748  14810  -1167  -2775  -1406       O  
ATOM   3872  CB  SER B  47     -22.352  59.809  42.808  1.00134.84           C  
ANISOU 3872  CB  SER B  47    20339  15160  15733   -989  -2377  -1414       C  
ATOM   3873  OG  SER B  47     -22.825  61.072  42.379  1.00144.13           O  
ANISOU 3873  OG  SER B  47    21561  16048  17155   -766  -2596  -1490       O  
ATOM   3874  N   ALA B  48     -21.017  60.890  45.407  1.00134.76           N  
ANISOU 3874  N   ALA B  48    20937  14913  15352  -1083  -2281  -1748       N  
ATOM   3875  CA  ALA B  48     -20.802  61.925  46.415  1.00129.65           C  
ANISOU 3875  CA  ALA B  48    20586  14022  14654   -991  -2340  -1988       C  
ATOM   3876  C   ALA B  48     -19.328  62.079  46.786  1.00128.23           C  
ANISOU 3876  C   ALA B  48    20686  13727  14308  -1231  -2558  -1886       C  
ATOM   3877  O   ALA B  48     -18.846  63.196  46.960  1.00134.15           O  
ANISOU 3877  O   ALA B  48    21652  14164  15155  -1212  -2800  -1959       O  
ATOM   3878  CB  ALA B  48     -21.627  61.637  47.657  1.00130.76           C  
ANISOU 3878  CB  ALA B  48    20763  14284  14636   -831  -1983  -2291       C  
ATOM   3879  N   ALA B  49     -18.622  60.958  46.921  1.00121.50           N  
ANISOU 3879  N   ALA B  49    19816  13106  13243  -1452  -2488  -1729       N  
ATOM   3880  CA  ALA B  49     -17.191  60.977  47.220  1.00114.80           C  
ANISOU 3880  CA  ALA B  49    19165  12161  12294  -1687  -2716  -1623       C  
ATOM   3881  C   ALA B  49     -16.421  61.706  46.127  1.00128.31           C  
ANISOU 3881  C   ALA B  49    20836  13635  14281  -1810  -2998  -1384       C  
ATOM   3882  O   ALA B  49     -15.409  62.353  46.390  1.00137.86           O  
ANISOU 3882  O   ALA B  49    22215  14603  15564  -1941  -3243  -1374       O  
ATOM   3883  CB  ALA B  49     -16.660  59.568  47.386  1.00 98.16           C  
ANISOU 3883  CB  ALA B  49    16990  10349   9957  -1876  -2590  -1473       C  
ATOM   3884  N   LEU B  50     -16.902  61.578  44.896  1.00126.84           N  
ANISOU 3884  N   LEU B  50    20437  13505  14250  -1769  -2961  -1188       N  
ATOM   3885  CA  LEU B  50     -16.322  62.297  43.775  1.00122.32           C  
ANISOU 3885  CA  LEU B  50    19872  12694  13911  -1851  -3169   -940       C  
ATOM   3886  C   LEU B  50     -16.511  63.794  43.975  1.00125.62           C  
ANISOU 3886  C   LEU B  50    20473  12728  14529  -1709  -3362  -1098       C  
ATOM   3887  O   LEU B  50     -15.579  64.571  43.794  1.00127.41           O  
ANISOU 3887  O   LEU B  50    20830  12664  14917  -1851  -3570   -989       O  
ATOM   3888  CB  LEU B  50     -16.957  61.845  42.461  1.00119.75           C  
ANISOU 3888  CB  LEU B  50    19353  12502  13646  -1780  -3101   -732       C  
ATOM   3889  CG  LEU B  50     -16.186  60.784  41.676  1.00116.63           C  
ANISOU 3889  CG  LEU B  50    18850  12308  13157  -1995  -3037   -427       C  
ATOM   3890  CD1 LEU B  50     -16.609  60.787  40.213  1.00119.86           C  
ANISOU 3890  CD1 LEU B  50    19197  12700  13646  -1912  -3074   -202       C  
ATOM   3891  CD2 LEU B  50     -14.680  60.985  41.817  1.00 94.58           C  
ANISOU 3891  CD2 LEU B  50    16157   9366  10411  -2257  -3144   -274       C  
ATOM   3892  N   ALA B  51     -17.722  64.182  44.370  1.00130.30           N  
ANISOU 3892  N   ALA B  51    21060  13307  15142  -1431  -3280  -1361       N  
ATOM   3893  CA  ALA B  51     -18.069  65.580  44.618  1.00123.47           C  
ANISOU 3893  CA  ALA B  51    20370  12078  14466  -1243  -3446  -1555       C  
ATOM   3894  C   ALA B  51     -17.225  66.191  45.742  1.00135.18           C  
ANISOU 3894  C   ALA B  51    22130  13338  15893  -1337  -3597  -1743       C  
ATOM   3895  O   ALA B  51     -16.834  67.358  45.670  1.00133.57           O  
ANISOU 3895  O   ALA B  51    22099  12753  15900  -1337  -3842  -1766       O  
ATOM   3896  CB  ALA B  51     -19.554  65.703  44.943  1.00116.61           C  
ANISOU 3896  CB  ALA B  51    19396  11279  13630   -912  -3274  -1832       C  
ATOM   3897  N   LEU B  52     -16.975  65.407  46.790  1.00138.48           N  
ANISOU 3897  N   LEU B  52    22614  13973  16028  -1405  -3471  -1887       N  
ATOM   3898  CA  LEU B  52     -16.100  65.826  47.884  1.00133.00           C  
ANISOU 3898  CA  LEU B  52    22210  13088  15234  -1500  -3665  -2070       C  
ATOM   3899  C   LEU B  52     -14.683  66.033  47.367  1.00127.85           C  
ANISOU 3899  C   LEU B  52    21551  12247  14781  -1807  -3945  -1809       C  
ATOM   3900  O   LEU B  52     -14.006  66.996  47.731  1.00136.66           O  
ANISOU 3900  O   LEU B  52    22859  13005  16061  -1873  -4233  -1905       O  
ATOM   3901  CB  LEU B  52     -16.101  64.788  49.007  1.00132.85           C  
ANISOU 3901  CB  LEU B  52    22290  13361  14827  -1509  -3476  -2225       C  
ATOM   3902  CG  LEU B  52     -17.458  64.407  49.600  1.00137.08           C  
ANISOU 3902  CG  LEU B  52    22813  14111  15160  -1237  -3103  -2463       C  
ATOM   3903  CD1 LEU B  52     -17.280  63.521  50.817  1.00128.51           C  
ANISOU 3903  CD1 LEU B  52    21938  13234  13657  -1263  -2936  -2605       C  
ATOM   3904  CD2 LEU B  52     -18.252  65.654  49.952  1.00145.04           C  
ANISOU 3904  CD2 LEU B  52    23975  14836  16298   -950  -3125  -2760       C  
ATOM   3905  N   TYR B  53     -14.246  65.101  46.526  1.00116.86           N  
ANISOU 3905  N   TYR B  53    19923  11086  13393  -1994  -3846  -1489       N  
ATOM   3906  CA  TYR B  53     -12.955  65.170  45.857  1.00114.40           C  
ANISOU 3906  CA  TYR B  53    19532  10630  13306  -2284  -4017  -1196       C  
ATOM   3907  C   TYR B  53     -12.933  66.384  44.940  1.00123.94           C  
ANISOU 3907  C   TYR B  53    20770  11465  14855  -2272  -4152  -1055       C  
ATOM   3908  O   TYR B  53     -11.949  67.120  44.883  1.00127.78           O  
ANISOU 3908  O   TYR B  53    21321  11621  15610  -2457  -4373   -976       O  
ATOM   3909  CB  TYR B  53     -12.706  63.891  45.064  1.00114.74           C  
ANISOU 3909  CB  TYR B  53    19327  11015  13254  -2424  -3814   -898       C  
ATOM   3910  CG  TYR B  53     -11.464  63.886  44.203  1.00113.05           C  
ANISOU 3910  CG  TYR B  53    18991  10676  13287  -2700  -3894   -565       C  
ATOM   3911  CD1 TYR B  53     -10.199  63.846  44.778  1.00105.72           C  
ANISOU 3911  CD1 TYR B  53    18064   9630  12476  -2930  -4084   -566       C  
ATOM   3912  CD2 TYR B  53     -11.555  63.896  42.817  1.00114.36           C  
ANISOU 3912  CD2 TYR B  53    19044  10835  13572  -2719  -3773   -253       C  
ATOM   3913  CE1 TYR B  53      -9.060  63.823  43.998  1.00114.85           C  
ANISOU 3913  CE1 TYR B  53    19056  10666  13915  -3185  -4107   -263       C  
ATOM   3914  CE2 TYR B  53     -10.420  63.876  42.027  1.00124.84           C  
ANISOU 3914  CE2 TYR B  53    20273  12044  15115  -2964  -3770     61       C  
ATOM   3915  CZ  TYR B  53      -9.176  63.840  42.622  1.00131.28           C  
ANISOU 3915  CZ  TYR B  53    21036  12747  16098  -3203  -3915     56       C  
ATOM   3916  OH  TYR B  53      -8.044  63.821  41.838  1.00145.65           O  
ANISOU 3916  OH  TYR B  53    22709  14439  18193  -3449  -3868    366       O  
ATOM   3917  N   ASP B  54     -14.036  66.579  44.221  1.00125.03           N  
ANISOU 3917  N   ASP B  54    20860  11643  15004  -2050  -4028  -1021       N  
ATOM   3918  CA  ASP B  54     -14.191  67.731  43.339  1.00127.30           C  
ANISOU 3918  CA  ASP B  54    21226  11569  15572  -1983  -4158   -888       C  
ATOM   3919  C   ASP B  54     -14.134  69.028  44.140  1.00121.38           C  
ANISOU 3919  C   ASP B  54    20716  10409  14993  -1904  -4398  -1160       C  
ATOM   3920  O   ASP B  54     -13.533  70.003  43.700  1.00119.52           O  
ANISOU 3920  O   ASP B  54    20583   9778  15052  -2014  -4585  -1025       O  
ATOM   3921  CB  ASP B  54     -15.506  67.653  42.552  1.00140.17           C  
ANISOU 3921  CB  ASP B  54    22771  13323  17163  -1707  -4035   -860       C  
ATOM   3922  CG  ASP B  54     -15.551  66.469  41.598  1.00135.98           C  
ANISOU 3922  CG  ASP B  54    22039  13136  16491  -1780  -3851   -580       C  
ATOM   3923  OD1 ASP B  54     -14.535  66.211  40.919  1.00138.18           O  
ANISOU 3923  OD1 ASP B  54    22296  13390  16816  -2024  -3840   -272       O  
ATOM   3924  OD2 ASP B  54     -16.608  65.805  41.513  1.00121.71           O  
ANISOU 3924  OD2 ASP B  54    20089  11606  14550  -1591  -3710   -675       O  
ATOM   3925  N   ALA B  55     -14.768  69.042  45.310  1.00129.60           N  
ANISOU 3925  N   ALA B  55    21868  11526  15849  -1709  -4376  -1542       N  
ATOM   3926  CA  ALA B  55     -14.722  70.214  46.178  1.00137.10           C  
ANISOU 3926  CA  ALA B  55    23089  12093  16912  -1610  -4609  -1849       C  
ATOM   3927  C   ALA B  55     -13.308  70.449  46.706  1.00150.59           C  
ANISOU 3927  C   ALA B  55    24906  13574  18739  -1908  -4877  -1843       C  
ATOM   3928  O   ALA B  55     -12.853  71.588  46.812  1.00157.19           O  
ANISOU 3928  O   ALA B  55    25908  13961  19856  -1957  -5150  -1909       O  
ATOM   3929  CB  ALA B  55     -15.699  70.058  47.335  1.00134.68           C  
ANISOU 3929  CB  ALA B  55    22902  11945  16324  -1325  -4464  -2260       C  
ATOM   3930  N   ALA B  56     -12.621  69.364  47.051  1.00156.92           N  
ANISOU 3930  N   ALA B  56    25602  14665  19354  -2101  -4821  -1775       N  
ATOM   3931  CA  ALA B  56     -11.271  69.457  47.598  1.00163.22           C  
ANISOU 3931  CA  ALA B  56    26455  15272  20288  -2376  -5108  -1787       C  
ATOM   3932  C   ALA B  56     -10.246  69.870  46.540  1.00162.79           C  
ANISOU 3932  C   ALA B  56    26227  14954  20674  -2669  -5210  -1419       C  
ATOM   3933  O   ALA B  56      -9.378  70.707  46.786  1.00159.79           O  
ANISOU 3933  O   ALA B  56    25923  14168  20623  -2840  -5512  -1461       O  
ATOM   3934  CB  ALA B  56     -10.869  68.131  48.226  1.00162.77           C  
ANISOU 3934  CB  ALA B  56    26330  15600  19915  -2472  -5025  -1807       C  
ATOM   3935  N   ILE B  57     -10.364  69.276  45.358  1.00166.23           N  
ANISOU 3935  N   ILE B  57    26439  15605  21117  -2724  -4945  -1063       N  
ATOM   3936  CA  ILE B  57      -9.425  69.522  44.266  1.00164.92           C  
ANISOU 3936  CA  ILE B  57    26118  15232  21312  -2993  -4935   -672       C  
ATOM   3937  C   ILE B  57      -9.494  70.960  43.745  1.00160.20           C  
ANISOU 3937  C   ILE B  57    25674  14130  21063  -2971  -5074   -605       C  
ATOM   3938  O   ILE B  57      -8.489  71.500  43.277  1.00159.04           O  
ANISOU 3938  O   ILE B  57    25470  13650  21309  -3235  -5157   -379       O  
ATOM   3939  CB  ILE B  57      -9.652  68.525  43.091  1.00151.97           C  
ANISOU 3939  CB  ILE B  57    24276  13947  19518  -3005  -4596   -322       C  
ATOM   3940  CG1 ILE B  57      -8.439  68.488  42.164  1.00149.68           C  
ANISOU 3940  CG1 ILE B  57    23818  13509  19543  -3318  -4524     71       C  
ATOM   3941  CG2 ILE B  57     -10.918  68.842  42.309  1.00149.18           C  
ANISOU 3941  CG2 ILE B  57    24010  13620  19053  -2725  -4464   -271       C  
ATOM   3942  CD1 ILE B  57      -7.171  68.095  42.867  1.00144.85           C  
ANISOU 3942  CD1 ILE B  57    23049  12879  19109  -3591  -4670     28       C  
ATOM   3943  N   THR B  58     -10.668  71.580  43.833  1.00158.02           N  
ANISOU 3943  N   THR B  58    25584  13778  20679  -2659  -5088   -799       N  
ATOM   3944  CA  THR B  58     -10.825  72.963  43.395  1.00153.07           C  
ANISOU 3944  CA  THR B  58    25140  12652  20367  -2598  -5243   -759       C  
ATOM   3945  C   THR B  58     -10.388  73.970  44.459  1.00167.08           C  
ANISOU 3945  C   THR B  58    27113  14005  22365  -2638  -5592  -1084       C  
ATOM   3946  O   THR B  58      -9.918  75.055  44.119  1.00167.77           O  
ANISOU 3946  O   THR B  58    27300  13600  22845  -2757  -5767   -981       O  
ATOM   3947  CB  THR B  58     -12.284  73.265  42.971  1.00150.06           C  
ANISOU 3947  CB  THR B  58    24863  12324  19830  -2219  -5147   -830       C  
ATOM   3948  OG1 THR B  58     -12.358  74.586  42.422  1.00159.77           O  
ANISOU 3948  OG1 THR B  58    26285  13044  21378  -2169  -5307   -736       O  
ATOM   3949  CG2 THR B  58     -13.234  73.162  44.149  1.00126.11           C  
ANISOU 3949  CG2 THR B  58    21917   9464  16533  -1925  -5165  -1294       C  
ATOM   3950  N   SER B  59     -10.540  73.617  45.735  1.00180.32           N  
ANISOU 3950  N   SER B  59    28877  15851  23785  -2536  -5696  -1473       N  
ATOM   3951  CA  SER B  59     -10.399  74.585  46.822  1.00176.31           C  
ANISOU 3951  CA  SER B  59    28643  14958  23389  -2474  -6042  -1863       C  
ATOM   3952  C   SER B  59      -8.961  75.082  46.892  1.00215.41           C  
ANISOU 3952  C   SER B  59    33547  19511  28789  -2845  -6349  -1766       C  
ATOM   3953  O   SER B  59      -8.721  76.281  47.042  1.00219.35           O  
ANISOU 3953  O   SER B  59    34220  19491  29631  -2877  -6629  -1876       O  
ATOM   3954  CB  SER B  59     -10.813  73.983  48.165  1.00172.16           C  
ANISOU 3954  CB  SER B  59    28272  14721  22421  -2284  -6055  -2278       C  
ATOM   3955  OG  SER B  59      -9.719  73.340  48.792  1.00133.27           O  
ANISOU 3955  OG  SER B  59    23288   9882  17467  -2538  -6226  -2304       O  
ATOM   3956  N   SER B  60      -8.027  74.133  46.829  1.00258.10           N  
ANISOU 3956  N   SER B  60    38701  25153  34212  -3117  -6303  -1581       N  
ATOM   3957  CA  SER B  60      -6.585  74.370  46.959  1.00278.72           C  
ANISOU 3957  CA  SER B  60    41169  27450  37282  -3489  -6581  -1496       C  
ATOM   3958  C   SER B  60      -6.155  74.715  48.382  1.00282.57           C  
ANISOU 3958  C   SER B  60    41874  27719  37770  -3485  -7045  -1949       C  
ATOM   3959  O   SER B  60      -4.979  74.605  48.714  1.00301.33           O  
ANISOU 3959  O   SER B  60    44100  29939  40454  -3767  -7321  -1947       O  
ATOM   3960  CB  SER B  60      -6.115  75.465  45.997  1.00296.27           C  
ANISOU 3960  CB  SER B  60    43341  29161  40067  -3687  -6608  -1202       C  
ATOM   3961  OG  SER B  60      -4.711  75.641  46.069  1.00310.88           O  
ANISOU 3961  OG  SER B  60    44978  30708  42434  -4071  -6831  -1100       O  
ATOM   3962  N   GLU B  61      -7.089  75.157  49.214  1.00252.05           N  
ANISOU 3962  N   GLU B  61    38368  23817  33582  -3156  -7143  -2345       N  
ATOM   3963  CA  GLU B  61      -6.748  75.490  50.589  1.00224.95           C  
ANISOU 3963  CA  GLU B  61    35227  20178  30065  -3104  -7581  -2799       C  
ATOM   3964  C   GLU B  61      -6.349  74.239  51.359  1.00213.13           C  
ANISOU 3964  C   GLU B  61    33680  19112  28189  -3128  -7596  -2888       C  
ATOM   3965  O   GLU B  61      -5.468  74.288  52.216  1.00211.56           O  
ANISOU 3965  O   GLU B  61    33435  18894  28053  -3174  -7875  -3019       O  
ATOM   3966  CB  GLU B  61      -7.911  76.179  51.287  1.00212.57           C  
ANISOU 3966  CB  GLU B  61    34085  18503  28179  -2707  -7603  -3204       C  
ATOM   3967  CG  GLU B  61      -8.238  77.549  50.729  1.00207.47           C  
ANISOU 3967  CG  GLU B  61    33521  17386  27922  -2639  -7664  -3171       C  
ATOM   3968  CD  GLU B  61      -9.271  78.267  51.564  1.00203.61           C  
ANISOU 3968  CD  GLU B  61    33431  16780  27150  -2228  -7710  -3613       C  
ATOM   3969  OE1 GLU B  61      -9.824  77.634  52.486  1.00198.61           O  
ANISOU 3969  OE1 GLU B  61    33018  16454  25991  -1995  -7621  -3921       O  
ATOM   3970  OE2 GLU B  61      -9.525  79.461  51.304  1.00207.85           O  
ANISOU 3970  OE2 GLU B  61    34069  16916  27989  -2132  -7807  -3646       O  
ATOM   3971  N   VAL B  62      -7.009  73.123  51.056  1.00201.14           N  
ANISOU 3971  N   VAL B  62    32060  18110  26254  -3017  -7184  -2745       N  
ATOM   3972  CA  VAL B  62      -6.714  71.846  51.702  1.00192.49           C  
ANISOU 3972  CA  VAL B  62    30939  17424  24774  -3037  -7160  -2793       C  
ATOM   3973  C   VAL B  62      -5.636  71.048  50.954  1.00188.37           C  
ANISOU 3973  C   VAL B  62    29972  17042  24557  -3379  -7112  -2403       C  
ATOM   3974  O   VAL B  62      -5.622  71.014  49.723  1.00184.18           O  
ANISOU 3974  O   VAL B  62    29140  16556  24284  -3504  -6817  -2022       O  
ATOM   3975  CB  VAL B  62      -8.003  71.001  51.830  1.00172.27           C  
ANISOU 3975  CB  VAL B  62    28474  15365  21617  -2730  -6699  -2843       C  
ATOM   3976  CG1 VAL B  62      -8.710  70.883  50.485  1.00166.49           C  
ANISOU 3976  CG1 VAL B  62    27454  14814  20990  -2700  -6267  -2492       C  
ATOM   3977  CG2 VAL B  62      -7.701  69.628  52.387  1.00163.73           C  
ANISOU 3977  CG2 VAL B  62    27362  14697  20150  -2767  -6632  -2834       C  
ATOM   3978  N   ARG B  63      -4.750  70.393  51.706  1.00183.96           N  
ANISOU 3978  N   ARG B  63    29397  16548  23950  -3507  -7401  -2506       N  
ATOM   3979  CA  ARG B  63      -3.856  69.382  51.142  1.00176.89           C  
ANISOU 3979  CA  ARG B  63    28086  15882  23242  -3766  -7303  -2177       C  
ATOM   3980  C   ARG B  63      -4.415  67.995  51.374  1.00176.75           C  
ANISOU 3980  C   ARG B  63    28097  16424  22638  -3609  -6990  -2147       C  
ATOM   3981  O   ARG B  63      -4.856  67.673  52.481  1.00184.12           O  
ANISOU 3981  O   ARG B  63    29390  17489  23076  -3396  -7092  -2459       O  
ATOM   3982  CB  ARG B  63      -2.448  69.455  51.739  1.00177.40           C  
ANISOU 3982  CB  ARG B  63    27928  15801  23676  -3919  -7685  -2209       C  
ATOM   3983  CG  ARG B  63      -1.474  70.345  50.986  1.00183.78           C  
ANISOU 3983  CG  ARG B  63    28356  16231  25243  -4188  -7767  -1979       C  
ATOM   3984  CD  ARG B  63      -0.072  70.295  51.591  1.00196.89           C  
ANISOU 3984  CD  ARG B  63    29718  17809  27281  -4309  -8107  -2013       C  
ATOM   3985  NE  ARG B  63       0.059  71.134  52.780  1.00209.79           N  
ANISOU 3985  NE  ARG B  63    31622  19220  28868  -4126  -8518  -2375       N  
ATOM   3986  CZ  ARG B  63       1.110  71.908  53.040  1.00214.03           C  
ANISOU 3986  CZ  ARG B  63    31936  19435  29950  -4247  -8844  -2415       C  
ATOM   3987  NH1 ARG B  63       2.131  71.959  52.195  1.00213.88           N  
ANISOU 3987  NH1 ARG B  63    31396  19281  30586  -4553  -8768  -2114       N  
ATOM   3988  NH2 ARG B  63       1.140  72.638  54.146  1.00217.19           N  
ANISOU 3988  NH2 ARG B  63    32638  19640  30245  -4060  -9229  -2757       N  
ATOM   3989  N   LEU B  64      -4.380  67.170  50.331  1.00166.67           N  
ANISOU 3989  N   LEU B  64    26465  15454  21410  -3715  -6601  -1769       N  
ATOM   3990  CA  LEU B  64      -5.006  65.862  50.397  1.00147.59           C  
ANISOU 3990  CA  LEU B  64    24048  13553  18477  -3574  -6262  -1710       C  
ATOM   3991  C   LEU B  64      -3.951  64.818  50.760  1.00139.76           C  
ANISOU 3991  C   LEU B  64    22889  12710  17503  -3743  -6440  -1645       C  
ATOM   3992  O   LEU B  64      -2.969  64.625  50.043  1.00131.30           O  
ANISOU 3992  O   LEU B  64    21438  11573  16878  -3998  -6457  -1377       O  
ATOM   3993  CB  LEU B  64      -5.663  65.520  49.056  1.00134.71           C  
ANISOU 3993  CB  LEU B  64    22167  12169  16850  -3557  -5763  -1366       C  
ATOM   3994  CG  LEU B  64      -6.895  66.317  48.609  1.00127.84           C  
ANISOU 3994  CG  LEU B  64    21440  11233  15900  -3337  -5546  -1406       C  
ATOM   3995  CD1 LEU B  64      -7.421  65.813  47.272  1.00112.55           C  
ANISOU 3995  CD1 LEU B  64    19260   9551  13953  -3327  -5126  -1057       C  
ATOM   3996  CD2 LEU B  64      -7.987  66.276  49.663  1.00138.36           C  
ANISOU 3996  CD2 LEU B  64    23122  12704  16746  -3027  -5503  -1769       C  
ATOM   3997  N   SER B  65      -4.174  64.146  51.885  1.00139.10           N  
ANISOU 3997  N   SER B  65    23106  12817  16929  -3585  -6556  -1890       N  
ATOM   3998  CA  SER B  65      -3.244  63.153  52.410  1.00137.34           C  
ANISOU 3998  CA  SER B  65    22809  12716  16657  -3692  -6791  -1877       C  
ATOM   3999  C   SER B  65      -3.423  61.826  51.694  1.00128.64           C  
ANISOU 3999  C   SER B  65    21436  12058  15385  -3719  -6357  -1570       C  
ATOM   4000  O   SER B  65      -4.426  61.610  51.013  1.00111.80           O  
ANISOU 4000  O   SER B  65    19259  10166  13055  -3610  -5897  -1435       O  
ATOM   4001  CB  SER B  65      -3.432  62.970  53.917  1.00138.53           C  
ANISOU 4001  CB  SER B  65    23467  12876  16294  -3482  -7082  -2246       C  
ATOM   4002  OG  SER B  65      -2.415  62.151  54.470  1.00133.93           O  
ANISOU 4002  OG  SER B  65    22750  12401  15737  -3509  -7300  -2191       O  
ATOM   4003  N   GLN B  66      -2.434  60.948  51.824  1.00126.16           N  
ANISOU 4003  N   GLN B  66    20925  11826  15182  -3859  -6533  -1469       N  
ATOM   4004  CA  GLN B  66      -2.495  59.633  51.201  1.00124.65           C  
ANISOU 4004  CA  GLN B  66    20490  12029  14843  -3886  -6164  -1196       C  
ATOM   4005  C   GLN B  66      -3.750  58.904  51.677  1.00132.37           C  
ANISOU 4005  C   GLN B  66    21789  13354  15151  -3638  -5842  -1293       C  
ATOM   4006  O   GLN B  66      -4.317  58.099  50.946  1.00132.39           O  
ANISOU 4006  O   GLN B  66    21624  13670  15006  -3613  -5414  -1081       O  
ATOM   4007  CB  GLN B  66      -1.239  58.814  51.523  1.00128.04           C  
ANISOU 4007  CB  GLN B  66    20724  12460  15466  -4030  -6478  -1142       C  
ATOM   4008  CG  GLN B  66      -0.943  58.632  53.010  1.00147.34           C  
ANISOU 4008  CG  GLN B  66    23572  14814  17595  -3918  -6971  -1461       C  
ATOM   4009  CD  GLN B  66      -0.141  59.785  53.609  1.00177.06           C  
ANISOU 4009  CD  GLN B  66    27314  18193  21769  -3904  -7403  -1638       C  
ATOM   4010  OE1 GLN B  66      -0.275  60.938  53.194  1.00191.79           O  
ANISOU 4010  OE1 GLN B  66    29134  19791  23948  -3978  -7420  -1671       O  
ATOM   4011  NE2 GLN B  66       0.701  59.472  54.589  1.00183.35           N  
ANISOU 4011  NE2 GLN B  66    28145  18948  22570  -3798  -7757  -1747       N  
ATOM   4012  N   GLN B  67      -4.188  59.216  52.896  1.00139.35           N  
ANISOU 4012  N   GLN B  67    23143  14156  15647  -3454  -6040  -1620       N  
ATOM   4013  CA  GLN B  67      -5.414  58.656  53.457  1.00145.99           C  
ANISOU 4013  CA  GLN B  67    24317  15277  15877  -3215  -5697  -1737       C  
ATOM   4014  C   GLN B  67      -6.611  58.953  52.555  1.00142.95           C  
ANISOU 4014  C   GLN B  67    23788  15029  15499  -3124  -5211  -1634       C  
ATOM   4015  O   GLN B  67      -7.472  58.098  52.338  1.00137.03           O  
ANISOU 4015  O   GLN B  67    23005  14603  14459  -3031  -4798  -1542       O  
ATOM   4016  CB  GLN B  67      -5.666  59.233  54.853  1.00159.55           C  
ANISOU 4016  CB  GLN B  67    26597  16804  17221  -3021  -5974  -2123       C  
ATOM   4017  CG  GLN B  67      -4.803  58.640  55.957  1.00165.47           C  
ANISOU 4017  CG  GLN B  67    27597  17520  17755  -2997  -6368  -2234       C  
ATOM   4018  CD  GLN B  67      -4.900  57.135  56.032  1.00165.74           C  
ANISOU 4018  CD  GLN B  67    27625  17907  17441  -2989  -6126  -2062       C  
ATOM   4019  OE1 GLN B  67      -5.967  56.558  55.826  1.00164.96           O  
ANISOU 4019  OE1 GLN B  67    27580  18086  17010  -2897  -5633  -1995       O  
ATOM   4020  NE2 GLN B  67      -3.780  56.487  56.326  1.00172.04           N  
ANISOU 4020  NE2 GLN B  67    28267  18705  18395  -3042  -6403  -1954       N  
ATOM   4021  N   HIS B  68      -6.643  60.176  52.032  1.00142.17           N  
ANISOU 4021  N   HIS B  68    23602  14654  15761  -3154  -5294  -1653       N  
ATOM   4022  CA  HIS B  68      -7.714  60.646  51.156  1.00133.08           C  
ANISOU 4022  CA  HIS B  68    22332  13557  14673  -3052  -4930  -1571       C  
ATOM   4023  C   HIS B  68      -7.833  59.827  49.883  1.00127.80           C  
ANISOU 4023  C   HIS B  68    21278  13159  14120  -3149  -4589  -1220       C  
ATOM   4024  O   HIS B  68      -8.911  59.348  49.537  1.00128.74           O  
ANISOU 4024  O   HIS B  68    21361  13534  14021  -3012  -4225  -1178       O  
ATOM   4025  CB  HIS B  68      -7.506  62.114  50.782  1.00136.27           C  
ANISOU 4025  CB  HIS B  68    22723  13560  15495  -3094  -5147  -1618       C  
ATOM   4026  CG  HIS B  68      -7.422  63.038  51.956  1.00140.00           C  
ANISOU 4026  CG  HIS B  68    23589  13720  15885  -2988  -5508  -1987       C  
ATOM   4027  ND1 HIS B  68      -6.498  62.885  52.967  1.00144.82           N  
ANISOU 4027  ND1 HIS B  68    24400  14201  16426  -3054  -5927  -2159       N  
ATOM   4028  CD2 HIS B  68      -8.145  64.137  52.272  1.00142.57           C  
ANISOU 4028  CD2 HIS B  68    24167  13817  16187  -2803  -5537  -2230       C  
ATOM   4029  CE1 HIS B  68      -6.655  63.852  53.853  1.00153.13           C  
ANISOU 4029  CE1 HIS B  68    25835  14956  17391  -2917  -6205  -2499       C  
ATOM   4030  NE2 HIS B  68      -7.651  64.623  53.457  1.00154.10           N  
ANISOU 4030  NE2 HIS B  68    25994  15017  17542  -2763  -5956  -2550       N  
ATOM   4031  N   PHE B  69      -6.714  59.697  49.177  1.00129.51           N  
ANISOU 4031  N   PHE B  69    21204  13295  14710  -3382  -4713   -978       N  
ATOM   4032  CA  PHE B  69      -6.696  59.035  47.880  1.00123.67           C  
ANISOU 4032  CA  PHE B  69    20131  12758  14100  -3475  -4406   -641       C  
ATOM   4033  C   PHE B  69      -6.902  57.528  47.972  1.00124.84           C  
ANISOU 4033  C   PHE B  69    20222  13292  13919  -3447  -4186   -560       C  
ATOM   4034  O   PHE B  69      -7.443  56.916  47.051  1.00125.67           O  
ANISOU 4034  O   PHE B  69    20157  13624  13968  -3424  -3867   -368       O  
ATOM   4035  CB  PHE B  69      -5.368  59.309  47.179  1.00121.30           C  
ANISOU 4035  CB  PHE B  69    19548  12242  14298  -3728  -4557   -415       C  
ATOM   4036  CG  PHE B  69      -5.121  60.760  46.880  1.00128.48           C  
ANISOU 4036  CG  PHE B  69    20470  12746  15602  -3795  -4725   -428       C  
ATOM   4037  CD1 PHE B  69      -5.675  61.358  45.762  1.00134.94           C  
ANISOU 4037  CD1 PHE B  69    21228  13494  16550  -3762  -4487   -244       C  
ATOM   4038  CD2 PHE B  69      -4.309  61.518  47.705  1.00136.48           C  
ANISOU 4038  CD2 PHE B  69    21571  13420  16867  -3892  -5150   -619       C  
ATOM   4039  CE1 PHE B  69      -5.438  62.693  45.479  1.00145.28           C  
ANISOU 4039  CE1 PHE B  69    22574  14399  18226  -3827  -4636   -235       C  
ATOM   4040  CE2 PHE B  69      -4.066  62.850  47.427  1.00138.54           C  
ANISOU 4040  CE2 PHE B  69    21838  13272  17526  -3970  -5309   -627       C  
ATOM   4041  CZ  PHE B  69      -4.632  63.439  46.313  1.00144.69           C  
ANISOU 4041  CZ  PHE B  69    22566  13983  18427  -3941  -5034   -424       C  
ATOM   4042  N   GLN B  70      -6.478  56.934  49.084  1.00125.12           N  
ANISOU 4042  N   GLN B  70    20430  13379  13730  -3443  -4379   -709       N  
ATOM   4043  CA  GLN B  70      -6.711  55.513  49.323  1.00113.08           C  
ANISOU 4043  CA  GLN B  70    18913  12187  11864  -3405  -4184   -649       C  
ATOM   4044  C   GLN B  70      -8.194  55.204  49.458  1.00 93.47           C  
ANISOU 4044  C   GLN B  70    16573   9928   9013  -3208  -3820   -739       C  
ATOM   4045  O   GLN B  70      -8.706  54.305  48.801  1.00 90.69           O  
ANISOU 4045  O   GLN B  70    16048   9833   8576  -3200  -3514   -577       O  
ATOM   4046  CB  GLN B  70      -5.962  55.043  50.568  1.00123.50           C  
ANISOU 4046  CB  GLN B  70    20464  13466  12994  -3417  -4510   -800       C  
ATOM   4047  CG  GLN B  70      -4.452  55.091  50.434  1.00118.73           C  
ANISOU 4047  CG  GLN B  70    19635  12671  12807  -3618  -4878   -703       C  
ATOM   4048  CD  GLN B  70      -3.755  55.095  51.779  1.00124.50           C  
ANISOU 4048  CD  GLN B  70    20662  13239  13404  -3594  -5351   -936       C  
ATOM   4049  OE1 GLN B  70      -4.383  54.888  52.818  1.00125.71           O  
ANISOU 4049  OE1 GLN B  70    21238  13459  13068  -3420  -5359  -1143       O  
ATOM   4050  NE2 GLN B  70      -2.452  55.341  51.767  1.00133.28           N  
ANISOU 4050  NE2 GLN B  70    21563  14118  14958  -3762  -5750   -908       N  
ATOM   4051  N   THR B  71      -8.875  55.958  50.315  1.00 95.89           N  
ANISOU 4051  N   THR B  71    17186  10117   9131  -3044  -3854  -1010       N  
ATOM   4052  CA  THR B  71     -10.302  55.767  50.555  1.00 99.05           C  
ANISOU 4052  CA  THR B  71    17703  10695   9237  -2845  -3489  -1130       C  
ATOM   4053  C   THR B  71     -11.083  55.863  49.251  1.00 93.23           C  
ANISOU 4053  C   THR B  71    16651  10055   8716  -2821  -3221   -964       C  
ATOM   4054  O   THR B  71     -12.019  55.100  49.018  1.00104.83           O  
ANISOU 4054  O   THR B  71    18024  11768  10039  -2743  -2896   -926       O  
ATOM   4055  CB  THR B  71     -10.848  56.807  51.556  1.00108.15           C  
ANISOU 4055  CB  THR B  71    19215  11646  10232  -2659  -3565  -1457       C  
ATOM   4056  OG1 THR B  71     -10.204  56.636  52.823  1.00108.16           O  
ANISOU 4056  OG1 THR B  71    19585  11562   9949  -2648  -3825  -1630       O  
ATOM   4057  CG2 THR B  71     -12.350  56.653  51.733  1.00115.22           C  
ANISOU 4057  CG2 THR B  71    20161  12712  10905  -2448  -3133  -1577       C  
ATOM   4058  N   LEU B  72     -10.679  56.801  48.402  1.00105.42           N  
ANISOU 4058  N   LEU B  72    18051  11384  10619  -2891  -3377   -863       N  
ATOM   4059  CA  LEU B  72     -11.316  57.010  47.109  1.00113.04           C  
ANISOU 4059  CA  LEU B  72    18781  12389  11780  -2855  -3194   -695       C  
ATOM   4060  C   LEU B  72     -11.019  55.885  46.126  1.00123.91           C  
ANISOU 4060  C   LEU B  72    19900  13996  13184  -2976  -3040   -410       C  
ATOM   4061  O   LEU B  72     -11.932  55.349  45.499  1.00133.43           O  
ANISOU 4061  O   LEU B  72    20980  15396  14323  -2890  -2803   -347       O  
ATOM   4062  CB  LEU B  72     -10.880  58.350  46.522  1.00110.58           C  
ANISOU 4062  CB  LEU B  72    18456  11742  11818  -2900  -3404   -646       C  
ATOM   4063  CG  LEU B  72     -12.033  59.267  46.126  1.00111.00           C  
ANISOU 4063  CG  LEU B  72    18541  11688  11947  -2698  -3317   -741       C  
ATOM   4064  CD1 LEU B  72     -13.027  59.392  47.259  1.00101.95           C  
ANISOU 4064  CD1 LEU B  72    17596  10589  10549  -2483  -3218  -1067       C  
ATOM   4065  CD2 LEU B  72     -11.476  60.624  45.771  1.00127.80           C  
ANISOU 4065  CD2 LEU B  72    20726  13431  14403  -2754  -3562   -710       C  
ATOM   4066  N   LEU B  73      -9.743  55.530  45.999  1.00120.79           N  
ANISOU 4066  N   LEU B  73    19419  13563  12912  -3168  -3190   -255       N  
ATOM   4067  CA  LEU B  73      -9.334  54.462  45.092  1.00111.58           C  
ANISOU 4067  CA  LEU B  73    18027  12594  11776  -3276  -3043      6       C  
ATOM   4068  C   LEU B  73      -9.960  53.125  45.486  1.00110.19           C  
ANISOU 4068  C   LEU B  73    17860  12727  11281  -3216  -2838    -28       C  
ATOM   4069  O   LEU B  73     -10.357  52.337  44.627  1.00 99.25           O  
ANISOU 4069  O   LEU B  73    16316  11530   9865  -3209  -2636    121       O  
ATOM   4070  CB  LEU B  73      -7.810  54.327  45.066  1.00 96.41           C  
ANISOU 4070  CB  LEU B  73    15996  10557  10080  -3478  -3237    142       C  
ATOM   4071  CG  LEU B  73      -7.048  55.232  44.101  1.00 97.94           C  
ANISOU 4071  CG  LEU B  73    16045  10497  10670  -3603  -3299    329       C  
ATOM   4072  CD1 LEU B  73      -5.594  54.801  44.005  1.00101.00           C  
ANISOU 4072  CD1 LEU B  73    16236  10826  11314  -3803  -3407    481       C  
ATOM   4073  CD2 LEU B  73      -7.703  55.218  42.732  1.00108.03           C  
ANISOU 4073  CD2 LEU B  73    17237  11853  11955  -3540  -3039    528       C  
ATOM   4074  N   TYR B  74     -10.058  52.881  46.788  1.00120.34           N  
ANISOU 4074  N   TYR B  74    19362  14042  12320  -3167  -2892   -227       N  
ATOM   4075  CA  TYR B  74     -10.671  51.661  47.284  1.00115.64           C  
ANISOU 4075  CA  TYR B  74    18819  13702  11417  -3116  -2670   -258       C  
ATOM   4076  C   TYR B  74     -12.139  51.659  46.875  1.00123.01           C  
ANISOU 4076  C   TYR B  74    19674  14757  12309  -2971  -2379   -314       C  
ATOM   4077  O   TYR B  74     -12.685  50.625  46.482  1.00138.90           O  
ANISOU 4077  O   TYR B  74    21549  16980  14244  -2971  -2158   -227       O  
ATOM   4078  CB  TYR B  74     -10.529  51.542  48.808  1.00109.51           C  
ANISOU 4078  CB  TYR B  74    18375  12891  10343  -3068  -2773   -462       C  
ATOM   4079  CG  TYR B  74      -9.100  51.466  49.318  1.00114.83           C  
ANISOU 4079  CG  TYR B  74    19131  13434  11066  -3192  -3131   -437       C  
ATOM   4080  CD1 TYR B  74      -8.031  51.283  48.447  1.00112.50           C  
ANISOU 4080  CD1 TYR B  74    18558  13102  11086  -3352  -3266   -222       C  
ATOM   4081  CD2 TYR B  74      -8.821  51.597  50.674  1.00125.03           C  
ANISOU 4081  CD2 TYR B  74    20783  14621  12102  -3134  -3342   -640       C  
ATOM   4082  CE1 TYR B  74      -6.726  51.226  48.913  1.00116.79           C  
ANISOU 4082  CE1 TYR B  74    19113  13507  11756  -3462  -3609   -214       C  
ATOM   4083  CE2 TYR B  74      -7.518  51.538  51.150  1.00123.32           C  
ANISOU 4083  CE2 TYR B  74    20628  14261  11968  -3234  -3741   -638       C  
ATOM   4084  CZ  TYR B  74      -6.477  51.353  50.264  1.00119.99           C  
ANISOU 4084  CZ  TYR B  74    19857  13804  11930  -3403  -3877   -427       C  
ATOM   4085  OH  TYR B  74      -5.184  51.295  50.732  1.00115.30           O  
ANISOU 4085  OH  TYR B  74    19262  13052  11494  -3500  -4285   -438       O  
ATOM   4086  N   LEU B  75     -12.762  52.832  46.940  1.00105.09           N  
ANISOU 4086  N   LEU B  75    17468  12329  10132  -2847  -2404   -466       N  
ATOM   4087  CA  LEU B  75     -14.154  52.984  46.541  1.00 96.99           C  
ANISOU 4087  CA  LEU B  75    16330  11377   9146  -2688  -2175   -543       C  
ATOM   4088  C   LEU B  75     -14.318  52.757  45.044  1.00114.37           C  
ANISOU 4088  C   LEU B  75    18266  13640  11549  -2715  -2149   -329       C  
ATOM   4089  O   LEU B  75     -15.355  52.279  44.587  1.00123.47           O  
ANISOU 4089  O   LEU B  75    19262  14933  12717  -2627  -1968   -338       O  
ATOM   4090  CB  LEU B  75     -14.674  54.369  46.927  1.00 89.50           C  
ANISOU 4090  CB  LEU B  75    15515  10206   8284  -2532  -2248   -759       C  
ATOM   4091  CG  LEU B  75     -16.195  54.519  46.953  1.00 96.72           C  
ANISOU 4091  CG  LEU B  75    16340  11186   9223  -2326  -1993   -922       C  
ATOM   4092  CD1 LEU B  75     -16.817  53.390  47.758  1.00105.08           C  
ANISOU 4092  CD1 LEU B  75    17419  12471  10035  -2306  -1676  -1000       C  
ATOM   4093  CD2 LEU B  75     -16.597  55.868  47.525  1.00 92.11           C  
ANISOU 4093  CD2 LEU B  75    15932  10365   8700  -2156  -2067  -1165       C  
ATOM   4094  N   CYS B  76     -13.286  53.111  44.286  1.00114.59           N  
ANISOU 4094  N   CYS B  76    18256  13545  11739  -2835  -2333   -141       N  
ATOM   4095  CA  CYS B  76     -13.292  52.939  42.838  1.00106.62           C  
ANISOU 4095  CA  CYS B  76    17079  12566  10867  -2854  -2309     81       C  
ATOM   4096  C   CYS B  76     -13.333  51.462  42.428  1.00 98.70           C  
ANISOU 4096  C   CYS B  76    15942  11820   9740  -2915  -2153    206       C  
ATOM   4097  O   CYS B  76     -14.059  51.084  41.506  1.00 85.86           O  
ANISOU 4097  O   CYS B  76    14197  10287   8138  -2843  -2072    269       O  
ATOM   4098  CB  CYS B  76     -12.071  53.630  42.232  1.00107.00           C  
ANISOU 4098  CB  CYS B  76    17142  12404  11110  -2984  -2475    266       C  
ATOM   4099  SG  CYS B  76     -12.201  55.439  42.198  1.00 90.97           S  
ANISOU 4099  SG  CYS B  76    15243  10021   9300  -2903  -2656    180       S  
ATOM   4100  N   SER B  77     -12.545  50.637  43.111  1.00100.82           N  
ANISOU 4100  N   SER B  77    16245  12179   9882  -3037  -2148    232       N  
ATOM   4101  CA  SER B  77     -12.542  49.196  42.871  1.00 83.45           C  
ANISOU 4101  CA  SER B  77    13945  10201   7560  -3094  -2008    334       C  
ATOM   4102  C   SER B  77     -13.824  48.576  43.379  1.00 84.55           C  
ANISOU 4102  C   SER B  77    14062  10494   7567  -2998  -1809    184       C  
ATOM   4103  O   SER B  77     -14.336  47.631  42.790  1.00107.10           O  
ANISOU 4103  O   SER B  77    16782  13500  10411  -2997  -1686    248       O  
ATOM   4104  CB  SER B  77     -11.342  48.529  43.531  1.00 84.78           C  
ANISOU 4104  CB  SER B  77    14171  10393   7650  -3231  -2087    396       C  
ATOM   4105  OG  SER B  77     -10.144  49.129  43.086  1.00 92.19           O  
ANISOU 4105  OG  SER B  77    15071  11168   8788  -3330  -2254    526       O  
ATOM   4106  N   ALA B  78     -14.321  49.100  44.493  1.00 78.02           N  
ANISOU 4106  N   ALA B  78    13375   9615   6655  -2921  -1767    -21       N  
ATOM   4107  CA  ALA B  78     -15.609  48.687  45.031  1.00112.76           C  
ANISOU 4107  CA  ALA B  78    17739  14125  10978  -2820  -1516   -176       C  
ATOM   4108  C   ALA B  78     -16.724  48.917  44.010  1.00111.94           C  
ANISOU 4108  C   ALA B  78    17402  14038  11093  -2706  -1465   -194       C  
ATOM   4109  O   ALA B  78     -17.726  48.194  43.982  1.00 99.82           O  
ANISOU 4109  O   ALA B  78    15707  12627   9592  -2667  -1267   -251       O  
ATOM   4110  CB  ALA B  78     -15.905  49.442  46.319  1.00110.76           C  
ANISOU 4110  CB  ALA B  78    17712  13772  10600  -2725  -1466   -401       C  
ATOM   4111  N   SER B  79     -16.534  49.939  43.182  1.00117.36           N  
ANISOU 4111  N   SER B  79    18074  14574  11945  -2653  -1661   -145       N  
ATOM   4112  CA  SER B  79     -17.486  50.311  42.142  1.00115.23           C  
ANISOU 4112  CA  SER B  79    17635  14272  11875  -2518  -1703   -154       C  
ATOM   4113  C   SER B  79     -17.521  49.359  40.945  1.00109.54           C  
ANISOU 4113  C   SER B  79    16772  13670  11178  -2560  -1727     16       C  
ATOM   4114  O   SER B  79     -18.551  49.240  40.288  1.00118.34           O  
ANISOU 4114  O   SER B  79    17723  14810  12430  -2446  -1739    -36       O  
ATOM   4115  CB  SER B  79     -17.182  51.723  41.651  1.00124.72           C  
ANISOU 4115  CB  SER B  79    18938  15239  13210  -2445  -1917   -129       C  
ATOM   4116  OG  SER B  79     -16.809  52.558  42.731  1.00127.55           O  
ANISOU 4116  OG  SER B  79    19476  15462  13527  -2442  -1949   -265       O  
ATOM   4117  N   ILE B  80     -16.395  48.710  40.650  1.00 94.62           N  
ANISOU 4117  N   ILE B  80    14946  11833   9173  -2710  -1755    205       N  
ATOM   4118  CA  ILE B  80     -16.278  47.866  39.458  1.00 87.17           C  
ANISOU 4118  CA  ILE B  80    13925  10975   8219  -2738  -1783    368       C  
ATOM   4119  C   ILE B  80     -17.331  46.761  39.380  1.00105.04           C  
ANISOU 4119  C   ILE B  80    16012  13396  10504  -2709  -1671    283       C  
ATOM   4120  O   ILE B  80     -17.979  46.592  38.345  1.00117.93           O  
ANISOU 4120  O   ILE B  80    17550  15030  12227  -2619  -1767    297       O  
ATOM   4121  CB  ILE B  80     -14.885  47.207  39.372  1.00 82.87           C  
ANISOU 4121  CB  ILE B  80    13456  10474   7558  -2900  -1773    555       C  
ATOM   4122  CG1 ILE B  80     -13.798  48.271  39.264  1.00 82.00           C  
ANISOU 4122  CG1 ILE B  80    13465  10181   7510  -2950  -1888    660       C  
ATOM   4123  CG2 ILE B  80     -14.798  46.278  38.173  1.00 92.30           C  
ANISOU 4123  CG2 ILE B  80    14601  11755   8713  -2907  -1770    701       C  
ATOM   4124  CD1 ILE B  80     -12.425  47.697  38.974  1.00 79.93           C  
ANISOU 4124  CD1 ILE B  80    13214   9937   7221  -3094  -1874    854       C  
ATOM   4125  N   THR B  81     -17.509  46.023  40.474  1.00110.12           N  
ANISOU 4125  N   THR B  81    16625  14145  11069  -2783  -1481    196       N  
ATOM   4126  CA  THR B  81     -18.462  44.915  40.502  1.00112.85           C  
ANISOU 4126  CA  THR B  81    16788  14616  11474  -2793  -1335    127       C  
ATOM   4127  C   THR B  81     -19.883  45.412  40.277  1.00114.24           C  
ANISOU 4127  C   THR B  81    16757  14749  11901  -2638  -1337    -48       C  
ATOM   4128  O   THR B  81     -20.692  44.742  39.636  1.00115.25           O  
ANISOU 4128  O   THR B  81    16683  14923  12185  -2610  -1361    -82       O  
ATOM   4129  CB  THR B  81     -18.403  44.141  41.830  1.00125.26           C  
ANISOU 4129  CB  THR B  81    18415  16274  12902  -2897  -1088     80       C  
ATOM   4130  OG1 THR B  81     -19.176  44.820  42.830  1.00130.75           O  
ANISOU 4130  OG1 THR B  81    19114  16926  13637  -2813   -925   -107       O  
ATOM   4131  CG2 THR B  81     -16.957  43.997  42.292  1.00124.52           C  
ANISOU 4131  CG2 THR B  81    18549  16177  12587  -3011  -1149    211       C  
ATOM   4132  N   ASP B  82     -20.189  46.580  40.830  1.00123.16           N  
ANISOU 4132  N   ASP B  82    17927  15773  13095  -2531  -1329   -175       N  
ATOM   4133  CA  ASP B  82     -21.481  47.209  40.606  1.00125.89           C  
ANISOU 4133  CA  ASP B  82    18064  16049  13720  -2353  -1355   -351       C  
ATOM   4134  C   ASP B  82     -21.485  47.904  39.241  1.00115.92           C  
ANISOU 4134  C   ASP B  82    16818  14668  12559  -2230  -1687   -274       C  
ATOM   4135  O   ASP B  82     -20.440  48.297  38.724  1.00 96.31           O  
ANISOU 4135  O   ASP B  82    14554  12119   9919  -2272  -1834   -102       O  
ATOM   4136  CB  ASP B  82     -21.787  48.208  41.730  1.00124.09           C  
ANISOU 4136  CB  ASP B  82    17904  15734  13510  -2261  -1210   -528       C  
ATOM   4137  CG  ASP B  82     -23.227  48.696  41.716  1.00131.93           C  
ANISOU 4137  CG  ASP B  82    18623  16668  14836  -2071  -1154   -743       C  
ATOM   4138  OD1 ASP B  82     -23.960  48.390  40.755  1.00143.74           O  
ANISOU 4138  OD1 ASP B  82    19874  18167  16573  -2004  -1304   -753       O  
ATOM   4139  OD2 ASP B  82     -23.627  49.388  42.678  1.00126.15           O  
ANISOU 4139  OD2 ASP B  82    17923  15874  14134  -1977   -971   -916       O  
ATOM   4140  N   ILE B  83     -22.665  48.045  38.654  1.00124.19           N  
ANISOU 4140  N   ILE B  83    17635  15671  13879  -2074  -1803   -397       N  
ATOM   4141  CA  ILE B  83     -22.805  48.784  37.407  1.00118.41           C  
ANISOU 4141  CA  ILE B  83    16965  14797  13226  -1915  -2145   -340       C  
ATOM   4142  C   ILE B  83     -23.435  50.133  37.743  1.00125.95           C  
ANISOU 4142  C   ILE B  83    17889  15587  14380  -1725  -2205   -498       C  
ATOM   4143  O   ILE B  83     -23.901  50.327  38.867  1.00134.61           O  
ANISOU 4143  O   ILE B  83    18870  16703  15574  -1709  -1962   -674       O  
ATOM   4144  CB  ILE B  83     -23.614  47.993  36.361  1.00 99.18           C  
ANISOU 4144  CB  ILE B  83    14338  12395  10951  -1847  -2342   -365       C  
ATOM   4145  CG1 ILE B  83     -24.738  47.216  37.040  1.00 95.41           C  
ANISOU 4145  CG1 ILE B  83    13482  12013  10757  -1870  -2139   -568       C  
ATOM   4146  CG2 ILE B  83     -22.725  46.954  35.706  1.00 81.50           C  
ANISOU 4146  CG2 ILE B  83    12259  10255   8452  -1994  -2369   -167       C  
ATOM   4147  CD1 ILE B  83     -26.114  47.683  36.698  1.00 95.15           C  
