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***  HYDROLASE 21-SEP-16 5GY1  ***

elNémo ID: 220423185446123146

Job options:

ID        	=	 220423185446123146
JOBID     	=	 HYDROLASE 21-SEP-16 5GY1
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


HEADER    HYDROLASE                               21-SEP-16   5GY1              
TITLE     CRYSTAL STRUCTURE OF ENDOGLUCANASE CELQ FROM CLOSTRIDIUM THERMOCELLUM 
TITLE    2 COMPLEXED WITH CELLOTRIOSE                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLUCANASE;                                                 
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 28-629;                                       
COMPND   5 EC: 3.2.1.-;                                                         
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: CLOSTRIDIUM THERMOCELLUM;                       
SOURCE   3 ORGANISM_TAXID: 1515;                                                
SOURCE   4 ATCC: 27405;                                                         
SOURCE   5 GENE: CELQ;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET-21A                                   
KEYWDS    CELLULASES, GLYCOSYL HYDROLASE, HYDROLASE, CELLULOSOME                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    W.Y.JENG,C.I.LIU,A.H.J.WANG                                           
REVDAT   3   29-JUL-20 5GY1    1       COMPND REMARK HETNAM LINK                
REVDAT   3 2                   1       SITE   ATOM                              
REVDAT   2   10-APR-19 5GY1    1       JRNL                                     
REVDAT   1   27-SEP-17 5GY1    0                                                
JRNL        AUTH   W.Y.JENG,C.I.LIU,T.J.LU,H.J.LIN,N.C.WANG,A.H.WANG            
JRNL        TITL   CRYSTAL STRUCTURES OF THE C-TERMINALLY TRUNCATED             
JRNL        TITL 2 ENDOGLUCANASE CEL9Q FROM CLOSTRIDIUM THERMOCELLUM COMPLEXED  
JRNL        TITL 3 WITH CELLODEXTRINS AND TRIS.                                 
JRNL        REF    CHEMBIOCHEM                   V.  20   295 2019              
JRNL        REFN                   ESSN 1439-7633                               
JRNL        PMID   30609216                                                     
JRNL        DOI    10.1002/CBIC.201800789                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.99 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.99                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 25.94                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 108469                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.156                           
REMARK   3   R VALUE            (WORKING SET) : 0.155                           
REMARK   3   FREE R VALUE                     : 0.184                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 5408                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 10                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.99                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.10                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 14063                        
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 93.62                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1780                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 734                          
REMARK   3   BIN FREE R VALUE                    : 0.2100                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 9592                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 88                                      
REMARK   3   SOLVENT ATOMS            : 905                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 28.70                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 20.90                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00000                                              
REMARK   3    B22 (A**2) : -1.01000                                             
REMARK   3    B33 (A**2) : 1.01000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.131         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.120         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.074         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.760         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.961                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.949                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  9972 ; 0.007 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 13559 ; 1.377 ; 1.936       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1198 ; 6.187 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   514 ;34.884 ;24.047       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1477 ;13.251 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    50 ;13.851 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1387 ; 0.100 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  7884 ; 0.007 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  5958 ; 1.169 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  9488 ; 1.934 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4014 ; 3.313 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  4070 ; 5.065 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    30        A   628                          
REMARK   3    ORIGIN FOR THE GROUP (A): -10.3406  46.3382  24.3521              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0205 T22:   0.0199                                     
REMARK   3      T33:   0.0242 T12:  -0.0008                                     
REMARK   3      T13:   0.0182 T23:   0.0023                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1947 L22:   0.0932                                     
REMARK   3      L33:   0.3727 L12:  -0.1204                                     
REMARK   3      L13:  -0.1891 L23:   0.1467                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0123 S12:  -0.0259 S13:  -0.0181                       
REMARK   3      S21:  -0.0268 S22:   0.0091 S23:  -0.0071                       
REMARK   3      S31:  -0.0343 S32:  -0.0053 S33:  -0.0214                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    30        B   628                          
REMARK   3    ORIGIN FOR THE GROUP (A):   3.1976 -14.1809  -4.8069              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0184 T22:   0.0094                                     
REMARK   3      T33:   0.0243 T12:   0.0046                                     
REMARK   3      T13:   0.0017 T23:   0.0077                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0459 L22:   0.4887                                     
REMARK   3      L33:   0.0713 L12:  -0.0445                                     
REMARK   3      L13:   0.0104 L23:  -0.1473                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0082 S12:   0.0011 S13:  -0.0137                       
REMARK   3      S21:  -0.0310 S22:  -0.0004 S23:   0.0236                       
REMARK   3      S31:   0.0019 S32:  -0.0123 S33:  -0.0078                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 5GY1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 29-SEP-16.                  
REMARK 100 THE DEPOSITION ID IS D_1300001620.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 26-MAR-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSRRC                              
REMARK 200  BEAMLINE                       : BL13B1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00000                            
REMARK 200  MONOCHROMATOR                  : LN2-COOLED FIXED-EXIT DOUBLE       
REMARK 200                                   CRYSTAL SI(111) MONOCHROMATOR      
REMARK 200  OPTICS                         : VERTICALLY COLLIMATING             
REMARK 200                                   PREMIRROR, TOROIDAL FOCUSING       
REMARK 200                                   MIRROR                             
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 108829                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.990                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 7.300                              
REMARK 200  R MERGE                    (I) : 0.13600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 13.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.99                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.06                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.57600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 2.500                              
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: 1GA2                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.30                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.88                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 9-12%(W/V) PEG 3350, 15-20%(V/V) PEG     
REMARK 280  550MME, 30MM NABR, 30MM NAF AND 30MM NAI, 0.1M TRIS, PH 8.5,        
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 295K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       53.27300            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       68.85800            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       54.31150            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       68.85800            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       53.27300            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       54.31150            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
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    27                                                      
REMARK 465     ALA A    28                                                      
REMARK 465     GLY A    29                                                      
REMARK 465     LEU A   629                                                      
REMARK 465     GLU A   630                                                      
REMARK 465     HIS A   631                                                      
REMARK 465     HIS A   632                                                      
REMARK 465     HIS A   633                                                      
REMARK 465     HIS A   634                                                      
REMARK 465     HIS A   635                                                      
REMARK 465     HIS A   636                                                      
REMARK 465     MET B    27                                                      
REMARK 465     ALA B    28                                                      
REMARK 465     GLY B    29                                                      
REMARK 465     LEU B   629                                                      
REMARK 465     GLU B   630                                                      
REMARK 465     HIS B   631                                                      
REMARK 465     HIS B   632                                                      
REMARK 465     HIS B   633                                                      
REMARK 465     HIS B   634                                                      
REMARK 465     HIS B   635                                                      
REMARK 465     HIS B   636                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OE1  GLN A   481     O    HOH A   801              2.07            
REMARK 500   O    HOH B  1097     O    HOH B  1183              2.13            
REMARK 500   OE2  GLU B   264     O4   BGC D     3              2.15            
REMARK 500   O    HOH B  1102     O    HOH B  1124              2.16            
REMARK 500   O    HOH A  1011     O    HOH A  1098              2.17            
REMARK 500   O    GLY B   456     O    HOH B   801              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A 192   NE  -  CZ  -  NH1 ANGL. DEV. =   4.1 DEGREES          
REMARK 500    ARG A 256   NE  -  CZ  -  NH1 ANGL. DEV. =   4.3 DEGREES          
REMARK 500    ARG A 256   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.3 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    ALA A  77     -123.35   -141.44                                   
REMARK 500    ALA A  79     -149.33   -130.18                                   
REMARK 500    LYS A 166       33.20   -140.70                                   
REMARK 500    ASN A 258     -127.35     51.06                                   
REMARK 500    GLN A 266       57.80    -93.03                                   
REMARK 500    VAL A 432      -65.23    -98.10                                   
REMARK 500    SER A 498       -9.61   -158.22                                   
REMARK 500    TRP A 499       63.59   -116.43                                   
REMARK 500    ASP A 506       59.94    -94.21                                   
REMARK 500    TYR A 534      132.30   -173.66                                   
REMARK 500    LEU A 549      -68.54    -99.28                                   
REMARK 500    ASP A 551     -126.77     54.59                                   
REMARK 500    MET A 612       79.68   -116.91                                   
REMARK 500    ALA B  77     -120.83   -141.49                                   
REMARK 500    ALA B  79     -152.09   -133.12                                   
REMARK 500    LYS B 166       31.27   -144.37                                   
REMARK 500    ASN B 258     -130.00     49.21                                   
REMARK 500    ASN B 372       45.49     39.64                                   
REMARK 500    VAL B 432      -66.78    -92.88                                   
REMARK 500    SER B 498       -8.04   -158.64                                   
REMARK 500    TRP B 499       60.73   -118.35                                   
REMARK 500    TYR B 534      131.20   -173.89                                   
REMARK 500    MET B 539       78.73   -105.99                                   
REMARK 500    LEU B 549      -71.81    -98.19                                   
REMARK 500    ASP B 551     -127.80     52.75                                   
REMARK 500    MET B 612       76.27   -119.30                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH B1253        DISTANCE =  6.26 ANGSTROMS                       
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                              CA A 701  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER A 221   OG                                                     
REMARK 620 2 GLY A 222   O    95.6                                              
REMARK 620 3 ASP A 225   OD1  81.2  78.0                                        
REMARK 620 4 ASP A 225   OD2  98.7 122.4  50.1                                  
REMARK 620 5 GLU A 226   OE1 162.3  75.6  82.0  74.3                            
REMARK 620 6 GLU A 226   OE2 145.5 113.8 120.9  81.0  50.7                      
REMARK 620 7 ASP A 272   O    69.0 155.3 116.6  80.2 124.2  77.1                
REMARK 620 8 HOH A 848   O    82.2  79.5 150.4 157.6 110.6  85.8  79.3          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 702  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 514   O                                                      
REMARK 620 2 GLU A 517   OE1  77.9                                              
REMARK 620 3 GLU A 517   OE2 103.4  50.1                                        
REMARK 620 4 ASP A 592   O   169.7  99.1  81.6                                  
REMARK 620 5 ASN A 595   OD1  94.8  86.1 125.8  75.2                            
REMARK 620 6 ASP A 596   OD1  83.7 154.7 153.5  95.8  78.1                      
REMARK 620 7 HOH A 990   O    98.0 125.9  80.0  91.6 147.4  73.7                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 702  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER B 221   OG                                                     
REMARK 620 2 GLY B 222   O    91.9                                              
REMARK 620 3 ASP B 225   OD1  75.7  79.8                                        
REMARK 620 4 ASP B 225   OD2 101.3 125.3  53.6                                  
REMARK 620 5 GLU B 226   OE1 157.7  74.2  84.6  74.4                            
REMARK 620 6 GLU B 226   OE2 149.0 113.9 123.7  78.3  52.6                      
REMARK 620 7 ASP B 272   O    71.5 151.0 116.8  82.1 128.1  77.8                
REMARK 620 8 HOH B 925   O    84.0  76.5 148.2 156.9 108.6  85.7  78.3          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 703  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 514   O                                                      
REMARK 620 2 GLU B 517   OE1  76.5                                              
REMARK 620 3 GLU B 517   OE2  99.7  51.1                                        
REMARK 620 4 ASP B 592   O   167.8  96.3  82.8                                  
REMARK 620 5 ASN B 595   OD1  92.9  83.7 127.4  76.3                            
REMARK 620 6 ASP B 596   OD1  86.9 155.9 151.1  96.7  79.8                      
REMARK 620 7 HOH B 913   O   101.8 127.0  78.1  90.5 148.2  73.1                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5GY0   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5GXZ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5GXY   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5GXX   RELATED DB: PDB                                   
DBREF  5GY1 A   28   628  UNP    Q9AJF8   Q9AJF8_CLOTM    28    628             
DBREF  5GY1 B   28   628  UNP    Q9AJF8   Q9AJF8_CLOTM    28    628             
SEQADV 5GY1 MET A   27  UNP  Q9AJF8              INITIATING METHIONINE          
SEQADV 5GY1 ALA A   79  UNP  Q9AJF8    ASP    79 ENGINEERED MUTATION            
SEQADV 5GY1 THR A  251  UNP  Q9AJF8    ILE   251 ENGINEERED MUTATION            
SEQADV 5GY1 LEU A  629  UNP  Q9AJF8              EXPRESSION TAG                 
SEQADV 5GY1 GLU A  630  UNP  Q9AJF8              EXPRESSION TAG                 
SEQADV 5GY1 HIS A  631  UNP  Q9AJF8              EXPRESSION TAG                 
SEQADV 5GY1 HIS A  632  UNP  Q9AJF8              EXPRESSION TAG                 
SEQADV 5GY1 HIS A  633  UNP  Q9AJF8              EXPRESSION TAG                 
SEQADV 5GY1 HIS A  634  UNP  Q9AJF8              EXPRESSION TAG                 
SEQADV 5GY1 HIS A  635  UNP  Q9AJF8              EXPRESSION TAG                 
SEQADV 5GY1 HIS A  636  UNP  Q9AJF8              EXPRESSION TAG                 
SEQADV 5GY1 MET B   27  UNP  Q9AJF8              INITIATING METHIONINE          
SEQADV 5GY1 ALA B   79  UNP  Q9AJF8    ASP    79 ENGINEERED MUTATION            
SEQADV 5GY1 THR B  251  UNP  Q9AJF8    ILE   251 ENGINEERED MUTATION            
SEQADV 5GY1 LEU B  629  UNP  Q9AJF8              EXPRESSION TAG                 
SEQADV 5GY1 GLU B  630  UNP  Q9AJF8              EXPRESSION TAG                 
SEQADV 5GY1 HIS B  631  UNP  Q9AJF8              EXPRESSION TAG                 
SEQADV 5GY1 HIS B  632  UNP  Q9AJF8              EXPRESSION TAG                 
SEQADV 5GY1 HIS B  633  UNP  Q9AJF8              EXPRESSION TAG                 
SEQADV 5GY1 HIS B  634  UNP  Q9AJF8              EXPRESSION TAG                 
SEQADV 5GY1 HIS B  635  UNP  Q9AJF8              EXPRESSION TAG                 
SEQADV 5GY1 HIS B  636  UNP  Q9AJF8              EXPRESSION TAG                 
SEQRES   1 A  610  MET ALA GLY SER TYR ASN TYR ALA GLU ALA LEU GLN LYS          
SEQRES   2 A  610  ALA ILE TYR PHE TYR GLU CYS GLN GLN ALA GLY PRO LEU          
SEQRES   3 A  610  PRO GLU TRP ASN ARG VAL GLU TRP ARG GLY ASP ALA THR          
SEQRES   4 A  610  MET ASN ASP GLU VAL LEU GLY GLY TRP TYR ASP ALA GLY          
SEQRES   5 A  610  ALA HIS VAL LYS PHE ASN LEU PRO MET ALA TYR SER ALA          
SEQRES   6 A  610  ALA MET LEU GLY TRP ALA LEU TYR GLU TYR GLY ASP ASP          
SEQRES   7 A  610  ILE GLU ALA SER GLY GLN ARG LEU HIS LEU GLU ARG ASN          
SEQRES   8 A  610  LEU ALA PHE ALA LEU ASP TYR LEU VAL ALA CYS ASP ARG          
SEQRES   9 A  610  GLY ASP SER VAL VAL TYR GLN ILE GLY ASP GLY ALA ALA          
SEQRES  10 A  610  ASP HIS LYS TRP TRP GLY SER ALA GLU VAL ILE GLU LYS          
SEQRES  11 A  610  GLU MET THR ARG PRO TYR PHE VAL GLY LYS GLY SER ALA          
SEQRES  12 A  610  VAL VAL GLY GLN MET ALA ALA ALA LEU ALA VAL GLY SER          
SEQRES  13 A  610  ILE VAL LEU LYS ASN ASP THR TYR LEU ARG TYR ALA LYS          
SEQRES  14 A  610  LYS TYR PHE GLU LEU ALA ASP ALA THR ARG SER ASP SER          
SEQRES  15 A  610  THR TYR THR ALA ALA ASN GLY PHE TYR SER SER HIS SER          
SEQRES  16 A  610  GLY PHE TRP ASP GLU LEU LEU TRP ALA SER THR TRP LEU          
SEQRES  17 A  610  TYR LEU ALA THR GLY ASP ARG ASN TYR LEU ASP LYS ALA          
SEQRES  18 A  610  GLU SER TYR THR PRO LYS LEU ASN ARG GLN ASN GLN THR          
SEQRES  19 A  610  THR ASP ILE GLU TYR GLN TRP ALA HIS CYS TRP ASP ASP          
SEQRES  20 A  610  CYS HIS TYR GLY ALA MET ILE LEU LEU ALA ARG ALA THR          
SEQRES  21 A  610  GLY LYS GLU GLU TYR HIS LYS PHE ALA GLN MET HIS LEU          
SEQRES  22 A  610  ASP TRP TRP THR PRO GLN GLY TYR ASN GLY LYS ARG VAL          
SEQRES  23 A  610  ALA TYR THR PRO GLY GLY LEU ALA HIS LEU ASP THR TRP          
SEQRES  24 A  610  GLY PRO LEU ARG TYR ALA THR THR GLU ALA PHE LEU ALA          
SEQRES  25 A  610  PHE VAL TYR ALA ASP SER ILE ASN ASP PRO ALA LEU LYS          
SEQRES  26 A  610  GLN LYS TYR TYR ASN PHE ALA LYS SER GLN ILE ASP TYR          
SEQRES  27 A  610  ALA LEU GLY SER ASN PRO ASP ASN ARG SER TYR VAL VAL          
SEQRES  28 A  610  GLY PHE GLY ASN ASN PRO PRO GLN ARG PRO HIS HIS ARG          
SEQRES  29 A  610  THR ALA HIS GLY THR TRP LEU ASP LYS ARG ASP ILE PRO          
SEQRES  30 A  610  GLU LYS HIS ARG HIS VAL LEU TYR GLY ALA LEU VAL GLY          
SEQRES  31 A  610  GLY PRO GLY ARG ASP ASP SER TYR GLU ASP ASN ILE GLU          
SEQRES  32 A  610  ASP TYR VAL LYS ASN GLU VAL ALA CYS ASP TYR ASN ALA          
SEQRES  33 A  610  GLY PHE VAL GLY ALA LEU CYS ARG LEU THR ALA GLU TYR          
SEQRES  34 A  610  GLY GLY THR PRO LEU ALA ASN PHE PRO PRO PRO GLU GLN          
SEQRES  35 A  610  ARG ASP ASP GLU PHE PHE VAL GLU ALA ALA ILE ASN GLN          
SEQRES  36 A  610  ALA SER ASP HIS PHE THR GLU ILE LYS ALA LEU LEU ASN          
SEQRES  37 A  610  ASN ARG SER SER TRP PRO ALA ARG LEU ILE LYS ASP LEU          
SEQRES  38 A  610  SER TYR ASN TYR TYR MET ASP LEU THR GLU VAL PHE GLU          
SEQRES  39 A  610  ALA GLY TYR SER VAL ASP ASP ILE LYS VAL THR ILE GLY          
SEQRES  40 A  610  TYR CYS GLU SER GLY MET ASP VAL GLU ILE SER PRO ILE          
SEQRES  41 A  610  THR HIS LEU TYR ASP ASN ILE TYR TYR ILE LYS ILE SER          
SEQRES  42 A  610  TYR ILE ASP GLY THR ASN ILE CYS PRO ILE GLY GLN GLU          
SEQRES  43 A  610  GLN TYR ALA ALA GLU LEU GLN PHE ARG ILE ALA ALA PRO          
SEQRES  44 A  610  GLN GLY THR LYS PHE TRP ASP PRO THR ASN ASP PHE SER          
SEQRES  45 A  610  TYR GLN GLY LEU THR ARG GLU LEU ALA LYS THR LYS TYR          
SEQRES  46 A  610  MET PRO VAL PHE ASP GLY ALA THR LYS ILE PHE GLY GLU          
SEQRES  47 A  610  VAL PRO GLY GLY LEU GLU HIS HIS HIS HIS HIS HIS              
SEQRES   1 B  610  MET ALA GLY SER TYR ASN TYR ALA GLU ALA LEU GLN LYS          
SEQRES   2 B  610  ALA ILE TYR PHE TYR GLU CYS GLN GLN ALA GLY PRO LEU          
SEQRES   3 B  610  PRO GLU TRP ASN ARG VAL GLU TRP ARG GLY ASP ALA THR          
SEQRES   4 B  610  MET ASN ASP GLU VAL LEU GLY GLY TRP TYR ASP ALA GLY          
SEQRES   5 B  610  ALA HIS VAL LYS PHE ASN LEU PRO MET ALA TYR SER ALA          
SEQRES   6 B  610  ALA MET LEU GLY TRP ALA LEU TYR GLU TYR GLY ASP ASP          
SEQRES   7 B  610  ILE GLU ALA SER GLY GLN ARG LEU HIS LEU GLU ARG ASN          
SEQRES   8 B  610  LEU ALA PHE ALA LEU ASP TYR LEU VAL ALA CYS ASP ARG          
SEQRES   9 B  610  GLY ASP SER VAL VAL TYR GLN ILE GLY ASP GLY ALA ALA          
SEQRES  10 B  610  ASP HIS LYS TRP TRP GLY SER ALA GLU VAL ILE GLU LYS          
SEQRES  11 B  610  GLU MET THR ARG PRO TYR PHE VAL GLY LYS GLY SER ALA          
SEQRES  12 B  610  VAL VAL GLY GLN MET ALA ALA ALA LEU ALA VAL GLY SER          
SEQRES  13 B  610  ILE VAL LEU LYS ASN ASP THR TYR LEU ARG TYR ALA LYS          
SEQRES  14 B  610  LYS TYR PHE GLU LEU ALA ASP ALA THR ARG SER ASP SER          
SEQRES  15 B  610  THR TYR THR ALA ALA ASN GLY PHE TYR SER SER HIS SER          
SEQRES  16 B  610  GLY PHE TRP ASP GLU LEU LEU TRP ALA SER THR TRP LEU          
SEQRES  17 B  610  TYR LEU ALA THR GLY ASP ARG ASN TYR LEU ASP LYS ALA          
SEQRES  18 B  610  GLU SER TYR THR PRO LYS LEU ASN ARG GLN ASN GLN THR          
SEQRES  19 B  610  THR ASP ILE GLU TYR GLN TRP ALA HIS CYS TRP ASP ASP          
SEQRES  20 B  610  CYS HIS TYR GLY ALA MET ILE LEU LEU ALA ARG ALA THR          
SEQRES  21 B  610  GLY LYS GLU GLU TYR HIS LYS PHE ALA GLN MET HIS LEU          
SEQRES  22 B  610  ASP TRP TRP THR PRO GLN GLY TYR ASN GLY LYS ARG VAL          
SEQRES  23 B  610  ALA TYR THR PRO GLY GLY LEU ALA HIS LEU ASP THR TRP          
SEQRES  24 B  610  GLY PRO LEU ARG TYR ALA THR THR GLU ALA PHE LEU ALA          
SEQRES  25 B  610  PHE VAL TYR ALA ASP SER ILE ASN ASP PRO ALA LEU LYS          
SEQRES  26 B  610  GLN LYS TYR TYR ASN PHE ALA LYS SER GLN ILE ASP TYR          
SEQRES  27 B  610  ALA LEU GLY SER ASN PRO ASP ASN ARG SER TYR VAL VAL          
SEQRES  28 B  610  GLY PHE GLY ASN ASN PRO PRO GLN ARG PRO HIS HIS ARG          
SEQRES  29 B  610  THR ALA HIS GLY THR TRP LEU ASP LYS ARG ASP ILE PRO          
SEQRES  30 B  610  GLU LYS HIS ARG HIS VAL LEU TYR GLY ALA LEU VAL GLY          
SEQRES  31 B  610  GLY PRO GLY ARG ASP ASP SER TYR GLU ASP ASN ILE GLU          
SEQRES  32 B  610  ASP TYR VAL LYS ASN GLU VAL ALA CYS ASP TYR ASN ALA          
SEQRES  33 B  610  GLY PHE VAL GLY ALA LEU CYS ARG LEU THR ALA GLU TYR          
SEQRES  34 B  610  GLY GLY THR PRO LEU ALA ASN PHE PRO PRO PRO GLU GLN          
SEQRES  35 B  610  ARG ASP ASP GLU PHE PHE VAL GLU ALA ALA ILE ASN GLN          
SEQRES  36 B  610  ALA SER ASP HIS PHE THR GLU ILE LYS ALA LEU LEU ASN          
SEQRES  37 B  610  ASN ARG SER SER TRP PRO ALA ARG LEU ILE LYS ASP LEU          
SEQRES  38 B  610  SER TYR ASN TYR TYR MET ASP LEU THR GLU VAL PHE GLU          
SEQRES  39 B  610  ALA GLY TYR SER VAL ASP ASP ILE LYS VAL THR ILE GLY          
SEQRES  40 B  610  TYR CYS GLU SER GLY MET ASP VAL GLU ILE SER PRO ILE          
SEQRES  41 B  610  THR HIS LEU TYR ASP ASN ILE TYR TYR ILE LYS ILE SER          
SEQRES  42 B  610  TYR ILE ASP GLY THR ASN ILE CYS PRO ILE GLY GLN GLU          
SEQRES  43 B  610  GLN TYR ALA ALA GLU LEU GLN PHE ARG ILE ALA ALA PRO          
SEQRES  44 B  610  GLN GLY THR LYS PHE TRP ASP PRO THR ASN ASP PHE SER          
SEQRES  45 B  610  TYR GLN GLY LEU THR ARG GLU LEU ALA LYS THR LYS TYR          
SEQRES  46 B  610  MET PRO VAL PHE ASP GLY ALA THR LYS ILE PHE GLY GLU          
SEQRES  47 B  610  VAL PRO GLY GLY LEU GLU HIS HIS HIS HIS HIS HIS              
HET    BGC  C   1      12                                                       
HET    BGC  C   2      11                                                       
HET    BGC  C   3      11                                                       
HET    BGC  D   1      12                                                       
HET    BGC  D   2      11                                                       
HET    BGC  D   3      11                                                       
HET     CA  A 701       1                                                       
HET     CA  A 702       1                                                       
HET     CL  A 703       1                                                       
HET     CL  A 704       1                                                       
HET     CL  A 705       1                                                       
HET     BR  A 706       1                                                       
HET     CL  A 707       1                                                       
HET     BR  A 708       1                                                       
HET     CL  A 709       1                                                       
HET     BR  A 710       1                                                       
HET     CL  A 714       1                                                       
HET     BR  B 701       1                                                       
HET     CA  B 702       1                                                       
HET     CA  B 703       1                                                       
HET     CL  B 704       1                                                       
HET     CL  B 705       1                                                       
HET     CL  B 706       1                                                       
HET     CL  B 707       1                                                       
HET     CL  B 708       1                                                       
HET     BR  B 709       1                                                       
HETNAM     BGC BETA-D-GLUCOPYRANOSE                                             
HETNAM      CA CALCIUM ION                                                      
HETNAM      CL CHLORIDE ION                                                     
HETNAM      BR BROMIDE ION                                                      
FORMUL   3  BGC    6(C6 H12 O6)                                                 
FORMUL   5   CA    4(CA 2+)                                                     
FORMUL   7   CL    11(CL 1-)                                                    
FORMUL  10   BR    5(BR 1-)                                                     
FORMUL  25  HOH   *905(H2 O)                                                    
HELIX    1 AA1 ASN A   32  GLN A   47  1                                  16    
HELIX    2 AA2 ASN A   84  GLY A  102  1                                  19    
HELIX    3 AA3 ASP A  103  GLY A  109  5                                   7    
HELIX    4 AA4 GLN A  110  CYS A  128  1                                  19    
HELIX    5 AA5 ASP A  140  LYS A  146  1                                   7    
HELIX    6 AA6 SER A  150  GLU A  152  5                                   3    
HELIX    7 AA7 VAL A  153  MET A  158  1                                   6    
HELIX    8 AA8 GLY A  167  LEU A  185  1                                  19    
HELIX    9 AA9 ASN A  187  ARG A  205  1                                  19    
HELIX   10 AB1 PHE A  223  GLY A  239  1                                  17    
HELIX   11 AB2 ASP A  240  THR A  251  1                                  12    
HELIX   12 AB3 PRO A  252  LEU A  254  5                                   3    
HELIX   13 AB4 CYS A  274  GLY A  287  1                                  14    
HELIX   14 AB5 LYS A  288  THR A  303  1                                  16    
HELIX   15 AB6 GLY A  326  ILE A  345  1                                  20    
HELIX   16 AB7 ASP A  347  GLY A  367  1                                  21    
HELIX   17 AB8 HIS A  389  GLY A  394  1                                   6    
HELIX   18 AB9 ALA A  437  GLY A  456  1                                  20    
HELIX   19 AC1 LEU A  515  ALA A  521  1                                   7    
HELIX   20 AC2 SER A  524  ILE A  528  5                                   5    
HELIX   21 AC3 ASP A  562  ILE A  566  5                                   5    
HELIX   22 AC4 ASP A  592  GLN A  600  5                                   9    
HELIX   23 AC5 ASN B   32  GLN B   47  1                                  16    
HELIX   24 AC6 ASN B   84  GLY B  102  1                                  19    
HELIX   25 AC7 ASP B  103  GLU B  106  5                                   4    
HELIX   26 AC8 GLN B  110  CYS B  128  1                                  19    
HELIX   27 AC9 ASP B  140  TRP B  147  1                                   8    
HELIX   28 AD1 SER B  150  GLU B  152  5                                   3    
HELIX   29 AD2 VAL B  153  MET B  158  1                                   6    
HELIX   30 AD3 GLY B  167  LEU B  185  1                                  19    
HELIX   31 AD4 ASN B  187  ARG B  205  1                                  19    
HELIX   32 AD5 PHE B  223  GLY B  239  1                                  17    
HELIX   33 AD6 ASP B  240  THR B  251  1                                  12    
HELIX   34 AD7 PRO B  252  LEU B  254  5                                   3    
HELIX   35 AD8 CYS B  274  GLY B  287  1                                  14    
HELIX   36 AD9 LYS B  288  THR B  303  1                                  16    
HELIX   37 AE1 GLY B  326  ILE B  345  1                                  20    
HELIX   38 AE2 ASP B  347  GLY B  367  1                                  21    
HELIX   39 AE3 HIS B  389  GLY B  394  1                                   6    
HELIX   40 AE4 ALA B  437  GLY B  456  1                                  20    
HELIX   41 AE5 LEU B  515  ALA B  521  1                                   7    
HELIX   42 AE6 SER B  524  ILE B  528  5                                   5    
HELIX   43 AE7 ASP B  562  ILE B  566  5                                   5    
HELIX   44 AE8 ASP B  592  GLN B  600  5                                   9    
SHEET    1 AA1 3 LYS A  82  PHE A  83  0                                        
SHEET    2 AA1 3 VAL A 134  ILE A 138 -1  O  ILE A 138   N  LYS A  82           
SHEET    3 AA1 3 TYR A 162  GLY A 165 -1  O  PHE A 163   N  TYR A 136           
SHEET    1 AA2 5 LYS A 529  CYS A 535  0                                        
SHEET    2 AA2 5 ALA A 575  ALA A 583 -1  O  ALA A 583   N  LYS A 529           
SHEET    3 AA2 5 PHE A 486  ASN A 495 -1  N  ILE A 489   O  PHE A 580           
SHEET    4 AA2 5 PHE A 473  SER A 483 -1  N  GLU A 476   O  LEU A 492           
SHEET    5 AA2 5 ALA A 607  THR A 609 -1  O  ALA A 607   N  ALA A 477           
SHEET    1 AA3 3 VAL A 541  ILE A 543  0                                        
SHEET    2 AA3 3 ILE A 553  TYR A 560 -1  O  SER A 559   N  GLU A 542           
SHEET    3 AA3 3 THR A 547  TYR A 550 -1  N  THR A 547   O  TYR A 555           
SHEET    1 AA4 5 VAL A 541  ILE A 543  0                                        
SHEET    2 AA4 5 ILE A 553  TYR A 560 -1  O  SER A 559   N  GLU A 542           
SHEET    3 AA4 5 LEU A 507  ASP A 514 -1  N  MET A 513   O  TYR A 554           
SHEET    4 AA4 5 VAL A 614  ASP A 616 -1  O  PHE A 615   N  SER A 508           
SHEET    5 AA4 5 THR A 619  PHE A 622 -1  O  ILE A 621   N  VAL A 614           
SHEET    1 AA5 3 LYS B  82  PHE B  83  0                                        
SHEET    2 AA5 3 VAL B 134  ILE B 138 -1  O  ILE B 138   N  LYS B  82           
SHEET    3 AA5 3 TYR B 162  GLY B 165 -1  O  GLY B 165   N  VAL B 134           
SHEET    1 AA6 5 LYS B 529  CYS B 535  0                                        
SHEET    2 AA6 5 ALA B 575  ALA B 583 -1  O  GLN B 579   N  TYR B 534           
SHEET    3 AA6 5 PHE B 486  ASN B 495 -1  N  THR B 487   O  ILE B 582           
SHEET    4 AA6 5 PHE B 473  ALA B 482 -1  N  PHE B 474   O  ASN B 494           
SHEET    5 AA6 5 ALA B 607  THR B 609 -1  O  ALA B 607   N  ALA B 477           
SHEET    1 AA7 3 VAL B 541  ILE B 543  0                                        
SHEET    2 AA7 3 ILE B 553  TYR B 560 -1  O  SER B 559   N  GLU B 542           
SHEET    3 AA7 3 THR B 547  TYR B 550 -1  N  TYR B 550   O  ILE B 553           
SHEET    1 AA8 5 VAL B 541  ILE B 543  0                                        
SHEET    2 AA8 5 ILE B 553  TYR B 560 -1  O  SER B 559   N  GLU B 542           
SHEET    3 AA8 5 LEU B 507  ASP B 514 -1  N  MET B 513   O  TYR B 554           
SHEET    4 AA8 5 VAL B 614  ASP B 616 -1  O  PHE B 615   N  SER B 508           
SHEET    5 AA8 5 THR B 619  PHE B 622 -1  O  THR B 619   N  ASP B 616           
SSBOND   1 CYS A  535    CYS B  535                          1555   1555  2.06  
LINK         O4  BGC C   1                 C1  BGC C   2     1555   1555  1.43  
LINK         O4  BGC C   2                 C1  BGC C   3     1555   1555  1.43  
LINK         O4  BGC D   1                 C1  BGC D   2     1555   1555  1.43  
LINK         O4  BGC D   2                 C1  BGC D   3     1555   1555  1.43  
LINK         OG  SER A 221                CA    CA A 701     1555   1555  2.47  
LINK         O   GLY A 222                CA    CA A 701     1555   1555  2.33  
LINK         OD1 ASP A 225                CA    CA A 701     1555   1555  2.60  
LINK         OD2 ASP A 225                CA    CA A 701     1555   1555  2.57  
LINK         OE1 GLU A 226                CA    CA A 701     1555   1555  2.59  
LINK         OE2 GLU A 226                CA    CA A 701     1555   1555  2.46  
LINK         O   ASP A 272                CA    CA A 701     1555   1555  2.33  
LINK         O   ASP A 514                CA    CA A 702     1555   1555  2.31  
LINK         OE1 GLU A 517                CA    CA A 702     1555   1555  2.72  
LINK         OE2 GLU A 517                CA    CA A 702     1555   1555  2.39  
LINK         O   ASP A 592                CA    CA A 702     1555   1555  2.31  
LINK         OD1 ASN A 595                CA    CA A 702     1555   1555  2.31  
LINK         OD1 ASP A 596                CA    CA A 702     1555   1555  2.55  
LINK        CA    CA A 701                 O   HOH A 848     1555   1555  2.41  
LINK        CA    CA A 702                 O   HOH A 990     1555   1555  2.39  
LINK         OG  SER B 221                CA    CA B 702     1555   1555  2.34  
LINK         O   GLY B 222                CA    CA B 702     1555   1555  2.33  
LINK         OD1 ASP B 225                CA    CA B 702     1555   1555  2.47  
LINK         OD2 ASP B 225                CA    CA B 702     1555   1555  2.34  
LINK         OE1 GLU B 226                CA    CA B 702     1555   1555  2.57  
LINK         OE2 GLU B 226                CA    CA B 702     1555   1555  2.36  
LINK         O   ASP B 272                CA    CA B 702     1555   1555  2.33  
LINK         O   ASP B 514                CA    CA B 703     1555   1555  2.31  
LINK         OE1 GLU B 517                CA    CA B 703     1555   1555  2.65  
LINK         OE2 GLU B 517                CA    CA B 703     1555   1555  2.42  
LINK         O   ASP B 592                CA    CA B 703     1555   1555  2.32  
LINK         OD1 ASN B 595                CA    CA B 703     1555   1555  2.32  
LINK         OD1 ASP B 596                CA    CA B 703     1555   1555  2.34  
LINK        CA    CA B 702                 O   HOH B 925     1555   1555  2.36  
LINK        CA    CA B 703                 O   HOH B 913     1555   1555  2.43  
CISPEP   1 GLY A   50    PRO A   51          0         2.48                     
CISPEP   2 ILE A  402    PRO A  403          0        -2.38                     
CISPEP   3 PHE A  463    PRO A  464          0        -2.62                     
CISPEP   4 TRP A  499    PRO A  500          0        -8.10                     
CISPEP   5 GLY B   50    PRO B   51          0        -0.18                     
CISPEP   6 ILE B  402    PRO B  403          0        -0.72                     
CISPEP   7 PHE B  463    PRO B  464          0         0.04                     
CISPEP   8 TRP B  499    PRO B  500          0        -3.63                     
CRYST1  106.546  108.623  137.716  90.00  90.00  90.00 P 21 21 21    8          
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      0.009386  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009206  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007261        0.00000                         
ATOM      1  N   SER A  30      -1.417  63.828  47.341  1.00 39.45           N  
ANISOU    1  N   SER A  30     4720   5414   4855   -180    338   -469       N  
ATOM      2  CA  SER A  30      -1.373  62.343  47.198  1.00 39.00           C  
ANISOU    2  CA  SER A  30     4646   5377   4794   -149    309   -434       C  
ATOM      3  C   SER A  30      -0.931  62.018  45.773  1.00 36.00           C  
ANISOU    3  C   SER A  30     4284   4963   4428   -163    318   -427       C  
ATOM      4  O   SER A  30       0.160  62.363  45.306  1.00 37.94           O  
ANISOU    4  O   SER A  30     4522   5213   4679   -192    337   -464       O  
ATOM      5  CB  SER A  30      -2.759  61.708  47.430  1.00 37.80           C  
ANISOU    5  CB  SER A  30     4510   5211   4640   -114    287   -380       C  
ATOM      6  OG  SER A  30      -3.393  62.162  48.617  1.00 46.16           O  
ANISOU    6  OG  SER A  30     5561   6289   5687   -102    282   -382       O  
ATOM      7  N   TYR A  31      -1.848  61.362  45.077  1.00 31.28           N  
ANISOU    7  N   TYR A  31     3713   4332   3838   -144    307   -379       N  
ATOM      8  CA  TYR A  31      -1.644  60.913  43.713  1.00 26.45           C  
ANISOU    8  CA  TYR A  31     3121   3688   3239   -150    312   -363       C  
ATOM      9  C   TYR A  31      -1.905  62.071  42.758  1.00 24.40           C  
ANISOU    9  C   TYR A  31     2903   3374   2991   -177    342   -371       C  
ATOM     10  O   TYR A  31      -2.566  63.042  43.119  1.00 21.97           O  
ANISOU   10  O   TYR A  31     2615   3049   2683   -182    355   -375       O  
ATOM     11  CB  TYR A  31      -2.610  59.746  43.464  1.00 25.67           C  
ANISOU   11  CB  TYR A  31     3032   3579   3143   -117    287   -310       C  
ATOM     12  CG  TYR A  31      -2.295  58.563  44.353  1.00 22.51           C  
ANISOU   12  CG  TYR A  31     2595   3227   2730    -89    261   -300       C  
ATOM     13  CD1 TYR A  31      -1.234  57.717  44.047  1.00 22.76           C  
ANISOU   13  CD1 TYR A  31     2604   3282   2760    -86    255   -309       C  
ATOM     14  CD2 TYR A  31      -3.011  58.328  45.528  1.00 21.84           C  
ANISOU   14  CD2 TYR A  31     2497   3166   2632    -64    245   -284       C  
ATOM     15  CE1 TYR A  31      -0.914  56.643  44.864  1.00 22.83           C  
ANISOU   15  CE1 TYR A  31     2582   3335   2755    -57    233   -300       C  
ATOM     16  CE2 TYR A  31      -2.695  57.244  46.349  1.00 20.40           C  
ANISOU   16  CE2 TYR A  31     2284   3028   2437    -35    224   -275       C  
ATOM     17  CZ  TYR A  31      -1.653  56.415  46.007  1.00 21.18           C  
ANISOU   17  CZ  TYR A  31     2365   3148   2534    -31    219   -282       C  
ATOM     18  OH  TYR A  31      -1.292  55.357  46.805  1.00 24.34           O  
ANISOU   18  OH  TYR A  31     2737   3591   2918      0    201   -272       O  
ATOM     19  N   ASN A  32      -1.386  61.966  41.541  1.00 22.80           N  
ANISOU   19  N   ASN A  32     2716   3146   2800   -192    355   -372       N  
ATOM     20  CA  ASN A  32      -1.776  62.885  40.481  1.00 20.78           C  
ANISOU   20  CA  ASN A  32     2506   2834   2554   -210    383   -369       C  
ATOM     21  C   ASN A  32      -3.092  62.384  39.873  1.00 20.20           C  
ANISOU   21  C   ASN A  32     2461   2730   2483   -181    368   -318       C  
ATOM     22  O   ASN A  32      -3.104  61.610  38.903  1.00 18.15           O  
ANISOU   22  O   ASN A  32     2210   2456   2230   -173    360   -295       O  
ATOM     23  CB  ASN A  32      -0.660  63.025  39.433  1.00 21.88           C  
ANISOU   23  CB  ASN A  32     2650   2958   2702   -238    405   -393       C  
ATOM     24  CG  ASN A  32      -0.997  64.044  38.364  1.00 21.01           C  
ANISOU   24  CG  ASN A  32     2590   2790   2600   -255    438   -391       C  
ATOM     25  OD1 ASN A  32      -2.125  64.532  38.291  1.00 22.49           O  
ANISOU   25  OD1 ASN A  32     2810   2947   2786   -241    442   -367       O  
ATOM     26  ND2 ASN A  32      -0.023  64.376  37.529  1.00 23.51           N  
ANISOU   26  ND2 ASN A  32     2915   3091   2925   -283    464   -416       N  
ATOM     27  N   TYR A  33      -4.200  62.848  40.445  1.00 18.72           N  
ANISOU   27  N   TYR A  33     2288   2534   2290   -167    364   -302       N  
ATOM     28  CA  TYR A  33      -5.521  62.407  40.010  1.00 18.17           C  
ANISOU   28  CA  TYR A  33     2240   2442   2221   -139    349   -257       C  
ATOM     29  C   TYR A  33      -5.833  62.852  38.584  1.00 18.99           C  
ANISOU   29  C   TYR A  33     2386   2497   2331   -144    368   -245       C  
ATOM     30  O   TYR A  33      -6.591  62.175  37.889  1.00 16.72           O  
ANISOU   30  O   TYR A  33     2111   2196   2046   -123    354   -211       O  
ATOM     31  CB  TYR A  33      -6.617  62.853  40.979  1.00 19.44           C  
ANISOU   31  CB  TYR A  33     2404   2608   2372   -122    342   -245       C  
ATOM     32  CG  TYR A  33      -6.483  62.312  42.396  1.00 18.86           C  
ANISOU   32  CG  TYR A  33     2291   2584   2290   -111    320   -250       C  
ATOM     33  CD1 TYR A  33      -6.665  60.956  42.677  1.00 14.93           C  
ANISOU   33  CD1 TYR A  33     1769   2112   1791    -88    292   -224       C  
ATOM     34  CD2 TYR A  33      -6.219  63.170  43.461  1.00 20.51           C  
ANISOU   34  CD2 TYR A  33     2487   2813   2491   -122    330   -281       C  
ATOM     35  CE1 TYR A  33      -6.536  60.463  43.981  1.00 16.23           C  
ANISOU   35  CE1 TYR A  33     1898   2321   1944    -74    274   -227       C  
ATOM     36  CE2 TYR A  33      -6.087  62.689  44.773  1.00 22.35           C  
ANISOU   36  CE2 TYR A  33     2683   3093   2714   -108    310   -286       C  
ATOM     37  CZ  TYR A  33      -6.245  61.333  45.021  1.00 19.47           C  
ANISOU   37  CZ  TYR A  33     2296   2754   2346    -83    283   -258       C  
ATOM     38  OH  TYR A  33      -6.139  60.859  46.307  1.00 19.97           O  
ANISOU   38  OH  TYR A  33     2325   2863   2396    -66    265   -261       O  
ATOM     39  N   ALA A  34      -5.265  63.980  38.154  1.00 17.18           N  
ANISOU   39  N   ALA A  34     2181   2242   2105   -170    402   -272       N  
ATOM     40  CA  ALA A  34      -5.468  64.453  36.793  1.00 17.02           C  
ANISOU   40  CA  ALA A  34     2203   2174   2088   -173    424   -262       C  
ATOM     41  C   ALA A  34      -4.853  63.475  35.789  1.00 16.40           C  
ANISOU   41  C   ALA A  34     2117   2095   2018   -174    415   -253       C  
ATOM     42  O   ALA A  34      -5.422  63.221  34.723  1.00 15.67           O  
ANISOU   42  O   ALA A  34     2049   1976   1927   -160    414   -227       O  
ATOM     43  CB  ALA A  34      -4.854  65.853  36.593  1.00 16.53           C  
ANISOU   43  CB  ALA A  34     2167   2082   2028   -203    467   -296       C  
ATOM     44  N   GLU A  35      -3.663  62.970  36.100  1.00 15.88           N  
ANISOU   44  N   GLU A  35     2017   2060   1956   -191    411   -278       N  
ATOM     45  CA  GLU A  35      -3.027  61.979  35.242  1.00 14.87           C  
ANISOU   45  CA  GLU A  35     1878   1936   1834   -191    401   -271       C  
ATOM     46  C   GLU A  35      -3.794  60.658  35.248  1.00 15.88           C  
ANISOU   46  C   GLU A  35     1993   2079   1962   -160    366   -233       C  
ATOM     47  O   GLU A  35      -3.961  60.017  34.210  1.00 14.69           O  
ANISOU   47  O   GLU A  35     1854   1911   1816   -151    359   -212       O  
ATOM     48  CB  GLU A  35      -1.576  61.742  35.667  1.00 17.82           C  
ANISOU   48  CB  GLU A  35     2214   2344   2209   -214    404   -308       C  
ATOM     49  CG  GLU A  35      -0.830  60.725  34.772  1.00 20.52           C  
ANISOU   49  CG  GLU A  35     2545   2691   2558   -214    395   -303       C  
ATOM     50  CD  GLU A  35       0.485  60.266  35.383  1.00 28.96           C  
ANISOU   50  CD  GLU A  35     3570   3806   3624   -227    389   -336       C  
ATOM     51  OE1 GLU A  35       1.074  61.054  36.150  1.00 33.95           O  
ANISOU   51  OE1 GLU A  35     4188   4458   4254   -248    405   -373       O  
ATOM     52  OE2 GLU A  35       0.928  59.127  35.111  1.00 25.91           O  
ANISOU   52  OE2 GLU A  35     3164   3440   3239   -215    370   -326       O  
ATOM     53  N   ALA A  36      -4.250  60.234  36.422  1.00 15.35           N  
ANISOU   53  N   ALA A  36     1900   2042   1888   -144    344   -225       N  
ATOM     54  CA  ALA A  36      -5.070  59.029  36.502  1.00 14.80           C  
ANISOU   54  CA  ALA A  36     1820   1983   1818   -116    314   -189       C  
ATOM     55  C   ALA A  36      -6.322  59.186  35.635  1.00 13.90           C  
ANISOU   55  C   ALA A  36     1740   1833   1705   -101    314   -159       C  
ATOM     56  O   ALA A  36      -6.677  58.272  34.893  1.00 14.49           O  
ANISOU   56  O   ALA A  36     1817   1901   1784    -88    300   -136       O  
ATOM     57  CB  ALA A  36      -5.447  58.751  37.958  1.00 14.32           C  
ANISOU   57  CB  ALA A  36     1733   1957   1749   -101    296   -185       C  
ATOM     58  N   LEU A  37      -6.973  60.346  35.711  1.00 13.49           N  
ANISOU   58  N   LEU A  37     1715   1761   1648   -101    331   -162       N  
ATOM     59  CA  LEU A  37      -8.173  60.601  34.915  1.00 12.79           C  
ANISOU   59  CA  LEU A  37     1659   1643   1556    -84    332   -136       C  
ATOM     60  C   LEU A  37      -7.863  60.582  33.428  1.00 12.51           C  
ANISOU   60  C   LEU A  37     1648   1578   1526    -88    345   -133       C  
ATOM     61  O   LEU A  37      -8.605  60.001  32.641  1.00 10.83           O  
ANISOU   61  O   LEU A  37     1445   1356   1313    -70    332   -108       O  
ATOM     62  CB  LEU A  37      -8.782  61.963  35.262  1.00 11.56           C  
ANISOU   62  CB  LEU A  37     1530   1470   1392    -83    352   -143       C  
ATOM     63  CG  LEU A  37     -10.047  62.390  34.522  1.00 13.78           C  
ANISOU   63  CG  LEU A  37     1845   1723   1665    -60    355   -119       C  
ATOM     64  CD1 LEU A  37     -11.188  61.380  34.748  1.00  9.84           C  
ANISOU   64  CD1 LEU A  37     1330   1244   1164    -34    323    -89       C  
ATOM     65  CD2 LEU A  37     -10.455  63.803  34.991  1.00 17.39           C  
ANISOU   65  CD2 LEU A  37     2329   2164   2114    -60    378   -129       C  
ATOM     66  N   GLN A  38      -6.793  61.275  33.051  1.00 13.69           N  
ANISOU   66  N   GLN A  38     1808   1713   1678   -113    371   -159       N  
ATOM     67  CA  GLN A  38      -6.329  61.291  31.673  1.00 14.16           C  
ANISOU   67  CA  GLN A  38     1890   1746   1743   -120    386   -159       C  
ATOM     68  C   GLN A  38      -6.215  59.855  31.138  1.00 14.82           C  
ANISOU   68  C   GLN A  38     1953   1844   1833   -110    361   -142       C  
ATOM     69  O   GLN A  38      -6.709  59.522  30.057  1.00 11.14           O  
ANISOU   69  O   GLN A  38     1505   1359   1366    -96    357   -123       O  
ATOM     70  CB  GLN A  38      -4.955  61.944  31.648  1.00 15.56           C  
ANISOU   70  CB  GLN A  38     2066   1918   1924   -153    414   -196       C  
ATOM     71  CG  GLN A  38      -4.270  62.011  30.285  1.00 15.57           C  
ANISOU   71  CG  GLN A  38     2089   1893   1931   -165    435   -200       C  
ATOM     72  CD  GLN A  38      -2.916  62.706  30.379  1.00 18.67           C  
ANISOU   72  CD  GLN A  38     2478   2284   2329   -201    465   -240       C  
ATOM     73  OE1 GLN A  38      -2.221  62.590  31.389  1.00 17.40           O  
ANISOU   73  OE1 GLN A  38     2283   2156   2170   -217    459   -265       O  
ATOM     74  NE2 GLN A  38      -2.530  63.416  29.325  1.00 18.47           N  
ANISOU   74  NE2 GLN A  38     2489   2222   2306   -215    498   -248       N  
ATOM     75  N   LYS A  39      -5.530  59.003  31.897  1.00 13.33           N  
ANISOU   75  N   LYS A  39     1727   1688   1649   -115    344   -150       N  
ATOM     76  CA  LYS A  39      -5.311  57.649  31.410  1.00 12.94           C  
ANISOU   76  CA  LYS A  39     1660   1651   1606   -107    323   -136       C  
ATOM     77  C   LYS A  39      -6.602  56.827  31.428  1.00 12.76           C  
ANISOU   77  C   LYS A  39     1635   1631   1582    -81    298   -104       C  
ATOM     78  O   LYS A  39      -6.861  56.048  30.496  1.00 13.14           O  
ANISOU   78  O   LYS A  39     1689   1670   1634    -72    289    -87       O  
ATOM     79  CB  LYS A  39      -4.151  57.000  32.173  1.00 12.46           C  
ANISOU   79  CB  LYS A  39     1561   1624   1547   -118    314   -155       C  
ATOM     80  CG  LYS A  39      -2.838  57.729  31.879  1.00 13.56           C  
ANISOU   80  CG  LYS A  39     1702   1760   1689   -146    340   -190       C  
ATOM     81  CD  LYS A  39      -1.672  57.121  32.648  1.00 13.29           C  
ANISOU   81  CD  LYS A  39     1627   1766   1654   -154    331   -212       C  
ATOM     82  CE  LYS A  39      -0.362  57.721  32.132  1.00 15.27           C  
ANISOU   82  CE  LYS A  39     1879   2015   1909   -184    356   -247       C  
ATOM     83  NZ  LYS A  39       0.785  57.365  33.030  1.00 14.11           N  
ANISOU   83  NZ  LYS A  39     1690   1914   1758   -192    350   -276       N  
ATOM     84  N   ALA A  40      -7.409  57.010  32.472  1.00 12.40           N  
ANISOU   84  N   ALA A  40     1582   1599   1530    -70    289    -96       N  
ATOM     85  CA  ALA A  40      -8.638  56.218  32.635  1.00 12.19           C  
ANISOU   85  CA  ALA A  40     1549   1578   1502    -48    267    -68       C  
ATOM     86  C   ALA A  40      -9.639  56.471  31.505  1.00 12.63           C  
ANISOU   86  C   ALA A  40     1634   1608   1555    -35    270    -52       C  
ATOM     87  O   ALA A  40     -10.452  55.611  31.169  1.00 13.81           O  
ANISOU   87  O   ALA A  40     1779   1761   1706    -20    253    -32       O  
ATOM     88  CB  ALA A  40      -9.274  56.536  33.971  1.00 12.07           C  
ANISOU   88  CB  ALA A  40     1523   1582   1480    -40    261    -66       C  
ATOM     89  N   ILE A  41      -9.577  57.669  30.927  1.00 12.83           N  
ANISOU   89  N   ILE A  41     1690   1609   1575    -39    293    -62       N  
ATOM     90  CA  ILE A  41     -10.403  58.035  29.786  1.00 13.33           C  
ANISOU   90  CA  ILE A  41     1783   1648   1631    -24    299    -49       C  
ATOM     91  C   ILE A  41      -9.824  57.459  28.493  1.00 12.51           C  
ANISOU   91  C   ILE A  41     1686   1531   1534    -28    301    -48       C  
ATOM     92  O   ILE A  41     -10.570  56.959  27.645  1.00 11.94           O  
ANISOU   92  O   ILE A  41     1620   1455   1459    -11    290    -32       O  
ATOM     93  CB  ILE A  41     -10.540  59.576  29.661  1.00 14.32           C  
ANISOU   93  CB  ILE A  41     1943   1749   1746    -24    326    -58       C  
ATOM     94  CG1 ILE A  41     -11.314  60.188  30.840  1.00 12.04           C  
ANISOU   94  CG1 ILE A  41     1653   1472   1450    -16    324    -57       C  
ATOM     95  CG2 ILE A  41     -11.190  59.942  28.311  1.00 10.68           C  
ANISOU   95  CG2 ILE A  41     1517   1263   1276     -5    335    -45       C  
ATOM     96  CD1 ILE A  41     -11.173  61.733  30.918  1.00 15.08           C  
ANISOU   96  CD1 ILE A  41     2070   1832   1826    -22    355    -71       C  
ATOM     97  N   TYR A  42      -8.501  57.528  28.353  1.00 11.31           N  
ANISOU   97  N   TYR A  42     1531   1377   1390    -50    314    -66       N  
ATOM     98  CA  TYR A  42      -7.799  56.980  27.188  1.00 12.39           C  
ANISOU   98  CA  TYR A  42     1672   1503   1533    -56    317    -68       C  
ATOM     99  C   TYR A  42      -8.113  55.487  27.029  1.00 10.89           C  
ANISOU   99  C   TYR A  42     1458   1329   1349    -45    289    -51       C  
ATOM    100  O   TYR A  42      -8.259  54.978  25.918  1.00 11.08           O  
ANISOU  100  O   TYR A  42     1490   1343   1375    -38    285    -43       O  
ATOM    101  CB  TYR A  42      -6.289  57.232  27.356  1.00 11.27           C  
ANISOU  101  CB  TYR A  42     1521   1362   1396    -83    334    -94       C  
ATOM    102  CG  TYR A  42      -5.372  56.592  26.337  1.00 12.50           C  
ANISOU  102  CG  TYR A  42     1674   1513   1560    -92    336    -99       C  
ATOM    103  CD1 TYR A  42      -4.908  55.294  26.516  1.00 11.37           C  
ANISOU  103  CD1 TYR A  42     1501   1393   1425    -92    315    -96       C  
ATOM    104  CD2 TYR A  42      -4.955  57.299  25.203  1.00 12.44           C  
ANISOU  104  CD2 TYR A  42     1697   1476   1550   -100    361   -106       C  
ATOM    105  CE1 TYR A  42      -4.040  54.721  25.587  1.00 13.66           C  
ANISOU  105  CE1 TYR A  42     1789   1678   1721   -100    317   -101       C  
ATOM    106  CE2 TYR A  42      -4.093  56.750  24.284  1.00 14.61           C  
ANISOU  106  CE2 TYR A  42     1971   1748   1832   -108    364   -111       C  
ATOM    107  CZ  TYR A  42      -3.635  55.461  24.485  1.00 15.48           C  
ANISOU  107  CZ  TYR A  42     2048   1882   1950   -109    341   -109       C  
ATOM    108  OH  TYR A  42      -2.775  54.898  23.575  1.00 13.94           O  
ANISOU  108  OH  TYR A  42     1851   1684   1761   -116    344   -114       O  
ATOM    109  N   PHE A  43      -8.245  54.774  28.138  1.00  9.93           N  
ANISOU  109  N   PHE A  43     1308   1233   1232    -44    271    -47       N  
ATOM    110  CA  PHE A  43      -8.672  53.364  28.081  1.00 10.99           C  
ANISOU  110  CA  PHE A  43     1422   1380   1372    -33    248    -31       C  
ATOM    111  C   PHE A  43      -9.823  53.133  27.088  1.00 11.86           C  
ANISOU  111  C   PHE A  43     1548   1479   1480    -17    242    -15       C  
ATOM    112  O   PHE A  43      -9.811  52.167  26.322  1.00 11.38           O  
ANISOU  112  O   PHE A  43     1482   1416   1426    -14    232     -8       O  
ATOM    113  CB  PHE A  43      -9.091  52.869  29.477  1.00  9.57           C  
ANISOU  113  CB  PHE A  43     1217   1224   1192    -27    234    -24       C  
ATOM    114  CG  PHE A  43      -9.745  51.511  29.461  1.00 11.32           C  
ANISOU  114  CG  PHE A  43     1424   1455   1420    -16    215     -5       C  
ATOM    115  CD1 PHE A  43      -9.007  50.371  29.163  1.00 12.50           C  
ANISOU  115  CD1 PHE A  43     1560   1608   1579    -20    209     -4       C  
ATOM    116  CD2 PHE A  43     -11.115  51.384  29.647  1.00 13.43           C  
ANISOU  116  CD2 PHE A  43     1692   1724   1684     -3    206      9       C  
ATOM    117  CE1 PHE A  43      -9.623  49.122  29.104  1.00 12.60           C  
ANISOU  117  CE1 PHE A  43     1563   1625   1599    -11    195     11       C  
ATOM    118  CE2 PHE A  43     -11.740  50.139  29.590  1.00 11.95           C  
ANISOU  118  CE2 PHE A  43     1491   1543   1504      2    192     23       C  
ATOM    119  CZ  PHE A  43     -10.987  48.997  29.328  1.00 14.09           C  
ANISOU  119  CZ  PHE A  43     1752   1816   1786     -2    188     24       C  
ATOM    120  N   TYR A  44     -10.838  53.996  27.113  1.00 11.86           N  
ANISOU  120  N   TYR A  44     1564   1472   1468     -4    246     -9       N  
ATOM    121  CA  TYR A  44     -11.972  53.821  26.196  1.00 12.19           C  
ANISOU  121  CA  TYR A  44     1618   1509   1504     13    238      2       C  
ATOM    122  C   TYR A  44     -11.620  53.914  24.707  1.00 13.28           C  
ANISOU  122  C   TYR A  44     1776   1628   1640     16    248      0       C  
ATOM    123  O   TYR A  44     -12.264  53.260  23.886  1.00 11.88           O  
ANISOU  123  O   TYR A  44     1598   1453   1463     28    237      8       O  
ATOM    124  CB  TYR A  44     -13.144  54.742  26.540  1.00 10.78           C  
ANISOU  124  CB  TYR A  44     1453   1331   1312     30    240      8       C  
ATOM    125  CG  TYR A  44     -13.746  54.368  27.883  1.00 11.30           C  
ANISOU  125  CG  TYR A  44     1494   1419   1379     32    227     14       C  
ATOM    126  CD1 TYR A  44     -14.673  53.342  27.973  1.00  9.66           C  
ANISOU  126  CD1 TYR A  44     1267   1227   1175     40    208     26       C  
ATOM    127  CD2 TYR A  44     -13.346  55.003  29.058  1.00 12.22           C  
ANISOU  127  CD2 TYR A  44     1606   1541   1495     23    233      7       C  
ATOM    128  CE1 TYR A  44     -15.214  52.978  29.193  1.00 10.86           C  
ANISOU  128  CE1 TYR A  44     1399   1398   1329     41    198     32       C  
ATOM    129  CE2 TYR A  44     -13.904  54.667  30.301  1.00 13.07           C  
ANISOU  129  CE2 TYR A  44     1693   1670   1603     26    221     13       C  
ATOM    130  CZ  TYR A  44     -14.818  53.629  30.360  1.00 13.28           C  
ANISOU  130  CZ  TYR A  44     1702   1710   1634     35    204     27       C  
ATOM    131  OH  TYR A  44     -15.380  53.249  31.568  1.00 10.55           O  
ANISOU  131  OH  TYR A  44     1336   1383   1288     38    194     34       O  
ATOM    132  N   GLU A  45     -10.604  54.703  24.358  1.00 11.38           N  
ANISOU  132  N   GLU A  45     1554   1370   1398      4    269    -11       N  
ATOM    133  CA  GLU A  45     -10.156  54.717  22.965  1.00 11.87           C  
ANISOU  133  CA  GLU A  45     1635   1414   1459      5    279    -13       C  
ATOM    134  C   GLU A  45      -9.521  53.387  22.573  1.00 12.55           C  
ANISOU  134  C   GLU A  45     1700   1508   1559     -3    265    -14       C  
ATOM    135  O   GLU A  45      -9.589  52.978  21.414  1.00 12.84           O  
ANISOU  135  O   GLU A  45     1745   1538   1595      3    263    -10       O  
ATOM    136  CB  GLU A  45      -9.214  55.902  22.722  1.00 13.32           C  
ANISOU  136  CB  GLU A  45     1845   1575   1639     -7    309    -27       C  
ATOM    137  CG  GLU A  45      -9.971  57.210  22.869  1.00 11.98           C  
ANISOU  137  CG  GLU A  45     1704   1392   1453      6    325    -24       C  
ATOM    138  CD  GLU A  45      -9.129  58.474  22.894  1.00 15.76           C  
ANISOU  138  CD  GLU A  45     2209   1847   1929     -9    359    -40       C  
ATOM    139  OE1 GLU A  45      -8.049  58.533  22.273  1.00 13.79           O  
ANISOU  139  OE1 GLU A  45     1968   1584   1686    -26    375    -52       O  
ATOM    140  OE2 GLU A  45      -9.608  59.439  23.519  1.00 17.16           O  
ANISOU  140  OE2 GLU A  45     2402   2019   2098     -4    370    -41       O  
ATOM    141  N   CYS A  46      -8.925  52.687  23.537  1.00 10.74           N  
ANISOU  141  N   CYS A  46     1443   1295   1341    -17    256    -17       N  
ATOM    142  CA  CYS A  46      -8.404  51.341  23.277  1.00 11.17           C  
ANISOU  142  CA  CYS A  46     1477   1357   1407    -22    243    -16       C  
ATOM    143  C   CYS A  46      -9.490  50.305  22.976  1.00 10.60           C  
ANISOU  143  C   CYS A  46     1395   1292   1338     -8    224     -1       C  
ATOM    144  O   CYS A  46      -9.237  49.278  22.340  1.00  9.36           O  
ANISOU  144  O   CYS A  46     1230   1135   1189    -10    216      0       O  
ATOM    145  CB  CYS A  46      -7.551  50.867  24.463  1.00 11.88           C  
ANISOU  145  CB  CYS A  46     1541   1465   1505    -34    238    -22       C  
ATOM    146  SG  CYS A  46      -6.135  51.935  24.841  1.00 12.08           S  
ANISOU  146  SG  CYS A  46     1570   1489   1528    -55    261    -46       S  
ATOM    147  N   GLN A  47     -10.690  50.570  23.480  1.00 10.49           N  
ANISOU  147  N   GLN A  47     1380   1286   1317      3    217      6       N  
ATOM    148  CA  GLN A  47     -11.831  49.675  23.354  1.00 10.70           C  
ANISOU  148  CA  GLN A  47     1395   1323   1346     13    201     16       C  
ATOM    149  C   GLN A  47     -12.700  49.996  22.137  1.00 11.77           C  
ANISOU  149  C   GLN A  47     1547   1453   1471     29    200     17       C  
ATOM    150  O   GLN A  47     -13.629  49.254  21.859  1.00 11.55           O  
ANISOU  150  O   GLN A  47     1507   1435   1443     37    188     21       O  
ATOM    151  CB  GLN A  47     -12.710  49.782  24.606  1.00  9.62           C  
ANISOU  151  CB  GLN A  47     1246   1201   1207     18    194     23       C  
ATOM    152  CG  GLN A  47     -12.003  49.410  25.894  1.00 12.87           C  
ANISOU  152  CG  GLN A  47     1639   1623   1626      7    192     23       C  
ATOM    153  CD  GLN A  47     -11.539  47.959  25.896  1.00 15.80           C  
ANISOU  153  CD  GLN A  47     1992   1998   2011      1    184     27       C  
ATOM    154  OE1 GLN A  47     -10.404  47.680  25.533  1.00 13.45           O  
ANISOU  154  OE1 GLN A  47     1695   1695   1719     -6    188     20       O  
ATOM    155  NE2 GLN A  47     -12.409  47.037  26.303  1.00 14.26           N  
ANISOU  155  NE2 GLN A  47     1784   1812   1822      4    174     37       N  
ATOM    156  N   GLN A  48     -12.420  51.076  21.412  1.00 10.76           N  
ANISOU  156  N   GLN A  48     1445   1310   1331     36    215     13       N  
ATOM    157  CA  GLN A  48     -13.290  51.485  20.306  1.00 12.57           C  
ANISOU  157  CA  GLN A  48     1692   1536   1544     57    216     15       C  
ATOM    158  C   GLN A  48     -13.323  50.510  19.126  1.00 13.54           C  
ANISOU  158  C   GLN A  48     1810   1662   1672     60    207     14       C  
ATOM    159  O   GLN A  48     -12.263  50.058  18.674  1.00 11.93           O  
ANISOU  159  O   GLN A  48     1605   1447   1477     47    211      9       O  
ATOM    160  CB  GLN A  48     -12.867  52.863  19.794  1.00 13.39           C  
ANISOU  160  CB  GLN A  48     1831   1620   1634     64    239     13       C  
ATOM    161  CG  GLN A  48     -13.282  53.985  20.739  1.00 12.85           C  
ANISOU  161  CG  GLN A  48     1774   1551   1556     70    248     14       C  
ATOM    162  CD  GLN A  48     -12.850  55.335  20.220  1.00 13.48           C  
ANISOU  162  CD  GLN A  48     1892   1606   1623     76    275     11       C  
ATOM    163  OE1 GLN A  48     -11.970  55.423  19.364  1.00 13.75           O  
ANISOU  163  OE1 GLN A  48     1941   1624   1659     69    289      6       O  
ATOM    164  NE2 GLN A  48     -13.455  56.393  20.741  1.00 15.83           N  
ANISOU  164  NE2 GLN A  48     2205   1900   1907     88    285     14       N  
ATOM    165  N   ALA A  49     -14.528  50.191  18.643  1.00 11.92           N  
ANISOU  165  N   ALA A  49     1599   1471   1459     77    194     16       N  
ATOM    166  CA  ALA A  49     -14.649  49.343  17.455  1.00 13.43           C  
ANISOU  166  CA  ALA A  49     1785   1666   1651     82    186     11       C  
ATOM    167  C   ALA A  49     -14.665  50.245  16.228  1.00 13.52           C  
ANISOU  167  C   ALA A  49     1826   1669   1643    103    197     10       C  
ATOM    168  O   ALA A  49     -14.887  51.444  16.357  1.00 14.05           O  
ANISOU  168  O   ALA A  49     1915   1729   1694    118    210     14       O  
ATOM    169  CB  ALA A  49     -15.922  48.477  17.511  1.00 10.61           C  
ANISOU  169  CB  ALA A  49     1403   1332   1295     87    168      9       C  
ATOM    170  N   GLY A  50     -14.419  49.703  15.039  1.00 14.49           N  
ANISOU  170  N   GLY A  50     1950   1789   1765    107    195      5       N  
ATOM    171  CA  GLY A  50     -14.355  50.558  13.845  1.00 15.16           C  
ANISOU  171  CA  GLY A  50     2065   1865   1829    130    208      5       C  
ATOM    172  C   GLY A  50     -15.702  51.079  13.376  1.00 15.84           C  
ANISOU  172  C   GLY A  50     2158   1970   1890    164    202      6       C  
ATOM    173  O   GLY A  50     -16.716  50.431  13.618  1.00 17.26           O  
ANISOU  173  O   GLY A  50     2312   2174   2070    168    184      2       O  
ATOM    174  N   PRO A  51     -15.730  52.211  12.649  1.00 17.20           N  
ANISOU  174  N   PRO A  51     2365   2131   2038    190    219     11       N  
ATOM    175  CA  PRO A  51     -14.541  52.942  12.239  1.00 16.10           C  
ANISOU  175  CA  PRO A  51     2258   1961   1899    184    243     14       C  
ATOM    176  C   PRO A  51     -14.081  53.857  13.369  1.00 15.78           C  
ANISOU  176  C   PRO A  51     2230   1902   1863    169    261     18       C  
ATOM    177  O   PRO A  51     -14.909  54.458  14.047  1.00 15.14           O  
ANISOU  177  O   PRO A  51     2151   1829   1771    183    260     22       O  
ATOM    178  CB  PRO A  51     -15.017  53.775  11.040  1.00 17.91           C  
ANISOU  178  CB  PRO A  51     2518   2188   2096    224    255     18       C  
ATOM    179  CG  PRO A  51     -16.502  53.958  11.243  1.00 16.46           C  
ANISOU  179  CG  PRO A  51     2325   2033   1893    253    240     20       C  
ATOM    180  CD  PRO A  51     -16.971  52.814  12.116  1.00 19.35           C  
ANISOU  180  CD  PRO A  51     2647   2422   2280    230    215     13       C  
ATOM    181  N   LEU A  52     -12.774  53.935  13.589  1.00 15.60           N  
ANISOU  181  N   LEU A  52     2213   1857   1856    142    276     14       N  
ATOM    182  CA  LEU A  52     -12.252  54.802  14.645  1.00 15.32           C  
ANISOU  182  CA  LEU A  52     2188   1806   1825    125    293     14       C  
ATOM    183  C   LEU A  52     -12.366  56.288  14.280  1.00 15.00           C  
ANISOU  183  C   LEU A  52     2192   1743   1762    146    322     19       C  
ATOM    184  O   LEU A  52     -12.137  56.669  13.145  1.00 15.54           O  
ANISOU  184  O   LEU A  52     2287   1797   1817    161    338     21       O  
ATOM    185  CB  LEU A  52     -10.801  54.440  14.947  1.00 14.80           C  
ANISOU  185  CB  LEU A  52     2113   1728   1782     90    302      5       C  
ATOM    186  CG  LEU A  52     -10.531  52.989  15.356  1.00 13.44           C  
ANISOU  186  CG  LEU A  52     1900   1574   1631     71    277      1       C  
ATOM    187  CD1 LEU A  52      -9.075  52.886  15.747  1.00 16.38           C  
ANISOU  187  CD1 LEU A  52     2267   1935   2019     41    289     -8       C  
ATOM    188  CD2 LEU A  52     -11.420  52.568  16.522  1.00 13.78           C  
ANISOU  188  CD2 LEU A  52     1917   1638   1679     71    258      5       C  
ATOM    189  N   PRO A  53     -12.711  57.149  15.242  1.00 14.87           N  
ANISOU  189  N   PRO A  53     2184   1722   1741    147    331     21       N  
ATOM    190  CA  PRO A  53     -12.751  58.580  14.950  1.00 14.46           C  
ANISOU  190  CA  PRO A  53     2178   1645   1669    165    363     25       C  
ATOM    191  C   PRO A  53     -11.329  59.136  14.726  1.00 16.35           C  
ANISOU  191  C   PRO A  53     2441   1851   1918    139    395     16       C  
ATOM    192  O   PRO A  53     -10.339  58.527  15.141  1.00 12.86           O  
ANISOU  192  O   PRO A  53     1975   1412   1499    104    392      5       O  
ATOM    193  CB  PRO A  53     -13.352  59.150  16.235  1.00 16.52           C  
ANISOU  193  CB  PRO A  53     2435   1912   1929    165    361     26       C  
ATOM    194  CG  PRO A  53     -12.812  58.222  17.305  1.00 12.93           C  
ANISOU  194  CG  PRO A  53     1938   1472   1501    129    343     18       C  
ATOM    195  CD  PRO A  53     -12.881  56.859  16.673  1.00 13.70           C  
ANISOU  195  CD  PRO A  53     2007   1589   1608    128    317     18       C  
ATOM    196  N   GLU A  54     -11.224  60.279  14.058  1.00 15.80           N  
ANISOU  196  N   GLU A  54     2419   1754   1830    155    429     21       N  
ATOM    197  CA  GLU A  54      -9.937  60.914  13.795  1.00 17.12           C  
ANISOU  197  CA  GLU A  54     2612   1888   2005    130    465     11       C  
ATOM    198  C   GLU A  54      -9.160  61.199  15.085  1.00 16.40           C  
ANISOU  198  C   GLU A  54     2505   1791   1934     90    475     -4       C  
ATOM    199  O   GLU A  54      -7.922  61.158  15.081  1.00 16.19           O  
ANISOU  199  O   GLU A  54     2475   1752   1922     56    491    -19       O  
ATOM    200  CB  GLU A  54     -10.168  62.226  13.030  1.00 18.77           C  
ANISOU  200  CB  GLU A  54     2878   2064   2188    159    503     20       C  
ATOM    201  CG  GLU A  54      -8.902  62.995  12.692  1.00 21.14           C  
ANISOU  201  CG  GLU A  54     3211   2326   2494    132    547     10       C  
ATOM    202  CD  GLU A  54      -8.273  63.734  13.869  1.00 28.42           C  
ANISOU  202  CD  GLU A  54     4135   3232   3431     96    570     -5       C  
ATOM    203  OE1 GLU A  54      -8.990  64.218  14.779  1.00 27.63           O  
ANISOU  203  OE1 GLU A  54     4035   3137   3326    105    566     -3       O  
ATOM    204  OE2 GLU A  54      -7.024  63.799  13.877  1.00 28.37           O  
ANISOU  204  OE2 GLU A  54     4126   3210   3440     58    591    -23       O  
ATOM    205  N   TRP A  55      -9.886  61.454  16.173  1.00 14.30           N  
ANISOU  205  N   TRP A  55     2228   1537   1666     94    464     -2       N  
ATOM    206  CA  TRP A  55      -9.252  61.813  17.445  1.00 13.73           C  
ANISOU  206  CA  TRP A  55     2143   1463   1609     60    473    -18       C  
ATOM    207  C   TRP A  55      -8.769  60.627  18.298  1.00 14.22           C  
ANISOU  207  C   TRP A  55     2151   1555   1694     33    443    -27       C  
ATOM    208  O   TRP A  55      -8.166  60.824  19.350  1.00 13.87           O  
ANISOU  208  O   TRP A  55     2092   1515   1662      5    448    -42       O  
ATOM    209  CB  TRP A  55     -10.175  62.753  18.243  1.00 14.20           C  
ANISOU  209  CB  TRP A  55     2219   1519   1655     77    480    -12       C  
ATOM    210  CG  TRP A  55     -11.616  62.267  18.377  1.00 14.86           C  
ANISOU  210  CG  TRP A  55     2287   1632   1727    112    447      3       C  
ATOM    211  CD1 TRP A  55     -12.677  62.623  17.576  1.00 16.12           C  
ANISOU  211  CD1 TRP A  55     2473   1791   1862    155    447     19       C  
ATOM    212  CD2 TRP A  55     -12.129  61.303  19.309  1.00 15.13           C  
ANISOU  212  CD2 TRP A  55     2275   1701   1772    106    410      4       C  
ATOM    213  NE1 TRP A  55     -13.826  61.988  17.995  1.00 17.16           N  
ANISOU  213  NE1 TRP A  55     2575   1956   1988    175    412     28       N  
ATOM    214  CE2 TRP A  55     -13.518  61.175  19.058  1.00 13.65           C  
ANISOU  214  CE2 TRP A  55     2087   1532   1567    144    390     19       C  
ATOM    215  CE3 TRP A  55     -11.560  60.557  20.355  1.00 16.55           C  
ANISOU  215  CE3 TRP A  55     2414   1899   1974     75    393     -5       C  
ATOM    216  CZ2 TRP A  55     -14.341  60.325  19.803  1.00 10.28           C  
ANISOU  216  CZ2 TRP A  55     1621   1138   1145    147    357     23       C  
ATOM    217  CZ3 TRP A  55     -12.396  59.722  21.119  1.00 14.98           C  
ANISOU  217  CZ3 TRP A  55     2179   1732   1779     81    360      0       C  
ATOM    218  CH2 TRP A  55     -13.766  59.607  20.832  1.00 11.37           C  
ANISOU  218  CH2 TRP A  55     1722   1289   1305    115    343     14       C  
ATOM    219  N   ASN A  56      -9.021  59.393  17.868  1.00 13.09           N  
ANISOU  219  N   ASN A  56     1981   1434   1556     41    412    -20       N  
ATOM    220  CA  ASN A  56      -8.474  58.220  18.555  1.00 12.46           C  
ANISOU  220  CA  ASN A  56     1856   1379   1497     17    387    -28       C  
ATOM    221  C   ASN A  56      -6.940  58.326  18.624  1.00 12.70           C  
ANISOU  221  C   ASN A  56     1883   1399   1541    -17    407    -47       C  
ATOM    222  O   ASN A  56      -6.273  58.478  17.597  1.00 12.78           O  
ANISOU  222  O   ASN A  56     1913   1391   1550    -21    425    -51       O  
ATOM    223  CB  ASN A  56      -8.897  56.925  17.838  1.00 12.56           C  
ANISOU  223  CB  ASN A  56     1848   1409   1512     30    358    -18       C  
ATOM    224  CG  ASN A  56      -8.367  55.676  18.521  1.00 12.42           C  
ANISOU  224  CG  ASN A  56     1789   1414   1515     10    335    -23       C  
ATOM    225  OD1 ASN A  56      -9.095  54.973  19.235  1.00 17.15           O  
ANISOU  225  OD1 ASN A  56     2362   2035   2118     15    310    -16       O  
ATOM    226  ND2 ASN A  56      -7.090  55.406  18.321  1.00  8.59           N  
ANISOU  226  ND2 ASN A  56     1297    925   1041    -12    344    -35       N  
ATOM    227  N   ARG A  57      -6.385  58.197  19.830  1.00 11.45           N  
ANISOU  227  N   ARG A  57     1698   1256   1395    -40    402    -61       N  
ATOM    228  CA  ARG A  57      -4.956  58.422  20.069  1.00 12.62           C  
ANISOU  228  CA  ARG A  57     1839   1401   1555    -73    422    -84       C  
ATOM    229  C   ARG A  57      -4.131  57.150  20.257  1.00 14.20           C  
ANISOU  229  C   ARG A  57     2000   1625   1769    -88    400    -91       C  
ATOM    230  O   ARG A  57      -2.970  57.212  20.696  1.00 13.69           O  
ANISOU  230  O   ARG A  57     1919   1568   1713   -114    411   -113       O  
ATOM    231  CB  ARG A  57      -4.814  59.265  21.337  1.00 13.05           C  
ANISOU  231  CB  ARG A  57     1890   1458   1610    -89    434    -99       C  
ATOM    232  CG  ARG A  57      -5.366  60.684  21.219  1.00 12.51           C  
ANISOU  232  CG  ARG A  57     1864   1360   1527    -80    464    -97       C  
ATOM    233  CD  ARG A  57      -5.434  61.292  22.630  1.00 15.48           C  
ANISOU  233  CD  ARG A  57     2230   1746   1906    -93    468   -110       C  
ATOM    234  NE  ARG A  57      -6.490  60.659  23.427  1.00 10.72           N  
ANISOU  234  NE  ARG A  57     1603   1170   1301    -73    434    -93       N  
ATOM    235  CZ  ARG A  57      -6.686  60.872  24.727  1.00 15.42           C  
ANISOU  235  CZ  ARG A  57     2180   1782   1897    -79    427   -100       C  
ATOM    236  NH1 ARG A  57      -5.850  61.665  25.394  1.00 14.23           N  
ANISOU  236  NH1 ARG A  57     2029   1627   1750   -105    450   -126       N  
ATOM    237  NH2 ARG A  57      -7.703  60.297  25.367  1.00 13.24           N  
ANISOU  237  NH2 ARG A  57     1884   1528   1618    -59    398    -84       N  
ATOM    238  N   VAL A  58      -4.714  56.005  19.897  1.00 13.09           N  
ANISOU  238  N   VAL A  58     1844   1499   1631    -70    371    -74       N  
ATOM    239  CA  VAL A  58      -4.086  54.712  20.142  1.00 12.62           C  
ANISOU  239  CA  VAL A  58     1748   1462   1584    -79    350    -78       C  
ATOM    240  C   VAL A  58      -3.409  54.185  18.872  1.00 13.50           C  
ANISOU  240  C   VAL A  58     1865   1564   1698    -81    353    -79       C  
ATOM    241  O   VAL A  58      -4.077  53.698  17.958  1.00 11.24           O  
ANISOU  241  O   VAL A  58     1588   1272   1408    -62    343    -64       O  
ATOM    242  CB  VAL A  58      -5.105  53.695  20.692  1.00 11.85           C  
ANISOU  242  CB  VAL A  58     1628   1385   1489    -61    318    -60       C  
ATOM    243  CG1 VAL A  58      -4.388  52.463  21.251  1.00 11.18           C  
ANISOU  243  CG1 VAL A  58     1507   1323   1415    -70    299    -64       C  
ATOM    244  CG2 VAL A  58      -5.930  54.330  21.830  1.00 11.52           C  
ANISOU  244  CG2 VAL A  58     1584   1349   1440    -56    315    -57       C  
ATOM    245  N   GLU A  59      -2.081  54.276  18.807  1.00 13.00           N  
ANISOU  245  N   GLU A  59     1796   1501   1642   -104    369    -99       N  
ATOM    246  CA  GLU A  59      -1.362  53.889  17.579  1.00 14.45           C  
ANISOU  246  CA  GLU A  59     1986   1674   1827   -108    376   -102       C  
ATOM    247  C   GLU A  59      -1.548  52.420  17.206  1.00 13.74           C  
ANISOU  247  C   GLU A  59     1876   1600   1745    -95    346    -89       C  
ATOM    248  O   GLU A  59      -1.403  52.065  16.036  1.00 15.39           O  
ANISOU  248  O   GLU A  59     2095   1799   1953    -89    348    -85       O  
ATOM    249  CB  GLU A  59       0.144  54.168  17.701  1.00 14.69           C  
ANISOU  249  CB  GLU A  59     2007   1708   1864   -137    396   -128       C  
ATOM    250  CG  GLU A  59       0.840  53.364  18.794  1.00 17.58           C  
ANISOU  250  CG  GLU A  59     2331   2108   2239   -147    378   -140       C  
ATOM    251  CD  GLU A  59       2.337  53.642  18.838  1.00 23.84           C  
ANISOU  251  CD  GLU A  59     3111   2908   3035   -175    397   -170       C  
ATOM    252  OE1 GLU A  59       2.968  53.637  17.766  1.00 27.57           O  
ANISOU  252  OE1 GLU A  59     3596   3368   3509   -182    412   -175       O  
ATOM    253  OE2 GLU A  59       2.887  53.894  19.928  1.00 21.48           O  
ANISOU  253  OE2 GLU A  59     2791   2632   2738   -190    400   -189       O  
ATOM    254  N   TRP A  60      -1.855  51.573  18.187  1.00 10.67           N  
ANISOU  254  N   TRP A  60     1458   1234   1362    -91    322    -84       N  
ATOM    255  CA  TRP A  60      -1.993  50.144  17.937  1.00 11.66           C  
ANISOU  255  CA  TRP A  60     1563   1371   1494    -81    298    -73       C  
ATOM    256  C   TRP A  60      -3.453  49.716  17.748  1.00 12.82           C  
ANISOU  256  C   TRP A  60     1714   1516   1638    -59    280    -53       C  
ATOM    257  O   TRP A  60      -3.759  48.514  17.717  1.00 11.99           O  
ANISOU  257  O   TRP A  60     1593   1421   1540    -52    260    -45       O  
ATOM    258  CB  TRP A  60      -1.319  49.338  19.062  1.00 11.57           C  
ANISOU  258  CB  TRP A  60     1519   1385   1490    -88    285    -79       C  
ATOM    259  CG  TRP A  60      -1.672  49.777  20.466  1.00 11.11           C  
ANISOU  259  CG  TRP A  60     1449   1341   1430    -89    282    -80       C  
ATOM    260  CD1 TRP A  60      -1.077  50.770  21.199  1.00 12.82           C  
ANISOU  260  CD1 TRP A  60     1664   1563   1643   -105    298    -98       C  
ATOM    261  CD2 TRP A  60      -2.708  49.233  21.297  1.00 10.69           C  
ANISOU  261  CD2 TRP A  60     1384   1299   1377    -75    263    -64       C  
ATOM    262  NE1 TRP A  60      -1.676  50.873  22.436  1.00 12.03           N  
ANISOU  262  NE1 TRP A  60     1552   1477   1540    -99    289    -94       N  
ATOM    263  CE2 TRP A  60      -2.678  49.940  22.522  1.00 10.46           C  
ANISOU  263  CE2 TRP A  60     1347   1281   1343    -81    267    -72       C  
ATOM    264  CE3 TRP A  60      -3.656  48.214  21.129  1.00 10.04           C  
ANISOU  264  CE3 TRP A  60     1298   1218   1299    -60    244    -46       C  
ATOM    265  CZ2 TRP A  60      -3.575  49.674  23.564  1.00 11.82           C  
ANISOU  265  CZ2 TRP A  60     1507   1466   1514    -70    253    -60       C  
ATOM    266  CZ3 TRP A  60      -4.564  47.956  22.163  1.00 11.95           C  
ANISOU  266  CZ3 TRP A  60     1528   1471   1540    -51    232    -35       C  
ATOM    267  CH2 TRP A  60      -4.507  48.687  23.371  1.00 13.47           C  
ANISOU  267  CH2 TRP A  60     1714   1675   1728    -56    236    -40       C  
ATOM    268  N   ARG A  61      -4.354  50.687  17.606  1.00 11.20           N  
ANISOU  268  N   ARG A  61     1532   1300   1422    -49    288    -48       N  
ATOM    269  CA  ARG A  61      -5.732  50.362  17.218  1.00 12.76           C  
ANISOU  269  CA  ARG A  61     1734   1499   1614    -27    273    -32       C  
ATOM    270  C   ARG A  61      -6.051  50.906  15.824  1.00 13.83           C  
ANISOU  270  C   ARG A  61     1900   1618   1737    -13    285    -29       C  
ATOM    271  O   ARG A  61      -5.753  52.066  15.539  1.00 13.01           O  
ANISOU  271  O   ARG A  61     1821   1496   1623    -15    308    -34       O  
ATOM    272  CB  ARG A  61      -6.750  50.880  18.252  1.00 11.84           C  
ANISOU  272  CB  ARG A  61     1616   1390   1492    -20    268    -26       C  
ATOM    273  CG  ARG A  61      -6.720  50.136  19.604  1.00 12.58           C  
ANISOU  273  CG  ARG A  61     1680   1504   1596    -27    253    -24       C  
ATOM    274  CD  ARG A  61      -6.980  48.627  19.422  1.00 12.86           C  
ANISOU  274  CD  ARG A  61     1694   1550   1641    -23    232    -17       C  
ATOM    275  NE  ARG A  61      -7.931  48.484  18.324  1.00 15.58           N  
ANISOU  275  NE  ARG A  61     2051   1889   1980     -8    227    -10       N  
ATOM    276  CZ  ARG A  61      -9.227  48.771  18.377  1.00 14.37           C  
ANISOU  276  CZ  ARG A  61     1902   1740   1818      6    220     -3       C  
ATOM    277  NH1 ARG A  61      -9.789  49.140  19.521  1.00 11.14           N  
ANISOU  277  NH1 ARG A  61     1486   1340   1406      7    218      0       N  
ATOM    278  NH2 ARG A  61      -9.968  48.676  17.269  1.00  9.37           N  
ANISOU  278  NH2 ARG A  61     1278   1106   1177     22    216     -1       N  
ATOM    279  N   GLY A  62      -6.671  50.083  14.978  1.00 12.71           N  
ANISOU  279  N   GLY A  62     1754   1480   1595      0    269    -23       N  
ATOM    280  CA  GLY A  62      -7.126  50.519  13.658  1.00 14.64           C  
ANISOU  280  CA  GLY A  62     2024   1713   1824     20    277    -19       C  
ATOM    281  C   GLY A  62      -8.605  50.189  13.517  1.00 15.39           C  
ANISOU  281  C   GLY A  62     2113   1823   1910     42    258    -10       C  
ATOM    282  O   GLY A  62      -9.226  49.688  14.460  1.00 14.97           O  
ANISOU  282  O   GLY A  62     2038   1785   1864     40    242     -7       O  
ATOM    283  N   ASP A  63      -9.172  50.453  12.345  1.00 15.71           N  
ANISOU  283  N   ASP A  63     2172   1861   1934     65    260     -8       N  
ATOM    284  CA  ASP A  63     -10.589  50.179  12.114  1.00 18.11           C  
ANISOU  284  CA  ASP A  63     2468   2183   2227     88    243     -3       C  
ATOM    285  C   ASP A  63     -10.773  48.666  12.184  1.00 17.92           C  
ANISOU  285  C   ASP A  63     2412   2176   2221     78    220     -7       C  
ATOM    286  O   ASP A  63     -10.132  47.923  11.449  1.00 22.63           O  
ANISOU  286  O   ASP A  63     3003   2768   2825     71    218    -12       O  
ATOM    287  CB  ASP A  63     -11.013  50.686  10.734  1.00 18.62           C  
ANISOU  287  CB  ASP A  63     2558   2246   2270    117    250     -2       C  
ATOM    288  CG  ASP A  63     -11.054  52.190  10.643  1.00 20.42           C  
ANISOU  288  CG  ASP A  63     2823   2456   2477    134    274      3       C  
ATOM    289  OD1 ASP A  63     -11.007  52.896  11.674  1.00 17.95           O  
ANISOU  289  OD1 ASP A  63     2515   2136   2166    125    284      5       O  
ATOM    290  OD2 ASP A  63     -11.146  52.675   9.501  1.00 27.53           O  
ANISOU  290  OD2 ASP A  63     3750   3350   3359    157    286      6       O  
ATOM    291  N   ALA A  64     -11.599  48.178  13.093  1.00 17.25           N  
ANISOU  291  N   ALA A  64     2304   2107   2142     75    205     -6       N  
ATOM    292  CA  ALA A  64     -11.800  46.735  13.215  1.00 15.34           C  
ANISOU  292  CA  ALA A  64     2033   1876   1917     63    188     -9       C  
ATOM    293  C   ALA A  64     -13.290  46.469  13.164  1.00 14.41           C  
ANISOU  293  C   ALA A  64     1902   1780   1790     78    174    -11       C  
ATOM    294  O   ALA A  64     -14.085  47.382  13.392  1.00 13.97           O  
ANISOU  294  O   ALA A  64     1855   1732   1719     95    175     -8       O  
ATOM    295  CB  ALA A  64     -11.231  46.228  14.537  1.00 12.74           C  
ANISOU  295  CB  ALA A  64     1687   1546   1607     41    186     -6       C  
ATOM    296  N   THR A  65     -13.637  45.208  12.923  1.00 14.81           N  
ANISOU  296  N   THR A  65     1931   1841   1854     70    161    -18       N  
ATOM    297  CA  THR A  65     -15.011  44.702  12.868  1.00 14.62           C  
ANISOU  297  CA  THR A  65     1888   1840   1826     78    147    -25       C  
ATOM    298  C   THR A  65     -15.892  45.585  11.978  1.00 15.69           C  
ANISOU  298  C   THR A  65     2035   1990   1933    108    146    -29       C  
ATOM    299  O   THR A  65     -17.040  45.886  12.290  1.00 13.87           O  
ANISOU  299  O   THR A  65     1796   1780   1691    121    139    -31       O  
ATOM    300  CB  THR A  65     -15.610  44.374  14.268  1.00 15.25           C  
ANISOU  300  CB  THR A  65     1948   1928   1917     65    143    -21       C  
ATOM    301  OG1 THR A  65     -15.627  45.533  15.107  1.00 17.73           O  
ANISOU  301  OG1 THR A  65     2275   2239   2221     72    149    -11       O  
ATOM    302  CG2 THR A  65     -14.791  43.298  14.971  1.00 14.73           C  
ANISOU  302  CG2 THR A  65     1870   1850   1876     40    144    -17       C  
ATOM    303  N   MET A  66     -15.342  45.972  10.831  1.00 16.31           N  
ANISOU  303  N   MET A  66     2134   2061   2001    121    153    -30       N  
ATOM    304  CA  MET A  66     -16.059  46.848   9.901  1.00 16.71           C  
ANISOU  304  CA  MET A  66     2201   2124   2021    156    154    -32       C  
ATOM    305  C   MET A  66     -17.245  46.172   9.229  1.00 17.75           C  
ANISOU  305  C   MET A  66     2310   2288   2144    169    137    -48       C  
ATOM    306  O   MET A  66     -18.100  46.845   8.655  1.00 16.94           O  
ANISOU  306  O   MET A  66     2215   2207   2015    201    135    -51       O  
ATOM    307  CB  MET A  66     -15.123  47.462   8.863  1.00 18.36           C  
ANISOU  307  CB  MET A  66     2440   2314   2219    167    169    -29       C  
ATOM    308  CG  MET A  66     -14.111  48.462   9.446  1.00 19.69           C  
ANISOU  308  CG  MET A  66     2635   2453   2390    159    190    -16       C  
ATOM    309  SD  MET A  66     -14.884  49.904  10.221  1.00 20.05           S  
ANISOU  309  SD  MET A  66     2700   2500   2415    180    199     -6       S  
ATOM    310  CE  MET A  66     -15.791  50.680   8.866  1.00 21.22           C  
ANISOU  310  CE  MET A  66     2872   2663   2525    228    202     -6       C  
ATOM    311  N   ASN A  67     -17.337  44.852   9.342  1.00 16.45           N  
ANISOU  311  N   ASN A  67     2118   2131   2001    146    127    -59       N  
ATOM    312  CA  ASN A  67     -18.515  44.187   8.794  1.00 18.64           C  
ANISOU  312  CA  ASN A  67     2369   2440   2271    154    112    -78       C  
ATOM    313  C   ASN A  67     -19.627  44.004   9.817  1.00 19.15           C  
ANISOU  313  C   ASN A  67     2410   2525   2339    147    105    -83       C  
ATOM    314  O   ASN A  67     -20.627  43.356   9.523  1.00 17.05           O  
ANISOU  314  O   ASN A  67     2118   2288   2071    148     94   -102       O  
ATOM    315  CB  ASN A  67     -18.138  42.863   8.123  1.00 17.83           C  
ANISOU  315  CB  ASN A  67     2250   2335   2187    134    107    -93       C  
ATOM    316  CG  ASN A  67     -17.361  43.068   6.833  1.00 24.68           C  
ANISOU  316  CG  ASN A  67     3138   3194   3044    149    112    -94       C  
ATOM    317  OD1 ASN A  67     -17.645  43.973   6.050  1.00 31.35           O  
ANISOU  317  OD1 ASN A  67     4000   4050   3860    182    113    -93       O  
ATOM    318  ND2 ASN A  67     -16.369  42.224   6.609  1.00 31.22           N  
ANISOU  318  ND2 ASN A  67     3965   4001   3892    127    115    -94       N  
ATOM    319  N   ASP A  68     -19.475  44.589  11.004  1.00 17.87           N  
ANISOU  319  N   ASP A  68     2255   2350   2182    141    111    -67       N  
ATOM    320  CA  ASP A  68     -20.501  44.443  12.033  1.00 17.92           C  
ANISOU  320  CA  ASP A  68     2240   2375   2192    134    105    -69       C  
ATOM    321  C   ASP A  68     -21.829  45.053  11.608  1.00 17.14           C  
ANISOU  321  C   ASP A  68     2134   2312   2063    165     96    -80       C  
ATOM    322  O   ASP A  68     -21.864  46.070  10.905  1.00 15.16           O  
ANISOU  322  O   ASP A  68     1907   2067   1787    198     99    -76       O  
ATOM    323  CB  ASP A  68     -20.047  45.097  13.346  1.00 18.74           C  
ANISOU  323  CB  ASP A  68     2356   2459   2302    126    114    -50       C  
ATOM    324  CG  ASP A  68     -19.134  44.211  14.176  1.00 20.33           C  
ANISOU  324  CG  ASP A  68     2551   2637   2534     93    118    -43       C  
ATOM    325  OD1 ASP A  68     -18.862  43.046  13.803  1.00 19.53           O  
ANISOU  325  OD1 ASP A  68     2437   2532   2450     75    116    -51       O  
ATOM    326  OD2 ASP A  68     -18.723  44.676  15.267  1.00 19.40           O  
ANISOU  326  OD2 ASP A  68     2441   2507   2422     85    125    -29       O  
ATOM    327  N   GLU A  69     -22.925  44.431  12.039  1.00 16.07           N  
ANISOU  327  N   GLU A  69     1968   2204   1933    156     87    -95       N  
ATOM    328  CA  GLU A  69     -24.262  44.998  11.824  1.00 17.14           C  
ANISOU  328  CA  GLU A  69     2091   2379   2040    186     78   -107       C  
ATOM    329  C   GLU A  69     -24.423  46.441  12.307  1.00 16.91           C  
ANISOU  329  C   GLU A  69     2087   2349   1989    214     83    -89       C  
ATOM    330  O   GLU A  69     -25.098  47.242  11.659  1.00 15.54           O  
ANISOU  330  O   GLU A  69     1921   2200   1783    253     79    -93       O  
ATOM    331  CB  GLU A  69     -25.318  44.108  12.477  1.00 18.10           C  
ANISOU  331  CB  GLU A  69     2175   2526   2174    164     71   -124       C  
ATOM    332  CG  GLU A  69     -26.770  44.525  12.225  1.00 20.35           C  
ANISOU  332  CG  GLU A  69     2439   2860   2431    192     60   -143       C  
ATOM    333  CD  GLU A  69     -27.208  44.441  10.771  1.00 24.53           C  
ANISOU  333  CD  GLU A  69     2960   3422   2937    218     50   -165       C  
ATOM    334  OE1 GLU A  69     -26.514  43.818   9.942  1.00 24.21           O  
ANISOU  334  OE1 GLU A  69     2924   3368   2907    208     52   -172       O  
ATOM    335  OE2 GLU A  69     -28.268  45.028  10.465  1.00 27.59           O  
ANISOU  335  OE2 GLU A  69     3337   3850   3293    251     42   -178       O  
ATOM    336  N   VAL A  70     -23.822  46.775  13.447  1.00 16.62           N  
ANISOU  336  N   VAL A  70     2062   2284   1966    198     92    -70       N  
ATOM    337  CA  VAL A  70     -23.818  48.157  13.942  1.00 16.57           C  
ANISOU  337  CA  VAL A  70     2083   2269   1941    221    100    -53       C  
ATOM    338  C   VAL A  70     -22.365  48.517  14.249  1.00 16.43           C  
ANISOU  338  C   VAL A  70     2094   2210   1939    206    115    -35       C  
ATOM    339  O   VAL A  70     -21.666  47.771  14.949  1.00 15.48           O  
ANISOU  339  O   VAL A  70     1964   2070   1846    173    117    -31       O  
ATOM    340  CB  VAL A  70     -24.693  48.336  15.195  1.00 16.72           C  
ANISOU  340  CB  VAL A  70     2086   2305   1961    217     97    -51       C  
ATOM    341  CG1 VAL A  70     -24.816  49.811  15.585  1.00 15.74           C  
ANISOU  341  CG1 VAL A  70     1990   2175   1813    246    105    -36       C  
ATOM    342  CG2 VAL A  70     -26.091  47.779  14.967  1.00 16.73           C  
ANISOU  342  CG2 VAL A  70     2052   2350   1952    225     82    -72       C  
ATOM    343  N   LEU A  71     -21.917  49.637  13.690  1.00 15.56           N  
ANISOU  343  N   LEU A  71     2018   2084   1808    231    127    -25       N  
ATOM    344  CA  LEU A  71     -20.513  50.048  13.743  1.00 15.74           C  
ANISOU  344  CA  LEU A  71     2069   2069   1842    217    144    -13       C  
ATOM    345  C   LEU A  71     -20.251  50.931  14.962  1.00 15.32           C  
ANISOU  345  C   LEU A  71     2031   1999   1791    211    155      0       C  
ATOM    346  O   LEU A  71     -21.190  51.451  15.544  1.00 15.25           O  
ANISOU  346  O   LEU A  71     2018   2007   1769    227    152      1       O  
ATOM    347  CB  LEU A  71     -20.159  50.819  12.470  1.00 15.76           C  
ANISOU  347  CB  LEU A  71     2104   2062   1821    246    155    -11       C  
ATOM    348  CG  LEU A  71     -20.244  49.964  11.206  1.00 18.78           C  
ANISOU  348  CG  LEU A  71     2474   2459   2201    252    145    -24       C  
ATOM    349  CD1 LEU A  71     -20.010  50.857   9.986  1.00 21.09           C  
ANISOU  349  CD1 LEU A  71     2802   2745   2465    287    157    -19       C  
ATOM    350  CD2 LEU A  71     -19.229  48.839  11.300  1.00 19.35           C  
ANISOU  350  CD2 LEU A  71     2532   2513   2305    213    144    -27       C  
ATOM    351  N   GLY A  72     -18.984  51.128  15.327  1.00 16.29           N  
ANISOU  351  N   GLY A  72     2168   2091   1929    190    169      6       N  
ATOM    352  CA  GLY A  72     -18.664  51.926  16.504  1.00 14.16           C  
ANISOU  352  CA  GLY A  72     1910   1807   1663    181    180     15       C  
ATOM    353  C   GLY A  72     -18.970  51.218  17.814  1.00 15.46           C  
ANISOU  353  C   GLY A  72     2043   1982   1846    159    169     15       C  
ATOM    354  O   GLY A  72     -19.116  49.994  17.841  1.00 16.12           O  
ANISOU  354  O   GLY A  72     2100   2078   1946    143    156     10       O  
ATOM    355  N   GLY A  73     -19.095  51.983  18.896  1.00 13.78           N  
ANISOU  355  N   GLY A  73     1836   1767   1630    159    175     22       N  
ATOM    356  CA  GLY A  73     -19.248  51.399  20.230  1.00 14.15           C  
ANISOU  356  CA  GLY A  73     1858   1822   1694    138    167     24       C  
ATOM    357  C   GLY A  73     -17.959  50.785  20.746  1.00 13.12           C  
ANISOU  357  C   GLY A  73     1721   1674   1587    108    171     25       C  
ATOM    358  O   GLY A  73     -16.914  50.863  20.095  1.00 15.62           O  
ANISOU  358  O   GLY A  73     2052   1973   1908    102    180     23       O  
ATOM    359  N   TRP A  74     -18.029  50.185  21.927  1.00 11.91           N  
ANISOU  359  N   TRP A  74     1546   1530   1449     92    165     28       N  
ATOM    360  CA  TRP A  74     -16.861  49.618  22.582  1.00 11.22           C  
ANISOU  360  CA  TRP A  74     1451   1430   1380     69    168     30       C  
ATOM    361  C   TRP A  74     -16.940  48.094  22.616  1.00 12.64           C  
ANISOU  361  C   TRP A  74     1606   1617   1578     55    158     29       C  
ATOM    362  O   TRP A  74     -18.017  47.538  22.828  1.00 11.43           O  
ANISOU  362  O   TRP A  74     1436   1480   1425     57    149     29       O  
ATOM    363  CB  TRP A  74     -16.814  50.091  24.050  1.00 11.03           C  
ANISOU  363  CB  TRP A  74     1422   1411   1358     63    171     35       C  
ATOM    364  CG  TRP A  74     -16.645  51.581  24.231  1.00  8.73           C  
ANISOU  364  CG  TRP A  74     1155   1110   1051     73    184     34       C  
ATOM    365  CD1 TRP A  74     -15.832  52.420  23.515  1.00 13.04           C  
ANISOU  365  CD1 TRP A  74     1727   1636   1591     74    200     29       C  
ATOM    366  CD2 TRP A  74     -17.300  52.392  25.209  1.00 11.91           C  
ANISOU  366  CD2 TRP A  74     1558   1520   1443     81    186     37       C  
ATOM    367  NE1 TRP A  74     -15.951  53.709  23.985  1.00 11.37           N  
ANISOU  367  NE1 TRP A  74     1534   1418   1366     82    213     29       N  
ATOM    368  CE2 TRP A  74     -16.853  53.718  25.020  1.00 12.14           C  
ANISOU  368  CE2 TRP A  74     1616   1533   1461     87    203     34       C  
ATOM    369  CE3 TRP A  74     -18.228  52.125  26.220  1.00 11.85           C  
ANISOU  369  CE3 TRP A  74     1532   1532   1436     84    176     42       C  
ATOM    370  CZ2 TRP A  74     -17.301  54.777  25.813  1.00 11.24           C  
ANISOU  370  CZ2 TRP A  74     1513   1420   1335     96    210     35       C  
ATOM    371  CZ3 TRP A  74     -18.701  53.190  27.007  1.00 13.03           C  
ANISOU  371  CZ3 TRP A  74     1690   1686   1573     94    181     44       C  
ATOM    372  CH2 TRP A  74     -18.217  54.494  26.809  1.00 16.34           C  
ANISOU  372  CH2 TRP A  74     2139   2088   1982    100    198     40       C  
ATOM    373  N   TYR A  75     -15.788  47.445  22.460  1.00 12.51           N  
ANISOU  373  N   TYR A  75     1588   1588   1575     41    161     29       N  
ATOM    374  CA  TYR A  75     -15.609  46.068  22.898  1.00 12.67           C  
ANISOU  374  CA  TYR A  75     1588   1610   1613     26    156     31       C  
ATOM    375  C   TYR A  75     -15.716  46.093  24.415  1.00 12.58           C  
ANISOU  375  C   TYR A  75     1567   1607   1605     22    156     39       C  
ATOM    376  O   TYR A  75     -15.252  47.024  25.081  1.00 11.51           O  
ANISOU  376  O   TYR A  75     1438   1470   1463     24    162     40       O  
ATOM    377  CB  TYR A  75     -14.248  45.537  22.443  1.00 11.46           C  
ANISOU  377  CB  TYR A  75     1439   1443   1470     16    160     29       C  
ATOM    378  CG  TYR A  75     -14.046  45.673  20.951  1.00 14.31           C  
ANISOU  378  CG  TYR A  75     1813   1795   1826     21    162     21       C  
ATOM    379  CD1 TYR A  75     -14.980  45.148  20.056  1.00 13.44           C  
ANISOU  379  CD1 TYR A  75     1698   1692   1715     28    154     16       C  
ATOM    380  CD2 TYR A  75     -12.955  46.377  20.429  1.00 12.26           C  
ANISOU  380  CD2 TYR A  75     1571   1522   1562     20    172     18       C  
ATOM    381  CE1 TYR A  75     -14.801  45.273  18.680  1.00 15.03           C  
ANISOU  381  CE1 TYR A  75     1912   1889   1910     35    155      9       C  
ATOM    382  CE2 TYR A  75     -12.776  46.510  19.050  1.00 12.00           C  
ANISOU  382  CE2 TYR A  75     1552   1481   1523     27    174     12       C  
ATOM    383  CZ  TYR A  75     -13.702  45.953  18.189  1.00 15.33           C  
ANISOU  383  CZ  TYR A  75     1969   1912   1944     36    165      8       C  
ATOM    384  OH  TYR A  75     -13.560  46.092  16.822  1.00 14.62           O  
ANISOU  384  OH  TYR A  75     1892   1816   1845     45    167      2       O  
ATOM    385  N   ASP A  76     -16.357  45.069  24.963  1.00 12.64           N  
ANISOU  385  N   ASP A  76     1556   1623   1622     17    151     44       N  
ATOM    386  CA  ASP A  76     -16.679  45.113  26.376  1.00 13.88           C  
ANISOU  386  CA  ASP A  76     1703   1789   1779     16    151     52       C  
ATOM    387  C   ASP A  76     -15.470  45.061  27.302  1.00 13.88           C  
ANISOU  387  C   ASP A  76     1702   1785   1783     11    156     58       C  
ATOM    388  O   ASP A  76     -15.348  45.891  28.200  1.00 12.96           O  
ANISOU  388  O   ASP A  76     1587   1676   1659     15    158     59       O  
ATOM    389  CB  ASP A  76     -17.602  43.958  26.764  1.00 14.18           C  
ANISOU  389  CB  ASP A  76     1723   1834   1827     10    149     56       C  
ATOM    390  CG  ASP A  76     -18.021  44.057  28.210  1.00 17.26           C  
ANISOU  390  CG  ASP A  76     2104   2235   2216     11    150     66       C  
ATOM    391  OD1 ASP A  76     -18.670  45.067  28.559  1.00 15.46           O  
ANISOU  391  OD1 ASP A  76     1879   2018   1975     20    148     65       O  
ATOM    392  OD2 ASP A  76     -17.643  43.164  28.993  1.00 15.37           O  
ANISOU  392  OD2 ASP A  76     1859   1993   1987      5    154     75       O  
ATOM    393  N   ALA A  77     -14.606  44.068  27.105  1.00 12.97           N  
ANISOU  393  N   ALA A  77     1584   1662   1680      4    158     59       N  
ATOM    394  CA  ALA A  77     -13.631  43.746  28.134  1.00 12.42           C  
ANISOU  394  CA  ALA A  77     1509   1596   1614      3    161     65       C  
ATOM    395  C   ALA A  77     -12.326  43.395  27.441  1.00 13.18           C  
ANISOU  395  C   ALA A  77     1609   1682   1714      0    164     59       C  
ATOM    396  O   ALA A  77     -11.819  44.196  26.648  1.00 14.00           O  
ANISOU  396  O   ALA A  77     1725   1780   1814     -2    166     49       O  
ATOM    397  CB  ALA A  77     -14.143  42.617  29.024  1.00 11.35           C  
ANISOU  397  CB  ALA A  77     1361   1464   1486      3    162     77       C  
ATOM    398  N   GLY A  78     -11.784  42.207  27.693  1.00 12.15           N  
ANISOU  398  N   GLY A  78     1473   1549   1594     -1    165     65       N  
ATOM    399  CA  GLY A  78     -10.521  41.855  27.052  1.00 12.22           C  
ANISOU  399  CA  GLY A  78     1485   1551   1606     -3    168     60       C  
ATOM    400  C   GLY A  78     -10.708  41.114  25.729  1.00 14.01           C  
ANISOU  400  C   GLY A  78     1717   1763   1842     -8    167     56       C  
ATOM    401  O   GLY A  78      -9.751  40.570  25.172  1.00 12.72           O  
ANISOU  401  O   GLY A  78     1555   1592   1683     -9    169     53       O  
ATOM    402  N   ALA A  79     -11.934  41.090  25.218  1.00 13.80           N  
ANISOU  402  N   ALA A  79     1691   1734   1817    -10    164     55       N  
ATOM    403  CA  ALA A  79     -12.207  40.473  23.918  1.00 14.85           C  
ANISOU  403  CA  ALA A  79     1828   1857   1957    -14    163     48       C  
ATOM    404  C   ALA A  79     -13.011  41.408  23.022  1.00 15.84           C  
ANISOU  404  C   ALA A  79     1960   1985   2073    -11    158     39       C  
ATOM    405  O   ALA A  79     -12.854  42.625  23.146  1.00 15.33           O  
ANISOU  405  O   ALA A  79     1904   1925   1997     -6    159     37       O  
ATOM    406  CB  ALA A  79     -12.911  39.110  24.090  1.00 16.01           C  
ANISOU  406  CB  ALA A  79     1966   1998   2116    -20    165     53       C  
ATOM    407  N   HIS A  80     -13.850  40.868  22.134  1.00 14.74           N  
ANISOU  407  N   HIS A  80     1817   1844   1936    -13    155     33       N  
ATOM    408  CA  HIS A  80     -14.377  41.674  21.028  1.00 14.32           C  
ANISOU  408  CA  HIS A  80     1772   1795   1872     -6    151     23       C  
ATOM    409  C   HIS A  80     -15.894  41.610  20.828  1.00 13.22           C  
ANISOU  409  C   HIS A  80     1623   1671   1728     -2    145     17       C  
ATOM    410  O   HIS A  80     -16.417  41.943  19.760  1.00 12.25           O  
ANISOU  410  O   HIS A  80     1503   1554   1595      5    141      7       O  
ATOM    411  CB  HIS A  80     -13.603  41.374  19.734  1.00 15.12           C  
ANISOU  411  CB  HIS A  80     1882   1886   1975     -7    152     15       C  
ATOM    412  CG  HIS A  80     -12.125  41.524  19.914  1.00 17.00           C  
ANISOU  412  CG  HIS A  80     2128   2114   2216    -10    158     18       C  
ATOM    413  ND1 HIS A  80     -11.282  40.443  20.050  1.00 14.35           N  
ANISOU  413  ND1 HIS A  80     1788   1770   1893    -17    160     21       N  
ATOM    414  CD2 HIS A  80     -11.366  42.626  20.129  1.00 14.01           C  
ANISOU  414  CD2 HIS A  80     1760   1733   1828     -7    163     18       C  
ATOM    415  CE1 HIS A  80     -10.053  40.876  20.267  1.00 13.14           C  
ANISOU  415  CE1 HIS A  80     1639   1614   1737    -17    165     21       C  
ATOM    416  NE2 HIS A  80     -10.076  42.196  20.324  1.00 14.46           N  
ANISOU  416  NE2 HIS A  80     1815   1784   1892    -13    167     19       N  
ATOM    417  N   VAL A  81     -16.605  41.225  21.882  1.00 11.31           N  
ANISOU  417  N   VAL A  81     1369   1437   1492     -7    146     22       N  
ATOM    418  CA  VAL A  81     -18.059  41.306  21.878  1.00 10.92           C  
ANISOU  418  CA  VAL A  81     1307   1405   1436     -5    141     16       C  
ATOM    419  C   VAL A  81     -18.552  42.711  22.220  1.00 11.94           C  
ANISOU  419  C   VAL A  81     1443   1547   1546     10    138     18       C  
ATOM    420  O   VAL A  81     -17.969  43.363  23.092  1.00 14.26           O  
ANISOU  420  O   VAL A  81     1744   1836   1837     13    141     28       O  
ATOM    421  CB  VAL A  81     -18.665  40.282  22.853  1.00 10.98           C  
ANISOU  421  CB  VAL A  81     1300   1415   1458    -18    146     20       C  
ATOM    422  CG1 VAL A  81     -20.193  40.330  22.757  1.00 10.85           C  
ANISOU  422  CG1 VAL A  81     1267   1419   1434    -17    142      9       C  
ATOM    423  CG2 VAL A  81     -18.162  38.891  22.456  1.00 11.24           C  
ANISOU  423  CG2 VAL A  81     1330   1430   1508    -32    152     18       C  
ATOM    424  N   LYS A  82     -19.589  43.186  21.535  1.00  9.60           N  
ANISOU  424  N   LYS A  82     1144   1267   1236     22    132      8       N  
ATOM    425  CA  LYS A  82     -20.290  44.386  21.971  1.00 11.53           C  
ANISOU  425  CA  LYS A  82     1392   1526   1462     39    129     10       C  
ATOM    426  C   LYS A  82     -21.517  43.916  22.765  1.00 12.60           C  
ANISOU  426  C   LYS A  82     1506   1680   1600     33    126      8       C  
ATOM    427  O   LYS A  82     -22.477  43.385  22.183  1.00 12.00           O  
ANISOU  427  O   LYS A  82     1414   1621   1523     32    122     -5       O  
ATOM    428  CB  LYS A  82     -20.669  45.262  20.759  1.00 10.84           C  
ANISOU  428  CB  LYS A  82     1317   1448   1353     61    125      1       C  
ATOM    429  CG  LYS A  82     -19.477  45.690  19.890  1.00 10.74           C  
ANISOU  429  CG  LYS A  82     1327   1414   1337     66    131      3       C  
ATOM    430  CD  LYS A  82     -19.993  46.509  18.697  1.00 11.76           C  
ANISOU  430  CD  LYS A  82     1470   1554   1443     92    129     -3       C  
ATOM    431  CE  LYS A  82     -18.942  46.635  17.605  1.00 15.69           C  
ANISOU  431  CE  LYS A  82     1988   2034   1940     94    135     -5       C  
ATOM    432  NZ  LYS A  82     -19.429  47.487  16.470  1.00 14.90           N  
ANISOU  432  NZ  LYS A  82     1904   1942   1814    124    135    -10       N  
ATOM    433  N   PHE A  83     -21.448  44.073  24.086  1.00  9.43           N  
ANISOU  433  N   PHE A  83     1102   1277   1202     29    130     20       N  
ATOM    434  CA  PHE A  83     -22.533  43.704  24.997  1.00 11.58           C  
ANISOU  434  CA  PHE A  83     1355   1566   1477     23    130     21       C  
ATOM    435  C   PHE A  83     -23.247  44.981  25.434  1.00 11.22           C  
ANISOU  435  C   PHE A  83     1312   1537   1411     43    125     23       C  
ATOM    436  O   PHE A  83     -22.693  45.743  26.224  1.00 11.05           O  
ANISOU  436  O   PHE A  83     1304   1509   1386     48    129     34       O  
ATOM    437  CB  PHE A  83     -21.972  43.068  26.278  1.00  8.19           C  
ANISOU  437  CB  PHE A  83      923   1125   1064      9    138     35       C  
ATOM    438  CG  PHE A  83     -21.531  41.641  26.142  1.00 10.66           C  
ANISOU  438  CG  PHE A  83     1230   1422   1396     -8    145     35       C  
ATOM    439  CD1 PHE A  83     -22.456  40.630  25.917  1.00 11.01           C  
ANISOU  439  CD1 PHE A  83     1258   1473   1451    -22    148     25       C  
ATOM    440  CD2 PHE A  83     -20.197  41.297  26.350  1.00 11.33           C  
ANISOU  440  CD2 PHE A  83     1326   1487   1491    -12    150     46       C  
ATOM    441  CE1 PHE A  83     -22.049  39.292  25.859  1.00 13.17           C  
ANISOU  441  CE1 PHE A  83     1530   1728   1744    -39    158     26       C  
ATOM    442  CE2 PHE A  83     -19.784  39.965  26.308  1.00 13.07           C  
ANISOU  442  CE2 PHE A  83     1544   1692   1728    -25    158     48       C  
ATOM    443  CZ  PHE A  83     -20.717  38.965  26.047  1.00 13.70           C  
ANISOU  443  CZ  PHE A  83     1611   1774   1819    -39    163     39       C  
ATOM    444  N   ASN A  84     -24.456  45.227  24.943  1.00 10.86           N  
ANISOU  444  N   ASN A  84     1256   1516   1352     54    119     10       N  
ATOM    445  CA  ASN A  84     -25.092  46.518  25.199  1.00 12.37           C  
ANISOU  445  CA  ASN A  84     1455   1723   1521     78    115     12       C  
ATOM    446  C   ASN A  84     -25.400  46.895  26.648  1.00 11.99           C  
ANISOU  446  C   ASN A  84     1402   1680   1472     77    118     23       C  
ATOM    447  O   ASN A  84     -25.429  48.080  26.967  1.00 12.01           O  
ANISOU  447  O   ASN A  84     1420   1685   1459     95    118     29       O  
ATOM    448  CB  ASN A  84     -26.346  46.740  24.350  1.00 10.10           C  
ANISOU  448  CB  ASN A  84     1156   1466   1214     95    107     -4       C  
ATOM    449  CG  ASN A  84     -26.027  47.066  22.908  1.00 12.38           C  
ANISOU  449  CG  ASN A  84     1459   1752   1491    112    104    -12       C  
ATOM    450  OD1 ASN A  84     -25.024  46.600  22.353  1.00 14.63           O  
ANISOU  450  OD1 ASN A  84     1753   2014   1788    100    107    -10       O  
ATOM    451  ND2 ASN A  84     -26.910  47.841  22.275  1.00  9.81           N  
ANISOU  451  ND2 ASN A  84     1135   1452   1140    141     97    -20       N  
ATOM    452  N   LEU A  85     -25.679  45.923  27.508  1.00 11.80           N  
ANISOU  452  N   LEU A  85     1360   1658   1464     57    121     26       N  
ATOM    453  CA  LEU A  85     -26.040  46.256  28.892  1.00 11.74           C  
ANISOU  453  CA  LEU A  85     1346   1658   1454     58    123     37       C  
ATOM    454  C   LEU A  85     -24.876  46.939  29.631  1.00 11.68           C  
ANISOU  454  C   LEU A  85     1359   1632   1447     61    128     51       C  
ATOM    455  O   LEU A  85     -25.018  48.091  30.072  1.00 12.55           O  
ANISOU  455  O   LEU A  85     1478   1748   1542     76    127     55       O  
ATOM    456  CB  LEU A  85     -26.649  45.044  29.631  1.00 10.69           C  
ANISOU  456  CB  LEU A  85     1191   1532   1338     37    129     37       C  
ATOM    457  CG  LEU A  85     -27.113  45.211  31.088  1.00 12.33           C  
ANISOU  457  CG  LEU A  85     1391   1749   1545     37    132     48       C  
ATOM    458  CD1 LEU A  85     -28.105  46.378  31.245  1.00 11.76           C  
ANISOU  458  CD1 LEU A  85     1316   1702   1450     58    125     43       C  
ATOM    459  CD2 LEU A  85     -27.713  43.939  31.665  1.00 15.33           C  
ANISOU  459  CD2 LEU A  85     1751   2132   1940     15    142     47       C  
ATOM    460  N   PRO A  86     -23.706  46.286  29.722  1.00 10.93           N  
ANISOU  460  N   PRO A  86     1269   1516   1367     47    133     58       N  
ATOM    461  CA  PRO A  86     -22.576  47.001  30.335  1.00  9.94           C  
ANISOU  461  CA  PRO A  86     1159   1377   1239     50    137     66       C  
ATOM    462  C   PRO A  86     -22.049  48.152  29.489  1.00 12.05           C  
ANISOU  462  C   PRO A  86     1447   1635   1493     62    137     61       C  
ATOM    463  O   PRO A  86     -21.546  49.110  30.070  1.00 11.91           O  
ANISOU  463  O   PRO A  86     1442   1614   1469     68    142     64       O  
ATOM    464  CB  PRO A  86     -21.500  45.926  30.498  1.00 10.57           C  
ANISOU  464  CB  PRO A  86     1237   1441   1337     34    142     72       C  
ATOM    465  CG  PRO A  86     -21.859  44.853  29.456  1.00 10.55           C  
ANISOU  465  CG  PRO A  86     1227   1436   1346     25    141     64       C  
ATOM    466  CD  PRO A  86     -23.357  44.911  29.304  1.00 10.74           C  
ANISOU  466  CD  PRO A  86     1236   1480   1362     29    137     56       C  
ATOM    467  N   MET A  87     -22.136  48.087  28.156  1.00 12.15           N  
ANISOU  467  N   MET A  87     1467   1645   1504     67    135     52       N  
ATOM    468  CA  MET A  87     -21.721  49.230  27.337  1.00 11.44           C  
ANISOU  468  CA  MET A  87     1401   1546   1399     82    138     48       C  
ATOM    469  C   MET A  87     -22.556  50.458  27.671  1.00 12.12           C  
ANISOU  469  C   MET A  87     1496   1644   1465    102    139     49       C  
ATOM    470  O   MET A  87     -22.016  51.526  27.959  1.00 11.37           O  
ANISOU  470  O   MET A  87     1420   1537   1361    109    147     51       O  
ATOM    471  CB  MET A  87     -21.835  48.962  25.829  1.00 11.09           C  
ANISOU  471  CB  MET A  87     1361   1499   1351     88    136     39       C  
ATOM    472  CG  MET A  87     -20.859  49.809  24.998  1.00 11.03           C  
ANISOU  472  CG  MET A  87     1382   1473   1336     95    144     38       C  
ATOM    473  SD  MET A  87     -21.371  50.009  23.278  1.00 14.95           S  
ANISOU  473  SD  MET A  87     1889   1974   1816    116    141     29       S  
ATOM    474  CE  MET A  87     -21.136  48.314  22.747  1.00 12.54           C  
ANISOU  474  CE  MET A  87     1561   1668   1533     94    134     22       C  
ATOM    475  N   ALA A  88     -23.877  50.312  27.605  1.00 10.89           N  
ANISOU  475  N   ALA A  88     1326   1512   1300    113    131     45       N  
ATOM    476  CA  ALA A  88     -24.772  51.410  27.940  1.00 12.17           C  
ANISOU  476  CA  ALA A  88     1494   1688   1441    135    130     45       C  
ATOM    477  C   ALA A  88     -24.609  51.860  29.394  1.00 11.57           C  
ANISOU  477  C   ALA A  88     1417   1611   1367    130    134     54       C  
ATOM    478  O   ALA A  88     -24.609  53.057  29.665  1.00 12.85           O  
ANISOU  478  O   ALA A  88     1597   1769   1513    145    140     56       O  
ATOM    479  CB  ALA A  88     -26.226  51.042  27.623  1.00 12.10           C  
ANISOU  479  CB  ALA A  88     1464   1710   1423    146    120     37       C  
ATOM    480  N   TYR A  89     -24.449  50.921  30.323  1.00 10.11           N  
ANISOU  480  N   TYR A  89     1212   1428   1199    110    132     59       N  
ATOM    481  CA  TYR A  89     -24.215  51.272  31.730  1.00  9.72           C  
ANISOU  481  CA  TYR A  89     1161   1380   1151    106    136     67       C  
ATOM    482  C   TYR A  89     -22.946  52.126  31.822  1.00 10.99           C  
ANISOU  482  C   TYR A  89     1344   1519   1311    105    145     67       C  
ATOM    483  O   TYR A  89     -22.926  53.133  32.531  1.00 10.95           O  
ANISOU  483  O   TYR A  89     1349   1515   1296    113    150     68       O  
ATOM    484  CB  TYR A  89     -24.015  50.030  32.614  1.00  9.34           C  
ANISOU  484  CB  TYR A  89     1091   1334   1121     87    136     74       C  
ATOM    485  CG  TYR A  89     -23.319  50.336  33.933  1.00 12.25           C  
ANISOU  485  CG  TYR A  89     1461   1701   1493     83    140     82       C  
ATOM    486  CD1 TYR A  89     -24.044  50.767  35.049  1.00  9.77           C  
ANISOU  486  CD1 TYR A  89     1139   1403   1170     90    139     86       C  
ATOM    487  CD2 TYR A  89     -21.930  50.228  34.049  1.00 13.41           C  
ANISOU  487  CD2 TYR A  89     1615   1831   1647     73    145     82       C  
ATOM    488  CE1 TYR A  89     -23.402  51.071  36.250  1.00 12.26           C  
ANISOU  488  CE1 TYR A  89     1454   1718   1485     88    143     92       C  
ATOM    489  CE2 TYR A  89     -21.273  50.515  35.249  1.00 13.42           C  
ANISOU  489  CE2 TYR A  89     1614   1835   1648     71    149     86       C  
ATOM    490  CZ  TYR A  89     -22.015  50.937  36.342  1.00 14.60           C  
ANISOU  490  CZ  TYR A  89     1756   2000   1789     79    147     91       C  
ATOM    491  OH  TYR A  89     -21.356  51.250  37.508  1.00 11.15           O  
ANISOU  491  OH  TYR A  89     1316   1569   1350     78    150     93       O  
ATOM    492  N   SER A  90     -21.879  51.731  31.126  1.00 10.86           N  
ANISOU  492  N   SER A  90     1335   1485   1304     94    149     65       N  
ATOM    493  CA  SER A  90     -20.622  52.482  31.237  1.00  9.79           C  
ANISOU  493  CA  SER A  90     1218   1332   1169     88    159     62       C  
ATOM    494  C   SER A  90     -20.813  53.884  30.672  1.00 10.94           C  
ANISOU  494  C   SER A  90     1390   1469   1297    105    168     57       C  
ATOM    495  O   SER A  90     -20.300  54.851  31.240  1.00 10.50           O  
ANISOU  495  O   SER A  90     1348   1404   1235    105    179     54       O  
ATOM    496  CB  SER A  90     -19.465  51.791  30.503  1.00 10.73           C  
ANISOU  496  CB  SER A  90     1338   1435   1301     74    162     58       C  
ATOM    497  OG  SER A  90     -19.257  50.493  31.028  1.00 12.37           O  
ANISOU  497  OG  SER A  90     1525   1649   1525     61    156     64       O  
ATOM    498  N   ALA A  91     -21.524  53.992  29.552  1.00  9.41           N  
ANISOU  498  N   ALA A  91     1205   1276   1092    121    165     55       N  
ATOM    499  CA  ALA A  91     -21.790  55.308  28.964  1.00 11.05           C  
ANISOU  499  CA  ALA A  91     1442   1475   1279    143    176     53       C  
ATOM    500  C   ALA A  91     -22.657  56.169  29.890  1.00 10.81           C  
ANISOU  500  C   ALA A  91     1414   1458   1235    159    176     56       C  
ATOM    501  O   ALA A  91     -22.392  57.366  30.020  1.00 11.69           O  
ANISOU  501  O   ALA A  91     1552   1554   1335    167    190     55       O  
ATOM    502  CB  ALA A  91     -22.418  55.193  27.560  1.00  9.53           C  
ANISOU  502  CB  ALA A  91     1257   1287   1076    162    171     51       C  
ATOM    503  N   ALA A  92     -23.676  55.585  30.526  1.00 11.45           N  
ANISOU  503  N   ALA A  92     1469   1563   1316    161    163     59       N  
ATOM    504  CA  ALA A  92     -24.487  56.302  31.514  1.00 11.80           C  
ANISOU  504  CA  ALA A  92     1511   1622   1348    174    162     62       C  
ATOM    505  C   ALA A  92     -23.632  56.849  32.669  1.00 11.38           C  
ANISOU  505  C   ALA A  92     1465   1558   1301    161    172     63       C  
ATOM    506  O   ALA A  92     -23.823  57.989  33.092  1.00 11.08           O  
ANISOU  506  O   ALA A  92     1444   1516   1249    174    181     62       O  
ATOM    507  CB  ALA A  92     -25.622  55.409  32.064  1.00 10.09           C  
ANISOU  507  CB  ALA A  92     1263   1436   1135    174    147     65       C  
ATOM    508  N   MET A  93     -22.663  56.064  33.137  1.00 11.54           N  
ANISOU  508  N   MET A  93     1471   1574   1340    137    171     62       N  
ATOM    509  CA  MET A  93     -21.763  56.488  34.225  1.00 11.62           C  
ANISOU  509  CA  MET A  93     1480   1577   1354    123    179     59       C  
ATOM    510  C   MET A  93     -20.802  57.609  33.822  1.00 12.42           C  
ANISOU  510  C   MET A  93     1612   1654   1452    121    197     50       C  
ATOM    511  O   MET A  93     -20.538  58.516  34.616  1.00 11.11           O  
ANISOU  511  O   MET A  93     1455   1484   1280    119    207     44       O  
ATOM    512  CB  MET A  93     -20.980  55.284  34.776  1.00 10.25           C  
ANISOU  512  CB  MET A  93     1284   1410   1201    103    173     62       C  
ATOM    513  CG  MET A  93     -21.886  54.278  35.485  1.00 11.53           C  
ANISOU  513  CG  MET A  93     1419   1593   1367    103    160     72       C  
ATOM    514  SD  MET A  93     -22.938  54.968  36.791  1.00 14.59           S  
ANISOU  514  SD  MET A  93     1799   2001   1741    117    158     76       S  
ATOM    515  CE  MET A  93     -21.701  55.138  38.064  1.00 12.36           C  
ANISOU  515  CE  MET A  93     1511   1718   1464    104    163     72       C  
ATOM    516  N   LEU A  94     -20.283  57.566  32.596  1.00 12.14           N  
ANISOU  516  N   LEU A  94     1592   1601   1418    119    203     46       N  
ATOM    517  CA  LEU A  94     -19.437  58.665  32.100  1.00 12.02           C  
ANISOU  517  CA  LEU A  94     1608   1559   1397    116    224     37       C  
ATOM    518  C   LEU A  94     -20.273  59.936  31.922  1.00 11.90           C  
ANISOU  518  C   LEU A  94     1621   1536   1361    141    236     38       C  
ATOM    519  O   LEU A  94     -19.829  61.052  32.204  1.00 13.04           O  
ANISOU  519  O   LEU A  94     1790   1663   1500    139    255     31       O  
ATOM    520  CB  LEU A  94     -18.760  58.293  30.770  1.00 11.42           C  
ANISOU  520  CB  LEU A  94     1544   1466   1328    111    229     35       C  
ATOM    521  CG  LEU A  94     -17.831  57.079  30.695  1.00 11.40           C  
ANISOU  521  CG  LEU A  94     1518   1466   1344     89    221     33       C  
ATOM    522  CD1 LEU A  94     -17.170  57.088  29.324  1.00 16.00           C  
ANISOU  522  CD1 LEU A  94     2120   2028   1928     86    231     29       C  
ATOM    523  CD2 LEU A  94     -16.753  57.095  31.796  1.00 10.44           C  
ANISOU  523  CD2 LEU A  94     1384   1348   1233     67    226     23       C  
ATOM    524  N   GLY A  95     -21.501  59.767  31.457  1.00 12.47           N  
ANISOU  524  N   GLY A  95     1692   1623   1422    165    224     47       N  
ATOM    525  CA  GLY A  95     -22.478  60.855  31.450  1.00 13.20           C  
ANISOU  525  CA  GLY A  95     1806   1716   1490    195    231     50       C  
ATOM    526  C   GLY A  95     -22.687  61.457  32.827  1.00 14.56           C  
ANISOU  526  C   GLY A  95     1974   1895   1660    193    233     49       C  
ATOM    527  O   GLY A  95     -22.661  62.678  32.989  1.00 15.08           O  
ANISOU  527  O   GLY A  95     2069   1945   1714    203    252     45       O  
ATOM    528  N   TRP A  96     -22.903  60.604  33.823  1.00 13.17           N  
ANISOU  528  N   TRP A  96     1763   1743   1495    180    217     51       N  
ATOM    529  CA  TRP A  96     -23.089  61.052  35.201  1.00 13.22           C  
ANISOU  529  CA  TRP A  96     1761   1761   1500    178    217     50       C  
ATOM    530  C   TRP A  96     -21.860  61.802  35.729  1.00 13.64           C  
ANISOU  530  C   TRP A  96     1829   1794   1559    159    236     37       C  
ATOM    531  O   TRP A  96     -21.985  62.872  36.345  1.00 14.20           O  
ANISOU  531  O   TRP A  96     1915   1858   1619    165    248     32       O  
ATOM    532  CB  TRP A  96     -23.463  59.857  36.087  1.00 12.07           C  
ANISOU  532  CB  TRP A  96     1576   1643   1366    168    197     56       C  
ATOM    533  CG  TRP A  96     -24.026  60.229  37.419  1.00 12.43           C  
ANISOU  533  CG  TRP A  96     1609   1706   1404    173    194     58       C  
ATOM    534  CD1 TRP A  96     -24.322  61.485  37.879  1.00 14.70           C  
ANISOU  534  CD1 TRP A  96     1918   1989   1677    187    205     54       C  
ATOM    535  CD2 TRP A  96     -24.393  59.323  38.461  1.00 12.33           C  
ANISOU  535  CD2 TRP A  96     1564   1718   1400    166    180     64       C  
ATOM    536  NE1 TRP A  96     -24.868  61.411  39.135  1.00 15.74           N  
ANISOU  536  NE1 TRP A  96     2029   2143   1807    189    196     57       N  
ATOM    537  CE2 TRP A  96     -24.889  60.096  39.529  1.00 15.67           C  
ANISOU  537  CE2 TRP A  96     1989   2153   1812    176    182     64       C  
ATOM    538  CE3 TRP A  96     -24.308  57.933  38.607  1.00 11.62           C  
ANISOU  538  CE3 TRP A  96     1447   1641   1325    152    168     71       C  
ATOM    539  CZ2 TRP A  96     -25.328  59.525  40.722  1.00 13.67           C  
ANISOU  539  CZ2 TRP A  96     1707   1923   1561    173    171     70       C  
ATOM    540  CZ3 TRP A  96     -24.730  57.367  39.803  1.00 12.26           C  
ANISOU  540  CZ3 TRP A  96     1504   1744   1409    150    160     78       C  
ATOM    541  CH2 TRP A  96     -25.252  58.164  40.838  1.00 10.65           C  
ANISOU  541  CH2 TRP A  96     1299   1552   1193    161    161     78       C  
ATOM    542  N   ALA A  97     -20.667  61.297  35.425  1.00 13.34           N  
ANISOU  542  N   ALA A  97     1786   1745   1537    135    239     30       N  
ATOM    543  CA  ALA A  97     -19.452  62.011  35.813  1.00 13.83           C  
ANISOU  543  CA  ALA A  97     1859   1790   1603    115    259     14       C  
ATOM    544  C   ALA A  97     -19.496  63.443  35.282  1.00 13.96           C  
ANISOU  544  C   ALA A  97     1919   1778   1607    126    284      7       C  
ATOM    545  O   ALA A  97     -19.230  64.394  36.029  1.00 16.84           O  
ANISOU  545  O   ALA A  97     2294   2134   1967    120    300     -3       O  
ATOM    546  CB  ALA A  97     -18.181  61.263  35.306  1.00 12.19           C  
ANISOU  546  CB  ALA A  97     1642   1575   1413     91    260      6       C  
ATOM    547  N   LEU A  98     -19.855  63.610  34.008  1.00 13.76           N  
ANISOU  547  N   LEU A  98     1918   1737   1572    143    290     15       N  
ATOM    548  CA  LEU A  98     -19.887  64.926  33.376  1.00 14.93           C  
ANISOU  548  CA  LEU A  98     2111   1854   1705    157    318     12       C  
ATOM    549  C   LEU A  98     -20.990  65.775  34.002  1.00 17.78           C  
ANISOU  549  C   LEU A  98     2485   2222   2048    183    320     17       C  
ATOM    550  O   LEU A  98     -20.816  66.981  34.170  1.00 18.70           O  
ANISOU  550  O   LEU A  98     2634   2315   2156    186    346      9       O  
ATOM    551  CB  LEU A  98     -20.092  64.836  31.851  1.00 13.05           C  
ANISOU  551  CB  LEU A  98     1896   1602   1459    176    322     21       C  
ATOM    552  CG  LEU A  98     -18.877  64.387  31.034  1.00 14.77           C  
ANISOU  552  CG  LEU A  98     2116   1802   1691    152    330     13       C  
ATOM    553  CD1 LEU A  98     -19.194  64.002  29.568  1.00 13.17           C  
ANISOU  553  CD1 LEU A  98     1926   1594   1481    172    327     24       C  
ATOM    554  CD2 LEU A  98     -17.779  65.437  31.089  1.00  9.82           C  
ANISOU  554  CD2 LEU A  98     1519   1143   1068    132    365     -2       C  
ATOM    555  N   TYR A  99     -22.114  65.137  34.326  1.00 16.84           N  
ANISOU  555  N   TYR A  99     2340   2134   1923    201    294     29       N  
ATOM    556  CA  TYR A  99     -23.289  65.817  34.852  1.00 17.01           C  
ANISOU  556  CA  TYR A  99     2369   2167   1925    230    292     36       C  
ATOM    557  C   TYR A  99     -22.968  66.422  36.213  1.00 17.45           C  
ANISOU  557  C   TYR A  99     2421   2224   1985    215    300     25       C  
ATOM    558  O   TYR A  99     -23.307  67.575  36.474  1.00 15.81           O  
ANISOU  558  O   TYR A  99     2242   2002   1762    230    318     23       O  
ATOM    559  CB  TYR A  99     -24.457  64.829  34.953  1.00 16.24           C  
ANISOU  559  CB  TYR A  99     2238   2108   1825    245    262     48       C  
ATOM    560  CG  TYR A  99     -25.754  65.395  35.523  1.00 17.13           C  
ANISOU  560  CG  TYR A  99     2352   2240   1917    275    257     54       C  
ATOM    561  CD1 TYR A  99     -26.662  66.052  34.693  1.00 17.74           C  
ANISOU  561  CD1 TYR A  99     2454   2315   1968    314    262     61       C  
ATOM    562  CD2 TYR A  99     -26.077  65.258  36.877  1.00 16.27           C  
ANISOU  562  CD2 TYR A  99     2217   2153   1812    268    246     53       C  
ATOM    563  CE1 TYR A  99     -27.850  66.546  35.192  1.00 16.05           C  
ANISOU  563  CE1 TYR A  99     2240   2122   1735    343    256     65       C  
ATOM    564  CE2 TYR A  99     -27.287  65.728  37.392  1.00 18.85           C  
ANISOU  564  CE2 TYR A  99     2543   2499   2120    295    240     59       C  
ATOM    565  CZ  TYR A  99     -28.154  66.384  36.535  1.00 18.34           C  
ANISOU  565  CZ  TYR A  99     2503   2433   2030    332    245     64       C  
ATOM    566  OH  TYR A  99     -29.339  66.875  36.996  1.00 21.04           O  
ANISOU  566  OH  TYR A  99     2844   2796   2352    362    240     69       O  
ATOM    567  N   GLU A 100     -22.295  65.650  37.065  1.00 16.71           N  
ANISOU  567  N   GLU A 100     2293   2145   1909    186    288     19       N  
ATOM    568  CA  GLU A 100     -21.857  66.137  38.367  1.00 17.54           C  
ANISOU  568  CA  GLU A 100     2390   2255   2018    170    295      6       C  
ATOM    569  C   GLU A 100     -20.647  67.075  38.317  1.00 19.42           C  
ANISOU  569  C   GLU A 100     2654   2462   2261    148    325    -14       C  
ATOM    570  O   GLU A 100     -20.695  68.153  38.915  1.00 20.15           O  
ANISOU  570  O   GLU A 100     2765   2543   2345    150    343    -25       O  
ATOM    571  CB  GLU A 100     -21.579  64.978  39.336  1.00 17.44           C  
ANISOU  571  CB  GLU A 100     2331   2273   2020    152    272      6       C  
ATOM    572  CG  GLU A 100     -22.745  64.003  39.556  1.00 16.18           C  
ANISOU  572  CG  GLU A 100     2145   2145   1859    169    246     24       C  
ATOM    573  CD  GLU A 100     -23.948  64.631  40.249  1.00 18.92           C  
ANISOU  573  CD  GLU A 100     2493   2506   2188    192    242     30       C  
ATOM    574  OE1 GLU A 100     -23.782  65.606  41.007  1.00 19.32           O  
ANISOU  574  OE1 GLU A 100     2557   2550   2233    192    256     20       O  
ATOM    575  OE2 GLU A 100     -25.076  64.130  40.077  1.00 17.85           O  
ANISOU  575  OE2 GLU A 100     2345   2390   2045    211    226     44       O  
ATOM    576  N   TYR A 101     -19.566  66.678  37.647  1.00 18.84           N  
ANISOU  576  N   TYR A 101     2581   2375   2201    126    332    -22       N  
ATOM    577  CA  TYR A 101     -18.251  67.320  37.808  1.00 19.49           C  
ANISOU  577  CA  TYR A 101     2674   2437   2293     96    358    -47       C  
ATOM    578  C   TYR A 101     -17.614  67.875  36.529  1.00 20.29           C  
ANISOU  578  C   TYR A 101     2814   2500   2395     90    385    -53       C  
ATOM    579  O   TYR A 101     -16.445  68.292  36.511  1.00 19.77           O  
ANISOU  579  O   TYR A 101     2755   2416   2337     61    408    -75       O  
ATOM    580  CB  TYR A 101     -17.291  66.363  38.541  1.00 19.45           C  
ANISOU  580  CB  TYR A 101     2626   2457   2304     68    342    -59       C  
ATOM    581  CG  TYR A 101     -17.865  65.871  39.859  1.00 20.72           C  
ANISOU  581  CG  TYR A 101     2753   2654   2463     75    318    -53       C  
ATOM    582  CD1 TYR A 101     -18.260  66.775  40.845  1.00 22.41           C  
ANISOU  582  CD1 TYR A 101     2973   2873   2668     80    326    -61       C  
ATOM    583  CD2 TYR A 101     -18.042  64.509  40.109  1.00 20.80           C  
ANISOU  583  CD2 TYR A 101     2727   2694   2481     77    290    -39       C  
ATOM    584  CE1 TYR A 101     -18.828  66.342  42.045  1.00 23.82           C  
ANISOU  584  CE1 TYR A 101     3121   3085   2844     88    305    -55       C  
ATOM    585  CE2 TYR A 101     -18.593  64.065  41.304  1.00 21.75           C  
ANISOU  585  CE2 TYR A 101     2819   2845   2599     84    272    -32       C  
ATOM    586  CZ  TYR A 101     -18.976  64.980  42.271  1.00 26.58           C  
ANISOU  586  CZ  TYR A 101     3436   3462   3200     90    278    -40       C  
ATOM    587  OH  TYR A 101     -19.530  64.542  43.457  1.00 25.29           O  
ANISOU  587  OH  TYR A 101     3244   3330   3034     98    261    -32       O  
ATOM    588  N   GLY A 102     -18.391  67.922  35.455  1.00 19.67           N  
ANISOU  588  N   GLY A 102     2759   2409   2304    118    385    -34       N  
ATOM    589  CA  GLY A 102     -17.873  68.400  34.176  1.00 23.84           C  
ANISOU  589  CA  GLY A 102     3325   2900   2829    118    412    -36       C  
ATOM    590  C   GLY A 102     -17.281  69.804  34.181  1.00 26.13           C  
ANISOU  590  C   GLY A 102     3658   3152   3116    107    454    -54       C  
ATOM    591  O   GLY A 102     -16.245  70.037  33.554  1.00 24.35           O  
ANISOU  591  O   GLY A 102     3449   2901   2899     84    478    -67       O  
ATOM    592  N   ASP A 103     -17.949  70.726  34.874  1.00 28.37           N  
ANISOU  592  N   ASP A 103     3960   3432   3387    122    465    -54       N  
ATOM    593  CA  ASP A 103     -17.491  72.112  35.011  1.00 31.62           C  
ANISOU  593  CA  ASP A 103     4414   3806   3794    111    508    -73       C  
ATOM    594  C   ASP A 103     -16.323  72.199  35.978  1.00 32.14           C  
ANISOU  594  C   ASP A 103     4456   3877   3879     66    517   -104       C  
ATOM    595  O   ASP A 103     -15.633  73.215  36.013  1.00 35.28           O  
ANISOU  595  O   ASP A 103     4883   4242   4278     45    556   -126       O  
ATOM    596  CB  ASP A 103     -18.576  73.030  35.578  1.00 31.97           C  
ANISOU  596  CB  ASP A 103     4480   3846   3818    141    515    -65       C  
ATOM    597  CG  ASP A 103     -19.755  73.225  34.646  1.00 39.40           C  
ANISOU  597  CG  ASP A 103     5453   4780   4736    191    512    -37       C  
ATOM    598  OD1 ASP A 103     -19.582  73.163  33.409  1.00 44.10           O  
ANISOU  598  OD1 ASP A 103     6073   5356   5328    201    523    -28       O  
ATOM    599  OD2 ASP A 103     -20.870  73.463  35.166  1.00 45.58           O  
ANISOU  599  OD2 ASP A 103     6234   5579   5502    221    499    -26       O  
ATOM    600  N   ASP A 104     -16.136  71.166  36.795  1.00 30.25           N  
ANISOU  600  N   ASP A 104     4163   3680   3651     53    483   -107       N  
ATOM    601  CA  ASP A 104     -15.114  71.181  37.837  1.00 29.99           C  
ANISOU  601  CA  ASP A 104     4101   3662   3632     15    487   -137       C  
ATOM    602  C   ASP A 104     -13.758  70.643  37.388  1.00 29.64           C  
ANISOU  602  C   ASP A 104     4041   3617   3604    -17    492   -156       C  
ATOM    603  O   ASP A 104     -12.814  70.700  38.165  1.00 29.07           O  
ANISOU  603  O   ASP A 104     3943   3558   3541    -48    497   -184       O  
ATOM    604  CB  ASP A 104     -15.589  70.388  39.062  1.00 29.36           C  
ANISOU  604  CB  ASP A 104     3973   3629   3552     22    449   -132       C  
ATOM    605  CG  ASP A 104     -16.832  70.985  39.684  1.00 33.10           C  
ANISOU  605  CG  ASP A 104     4460   4107   4010     51    445   -119       C  
ATOM    606  OD1 ASP A 104     -16.901  72.226  39.755  1.00 36.44           O  
ANISOU  606  OD1 ASP A 104     4919   4500   4424     51    477   -130       O  
ATOM    607  OD2 ASP A 104     -17.751  70.243  40.082  1.00 34.61           O  
ANISOU  607  OD2 ASP A 104     4625   4328   4195     73    413    -98       O  
ATOM    608  N   ILE A 105     -13.664  70.069  36.189  1.00 28.65           N  
ANISOU  608  N   ILE A 105     3923   3480   3481    -10    488   -140       N  
ATOM    609  CA  ILE A 105     -12.429  69.394  35.790  1.00 29.74           C  
ANISOU  609  CA  ILE A 105     4041   3624   3635    -40    488   -155       C  
ATOM    610  C   ILE A 105     -11.668  70.155  34.709  1.00 32.24           C  
ANISOU  610  C   ILE A 105     4398   3896   3953    -56    529   -168       C  
ATOM    611  O   ILE A 105     -10.765  69.620  34.061  1.00 30.45           O  
ANISOU  611  O   ILE A 105     4162   3668   3737    -75    531   -175       O  
ATOM    612  CB  ILE A 105     -12.647  67.917  35.379  1.00 28.07           C  
ANISOU  612  CB  ILE A 105     3797   3439   3428    -27    450   -132       C  
ATOM    613  CG1 ILE A 105     -13.500  67.798  34.111  1.00 24.32           C  
ANISOU  613  CG1 ILE A 105     3351   2944   2943      3    448   -104       C  
ATOM    614  CG2 ILE A 105     -13.227  67.128  36.546  1.00 29.26           C  
ANISOU  614  CG2 ILE A 105     3906   3632   3579    -17    415   -123       C  
ATOM    615  CD1 ILE A 105     -13.322  66.470  33.384  1.00 24.64           C  
ANISOU  615  CD1 ILE A 105     3368   3000   2993      5    423    -90       C  
ATOM    616  N   GLU A 106     -12.009  71.430  34.545  1.00 35.88           N  
ANISOU  616  N   GLU A 106     4906   4320   4404    -49    564   -171       N  
ATOM    617  CA  GLU A 106     -11.423  72.224  33.462  1.00 38.69           C  
ANISOU  617  CA  GLU A 106     5310   4629   4760    -60    607   -179       C  
ATOM    618  C   GLU A 106      -9.892  72.237  33.527  1.00 37.70           C  
ANISOU  618  C   GLU A 106     5167   4502   4652   -108    628   -216       C  
ATOM    619  O   GLU A 106      -9.227  72.101  32.498  1.00 39.74           O  
ANISOU  619  O   GLU A 106     5440   4741   4916   -120    644   -218       O  
ATOM    620  CB  GLU A 106     -12.051  73.625  33.409  1.00 40.55           C  
ANISOU  620  CB  GLU A 106     5600   4825   4980    -43    645   -177       C  
ATOM    621  CG  GLU A 106     -12.267  74.189  32.000  1.00 46.01           C  
ANISOU  621  CG  GLU A 106     6350   5471   5660    -21    676   -159       C  
ATOM    622  CD  GLU A 106     -13.205  73.365  31.120  1.00 52.73           C  
ANISOU  622  CD  GLU A 106     7200   6336   6499     21    643   -122       C  
ATOM    623  OE1 GLU A 106     -14.355  73.095  31.535  1.00 54.68           O  
ANISOU  623  OE1 GLU A 106     7433   6607   6734     54    613   -102       O  
ATOM    624  OE2 GLU A 106     -12.798  73.021  29.985  1.00 52.34           O  
ANISOU  624  OE2 GLU A 106     7163   6273   6452     21    650   -115       O  
ATOM    625  N   ALA A 107      -9.343  72.331  34.735  1.00 36.63           N  
ANISOU  625  N   ALA A 107     5000   4393   4525   -136    625   -245       N  
ATOM    626  CA  ALA A 107      -7.898  72.295  34.965  1.00 35.12           C  
ANISOU  626  CA  ALA A 107     4784   4211   4349   -181    641   -285       C  
ATOM    627  C   ALA A 107      -7.219  70.983  34.579  1.00 33.59           C  
ANISOU  627  C   ALA A 107     4550   4048   4165   -189    611   -282       C  
ATOM    628  O   ALA A 107      -6.031  70.982  34.259  1.00 34.06           O  
ANISOU  628  O   ALA A 107     4601   4104   4235   -222    630   -309       O  
ATOM    629  CB  ALA A 107      -7.585  72.607  36.427  1.00 35.26           C  
ANISOU  629  CB  ALA A 107     4769   4258   4369   -203    638   -317       C  
ATOM    630  N   SER A 108      -7.927  69.858  34.668  1.00 29.38           N  
ANISOU  630  N   SER A 108     3989   3544   3629   -160    566   -251       N  
ATOM    631  CA  SER A 108      -7.328  68.590  34.271  1.00 26.72           C  
ANISOU  631  CA  SER A 108     3617   3232   3300   -164    540   -246       C  
ATOM    632  C   SER A 108      -7.042  68.571  32.763  1.00 25.46           C  
ANISOU  632  C   SER A 108     3490   3039   3143   -164    558   -236       C  