ANISOU 4147  CD1 ILE B  83    13139  11873  11141  -1658  -2316   -774       C  
ATOM   4148  N   SER B  84     -23.407  51.061  36.787  1.00129.07           N  
ANISOU 4148  N   SER B  84    18426  15806  14810  -1573  -2510   -428       N  
ATOM   4149  CA  SER B  84     -23.813  52.462  36.990  1.00129.44           C  
ANISOU 4149  CA  SER B  84    18512  15648  15021  -1384  -2615   -543       C  
ATOM   4150  C   SER B  84     -22.781  53.239  37.813  1.00115.58           C  
ANISOU 4150  C   SER B  84    17018  13812  13086  -1483  -2489   -491       C  
ATOM   4151  O   SER B  84     -22.917  54.446  38.007  1.00111.80           O  
ANISOU 4151  O   SER B  84    16632  13136  12710  -1349  -2580   -569       O  
ATOM   4152  CB  SER B  84     -25.196  52.573  37.649  1.00125.10           C  
ANISOU 4152  CB  SER B  84    17609  15102  14821  -1228  -2503   -835       C  
ATOM   4153  OG  SER B  84     -25.145  52.217  39.019  1.00 91.33           O  
ANISOU 4153  OG  SER B  84    13267  10947  10488  -1347  -2110   -950       O  
ATOM   4154  N   LEU B  85     -21.760  52.549  38.310  1.00113.86           N  
ANISOU 4154  N   LEU B  85    16913  13726  12624  -1711  -2310   -374       N  
ATOM   4155  CA  LEU B  85     -20.690  53.217  39.035  1.00123.41           C  
ANISOU 4155  CA  LEU B  85    18362  14843  13686  -1819  -2257   -325       C  
ATOM   4156  C   LEU B  85     -19.346  52.936  38.379  1.00131.40           C  
ANISOU 4156  C   LEU B  85    19563  15855  14509  -1995  -2325    -47       C  
ATOM   4157  O   LEU B  85     -18.351  53.608  38.653  1.00148.04           O  
ANISOU 4157  O   LEU B  85    21856  17831  16562  -2088  -2358     37       O  
ATOM   4158  CB  LEU B  85     -20.661  52.763  40.494  1.00129.85           C  
ANISOU 4158  CB  LEU B  85    19151  15783  14402  -1911  -1978   -478       C  
ATOM   4159  CG  LEU B  85     -21.941  52.988  41.297  1.00137.88           C  
ANISOU 4159  CG  LEU B  85    19988  16806  15594  -1746  -1801   -758       C  
ATOM   4160  CD1 LEU B  85     -21.780  52.442  42.704  1.00143.31           C  
ANISOU 4160  CD1 LEU B  85    20744  17614  16093  -1847  -1488   -865       C  
ATOM   4161  CD2 LEU B  85     -22.305  54.463  41.331  1.00141.07           C  
ANISOU 4161  CD2 LEU B  85    20466  16968  16167  -1546  -1946   -889       C  
ATOM   4162  N   GLN B  86     -19.329  51.945  37.497  1.00126.47           N  
ANISOU 4162  N   GLN B  86    18880  15360  13814  -2037  -2345     85       N  
ATOM   4163  CA  GLN B  86     -18.091  51.503  36.878  1.00120.04           C  
ANISOU 4163  CA  GLN B  86    18216  14569  12824  -2194  -2344    339       C  
ATOM   4164  C   GLN B  86     -17.451  52.592  36.020  1.00118.16           C  
ANISOU 4164  C   GLN B  86    18203  14096  12596  -2159  -2494    524       C  
ATOM   4165  O   GLN B  86     -16.258  52.860  36.144  1.00117.89           O  
ANISOU 4165  O   GLN B  86    18292  13987  12515  -2311  -2442    672       O  
ATOM   4166  CB  GLN B  86     -18.353  50.246  36.054  1.00129.27           C  
ANISOU 4166  CB  GLN B  86    19300  15904  13914  -2204  -2342    409       C  
ATOM   4167  CG  GLN B  86     -17.106  49.516  35.622  1.00132.84           C  
ANISOU 4167  CG  GLN B  86    19867  16426  14180  -2368  -2262    633       C  
ATOM   4168  CD  GLN B  86     -17.438  48.305  34.788  1.00139.20           C  
ANISOU 4168  CD  GLN B  86    20619  17370  14901  -2350  -2279    673       C  
ATOM   4169  OE1 GLN B  86     -17.640  48.406  33.580  1.00141.06           O  
ANISOU 4169  OE1 GLN B  86    20977  17533  15086  -2231  -2433    763       O  
ATOM   4170  NE2 GLN B  86     -17.486  47.144  35.428  1.00137.73           N  
ANISOU 4170  NE2 GLN B  86    20285  17363  14682  -2461  -2134    606       N  
ATOM   4171  N   TYR B  87     -18.250  53.224  35.164  1.00115.52           N  
ANISOU 4171  N   TYR B  87    17920  13625  12346  -1959  -2684    517       N  
ATOM   4172  CA  TYR B  87     -17.726  54.203  34.211  1.00110.19           C  
ANISOU 4172  CA  TYR B  87    17510  12705  11652  -1910  -2815    726       C  
ATOM   4173  C   TYR B  87     -17.159  55.426  34.925  1.00113.34           C  
ANISOU 4173  C   TYR B  87    18006  12886  12171  -1966  -2813    713       C  
ATOM   4174  O   TYR B  87     -16.127  55.968  34.525  1.00107.36           O  
ANISOU 4174  O   TYR B  87    17433  11960  11398  -2075  -2793    930       O  
ATOM   4175  CB  TYR B  87     -18.792  54.614  33.190  1.00109.41           C  
ANISOU 4175  CB  TYR B  87    17481  12487  11604  -1651  -3069    706       C  
ATOM   4176  CG  TYR B  87     -20.025  55.296  33.729  1.00106.27           C  
ANISOU 4176  CG  TYR B  87    16919  12009  11450  -1451  -3205    439       C  
ATOM   4177  CD1 TYR B  87     -20.995  54.585  34.422  1.00107.32           C  
ANISOU 4177  CD1 TYR B  87    16730  12333  11715  -1409  -3137    186       C  
ATOM   4178  CD2 TYR B  87     -20.246  56.645  33.491  1.00115.46           C  
ANISOU 4178  CD2 TYR B  87    18248  12886  12736  -1293  -3387    447       C  
ATOM   4179  CE1 TYR B  87     -22.135  55.211  34.893  1.00120.62           C  
ANISOU 4179  CE1 TYR B  87    18232  13935  13664  -1212  -3218    -63       C  
ATOM   4180  CE2 TYR B  87     -21.386  57.276  33.949  1.00121.63           C  
ANISOU 4180  CE2 TYR B  87    18866  13580  13768  -1082  -3510    191       C  
ATOM   4181  CZ  TYR B  87     -22.324  56.560  34.655  1.00121.63           C  
ANISOU 4181  CZ  TYR B  87    18518  13785  13912  -1039  -3413    -69       C  
ATOM   4182  OH  TYR B  87     -23.455  57.195  35.117  1.00119.56           O  
ANISOU 4182  OH  TYR B  87    18061  13429  13939   -819  -3489   -330       O  
ATOM   4183  N   LEU B  88     -17.838  55.852  35.985  1.00110.46           N  
ANISOU 4183  N   LEU B  88    17518  12510  11941  -1892  -2818    451       N  
ATOM   4184  CA  LEU B  88     -17.342  56.939  36.816  1.00 96.53           C  
ANISOU 4184  CA  LEU B  88    15854  10541  10282  -1940  -2835    384       C  
ATOM   4185  C   LEU B  88     -16.009  56.541  37.443  1.00 97.90           C  
ANISOU 4185  C   LEU B  88    16051  10772  10373  -2202  -2707    476       C  
ATOM   4186  O   LEU B  88     -15.090  57.347  37.555  1.00114.83           O  
ANISOU 4186  O   LEU B  88    18324  12700  12605  -2312  -2757    571       O  
ATOM   4187  CB  LEU B  88     -18.353  57.275  37.917  1.00 99.93           C  
ANISOU 4187  CB  LEU B  88    16159  10985  10824  -1795  -2815     56       C  
ATOM   4188  CG  LEU B  88     -19.158  58.571  37.834  1.00107.61           C  
ANISOU 4188  CG  LEU B  88    17192  11696  11998  -1560  -2987    -76       C  
ATOM   4189  CD1 LEU B  88     -19.874  58.665  36.514  1.00105.79           C  
ANISOU 4189  CD1 LEU B  88    16969  11400  11827  -1374  -3175     30       C  
ATOM   4190  CD2 LEU B  88     -20.153  58.653  38.980  1.00110.05           C  
ANISOU 4190  CD2 LEU B  88    17338  12071  12404  -1419  -2878   -415       C  
ATOM   4191  N   ALA B  89     -15.918  55.284  37.853  1.00 89.08           N  
ANISOU 4191  N   ALA B  89    14796   9929   9121  -2300  -2561    443       N  
ATOM   4192  CA  ALA B  89     -14.717  54.764  38.492  1.00 88.81           C  
ANISOU 4192  CA  ALA B  89    14762   9965   9015  -2523  -2473    510       C  
ATOM   4193  C   ALA B  89     -13.511  54.711  37.552  1.00 98.25           C  
ANISOU 4193  C   ALA B  89    16024  11080  10226  -2671  -2457    810       C  
ATOM   4194  O   ALA B  89     -12.382  54.949  37.968  1.00107.27           O  
ANISOU 4194  O   ALA B  89    17185  12122  11451  -2841  -2461    879       O  
ATOM   4195  CB  ALA B  89     -14.996  53.388  39.088  1.00 86.30           C  
ANISOU 4195  CB  ALA B  89    14305   9943   8543  -2568  -2323    417       C  
ATOM   4196  N   ILE B  90     -13.737  54.384  36.288  1.00105.63           N  
ANISOU 4196  N   ILE B  90    16996  12047  11090  -2601  -2435    982       N  
ATOM   4197  CA  ILE B  90     -12.618  54.299  35.361  1.00123.88           C  
ANISOU 4197  CA  ILE B  90    19394  14282  13392  -2724  -2347   1274       C  
ATOM   4198  C   ILE B  90     -11.923  55.615  35.027  1.00146.64           C  
ANISOU 4198  C   ILE B  90    22428  16834  16455  -2780  -2390   1429       C  
ATOM   4199  O   ILE B  90     -10.718  55.735  35.228  1.00166.55           O  
ANISOU 4199  O   ILE B  90    24910  19261  19109  -2975  -2314   1550       O  
ATOM   4200  CB  ILE B  90     -13.057  53.629  34.067  1.00124.03           C  
ANISOU 4200  CB  ILE B  90    19491  14400  13236  -2609  -2312   1410       C  
ATOM   4201  CG1 ILE B  90     -13.482  52.196  34.393  1.00113.44           C  
ANISOU 4201  CG1 ILE B  90    17977  13365  11760  -2615  -2248   1287       C  
ATOM   4202  CG2 ILE B  90     -11.943  53.677  33.000  1.00133.07           C  
ANISOU 4202  CG2 ILE B  90    20787  15429  14345  -2702  -2166   1727       C  
ATOM   4203  CD1 ILE B  90     -14.679  51.720  33.622  1.00113.01           C  
ANISOU 4203  CD1 ILE B  90    17934  13403  11603  -2423  -2346   1223       C  
ATOM   4204  N   ASP B  91     -12.665  56.606  34.549  1.00141.18           N  
ANISOU 4204  N   ASP B  91    21892  15943  15807  -2612  -2521   1423       N  
ATOM   4205  CA  ASP B  91     -12.032  57.847  34.118  1.00136.58           C  
ANISOU 4205  CA  ASP B  91    21487  15013  15396  -2665  -2547   1605       C  
ATOM   4206  C   ASP B  91     -11.333  58.566  35.284  1.00131.64           C  
ANISOU 4206  C   ASP B  91    20783  14220  15015  -2827  -2612   1485       C  
ATOM   4207  O   ASP B  91     -10.200  59.030  35.140  1.00129.63           O  
ANISOU 4207  O   ASP B  91    20543  13759  14950  -3016  -2547   1667       O  
ATOM   4208  CB  ASP B  91     -13.050  58.769  33.425  1.00134.83           C  
ANISOU 4208  CB  ASP B  91    21475  14591  15166  -2424  -2716   1607       C  
ATOM   4209  CG  ASP B  91     -14.200  59.182  34.335  1.00132.90           C  
ANISOU 4209  CG  ASP B  91    21137  14359  15000  -2251  -2901   1273       C  
ATOM   4210  OD1 ASP B  91     -14.166  58.879  35.549  1.00142.57           O  
ANISOU 4210  OD1 ASP B  91    22187  15718  16265  -2327  -2876   1049       O  
ATOM   4211  OD2 ASP B  91     -15.139  59.834  33.835  1.00124.68           O  
ANISOU 4211  OD2 ASP B  91    20217  13176  13981  -2024  -3067   1235       O  
ATOM   4212  N   ARG B  92     -11.996  58.631  36.435  1.00118.09           N  
ANISOU 4212  N   ARG B  92    18986  12582  13301  -2752  -2732   1176       N  
ATOM   4213  CA  ARG B  92     -11.447  59.327  37.586  1.00114.49           C  
ANISOU 4213  CA  ARG B  92    18517  11955  13029  -2864  -2845   1016       C  
ATOM   4214  C   ARG B  92     -10.305  58.566  38.236  1.00118.97           C  
ANISOU 4214  C   ARG B  92    18939  12643  13624  -3092  -2790   1034       C  
ATOM   4215  O   ARG B  92      -9.300  59.153  38.627  1.00132.62           O  
ANISOU 4215  O   ARG B  92    20654  14149  15587  -3264  -2875   1064       O  
ATOM   4216  CB  ARG B  92     -12.538  59.557  38.631  1.00112.66           C  
ANISOU 4216  CB  ARG B  92    18290  11780  12736  -2685  -2951    669       C  
ATOM   4217  CG  ARG B  92     -13.512  60.689  38.375  1.00119.05           C  
ANISOU 4217  CG  ARG B  92    19230  12363  13641  -2462  -3081    575       C  
ATOM   4218  CD  ARG B  92     -12.930  62.035  38.753  1.00115.89           C  
ANISOU 4218  CD  ARG B  92    18973  11575  13484  -2529  -3240    548       C  
ATOM   4219  NE  ARG B  92     -13.178  63.057  37.739  1.00107.10           N  
ANISOU 4219  NE  ARG B  92    18028  10159  12505  -2427  -3322    719       N  
ATOM   4220  CZ  ARG B  92     -14.193  63.914  37.758  1.00121.68           C  
ANISOU 4220  CZ  ARG B  92    19979  11838  14416  -2184  -3462    563       C  
ATOM   4221  NH1 ARG B  92     -15.028  63.948  38.791  1.00126.47           N  
ANISOU 4221  NH1 ARG B  92    20524  12537  14990  -2025  -3502    216       N  
ATOM   4222  NH2 ARG B  92     -14.345  64.774  36.761  1.00132.78           N  
ANISOU 4222  NH2 ARG B  92    21570  12957  15924  -2092  -3549    757       N  
ATOM   4223  N   GLY B  93     -10.470  57.253  38.335  1.00 86.60           N  
ANISOU 4223  N   GLY B  93    14720   8873   9310  -3089  -2671   1011       N  
ATOM   4224  CA  GLY B  93      -9.554  56.403  39.073  1.00 85.45           C  
ANISOU 4224  CA  GLY B  93    14444   8867   9155  -3259  -2650    989       C  
ATOM   4225  C   GLY B  93      -8.100  56.509  38.672  1.00102.83           C  
ANISOU 4225  C   GLY B  93    16555  10913  11603  -3479  -2615   1219       C  
ATOM   4226  O   GLY B  93      -7.221  56.538  39.524  1.00119.06           O  
ANISOU 4226  O   GLY B  93    18528  12894  13814  -3625  -2740   1144       O  
ATOM   4227  N   PHE B  94      -7.844  56.569  37.371  1.00115.90           N  
ANISOU 4227  N   PHE B  94    18231  12504  13302  -3496  -2443   1497       N  
ATOM   4228  CA  PHE B  94      -6.487  56.726  36.860  1.00128.21           C  
ANISOU 4228  CA  PHE B  94    19687  13890  15138  -3702  -2327   1745       C  
ATOM   4229  C   PHE B  94      -5.986  58.108  37.246  1.00139.76           C  
ANISOU 4229  C   PHE B  94    21182  14971  16949  -3812  -2492   1723       C  
ATOM   4230  O   PHE B  94      -4.858  58.271  37.708  1.00137.90           O  
ANISOU 4230  O   PHE B  94    20780  14585  17030  -4014  -2558   1741       O  
ATOM   4231  CB  PHE B  94      -6.440  56.542  35.345  1.00136.23           C  
ANISOU 4231  CB  PHE B  94    20794  14903  16063  -3663  -2058   2049       C  
ATOM   4232  CG  PHE B  94      -6.821  55.166  34.889  1.00129.36           C  
ANISOU 4232  CG  PHE B  94    19899  14373  14877  -3566  -1914   2071       C  
ATOM   4233  CD1 PHE B  94      -5.929  54.117  34.997  1.00118.78           C  
ANISOU 4233  CD1 PHE B  94    18364  13194  13572  -3687  -1784   2131       C  
ATOM   4234  CD2 PHE B  94      -8.068  54.924  34.340  1.00133.33           C  
ANISOU 4234  CD2 PHE B  94    20564  15011  15083  -3348  -1934   2022       C  
ATOM   4235  CE1 PHE B  94      -6.277  52.855  34.571  1.00121.75           C  
ANISOU 4235  CE1 PHE B  94    18735  13855  13669  -3597  -1662   2144       C  
ATOM   4236  CE2 PHE B  94      -8.424  53.661  33.914  1.00124.24           C  
ANISOU 4236  CE2 PHE B  94    19390  14142  13672  -3269  -1832   2028       C  
ATOM   4237  CZ  PHE B  94      -7.526  52.627  34.028  1.00116.74           C  
ANISOU 4237  CZ  PHE B  94    18273  13346  12737  -3395  -1688   2091       C  
ATOM   4238  N   GLU B  95      -6.841  59.104  37.035  1.00158.02           N  
ANISOU 4238  N   GLU B  95    23702  17108  19232  -3672  -2580   1677       N  
ATOM   4239  CA  GLU B  95      -6.524  60.489  37.355  1.00163.27           C  
ANISOU 4239  CA  GLU B  95    24441  17376  20216  -3749  -2753   1644       C  
ATOM   4240  C   GLU B  95      -6.293  60.709  38.848  1.00160.96           C  
ANISOU 4240  C   GLU B  95    24088  17032  20036  -3808  -3040   1328       C  
ATOM   4241  O   GLU B  95      -5.335  61.378  39.239  1.00165.36           O  
ANISOU 4241  O   GLU B  95    24570  17301  20959  -3997  -3182   1328       O  
ATOM   4242  CB  GLU B  95      -7.646  61.406  36.869  1.00172.17           C  
ANISOU 4242  CB  GLU B  95    25823  18350  21246  -3535  -2813   1627       C  
ATOM   4243  CG  GLU B  95      -7.630  62.788  37.495  1.00180.54           C  
ANISOU 4243  CG  GLU B  95    26992  19029  22577  -3553  -3054   1482       C  
ATOM   4244  CD  GLU B  95      -8.855  63.598  37.136  1.00182.26           C  
ANISOU 4244  CD  GLU B  95    27447  19120  22685  -3296  -3142   1418       C  
ATOM   4245  OE1 GLU B  95      -9.494  63.289  36.107  1.00179.98           O  
ANISOU 4245  OE1 GLU B  95    27257  18944  22182  -3144  -3013   1581       O  
ATOM   4246  OE2 GLU B  95      -9.176  64.545  37.883  1.00185.46           O  
ANISOU 4246  OE2 GLU B  95    27948  19296  23223  -3231  -3365   1192       O  
ATOM   4247  N   ILE B  96      -7.170  60.145  39.676  1.00143.04           N  
ANISOU 4247  N   ILE B  96    21867  15025  17459  -3645  -3124   1057       N  
ATOM   4248  CA  ILE B  96      -7.045  60.262  41.127  1.00128.73           C  
ANISOU 4248  CA  ILE B  96    20081  13185  15646  -3658  -3379    745       C  
ATOM   4249  C   ILE B  96      -5.749  59.655  41.652  1.00122.64           C  
ANISOU 4249  C   ILE B  96    19121  12432  15043  -3875  -3470    768       C  
ATOM   4250  O   ILE B  96      -5.047  60.266  42.458  1.00142.34           O  
ANISOU 4250  O   ILE B  96    21618  14682  17784  -3988  -3745    629       O  
ATOM   4251  CB  ILE B  96      -8.229  59.587  41.843  1.00115.81           C  
ANISOU 4251  CB  ILE B  96    18536  11854  13610  -3443  -3352    492       C  
ATOM   4252  CG1 ILE B  96      -9.511  60.388  41.619  1.00126.60           C  
ANISOU 4252  CG1 ILE B  96    20061  13138  14901  -3211  -3344    381       C  
ATOM   4253  CG2 ILE B  96      -7.962  59.460  43.328  1.00107.44           C  
ANISOU 4253  CG2 ILE B  96    17553  10803  12466  -3460  -3566    206       C  
ATOM   4254  CD1 ILE B  96     -10.716  59.821  42.342  1.00119.92           C  
ANISOU 4254  CD1 ILE B  96    19266  12559  13739  -3002  -3273    123       C  
ATOM   4255  N   PHE B  97      -5.432  58.457  41.175  1.00 96.34           N  
ANISOU 4255  N   PHE B  97    15628   9375  11601  -3922  -3267    935       N  
ATOM   4256  CA  PHE B  97      -4.225  57.747  41.584  1.00 93.22           C  
ANISOU 4256  CA  PHE B  97    15022   9020  11378  -4101  -3343    971       C  
ATOM   4257  C   PHE B  97      -2.949  58.512  41.237  1.00111.97           C  
ANISOU 4257  C   PHE B  97    17211  11044  14288  -4334  -3405   1134       C  
ATOM   4258  O   PHE B  97      -2.042  58.618  42.059  1.00120.93           O  
ANISOU 4258  O   PHE B  97    18225  12029  15693  -4471  -3681   1016       O  
ATOM   4259  CB  PHE B  97      -4.182  56.357  40.953  1.00104.33           C  
ANISOU 4259  CB  PHE B  97    16295  10763  12584  -4086  -3074   1141       C  
ATOM   4260  CG  PHE B  97      -2.845  55.675  41.071  1.00108.03           C  
ANISOU 4260  CG  PHE B  97    16500  11235  13310  -4265  -3102   1239       C  
ATOM   4261  CD1 PHE B  97      -2.494  55.000  42.232  1.00113.96           C  
ANISOU 4261  CD1 PHE B  97    17227  12091  13982  -4276  -3345   1046       C  
ATOM   4262  CD2 PHE B  97      -1.938  55.708  40.023  1.00106.59           C  
ANISOU 4262  CD2 PHE B  97    16106  10940  13455  -4410  -2875   1527       C  
ATOM   4263  CE1 PHE B  97      -1.267  54.366  42.344  1.00111.85           C  
ANISOU 4263  CE1 PHE B  97    16697  11813  13988  -4420  -3413   1126       C  
ATOM   4264  CE2 PHE B  97      -0.708  55.082  40.128  1.00110.91           C  
ANISOU 4264  CE2 PHE B  97    16362  11482  14299  -4562  -2887   1606       C  
ATOM   4265  CZ  PHE B  97      -0.371  54.408  41.290  1.00113.44           C  
ANISOU 4265  CZ  PHE B  97    16628  11905  14570  -4563  -3181   1399       C  
ATOM   4266  N   ASP B  98      -2.869  59.010  40.007  1.00134.61           N  
ANISOU 4266  N   ASP B  98    20058  13769  17318  -4379  -3147   1411       N  
ATOM   4267  CA  ASP B  98      -1.662  59.684  39.538  1.00158.72           C  
ANISOU 4267  CA  ASP B  98    22912  16481  20912  -4619  -3103   1618       C  
ATOM   4268  C   ASP B  98      -1.390  60.996  40.281  1.00187.98           C  
ANISOU 4268  C   ASP B  98    26673  19782  24970  -4714  -3449   1446       C  
ATOM   4269  O   ASP B  98      -0.240  61.423  40.389  1.00210.91           O  
ANISOU 4269  O   ASP B  98    29343  22398  28396  -4946  -3552   1508       O  
ATOM   4270  CB  ASP B  98      -1.754  59.942  38.030  1.00151.90           C  
ANISOU 4270  CB  ASP B  98    22107  15545  20063  -4617  -2703   1970       C  
ATOM   4271  CG  ASP B  98      -1.272  58.762  37.205  1.00152.41           C  
ANISOU 4271  CG  ASP B  98    22004  15862  20042  -4644  -2352   2202       C  
ATOM   4272  OD1 ASP B  98      -0.467  57.962  37.727  1.00153.94           O  
ANISOU 4272  OD1 ASP B  98    21933  16173  20383  -4746  -2414   2146       O  
ATOM   4273  OD2 ASP B  98      -1.703  58.630  36.038  1.00150.67           O  
ANISOU 4273  OD2 ASP B  98    21940  15711  19596  -4546  -2036   2431       O  
ATOM   4274  N   ARG B  99      -2.439  61.633  40.791  1.00174.45           N  
ANISOU 4274  N   ARG B  99    25250  18028  23006  -4533  -3629   1219       N  
ATOM   4275  CA  ARG B  99      -2.277  62.833  41.606  1.00155.54           C  
ANISOU 4275  CA  ARG B  99    22958  15253  20886  -4587  -3991   1000       C  
ATOM   4276  C   ARG B  99      -1.610  62.509  42.943  1.00132.22           C  
ANISOU 4276  C   ARG B  99    19923  12296  18020  -4661  -4381    717       C  
ATOM   4277  O   ARG B  99      -0.713  63.218  43.400  1.00133.97           O  
ANISOU 4277  O   ARG B  99    20037  12163  18704  -4843  -4677    640       O  
ATOM   4278  CB  ARG B  99      -3.624  63.522  41.835  1.00161.31           C  
ANISOU 4278  CB  ARG B  99    24029  15961  21299  -4335  -4063    806       C  
ATOM   4279  CG  ARG B  99      -3.508  64.800  42.655  1.00178.55           C  
ANISOU 4279  CG  ARG B  99    26362  17730  23747  -4363  -4435    561       C  
ATOM   4280  CD  ARG B  99      -4.633  65.773  42.357  1.00183.49           C  
ANISOU 4280  CD  ARG B  99    27271  18200  24247  -4156  -4410    506       C  
ATOM   4281  NE  ARG B  99      -4.459  66.461  41.079  1.00192.83           N  
ANISOU 4281  NE  ARG B  99    28443  19124  25698  -4244  -4195    855       N  
ATOM   4282  CZ  ARG B  99      -5.188  66.222  39.992  1.00199.30           C  
ANISOU 4282  CZ  ARG B  99    29347  20106  26273  -4100  -3893   1083       C  
ATOM   4283  NH1 ARG B  99      -6.152  65.312  40.021  1.00194.97           N  
ANISOU 4283  NH1 ARG B  99    28843  19975  25261  -3877  -3781    989       N  
ATOM   4284  NH2 ARG B  99      -4.956  66.899  38.875  1.00205.22           N  
ANISOU 4284  NH2 ARG B  99    30154  20578  27245  -4178  -3713   1408       N  
ATOM   4285  N   MET B 100      -2.053  61.420  43.555  1.00115.57           N  
ANISOU 4285  N   MET B 100    17878  10565  15468  -4516  -4393    566       N  
ATOM   4286  CA  MET B 100      -1.535  60.994  44.845  1.00116.60           C  
ANISOU 4286  CA  MET B 100    18018  10721  15564  -4537  -4767    300       C  
ATOM   4287  C   MET B 100      -0.070  60.580  44.774  1.00123.26           C  
ANISOU 4287  C   MET B 100    18486  11463  16882  -4781  -4876    431       C  
ATOM   4288  O   MET B 100       0.721  60.921  45.652  1.00131.72           O  
ANISOU 4288  O   MET B 100    19509  12292  18248  -4887  -5309    240       O  
ATOM   4289  CB  MET B 100      -2.377  59.826  45.356  1.00117.61           C  
ANISOU 4289  CB  MET B 100    18311  11283  15093  -4329  -4663    176       C  
ATOM   4290  CG  MET B 100      -1.822  59.079  46.548  1.00128.26           C  
ANISOU 4290  CG  MET B 100    19695  12720  16317  -4333  -4981    -28       C  
ATOM   4291  SD  MET B 100      -2.435  57.377  46.564  1.00136.11           S  
ANISOU 4291  SD  MET B 100    20718  14234  16765  -4190  -4686     33       S  
ATOM   4292  CE  MET B 100      -0.987  56.499  45.982  1.00108.42           C  
ANISOU 4292  CE  MET B 100    16773  10757  13665  -4406  -4665    293       C  
ATOM   4293  N   VAL B 101       0.288  59.842  43.729  1.00121.88           N  
ANISOU 4293  N   VAL B 101    18050  11465  16796  -4858  -4498    743       N  
ATOM   4294  CA  VAL B 101       1.669  59.417  43.531  1.00130.67           C  
ANISOU 4294  CA  VAL B 101    18752  12487  18409  -5078  -4522    891       C  
ATOM   4295  C   VAL B 101       2.556  60.603  43.145  1.00143.04           C  
ANISOU 4295  C   VAL B 101    20099  13582  20669  -5322  -4584   1007       C  
ATOM   4296  O   VAL B 101       3.761  60.587  43.396  1.00164.09           O  
ANISOU 4296  O   VAL B 101    22419  16045  23883  -5523  -4788   1010       O  
ATOM   4297  CB  VAL B 101       1.779  58.296  42.473  1.00130.75           C  
ANISOU 4297  CB  VAL B 101    18567  12808  18305  -5069  -4048   1189       C  
ATOM   4298  CG1 VAL B 101       1.473  58.821  41.086  1.00132.06           C  
ANISOU 4298  CG1 VAL B 101    18754  12897  18526  -5091  -3594   1495       C  
ATOM   4299  CG2 VAL B 101       3.160  57.650  42.517  1.00136.88           C  
ANISOU 4299  CG2 VAL B 101    18915  13542  19552  -5246  -4110   1274       C  
ATOM   4300  N   SER B 102       1.952  61.625  42.536  1.00149.22           N  
ANISOU 4300  N   SER B 102    21072  14170  21455  -5303  -4416   1103       N  
ATOM   4301  CA  SER B 102       2.685  62.802  42.059  1.00158.60           C  
ANISOU 4301  CA  SER B 102    22094  14882  23286  -5538  -4407   1255       C  
ATOM   4302  C   SER B 102       3.446  63.520  43.168  1.00156.57           C  
ANISOU 4302  C   SER B 102    21740  14248  23503  -5688  -4979    974       C  
ATOM   4303  O   SER B 102       4.504  64.104  42.928  1.00151.46           O  
ANISOU 4303  O   SER B 102    20764  13225  23559  -5956  -5026   1092       O  
ATOM   4304  CB  SER B 102       1.729  63.782  41.379  1.00165.79           C  
ANISOU 4304  CB  SER B 102    23327  15645  24019  -5437  -4205   1360       C  
ATOM   4305  OG  SER B 102       2.415  64.935  40.919  1.00168.55           O  
ANISOU 4305  OG  SER B 102    23553  15504  24984  -5670  -4179   1526       O  
ATOM   4306  N   SER B 103       2.905  63.469  44.380  1.00163.06           N  
ANISOU 4306  N   SER B 103    22855  15154  23945  -5514  -5409    600       N  
ATOM   4307  CA  SER B 103       3.558  64.051  45.551  1.00175.13           C  
ANISOU 4307  CA  SER B 103    24378  16348  25817  -5608  -6030    277       C  
ATOM   4308  C   SER B 103       4.894  63.360  45.863  1.00192.24           C  
ANISOU 4308  C   SER B 103    26082  18551  28410  -5722  -6192    284       C  
ATOM   4309  O   SER B 103       5.714  63.879  46.625  1.00204.74           O  
ANISOU 4309  O   SER B 103    27501  19931  30359  -5715  -6561     83       O  
ATOM   4310  CB  SER B 103       2.623  63.977  46.758  1.00161.81           C  
ANISOU 4310  CB  SER B 103    23173  14815  23493  -5333  -6369   -114       C  
ATOM   4311  OG  SER B 103       1.385  64.605  46.472  1.00140.85           O  
ANISOU 4311  OG  SER B 103    20874  12187  20456  -5145  -6147   -133       O  
ATOM   4312  N   GLY B 104       5.096  62.188  45.262  1.00194.07           N  
ANISOU 4312  N   GLY B 104    26100  19064  28572  -5782  -5893    513       N  
ATOM   4313  CA  GLY B 104       6.316  61.413  45.414  1.00196.85           C  
ANISOU 4313  CA  GLY B 104    25986  19491  29319  -5851  -5966    549       C  
ATOM   4314  C   GLY B 104       6.235  60.366  46.507  1.00190.29           C  
ANISOU 4314  C   GLY B 104    25315  18940  28045  -5670  -6341    294       C  
ATOM   4315  O   GLY B 104       7.206  59.658  46.778  1.00173.88           O  
ANISOU 4315  O   GLY B 104    22894  16927  26244  -5679  -6479    286       O  
ATOM   4316  N   ILE B 105       5.064  60.258  47.127  1.00191.74           N  
ANISOU 4316  N   ILE B 105    26035  19284  27532  -5488  -6480     88       N  
ATOM   4317  CA  ILE B 105       4.820  59.213  48.114  1.00190.83           C  
ANISOU 4317  CA  ILE B 105    26165  19463  26881  -5293  -6740   -121       C  
ATOM   4318  C   ILE B 105       4.569  57.865  47.428  1.00184.08           C  
ANISOU 4318  C   ILE B 105    25193  19054  25696  -5209  -6258    124       C  
ATOM   4319  O   ILE B 105       3.729  57.752  46.531  1.00183.11           O  
ANISOU 4319  O   ILE B 105    25154  19147  25274  -5137  -5739    321       O  
ATOM   4320  CB  ILE B 105       3.631  59.577  49.035  1.00180.61           C  
ANISOU 4320  CB  ILE B 105    25479  18232  24911  -5051  -6914   -420       C  
ATOM   4321  CG1 ILE B 105       2.378  59.910  48.218  1.00169.08           C  
ANISOU 4321  CG1 ILE B 105    24215  16939  23087  -4936  -6380   -279       C  
ATOM   4322  CG2 ILE B 105       3.991  60.757  49.917  1.00177.76           C  
ANISOU 4322  CG2 ILE B 105    25223  17540  24777  -4972  -7330   -687       C  
ATOM   4323  CD1 ILE B 105       1.277  58.881  48.346  1.00149.55           C  
ANISOU 4323  CD1 ILE B 105    22023  14926  19874  -4695  -6082   -288       C  
ATOM   4324  N   SER B 106       5.318  56.846  47.842  1.00177.07           N  
ANISOU 4324  N   SER B 106    24115  18278  24884  -5211  -6466    102       N  
ATOM   4325  CA  SER B 106       5.165  55.509  47.278  1.00166.93           C  
ANISOU 4325  CA  SER B 106    22725  17388  23314  -5127  -6064    307       C  
ATOM   4326  C   SER B 106       3.794  54.923  47.604  1.00160.07           C  
ANISOU 4326  C   SER B 106    22343  16875  21600  -4880  -5876    226       C  
ATOM   4327  O   SER B 106       3.378  54.926  48.760  1.00171.32           O  
ANISOU 4327  O   SER B 106    24160  18306  22626  -4741  -6229    -45       O  
ATOM   4328  CB  SER B 106       6.266  54.576  47.792  1.00168.34           C  
ANISOU 4328  CB  SER B 106    22625  17571  23766  -5159  -6403    266       C  
ATOM   4329  OG  SER B 106       7.559  55.109  47.550  1.00157.94           O  
ANISOU 4329  OG  SER B 106    20796  15903  23312  -5392  -6597    319       O  
ATOM   4330  N   PRO B 107       3.070  54.457  46.576  1.00146.46           N  
ANISOU 4330  N   PRO B 107    20608  15428  19613  -4823  -5313    455       N  
ATOM   4331  CA  PRO B 107       1.690  53.974  46.702  1.00134.54           C  
ANISOU 4331  CA  PRO B 107    19487  14235  17398  -4611  -5071    402       C  
ATOM   4332  C   PRO B 107       1.580  52.724  47.586  1.00132.59           C  
ANISOU 4332  C   PRO B 107    19424  14235  16721  -4478  -5221    290       C  
ATOM   4333  O   PRO B 107       2.570  52.016  47.759  1.00131.51           O  
ANISOU 4333  O   PRO B 107    19055  14087  16826  -4539  -5408    330       O  
ATOM   4334  CB  PRO B 107       1.300  53.669  45.251  1.00125.45           C  
ANISOU 4334  CB  PRO B 107    18166  13267  16233  -4622  -4502    702       C  
ATOM   4335  CG  PRO B 107       2.598  53.351  44.588  1.00128.04           C  
ANISOU 4335  CG  PRO B 107    18039  13499  17113  -4796  -4428    910       C  
ATOM   4336  CD  PRO B 107       3.562  54.324  45.194  1.00139.00           C  
ANISOU 4336  CD  PRO B 107    19270  14495  19049  -4955  -4865    782       C  
ATOM   4337  N   ASN B 108       0.411  52.504  48.183  1.00131.34           N  
ANISOU 4337  N   ASN B 108    19678  14262  15962  -4296  -5148    145       N  
ATOM   4338  CA  ASN B 108       0.145  51.319  49.007  1.00135.51           C  
ANISOU 4338  CA  ASN B 108    20449  15019  16018  -4163  -5214     63       C  
ATOM   4339  C   ASN B 108      -0.153  50.085  48.159  1.00133.49           C  
ANISOU 4339  C   ASN B 108    20031  15079  15609  -4139  -4785    294       C  
ATOM   4340  O   ASN B 108      -0.639  50.217  47.035  1.00133.78           O  
ANISOU 4340  O   ASN B 108    19918  15210  15702  -4160  -4391    463       O  
ATOM   4341  CB  ASN B 108      -1.015  51.589  49.963  1.00142.84           C  
ANISOU 4341  CB  ASN B 108    21881  16004  16389  -3984  -5229   -171       C  
ATOM   4342  CG  ASN B 108      -0.861  52.898  50.693  1.00162.82           C  
ANISOU 4342  CG  ASN B 108    24613  18213  19039  -3984  -5611   -414       C  
ATOM   4343  OD1 ASN B 108      -1.427  53.912  50.289  1.00159.41           O  
ANISOU 4343  OD1 ASN B 108    24201  17675  18693  -3981  -5471   -442       O  
ATOM   4344  ND2 ASN B 108      -0.080  52.891  51.769  1.00181.72           N  
ANISOU 4344  ND2 ASN B 108    27173  20428  21446  -3976  -6130   -600       N  
ATOM   4345  N   GLU B 109       0.148  48.897  48.682  1.00129.56           N  
ANISOU 4345  N   GLU B 109    19591  14721  14917  -4087  -4887    297       N  
ATOM   4346  CA  GLU B 109      -0.140  47.647  47.972  1.00121.89           C  
ANISOU 4346  CA  GLU B 109    18501  14030  13782  -4055  -4516    490       C  
ATOM   4347  C   GLU B 109      -1.617  47.529  47.600  1.00115.39           C  
ANISOU 4347  C   GLU B 109    17874  13426  12543  -3953  -4101    504       C  
ATOM   4348  O   GLU B 109      -1.962  47.063  46.515  1.00103.88           O  
ANISOU 4348  O   GLU B 109    16239  12128  11102  -3962  -3741    681       O  
ATOM   4349  CB  GLU B 109       0.288  46.434  48.799  1.00129.80           C  
ANISOU 4349  CB  GLU B 109    19626  15115  14579  -3989  -4733    459       C  
ATOM   4350  CG  GLU B 109       0.114  45.095  48.073  1.00127.60           C  
ANISOU 4350  CG  GLU B 109    19210  15087  14185  -3963  -4387    653       C  
ATOM   4351  CD  GLU B 109      -1.304  44.563  48.153  1.00124.37           C  
ANISOU 4351  CD  GLU B 109    19098  14910  13246  -3856  -4050    639       C  
ATOM   4352  OE1 GLU B 109      -1.958  44.763  49.198  1.00138.95           O  
ANISOU 4352  OE1 GLU B 109    21328  16747  14720  -3769  -4151    469       O  
ATOM   4353  OE2 GLU B 109      -1.771  43.961  47.164  1.00108.28           O  
ANISOU 4353  OE2 GLU B 109    16910  13050  11180  -3857  -3679    790       O  
ATOM   4354  N   ALA B 110      -2.490  47.915  48.520  1.00119.79           N  
ANISOU 4354  N   ALA B 110    18803  13980  12730  -3846  -4159    306       N  
ATOM   4355  CA  ALA B 110      -3.917  47.880  48.249  1.00111.03           C  
ANISOU 4355  CA  ALA B 110    17839  13051  11297  -3745  -3783    290       C  
ATOM   4356  C   ALA B 110      -4.265  48.827  47.098  1.00102.35           C  
ANISOU 4356  C   ALA B 110    16537  11892  10460  -3783  -3585    377       C  
ATOM   4357  O   ALA B 110      -5.109  48.509  46.262  1.00 81.43           O  
ANISOU 4357  O   ALA B 110    13816   9410   7712  -3738  -3254    476       O  
ATOM   4358  CB  ALA B 110      -4.709  48.234  49.502  1.00107.33           C  
ANISOU 4358  CB  ALA B 110    17797  12554  10431  -3615  -3860     47       C  
ATOM   4359  N   SER B 111      -3.620  49.992  47.066  1.00118.48           N  
ANISOU 4359  N   SER B 111    18507  13672  12839  -3861  -3813    337       N  
ATOM   4360  CA  SER B 111      -3.898  51.004  46.042  1.00116.52           C  
ANISOU 4360  CA  SER B 111    18123  13312  12835  -3894  -3654    428       C  
ATOM   4361  C   SER B 111      -3.438  50.614  44.623  1.00105.31           C  
ANISOU 4361  C   SER B 111    16389  11955  11670  -3984  -3396    712       C  
ATOM   4362  O   SER B 111      -4.148  50.878  43.646  1.00 86.50           O  
ANISOU 4362  O   SER B 111    13987   9624   9254  -3938  -3133    818       O  
ATOM   4363  CB  SER B 111      -3.272  52.346  46.440  1.00107.30           C  
ANISOU 4363  CB  SER B 111    16977  11806  11988  -3970  -3975    314       C  
ATOM   4364  OG  SER B 111      -1.890  52.220  46.712  1.00118.12           O  
ANISOU 4364  OG  SER B 111    18157  13021  13703  -4111  -4269    344       O  
ATOM   4365  N   VAL B 112      -2.253  50.014  44.500  1.00 96.37           N  
ANISOU 4365  N   VAL B 112    15026  10800  10789  -4094  -3476    828       N  
ATOM   4366  CA  VAL B 112      -1.738  49.625  43.184  1.00 90.09           C  
ANISOU 4366  CA  VAL B 112    13953  10050  10226  -4166  -3193   1091       C  
ATOM   4367  C   VAL B 112      -2.600  48.534  42.559  1.00103.50           C  
ANISOU 4367  C   VAL B 112    15710  12045  11571  -4056  -2880   1176       C  
ATOM   4368  O   VAL B 112      -2.822  48.520  41.349  1.00121.39           O  
ANISOU 4368  O   VAL B 112    17903  14357  13862  -4044  -2598   1348       O  
ATOM   4369  CB  VAL B 112      -0.262  49.150  43.258  1.00 93.70           C  
ANISOU 4369  CB  VAL B 112    14116  10416  11071  -4292  -3334   1175       C  
ATOM   4370  CG1 VAL B 112      -0.054  48.206  44.411  1.00119.86           C  
ANISOU 4370  CG1 VAL B 112    17528  13828  14183  -4237  -3605   1030       C  
ATOM   4371  CG2 VAL B 112       0.170  48.489  41.956  1.00 84.55           C  
ANISOU 4371  CG2 VAL B 112    12711   9354  10060  -4324  -2968   1432       C  
ATOM   4372  N   THR B 113      -3.106  47.634  43.394  1.00102.55           N  
ANISOU 4372  N   THR B 113    15749  12103  11114  -3973  -2939   1052       N  
ATOM   4373  CA  THR B 113      -4.047  46.623  42.931  1.00 90.60           C  
ANISOU 4373  CA  THR B 113    14296  10843   9283  -3877  -2672   1098       C  
ATOM   4374  C   THR B 113      -5.358  47.266  42.514  1.00 80.82           C  
ANISOU 4374  C   THR B 113    13186   9639   7882  -3782  -2517   1046       C  
ATOM   4375  O   THR B 113      -5.971  46.865  41.532  1.00 90.85           O  
ANISOU 4375  O   THR B 113    14422  11033   9065  -3727  -2291   1145       O  
ATOM   4376  CB  THR B 113      -4.342  45.573  44.005  1.00 99.17           C  
ANISOU 4376  CB  THR B 113    15545  12074  10059  -3822  -2751    982       C  
ATOM   4377  OG1 THR B 113      -3.110  45.060  44.524  1.00111.23           O  
ANISOU 4377  OG1 THR B 113    16981  13536  11746  -3887  -2978   1006       O  
ATOM   4378  CG2 THR B 113      -5.138  44.443  43.399  1.00 73.99           C  
ANISOU 4378  CG2 THR B 113    12355   9114   6644  -3759  -2474   1057       C  
ATOM   4379  N   SER B 114      -5.771  48.277  43.269  1.00 82.72           N  
ANISOU 4379  N   SER B 114    13582   9751   8098  -3748  -2668    875       N  
ATOM   4380  CA  SER B 114      -7.032  48.959  43.025  1.00 93.18           C  
ANISOU 4380  CA  SER B 114    15019  11083   9304  -3635  -2557    791       C  
ATOM   4381  C   SER B 114      -7.044  49.556  41.620  1.00 97.77           C  
ANISOU 4381  C   SER B 114    15494  11583  10073  -3639  -2428    969       C  
ATOM   4382  O   SER B 114      -8.009  49.388  40.870  1.00 90.74           O  
ANISOU 4382  O   SER B 114    14620  10799   9058  -3537  -2266   1001       O  
ATOM   4383  CB  SER B 114      -7.266  50.045  44.079  1.00105.17           C  
ANISOU 4383  CB  SER B 114    16723  12428  10808  -3594  -2756    572       C  
ATOM   4384  OG  SER B 114      -8.564  50.604  43.965  1.00101.67           O  
ANISOU 4384  OG  SER B 114    16377  12004  10251  -3456  -2636    462       O  
ATOM   4385  N   VAL B 115      -5.964  50.247  41.269  1.00106.78           N  
ANISOU 4385  N   VAL B 115    16534  12514  11524  -3757  -2507   1088       N  
ATOM   4386  CA  VAL B 115      -5.812  50.798  39.930  1.00120.20           C  
ANISOU 4386  CA  VAL B 115    18175  14105  13390  -3774  -2348   1299       C  
ATOM   4387  C   VAL B 115      -5.640  49.681  38.911  1.00116.63           C  
ANISOU 4387  C   VAL B 115    17632  13834  12850  -3764  -2110   1486       C  
ATOM   4388  O   VAL B 115      -6.099  49.794  37.775  1.00119.15           O  
ANISOU 4388  O   VAL B 115    18012  14162  13098  -3690  -1944   1616       O  
ATOM   4389  CB  VAL B 115      -4.617  51.756  39.848  1.00137.18           C  
ANISOU 4389  CB  VAL B 115    20218  15964  15942  -3930  -2444   1397       C  
ATOM   4390  CG1 VAL B 115      -4.535  52.401  38.469  1.00132.83           C  
ANISOU 4390  CG1 VAL B 115    19672  15271  15527  -3940  -2231   1636       C  
ATOM   4391  CG2 VAL B 115      -4.742  52.815  40.918  1.00152.02           C  
ANISOU 4391  CG2 VAL B 115    22211  17644  17908  -3937  -2725   1181       C  
ATOM   4392  N   ALA B 116      -4.971  48.605  39.320  1.00112.77           N  
ANISOU 4392  N   ALA B 116    17026  13469  12352  -3822  -2117   1493       N  
ATOM   4393  CA  ALA B 116      -4.801  47.440  38.457  1.00109.19           C  
ANISOU 4393  CA  ALA B 116    16499  13186  11802  -3799  -1901   1639       C  
ATOM   4394  C   ALA B 116      -6.164  46.856  38.115  1.00107.70           C  
ANISOU 4394  C   ALA B 116    16444  13191  11285  -3655  -1811   1573       C  
ATOM   4395  O   ALA B 116      -6.426  46.517  36.964  1.00101.19           O  
ANISOU 4395  O   ALA B 116    15653  12424  10370  -3588  -1643   1696       O  
ATOM   4396  CB  ALA B 116      -3.915  46.392  39.118  1.00100.61           C  
ANISOU 4396  CB  ALA B 116    15275  12182  10772  -3866  -1970   1626       C  
ATOM   4397  N   ARG B 117      -7.029  46.752  39.123  1.00107.64           N  
ANISOU 4397  N   ARG B 117    16519  13265  11112  -3603  -1923   1371       N  
ATOM   4398  CA  ARG B 117      -8.399  46.285  38.923  1.00110.09           C  
ANISOU 4398  CA  ARG B 117    16903  13731  11195  -3480  -1846   1280       C  
ATOM   4399  C   ARG B 117      -9.149  47.228  37.999  1.00108.34           C  
ANISOU 4399  C   ARG B 117    16753  13416  10997  -3379  -1828   1309       C  
ATOM   4400  O   ARG B 117      -9.827  46.792  37.075  1.00126.40           O  
ANISOU 4400  O   ARG B 117    19065  15788  13175  -3285  -1751   1352       O  
ATOM   4401  CB  ARG B 117      -9.146  46.167  40.256  1.00122.96           C  
ANISOU 4401  CB  ARG B 117    18604  15428  12686  -3450  -1916   1062       C  
ATOM   4402  CG  ARG B 117      -8.611  45.100  41.190  1.00122.46           C  
ANISOU 4402  CG  ARG B 117    18544  15462  12523  -3517  -1942   1034       C  
ATOM   4403  CD  ARG B 117      -9.098  43.729  40.780  1.00130.76           C  
ANISOU 4403  CD  ARG B 117    19554  16700  13429  -3491  -1791   1076       C  
ATOM   4404  NE  ARG B 117      -8.110  42.694  41.061  1.00131.62           N  
ANISOU 4404  NE  ARG B 117    19625  16856  13530  -3565  -1813   1158       N  
ATOM   4405  CZ  ARG B 117      -7.989  42.071  42.227  1.00128.30           C  
ANISOU 4405  CZ  ARG B 117    19297  16473  12979  -3590  -1877   1082       C  
ATOM   4406  NH1 ARG B 117      -8.796  42.378  43.235  1.00114.14           N  
ANISOU 4406  NH1 ARG B 117    17656  14683  11029  -3552  -1880    925       N  
ATOM   4407  NH2 ARG B 117      -7.059  41.140  42.382  1.00137.22           N  
ANISOU 4407  NH2 ARG B 117    20387  17625  14126  -3637  -1928   1167       N  
ATOM   4408  N   LEU B 118      -9.037  48.522  38.274  1.00101.97           N  
ANISOU 4408  N   LEU B 118    15998  12414  10333  -3388  -1934   1273       N  
ATOM   4409  CA  LEU B 118      -9.677  49.555  37.467  1.00100.69           C  
ANISOU 4409  CA  LEU B 118    15931  12113  10212  -3284  -1951   1308       C  
ATOM   4410  C   LEU B 118      -9.174  49.512  36.026  1.00 90.42           C  
ANISOU 4410  C   LEU B 118    14672  10756   8926  -3282  -1823   1558       C  
ATOM   4411  O   LEU B 118      -9.953  49.613  35.073  1.00 75.41           O  
ANISOU 4411  O   LEU B 118    12883   8857   6913  -3146  -1808   1602       O  
ATOM   4412  CB  LEU B 118      -9.413  50.929  38.082  1.00112.21           C  
ANISOU 4412  CB  LEU B 118    17445  13333  11857  -3320  -2093   1239       C  
ATOM   4413  CG  LEU B 118     -10.565  51.915  38.270  1.00 77.79           C  
ANISOU 4413  CG  LEU B 118    13188   8875   7493  -3171  -2191   1078       C  
ATOM   4414  CD1 LEU B 118     -11.795  51.246  38.848  1.00 76.76           C  
ANISOU 4414  CD1 LEU B 118    13026   8950   7192  -3051  -2160    870       C  
ATOM   4415  CD2 LEU B 118     -10.092  52.999  39.198  1.00 88.22           C  
ANISOU 4415  CD2 LEU B 118    14562   9977   8980  -3234  -2345    969       C  
ATOM   4416  N   ALA B 119      -7.863  49.342  35.883  1.00 97.60           N  
ANISOU 4416  N   ALA B 119    15499  11607   9976  -3422  -1731   1717       N  
ATOM   4417  CA  ALA B 119      -7.234  49.243  34.574  1.00104.89           C  
ANISOU 4417  CA  ALA B 119    16472  12472  10911  -3428  -1533   1967       C  
ATOM   4418  C   ALA B 119      -7.698  48.009  33.844  1.00 99.87           C  
ANISOU 4418  C   ALA B 119    15883  12045  10017  -3324  -1427   1990       C  
ATOM   4419  O   ALA B 119      -8.261  48.108  32.770  1.00 81.93           O  
ANISOU 4419  O   ALA B 119    13791   9753   7586  -3194  -1384   2070       O  
ATOM   4420  CB  ALA B 119      -5.726  49.228  34.706  1.00117.02           C  
ANISOU 4420  CB  ALA B 119    17841  13907  12716  -3604  -1429   2105       C  
ATOM   4421  N   ALA B 120      -7.480  46.852  34.458  1.00113.87           N  
ANISOU 4421  N   ALA B 120    17520  14001  11746  -3373  -1419   1910       N  
ATOM   4422  CA  ALA B 120      -7.805  45.563  33.855  1.00111.17           C  
ANISOU 4422  CA  ALA B 120    17206  13842  11193  -3295  -1329   1919       C  
ATOM   4423  C   ALA B 120      -9.286  45.423  33.539  1.00 75.02           C  