ATOM    633  O   SER A 108      -6.254  67.763  32.283  1.00 25.10           O  
ANISOU  633  O   SER A 108     3423   3006   3107   -176    549   -240       O  
ATOM    634  CB  SER A 108      -8.261  67.427  34.609  1.00 26.11           C  
ANISOU  634  CB  SER A 108     3510   3188   3219   -132    493   -213       C  
ATOM    635  OG  SER A 108      -9.387  67.454  33.745  1.00 22.46           O  
ANISOU  635  OG  SER A 108     3081   2703   2748    -99    489   -180       O  
ATOM    636  N   GLY A 109      -7.710  69.446  32.017  1.00 24.45           N  
ANISOU  636  N   GLY A 109     3413   2869   3005   -146    584   -221       N  
ATOM    637  CA  GLY A 109      -7.710  69.401  30.557  1.00 23.75           C  
ANISOU  637  CA  GLY A 109     3359   2750   2915   -135    598   -204       C  
ATOM    638  C   GLY A 109      -8.421  68.200  29.952  1.00 22.58           C  
ANISOU  638  C   GLY A 109     3195   2620   2763   -103    558   -170       C  
ATOM    639  O   GLY A 109      -8.289  67.963  28.761  1.00 23.58           O  
ANISOU  639  O   GLY A 109     3340   2729   2889    -96    565   -158       O  
ATOM    640  N   GLN A 110      -9.209  67.456  30.727  1.00 20.82           N  
ANISOU  640  N   GLN A 110     2940   2433   2538    -84    519   -154       N  
ATOM    641  CA  GLN A 110      -9.759  66.189  30.235  1.00 19.71           C  
ANISOU  641  CA  GLN A 110     2777   2313   2397    -62    482   -128       C  
ATOM    642  C   GLN A 110     -11.220  66.252  29.792  1.00 19.21           C  
ANISOU  642  C   GLN A 110     2736   2245   2319    -20    470    -97       C  
ATOM    643  O   GLN A 110     -11.765  65.255  29.307  1.00 17.64           O  
ANISOU  643  O   GLN A 110     2521   2062   2119     -1    442    -77       O  
ATOM    644  CB  GLN A 110      -9.586  65.082  31.287  1.00 19.72           C  
ANISOU  644  CB  GLN A 110     2723   2359   2408    -69    446   -130       C  
ATOM    645  CG  GLN A 110      -8.123  64.786  31.627  1.00 19.35           C  
ANISOU  645  CG  GLN A 110     2649   2327   2375   -105    452   -160       C  
ATOM    646  CD  GLN A 110      -7.270  64.576  30.390  1.00 22.20           C  
ANISOU  646  CD  GLN A 110     3023   2669   2742   -117    467   -164       C  
ATOM    647  OE1 GLN A 110      -7.588  63.746  29.542  1.00 21.42           O  
ANISOU  647  OE1 GLN A 110     2924   2570   2644   -101    449   -143       O  
ATOM    648  NE2 GLN A 110      -6.171  65.322  30.287  1.00 22.36           N  
ANISOU  648  NE2 GLN A 110     3054   2673   2768   -149    500   -195       N  
ATOM    649  N   ARG A 111     -11.867  67.400  29.966  1.00 18.39           N  
ANISOU  649  N   ARG A 111     2666   2119   2200     -6    492    -95       N  
ATOM    650  CA  ARG A 111     -13.306  67.461  29.722  1.00 19.13           C  
ANISOU  650  CA  ARG A 111     2775   2216   2277     35    477    -68       C  
ATOM    651  C   ARG A 111     -13.695  67.049  28.304  1.00 17.75           C  
ANISOU  651  C   ARG A 111     2617   2031   2093     60    473    -48       C  
ATOM    652  O   ARG A 111     -14.626  66.264  28.116  1.00 16.73           O  
ANISOU  652  O   ARG A 111     2471   1927   1959     86    442    -29       O  
ATOM    653  CB  ARG A 111     -13.910  68.840  30.038  1.00 20.72           C  
ANISOU  653  CB  ARG A 111     3016   2393   2462     51    505    -69       C  
ATOM    654  CG  ARG A 111     -15.432  68.885  29.834  1.00 19.47           C  
ANISOU  654  CG  ARG A 111     2869   2244   2283     98    488    -42       C  
ATOM    655  CD  ARG A 111     -16.045  70.257  30.175  1.00 28.38           C  
ANISOU  655  CD  ARG A 111     4039   3349   3393    117    515    -42       C  
ATOM    656  NE  ARG A 111     -17.503  70.166  30.234  1.00 31.82           N  
ANISOU  656  NE  ARG A 111     4473   3805   3809    160    492    -19       N  
ATOM    657  CZ  ARG A 111     -18.313  71.012  30.867  1.00 38.99           C  
ANISOU  657  CZ  ARG A 111     5399   4711   4702    182    500    -16       C  
ATOM    658  NH1 ARG A 111     -17.840  72.073  31.511  1.00 40.46           N  
ANISOU  658  NH1 ARG A 111     5609   4872   4890    164    532    -33       N  
ATOM    659  NH2 ARG A 111     -19.620  70.789  30.866  1.00 35.80           N  
ANISOU  659  NH2 ARG A 111     4988   4331   4280    221    476      2       N  
ATOM    660  N   LEU A 112     -12.998  67.579  27.303  1.00 16.46           N  
ANISOU  660  N   LEU A 112     2489   1834   1929     53    504    -54       N  
ATOM    661  CA  LEU A 112     -13.378  67.290  25.925  1.00 16.10           C  
ANISOU  661  CA  LEU A 112     2464   1779   1872     81    502    -35       C  
ATOM    662  C   LEU A 112     -13.048  65.833  25.602  1.00 16.42           C  
ANISOU  662  C   LEU A 112     2463   1847   1927     70    469    -32       C  
ATOM    663  O   LEU A 112     -13.799  65.191  24.870  1.00 16.41           O  
ANISOU  663  O   LEU A 112     2457   1858   1917     97    448    -14       O  
ATOM    664  CB  LEU A 112     -12.710  68.253  24.932  1.00 16.09           C  
ANISOU  664  CB  LEU A 112     2514   1733   1865     77    548    -40       C  
ATOM    665  CG  LEU A 112     -13.018  67.957  23.455  1.00 20.73           C  
ANISOU  665  CG  LEU A 112     3124   2312   2440    107    547    -22       C  
ATOM    666  CD1 LEU A 112     -14.525  68.010  23.113  1.00 24.05           C  
ANISOU  666  CD1 LEU A 112     3557   2746   2835    159    529      2       C  
ATOM    667  CD2 LEU A 112     -12.176  68.795  22.496  1.00 25.41           C  
ANISOU  667  CD2 LEU A 112     3765   2860   3030     98    594    -28       C  
ATOM    668  N   HIS A 113     -11.957  65.302  26.156  1.00 15.95           N  
ANISOU  668  N   HIS A 113     2371   1798   1888     33    465    -50       N  
ATOM    669  CA  HIS A 113     -11.648  63.882  25.940  1.00 16.12           C  
ANISOU  669  CA  HIS A 113     2354   1846   1923     25    434    -47       C  
ATOM    670  C   HIS A 113     -12.780  63.001  26.459  1.00 15.65           C  
ANISOU  670  C   HIS A 113     2263   1820   1861     46    396    -30       C  
ATOM    671  O   HIS A 113     -13.209  62.070  25.778  1.00 15.78           O  
ANISOU  671  O   HIS A 113     2267   1849   1877     60    374    -17       O  
ATOM    672  CB  HIS A 113     -10.336  63.469  26.606  1.00 16.17           C  
ANISOU  672  CB  HIS A 113     2330   1864   1949    -13    435    -69       C  
ATOM    673  CG  HIS A 113      -9.118  64.039  25.944  1.00 15.31           C  
ANISOU  673  CG  HIS A 113     2243   1727   1846    -38    469    -88       C  
ATOM    674  ND1 HIS A 113      -8.810  63.822  24.616  1.00 17.94           N  
ANISOU  674  ND1 HIS A 113     2595   2043   2178    -33    478    -82       N  
ATOM    675  CD2 HIS A 113      -8.120  64.809  26.439  1.00 19.45           C  
ANISOU  675  CD2 HIS A 113     2772   2240   2377    -70    497   -115       C  
ATOM    676  CE1 HIS A 113      -7.679  64.442  24.322  1.00 18.92           C  
ANISOU  676  CE1 HIS A 113     2736   2143   2308    -61    511   -103       C  
ATOM    677  NE2 HIS A 113      -7.240  65.046  25.412  1.00 19.95           N  
ANISOU  677  NE2 HIS A 113     2858   2277   2444    -84    524   -124       N  
ATOM    678  N   LEU A 114     -13.285  63.331  27.642  1.00 13.42           N  
ANISOU  678  N   LEU A 114     1969   1551   1576     48    390    -31       N  
ATOM    679  CA  LEU A 114     -14.379  62.572  28.231  1.00 14.51           C  
ANISOU  679  CA  LEU A 114     2079   1720   1712     66    357    -17       C  
ATOM    680  C   LEU A 114     -15.654  62.705  27.402  1.00 13.95           C  
ANISOU  680  C   LEU A 114     2028   1650   1623    103    351      1       C  
ATOM    681  O   LEU A 114     -16.341  61.712  27.173  1.00 12.54           O  
ANISOU  681  O   LEU A 114     1826   1493   1445    116    324     12       O  
ATOM    682  CB  LEU A 114     -14.629  62.986  29.685  1.00 14.21           C  
ANISOU  682  CB  LEU A 114     2028   1697   1674     60    355    -23       C  
ATOM    683  CG  LEU A 114     -15.705  62.265  30.500  1.00 11.88           C  
ANISOU  683  CG  LEU A 114     1701   1434   1377     75    324    -10       C  
ATOM    684  CD1 LEU A 114     -15.575  60.739  30.437  1.00 13.21           C  
ANISOU  684  CD1 LEU A 114     1832   1625   1559     68    297     -3       C  
ATOM    685  CD2 LEU A 114     -15.655  62.773  31.950  1.00 15.25           C  
ANISOU  685  CD2 LEU A 114     2116   1872   1804     65    326    -20       C  
ATOM    686  N   GLU A 115     -15.981  63.921  26.977  1.00 12.85           N  
ANISOU  686  N   GLU A 115     1931   1486   1466    122    376      3       N  
ATOM    687  CA  GLU A 115     -17.202  64.148  26.200  1.00 14.08           C  
ANISOU  687  CA  GLU A 115     2106   1643   1598    164    372     19       C  
ATOM    688  C   GLU A 115     -17.164  63.416  24.864  1.00 12.81           C  
ANISOU  688  C   GLU A 115     1946   1484   1437    174    363     26       C  
ATOM    689  O   GLU A 115     -18.166  62.837  24.457  1.00 12.44           O  
ANISOU  689  O   GLU A 115     1885   1460   1379    199    341     37       O  
ATOM    690  CB  GLU A 115     -17.422  65.648  25.932  1.00 14.07           C  
ANISOU  690  CB  GLU A 115     2157   1611   1577    185    406     21       C  
ATOM    691  CG  GLU A 115     -17.768  66.433  27.185  1.00 15.06           C  
ANISOU  691  CG  GLU A 115     2284   1737   1698    184    413     16       C  
ATOM    692  CD  GLU A 115     -17.705  67.934  26.946  1.00 22.06           C  
ANISOU  692  CD  GLU A 115     3227   2586   2569    197    453     14       C  
ATOM    693  OE1 GLU A 115     -17.005  68.357  26.004  1.00 21.00           O  
ANISOU  693  OE1 GLU A 115     3125   2419   2433    193    481     11       O  
ATOM    694  OE2 GLU A 115     -18.355  68.677  27.703  1.00 21.31           O  
ANISOU  694  OE2 GLU A 115     3141   2491   2462    211    459     15       O  
ATOM    695  N   ARG A 116     -16.034  63.457  24.165  1.00 13.91           N  
ANISOU  695  N   ARG A 116     2100   1599   1585    155    382     18       N  
ATOM    696  CA  ARG A 116     -15.949  62.783  22.872  1.00 14.88           C  
ANISOU  696  CA  ARG A 116     2224   1722   1705    165    375     24       C  
ATOM    697  C   ARG A 116     -16.045  61.266  23.021  1.00 14.36           C  
ANISOU  697  C   ARG A 116     2110   1687   1656    153    340     25       C  
ATOM    698  O   ARG A 116     -16.782  60.592  22.298  1.00 12.33           O  
ANISOU  698  O   ARG A 116     1843   1448   1392    173    321     33       O  
ATOM    699  CB  ARG A 116     -14.643  63.137  22.170  1.00 15.58           C  
ANISOU  699  CB  ARG A 116     2338   1779   1802    144    404     15       C  
ATOM    700  CG  ARG A 116     -14.749  64.513  21.552  1.00 19.87           C  
ANISOU  700  CG  ARG A 116     2936   2288   2325    165    441     18       C  
ATOM    701  CD  ARG A 116     -13.532  64.802  20.694  1.00 27.79           C  
ANISOU  701  CD  ARG A 116     3965   3259   3334    146    471     10       C  
ATOM    702  NE  ARG A 116     -13.729  65.988  19.860  1.00 32.42           N  
ANISOU  702  NE  ARG A 116     4609   3811   3897    173    508     18       N  
ATOM    703  CZ  ARG A 116     -12.728  66.625  19.263  1.00 32.95           C  
ANISOU  703  CZ  ARG A 116     4709   3841   3966    157    546     10       C  
ATOM    704  NH1 ARG A 116     -11.489  66.167  19.416  1.00 32.85           N  
ANISOU  704  NH1 ARG A 116     4676   3826   3978    114    550     -7       N  
ATOM    705  NH2 ARG A 116     -12.964  67.698  18.521  1.00 30.74           N  
ANISOU  705  NH2 ARG A 116     4486   3529   3664    185    581     19       N  
ATOM    706  N   ASN A 117     -15.330  60.734  24.004  1.00 12.56           N  
ANISOU  706  N   ASN A 117     1853   1469   1449    121    332     16       N  
ATOM    707  CA  ASN A 117     -15.394  59.300  24.247  1.00 13.14           C  
ANISOU  707  CA  ASN A 117     1884   1568   1538    110    302     18       C  
ATOM    708  C   ASN A 117     -16.805  58.817  24.541  1.00 13.06           C  
ANISOU  708  C   ASN A 117     1854   1586   1520    132    278     28       C  
ATOM    709  O   ASN A 117     -17.212  57.756  24.052  1.00 14.15           O  
ANISOU  709  O   ASN A 117     1971   1741   1662    136    258     32       O  
ATOM    710  CB  ASN A 117     -14.403  58.916  25.351  1.00 12.15           C  
ANISOU  710  CB  ASN A 117     1734   1450   1433     77    300      7       C  
ATOM    711  CG  ASN A 117     -13.047  58.580  24.779  1.00 13.70           C  
ANISOU  711  CG  ASN A 117     1930   1632   1642     53    310     -3       C  
ATOM    712  OD1 ASN A 117     -12.882  57.515  24.183  1.00 15.31           O  
ANISOU  712  OD1 ASN A 117     2117   1844   1854     51    296      0       O  
ATOM    713  ND2 ASN A 117     -12.087  59.486  24.913  1.00 11.57           N  
ANISOU  713  ND2 ASN A 117     1679   1343   1374     36    337    -17       N  
ATOM    714  N   LEU A 118     -17.557  59.611  25.304  1.00 13.78           N  
ANISOU  714  N   LEU A 118     1953   1682   1599    146    281     31       N  
ATOM    715  CA  LEU A 118     -18.961  59.311  25.587  1.00 15.08           C  
ANISOU  715  CA  LEU A 118     2101   1875   1753    168    260     40       C  
ATOM    716  C   LEU A 118     -19.799  59.323  24.313  1.00 15.30           C  
ANISOU  716  C   LEU A 118     2142   1908   1762    200    256     45       C  
ATOM    717  O   LEU A 118     -20.587  58.404  24.057  1.00 13.16           O  
ANISOU  717  O   LEU A 118     1845   1663   1491    208    234     47       O  
ATOM    718  CB  LEU A 118     -19.565  60.305  26.588  1.00 14.25           C  
ANISOU  718  CB  LEU A 118     2005   1771   1636    180    267     41       C  
ATOM    719  CG  LEU A 118     -21.081  60.192  26.796  1.00 15.86           C  
ANISOU  719  CG  LEU A 118     2196   2005   1825    208    249     49       C  
ATOM    720  CD1 LEU A 118     -21.507  58.815  27.340  1.00 11.08           C  
ANISOU  720  CD1 LEU A 118     1546   1429   1235    194    222     50       C  
ATOM    721  CD2 LEU A 118     -21.551  61.277  27.768  1.00 13.84           C  
ANISOU  721  CD2 LEU A 118     1954   1748   1557    219    259     50       C  
ATOM    722  N   ALA A 119     -19.664  60.408  23.559  1.00 15.63           N  
ANISOU  722  N   ALA A 119     2224   1926   1785    220    279     47       N  
ATOM    723  CA  ALA A 119     -20.409  60.571  22.315  1.00 16.63           C  
ANISOU  723  CA  ALA A 119     2370   2059   1890    257    278     53       C  
ATOM    724  C   ALA A 119     -20.236  59.360  21.400  1.00 15.64           C  
ANISOU  724  C   ALA A 119     2222   1945   1774    250    262     50       C  
ATOM    725  O   ALA A 119     -21.195  58.928  20.756  1.00 16.76           O  
ANISOU  725  O   ALA A 119     2352   2112   1902    274    245     51       O  
ATOM    726  CB  ALA A 119     -20.010  61.855  21.600  1.00 16.34           C  
ANISOU  726  CB  ALA A 119     2385   1988   1835    275    311     56       C  
ATOM    727  N   PHE A 120     -19.031  58.809  21.343  1.00 16.23           N  
ANISOU  727  N   PHE A 120     2290   2005   1872    217    266     45       N  
ATOM    728  CA  PHE A 120     -18.757  57.649  20.493  1.00 14.47           C  
ANISOU  728  CA  PHE A 120     2047   1789   1659    208    252     42       C  
ATOM    729  C   PHE A 120     -19.628  56.437  20.845  1.00 14.93           C  
ANISOU  729  C   PHE A 120     2063   1881   1726    205    223     40       C  
ATOM    730  O   PHE A 120     -20.157  55.743  19.964  1.00 13.88           O  
ANISOU  730  O   PHE A 120     1918   1765   1588    217    209     38       O  
ATOM    731  CB  PHE A 120     -17.267  57.284  20.560  1.00 14.40           C  
ANISOU  731  CB  PHE A 120     2037   1759   1673    173    261     36       C  
ATOM    732  CG  PHE A 120     -16.854  56.258  19.538  1.00 13.32           C  
ANISOU  732  CG  PHE A 120     1889   1625   1546    166    252     33       C  
ATOM    733  CD1 PHE A 120     -16.568  56.647  18.231  1.00 18.42           C  
ANISOU  733  CD1 PHE A 120     2562   2255   2178    182    266     33       C  
ATOM    734  CD2 PHE A 120     -16.762  54.914  19.878  1.00 16.73           C  
ANISOU  734  CD2 PHE A 120     2284   2073   1998    146    231     30       C  
ATOM    735  CE1 PHE A 120     -16.207  55.713  17.273  1.00 18.17           C  
ANISOU  735  CE1 PHE A 120     2520   2227   2154    177    257     30       C  
ATOM    736  CE2 PHE A 120     -16.398  53.962  18.916  1.00 11.98           C  
ANISOU  736  CE2 PHE A 120     1672   1472   1404    140    224     26       C  
ATOM    737  CZ  PHE A 120     -16.103  54.375  17.629  1.00 15.59           C  
ANISOU  737  CZ  PHE A 120     2156   1916   1849    155    236     26       C  
ATOM    738  N   ALA A 121     -19.799  56.180  22.134  1.00 12.49           N  
ANISOU  738  N   ALA A 121     1732   1583   1430    188    214     41       N  
ATOM    739  CA  ALA A 121     -20.685  55.098  22.558  1.00 13.38           C  
ANISOU  739  CA  ALA A 121     1807   1725   1549    184    191     40       C  
ATOM    740  C   ALA A 121     -22.170  55.406  22.365  1.00 13.57           C  
ANISOU  740  C   ALA A 121     1828   1777   1551    216    182     40       C  
ATOM    741  O   ALA A 121     -22.942  54.534  21.946  1.00 13.40           O  
ANISOU  741  O   ALA A 121     1781   1780   1529    221    165     34       O  
ATOM    742  CB  ALA A 121     -20.399  54.696  24.015  1.00 13.17           C  
ANISOU  742  CB  ALA A 121     1758   1702   1541    159    187     41       C  
ATOM    743  N   LEU A 122     -22.560  56.651  22.626  1.00 12.82           N  
ANISOU  743  N   LEU A 122     1757   1677   1435    239    193     45       N  
ATOM    744  CA  LEU A 122     -23.955  57.042  22.457  1.00 14.33           C  
ANISOU  744  CA  LEU A 122     1946   1895   1601    274    184     45       C  
ATOM    745  C   LEU A 122     -24.377  56.953  20.987  1.00 14.35           C  
ANISOU  745  C   LEU A 122     1956   1909   1584    303    181     41       C  
ATOM    746  O   LEU A 122     -25.493  56.536  20.686  1.00 14.29           O  
ANISOU  746  O   LEU A 122     1927   1937   1564    321    164     34       O  
ATOM    747  CB  LEU A 122     -24.217  58.442  23.022  1.00 13.99           C  
ANISOU  747  CB  LEU A 122     1932   1843   1539    296    200     51       C  
ATOM    748  CG  LEU A 122     -24.000  58.562  24.537  1.00 12.71           C  
ANISOU  748  CG  LEU A 122     1758   1676   1392    272    201     53       C  
ATOM    749  CD1 LEU A 122     -24.367  59.975  24.967  1.00 10.37           C  
ANISOU  749  CD1 LEU A 122     1494   1372   1075    297    217     58       C  
ATOM    750  CD2 LEU A 122     -24.793  57.536  25.346  1.00 13.59           C  
ANISOU  750  CD2 LEU A 122     1826   1820   1515    259    179     51       C  
ATOM    751  N   ASP A 123     -23.489  57.318  20.068  1.00 13.93           N  
ANISOU  751  N   ASP A 123     1933   1830   1528    306    196     43       N  
ATOM    752  CA  ASP A 123     -23.823  57.168  18.648  1.00 14.96           C  
ANISOU  752  CA  ASP A 123     2070   1972   1640    333    193     39       C  
ATOM    753  C   ASP A 123     -24.106  55.713  18.266  1.00 14.44           C  
ANISOU  753  C   ASP A 123     1964   1932   1589    317    170     27       C  
ATOM    754  O   ASP A 123     -24.943  55.441  17.403  1.00 14.51           O  
ANISOU  754  O   ASP A 123     1962   1970   1580    342    158     19       O  
ATOM    755  CB  ASP A 123     -22.703  57.716  17.759  1.00 15.74           C  
ANISOU  755  CB  ASP A 123     2208   2034   1736    335    215     44       C  
ATOM    756  CG  ASP A 123     -22.527  59.223  17.887  1.00 16.45           C  
ANISOU  756  CG  ASP A 123     2344   2098   1806    357    242     54       C  
ATOM    757  OD1 ASP A 123     -23.427  59.948  18.360  1.00 19.96           O  
ANISOU  757  OD1 ASP A 123     2797   2555   2232    384    243     58       O  
ATOM    758  OD2 ASP A 123     -21.447  59.688  17.491  1.00 20.84           O  
ANISOU  758  OD2 ASP A 123     2931   2618   2367    347    265     57       O  
ATOM    759  N   TYR A 124     -23.383  54.775  18.871  1.00 12.95           N  
ANISOU  759  N   TYR A 124     1753   1732   1432    275    166     25       N  
ATOM    760  CA  TYR A 124     -23.635  53.346  18.628  1.00 13.60           C  
ANISOU  760  CA  TYR A 124     1799   1836   1532    256    148     14       C  
ATOM    761  C   TYR A 124     -25.028  52.947  19.137  1.00 14.32           C  
ANISOU  761  C   TYR A 124     1858   1966   1618    263    131      7       C  
ATOM    762  O   TYR A 124     -25.777  52.208  18.464  1.00 14.21           O  
ANISOU  762  O   TYR A 124     1820   1980   1599    269    118     -6       O  
ATOM    763  CB  TYR A 124     -22.517  52.491  19.248  1.00 11.30           C  
ANISOU  763  CB  TYR A 124     1495   1522   1274    214    149     17       C  
ATOM    764  CG  TYR A 124     -22.860  51.031  19.445  1.00 13.23           C  
ANISOU  764  CG  TYR A 124     1702   1784   1539    190    134      8       C  
ATOM    765  CD1 TYR A 124     -23.461  50.586  20.624  1.00 15.16           C  
ANISOU  765  CD1 TYR A 124     1921   2042   1794    176    127      8       C  
ATOM    766  CD2 TYR A 124     -22.589  50.100  18.444  1.00 14.93           C  
ANISOU  766  CD2 TYR A 124     1909   2001   1763    182    129      0       C  
ATOM    767  CE1 TYR A 124     -23.797  49.246  20.800  1.00 15.36           C  
ANISOU  767  CE1 TYR A 124     1916   2081   1839    154    118      0       C  
ATOM    768  CE2 TYR A 124     -22.901  48.757  18.608  1.00 15.54           C  
ANISOU  768  CE2 TYR A 124     1953   2090   1859    159    119    -10       C  
ATOM    769  CZ  TYR A 124     -23.514  48.345  19.778  1.00 17.54           C  
ANISOU  769  CZ  TYR A 124     2184   2355   2123    145    114     -8       C  
ATOM    770  OH  TYR A 124     -23.822  47.013  19.930  1.00 17.59           O  
ANISOU  770  OH  TYR A 124     2162   2370   2150    122    109    -17       O  
ATOM    771  N   LEU A 125     -25.375  53.444  20.323  1.00 12.84           N  
ANISOU  771  N   LEU A 125     1668   1779   1429    262    133     13       N  
ATOM    772  CA  LEU A 125     -26.652  53.091  20.938  1.00 13.43           C  
ANISOU  772  CA  LEU A 125     1711   1890   1499    265    119      6       C  
ATOM    773  C   LEU A 125     -27.781  53.587  20.041  1.00 14.46           C  
ANISOU  773  C   LEU A 125     1843   2054   1597    307    112     -2       C  
ATOM    774  O   LEU A 125     -28.775  52.888  19.892  1.00 12.78           O  
ANISOU  774  O   LEU A 125     1597   1877   1380    309     98    -17       O  
ATOM    775  CB  LEU A 125     -26.793  53.655  22.368  1.00 13.55           C  
ANISOU  775  CB  LEU A 125     1728   1901   1518    259    123     16       C  
ATOM    776  CG  LEU A 125     -25.756  53.124  23.368  1.00 12.05           C  
ANISOU  776  CG  LEU A 125     1533   1686   1359    221    129     24       C  
ATOM    777  CD1 LEU A 125     -26.007  53.652  24.789  1.00 11.30           C  
ANISOU  777  CD1 LEU A 125     1436   1593   1265    217    131     32       C  
ATOM    778  CD2 LEU A 125     -25.825  51.601  23.362  1.00  9.31           C  
ANISOU  778  CD2 LEU A 125     1152   1348   1034    193    119     16       C  
ATOM    779  N   VAL A 126     -27.613  54.766  19.440  1.00 13.16           N  
ANISOU  779  N   VAL A 126     1715   1877   1406    342    124      5       N  
ATOM    780  CA  VAL A 126     -28.620  55.308  18.527  1.00 15.39           C  
ANISOU  780  CA  VAL A 126     2003   2191   1652    389    118     -1       C  
ATOM    781  C   VAL A 126     -28.680  54.436  17.269  1.00 16.73           C  
ANISOU  781  C   VAL A 126     2156   2378   1819    391    108    -16       C  
ATOM    782  O   VAL A 126     -29.764  54.094  16.791  1.00 17.03           O  
ANISOU  782  O   VAL A 126     2168   2461   1841    411     93    -33       O  
ATOM    783  CB  VAL A 126     -28.334  56.777  18.135  1.00 16.27           C  
ANISOU  783  CB  VAL A 126     2165   2280   1735    427    138     13       C  
ATOM    784  CG1 VAL A 126     -29.227  57.234  16.964  1.00 16.22           C  
ANISOU  784  CG1 VAL A 126     2168   2307   1689    481    133      7       C  
ATOM    785  CG2 VAL A 126     -28.488  57.707  19.340  1.00 16.33           C  
ANISOU  785  CG2 VAL A 126     2188   2276   1740    431    147     24       C  
ATOM    786  N   ALA A 127     -27.511  54.056  16.766  1.00 15.82           N  
ANISOU  786  N   ALA A 127     2055   2231   1723    370    116    -12       N  
ATOM    787  CA  ALA A 127     -27.437  53.217  15.575  1.00 17.18           C  
ANISOU  787  CA  ALA A 127     2213   2416   1896    369    107    -26       C  
ATOM    788  C   ALA A 127     -28.007  51.814  15.786  1.00 17.31           C  
ANISOU  788  C   ALA A 127     2181   2460   1933    339     90    -45       C  
ATOM    789  O   ALA A 127     -28.258  51.130  14.803  1.00 17.97           O  
ANISOU  789  O   ALA A 127     2248   2565   2013    343     81    -62       O  
ATOM    790  CB  ALA A 127     -26.010  53.123  15.077  1.00 15.78           C  
ANISOU  790  CB  ALA A 127     2062   2198   1736    351    121    -17       C  
ATOM    791  N   CYS A 128     -28.174  51.379  17.032  1.00 14.30           N  
ANISOU  791  N   CYS A 128     1779   2078   1575    309     88    -43       N  
ATOM    792  CA  CYS A 128     -28.820  50.097  17.321  1.00 16.53           C  
ANISOU  792  CA  CYS A 128     2018   2385   1876    280     76    -62       C  
ATOM    793  C   CYS A 128     -30.333  50.079  17.098  1.00 16.90           C  
ANISOU  793  C   CYS A 128     2035   2485   1899    304     63    -82       C  
ATOM    794  O   CYS A 128     -30.920  49.005  17.136  1.00 17.96           O  
ANISOU  794  O   CYS A 128     2132   2642   2047    280     55   -102       O  
ATOM    795  CB  CYS A 128     -28.511  49.623  18.749  1.00 15.29           C  
ANISOU  795  CB  CYS A 128     1851   2209   1750    242     80    -52       C  
ATOM    796  SG  CYS A 128     -26.807  49.060  18.958  1.00 16.14           S  
ANISOU  796  SG  CYS A 128     1975   2266   1891    206     92    -37       S  
ATOM    797  N   ASP A 129     -30.962  51.232  16.876  1.00 16.81           N  
ANISOU  797  N   ASP A 129     2040   2494   1852    349     62    -79       N  
ATOM    798  CA  ASP A 129     -32.426  51.294  16.774  1.00 19.12           C  
ANISOU  798  CA  ASP A 129     2302   2841   2118    375     49    -99       C  
ATOM    799  C   ASP A 129     -32.989  50.428  15.640  1.00 21.17           C  
ANISOU  799  C   ASP A 129     2531   3141   2372    378     36   -129       C  
ATOM    800  O   ASP A 129     -32.542  50.539  14.500  1.00 19.87           O  
ANISOU  800  O   ASP A 129     2383   2971   2194    397     36   -130       O  
ATOM    801  CB  ASP A 129     -32.919  52.731  16.574  1.00 17.84           C  
ANISOU  801  CB  ASP A 129     2167   2693   1915    430     51    -89       C  
ATOM    802  CG  ASP A 129     -34.438  52.824  16.498  1.00 19.65           C  
ANISOU  802  CG  ASP A 129     2364   2984   2115    460     36   -111       C  
ATOM    803  OD1 ASP A 129     -35.131  52.103  17.246  1.00 23.30           O  
ANISOU  803  OD1 ASP A 129     2788   3471   2594    433     29   -125       O  
ATOM    804  OD2 ASP A 129     -34.951  53.621  15.688  1.00 21.23           O  
ANISOU  804  OD2 ASP A 129     2578   3211   2275    513     33   -114       O  
ATOM    805  N   ARG A 130     -33.968  49.583  15.958  1.00 22.91           N  
ANISOU  805  N   ARG A 130     2706   3399   2600    358     26   -153       N  
ATOM    806  CA  ARG A 130     -34.711  48.849  14.926  1.00 26.48           C  
ANISOU  806  CA  ARG A 130     3122   3897   3040    364     14   -188       C  
ATOM    807  C   ARG A 130     -36.234  49.027  15.074  1.00 27.62           C  
ANISOU  807  C   ARG A 130     3230   4104   3157    387      2   -213       C  
ATOM    808  O   ARG A 130     -37.016  48.190  14.616  1.00 28.91           O  
ANISOU  808  O   ARG A 130     3353   4311   3321    376     -6   -247       O  
ATOM    809  CB  ARG A 130     -34.304  47.365  14.910  1.00 24.98           C  
ANISOU  809  CB  ARG A 130     2908   3691   2890    309     16   -203       C  
ATOM    810  CG  ARG A 130     -32.836  47.083  14.545  1.00 26.93           C  
ANISOU  810  CG  ARG A 130     3187   3885   3161    290     26   -184       C  
ATOM    811  CD  ARG A 130     -32.551  47.521  13.107  1.00 29.61           C  
ANISOU  811  CD  ARG A 130     3545   4233   3473    328     22   -188       C  
ATOM    812  NE  ARG A 130     -31.202  47.206  12.643  1.00 31.48           N  
ANISOU  812  NE  ARG A 130     3808   4423   3730    310     31   -174       N  
ATOM    813  CZ  ARG A 130     -30.126  47.978  12.794  1.00 34.04           C  
ANISOU  813  CZ  ARG A 130     4174   4702   4056    317     42   -144       C  
ATOM    814  NH1 ARG A 130     -30.175  49.144  13.439  1.00 29.46           N  
ANISOU  814  NH1 ARG A 130     3620   4113   3460    341     48   -123       N  
ATOM    815  NH2 ARG A 130     -28.968  47.563  12.292  1.00 34.89           N  
ANISOU  815  NH2 ARG A 130     4299   4774   4182    299     49   -136       N  
ATOM    816  N   GLY A 131     -36.655  50.110  15.722  1.00 28.34           N  
ANISOU  816  N   GLY A 131     3338   4202   3227    418      3   -197       N  
ATOM    817  CA  GLY A 131     -38.065  50.487  15.808  1.00 30.05           C  
ANISOU  817  CA  GLY A 131     3525   4480   3410    450     -8   -217       C  
ATOM    818  C   GLY A 131     -38.798  49.864  16.979  1.00 30.96           C  
ANISOU  818  C   GLY A 131     3602   4612   3547    412     -8   -229       C  
ATOM    819  O   GLY A 131     -38.957  50.484  18.037  1.00 33.86           O  
ANISOU  819  O   GLY A 131     3981   4970   3915    416     -4   -211       O  
ATOM    820  N   ASP A 132     -39.235  48.625  16.792  1.00 30.72           N  
ANISOU  820  N   ASP A 132     3529   4606   3537    375    -12   -261       N  
ATOM    821  CA  ASP A 132     -39.932  47.866  17.829  1.00 30.90           C  
ANISOU  821  CA  ASP A 132     3514   4643   3583    333     -9   -276       C  
ATOM    822  C   ASP A 132     -38.955  47.002  18.628  1.00 28.34           C  
ANISOU  822  C   ASP A 132     3201   4259   3308    276      6   -258       C  
ATOM    823  O   ASP A 132     -39.365  46.183  19.453  1.00 25.68           O  
ANISOU  823  O   ASP A 132     2837   3925   2996    235     13   -268       O  
ATOM    824  CB  ASP A 132     -40.965  46.953  17.166  1.00 33.93           C  
ANISOU  824  CB  ASP A 132     3845   5086   3962    321    -17   -325       C  
ATOM    825  CG  ASP A 132     -40.341  45.702  16.547  1.00 41.45           C  
ANISOU  825  CG  ASP A 132     4787   6015   4946    278    -11   -340       C  
ATOM    826  OD1 ASP A 132     -39.259  45.779  15.915  1.00 48.03           O  
ANISOU  826  OD1 ASP A 132     5653   6809   5784    283     -9   -322       O  
ATOM    827  OD2 ASP A 132     -40.944  44.616  16.695  1.00 51.40           O  
ANISOU  827  OD2 ASP A 132     6006   7297   6227    237     -7   -372       O  
ATOM    828  N   SER A 133     -37.662  47.169  18.356  1.00 24.54           N  
ANISOU  828  N   SER A 133     2759   3725   2838    275     12   -231       N  
ATOM    829  CA  SER A 133     -36.628  46.393  19.028  1.00 23.96           C  
ANISOU  829  CA  SER A 133     2698   3596   2806    227     26   -212       C  
ATOM    830  C   SER A 133     -35.294  47.107  18.802  1.00 22.62           C  
ANISOU  830  C   SER A 133     2577   3378   2637    243     31   -180       C  
ATOM    831  O   SER A 133     -35.267  48.149  18.161  1.00 24.05           O  
ANISOU  831  O   SER A 133     2782   3568   2788    287     26   -173       O  
ATOM    832  CB  SER A 133     -36.596  44.979  18.439  1.00 23.64           C  
ANISOU  832  CB  SER A 133     2631   3559   2792    188     28   -239       C  
ATOM    833  OG  SER A 133     -36.369  45.079  17.047  1.00 24.06           O  
ANISOU  833  OG  SER A 133     2690   3624   2826    213     20   -252       O  
ATOM    834  N   VAL A 134     -34.199  46.552  19.314  1.00 21.46           N  
ANISOU  834  N   VAL A 134     2447   3182   2525    207     42   -161       N  
ATOM    835  CA  VAL A 134     -32.870  47.114  19.094  1.00 19.37           C  
ANISOU  835  CA  VAL A 134     2225   2872   2263    216     48   -134       C  
ATOM    836  C   VAL A 134     -31.895  45.968  18.836  1.00 18.47           C  
ANISOU  836  C   VAL A 134     2111   2723   2181    178     55   -134       C  
ATOM    837  O   VAL A 134     -32.160  44.820  19.214  1.00 17.87           O  
ANISOU  837  O   VAL A 134     2009   2649   2130    142     59   -147       O  
ATOM    838  CB  VAL A 134     -32.340  47.961  20.302  1.00 19.59           C  
ANISOU  838  CB  VAL A 134     2279   2868   2294    218     56   -104       C  
ATOM    839  CG1 VAL A 134     -33.233  49.175  20.626  1.00 19.35           C  
ANISOU  839  CG1 VAL A 134     2253   2866   2231    257     51   -101       C  
ATOM    840  CG2 VAL A 134     -32.091  47.100  21.533  1.00 14.42           C  
ANISOU  840  CG2 VAL A 134     1611   2192   1672    175     64    -96       C  
ATOM    841  N   VAL A 135     -30.777  46.279  18.187  1.00 17.67           N  
ANISOU  841  N   VAL A 135     2040   2591   2080    186     58   -120       N  
ATOM    842  CA  VAL A 135     -29.612  45.398  18.207  1.00 14.91           C  
ANISOU  842  CA  VAL A 135     1700   2202   1763    153     67   -112       C  
ATOM    843  C   VAL A 135     -29.065  45.550  19.617  1.00 17.35           C  
ANISOU  843  C   VAL A 135     2021   2482   2089    135     76    -88       C  
ATOM    844  O   VAL A 135     -28.860  46.682  20.069  1.00 16.74           O  
ANISOU  844  O   VAL A 135     1966   2397   1998    156     78    -70       O  
ATOM    845  CB  VAL A 135     -28.568  45.784  17.144  1.00 16.09           C  
ANISOU  845  CB  VAL A 135     1879   2329   1905    169     68   -104       C  
ATOM    846  CG1 VAL A 135     -27.317  44.897  17.289  1.00 14.30           C  
ANISOU  846  CG1 VAL A 135     1660   2061   1710    134     77    -94       C  
ATOM    847  CG2 VAL A 135     -29.172  45.577  15.733  1.00 14.46           C  
ANISOU  847  CG2 VAL A 135     1658   2156   1678    189     58   -130       C  
ATOM    848  N   TYR A 136     -28.923  44.441  20.342  1.00 14.28           N  
ANISOU  848  N   TYR A 136     1616   2080   1730     98     83    -88       N  
ATOM    849  CA  TYR A 136     -28.482  44.523  21.731  1.00 15.75           C  
ANISOU  849  CA  TYR A 136     1811   2243   1930     84     91    -66       C  
ATOM    850  C   TYR A 136     -27.158  43.824  21.972  1.00 14.67           C  
ANISOU  850  C   TYR A 136     1688   2067   1819     60    100    -52       C  
ATOM    851  O   TYR A 136     -26.653  43.803  23.099  1.00 15.26           O  
ANISOU  851  O   TYR A 136     1769   2123   1906     49    107    -34       O  
ATOM    852  CB  TYR A 136     -29.546  44.020  22.728  1.00 14.67           C  
ANISOU  852  CB  TYR A 136     1646   2126   1800     68     93    -73       C  
ATOM    853  CG  TYR A 136     -29.793  42.519  22.763  1.00 15.05           C  
ANISOU  853  CG  TYR A 136     1671   2173   1874     33    101    -87       C  
ATOM    854  CD1 TYR A 136     -30.736  41.916  21.928  1.00 15.51           C  
ANISOU  854  CD1 TYR A 136     1702   2261   1929     27     97   -118       C  
ATOM    855  CD2 TYR A 136     -29.118  41.717  23.674  1.00 12.33           C  
ANISOU  855  CD2 TYR A 136     1332   1797   1556      6    114    -71       C  
ATOM    856  CE1 TYR A 136     -30.976  40.546  21.990  1.00 17.98           C  
ANISOU  856  CE1 TYR A 136     1995   2569   2266     -7    108   -133       C  
ATOM    857  CE2 TYR A 136     -29.341  40.355  23.745  1.00 13.59           C  
ANISOU  857  CE2 TYR A 136     1474   1950   1738    -24    125    -83       C  
ATOM    858  CZ  TYR A 136     -30.285  39.778  22.913  1.00 18.37           C  
ANISOU  858  CZ  TYR A 136     2053   2582   2342    -33    123   -114       C  
ATOM    859  OH  TYR A 136     -30.482  38.422  23.015  1.00 18.24           O  
ANISOU  859  OH  TYR A 136     2023   2556   2351    -67    139   -127       O  
ATOM    860  N   GLN A 137     -26.619  43.215  20.921  1.00 14.74           N  
ANISOU  860  N   GLN A 137     1699   2065   1835     54    100    -61       N  
ATOM    861  CA  GLN A 137     -25.333  42.529  21.033  1.00 13.03           C  
ANISOU  861  CA  GLN A 137     1496   1813   1641     34    108    -49       C  
ATOM    862  C   GLN A 137     -24.716  42.295  19.661  1.00 14.59           C  
ANISOU  862  C   GLN A 137     1702   2003   1838     38    106    -58       C  
ATOM    863  O   GLN A 137     -25.426  41.977  18.693  1.00 15.14           O  
ANISOU  863  O   GLN A 137     1757   2094   1899     42    100    -79       O  
ATOM    864  CB  GLN A 137     -25.509  41.178  21.723  1.00 12.70           C  
ANISOU  864  CB  GLN A 137     1436   1763   1625      3    118    -51       C  
ATOM    865  CG  GLN A 137     -24.179  40.475  22.038  1.00 13.26           C  
ANISOU  865  CG  GLN A 137     1522   1799   1717    -12    127    -35       C  
ATOM    866  CD  GLN A 137     -24.367  39.310  22.987  1.00 17.84           C  
ANISOU  866  CD  GLN A 137     2090   2368   2318    -37    140    -31       C  
ATOM    867  OE1 GLN A 137     -25.039  39.449  24.006  1.00 16.70           O  
ANISOU  867  OE1 GLN A 137     1937   2234   2173    -39    143    -26       O  
ATOM    868  NE2 GLN A 137     -23.775  38.162  22.664  1.00 13.33           N  
ANISOU  868  NE2 GLN A 137     1521   1776   1767    -55    149    -33       N  
ATOM    869  N   ILE A 138     -23.398  42.461  19.572  1.00 14.37           N  
ANISOU  869  N   ILE A 138     1697   1946   1816     37    111    -43       N  
ATOM    870  CA  ILE A 138     -22.653  42.092  18.358  1.00 15.54           C  
ANISOU  870  CA  ILE A 138     1854   2082   1967     37    110    -50       C  
ATOM    871  C   ILE A 138     -21.546  41.129  18.745  1.00 15.44           C  
ANISOU  871  C   ILE A 138     1846   2040   1980     14    119    -41       C  
ATOM    872  O   ILE A 138     -20.710  41.426  19.610  1.00 14.59           O  
ANISOU  872  O   ILE A 138     1750   1915   1877     11    124    -23       O  
ATOM    873  CB  ILE A 138     -21.991  43.290  17.638  1.00 15.33           C  
ANISOU  873  CB  ILE A 138     1854   2049   1921     62    109    -43       C  
ATOM    874  CG1 ILE A 138     -22.987  44.436  17.415  1.00 17.98           C  
ANISOU  874  CG1 ILE A 138     2192   2410   2228     92    103    -47       C  
ATOM    875  CG2 ILE A 138     -21.277  42.833  16.369  1.00 17.69           C  
ANISOU  875  CG2 ILE A 138     2160   2337   2223     61    109    -51       C  
ATOM    876  CD1 ILE A 138     -23.681  44.508  16.098  1.00 19.46           C  
ANISOU  876  CD1 ILE A 138     2374   2623   2396    113     95    -66       C  
ATOM    877  N   GLY A 139     -21.543  39.967  18.102  1.00 15.33           N  
ANISOU  877  N   GLY A 139     1821   2022   1979     -1    120    -54       N  
ATOM    878  CA  GLY A 139     -20.592  38.926  18.448  1.00 15.90           C  
ANISOU  878  CA  GLY A 139     1898   2068   2076    -21    130    -46       C  
ATOM    879  C   GLY A 139     -21.234  37.932  19.394  1.00 18.15           C  
ANISOU  879  C   GLY A 139     2166   2351   2377    -42    139    -46       C  
ATOM    880  O   GLY A 139     -22.085  38.295  20.201  1.00 19.25           O  
ANISOU  880  O   GLY A 139     2295   2506   2511    -40    138    -44       O  
ATOM    881  N   ASP A 140     -20.807  36.678  19.290  1.00 19.02           N  
ANISOU  881  N   ASP A 140     2275   2442   2507    -60    148    -48       N  
ATOM    882  CA  ASP A 140     -21.287  35.586  20.139  1.00 21.66           C  
ANISOU  882  CA  ASP A 140     2599   2769   2860    -82    162    -48       C  
ATOM    883  C   ASP A 140     -20.263  35.415  21.256  1.00 19.59           C  
ANISOU  883  C   ASP A 140     2351   2483   2606    -81    171    -21       C  
ATOM    884  O   ASP A 140     -19.099  35.150  20.966  1.00 20.07           O  
ANISOU  884  O   ASP A 140     2427   2526   2673    -79    173    -14       O  
ATOM    885  CB  ASP A 140     -21.366  34.311  19.286  1.00 21.64           C  
ANISOU  885  CB  ASP A 140     2591   2757   2874   -101    170    -66       C  
ATOM    886  CG  ASP A 140     -21.841  33.086  20.064  1.00 29.57           C  
ANISOU  886  CG  ASP A 140     3588   3747   3899   -125    190    -67       C  
ATOM    887  OD1 ASP A 140     -21.043  32.490  20.813  1.00 31.34           O  
ANISOU  887  OD1 ASP A 140     3827   3945   4135   -129    203    -47       O  
ATOM    888  OD2 ASP A 140     -23.014  32.698  19.881  1.00 35.28           O  
ANISOU  888  OD2 ASP A 140     4291   4487   4625   -140    194    -89       O  
ATOM    889  N   GLY A 141     -20.676  35.524  22.518  1.00 18.96           N  
ANISOU  889  N   GLY A 141     2268   2406   2527    -83    177     -9       N  
ATOM    890  CA  GLY A 141     -19.721  35.416  23.624  1.00 18.41           C  
ANISOU  890  CA  GLY A 141     2212   2321   2462    -78    184     14       C  
ATOM    891  C   GLY A 141     -18.790  34.213  23.601  1.00 20.37           C  
ANISOU  891  C   GLY A 141     2470   2542   2726    -86    197     22       C  
ATOM    892  O   GLY A 141     -17.565  34.348  23.711  1.00 19.14           O  
ANISOU  892  O   GLY A 141     2327   2375   2567    -75    196     34       O  
ATOM    893  N   ALA A 142     -19.357  33.014  23.462  1.00 19.63           N  
ANISOU  893  N   ALA A 142     2371   2436   2647   -104    212     13       N  
ATOM    894  CA  ALA A 142     -18.525  31.810  23.500  1.00 20.90           C  
ANISOU  894  CA  ALA A 142     2546   2570   2824   -110    227     21       C  
ATOM    895  C   ALA A 142     -17.584  31.703  22.297  1.00 20.50           C  
ANISOU  895  C   ALA A 142     2504   2511   2774   -105    220     13       C  
ATOM    896  O   ALA A 142     -16.416  31.347  22.458  1.00 22.25           O  
ANISOU  896  O   ALA A 142     2739   2716   2998    -97    224     27       O  
ATOM    897  CB  ALA A 142     -19.390  30.549  23.648  1.00 22.04           C  
ANISOU  897  CB  ALA A 142     2686   2700   2986   -133    249     12       C  
ATOM    898  N   ALA A 143     -18.065  32.029  21.102  1.00 20.15           N  
ANISOU  898  N   ALA A 143     2450   2480   2726   -109    209     -8       N  
ATOM    899  CA  ALA A 143     -17.234  31.925  19.903  1.00 20.86           C  
ANISOU  899  CA  ALA A 143     2547   2562   2815   -105    202    -16       C  
ATOM    900  C   ALA A 143     -16.104  32.953  19.925  1.00 20.23           C  
ANISOU  900  C   ALA A 143     2478   2484   2721    -85    190     -3       C  
ATOM    901  O   ALA A 143     -14.951  32.634  19.652  1.00 20.47           O  
ANISOU  901  O   ALA A 143     2520   2501   2755    -80    192      3       O  
ATOM    902  CB  ALA A 143     -18.083  32.125  18.650  1.00 21.26           C  
ANISOU  902  CB  ALA A 143     2585   2631   2861   -111    192    -43       C  
ATOM    903  N   ASP A 144     -16.448  34.189  20.267  1.00 18.74           N  
ANISOU  903  N   ASP A 144     2287   2316   2518    -75    180      0       N  
ATOM    904  CA  ASP A 144     -15.479  35.275  20.337  1.00 17.39           C  
ANISOU  904  CA  ASP A 144     2125   2147   2333    -59    171      9       C  
ATOM    905  C   ASP A 144     -14.402  34.973  21.378  1.00 17.05           C  
ANISOU  905  C   ASP A 144     2090   2092   2293    -55    179     28       C  
ATOM    906  O   ASP A 144     -13.208  35.128  21.120  1.00 15.87           O  
ANISOU  906  O   ASP A 144     1950   1937   2142    -48    177     32       O  
ATOM    907  CB  ASP A 144     -16.214  36.583  20.663  1.00 17.50           C  
ANISOU  907  CB  ASP A 144     2135   2182   2331    -50    163      9       C  
ATOM    908  CG  ASP A 144     -15.287  37.795  20.653  1.00 21.35           C  
ANISOU  908  CG  ASP A 144     2635   2672   2805    -36    157     15       C  
ATOM    909  OD1 ASP A 144     -14.511  37.956  21.617  1.00 20.03           O  
ANISOU  909  OD1 ASP A 144     2472   2500   2638    -33    161     29       O  
ATOM    910  OD2 ASP A 144     -15.349  38.594  19.694  1.00 17.02           O  
ANISOU  910  OD2 ASP A 144     2092   2129   2244    -28    151      6       O  
ATOM    911  N   HIS A 145     -14.798  34.508  22.557  1.00 17.24           N  
ANISOU  911  N   HIS A 145     2111   2115   2323    -58    188     40       N  
ATOM    912  CA  HIS A 145     -13.803  34.322  23.614  1.00 18.32           C  
ANISOU  912  CA  HIS A 145     2254   2246   2460    -48    194     58       C  
ATOM    913  C   HIS A 145     -12.894  33.100  23.469  1.00 18.02           C  
ANISOU  913  C   HIS A 145     2226   2189   2433    -47    204     63       C  
ATOM    914  O   HIS A 145     -11.840  33.077  24.094  1.00 19.13           O  
ANISOU  914  O   HIS A 145     2371   2328   2568    -34    206     75       O  
ATOM    915  CB  HIS A 145     -14.446  34.312  25.001  1.00 17.89           C  
ANISOU  915  CB  HIS A 145     2195   2198   2404    -46    200     71       C  
ATOM    916  CG  HIS A 145     -15.091  35.609  25.375  1.00 21.00           C  
ANISOU  916  CG  HIS A 145     2582   2612   2785    -42    190     69       C  
ATOM    917  ND1 HIS A 145     -15.511  35.887  26.658  1.00 25.92           N  
ANISOU  917  ND1 HIS A 145     3200   3245   3403    -38    193     81       N  
ATOM    918  CD2 HIS A 145     -15.382  36.709  24.638  1.00 24.04           C  
ANISOU  918  CD2 HIS A 145     2965   3009   3159    -40    178     57       C  
ATOM    919  CE1 HIS A 145     -16.042  37.097  26.693  1.00 27.04           C  
ANISOU  919  CE1 HIS A 145     3337   3403   3532    -34    182     75       C  
ATOM    920  NE2 HIS A 145     -15.973  37.620  25.482  1.00 25.09           N  
ANISOU  920  NE2 HIS A 145     3093   3157   3281    -34    174     62       N  
ATOM    921  N   LYS A 146     -13.285  32.108  22.672  1.00 18.80           N  
ANISOU  921  N   LYS A 146     2325   2272   2544    -60    212     54       N  
ATOM    922  CA  LYS A 146     -12.431  30.950  22.376  1.00 21.51           C  
ANISOU  922  CA  LYS A 146     2680   2595   2898    -58    222     57       C  
ATOM    923  C   LYS A 146     -11.170  31.362  21.621  1.00 20.53           C  
ANISOU  923  C   LYS A 146     2560   2472   2766    -48    212     54       C  
ATOM    924  O   LYS A 146     -10.228  30.581  21.521  1.00 20.80           O  
ANISOU  924  O   LYS A 146     2604   2495   2805    -41    219     59       O  
ATOM    925  CB  LYS A 146     -13.137  29.925  21.480  1.00 22.35           C  
ANISOU  925  CB  LYS A 146     2785   2685   3019    -76    232     42       C  
ATOM    926  CG  LYS A 146     -14.177  29.018  22.127  1.00 31.50           C  
ANISOU  926  CG  LYS A 146     3943   3833   4191    -91    251     44       C  
ATOM    927  CD  LYS A 146     -14.447  27.809  21.235  1.00 37.23           C  
ANISOU  927  CD  LYS A 146     4673   4539   4934   -108    264     28       C  
ATOM    928  CE  LYS A 146     -15.921  27.611  20.868  1.00 44.63           C  
ANISOU  928  CE  LYS A 146     5595   5481   5879   -132    269      6       C  
ATOM    929  NZ  LYS A 146     -16.794  27.206  22.006  1.00 45.80           N  
ANISOU  929  NZ  LYS A 146     5741   5625   6034   -142    287     15       N  
ATOM    930  N   TRP A 147     -11.167  32.555  21.036  1.00 19.55           N  
ANISOU  930  N   TRP A 147     2431   2364   2631    -47    198     44       N  
ATOM    931  CA  TRP A 147     -10.058  32.956  20.170  1.00 20.28           C  
ANISOU  931  CA  TRP A 147     2529   2458   2719    -41    191     38       C  
ATOM    932  C   TRP A 147      -9.277  34.099  20.810  1.00 20.27           C  
ANISOU  932  C   TRP A 147     2527   2470   2703    -30    185     44       C  
ATOM    933  O   TRP A 147      -9.893  35.011  21.377  1.00 18.57           O  
ANISOU  933  O   TRP A 147     2307   2268   2480    -29    181     46       O  
ATOM    934  CB  TRP A 147     -10.599  33.420  18.825  1.00 18.95           C  
ANISOU  934  CB  TRP A 147     2359   2292   2548    -47    182     20       C  
ATOM    935  CG  TRP A 147      -9.546  33.935  17.881  1.00 21.70           C  
ANISOU  935  CG  TRP A 147     2714   2641   2889    -42    177     14       C  
ATOM    936  CD1 TRP A 147      -8.639  33.193  17.177  1.00 18.56           C  
ANISOU  936  CD1 TRP A 147     2321   2231   2497    -41    180     11       C  
ATOM    937  CD2 TRP A 147      -9.300  35.308  17.537  1.00 16.16           C  
ANISOU  937  CD2 TRP A 147     2015   1951   2173    -36    170     10       C  
ATOM    938  NE1 TRP A 147      -7.846  34.016  16.409  1.00 18.68           N  
ANISOU  938  NE1 TRP A 147     2341   2251   2502    -36    174      4       N  
ATOM    939  CE2 TRP A 147      -8.238  35.319  16.605  1.00 16.78           C  
ANISOU  939  CE2 TRP A 147     2100   2023   2250    -34    169      4       C  
ATOM    940  CE3 TRP A 147      -9.879  36.526  17.924  1.00 13.35           C  
ANISOU  940  CE3 TRP A 147     1658   1607   1805    -33    165     11       C  
ATOM    941  CZ2 TRP A 147      -7.737  36.503  16.048  1.00 16.27           C  
ANISOU  941  CZ2 TRP A 147     2043   1965   2173    -29    167      0       C  
ATOM    942  CZ3 TRP A 147      -9.386  37.707  17.372  1.00 12.81           C  
ANISOU  942  CZ3 TRP A 147     1598   1544   1725    -27    163      6       C  
ATOM    943  CH2 TRP A 147      -8.329  37.687  16.431  1.00 17.58           C  
ANISOU  943  CH2 TRP A 147     2210   2141   2328    -26    165      0       C  
ATOM    944  N   TRP A 148      -7.950  34.021  20.702  1.00 17.36           N  
ANISOU  944  N   TRP A 148     2162   2101   2331    -22    185     45       N  
ATOM    945  CA  TRP A 148      -7.038  35.001  21.273  1.00 16.59           C  
ANISOU  945  CA  TRP A 148     2062   2018   2221    -14    182     47       C  
ATOM    946  C   TRP A 148      -6.270  35.682  20.137  1.00 17.38           C  
ANISOU  946  C   TRP A 148     2166   2119   2316    -17    178     33       C  
ATOM    947  O   TRP A 148      -5.434  35.055  19.490  1.00 17.94           O  
ANISOU  947  O   TRP A 148     2241   2184   2391    -15    180     30       O  
ATOM    948  CB  TRP A 148      -6.093  34.357  22.297  1.00 17.41           C  
ANISOU  948  CB  TRP A 148     2164   2127   2323     -1    187     58       C  
ATOM    949  CG  TRP A 148      -5.423  35.371  23.187  1.00 16.94           C  
ANISOU  949  CG  TRP A 148     2096   2088   2249      5    184     58       C  
ATOM    950  CD1 TRP A 148      -4.275  36.072  22.929  1.00 16.19           C  
ANISOU  950  CD1 TRP A 148     1999   2005   2146      6    181     47       C  
ATOM    951  CD2 TRP A 148      -5.891  35.829  24.468  1.00 17.48           C  
ANISOU  951  CD2 TRP A 148     2159   2170   2312     10    184     66       C  
ATOM    952  NE1 TRP A 148      -4.002  36.933  23.972  1.00 19.87           N  
ANISOU  952  NE1 TRP A 148     2456   2490   2601     10    180     46       N  
ATOM    953  CE2 TRP A 148      -4.980  36.809  24.925  1.00 16.15           C  
ANISOU  953  CE2 TRP A 148     1983   2021   2130     13    181     58       C  
ATOM    954  CE3 TRP A 148      -6.990  35.503  25.269  1.00 16.35           C  
ANISOU  954  CE3 TRP A 148     2014   2024   2171     10    187     78       C  
ATOM    955  CZ2 TRP A 148      -5.134  37.467  26.154  1.00 18.77           C  
ANISOU  955  CZ2 TRP A 148     2308   2371   2453     19    180     62       C  
ATOM    956  CZ3 TRP A 148      -7.146  36.157  26.495  1.00 17.47           C  
ANISOU  956  CZ3 TRP A 148     2150   2183   2303     17    185     83       C  
ATOM    957  CH2 TRP A 148      -6.222  37.133  26.920  1.00 17.38           C  
ANISOU  957  CH2 TRP A 148     2131   2191   2279     21    181     75       C  
ATOM    958  N   GLY A 149      -6.580  36.947  19.859  1.00 15.51           N  
ANISOU  958  N   GLY A 149     1932   1890   2071    -20    174     26       N  
ATOM    959  CA  GLY A 149      -5.869  37.675  18.796  1.00 14.07           C  
ANISOU  959  CA  GLY A 149     1756   1706   1882    -22    174     15       C  
ATOM    960  C   GLY A 149      -6.448  39.076  18.697  1.00 13.60           C  
ANISOU  960  C   GLY A 149     1702   1651   1812    -23    173     10       C  
ATOM    961  O   GLY A 149      -7.346  39.426  19.458  1.00 13.79           O  
ANISOU  961  O   GLY A 149     1723   1682   1834    -22    171     16       O  
ATOM    962  N   SER A 150      -5.953  39.888  17.773  1.00 13.75           N  
ANISOU  962  N   SER A 150     1732   1667   1825    -25    176      1       N  
ATOM    963  CA  SER A 150      -6.269  41.323  17.809  1.00 12.88           C  
ANISOU  963  CA  SER A 150     1630   1559   1702    -24    180     -1       C  
ATOM    964  C   SER A 150      -7.549  41.666  17.071  1.00 13.45           C  
ANISOU  964  C   SER A 150     1710   1629   1768    -18    176     -1       C  
ATOM    965  O   SER A 150      -7.883  40.987  16.095  1.00 12.51           O  
ANISOU  965  O   SER A 150     1592   1506   1653    -17    172     -5       O  
ATOM    966  CB  SER A 150      -5.101  42.115  17.219  1.00 11.70           C  
ANISOU  966  CB  SER A 150     1491   1406   1547    -29    190    -11       C  
ATOM    967  OG  SER A 150      -3.911  41.883  17.974  1.00 12.84           O  
ANISOU  967  OG  SER A 150     1624   1558   1693    -33    193    -14       O  
ATOM    968  N   ALA A 151      -8.236  42.719  17.523  1.00 13.09           N  
ANISOU  968  N   ALA A 151     1671   1589   1713    -14    178      0       N  
ATOM    969  CA  ALA A 151      -9.525  43.099  16.960  1.00 13.16           C  
ANISOU  969  CA  ALA A 151     1684   1600   1713     -4    173      0       C  
ATOM    970  C   ALA A 151      -9.512  43.260  15.447  1.00 13.90           C  
ANISOU  970  C   ALA A 151     1791   1688   1799      2    175     -7       C  
ATOM    971  O   ALA A 151     -10.473  42.860  14.769  1.00 11.51           O  
ANISOU  971  O   ALA A 151     1485   1391   1494      9    167    -10       O  
ATOM    972  CB  ALA A 151     -10.057  44.390  17.614  1.00 12.72           C  
ANISOU  972  CB  ALA A 151     1637   1550   1644      1    178      2       C  
ATOM    973  N   GLU A 152      -8.439  43.862  14.927  1.00 13.94           N  
ANISOU  973  N   GLU A 152     1811   1683   1800      0    186    -11       N  
ATOM    974  CA  GLU A 152      -8.380  44.215  13.500  1.00 13.46           C  
ANISOU  974  CA  GLU A 152     1768   1616   1730      9    190    -16       C  
ATOM    975  C   GLU A 152      -8.353  43.013  12.544  1.00 14.01           C  
ANISOU  975  C   GLU A 152     1829   1685   1807      9    182    -22       C  
ATOM    976  O   GLU A 152      -8.585  43.171  11.341  1.00 15.99           O  
ANISOU  976  O   GLU A 152     2090   1935   2049     20    182    -26       O  
ATOM    977  CB  GLU A 152      -7.151  45.086  13.215  1.00 14.07           C  
ANISOU  977  CB  GLU A 152     1862   1681   1803      4    207    -20       C  
ATOM    978  CG  GLU A 152      -7.188  46.487  13.820  1.00 15.60           C  
ANISOU  978  CG  GLU A 152     2071   1870   1985      5    221    -18       C  
ATOM    979  CD  GLU A 152      -6.808  46.496  15.295  1.00 17.17           C  
ANISOU  979  CD  GLU A 152     2255   2076   2193     -7    220    -17       C  
ATOM    980  OE1 GLU A 152      -6.397  45.458  15.853  1.00 13.39           O  
ANISOU  980  OE1 GLU A 152     1755   1604   1727    -16    211    -17       O  
ATOM    981  OE2 GLU A 152      -6.901  47.573  15.909  1.00 16.45           O  
ANISOU  981  OE2 GLU A 152     2173   1982   2094     -7    230    -17       O  
ATOM    982  N   VAL A 153      -8.059  41.823  13.058  1.00 14.19           N  
ANISOU  982  N   VAL A 153     1834   1709   1846     -1    176    -21       N  
ATOM    983  CA  VAL A 153      -7.977  40.628  12.211  1.00 15.05           C  
ANISOU  983  CA  VAL A 153     1936   1815   1965     -3    170    -26       C  
ATOM    984  C   VAL A 153      -9.047  39.576  12.508  1.00 15.79           C  
ANISOU  984  C   VAL A 153     2013   1915   2068     -6    160    -27       C  
ATOM    985  O   VAL A 153      -9.037  38.511  11.886  1.00 17.70           O  
ANISOU  985  O   VAL A 153     2249   2154   2319    -10    157    -34       O  
ATOM    986  CB  VAL A 153      -6.580  39.967  12.258  1.00 14.52           C  
ANISOU  986  CB  VAL A 153     1867   1740   1909    -12    174    -27       C  
ATOM    987  CG1 VAL A 153      -5.513  40.895  11.648  1.00 13.84           C  
ANISOU  987  CG1 VAL A 153     1796   1648   1814    -12    185    -31       C  
ATOM    988  CG2 VAL A 153      -6.218  39.552  13.682  1.00 15.48           C  
ANISOU  988  CG2 VAL A 153     1976   1864   2040    -20    174    -19       C  
ATOM    989  N   ILE A 154      -9.992  39.876  13.401  1.00 15.69           N  
ANISOU  989  N   ILE A 154     1994   1912   2053     -5    157    -23       N  
ATOM    990  CA  ILE A 154     -10.966  38.866  13.830  1.00 15.54           C  
ANISOU  990  CA  ILE A 154     1958   1899   2044    -11    151    -24       C  
ATOM    991  C   ILE A 154     -11.882  38.355  12.718  1.00 15.83           C  
ANISOU  991  C   ILE A 154     1989   1944   2080     -8    145    -38       C  
ATOM    992  O   ILE A 154     -12.272  37.185  12.731  1.00 16.46           O  
ANISOU  992  O   ILE A 154     2056   2022   2173    -19    144    -44       O  
ATOM    993  CB  ILE A 154     -11.798  39.297  15.071  1.00 15.24           C  
ANISOU  993  CB  ILE A 154     1914   1871   2005    -11    150    -16       C  
ATOM    994  CG1 ILE A 154     -12.488  38.090  15.722  1.00 14.08           C  
ANISOU  994  CG1 ILE A 154     1751   1725   1873    -22    150    -16       C  
ATOM    995  CG2 ILE A 154     -12.824  40.353  14.694  1.00  9.73           C  
ANISOU  995  CG2 ILE A 154     1220   1188   1289      1    146    -21       C  
ATOM    996  CD1 ILE A 154     -12.987  38.339  17.166  1.00 14.05           C  
ANISOU  996  CD1 ILE A 154     1740   1727   1870    -24    151     -5       C  
ATOM    997  N   GLU A 155     -12.176  39.193  11.733  1.00 15.04           N  
ANISOU  997  N   GLU A 155     1899   1853   1963      5    142    -45       N  
ATOM    998  CA  GLU A 155     -13.062  38.758  10.656  1.00 17.31           C  
ANISOU  998  CA  GLU A 155     2177   2152   2244     11    135    -61       C  
ATOM    999  C   GLU A 155     -12.415  37.718   9.734  1.00 19.07           C  
ANISOU  999  C   GLU A 155     2400   2367   2479      4    135    -70       C  
ATOM   1000  O   GLU A 155     -13.129  37.100   8.949  1.00 18.42           O  
ANISOU 1000  O   GLU A 155     2306   2295   2396      4    130    -87       O  
ATOM   1001  CB  GLU A 155     -13.568  39.940   9.836  1.00 17.55           C  
ANISOU 1001  CB  GLU A 155     2220   2197   2250     35    132    -65       C  
ATOM   1002  CG  GLU A 155     -14.380  40.918  10.675  1.00 20.51           C  
ANISOU 1002  CG  GLU A 155     2595   2583   2612     45    132    -57       C  
ATOM   1003  CD  GLU A 155     -14.740  42.183   9.931  1.00 24.03           C  
ANISOU 1003  CD  GLU A 155     3058   3039   3030     72    133    -57       C  
ATOM   1004  OE1 GLU A 155     -13.985  42.539   8.999  1.00 25.27           O  
ANISOU 1004  OE1 GLU A 155     3234   3187   3180     81    139    -57       O  
ATOM   1005  OE2 GLU A 155     -15.759  42.818  10.287  1.00 21.78           O  
ANISOU 1005  OE2 GLU A 155     2770   2771   2731     85    129    -57       O  
ATOM   1006  N   LYS A 156     -11.099  37.528   9.827  1.00 17.85           N  
ANISOU 1006  N   LYS A 156     2254   2193   2333     -1    142    -62       N  
ATOM   1007  CA  LYS A 156     -10.449  36.434   9.102  1.00 19.76           C  
ANISOU 1007  CA  LYS A 156     2495   2425   2587     -9    143    -70       C  
ATOM   1008  C   LYS A 156     -10.653  35.118   9.843  1.00 20.25           C  
ANISOU 1008  C   LYS A 156     2543   2479   2670    -26    145    -70       C  
ATOM   1009  O   LYS A 156     -10.579  34.044   9.242  1.00 20.20           O  
ANISOU 1009  O   LYS A 156     2532   2466   2674    -33    146    -80       O  
ATOM   1010  CB  LYS A 156      -8.952  36.670   8.856  1.00 19.14           C  
ANISOU 1010  CB  LYS A 156     2430   2333   2509     -8    150    -63       C  
ATOM   1011  CG  LYS A 156      -8.587  37.902   8.016  1.00 21.01           C  
ANISOU 1011  CG  LYS A 156     2684   2571   2726      5    153    -63       C  
ATOM   1012  CD  LYS A 156      -9.214  37.986   6.618  1.00 24.06           C  
ANISOU 1012  CD  LYS A 156     3073   2969   3100     19    147    -76       C  
ATOM   1013  CE  LYS A 156      -8.841  36.818   5.718  1.00 26.57           C  
ANISOU 1013  CE  LYS A 156     3385   3281   3427     14    145    -88       C  
ATOM   1014  NZ  LYS A 156      -9.006  37.200   4.278  1.00 22.80           N  
ANISOU 1014  NZ  LYS A 156     2915   2813   2932     31    142    -98       N  
ATOM   1015  N   GLU A 157     -10.916  35.205  11.147  1.00 19.19           N  
ANISOU 1015  N   GLU A 157     2405   2344   2541    -31    148    -58       N  
ATOM   1016  CA  GLU A 157     -11.097  34.024  11.988  1.00 18.83           C  
ANISOU 1016  CA  GLU A 157     2351   2289   2514    -45    154    -55       C  
ATOM   1017  C   GLU A 157     -12.545  33.554  12.062  1.00 19.47           C  
ANISOU 1017  C   GLU A 157     2416   2380   2598    -54    153    -67       C  
ATOM   1018  O   GLU A 157     -12.787  32.358  12.230  1.00 20.38           O  
ANISOU 1018  O   GLU A 157     2526   2486   2731    -68    160    -72       O  
ATOM   1019  CB  GLU A 157     -10.588  34.306  13.407  1.00 18.93           C  
ANISOU 1019  CB  GLU A 157     2366   2297   2528    -45    159    -36       C  
ATOM   1020  CG  GLU A 157     -10.871  33.221  14.437  1.00 19.81           C  
ANISOU 1020  CG  GLU A 157     2472   2399   2655    -55    167    -28       C  
ATOM   1021  CD  GLU A 157      -9.999  31.987  14.268  1.00 25.78           C  
ANISOU 1021  CD  GLU A 157     3233   3136   3425    -59    176    -27       C  
ATOM   1022  OE1 GLU A 157      -8.946  32.054  13.599  1.00 22.17           O  
ANISOU 1022  OE1 GLU A 157     2782   2674   2964    -53    174    -28       O  
ATOM   1023  OE2 GLU A 157     -10.356  30.931  14.827  1.00 23.68           O  
ANISOU 1023  OE2 GLU A 157     2965   2859   3172    -67    186    -24       O  
ATOM   1024  N   MET A 158     -13.498  34.483  12.018  1.00 18.67           N  
ANISOU 1024  N   MET A 158     2310   2300   2483    -46    146    -72       N  
ATOM   1025  CA  MET A 158     -14.904  34.137  12.247  1.00 20.07           C  
ANISOU 1025  CA  MET A 158     2470   2492   2663    -54    144    -84       C  
ATOM   1026  C   MET A 158     -15.834  35.206  11.702  1.00 20.82           C  
ANISOU 1026  C   MET A 158     2560   2614   2736    -38    134    -94       C  
ATOM   1027  O   MET A 158     -15.424  36.348  11.459  1.00 19.19           O  
ANISOU 1027  O   MET A 158     2367   2411   2513    -20    130    -86       O  
ATOM   1028  CB  MET A 158     -15.193  33.912  13.737  1.00 20.38           C  
ANISOU 1028  CB  MET A 158     2505   2526   2712    -64    152    -70       C  
ATOM   1029  CG  MET A 158     -15.104  35.175  14.618  1.00 19.14           C  
ANISOU 1029  CG  MET A 158     2354   2376   2542    -51    148    -53       C  
ATOM   1030  SD  MET A 158     -15.233  34.814  16.380  1.00 19.60           S  
ANISOU 1030  SD  MET A 158     2409   2427   2611    -60    158    -35       S  
ATOM   1031  CE  MET A 158     -13.543  34.404  16.811  1.00 15.20           C  
ANISOU 1031  CE  MET A 158     1866   1846   2062    -58    165    -18       C  
ATOM   1032  N   THR A 159     -17.093  34.817  11.532  1.00 20.15           N  
ANISOU 1032  N   THR A 159     2455   2548   2650    -44    131   -113       N  
ATOM   1033  CA  THR A 159     -18.129  35.706  11.039  1.00 21.64           C  
ANISOU 1033  CA  THR A 159     2636   2769   2817    -27    120   -125       C  
ATOM   1034  C   THR A 159     -18.991  36.032  12.251  1.00 21.07           C  
ANISOU 1034  C   THR A 159     2554   2707   2745    -31    121   -119       C  
ATOM   1035  O   THR A 159     -19.456  35.126  12.937  1.00 21.04           O  
ANISOU 1035  O   THR A 159     2536   2698   2757    -52    129   -123       O  
ATOM   1036  CB  THR A 159     -18.956  34.996   9.939  1.00 23.11           C  
ANISOU 1036  CB  THR A 159     2802   2975   3001    -31    115   -156       C  
ATOM   1037  OG1 THR A 159     -18.098  34.760   8.813  1.00 25.27           O  
ANISOU 1037  OG1 THR A 159     3087   3239   3274    -26    114   -161       O  
ATOM   1038  CG2 THR A 159     -20.119  35.853   9.478  1.00 22.45           C  
ANISOU 1038  CG2 THR A 159     2706   2930   2892    -10    103   -171       C  
ATOM   1039  N   ARG A 160     -19.198  37.319  12.508  1.00 18.83           N  
ANISOU 1039  N   ARG A 160     2278   2435   2441    -10    116   -108       N  
ATOM   1040  CA  ARG A 160     -19.847  37.759  13.742  1.00 18.12           C  
ANISOU 1040  CA  ARG A 160     2182   2353   2349    -11    117    -99       C  
ATOM   1041  C   ARG A 160     -21.358  37.957  13.586  1.00 17.19           C  
ANISOU 1041  C   ARG A 160     2042   2270   2217     -4    109   -118       C  
ATOM   1042  O   ARG A 160     -21.791  38.717  12.720  1.00 18.42           O  
ANISOU 1042  O   ARG A 160     2198   2449   2349     19    100   -128       O  
ATOM   1043  CB  ARG A 160     -19.188  39.072  14.188  1.00 17.07           C  
ANISOU 1043  CB  ARG A 160     2071   2212   2202      6    117    -77       C  
ATOM   1044  CG  ARG A 160     -17.755  38.828  14.665  1.00 13.26           C  
ANISOU 1044  CG  ARG A 160     1604   1699   1734     -3    125    -59       C  
ATOM   1045  CD  ARG A 160     -16.904  40.093  14.622  1.00 13.87           C  
ANISOU 1045  CD  ARG A 160     1704   1768   1797     13    127    -46       C  
ATOM   1046  NE  ARG A 160     -17.431  41.250  15.361  1.00 13.61           N  
ANISOU 1046  NE  ARG A 160     1675   1745   1749     26    126    -37       N  
ATOM   1047  CZ  ARG A 160     -17.298  41.444  16.670  1.00 17.01           C  
ANISOU 1047  CZ  ARG A 160     2105   2171   2186     19    130    -24       C  
ATOM   1048  NH1 ARG A 160     -16.747  40.505  17.439  1.00 14.04           N  
ANISOU 1048  NH1 ARG A 160     1722   1781   1829      0    135    -17       N  
ATOM   1049  NH2 ARG A 160     -17.778  42.558  17.212  1.00 14.93           N  
ANISOU 1049  NH2 ARG A 160     1847   1917   1907     32    129    -18       N  
ATOM   1050  N   PRO A 161     -22.159  37.315  14.454  1.00 17.16           N  
ANISOU 1050  N   PRO A 161     2019   2273   2226    -23    114   -123       N  
ATOM   1051  CA  PRO A 161     -23.600  37.527  14.404  1.00 17.79           C  
ANISOU 1051  CA  PRO A 161     2076   2390   2293    -18    108   -143       C  
ATOM   1052  C   PRO A 161     -23.982  38.796  15.151  1.00 19.27           C  
ANISOU 1052  C   PRO A 161     2270   2590   2461      2    103   -128       C  
ATOM   1053  O   PRO A 161     -23.148  39.401  15.847  1.00 19.82           O  
ANISOU 1053  O   PRO A 161     2360   2637   2531      7    106   -103       O  
ATOM   1054  CB  PRO A 161     -24.162  36.327  15.167  1.00 17.45           C  
ANISOU 1054  CB  PRO A 161     2013   2342   2274    -51    119   -152       C  
ATOM   1055  CG  PRO A 161     -23.080  35.952  16.127  1.00 20.42           C  
ANISOU 1055  CG  PRO A 161     2409   2679   2670    -64    131   -125       C  
ATOM   1056  CD  PRO A 161     -21.774  36.299  15.454  1.00 16.42           C  
ANISOU 1056  CD  PRO A 161     1926   2153   2159    -50    128   -113       C  
ATOM   1057  N   TYR A 162     -25.247  39.168  15.013  1.00 17.91           N  
ANISOU 1057  N   TYR A 162     2078   2455   2271     14     95   -145       N  
ATOM   1058  CA  TYR A 162     -25.832  40.222  15.830  1.00 17.75           C  
ANISOU 1058  CA  TYR A 162     2059   2449   2234     32     91   -134       C  
ATOM   1059  C   TYR A 162     -27.126  39.666  16.415  1.00 18.62           C  
ANISOU 1059  C   TYR A 162     2138   2587   2349     16     92   -152       C  
ATOM   1060  O   TYR A 162     -27.601  38.611  15.972  1.00 17.31           O  
ANISOU 1060  O   TYR A 162     1950   2431   2196     -4     95   -177       O  
ATOM   1061  CB  TYR A 162     -26.043  41.504  15.015  1.00 17.88           C  
ANISOU 1061  CB  TYR A 162     2088   2488   2217     72     81   -135       C  
ATOM   1062  CG  TYR A 162     -27.110  41.444  13.939  1.00 18.53           C  
ANISOU 1062  CG  TYR A 162     2148   2613   2279     89     70   -165       C  
ATOM   1063  CD1 TYR A 162     -26.809  41.064  12.630  1.00 17.80           C  
ANISOU 1063  CD1 TYR A 162     2056   2525   2182     95     66   -180       C  
ATOM   1064  CD2 TYR A 162     -28.425  41.791  14.236  1.00 19.93           C  
ANISOU 1064  CD2 TYR A 162     2303   2831   2439    101     63   -179       C  
ATOM   1065  CE1 TYR A 162     -27.790  41.043  11.637  1.00 21.22           C  
ANISOU 1065  CE1 TYR A 162     2466   3002   2592    113     55   -210       C  
ATOM   1066  CE2 TYR A 162     -29.409  41.771  13.256  1.00 23.81           C  
ANISOU 1066  CE2 TYR A 162     2771   3368   2908    120     52   -209       C  
ATOM   1067  CZ  TYR A 162     -29.087  41.386  11.967  1.00 21.16           C  
ANISOU 1067  CZ  TYR A 162     2435   3036   2567    126     48   -225       C  
ATOM   1068  OH  TYR A 162     -30.102  41.376  11.039  1.00 24.74           O  
ANISOU 1068  OH  TYR A 162     2863   3541   2996    146     36   -257       O  
ATOM   1069  N   PHE A 163     -27.666  40.359  17.418  1.00 17.21           N  
ANISOU 1069  N   PHE A 163     1957   2418   2162     24     92   -141       N  
ATOM   1070  CA  PHE A 163     -28.829  39.895  18.167  1.00 16.98           C  
ANISOU 1070  CA  PHE A 163     1900   2412   2139      7     95   -155       C  
ATOM   1071  C   PHE A 163     -29.765  41.075  18.356  1.00 18.67           C  
ANISOU 1071  C   PHE A 163     2108   2662   2323     38     84   -157       C  
ATOM   1072  O   PHE A 163     -29.314  42.183  18.659  1.00 18.88           O  