ANISOU 4423  C   ALA B 120    12736   9345   6424  -3143  -1439   1789       C  
ATOM   4424  O   ALA B 120      -9.652  44.719  32.598  1.00 83.10           O  
ANISOU 4424  O   ALA B 120    13859  10439   7276  -3043  -1396   1826       O  
ATOM   4425  CB  ALA B 120      -7.364  44.428  34.767  1.00134.57           C  
ANISOU 4425  CB  ALA B 120    20009  16951  14169  -3379  -1337   1840       C  
ATOM   4426  N   ALA B 121     -10.131  46.083  34.328  1.00 71.55           N  
ANISOU 4426  N   ALA B 121    12271   8881   6033  -3117  -1587   1622       N  
ATOM   4427  CA  ALA B 121     -11.575  45.957  34.166  1.00 91.90           C  
ANISOU 4427  CA  ALA B 121    14874  11527   8516  -2976  -1697   1470       C  
ATOM   4428  C   ALA B 121     -11.965  46.361  32.759  1.00104.47           C  
ANISOU 4428  C   ALA B 121    16657  13024  10015  -2828  -1740   1576       C  
ATOM   4429  O   ALA B 121     -12.817  45.733  32.130  1.00121.93           O  
ANISOU 4429  O   ALA B 121    18908  15311  12109  -2710  -1818   1513       O  
ATOM   4430  CB  ALA B 121     -12.313  46.808  35.186  1.00 93.74           C  
ANISOU 4430  CB  ALA B 121    15053  11710   8856  -2955  -1806   1286       C  
ATOM   4431  N   LYS B 122     -11.330  47.417  32.270  1.00 97.40           N  
ANISOU 4431  N   LYS B 122    15896  11937   9175  -2834  -1703   1739       N  
ATOM   4432  CA  LYS B 122     -11.542  47.843  30.903  1.00112.33           C  
ANISOU 4432  CA  LYS B 122    18048  13705  10929  -2690  -1721   1883       C  
ATOM   4433  C   LYS B 122     -10.169  48.064  30.274  1.00107.70           C  
ANISOU 4433  C   LYS B 122    17571  12999  10350  -2782  -1477   2150       C  
ATOM   4434  O   LYS B 122      -9.956  49.014  29.524  1.00 90.81           O  
ANISOU 4434  O   LYS B 122    15649  10656   8200  -2734  -1433   2320       O  
ATOM   4435  CB  LYS B 122     -12.398  49.110  30.880  1.00128.22           C  
ANISOU 4435  CB  LYS B 122    20154  15547  13016  -2569  -1916   1819       C  
ATOM   4436  CG  LYS B 122     -13.761  48.904  31.538  1.00138.89           C  
ANISOU 4436  CG  LYS B 122    21340  17008  14425  -2473  -2112   1544       C  
ATOM   4437  CD  LYS B 122     -14.657  48.044  30.674  1.00142.27           C  
ANISOU 4437  CD  LYS B 122    21822  17533  14701  -2321  -2238   1483       C  
ATOM   4438  CE  LYS B 122     -15.783  47.382  31.445  1.00127.68           C  
ANISOU 4438  CE  LYS B 122    19706  15840  12965  -2299  -2336   1220       C  
ATOM   4439  NZ  LYS B 122     -17.046  48.176  31.393  1.00115.21           N  
ANISOU 4439  NZ  LYS B 122    18087  14160  11528  -2119  -2570   1061       N  
ATOM   4440  N   GLY B 123      -9.263  47.127  30.544  1.00119.88           N  
ANISOU 4440  N   GLY B 123    18965  14662  11922  -2905  -1304   2190       N  
ATOM   4441  CA  GLY B 123      -7.907  47.171  30.029  1.00120.14           C  
ANISOU 4441  CA  GLY B 123    19019  14599  12029  -3002  -1029   2424       C  
ATOM   4442  C   GLY B 123      -7.765  46.767  28.585  1.00113.84           C  
ANISOU 4442  C   GLY B 123    18503  13779  10970  -2872   -846   2598       C  
ATOM   4443  O   GLY B 123      -8.720  46.223  28.038  1.00 93.27           O  
ANISOU 4443  O   GLY B 123    16064  11264   8110  -2708   -988   2505       O  
ATOM   4444  N   ASN B 124      -6.607  46.991  27.951  1.00139.13           N  
ANISOU 4444  N   ASN B 124    21772  16856  14237  -2934   -529   2839       N  
ATOM   4445  CA  ASN B 124      -5.334  47.492  28.524  1.00131.31           C  
ANISOU 4445  CA  ASN B 124    20525  15743  13623  -3146   -346   2953       C  
ATOM   4446  C   ASN B 124      -4.823  46.718  29.747  1.00111.92           C  
ANISOU 4446  C   ASN B 124    17692  13440  11392  -3289   -423   2800       C  
ATOM   4447  O   ASN B 124      -4.805  47.230  30.866  1.00103.99           O  
ANISOU 4447  O   ASN B 124    16495  12401  10617  -3402   -620   2679       O  
ATOM   4448  CB  ASN B 124      -5.437  48.990  28.870  1.00128.66           C  
ANISOU 4448  CB  ASN B 124    20211  15175  13499  -3215   -461   2989       C  
ATOM   4449  CG  ASN B 124      -4.078  49.640  29.089  1.00121.35           C  
ANISOU 4449  CG  ASN B 124    19082  14047  12977  -3425   -241   3159       C  
ATOM   4450  OD1 ASN B 124      -3.078  48.959  29.315  1.00117.88           O  
ANISOU 4450  OD1 ASN B 124    18390  13670  12731  -3537    -68   3195       O  
ATOM   4451  ND2 ASN B 124      -4.037  50.966  29.017  1.00121.70           N  
ANISOU 4451  ND2 ASN B 124    19223  13828  13190  -3478   -260   3261       N  
ATOM   4452  N   GLY B 125      -4.418  45.477  29.508  1.00102.20           N  
ANISOU 4452  N   GLY B 125    16399  12362  10072  -3263   -282   2803       N  
ATOM   4453  CA  GLY B 125      -3.728  44.685  30.502  1.00 87.06           C  
ANISOU 4453  CA  GLY B 125    14157  10553   8367  -3382   -320   2708       C  
ATOM   4454  C   GLY B 125      -2.311  45.165  30.759  1.00 90.89           C  
ANISOU 4454  C   GLY B 125    14384  10878   9273  -3552   -153   2845       C  
ATOM   4455  O   GLY B 125      -1.811  45.076  31.885  1.00 88.46           O  
ANISOU 4455  O   GLY B 125    13802  10578   9231  -3676   -325   2740       O  
ATOM   4456  N   ASP B 126      -1.666  45.667  29.706  1.00 96.77           N  
ANISOU 4456  N   ASP B 126    15225  11460  10083  -3552    182   3080       N  
ATOM   4457  CA  ASP B 126      -0.247  46.034  29.741  1.00107.16           C  
ANISOU 4457  CA  ASP B 126    16256  12601  11857  -3715    426   3239       C  
ATOM   4458  C   ASP B 126       0.083  47.083  30.796  1.00116.94           C  
ANISOU 4458  C   ASP B 126    17261  13670  13502  -3900    182   3177       C  
ATOM   4459  O   ASP B 126       1.154  47.046  31.410  1.00103.60           O  
ANISOU 4459  O   ASP B 126    15213  11900  12250  -4051    172   3176       O  
ATOM   4460  CB  ASP B 126       0.191  46.538  28.367  1.00111.16           C  
ANISOU 4460  CB  ASP B 126    16981  12935  12322  -3676    875   3520       C  
ATOM   4461  CG  ASP B 126      -0.363  45.698  27.236  1.00110.07           C  
ANISOU 4461  CG  ASP B 126    17213  12932  11677  -3451   1058   3562       C  
ATOM   4462  OD1 ASP B 126      -1.569  45.836  26.933  1.00 88.08           O1-
ANISOU 4462  OD1 ASP B 126    14764  10203   8501  -3307    843   3485       O1-
ATOM   4463  OD2 ASP B 126       0.407  44.903  26.651  1.00116.08           O  
ANISOU 4463  OD2 ASP B 126    17927  13730  12449  -3409   1401   3657       O  
ATOM   4464  N   TYR B 127      -0.837  48.020  30.997  1.00124.83           N  
ANISOU 4464  N   TYR B 127    18464  14596  14371  -3876    -40   3111       N  
ATOM   4465  CA  TYR B 127      -0.666  49.037  32.024  1.00127.47           C  
ANISOU 4465  CA  TYR B 127    18638  14759  15036  -4024   -313   3014       C  
ATOM   4466  C   TYR B 127      -0.787  48.394  33.394  1.00120.86           C  
ANISOU 4466  C   TYR B 127    17617  14085  14220  -4051   -664   2752       C  
ATOM   4467  O   TYR B 127       0.043  48.622  34.273  1.00128.22           O  
ANISOU 4467  O   TYR B 127    18283  14908  15527  -4197   -828   2689       O  
ATOM   4468  CB  TYR B 127      -1.698  50.149  31.854  1.00129.80           C  
ANISOU 4468  CB  TYR B 127    19227  14934  15157  -3953   -453   2995       C  
ATOM   4469  CG  TYR B 127      -1.821  51.073  33.040  1.00131.68           C  
ANISOU 4469  CG  TYR B 127    19365  15035  15631  -4053   -798   2818       C  
ATOM   4470  CD1 TYR B 127      -0.810  51.970  33.357  1.00149.07           C  
ANISOU 4470  CD1 TYR B 127    21365  16958  18318  -4250   -805   2892       C  
ATOM   4471  CD2 TYR B 127      -2.955  51.056  33.835  1.00121.30           C  
ANISOU 4471  CD2 TYR B 127    18164  13853  14071  -3949  -1108   2569       C  
ATOM   4472  CE1 TYR B 127      -0.925  52.822  34.441  1.00155.45           C  
ANISOU 4472  CE1 TYR B 127    22122  17618  19324  -4328  -1154   2705       C  
ATOM   4473  CE2 TYR B 127      -3.080  51.901  34.920  1.00133.51           C  
ANISOU 4473  CE2 TYR B 127    19669  15266  15793  -4015  -1405   2390       C  
ATOM   4474  CZ  TYR B 127      -2.063  52.784  35.219  1.00147.83           C  
ANISOU 4474  CZ  TYR B 127    21319  16798  18052  -4199  -1448   2452       C  
ATOM   4475  OH  TYR B 127      -2.180  53.630  36.299  1.00150.13           O  
ANISOU 4475  OH  TYR B 127    21604  16935  18502  -4252  -1775   2252       O  
ATOM   4476  N   ALA B 128      -1.807  47.552  33.544  1.00113.12           N  
ANISOU 4476  N   ALA B 128    16791  13349  12839  -3906   -777   2607       N  
ATOM   4477  CA  ALA B 128      -2.078  46.851  34.794  1.00107.49           C  
ANISOU 4477  CA  ALA B 128    15985  12798  12060  -3909  -1061   2378       C  
ATOM   4478  C   ALA B 128      -0.868  46.027  35.225  1.00111.64           C  
ANISOU 4478  C   ALA B 128    16225  13347  12847  -3999  -1051   2395       C  
ATOM   4479  O   ALA B 128      -0.538  45.962  36.410  1.00121.43           O  
ANISOU 4479  O   ALA B 128    17333  14571  14231  -4069  -1331   2249       O  
ATOM   4480  CB  ALA B 128      -3.306  45.965  34.645  1.00 90.01           C  
ANISOU 4480  CB  ALA B 128    13961  10821   9416  -3750  -1086   2270       C  
ATOM   4481  N   PHE B 129      -0.230  45.384  34.253  1.00 80.11           N  
ANISOU 4481  N   PHE B 129    12160   9382   8897  -3973   -736   2565       N  
ATOM   4482  CA  PHE B 129       0.998  44.634  34.483  1.00102.12           C  
ANISOU 4482  CA  PHE B 129    14639  12165  11997  -4039   -681   2602       C  
ATOM   4483  C   PHE B 129       2.121  45.581  34.922  1.00125.23           C  
ANISOU 4483  C   PHE B 129    17271  14833  15478  -4220   -757   2647       C  
ATOM   4484  O   PHE B 129       2.890  45.265  35.833  1.00142.90           O  
ANISOU 4484  O   PHE B 129    19248  17037  18012  -4294   -995   2552       O  
ATOM   4485  CB  PHE B 129       1.392  43.858  33.225  1.00 92.44           C  
ANISOU 4485  CB  PHE B 129    13427  11000  10697  -3951   -268   2775       C  
ATOM   4486  CG  PHE B 129       2.463  42.814  33.449  1.00104.38           C  
ANISOU 4486  CG  PHE B 129    14638  12554  12470  -3963   -212   2778       C  
ATOM   4487  CD1 PHE B 129       2.910  42.502  34.725  1.00126.71           C  
ANISOU 4487  CD1 PHE B 129    17242  15382  15522  -4032   -571   2628       C  
ATOM   4488  CD2 PHE B 129       3.024  42.145  32.373  1.00112.58           C  
ANISOU 4488  CD2 PHE B 129    15644  13614  13516  -3883    193   2926       C  
ATOM   4489  CE1 PHE B 129       3.898  41.548  34.921  1.00129.59           C  
ANISOU 4489  CE1 PHE B 129    17327  15764  16150  -4022   -558   2629       C  
ATOM   4490  CE2 PHE B 129       4.010  41.189  32.561  1.00118.96           C  
ANISOU 4490  CE2 PHE B 129    16157  14446  14597  -3872    250   2920       C  
ATOM   4491  CZ  PHE B 129       4.446  40.890  33.840  1.00122.43           C  
ANISOU 4491  CZ  PHE B 129    16345  14881  15294  -3942   -143   2772       C  
ATOM   4492  N   LYS B 130       2.231  46.725  34.249  1.00120.76           N  
ANISOU 4492  N   LYS B 130    16750  14063  15070  -4289   -569   2798       N  
ATOM   4493  CA  LYS B 130       3.340  47.649  34.472  1.00122.47           C  
ANISOU 4493  CA  LYS B 130    16662  13992  15879  -4482   -579   2873       C  
ATOM   4494  C   LYS B 130       3.345  48.246  35.882  1.00124.91           C  
ANISOU 4494  C   LYS B 130    16887  14196  16378  -4578  -1089   2649       C  
ATOM   4495  O   LYS B 130       4.405  48.413  36.488  1.00129.83           O  
ANISOU 4495  O   LYS B 130    17171  14651  17506  -4717  -1267   2612       O  
ATOM   4496  CB  LYS B 130       3.300  48.780  33.444  1.00125.62           C  
ANISOU 4496  CB  LYS B 130    17203  14175  16353  -4531   -259   3094       C  
ATOM   4497  CG  LYS B 130       4.621  49.522  33.298  1.00139.17           C  
ANISOU 4497  CG  LYS B 130    18556  15578  18743  -4742    -86   3251       C  
ATOM   4498  CD  LYS B 130       5.667  48.598  32.698  1.00141.10           C  
ANISOU 4498  CD  LYS B 130    18507  15867  19239  -4743    295   3392       C  
ATOM   4499  CE  LYS B 130       6.985  49.303  32.430  1.00146.17           C  
ANISOU 4499  CE  LYS B 130    18740  16185  20611  -4957    556   3572       C  
ATOM   4500  NZ  LYS B 130       7.961  48.354  31.824  1.00145.20           N1+
ANISOU 4500  NZ  LYS B 130    18318  16116  20736  -4929    972   3697       N1+
ATOM   4501  N   VAL B 131       2.164  48.573  36.398  1.00116.23           N  
ANISOU 4501  N   VAL B 131    16097  13178  14886  -4494  -1331   2489       N  
ATOM   4502  CA  VAL B 131       2.053  49.145  37.739  1.00125.98           C  
ANISOU 4502  CA  VAL B 131    17342  14316  16208  -4550  -1795   2257       C  
ATOM   4503  C   VAL B 131       2.464  48.131  38.807  1.00130.98           C  
ANISOU 4503  C   VAL B 131    17850  15075  16841  -4531  -2094   2090       C  
ATOM   4504  O   VAL B 131       3.009  48.495  39.850  1.00136.93           O  
ANISOU 4504  O   VAL B 131    18494  15678  17856  -4614  -2476   1939       O  
ATOM   4505  CB  VAL B 131       0.629  49.651  38.036  1.00118.89           C  
ANISOU 4505  CB  VAL B 131    16811  13491  14869  -4433  -1927   2115       C  
ATOM   4506  CG1 VAL B 131       0.660  50.635  39.192  1.00133.37           C  
ANISOU 4506  CG1 VAL B 131    18678  15125  16873  -4505  -2328   1913       C  
ATOM   4507  CG2 VAL B 131       0.050  50.336  36.825  1.00109.45           C  
ANISOU 4507  CG2 VAL B 131    15799  12230  13557  -4385  -1625   2293       C  
ATOM   4508  N   VAL B 132       2.191  46.859  38.543  1.00122.02           N  
ANISOU 4508  N   VAL B 132    16764  14196  15401  -4413  -1945   2112       N  
ATOM   4509  CA  VAL B 132       2.552  45.795  39.467  1.00110.73           C  
ANISOU 4509  CA  VAL B 132    15256  12880  13936  -4377  -2200   1985       C  
ATOM   4510  C   VAL B 132       4.070  45.666  39.566  1.00111.09           C  
ANISOU 4510  C   VAL B 132    14886  12756  14569  -4489  -2277   2043       C  
ATOM   4511  O   VAL B 132       4.615  45.515  40.661  1.00122.38           O  
ANISOU 4511  O   VAL B 132    16218  14110  16170  -4517  -2690   1892       O  
ATOM   4512  CB  VAL B 132       1.947  44.441  39.032  1.00111.70           C  
ANISOU 4512  CB  VAL B 132    15514  13283  13644  -4233  -1989   2018       C  
ATOM   4513  CG1 VAL B 132       2.432  43.316  39.937  1.00106.84           C  
ANISOU 4513  CG1 VAL B 132    14820  12748  13025  -4197  -2239   1919       C  
ATOM   4514  CG2 VAL B 132       0.432  44.512  39.033  1.00114.01           C  
ANISOU 4514  CG2 VAL B 132    16160  13731  13427  -4128  -1957   1935       C  
ATOM   4515  N   LYS B 133       4.753  45.723  38.425  1.00110.48           N  
ANISOU 4515  N   LYS B 133    14569  12605  14804  -4541  -1879   2257       N  
ATOM   4516  CA  LYS B 133       6.212  45.650  38.412  1.00123.24           C  
ANISOU 4516  CA  LYS B 133    15718  14038  17068  -4653  -1883   2324       C  
ATOM   4517  C   LYS B 133       6.851  46.849  39.109  1.00144.74           C  
ANISOU 4517  C   LYS B 133    18240  16450  20303  -4830  -2224   2242       C  
ATOM   4518  O   LYS B 133       7.812  46.693  39.864  1.00153.42           O  
ANISOU 4518  O   LYS B 133    19030  17415  21848  -4895  -2572   2141       O  
ATOM   4519  CB  LYS B 133       6.744  45.537  36.983  1.00123.85           C  
ANISOU 4519  CB  LYS B 133    15613  14088  17357  -4668  -1293   2583       C  
ATOM   4520  CG  LYS B 133       6.078  44.464  36.140  1.00111.54           C  
ANISOU 4520  CG  LYS B 133    14302  12802  15278  -4486   -946   2661       C  
ATOM   4521  CD  LYS B 133       6.903  44.185  34.893  1.00117.93           C  
ANISOU 4521  CD  LYS B 133    14893  13559  16357  -4482   -394   2889       C  
ATOM   4522  CE  LYS B 133       8.372  43.979  35.272  1.00130.10           C  
ANISOU 4522  CE  LYS B 133    15883  14932  18616  -4582   -462   2891       C  
ATOM   4523  NZ  LYS B 133       9.292  44.062  34.104  1.00136.56           N1+
ANISOU 4523  NZ  LYS B 133    16425  15620  19842  -4624    131   3127       N1+
ATOM   4524  N   GLU B 134       6.325  48.042  38.843  1.00154.53           N  
ANISOU 4524  N   GLU B 134    19658  17555  21501  -4900  -2153   2278       N  
ATOM   4525  CA  GLU B 134       6.823  49.248  39.493  1.00160.53           C  
ANISOU 4525  CA  GLU B 134    20275  17994  22726  -5069  -2492   2184       C  
ATOM   4526  C   GLU B 134       6.640  49.192  40.992  1.00144.93           C  
ANISOU 4526  C   GLU B 134    18446  16016  20604  -5026  -3121   1887       C  
ATOM   4527  O   GLU B 134       7.456  49.720  41.739  1.00141.87           O  
ANISOU 4527  O   GLU B 134    17833  15371  20700  -5147  -3529   1763       O  
ATOM   4528  CB  GLU B 134       6.123  50.507  38.978  1.00171.53           C  
ANISOU 4528  CB  GLU B 134    21914  19246  24014  -5120  -2323   2263       C  
ATOM   4529  CG  GLU B 134       6.629  51.059  37.666  1.00183.36           C  
ANISOU 4529  CG  GLU B 134    23239  20569  25858  -5233  -1792   2562       C  
ATOM   4530  CD  GLU B 134       6.128  52.466  37.418  1.00192.23           C  
ANISOU 4530  CD  GLU B 134    24581  21456  27002  -5311  -1766   2613       C  
ATOM   4531  OE1 GLU B 134       5.046  52.807  37.937  1.00193.52           O  
ANISOU 4531  OE1 GLU B 134    25114  21698  26715  -5204  -2021   2445       O  
ATOM   4532  OE2 GLU B 134       6.816  53.231  36.708  1.00196.90           O1-
ANISOU 4532  OE2 GLU B 134    24972  21767  28074  -5477  -1473   2825       O1-
ATOM   4533  N   PHE B 135       5.561  48.563  41.432  1.00136.35           N  
ANISOU 4533  N   PHE B 135    17754  15199  18855  -4853  -3199   1769       N  
ATOM   4534  CA  PHE B 135       5.323  48.456  42.855  1.00135.86           C  
ANISOU 4534  CA  PHE B 135    17914  15142  18565  -4789  -3736   1500       C  
ATOM   4535  C   PHE B 135       6.288  47.486  43.537  1.00137.92           C  
ANISOU 4535  C   PHE B 135    17949  15404  19049  -4768  -4056   1428       C  
ATOM   4536  O   PHE B 135       6.861  47.812  44.575  1.00141.09           O  
ANISOU 4536  O   PHE B 135    18312  15610  19686  -4808  -4583   1243       O  
ATOM   4537  CB  PHE B 135       3.884  48.046  43.136  1.00146.10           C  
ANISOU 4537  CB  PHE B 135    19683  16710  19120  -4616  -3666   1410       C  
ATOM   4538  CG  PHE B 135       3.526  48.159  44.574  1.00163.42           C  
ANISOU 4538  CG  PHE B 135    22184  18875  21032  -4546  -4142   1143       C  
ATOM   4539  CD1 PHE B 135       3.345  49.401  45.144  1.00178.41           C  
ANISOU 4539  CD1 PHE B 135    24233  20551  23003  -4593  -4408    987       C  
ATOM   4540  CD2 PHE B 135       3.409  47.037  45.369  1.00163.09           C  
ANISOU 4540  CD2 PHE B 135    22313  19004  20650  -4428  -4325   1049       C  
ATOM   4541  CE1 PHE B 135       3.039  49.521  46.470  1.00181.42           C  
ANISOU 4541  CE1 PHE B 135    24947  20892  23092  -4509  -4831    730       C  
ATOM   4542  CE2 PHE B 135       3.098  47.161  46.693  1.00171.04           C  
ANISOU 4542  CE2 PHE B 135    23666  19967  21355  -4351  -4734    815       C  
ATOM   4543  CZ  PHE B 135       2.926  48.407  47.249  1.00178.14           C  
ANISOU 4543  CZ  PHE B 135    24727  20651  22306  -4386  -4988    648       C  
ATOM   4544  N   VAL B 136       6.475  46.302  42.959  1.00135.03           N  
ANISOU 4544  N   VAL B 136    17454  15240  18613  -4692  -3774   1561       N  
ATOM   4545  CA  VAL B 136       7.349  45.293  43.564  1.00139.53           C  
ANISOU 4545  CA  VAL B 136    17821  15813  19380  -4642  -4074   1500       C  
ATOM   4546  C   VAL B 136       8.794  45.810  43.578  1.00142.79           C  
ANISOU 4546  C   VAL B 136    17700  15914  20638  -4799  -4281   1510       C  
ATOM   4547  O   VAL B 136       9.631  45.336  44.350  1.00140.70           O  
ANISOU 4547  O   VAL B 136    17244  15549  20665  -4776  -4727   1395       O  
ATOM   4548  CB  VAL B 136       7.265  43.931  42.824  1.00121.49           C  
ANISOU 4548  CB  VAL B 136    15491  13784  16884  -4523  -3688   1648       C  
ATOM   4549  CG1 VAL B 136       7.927  44.016  41.458  1.00124.12           C  
ANISOU 4549  CG1 VAL B 136    15433  14068  17660  -4600  -3170   1878       C  
ATOM   4550  CG2 VAL B 136       7.898  42.823  43.653  1.00119.59           C  
ANISOU 4550  CG2 VAL B 136    15177  13565  16696  -4425  -4065   1553       C  
ATOM   4551  N   SER B 137       9.066  46.790  42.720  1.00142.64           N  
ANISOU 4551  N   SER B 137    17445  15725  21028  -4956  -3962   1652       N  
ATOM   4552  CA  SER B 137      10.360  47.464  42.655  1.00151.91           C  
ANISOU 4552  CA  SER B 137    18084  16562  23074  -5146  -4091   1677       C  
ATOM   4553  C   SER B 137      10.678  48.225  43.949  1.00154.66           C  
ANISOU 4553  C   SER B 137    18465  16643  23655  -5215  -4819   1412       C  
ATOM   4554  O   SER B 137      11.837  48.314  44.355  1.00156.17           O  
ANISOU 4554  O   SER B 137    18220  16584  24535  -5311  -5185   1336       O  
ATOM   4555  CB  SER B 137      10.398  48.412  41.458  1.00152.64           C  
ANISOU 4555  CB  SER B 137    18023  16519  23455  -5300  -3540   1907       C  
ATOM   4556  OG  SER B 137       9.802  47.811  40.321  1.00152.69           O  
ANISOU 4556  OG  SER B 137    18191  16787  23039  -5195  -2914   2118       O  
ATOM   4557  N   VAL B 138       9.651  48.810  44.561  1.00158.32           N  
ANISOU 4557  N   VAL B 138    19441  17141  23574  -5161  -5024   1262       N  
ATOM   4558  CA  VAL B 138       9.812  49.578  45.795  1.00168.41           C  
ANISOU 4558  CA  VAL B 138    20867  18166  24957  -5197  -5705    987       C  
ATOM   4559  C   VAL B 138      10.377  48.711  46.924  1.00181.37           C  
ANISOU 4559  C   VAL B 138    22524  19804  26585  -5080  -6309    792       C  
ATOM   4560  O   VAL B 138      11.453  48.992  47.458  1.00195.80           O  
ANISOU 4560  O   VAL B 138    24013  21337  29045  -5171  -6814    667       O  
ATOM   4561  CB  VAL B 138       8.467  50.194  46.250  1.00157.08           C  
ANISOU 4561  CB  VAL B 138    20045  16818  22822  -5104  -5742    854       C  
ATOM   4562  CG1 VAL B 138       8.617  50.882  47.603  1.00167.48           C  
ANISOU 4562  CG1 VAL B 138    21594  17881  24161  -5099  -6460    539       C  
ATOM   4563  CG2 VAL B 138       7.943  51.160  45.200  1.00140.95           C  
ANISOU 4563  CG2 VAL B 138    18001  14722  20832  -5208  -5242   1029       C  
ATOM   4564  N   GLY B 139       9.644  47.660  47.281  1.00189.36           N  
ANISOU 4564  N   GLY B 139    23934  21121  26892  -4877  -6273    768       N  
ATOM   4565  CA  GLY B 139      10.131  46.656  48.212  1.00174.21           C  
ANISOU 4565  CA  GLY B 139    22076  19226  24889  -4738  -6761    639       C  
ATOM   4566  C   GLY B 139      10.155  47.051  49.676  1.00171.66           C  
ANISOU 4566  C   GLY B 139    22136  18714  24373  -4668  -7516    339       C  
ATOM   4567  O   GLY B 139      10.338  46.194  50.544  1.00157.31           O  
ANISOU 4567  O   GLY B 139    20539  16942  22288  -4495  -7903    233       O  
ATOM   4568  N   GLY B 140       9.955  48.335  49.958  1.00190.43           N  
ANISOU 4568  N   GLY B 140    24640  20889  26825  -4734  -7656    208       N  
ATOM   4569  CA  GLY B 140       9.976  48.818  51.327  1.00194.52           C  
ANISOU 4569  CA  GLY B 140    25557  21268  27083  -4516  -8156    -67       C  
ATOM   4570  C   GLY B 140       8.791  48.272  52.092  1.00184.01           C  
ANISOU 4570  C   GLY B 140    24941  20174  24801  -4312  -8147   -158       C  
ATOM   4571  O   GLY B 140       8.941  47.659  53.148  1.00189.16           O  
ANISOU 4571  O   GLY B 140    25909  20838  25124  -4079  -8477   -278       O  
ATOM   4572  N   VAL B 141       7.603  48.496  51.545  1.00173.48           N  
ANISOU 4572  N   VAL B 141    23864  19015  23035  -4395  -7733    -87       N  
ATOM   4573  CA  VAL B 141       6.386  47.890  52.065  1.00169.15           C  
ANISOU 4573  CA  VAL B 141    23924  18729  21617  -4226  -7576   -132       C  
ATOM   4574  C   VAL B 141       5.632  47.357  50.857  1.00166.71           C  
ANISOU 4574  C   VAL B 141    23480  18723  21139  -4270  -6869    122       C  
ATOM   4575  O   VAL B 141       4.435  47.595  50.694  1.00162.60           O  
ANISOU 4575  O   VAL B 141    23266  18367  20146  -4213  -6498    128       O  
ATOM   4576  CB  VAL B 141       5.501  48.887  52.858  1.00171.29           C  
ANISOU 4576  CB  VAL B 141    24706  18933  21444  -4094  -7616   -341       C  
ATOM   4577  CG1 VAL B 141       4.453  48.136  53.678  1.00167.07           C  
ANISOU 4577  CG1 VAL B 141    24781  18631  20067  -3861  -7472   -403       C  
ATOM   4578  CG2 VAL B 141       6.347  49.756  53.777  1.00177.57           C  
ANISOU 4578  CG2 VAL B 141    25490  19406  22572  -3997  -8115   -550       C  
ATOM   4579  N   SER B 142       6.352  46.652  49.990  1.00165.82           N  
ANISOU 4579  N   SER B 142    22886  18677  21442  -4337  -6654    328       N  
ATOM   4580  CA  SER B 142       5.746  46.134  48.776  1.00159.51           C  
ANISOU 4580  CA  SER B 142    21949  18147  20511  -4344  -5977    568       C  
ATOM   4581  C   SER B 142       4.681  45.107  49.135  1.00188.36           C  
ANISOU 4581  C   SER B 142    26049  22092  23426  -4175  -5783    571       C  
ATOM   4582  O   SER B 142       3.518  45.266  48.765  1.00193.55           O  
ANISOU 4582  O   SER B 142    26930  22922  23690  -4140  -5385    606       O  
ATOM   4583  CB  SER B 142       6.802  45.513  47.855  1.00149.54           C  
ANISOU 4583  CB  SER B 142    20119  16878  19821  -4422  -5798    766       C  
ATOM   4584  OG  SER B 142       7.468  44.433  48.486  1.00146.74           O  
ANISOU 4584  OG  SER B 142    19733  16533  19487  -4324  -6138    725       O  
ATOM   4585  N   ILE B 143       5.072  44.085  49.893  1.00215.31           N  
ANISOU 4585  N   ILE B 143    29597  25532  26679  -4069  -6085    528       N  
ATOM   4586  CA  ILE B 143       4.149  43.022  50.269  1.00208.63           C  
ANISOU 4586  CA  ILE B 143    29166  24929  25175  -3924  -5895    552       C  
ATOM   4587  C   ILE B 143       3.443  42.525  49.009  1.00199.82           C  
ANISOU 4587  C   ILE B 143    27885  24065  23973  -3947  -5250    757       C  
ATOM   4588  O   ILE B 143       2.213  42.557  48.938  1.00199.61           O  
ANISOU 4588  O   ILE B 143    28145  24202  23494  -3901  -4930    752       O  
ATOM   4589  CB  ILE B 143       3.105  43.498  51.315  1.00205.18           C  
ANISOU 4589  CB  ILE B 143    29327  24499  24133  -3829  -5989    366       C  
ATOM   4590  CG1 ILE B 143       3.755  44.396  52.372  1.00211.86           C  
ANISOU 4590  CG1 ILE B 143    30338  25048  25110  -3822  -6616    133       C  
ATOM   4591  CG2 ILE B 143       2.398  42.313  51.966  1.00200.00           C  
ANISOU 4591  CG2 ILE B 143    29113  24024  22856  -3684  -5885    384       C  
ATOM   4592  CD1 ILE B 143       4.669  43.658  53.335  1.00211.70           C  
ANISOU 4592  CD1 ILE B 143    30434  24901  25100  -3705  -7146     63       C  
ATOM   4593  N   PRO B 144       4.219  42.121  47.986  1.00190.91           N  
ANISOU 4593  N   PRO B 144    26285  22948  23302  -4011  -5060    926       N  
ATOM   4594  CA  PRO B 144       3.609  41.852  46.681  1.00172.74           C  
ANISOU 4594  CA  PRO B 144    23844  20844  20945  -4031  -4474   1105       C  
ATOM   4595  C   PRO B 144       2.579  40.735  46.782  1.00166.90           C  
ANISOU 4595  C   PRO B 144    23426  20348  19641  -3918  -4239   1136       C  
ATOM   4596  O   PRO B 144       2.927  39.589  47.053  1.00172.30           O  
ANISOU 4596  O   PRO B 144    24131  21081  20253  -3846  -4329   1173       O  
ATOM   4597  CB  PRO B 144       4.805  41.440  45.824  1.00171.82           C  
ANISOU 4597  CB  PRO B 144    23223  20668  21392  -4085  -4380   1253       C  
ATOM   4598  CG  PRO B 144       5.749  40.823  46.803  1.00188.95           C  
ANISOU 4598  CG  PRO B 144    25352  22715  23725  -4028  -4883   1163       C  
ATOM   4599  CD  PRO B 144       5.636  41.711  48.012  1.00194.15           C  
ANISOU 4599  CD  PRO B 144    26307  23206  24255  -4034  -5361    955       C  
ATOM   4600  N   ARG B 145       1.316  41.085  46.569  1.00145.05           N  
ANISOU 4600  N   ARG B 145    20892  17709  16512  -3902  -3949   1118       N  
ATOM   4601  CA  ARG B 145       0.210  40.156  46.768  1.00136.53           C  
ANISOU 4601  CA  ARG B 145    20116  16831  14929  -3815  -3728   1123       C  
ATOM   4602  C   ARG B 145      -0.197  39.454  45.476  1.00139.85           C  
ANISOU 4602  C   ARG B 145    20361  17423  15353  -3812  -3297   1280       C  
ATOM   4603  O   ARG B 145      -0.065  40.014  44.389  1.00144.08           O  
ANISOU 4603  O   ARG B 145    20656  17948  16140  -3864  -3084   1368       O  
ATOM   4604  CB  ARG B 145      -0.992  40.909  47.352  1.00144.97           C  
ANISOU 4604  CB  ARG B 145    21523  17927  15632  -3785  -3667    986       C  
ATOM   4605  CG  ARG B 145      -2.116  40.037  47.878  1.00144.62           C  
ANISOU 4605  CG  ARG B 145    21815  18042  15092  -3705  -3477    962       C  
ATOM   4606  CD  ARG B 145      -1.949  39.736  49.363  1.00144.72           C  
ANISOU 4606  CD  ARG B 145    22215  17971  14802  -3634  -3794    848       C  
ATOM   4607  NE  ARG B 145      -2.103  40.929  50.195  1.00152.10           N  
ANISOU 4607  NE  ARG B 145    23384  18768  15639  -3613  -4011    666       N  
ATOM   4608  CZ  ARG B 145      -3.228  41.270  50.818  1.00157.79           C  
ANISOU 4608  CZ  ARG B 145    24448  19533  15972  -3549  -3842    549       C  
ATOM   4609  NH1 ARG B 145      -4.308  40.507  50.710  1.00158.88           N  
ANISOU 4609  NH1 ARG B 145    24699  19846  15823  -3518  -3452    605       N  
ATOM   4610  NH2 ARG B 145      -3.273  42.374  51.552  1.00159.17           N  
ANISOU 4610  NH2 ARG B 145    24842  19561  16074  -3515  -4057    368       N  
ATOM   4611  N   LEU B 146      -0.664  38.213  45.599  1.00147.80           N  
ANISOU 4611  N   LEU B 146    21519  18565  16076  -3748  -3179   1317       N  
ATOM   4612  CA  LEU B 146      -1.207  37.473  44.462  1.00161.45           C  
ANISOU 4612  CA  LEU B 146    23149  20448  17748  -3731  -2807   1430       C  
ATOM   4613  C   LEU B 146      -2.334  38.289  43.845  1.00157.60           C  
ANISOU 4613  C   LEU B 146    22708  20031  17142  -3745  -2556   1405       C  
ATOM   4614  O   LEU B 146      -2.524  38.313  42.630  1.00155.14           O  
ANISOU 4614  O   LEU B 146    22248  19777  16921  -3744  -2307   1494       O  
ATOM   4615  CB  LEU B 146      -1.705  36.086  44.889  1.00177.51           C  
ANISOU 4615  CB  LEU B 146    25391  22581  19473  -3672  -2752   1445       C  
ATOM   4616  CG  LEU B 146      -2.792  35.949  45.958  1.00190.04           C  
ANISOU 4616  CG  LEU B 146    27353  24211  20643  -3649  -2747   1350       C  
ATOM   4617  CD1 LEU B 146      -4.176  35.806  45.332  1.00187.03           C  
ANISOU 4617  CD1 LEU B 146    27008  23971  20083  -3654  -2391   1348       C  
ATOM   4618  CD2 LEU B 146      -2.483  34.771  46.869  1.00200.26           C  
ANISOU 4618  CD2 LEU B 146    28868  25474  21749  -3599  -2907   1374       C  
ATOM   4619  N   ARG B 147      -3.083  38.949  44.721  1.00147.54           N  
ANISOU 4619  N   ARG B 147    21669  18739  15651  -3737  -2637   1274       N  
ATOM   4620  CA  ARG B 147      -4.218  39.779  44.353  1.00131.50           C  
ANISOU 4620  CA  ARG B 147    19696  16752  13515  -3728  -2450   1216       C  
ATOM   4621  C   ARG B 147      -3.805  40.953  43.459  1.00121.14           C  
ANISOU 4621  C   ARG B 147    18182  15339  12507  -3771  -2430   1266       C  
ATOM   4622  O   ARG B 147      -4.577  41.401  42.615  1.00111.12           O  
ANISOU 4622  O   ARG B 147    16890  14114  11215  -3749  -2231   1288       O  
ATOM   4623  CB  ARG B 147      -4.906  40.273  45.630  1.00135.30           C  
ANISOU 4623  CB  ARG B 147    20473  17201  13733  -3695  -2555   1050       C  
ATOM   4624  CG  ARG B 147      -6.051  41.230  45.429  1.00130.60           C  
ANISOU 4624  CG  ARG B 147    19931  16623  13066  -3664  -2395    957       C  
ATOM   4625  CD  ARG B 147      -5.765  42.551  46.112  1.00115.47           C  
ANISOU 4625  CD  ARG B 147    18116  14539  11218  -3666  -2623    829       C  
ATOM   4626  NE  ARG B 147      -5.916  42.495  47.559  1.00103.27           N  
ANISOU 4626  NE  ARG B 147    16900  12951   9386  -3616  -2773    682       N  
ATOM   4627  CZ  ARG B 147      -5.279  43.303  48.399  1.00107.93           C  
ANISOU 4627  CZ  ARG B 147    17634  13366  10009  -3614  -3093    563       C  
ATOM   4628  NH1 ARG B 147      -4.437  44.215  47.932  1.00111.55           N  
ANISOU 4628  NH1 ARG B 147    17881  13670  10834  -3683  -3286    580       N  
ATOM   4629  NH2 ARG B 147      -5.474  43.194  49.704  1.00116.08           N  
ANISOU 4629  NH2 ARG B 147    19040  14358  10709  -3542  -3218    426       N  
ATOM   4630  N   THR B 148      -2.583  41.444  43.645  1.00129.08           N  
ANISOU 4630  N   THR B 148    19042  16186  13815  -3833  -2647   1287       N  
ATOM   4631  CA  THR B 148      -2.033  42.499  42.789  1.00125.75           C  
ANISOU 4631  CA  THR B 148    18409  15632  13737  -3899  -2599   1368       C  
ATOM   4632  C   THR B 148      -1.740  42.025  41.357  1.00115.82           C  
ANISOU 4632  C   THR B 148    16952  14437  12617  -3898  -2297   1556       C  
ATOM   4633  O   THR B 148      -2.184  42.634  40.383  1.00110.25           O  
ANISOU 4633  O   THR B 148    16244  13725  11922  -3889  -2091   1629       O  
ATOM   4634  CB  THR B 148      -0.737  43.089  43.403  1.00 91.58           C  
ANISOU 4634  CB  THR B 148    13930  11088   9777  -3985  -2920   1336       C  
ATOM   4635  OG1 THR B 148      -1.038  43.718  44.656  1.00100.95           O  
ANISOU 4635  OG1 THR B 148    15360  12185  10810  -3970  -3216   1144       O  
ATOM   4636  CG2 THR B 148      -0.118  44.112  42.476  1.00 88.29           C  
ANISOU 4636  CG2 THR B 148    13270  10510   9768  -4079  -2815   1450       C  
ATOM   4637  N   TYR B 149      -0.981  40.938  41.246  1.00115.62           N  
ANISOU 4637  N   TYR B 149    16794  14456  12679  -3889  -2283   1629       N  
ATOM   4638  CA  TYR B 149      -0.680  40.304  39.966  1.00103.28           C  
ANISOU 4638  CA  TYR B 149    15086  12958  11197  -3858  -1983   1786       C  
ATOM   4639  C   TYR B 149      -1.920  39.784  39.231  1.00101.43           C  
ANISOU 4639  C   TYR B 149    15035  12892  10612  -3771  -1751   1794       C  
ATOM   4640  O   TYR B 149      -1.889  39.598  38.017  1.00 71.11           O  
ANISOU 4640  O   TYR B 149    11157   9081   6782  -3730  -1500   1909       O  
ATOM   4641  CB  TYR B 149       0.312  39.155  40.170  1.00110.20           C  
ANISOU 4641  CB  TYR B 149    15802  13843  12225  -3839  -2047   1825       C  
ATOM   4642  CG  TYR B 149       1.772  39.551  40.130  1.00128.10           C  
ANISOU 4642  CG  TYR B 149    17742  15933  14998  -3913  -2132   1890       C  
ATOM   4643  CD1 TYR B 149       2.458  39.616  38.924  1.00139.16           C  
ANISOU 4643  CD1 TYR B 149    18910  17288  16677  -3924  -1813   2048       C  
ATOM   4644  CD2 TYR B 149       2.472  39.840  41.295  1.00135.14           C  
ANISOU 4644  CD2 TYR B 149    18557  16687  16103  -3965  -2528   1788       C  
ATOM   4645  CE1 TYR B 149       3.799  39.968  38.879  1.00141.82           C  
ANISOU 4645  CE1 TYR B 149    18889  17446  17550  -4003  -1846   2111       C  
ATOM   4646  CE2 TYR B 149       3.816  40.193  41.260  1.00132.04           C  
ANISOU 4646  CE2 TYR B 149    17805  16109  16255  -4040  -2636   1832       C  
ATOM   4647  CZ  TYR B 149       4.472  40.256  40.050  1.00129.99           C  
ANISOU 4647  CZ  TYR B 149    17260  15807  16323  -4068  -2274   1998       C  
ATOM   4648  OH  TYR B 149       5.804  40.606  40.013  1.00114.51           O  
ANISOU 4648  OH  TYR B 149    14890  13646  14971  -4155  -2340   2044       O  
ATOM   4649  N   ALA B 150      -2.994  39.519  39.972  1.00117.75           N  
ANISOU 4649  N   ALA B 150    17306  15053  12380  -3738  -1836   1667       N  
ATOM   4650  CA  ALA B 150      -4.161  38.816  39.426  1.00118.31           C  
ANISOU 4650  CA  ALA B 150    17504  15272  12177  -3665  -1665   1650       C  
ATOM   4651  C   ALA B 150      -4.882  39.526  38.262  1.00121.26           C  
ANISOU 4651  C   ALA B 150    17915  15649  12510  -3618  -1502   1689       C  
ATOM   4652  O   ALA B 150      -5.040  38.924  37.201  1.00134.42           O  
ANISOU 4652  O   ALA B 150    19593  17374  14105  -3556  -1340   1760       O  
ATOM   4653  CB  ALA B 150      -5.166  38.511  40.553  1.00117.70           C  
ANISOU 4653  CB  ALA B 150    17605  15264  11849  -3657  -1755   1507       C  
ATOM   4654  N   PRO B 151      -5.321  40.792  38.441  1.00106.70           N  
ANISOU 4654  N   PRO B 151    16121  13724  10697  -3631  -1566   1636       N  
ATOM   4655  CA  PRO B 151      -6.096  41.417  37.358  1.00101.95           C  
ANISOU 4655  CA  PRO B 151    15591  13112  10033  -3560  -1452   1671       C  
ATOM   4656  C   PRO B 151      -5.302  41.624  36.063  1.00 96.59           C  
ANISOU 4656  C   PRO B 151    14871  12356   9471  -3547  -1278   1857       C  
ATOM   4657  O   PRO B 151      -5.891  41.608  34.980  1.00 81.26           O  
ANISOU 4657  O   PRO B 151    13046  10438   7389  -3453  -1166   1907       O  
ATOM   4658  CB  PRO B 151      -6.512  42.762  37.958  1.00111.49           C  
ANISOU 4658  CB  PRO B 151    16852  14212  11298  -3576  -1579   1578       C  
ATOM   4659  CG  PRO B 151      -5.453  43.067  38.943  1.00115.97           C  
ANISOU 4659  CG  PRO B 151    17339  14676  12048  -3678  -1731   1560       C  
ATOM   4660  CD  PRO B 151      -5.072  41.745  39.539  1.00112.67           C  
ANISOU 4660  CD  PRO B 151    16890  14366  11553  -3692  -1764   1544       C  
ATOM   4661  N   ALA B 152      -3.995  41.844  36.181  1.00 95.63           N  
ANISOU 4661  N   ALA B 152    14595  12128   9614  -3634  -1257   1955       N  
ATOM   4662  CA  ALA B 152      -3.132  41.998  35.012  1.00 93.10           C  
ANISOU 4662  CA  ALA B 152    14215  11720   9438  -3632  -1016   2147       C  
ATOM   4663  C   ALA B 152      -3.153  40.735  34.157  1.00 97.14           C  
ANISOU 4663  C   ALA B 152    14780  12356   9772  -3532   -833   2199       C  
ATOM   4664  O   ALA B 152      -3.333  40.798  32.942  1.00 72.04           O  
ANISOU 4664  O   ALA B 152    11747   9164   6461  -3444   -635   2302       O  
ATOM   4665  CB  ALA B 152      -1.713  42.326  35.436  1.00 99.58           C  
ANISOU 4665  CB  ALA B 152    14783  12398  10654  -3756  -1031   2219       C  
ATOM   4666  N   LEU B 153      -2.959  39.591  34.805  1.00112.10           N  
ANISOU 4666  N   LEU B 153    16593  14353  11646  -3536   -914   2125       N  
ATOM   4667  CA  LEU B 153      -2.998  38.297  34.135  1.00107.85           C  
ANISOU 4667  CA  LEU B 153    16109  13919  10949  -3441   -778   2143       C  
ATOM   4668  C   LEU B 153      -4.396  37.962  33.633  1.00105.26           C  
ANISOU 4668  C   LEU B 153    16005  13689  10299  -3343   -804   2058       C  
ATOM   4669  O   LEU B 153      -4.566  37.503  32.504  1.00101.37           O  
ANISOU 4669  O   LEU B 153    15649  13217   9649  -3235   -659   2106       O  
ATOM   4670  CB  LEU B 153      -2.508  37.199  35.085  1.00 96.50           C  
ANISOU 4670  CB  LEU B 153    14548  12537   9582  -3471   -903   2080       C  
ATOM   4671  CG  LEU B 153      -2.539  35.751  34.597  1.00 79.22           C  
ANISOU 4671  CG  LEU B 153    12411  10436   7254  -3377   -806   2075       C  
ATOM   4672  CD1 LEU B 153      -1.294  35.008  35.038  1.00 77.54           C  
ANISOU 4672  CD1 LEU B 153    11995  10185   7281  -3390   -819   2113       C  
ATOM   4673  CD2 LEU B 153      -3.781  35.077  35.147  1.00 67.09           C  
ANISOU 4673  CD2 LEU B 153    11021   9004   5468  -3368   -953   1938       C  
ATOM   4674  N   LEU B 154      -5.392  38.206  34.480  1.00101.90           N  
ANISOU 4674  N   LEU B 154    15616  13310   9791  -3373   -993   1920       N  
ATOM   4675  CA  LEU B 154      -6.776  37.859  34.176  1.00 90.58           C  
ANISOU 4675  CA  LEU B 154    14319  11957   8140  -3297  -1049   1811       C  
ATOM   4676  C   LEU B 154      -7.280  38.585  32.943  1.00 91.50           C  
ANISOU 4676  C   LEU B 154    14592  12018   8154  -3193   -999   1862       C  
ATOM   4677  O   LEU B 154      -7.953  37.996  32.100  1.00100.17           O  
ANISOU 4677  O   LEU B 154    15823  13157   9079  -3087  -1003   1827       O  
ATOM   4678  CB  LEU B 154      -7.685  38.177  35.361  1.00 83.48           C  
ANISOU 4678  CB  LEU B 154    13398  11092   7229  -3350  -1204   1663       C  
ATOM   4679  CG  LEU B 154      -7.833  37.071  36.402  1.00 82.43           C  
ANISOU 4679  CG  LEU B 154    13229  11038   7051  -3405  -1252   1581       C  
ATOM   4680  CD1 LEU B 154      -8.964  37.392  37.363  1.00 89.22           C  
ANISOU 4680  CD1 LEU B 154    14114  11929   7857  -3430  -1323   1437       C  
ATOM   4681  CD2 LEU B 154      -8.079  35.750  35.720  1.00 78.28           C  
ANISOU 4681  CD2 LEU B 154    12740  10575   6426  -3353  -1189   1582       C  
ATOM   4682  N   CYS B 155      -6.946  39.865  32.842  1.00100.86           N  
ANISOU 4682  N   CYS B 155    15785  13089   9447  -3217   -979   1943       N  
ATOM   4683  CA  CYS B 155      -7.343  40.665  31.694  1.00107.67           C  
ANISOU 4683  CA  CYS B 155    16843  13863  10203  -3111   -936   2021       C  
ATOM   4684  C   CYS B 155      -6.665  40.151  30.436  1.00 70.89           C  
ANISOU 4684  C   CYS B 155    12325   9181   5429  -3025   -714   2169       C  
ATOM   4685  O   CYS B 155      -7.308  39.957  29.416  1.00 71.56           O  
ANISOU 4685  O   CYS B 155    12646   9265   5280  -2882   -725   2167       O  
ATOM   4686  CB  CYS B 155      -6.987  42.131  31.921  1.00132.96           C  
ANISOU 4686  CB  CYS B 155    20025  16913  13579  -3175   -941   2097       C  
ATOM   4687  SG  CYS B 155      -7.601  43.251  30.659  1.00 94.02           S  
ANISOU 4687  SG  CYS B 155    15381  11837   8507  -3037   -932   2197       S  
ATOM   4688  N   PHE B 156      -5.364  39.899  30.537  1.00 71.55           N  
ANISOU 4688  N   PHE B 156    12266   9236   5685  -3101   -521   2284       N  
ATOM   4689  CA  PHE B 156      -4.574  39.334  29.442  1.00 96.16           C  
ANISOU 4689  CA  PHE B 156    15486  12327   8725  -3017   -239   2422       C  
ATOM   4690  C   PHE B 156      -5.072  37.973  28.979  1.00 95.18           C  
ANISOU 4690  C   PHE B 156    15491  12318   8355  -2897   -269   2321       C  
ATOM   4691  O   PHE B 156      -4.899  37.602  27.819  1.00 88.61           O  
ANISOU 4691  O   PHE B 156    14889  11458   7321  -2761    -89   2393       O  
ATOM   4692  CB  PHE B 156      -3.104  39.231  29.855  1.00103.20           C  
ANISOU 4692  CB  PHE B 156    16100  13167   9943  -3130    -51   2527       C  
ATOM   4693  CG  PHE B 156      -2.294  40.459  29.542  1.00115.99           C  
ANISOU 4693  CG  PHE B 156    17669  14610  11792  -3205    147   2709       C  
ATOM   4694  CD1 PHE B 156      -2.727  41.365  28.581  1.00132.42           C  
ANISOU 4694  CD1 PHE B 156    20037  16583  13695  -3129    252   2822       C  
ATOM   4695  CD2 PHE B 156      -1.111  40.719  30.219  1.00109.45           C  
ANISOU 4695  CD2 PHE B 156    16508  13696  11380  -3353    205   2767       C  
ATOM   4696  CE1 PHE B 156      -1.980  42.490  28.279  1.00135.24           C  
ANISOU 4696  CE1 PHE B 156    20362  16746  14277  -3213    463   3011       C  
ATOM   4697  CE2 PHE B 156      -0.359  41.843  29.924  1.00117.22           C  
ANISOU 4697  CE2 PHE B 156    17413  14487  12638  -3446    397   2936       C  
ATOM   4698  CZ  PHE B 156      -0.795  42.729  28.952  1.00129.34           C  
ANISOU 4698  CZ  PHE B 156    19247  15911  13984  -3383    550   3068       C  
ATOM   4699  N   CYS B 157      -5.642  37.208  29.901  1.00110.93           N  
ANISOU 4699  N   CYS B 157    17358  14422  10369  -2947   -481   2157       N  
ATOM   4700  CA  CYS B 157      -6.222  35.913  29.569  1.00112.66           C  
ANISOU 4700  CA  CYS B 157    17679  14724  10401  -2859   -548   2044       C  
ATOM   4701  C   CYS B 157      -7.547  36.044  28.811  1.00108.89           C  
ANISOU 4701  C   CYS B 157    17442  14245   9687  -2737   -721   1947       C  
ATOM   4702  O   CYS B 157      -7.784  35.351  27.819  1.00 98.62           O  
ANISOU 4702  O   CYS B 157    16363  12937   8172  -2599   -713   1919       O  
ATOM   4703  CB  CYS B 157      -6.395  35.078  30.834  1.00 67.99           C  
ANISOU 4703  CB  CYS B 157    11818   9153   4862  -2968   -694   1924       C  
ATOM   4704  SG  CYS B 157      -4.884  34.164  31.226  1.00106.94           S  
ANISOU 4704  SG  CYS B 157    16569  14084   9980  -3007   -536   2004       S  
ATOM   4705  N   GLU B 158      -8.413  36.927  29.294  1.00116.86           N  
ANISOU 4705  N   GLU B 158    18406  15245  10751  -2776   -903   1879       N  
ATOM   4706  CA  GLU B 158      -9.701  37.165  28.657  1.00 99.05           C  
ANISOU 4706  CA  GLU B 158    16322  12967   8344  -2655  -1116   1774       C  
ATOM   4707  C   GLU B 158      -9.509  37.743  27.254  1.00102.70           C  
ANISOU 4707  C   GLU B 158    17121  13319   8581  -2492  -1039   1902       C  
ATOM   4708  O   GLU B 158     -10.270  37.441  26.332  1.00 86.16           O  
ANISOU 4708  O   GLU B 158    15271  11195   6270  -2334  -1198   1828       O  
ATOM   4709  CB  GLU B 158     -10.545  38.108  29.515  1.00 90.30           C  
ANISOU 4709  CB  GLU B 158    15067  11856   7388  -2719  -1287   1684       C  
ATOM   4710  CG  GLU B 158     -11.936  38.400  28.980  1.00122.17           C  
ANISOU 4710  CG  GLU B 158    19206  15859  11355  -2591  -1542   1552       C  
ATOM   4711  CD  GLU B 158     -12.926  37.287  29.254  1.00154.60           C  
ANISOU 4711  CD  GLU B 158    23189  20043  15509  -2602  -1704   1358       C  
ATOM   4712  OE1 GLU B 158     -12.506  36.117  29.377  1.00170.53           O  
ANISOU 4712  OE1 GLU B 158    25171  22119  17503  -2654  -1617   1349       O  
ATOM   4713  OE2 GLU B 158     -14.135  37.586  29.341  1.00172.38           O  
ANISOU 4713  OE2 GLU B 158    25363  22278  17855  -2557  -1916   1212       O  
ATOM   4714  N   LYS B 159      -8.457  38.544  27.099  1.00108.58           N  
ANISOU 4714  N   LYS B 159    17891  13984   9382  -2530   -793   2098       N  
ATOM   4715  CA  LYS B 159      -8.124  39.191  25.832  1.00 97.17           C  
ANISOU 4715  CA  LYS B 159    16791  12406   7723  -2392   -633   2269       C  
ATOM   4716  C   LYS B 159      -7.397  38.209  24.911  1.00 89.37           C  
ANISOU 4716  C   LYS B 159    16003  11424   6531  -2285   -385   2337       C  
ATOM   4717  O   LYS B 159      -7.057  38.533  23.773  1.00108.02           O  
ANISOU 4717  O   LYS B 159    18715  13678   8651  -2146   -189   2484       O  
ATOM   4718  CB  LYS B 159      -7.257  40.432  26.097  1.00108.59           C  
ANISOU 4718  CB  LYS B 159    18148  13737   9375  -2505   -426   2460       C  
ATOM   4719  CG  LYS B 159      -7.122  41.409  24.934  1.00124.72           C  
ANISOU 4719  CG  LYS B 159    20564  15602  11221  -2384   -279   2656       C  
ATOM   4720  CD  LYS B 159      -6.029  42.444  25.194  1.00127.60           C  
ANISOU 4720  CD  LYS B 159    20792  15831  11861  -2534      0   2866       C  
ATOM   4721  CE  LYS B 159      -6.301  43.249  26.455  1.00117.96           C  
ANISOU 4721  CE  LYS B 159    19264  14601  10956  -2695   -224   2773       C  
ATOM   4722  NZ  LYS B 159      -5.222  44.236  26.736  1.00109.85           N  
ANISOU 4722  NZ  LYS B 159    18084  13412  10243  -2855     -1   2954       N  
ATOM   4723  N   LEU B 160      -7.152  37.014  25.437  1.00 89.32           N  
ANISOU 4723  N   LEU B 160    15793  11529   6616  -2341   -379   2233       N  
ATOM   4724  CA  LEU B 160      -6.558  35.898  24.702  1.00 90.60           C  
ANISOU 4724  CA  LEU B 160    16110  11704   6611  -2230   -182   2244       C  
ATOM   4725  C   LEU B 160      -5.106  36.141  24.307  1.00 95.32           C  
ANISOU 4725  C   LEU B 160    16700  12231   7287  -2236    271   2461       C  
ATOM   4726  O   LEU B 160      -4.576  35.461  23.429  1.00 90.12           O  
ANISOU 4726  O   LEU B 160    16256  11546   6437  -2096    515   2503       O  
ATOM   4727  CB  LEU B 160      -7.381  35.565  23.453  1.00 80.43           C  
ANISOU 4727  CB  LEU B 160    15274  10364   4921  -2003   -331   2166       C  
ATOM   4728  CG  LEU B 160      -8.654  34.742  23.663  1.00 82.34           C  
ANISOU 4728  CG  LEU B 160    15493  10669   5125  -1976   -745   1913       C  
ATOM   4729  CD1 LEU B 160      -9.145  34.172  22.348  1.00 80.39           C  
ANISOU 4729  CD1 LEU B 160    15606  10345   4593  -1706   -859   1796       C  
ATOM   4730  CD2 LEU B 160      -8.429  33.627  24.675  1.00109.51           C  
ANISOU 4730  CD2 LEU B 160    18589  14215   8805  -2120   -750   1809       C  
ATOM   4731  N   GLU B 161      -4.456  37.092  24.968  1.00115.13           N  
ANISOU 4731  N   GLU B 161    18946  14695  10103  -2397    390   2588       N  
ATOM   4732  CA  GLU B 161      -3.026  37.289  24.777  1.00116.91           C  
ANISOU 4732  CA  GLU B 161    19039  14843  10539  -2445    815   2781       C  
ATOM   4733  C   GLU B 161      -2.282  36.303  25.662  1.00113.12           C  
ANISOU 4733  C   GLU B 161    18177  14450  10354  -2538    832   2707       C  
ATOM   4734  O   GLU B 161      -2.049  36.561  26.842  1.00114.26           O  
ANISOU 4734  O   GLU B 161    17972  14618  10822  -2710    676   2673       O  
ATOM   4735  CB  GLU B 161      -2.620  38.731  25.080  1.00117.75           C  
ANISOU 4735  CB  GLU B 161    19014  14824  10900  -2586    906   2941       C  
ATOM   4736  CG  GLU B 161      -3.139  39.734  24.060  1.00132.32           C  
ANISOU 4736  CG  GLU B 161    21282  16536  12456  -2473    962   3068       C  
ATOM   4737  CD  GLU B 161      -2.539  41.115  24.233  1.00154.61           C  
ANISOU 4737  CD  GLU B 161    23992  19191  15561  -2616   1133   3262       C  
ATOM   4738  OE1 GLU B 161      -1.781  41.320  25.203  1.00158.46           O  
ANISOU 4738  OE1 GLU B 161    24049  19669  16488  -2810   1154   3269       O  
ATOM   4739  OE2 GLU B 161      -2.825  41.996  23.394  1.00164.63           O  
ANISOU 4739  OE2 GLU B 161    25621  20315  16616  -2531   1222   3407       O  
ATOM   4740  N   ALA B 162      -1.913  35.171  25.075  1.00116.79           N  
ANISOU 4740  N   ALA B 162    18745  14944  10684  -2405   1002   2677       N  
ATOM   4741  CA  ALA B 162      -1.376  34.045  25.830  1.00118.03           C  
ANISOU 4741  CA  ALA B 162    18604  15175  11065  -2449    960   2582       C  
ATOM   4742  C   ALA B 162       0.003  34.336  26.401  1.00107.31           C  
ANISOU 4742  C   ALA B 162    16840  13760  10173  -2572   1183   2705       C  
ATOM   4743  O   ALA B 162       0.245  34.111  27.581  1.00 95.47           O  
ANISOU 4743  O   ALA B 162    15013  12300   8962  -2702    962   2635       O  
ATOM   4744  CB  ALA B 162      -1.326  32.800  24.957  1.00129.31           C  
ANISOU 4744  CB  ALA B 162    20279  16620  12232  -2251   1093   2512       C  
ATOM   4745  N   GLU B 163       0.913  34.812  25.558  1.00111.39           N  
ANISOU 4745  N   GLU B 163    17386  14166  10773  -2525   1621   2886       N  
ATOM   4746  CA  GLU B 163       2.284  35.056  25.992  1.00108.44           C  
ANISOU 4746  CA  GLU B 163    16576  13709  10918  -2638   1859   3000       C  
ATOM   4747  C   GLU B 163       2.353  36.106  27.094  1.00107.19           C  
ANISOU 4747  C   GLU B 163    16112  13506  11110  -2863   1601   3015       C  
ATOM   4748  O   GLU B 163       3.236  36.055  27.947  1.00100.37           O  
ANISOU 4748  O   GLU B 163    14829  12605  10701  -2980   1539   3009       O  
ATOM   4749  CB  GLU B 163       3.159  35.471  24.811  1.00123.20           C  
ANISOU 4749  CB  GLU B 163    18546  15444  12819  -2556   2440   3210       C  
ATOM   4750  CG  GLU B 163       4.550  34.857  24.852  1.00138.62           C  
ANISOU 4750  CG  GLU B 163    20112  17346  15213  -2542   2778   3259       C  
ATOM   4751  CD  GLU B 163       4.519  33.348  24.685  1.00147.27           C  
ANISOU 4751  CD  GLU B 163    21293  18537  16125  -2358   2752   3106       C  
ATOM   4752  OE1 GLU B 163       3.535  32.833  24.114  1.00156.86           O  
ANISOU 4752  OE1 GLU B 163    22958  19825  16816  -2211   2629   3007       O  
ATOM   4753  OE2 GLU B 163       5.476  32.674  25.122  1.00148.06           O  
ANISOU 4753  OE2 GLU B 163    21006  18621  16627  -2356   2828   3077       O  
ATOM   4754  N   LYS B 164       1.444  37.076  27.056  1.00117.80           N  
ANISOU 4754  N   LYS B 164    17676  14832  12250  -2908   1434   3026       N  
ATOM   4755  CA  LYS B 164       1.353  38.070  28.123  1.00124.24           C  
ANISOU 4755  CA  LYS B 164    18265  15601  13341  -3099   1151   3005       C  
ATOM   4756  C   LYS B 164       0.912  37.457  29.454  1.00115.46           C  
ANISOU 4756  C   LYS B 164    16984  14611  12273  -3165    709   2802       C  
ATOM   4757  O   LYS B 164       1.475  37.770  30.498  1.00130.93           O  
ANISOU 4757  O   LYS B 164    18634  16525  14590  -3306    530   2774       O  
ATOM   4758  CB  LYS B 164       0.417  39.218  27.727  1.00133.82           C  
ANISOU 4758  CB  LYS B 164    19781  16756  14310  -3099   1076   3051       C  
ATOM   4759  CG  LYS B 164       1.027  40.268  26.796  1.00138.08           C  
ANISOU 4759  CG  LYS B 164    20421  17104  14941  -3115   1472   3292       C  
ATOM   4760  CD  LYS B 164       1.314  39.753  25.395  1.00154.29           C  
ANISOU 4760  CD  LYS B 164    22782  19133  16707  -2929   1914   3421       C  
ATOM   4761  CE  LYS B 164       1.953  40.842  24.548  1.00163.07           C  
ANISOU 4761  CE  LYS B 164    24008  20029  17921  -2962   2355   3690       C  
ATOM   4762  NZ  LYS B 164       2.331  40.330  23.205  1.00174.44           N  
ANISOU 4762  NZ  LYS B 164    25782  21434  19064  -2767   2850   3825       N  
ATOM   4763  N   GLY B 165      -0.095  36.592  29.414  1.00100.81           N  
ANISOU 4763  N   GLY B 165    15354  12892  10059  -3063    531   2664       N  
ATOM   4764  CA  GLY B 165      -0.563  35.920  30.614  1.00 91.06           C  
ANISOU 4764  CA  GLY B 165    14010  11759   8829  -3119    178   2495       C  
ATOM   4765  C   GLY B 165       0.525  35.043  31.217  1.00 91.28           C  
ANISOU 4765  C   GLY B 165    13749  11781   9151  -3140    180   2486       C  
ATOM   4766  O   GLY B 165       0.676  34.964  32.439  1.00 96.72           O  
ANISOU 4766  O   GLY B 165    14259  12477  10012  -3237    -97   2409       O  
ATOM   4767  N   TYR B 166       1.286  34.389  30.348  1.00 79.69           N  
ANISOU 4767  N   TYR B 166    12262  10287   7729  -3028    489   2561       N  
ATOM   4768  CA  TYR B 166       2.377  33.516  30.756  1.00 81.73           C  
ANISOU 4768  CA  TYR B 166    12233  10521   8300  -3010    519   2555       C  
ATOM   4769  C   TYR B 166       3.471  34.350  31.408  1.00 87.55           C  
ANISOU 4769  C   TYR B 166    12584  11135   9547  -3150    495   2628       C  
ATOM   4770  O   TYR B 166       4.111  33.915  32.363  1.00101.89           O  
ANISOU 4770  O   TYR B 166    14133  12926  11654  -3192    267   2570       O  
ATOM   4771  CB  TYR B 166       2.933  32.744  29.555  1.00 98.72           C  
ANISOU 4771  CB  TYR B 166    14462  12654  10392  -2836    916   2615       C  
ATOM   4772  CG  TYR B 166       1.951  31.779  28.921  1.00101.56           C  
ANISOU 4772  CG  TYR B 166    15199  13106  10282  -2685    889   2513       C  
ATOM   4773  CD1 TYR B 166       0.637  31.691  29.369  1.00 99.58           C  
ANISOU 4773  CD1 TYR B 166    15152  12943   9741  -2725    552   2390       C  
ATOM   4774  CD2 TYR B 166       2.319  31.006  27.830  1.00104.32           C  
ANISOU 4774  CD2 TYR B 166    15706  13436  10496  -2499   1212   2531       C  
ATOM   4775  CE1 TYR B 166      -0.265  30.836  28.778  1.00 96.12           C  
ANISOU 4775  CE1 TYR B 166    15021  12560   8941  -2604    498   2285       C  
ATOM   4776  CE2 TYR B 166       1.419  30.152  27.226  1.00 95.82           C  
ANISOU 4776  CE2 TYR B 166    14991  12414   9002  -2360   1143   2417       C  
ATOM   4777  CZ  TYR B 166       0.127  30.070  27.707  1.00 88.79           C  
ANISOU 4777  CZ  TYR B 166    14259  11600   7878  -2423    766   2293       C  
ATOM   4778  OH  TYR B 166      -0.782  29.219  27.121  1.00 87.13           O  
ANISOU 4778  OH  TYR B 166    14368  11419   7318  -2302    660   2165       O  
ATOM   4779  N   GLU B 167       3.682  35.552  30.875  1.00 96.74           N  
ANISOU 4779  N   GLU B 167    13731  12198  10826  -3220    709   2756       N  
ATOM   4780  CA  GLU B 167       4.683  36.483  31.398  1.00103.19           C  
ANISOU 4780  CA  GLU B 167    14175  12860  12172  -3376    692   2828       C  
ATOM   4781  C   GLU B 167       4.350  36.911  32.823  1.00 95.76           C  
ANISOU 4781  C   GLU B 167    13153  11919  11311  -3508    186   2697       C  
ATOM   4782  O   GLU B 167       5.232  36.978  33.675  1.00108.53           O  
ANISOU 4782  O   GLU B 167    14438  13442  13356  -3592    -22   2664       O  
ATOM   4783  CB  GLU B 167       4.802  37.724  30.504  1.00110.83           C  
ANISOU 4783  CB  GLU B 167    15212  13698  13199  -3433   1031   3003       C  
ATOM   4784  CG  GLU B 167       6.053  37.759  29.635  1.00128.85           C  
ANISOU 4784  CG  GLU B 167    17255  15845  15857  -3416   1542   3178       C  
ATOM   4785  CD  GLU B 167       6.505  39.176  29.318  1.00140.31           C  
ANISOU 4785  CD  GLU B 167    18596  17094  17621  -3569   1769   3351       C  
ATOM   4786  OE1 GLU B 167       5.864  40.129  29.809  1.00139.08           O  
ANISOU 4786  OE1 GLU B 167    18552  16901  17392  -3680   1486   3321       O  
ATOM   4787  OE2 GLU B 167       7.504  39.339  28.584  1.00144.62           O  
ANISOU 4787  OE2 GLU B 167    18942  17502  18504  -3578   2251   3520       O  
ATOM   4788  N   VAL B 168       3.078  37.201  33.078  1.00 79.48           N  
ANISOU 4788  N   VAL B 168    11404   9950   8845  -3511    -15   2613       N  
ATOM   4789  CA  VAL B 168       2.651  37.578  34.417  1.00 78.02           C  
ANISOU 4789  CA  VAL B 168    11213   9771   8661  -3609   -448   2477       C  
ATOM   4790  C   VAL B 168       2.898  36.417  35.364  1.00102.39           C  
ANISOU 4790  C   VAL B 168    14218  12919  11765  -3573   -712   2367       C  
ATOM   4791  O   VAL B 168       3.355  36.609  36.489  1.00107.01           O  
ANISOU 4791  O   VAL B 168    14654  13433  12571  -3649  -1037   2294       O  
ATOM   4792  CB  VAL B 168       1.155  37.954  34.475  1.00 78.69           C  
ANISOU 4792  CB  VAL B 168    11639   9954   8306  -3591   -563   2395       C  
ATOM   4793  CG1 VAL B 168       0.805  38.501  35.849  1.00 77.93           C  
ANISOU 4793  CG1 VAL B 168    11544   9836   8230  -3686   -943   2261       C  
ATOM   4794  CG2 VAL B 168       0.804  38.965  33.404  1.00 82.93           C  
ANISOU 4794  CG2 VAL B 168    12326  10426   8757  -3582   -316   2511       C  
ATOM   4795  N   GLU B 169       2.616  35.206  34.889  1.00111.45           N  
ANISOU 4795  N   GLU B 169    15492  14177  12676  -3447   -589   2355       N  
ATOM   4796  CA  GLU B 169       2.841  34.007  35.685  1.00115.00           C  
ANISOU 4796  CA  GLU B 169    15902  14665  13128  -3397   -812   2273       C  
ATOM   4797  C   GLU B 169       4.310  33.901  36.049  1.00112.06           C  
ANISOU 4797  C   GLU B 169    15150  14161  13266  -3412   -881   2307       C  
ATOM   4798  O   GLU B 169       4.657  33.674  37.209  1.00122.48           O  
ANISOU 4798  O   GLU B 169    16386  15433  14717  -3440  -1250   2229       O  
ATOM   4799  CB  GLU B 169       2.395  32.745  34.933  1.00121.32           C  
ANISOU 4799  CB  GLU B 169    16886  15566  13645  -3257   -630   2263       C  
ATOM   4800  CG  GLU B 169       3.045  31.461  35.450  1.00135.03           C  
ANISOU 4800  CG  GLU B 169    18512  17285  15509  -3181   -762   2226       C  
ATOM   4801  CD  GLU B 169       2.738  30.240  34.597  1.00140.90           C  
ANISOU 4801  CD  GLU B 169    19421  18089  16026  -3036   -560   2214       C  
ATOM   4802  OE1 GLU B 169       1.545  29.950  34.380  1.00138.08           O  
ANISOU 4802  OE1 GLU B 169    19352  17820  15290  -3024   -572   2156       O  
ATOM   4803  OE2 GLU B 169       3.687  29.560  34.152  1.00148.22           O  
ANISOU 4803  OE2 GLU B 169    20179  18961  17178  -2930   -401   2249       O  
ATOM   4804  N   GLU B 170       5.166  34.095  35.052  1.00107.56           N  
ANISOU 4804  N   GLU B 170    14358  13517  12993  -3385   -524   2424       N  
ATOM   4805  CA  GLU B 170       6.604  34.034  35.248  1.00117.70           C  
ANISOU 4805  CA  GLU B 170    15204  14657  14859  -3398   -531   2460       C  
ATOM   4806  C   GLU B 170       7.051  35.053  36.293  1.00129.37           C  
ANISOU 4806  C   GLU B 170    16469  15998  16686  -3555   -899   2416       C  
ATOM   4807  O   GLU B 170       7.874  34.747  37.155  1.00139.97           O  
ANISOU 4807  O   GLU B 170    17556  17244  18381  -3558  -1228   2351       O  
ATOM   4808  CB  GLU B 170       7.338  34.258  33.919  1.00127.85           C  
ANISOU 4808  CB  GLU B 170    16305  15874  16398  -3359     13   2610       C  
ATOM   4809  CG  GLU B 170       8.831  33.929  33.951  1.00155.26           C  
ANISOU 4809  CG  GLU B 170    19274  19202  20514  -3334     99   2644       C  
ATOM   4810  CD  GLU B 170       9.131  32.543  34.503  1.00175.51           C  
ANISOU 4810  CD  GLU B 170    21780  21805  23103  -3192   -144   2541       C  
ATOM   4811  OE1 GLU B 170       8.382  31.592  34.192  1.00175.72           O  
ANISOU 4811  OE1 GLU B 170    22143  21964  22660  -3064    -85   2501       O  
ATOM   4812  OE2 GLU B 170      10.124  32.404  35.249  1.00185.34           O  
ANISOU 4812  OE2 GLU B 170    22640  22923  24858  -3205   -420   2497       O  
ATOM   4813  N   HIS B 171       6.486  36.255  36.232  1.00122.59           N  
ANISOU 4813  N   HIS B 171    15742  15115  15723  -3670   -883   2436       N  
ATOM   4814  CA  HIS B 171       6.829  37.295  37.195  1.00122.22           C  
ANISOU 4814  CA  HIS B 171    15541  14919  15979  -3818  -1245   2374       C  
ATOM   4815  C   HIS B 171       6.306  36.970  38.584  1.00114.51           C  
ANISOU 4815  C   HIS B 171    14780  13991  14737  -3806  -1762   2206       C  
ATOM   4816  O   HIS B 171       6.955  37.297  39.581  1.00124.68           O  
ANISOU 4816  O   HIS B 171    15901  15140  16333  -3867  -2168   2119       O  
ATOM   4817  CB  HIS B 171       6.307  38.652  36.732  1.00129.61           C  
ANISOU 4817  CB  HIS B 171    16598  15798  16850  -3928  -1081   2439       C  
ATOM   4818  CG  HIS B 171       7.058  39.202  35.566  1.00132.27           C  
ANISOU 4818  CG  HIS B 171    16697  16011  17550  -3975   -610   2623       C  
ATOM   4819  ND1 HIS B 171       7.254  40.558  35.375  1.00130.16           N  
ANISOU 4819  ND1 HIS B 171    16338  15565  17553  -4125   -530   2702       N  
ATOM   4820  CD2 HIS B 171       7.674  38.589  34.533  1.00134.74           C  
ANISOU 4820  CD2 HIS B 171    16864  16330  18001  -3889   -161   2750       C  
ATOM   4821  CE1 HIS B 171       7.950  40.745  34.275  1.00140.43           C  
ANISOU 4821  CE1 HIS B 171    17452  16769  19138  -4140    -33   2888       C  
ATOM   4822  NE2 HIS B 171       8.221  39.565  33.737  1.00138.29           N  
ANISOU 4822  NE2 HIS B 171    17149  16613  18783  -3990    214   2917       N  
ATOM   4823  N   MET B 172       5.134  36.345  38.654  1.00 92.21           N  
ANISOU 4823  N   MET B 172    12338  11345  11351  -3727  -1749   2158       N  
ATOM   4824  CA  MET B 172       4.610  35.888  39.933  1.00 91.43           C  
ANISOU 4824  CA  MET B 172    12485  11293  10961  -3702  -2153   2023       C  
ATOM   4825  C   MET B 172       5.600  34.923  40.578  1.00110.85           C  
ANISOU 4825  C   MET B 172    14766  13679  13673  -3631  -2425   1993       C  
ATOM   4826  O   MET B 172       5.858  34.993  41.778  1.00100.37           O  
ANISOU 4826  O   MET B 172    13490  12263  12382  -3643  -2870   1893       O  
ATOM   4827  CB  MET B 172       3.252  35.212  39.773  1.00 83.20           C  
ANISOU 4827  CB  MET B 172    11820  10438   9355  -3634  -2016   1998       C  
ATOM   4828  CG  MET B 172       2.131  36.122  39.312  1.00 75.46           C  
ANISOU 4828  CG  MET B 172    11042   9525   8106  -3679  -1841   1995       C  
ATOM   4829  SD  MET B 172       0.572  35.218  39.302  1.00 92.76           S  
ANISOU 4829  SD  MET B 172    13601  11906   9739  -3606  -1754   1934       S  
ATOM   4830  CE  MET B 172      -0.489  36.332  38.398  1.00 80.30           C  
ANISOU 4830  CE  MET B 172    12147  10372   7992  -3628  -1528   1949       C  
ATOM   4831  N   GLU B 173       6.147  34.022  39.765  1.00129.48           N  
ANISOU 4831  N   GLU B 173    16943  16063  16192  -3538  -2166   2074       N  
ATOM   4832  CA  GLU B 173       7.124  33.043  40.235  1.00132.38           C  
ANISOU 4832  CA  GLU B 173    17106  16348  16844  -3442  -2397   2052       C  
ATOM   4833  C   GLU B 173       8.387  33.723  40.750  1.00128.87           C  
ANISOU 4833  C   GLU B 173    16250  15694  17021  -3508  -2694   2022       C  
ATOM   4834  O   GLU B 173       8.972  33.276  41.734  1.00129.18           O  
ANISOU 4834  O   GLU B 173    16232  15631  17221  -3454  -3149   1942       O  
ATOM   4835  CB  GLU B 173       7.488  32.056  39.123  1.00137.31           C  
ANISOU 4835  CB  GLU B 173    17590  17022  17559  -3317  -2000   2137       C  
ATOM   4836  CG  GLU B 173       6.365  31.111  38.718  1.00142.20           C  
ANISOU 4836  CG  GLU B 173    18599  17810  17622  -3230  -1810   2136       C  
ATOM   4837  CD  GLU B 173       6.797  30.119  37.655  1.00149.38           C  
ANISOU 4837  CD  GLU B 173    19397  18739  18624  -3086  -1457   2193       C  
ATOM   4838  OE1 GLU B 173       7.907  30.283  37.104  1.00155.30           O  
ANISOU 4838  OE1 GLU B 173    19764  19390  19852  -3057  -1263   2250       O  
ATOM   4839  OE2 GLU B 173       6.028  29.174  37.375  1.00142.35           O  
ANISOU 4839  OE2 GLU B 173    18795  17947  17345  -3002  -1364   2174       O  
ATOM   4840  N   ALA B 174       8.809  34.793  40.080  1.00126.03           N  
ANISOU 4840  N   ALA B 174    15610  15249  17026  -3623  -2452   2089       N  
ATOM   4841  CA  ALA B 174       9.990  35.533  40.509  1.00125.70           C  
ANISOU 4841  CA  ALA B 174    15129  14977  17653  -3718  -2720   2058       C  
ATOM   4842  C   ALA B 174       9.683  36.139  41.868  1.00124.50           C  
ANISOU 4842  C   ALA B 174    15208  14749  17349  -3782  -3304   1907       C  
ATOM   4843  O   ALA B 174      10.503  36.099  42.789  1.00123.33           O  
ANISOU 4843  O   ALA B 174    14878  14434  17549  -3771  -3810   1805       O  
ATOM   4844  CB  ALA B 174      10.354  36.608  39.501  1.00130.89           C  
ANISOU 4844  CB  ALA B 174    15499  15544  18687  -3851  -2290   2180       C  
ATOM   4845  N   ALA B 175       8.484  36.702  41.979  1.00128.59           N  
ANISOU 4845  N   ALA B 175    16141  15379  17339  -3831  -3240   1883       N  
ATOM   4846  CA  ALA B 175       7.994  37.225  43.243  1.00132.96           C  
ANISOU 4846  CA  ALA B 175    17015  15884  17618  -3863  -3718   1731       C  
ATOM   4847  C   ALA B 175       7.710  36.026  44.138  1.00142.80           C  
ANISOU 4847  C   ALA B 175    18579  17207  18470  -3719  -4012   1663       C  
ATOM   4848  O   ALA B 175       7.810  34.880  43.699  1.00141.40           O  
ANISOU 4848  O   ALA B 175    18365  17121  18241  -3613  -3827   1736       O  
ATOM   4849  CB  ALA B 175       6.748  38.076  43.047  1.00122.73           C  
ANISOU 4849  CB  ALA B 175    16059  14692  15881  -3929  -3507   1725       C  
ATOM   4850  N   GLY B 176       7.334  36.269  45.385  1.00143.89           N  
ANISOU 4850  N   GLY B 176    19070  17297  18305  -3707  -4451   1528       N  
ATOM   4851  CA  GLY B 176       7.041  35.165  46.278  1.00145.03           C  
ANISOU 4851  CA  GLY B 176    19580  17488  18037  -3574  -4707   1486       C  
ATOM   4852  C   GLY B 176       5.642  34.607  46.104  1.00136.68           C  
ANISOU 4852  C   GLY B 176    18942  16650  16339  -3540  -4352   1531       C  
ATOM   4853  O   GLY B 176       5.164  33.845  46.945  1.00143.64           O  
ANISOU 4853  O   GLY B 176    20214  17564  16798  -3456  -4518   1501       O  
ATOM   4854  N   ILE B 177       4.991  34.959  45.000  1.00131.19           N  
ANISOU 4854  N   ILE B 177    18170  16090  15588  -3603  -3866   1607       N  
ATOM   4855  CA  ILE B 177       3.616  34.527  44.776  1.00127.83           C  
ANISOU 4855  CA  ILE B 177    18088  15854  14627  -3583  -3550   1630       C  
ATOM   4856  C   ILE B 177       3.426  33.212  44.032  1.00128.89           C  
ANISOU 4856  C   ILE B 177    18211  16105  14658  -3503  -3263   1728       C  
ATOM   4857  O   ILE B 177       3.972  33.014  42.949  1.00142.09           O  
ANISOU 4857  O   ILE B 177    19577  17787  16624  -3488  -3010   1812       O  
ATOM   4858  CB  ILE B 177       2.846  35.607  43.987  1.00119.71           C  
ANISOU 4858  CB  ILE B 177    17042  14898  13545  -3672  -3227   1642       C  
ATOM   4859  CG1 ILE B 177       2.758  36.895  44.801  1.00121.68           C  
ANISOU 4859  CG1 ILE B 177    17397  15035  13802  -3742  -3496   1524       C  
ATOM   4860  CG2 ILE B 177       1.451  35.125  43.642  1.00110.07           C  
ANISOU 4860  CG2 ILE B 177    16101  13861  11861  -3645  -2917   1656       C  
ATOM   4861  CD1 ILE B 177       2.194  36.670  46.181  1.00135.20           C  
ANISOU 4861  CD1 ILE B 177    19536  16742  15090  -3689  -3784   1404       C  
ATOM   4862  N   ALA B 178       2.663  32.307  44.643  1.00124.22           N  
ANISOU 4862  N   ALA B 178    17973  15580  13645  -3450  -3295   1714       N  
ATOM   4863  CA  ALA B 178       2.167  31.116  43.962  1.00120.48           C  
ANISOU 4863  CA  ALA B 178    17562  15213  13003  -3393  -3008   1786       C  
ATOM   4864  C   ALA B 178       0.716  31.343  43.530  1.00119.47           C  
ANISOU 4864  C   ALA B 178    17635  15232  12528  -3448  -2690   1773       C  
ATOM   4865  O   ALA B 178       0.023  32.185  44.104  1.00104.50           O  
ANISOU 4865  O   ALA B 178    15913  13353  10441  -3506  -2734   1702       O  
ATOM   4866  CB  ALA B 178       2.281  29.897  44.851  1.00113.11           C  
ANISOU 4866  CB  ALA B 178    16866  14222  11888  -3308  -3235   1796       C  
ATOM   4867  N   LEU B 179       0.256  30.588  42.535  1.00125.41           N  
ANISOU 4867  N   LEU B 179    18361  16074  13214  -3417  -2394   1824       N  
ATOM   4868  CA  LEU B 179      -1.068  30.813  41.945  1.00107.83           C  
ANISOU 4868  CA  LEU B 179    16259  13970  10742  -3459  -2123   1800       C  
ATOM   4869  C   LEU B 179      -2.187  30.016  42.619  1.00 96.73           C  
ANISOU 4869  C   LEU B 179    15152  12606   8993  -3474  -2095   1769       C  
ATOM   4870  O   LEU B 179      -2.055  28.812  42.832  1.00 91.69           O  
ANISOU 4870  O   LEU B 179    14607  11934   8297  -3432  -2127   1808       O  
ATOM   4871  CB  LEU B 179      -1.049  30.492  40.450  1.00 92.94           C  
ANISOU 4871  CB  LEU B 179    14220  12139   8955  -3412  -1840   1853       C  
ATOM   4872  CG  LEU B 179      -0.088  31.291  39.571  1.00 95.72           C  
ANISOU 4872  CG  LEU B 179    14295  12448   9626  -3402  -1737   1911       C  
ATOM   4873  CD1 LEU B 179       1.144  30.469  39.214  1.00 90.33           C  
ANISOU 4873  CD1 LEU B 179    13403  11695   9222  -3315  -1721   1972       C  
ATOM   4874  CD2 LEU B 179      -0.811  31.762  38.321  1.00109.36           C  
ANISOU 4874  CD2 LEU B 179    16051  14252  11250  -3394  -1452   1929       C  
ATOM   4875  N   GLU B 180      -3.299  30.684  42.916  1.00108.81           N  
ANISOU 4875  N   GLU B 180    16821  14197  10325  -3534  -2009   1703       N  
ATOM   4876  CA  GLU B 180      -4.496  30.004  43.409  1.00116.56           C  
ANISOU 4876  CA  GLU B 180    18035  15217  11035  -3566  -1890   1677       C  
ATOM   4877  C   GLU B 180      -5.273  29.435  42.229  1.00108.05           C  
ANISOU 4877  C   GLU B 180    16871  14212   9971  -3566  -1657   1679       C  
ATOM   4878  O   GLU B 180      -4.923  29.679  41.078  1.00 92.62           O  
ANISOU 4878  O   GLU B 180    14737  12284   8170  -3526  -1588   1696       O  
ATOM   4879  CB  GLU B 180      -5.380  30.947  44.223  1.00121.87           C  
ANISOU 4879  CB  GLU B 180    18864  15912  11528  -3615  -1865   1590       C  
ATOM   4880  CG  GLU B 180      -5.038  30.993  45.704  1.00134.94           C  
ANISOU 4880  CG  GLU B 180    20788  17479  13002  -3606  -2073   1573       C  
ATOM   4881  CD  GLU B 180      -5.878  31.998  46.463  1.00140.25           C  
ANISOU 4881  CD  GLU B 180    21634  18166  13488  -3630  -2017   1469       C  
ATOM   4882  OE1 GLU B 180      -7.048  32.216  46.074  1.00149.92           O  
ANISOU 4882  OE1 GLU B 180    22817  19473  14674  -3664  -1761   1422       O  
ATOM   4883  OE2 GLU B 180      -5.363  32.576  47.444  1.00134.54           O  
ANISOU 4883  OE2 GLU B 180    21087  17360  12672  -3603  -2248   1421       O  
ATOM   4884  N   GLU B 181      -6.321  28.673  42.516  1.00116.98           N  
ANISOU 4884  N   GLU B 181    18146  15355  10946  -3610  -1535   1660       N  
ATOM   4885  CA  GLU B 181      -7.038  27.933  41.481  1.00118.69           C  
ANISOU 4885  CA  GLU B 181    18296  15603  11198  -3610  -1381   1644       C  
ATOM   4886  C   GLU B 181      -7.583  28.834  40.367  1.00108.79           C  
ANISOU 4886  C   GLU B 181    16894  14425  10017  -3592  -1297   1581       C  
ATOM   4887  O   GLU B 181      -7.319  28.592  39.189  1.00119.35           O  
ANISOU 4887  O   GLU B 181    18146  15772  11431  -3527  -1263   1593       O  
ATOM   4888  CB  GLU B 181      -8.184  27.134  42.114  1.00123.52           C  
ANISOU 4888  CB  GLU B 181    19057  16190  11685  -3692  -1260   1624       C  
ATOM   4889  CG  GLU B 181      -9.073  26.407  41.117  1.00117.91           C  
ANISOU 4889  CG  GLU B 181    18263  15485  11052  -3711  -1143   1577       C  
ATOM   4890  CD  GLU B 181     -10.532  26.399  41.530  1.00119.96           C  
ANISOU 4890  CD  GLU B 181    18535  15749  11293  -3813   -983   1508       C  
ATOM   4891  OE1 GLU B 181     -10.843  26.864  42.649  1.00128.75           O  
ANISOU 4891  OE1 GLU B 181    19761  16864  12294  -3861   -913   1509       O  
ATOM   4892  OE2 GLU B 181     -11.369  25.932  40.730  1.00112.67           O  
ANISOU 4892  OE2 GLU B 181    17509  14817  10483  -3838   -928   1442       O  
ATOM   4893  N   ALA B 182      -8.309  29.881  40.752  1.00 97.76           N  
ANISOU 4893  N   ALA B 182    15500  13067   8579  -3630  -1268   1515       N  
ATOM   4894  CA  ALA B 182      -8.943  30.809  39.810  1.00101.71           C  
ANISOU 4894  CA  ALA B 182    15891  13617   9138  -3601  -1219   1453       C  
ATOM   4895  C   ALA B 182      -7.988  31.328  38.729  1.00 87.20           C  
ANISOU 4895  C   ALA B 182    13960  11774   7400  -3526  -1249   1516       C  
ATOM   4896  O   ALA B 182      -8.366  31.484  37.565  1.00 66.45           O  
ANISOU 4896  O   ALA B 182    11299   9164   4783  -3468  -1200   1499       O  
ATOM   4897  CB  ALA B 182      -9.559  31.979  40.575  1.00109.37           C  
ANISOU 4897  CB  ALA B 182    16883  14602  10070  -3632  -1213   1380       C  
ATOM   4898  N   GLU B 183      -6.761  31.635  39.133  1.00 96.67           N  
ANISOU 4898  N   GLU B 183    15123  12931   8677  -3524  -1329   1586       N  
ATOM   4899  CA  GLU B 183      -5.760  32.162  38.214  1.00 96.49           C  
ANISOU 4899  CA  GLU B 183    14982  12880   8800  -3471  -1301   1663       C  
ATOM   4900  C   GLU B 183      -5.278  31.110  37.235  1.00 97.52           C  
ANISOU 4900  C   GLU B 183    15092  13006   8956  -3393  -1207   1716       C  
ATOM   4901  O   GLU B 183      -5.130  31.388  36.044  1.00124.31           O  
ANISOU 4901  O   GLU B 183    18467  16399  12365  -3323  -1089   1751       O  
ATOM   4902  CB  GLU B 183      -4.567  32.733  38.985  1.00100.07           C  
ANISOU 4902  CB  GLU B 183    15351  13263   9410  -3503  -1432   1709       C  
ATOM   4903  CG  GLU B 183      -4.889  34.019  39.705  1.00112.04           C  
ANISOU 4903  CG  GLU B 183    16896  14755  10918  -3559  -1526   1650       C  
ATOM   4904  CD  GLU B 183      -5.606  33.792  41.019  1.00122.74           C  
ANISOU 4904  CD  GLU B 183    18424  16125  12086  -3598  -1612   1563       C  
ATOM   4905  OE1 GLU B 183      -5.288  32.805  41.710  1.00131.89           O  
ANISOU 4905  OE1 GLU B 183    19668  17266  13180  -3599  -1684   1583       O  
ATOM   4906  OE2 GLU B 183      -6.510  34.587  41.350  1.00123.54           O  
ANISOU 4906  OE2 GLU B 183    18595  16245  12099  -3616  -1587   1478       O  
ATOM   4907  N   ILE B 184      -5.039  29.903  37.738  1.00 82.24           N  
ANISOU 4907  N   ILE B 184    13196  11050   7002  -3391  -1253   1721       N  
ATOM   4908  CA  ILE B 184      -4.552  28.820  36.900  1.00 82.40           C  
ANISOU 4908  CA  ILE B 184    13210  11046   7053  -3302  -1174   1753       C  
ATOM   4909  C   ILE B 184      -5.606  28.439  35.875  1.00 99.39           C  
ANISOU 4909  C   ILE B 184    15464  13230   9070  -3260  -1089   1685       C  
ATOM   4910  O   ILE B 184      -5.289  28.185  34.714  1.00107.04           O  
ANISOU 4910  O   ILE B 184    16456  14187  10027  -3155   -985   1699       O  
ATOM   4911  CB  ILE B 184      -4.173  27.583  37.725  1.00 82.22           C  
ANISOU 4911  CB  ILE B 184    13235  10967   7039  -3304  -1272   1768       C  
ATOM   4912  CG1 ILE B 184      -3.425  27.988  38.996  1.00 95.41           C  
ANISOU 4912  CG1 ILE B 184    14870  12592   8789  -3349  -1448   1804       C  
ATOM   4913  CG2 ILE B 184      -3.322  26.640  36.895  1.00 74.23           C  
ANISOU 4913  CG2 ILE B 184    12175   9905   6124  -3186  -1196   1804       C  
ATOM   4914  CD1 ILE B 184      -2.753  26.830  39.711  1.00 96.54           C  
ANISOU 4914  CD1 ILE B 184    15065  12648   8967  -3311  -1583   1844       C  
ATOM   4915  N   SER B 185      -6.863  28.436  36.304  1.00105.33           N  
ANISOU 4915  N   SER B 185    16279  14011   9730  -3334  -1134   1602       N  
ATOM   4916  CA  SER B 185      -7.967  28.071  35.427  1.00119.82           C  
ANISOU 4916  CA  SER B 185    18180  15855  11491  -3305  -1121   1511       C  
ATOM   4917  C   SER B 185      -8.051  29.036  34.249  1.00100.71           C  
ANISOU 4917  C   SER B 185    15779  13456   9031  -3213  -1085   1508       C  
ATOM   4918  O   SER B 185      -8.277  28.622  33.114  1.00 92.76           O  
ANISOU 4918  O   SER B 185    14872  12428   7944  -3113  -1075   1469       O  
ATOM   4919  CB  SER B 185      -9.290  28.059  36.195  1.00137.49           C  
ANISOU 4919  CB  SER B 185    20413  18107  13719  -3414  -1156   1423       C  
ATOM   4920  OG  SER B 185      -9.792  29.373  36.372  1.00155.95           O  
ANISOU 4920  OG  SER B 185    22700  20491  16063  -3433  -1163   1391       O  
ATOM   4921  N   ALA B 186      -7.860  30.321  34.526  1.00 92.62           N  
ANISOU 4921  N   ALA B 186    14695  12453   8044  -3240  -1079   1550       N  
ATOM   4922  CA  ALA B 186      -7.852  31.325  33.476  1.00 86.54           C  
ANISOU 4922  CA  ALA B 186    13973  11675   7233  -3156  -1034   1580       C  
ATOM   4923  C   ALA B 186      -6.691  31.091  32.519  1.00 95.10           C  
ANISOU 4923  C   ALA B 186    15101  12722   8312  -3053   -884   1684       C  
ATOM   4924  O   ALA B 186      -6.849  31.205  31.304  1.00110.08           O  
ANISOU 4924  O   ALA B 186    17150  14597  10080  -2936   -822   1691       O  
ATOM   4925  CB  ALA B 186      -7.774  32.707  34.069  1.00 73.38           C  
ANISOU 4925  CB  ALA B 186    12232  10006   5642  -3217  -1056   1611       C  
ATOM   4926  N   LEU B 187      -5.533  30.747  33.070  1.00 77.36           N  
ANISOU 4926  N   LEU B 187    12732  10455   6206  -3083   -827   1760       N  
ATOM   4927  CA  LEU B 187      -4.373  30.418  32.255  1.00 84.17           C  
ANISOU 4927  CA  LEU B 187    13583  11274   7125  -2982   -641   1852       C  
ATOM   4928  C   LEU B 187      -4.615  29.161  31.427  1.00101.52           C  
ANISOU 4928  C   LEU B 187    15940  13460   9173  -2863   -601   1789       C  
ATOM   4929  O   LEU B 187      -4.184  29.070  30.274  1.00117.60           O  
ANISOU 4929  O   LEU B 187    18097  15463  11121  -2729   -421   1828       O  
ATOM   4930  CB  LEU B 187      -3.138  30.252  33.133  1.00 78.45           C  
ANISOU 4930  CB  LEU B 187    12644  10514   6649  -3035   -643   1921       C  
ATOM   4931  CG  LEU B 187      -2.452  31.559  33.516  1.00 76.13           C  
ANISOU 4931  CG  LEU B 187    12185  10181   6559  -3114   -630   2005       C  
ATOM   4932  CD1 LEU B 187      -1.287  31.297  34.446  1.00 89.55           C  
ANISOU 4932  CD1 LEU B 187    13662  11827   8536  -3160   -718   2041       C  
ATOM   4933  CD2 LEU B 187      -1.981  32.286  32.261  1.00 73.67           C  
ANISOU 4933  CD2 LEU B 187    11901   9824   6268  -3042   -369   2111       C  
ATOM   4934  N   LEU B 188      -5.313  28.197  32.020  1.00 85.95           N  
ANISOU 4934  N   LEU B 188    13992  11498   7168  -2912   -755   1690       N  
ATOM   4935  CA  LEU B 188      -5.689  26.975  31.319  1.00 95.95           C  
ANISOU 4935  CA  LEU B 188    15414  12727   8316  -2819   -770   1602       C  
ATOM   4936  C   LEU B 188      -6.646  27.278  30.172  1.00 97.18           C  
ANISOU 4936  C   LEU B 188    15772  12879   8272  -2730   -812   1520       C  
ATOM   4937  O   LEU B 188      -6.498  26.756  29.067  1.00 90.50           O  
ANISOU 4937  O   LEU B 188    15120  11985   7280  -2578   -746   1487       O  
ATOM   4938  CB  LEU B 188      -6.351  25.992  32.287  1.00106.41           C  
ANISOU 4938  CB  LEU B 188    16712  14034   9684  -2926   -927   1526       C  
ATOM   4939  CG  LEU B 188      -6.845  24.643  31.761  1.00 67.67           C  
ANISOU 4939  CG  LEU B 188    11945   9054   4711  -2869   -988   1420       C  
ATOM   4940  CD1 LEU B 188      -5.760  23.581  31.839  1.00 68.53           C  
ANISOU 4940  CD1 LEU B 188    12052   9093   4894  -2793   -919   1463       C  
ATOM   4941  CD2 LEU B 188      -8.117  24.213  32.472  1.00 67.14           C  
ANISOU 4941  CD2 LEU B 188    11860   8970   4682  -3013  -1137   1330       C  
ATOM   4942  N   LYS B 189      -7.611  28.152  30.451  1.00102.76           N  
ANISOU 4942  N   LYS B 189    16449  13623   8971  -2807   -935   1481       N  
ATOM   4943  CA  LYS B 189      -8.652  28.529  29.497  1.00 89.66           C  
ANISOU 4943  CA  LYS B 189    14959  11948   7159  -2722  -1055   1389       C  
ATOM   4944  C   LYS B 189      -8.042  29.036  28.204  1.00 92.33           C  
ANISOU 4944  C   LYS B 189    15519  12249   7311  -2550   -908   1468       C  
ATOM   4945  O   LYS B 189      -8.443  28.637  27.112  1.00109.19           O  
ANISOU 4945  O   LYS B 189    17912  14332   9244  -2402   -974   1389       O  
ATOM   4946  CB  LYS B 189      -9.550  29.606  30.109  1.00 67.26           C  
ANISOU 4946  CB  LYS B 189    12005   9151   4400  -2820  -1173   1360       C  
ATOM   4947  CG  LYS B 189     -10.558  30.224  29.173  1.00 68.29           C  
ANISOU 4947  CG  LYS B 189    12282   9250   4414  -2717  -1331   1277       C  
ATOM   4948  CD  LYS B 189     -11.728  29.287  28.945  1.00 81.76           C  
ANISOU 4948  CD  LYS B 189    14005  10915   6143  -2711  -1554   1093       C  
ATOM   4949  CE  LYS B 189     -13.050  30.038  28.912  1.00 89.63           C  
ANISOU 4949  CE  LYS B 189    14933  11901   7220  -2713  -1771    979       C  
ATOM   4950  NZ  LYS B 189     -13.346  30.709  30.212  1.00 82.62           N  
ANISOU 4950  NZ  LYS B 189    13788  11077   6528  -2867  -1709    996       N  
ATOM   4951  N   VAL B 190      -7.045  29.898  28.352  1.00 78.49           N  
ANISOU 4951  N   VAL B 190    13681  10507   5633  -2570   -705   1626       N  
ATOM   4952  CA  VAL B 190      -6.367  30.527  27.231  1.00 88.36           C  
ANISOU 4952  CA  VAL B 190    15126  11707   6738  -2433   -482   1746       C  
ATOM   4953  C   VAL B 190      -5.534  29.551  26.425  1.00 96.96           C  
ANISOU 4953  C   VAL B 190    16364  12754   7723  -2285   -270   1763       C  
ATOM   4954  O   VAL B 190      -5.564  29.567  25.193  1.00122.96           O  
ANISOU 4954  O   VAL B 190    19983  15989  10745  -2108   -171   1769       O  
ATOM   4955  CB  VAL B 190      -5.471  31.657  27.719  1.00 99.22           C  
ANISOU 4955  CB  VAL B 190    16309  13079   8312  -2529   -305   1912       C  
ATOM   4956  CG1 VAL B 190      -4.668  32.247  26.571  1.00106.05           C  
ANISOU 4956  CG1 VAL B 190    17363  13867   9064  -2405      5   2067       C  
ATOM   4957  CG2 VAL B 190      -6.324  32.692  28.358  1.00 98.28           C  
ANISOU 4957  CG2 VAL B 190    16110  12981   8252  -2635   -504   1881       C  
ATOM   4958  N   SER B 191      -4.785  28.710  27.125  1.00 80.82           N  
ANISOU 4958  N   SER B 191    14108  10723   5879  -2340   -204   1767       N  
ATOM   4959  CA  SER B 191      -3.936  27.732  26.465  1.00 92.18           C  
ANISOU 4959  CA  SER B 191    15644  12110   7268  -2191      8   1770       C  
ATOM   4960  C   SER B 191      -4.785  26.825  25.576  1.00 92.93           C  
ANISOU 4960  C   SER B 191    16074  12160   7075  -2045   -141   1605       C  
ATOM   4961  O   SER B 191      -4.357  26.421  24.494  1.00 78.26           O  
ANISOU 4961  O   SER B 191    14486  10240   5009  -1850     50   1598       O  
ATOM   4962  CB  SER B 191      -3.157  26.923  27.498  1.00 87.70           C  
ANISOU 4962  CB  SER B 191    14783  11549   6991  -2272     10   1778       C  
ATOM   4963  OG  SER B 191      -2.105  27.693  28.051  1.00 76.76           O  
ANISOU 4963  OG  SER B 191    13116  10168   5881  -2353    170   1924       O  
ATOM   4964  N   ALA B 192      -5.999  26.533  26.035  1.00105.94           N  
ANISOU 4964  N   ALA B 192    17706  13824   8723  -2139   -477   1466       N  
ATOM   4965  CA  ALA B 192      -6.968  25.765  25.261  1.00100.52           C  
ANISOU 4965  CA  ALA B 192    17296  13071   7826  -2031   -705   1284       C  
ATOM   4966  C   ALA B 192      -7.429  26.545  24.036  1.00 96.81           C  
ANISOU 4966  C   ALA B 192    17175  12562   7045  -1867   -738   1275       C  
ATOM   4967  O   ALA B 192      -7.515  25.998  22.939  1.00109.16           O  
ANISOU 4967  O   ALA B 192    19099  14042   8333  -1669   -759   1183       O  
ATOM   4968  CB  ALA B 192      -8.160  25.388  26.129  1.00100.43           C  
ANISOU 4968  CB  ALA B 192    17109  13070   7979  -2201  -1028   1152       C  
ATOM   4969  N   ALA B 193      -7.734  27.823  24.238  1.00 87.94           N  
ANISOU 4969  N   ALA B 193    15979  11484   5952  -1938   -764   1364       N  
ATOM   4970  CA  ALA B 193      -8.215  28.701  23.171  1.00 91.02           C  
ANISOU 4970  CA  ALA B 193    16708  11820   6054  -1786   -829   1380       C  
ATOM   4971  C   ALA B 193      -7.142  28.931  22.100  1.00 93.39           C  
ANISOU 4971  C   ALA B 193    17328  12063   6093  -1597   -448   1527       C  
ATOM   4972  O   ALA B 193      -7.460  29.064  20.917  1.00 83.63           O  
ANISOU 4972  O   ALA B 193    16483  10741   4552  -1375   -488   1483       O  
ATOM   4973  CB  ALA B 193      -8.693  30.030  23.746  1.00 85.59           C  
ANISOU 4973  CB  ALA B 193    15841  11176   5505  -1911   -921   1455       C  
ATOM   4974  N   THR B 194      -5.883  29.038  22.525  1.00 92.02           N  
ANISOU 4974  N   THR B 194    16925  11922   6117  -1664    -71   1690       N  