ANISOU 1072  O   PHE A 163     2159   2678   2335     62     82   -134       O  
ATOM   1073  CB  PHE A 163     -28.427  39.270  19.512  1.00 15.16           C  
ANISOU 1073  CB  PHE A 163     1674   2151   1935    -20    110   -135       C  
ATOM   1074  CG  PHE A 163     -27.440  38.149  19.374  1.00 16.76           C  
ANISOU 1074  CG  PHE A 163     1886   2316   2163    -45    122   -130       C  
ATOM   1075  CD1 PHE A 163     -26.079  38.416  19.319  1.00 16.87           C  
ANISOU 1075  CD1 PHE A 163     1929   2299   2182    -37    123   -108       C  
ATOM   1076  CD2 PHE A 163     -27.869  36.830  19.276  1.00 19.86           C  
ANISOU 1076  CD2 PHE A 163     2260   2707   2577    -76    134   -150       C  
ATOM   1077  CE1 PHE A 163     -25.150  37.396  19.165  1.00 15.33           C  
ANISOU 1077  CE1 PHE A 163     1742   2072   2008    -57    133   -103       C  
ATOM   1078  CE2 PHE A 163     -26.943  35.799  19.131  1.00 19.18           C  
ANISOU 1078  CE2 PHE A 163     2186   2585   2514    -96    146   -145       C  
ATOM   1079  CZ  PHE A 163     -25.582  36.085  19.056  1.00 20.54           C  
ANISOU 1079  CZ  PHE A 163     2386   2728   2688    -85    144   -121       C  
ATOM   1080  N   VAL A 164     -31.049  40.831  18.102  1.00 17.40           N  
ANISOU 1080  N   VAL A 164     1914   2542   2152     37     79   -186       N  
ATOM   1081  CA  VAL A 164     -32.096  41.840  18.184  1.00 17.58           C  
ANISOU 1081  CA  VAL A 164     1926   2607   2144     68     68   -193       C  
ATOM   1082  C   VAL A 164     -33.093  41.393  19.239  1.00 17.53           C  
ANISOU 1082  C   VAL A 164     1893   2619   2149     46     75   -203       C  
ATOM   1083  O   VAL A 164     -33.329  40.194  19.409  1.00 17.52           O  
ANISOU 1083  O   VAL A 164     1871   2613   2171      9     86   -219       O  
ATOM   1084  CB  VAL A 164     -32.788  42.129  16.822  1.00 18.46           C  
ANISOU 1084  CB  VAL A 164     2023   2763   2227     97     54   -222       C  
ATOM   1085  CG1 VAL A 164     -31.811  42.828  15.883  1.00 18.42           C  
ANISOU 1085  CG1 VAL A 164     2052   2740   2207    127     49   -206       C  
ATOM   1086  CG2 VAL A 164     -33.274  40.850  16.154  1.00 22.07           C  
ANISOU 1086  CG2 VAL A 164     2447   3239   2698     69     56   -258       C  
ATOM   1087  N   GLY A 165     -33.620  42.357  19.987  1.00 17.26           N  
ANISOU 1087  N   GLY A 165     1860   2601   2096     67     70   -191       N  
ATOM   1088  CA  GLY A 165     -34.658  42.075  20.973  1.00 17.89           C  
ANISOU 1088  CA  GLY A 165     1913   2703   2181     50     75   -201       C  
ATOM   1089  C   GLY A 165     -35.127  43.354  21.639  1.00 18.46           C  
ANISOU 1089  C   GLY A 165     1992   2793   2227     83     68   -186       C  
ATOM   1090  O   GLY A 165     -34.806  44.466  21.203  1.00 16.29           O  
ANISOU 1090  O   GLY A 165     1742   2519   1928    121     59   -173       O  
ATOM   1091  N   LYS A 166     -35.897  43.190  22.711  1.00 18.88           N  
ANISOU 1091  N   LYS A 166     2026   2859   2286     68     74   -188       N  
ATOM   1092  CA  LYS A 166     -36.481  44.337  23.388  1.00 18.54           C  
ANISOU 1092  CA  LYS A 166     1986   2837   2218     98     67   -177       C  
ATOM   1093  C   LYS A 166     -36.456  44.157  24.907  1.00 18.61           C  
ANISOU 1093  C   LYS A 166     1996   2826   2246     76     79   -157       C  
ATOM   1094  O   LYS A 166     -37.354  44.627  25.626  1.00 18.34           O  
ANISOU 1094  O   LYS A 166     1948   2820   2199     85     77   -159       O  
ATOM   1095  CB  LYS A 166     -37.902  44.576  22.872  1.00 19.59           C  
ANISOU 1095  CB  LYS A 166     2085   3033   2324    119     55   -210       C  
ATOM   1096  CG  LYS A 166     -38.815  43.357  22.955  1.00 23.18           C  
ANISOU 1096  CG  LYS A 166     2496   3513   2795     80     63   -244       C  
ATOM   1097  CD  LYS A 166     -40.198  43.737  22.429  1.00 29.88           C  
ANISOU 1097  CD  LYS A 166     3308   4430   3612    105     50   -279       C  
ATOM   1098  CE  LYS A 166     -40.791  42.659  21.546  1.00 39.57           C  
ANISOU 1098  CE  LYS A 166     4498   5688   4846     80     51   -323       C  
ATOM   1099  NZ  LYS A 166     -40.152  42.717  20.193  1.00 45.89           N  
ANISOU 1099  NZ  LYS A 166     5313   6485   5637    100     41   -328       N  
ATOM   1100  N   GLY A 167     -35.418  43.480  25.397  1.00 17.55           N  
ANISOU 1100  N   GLY A 167     1880   2646   2141     48     92   -137       N  
ATOM   1101  CA  GLY A 167     -35.289  43.231  26.837  1.00 16.47           C  
ANISOU 1101  CA  GLY A 167     1747   2489   2022     28    104   -117       C  
ATOM   1102  C   GLY A 167     -35.363  44.543  27.603  1.00 15.56           C  
ANISOU 1102  C   GLY A 167     1646   2380   1886     58     97    -97       C  
ATOM   1103  O   GLY A 167     -34.650  45.495  27.292  1.00 15.27           O  
ANISOU 1103  O   GLY A 167     1637   2329   1836     84     90    -82       O  
ATOM   1104  N   SER A 168     -36.252  44.618  28.587  1.00 16.47           N  
ANISOU 1104  N   SER A 168     1743   2515   1997     54    101    -98       N  
ATOM   1105  CA  SER A 168     -36.451  45.852  29.345  1.00 15.75           C  
ANISOU 1105  CA  SER A 168     1664   2433   1886     83     94    -82       C  
ATOM   1106  C   SER A 168     -35.188  46.356  30.051  1.00 16.03           C  
ANISOU 1106  C   SER A 168     1733   2426   1928     87     99    -50       C  
ATOM   1107  O   SER A 168     -34.933  47.562  30.095  1.00 15.42           O  
ANISOU 1107  O   SER A 168     1678   2347   1831    116     92    -38       O  
ATOM   1108  CB  SER A 168     -37.608  45.693  30.344  1.00 16.94           C  
ANISOU 1108  CB  SER A 168     1787   2612   2035     74     99    -89       C  
ATOM   1109  OG  SER A 168     -38.838  45.535  29.652  1.00 17.27           O  
ANISOU 1109  OG  SER A 168     1796   2703   2063     78     92   -122       O  
ATOM   1110  N   ALA A 169     -34.380  45.447  30.590  1.00 15.35           N  
ANISOU 1110  N   ALA A 169     1654   2307   1870     58    111    -37       N  
ATOM   1111  CA  ALA A 169     -33.155  45.895  31.274  1.00 15.98           C  
ANISOU 1111  CA  ALA A 169     1762   2352   1955     62    115     -9       C  
ATOM   1112  C   ALA A 169     -32.169  46.531  30.292  1.00 15.45           C  
ANISOU 1112  C   ALA A 169     1722   2267   1881     79    108     -6       C  
ATOM   1113  O   ALA A 169     -31.663  47.650  30.484  1.00 15.49           O  
ANISOU 1113  O   ALA A 169     1750   2263   1872    100    105      6       O  
ATOM   1114  CB  ALA A 169     -32.514  44.721  32.005  1.00 14.89           C  
ANISOU 1114  CB  ALA A 169     1624   2186   1845     31    129      2       C  
ATOM   1115  N   VAL A 170     -31.897  45.828  29.198  1.00 15.14           N  
ANISOU 1115  N   VAL A 170     1680   2221   1850     69    108    -18       N  
ATOM   1116  CA  VAL A 170     -30.908  46.359  28.259  1.00 14.54           C  
ANISOU 1116  CA  VAL A 170     1629   2125   1767     83    104    -14       C  
ATOM   1117  C   VAL A 170     -31.420  47.605  27.529  1.00 13.87           C  
ANISOU 1117  C   VAL A 170     1553   2062   1652    119     93    -21       C  
ATOM   1118  O   VAL A 170     -30.695  48.592  27.367  1.00 12.11           O  
ANISOU 1118  O   VAL A 170     1359   1822   1418    138     93     -9       O  
ATOM   1119  CB  VAL A 170     -30.347  45.300  27.277  1.00 14.74           C  
ANISOU 1119  CB  VAL A 170     1652   2135   1810     64    106    -23       C  
ATOM   1120  CG1 VAL A 170     -31.405  44.840  26.285  1.00 13.84           C  
ANISOU 1120  CG1 VAL A 170     1514   2054   1690     65    100    -51       C  
ATOM   1121  CG2 VAL A 170     -29.114  45.867  26.560  1.00 13.75           C  
ANISOU 1121  CG2 VAL A 170     1557   1985   1682     76    105    -14       C  
ATOM   1122  N   VAL A 171     -32.677  47.575  27.097  1.00 13.33           N  
ANISOU 1122  N   VAL A 171     1461   2032   1568    130     86    -41       N  
ATOM   1123  CA  VAL A 171     -33.228  48.748  26.419  1.00 13.93           C  
ANISOU 1123  CA  VAL A 171     1547   2132   1612    170     77    -47       C  
ATOM   1124  C   VAL A 171     -33.357  49.922  27.408  1.00 13.74           C  
ANISOU 1124  C   VAL A 171     1539   2108   1573    191     78    -30       C  
ATOM   1125  O   VAL A 171     -33.096  51.081  27.063  1.00 13.64           O  
ANISOU 1125  O   VAL A 171     1554   2088   1539    221     77    -22       O  
ATOM   1126  CB  VAL A 171     -34.564  48.427  25.726  1.00 14.22           C  
ANISOU 1126  CB  VAL A 171     1551   2216   1633    180     67    -75       C  
ATOM   1127  CG1 VAL A 171     -35.148  49.695  25.121  1.00 15.45           C  
ANISOU 1127  CG1 VAL A 171     1719   2400   1751    228     58    -78       C  
ATOM   1128  CG2 VAL A 171     -34.351  47.370  24.626  1.00 13.98           C  
ANISOU 1128  CG2 VAL A 171     1509   2186   1616    162     67    -93       C  
ATOM   1129  N   GLY A 172     -33.754  49.624  28.639  1.00 13.50           N  
ANISOU 1129  N   GLY A 172     1492   2082   1553    174     82    -25       N  
ATOM   1130  CA  GLY A 172     -33.848  50.656  29.676  1.00 13.27           C  
ANISOU 1130  CA  GLY A 172     1477   2052   1512    190     83    -10       C  
ATOM   1131  C   GLY A 172     -32.497  51.290  29.975  1.00 12.42           C  
ANISOU 1131  C   GLY A 172     1404   1904   1410    190     91      9       C  
ATOM   1132  O   GLY A 172     -32.390  52.510  30.126  1.00 14.24           O  
ANISOU 1132  O   GLY A 172     1658   2129   1622    216     92     17       O  
ATOM   1133  N   GLN A 173     -31.442  50.484  30.045  1.00 12.33           N  
ANISOU 1133  N   GLN A 173     1396   1863   1424    163     97     16       N  
ATOM   1134  CA  GLN A 173     -30.093  51.032  30.246  1.00 12.27           C  
ANISOU 1134  CA  GLN A 173     1418   1820   1421    161    104     31       C  
ATOM   1135  C   GLN A 173     -29.630  51.904  29.087  1.00 12.76           C  
ANISOU 1135  C   GLN A 173     1509   1872   1468    184    105     29       C  
ATOM   1136  O   GLN A 173     -29.076  52.994  29.306  1.00 13.51           O  
ANISOU 1136  O   GLN A 173     1630   1948   1552    198    111     38       O  
ATOM   1137  CB  GLN A 173     -29.047  49.948  30.583  1.00 11.18           C  
ANISOU 1137  CB  GLN A 173     1277   1658   1313    130    110     38       C  
ATOM   1138  CG  GLN A 173     -27.669  50.483  31.057  1.00 11.89           C  
ANISOU 1138  CG  GLN A 173     1391   1717   1408    126    117     51       C  
ATOM   1139  CD  GLN A 173     -27.731  51.266  32.365  1.00 12.77           C  
ANISOU 1139  CD  GLN A 173     1507   1832   1513    132    120     60       C  
ATOM   1140  OE1 GLN A 173     -27.413  52.459  32.400  1.00 15.58           O  
ANISOU 1140  OE1 GLN A 173     1884   2179   1854    148    124     63       O  
ATOM   1141  NE2 GLN A 173     -28.129  50.599  33.449  1.00 11.53           N  
ANISOU 1141  NE2 GLN A 173     1329   1685   1365    119    121     66       N  
ATOM   1142  N   MET A 174     -29.856  51.439  27.857  1.00 11.58           N  
ANISOU 1142  N   MET A 174     1352   1730   1315    188    100     16       N  
ATOM   1143  CA  MET A 174     -29.627  52.277  26.683  1.00 12.33           C  
ANISOU 1143  CA  MET A 174     1474   1820   1391    216    100     14       C  
ATOM   1144  C   MET A 174     -30.377  53.600  26.787  1.00 13.30           C  
ANISOU 1144  C   MET A 174     1611   1958   1482    253    101     16       C  
ATOM   1145  O   MET A 174     -29.816  54.645  26.453  1.00 14.14           O  
ANISOU 1145  O   MET A 174     1752   2044   1575    272    110     24       O  
ATOM   1146  CB  MET A 174     -29.947  51.535  25.364  1.00 11.82           C  
ANISOU 1146  CB  MET A 174     1396   1771   1324    218     93     -1       C  
ATOM   1147  CG  MET A 174     -29.119  50.245  25.193  1.00 11.02           C  
ANISOU 1147  CG  MET A 174     1284   1650   1252    182     95     -3       C  
ATOM   1148  SD  MET A 174     -29.775  49.160  23.887  1.00 15.42           S  
ANISOU 1148  SD  MET A 174     1815   2232   1811    178     86    -27       S  
ATOM   1149  CE  MET A 174     -29.722  50.274  22.488  1.00 11.40           C  
ANISOU 1149  CE  MET A 174     1334   1728   1269    221     84    -29       C  
ATOM   1150  N   ALA A 175     -31.621  53.572  27.261  1.00 13.37           N  
ANISOU 1150  N   ALA A 175     1597   2002   1481    262     92      9       N  
ATOM   1151  CA  ALA A 175     -32.384  54.817  27.434  1.00 14.69           C  
ANISOU 1151  CA  ALA A 175     1777   2185   1617    300     92     12       C  
ATOM   1152  C   ALA A 175     -31.745  55.772  28.443  1.00 14.09           C  
ANISOU 1152  C   ALA A 175     1728   2082   1542    300    104     28       C  
ATOM   1153  O   ALA A 175     -31.669  56.979  28.205  1.00 13.43           O  
ANISOU 1153  O   ALA A 175     1677   1988   1437    330    112     34       O  
ATOM   1154  CB  ALA A 175     -33.852  54.542  27.838  1.00 13.40           C  
ANISOU 1154  CB  ALA A 175     1579   2068   1442    309     81      0       C  
ATOM   1155  N   ALA A 176     -31.318  55.231  29.580  1.00 14.14           N  
ANISOU 1155  N   ALA A 176     1721   2077   1572    269    106     34       N  
ATOM   1156  CA  ALA A 176     -30.677  56.042  30.619  1.00 13.65           C  
ANISOU 1156  CA  ALA A 176     1680   1993   1513    266    116     47       C  
ATOM   1157  C   ALA A 176     -29.407  56.706  30.102  1.00 13.17           C  
ANISOU 1157  C   ALA A 176     1655   1894   1453    266    129     52       C  
ATOM   1158  O   ALA A 176     -29.208  57.894  30.328  1.00 12.75           O  
ANISOU 1158  O   ALA A 176     1630   1826   1386    283    140     57       O  
ATOM   1159  CB  ALA A 176     -30.373  55.195  31.842  1.00 12.07           C  
ANISOU 1159  CB  ALA A 176     1457   1791   1338    233    115     52       C  
ATOM   1160  N   ALA A 177     -28.555  55.936  29.417  1.00 13.26           N  
ANISOU 1160  N   ALA A 177     1665   1888   1482    246    130     50       N  
ATOM   1161  CA  ALA A 177     -27.292  56.445  28.885  1.00 13.44           C  
ANISOU 1161  CA  ALA A 177     1720   1877   1509    242    144     53       C  
ATOM   1162  C   ALA A 177     -27.558  57.602  27.926  1.00 14.83           C  
ANISOU 1162  C   ALA A 177     1929   2048   1657    278    152     53       C  
ATOM   1163  O   ALA A 177     -26.882  58.630  27.982  1.00 14.74           O  
ANISOU 1163  O   ALA A 177     1950   2009   1639    283    169     57       O  
ATOM   1164  CB  ALA A 177     -26.524  55.330  28.152  1.00 13.36           C  
ANISOU 1164  CB  ALA A 177     1699   1856   1518    218    141     49       C  
ATOM   1165  N   LEU A 178     -28.561  57.434  27.064  1.00 12.88           N  
ANISOU 1165  N   LEU A 178     1673   1827   1392    303    142     47       N  
ATOM   1166  CA  LEU A 178     -28.896  58.476  26.097  1.00 14.12           C  
ANISOU 1166  CA  LEU A 178     1861   1983   1518    343    150     47       C  
ATOM   1167  C   LEU A 178     -29.556  59.679  26.775  1.00 14.36           C  
ANISOU 1167  C   LEU A 178     1910   2019   1526    372    157     53       C  
ATOM   1168  O   LEU A 178     -29.310  60.806  26.355  1.00 14.25           O  
ANISOU 1168  O   LEU A 178     1937   1984   1494    397    174     59       O  
ATOM   1169  CB  LEU A 178     -29.761  57.913  24.957  1.00 13.38           C  
ANISOU 1169  CB  LEU A 178     1751   1923   1410    365    136     37       C  
ATOM   1170  CG  LEU A 178     -28.958  57.033  23.987  1.00 13.61           C  
ANISOU 1170  CG  LEU A 178     1776   1938   1456    345    134     32       C  
ATOM   1171  CD1 LEU A 178     -29.841  56.092  23.183  1.00 14.86           C  
ANISOU 1171  CD1 LEU A 178     1902   2134   1608    351    117     17       C  
ATOM   1172  CD2 LEU A 178     -28.083  57.860  23.040  1.00 11.87           C  
ANISOU 1172  CD2 LEU A 178     1599   1685   1223    361    152     39       C  
ATOM   1173  N   ALA A 179     -30.323  59.454  27.843  1.00 13.22           N  
ANISOU 1173  N   ALA A 179     1738   1899   1384    366    146     52       N  
ATOM   1174  CA  ALA A 179     -30.922  60.571  28.594  1.00 15.22           C  
ANISOU 1174  CA  ALA A 179     2007   2157   1618    391    152     57       C  
ATOM   1175  C   ALA A 179     -29.884  61.474  29.269  1.00 16.12           C  
ANISOU 1175  C   ALA A 179     2154   2231   1740    379    173     65       C  
ATOM   1176  O   ALA A 179     -29.915  62.702  29.082  1.00 15.83           O  
ANISOU 1176  O   ALA A 179     2155   2177   1680    407    190     69       O  
ATOM   1177  CB  ALA A 179     -31.946  60.076  29.633  1.00 13.76           C  
ANISOU 1177  CB  ALA A 179     1783   2008   1435    385    137     54       C  
ATOM   1178  N   VAL A 180     -28.993  60.884  30.069  1.00 14.74           N  
ANISOU 1178  N   VAL A 180     1965   2041   1594    338    173     65       N  
ATOM   1179  CA  VAL A 180     -27.920  61.697  30.662  1.00 15.90           C  
ANISOU 1179  CA  VAL A 180     2139   2152   1748    324    193     68       C  
ATOM   1180  C   VAL A 180     -27.014  62.261  29.564  1.00 16.20           C  
ANISOU 1180  C   VAL A 180     2215   2156   1782    328    213     67       C  
ATOM   1181  O   VAL A 180     -26.618  63.435  29.620  1.00 15.11           O  
ANISOU 1181  O   VAL A 180     2115   1991   1634    338    235     69       O  
ATOM   1182  CB  VAL A 180     -27.111  60.980  31.788  1.00 16.04           C  
ANISOU 1182  CB  VAL A 180     2133   2166   1796    282    189     66       C  
ATOM   1183  CG1 VAL A 180     -26.378  59.750  31.269  1.00 12.30           C  
ANISOU 1183  CG1 VAL A 180     1640   1688   1344    255    182     64       C  
ATOM   1184  CG2 VAL A 180     -26.106  61.937  32.414  1.00 15.96           C  
ANISOU 1184  CG2 VAL A 180     2148   2125   1789    270    210     64       C  
ATOM   1185  N   GLY A 181     -26.701  61.440  28.561  1.00 14.93           N  
ANISOU 1185  N   GLY A 181     2047   1996   1630    321    206     65       N  
ATOM   1186  CA  GLY A 181     -25.948  61.919  27.400  1.00 15.37           C  
ANISOU 1186  CA  GLY A 181     2137   2021   1679    329    224     66       C  
ATOM   1187  C   GLY A 181     -26.564  63.170  26.782  1.00 16.06           C  
ANISOU 1187  C   GLY A 181     2265   2103   1733    374    239     71       C  
ATOM   1188  O   GLY A 181     -25.847  64.117  26.443  1.00 14.33           O  
ANISOU 1188  O   GLY A 181     2087   1848   1508    379    266     73       O  
ATOM   1189  N   SER A 182     -27.890  63.202  26.665  1.00 15.38           N  
ANISOU 1189  N   SER A 182     2167   2051   1624    409    225     72       N  
ATOM   1190  CA  SER A 182     -28.550  64.345  26.034  1.00 17.17           C  
ANISOU 1190  CA  SER A 182     2431   2276   1815    459    238     78       C  
ATOM   1191  C   SER A 182     -28.336  65.624  26.846  1.00 18.54           C  
ANISOU 1191  C   SER A 182     2640   2422   1981    465    262     82       C  
ATOM   1192  O   SER A 182     -28.232  66.712  26.272  1.00 20.39           O  
ANISOU 1192  O   SER A 182     2922   2630   2194    494    287     88       O  
ATOM   1193  CB  SER A 182     -30.048  64.099  25.831  1.00 16.68           C  
ANISOU 1193  CB  SER A 182     2345   2263   1728    495    216     75       C  
ATOM   1194  OG  SER A 182     -30.756  64.188  27.059  1.00 17.65           O  
ANISOU 1194  OG  SER A 182     2446   2407   1851    493    207     75       O  
ATOM   1195  N   ILE A 183     -28.290  65.498  28.170  1.00 18.04           N  
ANISOU 1195  N   ILE A 183     2555   2363   1935    438    256     80       N  
ATOM   1196  CA  ILE A 183     -28.077  66.653  29.046  1.00 18.21           C  
ANISOU 1196  CA  ILE A 183     2605   2361   1952    439    278     81       C  
ATOM   1197  C   ILE A 183     -26.650  67.176  28.894  1.00 18.80           C  
ANISOU 1197  C   ILE A 183     2713   2386   2041    412    307     78       C  
ATOM   1198  O   ILE A 183     -26.445  68.348  28.554  1.00 18.92           O  
ANISOU 1198  O   ILE A 183     2777   2369   2040    432    337     81       O  
ATOM   1199  CB  ILE A 183     -28.306  66.317  30.540  1.00 18.44           C  
ANISOU 1199  CB  ILE A 183     2599   2409   1996    415    263     78       C  
ATOM   1200  CG1 ILE A 183     -29.711  65.742  30.767  1.00 17.62           C  
ANISOU 1200  CG1 ILE A 183     2459   2354   1880    437    236     79       C  
ATOM   1201  CG2 ILE A 183     -28.012  67.550  31.427  1.00 16.57           C  
ANISOU 1201  CG2 ILE A 183     2393   2146   1755    415    287     77       C  
ATOM   1202  CD1 ILE A 183     -29.958  65.204  32.177  1.00 14.94           C  
ANISOU 1202  CD1 ILE A 183     2081   2036   1558    411    220     77       C  
ATOM   1203  N   VAL A 184     -25.668  66.306  29.125  1.00 16.94           N  
ANISOU 1203  N   VAL A 184     2452   2146   1836    368    300     71       N  
ATOM   1204  CA  VAL A 184     -24.270  66.752  29.185  1.00 16.47           C  
ANISOU 1204  CA  VAL A 184     2416   2046   1794    336    327     63       C  
ATOM   1205  C   VAL A 184     -23.635  67.087  27.845  1.00 17.40           C  
ANISOU 1205  C   VAL A 184     2571   2133   1905    344    349     65       C  
ATOM   1206  O   VAL A 184     -22.644  67.826  27.806  1.00 17.44           O  
ANISOU 1206  O   VAL A 184     2608   2100   1916    326    379     58       O  
ATOM   1207  CB  VAL A 184     -23.376  65.770  29.981  1.00 15.84           C  
ANISOU 1207  CB  VAL A 184     2297   1974   1746    288    313     54       C  
ATOM   1208  CG1 VAL A 184     -23.990  65.557  31.362  1.00 15.02           C  
ANISOU 1208  CG1 VAL A 184     2162   1898   1647    283    296     54       C  
ATOM   1209  CG2 VAL A 184     -23.211  64.431  29.244  1.00 11.02           C  
ANISOU 1209  CG2 VAL A 184     1658   1380   1149    277    292     56       C  
ATOM   1210  N   LEU A 185     -24.186  66.544  26.760  1.00 17.83           N  
ANISOU 1210  N   LEU A 185     2621   2205   1947    369    335     72       N  
ATOM   1211  CA  LEU A 185     -23.719  66.865  25.410  1.00 18.71           C  
ANISOU 1211  CA  LEU A 185     2769   2290   2048    384    355     75       C  
ATOM   1212  C   LEU A 185     -24.725  67.734  24.663  1.00 20.67           C  
ANISOU 1212  C   LEU A 185     3053   2540   2258    441    365     86       C  
ATOM   1213  O   LEU A 185     -24.585  67.938  23.463  1.00 21.78           O  
ANISOU 1213  O   LEU A 185     3224   2668   2384    464    378     92       O  
ATOM   1214  CB  LEU A 185     -23.405  65.588  24.606  1.00 19.05           C  
ANISOU 1214  CB  LEU A 185     2783   2349   2106    369    334     73       C  
ATOM   1215  CG  LEU A 185     -22.380  64.625  25.218  1.00 17.98           C  
ANISOU 1215  CG  LEU A 185     2611   2212   2005    317    323     64       C  
ATOM   1216  CD1 LEU A 185     -22.139  63.355  24.382  1.00 17.04           C  
ANISOU 1216  CD1 LEU A 185     2466   2108   1899    306    304     62       C  
ATOM   1217  CD2 LEU A 185     -21.055  65.357  25.392  1.00 19.12           C  
ANISOU 1217  CD2 LEU A 185     2785   2316   2163    288    355     56       C  
ATOM   1218  N   LYS A 186     -25.739  68.227  25.371  1.00 21.75           N  
ANISOU 1218  N   LYS A 186     3189   2696   2378    467    359     90       N  
ATOM   1219  CA  LYS A 186     -26.777  69.098  24.805  1.00 23.81           C  
ANISOU 1219  CA  LYS A 186     3484   2964   2599    527    368    100       C  
ATOM   1220  C   LYS A 186     -27.233  68.637  23.423  1.00 23.08           C  
ANISOU 1220  C   LYS A 186     3390   2891   2486    561    356    105       C  
ATOM   1221  O   LYS A 186     -27.088  69.352  22.431  1.00 21.93           O  
ANISOU 1221  O   LYS A 186     3291   2721   2317    593    381    113       O  
ATOM   1222  CB  LYS A 186     -26.283  70.544  24.746  1.00 25.95           C  
ANISOU 1222  CB  LYS A 186     3818   3184   2857    539    412    105       C  
ATOM   1223  CG  LYS A 186     -26.022  71.153  26.111  1.00 28.03           C  
ANISOU 1223  CG  LYS A 186     4084   3431   3134    513    425     98       C  
ATOM   1224  CD  LYS A 186     -25.106  72.362  25.980  1.00 38.69           C  
ANISOU 1224  CD  LYS A 186     5492   4722   4483    505    473     97       C  
ATOM   1225  CE  LYS A 186     -24.966  73.080  27.314  1.00 44.51           C  
ANISOU 1225  CE  LYS A 186     6235   5445   5229    485    487     88       C  
ATOM   1226  NZ  LYS A 186     -23.873  74.094  27.272  1.00 47.99           N  
ANISOU 1226  NZ  LYS A 186     6725   5829   5678    462    535     80       N  
ATOM   1227  N   ASN A 187     -27.768  67.423  23.364  1.00 21.43           N  
ANISOU 1227  N   ASN A 187     3129   2727   2286    553    320     99       N  
ATOM   1228  CA  ASN A 187     -28.041  66.771  22.098  1.00 21.38           C  
ANISOU 1228  CA  ASN A 187     3113   2742   2266    575    306     99       C  
ATOM   1229  C   ASN A 187     -29.475  66.252  22.046  1.00 21.72           C  
ANISOU 1229  C   ASN A 187     3118   2844   2290    607    275     94       C  
ATOM   1230  O   ASN A 187     -29.845  65.337  22.781  1.00 18.72           O  
ANISOU 1230  O   ASN A 187     2688   2493   1928    580    249     86       O  
ATOM   1231  CB  ASN A 187     -27.016  65.661  21.862  1.00 22.13           C  
ANISOU 1231  CB  ASN A 187     3182   2829   2397    525    297     91       C  
ATOM   1232  CG  ASN A 187     -27.144  65.029  20.485  1.00 22.69           C  
ANISOU 1232  CG  ASN A 187     3246   2916   2456    545    287     89       C  
ATOM   1233  OD1 ASN A 187     -28.218  64.576  20.099  1.00 23.35           O  
ANISOU 1233  OD1 ASN A 187     3304   3044   2521    574    263     85       O  
ATOM   1234  ND2 ASN A 187     -26.043  64.986  19.740  1.00 23.30           N  
ANISOU 1234  ND2 ASN A 187     3346   2960   2544    528    304     91       N  
ATOM   1235  N   ASP A 188     -30.281  66.857  21.179  1.00 21.31           N  
ANISOU 1235  N   ASP A 188     3090   2808   2197    666    279    100       N  
ATOM   1236  CA  ASP A 188     -31.694  66.508  21.105  1.00 24.13           C  
ANISOU 1236  CA  ASP A 188     3412   3225   2529    702    251     93       C  
ATOM   1237  C   ASP A 188     -31.941  65.137  20.473  1.00 22.19           C  
ANISOU 1237  C   ASP A 188     3116   3019   2294    687    221     78       C  
ATOM   1238  O   ASP A 188     -32.944  64.486  20.780  1.00 23.06           O  
ANISOU 1238  O   ASP A 188     3180   3179   2401    690    194     67       O  
ATOM   1239  CB  ASP A 188     -32.488  67.589  20.363  1.00 26.40           C  
ANISOU 1239  CB  ASP A 188     3741   3524   2767    775    264    102       C  
ATOM   1240  CG  ASP A 188     -33.968  67.527  20.690  1.00 36.17           C  
ANISOU 1240  CG  ASP A 188     4945   4821   3977    812    239     94       C  
ATOM   1241  OD1 ASP A 188     -34.311  67.629  21.892  1.00 44.30           O  
ANISOU 1241  OD1 ASP A 188     5957   5856   5018    795    233     93       O  
ATOM   1242  OD2 ASP A 188     -34.782  67.354  19.751  1.00 45.22           O  
ANISOU 1242  OD2 ASP A 188     6080   6009   5091    857    225     88       O  
ATOM   1243  N   THR A 189     -31.036  64.702  19.602  1.00 19.92           N  
ANISOU 1243  N   THR A 189     2838   2709   2020    669    227     78       N  
ATOM   1244  CA  THR A 189     -31.123  63.377  18.997  1.00 20.74           C  
ANISOU 1244  CA  THR A 189     2898   2844   2138    650    202     64       C  
ATOM   1245  C   THR A 189     -30.980  62.310  20.092  1.00 19.26           C  
ANISOU 1245  C   THR A 189     2661   2664   1991    592    184     55       C  
ATOM   1246  O   THR A 189     -31.783  61.367  20.152  1.00 17.34           O  
ANISOU 1246  O   THR A 189     2371   2466   1751    585    159     40       O  
ATOM   1247  CB  THR A 189     -30.051  63.169  17.901  1.00 20.65           C  
ANISOU 1247  CB  THR A 189     2909   2802   2135    640    215     67       C  
ATOM   1248  OG1 THR A 189     -30.279  64.086  16.827  1.00 24.87           O  
ANISOU 1248  OG1 THR A 189     3487   3332   2628    698    232     75       O  
ATOM   1249  CG2 THR A 189     -30.088  61.752  17.344  1.00 22.34           C  
ANISOU 1249  CG2 THR A 189     3077   3045   2366    616    190     51       C  
ATOM   1250  N   TYR A 190     -29.976  62.456  20.957  1.00 17.45           N  
ANISOU 1250  N   TYR A 190     2445   2394   1792    551    198     62       N  
ATOM   1251  CA  TYR A 190     -29.865  61.529  22.087  1.00 17.79           C  
ANISOU 1251  CA  TYR A 190     2444   2444   1868    502    183     56       C  
ATOM   1252  C   TYR A 190     -31.142  61.465  22.932  1.00 17.70           C  
ANISOU 1252  C   TYR A 190     2403   2475   1847    515    166     51       C  
ATOM   1253  O   TYR A 190     -31.590  60.378  23.315  1.00 18.61           O  
ANISOU 1253  O   TYR A 190     2472   2620   1980    490    146     40       O  
ATOM   1254  CB  TYR A 190     -28.653  61.830  22.982  1.00 18.69           C  
ANISOU 1254  CB  TYR A 190     2577   2513   2011    463    201     63       C  
ATOM   1255  CG  TYR A 190     -27.312  61.715  22.287  1.00 15.95           C  
ANISOU 1255  CG  TYR A 190     2251   2127   1679    441    217     65       C  
ATOM   1256  CD1 TYR A 190     -27.155  60.915  21.159  1.00 20.48           C  
ANISOU 1256  CD1 TYR A 190     2814   2710   2255    441    207     59       C  
ATOM   1257  CD2 TYR A 190     -26.202  62.400  22.770  1.00 15.76           C  
ANISOU 1257  CD2 TYR A 190     2258   2060   1669    419    241     70       C  
ATOM   1258  CE1 TYR A 190     -25.929  60.806  20.516  1.00 16.61           C  
ANISOU 1258  CE1 TYR A 190     2345   2186   1780    421    222     61       C  
ATOM   1259  CE2 TYR A 190     -24.966  62.298  22.140  1.00 16.45           C  
ANISOU 1259  CE2 TYR A 190     2363   2114   1770    397    256     70       C  
ATOM   1260  CZ  TYR A 190     -24.840  61.491  21.025  1.00 15.31           C  
ANISOU 1260  CZ  TYR A 190     2208   1979   1628    399    246     66       C  
ATOM   1261  OH  TYR A 190     -23.631  61.396  20.389  1.00 16.42           O  
ANISOU 1261  OH  TYR A 190     2366   2088   1781    378    261     65       O  
ATOM   1262  N   LEU A 191     -31.721  62.621  23.245  1.00 18.94           N  
ANISOU 1262  N   LEU A 191     2585   2633   1976    552    176     58       N  
ATOM   1263  CA  LEU A 191     -32.954  62.646  24.023  1.00 18.37           C  
ANISOU 1263  CA  LEU A 191     2484   2602   1890    568    161     53       C  
ATOM   1264  C   LEU A 191     -34.121  61.957  23.308  1.00 18.86           C  
ANISOU 1264  C   LEU A 191     2510   2721   1934    592    137     37       C  
ATOM   1265  O   LEU A 191     -34.869  61.207  23.930  1.00 17.84           O  
ANISOU 1265  O   LEU A 191     2335   2628   1814    575    119     26       O  
ATOM   1266  CB  LEU A 191     -33.326  64.081  24.415  1.00 19.57           C  
ANISOU 1266  CB  LEU A 191     2676   2743   2014    608    178     64       C  
ATOM   1267  CG  LEU A 191     -34.594  64.311  25.246  1.00 23.58           C  
ANISOU 1267  CG  LEU A 191     3161   3292   2504    629    164     60       C  
ATOM   1268  CD1 LEU A 191     -34.562  63.489  26.523  1.00 19.53           C  
ANISOU 1268  CD1 LEU A 191     2607   2787   2026    580    152     55       C  
ATOM   1269  CD2 LEU A 191     -34.782  65.779  25.637  1.00 23.73           C  
ANISOU 1269  CD2 LEU A 191     3226   3292   2497    667    185     73       C  
ATOM   1270  N   ARG A 192     -34.290  62.234  22.017  1.00 18.79           N  
ANISOU 1270  N   ARG A 192     2519   2722   1897    632    139     36       N  
ATOM   1271  CA  ARG A 192     -35.303  61.588  21.183  1.00 19.40           C  
ANISOU 1271  CA  ARG A 192     2561   2855   1954    656    118     17       C  
ATOM   1272  C   ARG A 192     -35.229  60.071  21.333  1.00 18.16           C  
ANISOU 1272  C   ARG A 192     2352   2714   1832    604    100      1       C  
ATOM   1273  O   ARG A 192     -36.242  59.405  21.597  1.00 16.28           O  
ANISOU 1273  O   ARG A 192     2068   2524   1593    600     81    -16       O  
ATOM   1274  CB  ARG A 192     -35.174  62.085  19.725  1.00 21.22           C  
ANISOU 1274  CB  ARG A 192     2825   3084   2153    703    126     20       C  
ATOM   1275  CG  ARG A 192     -35.982  61.419  18.589  1.00 27.45           C  
ANISOU 1275  CG  ARG A 192     3582   3928   2919    730    106      0       C  
ATOM   1276  CD  ARG A 192     -35.863  62.145  17.201  1.00 28.63           C  
ANISOU 1276  CD  ARG A 192     3773   4074   3029    787    117      6       C  
ATOM   1277  NE  ARG A 192     -35.444  61.284  16.077  1.00 29.28           N  
ANISOU 1277  NE  ARG A 192     3841   4163   3119    776    110     -5       N  
ATOM   1278  CZ  ARG A 192     -34.433  61.504  15.225  1.00 24.43           C  
ANISOU 1278  CZ  ARG A 192     3266   3509   2506    779    127      6       C  
ATOM   1279  NH1 ARG A 192     -33.661  62.589  15.239  1.00  7.60           N  
ANISOU 1279  NH1 ARG A 192     1193   1324    368    792    156     30       N  
ATOM   1280  NH2 ARG A 192     -34.186  60.599  14.284  1.00 35.61           N  
ANISOU 1280  NH2 ARG A 192     4661   4938   3929    767    116     -7       N  
ATOM   1281  N   TYR A 193     -34.022  59.522  21.206  1.00 17.42           N  
ANISOU 1281  N   TYR A 193     2266   2580   1771    563    107      6       N  
ATOM   1282  CA  TYR A 193     -33.832  58.082  21.274  1.00 17.00           C  
ANISOU 1282  CA  TYR A 193     2171   2536   1752    515     94     -7       C  
ATOM   1283  C   TYR A 193     -34.018  57.554  22.700  1.00 15.98           C  
ANISOU 1283  C   TYR A 193     2012   2409   1650    476     89     -7       C  
ATOM   1284  O   TYR A 193     -34.524  56.445  22.876  1.00 15.75           O  
ANISOU 1284  O   TYR A 193     1940   2407   1636    450     75    -23       O  
ATOM   1285  CB  TYR A 193     -32.502  57.663  20.627  1.00 15.96           C  
ANISOU 1285  CB  TYR A 193     2057   2362   1643    488    103     -1       C  
ATOM   1286  CG  TYR A 193     -32.631  57.611  19.113  1.00 18.55           C  
ANISOU 1286  CG  TYR A 193     2392   2707   1947    520    100    -10       C  
ATOM   1287  CD1 TYR A 193     -32.594  58.779  18.346  1.00 19.35           C  
ANISOU 1287  CD1 TYR A 193     2538   2799   2013    570    113      0       C  
ATOM   1288  CD2 TYR A 193     -32.862  56.403  18.457  1.00 20.17           C  
ANISOU 1288  CD2 TYR A 193     2561   2939   2163    503     84    -30       C  
ATOM   1289  CE1 TYR A 193     -32.753  58.745  16.955  1.00 23.97           C  
ANISOU 1289  CE1 TYR A 193     3129   3402   2573    604    110     -7       C  
ATOM   1290  CE2 TYR A 193     -33.028  56.345  17.066  1.00 20.94           C  
ANISOU 1290  CE2 TYR A 193     2661   3056   2237    534     80    -40       C  
ATOM   1291  CZ  TYR A 193     -32.961  57.524  16.331  1.00 25.59           C  
ANISOU 1291  CZ  TYR A 193     3294   3636   2790    586     92    -28       C  
ATOM   1292  OH  TYR A 193     -33.109  57.484  14.967  1.00 27.18           O  
ANISOU 1292  OH  TYR A 193     3501   3859   2967    620     88    -37       O  
ATOM   1293  N   ALA A 194     -33.627  58.341  23.699  1.00 16.87           N  
ANISOU 1293  N   ALA A 194     2148   2493   1766    472    101      8       N  
ATOM   1294  CA  ALA A 194     -33.821  57.967  25.095  1.00 16.23           C  
ANISOU 1294  CA  ALA A 194     2043   2416   1708    440     97     10       C  
ATOM   1295  C   ALA A 194     -35.311  57.744  25.357  1.00 17.94           C  
ANISOU 1295  C   ALA A 194     2222   2686   1906    457     81     -4       C  
ATOM   1296  O   ALA A 194     -35.680  56.735  25.968  1.00 16.54           O  
ANISOU 1296  O   ALA A 194     2006   2527   1751    424     72    -13       O  
ATOM   1297  CB  ALA A 194     -33.259  59.021  26.031  1.00 14.97           C  
ANISOU 1297  CB  ALA A 194     1917   2222   1549    441    113     27       C  
ATOM   1298  N   LYS A 195     -36.151  58.649  24.855  1.00 17.80           N  
ANISOU 1298  N   LYS A 195     2217   2695   1849    509     80     -6       N  
ATOM   1299  CA  LYS A 195     -37.606  58.558  25.050  1.00 19.52           C  
ANISOU 1299  CA  LYS A 195     2399   2971   2046    531     65    -22       C  
ATOM   1300  C   LYS A 195     -38.179  57.348  24.330  1.00 19.91           C  
ANISOU 1300  C   LYS A 195     2404   3060   2101    517     49    -48       C  
ATOM   1301  O   LYS A 195     -38.996  56.622  24.902  1.00 20.57           O  
ANISOU 1301  O   LYS A 195     2444   3177   2192    497     39    -63       O  
ATOM   1302  CB  LYS A 195     -38.333  59.818  24.575  1.00 19.94           C  
ANISOU 1302  CB  LYS A 195     2478   3046   2052    596     67    -20       C  
ATOM   1303  CG  LYS A 195     -38.032  61.062  25.388  1.00 20.47           C  
ANISOU 1303  CG  LYS A 195     2586   3080   2111    612     83      1       C  
ATOM   1304  CD  LYS A 195     -38.653  62.262  24.690  1.00 30.68           C  
ANISOU 1304  CD  LYS A 195     3911   4389   3355    680     88      4       C  
ATOM   1305  CE  LYS A 195     -38.523  63.534  25.512  1.00 34.98           C  
ANISOU 1305  CE  LYS A 195     4496   4904   3887    700    105     23       C  
ATOM   1306  NZ  LYS A 195     -38.886  64.736  24.690  1.00 38.66           N  
ANISOU 1306  NZ  LYS A 195     5005   5374   4307    768    117     31       N  
ATOM   1307  N   LYS A 196     -37.714  57.134  23.101  1.00 18.83           N  
ANISOU 1307  N   LYS A 196     2277   2916   1958    526     49    -52       N  
ATOM   1308  CA  LYS A 196     -38.119  55.995  22.281  1.00 20.25           C  
ANISOU 1308  CA  LYS A 196     2418   3130   2144    512     36    -78       C  
ATOM   1309  C   LYS A 196     -37.744  54.683  22.969  1.00 18.09           C  
ANISOU 1309  C   LYS A 196     2115   2842   1916    448     36    -83       C  
ATOM   1310  O   LYS A 196     -38.583  53.796  23.151  1.00 16.92           O  
ANISOU 1310  O   LYS A 196     1921   2730   1775    429     27   -106       O  
ATOM   1311  CB  LYS A 196     -37.500  56.098  20.884  1.00 20.14           C  
ANISOU 1311  CB  LYS A 196     2429   3105   2119    532     39    -78       C  
ATOM   1312  CG  LYS A 196     -37.910  55.009  19.919  1.00 28.81           C  
ANISOU 1312  CG  LYS A 196     3488   4238   3217    523     25   -107       C  
ATOM   1313  CD  LYS A 196     -36.977  54.933  18.716  1.00 34.75           C  
ANISOU 1313  CD  LYS A 196     4267   4965   3970    529     30   -103       C  
ATOM   1314  CE  LYS A 196     -37.082  56.171  17.849  1.00 38.61           C  
ANISOU 1314  CE  LYS A 196     4795   5459   4414    593     35    -93       C  
ATOM   1315  NZ  LYS A 196     -38.267  56.043  16.960  1.00 39.99           N  
ANISOU 1315  NZ  LYS A 196     4938   5701   4552    633     18   -120       N  
ATOM   1316  N   TYR A 197     -36.503  54.588  23.438  1.00 16.70           N  
ANISOU 1316  N   TYR A 197     1964   2612   1769    417     48    -63       N  
ATOM   1317  CA  TYR A 197     -36.083  53.385  24.134  1.00 14.95           C  
ANISOU 1317  CA  TYR A 197     1719   2373   1589    362     50    -64       C  
ATOM   1318  C   TYR A 197     -36.826  53.200  25.456  1.00 17.08           C  
ANISOU 1318  C   TYR A 197     1962   2660   1866    346     48    -65       C  
ATOM   1319  O   TYR A 197     -37.230  52.077  25.774  1.00 17.57           O  
ANISOU 1319  O   TYR A 197     1988   2737   1949    312     46    -79       O  
ATOM   1320  CB  TYR A 197     -34.561  53.330  24.308  1.00 14.65           C  
ANISOU 1320  CB  TYR A 197     1711   2277   1576    336     62    -44       C  
ATOM   1321  CG  TYR A 197     -33.755  53.214  23.019  1.00 15.09           C  
ANISOU 1321  CG  TYR A 197     1786   2314   1631    342     64    -45       C  
ATOM   1322  CD1 TYR A 197     -34.348  52.823  21.815  1.00 17.52           C  
ANISOU 1322  CD1 TYR A 197     2077   2656   1923    359     54    -66       C  
ATOM   1323  CD2 TYR A 197     -32.375  53.448  23.024  1.00 14.95           C  
ANISOU 1323  CD2 TYR A 197     1802   2247   1630    328     76    -27       C  
ATOM   1324  CE1 TYR A 197     -33.586  52.685  20.642  1.00 16.80           C  
ANISOU 1324  CE1 TYR A 197     2003   2546   1831    364     56    -67       C  
ATOM   1325  CE2 TYR A 197     -31.615  53.334  21.866  1.00 15.59           C  
ANISOU 1325  CE2 TYR A 197     1901   2310   1710    332     80    -28       C  
ATOM   1326  CZ  TYR A 197     -32.221  52.946  20.679  1.00 18.04           C  
ANISOU 1326  CZ  TYR A 197     2195   2653   2004    350     69    -47       C  
ATOM   1327  OH  TYR A 197     -31.439  52.801  19.551  1.00 15.12           O  
ANISOU 1327  OH  TYR A 197     1843   2265   1635    353     73    -47       O  
ATOM   1328  N   PHE A 198     -37.031  54.272  26.217  1.00 16.19           N  
ANISOU 1328  N   PHE A 198     1868   2546   1738    369     52    -51       N  
ATOM   1329  CA  PHE A 198     -37.731  54.103  27.489  1.00 17.91           C  
ANISOU 1329  CA  PHE A 198     2061   2780   1962    354     51    -51       C  
ATOM   1330  C   PHE A 198     -39.152  53.600  27.248  1.00 18.33           C  
ANISOU 1330  C   PHE A 198     2070   2892   2001    361     39    -79       C  
ATOM   1331  O   PHE A 198     -39.618  52.700  27.951  1.00 18.23           O  
ANISOU 1331  O   PHE A 198     2025   2893   2009    327     39    -88       O  
ATOM   1332  CB  PHE A 198     -37.803  55.388  28.314  1.00 16.80           C  
ANISOU 1332  CB  PHE A 198     1947   2632   1804    381     56    -34       C  
ATOM   1333  CG  PHE A 198     -38.629  55.240  29.558  1.00 20.17           C  
ANISOU 1333  CG  PHE A 198     2346   3081   2233    370     53    -35       C  
ATOM   1334  CD1 PHE A 198     -38.125  54.553  30.659  1.00 17.75           C  
ANISOU 1334  CD1 PHE A 198     2031   2751   1959    328     60    -25       C  
ATOM   1335  CD2 PHE A 198     -39.923  55.750  29.619  1.00 18.96           C  
ANISOU 1335  CD2 PHE A 198     2176   2976   2051    403     45    -48       C  
ATOM   1336  CE1 PHE A 198     -38.888  54.386  31.814  1.00 21.04           C  
ANISOU 1336  CE1 PHE A 198     2424   3189   2380    318     60    -26       C  
ATOM   1337  CE2 PHE A 198     -40.700  55.579  30.759  1.00 21.08           C  
ANISOU 1337  CE2 PHE A 198     2419   3267   2323    391     44    -50       C  
ATOM   1338  CZ  PHE A 198     -40.182  54.913  31.864  1.00 21.40           C  
ANISOU 1338  CZ  PHE A 198     2452   3281   2396    348     51    -39       C  
ATOM   1339  N   GLU A 199     -39.829  54.191  26.264  1.00 18.19           N  
ANISOU 1339  N   GLU A 199     2052   2909   1947    405     30    -92       N  
ATOM   1340  CA  GLU A 199     -41.188  53.775  25.932  1.00 20.50           C  
ANISOU 1340  CA  GLU A 199     2301   3265   2223    415     18   -123       C  
ATOM   1341  C   GLU A 199     -41.240  52.289  25.571  1.00 19.98           C  
ANISOU 1341  C   GLU A 199     2197   3207   2184    370     17   -146       C  
ATOM   1342  O   GLU A 199     -42.165  51.590  25.982  1.00 21.68           O  
ANISOU 1342  O   GLU A 199     2371   3459   2406    349     15   -168       O  
ATOM   1343  CB  GLU A 199     -41.790  54.652  24.825  1.00 21.40           C  
ANISOU 1343  CB  GLU A 199     2424   3416   2291    476      9   -133       C  
ATOM   1344  CG  GLU A 199     -43.261  54.344  24.558  1.00 32.27           C  
ANISOU 1344  CG  GLU A 199     3750   4865   3643    491     -4   -167       C  
ATOM   1345  CD  GLU A 199     -43.861  55.049  23.346  1.00 45.40           C  
ANISOU 1345  CD  GLU A 199     5417   6571   5259    553    -15   -181       C  
ATOM   1346  OE1 GLU A 199     -43.125  55.721  22.585  1.00 48.89           O  
ANISOU 1346  OE1 GLU A 199     5903   6986   5687    584    -10   -164       O  
ATOM   1347  OE2 GLU A 199     -45.092  54.923  23.154  1.00 49.59           O  
ANISOU 1347  OE2 GLU A 199     5908   7168   5766    572    -27   -211       O  
ATOM   1348  N   LEU A 200     -40.262  51.804  24.812  1.00 18.05           N  
ANISOU 1348  N   LEU A 200     1969   2931   1958    354     21   -142       N  
ATOM   1349  CA  LEU A 200     -40.204  50.392  24.441  1.00 18.09           C  
ANISOU 1349  CA  LEU A 200     1943   2937   1990    310     22   -163       C  
ATOM   1350  C   LEU A 200     -39.983  49.491  25.646  1.00 17.71           C  
ANISOU 1350  C   LEU A 200     1883   2864   1980    259     34   -156       C  
ATOM   1351  O   LEU A 200     -40.654  48.465  25.769  1.00 17.23           O  
ANISOU 1351  O   LEU A 200     1783   2826   1934    228     36   -179       O  
ATOM   1352  CB  LEU A 200     -39.119  50.127  23.392  1.00 17.64           C  
ANISOU 1352  CB  LEU A 200     1911   2848   1943    307     24   -158       C  
ATOM   1353  CG  LEU A 200     -38.824  48.687  22.948  1.00 20.96           C  
ANISOU 1353  CG  LEU A 200     2309   3260   2395    262     27   -176       C  
ATOM   1354  CD1 LEU A 200     -40.054  47.983  22.353  1.00 21.64           C  
ANISOU 1354  CD1 LEU A 200     2345   3404   2470    258     19   -218       C  
ATOM   1355  CD2 LEU A 200     -37.651  48.675  21.956  1.00 20.46           C  
ANISOU 1355  CD2 LEU A 200     2276   3161   2336    266     29   -166       C  
ATOM   1356  N   ALA A 201     -39.031  49.865  26.500  1.00 15.80           N  
ANISOU 1356  N   ALA A 201     1674   2576   1754    250     42   -124       N  
ATOM   1357  CA  ALA A 201     -38.700  49.084  27.696  1.00 16.70           C  
ANISOU 1357  CA  ALA A 201     1781   2663   1902    207     54   -112       C  
ATOM   1358  C   ALA A 201     -39.862  49.007  28.684  1.00 16.01           C  
ANISOU 1358  C   ALA A 201     1662   2609   1809    201     55   -121       C  
ATOM   1359  O   ALA A 201     -40.132  47.948  29.264  1.00 15.40           O  
ANISOU 1359  O   ALA A 201     1561   2532   1757    162     65   -129       O  
ATOM   1360  CB  ALA A 201     -37.469  49.677  28.391  1.00 13.42           C  
ANISOU 1360  CB  ALA A 201     1404   2197   1496    207     62    -79       C  
ATOM   1361  N   ASP A 202     -40.514  50.147  28.890  1.00 18.04           N  
ANISOU 1361  N   ASP A 202     1924   2893   2035    240     47   -119       N  
ATOM   1362  CA  ASP A 202     -41.630  50.255  29.830  1.00 19.47           C  
ANISOU 1362  CA  ASP A 202     2078   3109   2209    241     47   -127       C  
ATOM   1363  C   ASP A 202     -42.888  49.547  29.324  1.00 20.22           C  
ANISOU 1363  C   ASP A 202     2126   3260   2297    233     42   -165       C  
ATOM   1364  O   ASP A 202     -43.656  49.027  30.130  1.00 19.32           O  
ANISOU 1364  O   ASP A 202     1982   3166   2192    210     48   -176       O  
ATOM   1365  CB  ASP A 202     -41.952  51.722  30.121  1.00 20.55           C  
ANISOU 1365  CB  ASP A 202     2235   3259   2312    289     40   -114       C  
ATOM   1366  CG  ASP A 202     -42.889  51.895  31.308  1.00 23.01           C  
ANISOU 1366  CG  ASP A 202     2526   3598   2618    288     41   -115       C  
ATOM   1367  OD1 ASP A 202     -42.756  51.184  32.327  1.00 23.97           O  
ANISOU 1367  OD1 ASP A 202     2637   3702   2767    250     51   -107       O  
ATOM   1368  OD2 ASP A 202     -43.759  52.778  31.224  1.00 24.00           O  
ANISOU 1368  OD2 ASP A 202     2646   3762   2710    328     32   -123       O  
ATOM   1369  N   ALA A 203     -43.086  49.502  28.006  1.00 20.61           N  
ANISOU 1369  N   ALA A 203     2166   3333   2329    251     32   -187       N  
ATOM   1370  CA  ALA A 203     -44.223  48.778  27.435  1.00 21.50           C  
ANISOU 1370  CA  ALA A 203     2231   3501   2435    242     27   -229       C  
ATOM   1371  C   ALA A 203     -43.950  47.284  27.490  1.00 21.59           C  
ANISOU 1371  C   ALA A 203     2223   3491   2486    183     42   -241       C  
ATOM   1372  O   ALA A 203     -44.865  46.507  27.740  1.00 22.75           O  
ANISOU 1372  O   ALA A 203     2330   3671   2642    155     48   -269       O  
ATOM   1373  CB  ALA A 203     -44.505  49.210  25.986  1.00 22.38           C  
ANISOU 1373  CB  ALA A 203     2339   3649   2514    283     12   -249       C  
ATOM   1374  N   THR A 204     -42.695  46.886  27.294  1.00 20.14           N  
ANISOU 1374  N   THR A 204     2069   3253   2327    164     49   -221       N  
ATOM   1375  CA  THR A 204     -42.332  45.469  27.189  1.00 20.10           C  
ANISOU 1375  CA  THR A 204     2052   3224   2359    113     63   -232       C  
ATOM   1376  C   THR A 204     -42.368  44.760  28.550  1.00 20.29           C  
ANISOU 1376  C   THR A 204     2069   3225   2412     73     82   -219       C  
ATOM   1377  O   THR A 204     -42.904  43.649  28.673  1.00 19.67           O  
ANISOU 1377  O   THR A 204     1961   3156   2354     33     96   -243       O  
ATOM   1378  CB  THR A 204     -40.948  45.333  26.500  1.00 18.61           C  
ANISOU 1378  CB  THR A 204     1899   2987   2184    112     64   -213       C  
ATOM   1379  OG1 THR A 204     -41.038  45.918  25.194  1.00 18.92           O  
ANISOU 1379  OG1 THR A 204     1941   3052   2195    149     48   -227       O  
ATOM   1380  CG2 THR A 204     -40.512  43.877  26.375  1.00 16.66           C  
ANISOU 1380  CG2 THR A 204     1642   2712   1974     62     80   -222       C  
ATOM   1381  N   ARG A 205     -41.794  45.413  29.559  1.00 18.54           N  
ANISOU 1381  N   ARG A 205     1877   2974   2192     83     85   -184       N  
ATOM   1382  CA  ARG A 205     -41.750  44.873  30.923  1.00 18.57           C  
ANISOU 1382  CA  ARG A 205     1879   2955   2220     52    102   -167       C  
ATOM   1383  C   ARG A 205     -41.406  43.385  30.985  1.00 19.25           C  
ANISOU 1383  C   ARG A 205     1959   3013   2343      3    123   -173       C  
ATOM   1384  O   ARG A 205     -42.105  42.571  31.600  1.00 19.64           O  
ANISOU 1384  O   ARG A 205     1983   3071   2406    -28    139   -186       O  
ATOM   1385  CB  ARG A 205     -43.049  45.190  31.657  1.00 19.97           C  
ANISOU 1385  CB  ARG A 205     2027   3177   2381     58    102   -181       C  
ATOM   1386  CG  ARG A 205     -43.121  46.674  31.994  1.00 21.11           C  
ANISOU 1386  CG  ARG A 205     2191   3334   2496    105     86   -163       C  
ATOM   1387  CD  ARG A 205     -44.372  47.068  32.757  1.00 25.15           C  
ANISOU 1387  CD  ARG A 205     2675   3890   2989    114     85   -174       C  
ATOM   1388  NE  ARG A 205     -44.343  48.512  32.988  1.00 22.99           N  
ANISOU 1388  NE  ARG A 205     2424   3623   2686    162     71   -155       N  
ATOM   1389  CZ  ARG A 205     -45.112  49.161  33.856  1.00 25.53           C  
ANISOU 1389  CZ  ARG A 205     2736   3971   2991    179     69   -152       C  
ATOM   1390  NH1 ARG A 205     -46.001  48.499  34.587  1.00 23.36           N  
ANISOU 1390  NH1 ARG A 205     2428   3721   2726    152     79   -167       N  
ATOM   1391  NH2 ARG A 205     -44.988  50.477  33.987  1.00 24.51           N  
ANISOU 1391  NH2 ARG A 205     2634   3843   2836    222     58   -135       N  
ATOM   1392  N   SER A 206     -40.312  43.045  30.317  1.00 17.53           N  
ANISOU 1392  N   SER A 206     1763   2757   2137     -2    123   -164       N  
ATOM   1393  CA  SER A 206     -39.845  41.669  30.229  1.00 17.80           C  
ANISOU 1393  CA  SER A 206     1798   2761   2205    -43    143   -168       C  
ATOM   1394  C   SER A 206     -38.404  41.619  29.751  1.00 16.88           C  
ANISOU 1394  C   SER A 206     1716   2599   2099    -39    141   -146       C  
ATOM   1395  O   SER A 206     -37.994  42.379  28.860  1.00 16.65           O  
ANISOU 1395  O   SER A 206     1701   2573   2052    -10    124   -145       O  
ATOM   1396  CB  SER A 206     -40.733  40.837  29.292  1.00 17.11           C  
ANISOU 1396  CB  SER A 206     1674   2705   2120    -65    146   -212       C  
ATOM   1397  OG  SER A 206     -40.225  39.523  29.160  1.00 19.63           O  
ANISOU 1397  OG  SER A 206     1996   2989   2471   -105    167   -215       O  
ATOM   1398  N   ASP A 207     -37.658  40.698  30.351  1.00 17.29           N  
ANISOU 1398  N   ASP A 207     1782   2608   2179    -68    160   -128       N  
ATOM   1399  CA  ASP A 207     -36.318  40.352  29.882  1.00 18.97           C  
ANISOU 1399  CA  ASP A 207     2023   2779   2406    -71    161   -112       C  
ATOM   1400  C   ASP A 207     -36.268  39.088  29.019  1.00 20.08           C  
ANISOU 1400  C   ASP A 207     2153   2908   2566   -101    173   -135       C  
ATOM   1401  O   ASP A 207     -35.192  38.580  28.723  1.00 18.55           O  
ANISOU 1401  O   ASP A 207     1980   2677   2388   -109    179   -122       O  
ATOM   1402  CB  ASP A 207     -35.370  40.199  31.074  1.00 19.40           C  
ANISOU 1402  CB  ASP A 207     2103   2792   2474    -76    174    -76       C  
ATOM   1403  CG  ASP A 207     -34.919  41.551  31.630  1.00 19.93           C  
ANISOU 1403  CG  ASP A 207     2190   2860   2522    -42    159    -52       C  
ATOM   1404  OD1 ASP A 207     -34.773  42.499  30.830  1.00 20.53           O  
ANISOU 1404  OD1 ASP A 207     2274   2948   2578    -15    141    -56       O  
ATOM   1405  OD2 ASP A 207     -34.652  41.648  32.844  1.00 18.39           O  
ANISOU 1405  OD2 ASP A 207     2004   2651   2331    -43    167    -29       O  
ATOM   1406  N   SER A 208     -37.415  38.590  28.571  1.00 21.30           N  
ANISOU 1406  N   SER A 208     2273   3097   2720   -118    177   -171       N  
ATOM   1407  CA  SER A 208     -37.407  37.281  27.914  1.00 22.06           C  
ANISOU 1407  CA  SER A 208     2360   3181   2840   -153    194   -194       C  
ATOM   1408  C   SER A 208     -36.722  37.288  26.548  1.00 21.96           C  
ANISOU 1408  C   SER A 208     2356   3162   2824   -142    180   -203       C  
ATOM   1409  O   SER A 208     -36.234  36.250  26.108  1.00 23.19           O  
ANISOU 1409  O   SER A 208     2518   3291   3002   -168    194   -210       O  
ATOM   1410  CB  SER A 208     -38.819  36.701  27.815  1.00 22.53           C  
ANISOU 1410  CB  SER A 208     2377   3279   2901   -179    204   -235       C  
ATOM   1411  OG  SER A 208     -39.534  37.452  26.857  1.00 23.10           O  
ANISOU 1411  OG  SER A 208     2426   3403   2945   -154    180   -263       O  
ATOM   1412  N   THR A 209     -36.660  38.435  25.876  1.00 21.32           N  
ANISOU 1412  N   THR A 209     2279   3104   2715   -104    155   -203       N  
ATOM   1413  CA  THR A 209     -35.975  38.495  24.589  1.00 20.51           C  
ANISOU 1413  CA  THR A 209     2188   2995   2607    -91    143   -210       C  
ATOM   1414  C   THR A 209     -34.507  38.894  24.760  1.00 20.75           C  
ANISOU 1414  C   THR A 209     2259   2981   2642    -76    141   -172       C  
ATOM   1415  O   THR A 209     -33.832  39.176  23.768  1.00 19.33           O  
ANISOU 1415  O   THR A 209     2093   2794   2454    -60    130   -172       O  
ATOM   1416  CB  THR A 209     -36.640  39.478  23.586  1.00 21.78           C  
ANISOU 1416  CB  THR A 209     2335   3206   2734    -54    120   -231       C  
ATOM   1417  OG1 THR A 209     -36.576  40.817  24.108  1.00 20.43           O  
ANISOU 1417  OG1 THR A 209     2181   3041   2539    -17    107   -206       O  
ATOM   1418  CG2 THR A 209     -38.099  39.077  23.276  1.00 20.91           C  
ANISOU 1418  CG2 THR A 209     2180   3149   2616    -67    120   -275       C  
ATOM   1419  N   TYR A 210     -34.044  38.965  26.008  1.00 18.34           N  
ANISOU 1419  N   TYR A 210     1971   2649   2347    -81    151   -141       N  
ATOM   1420  CA  TYR A 210     -32.640  39.259  26.301  1.00 17.16           C  
ANISOU 1420  CA  TYR A 210     1856   2459   2203    -70    150   -108       C  
ATOM   1421  C   TYR A 210     -31.993  37.944  26.690  1.00 17.09           C  
ANISOU 1421  C   TYR A 210     1855   2411   2224   -102    172    -99       C  
ATOM   1422  O   TYR A 210     -32.083  37.536  27.848  1.00 18.03           O  
ANISOU 1422  O   TYR A 210     1976   2517   2355   -116    187    -85       O  
ATOM   1423  CB  TYR A 210     -32.506  40.258  27.461  1.00 15.20           C  
ANISOU 1423  CB  TYR A 210     1621   2209   1943    -51    147    -81       C  
ATOM   1424  CG  TYR A 210     -31.079  40.610  27.874  1.00 16.68           C  
ANISOU 1424  CG  TYR A 210     1841   2359   2135    -41    147    -51       C  
ATOM   1425  CD1 TYR A 210     -30.208  41.279  27.005  1.00 12.77           C  
ANISOU 1425  CD1 TYR A 210     1366   1855   1630    -22    135    -46       C  
ATOM   1426  CD2 TYR A 210     -30.610  40.295  29.153  1.00 14.06           C  
ANISOU 1426  CD2 TYR A 210     1519   2006   1817    -51    160    -27       C  
ATOM   1427  CE1 TYR A 210     -28.892  41.615  27.403  1.00 13.93           C  
ANISOU 1427  CE1 TYR A 210     1539   1970   1780    -15    137    -21       C  
ATOM   1428  CE2 TYR A 210     -29.308  40.602  29.545  1.00 13.09           C  
ANISOU 1428  CE2 TYR A 210     1422   1855   1696    -42    159     -2       C  
ATOM   1429  CZ  TYR A 210     -28.466  41.286  28.683  1.00 13.39           C  
ANISOU 1429  CZ  TYR A 210     1477   1885   1724    -25    148     -1       C  
ATOM   1430  OH  TYR A 210     -27.189  41.587  29.107  1.00 13.36           O  
ANISOU 1430  OH  TYR A 210     1495   1856   1723    -19    149     19       O  
ATOM   1431  N   THR A 211     -31.327  37.294  25.742  1.00 17.57           N  
ANISOU 1431  N   THR A 211     1925   2455   2297   -111    174   -107       N  
ATOM   1432  CA  THR A 211     -30.779  35.964  25.984  1.00 18.99           C  
ANISOU 1432  CA  THR A 211     2112   2598   2504   -140    196   -102       C  
ATOM   1433  C   THR A 211     -29.321  35.804  25.532  1.00 18.42           C  
ANISOU 1433  C   THR A 211     2068   2491   2439   -133    194    -84       C  
ATOM   1434  O   THR A 211     -28.581  34.994  26.100  1.00 17.21           O  
ANISOU 1434  O   THR A 211     1930   2304   2304   -146    211    -67       O  
ATOM   1435  CB  THR A 211     -31.643  34.890  25.296  1.00 20.16           C  
ANISOU 1435  CB  THR A 211     2235   2757   2665   -170    208   -137       C  
ATOM   1436  OG1 THR A 211     -31.664  35.155  23.891  1.00 19.27           O  
ANISOU 1436  OG1 THR A 211     2115   2664   2541   -159    191   -161       O  
ATOM   1437  CG2 THR A 211     -33.082  34.905  25.800  1.00 23.33           C  
ANISOU 1437  CG2 THR A 211     2606   3193   3062   -182    213   -158       C  
ATOM   1438  N   ALA A 212     -28.890  36.587  24.542  1.00 17.44           N  
ANISOU 1438  N   ALA A 212     1950   2376   2299   -111    175    -88       N  
ATOM   1439  CA  ALA A 212     -27.587  36.342  23.909  1.00 17.28           C  
ANISOU 1439  CA  ALA A 212     1952   2327   2286   -108    174    -78       C  
ATOM   1440  C   ALA A 212     -26.384  36.574  24.818  1.00 17.22           C  
ANISOU 1440  C   ALA A 212     1970   2291   2283    -99    177    -45       C  
ATOM   1441  O   ALA A 212     -25.317  36.044  24.544  1.00 17.04           O  
ANISOU 1441  O   ALA A 212     1962   2240   2270   -102    182    -36       O  
ATOM   1442  CB  ALA A 212     -27.431  37.137  22.605  1.00 16.63           C  
ANISOU 1442  CB  ALA A 212     1872   2261   2185    -86    155    -91       C  
ATOM   1443  N   ALA A 213     -26.549  37.318  25.909  1.00 16.63           N  
ANISOU 1443  N   ALA A 213     1896   2222   2198    -87    176    -28       N  
ATOM   1444  CA  ALA A 213     -25.468  37.563  26.869  1.00 17.57           C  
ANISOU 1444  CA  ALA A 213     2036   2320   2319    -79    179      0       C  
ATOM   1445  C   ALA A 213     -25.520  36.633  28.084  1.00 17.90           C  
ANISOU 1445  C   ALA A 213     2077   2346   2376    -94    199     14       C  
ATOM   1446  O   ALA A 213     -24.762  36.812  29.044  1.00 18.45           O  
ANISOU 1446  O   ALA A 213     2161   2404   2445    -84    202     37       O  
ATOM   1447  CB  ALA A 213     -25.518  39.037  27.344  1.00 17.52           C  
ANISOU 1447  CB  ALA A 213     2034   2331   2292    -55    165      9       C  
ATOM   1448  N   ASN A 214     -26.435  35.669  28.077  1.00 17.82           N  
ANISOU 1448  N   ASN A 214     2052   2337   2379   -116    213      0       N  
ATOM   1449  CA  ASN A 214     -26.636  34.821  29.253  1.00 19.73           C  
ANISOU 1449  CA  ASN A 214     2297   2565   2634   -130    235     13       C  
ATOM   1450  C   ASN A 214     -25.354  34.096  29.647  1.00 19.39           C  
ANISOU 1450  C   ASN A 214     2277   2488   2603   -128    248     36       C  
ATOM   1451  O   ASN A 214     -24.666  33.544  28.790  1.00 18.32           O  
ANISOU 1451  O   ASN A 214     2149   2334   2475   -132    249     31       O  
ATOM   1452  CB  ASN A 214     -27.783  33.829  29.040  1.00 20.14           C  
ANISOU 1452  CB  ASN A 214     2331   2621   2701   -159    253     -9       C  
ATOM   1453  CG  ASN A 214     -29.147  34.481  29.195  1.00 24.81           C  
ANISOU 1453  CG  ASN A 214     2897   3250   3280   -160    246    -26       C  
ATOM   1454  OD1 ASN A 214     -29.255  35.676  29.494  1.00 22.84           O  
ANISOU 1454  OD1 ASN A 214     2645   3021   3010   -138    228    -19       O  
ATOM   1455  ND2 ASN A 214     -30.202  33.697  28.984  1.00 22.76           N  
ANISOU 1455  ND2 ASN A 214     2616   2999   3030   -187    261    -51       N  
ATOM   1456  N   GLY A 215     -24.997  34.161  30.927  1.00 20.02           N  
ANISOU 1456  N   GLY A 215     2366   2560   2679   -118    255     61       N  
ATOM   1457  CA  GLY A 215     -23.716  33.613  31.378  1.00 18.86           C  
ANISOU 1457  CA  GLY A 215     2241   2388   2538   -108    265     83       C  
ATOM   1458  C   GLY A 215     -22.584  34.629  31.406  1.00 19.64           C  
ANISOU 1458  C   GLY A 215     2348   2492   2621    -84    245     94       C  
ATOM   1459  O   GLY A 215     -21.612  34.440  32.133  1.00 19.17           O  
ANISOU 1459  O   GLY A 215     2301   2421   2559    -71    250    114       O  
ATOM   1460  N   PHE A 216     -22.684  35.688  30.603  1.00 18.08           N  
ANISOU 1460  N   PHE A 216     2144   2312   2412    -77    224     81       N  
ATOM   1461  CA  PHE A 216     -21.710  36.780  30.629  1.00 15.62           C  
ANISOU 1461  CA  PHE A 216     1842   2006   2087    -58    208     88       C  
ATOM   1462  C   PHE A 216     -22.311  37.977  31.363  1.00 15.52           C  
ANISOU 1462  C   PHE A 216     1821   2016   2057    -46    198     90       C  
ATOM   1463  O   PHE A 216     -21.748  38.439  32.357  1.00 14.05           O  
ANISOU 1463  O   PHE A 216     1640   1833   1864    -34    197    106       O  
ATOM   1464  CB  PHE A 216     -21.298  37.177  29.211  1.00 15.99           C  
ANISOU 1464  CB  PHE A 216     1891   2052   2130    -56    195     72       C  
ATOM   1465  CG  PHE A 216     -20.787  36.021  28.388  1.00 18.23           C  
ANISOU 1465  CG  PHE A 216     2181   2315   2430    -67    204     67       C  
ATOM   1466  CD1 PHE A 216     -19.452  35.655  28.439  1.00 22.27           C  
ANISOU 1466  CD1 PHE A 216     2706   2809   2944    -60    207     79       C  
ATOM   1467  CD2 PHE A 216     -21.651  35.290  27.587  1.00 19.12           C  
ANISOU 1467  CD2 PHE A 216     2284   2427   2553    -85    210     49       C  
ATOM   1468  CE1 PHE A 216     -18.984  34.590  27.680  1.00 22.84           C  
ANISOU 1468  CE1 PHE A 216     2786   2862   3031    -70    216     74       C  
ATOM   1469  CE2 PHE A 216     -21.188  34.214  26.838  1.00 21.46           C  
ANISOU 1469  CE2 PHE A 216     2586   2702   2863    -96    219     43       C  
ATOM   1470  CZ  PHE A 216     -19.858  33.870  26.890  1.00 18.44           C  
ANISOU 1470  CZ  PHE A 216     2220   2300   2484    -88    222     57       C  
ATOM   1471  N   TYR A 217     -23.457  38.444  30.861  1.00 13.95           N  
ANISOU 1471  N   TYR A 217     1610   1836   1853    -50    191     74       N  
ATOM   1472  CA  TYR A 217     -24.212  39.547  31.439  1.00 14.39           C  
ANISOU 1472  CA  TYR A 217     1658   1915   1893    -39    182     74       C  
ATOM   1473  C   TYR A 217     -25.709  39.211  31.523  1.00 14.97           C  
ANISOU 1473  C   TYR A 217     1712   2006   1969    -51    187     62       C  
ATOM   1474  O   TYR A 217     -26.551  39.971  31.026  1.00 15.30           O  
ANISOU 1474  O   TYR A 217     1743   2070   1997    -44    176     47       O  
ATOM   1475  CB  TYR A 217     -23.956  40.852  30.655  1.00 13.04           C  
ANISOU 1475  CB  TYR A 217     1494   1754   1706    -23    166     66       C  
ATOM   1476  CG  TYR A 217     -22.521  41.342  30.788  1.00 12.51           C  
ANISOU 1476  CG  TYR A 217     1444   1673   1636    -13    163     77       C  
ATOM   1477  CD1 TYR A 217     -22.101  42.022  31.930  1.00 10.04           C  
ANISOU 1477  CD1 TYR A 217     1136   1364   1315     -2    163     90       C  
ATOM   1478  CD2 TYR A 217     -21.575  41.100  29.793  1.00 12.38           C  
ANISOU 1478  CD2 TYR A 217     1438   1641   1625    -14    162     73       C  
ATOM   1479  CE1 TYR A 217     -20.782  42.459  32.077  1.00 12.97           C  
ANISOU 1479  CE1 TYR A 217     1518   1726   1682      4    161     96       C  
ATOM   1480  CE2 TYR A 217     -20.243  41.529  29.935  1.00 11.37           C  
ANISOU 1480  CE2 TYR A 217     1323   1503   1494     -7    160     80       C  
ATOM   1481  CZ  TYR A 217     -19.860  42.221  31.069  1.00 15.00           C  
ANISOU 1481  CZ  TYR A 217     1784   1968   1944      1    160     90       C  
ATOM   1482  OH  TYR A 217     -18.561  42.655  31.247  1.00 12.83           O  
ANISOU 1482  OH  TYR A 217     1519   1687   1666      6    160     93       O  
ATOM   1483  N   SER A 218     -26.033  38.085  32.161  1.00 15.20           N  
ANISOU 1483  N   SER A 218     1737   2025   2013    -67    206     67       N  
ATOM   1484  CA  SER A 218     -27.431  37.731  32.431  1.00 15.93           C  
ANISOU 1484  CA  SER A 218     1809   2134   2108    -82    214     55       C  
ATOM   1485  C   SER A 218     -28.094  38.807  33.276  1.00 16.64           C  
ANISOU 1485  C   SER A 218     1892   2249   2181    -67    206     60       C  
ATOM   1486  O   SER A 218     -27.447  39.423  34.113  1.00 17.20           O  
ANISOU 1486  O   SER A 218     1974   2317   2243    -52    202     78       O  
ATOM   1487  CB  SER A 218     -27.514  36.416  33.216  1.00 16.17           C  
ANISOU 1487  CB  SER A 218     1843   2144   2157   -100    241     65       C  
ATOM   1488  OG  SER A 218     -27.090  35.349  32.394  1.00 18.63           O  
ANISOU 1488  OG  SER A 218     2160   2432   2485   -116    251     58       O  
ATOM   1489  N   SER A 219     -29.392  39.014  33.093  1.00 17.51           N  
ANISOU 1489  N   SER A 219     1981   2385   2284    -73    203     42       N  
ATOM   1490  CA  SER A 219     -30.088  39.973  33.928  1.00 18.65           C  
ANISOU 1490  CA  SER A 219     2117   2553   2413    -58    196     46       C  
ATOM   1491  C   SER A 219     -30.380  39.241  35.239  1.00 20.04           C  
ANISOU 1491  C   SER A 219     2290   2722   2598    -71    216     61       C  
ATOM   1492  O   SER A 219     -31.178  38.307  35.262  1.00 21.38           O  
ANISOU 1492  O   SER A 219     2447   2893   2781    -93    232     50       O  
ATOM   1493  CB  SER A 219     -31.378  40.411  33.236  1.00 18.05           C  
ANISOU 1493  CB  SER A 219     2019   2512   2325    -57    186     20       C  
ATOM   1494  OG  SER A 219     -32.109  41.312  34.050  1.00 19.85           O  
ANISOU 1494  OG  SER A 219     2239   2764   2536    -43    180     24       O  
ATOM   1495  N   HIS A 220     -29.720  39.628  36.322  1.00 18.81           N  
ANISOU 1495  N   HIS A 220     2149   2560   2438    -56    216     84       N  
ATOM   1496  CA  HIS A 220     -29.872  38.930  37.601  1.00 19.64           C  
ANISOU 1496  CA  HIS A 220     2254   2656   2550    -63    236    102       C  
ATOM   1497  C   HIS A 220     -30.975  39.582  38.438  1.00 19.56           C  
ANISOU 1497  C   HIS A 220     2228   2674   2527    -58    234    100       C  
ATOM   1498  O   HIS A 220     -31.871  38.915  38.954  1.00 18.49           O  
ANISOU 1498  O   HIS A 220     2081   2544   2400    -74    252     98       O  
ATOM   1499  CB  HIS A 220     -28.532  38.918  38.354  1.00 19.14           C  
ANISOU 1499  CB  HIS A 220     2212   2574   2486    -48    238    127       C  
ATOM   1500  CG  HIS A 220     -27.450  38.161  37.647  1.00 23.32           C  
ANISOU 1500  CG  HIS A 220     2756   3077   3028    -53    243    129       C  
ATOM   1501  ND1 HIS A 220     -27.149  36.845  37.933  1.00 23.48           N  
ANISOU 1501  ND1 HIS A 220     2785   3071   3063    -64    266    140       N  
ATOM   1502  CD2 HIS A 220     -26.592  38.537  36.667  1.00 23.31           C  
ANISOU 1502  CD2 HIS A 220     2763   3068   3024    -46    228    123       C  
ATOM   1503  CE1 HIS A 220     -26.159  36.440  37.154  1.00 24.52           C  
ANISOU 1503  CE1 HIS A 220     2929   3183   3201    -64    264    140       C  
ATOM   1504  NE2 HIS A 220     -25.798  37.451  36.382  1.00 28.25           N  
ANISOU 1504  NE2 HIS A 220     3400   3668   3664    -54    241    129       N  
ATOM   1505  N   SER A 221     -30.937  40.906  38.532  1.00 17.58           N  
ANISOU 1505  N   SER A 221     1979   2442   2258    -36    214    101       N  
ATOM   1506  CA  SER A 221     -31.890  41.652  39.341  1.00 17.28           C  
ANISOU 1506  CA  SER A 221     1928   2431   2206    -27    210    101       C  
ATOM   1507  C   SER A 221     -33.266  41.851  38.702  1.00 18.11           C  
ANISOU 1507  C   SER A 221     2010   2565   2305    -33    205     75       C  
ATOM   1508  O   SER A 221     -34.188  42.294  39.379  1.00 19.32           O  
ANISOU 1508  O   SER A 221     2150   2743   2448    -28    205     73       O  
ATOM   1509  CB  SER A 221     -31.294  43.019  39.708  1.00 15.93           C  
ANISOU 1509  CB  SER A 221     1769   2266   2016      0    193    110       C  
ATOM   1510  OG  SER A 221     -30.822  43.699  38.545  1.00 15.85           O  
ANISOU 1510  OG  SER A 221     1767   2254   1999      8    177     99       O  
ATOM   1511  N   GLY A 222     -33.419  41.555  37.413  1.00 19.56           N  
ANISOU 1511  N   GLY A 222     2187   2750   2492    -42    201     55       N  