ATOM   4975  CA  THR B 194      -4.764  29.154  21.591  1.00 93.92           C  
ANISOU 4975  CA  THR B 194    17396  12100   6189  -1500    378   1838       C  
ATOM   4976  C   THR B 194      -4.410  27.770  21.046  1.00 96.92           C  
ANISOU 4976  C   THR B 194    17961  12436   6428  -1333    467   1715       C  
ATOM   4977  O   THR B 194      -3.581  27.633  20.144  1.00103.65           O  
ANISOU 4977  O   THR B 194    19070  13224   7087  -1148    850   1792       O  
ATOM   4978  CB  THR B 194      -3.521  29.775  22.270  1.00 93.97           C  
ANISOU 4978  CB  THR B 194    17016  12135   6556  -1644    738   2044       C  
ATOM   4979  OG1 THR B 194      -3.932  30.852  23.118  1.00 80.95           O  
ANISOU 4979  OG1 THR B 194    15116  10527   5114  -1839    559   2102       O  
ATOM   4980  CG2 THR B 194      -2.528  30.303  21.238  1.00100.05           C  
ANISOU 4980  CG2 THR B 194    18018  12817   7180  -1500   1243   2237       C  
ATOM   4981  N   GLY B 195      -5.073  26.753  21.590  1.00 83.55           N  
ANISOU 4981  N   GLY B 195    16151  10761   4834  -1394    128   1522       N  
ATOM   4982  CA  GLY B 195      -4.885  25.372  21.185  1.00 84.96           C  
ANISOU 4982  CA  GLY B 195    16492  10874   4913  -1252    130   1373       C  
ATOM   4983  C   GLY B 195      -3.463  24.852  21.289  1.00 95.95           C  
ANISOU 4983  C   GLY B 195    17720  12258   6479  -1198    555   1469       C  
ATOM   4984  O   GLY B 195      -3.055  23.982  20.519  1.00 96.68           O  
ANISOU 4984  O   GLY B 195    18079  12270   6386   -989    715   1387       O  
ATOM   4985  N   ARG B 196      -2.714  25.355  22.264  1.00107.52           N  
ANISOU 4985  N   ARG B 196    18737  13792   8323  -1375    712   1623       N  
ATOM   4986  CA  ARG B 196      -1.384  24.825  22.539  1.00109.17           C  
ANISOU 4986  CA  ARG B 196    18689  13984   8808  -1341   1042   1696       C  
ATOM   4987  C   ARG B 196      -1.510  23.772  23.623  1.00123.12           C  
ANISOU 4987  C   ARG B 196    20181  15761  10839  -1454    759   1586       C  
ATOM   4988  O   ARG B 196      -1.852  24.070  24.766  1.00136.96           O  
ANISOU 4988  O   ARG B 196    21641  17577  12820  -1671    519   1609       O  
ATOM   4989  CB  ARG B 196      -0.404  25.924  22.940  1.00 99.77           C  
ANISOU 4989  CB  ARG B 196    17164  12824   7920  -1454   1346   1917       C  
ATOM   4990  CG  ARG B 196      -0.976  26.952  23.880  1.00100.43           C  
ANISOU 4990  CG  ARG B 196    17015  12980   8163  -1693   1081   1976       C  
ATOM   4991  CD  ARG B 196       0.094  27.939  24.275  1.00106.00           C  
ANISOU 4991  CD  ARG B 196    17382  13680   9214  -1803   1361   2173       C  
ATOM   4992  NE  ARG B 196       0.214  29.041  23.329  1.00 98.09           N  
ANISOU 4992  NE  ARG B 196    16609  12628   8031  -1744   1657   2322       N  
ATOM   4993  CZ  ARG B 196       1.325  29.745  23.151  1.00 96.01           C  
ANISOU 4993  CZ  ARG B 196    16157  12304   8018  -1768   2068   2509       C  
ATOM   4994  NH1 ARG B 196       2.419  29.446  23.840  1.00 94.06           N  
ANISOU 4994  NH1 ARG B 196    15457  12043   8238  -1838   2197   2548       N  
ATOM   4995  NH2 ARG B 196       1.344  30.740  22.276  1.00102.95           N  
ANISOU 4995  NH2 ARG B 196    17299  13115   8701  -1720   2344   2661       N  
ATOM   4996  N   GLU B 197      -1.245  22.533  23.237  1.00129.15           N  
ANISOU 4996  N   GLU B 197    21085  16443  11543  -1293    800   1465       N  
ATOM   4997  CA  GLU B 197      -1.473  21.370  24.082  1.00123.82           C  
ANISOU 4997  CA  GLU B 197    20260  15732  11054  -1367    520   1349       C  
ATOM   4998  C   GLU B 197      -0.615  21.312  25.343  1.00124.05           C  
ANISOU 4998  C   GLU B 197    19830  15790  11515  -1506    537   1458       C  
ATOM   4999  O   GLU B 197      -1.139  21.100  26.435  1.00112.28           O  
ANISOU 4999  O   GLU B 197    18172  14322  10169  -1690    233   1439       O  
ATOM   5000  CB  GLU B 197      -1.244  20.100  23.262  1.00124.34           C  
ANISOU 5000  CB  GLU B 197    20610  15672  10960  -1129    597   1198       C  
ATOM   5001  CG  GLU B 197       0.144  19.991  22.600  1.00136.61           C  
ANISOU 5001  CG  GLU B 197    22159  17182  12566   -909   1092   1273       C  
ATOM   5002  CD  GLU B 197       0.289  20.826  21.328  1.00131.08           C  
ANISOU 5002  CD  GLU B 197    21801  16483  11521   -742   1439   1338       C  
ATOM   5003  OE1 GLU B 197      -0.281  21.936  21.252  1.00130.34           O  
ANISOU 5003  OE1 GLU B 197    21768  16459  11296   -851   1368   1424       O  
ATOM   5004  OE2 GLU B 197       0.987  20.369  20.399  1.00126.43           O  
ANISOU 5004  OE2 GLU B 197    21445  15812  10783   -487   1802   1306       O  
ATOM   5005  N   ASN B 198       0.691  21.515  25.195  1.00142.15           N  
ANISOU 5005  N   ASN B 198    21926  18067  14018  -1414    890   1572       N  
ATOM   5006  CA  ASN B 198       1.624  21.335  26.301  1.00145.69           C  
ANISOU 5006  CA  ASN B 198    21945  18507  14904  -1499    865   1651       C  
ATOM   5007  C   ASN B 198       1.338  22.304  27.435  1.00126.98           C  
ANISOU 5007  C   ASN B 198    19320  16224  12702  -1752    637   1744       C  
ATOM   5008  O   ASN B 198       1.510  21.971  28.604  1.00133.92           O  
ANISOU 5008  O   ASN B 198    19974  17094  13818  -1864    400   1754       O  
ATOM   5009  CB  ASN B 198       3.064  21.505  25.819  1.00167.25           C  
ANISOU 5009  CB  ASN B 198    24469  21191  17886  -1350   1306   1749       C  
ATOM   5010  CG  ASN B 198       3.449  22.959  25.640  1.00192.48           C  
ANISOU 5010  CG  ASN B 198    27515  24441  21179  -1441   1552   1915       C  
ATOM   5011  OD1 ASN B 198       4.047  23.566  26.528  1.00206.65           O  
ANISOU 5011  OD1 ASN B 198    28915  26250  23352  -1591   1495   2016       O  
ATOM   5012  ND2 ASN B 198       3.093  23.532  24.494  1.00200.29           N  
ANISOU 5012  ND2 ASN B 198    28846  25438  21817  -1350   1801   1942       N  
ATOM   5013  N   LYS B 199       0.902  23.507  27.080  1.00115.80           N  
ANISOU 5013  N   LYS B 199    17981  14876  11141  -1826    704   1811       N  
ATOM   5014  CA  LYS B 199       0.536  24.502  28.068  1.00 93.61           C  
ANISOU 5014  CA  LYS B 199    14978  12137   8451  -2049    495   1878       C  
ATOM   5015  C   LYS B 199      -0.711  24.068  28.818  1.00105.05           C  
ANISOU 5015  C   LYS B 199    16529  13620   9766  -2175    115   1770       C  
ATOM   5016  O   LYS B 199      -0.828  24.287  30.021  1.00117.31           O  
ANISOU 5016  O   LYS B 199    17895  15201  11475  -2337    -96   1794       O  
ATOM   5017  CB  LYS B 199       0.309  25.851  27.412  1.00 78.33           C  
ANISOU 5017  CB  LYS B 199    13141  10239   6381  -2075    659   1969       C  
ATOM   5018  CG  LYS B 199       1.209  26.929  27.952  1.00 86.55           C  
ANISOU 5018  CG  LYS B 199    13844  11276   7764  -2194    777   2117       C  
ATOM   5019  CD  LYS B 199       2.684  26.585  27.809  1.00 86.23           C  
ANISOU 5019  CD  LYS B 199    13532  11159   8071  -2099   1073   2190       C  
ATOM   5020  CE  LYS B 199       3.555  27.645  28.477  1.00 89.25           C  
ANISOU 5020  CE  LYS B 199    13520  11511   8879  -2248   1113   2317       C  
ATOM   5021  NZ  LYS B 199       5.002  27.414  28.209  1.00100.10           N  
ANISOU 5021  NZ  LYS B 199    14579  12793  10662  -2154   1441   2391       N  
ATOM   5022  N   VAL B 200      -1.653  23.473  28.094  1.00 94.84           N  
ANISOU 5022  N   VAL B 200    15542  12307   8186  -2098     35   1645       N  
ATOM   5023  CA  VAL B 200      -2.846  22.907  28.712  1.00 89.24           C  
ANISOU 5023  CA  VAL B 200    14903  11598   7406  -2217   -285   1533       C  
ATOM   5024  C   VAL B 200      -2.460  21.740  29.623  1.00 93.09           C  
ANISOU 5024  C   VAL B 200    15273  12016   8082  -2248   -400   1517       C  
ATOM   5025  O   VAL B 200      -3.023  21.556  30.704  1.00 80.62           O  
ANISOU 5025  O   VAL B 200    13620  10441   6569  -2409   -611   1512       O  
ATOM   5026  CB  VAL B 200      -3.856  22.431  27.646  1.00 74.70           C  
ANISOU 5026  CB  VAL B 200    13394   9711   5277  -2114   -375   1383       C  
ATOM   5027  CG1 VAL B 200      -5.060  21.773  28.289  1.00 73.46           C  
ANISOU 5027  CG1 VAL B 200    13248   9524   5138  -2256   -682   1266       C  
ATOM   5028  CG2 VAL B 200      -4.301  23.596  26.802  1.00 78.55           C  
ANISOU 5028  CG2 VAL B 200    14041  10249   5557  -2071   -317   1405       C  
ATOM   5029  N   TYR B 201      -1.482  20.961  29.176  1.00 97.78           N  
ANISOU 5029  N   TYR B 201    15868  12530   8754  -2078   -241   1514       N  
ATOM   5030  CA  TYR B 201      -0.989  19.821  29.936  1.00 76.18           C  
ANISOU 5030  CA  TYR B 201    13041   9699   6207  -2065   -351   1504       C  
ATOM   5031  C   TYR B 201      -0.335  20.252  31.248  1.00108.54           C  
ANISOU 5031  C   TYR B 201    16850  13822  10569  -2188   -454   1624       C  
ATOM   5032  O   TYR B 201      -0.682  19.748  32.315  1.00107.04           O  
ANISOU 5032  O   TYR B 201    16657  13593  10421  -2300   -685   1629       O  
ATOM   5033  CB  TYR B 201       0.001  19.023  29.094  1.00 78.84           C  
ANISOU 5033  CB  TYR B 201    13418   9938   6598  -1823   -130   1469       C  
ATOM   5034  CG  TYR B 201       0.492  17.773  29.766  1.00 82.77           C  
ANISOU 5034  CG  TYR B 201    13852  10307   7290  -1773   -262   1446       C  
ATOM   5035  CD1 TYR B 201      -0.353  16.687  29.955  1.00 92.73           C  
ANISOU 5035  CD1 TYR B 201    15322  11464   8446  -1809   -481   1344       C  
ATOM   5036  CD2 TYR B 201       1.798  17.677  30.220  1.00 86.45           C  
ANISOU 5036  CD2 TYR B 201    14040  10731   8077  -1691   -186   1528       C  
ATOM   5037  CE1 TYR B 201       0.093  15.533  30.574  1.00103.85           C  
ANISOU 5037  CE1 TYR B 201    16707  12725  10025  -1759   -608   1339       C  
ATOM   5038  CE2 TYR B 201       2.253  16.532  30.841  1.00107.28           C  
ANISOU 5038  CE2 TYR B 201    16638  13230  10895  -1623   -345   1511       C  
ATOM   5039  CZ  TYR B 201       1.396  15.463  31.018  1.00118.54           C  
ANISOU 5039  CZ  TYR B 201    18317  14549  12171  -1655   -549   1424       C  
ATOM   5040  OH  TYR B 201       1.850  14.321  31.636  1.00140.22           O  
ANISOU 5040  OH  TYR B 201    21057  17130  15090  -1583   -709   1423       O  
ATOM   5041  N   ARG B 202       0.589  21.209  31.160  1.00 98.06           N  
ANISOU 5041  N   ARG B 202    15303  12543   9413  -2168   -285   1722       N  
ATOM   5042  CA  ARG B 202       1.316  21.720  32.325  1.00 83.31           C  
ANISOU 5042  CA  ARG B 202    13152  10678   7824  -2268   -418   1817       C  
ATOM   5043  C   ARG B 202       0.346  22.304  33.345  1.00 86.74           C  
ANISOU 5043  C   ARG B 202    13640  11178   8138  -2476   -663   1823       C  
ATOM   5044  O   ARG B 202       0.487  22.073  34.544  1.00114.43           O  
ANISOU 5044  O   ARG B 202    17091  14648  11739  -2553   -892   1851       O  
ATOM   5045  CB  ARG B 202       2.359  22.767  31.909  1.00 88.38           C  
ANISOU 5045  CB  ARG B 202    13537  11341   8702  -2235   -179   1909       C  
ATOM   5046  CG  ARG B 202       3.068  23.453  33.073  1.00109.98           C  
ANISOU 5046  CG  ARG B 202    15973  14063  11752  -2351   -368   1984       C  
ATOM   5047  CD  ARG B 202       4.130  24.454  32.604  1.00130.57           C  
ANISOU 5047  CD  ARG B 202    18284  16655  14673  -2335   -116   2074       C  
ATOM   5048  NE  ARG B 202       4.885  25.015  33.727  1.00140.35           N  
ANISOU 5048  NE  ARG B 202    19214  17844  16269  -2436   -360   2118       N  
ATOM   5049  CZ  ARG B 202       5.966  25.783  33.605  1.00138.34           C  
ANISOU 5049  CZ  ARG B 202    18608  17530  16425  -2448   -223   2189       C  
ATOM   5050  NH1 ARG B 202       6.437  26.089  32.404  1.00136.66           N  
ANISOU 5050  NH1 ARG B 202    18318  17306  16303  -2365    222   2248       N  
ATOM   5051  NH2 ARG B 202       6.581  26.244  34.687  1.00132.68           N  
ANISOU 5051  NH2 ARG B 202    17632  16748  16035  -2540   -531   2200       N  
ATOM   5052  N   TYR B 203      -0.633  23.063  32.864  1.00 78.03           N  
ANISOU 5052  N   TYR B 203    12666  10162   6819  -2547   -612   1795       N  
ATOM   5053  CA  TYR B 203      -1.603  23.711  33.740  1.00 83.21           C  
ANISOU 5053  CA  TYR B 203    13359  10883   7374  -2725   -791   1788       C  
ATOM   5054  C   TYR B 203      -2.552  22.698  34.373  1.00 78.28           C  
ANISOU 5054  C   TYR B 203    12897  10217   6630  -2797   -960   1723       C  
ATOM   5055  O   TYR B 203      -3.107  22.940  35.444  1.00 85.86           O  
ANISOU 5055  O   TYR B 203    13872  11195   7554  -2936  -1097   1735       O  
ATOM   5056  CB  TYR B 203      -2.401  24.767  32.977  1.00 96.78           C  
ANISOU 5056  CB  TYR B 203    15159  12685   8929  -2755   -698   1766       C  
ATOM   5057  CG  TYR B 203      -1.603  25.995  32.617  1.00109.99           C  
ANISOU 5057  CG  TYR B 203    16682  14381  10727  -2742   -540   1860       C  
ATOM   5058  CD1 TYR B 203      -0.356  26.232  33.183  1.00109.06           C  
ANISOU 5058  CD1 TYR B 203    16315  14220  10901  -2749   -531   1942       C  
ATOM   5059  CD2 TYR B 203      -2.092  26.913  31.704  1.00119.93           C  
ANISOU 5059  CD2 TYR B 203    18049  15681  11839  -2722   -416   1867       C  
ATOM   5060  CE1 TYR B 203       0.377  27.352  32.851  1.00104.57           C  
ANISOU 5060  CE1 TYR B 203    15578  13644  10509  -2761   -373   2031       C  
ATOM   5061  CE2 TYR B 203      -1.365  28.031  31.363  1.00125.59           C  
ANISOU 5061  CE2 TYR B 203    18647  16390  12683  -2723   -244   1974       C  
ATOM   5062  CZ  TYR B 203      -0.135  28.247  31.943  1.00123.17           C  
ANISOU 5062  CZ  TYR B 203    18062  16036  12701  -2755   -209   2056       C  
ATOM   5063  OH  TYR B 203       0.588  29.365  31.605  1.00143.24           O  
ANISOU 5063  OH  TYR B 203    20455  18541  15428  -2780    -26   2165       O  
ATOM   5064  N   LEU B 204      -2.775  21.583  33.691  1.00 80.55           N  
ANISOU 5064  N   LEU B 204    13323  10432   6851  -2705   -929   1653       N  
ATOM   5065  CA  LEU B 204      -3.543  20.498  34.288  1.00 84.52           C  
ANISOU 5065  CA  LEU B 204    13961  10850   7303  -2781  -1072   1607       C  
ATOM   5066  C   LEU B 204      -2.791  19.847  35.451  1.00 87.38           C  
ANISOU 5066  C   LEU B 204    14286  11121   7794  -2790  -1197   1690       C  
ATOM   5067  O   LEU B 204      -3.397  19.483  36.454  1.00 96.85           O  
ANISOU 5067  O   LEU B 204    15583  12276   8941  -2915  -1314   1714       O  
ATOM   5068  CB  LEU B 204      -3.907  19.450  33.243  1.00 84.63           C  
ANISOU 5068  CB  LEU B 204    14140  10774   7241  -2674  -1040   1497       C  
ATOM   5069  CG  LEU B 204      -5.057  19.837  32.310  1.00 83.06           C  
ANISOU 5069  CG  LEU B 204    14056  10621   6881  -2692  -1037   1384       C  
ATOM   5070  CD1 LEU B 204      -5.253  18.761  31.254  1.00101.85           C  
ANISOU 5070  CD1 LEU B 204    16630  12883   9185  -2556  -1049   1255       C  
ATOM   5071  CD2 LEU B 204      -6.356  20.111  33.066  1.00 69.85           C  
ANISOU 5071  CD2 LEU B 204    12368   8978   5196  -2894  -1156   1357       C  
ATOM   5072  N   HIS B 205      -1.476  19.685  35.311  1.00 86.02           N  
ANISOU 5072  N   HIS B 205    13981  10905   7798  -2648  -1167   1736       N  
ATOM   5073  CA  HIS B 205      -0.657  19.173  36.410  1.00 78.00           C  
ANISOU 5073  CA  HIS B 205    12915   9790   6931  -2628  -1346   1812       C  
ATOM   5074  C   HIS B 205      -0.544  20.183  37.547  1.00 98.96           C  
ANISOU 5074  C   HIS B 205    15495  12504   9601  -2748  -1490   1881       C  
ATOM   5075  O   HIS B 205      -0.546  19.810  38.719  1.00103.08           O  
ANISOU 5075  O   HIS B 205    16129  12950  10089  -2799  -1688   1931       O  
ATOM   5076  CB  HIS B 205       0.745  18.802  35.929  1.00 75.58           C  
ANISOU 5076  CB  HIS B 205    12426   9412   6881  -2429  -1286   1825       C  
ATOM   5077  CG  HIS B 205       0.833  17.443  35.312  1.00 90.88           C  
ANISOU 5077  CG  HIS B 205    14488  11219   8824  -2283  -1240   1762       C  
ATOM   5078  ND1 HIS B 205      -0.230  16.563  35.300  1.00 98.06           N  
ANISOU 5078  ND1 HIS B 205    15655  12056   9547  -2348  -1297   1707       N  
ATOM   5079  CD2 HIS B 205       1.860  16.801  34.710  1.00 97.51           C  
ANISOU 5079  CD2 HIS B 205    15223  11967   9859  -2073  -1143   1738       C  
ATOM   5080  CE1 HIS B 205       0.137  15.446  34.700  1.00 96.54           C  
ANISOU 5080  CE1 HIS B 205    15536  11727   9415  -2185  -1260   1645       C  
ATOM   5081  NE2 HIS B 205       1.402  15.562  34.334  1.00 92.86           N  
ANISOU 5081  NE2 HIS B 205    14862  11253   9168  -2004  -1157   1660       N  
ATOM   5082  N   LYS B 206      -0.449  21.463  37.195  1.00105.18           N  
ANISOU 5082  N   LYS B 206    16133  13408  10422  -2785  -1393   1882       N  
ATOM   5083  CA  LYS B 206      -0.408  22.525  38.194  1.00100.78           C  
ANISOU 5083  CA  LYS B 206    15522  12898   9873  -2898  -1535   1921       C  
ATOM   5084  C   LYS B 206      -1.710  22.555  38.992  1.00 93.28           C  
ANISOU 5084  C   LYS B 206    14802  11978   8663  -3046  -1593   1902       C  
ATOM   5085  O   LYS B 206      -1.691  22.742  40.207  1.00102.81           O  
ANISOU 5085  O   LYS B 206    16101  13152   9809  -3109  -1767   1937       O  
ATOM   5086  CB  LYS B 206      -0.138  23.888  37.542  1.00100.07           C  
ANISOU 5086  CB  LYS B 206    15241  12900   9879  -2914  -1396   1924       C  
ATOM   5087  CG  LYS B 206       1.334  24.145  37.219  1.00101.38           C  
ANISOU 5087  CG  LYS B 206    15119  13013  10388  -2812  -1358   1972       C  
ATOM   5088  CD  LYS B 206       1.563  25.570  36.726  1.00110.80           C  
ANISOU 5088  CD  LYS B 206    16141  14266  11691  -2865  -1216   2000       C  
ATOM   5089  CE  LYS B 206       3.035  25.837  36.423  1.00124.00           C  
ANISOU 5089  CE  LYS B 206    17477  15862  13777  -2787  -1138   2055       C  
ATOM   5090  NZ  LYS B 206       3.253  27.159  35.762  1.00126.40           N  
ANISOU 5090  NZ  LYS B 206    17630  16195  14202  -2844   -926   2104       N  
ATOM   5091  N   LEU B 207      -2.836  22.356  38.314  1.00 83.42           N  
ANISOU 5091  N   LEU B 207    13651  10775   7269  -3092  -1449   1840       N  
ATOM   5092  CA  LEU B 207      -4.121  22.299  39.001  1.00 84.21           C  
ANISOU 5092  CA  LEU B 207    13918  10888   7191  -3234  -1454   1817       C  
ATOM   5093  C   LEU B 207      -4.140  21.121  39.956  1.00 94.19           C  
ANISOU 5093  C   LEU B 207    15368  12016   8402  -3258  -1555   1872       C  
ATOM   5094  O   LEU B 207      -4.621  21.224  41.081  1.00116.41           O  
ANISOU 5094  O   LEU B 207    18335  14810  11086  -3357  -1597   1911       O  
ATOM   5095  CB  LEU B 207      -5.277  22.182  38.011  1.00 94.06           C  
ANISOU 5095  CB  LEU B 207    15188  12176   8373  -3267  -1322   1724       C  
ATOM   5096  CG  LEU B 207      -5.773  23.489  37.399  1.00108.61           C  
ANISOU 5096  CG  LEU B 207    16936  14144  10188  -3287  -1247   1672       C  
ATOM   5097  CD1 LEU B 207      -7.008  23.236  36.547  1.00109.24           C  
ANISOU 5097  CD1 LEU B 207    17062  14232  10213  -3310  -1196   1565       C  
ATOM   5098  CD2 LEU B 207      -6.059  24.508  38.487  1.00113.38           C  
ANISOU 5098  CD2 LEU B 207    17532  14803  10744  -3391  -1288   1692       C  
ATOM   5099  N   ARG B 208      -3.609  19.998  39.493  1.00 86.77           N  
ANISOU 5099  N   ARG B 208    14448  10970   7552  -3153  -1576   1880       N  
ATOM   5100  CA  ARG B 208      -3.515  18.789  40.300  1.00 93.90           C  
ANISOU 5100  CA  ARG B 208    15547  11707   8425  -3152  -1685   1948       C  
ATOM   5101  C   ARG B 208      -2.619  18.963  41.525  1.00113.87           C  
ANISOU 5101  C   ARG B 208    18140  14177  10950  -3114  -1901   2042       C  
ATOM   5102  O   ARG B 208      -2.948  18.509  42.621  1.00 74.92           O  
ANISOU 5102  O   ARG B 208    13460   9144   5862  -3177  -1981   2116       O  
ATOM   5103  CB  ARG B 208      -3.010  17.645  39.429  1.00 78.48           C  
ANISOU 5103  CB  ARG B 208    13580   9641   6599  -3014  -1677   1918       C  
ATOM   5104  CG  ARG B 208      -2.734  16.376  40.173  1.00 87.59           C  
ANISOU 5104  CG  ARG B 208    14930  10591   7757  -2980  -1812   1996       C  
ATOM   5105  CD  ARG B 208      -1.897  15.453  39.314  1.00 89.34           C  
ANISOU 5105  CD  ARG B 208    15087  10706   8154  -2790  -1827   1954       C  
ATOM   5106  NE  ARG B 208      -0.567  15.992  39.029  1.00 78.98           N  
ANISOU 5106  NE  ARG B 208    13529   9446   7035  -2626  -1869   1956       N  
ATOM   5107  CZ  ARG B 208       0.402  16.147  39.925  1.00 87.66           C  
ANISOU 5107  CZ  ARG B 208    14569  10492   8248  -2561  -2081   2033       C  
ATOM   5108  NH1 ARG B 208       0.200  15.822  41.194  1.00105.34           N  
ANISOU 5108  NH1 ARG B 208    17044  12627  10352  -2628  -2279   2125       N  
ATOM   5109  NH2 ARG B 208       1.577  16.637  39.552  1.00 79.19           N  
ANISOU 5109  NH2 ARG B 208    13206   9453   7431  -2425  -2096   2020       N  
ATOM   5110  N   GLU B 209      -1.481  19.618  41.316  1.00111.53           N  
ANISOU 5110  N   GLU B 209    17622  13922  10832  -3007  -1997   2038       N  
ATOM   5111  CA  GLU B 209      -0.474  19.829  42.354  1.00 96.65           C  
ANISOU 5111  CA  GLU B 209    15745  11962   9016  -2945  -2276   2098       C  
ATOM   5112  C   GLU B 209      -0.921  20.804  43.436  1.00 79.65           C  
ANISOU 5112  C   GLU B 209    13738   9862   6664  -3059  -2367   2109       C  
ATOM   5113  O   GLU B 209      -0.520  20.685  44.593  1.00 93.17           O  
ANISOU 5113  O   GLU B 209    15645  11469   8284  -3031  -2620   2163       O  
ATOM   5114  CB  GLU B 209       0.824  20.328  41.724  1.00 98.24           C  
ANISOU 5114  CB  GLU B 209    15595  12182   9549  -2818  -2325   2075       C  
ATOM   5115  CG  GLU B 209       2.062  20.033  42.533  1.00103.98           C  
ANISOU 5115  CG  GLU B 209    16269  12765  10474  -2695  -2660   2118       C  
ATOM   5116  CD  GLU B 209       3.311  20.075  41.685  1.00117.47           C  
ANISOU 5116  CD  GLU B 209    17586  14451  12597  -2548  -2628   2093       C  
ATOM   5117  OE1 GLU B 209       3.192  20.347  40.473  1.00103.78           O  
ANISOU 5117  OE1 GLU B 209    15679  12817  10936  -2542  -2313   2054       O  
ATOM   5118  OE2 GLU B 209       4.411  19.839  42.226  1.00137.46           O  
ANISOU 5118  OE2 GLU B 209    19989  16852  15387  -2429  -2915   2111       O  
ATOM   5119  N   TYR B 210      -1.728  21.785  43.045  1.00 73.65           N  
ANISOU 5119  N   TYR B 210    12905   9250   5829  -3167  -2177   2050       N  
ATOM   5120  CA  TYR B 210      -2.101  22.876  43.940  1.00 82.21           C  
ANISOU 5120  CA  TYR B 210    14092  10390   6754  -3254  -2238   2032       C  
ATOM   5121  C   TYR B 210      -3.600  22.947  44.240  1.00 82.92           C  
ANISOU 5121  C   TYR B 210    14381  10535   6589  -3391  -2019   2012       C  
ATOM   5122  O   TYR B 210      -4.042  23.812  44.992  1.00 87.94           O  
ANISOU 5122  O   TYR B 210    15131  11215   7069  -3454  -2021   1986       O  
ATOM   5123  CB  TYR B 210      -1.603  24.209  43.368  1.00 77.14           C  
ANISOU 5123  CB  TYR B 210    13159   9848   6302  -3250  -2237   1977       C  
ATOM   5124  CG  TYR B 210      -0.093  24.266  43.259  1.00101.31           C  
ANISOU 5124  CG  TYR B 210    15983  12833   9676  -3136  -2448   1997       C  
ATOM   5125  CD1 TYR B 210       0.682  24.722  44.319  1.00128.04           C  
ANISOU 5125  CD1 TYR B 210    19402  16131  13116  -3110  -2779   1998       C  
ATOM   5126  CD2 TYR B 210       0.561  23.843  42.108  1.00104.02           C  
ANISOU 5126  CD2 TYR B 210    16071  13175  10277  -3043  -2319   2004       C  
ATOM   5127  CE1 TYR B 210       2.063  24.768  44.232  1.00138.47           C  
ANISOU 5127  CE1 TYR B 210    20448  17361  14803  -3010  -2997   2004       C  
ATOM   5128  CE2 TYR B 210       1.942  23.885  42.010  1.00116.83           C  
ANISOU 5128  CE2 TYR B 210    17424  14715  12250  -2938  -2470   2020       C  
ATOM   5129  CZ  TYR B 210       2.687  24.349  43.075  1.00136.14           C  
ANISOU 5129  CZ  TYR B 210    19848  17071  14807  -2928  -2819   2019       C  
ATOM   5130  OH  TYR B 210       4.061  24.393  42.982  1.00146.23           O  
ANISOU 5130  OH  TYR B 210    20801  18249  16512  -2828  -2994   2022       O  
ATOM   5131  N   VAL B 211      -4.386  22.069  43.623  1.00 89.56           N  
ANISOU 5131  N   VAL B 211    15242  11363   7422  -3433  -1827   2009       N  
ATOM   5132  CA  VAL B 211      -5.803  21.922  43.973  1.00100.16           C  
ANISOU 5132  CA  VAL B 211    16741  12717   8599  -3570  -1615   1997       C  
ATOM   5133  C   VAL B 211      -6.183  20.442  43.955  1.00109.48           C  
ANISOU 5133  C   VAL B 211    18070  13755   9774  -3600  -1546   2055       C  
ATOM   5134  O   VAL B 211      -5.631  19.660  43.177  1.00112.25           O  
ANISOU 5134  O   VAL B 211    18332  14046  10273  -3515  -1605   2053       O  
ATOM   5135  CB  VAL B 211      -6.753  22.694  43.012  1.00121.17           C  
ANISOU 5135  CB  VAL B 211    19188  15517  11333  -3633  -1427   1887       C  
ATOM   5136  CG1 VAL B 211      -8.154  22.794  43.612  1.00105.44           C  
ANISOU 5136  CG1 VAL B 211    17306  13533   9222  -3772  -1223   1862       C  
ATOM   5137  CG2 VAL B 211      -6.220  24.087  42.688  1.00124.48           C  
ANISOU 5137  CG2 VAL B 211    19426  16052  11819  -3585  -1497   1837       C  
ATOM   5138  N   GLY B 212      -7.129  20.056  44.802  1.00111.22           N  
ANISOU 5138  N   GLY B 212    18521  13903   9836  -3720  -1396   2105       N  
ATOM   5139  CA  GLY B 212      -7.594  18.685  44.798  1.00121.42           C  
ANISOU 5139  CA  GLY B 212    19950  15030  11153  -3780  -1303   2168       C  
ATOM   5140  C   GLY B 212      -8.923  18.636  44.079  1.00120.69           C  
ANISOU 5140  C   GLY B 212    19689  14978  11192  -3916  -1067   2074       C  
ATOM   5141  O   GLY B 212      -8.977  18.341  42.886  1.00103.93           O  
ANISOU 5141  O   GLY B 212    17368  12870   9250  -3883  -1094   1983       O  
ATOM   5142  N   CYS B 213      -9.995  18.950  44.797  1.00133.88           N  
ANISOU 5142  N   CYS B 213    21437  16655  12778  -4056   -841   2083       N  
ATOM   5143  CA  CYS B 213     -11.302  19.090  44.172  1.00137.84           C  
ANISOU 5143  CA  CYS B 213    21712  17197  13462  -4182   -639   1972       C  
ATOM   5144  C   CYS B 213     -11.415  20.462  43.521  1.00144.26           C  
ANISOU 5144  C   CYS B 213    22274  18214  14324  -4127   -680   1837       C  
ATOM   5145  O   CYS B 213     -11.134  21.482  44.149  1.00156.27           O  
ANISOU 5145  O   CYS B 213    23849  19832  15695  -4088   -693   1843       O  
ATOM   5146  CB  CYS B 213     -12.417  18.884  45.197  1.00133.14           C  
ANISOU 5146  CB  CYS B 213    21259  16514  12814  -4350   -332   2035       C  
ATOM   5147  SG  CYS B 213     -12.334  17.295  46.053  1.00204.96           S  
ANISOU 5147  SG  CYS B 213    30720  25329  21827  -4430   -243   2234       S  
ATOM   5148  N   VAL B 214     -11.826  20.481  42.258  1.00135.32           N  
ANISOU 5148  N   VAL B 214    20899  17126  13391  -4114   -721   1713       N  
ATOM   5149  CA  VAL B 214     -11.862  21.717  41.485  1.00120.46           C  
ANISOU 5149  CA  VAL B 214    18813  15410  11548  -4039   -786   1601       C  
ATOM   5150  C   VAL B 214     -13.274  22.271  41.405  1.00107.78           C  
ANISOU 5150  C   VAL B 214    17033  13846  10073  -4140   -636   1490       C  
ATOM   5151  O   VAL B 214     -14.251  21.543  41.589  1.00114.09           O  
ANISOU 5151  O   VAL B 214    17794  14538  11016  -4270   -494   1473       O  
ATOM   5152  CB  VAL B 214     -11.331  21.512  40.061  1.00126.46           C  
ANISOU 5152  CB  VAL B 214    19464  16188  12397  -3917   -947   1533       C  
ATOM   5153  CG1 VAL B 214      -9.893  21.031  40.102  1.00134.00           C  
ANISOU 5153  CG1 VAL B 214    20532  17101  13280  -3799  -1070   1629       C  
ATOM   5154  CG2 VAL B 214     -12.213  20.528  39.304  1.00131.21           C  
ANISOU 5154  CG2 VAL B 214    20004  16678  13172  -3978   -945   1443       C  
ATOM   5155  N   SER B 215     -13.378  23.564  41.124  1.00 97.14           N  
ANISOU 5155  N   SER B 215    15561  12634   8714  -4079   -668   1415       N  
ATOM   5156  CA  SER B 215     -14.682  24.196  41.015  1.00109.17           C  
ANISOU 5156  CA  SER B 215    16892  14196  10393  -4141   -556   1295       C  
ATOM   5157  C   SER B 215     -15.381  23.764  39.737  1.00121.00           C  
ANISOU 5157  C   SER B 215    18201  15652  12122  -4136   -671   1169       C  
ATOM   5158  O   SER B 215     -14.762  23.191  38.841  1.00123.67           O  
ANISOU 5158  O   SER B 215    18587  15958  12443  -4057   -836   1167       O  
ATOM   5159  CB  SER B 215     -14.552  25.717  41.049  1.00105.59           C  
ANISOU 5159  CB  SER B 215    16381  13873   9863  -4057   -591   1248       C  
ATOM   5160  OG  SER B 215     -15.824  26.329  40.942  1.00102.56           O  
ANISOU 5160  OG  SER B 215    15797  13513   9657  -4094   -494   1122       O  
ATOM   5161  N   GLU B 216     -16.680  24.029  39.668  1.00134.33           N  
ANISOU 5161  N   GLU B 216    19679  17326  14036  -4210   -590   1052       N  
ATOM   5162  CA  GLU B 216     -17.472  23.665  38.504  1.00147.20           C  
ANISOU 5162  CA  GLU B 216    21120  18892  15918  -4204   -757    904       C  
ATOM   5163  C   GLU B 216     -17.018  24.724  37.501  1.00153.48           C  
ANISOU 5163  C   GLU B 216    21916  19803  16595  -4022   -972    848       C  
ATOM   5164  O   GLU B 216     -16.949  24.452  36.305  1.00161.22           O  
ANISOU 5164  O   GLU B 216    22910  20751  17594  -3928  -1190    771       O  
ATOM   5165  CB  GLU B 216     -18.961  23.811  38.804  1.00155.99           C  
ANISOU 5165  CB  GLU B 216    21960  19953  17357  -4324   -620    789       C  
ATOM   5166  CG  GLU B 216     -19.461  22.842  39.859  1.00166.37           C  
ANISOU 5166  CG  GLU B 216    23278  21135  18799  -4521   -324    870       C  
ATOM   5167  CD  GLU B 216     -20.940  22.552  39.721  1.00184.30           C  
ANISOU 5167  CD  GLU B 216    25208  23289  21529  -4656   -242    731       C  
ATOM   5168  OE1 GLU B 216     -21.727  23.514  39.607  1.00193.88           O  
ANISOU 5168  OE1 GLU B 216    26177  24567  22921  -4617   -233    607       O  
ATOM   5169  OE2 GLU B 216     -21.315  21.360  39.714  1.00190.20           O  
ANISOU 5169  OE2 GLU B 216    25913  23860  22496  -4800   -198    741       O  
ATOM   5170  N   GLU B 217     -16.725  25.931  37.982  1.00149.53           N  
ANISOU 5170  N   GLU B 217    21434  19418  15965  -3970   -908    885       N  
ATOM   5171  CA  GLU B 217     -16.128  26.940  37.084  1.00144.46           C  
ANISOU 5171  CA  GLU B 217    20832  18860  15196  -3808  -1079    874       C  
ATOM   5172  C   GLU B 217     -15.014  26.390  36.034  1.00108.81           C  
ANISOU 5172  C   GLU B 217    16484  14330  10530  -3692  -1226    929       C  
ATOM   5173  O   GLU B 217     -15.203  26.137  34.841  1.00125.54           O  
ANISOU 5173  O   GLU B 217    18624  16409  12666  -3600  -1392    847       O  
ATOM   5174  CB  GLU B 217     -15.713  28.191  37.863  1.00149.37           C  
ANISOU 5174  CB  GLU B 217    21489  19574  15692  -3784   -989    931       C  
ATOM   5175  CG  GLU B 217     -16.843  28.902  38.578  1.00165.84           C  
ANISOU 5175  CG  GLU B 217    23421  21673  17918  -3837   -858    840       C  
ATOM   5176  CD  GLU B 217     -16.353  30.083  39.383  1.00185.86           C  
ANISOU 5176  CD  GLU B 217    26041  24275  20301  -3802   -787    882       C  
ATOM   5177  OE1 GLU B 217     -15.121  30.226  39.532  1.00178.28           O  
ANISOU 5177  OE1 GLU B 217    25244  23339  19156  -3767   -842    992       O  
ATOM   5178  OE2 GLU B 217     -17.200  30.864  39.869  1.00202.56           O  
ANISOU 5178  OE2 GLU B 217    28049  26404  22512  -3804   -685    793       O  
ATOM   5179  N   THR B 218     -13.944  25.978  36.706  1.00102.08           N  
ANISOU 5179  N   THR B 218    15758  13481   9548  -3713  -1139   1062       N  
ATOM   5180  CA  THR B 218     -12.967  25.079  36.105  1.00101.31           C  
ANISOU 5180  CA  THR B 218    15787  13335   9369  -3640  -1198   1117       C  
ATOM   5181  C   THR B 218     -13.284  23.761  35.407  1.00102.11           C  
ANISOU 5181  C   THR B 218    15931  13319   9548  -3638  -1280   1046       C  
ATOM   5182  O   THR B 218     -12.680  23.424  34.396  1.00101.23           O  
ANISOU 5182  O   THR B 218    15924  13184   9356  -3508  -1365   1031       O  
ATOM   5183  CB  THR B 218     -11.986  24.825  37.263  1.00106.35           C  
ANISOU 5183  CB  THR B 218    16517  13973   9920  -3684  -1108   1258       C  
ATOM   5184  OG1 THR B 218     -11.841  26.024  38.035  1.00114.67           O  
ANISOU 5184  OG1 THR B 218    17545  15109  10916  -3701  -1061   1294       O  
ATOM   5185  CG2 THR B 218     -10.620  24.417  36.729  1.00 96.31           C  
ANISOU 5185  CG2 THR B 218    15330  12685   8578  -3565  -1158   1335       C  
ATOM   5186  N   LEU B 219     -14.240  23.020  35.955  1.00110.11           N  
ANISOU 5186  N   LEU B 219    16871  14240  10725  -3783  -1236   1000       N  
ATOM   5187  CA  LEU B 219     -14.624  21.723  35.406  1.00115.81           C  
ANISOU 5187  CA  LEU B 219    17621  14811  11571  -3813  -1328    922       C  
ATOM   5188  C   LEU B 219     -15.153  21.828  33.974  1.00118.55           C  
ANISOU 5188  C   LEU B 219    17951  15130  11962  -3698  -1555    754       C  
ATOM   5189  O   LEU B 219     -14.807  21.014  33.119  1.00120.15           O  
ANISOU 5189  O   LEU B 219    18294  15242  12115  -3606  -1680    699       O  
ATOM   5190  CB  LEU B 219     -15.675  21.066  36.300  1.00117.21           C  
ANISOU 5190  CB  LEU B 219    17682  14876  11975  -4020  -1205    910       C  
ATOM   5191  CG  LEU B 219     -16.034  19.616  35.987  1.00119.33           C  
ANISOU 5191  CG  LEU B 219    17978  14942  12418  -4097  -1276    855       C  
ATOM   5192  CD1 LEU B 219     -14.870  18.703  36.329  1.00118.52           C  
ANISOU 5192  CD1 LEU B 219    18104  14772  12158  -4060  -1238    993       C  
ATOM   5193  CD2 LEU B 219     -17.288  19.207  36.739  1.00127.15           C  
ANISOU 5193  CD2 LEU B 219    18785  15814  13710  -4319  -1126    830       C  
ATOM   5194  N   LYS B 220     -15.972  22.843  33.713  1.00116.91           N  
ANISOU 5194  N   LYS B 220    17604  14987  11830  -3681  -1624    664       N  
ATOM   5195  CA  LYS B 220     -16.508  23.064  32.373  1.00115.91           C  
ANISOU 5195  CA  LYS B 220    17501  14823  11716  -3547  -1889    504       C  
ATOM   5196  C   LYS B 220     -15.387  23.440  31.411  1.00 99.20           C  
ANISOU 5196  C   LYS B 220    15638  12768   9287  -3336  -1933    559       C  
ATOM   5197  O   LYS B 220     -15.357  22.982  30.272  1.00109.46           O  
ANISOU 5197  O   LYS B 220    17112  13988  10492  -3200  -2114    460       O  
ATOM   5198  CB  LYS B 220     -17.581  24.157  32.386  1.00129.77           C  
ANISOU 5198  CB  LYS B 220    19049  16626  13632  -3555  -1964    409       C  
ATOM   5199  CG  LYS B 220     -18.238  24.405  31.029  1.00145.74           C  
ANISOU 5199  CG  LYS B 220    21114  18585  15676  -3401  -2305    234       C  
ATOM   5200  CD  LYS B 220     -19.249  25.545  31.090  1.00153.54           C  
ANISOU 5200  CD  LYS B 220    21882  19610  16845  -3387  -2396    146       C  
ATOM   5201  CE  LYS B 220     -19.890  25.792  29.730  1.00152.57           C  
ANISOU 5201  CE  LYS B 220    21840  19402  16729  -3207  -2798    -30       C  
ATOM   5202  NZ  LYS B 220     -20.852  26.929  29.768  1.00148.04           N  
ANISOU 5202  NZ  LYS B 220    21048  18848  16353  -3166  -2920   -117       N  
ATOM   5203  N   ILE B 221     -14.460  24.265  31.891  1.00 85.07           N  
ANISOU 5203  N   ILE B 221    13876  11102   7346  -3309  -1753    715       N  
ATOM   5204  CA  ILE B 221     -13.285  24.661  31.120  1.00 87.40           C  
ANISOU 5204  CA  ILE B 221    14366  11447   7396  -3137  -1708    802       C  
ATOM   5205  C   ILE B 221     -12.461  23.435  30.735  1.00 94.08           C  
ANISOU 5205  C   ILE B 221    15371  12211   8162  -3070  -1678    817       C  
ATOM   5206  O   ILE B 221     -11.991  23.322  29.604  1.00 93.30           O  
ANISOU 5206  O   ILE B 221    15478  12083   7888  -2893  -1713    788       O  
ATOM   5207  CB  ILE B 221     -12.411  25.663  31.908  1.00 83.52           C  
ANISOU 5207  CB  ILE B 221    13813  11070   6850  -3165  -1523    965       C  
ATOM   5208  CG1 ILE B 221     -13.111  27.022  31.984  1.00 83.75           C  
ANISOU 5208  CG1 ILE B 221    13746  11162   6912  -3170  -1566    939       C  
ATOM   5209  CG2 ILE B 221     -11.069  25.850  31.241  1.00 67.56           C  
ANISOU 5209  CG2 ILE B 221    11939   9070   4661  -3021  -1417   1074       C  
ATOM   5210  CD1 ILE B 221     -12.519  27.971  33.012  1.00 66.13           C  
ANISOU 5210  CD1 ILE B 221    11429   9014   4684  -3239  -1421   1060       C  
ATOM   5211  N   ILE B 222     -12.270  22.531  31.692  1.00103.19           N  
ANISOU 5211  N   ILE B 222    16459  13318   9433  -3196  -1599    867       N  
ATOM   5212  CA  ILE B 222     -11.602  21.256  31.438  1.00102.04           C  
ANISOU 5212  CA  ILE B 222    16448  13063   9260  -3139  -1592    867       C  
ATOM   5213  C   ILE B 222     -12.384  20.427  30.423  1.00 95.43           C  
ANISOU 5213  C   ILE B 222    15726  12086   8448  -3082  -1800    679       C  
ATOM   5214  O   ILE B 222     -11.810  19.806  29.528  1.00102.99           O  
ANISOU 5214  O   ILE B 222    16889  12970   9271  -2921  -1832    630       O  
ATOM   5215  CB  ILE B 222     -11.417  20.448  32.736  1.00103.22           C  
ANISOU 5215  CB  ILE B 222    16528  13155   9537  -3294  -1503    960       C  
ATOM   5216  CG1 ILE B 222     -10.599  21.255  33.747  1.00105.46           C  
ANISOU 5216  CG1 ILE B 222    16738  13556   9777  -3329  -1360   1124       C  
ATOM   5217  CG2 ILE B 222     -10.699  19.138  32.451  1.00 98.92           C  
ANISOU 5217  CG2 ILE B 222    16128  12475   8981  -3214  -1515    959       C  
ATOM   5218  CD1 ILE B 222     -10.887  20.901  35.182  1.00108.57           C  
ANISOU 5218  CD1 ILE B 222    17084  13913  10255  -3504  -1295   1203       C  
ATOM   5219  N   GLU B 223     -13.702  20.419  30.575  1.00 73.27           N  
ANISOU 5219  N   GLU B 223    12780   9226   5834  -3210  -1944    562       N  
ATOM   5220  CA  GLU B 223     -14.568  19.659  29.685  1.00 87.54           C  
ANISOU 5220  CA  GLU B 223    14655  10872   7733  -3180  -2208    358       C  
ATOM   5221  C   GLU B 223     -14.488  20.170  28.246  1.00103.01           C  
ANISOU 5221  C   GLU B 223    16852  12843   9446  -2940  -2384    252       C  
ATOM   5222  O   GLU B 223     -14.446  19.382  27.304  1.00105.39           O  
ANISOU 5222  O   GLU B 223    17382  13011   9649  -2809  -2551    120       O  
ATOM   5223  CB  GLU B 223     -16.008  19.704  30.195  1.00100.72           C  
ANISOU 5223  CB  GLU B 223    16052  12482   9736  -3375  -2314    257       C  
ATOM   5224  CG  GLU B 223     -16.939  18.710  29.532  1.00115.00           C  
ANISOU 5224  CG  GLU B 223    17858  14074  11761  -3406  -2604     42       C  
ATOM   5225  CD  GLU B 223     -18.357  18.802  30.062  1.00123.62           C  
ANISOU 5225  CD  GLU B 223    18606  15098  13268  -3611  -2675    -55       C  
ATOM   5226  OE1 GLU B 223     -18.613  19.666  30.929  1.00121.48           O  
ANISOU 5226  OE1 GLU B 223    18128  14958  13072  -3709  -2474     44       O  
ATOM   5227  OE2 GLU B 223     -19.213  18.009  29.613  1.00126.84           O  
ANISOU 5227  OE2 GLU B 223    18941  15304  13948  -3673  -2928   -240       O  
ATOM   5228  N   GLU B 224     -14.439  21.491  28.092  1.00111.14           N  
ANISOU 5228  N   GLU B 224    17865  14013  10351  -2872  -2341    316       N  
ATOM   5229  CA  GLU B 224     -14.437  22.129  26.777  1.00107.22           C  
ANISOU 5229  CA  GLU B 224    17630  13517   9590  -2644  -2494    246       C  
ATOM   5230  C   GLU B 224     -13.180  21.831  25.960  1.00107.45           C  
ANISOU 5230  C   GLU B 224    17987  13540   9297  -2435  -2338    311       C  
ATOM   5231  O   GLU B 224     -13.254  21.728  24.736  1.00139.92           O  
ANISOU 5231  O   GLU B 224    22422  17573  13170  -2230  -2496    198       O  
ATOM   5232  CB  GLU B 224     -14.607  23.644  26.920  1.00113.74           C  
ANISOU 5232  CB  GLU B 224    18363  14476  10376  -2633  -2447    334       C  
ATOM   5233  CG  GLU B 224     -16.013  24.077  27.301  1.00136.38           C  
ANISOU 5233  CG  GLU B 224    20962  17325  13531  -2751  -2659    214       C  
ATOM   5234  CD  GLU B 224     -17.073  23.552  26.347  1.00164.72           C  
ANISOU 5234  CD  GLU B 224    24632  20752  17202  -2672  -3066    -28       C  
ATOM   5235  OE1 GLU B 224     -16.819  23.513  25.122  1.00176.35           O  
ANISOU 5235  OE1 GLU B 224    26467  22162  18377  -2448  -3236    -94       O  
ATOM   5236  OE2 GLU B 224     -18.167  23.182  26.823  1.00174.82           O  
ANISOU 5236  OE2 GLU B 224    25619  21952  18853  -2830  -3216   -157       O  
ATOM   5237  N   TRP B 225     -12.032  21.718  26.622  1.00 75.66           N  
ANISOU 5237  N   TRP B 225    13892   9588   5267  -2472  -2031    485       N  
ATOM   5238  CA  TRP B 225     -10.793  21.378  25.926  1.00 76.46           C  
ANISOU 5238  CA  TRP B 225    14238   9675   5138  -2278  -1831    546       C  
ATOM   5239  C   TRP B 225     -10.853  19.979  25.326  1.00118.20           C  
ANISOU 5239  C   TRP B 225    19734  14791  10384  -2183  -1964    383       C  
ATOM   5240  O   TRP B 225     -10.463  19.766  24.179  1.00120.01           O  
ANISOU 5240  O   TRP B 225    20302  14957  10340  -1952  -1952    313       O  
ATOM   5241  CB  TRP B 225      -9.587  21.468  26.855  1.00 74.71           C  
ANISOU 5241  CB  TRP B 225    13829   9542   5015  -2347  -1525    745       C  
ATOM   5242  CG  TRP B 225      -8.409  20.676  26.353  1.00 89.62           C  
ANISOU 5242  CG  TRP B 225    15880  11370   6803  -2177  -1336    770       C  
ATOM   5243  CD1 TRP B 225      -7.995  19.456  26.801  1.00 89.18           C  
ANISOU 5243  CD1 TRP B 225    15787  11220   6878  -2197  -1321    750       C  
ATOM   5244  CD2 TRP B 225      -7.498  21.051  25.311  1.00 98.14           C  
ANISOU 5244  CD2 TRP B 225    17183  12461   7643  -1952  -1106    823       C  
ATOM   5245  NE1 TRP B 225      -6.886  19.046  26.103  1.00 92.36           N  
ANISOU 5245  NE1 TRP B 225    16352  11582   7159  -1986  -1113    768       N  
ATOM   5246  CE2 TRP B 225      -6.559  20.006  25.184  1.00 93.11           C  
ANISOU 5246  CE2 TRP B 225    16606  11745   7028  -1836   -951    816       C  
ATOM   5247  CE3 TRP B 225      -7.384  22.166  24.476  1.00121.28           C  
ANISOU 5247  CE3 TRP B 225    20285  15447  10348  -1831   -994    885       C  
ATOM   5248  CZ2 TRP B 225      -5.520  20.044  24.253  1.00108.47           C  
ANISOU 5248  CZ2 TRP B 225    18748  13673   8792  -1604   -654    859       C  
ATOM   5249  CZ3 TRP B 225      -6.349  22.203  23.551  1.00127.34           C  
ANISOU 5249  CZ3 TRP B 225    21281  16191  10911  -1614   -688    949       C  
ATOM   5250  CH2 TRP B 225      -5.432  21.148  23.449  1.00121.94           C  
ANISOU 5250  CH2 TRP B 225    20625  15437  10270  -1502   -505    930       C  