ATOM   1512  CA  GLY A 222     -34.635  41.945  36.705  1.00 18.11           C  
ANISOU 1512  CA  GLY A 222     1981   2602   2298    -41    191     28       C  
ATOM   1513  C   GLY A 222     -34.523  43.354  36.138  1.00 18.51           C  
ANISOU 1513  C   GLY A 222     2039   2667   2325    -10    168     25       C  
ATOM   1514  O   GLY A 222     -33.450  43.972  36.168  1.00 19.58           O  
ANISOU 1514  O   GLY A 222     2198   2784   2456      5    161     41       O  
ATOM   1515  N   PHE A 223     -35.637  43.879  35.634  1.00 17.80           N  
ANISOU 1515  N   PHE A 223     1930   2614   2219      0    158      4       N  
ATOM   1516  CA  PHE A 223     -35.598  45.109  34.838  1.00 16.55           C  
ANISOU 1516  CA  PHE A 223     1781   2470   2037     30    138     -1       C  
ATOM   1517  C   PHE A 223     -36.177  46.336  35.543  1.00 16.84           C  
ANISOU 1517  C   PHE A 223     1818   2529   2050     57    129      4       C  
ATOM   1518  O   PHE A 223     -36.076  47.448  35.009  1.00 16.06           O  
ANISOU 1518  O   PHE A 223     1733   2438   1931     86    116      3       O  
ATOM   1519  CB  PHE A 223     -36.325  44.900  33.505  1.00 15.34           C  
ANISOU 1519  CB  PHE A 223     1609   2341   1877     31    131    -31       C  
ATOM   1520  CG  PHE A 223     -37.773  44.518  33.692  1.00 16.01           C  
ANISOU 1520  CG  PHE A 223     1659   2465   1958     20    135    -53       C  
ATOM   1521  CD1 PHE A 223     -38.723  45.476  34.016  1.00 17.80           C  
ANISOU 1521  CD1 PHE A 223     1874   2728   2160     44    124    -59       C  
ATOM   1522  CD2 PHE A 223     -38.162  43.187  33.609  1.00 17.22           C  
ANISOU 1522  CD2 PHE A 223     1791   2616   2133    -15    150    -69       C  
ATOM   1523  CE1 PHE A 223     -40.059  45.121  34.240  1.00 20.10           C  
ANISOU 1523  CE1 PHE A 223     2131   3058   2447     34    128    -82       C  
ATOM   1524  CE2 PHE A 223     -39.491  42.820  33.824  1.00 22.65           C  
ANISOU 1524  CE2 PHE A 223     2445   3340   2818    -29    157    -93       C  
ATOM   1525  CZ  PHE A 223     -40.441  43.798  34.129  1.00 20.44           C  
ANISOU 1525  CZ  PHE A 223     2151   3101   2513     -4    145   -100       C  
ATOM   1526  N   TRP A 224     -36.769  46.168  36.726  1.00 15.54           N  
ANISOU 1526  N   TRP A 224     1640   2374   1887     49    138     10       N  
ATOM   1527  CA  TRP A 224     -37.435  47.297  37.369  1.00 15.89           C  
ANISOU 1527  CA  TRP A 224     1683   2445   1909     75    129     13       C  
ATOM   1528  C   TRP A 224     -36.428  48.373  37.762  1.00 16.39           C  
ANISOU 1528  C   TRP A 224     1776   2486   1963     97    123     33       C  
ATOM   1529  O   TRP A 224     -36.734  49.570  37.707  1.00 14.97           O  
ANISOU 1529  O   TRP A 224     1604   2321   1760    125    113     32       O  
ATOM   1530  CB  TRP A 224     -38.300  46.888  38.573  1.00 16.16           C  
ANISOU 1530  CB  TRP A 224     1696   2496   1948     61    140     15       C  
ATOM   1531  CG  TRP A 224     -39.451  45.980  38.231  1.00 19.95           C  
ANISOU 1531  CG  TRP A 224     2143   3002   2434     39    148     -9       C  
ATOM   1532  CD1 TRP A 224     -39.537  44.642  38.476  1.00 19.38           C  
ANISOU 1532  CD1 TRP A 224     2059   2917   2386      4    168    -12       C  
ATOM   1533  CD2 TRP A 224     -40.667  46.345  37.557  1.00 22.34           C  
ANISOU 1533  CD2 TRP A 224     2420   3350   2717     51    137    -37       C  
ATOM   1534  NE1 TRP A 224     -40.729  44.152  38.002  1.00 26.27           N  
ANISOU 1534  NE1 TRP A 224     2900   3823   3259    -10    171    -42       N  
ATOM   1535  CE2 TRP A 224     -41.445  45.173  37.436  1.00 20.77           C  
ANISOU 1535  CE2 TRP A 224     2191   3165   2534     18    152    -59       C  
ATOM   1536  CE3 TRP A 224     -41.168  47.546  37.040  1.00 23.42           C  
ANISOU 1536  CE3 TRP A 224     2556   3517   2824     88    119    -46       C  
ATOM   1537  CZ2 TRP A 224     -42.703  45.161  36.824  1.00 24.94           C  
ANISOU 1537  CZ2 TRP A 224     2685   3740   3049     20    146    -92       C  
ATOM   1538  CZ3 TRP A 224     -42.434  47.545  36.442  1.00 22.67           C  
ANISOU 1538  CZ3 TRP A 224     2429   3469   2713     94    112    -77       C  
ATOM   1539  CH2 TRP A 224     -43.178  46.351  36.330  1.00 22.67           C  
ANISOU 1539  CH2 TRP A 224     2396   3486   2729     59    125   -101       C  
ATOM   1540  N   ASP A 225     -35.213  47.964  38.120  1.00 15.66           N  
ANISOU 1540  N   ASP A 225     1702   2360   1888     84    131     51       N  
ATOM   1541  CA  ASP A 225     -34.205  48.980  38.421  1.00 16.63           C  
ANISOU 1541  CA  ASP A 225     1852   2464   2003    102    126     65       C  
ATOM   1542  C   ASP A 225     -33.780  49.792  37.193  1.00 15.46           C  
ANISOU 1542  C   ASP A 225     1723   2309   1842    121    117     58       C  
ATOM   1543  O   ASP A 225     -33.521  50.989  37.306  1.00 15.07           O  
ANISOU 1543  O   ASP A 225     1692   2257   1776    143    112     63       O  
ATOM   1544  CB  ASP A 225     -32.982  48.379  39.119  1.00 16.61           C  
ANISOU 1544  CB  ASP A 225     1861   2431   2018     87    135     83       C  
ATOM   1545  CG  ASP A 225     -32.407  47.217  38.346  1.00 17.79           C  
ANISOU 1545  CG  ASP A 225     2010   2560   2187     66    141     80       C  
ATOM   1546  OD1 ASP A 225     -33.030  46.139  38.355  1.00 20.52           O  
ANISOU 1546  OD1 ASP A 225     2338   2911   2545     46    151     74       O  
ATOM   1547  OD2 ASP A 225     -31.355  47.390  37.705  1.00 20.01           O  
ANISOU 1547  OD2 ASP A 225     2310   2821   2472     68    139     82       O  
ATOM   1548  N   GLU A 226     -33.686  49.165  36.026  1.00 15.18           N  
ANISOU 1548  N   GLU A 226     1684   2269   1814    112    115     46       N  
ATOM   1549  CA  GLU A 226     -33.359  49.908  34.806  1.00 14.64           C  
ANISOU 1549  CA  GLU A 226     1632   2196   1731    132    108     39       C  
ATOM   1550  C   GLU A 226     -34.478  50.871  34.416  1.00 15.23           C  
ANISOU 1550  C   GLU A 226     1704   2304   1779    162     98     27       C  
ATOM   1551  O   GLU A 226     -34.204  51.959  33.922  1.00 15.87           O  
ANISOU 1551  O   GLU A 226     1808   2380   1842    187     95     29       O  
ATOM   1552  CB  GLU A 226     -33.028  49.001  33.606  1.00 15.02           C  
ANISOU 1552  CB  GLU A 226     1677   2235   1792    117    108     28       C  
ATOM   1553  CG  GLU A 226     -31.657  48.326  33.681  1.00 15.67           C  
ANISOU 1553  CG  GLU A 226     1774   2281   1897     97    115     40       C  
ATOM   1554  CD  GLU A 226     -31.659  47.040  34.508  1.00 15.98           C  
ANISOU 1554  CD  GLU A 226     1797   2313   1959     69    126     46       C  
ATOM   1555  OE1 GLU A 226     -32.731  46.666  35.005  1.00 19.46           O  
ANISOU 1555  OE1 GLU A 226     2216   2776   2400     62    129     40       O  
ATOM   1556  OE2 GLU A 226     -30.610  46.383  34.690  1.00 16.86           O  
ANISOU 1556  OE2 GLU A 226     1918   2398   2087     54    133     57       O  
ATOM   1557  N   LEU A 227     -35.738  50.485  34.607  1.00 16.24           N  
ANISOU 1557  N   LEU A 227     1802   2465   1901    159     96     14       N  
ATOM   1558  CA  LEU A 227     -36.831  51.422  34.321  1.00 17.07           C  
ANISOU 1558  CA  LEU A 227     1902   2607   1978    192     87      3       C  
ATOM   1559  C   LEU A 227     -36.765  52.599  35.292  1.00 16.66           C  
ANISOU 1559  C   LEU A 227     1868   2551   1911    213     87     18       C  
ATOM   1560  O   LEU A 227     -37.025  53.742  34.905  1.00 18.57           O  
ANISOU 1560  O   LEU A 227     2126   2801   2127    247     82     17       O  
ATOM   1561  CB  LEU A 227     -38.203  50.743  34.417  1.00 15.43           C  
ANISOU 1561  CB  LEU A 227     1654   2440   1767    183     85    -16       C  
ATOM   1562  CG  LEU A 227     -38.504  49.624  33.408  1.00 19.75           C  
ANISOU 1562  CG  LEU A 227     2178   2998   2325    163     85    -38       C  
ATOM   1563  CD1 LEU A 227     -39.962  49.156  33.534  1.00 15.26           C  
ANISOU 1563  CD1 LEU A 227     1569   2477   1751    156     84    -62       C  
ATOM   1564  CD2 LEU A 227     -38.244  50.116  31.979  1.00 16.12           C  
ANISOU 1564  CD2 LEU A 227     1733   2540   1849    188     75    -47       C  
ATOM   1565  N   LEU A 228     -36.451  52.306  36.550  1.00 14.92           N  
ANISOU 1565  N   LEU A 228     1644   2318   1705    194     94     32       N  
ATOM   1566  CA  LEU A 228     -36.242  53.346  37.575  1.00 16.44           C  
ANISOU 1566  CA  LEU A 228     1854   2504   1887    210     96     46       C  
ATOM   1567  C   LEU A 228     -35.083  54.303  37.224  1.00 15.18           C  
ANISOU 1567  C   LEU A 228     1731   2312   1722    223     98     55       C  
ATOM   1568  O   LEU A 228     -35.206  55.524  37.302  1.00 15.04           O  
ANISOU 1568  O   LEU A 228     1734   2295   1684    250     98     57       O  
ATOM   1569  CB  LEU A 228     -35.977  52.699  38.943  1.00 16.28           C  
ANISOU 1569  CB  LEU A 228     1824   2476   1886    186    104     59       C  
ATOM   1570  CG  LEU A 228     -35.602  53.670  40.075  1.00 18.46           C  
ANISOU 1570  CG  LEU A 228     2116   2744   2153    198    106     73       C  
ATOM   1571  CD1 LEU A 228     -36.777  54.616  40.328  1.00 21.53           C  
ANISOU 1571  CD1 LEU A 228     2499   3163   2516    226    100     67       C  
ATOM   1572  CD2 LEU A 228     -35.215  52.951  41.368  1.00 18.03           C  
ANISOU 1572  CD2 LEU A 228     2052   2681   2116    176    114     86       C  
ATOM   1573  N   TRP A 229     -33.954  53.739  36.811  1.00 14.40           N  
ANISOU 1573  N   TRP A 229     1644   2185   1643    204    103     59       N  
ATOM   1574  CA  TRP A 229     -32.780  54.520  36.388  1.00 13.69           C  
ANISOU 1574  CA  TRP A 229     1586   2063   1550    211    107     65       C  
ATOM   1575  C   TRP A 229     -33.063  55.366  35.149  1.00 14.84           C  
ANISOU 1575  C   TRP A 229     1751   2212   1674    240    104     57       C  
ATOM   1576  O   TRP A 229     -32.782  56.570  35.151  1.00 15.03           O  
ANISOU 1576  O   TRP A 229     1803   2224   1683    261    110     61       O  
ATOM   1577  CB  TRP A 229     -31.638  53.523  36.156  1.00 11.64           C  
ANISOU 1577  CB  TRP A 229     1327   1777   1316    183    112     68       C  
ATOM   1578  CG  TRP A 229     -30.267  53.958  35.695  1.00 13.07           C  
ANISOU 1578  CG  TRP A 229     1536   1927   1502    181    117     72       C  
ATOM   1579  CD1 TRP A 229     -29.639  53.516  34.568  1.00 11.52           C  
ANISOU 1579  CD1 TRP A 229     1347   1714   1313    174    118     68       C  
ATOM   1580  CD2 TRP A 229     -29.298  54.759  36.394  1.00 13.94           C  
ANISOU 1580  CD2 TRP A 229     1666   2016   1611    180    125     79       C  
ATOM   1581  NE1 TRP A 229     -28.369  54.027  34.482  1.00 13.40           N  
ANISOU 1581  NE1 TRP A 229     1610   1925   1556    170    126     71       N  
ATOM   1582  CE2 TRP A 229     -28.126  54.777  35.604  1.00 14.96           C  
ANISOU 1582  CE2 TRP A 229     1815   2120   1750    173    130     77       C  
ATOM   1583  CE3 TRP A 229     -29.299  55.448  37.615  1.00 12.85           C  
ANISOU 1583  CE3 TRP A 229     1531   1881   1467    185    128     84       C  
ATOM   1584  CZ2 TRP A 229     -26.978  55.475  35.975  1.00 14.49           C  
ANISOU 1584  CZ2 TRP A 229     1775   2038   1691    168    139     79       C  
ATOM   1585  CZ3 TRP A 229     -28.159  56.153  37.979  1.00 11.50           C  
ANISOU 1585  CZ3 TRP A 229     1380   1689   1298    181    137     85       C  
ATOM   1586  CH2 TRP A 229     -27.007  56.144  37.174  1.00 13.46           C  
ANISOU 1586  CH2 TRP A 229     1646   1913   1556    172    143     82       C  
ATOM   1587  N   ALA A 230     -33.648  54.757  34.117  1.00 14.24           N  
ANISOU 1587  N   ALA A 230     1660   2154   1596    242     98     45       N  
ATOM   1588  CA  ALA A 230     -34.020  55.474  32.894  1.00 15.56           C  
ANISOU 1588  CA  ALA A 230     1843   2330   1739    274     94     37       C  
ATOM   1589  C   ALA A 230     -35.037  56.594  33.142  1.00 15.05           C  
ANISOU 1589  C   ALA A 230     1784   2290   1644    311     92     35       C  
ATOM   1590  O   ALA A 230     -34.840  57.712  32.667  1.00 15.28           O  
ANISOU 1590  O   ALA A 230     1845   2307   1652    341     97     39       O  
ATOM   1591  CB  ALA A 230     -34.563  54.508  31.832  1.00 13.73           C  
ANISOU 1591  CB  ALA A 230     1587   2119   1509    269     86     21       C  
ATOM   1592  N   SER A 231     -36.109  56.302  33.878  1.00 14.94           N  
ANISOU 1592  N   SER A 231     1740   2309   1626    310     85     30       N  
ATOM   1593  CA  SER A 231     -37.131  57.320  34.139  1.00 15.94           C  
ANISOU 1593  CA  SER A 231     1869   2463   1723    347     82     28       C  
ATOM   1594  C   SER A 231     -36.605  58.483  34.974  1.00 15.91           C  
ANISOU 1594  C   SER A 231     1898   2435   1713    359     92     43       C  
ATOM   1595  O   SER A 231     -36.989  59.643  34.780  1.00 16.23           O  
ANISOU 1595  O   SER A 231     1961   2480   1725    396     94     44       O  
ATOM   1596  CB  SER A 231     -38.393  56.716  34.767  1.00 15.90           C  
ANISOU 1596  CB  SER A 231     1822   2501   1715    341     74     17       C  
ATOM   1597  OG  SER A 231     -38.108  56.025  35.968  1.00 16.75           O  
ANISOU 1597  OG  SER A 231     1916   2599   1850    307     79     26       O  
ATOM   1598  N   THR A 232     -35.684  58.176  35.880  1.00 16.24           N  
ANISOU 1598  N   THR A 232     1941   2449   1778    328     98     53       N  
ATOM   1599  CA  THR A 232     -35.062  59.208  36.710  1.00 16.65           C  
ANISOU 1599  CA  THR A 232     2021   2477   1827    334    108     63       C  
ATOM   1600  C   THR A 232     -34.236  60.137  35.829  1.00 17.01           C  
ANISOU 1600  C   THR A 232     2107   2490   1862    350    119     65       C  
ATOM   1601  O   THR A 232     -34.312  61.371  35.931  1.00 15.12           O  
ANISOU 1601  O   THR A 232     1898   2242   1603    377    128     68       O  
ATOM   1602  CB  THR A 232     -34.205  58.548  37.817  1.00 17.15           C  
ANISOU 1602  CB  THR A 232     2073   2523   1917    298    112     71       C  
ATOM   1603  OG1 THR A 232     -35.080  57.809  38.685  1.00 17.80           O  
ANISOU 1603  OG1 THR A 232     2121   2635   2005    287    105     70       O  
ATOM   1604  CG2 THR A 232     -33.420  59.586  38.636  1.00 16.82           C  
ANISOU 1604  CG2 THR A 232     2058   2457   1873    300    123     78       C  
ATOM   1605  N   TRP A 233     -33.425  59.537  34.964  1.00 16.04           N  
ANISOU 1605  N   TRP A 233     1989   2348   1754    333    121     64       N  
ATOM   1606  CA  TRP A 233     -32.604  60.353  34.090  1.00 16.05           C  
ANISOU 1606  CA  TRP A 233     2031   2319   1749    346    133     66       C  
ATOM   1607  C   TRP A 233     -33.450  61.121  33.067  1.00 16.42           C  
ANISOU 1607  C   TRP A 233     2095   2380   1762    391    133     62       C  
ATOM   1608  O   TRP A 233     -33.131  62.270  32.754  1.00 14.46           O  
ANISOU 1608  O   TRP A 233     1886   2109   1498    414    148     67       O  
ATOM   1609  CB  TRP A 233     -31.508  59.526  33.411  1.00 16.64           C  
ANISOU 1609  CB  TRP A 233     2105   2370   1845    318    135     65       C  
ATOM   1610  CG  TRP A 233     -30.283  59.373  34.262  1.00 14.53           C  
ANISOU 1610  CG  TRP A 233     1841   2075   1601    286    143     69       C  
ATOM   1611  CD1 TRP A 233     -29.784  58.211  34.778  1.00 16.88           C  
ANISOU 1611  CD1 TRP A 233     2113   2373   1924    254    138     71       C  
ATOM   1612  CD2 TRP A 233     -29.401  60.417  34.689  1.00 13.98           C  
ANISOU 1612  CD2 TRP A 233     1802   1977   1530    285    159     72       C  
ATOM   1613  NE1 TRP A 233     -28.646  58.468  35.504  1.00 15.45           N  
ANISOU 1613  NE1 TRP A 233     1943   2169   1756    235    148     74       N  
ATOM   1614  CE2 TRP A 233     -28.383  59.812  35.455  1.00 13.05           C  
ANISOU 1614  CE2 TRP A 233     1673   1848   1438    252    161     72       C  
ATOM   1615  CE3 TRP A 233     -29.383  61.812  34.512  1.00 13.72           C  
ANISOU 1615  CE3 TRP A 233     1807   1927   1477    310    175     72       C  
ATOM   1616  CZ2 TRP A 233     -27.351  60.551  36.051  1.00 15.50           C  
ANISOU 1616  CZ2 TRP A 233     2002   2134   1752    240    175     70       C  
ATOM   1617  CZ3 TRP A 233     -28.346  62.544  35.092  1.00 16.70           C  
ANISOU 1617  CZ3 TRP A 233     2207   2276   1862    296    192     70       C  
ATOM   1618  CH2 TRP A 233     -27.356  61.913  35.865  1.00 17.08           C  
ANISOU 1618  CH2 TRP A 233     2237   2318   1935    260    191     68       C  
ATOM   1619  N   LEU A 234     -34.510  60.496  32.551  1.00 15.42           N  
ANISOU 1619  N   LEU A 234     1940   2292   1627    403    118     53       N  
ATOM   1620  CA  LEU A 234     -35.427  61.225  31.661  1.00 18.13           C  
ANISOU 1620  CA  LEU A 234     2296   2658   1934    451    116     49       C  
ATOM   1621  C   LEU A 234     -36.128  62.363  32.394  1.00 18.52           C  
ANISOU 1621  C   LEU A 234     2360   2717   1959    483    120     54       C  
ATOM   1622  O   LEU A 234     -36.385  63.424  31.813  1.00 19.37           O  
ANISOU 1622  O   LEU A 234     2500   2821   2037    525    129     57       O  
ATOM   1623  CB  LEU A 234     -36.464  60.299  31.021  1.00 15.92           C  
ANISOU 1623  CB  LEU A 234     1976   2424   1647    456     98     34       C  
ATOM   1624  CG  LEU A 234     -35.877  59.542  29.829  1.00 17.30           C  
ANISOU 1624  CG  LEU A 234     2150   2589   1834    444     96     28       C  
ATOM   1625  CD1 LEU A 234     -36.788  58.364  29.520  1.00 17.77           C  
ANISOU 1625  CD1 LEU A 234     2161   2692   1897    432     80      9       C  
ATOM   1626  CD2 LEU A 234     -35.727  60.498  28.649  1.00 16.37           C  
ANISOU 1626  CD2 LEU A 234     2071   2460   1687    486    105     31       C  
ATOM   1627  N   TYR A 235     -36.436  62.148  33.669  1.00 19.79           N  
ANISOU 1627  N   TYR A 235     2498   2890   2131    464    116     55       N  
ATOM   1628  CA  TYR A 235     -36.969  63.249  34.451  1.00 19.26           C  
ANISOU 1628  CA  TYR A 235     2446   2828   2043    491    121     60       C  
ATOM   1629  C   TYR A 235     -35.957  64.387  34.545  1.00 19.89           C  
ANISOU 1629  C   TYR A 235     2575   2859   2120    497    143     70       C  
ATOM   1630  O   TYR A 235     -36.308  65.550  34.320  1.00 19.65           O  
ANISOU 1630  O   TYR A 235     2578   2824   2062    536    154     73       O  
ATOM   1631  CB  TYR A 235     -37.384  62.820  35.854  1.00 20.66           C  
ANISOU 1631  CB  TYR A 235     2591   3023   2233    469    114     60       C  
ATOM   1632  CG  TYR A 235     -37.981  63.992  36.602  1.00 21.13           C  
ANISOU 1632  CG  TYR A 235     2668   3090   2270    500    120     64       C  
ATOM   1633  CD1 TYR A 235     -39.127  64.637  36.124  1.00 24.31           C  
ANISOU 1633  CD1 TYR A 235     3074   3525   2637    548    115     60       C  
ATOM   1634  CD2 TYR A 235     -37.405  64.446  37.781  1.00 21.63           C  
ANISOU 1634  CD2 TYR A 235     2742   3131   2344    483    129     72       C  
ATOM   1635  CE1 TYR A 235     -39.685  65.715  36.805  1.00 25.09           C  
ANISOU 1635  CE1 TYR A 235     3190   3629   2712    579    121     64       C  
ATOM   1636  CE2 TYR A 235     -37.950  65.517  38.466  1.00 26.33           C  
ANISOU 1636  CE2 TYR A 235     3354   3732   2918    511    135     74       C  
ATOM   1637  CZ  TYR A 235     -39.085  66.137  37.978  1.00 27.39           C  
ANISOU 1637  CZ  TYR A 235     3493   3895   3018    558    131     72       C  
ATOM   1638  OH  TYR A 235     -39.598  67.202  38.669  1.00 24.73           O  
ANISOU 1638  OH  TYR A 235     3174   3561   2659    587    137     75       O  
ATOM   1639  N   LEU A 236     -34.712  64.054  34.884  1.00 18.09           N  
ANISOU 1639  N   LEU A 236     2353   2597   1922    457    151     73       N  
ATOM   1640  CA  LEU A 236     -33.656  65.061  34.945  1.00 18.53           C  
ANISOU 1640  CA  LEU A 236     2453   2607   1979    455    174     77       C  
ATOM   1641  C   LEU A 236     -33.355  65.738  33.608  1.00 18.88           C  
ANISOU 1641  C   LEU A 236     2538   2629   2006    482    189     79       C  
ATOM   1642  O   LEU A 236     -32.895  66.880  33.587  1.00 19.92           O  
ANISOU 1642  O   LEU A 236     2713   2728   2127    496    211     83       O  
ATOM   1643  CB  LEU A 236     -32.367  64.510  35.580  1.00 17.90           C  
ANISOU 1643  CB  LEU A 236     2365   2502   1933    407    178     77       C  
ATOM   1644  CG  LEU A 236     -32.452  64.079  37.048  1.00 16.83           C  
ANISOU 1644  CG  LEU A 236     2200   2381   1813    383    170     77       C  
ATOM   1645  CD1 LEU A 236     -31.137  63.469  37.497  1.00 15.89           C  
ANISOU 1645  CD1 LEU A 236     2073   2240   1723    341    174     76       C  
ATOM   1646  CD2 LEU A 236     -32.795  65.235  38.003  1.00 20.76           C  
ANISOU 1646  CD2 LEU A 236     2715   2877   2295    401    180     79       C  
ATOM   1647  N   ALA A 237     -33.579  65.037  32.501  1.00 19.16           N  
ANISOU 1647  N   ALA A 237     2562   2680   2038    489    178     76       N  
ATOM   1648  CA  ALA A 237     -33.371  65.602  31.167  1.00 20.34           C  
ANISOU 1648  CA  ALA A 237     2748   2811   2168    519    191     78       C  
ATOM   1649  C   ALA A 237     -34.500  66.520  30.702  1.00 21.81           C  
ANISOU 1649  C   ALA A 237     2954   3018   2312    578    193     81       C  
ATOM   1650  O   ALA A 237     -34.246  67.446  29.936  1.00 23.93           O  
ANISOU 1650  O   ALA A 237     3269   3262   2561    608    213     87       O  
ATOM   1651  CB  ALA A 237     -33.170  64.499  30.139  1.00 19.08           C  
ANISOU 1651  CB  ALA A 237     2567   2662   2019    505    178     73       C  
ATOM   1652  N   THR A 238     -35.729  66.255  31.138  1.00 20.99           N  
ANISOU 1652  N   THR A 238     2816   2962   2195    595    174     76       N  
ATOM   1653  CA  THR A 238     -36.903  66.926  30.589  1.00 22.78           C  
ANISOU 1653  CA  THR A 238     3053   3220   2380    654    171     75       C  
ATOM   1654  C   THR A 238     -37.647  67.804  31.590  1.00 23.63           C  
ANISOU 1654  C   THR A 238     3168   3340   2470    678    174     79       C  
ATOM   1655  O   THR A 238     -38.250  68.796  31.197  1.00 25.18           O  
ANISOU 1655  O   THR A 238     3395   3542   2629    731    183     83       O  
ATOM   1656  CB  THR A 238     -37.927  65.919  30.045  1.00 22.87           C  
ANISOU 1656  CB  THR A 238     3016   3289   2383    663    144     62       C  
ATOM   1657  OG1 THR A 238     -38.395  65.115  31.137  1.00 20.26           O  
ANISOU 1657  OG1 THR A 238     2638   2986   2073    630    128     55       O  
ATOM   1658  CG2 THR A 238     -37.309  65.030  28.977  1.00 21.17           C  
ANISOU 1658  CG2 THR A 238     2792   3066   2183    643    140     56       C  
ATOM   1659  N   GLY A 239     -37.625  67.441  32.867  1.00 24.70           N  
ANISOU 1659  N   GLY A 239     3276   3480   2627    643    167     77       N  
ATOM   1660  CA  GLY A 239     -38.539  68.014  33.859  1.00 24.44           C  
ANISOU 1660  CA  GLY A 239     3236   3471   2578    664    164     78       C  
ATOM   1661  C   GLY A 239     -40.005  67.641  33.705  1.00 26.95           C  
ANISOU 1661  C   GLY A 239     3516   3851   2871    695    142     68       C  
ATOM   1662  O   GLY A 239     -40.868  68.260  34.331  1.00 28.29           O  
ANISOU 1662  O   GLY A 239     3684   4044   3019    723    140     69       O  
ATOM   1663  N   ASP A 240     -40.307  66.652  32.869  1.00 26.14           N  
ANISOU 1663  N   ASP A 240     3381   3779   2772    689    125     58       N  
ATOM   1664  CA  ASP A 240     -41.673  66.169  32.679  1.00 27.42           C  
ANISOU 1664  CA  ASP A 240     3499   4004   2912    712    104     43       C  
ATOM   1665  C   ASP A 240     -42.056  65.260  33.852  1.00 27.74           C  
ANISOU 1665  C   ASP A 240     3491   4069   2979    670     91     36       C  
ATOM   1666  O   ASP A 240     -41.474  64.200  34.090  1.00 24.68           O  
ANISOU 1666  O   ASP A 240     3079   3670   2627    620     87     34       O  
ATOM   1667  CB  ASP A 240     -41.786  65.475  31.316  1.00 27.76           C  
ANISOU 1667  CB  ASP A 240     3528   4068   2949    720     94     32       C  
ATOM   1668  CG  ASP A 240     -43.173  64.920  31.023  1.00 30.96           C  
ANISOU 1668  CG  ASP A 240     3885   4544   3334    742     72     11       C  
ATOM   1669  OD1 ASP A 240     -44.094  64.977  31.864  1.00 36.98           O  
ANISOU 1669  OD1 ASP A 240     4621   5342   4087    748     64      5       O  
ATOM   1670  OD2 ASP A 240     -43.339  64.376  29.914  1.00 36.62           O  
ANISOU 1670  OD2 ASP A 240     4586   5283   4042    750     63      0       O  
ATOM   1671  N   ARG A 241     -43.048  65.709  34.613  1.00 27.01           N  
ANISOU 1671  N   ARG A 241     3386   4009   2867    693     86     34       N  
ATOM   1672  CA  ARG A 241     -43.455  65.015  35.824  1.00 27.43           C  
ANISOU 1672  CA  ARG A 241     3397   4083   2941    658     76     29       C  
ATOM   1673  C   ARG A 241     -43.920  63.581  35.598  1.00 25.66           C  
ANISOU 1673  C   ARG A 241     3118   3895   2734    626     61     12       C  
ATOM   1674  O   ARG A 241     -43.847  62.747  36.503  1.00 23.67           O  
ANISOU 1674  O   ARG A 241     2837   3644   2511    582     59     11       O  
ATOM   1675  CB  ARG A 241     -44.515  65.852  36.543  1.00 28.35           C  
ANISOU 1675  CB  ARG A 241     3511   4231   3027    696     74     29       C  
ATOM   1676  CG  ARG A 241     -43.855  66.959  37.355  1.00 33.18           C  
ANISOU 1676  CG  ARG A 241     4167   4798   3639    702     92     46       C  
ATOM   1677  CD  ARG A 241     -43.514  66.445  38.747  1.00 36.76           C  
ANISOU 1677  CD  ARG A 241     4599   5242   4125    654     91     50       C  
ATOM   1678  NE  ARG A 241     -44.723  65.934  39.399  1.00 40.38           N  
ANISOU 1678  NE  ARG A 241     5011   5754   4578    654     77     39       N  
ATOM   1679  CZ  ARG A 241     -45.441  66.579  40.317  1.00 41.18           C  
ANISOU 1679  CZ  ARG A 241     5109   5875   4662    675     76     41       C  
ATOM   1680  NH1 ARG A 241     -45.078  67.779  40.760  1.00 37.73           N  
ANISOU 1680  NH1 ARG A 241     4715   5407   4213    697     90     53       N  
ATOM   1681  NH2 ARG A 241     -46.524  66.000  40.816  1.00 39.28           N  
ANISOU 1681  NH2 ARG A 241     4822   5685   4417    672     63     30       N  
ATOM   1682  N   ASN A 242     -44.381  63.275  34.392  1.00 25.19           N  
ANISOU 1682  N   ASN A 242     3047   3866   2659    647     52     -1       N  
ATOM   1683  CA  ASN A 242     -44.762  61.893  34.118  1.00 26.14           C  
ANISOU 1683  CA  ASN A 242     3117   4017   2798    612     40    -20       C  
ATOM   1684  C   ASN A 242     -43.635  60.886  34.344  1.00 24.43           C  
ANISOU 1684  C   ASN A 242     2897   3758   2626    553     46    -14       C  
ATOM   1685  O   ASN A 242     -43.915  59.761  34.752  1.00 23.40           O  
ANISOU 1685  O   ASN A 242     2726   3644   2518    514     41    -24       O  
ATOM   1686  CB  ASN A 242     -45.338  61.738  32.709  1.00 26.87           C  
ANISOU 1686  CB  ASN A 242     3198   4147   2864    644     30    -39       C  
ATOM   1687  CG  ASN A 242     -46.677  62.435  32.574  1.00 31.61           C  
ANISOU 1687  CG  ASN A 242     3785   4805   3420    699     21    -52       C  
ATOM   1688  OD1 ASN A 242     -47.487  62.407  33.498  1.00 35.77           O  
ANISOU 1688  OD1 ASN A 242     4283   5362   3943    696     16    -58       O  
ATOM   1689  ND2 ASN A 242     -46.909  63.078  31.440  1.00 33.03           N  
ANISOU 1689  ND2 ASN A 242     3985   5000   3563    751     18    -55       N  
ATOM   1690  N   TYR A 243     -42.394  61.295  34.071  1.00 22.84           N  
ANISOU 1690  N   TYR A 243     2738   3504   2436    548     58      2       N  
ATOM   1691  CA  TYR A 243     -41.218  60.446  34.282  1.00 20.83           C  
ANISOU 1691  CA  TYR A 243     2484   3208   2221    497     64      9       C  
ATOM   1692  C   TYR A 243     -40.928  60.287  35.776  1.00 20.78           C  
ANISOU 1692  C   TYR A 243     2471   3186   2237    466     69     20       C  
ATOM   1693  O   TYR A 243     -40.546  59.201  36.211  1.00 19.46           O  
ANISOU 1693  O   TYR A 243     2282   3011   2101    423     69     20       O  
ATOM   1694  CB  TYR A 243     -39.981  61.002  33.572  1.00 19.78           C  
ANISOU 1694  CB  TYR A 243     2398   3027   2091    502     76     21       C  
ATOM   1695  CG  TYR A 243     -40.048  60.868  32.067  1.00 21.32           C  
ANISOU 1695  CG  TYR A 243     2597   3231   2270    524     71     11       C  
ATOM   1696  CD1 TYR A 243     -40.194  59.616  31.468  1.00 20.19           C  
ANISOU 1696  CD1 TYR A 243     2418   3107   2143    498     62     -3       C  
ATOM   1697  CD2 TYR A 243     -40.011  61.991  31.247  1.00 20.59           C  
ANISOU 1697  CD2 TYR A 243     2545   3131   2147    571     79     17       C  
ATOM   1698  CE1 TYR A 243     -40.287  59.488  30.083  1.00 19.67           C  
ANISOU 1698  CE1 TYR A 243     2356   3055   2063    519     57    -14       C  
ATOM   1699  CE2 TYR A 243     -40.098  61.876  29.862  1.00 18.62           C  
ANISOU 1699  CE2 TYR A 243     2300   2893   1881    595     75      8       C  
ATOM   1700  CZ  TYR A 243     -40.228  60.627  29.293  1.00 22.06           C  
ANISOU 1700  CZ  TYR A 243     2698   3351   2333    568     63     -7       C  
ATOM   1701  OH  TYR A 243     -40.296  60.502  27.925  1.00 22.99           O  
ANISOU 1701  OH  TYR A 243     2818   3481   2433    592     58    -17       O  
ATOM   1702  N   LEU A 244     -41.120  61.347  36.560  1.00 20.94           N  
ANISOU 1702  N   LEU A 244     2510   3203   2241    489     74     29       N  
ATOM   1703  CA  LEU A 244     -40.908  61.236  38.009  1.00 21.49           C  
ANISOU 1703  CA  LEU A 244     2572   3263   2330    463     78     39       C  
ATOM   1704  C   LEU A 244     -41.950  60.311  38.621  1.00 22.75           C  
ANISOU 1704  C   LEU A 244     2682   3465   2494    446     69     28       C  
ATOM   1705  O   LEU A 244     -41.622  59.466  39.461  1.00 22.35           O  
ANISOU 1705  O   LEU A 244     2614   3405   2471    407     71     33       O  
ATOM   1706  CB  LEU A 244     -40.931  62.595  38.717  1.00 22.86           C  
ANISOU 1706  CB  LEU A 244     2776   3425   2483    491     86     48       C  
ATOM   1707  CG  LEU A 244     -40.668  62.571  40.233  1.00 20.49           C  
ANISOU 1707  CG  LEU A 244     2469   3115   2199    467     90     57       C  
ATOM   1708  CD1 LEU A 244     -39.316  61.951  40.588  1.00 17.44           C  
ANISOU 1708  CD1 LEU A 244     2089   2691   1847    425     97     65       C  
ATOM   1709  CD2 LEU A 244     -40.734  63.980  40.812  1.00 19.40           C  
ANISOU 1709  CD2 LEU A 244     2363   2967   2039    498     98     64       C  
ATOM   1710  N   ASP A 245     -43.195  60.469  38.171  1.00 23.62           N  
ANISOU 1710  N   ASP A 245     2772   3622   2577    476     59     13       N  
ATOM   1711  CA  ASP A 245     -44.300  59.611  38.588  1.00 24.87           C  
ANISOU 1711  CA  ASP A 245     2882   3826   2739    461     52     -1       C  
ATOM   1712  C   ASP A 245     -44.003  58.151  38.276  1.00 23.75           C  
ANISOU 1712  C   ASP A 245     2714   3680   2629    415     52     -9       C  
ATOM   1713  O   ASP A 245     -44.203  57.285  39.132  1.00 22.05           O  
ANISOU 1713  O   ASP A 245     2472   3471   2435    381     56    -10       O  
ATOM   1714  CB  ASP A 245     -45.602  60.021  37.887  1.00 27.87           C  
ANISOU 1714  CB  ASP A 245     3245   4261   3082    503     41    -20       C  
ATOM   1715  CG  ASP A 245     -46.243  61.266  38.508  1.00 34.35           C  
ANISOU 1715  CG  ASP A 245     4080   5098   3872    546     40    -14       C  
ATOM   1716  OD1 ASP A 245     -45.634  61.942  39.375  1.00 40.31           O  
ANISOU 1716  OD1 ASP A 245     4863   5819   4632    545     49      4       O  
ATOM   1717  OD2 ASP A 245     -47.382  61.572  38.100  1.00 43.09           O  
ANISOU 1717  OD2 ASP A 245     5168   6254   4947    582     31    -30       O  
ATOM   1718  N   LYS A 246     -43.514  57.887  37.064  1.00 22.01           N  
ANISOU 1718  N   LYS A 246     2504   3448   2411    415     50    -15       N  
ATOM   1719  CA  LYS A 246     -43.061  56.538  36.715  1.00 23.06           C  
ANISOU 1719  CA  LYS A 246     2617   3568   2575    372     53    -22       C  
ATOM   1720  C   LYS A 246     -41.998  56.066  37.711  1.00 21.79           C  
ANISOU 1720  C   LYS A 246     2467   3363   2446    334     64     -2       C  
ATOM   1721  O   LYS A 246     -42.118  54.986  38.290  1.00 21.42           O  
ANISOU 1721  O   LYS A 246     2395   3320   2423    298     69     -4       O  
ATOM   1722  CB  LYS A 246     -42.526  56.486  35.283  1.00 22.72           C  
ANISOU 1722  CB  LYS A 246     2589   3513   2528    381     50    -28       C  
ATOM   1723  CG  LYS A 246     -43.589  56.678  34.213  1.00 28.36           C  
ANISOU 1723  CG  LYS A 246     3286   4276   3212    416     39    -51       C  
ATOM   1724  CD  LYS A 246     -44.094  55.333  33.732  1.00 35.28           C  
ANISOU 1724  CD  LYS A 246     4119   5180   4104    384     35    -76       C  
ATOM   1725  CE  LYS A 246     -45.132  55.451  32.623  1.00 36.46           C  
ANISOU 1725  CE  LYS A 246     4246   5385   4222    417     23   -103       C  
ATOM   1726  NZ  LYS A 246     -45.761  54.099  32.486  1.00 34.11           N  
ANISOU 1726  NZ  LYS A 246     3899   5116   3943    378     22   -131       N  
ATOM   1727  N   ALA A 247     -40.968  56.884  37.914  1.00 21.29           N  
ANISOU 1727  N   ALA A 247     2443   3262   2383    344     69     15       N  
ATOM   1728  CA  ALA A 247     -39.830  56.504  38.754  1.00 20.71           C  
ANISOU 1728  CA  ALA A 247     2381   3148   2337    312     78     32       C  
ATOM   1729  C   ALA A 247     -40.305  56.063  40.134  1.00 21.98           C  
ANISOU 1729  C   ALA A 247     2518   3323   2508    294     82     37       C  
ATOM   1730  O   ALA A 247     -39.974  54.966  40.610  1.00 18.87           O  
ANISOU 1730  O   ALA A 247     2109   2919   2140    259     88     41       O  
ATOM   1731  CB  ALA A 247     -38.828  57.654  38.865  1.00 18.91           C  
ANISOU 1731  CB  ALA A 247     2195   2885   2103    329     84     46       C  
ATOM   1732  N   GLU A 248     -41.141  56.906  40.737  1.00 21.73           N  
ANISOU 1732  N   GLU A 248     2484   3317   2454    320     78     37       N  
ATOM   1733  CA  GLU A 248     -41.658  56.632  42.073  1.00 24.05           C  
ANISOU 1733  CA  GLU A 248     2757   3626   2753    307     82     42       C  
ATOM   1734  C   GLU A 248     -42.548  55.403  42.092  1.00 23.70           C  
ANISOU 1734  C   GLU A 248     2673   3611   2721    282     83     28       C  
ATOM   1735  O   GLU A 248     -42.543  54.669  43.080  1.00 22.68           O  
ANISOU 1735  O   GLU A 248     2528   3479   2609    256     91     36       O  
ATOM   1736  CB  GLU A 248     -42.358  57.870  42.659  1.00 22.79           C  
ANISOU 1736  CB  GLU A 248     2605   3487   2566    343     78     43       C  
ATOM   1737  CG  GLU A 248     -41.398  59.037  42.788  1.00 26.27           C  
ANISOU 1737  CG  GLU A 248     3088   3893   2999    361     82     56       C  
ATOM   1738  CD  GLU A 248     -41.973  60.271  43.476  1.00 34.91           C  
ANISOU 1738  CD  GLU A 248     4194   5002   4068    394     81     59       C  
ATOM   1739  OE1 GLU A 248     -43.209  60.449  43.510  1.00 41.87           O  
ANISOU 1739  OE1 GLU A 248     5055   5924   4929    415     75     50       O  
ATOM   1740  OE2 GLU A 248     -41.172  61.101  43.953  1.00 35.38           O  
ANISOU 1740  OE2 GLU A 248     4284   5032   4126    400     88     70       O  
ATOM   1741  N   SER A 249     -43.276  55.158  41.004  1.00 23.93           N  
ANISOU 1741  N   SER A 249     2684   3668   2740    290     76      8       N  
ATOM   1742  CA  SER A 249     -44.114  53.962  40.921  1.00 25.44           C  
ANISOU 1742  CA  SER A 249     2835   3887   2943    262     79    -10       C  
ATOM   1743  C   SER A 249     -43.305  52.652  40.884  1.00 25.54           C  
ANISOU 1743  C   SER A 249     2845   3867   2990    219     91     -5       C  
ATOM   1744  O   SER A 249     -43.852  51.588  41.188  1.00 25.14           O  
ANISOU 1744  O   SER A 249     2765   3829   2955    189    100    -14       O  
ATOM   1745  CB  SER A 249     -45.050  54.026  39.708  1.00 25.68           C  
ANISOU 1745  CB  SER A 249     2845   3959   2953    281     69    -37       C  
ATOM   1746  OG  SER A 249     -44.333  53.752  38.514  1.00 28.71           O  
ANISOU 1746  OG  SER A 249     3243   4322   3343    278     66    -41       O  
ATOM   1747  N   TYR A 250     -42.027  52.714  40.510  1.00 22.52           N  
ANISOU 1747  N   TYR A 250     2493   3443   2619    215     92      8       N  
ATOM   1748  CA  TYR A 250     -41.222  51.492  40.395  1.00 23.47           C  
ANISOU 1748  CA  TYR A 250     2613   3533   2770    179    102     13       C  
ATOM   1749  C   TYR A 250     -40.644  51.001  41.720  1.00 23.77           C  
ANISOU 1749  C   TYR A 250     2655   3546   2827    157    115     34       C  
ATOM   1750  O   TYR A 250     -40.260  49.835  41.838  1.00 23.25           O  
ANISOU 1750  O   TYR A 250     2584   3463   2786    126    127     37       O  
ATOM   1751  CB  TYR A 250     -40.072  51.664  39.394  1.00 21.00           C  
ANISOU 1751  CB  TYR A 250     2328   3188   2462    183     99     17       C  
ATOM   1752  CG  TYR A 250     -40.504  51.974  37.973  1.00 22.73           C  
ANISOU 1752  CG  TYR A 250     2544   3426   2663    203     88     -2       C  
ATOM   1753  CD1 TYR A 250     -41.506  51.238  37.340  1.00 19.32           C  
ANISOU 1753  CD1 TYR A 250     2079   3029   2231    193     86    -27       C  
ATOM   1754  CD2 TYR A 250     -39.880  52.986  37.250  1.00 20.54           C  
ANISOU 1754  CD2 TYR A 250     2298   3134   2371    232     81      3       C  
ATOM   1755  CE1 TYR A 250     -41.886  51.518  36.027  1.00 22.64           C  
ANISOU 1755  CE1 TYR A 250     2495   3472   2633    215     75    -46       C  
ATOM   1756  CE2 TYR A 250     -40.260  53.284  35.947  1.00 18.89           C  
ANISOU 1756  CE2 TYR A 250     2089   2944   2143    255     72    -13       C  
ATOM   1757  CZ  TYR A 250     -41.256  52.548  35.339  1.00 21.79           C  
ANISOU 1757  CZ  TYR A 250     2422   3349   2509    248     68    -37       C  
ATOM   1758  OH  TYR A 250     -41.613  52.854  34.042  1.00 22.86           O  
ANISOU 1758  OH  TYR A 250     2556   3507   2623    274     58    -54       O  
ATOM   1759  N   THR A 251     -40.550  51.883  42.712  1.00 24.34           N  
ANISOU 1759  N   THR A 251     2740   3619   2888    175    114     48       N  
ATOM   1760  CA  THR A 251     -39.813  51.521  43.924  1.00 24.93           C  
ANISOU 1760  CA  THR A 251     2823   3670   2978    160    124     69       C  
ATOM   1761  C   THR A 251     -40.410  50.335  44.695  1.00 25.33           C  
ANISOU 1761  C   THR A 251     2849   3729   3044    132    139     70       C  
ATOM   1762  O   THR A 251     -39.644  49.503  45.182  1.00 24.17           O  
ANISOU 1762  O   THR A 251     2709   3556   2917    112    151     85       O  
ATOM   1763  CB  THR A 251     -39.487  52.735  44.833  1.00 25.42           C  
ANISOU 1763  CB  THR A 251     2903   3729   3024    184    120     83       C  
ATOM   1764  OG1 THR A 251     -40.701  53.317  45.306  1.00 29.32           O  
ANISOU 1764  OG1 THR A 251     3382   4258   3498    201    115     76       O  
ATOM   1765  CG2 THR A 251     -38.689  53.800  44.077  1.00 26.25           C  
ANISOU 1765  CG2 THR A 251     3039   3816   3119    206    111     83       C  
ATOM   1766  N   PRO A 252     -41.754  50.204  44.751  1.00 24.80           N  
ANISOU 1766  N   PRO A 252     2754   3700   2969    131    140     54       N  
ATOM   1767  CA  PRO A 252     -42.312  48.982  45.318  1.00 24.50           C  
ANISOU 1767  CA  PRO A 252     2693   3666   2948    100    158     52       C  
ATOM   1768  C   PRO A 252     -42.014  47.707  44.525  1.00 24.89           C  
ANISOU 1768  C   PRO A 252     2738   3696   3022     69    170     44       C  
ATOM   1769  O   PRO A 252     -42.216  46.617  45.065  1.00 25.01           O  
ANISOU 1769  O   PRO A 252     2742   3703   3054     41    190     47       O  
ATOM   1770  CB  PRO A 252     -43.829  49.237  45.299  1.00 26.56           C  
ANISOU 1770  CB  PRO A 252     2922   3974   3192    106    155     30       C  
ATOM   1771  CG  PRO A 252     -43.995  50.701  45.199  1.00 25.53           C  
ANISOU 1771  CG  PRO A 252     2803   3862   3034    146    136     30       C  
ATOM   1772  CD  PRO A 252     -42.822  51.136  44.351  1.00 25.12           C  
ANISOU 1772  CD  PRO A 252     2782   3779   2983    158    126     37       C  
ATOM   1773  N   LYS A 253     -41.576  47.826  43.271  1.00 22.68           N  
ANISOU 1773  N   LYS A 253     2466   3408   2741     73    159     33       N  
ATOM   1774  CA  LYS A 253     -41.273  46.657  42.443  1.00 22.88           C  
ANISOU 1774  CA  LYS A 253     2487   3416   2788     45    169     23       C  
ATOM   1775  C   LYS A 253     -39.808  46.224  42.569  1.00 21.72           C  
ANISOU 1775  C   LYS A 253     2369   3222   2659     37    176     46       C  
ATOM   1776  O   LYS A 253     -39.404  45.205  42.006  1.00 20.54           O  
ANISOU 1776  O   LYS A 253     2221   3052   2530     14    186     42       O  
ATOM   1777  CB  LYS A 253     -41.581  46.949  40.969  1.00 22.81           C  
ANISOU 1777  CB  LYS A 253     2471   3425   2769     55    154     -1       C  
ATOM   1778  CG  LYS A 253     -42.999  47.459  40.711  1.00 28.22           C  
ANISOU 1778  CG  LYS A 253     3127   4162   3432     70    145    -26       C  
ATOM   1779  CD  LYS A 253     -43.981  46.396  40.214  1.00 36.31           C  
ANISOU 1779  CD  LYS A 253     4116   5213   4467     40    156    -57       C  
ATOM   1780  CE  LYS A 253     -44.109  45.202  41.149  1.00 42.26           C  
ANISOU 1780  CE  LYS A 253     4860   5949   5246      1    182    -50       C  
ATOM   1781  NZ  LYS A 253     -45.013  44.145  40.615  1.00 47.26           N  
ANISOU 1781  NZ  LYS A 253     5460   6604   5892    -31    197    -83       N  
ATOM   1782  N   LEU A 254     -39.003  47.016  43.270  1.00 20.60           N  
ANISOU 1782  N   LEU A 254     2250   3067   2510     57    169     67       N  
ATOM   1783  CA  LEU A 254     -37.577  46.696  43.423  1.00 20.42           C  
ANISOU 1783  CA  LEU A 254     2252   3005   2500     53    174     87       C  
ATOM   1784  C   LEU A 254     -37.420  45.487  44.334  1.00 20.74           C  
ANISOU 1784  C   LEU A 254     2290   3029   2559     30    196    102       C  
ATOM   1785  O   LEU A 254     -38.290  45.216  45.168  1.00 20.42           O  
ANISOU 1785  O   LEU A 254     2234   3005   2518     23    207    103       O  
ATOM   1786  CB  LEU A 254     -36.805  47.889  43.986  1.00 19.81           C  
ANISOU 1786  CB  LEU A 254     2196   2922   2408     79    162    102       C  
ATOM   1787  CG  LEU A 254     -36.739  49.128  43.086  1.00 21.27           C  
ANISOU 1787  CG  LEU A 254     2391   3113   2575    103    144     91       C  
ATOM   1788  CD1 LEU A 254     -36.083  50.236  43.877  1.00 18.40           C  
ANISOU 1788  CD1 LEU A 254     2048   2744   2199    124    139    105       C  
ATOM   1789  CD2 LEU A 254     -35.946  48.829  41.800  1.00 22.17           C  
ANISOU 1789  CD2 LEU A 254     2518   3206   2698     97    141     85       C  
ATOM   1790  N   ASN A 255     -36.323  44.754  44.178  1.00 20.40           N  
ANISOU 1790  N   ASN A 255     2263   2953   2532     20    204    113       N  
ATOM   1791  CA  ASN A 255     -36.096  43.588  45.031  1.00 20.90           C  
ANISOU 1791  CA  ASN A 255     2330   2998   2612      3    228    130       C  
ATOM   1792  C   ASN A 255     -35.903  44.021  46.471  1.00 20.05           C  
ANISOU 1792  C   ASN A 255     2228   2894   2493     20    230    151       C  
ATOM   1793  O   ASN A 255     -35.394  45.113  46.713  1.00 18.19           O  
ANISOU 1793  O   ASN A 255     2002   2665   2243     42    214    156       O  
ATOM   1794  CB  ASN A 255     -34.886  42.794  44.539  1.00 21.87           C  
ANISOU 1794  CB  ASN A 255     2472   3086   2751     -4    234    138       C  
ATOM   1795  CG  ASN A 255     -35.046  42.371  43.098  1.00 23.13           C  
ANISOU 1795  CG  ASN A 255     2625   3241   2920    -20    231    116       C  
ATOM   1796  OD1 ASN A 255     -36.098  41.871  42.727  1.00 20.33           O  
ANISOU 1796  OD1 ASN A 255     2251   2901   2571    -38    240     98       O  
ATOM   1797  ND2 ASN A 255     -34.048  42.636  42.266  1.00 24.76           N  
ANISOU 1797  ND2 ASN A 255     2847   3432   3127    -12    219    116       N  
ATOM   1798  N   ARG A 256     -36.305  43.163  47.409  1.00 20.37           N  
ANISOU 1798  N   ARG A 256     2264   2932   2541      8    253    163       N  
ATOM   1799  CA  ARG A 256     -36.185  43.436  48.843  1.00 21.30           C  
ANISOU 1799  CA  ARG A 256     2387   3056   2649     23    258    184       C  
ATOM   1800  C   ARG A 256     -34.861  42.920  49.395  1.00 21.92           C  
ANISOU 1800  C   ARG A 256     2487   3108   2732     31    266    207       C  
ATOM   1801  O   ARG A 256     -34.246  42.016  48.820  1.00 23.26           O  
ANISOU 1801  O   ARG A 256     2668   3252   2917     19    276    209       O  
ATOM   1802  CB  ARG A 256     -37.341  42.793  49.643  1.00 21.46           C  
ANISOU 1802  CB  ARG A 256     2392   3088   2672      9    280    185       C  
ATOM   1803  CG  ARG A 256     -38.750  43.199  49.213  1.00 23.45           C  
ANISOU 1803  CG  ARG A 256     2617   3372   2918      0    275    160       C  
ATOM   1804  CD  ARG A 256     -38.762  44.384  48.247  1.00 30.32           C  
ANISOU 1804  CD  ARG A 256     3484   4259   3775     17    245    142       C  
ATOM   1805  NE  ARG A 256     -39.086  45.630  48.920  1.00 30.74           N  
ANISOU 1805  NE  ARG A 256     3535   4337   3806     42    229    145       N  
ATOM   1806  CZ  ARG A 256     -39.304  46.810  48.345  1.00 31.23           C  
ANISOU 1806  CZ  ARG A 256     3595   4419   3852     62    207    132       C  
ATOM   1807  NH1 ARG A 256     -39.219  47.042  47.027  1.00 25.62           N  
ANISOU 1807  NH1 ARG A 256     2885   3706   3140     63    194    115       N  
ATOM   1808  NH2 ARG A 256     -39.613  47.802  49.160  1.00 26.95           N  
ANISOU 1808  NH2 ARG A 256     3051   3895   3290     84    198    137       N  
ATOM   1809  N   GLN A 257     -34.429  43.482  50.520  1.00 21.86           N  
ANISOU 1809  N   GLN A 257     2486   3108   2710     53    262    223       N  
ATOM   1810  CA  GLN A 257     -33.287  42.923  51.240  1.00 22.68           C  
ANISOU 1810  CA  GLN A 257     2607   3194   2815     65    272    246       C  
ATOM   1811  C   GLN A 257     -33.707  41.667  52.003  1.00 23.49           C  
ANISOU 1811  C   GLN A 257     2712   3286   2927     54    303    262       C  
ATOM   1812  O   GLN A 257     -34.455  41.760  52.980  1.00 24.21           O  
ANISOU 1812  O   GLN A 257     2795   3392   3009     58    312    270       O  
ATOM   1813  CB  GLN A 257     -32.687  43.932  52.217  1.00 20.30           C  
ANISOU 1813  CB  GLN A 257     2309   2909   2493     92    257    255       C  
ATOM   1814  CG  GLN A 257     -31.349  43.461  52.770  1.00 22.09           C  
ANISOU 1814  CG  GLN A 257     2551   3122   2718    107    263    273       C  
ATOM   1815  CD  GLN A 257     -30.322  43.255  51.671  1.00 19.37           C  
ANISOU 1815  CD  GLN A 257     2217   2757   2383    102    255    266       C  
ATOM   1816  OE1 GLN A 257     -30.068  44.152  50.870  1.00 19.07           O  
ANISOU 1816  OE1 GLN A 257     2179   2723   2344    102    236    249       O  
ATOM   1817  NE2 GLN A 257     -29.758  42.059  51.607  1.00 18.06           N  
ANISOU 1817  NE2 GLN A 257     2064   2569   2229     98    273    279       N  
ATOM   1818  N   ASN A 258     -33.241  40.513  51.529  1.00 24.38           N  
ANISOU 1818  N   ASN A 258     2836   3369   3055     41    321    268       N  
ATOM   1819  CA  ASN A 258     -33.559  39.213  52.107  1.00 28.01           C  
ANISOU 1819  CA  ASN A 258     3304   3811   3526     30    356    284       C  
ATOM   1820  C   ASN A 258     -35.071  39.034  52.281  1.00 30.17           C  
ANISOU 1820  C   ASN A 258     3560   4098   3804      8    371    273       C  
ATOM   1821  O   ASN A 258     -35.820  39.259  51.324  1.00 29.04           O  
ANISOU 1821  O   ASN A 258     3400   3965   3668    -11    362    247       O  
ATOM   1822  CB  ASN A 258     -32.785  39.013  53.413  1.00 27.52           C  
ANISOU 1822  CB  ASN A 258     3258   3746   3450     58    366    313       C  
ATOM   1823  CG  ASN A 258     -31.277  39.038  53.197  1.00 31.94           C  
ANISOU 1823  CG  ASN A 258     3834   4295   4006     77    353    321       C  
ATOM   1824  OD1 ASN A 258     -30.564  39.900  53.714  1.00 32.86           O  
ANISOU 1824  OD1 ASN A 258     3949   4429   4104    103    333    325       O  
ATOM   1825  ND2 ASN A 258     -30.790  38.095  52.403  1.00 31.87           N  
ANISOU 1825  ND2 ASN A 258     3838   4258   4013     65    365    321       N  
ATOM   1826  N   GLN A 259     -35.517  38.678  53.485  1.00 32.01           N  
ANISOU 1826  N   GLN A 259     3794   4334   4031     12    393    291       N  
ATOM   1827  CA  GLN A 259     -36.950  38.505  53.738  1.00 34.18           C  
ANISOU 1827  CA  GLN A 259     4052   4624   4311     -8    410    280       C  
ATOM   1828  C   GLN A 259     -37.557  39.699  54.472  1.00 33.81           C  
ANISOU 1828  C   GLN A 259     3988   4614   4244      8    391    277       C  
ATOM   1829  O   GLN A 259     -38.581  39.557  55.150  1.00 33.94           O  
ANISOU 1829  O   GLN A 259     3992   4644   4258      0    407    277       O  
ATOM   1830  CB  GLN A 259     -37.258  37.213  54.514  1.00 35.32           C  
ANISOU 1830  CB  GLN A 259     4208   4744   4465    -21    454    298       C  
ATOM   1831  CG  GLN A 259     -36.529  35.939  54.090  1.00 40.46           C  
ANISOU 1831  CG  GLN A 259     4884   5354   5134    -31    480    309       C  
ATOM   1832  CD  GLN A 259     -36.583  35.652  52.595  1.00 48.74           C  
ANISOU 1832  CD  GLN A 259     5926   6392   6201    -59    474    282       C  
ATOM   1833  OE1 GLN A 259     -35.540  35.482  51.958  1.00 52.41           O  
ANISOU 1833  OE1 GLN A 259     6405   6837   6670    -51    464    285       O  
ATOM   1834  NE2 GLN A 259     -37.786  35.591  52.030  1.00 48.34           N  
ANISOU 1834  NE2 GLN A 259     5851   6354   6160    -90    479    254       N  
ATOM   1835  N   THR A 260     -36.925  40.863  54.346  1.00 31.69           N  
ANISOU 1835  N   THR A 260     3719   4361   3960     32    357    274       N  
ATOM   1836  CA  THR A 260     -37.452  42.087  54.938  1.00 30.35           C  
ANISOU 1836  CA  THR A 260     3535   4225   3771     50    337    269       C  
ATOM   1837  C   THR A 260     -38.244  42.909  53.926  1.00 30.54           C  
ANISOU 1837  C   THR A 260     3539   4270   3793     41    316    240       C  
ATOM   1838  O   THR A 260     -38.403  42.543  52.758  1.00 29.21           O  
ANISOU 1838  O   THR A 260     3367   4093   3638     21    315    222       O  
ATOM   1839  CB  THR A 260     -36.354  42.996  55.526  1.00 30.78           C  
ANISOU 1839  CB  THR A 260     3601   4285   3808     82    316    282       C  
ATOM   1840  OG1 THR A 260     -35.631  43.612  54.453  1.00 29.94           O  
ANISOU 1840  OG1 THR A 260     3499   4174   3703     85    292    267       O  
ATOM   1841  CG2 THR A 260     -35.388  42.221  56.422  1.00 28.44           C  
ANISOU 1841  CG2 THR A 260     3323   3971   3509     97    333    309       C  
ATOM   1842  N   THR A 261     -38.733  44.052  54.390  1.00 30.88           N  
ANISOU 1842  N   THR A 261     3571   4342   3817     59    298    235       N  
ATOM   1843  CA  THR A 261     -39.508  44.929  53.532  1.00 30.35           C  
ANISOU 1843  CA  THR A 261     3487   4298   3743     58    277    209       C  
ATOM   1844  C   THR A 261     -38.621  46.071  53.057  1.00 28.22           C  
ANISOU 1844  C   THR A 261     3230   4029   3463     80    249    206       C  
ATOM   1845  O   THR A 261     -39.099  46.952  52.346  1.00 30.51           O  
ANISOU 1845  O   THR A 261     3512   4335   3743     87    231    187       O  
ATOM   1846  CB  THR A 261     -40.734  45.500  54.279  1.00 30.84           C  
ANISOU 1846  CB  THR A 261     3529   4395   3791     64    277    204       C  
ATOM   1847  OG1 THR A 261     -40.281  46.277  55.393  1.00 31.09           O  
ANISOU 1847  OG1 THR A 261     3571   4435   3806     91    269    221       O  
ATOM   1848  CG2 THR A 261     -41.668  44.388  54.755  1.00 31.98           C  
ANISOU 1848  CG2 THR A 261     3662   4542   3948     39    308    205       C  
ATOM   1849  N   ASP A 262     -37.354  46.078  53.462  1.00 26.45           N  
ANISOU 1849  N   ASP A 262     3025   3785   3237     93    247    223       N  
ATOM   1850  CA  ASP A 262     -36.408  47.095  53.002  1.00 25.17           C  
ANISOU 1850  CA  ASP A 262     2875   3619   3067    110    225    217       C  
ATOM   1851  C   ASP A 262     -36.086  46.834  51.533  1.00 23.00           C  
ANISOU 1851  C   ASP A 262     2606   3328   2806     96    219    203       C  
ATOM   1852  O   ASP A 262     -36.024  45.681  51.106  1.00 21.49           O  
ANISOU 1852  O   ASP A 262     2414   3118   2630     77    234    205       O  
ATOM   1853  CB  ASP A 262     -35.088  47.042  53.776  1.00 26.39           C  
ANISOU 1853  CB  ASP A 262     3046   3760   3218    124    226    236       C  
ATOM   1854  CG  ASP A 262     -35.211  47.545  55.215  1.00 32.13           C  
ANISOU 1854  CG  ASP A 262     3771   4508   3929    144    226    248       C  
ATOM   1855  OD1 ASP A 262     -35.942  48.526  55.469  1.00 35.25           O  
ANISOU 1855  OD1 ASP A 262     4157   4926   4311    153    215    239       O  
ATOM   1856  OD2 ASP A 262     -34.539  46.969  56.096  1.00 35.67           O  
ANISOU 1856  OD2 ASP A 262     4226   4950   4375    152    237    266       O  
ATOM   1857  N   ILE A 263     -35.871  47.899  50.771  1.00 21.36           N  
ANISOU 1857  N   ILE A 263     2403   3124   2589    108    199    190       N  
ATOM   1858  CA  ILE A 263     -35.319  47.758  49.426  1.00 22.08           C  
ANISOU 1858  CA  ILE A 263     2502   3198   2690     99    192    179       C  
ATOM   1859  C   ILE A 263     -33.907  47.178  49.536  1.00 21.62           C  
ANISOU 1859  C   ILE A 263     2460   3112   2641     97    198    192       C  
ATOM   1860  O   ILE A 263     -33.152  47.563  50.422  1.00 21.36           O  
ANISOU 1860  O   ILE A 263     2435   3079   2600    112    196    204       O  
ATOM   1861  CB  ILE A 263     -35.285  49.117  48.691  1.00 22.03           C  
ANISOU 1861  CB  ILE A 263     2502   3198   2668    116    173    164       C  
ATOM   1862  CG1 ILE A 263     -36.717  49.637  48.500  1.00 24.01           C  
ANISOU 1862  CG1 ILE A 263     2736   3478   2907    122    167    150       C  
ATOM   1863  CG2 ILE A 263     -34.523  48.993  47.362  1.00 20.58           C  
ANISOU 1863  CG2 ILE A 263     2330   2993   2494    110    167    156       C  
ATOM   1864  CD1 ILE A 263     -36.801  51.066  48.001  1.00 24.99           C  
ANISOU 1864  CD1 ILE A 263     2870   3613   3012    145    150    139       C  
ATOM   1865  N   GLU A 264     -33.555  46.223  48.681  1.00 21.21           N  
ANISOU 1865  N   GLU A 264     2412   3040   2606     80    205    190       N  
ATOM   1866  CA  GLU A 264     -32.191  45.694  48.681  1.00 21.20           C  
ANISOU 1866  CA  GLU A 264     2427   3015   2613     81    209    202       C  
ATOM   1867  C   GLU A 264     -31.116  46.788  48.677  1.00 20.00           C  
ANISOU 1867  C   GLU A 264     2286   2861   2449     99    193    200       C  
ATOM   1868  O   GLU A 264     -31.122  47.688  47.830  1.00 20.09           O  
ANISOU 1868  O   GLU A 264     2301   2874   2455    102    179    185       O  
ATOM   1869  CB  GLU A 264     -31.991  44.776  47.474  1.00 21.83           C  
ANISOU 1869  CB  GLU A 264     2509   3073   2710     62    215    194       C  
ATOM   1870  CG  GLU A 264     -30.595  44.177  47.377  1.00 25.16           C  
ANISOU 1870  CG  GLU A 264     2947   3471   3141     63    219    205       C  
ATOM   1871  CD  GLU A 264     -30.623  42.919  46.535  1.00 34.19           C  
ANISOU 1871  CD  GLU A 264     4092   4592   4303     42    233    203       C  
ATOM   1872  OE1 GLU A 264     -30.493  43.010  45.295  1.00 27.29           O  
ANISOU 1872  OE1 GLU A 264     3220   3712   3436     34    224    187       O  
ATOM   1873  OE2 GLU A 264     -30.846  41.839  47.126  1.00 40.67           O  
ANISOU 1873  OE2 GLU A 264     4914   5404   5133     34    254    215       O  
ATOM   1874  N   TYR A 265     -30.172  46.682  49.607  1.00 17.92           N  
ANISOU 1874  N   TYR A 265     2030   2596   2182    110    196    213       N  
ATOM   1875  CA  TYR A 265     -29.094  47.665  49.714  1.00 17.10           C  
ANISOU 1875  CA  TYR A 265     1935   2493   2067    123    183    208       C  
ATOM   1876  C   TYR A 265     -27.698  47.040  49.793  1.00 15.39           C  
ANISOU 1876  C   TYR A 265     1728   2263   1856    126    187    216       C  
ATOM   1877  O   TYR A 265     -26.709  47.742  49.666  1.00 15.39           O  
ANISOU 1877  O   TYR A 265     1734   2262   1850    133    178    208       O  
ATOM   1878  CB  TYR A 265     -29.341  48.613  50.899  1.00 16.61           C  
ANISOU 1878  CB  TYR A 265     1868   2453   1987    140    178    210       C  
ATOM   1879  CG  TYR A 265     -29.244  47.936  52.248  1.00 20.40           C  
ANISOU 1879  CG  TYR A 265     2343   2942   2462    149    190    229       C  
ATOM   1880  CD1 TYR A 265     -30.369  47.363  52.842  1.00 21.40           C  
ANISOU 1880  CD1 TYR A 265     2460   3077   2590    146    202    239       C  
ATOM   1881  CD2 TYR A 265     -28.034  47.881  52.932  1.00 22.37           C  
ANISOU 1881  CD2 TYR A 265     2598   3194   2706    162    189    236       C  
ATOM   1882  CE1 TYR A 265     -30.282  46.716  54.072  1.00 26.44           C  
ANISOU 1882  CE1 TYR A 265     3098   3723   3224    156    215    259       C  
ATOM   1883  CE2 TYR A 265     -27.937  47.250  54.175  1.00 24.51           C  
ANISOU 1883  CE2 TYR A 265     2865   3475   2969    176    200    254       C  
ATOM   1884  CZ  TYR A 265     -29.063  46.676  54.732  1.00 26.96           C  
ANISOU 1884  CZ  TYR A 265     3170   3791   3281    173    214    267       C  
ATOM   1885  OH  TYR A 265     -28.963  46.037  55.945  1.00 28.58           O  
ANISOU 1885  OH  TYR A 265     3375   4004   3478    188    227    286       O  
ATOM   1886  N   GLN A 266     -27.616  45.725  49.959  1.00 15.14           N  
ANISOU 1886  N   GLN A 266     1697   2219   1834    120    202    231       N  
ATOM   1887  CA  GLN A 266     -26.354  45.047  50.235  1.00 16.04           C  
ANISOU 1887  CA  GLN A 266     1819   2324   1950    128    207    241       C  
ATOM   1888  C   GLN A 266     -25.690  44.560  48.953  1.00 16.12           C  
ANISOU 1888  C   GLN A 266     1838   2312   1975    116    206    234       C  
ATOM   1889  O   GLN A 266     -25.418  43.371  48.782  1.00 15.30           O  
ANISOU 1889  O   GLN A 266     1740   2191   1881    111    220    244       O  
ATOM   1890  CB  GLN A 266     -26.589  43.880  51.191  1.00 18.29           C  
ANISOU 1890  CB  GLN A 266     2105   2606   2235    134    228    263       C  
ATOM   1891  CG  GLN A 266     -26.959  44.354  52.590  1.00 19.37           C  
ANISOU 1891  CG  GLN A 266     2235   2768   2355    151    228    272       C  
ATOM   1892  CD  GLN A 266     -27.045  43.220  53.593  1.00 22.91           C  
ANISOU 1892  CD  GLN A 266     2687   3213   2802    161    250    297       C  
ATOM   1893  OE1 GLN A 266     -26.689  42.071  53.304  1.00 23.30           O  
ANISOU 1893  OE1 GLN A 266     2747   3242   2862    158    266    308       O  
ATOM   1894  NE2 GLN A 266     -27.517  43.549  54.790  1.00 20.46           N  
ANISOU 1894  NE2 GLN A 266     2371   2925   2477    176    253    306       N  
ATOM   1895  N   TRP A 267     -25.438  45.508  48.058  1.00 14.24           N  
ANISOU 1895  N   TRP A 267     1602   2072   1736    112    192    216       N  
ATOM   1896  CA  TRP A 267     -24.764  45.227  46.802  1.00 15.07           C  
ANISOU 1896  CA  TRP A 267     1715   2158   1852    101    189    207       C  
ATOM   1897  C   TRP A 267     -24.228  46.567  46.311  1.00 15.31           C  
ANISOU 1897  C   TRP A 267     1750   2192   1874    104    174    190       C  
ATOM   1898  O   TRP A 267     -24.331  47.578  47.015  1.00 13.52           O  
ANISOU 1898  O   TRP A 267     1520   1981   1633    114    168    186       O  
ATOM   1899  CB  TRP A 267     -25.696  44.549  45.786  1.00 16.48           C  
ANISOU 1899  CB  TRP A 267     1892   2323   2045     83    195    203       C  
ATOM   1900  CG  TRP A 267     -24.923  43.827  44.708  1.00 17.37           C  
ANISOU 1900  CG  TRP A 267     2014   2414   2172     73    197    199       C  
ATOM   1901  CD1 TRP A 267     -24.758  44.223  43.409  1.00 18.34           C  
ANISOU 1901  CD1 TRP A 267     2141   2528   2299     65    187    184       C  
ATOM   1902  CD2 TRP A 267     -24.147  42.628  44.862  1.00 17.90           C  
ANISOU 1902  CD2 TRP A 267     2088   2466   2248     73    209    212       C  
ATOM   1903  NE1 TRP A 267     -23.960  43.326  42.733  1.00 16.02           N  
ANISOU 1903  NE1 TRP A 267     1853   2214   2017     58    193    185       N  
ATOM   1904  CE2 TRP A 267     -23.571  42.338  43.602  1.00 18.87           C  
ANISOU 1904  CE2 TRP A 267     2217   2570   2381     63    206    203       C  
ATOM   1905  CE3 TRP A 267     -23.914  41.753  45.930  1.00 19.75           C  
ANISOU 1905  CE3 TRP A 267     2324   2699   2479     83    224    232       C  
ATOM   1906  CZ2 TRP A 267     -22.760  41.217  43.393  1.00 18.15           C  
ANISOU 1906  CZ2 TRP A 267     2134   2461   2299     62    216    211       C  
ATOM   1907  CZ3 TRP A 267     -23.099  40.643  45.721  1.00 19.51           C  
ANISOU 1907  CZ3 TRP A 267     2305   2650   2458     84    235    242       C  
ATOM   1908  CH2 TRP A 267     -22.545  40.379  44.465  1.00 17.46           C  
ANISOU 1908  CH2 TRP A 267     2050   2372   2209     73    231    231       C  
ATOM   1909  N   ALA A 268     -23.644  46.553  45.117  1.00 14.34           N  
ANISOU 1909  N   ALA A 268     1635   2053   1759     96    171    180       N  
ATOM   1910  CA  ALA A 268     -23.116  47.747  44.474  1.00 14.37           C  
ANISOU 1910  CA  ALA A 268     1646   2055   1757     96    161    163       C  
ATOM   1911  C   ALA A 268     -24.003  48.165  43.306  1.00 14.92           C  
ANISOU 1911  C   ALA A 268     1720   2118   1830     89    157    153       C  
ATOM   1912  O   ALA A 268     -24.578  47.331  42.596  1.00 13.50           O  
ANISOU 1912  O   ALA A 268     1537   1930   1660     80    160    154       O  
ATOM   1913  CB  ALA A 268     -21.715  47.460  43.927  1.00 13.03           C  
ANISOU 1913  CB  ALA A 268     1483   1872   1593     93    161    158       C  
ATOM   1914  N   HIS A 269     -24.049  49.476  43.105  1.00 13.01           N  
ANISOU 1914  N   HIS A 269     1485   1880   1576     95    151    141       N  
ATOM   1915  CA  HIS A 269     -24.390  50.068  41.822  1.00 14.42           C  
ANISOU 1915  CA  HIS A 269     1674   2049   1753     94    147    129       C  
ATOM   1916  C   HIS A 269     -23.482  49.437  40.763  1.00 12.96           C  
ANISOU 1916  C   HIS A 269     1496   1845   1581     84    148    126       C  
ATOM   1917  O   HIS A 269     -22.260  49.444  40.906  1.00 13.04           O  
ANISOU 1917  O   HIS A 269     1511   1848   1593     82    150    124       O  
ATOM   1918  CB  HIS A 269     -24.152  51.578  41.905  1.00 12.36           C  
ANISOU 1918  CB  HIS A 269     1427   1790   1479    104    145    119       C  
ATOM   1919  CG  HIS A 269     -24.695  52.340  40.741  1.00 14.10           C  
ANISOU 1919  CG  HIS A 269     1660   2003   1693    109    143    109       C  
ATOM   1920  ND1 HIS A 269     -25.993  52.806  40.704  1.00 14.34           N  
ANISOU 1920  ND1 HIS A 269     1688   2048   1713    120    139    109       N  
ATOM   1921  CD2 HIS A 269     -24.124  52.722  39.573  1.00 15.51           C  
ANISOU 1921  CD2 HIS A 269     1855   2165   1873    107    144    101       C  
ATOM   1922  CE1 HIS A 269     -26.197  53.442  39.563  1.00 14.13           C  
ANISOU 1922  CE1 HIS A 269     1676   2013   1679    128    138    100       C  
ATOM   1923  NE2 HIS A 269     -25.081  53.402  38.856  1.00 15.53           N  
ANISOU 1923  NE2 HIS A 269     1866   2170   1864    119    142     96       N  
ATOM   1924  N   CYS A 270     -24.073  48.903  39.698  1.00 12.94           N  
ANISOU 1924  N   CYS A 270     1493   1836   1585     77    147    123       N  
ATOM   1925  CA  CYS A 270     -23.308  48.159  38.705  1.00 12.37           C  
ANISOU 1925  CA  CYS A 270     1426   1747   1526     67    149    120       C  
ATOM   1926  C   CYS A 270     -24.111  47.937  37.434  1.00 12.48           C  
ANISOU 1926  C   CYS A 270     1440   1758   1543     64    146    112       C  
ATOM   1927  O   CYS A 270     -25.303  48.274  37.361  1.00 11.53           O  
ANISOU 1927  O   CYS A 270     1314   1652   1415     70    142    108       O  
ATOM   1928  CB  CYS A 270     -22.875  46.798  39.259  1.00 10.27           C  
ANISOU 1928  CB  CYS A 270     1151   1475   1272     60    156    132       C  
ATOM   1929  SG  CYS A 270     -24.271  45.682  39.578  1.00 15.67           S  
ANISOU 1929  SG  CYS A 270     1821   2167   1965     52    162    140       S  
ATOM   1930  N   TRP A 271     -23.462  47.321  36.452  1.00 11.82           N  
ANISOU 1930  N   TRP A 271     1362   1659   1470     55    147    108       N  
ATOM   1931  CA  TRP A 271     -24.064  47.126  35.127  1.00 12.47           C  
ANISOU 1931  CA  TRP A 271     1444   1739   1554     53    143     98       C  
ATOM   1932  C   TRP A 271     -25.427  46.434  35.179  1.00 13.40           C  
ANISOU 1932  C   TRP A 271     1544   1871   1675     47    144     95       C  
ATOM   1933  O   TRP A 271     -26.251  46.638  34.292  1.00 14.00           O  
ANISOU 1933  O   TRP A 271     1616   1957   1745     51    139     84       O  
ATOM   1934  CB  TRP A 271     -23.104  46.333  34.222  1.00 12.07           C  
ANISOU 1934  CB  TRP A 271     1399   1668   1516     42    146     95       C  
ATOM   1935  CG  TRP A 271     -22.783  44.943  34.770  1.00 11.56           C  
ANISOU 1935  CG  TRP A 271     1326   1596   1468     30    154    105       C  
ATOM   1936  CD1 TRP A 271     -21.675  44.570  35.485  1.00 13.98           C  
ANISOU 1936  CD1 TRP A 271     1636   1895   1779     30    158    115       C  
ATOM   1937  CD2 TRP A 271     -23.580  43.760  34.623  1.00 12.71           C  
ANISOU 1937  CD2 TRP A 271     1460   1743   1626     18    159    105       C  
ATOM   1938  NE1 TRP A 271     -21.740  43.225  35.800  1.00 10.81           N  
ANISOU 1938  NE1 TRP A 271     1228   1486   1390     21    168    124       N  
ATOM   1939  CE2 TRP A 271     -22.897  42.705  35.279  1.00 14.84           C  
ANISOU 1939  CE2 TRP A 271     1730   2000   1907     11    170    118       C  
ATOM   1940  CE3 TRP A 271     -24.795  43.484  33.985  1.00 11.18           C  
ANISOU 1940  CE3 TRP A 271     1254   1558   1433     11    158     93       C  
ATOM   1941  CZ2 TRP A 271     -23.399  41.400  35.332  1.00 12.04           C  
ANISOU 1941  CZ2 TRP A 271     1368   1637   1566     -1    182    121       C  
ATOM   1942  CZ3 TRP A 271     -25.298  42.181  34.037  1.00 11.95           C  
ANISOU 1942  CZ3 TRP A 271     1342   1652   1546     -4    169     93       C  
ATOM   1943  CH2 TRP A 271     -24.601  41.160  34.705  1.00 11.73           C  
ANISOU 1943  CH2 TRP A 271     1318   1606   1531    -12    182    107       C  
ATOM   1944  N   ASP A 272     -25.653  45.609  36.199  1.00 12.95           N  
ANISOU 1944  N   ASP A 272     1475   1817   1626     39    151    106       N  
ATOM   1945  CA  ASP A 272     -26.887  44.832  36.348  1.00 13.33           C  
ANISOU 1945  CA  ASP A 272     1505   1877   1680     29    156    103       C  
ATOM   1946  C   ASP A 272     -27.975  45.553  37.135  1.00 14.65           C  
ANISOU 1946  C   ASP A 272     1663   2069   1834     39    153    102       C  
ATOM   1947  O   ASP A 272     -29.158  45.220  37.023  1.00 15.65           O  
ANISOU 1947  O   ASP A 272     1773   2211   1960     33    155     94       O  
ATOM   1948  CB  ASP A 272     -26.604  43.492  37.045  1.00 12.66           C  
ANISOU 1948  CB  ASP A 272     1417   1780   1612     15    171    115       C  
ATOM   1949  CG  ASP A 272     -27.837  42.605  37.108  1.00 15.75           C  
ANISOU 1949  CG  ASP A 272     1791   2180   2012      0    180    109       C  
ATOM   1950  OD1 ASP A 272     -28.304  42.191  36.029  1.00 16.49           O  
ANISOU 1950  OD1 ASP A 272     1878   2274   2111    -10    180     93       O  
ATOM   1951  OD2 ASP A 272     -28.350  42.330  38.214  1.00 17.05           O  