ATOM   5251  N   PHE B 226     -11.322  19.024  26.122  1.00106.04           N  
ANISOU 5251  N   PHE B 226    18019  13162   9110  -2359  -2070    327       N  
ATOM   5252  CA  PHE B 226     -11.377  17.625  25.708  1.00116.67           C  
ANISOU 5252  CA  PHE B 226    19537  14315  10479  -2301  -2206    175       C  
ATOM   5253  C   PHE B 226     -12.342  17.408  24.547  1.00124.93           C  
ANISOU 5253  C   PHE B 226    20828  15224  11417  -2184  -2560    -70       C  
ATOM   5254  O   PHE B 226     -12.134  16.525  23.715  1.00124.17           O  
ANISOU 5254  O   PHE B 226    21029  14975  11175  -2017  -2660   -215       O  
ATOM   5255  CB  PHE B 226     -11.750  16.740  26.894  1.00120.59           C  
ANISOU 5255  CB  PHE B 226    19789  14723  11309  -2545  -2233    196       C  
ATOM   5256  CG  PHE B 226     -10.618  16.533  27.858  1.00115.63           C  
ANISOU 5256  CG  PHE B 226    19047  14154  10732  -2586  -1956    398       C  
ATOM   5257  CD1 PHE B 226      -9.467  15.872  27.460  1.00110.85           C  
ANISOU 5257  CD1 PHE B 226    18612  13492  10014  -2401  -1820    419       C  
ATOM   5258  CD2 PHE B 226     -10.698  17.001  29.155  1.00104.37           C  
ANISOU 5258  CD2 PHE B 226    17361  12827   9469  -2791  -1845    555       C  
ATOM   5259  CE1 PHE B 226      -8.416  15.684  28.335  1.00 83.60           C  
ANISOU 5259  CE1 PHE B 226    15035  10077   6653  -2421  -1618    592       C  
ATOM   5260  CE2 PHE B 226      -9.650  16.814  30.035  1.00 94.62           C  
ANISOU 5260  CE2 PHE B 226    16054  11626   8271  -2808  -1658    726       C  
ATOM   5261  CZ  PHE B 226      -8.507  16.153  29.621  1.00 87.49           C  
ANISOU 5261  CZ  PHE B 226    15286  10660   7295  -2624  -1565    744       C  
ATOM   5262  N   CYS B 227     -13.410  18.198  24.516  1.00137.44           N  
ANISOU 5262  N   CYS B 227    22288  16845  13087  -2263  -2775   -132       N  
ATOM   5263  CA  CYS B 227     -14.343  18.197  23.392  1.00152.87           C  
ANISOU 5263  CA  CYS B 227    24471  18672  14941  -2130  -3174   -366       C  
ATOM   5264  C   CYS B 227     -13.732  18.875  22.160  1.00151.22           C  
ANISOU 5264  C   CYS B 227    24697  18508  14254  -1823  -3124   -353       C  
ATOM   5265  O   CYS B 227     -14.241  18.738  21.048  1.00166.30           O  
ANISOU 5265  O   CYS B 227    26948  20286  15954  -1636  -3448   -548       O  
ATOM   5266  CB  CYS B 227     -15.645  18.897  23.786  1.00163.25           C  
ANISOU 5266  CB  CYS B 227    25476  20007  16543  -2295  -3416   -429       C  
ATOM   5267  SG  CYS B 227     -16.528  18.106  25.145  1.00149.55           S  
ANISOU 5267  SG  CYS B 227    23257  18185  15379  -2655  -3434   -452       S  
ATOM   5268  N   GLY B 228     -12.637  19.600  22.374  1.00152.11           N  
ANISOU 5268  N   GLY B 228    24808  18786  14201  -1774  -2718   -120       N  
ATOM   5269  CA  GLY B 228     -11.933  20.294  21.311  1.00136.84           C  
ANISOU 5269  CA  GLY B 228    23265  16893  11835  -1508  -2552    -52       C  
ATOM   5270  C   GLY B 228     -11.307  19.357  20.295  1.00138.11           C  
ANISOU 5270  C   GLY B 228    23867  16918  11690  -1255  -2501   -164       C  
ATOM   5271  O   GLY B 228     -10.735  18.332  20.661  1.00130.28           O  
ANISOU 5271  O   GLY B 228    22804  15870  10824  -1283  -2366   -177       O  
ATOM   5272  N   GLU B 229     -11.435  19.702  19.015  1.00153.02           N  
ANISOU 5272  N   GLU B 229    26245  18737  13159   -990  -2619   -252       N  
ATOM   5273  CA  GLU B 229     -10.896  18.886  17.929  1.00165.82           C  
ANISOU 5273  CA  GLU B 229    28377  20215  14411   -704  -2566   -382       C  
ATOM   5274  C   GLU B 229      -9.393  18.704  18.112  1.00160.41           C  
ANISOU 5274  C   GLU B 229    27660  19611  13679   -635  -1984   -191       C  
ATOM   5275  O   GLU B 229      -8.839  17.643  17.819  1.00164.33           O  
ANISOU 5275  O   GLU B 229    28331  19996  14111   -503  -1880   -291       O  
ATOM   5276  CB  GLU B 229     -11.179  19.532  16.566  1.00181.76           C  
ANISOU 5276  CB  GLU B 229    30764  22166  16132   -401  -2642   -436       C  
ATOM   5277  CG  GLU B 229     -12.638  19.514  16.129  1.00188.12           C  
ANISOU 5277  CG  GLU B 229    31569  22834  17075   -381  -3236   -668       C  
ATOM   5278  CD  GLU B 229     -13.232  18.121  16.094  1.00192.81           C  
ANISOU 5278  CD  GLU B 229    32212  23229  17819   -415  -3634   -951       C  
ATOM   5279  OE1 GLU B 229     -12.574  17.196  15.573  1.00196.67           O  
ANISOU 5279  OE1 GLU B 229    33020  23607  18100   -243  -3505  -1039       O  
ATOM   5280  OE2 GLU B 229     -14.366  17.954  16.589  1.00196.26           O  
ANISOU 5280  OE2 GLU B 229    32356  23603  18610   -617  -4070  -1091       O  
ATOM   5281  N   LYS B 230      -8.753  19.759  18.605  1.00154.20           N  
ANISOU 5281  N   LYS B 230    26627  19000  12963   -723  -1625     73       N  
ATOM   5282  CA  LYS B 230      -7.321  19.780  18.888  1.00144.72           C  
ANISOU 5282  CA  LYS B 230    25286  17881  11821   -690  -1080    275       C  
ATOM   5283  C   LYS B 230      -6.895  18.688  19.861  1.00142.67           C  
ANISOU 5283  C   LYS B 230    24674  17599  11935   -828  -1039    256       C  
ATOM   5284  O   LYS B 230      -5.849  18.069  19.687  1.00154.32           O  
ANISOU 5284  O   LYS B 230    26204  19035  13397   -687   -724    281       O  
ATOM   5285  CB  LYS B 230      -6.927  21.153  19.428  1.00153.50           C  
ANISOU 5285  CB  LYS B 230    26111  19161  13050   -826   -821    538       C  
ATOM   5286  CG  LYS B 230      -7.295  22.277  18.469  1.00178.27           C  
ANISOU 5286  CG  LYS B 230    29623  22298  15814   -683   -841    587       C  
ATOM   5287  CD  LYS B 230      -7.150  23.646  19.104  1.00177.97           C  
ANISOU 5287  CD  LYS B 230    29276  22396  15950   -857   -687    819       C  
ATOM   5288  CE  LYS B 230      -7.462  24.750  18.102  1.00177.64           C  
ANISOU 5288  CE  LYS B 230    29495  22322  15680   -680   -677    868       C  
ATOM   5289  NZ  LYS B 230      -7.321  26.110  18.695  1.00170.79           N  
ANISOU 5289  NZ  LYS B 230    28344  21557  14990   -841   -537   1085       N  
ATOM   5290  N   ALA B 231      -7.705  18.472  20.892  1.00136.19           N  
ANISOU 5290  N   ALA B 231    23500  16792  11453  -1094  -1342    219       N  
ATOM   5291  CA  ALA B 231      -7.415  17.475  21.917  1.00133.06           C  
ANISOU 5291  CA  ALA B 231    22798  16356  11404  -1245  -1336    224       C  
ATOM   5292  C   ALA B 231      -7.356  16.059  21.345  1.00139.17           C  
ANISOU 5292  C   ALA B 231    23849  16925  12104  -1086  -1448     18       C  
ATOM   5293  O   ALA B 231      -6.515  15.257  21.753  1.00129.92           O  
ANISOU 5293  O   ALA B 231    22573  15703  11088  -1058  -1265     54       O  
ATOM   5294  CB  ALA B 231      -8.447  17.550  23.026  1.00128.26           C  
ANISOU 5294  CB  ALA B 231    21840  15776  11117  -1550  -1620    221       C  
ATOM   5295  N   GLY B 232      -8.273  15.752  20.428  1.00153.11           N  
ANISOU 5295  N   GLY B 232    25966  18553  13654   -978  -1788   -212       N  
ATOM   5296  CA  GLY B 232      -8.339  14.448  19.785  1.00158.66           C  
ANISOU 5296  CA  GLY B 232    26989  19031  14265   -815  -1959   -449       C  
ATOM   5297  C   GLY B 232      -7.121  14.153  18.927  1.00160.19           C  
ANISOU 5297  C   GLY B 232    27526  19189  14150   -491  -1573   -446       C  
ATOM   5298  O   GLY B 232      -6.563  13.060  18.958  1.00162.20           O  
ANISOU 5298  O   GLY B 232    27831  19310  14486   -397  -1492   -526       O  
ATOM   5299  N   GLU B 233      -6.721  15.146  18.146  1.00160.93           N  
ANISOU 5299  N   GLU B 233    27864  19386  13895   -312  -1314   -349       N  
ATOM   5300  CA  GLU B 233      -5.595  15.040  17.225  1.00155.44           C  
ANISOU 5300  CA  GLU B 233    27524  18662  12873     11   -866   -327       C  
ATOM   5301  C   GLU B 233      -4.261  14.868  17.951  1.00146.80           C  
ANISOU 5301  C   GLU B 233    26043  17647  12086    -15   -392   -134       C  
ATOM   5302  O   GLU B 233      -3.368  14.163  17.476  1.00138.75           O  
ANISOU 5302  O   GLU B 233    25199  16534  10985    224    -93   -188       O  
ATOM   5303  CB  GLU B 233      -5.529  16.280  16.332  1.00158.14           C  
ANISOU 5303  CB  GLU B 233    28193  19093  12799    164   -666   -217       C  
ATOM   5304  CG  GLU B 233      -6.810  16.574  15.557  1.00165.46           C  
ANISOU 5304  CG  GLU B 233    29531  19933  13402    227  -1169   -399       C  
ATOM   5305  CD  GLU B 233      -6.823  17.970  14.963  1.00162.12           C  
ANISOU 5305  CD  GLU B 233    29228  19612  12760    308   -995   -226       C  
ATOM   5306  OE1 GLU B 233      -5.790  18.666  15.055  1.00157.58           O  
ANISOU 5306  OE1 GLU B 233    28574  19158  12141    327   -457     24       O  
ATOM   5307  OE2 GLU B 233      -7.867  18.375  14.412  1.00156.75           O  
ANISOU 5307  OE2 GLU B 233    28628  18870  12058    347  -1390   -334       O  
ATOM   5308  N   VAL B 234      -4.139  15.522  19.103  1.00163.93           N  
ANISOU 5308  N   VAL B 234    27690  19977  14619   -290   -344     77       N  
ATOM   5309  CA  VAL B 234      -2.847  15.780  19.742  1.00181.21           C  
ANISOU 5309  CA  VAL B 234    29496  22268  17088   -315     94    297       C  
ATOM   5310  C   VAL B 234      -2.195  14.623  20.519  1.00174.15           C  
ANISOU 5310  C   VAL B 234    28333  21283  16551   -333    112    274       C  
ATOM   5311  O   VAL B 234      -1.000  14.689  20.810  1.00168.10           O  
ANISOU 5311  O   VAL B 234    27311  20559  16001   -270    477    413       O  
ATOM   5312  CB  VAL B 234      -2.968  16.971  20.710  1.00187.30           C  
ANISOU 5312  CB  VAL B 234    29842  23225  18100   -595     86    517       C  
ATOM   5313  CG1 VAL B 234      -3.541  16.514  22.045  1.00176.22           C  
ANISOU 5313  CG1 VAL B 234    28072  21825  17059   -879   -258    512       C  
ATOM   5314  CG2 VAL B 234      -1.621  17.596  20.909  1.00198.28           C  
ANISOU 5314  CG2 VAL B 234    30960  24708  19669   -558    570    736       C  
ATOM   5315  N   GLY B 235      -2.957  13.585  20.861  1.00170.83           N  
ANISOU 5315  N   GLY B 235    27958  20721  16227   -418   -283    106       N  
ATOM   5316  CA  GLY B 235      -2.480  12.544  21.765  1.00199.56           C  
ANISOU 5316  CA  GLY B 235    31340  24260  20224   -477   -329    113       C  
ATOM   5317  C   GLY B 235      -1.060  12.066  21.499  1.00228.19           C  
ANISOU 5317  C   GLY B 235    34934  27832  23936   -219     74    142       C  
ATOM   5318  O   GLY B 235      -0.295  11.858  22.433  1.00216.23           O  
ANISOU 5318  O   GLY B 235    33045  26331  22782   -286    157    272       O  
ATOM   5319  N   ASP B 236      -0.718  11.926  20.218  1.00248.50           N  
ANISOU 5319  N   ASP B 236    37909  30336  26173     90    323     19       N  
ATOM   5320  CA  ASP B 236       0.648  11.658  19.745  1.00252.58           C  
ANISOU 5320  CA  ASP B 236    38420  30815  26736    378    817     45       C  
ATOM   5321  C   ASP B 236       1.412  10.636  20.591  1.00240.31           C  
ANISOU 5321  C   ASP B 236    36544  29146  25617    396    805     51       C  
ATOM   5322  O   ASP B 236       0.998   9.483  20.725  1.00233.39           O  
ANISOU 5322  O   ASP B 236    35818  28080  24781    416    502   -117       O  
ATOM   5323  CB  ASP B 236       1.443  12.973  19.678  1.00258.86           C  
ANISOU 5323  CB  ASP B 236    38977  31802  27578    368   1267    285       C  
ATOM   5324  CG  ASP B 236       2.724  12.851  18.863  1.00265.77           C  
ANISOU 5324  CG  ASP B 236    39923  32628  28427    694   1862    297       C  
ATOM   5325  OD1 ASP B 236       2.837  11.891  18.073  1.00268.30           O  
ANISOU 5325  OD1 ASP B 236    40627  32782  28533    973   1938     92       O  
ATOM   5326  OD2 ASP B 236       3.617  13.710  19.026  1.00266.11           O  
ANISOU 5326  OD2 ASP B 236    39630  32786  28693    668   2262    505       O  
ATOM   5327  N   ASN B 237       2.531  11.077  21.157  1.00249.54           N  
ANISOU 5327  N   ASN B 237    37271  30409  27133    390   1112    244       N  
ATOM   5328  CA  ASN B 237       3.335  10.258  22.052  1.00240.99           C  
ANISOU 5328  CA  ASN B 237    35838  29225  26503    410   1070    278       C  
ATOM   5329  C   ASN B 237       3.975  11.095  23.159  1.00236.51           C  
ANISOU 5329  C   ASN B 237    34714  28808  26339    209   1112    523       C  
ATOM   5330  O   ASN B 237       4.248  12.279  22.963  1.00235.95           O  
ANISOU 5330  O   ASN B 237    34502  28902  26247    153   1373    663       O  
ATOM   5331  CB  ASN B 237       4.413   9.521  21.250  1.00232.44           C  
ANISOU 5331  CB  ASN B 237    34857  27999  25459    791   1470    164       C  
ATOM   5332  CG  ASN B 237       5.410  10.468  20.598  1.00233.79           C  
ANISOU 5332  CG  ASN B 237    34892  28294  25645    945   2068    288       C  
ATOM   5333  OD1 ASN B 237       5.131  11.653  20.412  1.00236.86           O  
ANISOU 5333  OD1 ASN B 237    35277  28851  25867    804   2183    421       O  
ATOM   5334  ND2 ASN B 237       6.578   9.944  20.239  1.00236.12           N  
ANISOU 5334  ND2 ASN B 237    35067  28484  26162   1237   2472    247       N  
ATOM   5335  N   GLY B 238       4.202  10.496  24.326  1.00233.96           N  
ANISOU 5335  N   GLY B 238    34108  28409  26376    103    833    576       N  
ATOM   5336  CA  GLY B 238       3.727   9.161  24.645  1.00239.88           C  
ANISOU 5336  CA  GLY B 238    35051  28948  27144    119    490    440       C  
ATOM   5337  C   GLY B 238       4.669   8.029  24.290  1.00246.69           C  
ANISOU 5337  C   GLY B 238    35943  29603  28187    442    648    319       C  
ATOM   5338  O   GLY B 238       4.312   6.866  24.449  1.00247.00           O  
ANISOU 5338  O   GLY B 238    36182  29429  28237    482    379    194       O  
ATOM   5339  N   ILE B 239       5.867   8.375  23.825  1.00248.80           N  
ANISOU 5339  N   ILE B 239    35994  29913  28627    669   1096    359       N  
ATOM   5340  CA  ILE B 239       6.848   7.405  23.339  1.00265.46           C  
ANISOU 5340  CA  ILE B 239    38109  31833  30921   1025   1343    231       C  
ATOM   5341  C   ILE B 239       7.250   6.497  24.512  1.00271.13           C  
ANISOU 5341  C   ILE B 239    38563  32384  32071   1004    991    268       C  
ATOM   5342  O   ILE B 239       7.324   6.965  25.650  1.00261.96           O  
ANISOU 5342  O   ILE B 239    37065  31307  31163    773    749    449       O  
ATOM   5343  CB  ILE B 239       8.079   8.152  22.710  1.00207.12           C  
ANISOU 5343  CB  ILE B 239    30440  24543  23712   1232   1953    307       C  
ATOM   5344  CG1 ILE B 239       8.741   7.347  21.584  1.00209.72           C  
ANISOU 5344  CG1 ILE B 239    31010  24707  23965   1649   2375    113       C  
ATOM   5345  CG2 ILE B 239       9.085   8.587  23.772  1.00206.20           C  
ANISOU 5345  CG2 ILE B 239    29679  24479  24190   1143   1939    496       C  
ATOM   5346  CD1 ILE B 239      10.074   7.892  21.129  1.00212.99           C  
ANISOU 5346  CD1 ILE B 239    31063  25172  24691   1860   3006    195       C  
ATOM   5347  N   GLY B 240       7.473   5.203  24.271  1.00279.08           N  
ANISOU 5347  N   GLY B 240    39760  33136  33140   1248    931     98       N  
ATOM   5348  CA  GLY B 240       7.480   4.580  22.952  1.00283.35           C  
ANISOU 5348  CA  GLY B 240    40723  33548  33390   1562   1211   -141       C  
ATOM   5349  C   GLY B 240       6.266   4.171  22.107  1.00279.79           C  
ANISOU 5349  C   GLY B 240    40882  33013  32412   1553   1046   -348       C  
ATOM   5350  O   GLY B 240       6.409   4.143  20.884  1.00282.88           O  
ANISOU 5350  O   GLY B 240    41607  33379  32494   1820   1391   -509       O  
ATOM   5351  N   SER B 241       5.092   3.855  22.666  1.00255.55           N  
ANISOU 5351  N   SER B 241    37982  29882  29232   1271    548   -359       N  
ATOM   5352  CA  SER B 241       4.763   3.932  24.086  1.00221.74           C  
ANISOU 5352  CA  SER B 241    33400  25627  25222    941    165   -163       C  
ATOM   5353  C   SER B 241       5.451   2.865  24.917  1.00207.56           C  
ANISOU 5353  C   SER B 241    31432  23597  23834   1045    -16   -139       C  
ATOM   5354  O   SER B 241       5.739   1.767  24.439  1.00210.24           O  
ANISOU 5354  O   SER B 241    31989  23683  24209   1311     -2   -323       O  
ATOM   5355  CB  SER B 241       3.245   3.826  24.281  1.00197.05           C  
ANISOU 5355  CB  SER B 241    30551  22470  21850    635   -241   -207       C  
ATOM   5356  OG  SER B 241       2.561   4.877  23.617  1.00182.59           O  
ANISOU 5356  OG  SER B 241    28853  20854  19671    530   -143   -217       O  
ATOM   5357  N   ASP B 242       5.700   3.202  26.175  1.00186.97           N  
ANISOU 5357  N   ASP B 242    28463  21059  21519    844   -209     85       N  
ATOM   5358  CA  ASP B 242       6.277   2.267  27.119  1.00181.39           C  
ANISOU 5358  CA  ASP B 242    27614  20124  21181    915   -460    145       C  
ATOM   5359  C   ASP B 242       5.483   2.342  28.410  1.00174.26           C  
ANISOU 5359  C   ASP B 242    26697  19222  20290    549   -873    329       C  
ATOM   5360  O   ASP B 242       5.765   3.179  29.268  1.00173.50           O  
ANISOU 5360  O   ASP B 242    26293  19300  20329    392   -927    526       O  
ATOM   5361  CB  ASP B 242       7.756   2.580  27.362  1.00196.97           C  
ANISOU 5361  CB  ASP B 242    29121  22147  23571   1137   -239    233       C  
ATOM   5362  CG  ASP B 242       8.490   1.447  28.055  1.00214.74           C  
ANISOU 5362  CG  ASP B 242    31274  24107  26210   1329   -481    234       C  
ATOM   5363  OD1 ASP B 242       7.900   0.801  28.946  1.00222.43           O  
ANISOU 5363  OD1 ASP B 242    32421  24913  27180   1157   -899    308       O  
ATOM   5364  OD2 ASP B 242       9.663   1.200  27.707  1.00218.98           O  
ANISOU 5364  OD2 ASP B 242    31563  24568  27069   1659   -238    168       O  
ATOM   5365  N   VAL B 243       4.475   1.483  28.532  1.00170.31           N  
ANISOU 5365  N   VAL B 243    26544  18516  19650    413  -1148    260       N  
ATOM   5366  CA  VAL B 243       3.661   1.442  29.738  1.00158.70           C  
ANISOU 5366  CA  VAL B 243    25106  17009  18185     69  -1482    437       C  
ATOM   5367  C   VAL B 243       4.556   1.151  30.943  1.00171.70           C  
ANISOU 5367  C   VAL B 243    26535  18548  20154    123  -1667    625       C  
ATOM   5368  O   VAL B 243       4.311   1.647  32.037  1.00174.94           O  
ANISOU 5368  O   VAL B 243    26848  19049  20573   -118  -1842    828       O  
ATOM   5369  CB  VAL B 243       2.528   0.399  29.634  1.00146.57           C  
ANISOU 5369  CB  VAL B 243    23957  15200  16535    -67  -1718    326       C  
ATOM   5370  CG1 VAL B 243       1.515   0.826  28.581  1.00140.26           C  
ANISOU 5370  CG1 VAL B 243    23354  14516  15424   -163  -1633    149       C  
ATOM   5371  CG2 VAL B 243       3.084  -0.983  29.313  1.00152.13           C  
ANISOU 5371  CG2 VAL B 243    24849  15547  17408    227  -1786    180       C  
ATOM   5372  N   GLY B 244       5.599   0.353  30.724  1.00189.21           N  
ANISOU 5372  N   GLY B 244    28696  20565  22630    461  -1636    544       N  
ATOM   5373  CA  GLY B 244       6.582   0.058  31.749  1.00198.05           C  
ANISOU 5373  CA  GLY B 244    29594  21561  24095    581  -1840    694       C  
ATOM   5374  C   GLY B 244       7.317   1.296  32.232  1.00202.13           C  
ANISOU 5374  C   GLY B 244    29678  22356  24765    545  -1765    840       C  
ATOM   5375  O   GLY B 244       7.407   1.533  33.433  1.00198.56           O  
ANISOU 5375  O   GLY B 244    29138  21905  24399    401  -2050   1032       O  
ATOM   5376  N   MET B 245       7.834   2.089  31.295  1.00202.63           N  
ANISOU 5376  N   MET B 245    29500  22637  24853    675  -1382    750       N  
ATOM   5377  CA  MET B 245       8.532   3.329  31.637  1.00188.81           C  
ANISOU 5377  CA  MET B 245    27314  21138  23287    626  -1278    875       C  
ATOM   5378  C   MET B 245       7.589   4.313  32.306  1.00172.78           C  
ANISOU 5378  C   MET B 245    25336  19325  20986    242  -1413   1025       C  
ATOM   5379  O   MET B 245       7.951   4.967  33.283  1.00180.25           O  
ANISOU 5379  O   MET B 245    26047  20358  22084    130  -1602   1181       O  
ATOM   5380  CB  MET B 245       9.145   3.982  30.394  1.00193.30           C  
ANISOU 5380  CB  MET B 245    27668  21875  23902    814   -769    760       C  
ATOM   5381  CG  MET B 245       9.667   5.399  30.632  1.00192.17           C  
ANISOU 5381  CG  MET B 245    27101  21997  23919    697   -622    892       C  
ATOM   5382  SD  MET B 245      10.223   6.258  29.142  1.00153.98           S  
ANISOU 5382  SD  MET B 245    22083  17349  19072    866     47    800       S  
ATOM   5383  CE  MET B 245      11.663   5.288  28.698  1.00183.00           C  
ANISOU 5383  CE  MET B 245    25494  20789  23250   1324    272    671       C  
ATOM   5384  N   LEU B 246       6.380   4.418  31.767  1.00168.46           N  
ANISOU 5384  N   LEU B 246    25100  18854  20054     56  -1332    959       N  
ATOM   5385  CA  LEU B 246       5.376   5.315  32.319  1.00160.85           C  
ANISOU 5385  CA  LEU B 246    24193  18085  18836   -296  -1430   1077       C  
ATOM   5386  C   LEU B 246       4.987   4.882  33.731  1.00160.81           C  
ANISOU 5386  C   LEU B 246    24315  17941  18843   -483  -1816   1239       C  
ATOM   5387  O   LEU B 246       4.989   5.693  34.653  1.00160.80           O  
ANISOU 5387  O   LEU B 246    24181  18075  18841   -654  -1943   1392       O  
ATOM   5388  CB  LEU B 246       4.143   5.362  31.415  1.00148.88           C  
ANISOU 5388  CB  LEU B 246    22978  16629  16961   -426  -1307    948       C  
ATOM   5389  CG  LEU B 246       4.149   6.422  30.310  1.00145.55           C  
ANISOU 5389  CG  LEU B 246    22473  16455  16374   -386   -959    872       C  
ATOM   5390  CD1 LEU B 246       2.821   6.422  29.570  1.00148.01           C  
ANISOU 5390  CD1 LEU B 246    23117  16792  16329   -523   -960    746       C  
ATOM   5391  CD2 LEU B 246       4.463   7.805  30.865  1.00145.25           C  
ANISOU 5391  CD2 LEU B 246    22110  16670  16407   -535   -902   1036       C  
ATOM   5392  N   ARG B 247       4.666   3.598  33.892  1.00150.95           N  
ANISOU 5392  N   ARG B 247    23356  16402  17595   -441  -1992   1205       N  
ATOM   5393  CA  ARG B 247       4.273   3.044  35.189  1.00143.12           C  
ANISOU 5393  CA  ARG B 247    22566  15226  16587   -605  -2320   1375       C  
ATOM   5394  C   ARG B 247       5.432   3.091  36.184  1.00140.90           C  
ANISOU 5394  C   ARG B 247    22085  14881  16570   -458  -2553   1515       C  
ATOM   5395  O   ARG B 247       5.221   3.273  37.383  1.00144.67           O  
ANISOU 5395  O   ARG B 247    22662  15336  16970   -622  -2797   1694       O  
ATOM   5396  CB  ARG B 247       3.762   1.610  35.031  1.00146.46           C  
ANISOU 5396  CB  ARG B 247    23342  15309  16997   -573  -2434   1305       C  
ATOM   5397  CG  ARG B 247       3.067   1.033  36.258  1.00137.14           C  
ANISOU 5397  CG  ARG B 247    22450  13921  15736   -802  -2695   1495       C  
ATOM   5398  CD  ARG B 247       2.305  -0.236  35.897  1.00127.79           C  
ANISOU 5398  CD  ARG B 247    21605  12416  14534   -843  -2744   1406       C  
ATOM   5399  NE  ARG B 247       3.123  -1.154  35.109  1.00124.10           N  
ANISOU 5399  NE  ARG B 247    21151  11735  14267   -496  -2741   1233       N  
ATOM   5400  CZ  ARG B 247       2.645  -2.199  34.441  1.00118.68           C  
ANISOU 5400  CZ  ARG B 247    20723  10779  13591   -453  -2754   1075       C  
ATOM   5401  NH1 ARG B 247       1.346  -2.463  34.460  1.00123.32           N  
ANISOU 5401  NH1 ARG B 247    21543  11273  14040   -756  -2784   1070       N  
ATOM   5402  NH2 ARG B 247       3.465  -2.978  33.749  1.00115.44           N  
ANISOU 5402  NH2 ARG B 247    20326  10178  13358   -105  -2737    908       N  
ATOM   5403  N   GLU B 248       6.653   2.919  35.681  1.00139.65           N  
ANISOU 5403  N   GLU B 248    21653  14679  16728   -137  -2481   1423       N  
ATOM   5404  CA  GLU B 248       7.850   3.062  36.506  1.00136.38           C  
ANISOU 5404  CA  GLU B 248    20961  14210  16648     29  -2722   1522       C  
ATOM   5405  C   GLU B 248       7.963   4.509  36.960  1.00125.77           C  
ANISOU 5405  C   GLU B 248    19346  13159  15283   -146  -2712   1617       C  
ATOM   5406  O   GLU B 248       8.355   4.792  38.092  1.00125.81           O  
ANISOU 5406  O   GLU B 248    19294  13131  15374   -181  -3039   1754       O  
ATOM   5407  CB  GLU B 248       9.101   2.640  35.734  1.00144.35           C  
ANISOU 5407  CB  GLU B 248    21661  15120  18063    411  -2578   1378       C  
ATOM   5408  CG  GLU B 248      10.415   2.937  36.433  1.00159.52           C  
ANISOU 5408  CG  GLU B 248    23176  17004  20429    596  -2810   1446       C  
ATOM   5409  CD  GLU B 248      11.611   2.456  35.635  1.00175.59           C  
ANISOU 5409  CD  GLU B 248    24872  18922  22921    982  -2619   1292       C  
ATOM   5410  OE1 GLU B 248      11.428   2.072  34.459  1.00174.94           O  
ANISOU 5410  OE1 GLU B 248    24881  18837  22750   1101  -2242   1130       O  
ATOM   5411  OE2 GLU B 248      12.733   2.457  36.182  1.00186.77           O  
ANISOU 5411  OE2 GLU B 248    25935  20237  24792   1179  -2853   1323       O  
ATOM   5412  N   ALA B 249       7.615   5.418  36.054  1.00123.91           N  
ANISOU 5412  N   ALA B 249    18976  13187  14916   -245  -2352   1538       N  
ATOM   5413  CA  ALA B 249       7.586   6.844  36.347  1.00109.88           C  
ANISOU 5413  CA  ALA B 249    16970  11685  13095   -433  -2301   1614       C  
ATOM   5414  C   ALA B 249       6.358   7.183  37.192  1.00106.62           C  
ANISOU 5414  C   ALA B 249    16867  11342  12302   -761  -2458   1731       C  
ATOM   5415  O   ALA B 249       6.404   8.098  38.011  1.00101.08           O  
ANISOU 5415  O   ALA B 249    16067  10766  11572   -902  -2602   1835       O  
ATOM   5416  CB  ALA B 249       7.601   7.660  35.065  1.00108.40           C  
ANISOU 5416  CB  ALA B 249    16587  11723  12878   -415  -1853   1505       C  
ATOM   5417  N   VAL B 250       5.253   6.470  36.972  1.00117.31           N  
ANISOU 5417  N   VAL B 250    18583  12604  13384   -881  -2415   1701       N  
ATOM   5418  CA  VAL B 250       4.055   6.670  37.788  1.00116.04           C  
ANISOU 5418  CA  VAL B 250    18704  12476  12912  -1188  -2519   1813       C  
ATOM   5419  C   VAL B 250       4.364   6.275  39.227  1.00121.63           C  
ANISOU 5419  C   VAL B 250    19572  13001  13639  -1195  -2881   1986       C  
ATOM   5420  O   VAL B 250       3.966   6.960  40.161  1.00125.81           O  
ANISOU 5420  O   VAL B 250    20188  13626  13990  -1384  -2989   2107       O  
ATOM   5421  CB  VAL B 250       2.836   5.838  37.295  1.00164.05           C  
ANISOU 5421  CB  VAL B 250    25108  18434  18789  -1317  -2423   1743       C  
ATOM   5422  CG1 VAL B 250       1.727   5.832  38.341  1.00160.60           C  
ANISOU 5422  CG1 VAL B 250    24945  17957  18120  -1615  -2531   1887       C  
ATOM   5423  CG2 VAL B 250       2.297   6.370  35.988  1.00158.93           C  
ANISOU 5423  CG2 VAL B 250    24383  17975  18030  -1347  -2128   1578       C  
ATOM   5424  N   LEU B 251       5.086   5.170  39.392  1.00116.33           N  
ANISOU 5424  N   LEU B 251    18972  12055  13173   -966  -3074   1992       N  
ATOM   5425  CA  LEU B 251       5.455   4.673  40.713  1.00112.83           C  
ANISOU 5425  CA  LEU B 251    18739  11390  12740   -923  -3460   2159       C  
ATOM   5426  C   LEU B 251       6.382   5.639  41.437  1.00121.39           C  
ANISOU 5426  C   LEU B 251    19559  12594  13970   -857  -3689   2219       C  
ATOM   5427  O   LEU B 251       6.210   5.913  42.624  1.00139.46           O  
ANISOU 5427  O   LEU B 251    22069  14850  16070   -966  -3948   2365       O  
ATOM   5428  CB  LEU B 251       6.124   3.298  40.590  1.00119.93           C  
ANISOU 5428  CB  LEU B 251    19736  11955  13878   -647  -3627   2131       C  
ATOM   5429  CG  LEU B 251       6.505   2.512  41.849  1.00125.66           C  
ANISOU 5429  CG  LEU B 251    20763  12371  14613   -552  -4057   2305       C  
ATOM   5430  CD1 LEU B 251       6.274   1.026  41.613  1.00123.57           C  
ANISOU 5430  CD1 LEU B 251    20810  11758  14385   -454  -4090   2296       C  
ATOM   5431  CD2 LEU B 251       7.954   2.760  42.264  1.00111.81           C  
ANISOU 5431  CD2 LEU B 251    18689  10576  13217   -270  -4379   2304       C  
ATOM   5432  N   ASN B 252       7.362   6.152  40.703  1.00128.09           N  
ANISOU 5432  N   ASN B 252    19943  13564  15162   -678  -3583   2100       N  
ATOM   5433  CA  ASN B 252       8.429   6.963  41.281  1.00133.97           C  
ANISOU 5433  CA  ASN B 252    20349  14368  16184   -581  -3831   2126       C  
ATOM   5434  C   ASN B 252       7.917   8.328  41.773  1.00140.81           C  
ANISOU 5434  C   ASN B 252    21195  15489  16818   -843  -3812   2183       C  
ATOM   5435  O   ASN B 252       8.459   8.903  42.714  1.00143.08           O  
ANISOU 5435  O   ASN B 252    21414  15768  17183   -834  -4148   2246       O  
ATOM   5436  CB  ASN B 252       9.542   7.131  40.240  1.00131.05           C  
ANISOU 5436  CB  ASN B 252    19455  14049  16290   -341  -3624   1982       C  
ATOM   5437  CG  ASN B 252      10.844   7.634  40.827  1.00137.93           C  
ANISOU 5437  CG  ASN B 252    19917  14878  17611   -182  -3943   1992       C  
ATOM   5438  OD1 ASN B 252      10.888   8.178  41.926  1.00142.14           O  
ANISOU 5438  OD1 ASN B 252    20531  15412  18063   -280  -4309   2087       O  
ATOM   5439  ND2 ASN B 252      11.928   7.436  40.085  1.00144.41           N  
ANISOU 5439  ND2 ASN B 252    20292  15645  18934     78  -3808   1881       N  
ATOM   5440  N   ASN B 253       6.840   8.818  41.166  1.00161.15           N  
ANISOU 5440  N   ASN B 253    23858  18267  19104  -1065  -3455   2150       N  
ATOM   5441  CA  ASN B 253       6.322  10.158  41.462  1.00162.48           C  
ANISOU 5441  CA  ASN B 253    23977  18683  19077  -1297  -3383   2178       C  
ATOM   5442  C   ASN B 253       5.192  10.175  42.495  1.00138.80           C  
ANISOU 5442  C   ASN B 253    21429  15668  15641  -1530  -3486   2299       C  
ATOM   5443  O   ASN B 253       4.407  11.125  42.559  1.00136.34           O  
ANISOU 5443  O   ASN B 253    21143  15557  15102  -1743  -3329   2302       O  
ATOM   5444  CB  ASN B 253       5.845  10.836  40.173  1.00171.90           C  
ANISOU 5444  CB  ASN B 253    24972  20111  20231  -1386  -2937   2069       C  
ATOM   5445  CG  ASN B 253       6.985  11.160  39.221  1.00175.59           C  
ANISOU 5445  CG  ASN B 253    24979  20632  21105  -1185  -2759   1973       C  
ATOM   5446  OD1 ASN B 253       7.614  12.213  39.326  1.00174.59           O  
ANISOU 5446  OD1 ASN B 253    24527  20623  21184  -1202  -2774   1979       O  
ATOM   5447  ND2 ASN B 253       7.249  10.261  38.281  1.00180.24           N  
ANISOU 5447  ND2 ASN B 253    25543  21119  21821   -996  -2566   1881       N  
ATOM   5448  N   GLY B 254       5.102   9.122  43.297  1.00133.84           N  
ANISOU 5448  N   GLY B 254    21167  14785  14900  -1481  -3726   2403       N  
ATOM   5449  CA  GLY B 254       3.996   8.978  44.224  1.00129.51           C  
ANISOU 5449  CA  GLY B 254    21084  14184  13939  -1696  -3741   2534       C  
ATOM   5450  C   GLY B 254       2.917   8.172  43.542  1.00129.28           C  
ANISOU 5450  C   GLY B 254    21235  14097  13788  -1821  -3437   2509       C  
ATOM   5451  O   GLY B 254       3.142   7.635  42.471  1.00135.50           O  
ANISOU 5451  O   GLY B 254    21849  14852  14782  -1703  -3300   2392       O  
ATOM   5452  N   GLY B 255       1.746   8.073  44.152  1.00133.11           N  
ANISOU 5452  N   GLY B 255    22067  14552  13956  -2055  -3329   2610       N  
ATOM   5453  CA  GLY B 255       0.661   7.340  43.530  1.00166.27           C  
ANISOU 5453  CA  GLY B 255    26399  18677  18099  -2203  -3064   2576       C  
ATOM   5454  C   GLY B 255       0.054   8.023  42.316  1.00167.35           C  
ANISOU 5454  C   GLY B 255    26244  19064  18279  -2303  -2762   2405       C  
ATOM   5455  O   GLY B 255      -0.353   7.372  41.351  1.00148.10           O  
ANISOU 5455  O   GLY B 255    23784  16558  15928  -2300  -2620   2295       O  
ATOM   5456  N   GLY B 256       0.025   9.349  42.357  1.00176.73           N  
ANISOU 5456  N   GLY B 256    27229  20520  19399  -2376  -2695   2376       N  
ATOM   5457  CA  GLY B 256      -0.844  10.139  41.501  1.00164.87           C  
ANISOU 5457  CA  GLY B 256    25551  19246  17844  -2525  -2423   2258       C  
ATOM   5458  C   GLY B 256      -0.651  10.240  39.999  1.00150.63           C  
ANISOU 5458  C   GLY B 256    23489  17547  16196  -2414  -2262   2083       C  
ATOM   5459  O   GLY B 256      -1.629  10.190  39.255  1.00155.56           O  
ANISOU 5459  O   GLY B 256    24133  18215  16760  -2528  -2090   1987       O  
ATOM   5460  N   TRP B 257       0.587  10.381  39.537  1.00135.42           N  
ANISOU 5460  N   TRP B 257    21329  15648  14476  -2186  -2313   2037       N  
ATOM   5461  CA  TRP B 257       0.798  10.886  38.185  1.00125.73           C  
ANISOU 5461  CA  TRP B 257    19859  14578  13335  -2092  -2093   1893       C  
ATOM   5462  C   TRP B 257       2.114  10.494  37.511  1.00133.13           C  
ANISOU 5462  C   TRP B 257    20594  15445  14544  -1805  -2077   1830       C  
ATOM   5463  O   TRP B 257       3.063  10.069  38.167  1.00123.98           O  
ANISOU 5463  O   TRP B 257    19384  14149  13573  -1665  -2284   1896       O  
ATOM   5464  CB  TRP B 257       0.702  12.410  38.221  1.00124.65           C  
ANISOU 5464  CB  TRP B 257    19525  14701  13135  -2202  -2004   1903       C  
ATOM   5465  CG  TRP B 257       1.711  13.021  39.149  1.00132.15           C  
ANISOU 5465  CG  TRP B 257    20322  15672  14218  -2149  -2199   1998       C  
ATOM   5466  CD1 TRP B 257       1.624  13.117  40.509  1.00133.46           C  
ANISOU 5466  CD1 TRP B 257    20654  15780  14275  -2241  -2434   2114       C  
ATOM   5467  CD2 TRP B 257       2.961  13.617  38.788  1.00136.23           C  
ANISOU 5467  CD2 TRP B 257    20495  16250  15015  -1989  -2189   1975       C  
ATOM   5468  NE1 TRP B 257       2.742  13.733  41.014  1.00133.79           N  
ANISOU 5468  NE1 TRP B 257    20486  15839  14508  -2141  -2631   2147       N  
ATOM   5469  CE2 TRP B 257       3.581  14.053  39.975  1.00133.35           C  
ANISOU 5469  CE2 TRP B 257    20079  15855  14734  -1997  -2480   2065       C  
ATOM   5470  CE3 TRP B 257       3.620  13.827  37.571  1.00141.61           C  
ANISOU 5470  CE3 TRP B 257    20916  16994  15893  -1837  -1947   1888       C  
ATOM   5471  CZ2 TRP B 257       4.820  14.683  39.986  1.00138.01           C  
ANISOU 5471  CZ2 TRP B 257    20314  16466  15658  -1877  -2569   2060       C  
ATOM   5472  CZ3 TRP B 257       4.851  14.453  37.583  1.00144.72           C  
ANISOU 5472  CZ3 TRP B 257    20957  17416  16614  -1723  -1966   1905       C  
ATOM   5473  CH2 TRP B 257       5.439  14.874  38.782  1.00141.99           C  
ANISOU 5473  CH2 TRP B 257    20512  17030  16408  -1751  -2291   1984       C  
ATOM   5474  N   HIS B 258       2.137  10.627  36.184  1.00145.57           N  
ANISOU 5474  N   HIS B 258    22073  17103  16134  -1707  -1825   1696       N  
ATOM   5475  CA  HIS B 258       3.362  10.527  35.386  1.00154.97           C  
ANISOU 5475  CA  HIS B 258    23030  18276  17577  -1437  -1688   1627       C  
ATOM   5476  C   HIS B 258       3.582  11.794  34.551  1.00161.45           C  
ANISOU 5476  C   HIS B 258    23618  19330  18397  -1435  -1409   1593       C  
ATOM   5477  O   HIS B 258       2.642  12.347  33.984  1.00169.59           O  
ANISOU 5477  O   HIS B 258    24763  20493  19181  -1565  -1272   1546       O  
ATOM   5478  CB  HIS B 258       3.317   9.289  34.489  1.00156.27           C  
ANISOU 5478  CB  HIS B 258    23374  18257  17744  -1258  -1602   1493       C  
ATOM   5479  CG  HIS B 258       2.270   9.347  33.421  1.00152.30           C  
ANISOU 5479  CG  HIS B 258    23066  17823  16979  -1328  -1420   1362       C  
ATOM   5480  ND1 HIS B 258       2.429  10.069  32.258  1.00144.41           N  
ANISOU 5480  ND1 HIS B 258    21983  16980  15906  -1233  -1134   1273       N  
ATOM   5481  CD2 HIS B 258       1.043   8.779  33.347  1.00153.08           C  
ANISOU 5481  CD2 HIS B 258    23446  17833  16885  -1480  -1506   1304       C  
ATOM   5482  CE1 HIS B 258       1.350   9.932  31.507  1.00137.76           C  
ANISOU 5482  CE1 HIS B 258    21390  16143  14808  -1303  -1094   1155       C  
ATOM   5483  NE2 HIS B 258       0.493   9.159  32.147  1.00147.83           N  
ANISOU 5483  NE2 HIS B 258    22858  17272  16040  -1461  -1325   1163       N  
ATOM   5484  N   GLY B 259       4.831  12.242  34.479  1.00158.59           N  
ANISOU 5484  N   GLY B 259    22924  18994  18339  -1286  -1333   1619       N  
ATOM   5485  CA  GLY B 259       5.167  13.520  33.871  1.00149.98           C  
ANISOU 5485  CA  GLY B 259    21587  18094  17304  -1307  -1070   1630       C  
ATOM   5486  C   GLY B 259       5.254  13.673  32.358  1.00132.94           C  
ANISOU 5486  C   GLY B 259    19448  15998  15067  -1165   -657   1534       C  
ATOM   5487  O   GLY B 259       5.115  14.785  31.849  1.00128.15           O  
ANISOU 5487  O   GLY B 259    18767  15550  14373  -1242   -443   1560       O  
ATOM   5488  N   HIS B 260       5.504  12.579  31.643  1.00125.39           N  
ANISOU 5488  N   HIS B 260    18620  14898  14124   -944   -542   1425       N  
ATOM   5489  CA  HIS B 260       5.981  12.638  30.256  1.00128.73           C  
ANISOU 5489  CA  HIS B 260    19039  15340  14533   -729   -115   1336       C  
ATOM   5490  C   HIS B 260       5.091  13.364  29.231  1.00123.06           C  
ANISOU 5490  C   HIS B 260    18572  14766  13418   -798    114   1290       C  
ATOM   5491  O   HIS B 260       5.612  14.020  28.333  1.00121.90           O  
ANISOU 5491  O   HIS B 260    18346  14693  13276   -688    492   1298       O  
ATOM   5492  CB  HIS B 260       6.259  11.220  29.760  1.00135.55           C  
ANISOU 5492  CB  HIS B 260    20075  15996  15431   -474    -84   1201       C  
ATOM   5493  CG  HIS B 260       7.479  10.598  30.368  1.00139.49           C  
ANISOU 5493  CG  HIS B 260    20270  16341  16389   -296   -181   1228       C  
ATOM   5494  ND1 HIS B 260       7.528  10.188  31.683  1.00140.46           N  
ANISOU 5494  ND1 HIS B 260    20333  16361  16673   -389   -612   1312       N  
ATOM   5495  CD2 HIS B 260       8.697  10.324  29.843  1.00146.80           C  
ANISOU 5495  CD2 HIS B 260    20934  17183  17658    -18     94   1182       C  
ATOM   5496  CE1 HIS B 260       8.722   9.683  31.940  1.00145.74           C  
ANISOU 5496  CE1 HIS B 260    20719  16886  17770   -168   -652   1310       C  
ATOM   5497  NE2 HIS B 260       9.450   9.754  30.841  1.00149.81           N  
ANISOU 5497  NE2 HIS B 260    21075  17413  18434     57   -218   1227       N  
ATOM   5498  N   GLY B 261       3.771  13.241  29.332  1.00111.07           N  
ANISOU 5498  N   GLY B 261    17357  13269  11574   -969   -103   1244       N  
ATOM   5499  CA  GLY B 261       2.900  13.976  28.426  1.00 88.22           C  
ANISOU 5499  CA  GLY B 261    14689  10499   8330  -1028     37   1197       C  
ATOM   5500  C   GLY B 261       1.578  13.320  28.075  1.00123.57           C  
ANISOU 5500  C   GLY B 261    19546  14909  12496  -1088   -165   1057       C  
ATOM   5501  O   GLY B 261       0.993  12.607  28.890  1.00121.58           O  
ANISOU 5501  O   GLY B 261    19349  14561  12287  -1220   -462   1047       O  
ATOM   5502  N   TRP B 262       1.101  13.572  26.857  1.00110.92           N  
ANISOU 5502  N   TRP B 262    18217  13339  10588   -991    -11    950       N  
ATOM   5503  CA  TRP B 262      -0.159  12.997  26.394  1.00107.16           C  
ANISOU 5503  CA  TRP B 262    18091  12781   9846  -1034   -239    787       C  
ATOM   5504  C   TRP B 262       0.077  11.592  25.851  1.00115.07           C  
ANISOU 5504  C   TRP B 262    19326  13561  10835   -814   -254    619       C  
ATOM   5505  O   TRP B 262       1.171  11.278  25.373  1.00106.93           O  
ANISOU 5505  O   TRP B 262    18267  12476   9887   -563     20    602       O  
ATOM   5506  CB  TRP B 262      -0.803  13.864  25.316  1.00 95.65           C  
ANISOU 5506  CB  TRP B 262    16872  11425   8046  -1001   -144    728       C  
ATOM   5507  CG  TRP B 262      -1.073  15.269  25.739  1.00 93.45           C  
ANISOU 5507  CG  TRP B 262    16398  11341   7769  -1195   -127    878       C  
ATOM   5508  CD1 TRP B 262      -0.280  16.357  25.521  1.00 98.07           C  
ANISOU 5508  CD1 TRP B 262    16824  12050   8387  -1153    177   1018       C  
ATOM   5509  CD2 TRP B 262      -2.206  15.738  26.483  1.00 91.33           C  
ANISOU 5509  CD2 TRP B 262    16060  11143   7498  -1463   -412    902       C  
ATOM   5510  NE1 TRP B 262      -0.860  17.479  26.063  1.00101.63           N  
ANISOU 5510  NE1 TRP B 262    17139  12640   8837  -1372     68   1118       N  
ATOM   5511  CE2 TRP B 262      -2.039  17.126  26.662  1.00 94.51           C  
ANISOU 5511  CE2 TRP B 262    16286  11715   7907  -1554   -284   1045       C  
ATOM   5512  CE3 TRP B 262      -3.345  15.120  27.006  1.00 81.80           C  
ANISOU 5512  CE3 TRP B 262    14912   9858   6312  -1636   -736    815       C  
ATOM   5513  CZ2 TRP B 262      -2.973  17.906  27.346  1.00 78.93           C  
ANISOU 5513  CZ2 TRP B 262    14211   9841   5936  -1788   -478   1089       C  
ATOM   5514  CZ3 TRP B 262      -4.270  15.897  27.682  1.00 79.50           C  
ANISOU 5514  CZ3 TRP B 262    14494   9670   6041  -1875   -892    868       C  
ATOM   5515  CH2 TRP B 262      -4.078  17.275  27.846  1.00 78.04           C  
ANISOU 5515  CH2 TRP B 262    14152   9662   5839  -1937   -767    997       C  
ATOM   5516  N   VAL B 263      -0.950  10.749  25.923  1.00125.08           N  
ANISOU 5516  N   VAL B 263    20809  14683  12032   -907   -564    488       N  
ATOM   5517  CA  VAL B 263      -0.830   9.362  25.481  1.00139.16           C  
ANISOU 5517  CA  VAL B 263    22833  16218  13822   -722   -636    314       C  
ATOM   5518  C   VAL B 263      -1.928   8.967  24.494  1.00139.20           C  
ANISOU 5518  C   VAL B 263    23237  16109  13542   -689   -826     82       C  
ATOM   5519  O   VAL B 263      -3.078   9.375  24.647  1.00130.02           O  
ANISOU 5519  O   VAL B 263    22095  14996  12310   -912  -1060     64       O  
ATOM   5520  CB  VAL B 263      -0.868   8.393  26.688  1.00146.91           C  
ANISOU 5520  CB  VAL B 263    23690  17033  15096   -863   -885    376       C  
ATOM   5521  CG1 VAL B 263      -0.731   6.947  26.233  1.00148.92           C  
ANISOU 5521  CG1 VAL B 263    24201  16999  15383   -668   -971    195       C  
ATOM   5522  CG2 VAL B 263       0.229   8.736  27.683  1.00154.16           C  
ANISOU 5522  CG2 VAL B 263    24248  18034  16292   -869   -778    585       C  
ATOM   5523  N   GLY B 264      -1.558   8.158  23.500  1.00152.63           N  
ANISOU 5523  N   GLY B 264    25249  17643  15101   -398   -739   -108       N  
ATOM   5524  CA  GLY B 264      -2.503   7.503  22.608  1.00163.63           C  
ANISOU 5524  CA  GLY B 264    27057  18853  16260   -333   -994   -370       C  
ATOM   5525  C   GLY B 264      -3.036   8.269  21.412  1.00169.12           C  
ANISOU 5525  C   GLY B 264    28076  19638  16544   -222   -973   -489       C  
ATOM   5526  O   GLY B 264      -2.557   9.352  21.079  1.00164.60           O  
ANISOU 5526  O   GLY B 264    27454  19271  15813   -150   -670   -362       O  
ATOM   5527  N   GLU B 265      -4.034   7.681  20.755  1.00181.94           N  
ANISOU 5527  N   GLU B 265    30049  21078  18003   -203  -1321   -737       N  
ATOM   5528  CA  GLU B 265      -4.639   8.261  19.558  1.00185.86           C  
ANISOU 5528  CA  GLU B 265    30939  21603  18076    -65  -1406   -891       C  
ATOM   5529  C   GLU B 265      -6.156   8.331  19.655  1.00177.29           C  
ANISOU 5529  C   GLU B 265    29867  20454  17040   -313  -1913  -1012       C  
ATOM   5530  O   GLU B 265      -6.778   7.626  20.450  1.00165.92           O  
ANISOU 5530  O   GLU B 265    28223  18876  15942   -556  -2195  -1039       O  
ATOM   5531  CB  GLU B 265      -4.288   7.454  18.306  1.00190.45           C  
ANISOU 5531  CB  GLU B 265    32059  21975  18327    313  -1352  -1152       C  
ATOM   5532  CG  GLU B 265      -2.817   7.314  17.978  1.00187.44           C  
ANISOU 5532  CG  GLU B 265    31717  21621  17880    620   -811  -1084       C  
ATOM   5533  CD  GLU B 265      -2.571   6.225  16.950  1.00180.63           C  
ANISOU 5533  CD  GLU B 265    31373  20493  16765    974   -808  -1377       C  
ATOM   5534  OE1 GLU B 265      -3.555   5.602  16.499  1.00171.23           O  
ANISOU 5534  OE1 GLU B 265    30522  19094  15446    968  -1270  -1636       O  
ATOM   5535  OE2 GLU B 265      -1.399   6.000  16.586  1.00184.01           O  
ANISOU 5535  OE2 GLU B 265    31864  20910  17143   1263   -348  -1360       O  
ATOM   5536  N   GLY B 266      -6.746   9.194  18.836  1.00175.40           N  
ANISOU 5536  N   GLY B 266    29868  20301  16475   -246  -2020  -1078       N  
ATOM   5537  CA  GLY B 266      -8.187   9.244  18.706  1.00173.72           C  
ANISOU 5537  CA  GLY B 266    29702  19997  16306   -419  -2536  -1244       C  
ATOM   5538  C   GLY B 266      -8.774  10.360  19.535  1.00156.49           C  
ANISOU 5538  C   GLY B 266    27099  18039  14322   -716  -2567  -1042       C  
ATOM   5539  O   GLY B 266      -8.051  11.177  20.096  1.00149.79           O  
ANISOU 5539  O   GLY B 266    25988  17417  13509   -766  -2203   -784       O  
ATOM   5540  N   LYS B 267     -10.094  10.381  19.631  1.00149.83           N  
ANISOU 5540  N   LYS B 267    26171  17113  13646   -913  -3012  -1173       N  
ATOM   5541  CA  LYS B 267     -10.772  11.417  20.388  1.00136.81           C  
ANISOU 5541  CA  LYS B 267    24129  15652  12199  -1181  -3058  -1015       C  
ATOM   5542  C   LYS B 267     -10.916  10.972  21.839  1.00134.47           C  
ANISOU 5542  C   LYS B 267    23362  15350  12379  -1511  -3006   -869       C  
ATOM   5543  O   LYS B 267     -10.791   9.785  22.154  1.00116.12           O  
ANISOU 5543  O   LYS B 267    21042  12823  10254  -1555  -3060   -932       O  
ATOM   5544  CB  LYS B 267     -12.144  11.730  19.785  1.00129.05           C  
ANISOU 5544  CB  LYS B 267    23248  14581  11203  -1219  -3550  -1229       C  
ATOM   5545  CG  LYS B 267     -13.024  10.505  19.599  1.00138.84           C  
ANISOU 5545  CG  LYS B 267    24560  15504  12689  -1294  -4007  -1511       C  
ATOM   5546  CD  LYS B 267     -14.455  10.762  20.044  1.00135.76           C  
ANISOU 5546  CD  LYS B 267    23818  15065  12701  -1582  -4393  -1590       C  
ATOM   5547  CE  LYS B 267     -15.258   9.468  20.046  1.00122.90           C  
ANISOU 5547  CE  LYS B 267    22162  13094  11438  -1718  -4795  -1839       C  
ATOM   5548  NZ  LYS B 267     -16.626   9.645  20.609  1.00107.00           N  
ANISOU 5548  NZ  LYS B 267    19710  11014   9929  -2035  -5101  -1898       N  
ATOM   5549  N   TRP B 268     -11.147  11.939  22.719  1.00139.57           N  
ANISOU 5549  N   TRP B 268    23643  16204  13182  -1725  -2889   -667       N  
ATOM   5550  CA  TRP B 268     -11.315  11.676  24.141  1.00143.44           C  
ANISOU 5550  CA  TRP B 268    23734  16705  14060  -2029  -2809   -506       C  
ATOM   5551  C   TRP B 268     -12.755  11.264  24.430  1.00142.74           C  
ANISOU 5551  C   TRP B 268    23475  16449  14309  -2280  -3160   -650       C  
ATOM   5552  O   TRP B 268     -13.684  11.712  23.755  1.00142.02           O  
ANISOU 5552  O   TRP B 268    23433  16338  14192  -2263  -3451   -816       O  
ATOM   5553  CB  TRP B 268     -10.944  12.909  24.965  1.00135.91           C  
ANISOU 5553  CB  TRP B 268    22495  16031  13112  -2136  -2530   -247       C  
ATOM   5554  CG  TRP B 268      -9.490  13.274  24.933  1.00134.20           C  
ANISOU 5554  CG  TRP B 268    22330  15958  12702  -1953  -2166    -77       C  
ATOM   5555  CD1 TRP B 268      -8.925  14.324  24.272  1.00134.97           C  
ANISOU 5555  CD1 TRP B 268    22535  16223  12523  -1777  -1975     -9       C  
ATOM   5556  CD2 TRP B 268      -8.423  12.621  25.637  1.00132.10           C  
ANISOU 5556  CD2 TRP B 268    21974  15662  12556  -1938  -1948     57       C  
ATOM   5557  NE1 TRP B 268      -7.569  14.349  24.497  1.00141.06           N  
ANISOU 5557  NE1 TRP B 268    23255  17068  13272  -1665  -1633    149       N  
ATOM   5558  CE2 TRP B 268      -7.236  13.317  25.334  1.00138.99           C  
ANISOU 5558  CE2 TRP B 268    22863  16691  13256  -1751  -1635    183       C  
ATOM   5559  CE3 TRP B 268      -8.355  11.510  26.480  1.00128.29           C  
ANISOU 5559  CE3 TRP B 268    21405  15015  12326  -2059  -1996     85       C  
ATOM   5560  CZ2 TRP B 268      -5.995  12.937  25.848  1.00138.51           C  
ANISOU 5560  CZ2 TRP B 268    22692  16631  13306  -1675  -1400    315       C  
ATOM   5561  CZ3 TRP B 268      -7.124  11.140  26.993  1.00138.27           C  
ANISOU 5561  CZ3 TRP B 268    22609  16279  13647  -1969  -1781    225       C  
ATOM   5562  CH2 TRP B 268      -5.961  11.848  26.672  1.00137.35           C  
ANISOU 5562  CH2 TRP B 268    22469  16324  13393  -1775  -1501    328       C  
ATOM   5563  N   THR B 269     -12.939  10.410  25.431  1.00136.90           N  
ANISOU 5563  N   THR B 269    22535  15573  13908  -2510  -3133   -582       N  
ATOM   5564  CA  THR B 269     -14.279  10.060  25.881  1.00130.35           C  
ANISOU 5564  CA  THR B 269    21467  14582  13478  -2795  -3373   -673       C  
ATOM   5565  C   THR B 269     -14.509  10.555  27.303  1.00122.58           C  
ANISOU 5565  C   THR B 269    20113  13736  12726  -3074  -3122   -428       C  
ATOM   5566  O   THR B 269     -13.793  10.176  28.230  1.00117.10           O  
ANISOU 5566  O   THR B 269    19379  13050  12064  -3141  -2872   -227       O  
ATOM   5567  CB  THR B 269     -14.506   8.538  25.827  1.00136.55           C  
ANISOU 5567  CB  THR B 269    22363  15016  14502  -2859  -3560   -815       C  
ATOM   5568  OG1 THR B 269     -14.253   8.059  24.500  1.00139.34           O  
ANISOU 5568  OG1 THR B 269    23114  15228  14601  -2571  -3795  -1064       O  
ATOM   5569  CG2 THR B 269     -15.932   8.193  26.229  1.00141.24           C  
ANISOU 5569  CG2 THR B 269    22675  15417  15574  -3172  -3792   -914       C  
ATOM   5570  N   VAL B 270     -15.538  11.379  27.470  1.00120.61           N  
ANISOU 5570  N   VAL B 270    19611  13575  12639  -3222  -3209   -457       N  
ATOM   5571  CA  VAL B 270     -15.811  12.024  28.748  1.00107.32           C  
ANISOU 5571  CA  VAL B 270    17609  12043  11126  -3454  -2951   -245       C  
ATOM   5572  C   VAL B 270     -17.078  11.478  29.392  1.00120.15           C  
ANISOU 5572  C   VAL B 270    18952  13470  13228  -3762  -3020   -295       C  
ATOM   5573  O   VAL B 270     -18.146  11.484  28.787  1.00127.24           O  
ANISOU 5573  O   VAL B 270    19731  14251  14362  -3811  -3315   -510       O  
ATOM   5574  CB  VAL B 270     -15.949  13.556  28.581  1.00 96.93           C  
ANISOU 5574  CB  VAL B 270    16186  11000   9642  -3382  -2909   -210       C  
ATOM   5575  CG1 VAL B 270     -16.450  14.200  29.866  1.00 93.19           C  
ANISOU 5575  CG1 VAL B 270    15385  10646   9376  -3623  -2679    -45       C  
ATOM   5576  CG2 VAL B 270     -14.625  14.169  28.143  1.00 83.64           C  
ANISOU 5576  CG2 VAL B 270    14733   9509   7536  -3124  -2744   -102       C  
ATOM   5577  N   LYS B 271     -16.953  11.011  30.628  1.00135.85           N  
ANISOU 5577  N   LYS B 271    20840  15407  15370  -3966  -2746    -92       N  
ATOM   5578  CA  LYS B 271     -18.099  10.528  31.382  1.00149.58           C  
ANISOU 5578  CA  LYS B 271    22308  16957  17568  -4281  -2697    -87       C  
ATOM   5579  C   LYS B 271     -18.091  11.120  32.786  1.00150.23           C  
ANISOU 5579  C   LYS B 271    22228  17196  17655  -4451  -2304    173       C  
ATOM   5580  O   LYS B 271     -17.047  11.204  33.431  1.00155.69           O  
ANISOU 5580  O   LYS B 271    23089  18003  18064  -4378  -2090    379       O  
ATOM   5581  CB  LYS B 271     -18.116   8.997  31.434  1.00159.32           C  
ANISOU 5581  CB  LYS B 271    23667  17844  19025  -4385  -2774   -119       C  
ATOM   5582  CG  LYS B 271     -18.544   8.340  30.126  1.00165.86           C  
ANISOU 5582  CG  LYS B 271    24601  18443  19977  -4284  -3211   -432       C  
ATOM   5583  CD  LYS B 271     -18.285   6.837  30.116  1.00170.72           C  
ANISOU 5583  CD  LYS B 271    25415  18713  20737  -4330  -3288   -461       C  
ATOM   5584  CE  LYS B 271     -16.802   6.518  30.012  1.00173.70           C  
ANISOU 5584  CE  LYS B 271    26149  19158  20691  -4069  -3177   -353       C  
ATOM   5585  NZ  LYS B 271     -16.562   5.051  29.895  1.00174.39           N  
ANISOU 5585  NZ  LYS B 271    26452  18886  20923  -4077  -3294   -412       N  
ATOM   5586  N   LYS B 272     -19.262  11.540  33.250  1.00144.72           N  
ANISOU 5586  N   LYS B 272    21207  16492  17289  -4662  -2221    148       N  
ATOM   5587  CA  LYS B 272     -19.391  12.066  34.601  1.00136.97           C  
ANISOU 5587  CA  LYS B 272    20098  15629  16314  -4824  -1824    373       C  
ATOM   5588  C   LYS B 272     -20.095  11.036  35.480  1.00133.26           C  
ANISOU 5588  C   LYS B 272    19530  14878  16223  -5122  -1611    467       C  
ATOM   5589  O   LYS B 272     -21.284  10.761  35.302  1.00130.48           O  
ANISOU 5589  O   LYS B 272    18886  14348  16343  -5308  -1676    326       O  
ATOM   5590  CB  LYS B 272     -20.166  13.385  34.590  1.00138.56           C  
ANISOU 5590  CB  LYS B 272    20010  16034  16602  -4831  -1797    299       C  
ATOM   5591  CG  LYS B 272     -19.665  14.413  35.586  1.00135.56           C  
ANISOU 5591  CG  LYS B 272    19661  15910  15935  -4806  -1477    502       C  
ATOM   5592  CD  LYS B 272     -20.685  15.519  35.784  1.00145.42           C  
ANISOU 5592  CD  LYS B 272    20582  17284  17387  -4870  -1395    427       C  
ATOM   5593  CE  LYS B 272     -21.985  14.963  36.342  1.00157.59           C  
ANISOU 5593  CE  LYS B 272    21813  18613  19453  -5150  -1220    393       C  
ATOM   5594  NZ  LYS B 272     -22.979  16.035  36.623  1.00155.18           N  
ANISOU 5594  NZ  LYS B 272    21155  18421  19385  -5202  -1093    318       N  
ATOM   5595  N   GLY B 273     -19.354  10.479  36.434  1.00133.36           N  
ANISOU 5595  N   GLY B 273    19787  14835  16047  -5165  -1360    710       N  
ATOM   5596  CA  GLY B 273     -19.840   9.361  37.221  1.00147.07           C  
ANISOU 5596  CA  GLY B 273    21537  16264  18080  -5426  -1151    835       C  
ATOM   5597  C   GLY B 273     -19.314   9.306  38.641  1.00152.51           C  
ANISOU 5597  C   GLY B 273    22452  16975  18519  -5495   -764   1149       C  
ATOM   5598  O   GLY B 273     -18.284   9.895  38.963  1.00135.40           O  
ANISOU 5598  O   GLY B 273    20496  15030  15922  -5307   -737   1266       O  
ATOM   5599  N   ASN B 274     -20.027   8.577  39.492  1.00167.16           N  
ANISOU 5599  N   ASN B 274    24279  18574  20658  -5767   -471   1287       N  
ATOM   5600  CA  ASN B 274     -19.560   8.290  40.839  1.00178.17           C  
ANISOU 5600  CA  ASN B 274    25987  19911  21798  -5834   -120   1598       C  
ATOM   5601  C   ASN B 274     -18.424   7.272  40.838  1.00171.87           C  
ANISOU 5601  C   ASN B 274    25586  18946  20771  -5704   -290   1713       C  
ATOM   5602  O   ASN B 274     -18.038   6.757  39.788  1.00162.37           O  
ANISOU 5602  O   ASN B 274    24400  17666  19627  -5572   -640   1542       O  
ATOM   5603  CB  ASN B 274     -20.713   7.771  41.701  1.00192.36           C  
ANISOU 5603  CB  ASN B 274    27660  21449  23979  -6170    292   1725       C  
ATOM   5604  CG  ASN B 274     -21.622   8.880  42.194  1.00195.58           C  
ANISOU 5604  CG  ASN B 274    27764  22049  24499  -6271    612   1705       C  
ATOM   5605  OD1 ASN B 274     -22.764   9.004  41.750  1.00199.46           O  
ANISOU 5605  OD1 ASN B 274    27822  22472  25492  -6427    625   1528       O  
ATOM   5606  ND2 ASN B 274     -21.118   9.697  43.114  1.00193.86           N  
ANISOU 5606  ND2 ASN B 274    27767  22056  23834  -6170    848   1872       N  
ATOM   5607  N   VAL B 275     -17.886   6.997  42.021  1.00169.09           N  
ANISOU 5607  N   VAL B 275    25575  18529  20143  -5721    -50   1995       N  
ATOM   5608  CA  VAL B 275     -16.838   5.996  42.177  1.00162.96           C  
ANISOU 5608  CA  VAL B 275    25184  17559  19176  -5598   -201   2129       C  
ATOM   5609  C   VAL B 275     -17.170   5.051  43.328  1.00174.86           C  
ANISOU 5609  C   VAL B 275    26966  18731  20742  -5819    118   2407       C  
ATOM   5610  O   VAL B 275     -17.934   5.402  44.229  1.00181.27           O  
ANISOU 5610  O   VAL B 275    27751  19542  21581  -6014    516   2546       O  
ATOM   5611  CB  VAL B 275     -15.465   6.642  42.434  1.00147.67           C  
ANISOU 5611  CB  VAL B 275    23478  15881  16749  -5303   -341   2209       C  
ATOM   5612  CG1 VAL B 275     -14.947   7.322  41.175  1.00142.43           C  
ANISOU 5612  CG1 VAL B 275    22608  15475  16035  -5068   -658   1959       C  
ATOM   5613  CG2 VAL B 275     -15.551   7.625  43.593  1.00140.73           C  
ANISOU 5613  CG2 VAL B 275    22682  15200  15591  -5339    -50   2376       C  
ATOM   5614  N   SER B 276     -16.589   3.856  43.298  1.00178.78           N  
ANISOU 5614  N   SER B 276    27750  18930  21248  -5776    -34   2494       N  
ATOM   5615  CA  SER B 276     -16.860   2.848  44.318  1.00188.26           C  
ANISOU 5615  CA  SER B 276    29266  19758  22504  -5977    246   2775       C  
ATOM   5616  C   SER B 276     -16.233   3.223  45.653  1.00192.88           C  
ANISOU 5616  C   SER B 276    30267  20430  22591  -5890    455   3070       C  
ATOM   5617  O   SER B 276     -15.440   4.160  45.736  1.00188.06           O  
ANISOU 5617  O   SER B 276    29695  20144  21615  -5656    310   3041       O  
ATOM   5618  CB  SER B 276     -16.345   1.481  43.874  1.00187.24           C  
ANISOU 5618  CB  SER B 276    29356  19271  22516  -5922    -24   2775       C  
ATOM   5619  OG  SER B 276     -16.491   0.511  44.897  1.00192.53           O  
ANISOU 5619  OG  SER B 276    30396  19561  23195  -6093    233   3080       O  
ATOM   5620  N   SER B 277     -16.608   2.496  46.700  1.00196.20           N  
ANISOU 5620  N   SER B 277    30954  20578  23014  -6025    783   3322       N  
ATOM   5621  CA  SER B 277     -15.948   2.620  47.994  1.00181.99           C  
ANISOU 5621  CA  SER B 277    29532  18868  20747  -5792    902   3535       C  
ATOM   5622  C   SER B 277     -14.486   2.216  47.868  1.00160.20           C  
ANISOU 5622  C   SER B 277    27118  16061  17689  -5515    456   3582       C  
ATOM   5623  O   SER B 277     -13.609   2.822  48.482  1.00149.55           O  
ANISOU 5623  O   SER B 277    25971  14924  15928  -5266    332   3638       O  
ATOM   5624  CB  SER B 277     -16.644   1.760  49.043  1.00182.82           C  
ANISOU 5624  CB  SER B 277    29795  18703  20964  -5895   1313   3747       C  
ATOM   5625  OG  SER B 277     -15.991   1.831  50.296  1.00190.74           O  
ANISOU 5625  OG  SER B 277    30435  19720  22319  -6150   1751   3712       O  
ATOM   5626  N   THR B 278     -14.239   1.174  47.077  1.00155.86           N  
ANISOU 5626  N   THR B 278    26621  15208  17390  -5554    202   3545       N  
ATOM   5627  CA  THR B 278     -12.883   0.753  46.737  1.00146.63           C  
ANISOU 5627  CA  THR B 278    25722  13959  16033  -5293   -238   3560       C  
ATOM   5628  C   THR B 278     -12.277   1.746  45.745  1.00146.96           C  
ANISOU 5628  C   THR B 278    25400  14410  16030  -5060   -526   3274       C  
ATOM   5629  O   THR B 278     -11.085   1.700  45.444  1.00147.05           O  
ANISOU 5629  O   THR B 278    25486  14490  15898  -4764   -858   3224       O  
ATOM   5630  CB  THR B 278     -12.853  -0.675  46.148  1.00131.77           C  
ANISOU 5630  CB  THR B 278    23929  11656  14482  -5328   -411   3533       C  
ATOM   5631  OG1 THR B 278     -11.506  -1.166  46.135  1.00120.61           O  
ANISOU 5631  OG1 THR B 278    22793  10162  12873  -5003   -780   3573       O  
ATOM   5632  CG2 THR B 278     -13.414  -0.689  44.737  1.00130.85           C  
ANISOU 5632  CG2 THR B 278    23338  11596  14783  -5390   -548   3187       C  
ATOM   5633  N   GLY B 279     -13.119   2.633  45.227  1.00140.31           N  
ANISOU 5633  N   GLY B 279    24149  13822  15340  -5190   -383   3089       N  
ATOM   5634  CA  GLY B 279     -12.670   3.686  44.341  1.00130.62           C  
ANISOU 5634  CA  GLY B 279    22597  12983  14051  -4992   -595   2844       C  
ATOM   5635  C   GLY B 279     -12.559   3.356  42.869  1.00123.23           C  
ANISOU 5635  C   GLY B 279    21402  12041  13378  -4887   -873   2558       C  
ATOM   5636  O   GLY B 279     -11.802   4.009  42.158  1.00122.59           O  
ANISOU 5636  O   GLY B 279    21179  12224  13177  -4648  -1082   2402       O  
ATOM   5637  N   ARG B 280     -13.299   2.360  42.393  1.00144.12           N  
ANISOU 5637  N   ARG B 280    24002  14375  16381  -5059   -874   2483       N  
ATOM   5638  CA  ARG B 280     -13.292   2.091  40.961  1.00147.00           C  
ANISOU 5638  CA  ARG B 280    24158  14728  16968  -4952  -1153   2179       C  
ATOM   5639  C   ARG B 280     -14.274   3.038  40.279  1.00141.71           C  
ANISOU 5639  C   ARG B 280    23086  14295  16460  -5068  -1109   1961       C  
ATOM   5640  O   ARG B 280     -15.431   3.146  40.685  1.00149.18           O  
ANISOU 5640  O   ARG B 280    23870  15172  17641  -5353   -871   1997       O  
ATOM   5641  CB  ARG B 280     -13.613   0.617  40.656  1.00156.12           C  
ANISOU 5641  CB  ARG B 280    25447  15424  18449  -5062  -1251   2150       C  
ATOM   5642  CG  ARG B 280     -14.993   0.137  41.065  1.00167.77           C  
ANISOU 5642  CG  ARG B 280    26822  16621  20300  -5452  -1000   2217       C  
ATOM   5643  CD  ARG B 280     -15.215  -1.321  40.691  1.00180.27           C  
ANISOU 5643  CD  ARG B 280    28539  17723  22232  -5549  -1143   2172       C  
ATOM   5644  NE  ARG B 280     -15.261  -1.513  39.245  1.00183.31           N  
ANISOU 5644  NE  ARG B 280    28742  18096  22811  -5422  -1497   1810       N  
ATOM   5645  CZ  ARG B 280     -16.372  -1.438  38.518  1.00189.62           C  
ANISOU 5645  CZ  ARG B 280    29218  18839  23991  -5612  -1568   1572       C  
ATOM   5646  NH1 ARG B 280     -17.532  -1.177  39.104  1.00189.46           N  
ANISOU 5646  NH1 ARG B 280    28957  18773  24255  -5948  -1276   1661       N  
ATOM   5647  NH2 ARG B 280     -16.323  -1.625  37.207  1.00193.93           N  
ANISOU 5647  NH2 ARG B 280    29686  19361  24636  -5453  -1932   1239       N  
ATOM   5648  N   CYS B 281     -13.798   3.763  39.272  1.00128.15           N  
ANISOU 5648  N   CYS B 281    21214  12856  14622  -4837  -1321   1744       N  
ATOM   5649  CA  CYS B 281     -14.662   4.692  38.553  1.00131.25           C  
ANISOU 5649  CA  CYS B 281    21264  13466  15140  -4903  -1337   1532       C  
ATOM   5650  C   CYS B 281     -15.639   3.927  37.680  1.00127.89           C  
ANISOU 5650  C   CYS B 281    20693  12771  15128  -5049  -1498   1309       C  
ATOM   5651  O   CYS B 281     -15.237   3.151  36.812  1.00120.53           O  
ANISOU 5651  O   CYS B 281    19885  11667  14243  -4904  -1763   1151       O  
ATOM   5652  CB  CYS B 281     -13.860   5.676  37.700  1.00140.06           C  
ANISOU 5652  CB  CYS B 281    22307  14924  15986  -4610  -1507   1385       C  
ATOM   5653  SG  CYS B 281     -14.894   6.837  36.741  1.00 95.97           S  
ANISOU 5653  SG  CYS B 281    16359   9582  10522  -4652  -1581   1127       S  
ATOM   5654  N   LEU B 282     -16.923   4.165  37.920  1.00134.95           N  
ANISOU 5654  N   LEU B 282    21317  13618  16340  -5329  -1344   1282       N  
ATOM   5655  CA  LEU B 282     -18.006   3.451  37.258  1.00151.42           C  
ANISOU 5655  CA  LEU B 282    23208  15409  18918  -5525  -1495   1079       C  
ATOM   5656  C   LEU B 282     -17.909   3.576  35.742  1.00167.83           C  
ANISOU 5656  C   LEU B 282    25227  17549  20991  -5306  -1919    738       C  
ATOM   5657  O   LEU B 282     -18.276   2.656  35.004  1.00186.34           O  
ANISOU 5657  O   LEU B 282    27588  19589  23622  -5345  -2183    544       O  
ATOM   5658  CB  LEU B 282     -19.348   3.990  37.739  1.00142.87           C  
ANISOU 5658  CB  LEU B 282    21756  14342  18184  -5823  -1245   1089       C  
ATOM   5659  CG  LEU B 282     -19.520   3.959  39.255  1.00129.66           C  
ANISOU 5659  CG  LEU B 282    20177  12617  16471  -6033   -759   1428       C  
ATOM   5660  CD1 LEU B 282     -20.896   4.466  39.640  1.00127.77           C  
ANISOU 5660  CD1 LEU B 282    19536  12378  16633  -6317   -473   1409       C  
ATOM   5661  CD2 LEU B 282     -19.271   2.560  39.802  1.00133.00           C  
ANISOU 5661  CD2 LEU B 282    20912  12631  16989  -6151   -676   1620       C  
ATOM   5662  N   SER B 283     -17.414   4.726  35.295  1.00152.94           N  
ANISOU 5662  N   SER B 283    23304  16041  18766  -5073  -1979    671       N  
ATOM   5663  CA  SER B 283     -17.321   5.033  33.877  1.00141.41           C  
ANISOU 5663  CA  SER B 283    21836  14675  17218  -4843  -2333    373       C  
ATOM   5664  C   SER B 283     -16.320   4.154  33.124  1.00151.26           C  
ANISOU 5664  C   SER B 283    23416  15774  18281  -4585  -2554    276       C  
ATOM   5665  O   SER B 283     -16.654   3.601  32.077  1.00169.18           O  
ANISOU 5665  O   SER B 283    25739  17851  20691  -4522  -2870      8       O  
ATOM   5666  CB  SER B 283     -16.959   6.504  33.702  1.00130.28           C  
ANISOU 5666  CB  SER B 283    20341  13688  15471  -4665  -2277    380       C  
ATOM   5667  OG  SER B 283     -17.849   7.329  34.435  1.00130.97           O  
ANISOU 5667  OG  SER B 283    20135  13908  15721  -4878  -2060    463       O  
ATOM   5668  N   CYS B 284     -15.102   4.020  33.644  1.00144.37           N  
ANISOU 5668  N   CYS B 284    22768  14976  17109  -4423  -2405    474       N  
ATOM   5669  CA  CYS B 284     -14.067   3.278  32.923  1.00145.38           C  
ANISOU 5669  CA  CYS B 284    23185  14988  17065  -4139  -2576    377       C  
ATOM   5670  C   CYS B 284     -13.665   1.998  33.650  1.00144.04           C  
ANISOU 5670  C   CYS B 284    23226  14484  17019  -4202  -2522    538       C  
ATOM   5671  O   CYS B 284     -12.755   1.293  33.209  1.00132.97           O  
ANISOU 5671  O   CYS B 284    22062  12953  15505  -3963  -2638    481       O  
ATOM   5672  CB  CYS B 284     -12.824   4.142  32.682  1.00154.40           C  
ANISOU 5672  CB  CYS B 284    24403  16469  17794  -3827  -2498    429       C  
ATOM   5673  SG  CYS B 284     -11.872   4.601  34.155  1.00127.69           S  
ANISOU 5673  SG  CYS B 284    21032  13268  14215  -3831  -2203    793       S  
ATOM   5674  N   SER B 285     -14.315   1.729  34.781  1.00164.66           N  
ANISOU 5674  N   SER B 285    25767  16949  19848  -4509  -2322    751       N  
ATOM   5675  CA  SER B 285     -14.111   0.493  35.540  1.00179.14           C  
ANISOU 5675  CA  SER B 285    27827  18415  21824  -4613  -2260    932       C  
ATOM   5676  C   SER B 285     -12.681   0.370  36.056  1.00179.53           C  
ANISOU 5676  C   SER B 285    28132  18536  21548  -4355  -2209   1124       C  
ATOM   5677  O   SER B 285     -12.190  -0.734  36.298  1.00191.80           O  
ANISOU 5677  O   SER B 285    29936  19777  23163  -4301  -2272   1203       O  
ATOM   5678  CB  SER B 285     -14.468  -0.730  34.694  1.00184.09           C  
ANISOU 5678  CB  SER B 285    28557  18637  22751  -4630  -2535    703       C  
ATOM   5679  OG  SER B 285     -14.333  -1.920  35.450  1.00188.22           O  
ANISOU 5679  OG  SER B 285    29305  18772  23440  -4749  -2469    893       O  
ATOM   5680  N   GLU B 286     -12.021   1.509  36.224  1.00152.46           N  
ANISOU 5680  N   GLU B 286    24625  15496  17808  -4195  -2116   1193       N  
ATOM   5681  CA  GLU B 286     -10.668   1.541  36.756  1.00135.13           C  
ANISOU 5681  CA  GLU B 286    22602  13388  15351  -3955  -2092   1367       C  
ATOM   5682  C   GLU B 286     -10.677   2.199  38.122  1.00138.31           C  
ANISOU 5682  C   GLU B 286    23007  13938  15605  -4094  -1868   1653       C  
ATOM   5683  O   GLU B 286     -11.382   3.187  38.330  1.00141.88           O  
ANISOU 5683  O   GLU B 286    23257  14621  16029  -4248  -1722   1658       O  
ATOM   5684  CB  GLU B 286      -9.731   2.295  35.812  1.00130.96           C  
ANISOU 5684  CB  GLU B 286    21995  13161  14603  -3629  -2179   1207       C  
ATOM   5685  CG  GLU B 286      -8.325   1.725  35.729  1.00130.54           C  
ANISOU 5685  CG  GLU B 286    22117  13028  14455  -3315  -2266   1239       C  
ATOM   5686  CD  GLU B 286      -8.213   0.612  34.706  1.00146.00           C  
ANISOU 5686  CD  GLU B 286    24229  14698  16545  -3162  -2444   1015       C  
ATOM   5687  OE1 GLU B 286      -9.255   0.207  34.149  1.00154.82           O  
ANISOU 5687  OE1 GLU B 286    25343  15644  17838  -3327  -2534    845       O  
ATOM   5688  OE2 GLU B 286      -7.081   0.147  34.453  1.00147.94           O  
ANISOU 5688  OE2 GLU B 286    24593  14877  16742  -2869  -2505    992       O  
ATOM   5689  N   GLN B 287      -9.934   1.634  39.069  1.00144.07           N  
ANISOU 5689  N   GLN B 287    23994  14510  16235  -4032  -1856   1885       N  
ATOM   5690  CA  GLN B 287      -9.879   2.225  40.400  1.00134.16           C  
ANISOU 5690  CA  GLN B 287    22826  13371  14779  -4130  -1676   2153       C  
ATOM   5691  C   GLN B 287      -8.705   3.179  40.560  1.00118.21           C  
ANISOU 5691  C   GLN B 287    20761  11666  12487  -3871  -1751   2186       C  
ATOM   5692  O   GLN B 287      -7.610   2.950  40.044  1.00 98.30           O  
ANISOU 5692  O   GLN B 287    18256   9151   9944  -3591  -1933   2113       O  
ATOM   5693  CB  GLN B 287      -9.845   1.155  41.488  1.00136.58           C  
ANISOU 5693  CB  GLN B 287    23489  13308  15096  -4230  -1624   2416       C  
ATOM   5694  CG  GLN B 287      -8.622   0.289  41.523  1.00151.72           C  
ANISOU 5694  CG  GLN B 287    25656  15023  16967  -3955  -1859   2472       C  
ATOM   5695  CD  GLN B 287      -8.625  -0.599  42.744  1.00177.03           C  
ANISOU 5695  CD  GLN B 287    29261  17878  20123  -4056  -1804   2774       C  
ATOM   5696  OE1 GLN B 287      -9.684  -0.912  43.292  1.00184.61           O  
ANISOU 5696  OE1 GLN B 287    30313  18651  21179  -4363  -1567   2904       O  
ATOM   5697  NE2 GLN B 287      -7.443  -1.007  43.183  1.00189.26           N  
ANISOU 5697  NE2 GLN B 287    31052  19320  21537  -3793  -2014   2893       N  
ATOM   5698  N   LEU B 288      -8.971   4.261  41.281  1.00120.51           N  
ANISOU 5698  N   LEU B 288    20980  12205  12604  -3973  -1595   2289       N  
ATOM   5699  CA  LEU B 288      -8.029   5.353  41.470  1.00126.09           C  
ANISOU 5699  CA  LEU B 288    21598  13220  13090  -3781  -1659   2307       C  
ATOM   5700  C   LEU B 288      -6.845   4.952  42.352  1.00141.47           C  
ANISOU 5700  C   LEU B 288    23807  15049  14897  -3595  -1820   2495       C  
ATOM   5701  O   LEU B 288      -6.981   4.124  43.254  1.00164.71           O  
ANISOU 5701  O   LEU B 288    27067  17715  17800  -3676  -1805   2689       O  
ATOM   5702  CB  LEU B 288      -8.760   6.553  42.076  1.00127.49           C  
ANISOU 5702  CB  LEU B 288    21665  13643  13132  -3958  -1455   2358       C  
ATOM   5703  CG  LEU B 288     -10.114   6.868  41.432  1.00129.93           C  
ANISOU 5703  CG  LEU B 288    21727  14015  13625  -4175  -1296   2202       C  
ATOM   5704  CD1 LEU B 288     -10.794   8.040  42.116  1.00137.09           C  
ANISOU 5704  CD1 LEU B 288    22530  15146  14412  -4324  -1080   2256       C  
ATOM   5705  CD2 LEU B 288      -9.956   7.135  39.943  1.00121.88           C  
ANISOU 5705  CD2 LEU B 288    20466  13131  12710  -4026  -1446   1941       C  
ATOM   5706  N   ALA B 289      -5.683   5.533  42.070  1.00124.53           N  
ANISOU 5706  N   ALA B 289    21526  13091  12699  -3341  -1981   2438       N  
ATOM   5707  CA  ALA B 289      -4.452   5.229  42.799  1.00115.05           C  
ANISOU 5707  CA  ALA B 289    20501  11785  11428  -3124  -2203   2576       C  
ATOM   5708  C   ALA B 289      -4.453   5.798  44.225  1.00115.77           C  
ANISOU 5708  C   ALA B 289    20815  11917  11257  -3202  -2205   2786       C  
ATOM   5709  O   ALA B 289      -5.250   6.676  44.558  1.00107.58           O  
ANISOU 5709  O   ALA B 289    19727  11063  10086  -3389  -2009   2798       O  
ATOM   5710  CB  ALA B 289      -3.253   5.744  42.029  1.00111.96           C  
ANISOU 5710  CB  ALA B 289    19828  11579  11133  -2847  -2346   2437       C  
ATOM   5711  N   CYS B 290      -3.566   5.273  45.068  1.00180.32           N  
ANISOU 5711  N   CYS B 290    29170  26889  12455  -5927  -1183   3806       N  
ATOM   5712  CA  CYS B 290      -3.432   5.732  46.451  1.00175.70           C  
ANISOU 5712  CA  CYS B 290    28493  25880  12387  -5924  -1168   3911       C  
ATOM   5713  C   CYS B 290      -2.781   7.109  46.589  1.00164.30           C  
ANISOU 5713  C   CYS B 290    26845  24406  11175  -6029  -1082   4344       C  
ATOM   5714  O   CYS B 290      -1.802   7.422  45.909  1.00149.23           O  
ANISOU 5714  O   CYS B 290    24837  22852   9011  -6071   -858   4455       O  
ATOM   5715  CB  CYS B 290      -2.622   4.714  47.263  1.00176.66           C  
ANISOU 5715  CB  CYS B 290    28660  25963  12500  -5780   -917   3517       C  
ATOM   5716  SG  CYS B 290      -0.914   4.488  46.697  1.00247.31           S  
ANISOU 5716  SG  CYS B 290    37490  35427  21051  -5700   -486   3400       S  
ATOM   5717  N   VAL B 291      -3.340   7.926  47.477  1.00172.18           N  
ANISOU 5717  N   VAL B 291    27786  24975  12659  -6077  -1262   4576       N  
ATOM   5718  CA  VAL B 291      -2.752   9.213  47.837  1.00183.60           C  
ANISOU 5718  CA  VAL B 291    29066  26285  14407  -6183  -1197   4938       C  
ATOM   5719  C   VAL B 291      -1.401   9.058  48.537  1.00195.50           C  
ANISOU 5719  C   VAL B 291    30449  27867  15965  -6167   -871   4804       C  
ATOM   5720  O   VAL B 291      -1.261   8.257  49.460  1.00221.28           O  
ANISOU 5720  O   VAL B 291    33746  30997  19333  -6052   -793   4497       O  
ATOM   5721  CB  VAL B 291      -3.714  10.024  48.749  1.00194.69           C  
ANISOU 5721  CB  VAL B 291    30459  27179  16337  -6201  -1471   5142       C  
ATOM   5722  CG1 VAL B 291      -4.268   9.155  49.879  1.00189.61           C  
ANISOU 5722  CG1 VAL B 291    29888  26250  15907  -6085  -1537   4816       C  
ATOM   5723  CG2 VAL B 291      -3.044  11.288  49.279  1.00192.13           C  
ANISOU 5723  CG2 VAL B 291    29989  26651  16360  -6308  -1396   5448       C  
ATOM   5724  N   ASP B 292      -0.401   9.804  48.077  1.00182.35           N  
ANISOU 5724  N   ASP B 292    28637  26440  14206  -6289   -682   5039       N  
ATOM   5725  CA  ASP B 292       0.875   9.895  48.783  1.00170.93           C  
ANISOU 5725  CA  ASP B 292    27021  25068  12856  -6317   -399   4981       C  
ATOM   5726  C   ASP B 292       1.199  11.352  49.103  1.00173.58           C  
ANISOU 5726  C   ASP B 292    27217  25186  13550  -6521   -430   5378       C  
ATOM   5727  O   ASP B 292       1.328  12.181  48.202  1.00185.00           O  
ANISOU 5727  O   ASP B 292    28630  26774  14887  -6671   -446   5706       O  
ATOM   5728  CB  ASP B 292       2.009   9.260  47.975  1.00166.70           C  
ANISOU 5728  CB  ASP B 292    26410  25102  11827  -6283    -79   4817       C  
ATOM   5729  CG  ASP B 292       1.962   7.740  47.988  1.00163.05           C  
ANISOU 5729  CG  ASP B 292    26084  24797  11071  -6051      9   4338       C  
ATOM   5730  OD1 ASP B 292       1.298   7.168  48.875  1.00141.84           O  
ANISOU 5730  OD1 ASP B 292    23519  21760   8613  -5940   -127   4129       O  
ATOM   5731  OD2 ASP B 292       2.603   7.113  47.119  1.00173.47           O  
ANISOU 5731  OD2 ASP B 292    27397  26586  11930  -5977    218   4161       O  
ATOM   5732  N   THR B 293       1.325  11.659  50.389  1.00165.94           N  
ANISOU 5732  N   THR B 293    26182  23867  13003  -6531   -442   5345       N  
ATOM   5733  CA  THR B 293       1.521  13.034  50.841  1.00164.72           C  
ANISOU 5733  CA  THR B 293    25927  23417  13244  -6722   -508   5674       C  
ATOM   5734  C   THR B 293       2.910  13.547  50.465  1.00168.81           C  
ANISOU 5734  C   THR B 293    26251  24273  13617  -6919   -235   5829       C  
ATOM   5735  O   THR B 293       3.862  12.770  50.379  1.00165.91           O  
ANISOU 5735  O   THR B 293    25773  24314  12950  -6872     38   5605       O  
ATOM   5736  CB  THR B 293       1.317  13.158  52.364  1.00161.22           C  
ANISOU 5736  CB  THR B 293    25460  22534  13262  -6677   -583   5547       C  
ATOM   5737  OG1 THR B 293       2.165  12.224  53.043  1.00174.62           O  
ANISOU 5737  OG1 THR B 293    27070  24434  14844  -6587   -343   5223       O  
ATOM   5738  CG2 THR B 293      -0.135  12.873  52.732  1.00151.07           C  
ANISOU 5738  CG2 THR B 293    24342  20891  12166  -6519   -873   5462       C  
ATOM   5739  N   ASN B 294       3.019  14.854  50.235  1.00178.67           N  
ANISOU 5739  N   ASN B 294    27457  25353  15075  -7138   -310   6211       N  
ATOM   5740  CA  ASN B 294       4.258  15.452  49.738  1.00181.60           C  
ANISOU 5740  CA  ASN B 294    27649  26047  15303  -7377    -75   6415       C  
ATOM   5741  C   ASN B 294       5.394  15.363  50.748  1.00188.78           C  
ANISOU 5741  C   ASN B 294    28344  27035  16350  -7460    151   6245       C  
ATOM   5742  O   ASN B 294       5.237  15.744  51.907  1.00197.71           O  
ANISOU 5742  O   ASN B 294    29463  27758  17900  -7483     50   6200       O  
ATOM   5743  CB  ASN B 294       4.034  16.919  49.364  1.00176.12           C  
ANISOU 5743  CB  ASN B 294    26995  25063  14860  -7603   -238   6875       C  
ATOM   5744  CG  ASN B 294       2.856  17.114  48.438  1.00169.11           C  
ANISOU 5744  CG  ASN B 294    26308  24076  13869  -7515   -494   7082       C  
ATOM   5745  OD1 ASN B 294       1.863  17.742  48.805  1.00156.64           O  
ANISOU 5745  OD1 ASN B 294    24855  22015  12648  -7467   -775   7225       O  
ATOM   5746  ND2 ASN B 294       2.958  16.579  47.227  1.00179.05           N  
ANISOU 5746  ND2 ASN B 294    27591  25815  14626  -7486   -398   7094       N  
ATOM   5747  N   GLU B 295       6.538  14.864  50.295  1.00187.35           N  
ANISOU 5747  N   GLU B 295    27979  27407  15797  -7500    458   6144       N  
ATOM   5748  CA  GLU B 295       7.692  14.652  51.162  1.00187.77           C  
ANISOU 5748  CA  GLU B 295    27787  27651  15904  -7560    696   5964       C  
ATOM   5749  C   GLU B 295       8.162  15.922  51.878  1.00192.95           C  
ANISOU 5749  C   GLU B 295    28313  28012  16990  -7870    655   6204       C  
ATOM   5750  O   GLU B 295       8.317  15.923  53.097  1.00185.79           O  
ANISOU 5750  O   GLU B 295    27335  26877  16379  -7870    638   6047       O  
ATOM   5751  CB  GLU B 295       8.846  14.051  50.357  1.00182.70           C  
ANISOU 5751  CB  GLU B 295    26941  27707  14769  -7561   1034   5866       C  
ATOM   5752  CG  GLU B 295      10.079  13.715  51.182  1.00189.40           C  
ANISOU 5752  CG  GLU B 295    27493  28855  15615  -7586   1296   5658       C  
ATOM   5753  CD  GLU B 295      11.061  14.866  51.258  1.00203.00           C  
ANISOU 5753  CD  GLU B 295    28957  30671  17502  -7971   1401   5943       C  
ATOM   5754  OE1 GLU B 295      10.909  15.827  50.476  1.00210.94           O  
ANISOU 5754  OE1 GLU B 295    30022  31587  18539  -8205   1318   6301       O  
ATOM   5755  OE2 GLU B 295      11.980  14.815  52.101  1.00206.38           O  
ANISOU 5755  OE2 GLU B 295    29123  31265  18026  -8049   1558   5812       O  
ATOM   5756  N   VAL B 296       8.403  16.990  51.122  1.00203.14           N  
ANISOU 5756  N   VAL B 296    29579  29307  18300  -8141    640   6578       N  
ATOM   5757  CA  VAL B 296       8.898  18.242  51.700  1.00217.63           C  
ANISOU 5757  CA  VAL B 296    31306  30850  20533  -8466    603   6810       C  
ATOM   5758  C   VAL B 296       7.928  18.855  52.713  1.00217.06           C  
ANISOU 5758  C   VAL B 296    31414  30067  20993  -8425    303   6821       C  
ATOM   5759  O   VAL B 296       8.353  19.449  53.705  1.00226.68           O  
ANISOU 5759  O   VAL B 296    32530  31035  22565  -8598    292   6798       O  
ATOM   5760  CB  VAL B 296       9.221  19.288  50.596  1.00186.27           C  
ANISOU 5760  CB  VAL B 296    27328  26970  16477  -8758    621   7243       C  
ATOM   5761  CG1 VAL B 296       7.975  19.655  49.799  1.00189.40           C  
ANISOU 5761  CG1 VAL B 296    28018  27064  16880  -8650    356   7487       C  
ATOM   5762  CG2 VAL B 296       9.867  20.533  51.197  1.00186.74           C  
ANISOU 5762  CG2 VAL B 296    27271  26745  16937  -9121    608   7454       C  
ATOM   5763  N   GLU B 297       6.629  18.697  52.476  1.00212.19           N  
ANISOU 5763  N   GLU B 297    31051  29149  20425  -8196     60   6837       N  
ATOM   5764  CA  GLU B 297       5.632  19.203  53.412  1.00188.87           C  
ANISOU 5764  CA  GLU B 297    28255  25556  17952  -8110   -219   6821       C  
ATOM   5765  C   GLU B 297       5.609  18.393  54.706  1.00178.74           C  
ANISOU 5765  C   GLU B 297    26921  24194  16798  -7943   -190   6432       C  
ATOM   5766  O   GLU B 297       5.467  18.959  55.790  1.00169.55           O  
ANISOU 5766  O   GLU B 297    25759  22612  16052  -8000   -301   6384       O  
ATOM   5767  CB  GLU B 297       4.249  19.219  52.761  1.00170.84           C  
ANISOU 5767  CB  GLU B 297    26217  23040  15656  -7908   -482   6949       C  
ATOM   5768  CG  GLU B 297       4.136  20.222  51.625  1.00165.58           C  
ANISOU 5768  CG  GLU B 297    25631  22342  14942  -8074   -565   7385       C  
ATOM   5769  CD  GLU B 297       4.495  21.630  52.068  1.00159.03           C  
ANISOU 5769  CD  GLU B 297    24785  21091  14546  -8339   -629   7643       C  
ATOM   5770  OE1 GLU B 297       4.028  22.051  53.147  1.00158.43           O  
ANISOU 5770  OE1 GLU B 297    24766  20512  14919  -8288   -790   7544       O  
ATOM   5771  OE2 GLU B 297       5.255  22.311  51.347  1.00171.16           O  
ANISOU 5771  OE2 GLU B 297    26256  22800  15975  -8605   -515   7933       O  
ATOM   5772  N   THR B 298       5.744  17.074  54.587  1.00180.49           N  
ANISOU 5772  N   THR B 298    27111  24810  16656  -7732    -42   6153       N  
ATOM   5773  CA  THR B 298       5.824  16.197  55.754  1.00173.90           C  
ANISOU 5773  CA  THR B 298    26229  23962  15882  -7564     16   5797       C  
ATOM   5774  C   THR B 298       7.031  16.577  56.614  1.00181.68           C  
ANISOU 5774  C   THR B 298    26965  25056  17010  -7791    190   5750       C  
ATOM   5775  O   THR B 298       6.925  16.652  57.838  1.00193.00           O  
ANISOU 5775  O   THR B 298    28382  26207  18744  -7781    123   5598       O  
ATOM   5776  CB  THR B 298       5.898  14.698  55.368  1.00156.13           C  
ANISOU 5776  CB  THR B 298    23998  22142  13182  -7298    171   5511       C  
ATOM   5777  OG1 THR B 298       7.026  14.463  54.517  1.00160.95           O  
ANISOU 5777  OG1 THR B 298    24427  23326  13400  -7390    447   5541       O  
ATOM   5778  CG2 THR B 298       4.628  14.266  54.656  1.00136.14           C  
ANISOU 5778  CG2 THR B 298    21713  19480  10536  -7094    -28   5510       C  
ATOM   5779  N   GLN B 299       8.178  16.791  55.972  1.00177.41           N  
ANISOU 5779  N   GLN B 299    26213  24958  16236  -8002    417   5870       N  
ATOM   5780  CA  GLN B 299       9.401  17.150  56.687  1.00172.85           C  
ANISOU 5780  CA  GLN B 299    25348  24568  15759  -8253    592   5833       C  
ATOM   5781  C   GLN B 299       9.229  18.454  57.459  1.00182.26           C  
ANISOU 5781  C   GLN B 299    26568  25209  17472  -8510    402   5984       C  
ATOM   5782  O   GLN B 299       9.698  18.576  58.591  1.00185.42           O  
ANISOU 5782  O   GLN B 299    26826  25536  18092  -8617    429   5826       O  
ATOM   5783  CB  GLN B 299      10.578  17.268  55.718  1.00174.61           C  
ANISOU 5783  CB  GLN B 299    25328  25368  15646  -8457    854   5978       C  
ATOM   5784  CG  GLN B 299      10.965  15.961  55.050  1.00181.73           C  
ANISOU 5784  CG  GLN B 299    26153  26872  16025  -8198   1088   5767       C  
ATOM   5785  CD  GLN B 299      11.417  14.906  56.044  1.00185.46           C  
ANISOU 5785  CD  GLN B 299    26482  27573  16411  -7983   1229   5399       C  
ATOM   5786  OE1 GLN B 299      11.937  15.220  57.116  1.00183.32           O  
ANISOU 5786  OE1 GLN B 299    26033  27238  16383  -8128   1248   5334       O  
ATOM   5787  NE2 GLN B 299      11.220  13.642  55.688  1.00187.11           N  
ANISOU 5787  NE2 GLN B 299    26776  28050  16265  -7632   1323   5150       N  
ATOM   5788  N   LYS B 300       8.565  19.428  56.843  1.00191.47           N  
ANISOU 5788  N   LYS B 300    27921  25997  18830  -8600    208   6279       N  
ATOM   5789  CA  LYS B 300       8.303  20.702  57.504  1.00207.83           C  
ANISOU 5789  CA  LYS B 300    30067  27484  21416  -8801     10   6412       C  
ATOM   5790  C   LYS B 300       7.297  20.488  58.624  1.00222.58           C  
ANISOU 5790  C   LYS B 300    32091  28886  23593  -8567   -194   6180       C  
ATOM   5791  O   LYS B 300       7.321  21.188  59.634  1.00225.11           O  
ANISOU 5791  O   LYS B 300    32397  28820  24315  -8698   -293   6111       O  
ATOM   5792  CB  LYS B 300       7.796  21.751  56.514  1.00211.00           C  
ANISOU 5792  CB  LYS B 300    30647  27598  21924  -8905   -146   6798       C  
ATOM   5793  CG  LYS B 300       8.829  22.169  55.479  1.00215.00           C  
ANISOU 5793  CG  LYS B 300    31000  28515  22173  -9198     49   7068       C  
ATOM   5794  CD  LYS B 300      10.158  22.539  56.129  1.00212.00           C  
ANISOU 5794  CD  LYS B 300    30328  28327  21897  -9537    232   7002       C  
ATOM   5795  CE  LYS B 300      10.062  23.823  56.940  1.00210.37           C  
ANISOU 5795  CE  LYS B 300    30191  27493  22246  -9768     48   7083       C  
ATOM   5796  NZ  LYS B 300      11.371  24.181  57.555  1.00211.63           N  
ANISOU 5796  NZ  LYS B 300    30047  27865  22497 -10130    215   7001       N  
ATOM   5797  N   PHE B 301       6.412  19.514  58.432  1.00229.05           N  
ANISOU 5797  N   PHE B 301    33057  29753  24219  -8232   -255   6048       N  
ATOM   5798  CA  PHE B 301       5.470  19.121  59.473  1.00219.33           C  
ANISOU 5798  CA  PHE B 301    31952  28166  23217  -7995   -417   5811       C  
ATOM   5799  C   PHE B 301       6.170  18.454  60.648  1.00200.16           C  
ANISOU 5799  C   PHE B 301    29353  25928  20771  -7999   -265   5506       C  
ATOM   5800  O   PHE B 301       5.850  18.730  61.803  1.00199.04           O  
ANISOU 5800  O   PHE B 301    29235  25428  20961  -8000   -377   5360       O  
ATOM   5801  CB  PHE B 301       4.402  18.183  58.918  1.00219.77           C  
ANISOU 5801  CB  PHE B 301    32188  28273  23040  -7665   -510   5745       C  
ATOM   5802  CG  PHE B 301       3.318  17.867  59.900  1.00220.60           C  