ANISOU 1951  OD2 ASP A 272     1949   2351   2177     -2    190    119       O  
ATOM   1952  N   ASP A 273     -27.577  46.552  37.923  1.00 14.16           N  
ANISOU 1952  N   ASP A 273     1609   2010   1759     53    149    110       N  
ATOM   1953  CA  ASP A 273     -28.478  47.094  38.938  1.00 15.74           C  
ANISOU 1953  CA  ASP A 273     1800   2231   1948     62    149    113       C  
ATOM   1954  C   ASP A 273     -28.054  48.502  39.340  1.00 14.10           C  
ANISOU 1954  C   ASP A 273     1606   2027   1724     80    142    115       C  
ATOM   1955  O   ASP A 273     -27.041  48.706  40.007  1.00 12.33           O  
ANISOU 1955  O   ASP A 273     1390   1793   1500     82    144    123       O  
ATOM   1956  CB  ASP A 273     -28.521  46.148  40.142  1.00 13.71           C  
ANISOU 1956  CB  ASP A 273     1533   1973   1700     53    160    128       C  
ATOM   1957  CG  ASP A 273     -29.644  46.478  41.108  1.00 18.47           C  
ANISOU 1957  CG  ASP A 273     2123   2599   2293     58    161    130       C  
ATOM   1958  OD1 ASP A 273     -30.311  47.529  40.959  1.00 15.10           O  
ANISOU 1958  OD1 ASP A 273     1695   2190   1851     72    152    122       O  
ATOM   1959  OD2 ASP A 273     -29.847  45.676  42.042  1.00 20.37           O  
ANISOU 1959  OD2 ASP A 273     2357   2840   2541     51    173    142       O  
ATOM   1960  N   CYS A 274     -28.834  49.465  38.867  1.00 14.64           N  
ANISOU 1960  N   CYS A 274     1676   2108   1776     94    135    105       N  
ATOM   1961  CA  CYS A 274     -28.526  50.876  39.057  1.00 14.25           C  
ANISOU 1961  CA  CYS A 274     1643   2058   1711    112    132    104       C  
ATOM   1962  C   CYS A 274     -29.512  51.555  39.997  1.00 13.94           C  
ANISOU 1962  C   CYS A 274     1596   2041   1657    125    130    106       C  
ATOM   1963  O   CYS A 274     -29.558  52.787  40.019  1.00 13.01           O  
ANISOU 1963  O   CYS A 274     1493   1925   1523    142    127    102       O  
ATOM   1964  CB  CYS A 274     -28.563  51.595  37.702  1.00 12.32           C  
ANISOU 1964  CB  CYS A 274     1414   1808   1456    123    127     93       C  
ATOM   1965  SG  CYS A 274     -27.086  51.317  36.695  1.00 16.19           S  
ANISOU 1965  SG  CYS A 274     1922   2269   1960    113    131     91       S  
ATOM   1966  N   HIS A 275     -30.304  50.784  40.744  1.00 14.00           N  
ANISOU 1966  N   HIS A 275     1584   2064   1670    117    132    111       N  
ATOM   1967  CA  HIS A 275     -31.271  51.426  41.636  1.00 14.87           C  
ANISOU 1967  CA  HIS A 275     1686   2198   1766    130    130    112       C  
ATOM   1968  C   HIS A 275     -30.615  52.214  42.760  1.00 15.48           C  
ANISOU 1968  C   HIS A 275     1773   2272   1836    139    132    120       C  
ATOM   1969  O   HIS A 275     -31.203  53.186  43.214  1.00 15.02           O  
ANISOU 1969  O   HIS A 275     1716   2227   1761    155    129    118       O  
ATOM   1970  CB  HIS A 275     -32.365  50.488  42.139  1.00 13.61           C  
ANISOU 1970  CB  HIS A 275     1501   2057   1612    120    134    113       C  
ATOM   1971  CG  HIS A 275     -31.968  49.608  43.279  1.00 15.20           C  
ANISOU 1971  CG  HIS A 275     1696   2253   1826    107    145    128       C  
ATOM   1972  ND1 HIS A 275     -31.350  48.391  43.096  1.00 15.90           N  
ANISOU 1972  ND1 HIS A 275     1784   2323   1933     89    153    134       N  
ATOM   1973  CD2 HIS A 275     -32.177  49.729  44.613  1.00 16.28           C  
ANISOU 1973  CD2 HIS A 275     1827   2401   1958    112    149    139       C  
ATOM   1974  CE1 HIS A 275     -31.150  47.819  44.271  1.00 17.75           C  
ANISOU 1974  CE1 HIS A 275     2014   2556   2172     85    163    149       C  
ATOM   1975  NE2 HIS A 275     -31.663  48.600  45.205  1.00 15.83           N  
ANISOU 1975  NE2 HIS A 275     1766   2331   1914     98    160    152       N  
ATOM   1976  N   TYR A 276     -29.402  51.821  43.154  1.00 14.95           N  
ANISOU 1976  N   TYR A 276     1711   2188   1779    129    136    127       N  
ATOM   1977  CA  TYR A 276     -28.609  52.542  44.148  1.00 15.84           C  
ANISOU 1977  CA  TYR A 276     1832   2300   1885    136    138    131       C  
ATOM   1978  C   TYR A 276     -28.372  53.989  43.712  1.00 15.75           C  
ANISOU 1978  C   TYR A 276     1841   2282   1860    149    135    120       C  
ATOM   1979  O   TYR A 276     -28.710  54.919  44.447  1.00 16.75           O  
ANISOU 1979  O   TYR A 276     1970   2419   1973    161    135    118       O  
ATOM   1980  CB  TYR A 276     -27.288  51.813  44.419  1.00 16.03           C  
ANISOU 1980  CB  TYR A 276     1857   2309   1921    125    142    136       C  
ATOM   1981  CG  TYR A 276     -27.509  50.329  44.686  1.00 18.38           C  
ANISOU 1981  CG  TYR A 276     2141   2608   2233    114    148    148       C  
ATOM   1982  CD1 TYR A 276     -27.838  49.862  45.961  1.00 16.70           C  
ANISOU 1982  CD1 TYR A 276     1916   2408   2019    116    153    161       C  
ATOM   1983  CD2 TYR A 276     -27.455  49.405  43.647  1.00 18.70           C  
ANISOU 1983  CD2 TYR A 276     2181   2635   2288    101    150    146       C  
ATOM   1984  CE1 TYR A 276     -28.062  48.504  46.186  1.00 17.52           C  
ANISOU 1984  CE1 TYR A 276     2011   2509   2135    106    163    172       C  
ATOM   1985  CE2 TYR A 276     -27.672  48.050  43.873  1.00 20.47           C  
ANISOU 1985  CE2 TYR A 276     2396   2856   2525     89    159    156       C  
ATOM   1986  CZ  TYR A 276     -27.978  47.618  45.142  1.00 19.46           C  
ANISOU 1986  CZ  TYR A 276     2259   2739   2396     92    166    169       C  
ATOM   1987  OH  TYR A 276     -28.225  46.274  45.356  1.00 35.97           O  
ANISOU 1987  OH  TYR A 276     4343   4823   4499     81    179    180       O  
ATOM   1988  N   GLY A 277     -27.823  54.187  42.513  1.00 15.22           N  
ANISOU 1988  N   GLY A 277     1789   2196   1796    146    136    112       N  
ATOM   1989  CA  GLY A 277     -27.557  55.531  42.002  1.00 13.19           C  
ANISOU 1989  CA  GLY A 277     1556   1928   1527    158    138    103       C  
ATOM   1990  C   GLY A 277     -28.864  56.278  41.783  1.00 14.82           C  
ANISOU 1990  C   GLY A 277     1765   2149   1715    179    135    100       C  
ATOM   1991  O   GLY A 277     -28.967  57.481  42.044  1.00 13.96           O  
ANISOU 1991  O   GLY A 277     1672   2039   1591    193    138     96       O  
ATOM   1992  N   ALA A 278     -29.871  55.578  41.267  1.00 15.20           N  
ANISOU 1992  N   ALA A 278     1797   2212   1764    180    129    100       N  
ATOM   1993  CA  ALA A 278     -31.168  56.223  41.054  1.00 15.37           C  
ANISOU 1993  CA  ALA A 278     1818   2254   1767    202    124     96       C  
ATOM   1994  C   ALA A 278     -31.740  56.752  42.386  1.00 16.32           C  
ANISOU 1994  C   ALA A 278     1930   2392   1876    211    124    101       C  
ATOM   1995  O   ALA A 278     -32.278  57.860  42.443  1.00 17.52           O  
ANISOU 1995  O   ALA A 278     2096   2551   2010    233    124     97       O  
ATOM   1996  CB  ALA A 278     -32.136  55.275  40.365  1.00 13.53           C  
ANISOU 1996  CB  ALA A 278     1563   2039   1537    198    118     92       C  
ATOM   1997  N   MET A 279     -31.613  55.995  43.466  1.00 16.14           N  
ANISOU 1997  N   MET A 279     1889   2376   1865    197    125    109       N  
ATOM   1998  CA  MET A 279     -32.185  56.447  44.741  1.00 17.99           C  
ANISOU 1998  CA  MET A 279     2115   2630   2089    206    125    113       C  
ATOM   1999  C   MET A 279     -31.464  57.687  45.255  1.00 17.73           C  
ANISOU 1999  C   MET A 279     2104   2584   2046    216    129    110       C  
ATOM   2000  O   MET A 279     -32.078  58.589  45.822  1.00 17.78           O  
ANISOU 2000  O   MET A 279     2115   2604   2037    233    129    108       O  
ATOM   2001  CB  MET A 279     -32.131  55.342  45.804  1.00 17.69           C  
ANISOU 2001  CB  MET A 279     2056   2600   2064    190    127    124       C  
ATOM   2002  CG  MET A 279     -32.961  54.097  45.522  1.00 23.18           C  
ANISOU 2002  CG  MET A 279     2728   3307   2769    178    127    126       C  
ATOM   2003  SD  MET A 279     -34.735  54.389  45.518  1.00 28.27           S  
ANISOU 2003  SD  MET A 279     3356   3986   3399    192    123    119       S  
ATOM   2004  CE  MET A 279     -35.068  54.336  47.285  1.00 30.13           C  
ANISOU 2004  CE  MET A 279     3578   4239   3631    193    127    131       C  
ATOM   2005  N   ILE A 280     -30.149  57.726  45.089  1.00 16.19           N  
ANISOU 2005  N   ILE A 280     1923   2368   1861    204    134    108       N  
ATOM   2006  CA  ILE A 280     -29.371  58.923  45.404  1.00 16.92           C  
ANISOU 2006  CA  ILE A 280     2036   2445   1945    209    142    100       C  
ATOM   2007  C   ILE A 280     -29.844  60.141  44.604  1.00 18.57           C  
ANISOU 2007  C   ILE A 280     2271   2645   2137    229    146     92       C  
ATOM   2008  O   ILE A 280     -30.071  61.211  45.178  1.00 17.87           O  
ANISOU 2008  O   ILE A 280     2194   2558   2035    242    151     89       O  
ATOM   2009  CB  ILE A 280     -27.867  58.640  45.235  1.00 16.03           C  
ANISOU 2009  CB  ILE A 280     1929   2313   1847    190    147     95       C  
ATOM   2010  CG1 ILE A 280     -27.416  57.761  46.411  1.00 16.04           C  
ANISOU 2010  CG1 ILE A 280     1908   2328   1857    179    144    103       C  
ATOM   2011  CG2 ILE A 280     -27.032  59.932  45.078  1.00 16.44           C  
ANISOU 2011  CG2 ILE A 280     2008   2344   1892    191    158     82       C  
ATOM   2012  CD1 ILE A 280     -26.047  57.103  46.232  1.00 18.42           C  
ANISOU 2012  CD1 ILE A 280     2209   2617   2173    162    147    100       C  
ATOM   2013  N   LEU A 281     -30.037  59.971  43.298  1.00 16.87           N  
ANISOU 2013  N   LEU A 281     2064   2422   1922    233    145     91       N  
ATOM   2014  CA  LEU A 281     -30.546  61.047  42.445  1.00 17.33           C  
ANISOU 2014  CA  LEU A 281     2149   2473   1962    257    149     86       C  
ATOM   2015  C   LEU A 281     -31.934  61.532  42.883  1.00 17.09           C  
ANISOU 2015  C   LEU A 281     2111   2468   1911    282    144     88       C  
ATOM   2016  O   LEU A 281     -32.192  62.739  42.902  1.00 18.36           O  
ANISOU 2016  O   LEU A 281     2296   2623   2054    304    151     85       O  
ATOM   2017  CB  LEU A 281     -30.560  60.595  40.979  1.00 16.21           C  
ANISOU 2017  CB  LEU A 281     2013   2323   1823    259    147     85       C  
ATOM   2018  CG  LEU A 281     -29.166  60.349  40.391  1.00 16.80           C  
ANISOU 2018  CG  LEU A 281     2100   2369   1914    238    155     81       C  
ATOM   2019  CD1 LEU A 281     -29.240  59.591  39.051  1.00 16.84           C  
ANISOU 2019  CD1 LEU A 281     2102   2370   1923    236    150     81       C  
ATOM   2020  CD2 LEU A 281     -28.392  61.660  40.222  1.00 19.03           C  
ANISOU 2020  CD2 LEU A 281     2418   2623   2187    244    172     74       C  
ATOM   2021  N   LEU A 282     -32.808  60.599  43.254  1.00 16.57           N  
ANISOU 2021  N   LEU A 282     2014   2432   1850    279    133     93       N  
ATOM   2022  CA  LEU A 282     -34.173  60.928  43.688  1.00 18.17           C  
ANISOU 2022  CA  LEU A 282     2204   2663   2033    301    127     93       C  
ATOM   2023  C   LEU A 282     -34.189  61.616  45.058  1.00 19.27           C  
ANISOU 2023  C   LEU A 282     2345   2809   2167    305    130     95       C  
ATOM   2024  O   LEU A 282     -34.997  62.525  45.305  1.00 19.00           O  
ANISOU 2024  O   LEU A 282     2319   2787   2112    331    131     94       O  
ATOM   2025  CB  LEU A 282     -35.082  59.689  43.671  1.00 17.07           C  
ANISOU 2025  CB  LEU A 282     2030   2554   1902    291    117     94       C  
ATOM   2026  CG  LEU A 282     -35.437  59.145  42.278  1.00 17.39           C  
ANISOU 2026  CG  LEU A 282     2066   2598   1943    293    112     88       C  
ATOM   2027  CD1 LEU A 282     -36.153  57.815  42.385  1.00 21.17           C  
ANISOU 2027  CD1 LEU A 282     2508   3100   2433    275    106     86       C  
ATOM   2028  CD2 LEU A 282     -36.353  60.096  41.511  1.00 19.22           C  
ANISOU 2028  CD2 LEU A 282     2310   2845   2147    330    109     81       C  
ATOM   2029  N   ALA A 283     -33.296  61.179  45.939  1.00 19.25           N  
ANISOU 2029  N   ALA A 283     2335   2799   2180    283    133     99       N  
ATOM   2030  CA  ALA A 283     -33.115  61.805  47.246  1.00 19.41           C  
ANISOU 2030  CA  ALA A 283     2355   2823   2195    285    137     99       C  
ATOM   2031  C   ALA A 283     -32.854  63.293  47.063  1.00 21.35           C  
ANISOU 2031  C   ALA A 283     2635   3049   2425    302    147     90       C  
ATOM   2032  O   ALA A 283     -33.499  64.139  47.696  1.00 22.23           O  
ANISOU 2032  O   ALA A 283     2753   3173   2521    321    149     89       O  
ATOM   2033  CB  ALA A 283     -31.955  61.157  47.980  1.00 18.48           C  
ANISOU 2033  CB  ALA A 283     2228   2698   2095    260    139    101       C  
ATOM   2034  N   ARG A 284     -31.922  63.599  46.166  1.00 21.14           N  
ANISOU 2034  N   ARG A 284     2633   2993   2404    295    156     84       N  
ATOM   2035  CA  ARG A 284     -31.545  64.964  45.847  1.00 23.72           C  
ANISOU 2035  CA  ARG A 284     2997   3296   2719    308    172     76       C  
ATOM   2036  C   ARG A 284     -32.621  65.744  45.079  1.00 24.11           C  
ANISOU 2036  C   ARG A 284     3066   3347   2745    342    173     77       C  
ATOM   2037  O   ARG A 284     -32.878  66.908  45.394  1.00 25.90           O  
ANISOU 2037  O   ARG A 284     3317   3567   2955    362    184     74       O  
ATOM   2038  CB  ARG A 284     -30.187  64.979  45.125  1.00 23.50           C  
ANISOU 2038  CB  ARG A 284     2988   3235   2705    287    183     68       C  
ATOM   2039  CG  ARG A 284     -29.669  66.394  44.853  1.00 27.82           C  
ANISOU 2039  CG  ARG A 284     3576   3751   3242    295    204     58       C  
ATOM   2040  CD  ARG A 284     -28.315  66.390  44.157  1.00 28.17           C  
ANISOU 2040  CD  ARG A 284     3636   3764   3300    272    217     49       C  
ATOM   2041  NE  ARG A 284     -28.360  65.777  42.828  1.00 25.04           N  
ANISOU 2041  NE  ARG A 284     3244   3361   2908    275    213     55       N  
ATOM   2042  CZ  ARG A 284     -27.272  65.513  42.107  1.00 24.02           C  
ANISOU 2042  CZ  ARG A 284     3124   3210   2793    255    221     50       C  
ATOM   2043  NH1 ARG A 284     -26.072  65.815  42.590  1.00 20.95           N  
ANISOU 2043  NH1 ARG A 284     2739   2805   2415    231    233     37       N  
ATOM   2044  NH2 ARG A 284     -27.389  64.964  40.903  1.00 19.72           N  
ANISOU 2044  NH2 ARG A 284     2581   2660   2250    259    216     55       N  
ATOM   2045  N   ALA A 285     -33.263  65.119  44.095  1.00 23.81           N  
ANISOU 2045  N   ALA A 285     3019   3321   2704    351    164     82       N  
ATOM   2046  CA  ALA A 285     -34.332  65.771  43.338  1.00 23.16           C  
ANISOU 2046  CA  ALA A 285     2952   3249   2597    388    164     82       C  
ATOM   2047  C   ALA A 285     -35.590  66.033  44.170  1.00 24.14           C  
ANISOU 2047  C   ALA A 285     3060   3407   2704    410    155     84       C  
ATOM   2048  O   ALA A 285     -36.273  67.033  43.955  1.00 25.60           O  
ANISOU 2048  O   ALA A 285     3267   3595   2864    445    160     84       O  
ATOM   2049  CB  ALA A 285     -34.719  64.948  42.113  1.00 22.84           C  
ANISOU 2049  CB  ALA A 285     2901   3220   2558    392    154     83       C  
ATOM   2050  N   THR A 286     -35.942  65.117  45.067  1.00 22.32           N  
ANISOU 2050  N   THR A 286     2792   3203   2485    393    143     87       N  
ATOM   2051  CA  THR A 286     -37.246  65.218  45.716  1.00 22.75           C  
ANISOU 2051  CA  THR A 286     2826   3293   2522    413    134     89       C  
ATOM   2052  C   THR A 286     -37.133  65.679  47.168  1.00 23.52           C  
ANISOU 2052  C   THR A 286     2922   3395   2620    409    138     90       C  
ATOM   2053  O   THR A 286     -38.104  66.168  47.737  1.00 24.74           O  
ANISOU 2053  O   THR A 286     3070   3573   2756    432    134     91       O  
ATOM   2054  CB  THR A 286     -38.006  63.878  45.711  1.00 21.79           C  
ANISOU 2054  CB  THR A 286     2662   3205   2410    400    120     90       C  
ATOM   2055  OG1 THR A 286     -37.318  62.960  46.572  1.00 20.99           O  
ANISOU 2055  OG1 THR A 286     2541   3099   2333    366    119     95       O  
ATOM   2056  CG2 THR A 286     -38.090  63.314  44.302  1.00 21.26           C  
ANISOU 2056  CG2 THR A 286     2593   3138   2345    401    116     86       C  
ATOM   2057  N   GLY A 287     -35.970  65.479  47.781  1.00 24.24           N  
ANISOU 2057  N   GLY A 287     3013   3465   2729    382    143     90       N  
ATOM   2058  CA  GLY A 287     -35.802  65.767  49.199  1.00 26.48           C  
ANISOU 2058  CA  GLY A 287     3290   3756   3014    376    145     90       C  
ATOM   2059  C   GLY A 287     -36.606  64.869  50.125  1.00 27.81           C  
ANISOU 2059  C   GLY A 287     3419   3960   3185    370    133     97       C  
ATOM   2060  O   GLY A 287     -36.813  65.219  51.291  1.00 28.56           O  
ANISOU 2060  O   GLY A 287     3508   4069   3274    375    134     98       O  
ATOM   2061  N   LYS A 288     -37.070  63.723  49.627  1.00 27.01           N  
ANISOU 2061  N   LYS A 288     3294   3874   3093    361    125    102       N  
ATOM   2062  CA  LYS A 288     -37.882  62.815  50.437  1.00 26.78           C  
ANISOU 2062  CA  LYS A 288     3229   3877   3067    354    118    108       C  
ATOM   2063  C   LYS A 288     -37.069  61.991  51.433  1.00 28.09           C  
ANISOU 2063  C   LYS A 288     3380   4039   3252    328    120    116       C  
ATOM   2064  O   LYS A 288     -36.041  61.398  51.087  1.00 26.42           O  
ANISOU 2064  O   LYS A 288     3172   3807   3058    307    122    117       O  
ATOM   2065  CB  LYS A 288     -38.711  61.870  49.567  1.00 27.34           C  
ANISOU 2065  CB  LYS A 288     3279   3966   3142    350    111    108       C  
ATOM   2066  CG  LYS A 288     -39.815  62.563  48.796  1.00 32.39           C  
ANISOU 2066  CG  LYS A 288     3924   4624   3758    381    106    100       C  
ATOM   2067  CD  LYS A 288     -40.549  61.626  47.850  1.00 40.05           C  
ANISOU 2067  CD  LYS A 288     4870   5614   4731    376     99     94       C  
ATOM   2068  CE  LYS A 288     -41.491  60.690  48.573  1.00 40.71           C  
ANISOU 2068  CE  LYS A 288     4915   5731   4820    363     96     95       C  
ATOM   2069  NZ  LYS A 288     -42.559  60.303  47.611  1.00 45.34           N  
ANISOU 2069  NZ  LYS A 288     5481   6347   5397    372     90     82       N  
ATOM   2070  N   GLU A 289     -37.579  61.909  52.658  1.00 27.75           N  
ANISOU 2070  N   GLU A 289     3320   4019   3204    330    118    121       N  
ATOM   2071  CA  GLU A 289     -36.924  61.151  53.718  1.00 29.90           C  
ANISOU 2071  CA  GLU A 289     3577   4293   3490    312    121    129       C  
ATOM   2072  C   GLU A 289     -36.682  59.680  53.354  1.00 28.64           C  
ANISOU 2072  C   GLU A 289     3401   4129   3351    289    122    137       C  
ATOM   2073  O   GLU A 289     -35.611  59.147  53.652  1.00 27.80           O  
ANISOU 2073  O   GLU A 289     3296   4009   3258    274    125    142       O  
ATOM   2074  CB  GLU A 289     -37.739  61.259  55.012  1.00 31.51           C  
ANISOU 2074  CB  GLU A 289     3763   4525   3681    323    120    135       C  
ATOM   2075  CG  GLU A 289     -36.912  61.142  56.280  1.00 40.18           C  
ANISOU 2075  CG  GLU A 289     4858   5624   4783    316    123    140       C  
ATOM   2076  CD  GLU A 289     -36.730  59.702  56.738  1.00 53.03           C  
ANISOU 2076  CD  GLU A 289     6464   7257   6426    298    126    154       C  
ATOM   2077  OE1 GLU A 289     -37.585  58.849  56.402  1.00 57.95           O  
ANISOU 2077  OE1 GLU A 289     7072   7891   7055    291    127    160       O  
ATOM   2078  OE2 GLU A 289     -35.731  59.414  57.438  1.00 56.27           O  
ANISOU 2078  OE2 GLU A 289     6874   7662   6842    291    129    158       O  
ATOM   2079  N   GLU A 290     -37.650  59.030  52.712  1.00 27.03           N  
ANISOU 2079  N   GLU A 290     3182   3938   3149    286    120    137       N  
ATOM   2080  CA  GLU A 290     -37.505  57.625  52.330  1.00 27.67           C  
ANISOU 2080  CA  GLU A 290     3249   4015   3250    263    123    143       C  
ATOM   2081  C   GLU A 290     -36.222  57.407  51.511  1.00 25.58           C  
ANISOU 2081  C   GLU A 290     3000   3718   2998    250    124    142       C  
ATOM   2082  O   GLU A 290     -35.508  56.431  51.726  1.00 24.63           O  
ANISOU 2082  O   GLU A 290     2875   3587   2894    233    129    150       O  
ATOM   2083  CB  GLU A 290     -38.741  57.108  51.567  1.00 29.35           C  
ANISOU 2083  CB  GLU A 290     3443   4246   3461    261    121    137       C  
ATOM   2084  CG  GLU A 290     -38.684  55.616  51.164  1.00 35.92           C  
ANISOU 2084  CG  GLU A 290     4259   5072   4315    235    127    140       C  
ATOM   2085  CD  GLU A 290     -39.412  55.244  49.863  1.00 44.50           C  
ANISOU 2085  CD  GLU A 290     5336   6166   5403    230    124    127       C  
ATOM   2086  OE1 GLU A 290     -40.409  55.909  49.499  1.00 47.59           O  
ANISOU 2086  OE1 GLU A 290     5722   6581   5776    249    117    115       O  
ATOM   2087  OE2 GLU A 290     -38.997  54.260  49.202  1.00 40.07           O  
ANISOU 2087  OE2 GLU A 290     4773   5590   4860    209    128    126       O  
ATOM   2088  N   TYR A 291     -35.911  58.322  50.594  1.00 24.23           N  
ANISOU 2088  N   TYR A 291     2851   3532   2820    261    121    132       N  
ATOM   2089  CA  TYR A 291     -34.800  58.128  49.669  1.00 22.62           C  
ANISOU 2089  CA  TYR A 291     2663   3300   2629    249    123    129       C  
ATOM   2090  C   TYR A 291     -33.460  58.378  50.353  1.00 22.06           C  
ANISOU 2090  C   TYR A 291     2604   3214   2564    242    127    130       C  
ATOM   2091  O   TYR A 291     -32.468  57.702  50.073  1.00 20.07           O  
ANISOU 2091  O   TYR A 291     2353   2945   2326    226    130    132       O  
ATOM   2092  CB  TYR A 291     -34.939  59.029  48.438  1.00 23.55           C  
ANISOU 2092  CB  TYR A 291     2802   3407   2736    264    121    118       C  
ATOM   2093  CG  TYR A 291     -36.141  58.721  47.574  1.00 26.39           C  
ANISOU 2093  CG  TYR A 291     3150   3786   3089    272    116    113       C  
ATOM   2094  CD1 TYR A 291     -36.498  57.404  47.304  1.00 33.09           C  
ANISOU 2094  CD1 TYR A 291     3974   4643   3952    253    115    115       C  
ATOM   2095  CD2 TYR A 291     -36.916  59.733  47.020  1.00 24.36           C  
ANISOU 2095  CD2 TYR A 291     2904   3538   2811    299    112    106       C  
ATOM   2096  CE1 TYR A 291     -37.601  57.105  46.520  1.00 34.22           C  
ANISOU 2096  CE1 TYR A 291     4103   4808   4090    259    110    106       C  
ATOM   2097  CE2 TYR A 291     -38.023  59.444  46.222  1.00 29.09           C  
ANISOU 2097  CE2 TYR A 291     3489   4162   3402    309    106     99       C  
ATOM   2098  CZ  TYR A 291     -38.356  58.124  45.979  1.00 30.68           C  
ANISOU 2098  CZ  TYR A 291     3663   4373   3618    287    104     98       C  
ATOM   2099  OH  TYR A 291     -39.440  57.776  45.213  1.00 31.35           O  
ANISOU 2099  OH  TYR A 291     3729   4485   3695    294     99     86       O  
ATOM   2100  N   HIS A 292     -33.430  59.385  51.221  1.00 21.09           N  
ANISOU 2100  N   HIS A 292     2488   3097   2428    255    128    127       N  
ATOM   2101  CA  HIS A 292     -32.265  59.635  52.061  1.00 20.99           C  
ANISOU 2101  CA  HIS A 292     2480   3077   2417    249    132    124       C  
ATOM   2102  C   HIS A 292     -31.966  58.469  52.992  1.00 20.84           C  
ANISOU 2102  C   HIS A 292     2439   3070   2407    238    133    137       C  
ATOM   2103  O   HIS A 292     -30.801  58.119  53.199  1.00 21.31           O  
ANISOU 2103  O   HIS A 292     2500   3120   2475    229    135    136       O  
ATOM   2104  CB  HIS A 292     -32.441  60.933  52.860  1.00 20.80           C  
ANISOU 2104  CB  HIS A 292     2465   3060   2375    265    134    116       C  
ATOM   2105  CG  HIS A 292     -32.211  62.160  52.035  1.00 20.45           C  
ANISOU 2105  CG  HIS A 292     2450   2994   2323    273    139    103       C  
ATOM   2106  ND1 HIS A 292     -30.948  62.576  51.670  1.00 23.97           N  
ANISOU 2106  ND1 HIS A 292     2914   3416   2775    262    147     92       N  
ATOM   2107  CD2 HIS A 292     -33.080  63.014  51.441  1.00 21.98           C  
ANISOU 2107  CD2 HIS A 292     2660   3187   2503    292    140     99       C  
ATOM   2108  CE1 HIS A 292     -31.047  63.662  50.920  1.00 22.96           C  
ANISOU 2108  CE1 HIS A 292     2814   3270   2639    272    154     83       C  
ATOM   2109  NE2 HIS A 292     -32.328  63.959  50.779  1.00 22.53           N  
ANISOU 2109  NE2 HIS A 292     2759   3229   2570    293    150     88       N  
ATOM   2110  N   LYS A 293     -33.017  57.887  53.561  1.00 20.64           N  
ANISOU 2110  N   LYS A 293     2396   3066   2380    242    132    148       N  
ATOM   2111  CA  LYS A 293     -32.865  56.741  54.447  1.00 21.92           C  
ANISOU 2111  CA  LYS A 293     2541   3238   2550    234    136    162       C  
ATOM   2112  C   LYS A 293     -32.229  55.580  53.688  1.00 20.57           C  
ANISOU 2112  C   LYS A 293     2370   3049   2398    217    139    167       C  
ATOM   2113  O   LYS A 293     -31.320  54.921  54.199  1.00 19.88           O  
ANISOU 2113  O   LYS A 293     2279   2957   2315    213    143    175       O  
ATOM   2114  CB  LYS A 293     -34.219  56.321  55.025  1.00 22.37           C  
ANISOU 2114  CB  LYS A 293     2579   3317   2601    239    138    171       C  
ATOM   2115  CG  LYS A 293     -34.153  55.067  55.886  1.00 29.94           C  
ANISOU 2115  CG  LYS A 293     3524   4283   3569    231    146    188       C  
ATOM   2116  CD  LYS A 293     -35.538  54.592  56.303  1.00 39.18           C  
ANISOU 2116  CD  LYS A 293     4676   5473   4735    231    151    196       C  
ATOM   2117  CE  LYS A 293     -35.555  53.093  56.574  1.00 43.07           C  
ANISOU 2117  CE  LYS A 293     5159   5961   5242    217    165    211       C  
ATOM   2118  NZ  LYS A 293     -34.941  52.794  57.894  1.00 43.18           N  
ANISOU 2118  NZ  LYS A 293     5173   5982   5252    226    171    226       N  
ATOM   2119  N   PHE A 294     -32.712  55.327  52.474  1.00 20.38           N  
ANISOU 2119  N   PHE A 294     2347   3015   2380    210    138    163       N  
ATOM   2120  CA  PHE A 294     -32.168  54.228  51.666  1.00 19.25           C  
ANISOU 2120  CA  PHE A 294     2204   2853   2254    193    142    167       C  
ATOM   2121  C   PHE A 294     -30.696  54.486  51.392  1.00 16.97           C  
ANISOU 2121  C   PHE A 294     1931   2546   1971    190    141    161       C  
ATOM   2122  O   PHE A 294     -29.867  53.609  51.619  1.00 17.83           O  
ANISOU 2122  O   PHE A 294     2037   2648   2089    182    145    169       O  
ATOM   2123  CB  PHE A 294     -32.889  54.028  50.320  1.00 18.34           C  
ANISOU 2123  CB  PHE A 294     2089   2733   2145    187    139    159       C  
ATOM   2124  CG  PHE A 294     -32.196  53.023  49.445  1.00 19.33           C  
ANISOU 2124  CG  PHE A 294     2218   2838   2289    170    143    161       C  
ATOM   2125  CD1 PHE A 294     -32.422  51.668  49.619  1.00 21.84           C  
ANISOU 2125  CD1 PHE A 294     2523   3155   2620    156    151    171       C  
ATOM   2126  CD2 PHE A 294     -31.238  53.419  48.532  1.00 18.33           C  
ANISOU 2126  CD2 PHE A 294     2107   2690   2165    168    139    152       C  
ATOM   2127  CE1 PHE A 294     -31.746  50.722  48.867  1.00 17.96           C  
ANISOU 2127  CE1 PHE A 294     2035   2643   2145    141    156    172       C  
ATOM   2128  CE2 PHE A 294     -30.539  52.476  47.775  1.00 20.60           C  
ANISOU 2128  CE2 PHE A 294     2398   2960   2469    153    142    154       C  
ATOM   2129  CZ  PHE A 294     -30.813  51.131  47.931  1.00 16.72           C  
ANISOU 2129  CZ  PHE A 294     1893   2468   1990    140    150    164       C  
ATOM   2130  N   ALA A 295     -30.391  55.689  50.912  1.00 18.01           N  
ANISOU 2130  N   ALA A 295     2078   2669   2094    196    137    148       N  
ATOM   2131  CA  ALA A 295     -29.028  56.072  50.540  1.00 17.02           C  
ANISOU 2131  CA  ALA A 295     1967   2526   1973    191    138    138       C  
ATOM   2132  C   ALA A 295     -28.051  55.898  51.694  1.00 18.00           C  
ANISOU 2132  C   ALA A 295     2084   2659   2095    191    140    140       C  
ATOM   2133  O   ALA A 295     -26.956  55.371  51.512  1.00 15.95           O  
ANISOU 2133  O   ALA A 295     1825   2389   1844    183    142    139       O  
ATOM   2134  CB  ALA A 295     -28.990  57.509  50.054  1.00 16.77           C  
ANISOU 2134  CB  ALA A 295     1956   2485   1931    199    138    123       C  
ATOM   2135  N   GLN A 296     -28.446  56.372  52.876  1.00 17.25           N  
ANISOU 2135  N   GLN A 296     1981   2583   1987    203    139    142       N  
ATOM   2136  CA  GLN A 296     -27.597  56.249  54.062  1.00 16.50           C  
ANISOU 2136  CA  GLN A 296     1877   2503   1887    207    140    143       C  
ATOM   2137  C   GLN A 296     -27.452  54.806  54.544  1.00 16.41           C  
ANISOU 2137  C   GLN A 296     1852   2498   1882    206    144    162       C  
ATOM   2138  O   GLN A 296     -26.377  54.417  54.988  1.00 18.71           O  
ANISOU 2138  O   GLN A 296     2140   2794   2173    207    145    162       O  
ATOM   2139  CB  GLN A 296     -28.130  57.172  55.165  1.00 17.03           C  
ANISOU 2139  CB  GLN A 296     1941   2592   1938    221    139    139       C  
ATOM   2140  CG  GLN A 296     -27.872  58.645  54.818  1.00 18.69           C  
ANISOU 2140  CG  GLN A 296     2168   2791   2140    222    140    117       C  
ATOM   2141  CD  GLN A 296     -28.577  59.632  55.734  1.00 26.19           C  
ANISOU 2141  CD  GLN A 296     3117   3758   3073    236    139    112       C  
ATOM   2142  OE1 GLN A 296     -28.813  59.344  56.906  1.00 23.65           O  
ANISOU 2142  OE1 GLN A 296     2780   3460   2744    245    137    121       O  
ATOM   2143  NE2 GLN A 296     -28.921  60.801  55.196  1.00 22.86           N  
ANISOU 2143  NE2 GLN A 296     2715   3325   2646    240    141    100       N  
ATOM   2144  N   MET A 297     -28.511  54.010  54.449  1.00 16.71           N  
ANISOU 2144  N   MET A 297     1883   2537   1926    204    147    176       N  
ATOM   2145  CA  MET A 297     -28.434  52.584  54.748  1.00 18.88           C  
ANISOU 2145  CA  MET A 297     2151   2812   2210    201    155    195       C  
ATOM   2146  C   MET A 297     -27.423  51.890  53.837  1.00 18.02           C  
ANISOU 2146  C   MET A 297     2049   2682   2114    190    156    194       C  
ATOM   2147  O   MET A 297     -26.528  51.160  54.287  1.00 17.19           O  
ANISOU 2147  O   MET A 297     1943   2578   2011    194    161    202       O  
ATOM   2148  CB  MET A 297     -29.798  51.935  54.541  1.00 17.70           C  
ANISOU 2148  CB  MET A 297     1994   2663   2066    195    161    205       C  
ATOM   2149  CG  MET A 297     -29.915  50.520  55.100  1.00 24.68           C  
ANISOU 2149  CG  MET A 297     2871   3546   2957    192    174    226       C  
ATOM   2150  SD  MET A 297     -31.580  49.796  55.079  1.00 31.60           S  
ANISOU 2150  SD  MET A 297     3736   4427   3840    182    185    234       S  
ATOM   2151  CE  MET A 297     -32.606  51.273  55.100  1.00 36.08           C  
ANISOU 2151  CE  MET A 297     4299   5015   4392    191    172    219       C  
ATOM   2152  N   HIS A 298     -27.623  52.090  52.537  1.00 18.47           N  
ANISOU 2152  N   HIS A 298     2114   2721   2181    178    153    184       N  
ATOM   2153  CA  HIS A 298     -26.763  51.504  51.510  1.00 16.52           C  
ANISOU 2153  CA  HIS A 298     1875   2453   1947    167    154    181       C  
ATOM   2154  C   HIS A 298     -25.311  51.938  51.703  1.00 15.82           C  
ANISOU 2154  C   HIS A 298     1791   2364   1854    170    152    171       C  
ATOM   2155  O   HIS A 298     -24.415  51.103  51.791  1.00 14.51           O  
ANISOU 2155  O   HIS A 298     1623   2195   1693    170    155    177       O  
ATOM   2156  CB  HIS A 298     -27.261  51.899  50.110  1.00 17.26           C  
ANISOU 2156  CB  HIS A 298     1977   2531   2047    157    151    170       C  
ATOM   2157  CG  HIS A 298     -26.248  51.676  49.032  1.00 13.34           C  
ANISOU 2157  CG  HIS A 298     1491   2014   1561    147    150    163       C  
ATOM   2158  ND1 HIS A 298     -25.852  50.416  48.637  1.00 14.22           N  
ANISOU 2158  ND1 HIS A 298     1602   2114   1687    138    155    172       N  
ATOM   2159  CD2 HIS A 298     -25.512  52.551  48.307  1.00 13.49           C  
ANISOU 2159  CD2 HIS A 298     1523   2021   1579    144    146    148       C  
ATOM   2160  CE1 HIS A 298     -24.941  50.526  47.686  1.00 15.57           C  
ANISOU 2160  CE1 HIS A 298     1782   2267   1864    131    153    162       C  
ATOM   2161  NE2 HIS A 298     -24.714  51.811  47.472  1.00 12.73           N  
ANISOU 2161  NE2 HIS A 298     1431   1908   1496    134    148    148       N  
ATOM   2162  N   LEU A 299     -25.066  53.243  51.771  1.00 15.68           N  
ANISOU 2162  N   LEU A 299     1779   2351   1827    173    147    154       N  
ATOM   2163  CA  LEU A 299     -23.685  53.708  51.880  1.00 15.45           C  
ANISOU 2163  CA  LEU A 299     1752   2322   1794    172    146    139       C  
ATOM   2164  C   LEU A 299     -23.014  53.299  53.197  1.00 15.89           C  
ANISOU 2164  C   LEU A 299     1795   2402   1841    184    146    144       C  
ATOM   2165  O   LEU A 299     -21.830  52.949  53.209  1.00 16.55           O  
ANISOU 2165  O   LEU A 299     1875   2488   1925    184    147    139       O  
ATOM   2166  CB  LEU A 299     -23.606  55.216  51.650  1.00 14.99           C  
ANISOU 2166  CB  LEU A 299     1705   2260   1729    170    145    118       C  
ATOM   2167  CG  LEU A 299     -23.898  55.709  50.227  1.00 17.04           C  
ANISOU 2167  CG  LEU A 299     1983   2494   1995    161    146    110       C  
ATOM   2168  CD1 LEU A 299     -23.976  57.243  50.200  1.00 17.61           C  
ANISOU 2168  CD1 LEU A 299     2070   2562   2057    163    149     92       C  
ATOM   2169  CD2 LEU A 299     -22.835  55.225  49.239  1.00 15.20           C  
ANISOU 2169  CD2 LEU A 299     1756   2243   1775    148    148    105       C  
ATOM   2170  N   ASP A 300     -23.756  53.335  54.305  1.00 15.23           N  
ANISOU 2170  N   ASP A 300     1702   2339   1747    197    147    154       N  
ATOM   2171  CA  ASP A 300     -23.237  52.832  55.580  1.00 15.77           C  
ANISOU 2171  CA  ASP A 300     1757   2431   1803    214    148    162       C  
ATOM   2172  C   ASP A 300     -22.750  51.381  55.497  1.00 15.00           C  
ANISOU 2172  C   ASP A 300     1657   2328   1712    217    154    180       C  
ATOM   2173  O   ASP A 300     -21.672  51.051  56.004  1.00 15.90           O  
ANISOU 2173  O   ASP A 300     1764   2456   1818    228    153    178       O  
ATOM   2174  CB  ASP A 300     -24.316  52.938  56.671  1.00 15.77           C  
ANISOU 2174  CB  ASP A 300     1749   2450   1791    227    149    175       C  
ATOM   2175  CG  ASP A 300     -24.486  54.350  57.224  1.00 19.27           C  
ANISOU 2175  CG  ASP A 300     2191   2908   2222    231    144    156       C  
ATOM   2176  OD1 ASP A 300     -23.807  55.329  56.834  1.00 18.97           O  
ANISOU 2176  OD1 ASP A 300     2159   2865   2182    223    141    132       O  
ATOM   2177  OD2 ASP A 300     -25.376  54.501  58.079  1.00 20.50           O  
ANISOU 2177  OD2 ASP A 300     2340   3079   2367    242    144    165       O  
ATOM   2178  N   TRP A 301     -23.544  50.510  54.872  1.00 14.77           N  
ANISOU 2178  N   TRP A 301     1634   2280   1697    208    160    197       N  
ATOM   2179  CA  TRP A 301     -23.163  49.114  54.647  1.00 14.68           C  
ANISOU 2179  CA  TRP A 301     1626   2257   1695    209    169    214       C  
ATOM   2180  C   TRP A 301     -21.801  48.971  53.953  1.00 15.28           C  
ANISOU 2180  C   TRP A 301     1705   2324   1775    206    165    202       C  
ATOM   2181  O   TRP A 301     -21.046  48.032  54.226  1.00 13.47           O  
ANISOU 2181  O   TRP A 301     1475   2098   1544    217    171    213       O  
ATOM   2182  CB  TRP A 301     -24.236  48.388  53.829  1.00 14.81           C  
ANISOU 2182  CB  TRP A 301     1648   2250   1728    194    176    225       C  
ATOM   2183  CG  TRP A 301     -23.996  46.901  53.695  1.00 15.16           C  
ANISOU 2183  CG  TRP A 301     1696   2280   1782    194    189    244       C  
ATOM   2184  CD1 TRP A 301     -24.196  45.934  54.662  1.00 13.28           C  
ANISOU 2184  CD1 TRP A 301     1457   2047   1538    208    203    267       C  
ATOM   2185  CD2 TRP A 301     -23.512  46.211  52.537  1.00 16.34           C  
ANISOU 2185  CD2 TRP A 301     1855   2405   1947    181    192    242       C  
ATOM   2186  NE1 TRP A 301     -23.858  44.696  54.166  1.00 13.02           N  
ANISOU 2186  NE1 TRP A 301     1434   1992   1517    204    216    279       N  
ATOM   2187  CE2 TRP A 301     -23.435  44.836  52.869  1.00 13.97           C  
ANISOU 2187  CE2 TRP A 301     1559   2095   1651    187    208    264       C  
ATOM   2188  CE3 TRP A 301     -23.116  46.625  51.257  1.00 16.60           C  
ANISOU 2188  CE3 TRP A 301     1893   2422   1990    165    184    225       C  
ATOM   2189  CZ2 TRP A 301     -23.000  43.867  51.960  1.00 14.89           C  
ANISOU 2189  CZ2 TRP A 301     1685   2187   1782    177    216    268       C  
ATOM   2190  CZ3 TRP A 301     -22.668  45.657  50.354  1.00 17.49           C  
ANISOU 2190  CZ3 TRP A 301     2014   2513   2118    156    190    229       C  
ATOM   2191  CH2 TRP A 301     -22.627  44.295  50.712  1.00 13.54           C  
ANISOU 2191  CH2 TRP A 301     1517   2004   1622    162    205    250       C  
ATOM   2192  N   TRP A 302     -21.498  49.904  53.050  1.00 14.34           N  
ANISOU 2192  N   TRP A 302     1591   2195   1661    191    158    181       N  
ATOM   2193  CA  TRP A 302     -20.186  49.977  52.391  1.00 14.40           C  
ANISOU 2193  CA  TRP A 302     1601   2196   1671    185    155    166       C  
ATOM   2194  C   TRP A 302     -19.017  50.529  53.222  1.00 14.57           C  
ANISOU 2194  C   TRP A 302     1612   2246   1678    197    151    149       C  
ATOM   2195  O   TRP A 302     -17.854  50.240  52.910  1.00 15.13           O  
ANISOU 2195  O   TRP A 302     1680   2318   1749    197    150    140       O  
ATOM   2196  CB  TRP A 302     -20.309  50.766  51.086  1.00 13.09           C  
ANISOU 2196  CB  TRP A 302     1447   2009   1517    166    152    149       C  
ATOM   2197  CG  TRP A 302     -20.832  49.888  49.993  1.00 12.47           C  
ANISOU 2197  CG  TRP A 302     1377   1905   1455    154    156    161       C  
ATOM   2198  CD1 TRP A 302     -22.153  49.667  49.675  1.00 12.41           C  
ANISOU 2198  CD1 TRP A 302     1371   1888   1454    149    158    171       C  
ATOM   2199  CD2 TRP A 302     -20.063  49.058  49.120  1.00 13.66           C  
ANISOU 2199  CD2 TRP A 302     1533   2040   1618    147    158    162       C  
ATOM   2200  NE1 TRP A 302     -22.243  48.768  48.636  1.00 11.24           N  
ANISOU 2200  NE1 TRP A 302     1229   1719   1321    138    161    176       N  
ATOM   2201  CE2 TRP A 302     -20.977  48.369  48.289  1.00 13.27           C  
ANISOU 2201  CE2 TRP A 302     1490   1971   1582    137    162    172       C  
ATOM   2202  CE3 TRP A 302     -18.688  48.838  48.950  1.00 10.48           C  
ANISOU 2202  CE3 TRP A 302     1129   1638   1214    149    157    153       C  
ATOM   2203  CZ2 TRP A 302     -20.560  47.467  47.306  1.00 10.45           C  
ANISOU 2203  CZ2 TRP A 302     1139   1593   1239    128    165    175       C  
ATOM   2204  CZ3 TRP A 302     -18.274  47.951  47.953  1.00 13.35           C  
ANISOU 2204  CZ3 TRP A 302     1498   1981   1590    141    160    158       C  
ATOM   2205  CH2 TRP A 302     -19.211  47.285  47.143  1.00 13.32           C  
ANISOU 2205  CH2 TRP A 302     1502   1956   1601    130    164    169       C  
ATOM   2206  N   THR A 303     -19.313  51.351  54.230  1.00 14.98           N  
ANISOU 2206  N   THR A 303     1656   2320   1715    206    148    142       N  
ATOM   2207  CA  THR A 303     -18.271  51.967  55.065  1.00 16.72           C  
ANISOU 2207  CA  THR A 303     1863   2570   1919    216    144    121       C  
ATOM   2208  C   THR A 303     -17.680  50.988  56.079  1.00 16.91           C  
ANISOU 2208  C   THR A 303     1874   2621   1930    241    145    135       C  
ATOM   2209  O   THR A 303     -18.307  49.974  56.395  1.00 16.62           O  
ANISOU 2209  O   THR A 303     1840   2579   1893    253    151    163       O  
ATOM   2210  CB  THR A 303     -18.772  53.199  55.852  1.00 17.03           C  
ANISOU 2210  CB  THR A 303     1897   2625   1946    218    141    107       C  
ATOM   2211  OG1 THR A 303     -19.765  52.792  56.804  1.00 19.64           O  
ANISOU 2211  OG1 THR A 303     2224   2969   2270    234    142    130       O  
ATOM   2212  CG2 THR A 303     -19.344  54.257  54.911  1.00 16.91           C  
ANISOU 2212  CG2 THR A 303     1898   2585   1942    197    142     94       C  
ATOM   2213  N   PRO A 304     -16.475  51.285  56.600  1.00 16.89           N  
ANISOU 2213  N   PRO A 304     1856   2647   1912    251    140    114       N  
ATOM   2214  CA  PRO A 304     -15.895  50.374  57.581  1.00 17.02           C  
ANISOU 2214  CA  PRO A 304     1861   2693   1911    281    141    127       C  
ATOM   2215  C   PRO A 304     -16.702  50.210  58.871  1.00 17.98           C  
ANISOU 2215  C   PRO A 304     1977   2835   2017    304    143    146       C  
ATOM   2216  O   PRO A 304     -16.545  49.184  59.524  1.00 18.02           O  
ANISOU 2216  O   PRO A 304     1980   2854   2011    331    148    168       O  
ATOM   2217  CB  PRO A 304     -14.531  51.018  57.885  1.00 18.24           C  
ANISOU 2217  CB  PRO A 304     1997   2881   2052    284    134     92       C  
ATOM   2218  CG  PRO A 304     -14.179  51.729  56.608  1.00 17.65           C  
ANISOU 2218  CG  PRO A 304     1931   2779   1995    251    134     69       C  
ATOM   2219  CD  PRO A 304     -15.519  52.348  56.233  1.00 15.62           C  
ANISOU 2219  CD  PRO A 304     1690   2493   1751    235    137     77       C  
ATOM   2220  N   GLN A 305     -17.533  51.183  59.238  1.00 18.41           N  
ANISOU 2220  N   GLN A 305     2031   2892   2070    296    141    138       N  
ATOM   2221  CA  GLN A 305     -18.366  51.078  60.441  1.00 20.22           C  
ANISOU 2221  CA  GLN A 305     2255   3141   2285    317    143    156       C  
ATOM   2222  C   GLN A 305     -19.633  50.252  60.185  1.00 19.44           C  
ANISOU 2222  C   GLN A 305     2171   3014   2199    314    153    189       C  
ATOM   2223  O   GLN A 305     -20.215  49.713  61.115  1.00 16.93           O  
ANISOU 2223  O   GLN A 305     1852   2709   1871    333    159    212       O  
ATOM   2224  CB  GLN A 305     -18.726  52.458  61.003  1.00 19.89           C  
ANISOU 2224  CB  GLN A 305     2206   3116   2234    312    137    134       C  
ATOM   2225  CG  GLN A 305     -17.522  53.265  61.492  1.00 27.64           C  
ANISOU 2225  CG  GLN A 305     3169   4130   3200    316    130     98       C  
ATOM   2226  CD  GLN A 305     -16.992  52.794  62.852  1.00 27.95           C  
ANISOU 2226  CD  GLN A 305     3190   4215   3212    351    127    102       C  
ATOM   2227  OE1 GLN A 305     -17.751  52.354  63.714  1.00 33.40           O  
ANISOU 2227  OE1 GLN A 305     3881   4916   3893    372    131    127       O  
ATOM   2228  NE2 GLN A 305     -15.688  52.908  63.051  1.00 28.15           N  
ANISOU 2228  NE2 GLN A 305     3198   4271   3225    359    122     77       N  
ATOM   2229  N   GLY A 306     -20.037  50.094  58.926  1.00 19.05           N  
ANISOU 2229  N   GLY A 306     2135   2929   2172    289    155    192       N  
ATOM   2230  CA  GLY A 306     -21.191  49.250  58.623  1.00 18.48           C  
ANISOU 2230  CA  GLY A 306     2074   2832   2114    283    166    219       C  
ATOM   2231  C   GLY A 306     -22.530  49.888  58.957  1.00 19.29           C  
ANISOU 2231  C   GLY A 306     2177   2936   2216    278    166    221       C  
ATOM   2232  O   GLY A 306     -22.602  51.052  59.345  1.00 19.97           O  
ANISOU 2232  O   GLY A 306     2256   3037   2292    278    157    203       O  
ATOM   2233  N   TYR A 307     -23.598  49.115  58.790  1.00 18.89           N  
ANISOU 2233  N   TYR A 307     2132   2868   2175    272    176    243       N  
ATOM   2234  CA  TYR A 307     -24.953  49.535  59.120  1.00 19.74           C  
ANISOU 2234  CA  TYR A 307     2237   2978   2282    268    178    248       C  
ATOM   2235  C   TYR A 307     -25.525  48.520  60.108  1.00 19.74           C  
ANISOU 2235  C   TYR A 307     2236   2986   2276    284    193    276       C  
ATOM   2236  O   TYR A 307     -25.904  47.416  59.709  1.00 17.49           O  
ANISOU 2236  O   TYR A 307     1960   2681   2005    276    207    293       O  
ATOM   2237  CB  TYR A 307     -25.827  49.579  57.855  1.00 19.52           C  
ANISOU 2237  CB  TYR A 307     2217   2924   2274    243    178    244       C  
ATOM   2238  CG  TYR A 307     -27.291  49.887  58.145  1.00 20.58           C  
ANISOU 2238  CG  TYR A 307     2347   3064   2407    240    181    249       C  
ATOM   2239  CD1 TYR A 307     -27.696  51.180  58.473  1.00 21.79           C  
ANISOU 2239  CD1 TYR A 307     2495   3232   2549    244    170    234       C  
ATOM   2240  CD2 TYR A 307     -28.265  48.893  58.057  1.00 20.60           C  
ANISOU 2240  CD2 TYR A 307     2349   3056   2419    232    195    267       C  
ATOM   2241  CE1 TYR A 307     -29.043  51.464  58.734  1.00 24.08           C  
ANISOU 2241  CE1 TYR A 307     2781   3530   2836    243    172    238       C  
ATOM   2242  CE2 TYR A 307     -29.612  49.161  58.336  1.00 21.27           C  
ANISOU 2242  CE2 TYR A 307     2428   3150   2503    228    197    269       C  
ATOM   2243  CZ  TYR A 307     -29.989  50.454  58.654  1.00 22.23           C  
ANISOU 2243  CZ  TYR A 307     2545   3289   2612    235    185    255       C  
ATOM   2244  OH  TYR A 307     -31.318  50.728  58.914  1.00 27.14           O  
ANISOU 2244  OH  TYR A 307     3158   3921   3230    233    187    256       O  
ATOM   2245  N   ASN A 308     -25.524  48.885  61.390  1.00 20.34           N  
ANISOU 2245  N   ASN A 308     2303   3091   2331    306    192    279       N  
ATOM   2246  CA  ASN A 308     -26.142  48.083  62.442  1.00 22.08           C  
ANISOU 2246  CA  ASN A 308     2523   3321   2542    323    207    305       C  
ATOM   2247  C   ASN A 308     -25.653  46.635  62.432  1.00 20.86           C  
ANISOU 2247  C   ASN A 308     2380   3152   2392    332    224    328       C  
ATOM   2248  O   ASN A 308     -26.461  45.704  62.435  1.00 20.32           O  
ANISOU 2248  O   ASN A 308     2320   3066   2333    326    244    349       O  
ATOM   2249  CB  ASN A 308     -27.672  48.131  62.315  1.00 22.40           C  
ANISOU 2249  CB  ASN A 308     2563   3352   2592    307    214    312       C  
ATOM   2250  CG  ASN A 308     -28.265  49.493  62.676  1.00 29.88           C  
ANISOU 2250  CG  ASN A 308     3502   4320   3531    307    200    294       C  
ATOM   2251  OD1 ASN A 308     -27.594  50.378  63.219  1.00 35.07           O  
ANISOU 2251  OD1 ASN A 308     4152   4999   4172    320    188    279       O  
ATOM   2252  ND2 ASN A 308     -29.547  49.662  62.365  1.00 32.18           N  
ANISOU 2252  ND2 ASN A 308     3791   4605   3830    292    203    295       N  
ATOM   2253  N   GLY A 309     -24.338  46.451  62.348  1.00 18.86           N  
ANISOU 2253  N   GLY A 309     2128   2906   2132    346    219    323       N  
ATOM   2254  CA  GLY A 309     -23.744  45.115  62.427  1.00 17.89           C  
ANISOU 2254  CA  GLY A 309     2016   2771   2008    362    235    345       C  
ATOM   2255  C   GLY A 309     -23.591  44.385  61.094  1.00 18.60           C  
ANISOU 2255  C   GLY A 309     2119   2825   2123    338    241    346       C  
ATOM   2256  O   GLY A 309     -23.090  43.263  61.066  1.00 16.08           O  
ANISOU 2256  O   GLY A 309     1813   2493   1804    351    256    364       O  
ATOM   2257  N   LYS A 310     -24.032  45.014  60.006  1.00 15.57           N  
ANISOU 2257  N   LYS A 310     1734   2424   1757    307    231    327       N  
ATOM   2258  CA  LYS A 310     -23.988  44.426  58.663  1.00 17.40           C  
ANISOU 2258  CA  LYS A 310     1975   2622   2012    283    235    325       C  
ATOM   2259  C   LYS A 310     -23.055  45.280  57.818  1.00 15.93           C  
ANISOU 2259  C   LYS A 310     1785   2438   1829    274    215    298       C  
ATOM   2260  O   LYS A 310     -23.122  46.506  57.883  1.00 15.19           O  
ANISOU 2260  O   LYS A 310     1683   2360   1730    270    200    278       O  
ATOM   2261  CB  LYS A 310     -25.388  44.443  58.023  1.00 17.71           C  
ANISOU 2261  CB  LYS A 310     2016   2643   2070    255    241    324       C  
ATOM   2262  CG  LYS A 310     -26.465  43.741  58.856  1.00 19.23           C  
ANISOU 2262  CG  LYS A 310     2210   2835   2261    259    262    346       C  
ATOM   2263  CD  LYS A 310     -26.119  42.265  58.928  1.00 28.27           C  
ANISOU 2263  CD  LYS A 310     3371   3958   3411    266    286    370       C  
ATOM   2264  CE  LYS A 310     -27.110  41.466  59.761  1.00 37.09           C  
ANISOU 2264  CE  LYS A 310     4494   5071   4527    269    313    393       C  
ATOM   2265  NZ  LYS A 310     -26.541  40.096  59.909  1.00 43.01           N  
ANISOU 2265  NZ  LYS A 310     5264   5799   5278    283    338    417       N  
ATOM   2266  N   ARG A 311     -22.207  44.631  57.027  1.00 16.76           N  
ANISOU 2266  N   ARG A 311     1897   2525   1942    271    217    298       N  
ATOM   2267  CA  ARG A 311     -21.176  45.332  56.258  1.00 16.42           C  
ANISOU 2267  CA  ARG A 311     1851   2484   1902    263    201    273       C  
ATOM   2268  C   ARG A 311     -20.660  44.468  55.107  1.00 15.68           C  
ANISOU 2268  C   ARG A 311     1768   2362   1825    251    206    275       C  
ATOM   2269  O   ARG A 311     -20.561  43.251  55.217  1.00 15.93           O  
ANISOU 2269  O   ARG A 311     1810   2382   1859    260    222    296       O  
ATOM   2270  CB  ARG A 311     -19.994  45.696  57.169  1.00 16.96           C  
ANISOU 2270  CB  ARG A 311     1908   2586   1947    289    193    264       C  
ATOM   2271  CG  ARG A 311     -19.016  46.699  56.555  1.00 17.90           C  
ANISOU 2271  CG  ARG A 311     2020   2713   2065    279    177    233       C  
ATOM   2272  CD  ARG A 311     -17.815  46.918  57.488  1.00 16.37           C  
ANISOU 2272  CD  ARG A 311     1813   2558   1849    305    171    222       C  
ATOM   2273  NE  ARG A 311     -16.976  45.720  57.545  1.00 15.61           N  
ANISOU 2273  NE  ARG A 311     1720   2463   1747    325    178    237       N  
ATOM   2274  CZ  ARG A 311     -15.763  45.691  58.092  1.00 20.17           C  
ANISOU 2274  CZ  ARG A 311     2286   3073   2305    349    173    226       C  
ATOM   2275  NH1 ARG A 311     -15.245  46.786  58.642  1.00 16.07           N  
ANISOU 2275  NH1 ARG A 311     1747   2587   1770    352    160    198       N  
ATOM   2276  NH2 ARG A 311     -15.052  44.574  58.077  1.00 17.19           N  
ANISOU 2276  NH2 ARG A 311     1913   2695   1921    371    180    241       N  
ATOM   2277  N   VAL A 312     -20.325  45.117  53.998  1.00 16.81           N  
ANISOU 2277  N   VAL A 312     1911   2494   1978    231    195    254       N  
ATOM   2278  CA  VAL A 312     -19.627  44.463  52.899  1.00 16.52           C  
ANISOU 2278  CA  VAL A 312     1884   2436   1956    221    197    251       C  
ATOM   2279  C   VAL A 312     -18.312  43.887  53.440  1.00 16.60           C  
ANISOU 2279  C   VAL A 312     1892   2461   1952    247    198    256       C  
ATOM   2280  O   VAL A 312     -17.738  44.425  54.386  1.00 13.63           O  
ANISOU 2280  O   VAL A 312     1504   2117   1556    266    191    249       O  
ATOM   2281  CB  VAL A 312     -19.334  45.468  51.756  1.00 17.04           C  
ANISOU 2281  CB  VAL A 312     1949   2493   2030    200    183    225       C  
ATOM   2282  CG1 VAL A 312     -18.278  46.506  52.177  1.00 15.52           C  
ANISOU 2282  CG1 VAL A 312     1747   2326   1823    208    172    203       C  
ATOM   2283  CG2 VAL A 312     -18.895  44.740  50.471  1.00 14.76           C  
ANISOU 2283  CG2 VAL A 312     1671   2177   1759    186    186    224       C  
ATOM   2284  N   ALA A 313     -17.848  42.781  52.866  1.00 15.76           N  
ANISOU 2284  N   ALA A 313     1796   2335   1854    248    208    267       N  
ATOM   2285  CA  ALA A 313     -16.522  42.273  53.229  1.00 17.21           C  
ANISOU 2285  CA  ALA A 313     1978   2536   2024    274    208    269       C  
ATOM   2286  C   ALA A 313     -15.460  43.299  52.871  1.00 16.80           C  
ANISOU 2286  C   ALA A 313     1913   2503   1965    269    190    238       C  
ATOM   2287  O   ALA A 313     -15.588  43.995  51.854  1.00 16.65           O  
ANISOU 2287  O   ALA A 313     1895   2468   1961    242    183    220       O  
ATOM   2288  CB  ALA A 313     -16.217  40.945  52.539  1.00 16.72           C  
ANISOU 2288  CB  ALA A 313     1932   2446   1973    275    221    285       C  
ATOM   2289  N   TYR A 314     -14.434  43.374  53.716  1.00 16.17           N  
ANISOU 2289  N   TYR A 314     1821   2458   1864    296    185    232       N  
ATOM   2290  CA  TYR A 314     -13.255  44.211  53.503  1.00 16.86           C  
ANISOU 2290  CA  TYR A 314     1894   2569   1943    293    172    201       C  
ATOM   2291  C   TYR A 314     -12.000  43.349  53.518  1.00 16.94           C  
ANISOU 2291  C   TYR A 314     1901   2593   1942    318    173    203       C  
ATOM   2292  O   TYR A 314     -11.896  42.402  54.299  1.00 19.01           O  
ANISOU 2292  O   TYR A 314     2167   2866   2190    350    182    226       O  
ATOM   2293  CB  TYR A 314     -13.126  45.264  54.610  1.00 14.58           C  
ANISOU 2293  CB  TYR A 314     1586   2319   1634    304    163    183       C  
ATOM   2294  CG  TYR A 314     -13.750  46.603  54.290  1.00 15.91           C  
ANISOU 2294  CG  TYR A 314     1752   2480   1811    275    156    163       C  
ATOM   2295  CD1 TYR A 314     -15.094  46.862  54.575  1.00 14.30           C  
ANISOU 2295  CD1 TYR A 314     1555   2264   1613    268    159    176       C  
ATOM   2296  CD2 TYR A 314     -12.986  47.622  53.744  1.00 13.24           C  
ANISOU 2296  CD2 TYR A 314     1406   2148   1476    257    148    129       C  
ATOM   2297  CE1 TYR A 314     -15.665  48.107  54.301  1.00 14.33           C  
ANISOU 2297  CE1 TYR A 314     1558   2262   1622    247    154    158       C  
ATOM   2298  CE2 TYR A 314     -13.550  48.860  53.452  1.00 14.98           C  
ANISOU 2298  CE2 TYR A 314     1629   2358   1703    233    145    111       C  
ATOM   2299  CZ  TYR A 314     -14.885  49.090  53.734  1.00 16.65           C  
ANISOU 2299  CZ  TYR A 314     1848   2558   1918    230    147    127       C  
ATOM   2300  OH  TYR A 314     -15.439  50.311  53.440  1.00 12.98           O  
ANISOU 2300  OH  TYR A 314     1388   2085   1459    210    145    110       O  
ATOM   2301  N   THR A 315     -11.037  43.655  52.656  1.00 17.94           N  
ANISOU 2301  N   THR A 315     2022   2720   2074    304    166    179       N  
ATOM   2302  CA  THR A 315      -9.724  43.014  52.777  1.00 17.87           C  
ANISOU 2302  CA  THR A 315     2005   2735   2050    330    165    175       C  
ATOM   2303  C   THR A 315      -9.010  43.565  54.015  1.00 18.43           C  
ANISOU 2303  C   THR A 315     2051   2859   2090    357    157    158       C  
ATOM   2304  O   THR A 315      -9.373  44.633  54.527  1.00 17.88           O  
ANISOU 2304  O   THR A 315     1971   2805   2017    346    150    141       O  
ATOM   2305  CB  THR A 315      -8.842  43.272  51.545  1.00 18.85           C  
ANISOU 2305  CB  THR A 315     2126   2847   2185    308    159    151       C  
ATOM   2306  OG1 THR A 315      -8.404  44.635  51.581  1.00 17.33           O  
ANISOU 2306  OG1 THR A 315     1916   2677   1989    289    149    115       O  
ATOM   2307  CG2 THR A 315      -9.608  42.995  50.239  1.00 13.82           C  
ANISOU 2307  CG2 THR A 315     1511   2160   1578    277    165    162       C  
ATOM   2308  N   PRO A 316      -7.999  42.834  54.518  1.00 18.28           N  
ANISOU 2308  N   PRO A 316     2024   2871   2049    393    157    161       N  
ATOM   2309  CA  PRO A 316      -7.190  43.388  55.603  1.00 17.93           C  
ANISOU 2309  CA  PRO A 316     1951   2884   1974    419    147    138       C  
ATOM   2310  C   PRO A 316      -6.575  44.735  55.255  1.00 18.58           C  
ANISOU 2310  C   PRO A 316     2013   2986   2061    388    136     92       C  
ATOM   2311  O   PRO A 316      -6.423  45.585  56.135  1.00 16.93           O  
ANISOU 2311  O   PRO A 316     1782   2814   1834    393    129     69       O  
ATOM   2312  CB  PRO A 316      -6.120  42.314  55.818  1.00 17.54           C  
ANISOU 2312  CB  PRO A 316     1899   2861   1905    460    149    146       C  
ATOM   2313  CG  PRO A 316      -6.893  41.048  55.551  1.00 18.98           C  
ANISOU 2313  CG  PRO A 316     2113   2997   2098    470    166    191       C  
ATOM   2314  CD  PRO A 316      -7.710  41.402  54.315  1.00 17.26           C  
ANISOU 2314  CD  PRO A 316     1911   2727   1917    419    168    189       C  
ATOM   2315  N   GLY A 317      -6.298  44.945  53.970  1.00 18.47           N  
ANISOU 2315  N   GLY A 317     2005   2942   2068    355    136     78       N  
ATOM   2316  CA  GLY A 317      -5.671  46.177  53.505  1.00 18.58           C  
ANISOU 2316  CA  GLY A 317     2003   2967   2088    324    129     35       C  
ATOM   2317  C   GLY A 317      -6.638  47.342  53.389  1.00 20.06           C  
ANISOU 2317  C   GLY A 317     2198   3133   2291    291    130     26       C  
ATOM   2318  O   GLY A 317      -6.221  48.453  53.082  1.00 19.53           O  
ANISOU 2318  O   GLY A 317     2121   3071   2227    264    128     -9       O  
ATOM   2319  N   GLY A 318      -7.925  47.103  53.625  1.00 17.98           N  
ANISOU 2319  N   GLY A 318     1952   2844   2035    293    134     56       N  
ATOM   2320  CA  GLY A 318      -8.910  48.180  53.613  1.00 17.85           C  
ANISOU 2320  CA  GLY A 318     1942   2810   2029    267    135     50       C  
ATOM   2321  C   GLY A 318      -9.677  48.397  52.318  1.00 17.35           C  
ANISOU 2321  C   GLY A 318     1903   2696   1994    235    139     57       C  
ATOM   2322  O   GLY A 318     -10.333  49.428  52.150  1.00 16.51           O  
ANISOU 2322  O   GLY A 318     1802   2575   1895    213    140     46       O  
ATOM   2323  N   LEU A 319      -9.650  47.414  51.423  1.00 16.05           N  
ANISOU 2323  N   LEU A 319     1751   2503   1842    233    143     75       N  
ATOM   2324  CA  LEU A 319     -10.483  47.479  50.220  1.00 16.05           C  
ANISOU 2324  CA  LEU A 319     1773   2458   1867    206    147     84       C  
ATOM   2325  C   LEU A 319     -11.856  46.834  50.442  1.00 16.77           C  
ANISOU 2325  C   LEU A 319     1878   2528   1964    212    152    117       C  
ATOM   2326  O   LEU A 319     -11.928  45.670  50.843  1.00 17.08           O  
ANISOU 2326  O   LEU A 319     1921   2568   2000    234    157    142       O  
ATOM   2327  CB  LEU A 319      -9.795  46.744  49.069  1.00 13.84           C  
ANISOU 2327  CB  LEU A 319     1500   2157   1598    199    149     85       C  
ATOM   2328  CG  LEU A 319     -10.622  46.600  47.787  1.00 15.66           C  
ANISOU 2328  CG  LEU A 319     1753   2343   1853    176    153     96       C  
ATOM   2329  CD1 LEU A 319     -10.844  47.950  47.092  1.00 15.39           C  
ANISOU 2329  CD1 LEU A 319     1724   2295   1827    148    152     73       C  
ATOM   2330  CD2 LEU A 319      -9.944  45.640  46.835  1.00 17.00           C  
ANISOU 2330  CD2 LEU A 319     1929   2497   2033    175    155    101       C  
ATOM   2331  N   ALA A 320     -12.937  47.553  50.144  1.00 16.10           N  
ANISOU 2331  N   ALA A 320     1802   2424   1890    194    152    118       N  
ATOM   2332  CA  ALA A 320     -14.264  46.930  50.163  1.00 15.50           C  
ANISOU 2332  CA  ALA A 320     1737   2327   1822    194    157    145       C  
ATOM   2333  C   ALA A 320     -14.316  45.883  49.056  1.00 16.53           C  
ANISOU 2333  C   ALA A 320     1881   2426   1971    186    163    159       C  
ATOM   2334  O   ALA A 320     -14.105  46.211  47.884  1.00 15.50           O  
ANISOU 2334  O   ALA A 320     1758   2276   1853    166    161    146       O  
ATOM   2335  CB  ALA A 320     -15.380  47.961  50.011  1.00 14.33           C  
ANISOU 2335  CB  ALA A 320     1595   2168   1680    178    155    140       C  
ATOM   2336  N   HIS A 321     -14.550  44.627  49.431  1.00 15.75           N  
ANISOU 2336  N   HIS A 321     1788   2323   1872    202    172    184       N  
ATOM   2337  CA  HIS A 321     -14.382  43.507  48.506  1.00 16.97           C  
ANISOU 2337  CA  HIS A 321     1955   2451   2042    197    179    196       C  
ATOM   2338  C   HIS A 321     -15.703  42.746  48.329  1.00 17.53           C  
ANISOU 2338  C   HIS A 321     2036   2495   2126    188    190    218       C  
ATOM   2339  O   HIS A 321     -15.999  41.811  49.086  1.00 18.68           O  
ANISOU 2339  O   HIS A 321     2187   2642   2268    205    202    240       O  
ATOM   2340  CB  HIS A 321     -13.262  42.596  49.024  1.00 16.96           C  
ANISOU 2340  CB  HIS A 321     1950   2465   2027    224    183    204       C  
ATOM   2341  CG  HIS A 321     -12.637  41.738  47.971  1.00 20.24           C  
ANISOU 2341  CG  HIS A 321     2376   2859   2455    219    187    207       C  
ATOM   2342  ND1 HIS A 321     -13.256  40.620  47.462  1.00 18.37           N  
ANISOU 2342  ND1 HIS A 321     2155   2590   2233    214    200    227       N  
ATOM   2343  CD2 HIS A 321     -11.439  41.819  47.344  1.00 15.64           C  
ANISOU 2343  CD2 HIS A 321     1788   2281   1871    218    181    189       C  
ATOM   2344  CE1 HIS A 321     -12.478  40.057  46.556  1.00 17.50           C  
ANISOU 2344  CE1 HIS A 321     2051   2467   2131    211    201    223       C  
ATOM   2345  NE2 HIS A 321     -11.374  40.774  46.455  1.00 18.84           N  
ANISOU 2345  NE2 HIS A 321     2208   2658   2290    214    189    201       N  
ATOM   2346  N   LEU A 322     -16.497  43.141  47.333  1.00 15.99           N  
ANISOU 2346  N   LEU A 322     1847   2280   1947    163    188    210       N  
ATOM   2347  CA  LEU A 322     -17.891  42.689  47.267  1.00 16.32           C  
ANISOU 2347  CA  LEU A 322     1894   2306   2000    153    196    224       C  
ATOM   2348  C   LEU A 322     -17.983  41.246  46.797  1.00 16.83           C  
ANISOU 2348  C   LEU A 322     1970   2346   2078    150    211    240       C  
ATOM   2349  O   LEU A 322     -18.812  40.487  47.282  1.00 16.38           O  
ANISOU 2349  O   LEU A 322     1917   2281   2024    151    226    257       O  
ATOM   2350  CB  LEU A 322     -18.732  43.573  46.344  1.00 14.93           C  
ANISOU 2350  CB  LEU A 322     1719   2120   1833    131    189    209       C  
ATOM   2351  CG  LEU A 322     -20.217  43.222  46.210  1.00 14.96           C  
ANISOU 2351  CG  LEU A 322     1723   2112   1846    119    196    217       C  
ATOM   2352  CD1 LEU A 322     -20.950  43.395  47.540  1.00 15.35           C  
ANISOU 2352  CD1 LEU A 322     1766   2181   1884    131    200    228       C  
ATOM   2353  CD2 LEU A 322     -20.880  44.069  45.109  1.00 12.26           C  
ANISOU 2353  CD2 LEU A 322     1382   1764   1511    102    187    200       C  
ATOM   2354  N   ASP A 323     -17.130  40.884  45.846  1.00 17.39           N  
ANISOU 2354  N   ASP A 323     2047   2403   2157    145    209    233       N  
ATOM   2355  CA  ASP A 323     -17.219  39.583  45.189  1.00 20.24           C  
ANISOU 2355  CA  ASP A 323     2420   2736   2532    139    223    244       C  
ATOM   2356  C   ASP A 323     -15.873  39.274  44.558  1.00 20.03           C  
ANISOU 2356  C   ASP A 323     2397   2706   2506    145    220    238       C  
ATOM   2357  O   ASP A 323     -15.018  40.153  44.398  1.00 20.16           O  
ANISOU 2357  O   ASP A 323     2406   2738   2514    147    206    221       O  
ATOM   2358  CB  ASP A 323     -18.303  39.614  44.104  1.00 20.85           C  
ANISOU 2358  CB  ASP A 323     2499   2793   2628    111    224    235       C  
ATOM   2359  CG  ASP A 323     -18.631  38.232  43.548  1.00 28.04           C  
ANISOU 2359  CG  ASP A 323     3421   3675   3555    101    242    246       C  
ATOM   2360  OD1 ASP A 323     -18.741  37.258  44.328  1.00 27.71           O  
ANISOU 2360  OD1 ASP A 323     3386   3627   3512    112    260    265       O  
ATOM   2361  OD2 ASP A 323     -18.777  38.121  42.308  1.00 30.81           O  
ANISOU 2361  OD2 ASP A 323     3775   4011   3921     82    239    233       O  
ATOM   2362  N   THR A 324     -15.695  38.008  44.201  1.00 19.81           N  
ANISOU 2362  N   THR A 324     2381   2656   2487    147    234    250       N  
ATOM   2363  CA  THR A 324     -14.527  37.568  43.455  1.00 20.73           C  
ANISOU 2363  CA  THR A 324     2503   2765   2606    151    232    245       C  
ATOM   2364  C   THR A 324     -14.248  38.386  42.192  1.00 19.68           C  
ANISOU 2364  C   THR A 324     2365   2627   2481    130    217    221       C  
ATOM   2365  O   THR A 324     -13.102  38.762  41.935  1.00 19.31           O  
ANISOU 2365  O   THR A 324     2315   2593   2428    136    208    209       O  
ATOM   2366  CB  THR A 324     -14.718  36.089  43.057  1.00 21.97           C  
ANISOU 2366  CB  THR A 324     2678   2892   2778    149    252    261       C  
ATOM   2367  OG1 THR A 324     -14.966  35.352  44.259  1.00 26.52           O  
ANISOU 2367  OG1 THR A 324     3261   3470   3344    171    270    285       O  
ATOM   2368  CG2 THR A 324     -13.471  35.549  42.368  1.00 22.54           C  
ANISOU 2368  CG2 THR A 324     2756   2958   2850    158    251    257       C  
ATOM   2369  N   TRP A 325     -15.288  38.647  41.406  1.00 18.70           N  
ANISOU 2369  N   TRP A 325     2243   2489   2372    106    215    214       N  
ATOM   2370  CA  TRP A 325     -15.131  39.334  40.119  1.00 19.94           C  
ANISOU 2370  CA  TRP A 325     2400   2639   2537     88    204    194       C  
ATOM   2371  C   TRP A 325     -15.044  40.843  40.309  1.00 16.95           C  
ANISOU 2371  C   TRP A 325     2012   2280   2146     87    190    178       C  
ATOM   2372  O   TRP A 325     -15.928  41.409  40.962  1.00 16.82           O  
ANISOU 2372  O   TRP A 325     1991   2273   2124     87    189    180       O  
ATOM   2373  CB  TRP A 325     -16.371  39.096  39.254  1.00 20.42           C  
ANISOU 2373  CB  TRP A 325     2464   2681   2613     67    207    190       C  
ATOM   2374  CG  TRP A 325     -16.486  37.714  38.724  1.00 26.37           C  
ANISOU 2374  CG  TRP A 325     3227   3410   3381     60    222    199       C  
ATOM   2375  CD1 TRP A 325     -17.326  36.725  39.160  1.00 30.57           C  
ANISOU 2375  CD1 TRP A 325     3763   3929   3921     57    239    212       C  
ATOM   2376  CD2 TRP A 325     -15.750  37.169  37.625  1.00 29.09           C  
ANISOU 2376  CD2 TRP A 325     3579   3738   3735     55    222    192       C  
ATOM   2377  NE1 TRP A 325     -17.136  35.588  38.408  1.00 31.11           N  
ANISOU 2377  NE1 TRP A 325     3842   3973   4004     49    251    214       N  
ATOM   2378  CE2 TRP A 325     -16.187  35.838  37.450  1.00 32.62           C  
ANISOU 2378  CE2 TRP A 325     4035   4162   4196     48    240    202       C  
ATOM   2379  CE3 TRP A 325     -14.761  37.676  36.774  1.00 29.37           C  
ANISOU 2379  CE3 TRP A 325     3615   3775   3769     54    210    178       C  
ATOM   2380  CZ2 TRP A 325     -15.660  35.004  36.459  1.00 35.19           C  
ANISOU 2380  CZ2 TRP A 325     4369   4466   4532     42    245    198       C  
ATOM   2381  CZ3 TRP A 325     -14.238  36.849  35.788  1.00 31.25           C  
ANISOU 2381  CZ3 TRP A 325     3860   3993   4017     49    214    175       C  
ATOM   2382  CH2 TRP A 325     -14.688  35.525  35.641  1.00 33.29           C  
ANISOU 2382  CH2 TRP A 325     4128   4230   4289     43    231    186       C  
ATOM   2383  N   GLY A 326     -14.054  41.487  39.694  1.00 15.67           N  
ANISOU 2383  N   GLY A 326     1849   2121   1981     84    182    162       N  
ATOM   2384  CA  GLY A 326     -13.994  42.958  39.658  1.00 14.63           C  
ANISOU 2384  CA  GLY A 326     1715   2002   1842     79    173    144       C  
ATOM   2385  C   GLY A 326     -14.287  43.653  40.983  1.00 14.38           C  
ANISOU 2385  C   GLY A 326     1674   1993   1796     90    171    146       C  
ATOM   2386  O   GLY A 326     -15.127  44.548  41.072  1.00 12.98           O  
ANISOU 2386  O   GLY A 326     1496   1818   1616     84    168    141       O  
ATOM   2387  N   PRO A 327     -13.589  43.246  42.053  1.00 15.09           N  
ANISOU 2387  N   PRO A 327     1756   2102   1875    108    173    153       N  
ATOM   2388  CA  PRO A 327     -13.773  43.974  43.308  1.00 14.08           C  
ANISOU 2388  CA  PRO A 327     1618   1999   1732    119    170    152       C  
ATOM   2389  C   PRO A 327     -13.402  45.455  43.220  1.00 13.70           C  
ANISOU 2389  C   PRO A 327     1565   1961   1676    110    163    128       C  
ATOM   2390  O   PRO A 327     -14.085  46.281  43.835  1.00 12.45           O  
ANISOU 2390  O   PRO A 327     1404   1813   1511    110    161    126       O  
ATOM   2391  CB  PRO A 327     -12.864  43.225  44.291  1.00 14.20           C  
ANISOU 2391  CB  PRO A 327     1626   2035   1735    143    173    161       C  
ATOM   2392  CG  PRO A 327     -11.815  42.606  43.428  1.00 14.23           C  
ANISOU 2392  CG  PRO A 327     1633   2029   1744    142    174    156       C  
ATOM   2393  CD  PRO A 327     -12.556  42.200  42.166  1.00 15.81           C  
ANISOU 2393  CD  PRO A 327     1846   2195   1963    122    177    160       C  
ATOM   2394  N   LEU A 328     -12.358  45.806  42.471  1.00 12.56           N  
ANISOU 2394  N   LEU A 328     1423   1816   1534    102    161    110       N  
ATOM   2395  CA  LEU A 328     -11.992  47.221  42.354  1.00 12.85           C  
ANISOU 2395  CA  LEU A 328     1457   1858   1564     91    159     86       C  
ATOM   2396  C   LEU A 328     -13.095  48.010  41.660  1.00 13.04           C  
ANISOU 2396  C   LEU A 328     1495   1862   1595     77    160     84       C  
ATOM   2397  O   LEU A 328     -13.400  49.132  42.062  1.00 11.82           O  
ANISOU 2397  O   LEU A 328     1341   1714   1433     75    160     74       O  
ATOM   2398  CB  LEU A 328     -10.659  47.434  41.624  1.00 11.76           C  
ANISOU 2398  CB  LEU A 328     1319   1720   1429     82    160     65       C  
ATOM   2399  CG  LEU A 328      -9.451  46.964  42.430  1.00 12.32           C  
ANISOU 2399  CG  LEU A 328     1372   1820   1487     97    159     59       C  
ATOM   2400  CD1 LEU A 328      -8.181  46.981  41.590  1.00 11.44           C  
ANISOU 2400  CD1 LEU A 328     1258   1707   1378     88    161     40       C  
ATOM   2401  CD2 LEU A 328      -9.314  47.819  43.682  1.00 12.51           C  
ANISOU 2401  CD2 LEU A 328     1382   1875   1495    104    157     46       C  
ATOM   2402  N   ARG A 329     -13.697  47.414  40.633  1.00 12.83           N  
ANISOU 2402  N   ARG A 329     1480   1813   1582     71    160     94       N  
ATOM   2403  CA  ARG A 329     -14.833  47.998  39.906  1.00 12.24           C  
ANISOU 2403  CA  ARG A 329     1416   1722   1511     63    160     94       C  
ATOM   2404  C   ARG A 329     -15.976  48.373  40.853  1.00 12.84           C  
ANISOU 2404  C   ARG A 329     1488   1810   1580     70    158    102       C  
ATOM   2405  O   ARG A 329     -16.478  49.501  40.850  1.00 11.80           O  
ANISOU 2405  O   ARG A 329     1362   1679   1441     69    158     94       O  
ATOM   2406  CB  ARG A 329     -15.292  47.017  38.808  1.00 10.23           C  
ANISOU 2406  CB  ARG A 329     1168   1447   1269     57    160    103       C  
ATOM   2407  CG  ARG A 329     -16.702  47.227  38.233  1.00 12.15           C  
ANISOU 2407  CG  ARG A 329     1417   1682   1515     54    159    107       C  
ATOM   2408  CD  ARG A 329     -17.764  46.318  38.875  1.00 11.13           C  
ANISOU 2408  CD  ARG A 329     1280   1559   1391     57    160    123       C  
ATOM   2409  NE  ARG A 329     -17.351  44.913  39.050  1.00  9.23           N  
ANISOU 2409  NE  ARG A 329     1034   1312   1158     58    165    136       N  
ATOM   2410  CZ  ARG A 329     -17.678  43.918  38.226  1.00 13.59           C  
ANISOU 2410  CZ  ARG A 329     1590   1849   1724     50    169    140       C  
ATOM   2411  NH1 ARG A 329     -18.341  44.163  37.097  1.00 12.68           N  
ANISOU 2411  NH1 ARG A 329     1479   1724   1613     41    165    131       N  
ATOM   2412  NH2 ARG A 329     -17.315  42.667  38.500  1.00 12.32           N  
ANISOU 2412  NH2 ARG A 329     1428   1681   1569     53    176    152       N  
ATOM   2413  N   TYR A 330     -16.358  47.441  41.720  1.00 12.64           N  
ANISOU 2413  N   TYR A 330     1453   1794   1554     80    159    119       N  
ATOM   2414  CA  TYR A 330     -17.473  47.711  42.607  1.00 13.35           C  
ANISOU 2414  CA  TYR A 330     1538   1896   1637     86    158    128       C  
ATOM   2415  C   TYR A 330     -17.139  48.807  43.618  1.00 12.84           C  
ANISOU 2415  C   TYR A 330     1467   1851   1557     93    156    118       C  
ATOM   2416  O   TYR A 330     -17.960  49.679  43.866  1.00 12.42           O  
ANISOU 2416  O   TYR A 330     1417   1802   1499     94    155    115       O  
ATOM   2417  CB  TYR A 330     -17.882  46.447  43.356  1.00 12.77           C  
ANISOU 2417  CB  TYR A 330     1457   1827   1567     95    163    149       C  
ATOM   2418  CG  TYR A 330     -18.529  45.372  42.523  1.00 13.12           C  
ANISOU 2418  CG  TYR A 330     1506   1851   1625     86    168    159       C  
ATOM   2419  CD1 TYR A 330     -19.650  45.632  41.736  1.00 11.60           C  
ANISOU 2419  CD1 TYR A 330     1317   1651   1439     75    166    155       C  
ATOM   2420  CD2 TYR A 330     -18.035  44.074  42.565  1.00 10.50           C  
ANISOU 2420  CD2 TYR A 330     1175   1512   1301     89    176    171       C  
ATOM   2421  CE1 TYR A 330     -20.262  44.612  40.993  1.00 14.02           C  
ANISOU 2421  CE1 TYR A 330     1624   1941   1759     65    171    160       C  
ATOM   2422  CE2 TYR A 330     -18.658  43.043  41.866  1.00 13.01           C  
ANISOU 2422  CE2 TYR A 330     1497   1810   1633     78    183    178       C  
ATOM   2423  CZ  TYR A 330     -19.758  43.320  41.071  1.00 14.56           C  
ANISOU 2423  CZ  TYR A 330     1695   2000   1837     65    180    171       C  
ATOM   2424  OH  TYR A 330     -20.331  42.281  40.373  1.00  9.80           O  
ANISOU 2424  OH  TYR A 330     1093   1381   1249     53    188    174       O  
ATOM   2425  N   ALA A 331     -15.940  48.761  44.190  1.00 13.67           N  
ANISOU 2425  N   ALA A 331     1564   1970   1656     99    157    111       N  
ATOM   2426  CA  ALA A 331     -15.594  49.674  45.275  1.00 12.40           C  
ANISOU 2426  CA  ALA A 331     1395   1834   1481    106    155     99       C  
ATOM   2427  C   ALA A 331     -15.394  51.084  44.726  1.00 13.85           C  
ANISOU 2427  C   ALA A 331     1588   2010   1663     93    157     76       C  
ATOM   2428  O   ALA A 331     -15.791  52.062  45.365  1.00 12.65           O  
ANISOU 2428  O   ALA A 331     1436   1867   1502     95    157     68       O  
ATOM   2429  CB  ALA A 331     -14.348  49.200  45.997  1.00 12.40           C  
ANISOU 2429  CB  ALA A 331     1381   1856   1472    117    155     94       C  
ATOM   2430  N   THR A 332     -14.768  51.195  43.556  1.00 11.92           N  
ANISOU 2430  N   THR A 332     1354   1746   1427     80    160     65       N  
ATOM   2431  CA  THR A 332     -14.589  52.518  42.942  1.00 13.41           C  
ANISOU 2431  CA  THR A 332     1556   1922   1614     68    166     44       C  
ATOM   2432  C   THR A 332     -15.910  53.130  42.432  1.00 13.66           C  
ANISOU 2432  C   THR A 332     1604   1938   1646     69    167     51       C  
ATOM   2433  O   THR A 332     -16.082  54.353  42.480  1.00 15.34           O  
ANISOU 2433  O   THR A 332     1828   2146   1851     66    172     38       O  
ATOM   2434  CB  THR A 332     -13.555  52.502  41.790  1.00 11.82           C  
ANISOU 2434  CB  THR A 332     1364   1705   1421     54    171     31       C  
ATOM   2435  OG1 THR A 332     -13.997  51.598  40.766  1.00 11.28           O  
ANISOU 2435  OG1 THR A 332     1302   1618   1363     54    168     46       O  
ATOM   2436  CG2 THR A 332     -12.161  52.088  42.278  1.00 10.90           C  
ANISOU 2436  CG2 THR A 332     1230   1609   1302     54    171     19       C  
ATOM   2437  N   THR A 333     -16.843  52.313  41.942  1.00 12.00           N  
ANISOU 2437  N   THR A 333     1396   1720   1443     72    162     69       N  
ATOM   2438  CA  THR A 333     -18.183  52.813  41.623  1.00 12.26           C  
ANISOU 2438  CA  THR A 333     1439   1746   1473     77    161     75       C  
ATOM   2439  C   THR A 333     -18.885  53.326  42.884  1.00 12.88           C  
ANISOU 2439  C   THR A 333     1509   1844   1540     88    159     78       C  
ATOM   2440  O   THR A 333     -19.482  54.406  42.890  1.00 10.00           O  
ANISOU 2440  O   THR A 333     1155   1476   1166     92    161     72       O  
ATOM   2441  CB  THR A 333     -19.056  51.718  40.956  1.00 10.25           C  
ANISOU 2441  CB  THR A 333     1181   1485   1227     78    156     91       C  
ATOM   2442  OG1 THR A 333     -18.382  51.224  39.788  1.00 12.79           O  
ANISOU 2442  OG1 THR A 333     1510   1789   1559     69    158     87       O  
ATOM   2443  CG2 THR A 333     -20.402  52.299  40.544  1.00 10.74           C  
ANISOU 2443  CG2 THR A 333     1251   1544   1283     84    154     92       C  
ATOM   2444  N   GLU A 334     -18.828  52.548  43.962  1.00 12.31           N  
ANISOU 2444  N   GLU A 334     1419   1790   1466     94    156     89       N  
ATOM   2445  CA  GLU A 334     -19.403  53.041  45.223  1.00 12.48           C  
ANISOU 2445  CA  GLU A 334     1433   1831   1476    104    154     91       C  
ATOM   2446  C   GLU A 334     -18.747  54.320  45.733  1.00 13.16           C  
ANISOU 2446  C   GLU A 334     1522   1925   1552    103    158     71       C  
ATOM   2447  O   GLU A 334     -19.422  55.172  46.311  1.00 12.99           O  
ANISOU 2447  O   GLU A 334     1503   1910   1521    109    159     68       O  
ATOM   2448  CB  GLU A 334     -19.356  51.966  46.303  1.00 12.66           C  
ANISOU 2448  CB  GLU A 334     1438   1873   1497    114    152    107       C  
ATOM   2449  CG  GLU A 334     -20.334  50.848  46.003  1.00 14.52           C  
ANISOU 2449  CG  GLU A 334     1672   2102   1743    114    152    127       C  
ATOM   2450  CD  GLU A 334     -21.780  51.292  46.070  1.00 19.19           C  
ANISOU 2450  CD  GLU A 334     2264   2696   2330    117    150    131       C  
ATOM   2451  OE1 GLU A 334     -22.157  52.118  46.941  1.00 20.21           O  
ANISOU 2451  OE1 GLU A 334     2390   2840   2447    126    149    128       O  
ATOM   2452  OE2 GLU A 334     -22.548  50.791  45.230  1.00 17.79           O  
ANISOU 2452  OE2 GLU A 334     2089   2508   2161    112    150    137       O  
ATOM   2453  N   ALA A 335     -17.452  54.478  45.476  1.00 13.43           N  
ANISOU 2453  N   ALA A 335     1557   1957   1589     93    162     55       N  
ATOM   2454  CA  ALA A 335     -16.755  55.709  45.852  1.00 13.87           C  
ANISOU 2454  CA  ALA A 335     1616   2017   1636     87    169     30       C  
ATOM   2455  C   ALA A 335     -17.384  56.906  45.148  1.00 13.72           C  
ANISOU 2455  C   ALA A 335     1621   1975   1614     83    177     22       C  
ATOM   2456  O   ALA A 335     -17.638  57.945  45.762  1.00 13.72           O  
ANISOU 2456  O   ALA A 335     1626   1980   1606     86    182     12       O  
ATOM   2457  CB  ALA A 335     -15.277  55.608  45.512  1.00 11.57           C  
ANISOU 2457  CB  ALA A 335     1320   1726   1349     75    174     12       C  
ATOM   2458  N   PHE A 336     -17.671  56.745  43.859  1.00 13.70           N  
ANISOU 2458  N   PHE A 336     1635   1949   1620     80    179     28       N  
ATOM   2459  CA  PHE A 336     -18.334  57.809  43.105  1.00 14.85           C  
ANISOU 2459  CA  PHE A 336     1805   2074   1761     82    187     25       C  
ATOM   2460  C   PHE A 336     -19.711  58.128  43.694  1.00 13.66           C  
ANISOU 2460  C   PHE A 336     1655   1934   1600     98    182     36       C  
ATOM   2461  O   PHE A 336     -20.046  59.298  43.915  1.00 15.41           O  
ANISOU 2461  O   PHE A 336     1891   2151   1812    103    190     27       O  
ATOM   2462  CB  PHE A 336     -18.471  57.428  41.624  1.00 12.37           C  
ANISOU 2462  CB  PHE A 336     1506   1738   1455     80    188     31       C  
ATOM   2463  CG  PHE A 336     -19.193  58.463  40.801  1.00 15.96           C  
ANISOU 2463  CG  PHE A 336     1988   2173   1901     88    196     29       C  
ATOM   2464  CD1 PHE A 336     -18.701  59.763  40.701  1.00 14.29           C  
ANISOU 2464  CD1 PHE A 336     1800   1946   1684     83    213     12       C  
ATOM   2465  CD2 PHE A 336     -20.351  58.140  40.106  1.00 16.38           C  
ANISOU 2465  CD2 PHE A 336     2046   2224   1952    102    189     43       C  
ATOM   2466  CE1 PHE A 336     -19.356  60.724  39.936  1.00 16.43           C  
ANISOU 2466  CE1 PHE A 336     2100   2196   1945     95    224     12       C  
ATOM   2467  CE2 PHE A 336     -21.020  59.101  39.335  1.00 17.53           C  
ANISOU 2467  CE2 PHE A 336     2218   2355   2087    115    197     42       C  
ATOM   2468  CZ  PHE A 336     -20.523  60.396  39.254  1.00 13.99           C  
ANISOU 2468  CZ  PHE A 336     1795   1889   1631    113    214     28       C  
ATOM   2469  N   LEU A 337     -20.529  57.106  43.928  1.00 13.94           N  
ANISOU 2469  N   LEU A 337     1675   1982   1639    106    170     55       N  
ATOM   2470  CA  LEU A 337     -21.824  57.356  44.566  1.00 15.25           C  
ANISOU 2470  CA  LEU A 337     1836   2161   1795    121    165     65       C  
ATOM   2471  C   LEU A 337     -21.711  58.074  45.923  1.00 17.42           C  
ANISOU 2471  C   LEU A 337     2105   2454   2059    125    167     57       C  
ATOM   2472  O   LEU A 337     -22.542  58.942  46.257  1.00 16.56           O  
ANISOU 2472  O   LEU A 337     2004   2348   1939    136    169     56       O  
ATOM   2473  CB  LEU A 337     -22.631  56.064  44.738  1.00 14.97           C  
ANISOU 2473  CB  LEU A 337     1783   2139   1766    125    156     84       C  
ATOM   2474  CG  LEU A 337     -23.566  55.624  43.604  1.00 17.20           C  
ANISOU 2474  CG  LEU A 337     2070   2413   2052    128    152     92       C  
ATOM   2475  CD1 LEU A 337     -22.801  55.292  42.314  1.00 11.98           C  
ANISOU 2475  CD1 LEU A 337     1419   1730   1400    117    155     87       C  
ATOM   2476  CD2 LEU A 337     -24.424  54.426  44.023  1.00 10.46           C  
ANISOU 2476  CD2 LEU A 337     1196   1575   1204    129    146    108       C  
ATOM   2477  N   ALA A 338     -20.732  57.653  46.724  1.00 16.32           N  
ANISOU 2477  N   ALA A 338     1949   2329   1922    119    166     52       N  
ATOM   2478  CA  ALA A 338     -20.529  58.235  48.054  1.00 17.54           C  
ANISOU 2478  CA  ALA A 338     2094   2505   2066    124    167     43       C  
ATOM   2479  C   ALA A 338     -20.138  59.708  47.919  1.00 17.41           C  
ANISOU 2479  C   ALA A 338     2096   2475   2043    117    180     19       C  
ATOM   2480  O   ALA A 338     -20.641  60.546  48.671  1.00 19.18           O  
ANISOU 2480  O   ALA A 338     2322   2707   2256    125    182     14       O  
ATOM   2481  CB  ALA A 338     -19.458  57.464  48.829  1.00 13.82           C  
ANISOU 2481  CB  ALA A 338     1600   2054   1596    121    164     40       C  
ATOM   2482  N   PHE A 339     -19.259  60.016  46.965  1.00 17.24           N  
ANISOU 2482  N   PHE A 339     2089   2432   2029    103    190      5       N  
ATOM   2483  CA  PHE A 339     -18.899  61.401  46.673  1.00 18.36           C  
ANISOU 2483  CA  PHE A 339     2253   2554   2165     95    207    -16       C  
ATOM   2484  C   PHE A 339     -20.126  62.236  46.311  1.00 18.04           C  
ANISOU 2484  C   PHE A 339     2237   2499   2116    109    211     -8       C  
ATOM   2485  O   PHE A 339     -20.284  63.361  46.792  1.00 19.50           O  
ANISOU 2485  O   PHE A 339     2435   2680   2291    112    222    -21       O  
ATOM   2486  CB  PHE A 339     -17.913  61.487  45.508  1.00 17.09           C  
ANISOU 2486  CB  PHE A 339     2109   2370   2015     78    218    -28       C  
ATOM   2487  CG  PHE A 339     -16.477  61.251  45.878  1.00 20.50           C  
ANISOU 2487  CG  PHE A 339     2522   2814   2452     60    221    -49       C  
ATOM   2488  CD1 PHE A 339     -15.885  61.876  46.979  1.00 19.98           C  
ANISOU 2488  CD1 PHE A 339     2444   2768   2379     54    226    -72       C  
ATOM   2489  CD2 PHE A 339     -15.683  60.459  45.057  1.00 16.74           C  
ANISOU 2489  CD2 PHE A 339     2042   2331   1986     50    219    -48       C  
ATOM   2490  CE1 PHE A 339     -14.533  61.667  47.278  1.00 22.02           C  
ANISOU 2490  CE1 PHE A 339     2683   3042   2639     39    229    -95       C  
ATOM   2491  CE2 PHE A 339     -14.326  60.245  45.343  1.00 16.97           C  
ANISOU 2491  CE2 PHE A 339     2054   2375   2019     36    222    -69       C  
ATOM   2492  CZ  PHE A 339     -13.751  60.859  46.451  1.00 19.99           C  
ANISOU 2492  CZ  PHE A 339     2422   2780   2393     30    227    -93       C  
ATOM   2493  N   VAL A 340     -20.978  61.698  45.442  1.00 17.97           N  
ANISOU 2493  N   VAL A 340     2235   2482   2110    120    204     10       N  
ATOM   2494  CA  VAL A 340     -22.148  62.416  44.943  1.00 17.73           C  
ANISOU 2494  CA  VAL A 340     2226   2440   2069    138    207     18       C  
ATOM   2495  C   VAL A 340     -23.120  62.659  46.093  1.00 18.39           C  
ANISOU 2495  C   VAL A 340     2298   2546   2140    153    200     24       C  
ATOM   2496  O   VAL A 340     -23.646  63.765  46.249  1.00 19.21           O  
ANISOU 2496  O   VAL A 340     2421   2644   2232    165    209     19       O  
ATOM   2497  CB  VAL A 340     -22.834  61.687  43.756  1.00 17.53           C  
ANISOU 2497  CB  VAL A 340     2204   2408   2047    146    199     34       C  
ATOM   2498  CG1 VAL A 340     -24.167  62.342  43.403  1.00 18.63           C  
ANISOU 2498  CG1 VAL A 340     2360   2547   2172    170    199     42       C  
ATOM   2499  CG2 VAL A 340     -21.926  61.707  42.532  1.00 13.58           C  
ANISOU 2499  CG2 VAL A 340     1722   1881   1555    134    209     27       C  
ATOM   2500  N   TYR A 341     -23.349  61.631  46.901  1.00 17.52           N  
ANISOU 2500  N   TYR A 341     2158   2463   2034    154    186     36       N  
ATOM   2501  CA  TYR A 341     -24.282  61.775  48.009  1.00 18.72           C  
ANISOU 2501  CA  TYR A 341     2298   2638   2175    168    179     44       C  
ATOM   2502  C   TYR A 341     -23.730  62.770  49.041  1.00 19.13           C  
ANISOU 2502  C   TYR A 341     2353   2696   2220    165    188     25       C  
ATOM   2503  O   TYR A 341     -24.429  63.711  49.431  1.00 20.95           O  
ANISOU 2503  O   TYR A 341     2595   2928   2438    178    192     22       O  
ATOM   2504  CB  TYR A 341     -24.669  60.430  48.631  1.00 17.79           C  
ANISOU 2504  CB  TYR A 341     2151   2545   2064    170    165     61       C  
ATOM   2505  CG  TYR A 341     -25.782  60.601  49.646  1.00 18.31           C  
ANISOU 2505  CG  TYR A 341     2205   2633   2117    186    160     70       C  
ATOM   2506  CD1 TYR A 341     -27.071  60.950  49.241  1.00 15.21           C  
ANISOU 2506  CD1 TYR A 341     1821   2242   1716    201    157     77       C  
ATOM   2507  CD2 TYR A 341     -25.531  60.454  51.003  1.00 17.65           C  
ANISOU 2507  CD2 TYR A 341     2104   2573   2030    187    157     70       C  
ATOM   2508  CE1 TYR A 341     -28.096  61.153  50.168  1.00 17.06           C  
ANISOU 2508  CE1 TYR A 341     2044   2497   1938    215    153     84       C  
ATOM   2509  CE2 TYR A 341     -26.540  60.654  51.940  1.00 19.86           C  
ANISOU 2509  CE2 TYR A 341     2374   2873   2297    202    153     78       C  
ATOM   2510  CZ  TYR A 341     -27.810  61.002  51.522  1.00 20.26           C  
ANISOU 2510  CZ  TYR A 341     2433   2923   2341    215    151     84       C  
ATOM   2511  OH  TYR A 341     -28.791  61.185  52.471  1.00 21.89           O  
ANISOU 2511  OH  TYR A 341     2628   3152   2536    229    147     91       O  
ATOM   2512  N   ALA A 342     -22.472  62.597  49.430  1.00 19.41           N  
ANISOU 2512  N   ALA A 342     2377   2736   2262    149    191     11       N  
ATOM   2513  CA  ALA A 342     -21.812  63.487  50.386  1.00 22.00           C  
ANISOU 2513  CA  ALA A 342     2702   3072   2582    143    199    -11       C  
ATOM   2514  C   ALA A 342     -21.841  64.949  49.936  1.00 22.33           C  
ANISOU 2514  C   ALA A 342     2778   3088   2619    141    219    -28       C  
ATOM   2515  O   ALA A 342     -22.039  65.850  50.747  1.00 23.12           O  
ANISOU 2515  O   ALA A 342     2882   3193   2708    145    225    -41       O  
ATOM   2516  CB  ALA A 342     -20.369  63.030  50.638  1.00 22.58           C  
ANISOU 2516  CB  ALA A 342     2760   3156   2663    126    200    -27       C  
ATOM   2517  N   ASP A 343     -21.635  65.190  48.646  1.00 23.76           N  
ANISOU 2517  N   ASP A 343     2984   3238   2805    135    229    -30       N  
ATOM   2518  CA  ASP A 343     -21.689  66.542  48.097  1.00 25.27           C  
ANISOU 2518  CA  ASP A 343     3213   3398   2990    136    251    -43       C  
ATOM   2519  C   ASP A 343     -23.099  67.111  48.113  1.00 25.83           C  
ANISOU 2519  C   ASP A 343     3300   3467   3047    162    250    -29       C  
ATOM   2520  O   ASP A 343     -23.271  68.314  47.973  1.00 27.12           O  
ANISOU 2520  O   ASP A 343     3494   3609   3201    168    269    -39       O  
ATOM   2521  CB  ASP A 343     -21.217  66.586  46.643  1.00 24.51           C  
ANISOU 2521  CB  ASP A 343     3141   3270   2902    127    263    -44       C  
ATOM   2522  CG  ASP A 343     -19.712  66.515  46.504  1.00 25.93           C  
ANISOU 2522  CG  ASP A 343     3316   3443   3094     99    274    -67       C  
ATOM   2523  OD1 ASP A 343     -18.974  66.749  47.484  1.00 26.00           O  
ANISOU 2523  OD1 ASP A 343     3308   3468   3103     85    278    -88       O  
ATOM   2524  OD2 ASP A 343     -19.265  66.231  45.378  1.00 24.83           O  
ANISOU 2524  OD2 ASP A 343     3188   3283   2963     91    279    -65       O  
ATOM   2525  N   SER A 344     -24.114  66.265  48.229  1.00 25.04           N  
ANISOU 2525  N   SER A 344     3181   3389   2944    179    230     -6       N  
ATOM   2526  CA  SER A 344     -25.462  66.785  48.153  1.00 27.20           C  
ANISOU 2526  CA  SER A 344     3467   3663   3202    206    228      5       C  
ATOM   2527  C   SER A 344     -26.157  66.950  49.507  1.00 27.72           C  
ANISOU 2527  C   SER A 344     3515   3757   3257    217    220      8       C  
ATOM   2528  O   SER A 344     -27.297  67.393  49.533  1.00 28.92           O  
ANISOU 2528  O   SER A 344     3677   3914   3396    240    218     17       O  
ATOM   2529  CB  SER A 344     -26.295  65.947  47.187  1.00 28.94           C  
ANISOU 2529  CB  SER A 344     3684   3887   3423    218    215     26       C  
ATOM   2530  OG  SER A 344     -26.872  64.850  47.871  1.00 34.36           O  
ANISOU 2530  OG  SER A 344     4336   4605   4113    221    196     40       O  
ATOM   2531  N   ILE A 345     -25.484  66.638  50.613  1.00 28.01           N  
ANISOU 2531  N   ILE A 345     3527   3814   3299    204    215      0       N  
ATOM   2532  CA  ILE A 345     -26.054  66.766  51.964  1.00 29.87           C  
ANISOU 2532  CA  ILE A 345     3746   4079   3525    215    208      1       C  
ATOM   2533  C   ILE A 345     -25.258  67.757  52.818  1.00 31.39           C  
ANISOU 2533  C   ILE A 345     3942   4270   3712    204    221    -25       C  
ATOM   2534  O   ILE A 345     -24.179  68.180  52.414  1.00 31.12           O  
ANISOU 2534  O   ILE A 345     3921   4215   3685    185    236    -45       O  
ATOM   2535  CB  ILE A 345     -26.162  65.404  52.702  1.00 27.85           C  
ANISOU 2535  CB  ILE A 345     3452   3855   3274    214    189     16       C  
ATOM   2536  CG1 ILE A 345     -24.774  64.818  52.992  1.00 26.62           C  
ANISOU 2536  CG1 ILE A 345     3279   3704   3129    193    188      5       C  
ATOM   2537  CG2 ILE A 345     -27.077  64.465  51.932  1.00 29.54           C  
ANISOU 2537  CG2 ILE A 345     3660   4071   3492    223    177     40       C  
ATOM   2538  CD1 ILE A 345     -24.787  63.477  53.724  1.00 24.08           C  
ANISOU 2538  CD1 ILE A 345     2924   3412   2811    196    173     22       C  
ATOM   2539  N   ASN A 346     -25.772  68.116  53.994  1.00 34.34           N  
ANISOU 2539  N   ASN A 346     4305   4666   4074    215    217    -27       N  
ATOM   2540  CA  ASN A 346     -25.101  69.093  54.865  1.00 36.58           C  
ANISOU 2540  CA  ASN A 346     4592   4951   4353    206    230    -55       C  
ATOM   2541  C   ASN A 346     -24.453  68.576  56.148  1.00 36.72           C  
ANISOU 2541  C   ASN A 346     4574   5005   4370    198    220    -64       C  
ATOM   2542  O   ASN A 346     -23.470  69.142  56.629  1.00 37.54           O  
ANISOU 2542  O   ASN A 346     4675   5111   4474    182    231    -93       O  
ATOM   2543  CB  ASN A 346     -26.063  70.234  55.205  1.00 37.62           C  
ANISOU 2543  CB  ASN A 346     4746   5077   4469    225    239    -56       C  
ATOM   2544  CG  ASN A 346     -26.320  71.131  54.016  1.00 40.92           C  
ANISOU 2544  CG  ASN A 346     5206   5454   4884    231    258    -58       C  
ATOM   2545  OD1 ASN A 346     -25.394  71.481  53.279  1.00 47.33           O  
ANISOU 2545  OD1 ASN A 346     6038   6238   5705    212    275    -73       O  
ATOM   2546  ND2 ASN A 346     -27.582  71.488  53.805  1.00 43.29           N  
ANISOU 2546  ND2 ASN A 346     5522   5754   5171    259    256    -41       N  
ATOM   2547  N   ASP A 347     -25.011  67.502  56.695  1.00 36.82           N  
ANISOU 2547  N   ASP A 347     4560   5048   4382    211    201    -41       N  
ATOM   2548  CA  ASP A 347     -24.514  66.870  57.918  1.00 37.27           C  
ANISOU 2548  CA  ASP A 347     4583   5140   4435    211    190    -44       C  
ATOM   2549  C   ASP A 347     -23.009  66.585  57.854  1.00 37.62           C  
ANISOU 2549  C   ASP A 347     4616   5189   4488    190    193    -65       C  
ATOM   2550  O   ASP A 347     -22.568  65.745  57.066  1.00 37.61           O  
ANISOU 2550  O   ASP A 347     4612   5178   4498    182    190    -55       O  
ATOM   2551  CB  ASP A 347     -25.319  65.589  58.147  1.00 37.24           C  
ANISOU 2551  CB  ASP A 347     4560   5158   4432    226    173    -11       C  
ATOM   2552  CG  ASP A 347     -24.928  64.841  59.407  1.00 37.47           C  
ANISOU 2552  CG  ASP A 347     4557   5225   4455    232    163     -8       C  
ATOM   2553  OD1 ASP A 347     -23.749  64.820  59.807  1.00 39.48           O  
ANISOU 2553  OD1 ASP A 347     4798   5491   4709    222    165    -28       O  
ATOM   2554  OD2 ASP A 347     -25.827  64.211  59.992  1.00 45.29           O  
ANISOU 2554  OD2 ASP A 347     5533   6233   5439    248    154     14       O  
ATOM   2555  N   PRO A 348     -22.207  67.268  58.694  1.00 37.70           N  
ANISOU 2555  N   PRO A 348     4618   5215   4492    181    200    -96       N  
ATOM   2556  CA  PRO A 348     -20.759  67.127  58.525  1.00 36.48           C  
ANISOU 2556  CA  PRO A 348     4452   5064   4344    160    206   -121       C  
ATOM   2557  C   PRO A 348     -20.223  65.760  58.947  1.00 35.04           C  
ANISOU 2557  C   PRO A 348     4238   4913   4162    167    189   -108       C  
ATOM   2558  O   PRO A 348     -19.231  65.304  58.380  1.00 33.74           O  
ANISOU 2558  O   PRO A 348     4068   4745   4006    153    191   -117       O  
ATOM   2559  CB  PRO A 348     -20.174  68.246  59.390  1.00 37.79           C  
ANISOU 2559  CB  PRO A 348     4614   5242   4501    150    218   -160       C  
ATOM   2560  CG  PRO A 348     -21.241  68.557  60.407  1.00 38.22           C  
ANISOU 2560  CG  PRO A 348     4665   5316   4541    172    211   -149       C  
ATOM   2561  CD  PRO A 348     -22.568  68.113  59.849  1.00 38.08           C  
ANISOU 2561  CD  PRO A 348     4660   5281   4524    191    203   -110       C  
ATOM   2562  N   ALA A 349     -20.865  65.104  59.911  1.00 32.20           N  
ANISOU 2562  N   ALA A 349     3858   4583   3792    189    175    -87       N  
ATOM   2563  CA  ALA A 349     -20.440  63.752  60.283  1.00 31.73           C  
ANISOU 2563  CA  ALA A 349     3773   4550   3731    199    162    -70       C  
ATOM   2564  C   ALA A 349     -20.575  62.763  59.110  1.00 29.52           C  
ANISOU 2564  C   ALA A 349     3502   4245   3466    195    159    -44       C  
ATOM   2565  O   ALA A 349     -19.624  62.054  58.794  1.00 28.07           O  
ANISOU 2565  O   ALA A 349     3310   4066   3289    189    158    -47       O  
ATOM   2566  CB  ALA A 349     -21.189  63.252  61.522  1.00 30.74           C  
ANISOU 2566  CB  ALA A 349     3629   4458   3591    224    151    -49       C  
ATOM   2567  N   LEU A 350     -21.752  62.722  58.485  1.00 28.51           N  
ANISOU 2567  N   LEU A 350     3392   4094   3344    200    159    -21       N  
ATOM   2568  CA  LEU A 350     -22.023  61.896  57.311  1.00 27.54           C  
ANISOU 2568  CA  LEU A 350     3280   3947   3236    195    157      0       C  
ATOM   2569  C   LEU A 350     -21.106  62.245  56.134  1.00 26.76           C  
ANISOU 2569  C   LEU A 350     3197   3820   3149    174    167    -18       C  
ATOM   2570  O   LEU A 350     -20.462  61.362  55.564  1.00 27.17           O  
ANISOU 2570  O   LEU A 350     3244   3868   3211    168    164    -12       O  
ATOM   2571  CB  LEU A 350     -23.493  62.011  56.900  1.00 27.00           C  
ANISOU 2571  CB  LEU A 350     3226   3863   3168    204    156     21       C  
ATOM   2572  CG  LEU A 350     -24.562  61.436  57.838  1.00 28.66           C  
ANISOU 2572  CG  LEU A 350     3420   4097   3369    223    148     44       C  
ATOM   2573  CD1 LEU A 350     -25.955  61.648  57.271  1.00 31.50           C  
ANISOU 2573  CD1 LEU A 350     3794   4443   3730    230    147     59       C  
ATOM   2574  CD2 LEU A 350     -24.337  59.954  58.091  1.00 30.69           C  
ANISOU 2574  CD2 LEU A 350     3660   4368   3632    228    142     65       C  
ATOM   2575  N   LYS A 351     -21.026  63.528  55.791  1.00 26.54           N  
ANISOU 2575  N   LYS A 351     3190   3772   3120    164    179    -40       N  
ATOM   2576  CA  LYS A 351     -20.166  63.981  54.703  1.00 26.91           C  
ANISOU 2576  CA  LYS A 351     3254   3790   3177    143    192    -59       C  
ATOM   2577  C   LYS A 351     -18.748  63.427  54.823  1.00 26.91           C  
ANISOU 2577  C   LYS A 351     3234   3806   3181    130    191    -76       C  
ATOM   2578  O   LYS A 351     -18.179  62.940  53.837  1.00 25.99           O  
ANISOU 2578  O   LYS A 351     3123   3672   3077    119    193    -74       O  
ATOM   2579  CB  LYS A 351     -20.122  65.508  54.607  1.00 27.13           C  
ANISOU 2579  CB  LYS A 351     3307   3798   3201    134    211    -85       C  
ATOM   2580  CG  LYS A 351     -21.401  66.136  54.077  1.00 27.40           C  
ANISOU 2580  CG  LYS A 351     3369   3808   3231    147    215    -70       C  
ATOM   2581  CD  LYS A 351     -21.347  67.650  54.241  1.00 30.07           C  
ANISOU 2581  CD  LYS A 351     3732   4129   3563    141    235    -96       C  
ATOM   2582  CE  LYS A 351     -20.473  68.294  53.164  1.00 27.83           C  
ANISOU 2582  CE  LYS A 351     3475   3810   3289    119    257   -116       C  
ATOM   2583  NZ  LYS A 351     -21.199  68.326  51.864  1.00 26.90           N  
ANISOU 2583  NZ  LYS A 351     3386   3659   3174    129    261    -95       N  
ATOM   2584  N   GLN A 352     -18.195  63.512  56.032  1.00 25.99           N  
ANISOU 2584  N   GLN A 352     3094   3725   3054    134    188    -93       N  
ATOM   2585  CA  GLN A 352     -16.829  63.081  56.282  1.00 26.64           C  
ANISOU 2585  CA  GLN A 352     3153   3830   3136    125    186   -114       C  
ATOM   2586  C   GLN A 352     -16.696  61.560  56.224  1.00 24.75           C  
ANISOU 2586  C   GLN A 352     2898   3605   2899    139    172    -86       C  
ATOM   2587  O   GLN A 352     -15.713  61.060  55.682  1.00 24.00           O  
ANISOU 2587  O   GLN A 352     2796   3509   2810    129    173    -94       O  
ATOM   2588  CB  GLN A 352     -16.300  63.611  57.625  1.00 29.21           C  
ANISOU 2588  CB  GLN A 352     3456   4196   3446    128    186   -142       C  
ATOM   2589  CG  GLN A 352     -14.766  63.571  57.772  1.00 33.68           C  
ANISOU 2589  CG  GLN A 352     4000   4785   4010    114    189   -177       C  
ATOM   2590  CD  GLN A 352     -14.024  64.507  56.813  1.00 43.19           C  
ANISOU 2590  CD  GLN A 352     5223   5959   5226     82    209   -209       C  
ATOM   2591  OE1 GLN A 352     -14.381  65.676  56.653  1.00 46.13           O  
ANISOU 2591  OE1 GLN A 352     5618   6307   5600     69    225   -225       O  
ATOM   2592  NE2 GLN A 352     -12.976  63.992  56.176  1.00 43.09           N  
ANISOU 2592  NE2 GLN A 352     5202   5948   5221     69    210   -220       N  
ATOM   2593  N   LYS A 353     -17.646  60.835  56.805  1.00 22.03           N  
ANISOU 2593  N   LYS A 353     2547   3273   2550    160    161    -55       N  
ATOM   2594  CA  LYS A 353     -17.597  59.376  56.759  1.00 22.13           C  
ANISOU 2594  CA  LYS A 353     2548   3294   2565    173    152    -27       C  
ATOM   2595  C   LYS A 353     -17.596  58.930  55.287  1.00 19.84           C  
ANISOU 2595  C   LYS A 353     2276   2967   2293    160    155    -16       C  
ATOM   2596  O   LYS A 353     -16.786  58.084  54.901  1.00 19.21           O  
ANISOU 2596  O   LYS A 353     2189   2889   2218    158    153    -14       O  
ATOM   2597  CB  LYS A 353     -18.772  58.762  57.532  1.00 22.52           C  
ANISOU 2597  CB  LYS A 353     2592   3356   2607    196    145      3       C  
ATOM   2598  CG  LYS A 353     -18.899  57.235  57.470  1.00 24.26           C  
ANISOU 2598  CG  LYS A 353     2806   3578   2832    208    140     35       C  
ATOM   2599  CD  LYS A 353     -19.970  56.669  58.421  1.00 20.73           C  
ANISOU 2599  CD  LYS A 353     2352   3147   2376    229    136     63       C  
ATOM   2600  CE  LYS A 353     -21.378  57.099  58.080  1.00 27.99           C  
ANISOU 2600  CE  LYS A 353     3287   4047   3301    226    138     75       C  
ATOM   2601  NZ  LYS A 353     -22.353  56.476  59.021  1.00 29.95           N  
ANISOU 2601  NZ  LYS A 353     3525   4311   3540    244    136    100       N  
ATOM   2602  N   TYR A 354     -18.474  59.527  54.483  1.00 18.61           N  
ANISOU 2602  N   TYR A 354     2144   2781   2145    152    160    -11       N  
ATOM   2603  CA  TYR A 354     -18.659  59.093  53.095  1.00 18.96           C  
ANISOU 2603  CA  TYR A 354     2206   2793   2205    143    162      1       C  
ATOM   2604  C   TYR A 354     -17.486  59.475  52.198  1.00 20.37           C  
ANISOU 2604  C   TYR A 354     2393   2955   2392    123    171    -22       C  
ATOM   2605  O   TYR A 354     -17.020  58.663  51.394  1.00 21.12           O  
ANISOU 2605  O   TYR A 354     2488   3038   2496    117    169    -15       O  
ATOM   2606  CB  TYR A 354     -19.999  59.582  52.550  1.00 18.06           C  
ANISOU 2606  CB  TYR A 354     2111   2656   2092    146    164     14       C  
ATOM   2607  CG  TYR A 354     -21.193  58.968  53.254  1.00 16.91           C  
ANISOU 2607  CG  TYR A 354     1955   2526   1941    164    155     40       C  
ATOM   2608  CD1 TYR A 354     -21.159  57.664  53.732  1.00 18.53           C  
ANISOU 2608  CD1 TYR A 354     2143   2748   2148    173    149     60       C  
ATOM   2609  CD2 TYR A 354     -22.376  59.688  53.407  1.00 17.92           C  
ANISOU 2609  CD2 TYR A 354     2094   2652   2063    172    156     44       C  
ATOM   2610  CE1 TYR A 354     -22.257  57.105  54.381  1.00 19.20           C  
ANISOU 2610  CE1 TYR A 354     2220   2845   2228    187    145     82       C  
ATOM   2611  CE2 TYR A 354     -23.484  59.132  54.034  1.00 20.05           C  
ANISOU 2611  CE2 TYR A 354     2352   2936   2327    187    149     66       C  
ATOM   2612  CZ  TYR A 354     -23.407  57.850  54.533  1.00 20.93           C  
ANISOU 2612  CZ  TYR A 354     2446   3063   2441    192    145     85       C  
ATOM   2613  OH  TYR A 354     -24.512  57.313  55.143  1.00 21.60           O  
ANISOU 2613  OH  TYR A 354     2522   3161   2522    204    142    105       O  
ATOM   2614  N   TYR A 355     -16.990  60.699  52.370  1.00 20.26           N  
ANISOU 2614  N   TYR A 355     2385   2939   2373    111    182    -52       N  
ATOM   2615  CA  TYR A 355     -15.800  61.171  51.679  1.00 21.52           C  
ANISOU 2615  CA  TYR A 355     2551   3086   2539     89    194    -80       C  
ATOM   2616  C   TYR A 355     -14.573  60.319  51.991  1.00 21.22           C  
ANISOU 2616  C   TYR A 355     2487   3075   2501     87    188    -90       C  
ATOM   2617  O   TYR A 355     -13.835  59.915  51.073  1.00 20.92           O  
ANISOU 2617  O   TYR A 355     2451   3023   2472     75    191    -93       O  
ATOM   2618  CB  TYR A 355     -15.544  62.659  51.964  1.00 22.32           C  
ANISOU 2618  CB  TYR A 355     2663   3181   2635     75    210   -113       C  
ATOM   2619  CG  TYR A 355     -14.361  63.228  51.216  1.00 27.36           C  
ANISOU 2619  CG  TYR A 355     3310   3803   3281     49    227   -144       C  
ATOM   2620  CD1 TYR A 355     -13.061  63.042  51.686  1.00 31.54           C  
ANISOU 2620  CD1 TYR A 355     3814   4361   3808     38    227   -171       C  
ATOM   2621  CD2 TYR A 355     -14.539  63.955  50.039  1.00 29.93           C  
ANISOU 2621  CD2 TYR A 355     3670   4085   3615     36    244   -146       C  
ATOM   2622  CE1 TYR A 355     -11.973  63.557  50.998  1.00 32.26           C  
ANISOU 2622  CE1 TYR A 355     3911   4438   3906     11    245   -202       C  
ATOM   2623  CE2 TYR A 355     -13.459  64.482  49.352  1.00 31.47           C  
ANISOU 2623  CE2 TYR A 355     3875   4264   3817     11    263   -175       C  
ATOM   2624  CZ  TYR A 355     -12.179  64.270  49.836  1.00 30.30           C  
ANISOU 2624  CZ  TYR A 355     3698   4144   3668     -2    263   -203       C  
ATOM   2625  OH  TYR A 355     -11.092  64.783  49.168  1.00 34.26           O  
ANISOU 2625  OH  TYR A 355     4207   4631   4177    -30    283   -234       O  
ATOM   2626  N   ASN A 356     -14.357  60.040  53.273  1.00 20.57           N  
ANISOU 2626  N   ASN A 356     2377   3031   2404    102    179    -93       N  
ATOM   2627  CA  ASN A 356     -13.225  59.202  53.661  1.00 21.76           C  
ANISOU 2627  CA  ASN A 356     2502   3214   2550    107    172   -101       C  
ATOM   2628  C   ASN A 356     -13.302  57.809  53.041  1.00 20.31           C  
ANISOU 2628  C   ASN A 356     2319   3021   2374    117    164    -70       C  
ATOM   2629  O   ASN A 356     -12.278  57.274  52.612  1.00 20.53           O  
ANISOU 2629  O   ASN A 356     2339   3054   2406    112    164    -79       O  
ATOM   2630  CB  ASN A 356     -13.103  59.064  55.184  1.00 21.76           C  
ANISOU 2630  CB  ASN A 356     2475   3260   2530    127    163   -106       C  
ATOM   2631  CG  ASN A 356     -12.603  60.342  55.855  1.00 28.04           C  
ANISOU 2631  CG  ASN A 356     3262   4074   3316    115    172   -147       C  
ATOM   2632  OD1 ASN A 356     -12.234  61.315  55.187  1.00 31.78           O  
ANISOU 2632  OD1 ASN A 356     3750   4525   3799     89    187   -174       O  
ATOM   2633  ND2 ASN A 356     -12.629  60.358  57.185  1.00 27.86           N  
ANISOU 2633  ND2 ASN A 356     3217   4092   3276    133    164   -153       N  
ATOM   2634  N   PHE A 357     -14.498  57.221  53.056  1.00 17.60           N  
ANISOU 2634  N   PHE A 357     1985   2666   2034    131    158    -36       N  
ATOM   2635  CA  PHE A 357     -14.727  55.942  52.387  1.00 17.81           C  
ANISOU 2635  CA  PHE A 357     2016   2679   2071    137    154     -6       C  
ATOM   2636  C   PHE A 357     -14.344  56.050  50.904  1.00 17.07           C  
ANISOU 2636  C   PHE A 357     1939   2550   1993    117    160    -13       C  
ATOM   2637  O   PHE A 357     -13.568  55.240  50.399  1.00 17.44           O  
ANISOU 2637  O   PHE A 357     1982   2597   2046    115    158    -12       O  
ATOM   2638  CB  PHE A 357     -16.189  55.500  52.504  1.00 17.45           C  
ANISOU 2638  CB  PHE A 357     1979   2622   2028    149    150     25       C  
ATOM   2639  CG  PHE A 357     -16.560  54.443  51.505  1.00 19.32           C  
ANISOU 2639  CG  PHE A 357     2226   2834   2280    147    149     48       C  
ATOM   2640  CD1 PHE A 357     -16.073  53.143  51.631  1.00 18.72           C  
ANISOU 2640  CD1 PHE A 357     2141   2767   2205    158    147     64       C  
ATOM   2641  CD2 PHE A 357     -17.335  54.767  50.396  1.00 20.68           C  
ANISOU 2641  CD2 PHE A 357     2418   2974   2463    135    152     53       C  
ATOM   2642  CE1 PHE A 357     -16.374  52.165  50.684  1.00 16.72           C  
ANISOU 2642  CE1 PHE A 357     1897   2488   1966    154    148     83       C  
ATOM   2643  CE2 PHE A 357     -17.640  53.802  49.452  1.00 20.22           C  
ANISOU 2643  CE2 PHE A 357     2367   2895   2418    132    152     71       C  
ATOM   2644  CZ  PHE A 357     -17.165  52.507  49.597  1.00 18.06           C  
ANISOU 2644  CZ  PHE A 357     2084   2628   2147    139    150     85       C  
ATOM   2645  N   ALA A 358     -14.897  57.043  50.214  1.00 16.47           N  
ANISOU 2645  N   ALA A 358     1886   2448   1924    103    168    -21       N  
ATOM   2646  CA  ALA A 358     -14.725  57.158  48.763  1.00 16.69           C  
ANISOU 2646  CA  ALA A 358     1934   2442   1965     87    174    -23       C  
ATOM   2647  C   ALA A 358     -13.255  57.296  48.423  1.00 17.57           C  
ANISOU 2647  C   ALA A 358     2039   2558   2079     72    181    -50       C  
ATOM   2648  O   ALA A 358     -12.720  56.583  47.564  1.00 17.09           O  
ANISOU 2648  O   ALA A 358     1980   2486   2028     66    180    -46       O  
ATOM   2649  CB  ALA A 358     -15.502  58.349  48.213  1.00 15.73           C  
ANISOU 2649  CB  ALA A 358     1838   2293   1844     80    184    -29       C  
ATOM   2650  N   LYS A 359     -12.608  58.238  49.102  1.00 17.85           N  
ANISOU 2650  N   LYS A 359     2066   2610   2105     63    188    -80       N  
ATOM   2651  CA  LYS A 359     -11.202  58.510  48.839  1.00 18.09           C  
ANISOU 2651  CA  LYS A 359     2087   2648   2137     45    196   -112       C  
ATOM   2652  C   LYS A 359     -10.334  57.310  49.161  1.00 17.53           C  
ANISOU 2652  C   LYS A 359     1990   2606   2062     57    185   -109       C  
ATOM   2653  O   LYS A 359      -9.370  57.051  48.449  1.00 16.22           O  
ANISOU 2653  O   LYS A 359     1821   2437   1902     45    189   -122       O  
ATOM   2654  CB  LYS A 359     -10.689  59.769  49.558  1.00 18.94           C  
ANISOU 2654  CB  LYS A 359     2189   2771   2236     32    208   -150       C  
ATOM   2655  CG  LYS A 359      -9.311  60.223  49.070  1.00 21.04           C  
ANISOU 2655  CG  LYS A 359     2449   3037   2506      6    222   -188       C  
ATOM   2656  CD  LYS A 359      -8.881  61.538  49.741  1.00 21.54           C  
ANISOU 2656  CD  LYS A 359     2508   3112   2562    -10    237   -229       C  
ATOM   2657  CE  LYS A 359      -7.557  62.039  49.171  1.00 21.68           C  
ANISOU 2657  CE  LYS A 359     2523   3128   2586    -40    255   -268       C  
ATOM   2658  NZ  LYS A 359      -6.400  61.233  49.626  1.00 19.88           N  
ANISOU 2658  NZ  LYS A 359     2256   2944   2350    -36    244   -285       N  
ATOM   2659  N   SER A 360     -10.641  56.583  50.231  1.00 17.51           N  
ANISOU 2659  N   SER A 360     1969   2633   2048     82    173    -92       N  
ATOM   2660  CA  SER A 360      -9.782  55.450  50.569  1.00 18.00           C  
ANISOU 2660  CA  SER A 360     2010   2725   2104     98    164    -87       C  
ATOM   2661  C   SER A 360      -9.852  54.367  49.492  1.00 16.85           C  
ANISOU 2661  C   SER A 360     1876   2553   1972     99    161    -62       C  
ATOM   2662  O   SER A 360      -8.866  53.664  49.240  1.00 15.02           O  
ANISOU 2662  O   SER A 360     1633   2333   1739    102    159    -67       O  
ATOM   2663  CB  SER A 360     -10.151  54.859  51.938  1.00 19.53           C  
ANISOU 2663  CB  SER A 360     2185   2953   2281    127    153    -71       C  
ATOM   2664  OG  SER A 360     -11.374  54.152  51.830  1.00 22.47           O  
ANISOU 2664  OG  SER A 360     2572   3304   2659    140    150    -32       O  
ATOM   2665  N   GLN A 361     -11.022  54.176  48.887  1.00 15.24           N  
ANISOU 2665  N   GLN A 361     1693   2316   1779     98    162    -35       N  
ATOM   2666  CA  GLN A 361     -11.129  53.117  47.873  1.00 15.48           C  
ANISOU 2666  CA  GLN A 361     1734   2322   1822     99    160    -13       C  
ATOM   2667  C   GLN A 361     -10.377  53.465  46.587  1.00 13.58           C  
ANISOU 2667  C   GLN A 361     1505   2059   1593     76    167    -31       C  
ATOM   2668  O   GLN A 361      -9.754  52.612  45.947  1.00 13.57           O  
ANISOU 2668  O   GLN A 361     1503   2054   1599     77    166    -27       O  
ATOM   2669  CB  GLN A 361     -12.597  52.825  47.538  1.00 14.69           C  
ANISOU 2669  CB  GLN A 361     1652   2197   1731    102    158     15       C  
ATOM   2670  CG  GLN A 361     -13.418  52.383  48.746  1.00 15.93           C  
ANISOU 2670  CG  GLN A 361     1799   2374   1878    123    153     36       C  
ATOM   2671  CD  GLN A 361     -12.803  51.172  49.415  1.00 16.73           C  
ANISOU 2671  CD  GLN A 361     1884   2498   1972    144    149     48       C  
ATOM   2672  OE1 GLN A 361     -12.835  50.069  48.872  1.00 16.28           O  
ANISOU 2672  OE1 GLN A 361     1834   2427   1924    148    149     68       O  
ATOM   2673  NE2 GLN A 361     -12.218  51.375  50.591  1.00 18.59           N  
ANISOU 2673  NE2 GLN A 361     2101   2771   2190    158    146     37       N  
ATOM   2674  N   ILE A 362     -10.456  54.728  46.188  1.00 14.29           N  
ANISOU 2674  N   ILE A 362     1609   2133   1686     57    177    -52       N  
ATOM   2675  CA  ILE A 362      -9.736  55.162  44.989  1.00 14.04           C  
ANISOU 2675  CA  ILE A 362     1590   2078   1664     36    188    -70       C  
ATOM   2676  C   ILE A 362      -8.234  55.094  45.273  1.00 14.09           C  
ANISOU 2676  C   ILE A 362     1575   2113   1666     29    190    -98       C  
ATOM   2677  O   ILE A 362      -7.442  54.566  44.477  1.00 12.26           O  
ANISOU 2677  O   ILE A 362     1342   1876   1440     23    191   -102       O  
ATOM   2678  CB  ILE A 362     -10.136  56.609  44.599  1.00 14.46           C  
ANISOU 2678  CB  ILE A 362     1666   2107   1719     19    202    -86       C  
ATOM   2679  CG1 ILE A 362     -11.640  56.720  44.318  1.00 13.65           C  
ANISOU 2679  CG1 ILE A 362     1584   1982   1619     29    199    -59       C  
ATOM   2680  CG2 ILE A 362      -9.279  57.110  43.445  1.00 13.53           C  
ANISOU 2680  CG2 ILE A 362     1563   1967   1610     -3    217   -107       C  
ATOM   2681  CD1 ILE A 362     -12.156  55.744  43.245  1.00 20.11           C  
ANISOU 2681  CD1 ILE A 362     2413   2779   2449     34    193    -34       C  
ATOM   2682  N   ASP A 363      -7.842  55.581  46.446  1.00 13.33           N  
ANISOU 2682  N   ASP A 363     1458   2050   1555     33    189   -119       N  
ATOM   2683  CA  ASP A 363      -6.415  55.565  46.786  1.00 15.05           C  
ANISOU 2683  CA  ASP A 363     1650   2302   1765     28    191   -151       C  
ATOM   2684  C   ASP A 363      -5.884  54.133  46.878  1.00 14.51           C  
ANISOU 2684  C   ASP A 363     1564   2255   1692     50    178   -134       C  
ATOM   2685  O   ASP A 363      -4.756  53.882  46.459  1.00 15.99           O  
ANISOU 2685  O   ASP A 363     1740   2454   1879     44    180   -152       O  
ATOM   2686  CB  ASP A 363      -6.108  56.369  48.059  1.00 16.75           C  
ANISOU 2686  CB  ASP A 363     1843   2554   1964     28    192   -179       C  
ATOM   2687  CG  ASP A 363      -6.175  57.876  47.829  1.00 20.44           C  
ANISOU 2687  CG  ASP A 363     2327   3001   2436      0    211   -208       C  
ATOM   2688  OD1 ASP A 363      -6.405  58.328  46.686  1.00 18.77           O  
ANISOU 2688  OD1 ASP A 363     2144   2748   2240    -18    224   -206       O  
ATOM   2689  OD2 ASP A 363      -6.038  58.635  48.807  1.00 18.49           O  
ANISOU 2689  OD2 ASP A 363     2066   2780   2179     -2    214   -233       O  
ATOM   2690  N   TYR A 364      -6.685  53.188  47.378  1.00 14.25           N  
ANISOU 2690  N   TYR A 364     1533   2225   1656     76    167    -98       N  
ATOM   2691  CA  TYR A 364      -6.261  51.777  47.317  1.00 15.14           C  
ANISOU 2691  CA  TYR A 364     1637   2349   1767     98    159    -78       C  
ATOM   2692  C   TYR A 364      -5.930  51.351  45.880  1.00 14.07           C  
ANISOU 2692  C   TYR A 364     1516   2181   1647     83    163    -74       C  
ATOM   2693  O   TYR A 364      -4.876  50.761  45.619  1.00 14.42           O  
ANISOU 2693  O   TYR A 364     1548   2240   1688     88    162    -84       O  
ATOM   2694  CB  TYR A 364      -7.315  50.832  47.922  1.00 13.63           C  
ANISOU 2694  CB  TYR A 364     1450   2154   1572    124    152    -39       C  
ATOM   2695  CG  TYR A 364      -6.877  49.376  48.015  1.00 13.05           C  
ANISOU 2695  CG  TYR A 364     1370   2092   1493    149    147    -18       C  
ATOM   2696  CD1 TYR A 364      -6.733  48.596  46.870  1.00 12.18           C  
ANISOU 2696  CD1 TYR A 364     1274   1953   1398    144    149     -5       C  
ATOM   2697  CD2 TYR A 364      -6.617  48.779  49.254  1.00 16.73           C  
ANISOU 2697  CD2 TYR A 364     1818   2597   1939    182    142    -10       C  
ATOM   2698  CE1 TYR A 364      -6.319  47.268  46.958  1.00 11.66           C  
ANISOU 2698  CE1 TYR A 364     1205   1895   1327    168    147     14       C  
ATOM   2699  CE2 TYR A 364      -6.206  47.443  49.355  1.00 11.59           C  
ANISOU 2699  CE2 TYR A 364     1166   1955   1282    209    140     10       C  
ATOM   2700  CZ  TYR A 364      -6.067  46.707  48.201  1.00 13.89           C  
ANISOU 2700  CZ  TYR A 364     1472   2214   1589    201    143     22       C  
ATOM   2701  OH  TYR A 364      -5.656  45.404  48.248  1.00 15.62           O  
ANISOU 2701  OH  TYR A 364     1693   2439   1803    227    144     43       O  
ATOM   2702  N   ALA A 365      -6.835  51.649  44.946  1.00 12.55           N  
ANISOU 2702  N   ALA A 365     1350   1947   1470     68    168    -61       N  
ATOM   2703  CA  ALA A 365      -6.658  51.276  43.544  1.00 12.92           C  
ANISOU 2703  CA  ALA A 365     1413   1962   1533     55    172    -56       C  
ATOM   2704  C   ALA A 365      -5.410  51.908  42.908  1.00 13.53           C  
ANISOU 2704  C   ALA A 365     1485   2042   1611     34    181    -90       C  
ATOM   2705  O   ALA A 365      -4.790  51.308  42.023  1.00 14.38           O  
ANISOU 2705  O   ALA A 365     1596   2141   1727     30    182    -90       O  
ATOM   2706  CB  ALA A 365      -7.927  51.649  42.739  1.00 13.48           C  
ANISOU 2706  CB  ALA A 365     1510   1992   1616     45    175    -39       C  
ATOM   2707  N   LEU A 366      -5.048  53.106  43.361  1.00 13.88           N  
ANISOU 2707  N   LEU A 366     1524   2100   1650     19    189   -121       N  
ATOM   2708  CA  LEU A 366      -3.913  53.852  42.819  1.00 16.86           C  
ANISOU 2708  CA  LEU A 366     1897   2478   2029     -6    203   -158       C  
ATOM   2709  C   LEU A 366      -2.561  53.484  43.436  1.00 17.21           C  
ANISOU 2709  C   LEU A 366     1908   2570   2061      0    199   -184       C  
ATOM   2710  O   LEU A 366      -1.523  53.822  42.872  1.00 16.50           O  
ANISOU 2710  O   LEU A 366     1811   2483   1973    -19    209   -213       O  
ATOM   2711  CB  LEU A 366      -4.144  55.361  42.962  1.00 15.89           C  
ANISOU 2711  CB  LEU A 366     1786   2345   1907    -28    218   -182       C  
ATOM   2712  CG  LEU A 366      -5.378  55.918  42.251  1.00 19.09           C  
ANISOU 2712  CG  LEU A 366     2226   2704   2322    -33    225   -162       C  
ATOM   2713  CD1 LEU A 366      -5.411  57.452  42.348  1.00 16.81           C  
ANISOU 2713  CD1 LEU A 366     1951   2402   2032    -55    245   -189       C  
ATOM   2714  CD2 LEU A 366      -5.337  55.460  40.803  1.00 13.81           C  
ANISOU 2714  CD2 LEU A 366     1577   2002   1667    -40    228   -149       C  
ATOM   2715  N   GLY A 367      -2.575  52.836  44.602  1.00 16.19           N  
ANISOU 2715  N   GLY A 367     1756   2477   1916     28    185   -174       N  
ATOM   2716  CA  GLY A 367      -1.350  52.349  45.229  1.00 16.89           C  
ANISOU 2716  CA  GLY A 367     1812   2616   1988     42    179   -196       C  
ATOM   2717  C   GLY A 367      -1.320  52.304  46.751  1.00 18.90           C  
ANISOU 2717  C   GLY A 367     2041   2919   2221     67    169   -201       C  
ATOM   2718  O   GLY A 367      -0.312  51.912  47.321  1.00 19.90           O  
ANISOU 2718  O   GLY A 367     2137   3091   2330     83    163   -220       O  
ATOM   2719  N   SER A 368      -2.376  52.737  47.437  1.00 18.39           N  
ANISOU 2719  N   SER A 368     1985   2847   2155     72    168   -187       N  
ATOM   2720  CA  SER A 368      -2.354  52.721  48.902  1.00 19.33           C  
ANISOU 2720  CA  SER A 368     2079   3013   2252     97    159   -192       C  
ATOM   2721  C   SER A 368      -2.875  51.385  49.405  1.00 19.79           C  
ANISOU 2721  C   SER A 368     2139   3077   2302    136    147   -150       C  
ATOM   2722  O   SER A 368      -3.987  51.301  49.911  1.00 19.86           O  
ANISOU 2722  O   SER A 368     2160   3074   2311    147    145   -122       O  
ATOM   2723  CB  SER A 368      -3.227  53.830  49.483  1.00 18.53           C  
ANISOU 2723  CB  SER A 368     1986   2903   2151     85    164   -199       C  
ATOM   2724  OG  SER A 368      -2.732  55.073  49.032  1.00 21.39           O  
ANISOU 2724  OG  SER A 368     2350   3256   2521     48    179   -239       O  
ATOM   2725  N   ASN A 369      -2.050  50.355  49.273  1.00 20.12           N  
ANISOU 2725  N   ASN A 369     2169   3138   2335    157    142   -145       N  
ATOM   2726  CA  ASN A 369      -2.451  48.989  49.571  1.00 20.25           C  
ANISOU 2726  CA  ASN A 369     2193   3153   2345    193    135   -103       C  
ATOM   2727  C   ASN A 369      -1.246  48.206  50.101  1.00 20.79           C  
ANISOU 2727  C   ASN A 369     2236   3272   2391    226    129   -113       C  
ATOM   2728  O   ASN A 369      -0.128  48.722  50.081  1.00 21.72           O  
ANISOU 2728  O   ASN A 369     2329   3423   2500    216    129   -153       O  
ATOM   2729  CB  ASN A 369      -3.026  48.349  48.301  1.00 17.40           C  
ANISOU 2729  CB  ASN A 369     1862   2738   2009    181    140    -74       C  
ATOM   2730  CG  ASN A 369      -2.089  48.461  47.130  1.00 18.12           C  
ANISOU 2730  CG  ASN A 369     1953   2818   2111    158    144    -96       C  
ATOM   2731  OD1 ASN A 369      -0.963  47.961  47.165  1.00 18.05           O  
ANISOU 2731  OD1 ASN A 369     1926   2841   2091    172    141   -110       O  
ATOM   2732  ND2 ASN A 369      -2.543  49.126  46.081  1.00 17.07           N  
ANISOU 2732  ND2 ASN A 369     1842   2644   2000    125    152    -99       N  
ATOM   2733  N   PRO A 370      -1.457  46.964  50.575  1.00 23.09           N  
ANISOU 2733  N   PRO A 370     2532   3570   2671    265    125    -77       N  
ATOM   2734  CA  PRO A 370      -0.350  46.201  51.165  1.00 24.17           C  
ANISOU 2734  CA  PRO A 370     2645   3756   2780    304    119    -84       C  
ATOM   2735  C   PRO A 370       0.857  46.004  50.245  1.00 26.53           C  
ANISOU 2735  C   PRO A 370     2933   4063   3081    295    119   -107       C  
ATOM   2736  O   PRO A 370       1.962  45.793  50.744  1.00 25.60           O  
ANISOU 2736  O   PRO A 370     2787   3999   2939    319    114   -130       O  
ATOM   2737  CB  PRO A 370      -1.000  44.857  51.508  1.00 23.73           C  
ANISOU 2737  CB  PRO A 370     2610   3685   2720    342    121    -33       C  
ATOM   2738  CG  PRO A 370      -2.448  45.231  51.802  1.00 22.62           C  
ANISOU 2738  CG  PRO A 370     2489   3512   2593    329    125    -11       C  
ATOM   2739  CD  PRO A 370      -2.750  46.274  50.759  1.00 21.76           C  
ANISOU 2739  CD  PRO A 370     2390   3367   2511    279    128    -31       C  
ATOM   2740  N   ASP A 371       0.666  46.088  48.930  1.00 27.06           N  
ANISOU 2740  N   ASP A 371     3022   4081   3176    261    126   -104       N  
ATOM   2741  CA  ASP A 371       1.794  46.035  47.992  1.00 28.30           C  
ANISOU 2741  CA  ASP A 371     3169   4243   3337    247    127   -129       C  
ATOM   2742  C   ASP A 371       2.324  47.383  47.510  1.00 28.07           C  
ANISOU 2742  C   ASP A 371     3127   4218   3318    203    133   -176       C  
ATOM   2743  O   ASP A 371       3.282  47.437  46.739  1.00 31.50           O  
ANISOU 2743  O   ASP A 371     3553   4658   3756    188    136   -201       O  
ATOM   2744  CB  ASP A 371       1.460  45.173  46.776  1.00 28.08           C  
ANISOU 2744  CB  ASP A 371     3172   4164   3332    241    131    -98       C  
ATOM   2745  CG  ASP A 371       1.525  43.681  47.068  1.00 31.94           C  
ANISOU 2745  CG  ASP A 371     3668   4658   3808    286    129    -63       C  
ATOM   2746  OD1 ASP A 371       2.532  43.212  47.637  1.00 36.62           O  
ANISOU 2746  OD1 ASP A 371     4238   5300   4376    319    124    -74       O  
ATOM   2747  OD2 ASP A 371       0.575  42.958  46.706  1.00 34.95           O  
ANISOU 2747  OD2 ASP A 371     4078   4994   4205    289    134    -25       O  
ATOM   2748  N   ASN A 372       1.739  48.480  47.968  1.00 28.18           N  
ANISOU 2748  N   ASN A 372     3141   4228   3335    182    136   -190       N  
ATOM   2749  CA  ASN A 372       2.120  49.803  47.480  1.00 28.19           C  
ANISOU 2749  CA  ASN A 372     3138   4225   3348    137    147   -232       C  
ATOM   2750  C   ASN A 372       2.074  49.940  45.958  1.00 26.34           C  
ANISOU 2750  C   ASN A 372     2929   3938   3140    104    157   -229       C  
ATOM   2751  O   ASN A 372       2.807  50.763  45.386  1.00 25.63           O  
ANISOU 2751  O   ASN A 372     2832   3849   3057     72    168   -267       O  
ATOM   2752  CB  ASN A 372       3.530  50.161  47.956  1.00 30.14           C  
ANISOU 2752  CB  ASN A 372     3344   4533   3575    138    146   -283       C  
ATOM   2753  CG  ASN A 372       3.532  51.412  48.786  1.00 37.83           C  
ANISOU 2753  CG  ASN A 372     4299   5532   4540    119    151   -320       C  
ATOM   2754  OD1 ASN A 372       2.979  51.435  49.893  1.00 44.09           O  
ANISOU 2754  OD1 ASN A 372     5085   6346   5319    142    143   -310       O  
ATOM   2755  ND2 ASN A 372       4.132  52.474  48.252  1.00 43.77           N  
ANISOU 2755  ND2 ASN A 372     5046   6281   5303     76    165   -364       N  
ATOM   2756  N   ARG A 373       1.221  49.149  45.307  1.00 21.49           N  
ANISOU 2756  N   ARG A 373     2344   3280   2540    112    155   -186       N  
ATOM   2757  CA  ARG A 373       1.225  49.122  43.846  1.00 20.60           C  
ANISOU 2757  CA  ARG A 373     2255   3122   2450     87    163   -182       C  
ATOM   2758  C   ARG A 373      -0.082  49.607  43.211  1.00 18.56           C  
ANISOU 2758  C   ARG A 373     2030   2808   2212     66    169   -160       C  
ATOM   2759  O   ARG A 373      -1.175  49.341  43.714  1.00 17.39           O  
ANISOU 2759  O   ARG A 373     1893   2648   2064     81    164   -130       O  
ATOM   2760  CB  ARG A 373       1.621  47.734  43.345  1.00 21.40           C  
ANISOU 2760  CB  ARG A 373     2358   3220   2550    111    157   -159       C  
ATOM   2761  CG  ARG A 373       0.622  46.629  43.688  1.00 22.63           C  
ANISOU 2761  CG  ARG A 373     2531   3359   2707    141    150   -111       C  
ATOM   2762  CD  ARG A 373      -0.246  46.297  42.489  1.00 26.57           C  
ANISOU 2762  CD  ARG A 373     3063   3800   3230    125    154    -84       C  
ATOM   2763  NE  ARG A 373       0.578  46.052  41.304  1.00 31.43           N  
ANISOU 2763  NE  ARG A 373     3681   4404   3855    111    158    -96       N  
ATOM   2764  CZ  ARG A 373       1.308  44.956  41.117  1.00 30.08           C  
ANISOU 2764  CZ  ARG A 373     3504   4245   3678    134    154    -88       C  
ATOM   2765  NH1 ARG A 373       1.289  44.008  42.039  1.00 25.07           N  
ANISOU 2765  NH1 ARG A 373     2863   3633   3027    171    148    -67       N  
ATOM   2766  NH2 ARG A 373       2.046  44.804  40.021  1.00 27.04           N  
ANISOU 2766  NH2 ARG A 373     3122   3850   3302    120    158   -100       N  
ATOM   2767  N   SER A 374       0.059  50.325  42.103  1.00 17.73           N  
ANISOU 2767  N   SER A 374     1941   2673   2123     34    181   -175       N  
ATOM   2768  CA  SER A 374      -1.060  50.745  41.274  1.00 17.40           C  
ANISOU 2768  CA  SER A 374     1931   2579   2098     17    188   -156       C  
ATOM   2769  C   SER A 374      -1.735  49.523  40.672  1.00 16.65           C  
ANISOU 2769  C   SER A 374     1854   2458   2014     34    180   -116       C  
ATOM   2770  O   SER A 374      -1.057  48.594  40.227  1.00 16.79           O  
ANISOU 2770  O   SER A 374     1867   2481   2032     43    176   -111       O  
ATOM   2771  CB  SER A 374      -0.555  51.616  40.115  1.00 16.50           C  
ANISOU 2771  CB  SER A 374     1831   2440   1997    -16    204   -181       C  
ATOM   2772  OG  SER A 374      -1.611  51.800  39.177  1.00 17.40           O  
ANISOU 2772  OG  SER A 374     1978   2506   2126    -25    208   -157       O  
ATOM   2773  N   TYR A 375      -3.063  49.569  40.620  1.00 15.44           N  
ANISOU 2773  N   TYR A 375     1720   2276   1867     35    178    -90       N  
ATOM   2774  CA  TYR A 375      -3.840  48.552  39.928  1.00 14.58           C  
ANISOU 2774  CA  TYR A 375     1631   2138   1771     44    174    -56       C  
ATOM   2775  C   TYR A 375      -4.395  49.139  38.623  1.00 14.92           C  
ANISOU 2775  C   TYR A 375     1699   2139   1829     22    182    -55       C  
ATOM   2776  O   TYR A 375      -5.324  48.598  38.035  1.00 15.44           O  
ANISOU 2776  O   TYR A 375     1781   2179   1905     25    179    -31       O  
ATOM   2777  CB  TYR A 375      -4.966  48.048  40.842  1.00 14.72           C  
ANISOU 2777  CB  TYR A 375     1649   2157   1784     65    167    -28       C  
ATOM   2778  CG  TYR A 375      -4.471  47.036  41.868  1.00 14.68           C  
ANISOU 2778  CG  TYR A 375     1626   2186   1766     94    160    -18       C  
ATOM   2779  CD1 TYR A 375      -4.132  45.737  41.494  1.00 15.83           C  
ANISOU 2779  CD1 TYR A 375     1773   2326   1913    110    158      0       C  
ATOM   2780  CD2 TYR A 375      -4.271  47.404  43.197  1.00 17.83           C  
ANISOU 2780  CD2 TYR A 375     2005   2622   2146    109    157    -28       C  
ATOM   2781  CE1 TYR A 375      -3.659  44.808  42.427  1.00 16.68           C  
ANISOU 2781  CE1 TYR A 375     1868   2464   2005    142    154     10       C  
ATOM   2782  CE2 TYR A 375      -3.799  46.488  44.136  1.00 15.86           C  
ANISOU 2782  CE2 TYR A 375     1740   2406   1880    140    151    -18       C  
ATOM   2783  CZ  TYR A 375      -3.496  45.200  43.745  1.00 17.38           C  
ANISOU 2783  CZ  TYR A 375     1937   2590   2074    158    151      1       C  
ATOM   2784  OH  TYR A 375      -3.016  44.299  44.670  1.00 17.21           O  
ANISOU 2784  OH  TYR A 375     1904   2601   2034    194    148     12       O  
ATOM   2785  N   VAL A 376      -3.828  50.260  38.193  1.00 14.15           N  
ANISOU 2785  N   VAL A 376     1605   2038   1733      0    193    -84       N  
ATOM   2786  CA  VAL A 376      -4.223  50.941  36.954  1.00 14.40           C  
ANISOU 2786  CA  VAL A 376     1663   2031   1776    -19    203    -85       C  
ATOM   2787  C   VAL A 376      -3.081  50.791  35.945  1.00 13.37           C  
ANISOU 2787  C   VAL A 376     1532   1895   1651    -32    211   -102       C  
ATOM   2788  O   VAL A 376      -1.980  51.306  36.155  1.00 15.25           O  
ANISOU 2788  O   VAL A 376     1756   2153   1884    -45    219   -132       O  
ATOM   2789  CB  VAL A 376      -4.534  52.434  37.205  1.00 13.09           C  
ANISOU 2789  CB  VAL A 376     1508   1858   1607    -35    216   -103       C  
ATOM   2790  CG1 VAL A 376      -4.924  53.129  35.900  1.00 15.32           C  
ANISOU 2790  CG1 VAL A 376     1821   2101   1898    -50    229   -103       C  
ATOM   2791  CG2 VAL A 376      -5.694  52.584  38.207  1.00 13.80           C  
ANISOU 2791  CG2 VAL A 376     1597   1954   1690    -20    208    -87       C  
ATOM   2792  N   VAL A 377      -3.328  50.066  34.859  1.00 13.36           N  
ANISOU 2792  N   VAL A 377     1546   1870   1660    -30    208    -84       N  
ATOM   2793  CA  VAL A 377      -2.286  49.817  33.853  1.00 12.51           C  
ANISOU 2793  CA  VAL A 377     1439   1757   1558    -41    214    -97       C  
ATOM   2794  C   VAL A 377      -1.654  51.136  33.394  1.00 13.62           C  
ANISOU 2794  C   VAL A 377     1587   1888   1698    -67    233   -128       C  
ATOM   2795  O   VAL A 377      -2.350  52.124  33.118  1.00 12.18           O  
ANISOU 2795  O   VAL A 377     1426   1682   1517    -77    244   -128       O  
ATOM   2796  CB  VAL A 377      -2.835  49.032  32.632  1.00 13.63           C  
ANISOU 2796  CB  VAL A 377     1598   1868   1710    -37    210    -75       C  
ATOM   2797  CG1 VAL A 377      -1.753  48.809  31.553  1.00 11.97           C  
ANISOU 2797  CG1 VAL A 377     1390   1651   1505    -48    216    -89       C  
ATOM   2798  CG2 VAL A 377      -3.431  47.689  33.061  1.00 11.09           C  
ANISOU 2798  CG2 VAL A 377     1270   1551   1390    -15    195    -47       C  
ATOM   2799  N   GLY A 378      -0.323  51.151  33.363  1.00 14.49           N  
ANISOU 2799  N   GLY A 378     1680   2019   1805    -77    239   -154       N  
ATOM   2800  CA  GLY A 378       0.441  52.299  32.867  1.00 15.25           C  
ANISOU 2800  CA  GLY A 378     1783   2108   1903   -105    261   -186       C  
ATOM   2801  C   GLY A 378       0.428  53.530  33.750  1.00 16.97           C  
ANISOU 2801  C   GLY A 378     1997   2336   2115   -119    274   -210       C  
ATOM   2802  O   GLY A 378       0.804  54.612  33.295  1.00 16.97           O  
ANISOU 2802  O   GLY A 378     2011   2319   2117   -145    297   -234       O  
ATOM   2803  N   PHE A 379       0.004  53.384  35.004  1.00 15.46           N  
ANISOU 2803  N   PHE A 379     1789   2170   1914   -104    261   -204       N  
ATOM   2804  CA  PHE A 379      -0.060  54.520  35.926  1.00 15.78           C  
ANISOU 2804  CA  PHE A 379     1824   2222   1948   -115    271   -227       C  
ATOM   2805  C   PHE A 379       0.615  54.125  37.235  1.00 18.08           C  
ANISOU 2805  C   PHE A 379     2076   2565   2225   -103    259   -243       C  
ATOM   2806  O   PHE A 379       0.444  52.994  37.711  1.00 15.88           O  
ANISOU 2806  O   PHE A 379     1784   2307   1942    -76    239   -220       O  
ATOM   2807  CB  PHE A 379      -1.504  54.964  36.230  1.00 13.93           C  
ANISOU 2807  CB  PHE A 379     1612   1966   1714   -106    269   -203       C  
ATOM   2808  CG  PHE A 379      -1.609  55.980  37.354  1.00 17.64           C  
ANISOU 2808  CG  PHE A 379     2074   2452   2175   -113    276   -224       C  
ATOM   2809  CD1 PHE A 379      -1.519  57.346  37.097  1.00 18.04           C  
ANISOU 2809  CD1 PHE A 379     2144   2481   2229   -138    302   -248       C  
ATOM   2810  CD2 PHE A 379      -1.766  55.569  38.670  1.00 17.76           C  
ANISOU 2810  CD2 PHE A 379     2062   2504   2179    -94    259   -220       C  
ATOM   2811  CE1 PHE A 379      -1.591  58.278  38.132  1.00 17.92           C  
ANISOU 2811  CE1 PHE A 379     2121   2480   2205   -146    310   -269       C  
ATOM   2812  CE2 PHE A 379      -1.824  56.490  39.720  1.00 18.77           C  
ANISOU 2812  CE2 PHE A 379     2181   2649   2298   -100    266   -241       C  
ATOM   2813  CZ  PHE A 379      -1.742  57.851  39.445  1.00 17.61           C  
ANISOU 2813  CZ  PHE A 379     2053   2480   2155   -127    291   -267       C  
ATOM   2814  N   GLY A 380       1.345  55.078  37.809  1.00 18.26           N  
ANISOU 2814  N   GLY A 380     2083   2610   2242   -123    273   -282       N  
ATOM   2815  CA  GLY A 380       1.843  54.962  39.178  1.00 20.37           C  
ANISOU 2815  CA  GLY A 380     2315   2931   2494   -112    263   -302       C  
ATOM   2816  C   GLY A 380       2.907  53.898  39.380  1.00 21.58           C  
ANISOU 2816  C   GLY A 380     2435   3126   2637    -95    249   -310       C  
ATOM   2817  O   GLY A 380       3.656  53.550  38.454  1.00 21.46           O  
ANISOU 2817  O   GLY A 380     2419   3104   2627   -104    254   -317       O  
ATOM   2818  N   ASN A 381       2.948  53.371  40.602  1.00 21.77           N  
ANISOU 2818  N   ASN A 381     2431   3193   2644    -68    232   -307       N  
ATOM   2819  CA  ASN A 381       4.020  52.476  41.027  1.00 21.94           C  
ANISOU 2819  CA  ASN A 381     2419   3265   2651    -47    220   -319       C  
ATOM   2820  C   ASN A 381       3.753  51.000  40.736  1.00 21.65           C  
ANISOU 2820  C   ASN A 381     2389   3221   2614    -13    203   -277       C  
ATOM   2821  O   ASN A 381       2.747  50.447  41.189  1.00 19.92           O  
ANISOU 2821  O   ASN A 381     2182   2991   2394     10    192   -240       O  
ATOM   2822  CB  ASN A 381       4.306  52.691  42.519  1.00 22.41           C  
ANISOU 2822  CB  ASN A 381     2444   3379   2688    -31    212   -341       C  
ATOM   2823  CG  ASN A 381       5.493  51.895  42.995  1.00 28.73           C  
ANISOU 2823  CG  ASN A 381     3207   4238   3469     -7    201   -359       C  
ATOM   2824  OD1 ASN A 381       6.606  52.089  42.503  1.00 31.71           O  
ANISOU 2824  OD1 ASN A 381     3567   4633   3846    -26    209   -394       O  
ATOM   2825  ND2 ASN A 381       5.263  50.970  43.927  1.00 29.92           N  
ANISOU 2825  ND2 ASN A 381     3345   4419   3603     35    182   -334       N  
ATOM   2826  N   ASN A 382       4.646  50.383  39.965  1.00 20.25           N  
ANISOU 2826  N   ASN A 382     2206   3049   2439    -13    203   -283       N  
ATOM   2827  CA  ASN A 382       4.590  48.957  39.669  1.00 21.85           C  
ANISOU 2827  CA  ASN A 382     2413   3247   2640     17    190   -249       C  
ATOM   2828  C   ASN A 382       3.206  48.504  39.161  1.00 21.31           C  
ANISOU 2828  C   ASN A 382     2381   3127   2588     23    187   -203       C  
ATOM   2829  O   ASN A 382       2.638  47.529  39.659  1.00 20.27           O  
ANISOU 2829  O   ASN A 382     2252   2997   2451     53    175   -170       O  
ATOM   2830  CB  ASN A 382       5.062  48.177  40.905  1.00 22.63           C  