ANISOU 5802  CG  PHE B 301    32428  27999  23393  -7437   -694   5544       C  
ATOM   5803  CD1 PHE B 301       2.346  18.802  60.206  1.00222.45           C  
ANISOU 5803  CD1 PHE B 301    32798  27690  24032  -7415   -953   5658       C  
ATOM   5804  CD2 PHE B 301       3.282  16.635  60.531  1.00222.96           C  
ANISOU 5804  CD2 PHE B 301    32713  28486  23516  -7238   -604   5244       C  
ATOM   5805  CE1 PHE B 301       1.351  18.509  61.118  1.00223.58           C  
ANISOU 5805  CE1 PHE B 301    33038  27521  24391  -7209  -1108   5469       C  
ATOM   5806  CE2 PHE B 301       2.293  16.336  61.443  1.00221.29           C  
ANISOU 5806  CE2 PHE B 301    32595  27949  23538  -7019   -763   5046       C  
ATOM   5807  CZ  PHE B 301       1.325  17.274  61.736  1.00221.36           C  
ANISOU 5807  CZ  PHE B 301    32728  27453  23926  -7031  -1009   5173       C  
ATOM   5808  N   VAL B 302       7.108  17.563  60.344  1.00176.64           N  
ANISOU 5808  N   VAL B 302    26197  23528  17390  -7986     -7   5404       N  
ATOM   5809  CA  VAL B 302       7.924  16.928  61.369  1.00158.57           C  
ANISOU 5809  CA  VAL B 302    23672  21503  15076  -7924    151   5092       C  
ATOM   5810  C   VAL B 302       8.695  17.978  62.159  1.00158.73           C  
ANISOU 5810  C   VAL B 302    23489  21389  15433  -8251    151   5104       C  
ATOM   5811  O   VAL B 302       8.676  17.984  63.388  1.00154.36           O  
ANISOU 5811  O   VAL B 302    22830  20650  15171  -8126     78   4805       O  
ATOM   5812  CB  VAL B 302       8.915  15.916  60.755  1.00147.12           C  
ANISOU 5812  CB  VAL B 302    22024  20732  13143  -7830    438   4992       C  
ATOM   5813  CG1 VAL B 302       9.884  15.406  61.813  1.00130.18           C  
ANISOU 5813  CG1 VAL B 302    19544  18864  11054  -7690    576   4639       C  
ATOM   5814  CG2 VAL B 302       8.166  14.765  60.097  1.00133.45           C  
ANISOU 5814  CG2 VAL B 302    20501  19110  11093  -7479    432   4889       C  
ATOM   5815  N   ASP B 303       9.368  18.866  61.433  1.00159.84           N  
ANISOU 5815  N   ASP B 303    23563  21632  15539  -8650    224   5422       N  
ATOM   5816  CA  ASP B 303      10.152  19.942  62.031  1.00166.48           C  
ANISOU 5816  CA  ASP B 303    24219  22343  16692  -9036    222   5465       C  
ATOM   5817  C   ASP B 303       9.303  20.905  62.860  1.00177.13           C  
ANISOU 5817  C   ASP B 303    25765  22967  18569  -9080    -56   5440       C  
ATOM   5818  O   ASP B 303       9.734  21.370  63.914  1.00173.87           O  
ANISOU 5818  O   ASP B 303    25209  22411  18445  -9245    -87   5252       O  
ATOM   5819  CB  ASP B 303      10.891  20.717  60.940  1.00174.94           C  
ANISOU 5819  CB  ASP B 303    25182  23610  17676  -9326    317   5766       C  
ATOM   5820  CG  ASP B 303      11.972  19.891  60.270  1.00172.25           C  
ANISOU 5820  CG  ASP B 303    24561  24043  16842  -9338    625   5749       C  
ATOM   5821  OD1 ASP B 303      11.918  18.646  60.364  1.00153.69           O  
ANISOU 5821  OD1 ASP B 303    22184  22033  14178  -9032    741   5535       O  
ATOM   5822  OD2 ASP B 303      12.875  20.487  59.646  1.00176.86           O  
ANISOU 5822  OD2 ASP B 303    24952  24895  17351  -9640    753   5942       O  
ATOM   5823  N   SER B 304       8.109  21.218  62.364  1.00193.23           N  
ANISOU 5823  N   SER B 304    28100  24576  20744  -8885   -263   5583       N  
ATOM   5824  CA  SER B 304       7.199  22.141  63.041  1.00202.14           C  
ANISOU 5824  CA  SER B 304    29426  25012  22367  -8864   -528   5563       C  
ATOM   5825  C   SER B 304       6.700  21.616  64.388  1.00200.29           C  
ANISOU 5825  C   SER B 304    29189  24607  22304  -8640   -604   5185       C  
ATOM   5826  O   SER B 304       6.700  22.344  65.379  1.00213.01           O  
ANISOU 5826  O   SER B 304    30764  25860  24308  -8720   -715   4999       O  
ATOM   5827  CB  SER B 304       6.005  22.462  62.146  1.00209.66           C  
ANISOU 5827  CB  SER B 304    30653  25637  23373  -8649   -722   5799       C  
ATOM   5828  OG  SER B 304       5.332  21.276  61.775  1.00213.80           O  
ANISOU 5828  OG  SER B 304    31259  26403  23571  -8322   -706   5723       O  
ATOM   5829  N   LEU B 305       6.253  20.362  64.419  1.00181.84           N  
ANISOU 5829  N   LEU B 305    26846  22536  19708  -8236   -556   4975       N  
ATOM   5830  CA  LEU B 305       5.745  19.777  65.658  1.00163.17           C  
ANISOU 5830  CA  LEU B 305    24422  20069  17505  -7878   -624   4549       C  
ATOM   5831  C   LEU B 305       6.861  19.637  66.686  1.00149.08           C  
ANISOU 5831  C   LEU B 305    22322  18567  15755  -7941   -496   4241       C  
ATOM   5832  O   LEU B 305       6.638  19.836  67.880  1.00145.59           O  
ANISOU 5832  O   LEU B 305    21821  17908  15590  -7834   -594   3945       O  
ATOM   5833  CB  LEU B 305       5.068  18.425  65.393  1.00169.80           C  
ANISOU 5833  CB  LEU B 305    25339  21131  18048  -7476   -595   4429       C  
ATOM   5834  CG  LEU B 305       5.812  17.237  64.771  1.00181.02           C  
ANISOU 5834  CG  LEU B 305    26640  23143  18997  -7372   -364   4391       C  
ATOM   5835  CD1 LEU B 305       6.636  16.456  65.788  1.00182.81           C  
ANISOU 5835  CD1 LEU B 305    26595  23700  19167  -7197   -224   4028       C  
ATOM   5836  CD2 LEU B 305       4.817  16.309  64.088  1.00185.67           C  
ANISOU 5836  CD2 LEU B 305    27444  23750  19352  -7087   -415   4412       C  
ATOM   5837  N   VAL B 306       8.057  19.292  66.218  1.00141.41           N  
ANISOU 5837  N   VAL B 306    21130  18115  14484  -8105   -279   4306       N  
ATOM   5838  CA  VAL B 306       9.220  19.194  67.088  1.00127.63           C  
ANISOU 5838  CA  VAL B 306    19041  16708  12744  -8191   -160   4050       C  
ATOM   5839  C   VAL B 306       9.457  20.558  67.726  1.00173.05           C  
ANISOU 5839  C   VAL B 306    24760  22082  18909  -8561   -285   4045       C  
ATOM   5840  O   VAL B 306       9.770  20.662  68.912  1.00171.88           O  
ANISOU 5840  O   VAL B 306    24435  21931  18941  -8533   -327   3720       O  
ATOM   5841  CB  VAL B 306      10.475  18.733  66.317  1.00130.08           C  
ANISOU 5841  CB  VAL B 306    19097  17659  12667  -8340     99   4167       C  
ATOM   5842  CG1 VAL B 306      11.733  18.953  67.143  1.00155.62           C  
ANISOU 5842  CG1 VAL B 306    21945  21221  15961  -8534    192   3967       C  
ATOM   5843  CG2 VAL B 306      10.346  17.273  65.916  1.00127.38           C  
ANISOU 5843  CG2 VAL B 306    18764  17697  11938  -7915    227   4055       C  
ATOM   5844  N   ALA B 307       9.282  21.603  66.922  1.00176.98           N  
ANISOU 5844  N   ALA B 307    25448  22247  19551  -8908   -356   4410       N  
ATOM   5845  CA  ALA B 307       9.440  22.981  67.375  1.00187.03           C  
ANISOU 5845  CA  ALA B 307    26757  23058  21248  -9291   -491   4448       C  
ATOM   5846  C   ALA B 307       8.428  23.316  68.469  1.00195.40           C  
ANISOU 5846  C   ALA B 307    27970  23581  22694  -9042   -716   4147       C  
ATOM   5847  O   ALA B 307       8.745  24.043  69.412  1.00201.43           O  
ANISOU 5847  O   ALA B 307    28644  24126  23765  -9218   -798   3913       O  
ATOM   5848  CB  ALA B 307       9.303  23.946  66.207  1.00187.06           C  
ANISOU 5848  CB  ALA B 307    26996  22759  21319  -9660   -538   4954       C  
ATOM   5849  N   LEU B 308       7.209  22.799  68.332  1.00194.94           N  
ANISOU 5849  N   LEU B 308    28129  23329  22608  -8644   -814   4139       N  
ATOM   5850  CA  LEU B 308       6.157  23.046  69.318  1.00203.72           C  
ANISOU 5850  CA  LEU B 308    29367  23986  24051  -8370  -1008   3857       C  
ATOM   5851  C   LEU B 308       6.462  22.347  70.639  1.00210.27           C  
ANISOU 5851  C   LEU B 308    29951  25107  24836  -8141   -956   3385       C  
ATOM   5852  O   LEU B 308       5.938  22.721  71.687  1.00221.63           O  
ANISOU 5852  O   LEU B 308    31411  26246  26554  -8013  -1087   3086       O  
ATOM   5853  CB  LEU B 308       4.797  22.579  68.796  1.00201.71           C  
ANISOU 5853  CB  LEU B 308    29358  23540  23741  -8014  -1113   3979       C  
ATOM   5854  CG  LEU B 308       4.325  23.068  67.426  1.00203.95           C  
ANISOU 5854  CG  LEU B 308    29898  23601  23994  -8151  -1186   4465       C  
ATOM   5855  CD1 LEU B 308       2.917  22.564  67.143  1.00194.70           C  
ANISOU 5855  CD1 LEU B 308    28919  22268  22790  -7764  -1319   4496       C  
ATOM   5856  CD2 LEU B 308       4.391  24.586  67.327  1.00212.23           C  
ANISOU 5856  CD2 LEU B 308    31094  24099  25444  -8501  -1330   4676       C  
ATOM   5857  N   ALA B 309       7.294  21.313  70.575  1.00200.87           N  
ANISOU 5857  N   ALA B 309    28529  24516  23277  -8066   -765   3322       N  
ATOM   5858  CA  ALA B 309       7.681  20.565  71.764  1.00178.06           C  
ANISOU 5858  CA  ALA B 309    25398  21961  20297  -7838   -712   2927       C  
ATOM   5859  C   ALA B 309       8.747  21.332  72.541  1.00179.77           C  
ANISOU 5859  C   ALA B 309    25366  22262  20677  -8172   -712   2741       C  
ATOM   5860  O   ALA B 309       8.677  21.456  73.762  1.00174.69           O  
ANISOU 5860  O   ALA B 309    24628  21562  20184  -8076   -797   2389       O  
ATOM   5861  CB  ALA B 309       8.181  19.184  71.387  1.00158.49           C  
ANISOU 5861  CB  ALA B 309    22775  20057  17387  -7604   -523   2937       C  
ATOM   5862  N   MET B 310       9.742  21.833  71.816  1.00188.63           N  
ANISOU 5862  N   MET B 310    26372  23555  21745  -8581   -615   2977       N  
ATOM   5863  CA  MET B 310      10.813  22.638  72.396  1.00210.54           C  
ANISOU 5863  CA  MET B 310    28900  26417  24677  -8988   -616   2843       C  
ATOM   5864  C   MET B 310      10.292  23.924  73.047  1.00218.52           C  
ANISOU 5864  C   MET B 310    30091  26776  26161  -9186   -831   2705       C  
ATOM   5865  O   MET B 310      10.952  24.509  73.908  1.00227.30           O  
ANISOU 5865  O   MET B 310    31018  27902  27443  -9432   -882   2442       O  
ATOM   5866  CB  MET B 310      11.847  22.981  71.321  1.00223.75           C  
ANISOU 5866  CB  MET B 310    30442  28365  26206  -9428   -464   3193       C  
ATOM   5867  CG  MET B 310      12.519  21.761  70.718  1.00226.79           C  
ANISOU 5867  CG  MET B 310    30604  29447  26121  -9239   -233   3274       C  
ATOM   5868  SD  MET B 310      13.397  20.759  71.932  1.00264.23           S  
ANISOU 5868  SD  MET B 310    34918  34818  30659  -8959   -153   2839       S  
ATOM   5869  CE  MET B 310      14.058  19.469  70.881  1.00203.46           C  
ANISOU 5869  CE  MET B 310    27047  27808  22451  -8735    117   3018       C  
ATOM   5870  N   ASP B 311       9.102  24.350  72.635  1.00193.66           N  
ANISOU 5870  N   ASP B 311    27297  23063  23222  -9062   -964   2865       N  
ATOM   5871  CA  ASP B 311       8.473  25.551  73.172  1.00168.77           C  
ANISOU 5871  CA  ASP B 311    24355  19233  20537  -9174  -1174   2737       C  
ATOM   5872  C   ASP B 311       7.453  25.205  74.251  1.00150.68           C  
ANISOU 5872  C   ASP B 311    22123  16783  18345  -8716  -1285   2346       C  
ATOM   5873  O   ASP B 311       6.259  25.447  74.088  1.00136.49           O  
ANISOU 5873  O   ASP B 311    20591  14535  16733  -8484  -1410   2405       O  
ATOM   5874  CB  ASP B 311       7.794  26.338  72.047  1.00161.55           C  
ANISOU 5874  CB  ASP B 311    23785  17777  19819  -9313  -1270   3176       C  
ATOM   5875  CG  ASP B 311       7.830  27.837  72.272  1.00159.55           C  
ANISOU 5875  CG  ASP B 311    23696  16877  20049  -9684  -1438   3176       C  
ATOM   5876  OD1 ASP B 311       8.878  28.349  72.718  1.00164.69           O  
ANISOU 5876  OD1 ASP B 311    24154  17628  20792 -10085  -1409   3035       O  
ATOM   5877  OD2 ASP B 311       6.805  28.500  72.007  1.00152.26           O  
ANISOU 5877  OD2 ASP B 311    23091  15338  19423  -9570  -1608   3309       O  
ATOM   5878  N   ASN B 322      13.471  20.442  74.621  1.00228.46           N  
ANISOU 5878  N   ASN B 322    30100  30408  26296  -8610   -354   2074       N  
ATOM   5879  CA  ASN B 322      12.914  19.195  75.131  1.00226.07           C  
ANISOU 5879  CA  ASN B 322    29837  30268  25790  -8052   -343   1912       C  
ATOM   5880  C   ASN B 322      13.943  18.070  75.079  1.00233.53           C  
ANISOU 5880  C   ASN B 322    30449  31916  26364  -7842   -171   1885       C  
ATOM   5881  O   ASN B 322      14.011  17.322  74.102  1.00233.75           O  
ANISOU 5881  O   ASN B 322    30521  32149  26147  -7682    -20   2092       O  
ATOM   5882  CB  ASN B 322      11.661  18.810  74.338  1.00209.52           C  
ANISOU 5882  CB  ASN B 322    28130  27799  23679  -7797   -353   2120       C  
ATOM   5883  CG  ASN B 322      10.779  17.820  75.078  1.00194.97           C  
ANISOU 5883  CG  ASN B 322    26401  25923  21754  -7298   -404   1923       C  
ATOM   5884  OD1 ASN B 322      11.267  16.941  75.787  1.00194.81           O  
ANISOU 5884  OD1 ASN B 322    26169  26315  21534  -7042   -353   1738       O  
ATOM   5885  ND2 ASN B 322       9.468  17.958  74.911  1.00186.75           N  
ANISOU 5885  ND2 ASN B 322    25688  24400  20868  -7160   -508   1981       N  
ATOM   5886  N   VAL B 323      14.745  17.963  76.135  1.00234.22           N  
ANISOU 5886  N   VAL B 323    30202  32383  26409  -7830   -202   1616       N  
ATOM   5887  CA  VAL B 323      15.755  16.914  76.240  1.00233.53           C  
ANISOU 5887  CA  VAL B 323    29763  32975  25993  -7584    -66   1564       C  
ATOM   5888  C   VAL B 323      15.117  15.533  76.328  1.00224.62           C  
ANISOU 5888  C   VAL B 323    28801  31895  24650  -6998    -28   1544       C  
ATOM   5889  O   VAL B 323      15.718  14.532  75.938  1.00220.82           O  
ANISOU 5889  O   VAL B 323    28161  31851  23889  -6730    119   1597       O  
ATOM   5890  CB  VAL B 323      16.666  17.130  77.466  1.00234.79           C  
ANISOU 5890  CB  VAL B 323    29529  33522  26160  -7679   -151   1270       C  
ATOM   5891  CG1 VAL B 323      17.497  18.392  77.294  1.00239.68           C  
ANISOU 5891  CG1 VAL B 323    29929  34177  26961  -8299   -167   1292       C  
ATOM   5892  CG2 VAL B 323      15.839  17.201  78.745  1.00227.86           C  
ANISOU 5892  CG2 VAL B 323    28805  32352  25421  -7485   -343    992       C  
ATOM   5893  N   VAL B 324      13.899  15.487  76.853  1.00220.14           N  
ANISOU 5893  N   VAL B 324    28548  30872  24224  -6804   -158   1458       N  
ATOM   5894  CA  VAL B 324      13.134  14.253  76.924  1.00220.98           C  
ANISOU 5894  CA  VAL B 324    28861  30933  24168  -6310   -137   1461       C  
ATOM   5895  C   VAL B 324      12.721  13.761  75.535  1.00228.15           C  
ANISOU 5895  C   VAL B 324    30009  31722  24954  -6226    -15   1724       C  
ATOM   5896  O   VAL B 324      12.709  12.559  75.263  1.00232.75           O  
ANISOU 5896  O   VAL B 324    30636  32493  25304  -5858     79   1750       O  
ATOM   5897  CB  VAL B 324      11.887  14.434  77.796  1.00210.42           C  
ANISOU 5897  CB  VAL B 324    27779  29152  23020  -6183   -300   1316       C  
ATOM   5898  CG1 VAL B 324      11.068  13.177  77.784  1.00207.08           C  
ANISOU 5898  CG1 VAL B 324    27577  28666  22439  -5735   -272   1355       C  
ATOM   5899  CG2 VAL B 324      12.287  14.796  79.218  1.00209.02           C  
ANISOU 5899  CG2 VAL B 324    27367  29151  22899  -6222   -416   1022       C  
ATOM   5900  N   PHE B 325      12.395  14.701  74.656  1.00222.03           N  
ANISOU 5900  N   PHE B 325    29398  30630  24333  -6571    -24   1917       N  
ATOM   5901  CA  PHE B 325      12.002  14.369  73.293  1.00206.96           C  
ANISOU 5901  CA  PHE B 325    27715  28630  22290  -6541     76   2176       C  
ATOM   5902  C   PHE B 325      13.200  13.919  72.463  1.00197.88           C  
ANISOU 5902  C   PHE B 325    26310  28024  20850  -6575    286   2283       C  
ATOM   5903  O   PHE B 325      13.069  13.069  71.585  1.00209.26           O  
ANISOU 5903  O   PHE B 325    27872  29583  22055  -6354    404   2386       O  
ATOM   5904  CB  PHE B 325      11.324  15.564  72.627  1.00204.44           C  
ANISOU 5904  CB  PHE B 325    27638  27826  22213  -6901    -14   2382       C  
ATOM   5905  CG  PHE B 325      10.948  15.326  71.195  1.00197.09           C  
ANISOU 5905  CG  PHE B 325    26929  26839  21118  -6911     72   2670       C  
ATOM   5906  CD1 PHE B 325       9.904  14.476  70.870  1.00180.91           C  
ANISOU 5906  CD1 PHE B 325    25160  24608  18971  -6578     43   2690       C  
ATOM   5907  CD2 PHE B 325      11.646  15.947  70.172  1.00199.96           C  
ANISOU 5907  CD2 PHE B 325    27213  27360  21404  -7275    180   2922       C  
ATOM   5908  CE1 PHE B 325       9.559  14.256  69.556  1.00178.82           C  
ANISOU 5908  CE1 PHE B 325    25093  24322  18528  -6595    106   2931       C  
ATOM   5909  CE2 PHE B 325      11.305  15.728  68.859  1.00198.92           C  
ANISOU 5909  CE2 PHE B 325    27282  27222  21076  -7285    257   3186       C  
ATOM   5910  CZ  PHE B 325      10.263  14.881  68.549  1.00193.14           C  
ANISOU 5910  CZ  PHE B 325    26830  26315  20240  -6938    214   3178       C  
ATOM   5911  N   SER B 326      14.364  14.495  72.744  1.00183.68           N  
ANISOU 5911  N   SER B 326    24148  26575  19066  -6858    333   2237       N  
ATOM   5912  CA  SER B 326      15.605  14.068  72.107  1.00173.24           C  
ANISOU 5912  CA  SER B 326    22496  25861  17464  -6875    542   2301       C  
ATOM   5913  C   SER B 326      15.864  12.587  72.386  1.00176.89           C  
ANISOU 5913  C   SER B 326    22866  26679  17665  -6319    626   2146       C  
ATOM   5914  O   SER B 326      16.379  11.867  71.531  1.00165.10           O  
ANISOU 5914  O   SER B 326    21290  25542  15900  -6152    811   2216       O  
ATOM   5915  CB  SER B 326      16.780  14.923  72.591  1.00172.54           C  
ANISOU 5915  CB  SER B 326    21987  26106  17463  -7272    548   2236       C  
ATOM   5916  OG  SER B 326      18.024  14.356  72.217  1.00169.01           O  
ANISOU 5916  OG  SER B 326    21141  26342  16732  -7204    747   2238       O  
ATOM   5917  N   GLU B 327      15.498  12.145  73.587  1.00211.45           N  
ANISOU 5917  N   GLU B 327    27268  30949  22122  -6031    489   1938       N  
ATOM   5918  CA  GLU B 327      15.575  10.733  73.962  1.00230.34           C  
ANISOU 5918  CA  GLU B 327    29648  33561  24310  -5485    531   1817       C  
ATOM   5919  C   GLU B 327      14.662   9.889  73.080  1.00219.59           C  
ANISOU 5919  C   GLU B 327    28678  31922  22835  -5217    586   1920       C  
ATOM   5920  O   GLU B 327      15.030   8.798  72.643  1.00219.55           O  
ANISOU 5920  O   GLU B 327    28651  32177  22592  -4867    716   1898       O  
ATOM   5921  CB  GLU B 327      15.193  10.544  75.434  1.00237.06           C  
ANISOU 5921  CB  GLU B 327    30504  34290  25279  -5285    354   1621       C  
ATOM   5922  CG  GLU B 327      16.236  11.026  76.429  1.00234.16           C  
ANISOU 5922  CG  GLU B 327    29705  34328  24939  -5428    296   1461       C  
ATOM   5923  CD  GLU B 327      17.300   9.986  76.715  1.00231.45           C  
ANISOU 5923  CD  GLU B 327    29027  34571  24341  -5047    382   1384       C  
ATOM   5924  OE1 GLU B 327      17.046   9.092  77.549  1.00226.86           O  
ANISOU 5924  OE1 GLU B 327    28509  33997  23689  -4634    307   1292       O  
ATOM   5925  OE2 GLU B 327      18.390  10.066  76.111  1.00233.61           O  
ANISOU 5925  OE2 GLU B 327    28968  35308  24485  -5158    525   1428       O  
ATOM   5926  N   PHE B 328      13.462  10.404  72.834  1.00196.92           N  
ANISOU 5926  N   PHE B 328    26160  28519  20139  -5376    477   2015       N  
ATOM   5927  CA  PHE B 328      12.473   9.714  72.017  1.00167.04           C  
ANISOU 5927  CA  PHE B 328    22755  24446  16268  -5180    494   2107       C  
ATOM   5928  C   PHE B 328      12.948   9.579  70.573  1.00166.55           C  
ANISOU 5928  C   PHE B 328    22686  24627  15967  -5263    676   2263       C  
ATOM   5929  O   PHE B 328      12.749   8.539  69.942  1.00153.26           O  
ANISOU 5929  O   PHE B 328    21166  22991  14074  -4963    762   2248       O  
ATOM   5930  CB  PHE B 328      11.130  10.440  72.061  1.00150.98           C  
ANISOU 5930  CB  PHE B 328    21041  21841  14484  -5362    324   2185       C  
ATOM   5931  CG  PHE B 328       9.990   9.633  71.508  1.00137.64           C  
ANISOU 5931  CG  PHE B 328    19717  19854  12724  -5129    296   2234       C  
ATOM   5932  CD1 PHE B 328      10.010   8.250  71.575  1.00131.41           C  
ANISOU 5932  CD1 PHE B 328    18995  19192  11743  -4723    361   2132       C  
ATOM   5933  CD2 PHE B 328       8.902  10.252  70.926  1.00133.10           C  
ANISOU 5933  CD2 PHE B 328    19418  18869  12286  -5315    192   2382       C  
ATOM   5934  CE1 PHE B 328       8.963   7.501  71.074  1.00121.93           C  
ANISOU 5934  CE1 PHE B 328    18132  17709  10486  -4549    326   2160       C  
ATOM   5935  CE2 PHE B 328       7.848   9.507  70.424  1.00123.37           C  
ANISOU 5935  CE2 PHE B 328    18493  17399  10982  -5124    151   2416       C  
ATOM   5936  CZ  PHE B 328       7.880   8.130  70.498  1.00116.17           C  
ANISOU 5936  CZ  PHE B 328    17648  16614   9879  -4761    220   2297       C  
ATOM   5937  N   GLN B 329      13.562  10.643  70.057  1.00179.97           N  
ANISOU 5937  N   GLN B 329    24208  26476  17697  -5687    734   2408       N  
ATOM   5938  CA  GLN B 329      14.056  10.669  68.681  1.00179.51           C  
ANISOU 5938  CA  GLN B 329    24115  26701  17390  -5833    920   2585       C  
ATOM   5939  C   GLN B 329      15.004   9.503  68.425  1.00189.92           C  
ANISOU 5939  C   GLN B 329    25209  28559  18392  -5466   1120   2451       C  
ATOM   5940  O   GLN B 329      14.857   8.766  67.449  1.00184.36           O  
ANISOU 5940  O   GLN B 329    24665  27945  17439  -5274   1240   2475       O  
ATOM   5941  CB  GLN B 329      14.780  11.991  68.386  1.00169.08           C  
ANISOU 5941  CB  GLN B 329    22560  25526  16156  -6373    962   2762       C  
ATOM   5942  CG  GLN B 329      13.906  13.244  68.425  1.00154.15           C  
ANISOU 5942  CG  GLN B 329    20914  23073  14583  -6756    776   2929       C  
ATOM   5943  CD  GLN B 329      14.722  14.525  68.313  1.00143.99           C  
ANISOU 5943  CD  GLN B 329    19388  21899  13424  -7299    804   3081       C  
ATOM   5944  OE1 GLN B 329      15.873  14.584  68.749  1.00138.37           O  
ANISOU 5944  OE1 GLN B 329    18276  21635  12665  -7397    895   2974       O  
ATOM   5945  NE2 GLN B 329      14.131  15.554  67.719  1.00142.29           N  
ANISOU 5945  NE2 GLN B 329    19413  21275  13374  -7662    717   3342       N  
ATOM   5946  N   ASP B 330      15.979   9.347  69.315  1.00221.09           N  
ANISOU 5946  N   ASP B 330    28780  32873  22350  -5357   1146   2293       N  
ATOM   5947  CA  ASP B 330      16.948   8.264  69.221  1.00245.27           C  
ANISOU 5947  CA  ASP B 330    31582  36461  25147  -4958   1317   2150       C  
ATOM   5948  C   ASP B 330      16.294   6.895  69.388  1.00238.62           C  
ANISOU 5948  C   ASP B 330    31039  35399  24228  -4412   1283   2008       C  
ATOM   5949  O   ASP B 330      16.609   5.956  68.660  1.00244.97           O  
ANISOU 5949  O   ASP B 330    31864  36432  24780  -4098   1440   1945       O  
ATOM   5950  CB  ASP B 330      18.045   8.450  70.271  1.00263.62           C  
ANISOU 5950  CB  ASP B 330    33431  39202  27529  -4956   1302   2020       C  
ATOM   5951  CG  ASP B 330      19.087   7.353  70.224  1.00276.68           C  
ANISOU 5951  CG  ASP B 330    34778  41423  28927  -4503   1466   1874       C  
ATOM   5952  OD1 ASP B 330      19.366   6.842  69.118  1.00285.83           O  
ANISOU 5952  OD1 ASP B 330    35949  42820  29833  -4370   1665   1900       O  
ATOM   5953  OD2 ASP B 330      19.628   7.000  71.293  1.00277.87           O  
ANISOU 5953  OD2 ASP B 330    34670  41792  29118  -4260   1391   1728       O  
ATOM   5954  N   TRP B 331      15.383   6.791  70.351  1.00211.19           N  
ANISOU 5954  N   TRP B 331    27795  31477  20970  -4309   1081   1953       N  
ATOM   5955  CA  TRP B 331      14.734   5.522  70.661  1.00187.38           C  
ANISOU 5955  CA  TRP B 331    25064  28217  17917  -3837   1029   1840       C  
ATOM   5956  C   TRP B 331      13.899   5.030  69.482  1.00165.15           C  
ANISOU 5956  C   TRP B 331    22640  25136  14974  -3782   1079   1898       C  
ATOM   5957  O   TRP B 331      13.915   3.842  69.147  1.00152.50           O  
ANISOU 5957  O   TRP B 331    21177  23563  13205  -3389   1155   1789       O  
ATOM   5958  CB  TRP B 331      13.879   5.654  71.924  1.00182.10           C  
ANISOU 5958  CB  TRP B 331    24543  27151  17496  -3819    812   1799       C  
ATOM   5959  CG  TRP B 331      13.301   4.354  72.387  1.00179.86           C  
ANISOU 5959  CG  TRP B 331    24515  26643  17180  -3366    759   1710       C  
ATOM   5960  CD1 TRP B 331      13.914   3.416  73.166  1.00183.41           C  
ANISOU 5960  CD1 TRP B 331    24825  27308  17556  -2956    764   1601       C  
ATOM   5961  CD2 TRP B 331      11.987   3.858  72.122  1.00173.40           C  
ANISOU 5961  CD2 TRP B 331    24137  25333  16413  -3295    679   1740       C  
ATOM   5962  NE1 TRP B 331      13.067   2.358  73.390  1.00178.94           N  
ANISOU 5962  NE1 TRP B 331    24612  26380  16998  -2645    701   1576       N  
ATOM   5963  CE2 TRP B 331      11.876   2.607  72.761  1.00173.94           C  
ANISOU 5963  CE2 TRP B 331    24327  25320  16440  -2863    650   1650       C  
ATOM   5964  CE3 TRP B 331      10.895   4.348  71.403  1.00175.45           C  
ANISOU 5964  CE3 TRP B 331    24691  25224  16749  -3558    620   1847       C  
ATOM   5965  CZ2 TRP B 331      10.716   1.841  72.703  1.00173.71           C  
ANISOU 5965  CZ2 TRP B 331    24701  24850  16451  -2729    575   1656       C  
ATOM   5966  CZ3 TRP B 331       9.747   3.587  71.346  1.00179.23           C  
ANISOU 5966  CZ3 TRP B 331    25540  25305  17255  -3404    538   1837       C  
ATOM   5967  CH2 TRP B 331       9.665   2.346  71.990  1.00174.51           C  
ANISOU 5967  CH2 TRP B 331    25054  24630  16622  -3013    522   1738       C  
ATOM   5968  N   LEU B 332      13.163   5.949  68.865  1.00158.43           N  
ANISOU 5968  N   LEU B 332    21973  24016  14208  -4171   1021   2064       N  
ATOM   5969  CA  LEU B 332      12.310   5.604  67.738  1.00154.73           C  
ANISOU 5969  CA  LEU B 332    21865  23315  13610  -4167   1036   2134       C  
ATOM   5970  C   LEU B 332      13.179   5.178  66.563  1.00170.99           C  
ANISOU 5970  C   LEU B 332    23807  25832  15330  -4086   1270   2118       C  
ATOM   5971  O   LEU B 332      12.840   4.244  65.838  1.00172.68           O  
ANISOU 5971  O   LEU B 332    24264  25999  15350  -3837   1328   2033       O  
ATOM   5972  CB  LEU B 332      11.421   6.777  67.340  1.00143.78           C  
ANISOU 5972  CB  LEU B 332    20658  21588  12384  -4598    911   2345       C  
ATOM   5973  CG  LEU B 332      10.350   6.436  66.304  1.00142.63           C  
ANISOU 5973  CG  LEU B 332    20900  21169  12124  -4592    869   2422       C  
ATOM   5974  CD1 LEU B 332       9.489   5.278  66.777  1.00137.62           C  
ANISOU 5974  CD1 LEU B 332    20536  20224  11529  -4235    772   2258       C  
ATOM   5975  CD2 LEU B 332       9.495   7.651  65.996  1.00142.94           C  
ANISOU 5975  CD2 LEU B 332    21088  20877  12345  -4985    720   2653       C  
ATOM   5976  N   GLU B 333      14.296   5.879  66.384  1.00183.09           N  
ANISOU 5976  N   GLU B 333    24956  27820  16788  -4312   1405   2187       N  
ATOM   5977  CA  GLU B 333      15.262   5.570  65.334  1.00197.70           C  
ANISOU 5977  CA  GLU B 333    26607  30210  18298  -4255   1658   2170       C  
ATOM   5978  C   GLU B 333      15.784   4.141  65.490  1.00210.27           C  
ANISOU 5978  C   GLU B 333    28147  32023  19723  -3677   1766   1905       C  
ATOM   5979  O   GLU B 333      15.882   3.390  64.518  1.00223.77           O  
ANISOU 5979  O   GLU B 333    29972  33896  21154  -3458   1915   1812       O  
ATOM   5980  CB  GLU B 333      16.432   6.562  65.382  1.00203.61           C  
ANISOU 5980  CB  GLU B 333    26885  31436  19040  -4607   1774   2281       C  
ATOM   5981  CG  GLU B 333      16.239   7.877  64.622  1.00203.75           C  
ANISOU 5981  CG  GLU B 333    26938  31397  19081  -5191   1775   2579       C  
ATOM   5982  CD  GLU B 333      16.253   7.706  63.106  1.00199.33           C  
ANISOU 5982  CD  GLU B 333    26498  31080  18159  -5256   1958   2692       C  
ATOM   5983  OE1 GLU B 333      17.230   7.135  62.580  1.00196.69           O  
ANISOU 5983  OE1 GLU B 333    25899  31314  17519  -5071   2198   2583       O  
ATOM   5984  OE2 GLU B 333      15.298   8.152  62.435  1.00196.18           O  
ANISOU 5984  OE2 GLU B 333    26441  30335  17764  -5484   1860   2886       O  
ATOM   5985  N   LYS B 334      16.101   3.777  66.729  1.00208.06           N  
ANISOU 5985  N   LYS B 334    27707  31733  19612  -3421   1679   1783       N  
ATOM   5986  CA  LYS B 334      16.621   2.453  67.070  1.00199.85           C  
ANISOU 5986  CA  LYS B 334    26612  30855  18468  -2842   1745   1559       C  
ATOM   5987  C   LYS B 334      15.681   1.267  66.817  1.00190.16           C  
ANISOU 5987  C   LYS B 334    25864  29182  17205  -2482   1688   1438       C  
ATOM   5988  O   LYS B 334      16.067   0.288  66.180  1.00188.38           O  
ANISOU 5988  O   LYS B 334    25687  29128  16760  -2113   1833   1272       O  
ATOM   5989  CB  LYS B 334      17.039   2.445  68.546  1.00197.24           C  
ANISOU 5989  CB  LYS B 334    26031  30571  18341  -2696   1617   1509       C  
ATOM   5990  CG  LYS B 334      17.602   1.121  69.037  1.00199.44           C  
ANISOU 5990  CG  LYS B 334    26242  30995  18542  -2078   1652   1320       C  
ATOM   5991  CD  LYS B 334      18.860   0.736  68.276  1.00207.64           C  
ANISOU 5991  CD  LYS B 334    26927  32661  19307  -1846   1903   1208       C  
ATOM   5992  CE  LYS B 334      19.527  -0.484  68.890  1.00205.59           C  
ANISOU 5992  CE  LYS B 334    26543  32563  19007  -1202   1916   1030       C  
ATOM   5993  NZ  LYS B 334      19.969  -0.225  70.289  1.00201.38           N  
ANISOU 5993  NZ  LYS B 334    25706  32163  18645  -1165   1761   1065       N  
ATOM   5994  N   HIS B 335      14.449   1.364  67.310  1.00180.54           N  
ANISOU 5994  N   HIS B 335    24993  27398  16206  -2599   1478   1508       N  
ATOM   5995  CA  HIS B 335      13.522   0.226  67.330  1.00179.79           C  
ANISOU 5995  CA  HIS B 335    25333  26847  16133  -2287   1390   1400       C  
ATOM   5996  C   HIS B 335      12.655   0.038  66.084  1.00176.95           C  
ANISOU 5996  C   HIS B 335    25347  26261  15626  -2407   1405   1401       C  
ATOM   5997  O   HIS B 335      11.704  -0.743  66.110  1.00176.39           O  
ANISOU 5997  O   HIS B 335    25655  25755  15609  -2260   1297   1331       O  
ATOM   5998  CB  HIS B 335      12.620   0.308  68.566  1.00176.93           C  
ANISOU 5998  CB  HIS B 335    25129  26033  16062  -2330   1162   1462       C  
ATOM   5999  CG  HIS B 335      13.310  -0.003  69.845  1.00174.46           C  
ANISOU 5999  CG  HIS B 335    24565  25874  15847  -2061   1121   1411       C  
ATOM   6000  ND1 HIS B 335      14.679  -0.254  69.924  1.00175.86           N  
ANISOU 6000  ND1 HIS B 335    24358  26572  15888  -1807   1261   1323       N  
ATOM   6001  CD2 HIS B 335      12.861  -0.129  71.116  1.00164.19           C  
ANISOU 6001  CD2 HIS B 335    23317  24327  14741  -1988    955   1437       C  
ATOM   6002  CE1 HIS B 335      15.015  -0.502  71.161  1.00170.45           C  
ANISOU 6002  CE1 HIS B 335    23513  25936  15313  -1595   1165   1308       C  
ATOM   6003  NE2 HIS B 335      13.918  -0.433  71.920  1.00162.09           N  
ANISOU 6003  NE2 HIS B 335    22725  24413  14448  -1706    980   1380       N  
ATOM   6004  N   GLY B 336      12.953   0.770  65.015  1.00180.65           N  
ANISOU 6004  N   GLY B 336    25707  27030  15903  -2702   1529   1495       N  
ATOM   6005  CA  GLY B 336      12.150   0.699  63.804  1.00186.61           C  
ANISOU 6005  CA  GLY B 336    26792  27631  16480  -2849   1529   1519       C  
ATOM   6006  C   GLY B 336      12.147  -0.707  63.223  1.00191.10           C  
ANISOU 6006  C   GLY B 336    27602  28168  16838  -2422   1616   1252       C  
ATOM   6007  O   GLY B 336      13.087  -1.470  63.446  1.00209.37           O  
ANISOU 6007  O   GLY B 336    29744  30738  19069  -2025   1751   1067       O  
ATOM   6008  N   ASP B 337      11.099  -1.060  62.482  1.00176.28           N  
ANISOU 6008  N   ASP B 337    26124  25977  14880  -2490   1530   1219       N  
ATOM   6009  CA  ASP B 337      10.033  -0.135  62.131  1.00162.61           C  
ANISOU 6009  CA  ASP B 337    24561  24000  13223  -2933   1371   1448       C  
ATOM   6010  C   ASP B 337       8.675  -0.738  62.474  1.00154.76           C  
ANISOU 6010  C   ASP B 337    23961  22429  12411  -2890   1150   1399       C  
ATOM   6011  O   ASP B 337       8.498  -1.953  62.451  1.00160.99           O  
ANISOU 6011  O   ASP B 337    24982  23032  13152  -2571   1152   1171       O  
ATOM   6012  CB  ASP B 337      10.083   0.198  60.635  1.00178.35           C  
ANISOU 6012  CB  ASP B 337    26607  26298  14858  -3142   1484   1501       C  
ATOM   6013  CG  ASP B 337      11.474   0.583  60.158  1.00181.64           C  
ANISOU 6013  CG  ASP B 337    26636  27350  15029  -3157   1747   1518       C  
ATOM   6014  OD1 ASP B 337      12.072   1.518  60.730  1.00182.09           O  
ANISOU 6014  OD1 ASP B 337    26363  27586  15237  -3367   1769   1700       O  
ATOM   6015  OD2 ASP B 337      11.969  -0.047  59.200  1.00178.26           O  
ANISOU 6015  OD2 ASP B 337    26224  27259  14248  -2969   1934   1336       O  
ATOM   6016  N   TYR B 338       7.723   0.125  62.804  1.00151.16           N  
ANISOU 6016  N   TYR B 338    23571  21686  12176  -3216    960   1612       N  
ATOM   6017  CA  TYR B 338       6.374  -0.291  63.161  1.00150.31           C  
ANISOU 6017  CA  TYR B 338    23780  21076  12254  -3235    748   1598       C  
ATOM   6018  C   TYR B 338       5.381   0.144  62.078  1.00145.94           C  
ANISOU 6018  C   TYR B 338    23443  20428  11578  -3529    636   1712       C  
ATOM   6019  O   TYR B 338       5.403   1.290  61.640  1.00149.05           O  
ANISOU 6019  O   TYR B 338    23713  20972  11946  -3831    623   1938       O  
ATOM   6020  CB  TYR B 338       6.002   0.282  64.533  1.00156.28           C  
ANISOU 6020  CB  TYR B 338    24418  21591  13372  -3321    608   1723       C  
ATOM   6021  CG  TYR B 338       6.937  -0.175  65.641  1.00166.57           C  
ANISOU 6021  CG  TYR B 338    25511  23008  14772  -3028    690   1622       C  
ATOM   6022  CD1 TYR B 338       7.546  -1.423  65.591  1.00173.62           C  
ANISOU 6022  CD1 TYR B 338    26469  23971  15526  -2632    804   1411       C  
ATOM   6023  CD2 TYR B 338       7.232   0.651  66.721  1.00165.23           C  
ANISOU 6023  CD2 TYR B 338    25074  22884  14821  -3133    646   1730       C  
ATOM   6024  CE1 TYR B 338       8.409  -1.843  66.589  1.00177.11           C  
ANISOU 6024  CE1 TYR B 338    26710  24536  16048  -2336    860   1344       C  
ATOM   6025  CE2 TYR B 338       8.095   0.237  67.724  1.00170.26           C  
ANISOU 6025  CE2 TYR B 338    25503  23672  15515  -2864    702   1646       C  
ATOM   6026  CZ  TYR B 338       8.679  -1.010  67.654  1.00174.60           C  
ANISOU 6026  CZ  TYR B 338    26114  24302  15924  -2459    805   1471       C  
ATOM   6027  OH  TYR B 338       9.537  -1.426  68.649  1.00171.89           O  
ANISOU 6027  OH  TYR B 338    25556  24121  15632  -2165    842   1412       O  
ATOM   6028  N   GLU B 339       4.530  -0.773  61.633  1.00134.28           N  
ANISOU 6028  N   GLU B 339    22291  18706  10023  -3448    546   1562       N  
ATOM   6029  CA  GLU B 339       3.531  -0.464  60.613  1.00122.38           C  
ANISOU 6029  CA  GLU B 339    20990  17129   8380  -3707    411   1652       C  
ATOM   6030  C   GLU B 339       2.473   0.504  61.133  1.00111.29           C  
ANISOU 6030  C   GLU B 339    19569  15447   7270  -3983    191   1899       C  
ATOM   6031  O   GLU B 339       1.934   1.311  60.384  1.00111.77           O  
ANISOU 6031  O   GLU B 339    19662  15552   7256  -4245     91   2093       O  
ATOM   6032  CB  GLU B 339       2.868  -1.753  60.114  1.00139.33           C  
ANISOU 6032  CB  GLU B 339    23481  19066  10392  -3560    351   1393       C  
ATOM   6033  CG  GLU B 339       3.805  -2.644  59.331  1.00162.62           C  
ANISOU 6033  CG  GLU B 339    26487  22295  13005  -3294    560   1121       C  
ATOM   6034  CD  GLU B 339       3.748  -2.415  57.834  1.00185.53           C  
ANISOU 6034  CD  GLU B 339    29478  25513  15502  -3459    598   1115       C  
ATOM   6035  OE1 GLU B 339       2.634  -2.374  57.272  1.00188.31           O  
ANISOU 6035  OE1 GLU B 339    30048  25701  15800  -3668    408   1155       O  
ATOM   6036  OE2 GLU B 339       4.823  -2.251  57.221  1.00197.92           O  
ANISOU 6036  OE2 GLU B 339    30877  27534  16791  -3387    819   1082       O  
ATOM   6037  N   ALA B 340       2.175   0.421  62.421  1.00113.77           N  
ANISOU 6037  N   ALA B 340    19830  15488   7910  -3907    115   1894       N  
ATOM   6038  CA  ALA B 340       1.215   1.334  63.025  1.00116.91           C  
ANISOU 6038  CA  ALA B 340    20180  15639   8599  -4124    -75   2089       C  
ATOM   6039  C   ALA B 340       1.641   1.746  64.419  1.00129.40           C  
ANISOU 6039  C   ALA B 340    21534  17166  10464  -4061    -52   2119       C  
ATOM   6040  O   ALA B 340       2.483   1.100  65.041  1.00166.69           O  
ANISOU 6040  O   ALA B 340    26173  21982  15178  -3823     74   1983       O  
ATOM   6041  CB  ALA B 340      -0.165   0.701  63.066  1.00115.36           C  
ANISOU 6041  CB  ALA B 340    20228  15112   8491  -4151   -263   2028       C  
ATOM   6042  N   ILE B 341       1.066   2.844  64.895  1.00121.79           N  
ANISOU 6042  N   ILE B 341    20467  16064   9745  -4263   -182   2291       N  
ATOM   6043  CA  ILE B 341       1.317   3.317  66.247  1.00100.70           C  
ANISOU 6043  CA  ILE B 341    17590  13328   7342  -4231   -187   2297       C  
ATOM   6044  C   ILE B 341      -0.012   3.802  66.830  1.00110.39           C  
ANISOU 6044  C   ILE B 341    18864  14242   8838  -4349   -385   2369       C  
ATOM   6045  O   ILE B 341      -0.844   4.359  66.116  1.00 98.99           O  
ANISOU 6045  O   ILE B 341    17507  12696   7408  -4523   -514   2499       O  
ATOM   6046  CB  ILE B 341       2.394   4.426  66.285  1.00101.72           C  
ANISOU 6046  CB  ILE B 341    17456  13701   7492  -4365    -92   2407       C  
ATOM   6047  CG1 ILE B 341       2.030   5.568  65.348  1.00127.83           C  
ANISOU 6047  CG1 ILE B 341    20786  16990  10792  -4658   -172   2634       C  
ATOM   6048  CG2 ILE B 341       3.760   3.875  65.904  1.00103.86           C  
ANISOU 6048  CG2 ILE B 341    17614  14339   7509  -4214    122   2310       C  
ATOM   6049  CD1 ILE B 341       1.484   6.747  66.069  1.00141.63           C  
ANISOU 6049  CD1 ILE B 341    22442  18503  12869  -4825   -316   2751       C  
ATOM   6050  N   VAL B 342      -0.216   3.562  68.123  1.00112.72           N  
ANISOU 6050  N   VAL B 342    19089  14414   9327  -4238   -408   2287       N  
ATOM   6051  CA  VAL B 342      -1.508   3.806  68.760  1.00104.85           C  
ANISOU 6051  CA  VAL B 342    18122  13158   8559  -4306   -569   2314       C  
ATOM   6052  C   VAL B 342      -1.481   4.915  69.802  1.00102.59           C  
ANISOU 6052  C   VAL B 342    17619  12835   8527  -4373   -610   2343       C  
ATOM   6053  O   VAL B 342      -0.522   5.056  70.565  1.00 94.90           O  
ANISOU 6053  O   VAL B 342    16476  12007   7575  -4301   -514   2280       O  
ATOM   6054  CB  VAL B 342      -2.046   2.535  69.458  1.00 94.45           C  
ANISOU 6054  CB  VAL B 342    16931  11704   7250  -4146   -577   2192       C  
ATOM   6055  CG1 VAL B 342      -3.558   2.619  69.638  1.00 93.51           C  
ANISOU 6055  CG1 VAL B 342    16879  11363   7290  -4260   -742   2231       C  
ATOM   6056  CG2 VAL B 342      -1.657   1.287  68.686  1.00 97.38           C  
ANISOU 6056  CG2 VAL B 342    17508  12116   7378  -4012   -494   2095       C  
ATOM   6057  N   ASP B 343      -2.561   5.687  69.830  1.00104.43           N  
ANISOU 6057  N   ASP B 343    17851  12878   8950  -4500   -761   2421       N  
ATOM   6058  CA  ASP B 343      -2.764   6.707  70.843  1.00111.19           C  
ANISOU 6058  CA  ASP B 343    18532  13647  10070  -4543   -819   2405       C  
ATOM   6059  C   ASP B 343      -3.347   6.043  72.083  1.00120.51           C  
ANISOU 6059  C   ASP B 343    19680  14775  11332  -4410   -825   2275       C  
ATOM   6060  O   ASP B 343      -4.548   5.774  72.144  1.00107.91           O  
ANISOU 6060  O   ASP B 343    18153  13040   9807  -4419   -923   2280       O  
ATOM   6061  CB  ASP B 343      -3.681   7.816  70.313  1.00113.17           C  
ANISOU 6061  CB  ASP B 343    18796  13707  10495  -4694   -981   2540       C  
ATOM   6062  CG  ASP B 343      -4.041   8.844  71.371  1.00118.89           C  
ANISOU 6062  CG  ASP B 343    19361  14295  11516  -4706  -1051   2480       C  
ATOM   6063  OD1 ASP B 343      -3.375   8.890  72.427  1.00140.29           O  
ANISOU 6063  OD1 ASP B 343    21934  17098  14273  -4647   -968   2344       O  
ATOM   6064  OD2 ASP B 343      -4.985   9.627  71.138  1.00 96.58           O  
ANISOU 6064  OD2 ASP B 343    16544  11279   8872  -4763  -1198   2560       O  
ATOM   6065  N   GLY B 344      -2.475   5.752  73.046  1.00136.93           N  
ANISOU 6065  N   GLY B 344    21644  17002  13382  -4294   -720   2172       N  
ATOM   6066  CA  GLY B 344      -2.842   5.018  74.244  1.00137.91           C  
ANISOU 6066  CA  GLY B 344    21745  17129  13526  -4161   -704   2078       C  
ATOM   6067  C   GLY B 344      -4.017   5.584  75.020  1.00125.10           C  
ANISOU 6067  C   GLY B 344    20042  15381  12108  -4209   -804   2043       C  
ATOM   6068  O   GLY B 344      -4.927   4.849  75.400  1.00115.04           O  
ANISOU 6068  O   GLY B 344    18833  14044  10831  -4173   -829   2035       O  
ATOM   6069  N   ALA B 345      -3.997   6.893  75.250  1.00121.77           N  
ANISOU 6069  N   ALA B 345    19476  14922  11868  -4296   -858   2016       N  
ATOM   6070  CA  ALA B 345      -5.049   7.565  76.011  1.00112.77           C  
ANISOU 6070  CA  ALA B 345    18234  13677  10936  -4308   -946   1944       C  
ATOM   6071  C   ALA B 345      -6.423   7.395  75.366  1.00112.86           C  
ANISOU 6071  C   ALA B 345    18342  13532  11009  -4349  -1055   2029       C  
ATOM   6072  O   ALA B 345      -7.383   7.023  76.032  1.00107.48           O  
ANISOU 6072  O   ALA B 345    17617  12850  10371  -4308  -1075   1977       O  
ATOM   6073  CB  ALA B 345      -4.725   9.036  76.170  1.00112.12           C  
ANISOU 6073  CB  ALA B 345    18022  13521  11056  -4391   -996   1893       C  
ATOM   6074  N   ASN B 346      -6.505   7.680  74.070  1.00129.47           N  
ANISOU 6074  N   ASN B 346    20558  15539  13097  -4442  -1126   2166       N  
ATOM   6075  CA  ASN B 346      -7.770   7.648  73.341  1.00129.62           C  
ANISOU 6075  CA  ASN B 346    20647  15436  13167  -4492  -1261   2257       C  
ATOM   6076  C   ASN B 346      -8.532   6.336  73.457  1.00127.47           C  
ANISOU 6076  C   ASN B 346    20457  15198  12776  -4471  -1252   2237       C  
ATOM   6077  O   ASN B 346      -9.738   6.339  73.715  1.00132.26           O  
ANISOU 6077  O   ASN B 346    20995  15765  13492  -4484  -1339   2225       O  
ATOM   6078  CB  ASN B 346      -7.531   7.943  7