ANISOU 2830  CB  ASN A 382     2482   3402   2715     57    175   -248       C  
ATOM   2831  CG  ASN A 382       5.226  46.696  40.649  1.00 28.14           C  
ANISOU 2831  CG  ASN A 382     3183   4099   3408     91    165   -217       C  
ATOM   2832  OD1 ASN A 382       5.579  46.264  39.548  1.00 33.01           O  
ANISOU 2832  OD1 ASN A 382     3811   4693   4036     83    168   -213       O  
ATOM   2833  ND2 ASN A 382       4.966  45.899  41.680  1.00 29.40           N  
ANISOU 2833  ND2 ASN A 382     3335   4283   3550    131    154   -194       N  
ATOM   2834  N   PRO A 383       2.656  49.193  38.140  1.00 20.04           N  
ANISOU 2834  N   PRO A 383     2247   2920   2446     -5    198   -200       N  
ATOM   2835  CA  PRO A 383       1.299  48.834  37.701  1.00 17.79           C  
ANISOU 2835  CA  PRO A 383     1993   2592   2174      0    195   -161       C  
ATOM   2836  C   PRO A 383       1.246  47.469  36.989  1.00 17.59           C  
ANISOU 2836  C   PRO A 383     1976   2550   2155     17    187   -133       C  
ATOM   2837  O   PRO A 383       2.298  46.916  36.640  1.00 16.69           O  
ANISOU 2837  O   PRO A 383     1850   2453   2037     22    186   -144       O  
ATOM   2838  CB  PRO A 383       0.938  49.989  36.759  1.00 18.02           C  
ANISOU 2838  CB  PRO A 383     2046   2583   2216    -32    210   -172       C  
ATOM   2839  CG  PRO A 383       2.258  50.397  36.165  1.00 17.93           C  
ANISOU 2839  CG  PRO A 383     2023   2582   2205    -53    222   -207       C  
ATOM   2840  CD  PRO A 383       3.222  50.292  37.331  1.00 19.81           C  
ANISOU 2840  CD  PRO A 383     2224   2876   2425    -42    216   -233       C  
ATOM   2841  N   PRO A 384       0.045  46.890  36.812  1.00 16.41           N  
ANISOU 2841  N   PRO A 384     1848   2371   2014     28    182    -97       N  
ATOM   2842  CA  PRO A 384      -0.017  45.607  36.108  1.00 17.22           C  
ANISOU 2842  CA  PRO A 384     1960   2456   2124     41    177    -73       C  
ATOM   2843  C   PRO A 384       0.520  45.714  34.679  1.00 18.66           C  
ANISOU 2843  C   PRO A 384     2154   2616   2319     21    184    -84       C  
ATOM   2844  O   PRO A 384       0.267  46.709  33.992  1.00 19.08           O  
ANISOU 2844  O   PRO A 384     2221   2646   2380     -2    193    -96       O  
ATOM   2845  CB  PRO A 384      -1.518  45.284  36.082  1.00 16.77           C  
ANISOU 2845  CB  PRO A 384     1924   2369   2077     46    174    -41       C  
ATOM   2846  CG  PRO A 384      -2.079  46.087  37.232  1.00 14.88           C  
ANISOU 2846  CG  PRO A 384     1678   2146   1829     48    173    -45       C  
ATOM   2847  CD  PRO A 384      -1.301  47.367  37.191  1.00 15.76           C  
ANISOU 2847  CD  PRO A 384     1780   2270   1936     26    181    -80       C  
ATOM   2848  N   GLN A 385       1.255  44.692  34.248  1.00 17.68           N  
ANISOU 2848  N   GLN A 385     2025   2497   2194     34    180    -81       N  
ATOM   2849  CA  GLN A 385       1.856  44.683  32.926  1.00 18.77           C  
ANISOU 2849  CA  GLN A 385     2172   2618   2342     17    186    -91       C  
ATOM   2850  C   GLN A 385       1.263  43.626  31.998  1.00 16.79           C  
ANISOU 2850  C   GLN A 385     1940   2333   2104     25    183    -64       C  
ATOM   2851  O   GLN A 385       1.518  43.650  30.795  1.00 16.44           O  
ANISOU 2851  O   GLN A 385     1907   2267   2069     10    188    -69       O  
ATOM   2852  CB  GLN A 385       3.370  44.516  33.061  1.00 20.32           C  
ANISOU 2852  CB  GLN A 385     2343   2851   2527     22    187   -117       C  
ATOM   2853  CG  GLN A 385       3.958  45.711  33.790  1.00 25.81           C  
ANISOU 2853  CG  GLN A 385     3018   3576   3211      7    193   -152       C  
ATOM   2854  CD  GLN A 385       5.418  45.888  33.498  1.00 35.20           C  
ANISOU 2854  CD  GLN A 385     4185   4794   4393     -1    199   -186       C  
ATOM   2855  OE1 GLN A 385       5.815  45.985  32.335  1.00 35.32           O  
ANISOU 2855  OE1 GLN A 385     4210   4788   4418    -19    207   -194       O  
ATOM   2856  NE2 GLN A 385       6.234  45.925  34.550  1.00 35.94           N  
ANISOU 2856  NE2 GLN A 385     4247   4938   4468     11    195   -208       N  
ATOM   2857  N   ARG A 386       0.471  42.711  32.553  1.00 15.37           N  
ANISOU 2857  N   ARG A 386     1766   2149   1925     45    177    -36       N  
ATOM   2858  CA  ARG A 386      -0.130  41.640  31.766  1.00 14.18           C  
ANISOU 2858  CA  ARG A 386     1632   1967   1786     51    175    -12       C  
ATOM   2859  C   ARG A 386      -1.654  41.575  31.922  1.00 14.76           C  
ANISOU 2859  C   ARG A 386     1721   2017   1869     50    174     10       C  
ATOM   2860  O   ARG A 386      -2.199  40.533  32.309  1.00 13.23           O  
ANISOU 2860  O   ARG A 386     1531   1816   1676     66    173     32       O  
ATOM   2861  CB  ARG A 386       0.487  40.281  32.130  1.00 15.44           C  
ANISOU 2861  CB  ARG A 386     1785   2140   1939     79    172      0       C  
ATOM   2862  CG  ARG A 386       1.985  40.143  31.861  1.00 15.85           C  
ANISOU 2862  CG  ARG A 386     1822   2217   1982     84    172    -20       C  
ATOM   2863  CD  ARG A 386       2.260  39.920  30.369  1.00 16.98           C  
ANISOU 2863  CD  ARG A 386     1978   2334   2139     69    176    -24       C  
ATOM   2864  NE  ARG A 386       2.040  38.527  30.000  1.00 15.84           N  
ANISOU 2864  NE  ARG A 386     1845   2170   2000     86    175     -1       N  
ATOM   2865  CZ  ARG A 386       2.009  38.037  28.766  1.00 20.79           C  
ANISOU 2865  CZ  ARG A 386     2487   2771   2641     77    177      1       C  
ATOM   2866  NH1 ARG A 386       2.126  38.837  27.714  1.00 19.94           N  
ANISOU 2866  NH1 ARG A 386     2385   2650   2541     52    180    -14       N  
ATOM   2867  NH2 ARG A 386       1.879  36.725  28.584  1.00 17.68           N  
ANISOU 2867  NH2 ARG A 386     2104   2362   2252     94    178     21       N  
ATOM   2868  N   PRO A 387      -2.360  42.672  31.597  1.00 13.41           N  
ANISOU 2868  N   PRO A 387     1559   1832   1702     30    177      3       N  
ATOM   2869  CA  PRO A 387      -3.825  42.604  31.688  1.00 14.49           C  
ANISOU 2869  CA  PRO A 387     1708   1950   1846     30    175     22       C  
ATOM   2870  C   PRO A 387      -4.398  41.580  30.709  1.00 13.61           C  
ANISOU 2870  C   PRO A 387     1611   1812   1748     30    174     38       C  
ATOM   2871  O   PRO A 387      -3.816  41.346  29.640  1.00 14.13           O  
ANISOU 2871  O   PRO A 387     1682   1866   1819     23    176     30       O  
ATOM   2872  CB  PRO A 387      -4.273  44.006  31.245  1.00 13.64           C  
ANISOU 2872  CB  PRO A 387     1610   1832   1739     11    179      9       C  
ATOM   2873  CG  PRO A 387      -3.148  44.515  30.413  1.00 12.58           C  
ANISOU 2873  CG  PRO A 387     1476   1697   1605     -1    185    -12       C  
ATOM   2874  CD  PRO A 387      -1.905  43.960  31.053  1.00 12.25           C  
ANISOU 2874  CD  PRO A 387     1415   1685   1555      9    183    -20       C  
ATOM   2875  N   HIS A 388      -5.557  41.033  31.065  1.00 13.28           N  
ANISOU 2875  N   HIS A 388     1573   1759   1710     35    173     56       N  
ATOM   2876  CA  HIS A 388      -6.208  40.005  30.279  1.00 13.69           C  
ANISOU 2876  CA  HIS A 388     1636   1787   1776     33    175     69       C  
ATOM   2877  C   HIS A 388      -6.959  40.651  29.118  1.00 13.87           C  
ANISOU 2877  C   HIS A 388     1671   1792   1806     17    174     62       C  
ATOM   2878  O   HIS A 388      -8.180  40.825  29.180  1.00 13.94           O  
ANISOU 2878  O   HIS A 388     1683   1794   1817     13    172     68       O  
ATOM   2879  CB  HIS A 388      -7.113  39.187  31.206  1.00 13.59           C  
ANISOU 2879  CB  HIS A 388     1623   1773   1765     44    177     89       C  
ATOM   2880  CG  HIS A 388      -7.681  37.957  30.570  1.00 15.61           C  
ANISOU 2880  CG  HIS A 388     1888   2006   2034     42    182    101       C  
ATOM   2881  ND1 HIS A 388      -8.905  37.950  29.935  1.00 19.98           N  
ANISOU 2881  ND1 HIS A 388     2449   2543   2599     28    182    102       N  
ATOM   2882  CD2 HIS A 388      -7.215  36.687  30.507  1.00 17.93           C  
ANISOU 2882  CD2 HIS A 388     2187   2290   2333     52    188    111       C  
ATOM   2883  CE1 HIS A 388      -9.162  36.729  29.496  1.00 17.97           C  
ANISOU 2883  CE1 HIS A 388     2200   2270   2355     27    189    109       C  
ATOM   2884  NE2 HIS A 388      -8.145  35.947  29.815  1.00 17.16           N  
ANISOU 2884  NE2 HIS A 388     2099   2170   2250     41    194    116       N  
ATOM   2885  N   HIS A 389      -6.208  41.050  28.089  1.00 11.93           N  
ANISOU 2885  N   HIS A 389     1430   1541   1561      9    175     48       N  
ATOM   2886  CA  HIS A 389      -6.730  41.903  27.019  1.00 11.87           C  
ANISOU 2886  CA  HIS A 389     1435   1520   1556     -2    175     39       C  
ATOM   2887  C   HIS A 389      -6.013  41.495  25.733  1.00 12.08           C  
ANISOU 2887  C   HIS A 389     1467   1533   1587     -7    177     32       C  
ATOM   2888  O   HIS A 389      -4.793  41.612  25.644  1.00 12.42           O  
ANISOU 2888  O   HIS A 389     1506   1584   1627     -8    180     21       O  
ATOM   2889  CB  HIS A 389      -6.454  43.382  27.340  1.00 11.66           C  
ANISOU 2889  CB  HIS A 389     1408   1502   1518     -8    179     26       C  
ATOM   2890  CG  HIS A 389      -7.174  44.349  26.444  1.00 12.42           C  
ANISOU 2890  CG  HIS A 389     1521   1584   1614    -15    181     21       C  
ATOM   2891  ND1 HIS A 389      -6.728  44.676  25.176  1.00  8.99           N  
ANISOU 2891  ND1 HIS A 389     1099   1136   1180    -21    186     11       N  
ATOM   2892  CD2 HIS A 389      -8.304  45.070  26.641  1.00 10.20           C  
ANISOU 2892  CD2 HIS A 389     1246   1301   1327    -13    180     25       C  
ATOM   2893  CE1 HIS A 389      -7.561  45.545  24.629  1.00 10.20           C  
ANISOU 2893  CE1 HIS A 389     1267   1280   1329    -22    189     10       C  
ATOM   2894  NE2 HIS A 389      -8.522  45.810  25.499  1.00 12.42           N  
ANISOU 2894  NE2 HIS A 389     1543   1568   1605    -16    185     18       N  
ATOM   2895  N   ARG A 390      -6.757  40.908  24.800  1.00 11.83           N  
ANISOU 2895  N   ARG A 390     1443   1486   1565     -9    175     36       N  
ATOM   2896  CA  ARG A 390      -6.179  40.369  23.567  1.00 11.52           C  
ANISOU 2896  CA  ARG A 390     1410   1434   1532    -13    176     30       C  
ATOM   2897  C   ARG A 390      -5.450  41.391  22.706  1.00 12.50           C  
ANISOU 2897  C   ARG A 390     1542   1555   1650    -20    180     15       C  
ATOM   2898  O   ARG A 390      -4.324  41.156  22.260  1.00 13.05           O  
ANISOU 2898  O   ARG A 390     1612   1626   1721    -21    183      8       O  
ATOM   2899  CB  ARG A 390      -7.278  39.711  22.731  1.00 10.60           C  
ANISOU 2899  CB  ARG A 390     1299   1303   1423    -15    173     34       C  
ATOM   2900  CG  ARG A 390      -7.850  38.460  23.402  1.00 12.66           C  
ANISOU 2900  CG  ARG A 390     1554   1562   1693    -11    173     47       C  
ATOM   2901  CD  ARG A 390      -9.251  38.103  22.912  1.00 14.38           C  
ANISOU 2901  CD  ARG A 390     1774   1772   1918    -17    171     48       C  
ATOM   2902  NE  ARG A 390      -9.781  36.877  23.513  1.00 15.17           N  
ANISOU 2902  NE  ARG A 390     1869   1866   2028    -17    176     59       N  
ATOM   2903  CZ  ARG A 390     -10.173  36.769  24.783  1.00 16.52           C  
ANISOU 2903  CZ  ARG A 390     2034   2044   2197    -13    179     70       C  
ATOM   2904  NH1 ARG A 390     -10.064  37.799  25.610  1.00 14.86           N  
ANISOU 2904  NH1 ARG A 390     1821   1849   1976     -8    176     72       N  
ATOM   2905  NH2 ARG A 390     -10.672  35.629  25.240  1.00 14.97           N  
ANISOU 2905  NH2 ARG A 390     1838   1839   2011    -14    187     80       N  
ATOM   2906  N   THR A 391      -6.083  42.529  22.447  1.00 12.59           N  
ANISOU 2906  N   THR A 391     1563   1563   1654    -23    182     11       N  
ATOM   2907  CA  THR A 391      -5.475  43.444  21.485  1.00 12.50           C  
ANISOU 2907  CA  THR A 391     1565   1544   1638    -29    190      0       C  
ATOM   2908  C   THR A 391      -4.266  44.161  22.077  1.00 13.15           C  
ANISOU 2908  C   THR A 391     1642   1637   1715    -36    199    -12       C  
ATOM   2909  O   THR A 391      -3.314  44.446  21.345  1.00 13.62           O  
ANISOU 2909  O   THR A 391     1708   1692   1774    -43    207    -24       O  
ATOM   2910  CB  THR A 391      -6.520  44.374  20.830  1.00 12.71           C  
ANISOU 2910  CB  THR A 391     1608   1561   1657    -27    193      0       C  
ATOM   2911  OG1 THR A 391      -7.487  43.551  20.177  1.00 13.38           O  
ANISOU 2911  OG1 THR A 391     1694   1642   1748    -21    184      6       O  
ATOM   2912  CG2 THR A 391      -5.904  45.276  19.752  1.00 12.18           C  
ANISOU 2912  CG2 THR A 391     1560   1483   1585    -31    204    -11       C  
ATOM   2913  N   ALA A 392      -4.259  44.401  23.390  1.00 11.64           N  
ANISOU 2913  N   ALA A 392     1440   1462   1520    -35    198    -11       N  
ATOM   2914  CA  ALA A 392      -3.083  45.010  24.022  1.00 12.02           C  
ANISOU 2914  CA  ALA A 392     1478   1525   1562    -42    205    -27       C  
ATOM   2915  C   ALA A 392      -1.909  44.043  24.050  1.00 12.98           C  
ANISOU 2915  C   ALA A 392     1585   1659   1687    -39    203    -32       C  
ATOM   2916  O   ALA A 392      -0.745  44.459  24.030  1.00 13.64           O  
ANISOU 2916  O   ALA A 392     1662   1753   1767    -47    211    -50       O  
ATOM   2917  CB  ALA A 392      -3.388  45.506  25.459  1.00 12.97           C  
ANISOU 2917  CB  ALA A 392     1588   1663   1676    -39    204    -26       C  
ATOM   2918  N   HIS A 393      -2.211  42.751  24.160  1.00 14.34           N  
ANISOU 2918  N   HIS A 393     1752   1830   1864    -27    193    -16       N  
ATOM   2919  CA  HIS A 393      -1.179  41.719  24.210  1.00 14.84           C  
ANISOU 2919  CA  HIS A 393     1804   1904   1929    -19    191    -17       C  
ATOM   2920  C   HIS A 393      -0.434  41.651  22.868  1.00 16.12           C  
ANISOU 2920  C   HIS A 393     1973   2055   2095    -27    196    -28       C  
ATOM   2921  O   HIS A 393       0.802  41.699  22.815  1.00 16.25           O  
ANISOU 2921  O   HIS A 393     1980   2085   2107    -29    200    -43       O  
ATOM   2922  CB  HIS A 393      -1.821  40.360  24.539  1.00 15.14           C  
ANISOU 2922  CB  HIS A 393     1840   1937   1973     -4    184      2       C  
ATOM   2923  CG  HIS A 393      -0.851  39.214  24.534  1.00 15.96           C  
ANISOU 2923  CG  HIS A 393     1937   2048   2077      7    183      4       C  
ATOM   2924  ND1 HIS A 393      -1.215  37.933  24.179  1.00 17.33           N  
ANISOU 2924  ND1 HIS A 393     2117   2206   2260     15    182     19       N  
ATOM   2925  CD2 HIS A 393       0.475  39.164  24.809  1.00 16.18           C  
ANISOU 2925  CD2 HIS A 393     1951   2098   2097     13    184     -7       C  
ATOM   2926  CE1 HIS A 393      -0.166  37.134  24.276  1.00 19.06           C  
ANISOU 2926  CE1 HIS A 393     2330   2436   2476     28    182     18       C  
ATOM   2927  NE2 HIS A 393       0.876  37.857  24.651  1.00 17.72           N  
ANISOU 2927  NE2 HIS A 393     2147   2291   2295     28    183      1       N  
ATOM   2928  N   GLY A 394      -1.201  41.561  21.787  1.00 16.26           N  
ANISOU 2928  N   GLY A 394     2007   2050   2119    -30    195    -22       N  
ATOM   2929  CA  GLY A 394      -0.649  41.573  20.429  1.00 17.20           C  
ANISOU 2929  CA  GLY A 394     2136   2157   2241    -37    200    -31       C  
ATOM   2930  C   GLY A 394       0.015  40.268  20.005  1.00 18.31           C  
ANISOU 2930  C   GLY A 394     2271   2297   2387    -29    196    -28       C  
ATOM   2931  O   GLY A 394       1.174  40.256  19.615  1.00 18.86           O  
ANISOU 2931  O   GLY A 394     2336   2373   2455    -32    201    -41       O  
ATOM   2932  N   THR A 395      -0.699  39.154  20.081  1.00 18.39           N  
ANISOU 2932  N   THR A 395     2282   2299   2405    -20    189    -13       N  
ATOM   2933  CA  THR A 395      -0.116  37.888  19.655  1.00 18.41           C  
ANISOU 2933  CA  THR A 395     2282   2297   2413    -11    187    -10       C  
ATOM   2934  C   THR A 395      -0.329  37.718  18.148  1.00 17.49           C  
ANISOU 2934  C   THR A 395     2179   2161   2302    -18    188    -14       C  
ATOM   2935  O   THR A 395      -1.065  38.491  17.513  1.00 16.75           O  
ANISOU 2935  O   THR A 395     2096   2058   2208    -25    189    -17       O  
ATOM   2936  CB  THR A 395      -0.731  36.711  20.436  1.00 18.66           C  
ANISOU 2936  CB  THR A 395     2311   2326   2450      0    184      6       C  
ATOM   2937  OG1 THR A 395       0.026  35.514  20.191  1.00 21.39           O  
ANISOU 2937  OG1 THR A 395     2657   2670   2799     11    185      9       O  
ATOM   2938  CG2 THR A 395      -2.149  36.480  19.971  1.00 18.25           C  
ANISOU 2938  CG2 THR A 395     2270   2256   2407     -5    182     14       C  
ATOM   2939  N   TRP A 396       0.342  36.718  17.583  1.00 16.99           N  
ANISOU 2939  N   TRP A 396     2116   2095   2245    -12    188    -15       N  
ATOM   2940  CA  TRP A 396       0.160  36.324  16.191  1.00 17.06           C  
ANISOU 2940  CA  TRP A 396     2135   2086   2260    -16    187    -18       C  
ATOM   2941  C   TRP A 396      -0.290  34.874  16.029  1.00 20.15           C  
ANISOU 2941  C   TRP A 396     2529   2465   2662     -9    185     -9       C  
ATOM   2942  O   TRP A 396      -0.600  34.416  14.920  1.00 19.43           O  
ANISOU 2942  O   TRP A 396     2445   2359   2576    -12    184    -12       O  
ATOM   2943  CB  TRP A 396       1.458  36.549  15.396  1.00 17.66           C  
ANISOU 2943  CB  TRP A 396     2211   2167   2332    -19    192    -32       C  
ATOM   2944  CG  TRP A 396       2.703  35.915  16.013  1.00 15.18           C  
ANISOU 2944  CG  TRP A 396     1884   1870   2014     -9    193    -34       C  
ATOM   2945  CD1 TRP A 396       3.247  34.704  15.688  1.00 16.27           C  
ANISOU 2945  CD1 TRP A 396     2021   2004   2156      1    191    -31       C  
ATOM   2946  CD2 TRP A 396       3.538  36.463  17.041  1.00 19.60           C  
ANISOU 2946  CD2 TRP A 396     2428   2453   2563     -7    195    -41       C  
ATOM   2947  NE1 TRP A 396       4.373  34.467  16.440  1.00 17.33           N  
ANISOU 2947  NE1 TRP A 396     2141   2160   2281     13    192    -35       N  
ATOM   2948  CE2 TRP A 396       4.578  35.532  17.276  1.00 19.04           C  
ANISOU 2948  CE2 TRP A 396     2347   2396   2489      7    194    -42       C  
ATOM   2949  CE3 TRP A 396       3.516  37.657  17.781  1.00 16.70           C  
ANISOU 2949  CE3 TRP A 396     2055   2099   2189    -15    198    -48       C  
ATOM   2950  CZ2 TRP A 396       5.575  35.743  18.234  1.00 20.78           C  
ANISOU 2950  CZ2 TRP A 396     2550   2647   2698     15    195    -51       C  
ATOM   2951  CZ3 TRP A 396       4.523  37.877  18.710  1.00 20.43           C  
ANISOU 2951  CZ3 TRP A 396     2510   2600   2652    -11    200    -58       C  
ATOM   2952  CH2 TRP A 396       5.534  36.918  18.940  1.00 21.48           C  
ANISOU 2952  CH2 TRP A 396     2631   2750   2780      4    197    -60       C  
ATOM   2953  N   LEU A 397      -0.340  34.138  17.130  1.00 20.06           N  
ANISOU 2953  N   LEU A 397     2512   2458   2652      0    185      2       N  
ATOM   2954  CA  LEU A 397      -0.633  32.717  16.985  1.00 22.83           C  
ANISOU 2954  CA  LEU A 397     2868   2792   3013      6    187     10       C  
ATOM   2955  C   LEU A 397      -1.621  32.126  17.991  1.00 22.22           C  
ANISOU 2955  C   LEU A 397     2791   2709   2941      9    190     25       C  
ATOM   2956  O   LEU A 397      -1.519  30.951  18.335  1.00 22.16           O  
ANISOU 2956  O   LEU A 397     2788   2692   2939     19    197     35       O  
ATOM   2957  CB  LEU A 397       0.673  31.913  16.896  1.00 25.94           C  
ANISOU 2957  CB  LEU A 397     3259   3189   3404     19    190     10       C  
ATOM   2958  CG  LEU A 397       1.855  32.288  17.790  1.00 27.69           C  
ANISOU 2958  CG  LEU A 397     3470   3438   3613     31    190      8       C  
ATOM   2959  CD1 LEU A 397       1.419  32.253  19.234  1.00 28.78           C  
ANISOU 2959  CD1 LEU A 397     3603   3585   3746     41    191     21       C  
ATOM   2960  CD2 LEU A 397       3.013  31.324  17.571  1.00 30.92           C  
ANISOU 2960  CD2 LEU A 397     3877   3850   4018     47    193      7       C  
ATOM   2961  N   ASP A 398      -2.597  32.925  18.420  1.00 20.35           N  
ANISOU 2961  N   ASP A 398     2552   2477   2703      1    187     26       N  
ATOM   2962  CA  ASP A 398      -3.708  32.434  19.228  1.00 19.49           C  
ANISOU 2962  CA  ASP A 398     2443   2361   2600      0    191     38       C  
ATOM   2963  C   ASP A 398      -3.223  31.755  20.515  1.00 20.28           C  
ANISOU 2963  C   ASP A 398     2542   2467   2697     17    197     53       C  
ATOM   2964  O   ASP A 398      -3.712  30.702  20.904  1.00 18.42           O  
ANISOU 2964  O   ASP A 398     2312   2216   2469     21    206     64       O  
ATOM   2965  CB  ASP A 398      -4.620  31.550  18.360  1.00 20.08           C  
ANISOU 2965  CB  ASP A 398     2524   2415   2688     -9    194     35       C  
ATOM   2966  CG  ASP A 398      -5.941  31.182  19.029  1.00 22.62           C  
ANISOU 2966  CG  ASP A 398     2845   2730   3017    -15    199     42       C  
ATOM   2967  OD1 ASP A 398      -6.436  31.895  19.933  1.00 23.44           O  
ANISOU 2967  OD1 ASP A 398     2943   2846   3115    -14    197     48       O  
ATOM   2968  OD2 ASP A 398      -6.503  30.139  18.636  1.00 22.38           O  
ANISOU 2968  OD2 ASP A 398     2820   2683   3000    -22    207     40       O  
ATOM   2969  N   LYS A 399      -2.247  32.367  21.179  1.00 20.25           N  
ANISOU 2969  N   LYS A 399     2529   2484   2679     28    194     52       N  
ATOM   2970  CA  LYS A 399      -1.773  31.909  22.482  1.00 22.89           C  
ANISOU 2970  CA  LYS A 399     2860   2831   3005     47    199     65       C  
ATOM   2971  C   LYS A 399      -1.662  33.099  23.433  1.00 23.42           C  
ANISOU 2971  C   LYS A 399     2914   2923   3060     49    193     62       C  
ATOM   2972  O   LYS A 399      -1.384  34.217  22.999  1.00 20.70           O  
ANISOU 2972  O   LYS A 399     2565   2589   2711     37    188     47       O  
ATOM   2973  CB  LYS A 399      -0.384  31.281  22.363  1.00 23.88           C  
ANISOU 2973  CB  LYS A 399     2984   2964   3124     65    200     63       C  
ATOM   2974  CG  LYS A 399      -0.350  29.913  21.691  1.00 29.58           C  
ANISOU 2974  CG  LYS A 399     3720   3661   3856     70    209     69       C  
ATOM   2975  CD  LYS A 399       1.105  29.508  21.471  1.00 36.33           C  
ANISOU 2975  CD  LYS A 399     4572   4529   4702     89    209     65       C  
ATOM   2976  CE  LYS A 399       1.251  28.003  21.355  1.00 40.93           C  
ANISOU 2976  CE  LYS A 399     5170   5090   5290    105    220     77       C  
ATOM   2977  NZ  LYS A 399       1.022  27.392  22.693  1.00 45.25           N  
ANISOU 2977  NZ  LYS A 399     5722   5639   5831    126    230     98       N  
ATOM   2978  N   ARG A 400      -1.840  32.834  24.725  1.00 22.03           N  
ANISOU 2978  N   ARG A 400     2735   2757   2877     63    196     76       N  
ATOM   2979  CA  ARG A 400      -1.665  33.856  25.752  1.00 23.61           C  
ANISOU 2979  CA  ARG A 400     2922   2983   3064     67    191     72       C  
ATOM   2980  C   ARG A 400      -0.224  33.979  26.228  1.00 23.55           C  
ANISOU 2980  C   ARG A 400     2901   3004   3040     84    189     64       C  
ATOM   2981  O   ARG A 400       0.197  35.047  26.676  1.00 24.49           O  
ANISOU 2981  O   ARG A 400     3007   3148   3149     80    185     51       O  
ATOM   2982  CB  ARG A 400      -2.596  33.578  26.939  1.00 23.55           C  
ANISOU 2982  CB  ARG A 400     2916   2975   3055     75    196     90       C  
ATOM   2983  CG  ARG A 400      -4.068  33.732  26.577  1.00 24.57           C  
ANISOU 2983  CG  ARG A 400     3053   3084   3198     56    197     93       C  
ATOM   2984  CD  ARG A 400      -5.022  33.400  27.717  1.00 29.67           C  
ANISOU 2984  CD  ARG A 400     3700   3729   3843     62    203    110       C  
ATOM   2985  NE  ARG A 400      -4.789  32.061  28.245  1.00 33.06           N  
ANISOU 2985  NE  ARG A 400     4138   4149   4273     81    215    127       N  
ATOM   2986  CZ  ARG A 400      -5.322  30.942  27.765  1.00 36.09           C  
ANISOU 2986  CZ  ARG A 400     4536   4505   4672     76    227    135       C  
ATOM   2987  NH1 ARG A 400      -6.156  30.967  26.734  1.00 39.68           N  
ANISOU 2987  NH1 ARG A 400     4993   4940   5140     52    226    125       N  
ATOM   2988  NH2 ARG A 400      -5.013  29.785  28.330  1.00 37.88           N  
ANISOU 2988  NH2 ARG A 400     4773   4721   4896     96    241    151       N  
ATOM   2989  N   ASP A 401       0.538  32.895  26.126  1.00 23.90           N  
ANISOU 2989  N   ASP A 401     2949   3048   3082    103    193     70       N  
ATOM   2990  CA  ASP A 401       1.894  32.876  26.669  1.00 26.09           C  
ANISOU 2990  CA  ASP A 401     3212   3358   3342    125    191     62       C  
ATOM   2991  C   ASP A 401       2.932  33.495  25.739  1.00 26.05           C  
ANISOU 2991  C   ASP A 401     3197   3365   3335    113    187     38       C  
ATOM   2992  O   ASP A 401       4.029  33.830  26.182  1.00 25.90           O  
ANISOU 2992  O   ASP A 401     3160   3380   3300    124    184     24       O  
ATOM   2993  CB  ASP A 401       2.313  31.471  27.136  1.00 26.50           C  
ANISOU 2993  CB  ASP A 401     3272   3409   3387    157    198     80       C  
ATOM   2994  CG  ASP A 401       2.313  30.433  26.016  1.00 32.03           C  
ANISOU 2994  CG  ASP A 401     3989   4077   4101    155    205     85       C  
ATOM   2995  OD1 ASP A 401       1.648  30.619  24.977  1.00 37.06           O  
ANISOU 2995  OD1 ASP A 401     4634   4689   4755    129    204     80       O  
ATOM   2996  OD2 ASP A 401       2.980  29.387  26.168  1.00 42.58           O  
ANISOU 2996  OD2 ASP A 401     5332   5415   5430    182    211     95       O  
ATOM   2997  N   ILE A 402       2.575  33.685  24.472  1.00 24.83           N  
ANISOU 2997  N   ILE A 402     3052   3185   3194     90    187     32       N  
ATOM   2998  CA  ILE A 402       3.476  34.274  23.491  1.00 24.01           C  
ANISOU 2998  CA  ILE A 402     2943   3088   3089     77    185     10       C  
ATOM   2999  C   ILE A 402       2.802  35.403  22.711  1.00 22.44           C  
ANISOU 2999  C   ILE A 402     2751   2875   2900     48    185      0       C  
ATOM   3000  O   ILE A 402       1.715  35.196  22.173  1.00 22.72           O  
ANISOU 3000  O   ILE A 402     2801   2883   2947     39    185     10       O  
ATOM   3001  CB  ILE A 402       3.999  33.199  22.506  1.00 24.96           C  
ANISOU 3001  CB  ILE A 402     3072   3193   3216     84    188     12       C  
ATOM   3002  CG1 ILE A 402       4.755  32.107  23.274  1.00 29.01           C  
ANISOU 3002  CG1 ILE A 402     3581   3723   3717    117    190     22       C  
ATOM   3003  CG2 ILE A 402       4.883  33.830  21.429  1.00 24.80           C  
ANISOU 3003  CG2 ILE A 402     3047   3179   3195     69    187     -9       C  
ATOM   3004  CD1 ILE A 402       5.042  30.850  22.468  1.00 36.10           C  
ANISOU 3004  CD1 ILE A 402     4493   4600   4622    129    194     30       C  
ATOM   3005  N   PRO A 403       3.423  36.597  22.655  1.00 21.40           N  
ANISOU 3005  N   PRO A 403     2609   2760   2761     35    186    -19       N  
ATOM   3006  CA  PRO A 403       4.679  36.992  23.300  1.00 22.17           C  
ANISOU 3006  CA  PRO A 403     2685   2892   2843     41    187    -37       C  
ATOM   3007  C   PRO A 403       4.536  37.016  24.822  1.00 22.37           C  
ANISOU 3007  C   PRO A 403     2698   2942   2857     57    184    -30       C  
ATOM   3008  O   PRO A 403       3.426  37.186  25.337  1.00 19.93           O  
ANISOU 3008  O   PRO A 403     2396   2621   2552     55    182    -16       O  
ATOM   3009  CB  PRO A 403       4.930  38.410  22.759  1.00 20.93           C  
ANISOU 3009  CB  PRO A 403     2527   2736   2686     14    193    -59       C  
ATOM   3010  CG  PRO A 403       3.570  38.926  22.452  1.00 21.73           C  
ANISOU 3010  CG  PRO A 403     2647   2810   2798      1    193    -48       C  
ATOM   3011  CD  PRO A 403       2.836  37.723  21.906  1.00 21.85           C  
ANISOU 3011  CD  PRO A 403     2676   2801   2824     11    189    -28       C  
ATOM   3012  N   GLU A 404       5.650  36.835  25.526  1.00 22.19           N  
ANISOU 3012  N   GLU A 404     2656   2956   2819     75    182    -41       N  
ATOM   3013  CA  GLU A 404       5.640  36.817  26.992  1.00 23.19           C  
ANISOU 3013  CA  GLU A 404     2768   3111   2931     95    179    -37       C  
ATOM   3014  C   GLU A 404       5.470  38.196  27.619  1.00 22.33           C  
ANISOU 3014  C   GLU A 404     2647   3017   2817     77    179    -54       C  
ATOM   3015  O   GLU A 404       5.159  38.315  28.810  1.00 21.16           O  
ANISOU 3015  O   GLU A 404     2490   2888   2659     89    176    -48       O  
ATOM   3016  CB  GLU A 404       6.917  36.162  27.530  1.00 26.13           C  
ANISOU 3016  CB  GLU A 404     3120   3521   3284    124    176    -45       C  
ATOM   3017  CG  GLU A 404       8.184  36.904  27.134  1.00 32.53           C  
ANISOU 3017  CG  GLU A 404     3910   4361   4087    110    178    -79       C  
ATOM   3018  CD  GLU A 404       9.450  36.287  27.726  1.00 43.23           C  
ANISOU 3018  CD  GLU A 404     5241   5762   5420    142    174    -90       C  
ATOM   3019  OE1 GLU A 404       9.361  35.180  28.297  1.00 43.13           O  
ANISOU 3019  OE1 GLU A 404     5234   5753   5399    177    171    -67       O  
ATOM   3020  OE2 GLU A 404      10.535  36.903  27.607  1.00 46.11           O  
ANISOU 3020  OE2 GLU A 404     5582   6159   5775    132    175   -122       O  
ATOM   3021  N   LYS A 405       5.697  39.248  26.835  1.00 21.30           N  
ANISOU 3021  N   LYS A 405     2518   2880   2693     47    185    -75       N  
ATOM   3022  CA  LYS A 405       5.398  40.604  27.300  1.00 21.04           C  
ANISOU 3022  CA  LYS A 405     2481   2854   2658     27    190    -90       C  
ATOM   3023  C   LYS A 405       4.337  41.199  26.391  1.00 19.60           C  
ANISOU 3023  C   LYS A 405     2324   2631   2492      5    194    -82       C  
ATOM   3024  O   LYS A 405       4.384  40.982  25.182  1.00 18.69           O  
ANISOU 3024  O   LYS A 405     2221   2492   2385     -3    197    -81       O  
ATOM   3025  CB  LYS A 405       6.649  41.492  27.284  1.00 22.72           C  
ANISOU 3025  CB  LYS A 405     2672   3096   2862     11    197   -127       C  
ATOM   3026  CG  LYS A 405       7.684  41.086  28.348  1.00 31.77           C  
ANISOU 3026  CG  LYS A 405     3788   4292   3988     35    191   -140       C  
ATOM   3027  CD  LYS A 405       9.079  41.653  28.069  1.00 42.08           C  
ANISOU 3027  CD  LYS A 405     5072   5630   5287     20    198   -179       C  
ATOM   3028  CE  LYS A 405       9.516  42.680  29.109  1.00 49.01           C  
ANISOU 3028  CE  LYS A 405     5923   6545   6151     10    202   -209       C  
ATOM   3029  NZ  LYS A 405       8.850  44.003  28.914  1.00 51.51           N  
ANISOU 3029  NZ  LYS A 405     6255   6836   6479    -23    214   -218       N  
ATOM   3030  N   HIS A 406       3.404  41.969  26.936  1.00 18.42           N  
ANISOU 3030  N   HIS A 406     2180   2474   2343     -2    195    -77       N  
ATOM   3031  CA  HIS A 406       2.471  42.683  26.054  1.00 16.26           C  
ANISOU 3031  CA  HIS A 406     1929   2167   2080    -20    201    -73       C  
ATOM   3032  C   HIS A 406       3.222  43.607  25.112  1.00 16.98           C  
ANISOU 3032  C   HIS A 406     2026   2253   2173    -43    214    -97       C  
ATOM   3033  O   HIS A 406       4.171  44.268  25.517  1.00 15.97           O  
ANISOU 3033  O   HIS A 406     1882   2148   2037    -53    221   -122       O  
ATOM   3034  CB  HIS A 406       1.497  43.538  26.860  1.00 15.56           C  
ANISOU 3034  CB  HIS A 406     1844   2076   1989    -25    201    -69       C  
ATOM   3035  CG  HIS A 406       0.365  42.749  27.439  1.00 14.70           C  
ANISOU 3035  CG  HIS A 406     1740   1961   1883     -8    192    -42       C  
ATOM   3036  ND1 HIS A 406       0.514  41.441  27.850  1.00 17.13           N  
ANISOU 3036  ND1 HIS A 406     2041   2277   2190     12    185    -26       N  
ATOM   3037  CD2 HIS A 406      -0.923  43.086  27.692  1.00 13.21           C  
ANISOU 3037  CD2 HIS A 406     1562   1758   1698     -9    190    -28       C  
ATOM   3038  CE1 HIS A 406      -0.636  41.006  28.344  1.00 13.71           C  
ANISOU 3038  CE1 HIS A 406     1614   1833   1760     21    181     -5       C  
ATOM   3039  NE2 HIS A 406      -1.524  41.983  28.252  1.00 14.07           N  
ANISOU 3039  NE2 HIS A 406     1669   1867   1808      7    183     -6       N  
ATOM   3040  N   ARG A 407       2.732  43.708  23.885  1.00 15.79           N  
ANISOU 3040  N   ARG A 407     1897   2071   2031    -52    218    -90       N  
ATOM   3041  CA  ARG A 407       3.329  44.603  22.901  1.00 16.13           C  
ANISOU 3041  CA  ARG A 407     1950   2102   2075    -72    233   -110       C  
ATOM   3042  C   ARG A 407       2.837  46.040  23.094  1.00 15.47           C  
ANISOU 3042  C   ARG A 407     1878   2008   1988    -88    246   -118       C  
ATOM   3043  O   ARG A 407       3.487  46.988  22.656  1.00 13.94           O  
ANISOU 3043  O   ARG A 407     1690   1810   1793   -107    264   -139       O  
ATOM   3044  CB  ARG A 407       3.021  44.076  21.507  1.00 15.00           C  
ANISOU 3044  CB  ARG A 407     1825   1931   1940    -71    232    -98       C  
ATOM   3045  CG  ARG A 407       3.912  42.889  21.139  1.00 20.27           C  
ANISOU 3045  CG  ARG A 407     2482   2610   2610    -61    226    -99       C  
ATOM   3046  CD  ARG A 407       3.357  42.180  19.907  1.00 25.35           C  
ANISOU 3046  CD  ARG A 407     3143   3226   3262    -56    222    -84       C  
ATOM   3047  NE  ARG A 407       4.338  42.039  18.843  1.00 25.80           N  
ANISOU 3047  NE  ARG A 407     3202   3280   3320    -63    229    -96       N  
ATOM   3048  CZ  ARG A 407       4.062  41.589  17.623  1.00 24.58           C  
ANISOU 3048  CZ  ARG A 407     3062   3104   3172    -61    228    -89       C  
ATOM   3049  NH1 ARG A 407       2.839  41.187  17.287  1.00 21.87           N  
ANISOU 3049  NH1 ARG A 407     2732   2742   2834    -54    220    -71       N  
ATOM   3050  NH2 ARG A 407       5.038  41.520  16.737  1.00 27.91           N  
ANISOU 3050  NH2 ARG A 407     3484   3526   3593    -67    235   -102       N  
ATOM   3051  N   HIS A 408       1.702  46.201  23.768  1.00 12.25           N  
ANISOU 3051  N   HIS A 408     1477   1597   1581    -80    239   -103       N  
ATOM   3052  CA  HIS A 408       1.114  47.525  23.903  1.00 13.96           C  
ANISOU 3052  CA  HIS A 408     1708   1800   1794    -92    251   -108       C  
ATOM   3053  C   HIS A 408       0.746  47.860  25.343  1.00 14.08           C  
ANISOU 3053  C   HIS A 408     1710   1835   1803    -87    246   -108       C  
ATOM   3054  O   HIS A 408       0.482  46.971  26.158  1.00 14.87           O  
ANISOU 3054  O   HIS A 408     1794   1952   1902    -71    231    -95       O  
ATOM   3055  CB  HIS A 408      -0.126  47.659  23.016  1.00 12.57           C  
ANISOU 3055  CB  HIS A 408     1559   1595   1622    -86    250    -89       C  
ATOM   3056  CG  HIS A 408       0.077  47.140  21.626  1.00 12.62           C  
ANISOU 3056  CG  HIS A 408     1577   1583   1633    -85    251    -85       C  
ATOM   3057  ND1 HIS A 408       0.998  47.683  20.757  1.00 12.92           N  
ANISOU 3057  ND1 HIS A 408     1624   1612   1670   -100    268   -102       N  
ATOM   3058  CD2 HIS A 408      -0.506  46.111  20.966  1.00 12.50           C  
ANISOU 3058  CD2 HIS A 408     1566   1559   1624    -73    239    -68       C  
ATOM   3059  CE1 HIS A 408       0.977  47.009  19.620  1.00 13.09           C  
ANISOU 3059  CE1 HIS A 408     1655   1621   1696    -94    264    -94       C  
ATOM   3060  NE2 HIS A 408       0.080  46.045  19.724  1.00 14.17           N  
ANISOU 3060  NE2 HIS A 408     1788   1757   1837    -78    246    -75       N  
ATOM   3061  N   VAL A 409       0.684  49.162  25.614  1.00 13.77           N  
ANISOU 3061  N   VAL A 409     1679   1791   1760   -102    262   -123       N  
ATOM   3062  CA  VAL A 409       0.324  49.664  26.936  1.00 13.39           C  
ANISOU 3062  CA  VAL A 409     1621   1761   1706   -100    259   -126       C  
ATOM   3063  C   VAL A 409      -1.145  50.061  27.008  1.00 13.45           C  
ANISOU 3063  C   VAL A 409     1647   1749   1713    -91    256   -106       C  
ATOM   3064  O   VAL A 409      -1.566  51.046  26.387  1.00 13.30           O  
ANISOU 3064  O   VAL A 409     1654   1706   1693    -99    271   -108       O  
ATOM   3065  CB  VAL A 409       1.209  50.868  27.336  1.00 12.99           C  
ANISOU 3065  CB  VAL A 409     1564   1720   1650   -122    279   -159       C  
ATOM   3066  CG1 VAL A 409       0.911  51.271  28.763  1.00 14.14           C  
ANISOU 3066  CG1 VAL A 409     1694   1888   1788   -119    275   -164       C  
ATOM   3067  CG2 VAL A 409       2.703  50.507  27.197  1.00 14.29           C  
ANISOU 3067  CG2 VAL A 409     1706   1909   1814   -132    283   -183       C  
ATOM   3068  N   LEU A 410      -1.912  49.316  27.802  1.00 11.79           N  
ANISOU 3068  N   LEU A 410     1427   1550   1502    -74    239    -86       N  
ATOM   3069  CA  LEU A 410      -3.338  49.600  27.944  1.00 11.39           C  
ANISOU 3069  CA  LEU A 410     1390   1485   1450    -65    234    -68       C  
ATOM   3070  C   LEU A 410      -3.551  50.674  29.023  1.00 12.64           C  
ANISOU 3070  C   LEU A 410     1545   1654   1601    -69    241    -78       C  
ATOM   3071  O   LEU A 410      -4.143  50.422  30.087  1.00 11.36           O  
ANISOU 3071  O   LEU A 410     1371   1508   1435    -58    230    -68       O  
ATOM   3072  CB  LEU A 410      -4.110  48.299  28.224  1.00 10.17           C  
ANISOU 3072  CB  LEU A 410     1226   1336   1300    -47    216    -44       C  
ATOM   3073  CG  LEU A 410      -5.641  48.320  28.248  1.00 12.31           C  
ANISOU 3073  CG  LEU A 410     1509   1596   1572    -37    209    -24       C  
ATOM   3074  CD1 LEU A 410      -6.226  48.383  26.826  1.00  5.65           C  
ANISOU 3074  CD1 LEU A 410      687    727    732    -37    211    -18       C  
ATOM   3075  CD2 LEU A 410      -6.140  47.062  28.952  1.00 10.82           C  
ANISOU 3075  CD2 LEU A 410     1304   1418   1386    -23    195     -6       C  
ATOM   3076  N   TYR A 411      -3.043  51.877  28.772  1.00 12.09           N  
ANISOU 3076  N   TYR A 411     1489   1575   1529    -86    261    -99       N  
ATOM   3077  CA  TYR A 411      -3.037  52.918  29.804  1.00 11.32           C  
ANISOU 3077  CA  TYR A 411     1387   1489   1424    -94    270   -115       C  
ATOM   3078  C   TYR A 411      -4.443  53.129  30.355  1.00 12.59           C  
ANISOU 3078  C   TYR A 411     1557   1645   1581    -79    261    -95       C  
ATOM   3079  O   TYR A 411      -5.420  53.224  29.600  1.00 11.46           O  
ANISOU 3079  O   TYR A 411     1435   1479   1439    -71    261    -78       O  
ATOM   3080  CB  TYR A 411      -2.611  54.280  29.236  1.00 12.65           C  
ANISOU 3080  CB  TYR A 411     1579   1636   1592   -115    297   -137       C  
ATOM   3081  CG  TYR A 411      -1.141  54.446  28.902  1.00 14.26           C  
ANISOU 3081  CG  TYR A 411     1773   1846   1798   -137    313   -165       C  
ATOM   3082  CD1 TYR A 411      -0.209  54.669  29.911  1.00 11.65           C  
ANISOU 3082  CD1 TYR A 411     1415   1547   1464   -149    316   -193       C  
ATOM   3083  CD2 TYR A 411      -0.693  54.392  27.585  1.00 13.55           C  
ANISOU 3083  CD2 TYR A 411     1700   1734   1712   -145    324   -167       C  
ATOM   3084  CE1 TYR A 411       1.140  54.833  29.628  1.00 16.00           C  
ANISOU 3084  CE1 TYR A 411     1954   2109   2016   -170    330   -223       C  
ATOM   3085  CE2 TYR A 411       0.663  54.552  27.285  1.00 13.66           C  
ANISOU 3085  CE2 TYR A 411     1704   1756   1729   -166    339   -195       C  
ATOM   3086  CZ  TYR A 411       1.565  54.787  28.315  1.00 14.96           C  
ANISOU 3086  CZ  TYR A 411     1840   1953   1890   -179    342   -223       C  
ATOM   3087  OH  TYR A 411       2.901  54.972  28.061  1.00 16.19           O  
ANISOU 3087  OH  TYR A 411     1982   2121   2047   -202    358   -255       O  
ATOM   3088  N   GLY A 412      -4.531  53.264  31.676  1.00 11.68           N  
ANISOU 3088  N   GLY A 412     1423   1554   1460    -76    255    -99       N  
ATOM   3089  CA  GLY A 412      -5.765  53.687  32.306  1.00 10.41           C  
ANISOU 3089  CA  GLY A 412     1269   1390   1294    -64    251    -85       C  
ATOM   3090  C   GLY A 412      -6.693  52.574  32.730  1.00 12.61           C  
ANISOU 3090  C   GLY A 412     1537   1679   1574    -44    230    -58       C  
ATOM   3091  O   GLY A 412      -7.638  52.830  33.494  1.00 13.05           O  
ANISOU 3091  O   GLY A 412     1592   1740   1624    -35    225    -48       O  
ATOM   3092  N   ALA A 413      -6.429  51.350  32.273  1.00 11.13           N  
ANISOU 3092  N   ALA A 413     1341   1493   1393    -39    220    -48       N  
ATOM   3093  CA  ALA A 413      -7.317  50.239  32.623  1.00 13.10           C  
ANISOU 3093  CA  ALA A 413     1582   1748   1646    -22    204    -23       C  
ATOM   3094  C   ALA A 413      -7.227  49.856  34.106  1.00 12.36           C  
ANISOU 3094  C   ALA A 413     1465   1683   1545    -12    196    -20       C  
ATOM   3095  O   ALA A 413      -6.145  49.557  34.617  1.00 11.16           O  
ANISOU 3095  O   ALA A 413     1296   1553   1390    -11    195    -31       O  
ATOM   3096  CB  ALA A 413      -7.026  49.019  31.765  1.00 13.09           C  
ANISOU 3096  CB  ALA A 413     1579   1739   1653    -19    198    -13       C  
ATOM   3097  N   LEU A 414      -8.371  49.863  34.790  1.00 11.75           N  
ANISOU 3097  N   LEU A 414     1388   1609   1465     -1    190     -5       N  
ATOM   3098  CA  LEU A 414      -8.422  49.406  36.171  1.00 12.55           C  
ANISOU 3098  CA  LEU A 414     1470   1737   1560     11    182      1       C  
ATOM   3099  C   LEU A 414      -8.618  47.896  36.114  1.00 13.61           C  
ANISOU 3099  C   LEU A 414     1599   1871   1701     23    175     23       C  
ATOM   3100  O   LEU A 414      -9.609  47.450  35.535  1.00 13.22           O  
ANISOU 3100  O   LEU A 414     1559   1803   1659     24    172     38       O  
ATOM   3101  CB  LEU A 414      -9.625  50.030  36.890  1.00 11.52           C  
ANISOU 3101  CB  LEU A 414     1343   1608   1424     16    181     10       C  
ATOM   3102  CG  LEU A 414      -9.854  49.672  38.365  1.00 15.17           C  
ANISOU 3102  CG  LEU A 414     1788   2097   1878     31    174     18       C  
ATOM   3103  CD1 LEU A 414      -8.641  50.100  39.208  1.00 11.13           C  
ANISOU 3103  CD1 LEU A 414     1259   1613   1356     30    177     -3       C  
ATOM   3104  CD2 LEU A 414     -11.147  50.331  38.892  1.00 12.91           C  
ANISOU 3104  CD2 LEU A 414     1508   1810   1587     35    173     27       C  
ATOM   3105  N   VAL A 415      -7.736  47.118  36.740  1.00 12.74           N  
ANISOU 3105  N   VAL A 415     1473   1781   1586     33    172     23       N  
ATOM   3106  CA  VAL A 415      -7.851  45.663  36.611  1.00 13.87           C  
ANISOU 3106  CA  VAL A 415     1614   1918   1735     45    168     43       C  
ATOM   3107  C   VAL A 415      -8.860  45.131  37.631  1.00 12.89           C  
ANISOU 3107  C   VAL A 415     1486   1801   1608     59    165     65       C  
ATOM   3108  O   VAL A 415      -9.272  45.882  38.513  1.00 13.91           O  
ANISOU 3108  O   VAL A 415     1611   1944   1729     62    165     62       O  
ATOM   3109  CB  VAL A 415      -6.482  44.946  36.735  1.00 13.06           C  
ANISOU 3109  CB  VAL A 415     1499   1833   1628     54    168     37       C  
ATOM   3110  CG1 VAL A 415      -5.544  45.402  35.617  1.00 15.73           C  
ANISOU 3110  CG1 VAL A 415     1841   2162   1970     38    172     16       C  
ATOM   3111  CG2 VAL A 415      -5.849  45.192  38.122  1.00 12.68           C  
ANISOU 3111  CG2 VAL A 415     1431   1822   1563     68    166     28       C  
ATOM   3112  N   GLY A 416      -9.265  43.870  37.511  1.00 12.41           N  
ANISOU 3112  N   GLY A 416     1430   1729   1555     67    166     85       N  
ATOM   3113  CA  GLY A 416     -10.111  43.204  38.528  1.00 13.26           C  
ANISOU 3113  CA  GLY A 416     1535   1842   1660     81    168    106       C  
ATOM   3114  C   GLY A 416      -9.658  43.483  39.949  1.00 14.11           C  
ANISOU 3114  C   GLY A 416     1628   1981   1751     98    166    105       C  
ATOM   3115  O   GLY A 416     -10.430  43.954  40.790  1.00 16.17           O  
ANISOU 3115  O   GLY A 416     1886   2252   2006    102    165    110       O  
ATOM   3116  N   GLY A 417      -8.388  43.235  40.240  1.00 12.94           N  
ANISOU 3116  N   GLY A 417     1469   1852   1592    110    165     96       N  
ATOM   3117  CA  GLY A 417      -7.879  43.607  41.557  1.00 14.77           C  
ANISOU 3117  CA  GLY A 417     1684   2120   1805    127    162     90       C  
ATOM   3118  C   GLY A 417      -7.479  42.406  42.399  1.00 16.49           C  
ANISOU 3118  C   GLY A 417     1898   2355   2013    157    165    109       C  
ATOM   3119  O   GLY A 417      -7.501  41.270  41.918  1.00 15.44           O  
ANISOU 3119  O   GLY A 417     1775   2202   1888    164    170    125       O  
ATOM   3120  N   PRO A 418      -7.121  42.647  43.672  1.00 17.49           N  
ANISOU 3120  N   PRO A 418     2008   2516   2119    178    162    105       N  
ATOM   3121  CA  PRO A 418      -6.642  41.534  44.491  1.00 17.28           C  
ANISOU 3121  CA  PRO A 418     1979   2509   2078    212    166    123       C  
ATOM   3122  C   PRO A 418      -7.764  40.629  44.976  1.00 18.09           C  
ANISOU 3122  C   PRO A 418     2095   2591   2184    224    175    156       C  
ATOM   3123  O   PRO A 418      -8.946  40.956  44.827  1.00 16.93           O  
ANISOU 3123  O   PRO A 418     1958   2424   2050    206    177    163       O  
ATOM   3124  CB  PRO A 418      -5.968  42.237  45.670  1.00 19.24           C  
ANISOU 3124  CB  PRO A 418     2203   2803   2302    229    159    105       C  
ATOM   3125  CG  PRO A 418      -6.732  43.529  45.812  1.00 18.40           C  
ANISOU 3125  CG  PRO A 418     2095   2695   2201    206    156     92       C  
ATOM   3126  CD  PRO A 418      -7.108  43.928  44.402  1.00 16.57           C  
ANISOU 3126  CD  PRO A 418     1878   2425   1992    172    157     85       C  
ATOM   3127  N   GLY A 419      -7.387  39.488  45.551  1.00 18.78           N  
ANISOU 3127  N   GLY A 419     2188   2687   2261    256    183    176       N  
ATOM   3128  CA  GLY A 419      -8.359  38.616  46.196  1.00 19.03           C  
ANISOU 3128  CA  GLY A 419     2234   2702   2293    270    196    208       C  
ATOM   3129  C   GLY A 419      -8.737  39.161  47.563  1.00 18.95           C  
ANISOU 3129  C   GLY A 419     2212   2721   2264    286    193    211       C  
ATOM   3130  O   GLY A 419      -8.293  40.235  47.982  1.00 17.32           O  
ANISOU 3130  O   GLY A 419     1986   2546   2045    285    181    187       O  
ATOM   3131  N   ARG A 420      -9.545  38.387  48.281  1.00 19.54           N  
ANISOU 3131  N   ARG A 420     2300   2786   2337    302    207    240       N  
ATOM   3132  CA  ARG A 420     -10.155  38.843  49.518  1.00 20.68           C  
ANISOU 3132  CA  ARG A 420     2436   2952   2467    314    207    246       C  
ATOM   3133  C   ARG A 420      -9.120  39.125  50.601  1.00 20.93           C  
ANISOU 3133  C   ARG A 420     2449   3034   2468    349    199    237       C  
ATOM   3134  O   ARG A 420      -9.414  39.821  51.571  1.00 19.80           O  
ANISOU 3134  O   ARG A 420     2293   2917   2310    357    194    233       O  
ATOM   3135  CB  ARG A 420     -11.087  37.763  50.060  1.00 22.74           C  
ANISOU 3135  CB  ARG A 420     2717   3190   2730    328    228    281       C  
ATOM   3136  CG  ARG A 420     -12.113  37.271  49.075  1.00 29.30           C  
ANISOU 3136  CG  ARG A 420     3565   3975   3590    296    239    290       C  
ATOM   3137  CD  ARG A 420     -12.158  35.755  49.194  1.00 42.10           C  
ANISOU 3137  CD  ARG A 420     5210   5572   5213    315    263    319       C  
ATOM   3138  NE  ARG A 420     -13.032  35.311  50.271  1.00 49.90           N  
ANISOU 3138  NE  ARG A 420     6207   6557   6193    330    280    344       N  
ATOM   3139  CZ  ARG A 420     -12.752  34.323  51.120  1.00 54.77           C  
ANISOU 3139  CZ  ARG A 420     6838   7176   6794    367    299    370       C  
ATOM   3140  NH1 ARG A 420     -11.594  33.673  51.064  1.00 52.74           N  
ANISOU 3140  NH1 ARG A 420     6588   6927   6524    396    301    374       N  
ATOM   3141  NH2 ARG A 420     -13.642  34.001  52.052  1.00 54.55           N  
ANISOU 3141  NH2 ARG A 420     6821   7144   6762    376    317    392       N  
ATOM   3142  N   ASP A 421      -7.929  38.561  50.442  1.00 19.73           N  
ANISOU 3142  N   ASP A 421     2294   2897   2304    372    198    233       N  
ATOM   3143  CA  ASP A 421      -6.843  38.734  51.402  1.00 21.54           C  
ANISOU 3143  CA  ASP A 421     2502   3178   2501    408    190    221       C  
ATOM   3144  C   ASP A 421      -5.755  39.685  50.889  1.00 21.20           C  
ANISOU 3144  C   ASP A 421     2435   3163   2456    392    173    181       C  
ATOM   3145  O   ASP A 421      -4.629  39.694  51.400  1.00 21.36           O  
ANISOU 3145  O   ASP A 421     2436   3228   2452    420    166    165       O  
ATOM   3146  CB  ASP A 421      -6.245  37.357  51.704  1.00 22.24           C  
ANISOU 3146  CB  ASP A 421     2604   3270   2574    452    203    247       C  
ATOM   3147  CG  ASP A 421      -5.644  36.700  50.469  1.00 26.87           C  
ANISOU 3147  CG  ASP A 421     3203   3831   3176    442    205    245       C  
ATOM   3148  OD1 ASP A 421      -5.880  37.166  49.329  1.00 24.49           O  
ANISOU 3148  OD1 ASP A 421     2903   3502   2901    400    200    229       O  
ATOM   3149  OD2 ASP A 421      -4.934  35.689  50.637  1.00 30.90           O  
ANISOU 3149  OD2 ASP A 421     3721   4348   3671    479    214    259       O  
ATOM   3150  N   ASP A 422      -6.105  40.494  49.890  1.00 18.63           N  
ANISOU 3150  N   ASP A 422     2110   2811   2154    349    168    163       N  
ATOM   3151  CA  ASP A 422      -5.185  41.438  49.249  1.00 19.59           C  
ANISOU 3151  CA  ASP A 422     2214   2949   2278    326    157    124       C  
ATOM   3152  C   ASP A 422      -4.138  40.778  48.342  1.00 19.41           C  
ANISOU 3152  C   ASP A 422     2194   2923   2259    330    157    118       C  
ATOM   3153  O   ASP A 422      -3.260  41.465  47.829  1.00 20.16           O  
ANISOU 3153  O   ASP A 422     2272   3034   2353    313    150     86       O  
ATOM   3154  CB  ASP A 422      -4.475  42.350  50.257  1.00 19.65           C  
ANISOU 3154  CB  ASP A 422     2192   3011   2260    339    147     95       C  
ATOM   3155  CG  ASP A 422      -5.433  43.216  51.048  1.00 22.47           C  
ANISOU 3155  CG  ASP A 422     2547   3374   2617    330    145     95       C  
ATOM   3156  OD1 ASP A 422      -6.025  44.167  50.486  1.00 22.38           O  
ANISOU 3156  OD1 ASP A 422     2539   3339   2623    294    144     82       O  
ATOM   3157  OD2 ASP A 422      -5.579  42.962  52.260  1.00 18.71           O  
ANISOU 3157  OD2 ASP A 422     2063   2925   2118    362    146    107       O  
ATOM   3158  N   SER A 423      -4.231  39.475  48.098  1.00 18.61           N  
ANISOU 3158  N   SER A 423     2111   2798   2160    349    168    147       N  
ATOM   3159  CA  SER A 423      -3.208  38.815  47.290  1.00 19.68           C  
ANISOU 3159  CA  SER A 423     2249   2932   2297    356    168    142       C  
ATOM   3160  C   SER A 423      -3.427  39.109  45.807  1.00 20.05           C  
ANISOU 3160  C   SER A 423     2306   2939   2373    313    168    132       C  
ATOM   3161  O   SER A 423      -4.558  39.256  45.334  1.00 16.23           O  
ANISOU 3161  O   SER A 423     1839   2417   1911    287    172    143       O  
ATOM   3162  CB  SER A 423      -3.181  37.303  47.515  1.00 18.73           C  
ANISOU 3162  CB  SER A 423     2148   2799   2168    393    181    177       C  
ATOM   3163  OG  SER A 423      -4.416  36.745  47.101  1.00 23.61           O  
ANISOU 3163  OG  SER A 423     2793   3366   2810    375    194    204       O  
ATOM   3164  N   TYR A 424      -2.319  39.185  45.085  1.00 19.55           N  
ANISOU 3164  N   TYR A 424     2233   2886   2309    308    163    109       N  
ATOM   3165  CA  TYR A 424      -2.392  39.512  43.667  1.00 21.21           C  
ANISOU 3165  CA  TYR A 424     2452   3062   2544    270    162     98       C  
ATOM   3166  C   TYR A 424      -1.079  39.084  43.036  1.00 21.32           C  
ANISOU 3166  C   TYR A 424     2458   3089   2552    279    160     83       C  
ATOM   3167  O   TYR A 424      -0.035  39.234  43.660  1.00 20.57           O  
ANISOU 3167  O   TYR A 424     2340   3041   2434    301    154     64       O  
ATOM   3168  CB  TYR A 424      -2.568  41.026  43.501  1.00 20.38           C  
ANISOU 3168  CB  TYR A 424     2335   2961   2444    236    156     69       C  
ATOM   3169  CG  TYR A 424      -2.446  41.476  42.062  1.00 20.16           C  
ANISOU 3169  CG  TYR A 424     2315   2904   2438    201    156     53       C  
ATOM   3170  CD1 TYR A 424      -3.527  41.393  41.184  1.00 19.63           C  
ANISOU 3170  CD1 TYR A 424     2271   2792   2394    179    161     68       C  
ATOM   3171  CD2 TYR A 424      -1.236  41.951  41.576  1.00 19.84           C  
ANISOU 3171  CD2 TYR A 424     2259   2884   2393    192    154     22       C  
ATOM   3172  CE1 TYR A 424      -3.405  41.794  39.850  1.00 14.57           C  
ANISOU 3172  CE1 TYR A 424     1639   2126   1770    150    161     55       C  
ATOM   3173  CE2 TYR A 424      -1.095  42.344  40.245  1.00 18.77           C  
ANISOU 3173  CE2 TYR A 424     2134   2721   2276    161    156      9       C  
ATOM   3174  CZ  TYR A 424      -2.175  42.259  39.398  1.00 19.95           C  
ANISOU 3174  CZ  TYR A 424     2307   2825   2446    142    160     26       C  
ATOM   3175  OH  TYR A 424      -1.985  42.661  38.098  1.00 20.87           O  
ANISOU 3175  OH  TYR A 424     2433   2918   2578    116    162     13       O  
ATOM   3176  N   GLU A 425      -1.136  38.551  41.820  1.00 22.02           N  
ANISOU 3176  N   GLU A 425     2564   3141   2661    263    164     90       N  
ATOM   3177  CA  GLU A 425       0.054  38.413  40.985  1.00 23.79           C  
ANISOU 3177  CA  GLU A 425     2779   3374   2883    261    162     70       C  
ATOM   3178  C   GLU A 425      -0.350  38.812  39.567  1.00 22.61           C  
ANISOU 3178  C   GLU A 425     2645   3184   2762    221    163     63       C  
ATOM   3179  O   GLU A 425      -1.467  38.539  39.130  1.00 19.55           O  
ANISOU 3179  O   GLU A 425     2278   2758   2392    207    168     83       O  
ATOM   3180  CB  GLU A 425       0.594  36.981  41.007  1.00 25.85           C  
ANISOU 3180  CB  GLU A 425     3051   3636   3135    298    167     91       C  
ATOM   3181  CG  GLU A 425       1.513  36.713  42.194  1.00 37.31           C  
ANISOU 3181  CG  GLU A 425     4481   5140   4553    342    164     87       C  
ATOM   3182  CD  GLU A 425       1.740  35.238  42.487  1.00 48.28           C  
ANISOU 3182  CD  GLU A 425     5887   6526   5930    386    173    117       C  
ATOM   3183  OE1 GLU A 425       2.008  34.455  41.543  1.00 50.75           O  
ANISOU 3183  OE1 GLU A 425     6215   6811   6254    385    179    125       O  
ATOM   3184  OE2 GLU A 425       1.665  34.877  43.685  1.00 50.07           O  
ANISOU 3184  OE2 GLU A 425     6111   6776   6134    423    176    133       O  
ATOM   3185  N   ASP A 426       0.556  39.492  38.877  1.00 20.79           N  
ANISOU 3185  N   ASP A 426     2402   2965   2532    202    160     33       N  
ATOM   3186  CA  ASP A 426       0.335  39.990  37.522  1.00 20.57           C  
ANISOU 3186  CA  ASP A 426     2386   2903   2526    166    162     23       C  
ATOM   3187  C   ASP A 426       0.535  38.855  36.514  1.00 21.01           C  
ANISOU 3187  C   ASP A 426     2458   2933   2593    171    165     37       C  
ATOM   3188  O   ASP A 426       1.667  38.534  36.163  1.00 21.56           O  
ANISOU 3188  O   ASP A 426     2517   3019   2655    180    164     24       O  
ATOM   3189  CB  ASP A 426       1.345  41.120  37.298  1.00 20.82           C  
ANISOU 3189  CB  ASP A 426     2397   2960   2551    147    160    -15       C  
ATOM   3190  CG  ASP A 426       1.163  41.843  35.979  1.00 19.16           C  
ANISOU 3190  CG  ASP A 426     2200   2717   2360    111    164    -28       C  
ATOM   3191  OD1 ASP A 426       0.132  41.705  35.279  1.00 20.44           O  
ANISOU 3191  OD1 ASP A 426     2384   2840   2539     98    167     -9       O  
ATOM   3192  OD2 ASP A 426       2.099  42.602  35.672  1.00 18.61           O  
ANISOU 3192  OD2 ASP A 426     2117   2665   2288     95    167    -58       O  
ATOM   3193  N   ASN A 427      -0.556  38.272  36.031  1.00 19.13           N  
ANISOU 3193  N   ASN A 427     2242   2654   2371    164    170     61       N  
ATOM   3194  CA  ASN A 427      -0.527  37.054  35.227  1.00 20.11           C  
ANISOU 3194  CA  ASN A 427     2383   2751   2506    171    175     77       C  
ATOM   3195  C   ASN A 427      -1.666  37.142  34.213  1.00 20.10           C  
ANISOU 3195  C   ASN A 427     2400   2707   2528    143    178     84       C  
ATOM   3196  O   ASN A 427      -2.830  37.303  34.595  1.00 18.24           O  
ANISOU 3196  O   ASN A 427     2172   2459   2299    136    180     97       O  
ATOM   3197  CB  ASN A 427      -0.731  35.830  36.127  1.00 20.90           C  
ANISOU 3197  CB  ASN A 427     2491   2852   2597    206    182    105       C  
ATOM   3198  CG  ASN A 427      -0.646  34.496  35.392  1.00 24.62           C  
ANISOU 3198  CG  ASN A 427     2981   3294   3077    215    191    122       C  
ATOM   3199  OD1 ASN A 427      -0.576  34.414  34.163  1.00 23.16           O  
ANISOU 3199  OD1 ASN A 427     2804   3086   2908    195    191    115       O  
ATOM   3200  ND2 ASN A 427      -0.706  33.416  36.170  1.00 30.73           N  
ANISOU 3200  ND2 ASN A 427     3765   4068   3842    247    200    147       N  
ATOM   3201  N   ILE A 428      -1.302  37.065  32.933  1.00 18.25           N  
ANISOU 3201  N   ILE A 428     2172   2455   2305    127    178     74       N  
ATOM   3202  CA  ILE A 428      -2.257  37.117  31.833  1.00 18.78           C  
ANISOU 3202  CA  ILE A 428     2256   2487   2393    103    180     78       C  
ATOM   3203  C   ILE A 428      -3.287  35.996  31.948  1.00 19.73           C  
ANISOU 3203  C   ILE A 428     2392   2582   2523    109    187    103       C  
ATOM   3204  O   ILE A 428      -4.427  36.168  31.513  1.00 20.25           O  
ANISOU 3204  O   ILE A 428     2466   2625   2601     91    188    107       O  
ATOM   3205  CB  ILE A 428      -1.555  37.111  30.448  1.00 16.57           C  
ANISOU 3205  CB  ILE A 428     1980   2195   2121     89    179     63       C  
ATOM   3206  CG1 ILE A 428      -2.485  37.671  29.359  1.00 16.84           C  
ANISOU 3206  CG1 ILE A 428     2026   2201   2169     63    179     59       C  
ATOM   3207  CG2 ILE A 428      -1.084  35.699  30.094  1.00 18.01           C  
ANISOU 3207  CG2 ILE A 428     2170   2366   2305    106    184     75       C  
ATOM   3208  CD1 ILE A 428      -1.867  37.676  27.953  1.00 21.19           C  
ANISOU 3208  CD1 ILE A 428     2583   2740   2728     51    179     46       C  
ATOM   3209  N   GLU A 429      -2.907  34.879  32.566  1.00 20.88           N  
ANISOU 3209  N   GLU A 429     2540   2730   2661    135    194    119       N  
ATOM   3210  CA  GLU A 429      -3.851  33.772  32.745  1.00 22.83           C  
ANISOU 3210  CA  GLU A 429     2805   2951   2919    140    206    143       C  
ATOM   3211  C   GLU A 429      -4.933  34.098  33.773  1.00 23.08           C  
ANISOU 3211  C   GLU A 429     2835   2985   2948    140    208    154       C  
ATOM   3212  O   GLU A 429      -5.966  33.431  33.812  1.00 22.46           O  
ANISOU 3212  O   GLU A 429     2769   2883   2881    134    218    169       O  
ATOM   3213  CB  GLU A 429      -3.155  32.475  33.179  1.00 23.37           C  
ANISOU 3213  CB  GLU A 429     2881   3019   2979    172    216    159       C  
ATOM   3214  CG  GLU A 429      -2.055  31.960  32.247  1.00 26.66           C  
ANISOU 3214  CG  GLU A 429     3299   3432   3395    177    215    150       C  
ATOM   3215  CD  GLU A 429      -2.556  31.610  30.853  1.00 30.39           C  
ANISOU 3215  CD  GLU A 429     3785   3869   3890    152    218    146       C  
ATOM   3216  OE1 GLU A 429      -3.765  31.369  30.667  1.00 34.98           O  
ANISOU 3216  OE1 GLU A 429     4377   4425   4486    135    225    154       O  
ATOM   3217  OE2 GLU A 429      -1.732  31.558  29.920  1.00 35.85           O  
ANISOU 3217  OE2 GLU A 429     4476   4561   4584    148    214    133       O  
ATOM   3218  N   ASP A 430      -4.687  35.091  34.626  1.00 22.02           N  
ANISOU 3218  N   ASP A 430     2685   2882   2799    145    200    146       N  
ATOM   3219  CA  ASP A 430      -5.640  35.370  35.696  1.00 21.99           C  
ANISOU 3219  CA  ASP A 430     2679   2883   2790    149    202    157       C  
ATOM   3220  C   ASP A 430      -6.773  36.240  35.157  1.00 21.53           C  
ANISOU 3220  C   ASP A 430     2622   2811   2745    119    197    149       C  
ATOM   3221  O   ASP A 430      -6.733  37.472  35.244  1.00 19.99           O  
ANISOU 3221  O   ASP A 430     2417   2633   2545    109    188    134       O  
ATOM   3222  CB  ASP A 430      -4.967  35.982  36.930  1.00 20.26           C  
ANISOU 3222  CB  ASP A 430     2443   2704   2548    170    196    153       C  
ATOM   3223  CG  ASP A 430      -5.834  35.868  38.185  1.00 22.13           C  
ANISOU 3223  CG  ASP A 430     2681   2947   2779    183    202    171       C  
ATOM   3224  OD1 ASP A 430      -7.075  35.695  38.079  1.00 20.02           O  
ANISOU 3224  OD1 ASP A 430     2425   2656   2526    168    208    183       O  
ATOM   3225  OD2 ASP A 430      -5.267  35.932  39.295  1.00 20.06           O  
ANISOU 3225  OD2 ASP A 430     2408   2716   2496    209    200    174       O  
ATOM   3226  N   TYR A 431      -7.778  35.583  34.586  1.00 20.88           N  
ANISOU 3226  N   TYR A 431     2553   2700   2680    106    205    159       N  
ATOM   3227  CA  TYR A 431      -8.902  36.287  33.972  1.00 21.20           C  
ANISOU 3227  CA  TYR A 431     2593   2728   2731     81    201    151       C  
ATOM   3228  C   TYR A 431      -9.841  36.893  35.018  1.00 21.16           C  
ANISOU 3228  C   TYR A 431     2583   2736   2720     82    200    157       C  
ATOM   3229  O   TYR A 431     -10.864  37.458  34.651  1.00 19.90           O  
ANISOU 3229  O   TYR A 431     2423   2570   2567     65    197    152       O  
ATOM   3230  CB  TYR A 431      -9.683  35.375  33.006  1.00 22.23           C  
ANISOU 3230  CB  TYR A 431     2736   2828   2880     66    209    155       C  
ATOM   3231  CG  TYR A 431     -10.188  34.093  33.641  1.00 24.68           C  
ANISOU 3231  CG  TYR A 431     3056   3124   3196     75    226    175       C  
ATOM   3232  CD1 TYR A 431     -11.345  34.099  34.416  1.00 28.03           C  
ANISOU 3232  CD1 TYR A 431     3480   3548   3622     71    232    185       C  
ATOM   3233  CD2 TYR A 431      -9.497  32.888  33.494  1.00 29.45           C  
ANISOU 3233  CD2 TYR A 431     3672   3714   3803     87    237    185       C  
ATOM   3234  CE1 TYR A 431     -11.819  32.951  35.018  1.00 26.61           C  
ANISOU 3234  CE1 TYR A 431     3310   3352   3446     77    252    203       C  
ATOM   3235  CE2 TYR A 431      -9.962  31.719  34.108  1.00 30.51           C  
ANISOU 3235  CE2 TYR A 431     3819   3831   3941     96    257    204       C  
ATOM   3236  CZ  TYR A 431     -11.130  31.766  34.855  1.00 32.78           C  
ANISOU 3236  CZ  TYR A 431     4106   4117   4232     89    265    213       C  
ATOM   3237  OH  TYR A 431     -11.642  30.649  35.472  1.00 30.50           O  
ANISOU 3237  OH  TYR A 431     3831   3808   3947     95    289    232       O  
ATOM   3238  N   VAL A 432      -9.528  36.736  36.304  1.00 20.35           N  
ANISOU 3238  N   VAL A 432     2475   2652   2604    103    203    169       N  
ATOM   3239  CA  VAL A 432     -10.266  37.421  37.360  1.00 19.24           C  
ANISOU 3239  CA  VAL A 432     2328   2528   2455    106    201    173       C  
ATOM   3240  C   VAL A 432      -9.515  38.677  37.793  1.00 17.94           C  
ANISOU 3240  C   VAL A 432     2149   2391   2275    110    190    156       C  
ATOM   3241  O   VAL A 432      -9.975  39.792  37.552  1.00 17.10           O  
ANISOU 3241  O   VAL A 432     2040   2288   2170     95    183    143       O  
ATOM   3242  CB  VAL A 432     -10.564  36.483  38.560  1.00 20.59           C  
ANISOU 3242  CB  VAL A 432     2502   2700   2619    127    214    197       C  
ATOM   3243  CG1 VAL A 432     -11.157  37.264  39.728  1.00 20.00           C  
ANISOU 3243  CG1 VAL A 432     2418   2647   2533    133    211    200       C  
ATOM   3244  CG2 VAL A 432     -11.496  35.342  38.111  1.00 19.24           C  
ANISOU 3244  CG2 VAL A 432     2346   2497   2466    116    230    210       C  
ATOM   3245  N   LYS A 433      -8.331  38.501  38.375  1.00 16.87           N  
ANISOU 3245  N   LYS A 433     2006   2278   2125    131    188    154       N  
ATOM   3246  CA  LYS A 433      -7.584  39.615  38.954  1.00 15.86           C  
ANISOU 3246  CA  LYS A 433     1862   2182   1982    135    179    136       C  
ATOM   3247  C   LYS A 433      -7.065  40.591  37.896  1.00 15.15           C  
ANISOU 3247  C   LYS A 433     1770   2089   1897    113    173    110       C  
ATOM   3248  O   LYS A 433      -6.920  41.779  38.184  1.00 13.45           O  
ANISOU 3248  O   LYS A 433     1546   1890   1674    105    169     93       O  
ATOM   3249  CB  LYS A 433      -6.431  39.094  39.821  1.00 16.63           C  
ANISOU 3249  CB  LYS A 433     1948   2308   2060    165    180    138       C  
ATOM   3250  CG  LYS A 433      -6.899  38.171  40.983  1.00 19.21           C  
ANISOU 3250  CG  LYS A 433     2280   2640   2378    192    189    165       C  
ATOM   3251  CD  LYS A 433      -5.886  38.171  42.126  1.00 22.71           C  
ANISOU 3251  CD  LYS A 433     2707   3124   2795    224    185    162       C  
ATOM   3252  CE  LYS A 433      -6.111  37.083  43.182  1.00 26.00           C  
ANISOU 3252  CE  LYS A 433     3133   3545   3200    258    197    191       C  
ATOM   3253  NZ  LYS A 433      -5.727  35.773  42.608  1.00 31.60           N  
ANISOU 3253  NZ  LYS A 433     3858   4232   3914    271    208    206       N  
ATOM   3254  N   ASN A 434      -6.768  40.073  36.705  1.00 13.68           N  
ANISOU 3254  N   ASN A 434     1593   1882   1723    104    175    108       N  
ATOM   3255  CA  ASN A 434      -6.222  40.867  35.599  1.00 14.70           C  
ANISOU 3255  CA  ASN A 434     1723   2005   1857     84    171     86       C  
ATOM   3256  C   ASN A 434      -7.188  41.178  34.456  1.00 14.84           C  
ANISOU 3256  C   ASN A 434     1754   1993   1889     63    172     86       C  
ATOM   3257  O   ASN A 434      -6.776  41.690  33.410  1.00 13.74           O  
ANISOU 3257  O   ASN A 434     1620   1845   1754     49    171     71       O  
ATOM   3258  CB  ASN A 434      -4.905  40.298  35.056  1.00 15.70           C  
ANISOU 3258  CB  ASN A 434     1846   2136   1982     90    172     78       C  
ATOM   3259  CG  ASN A 434      -3.705  41.006  35.639  1.00 17.59           C  
ANISOU 3259  CG  ASN A 434     2067   2410   2205     96    169     56       C  
ATOM   3260  OD1 ASN A 434      -3.853  41.850  36.530  1.00 17.46           O  
ANISOU 3260  OD1 ASN A 434     2040   2413   2178     96    167     49       O  
ATOM   3261  ND2 ASN A 434      -2.518  40.704  35.124  1.00 19.50           N  
ANISOU 3261  ND2 ASN A 434     2303   2661   2444     99    169     44       N  
ATOM   3262  N   GLU A 435      -8.473  40.910  34.682  1.00 13.06           N  
ANISOU 3262  N   GLU A 435     1534   1756   1670     62    173    101       N  
ATOM   3263  CA  GLU A 435      -9.516  41.326  33.743  1.00 14.21           C  
ANISOU 3263  CA  GLU A 435     1690   1882   1826     45    172     98       C  
ATOM   3264  C   GLU A 435      -9.599  42.851  33.739  1.00 12.57           C  
ANISOU 3264  C   GLU A 435     1482   1682   1610     36    169     83       C  
ATOM   3265  O   GLU A 435      -9.279  43.497  34.742  1.00 10.31           O  
ANISOU 3265  O   GLU A 435     1186   1416   1312     42    168     78       O  
ATOM   3266  CB  GLU A 435     -10.863  40.720  34.166  1.00 14.14           C  
ANISOU 3266  CB  GLU A 435     1683   1865   1822     46    175    115       C  
ATOM   3267  CG  GLU A 435     -12.040  40.931  33.210  1.00 21.10           C  
ANISOU 3267  CG  GLU A 435     2572   2731   2714     31    174    112       C  
ATOM   3268  CD  GLU A 435     -11.871  40.314  31.825  1.00 28.69           C  
ANISOU 3268  CD  GLU A 435     3541   3673   3686     22    175    107       C  
ATOM   3269  OE1 GLU A 435     -10.761  40.305  31.253  1.00 33.70           O  
ANISOU 3269  OE1 GLU A 435     4178   4305   4321     22    174     99       O  
ATOM   3270  OE2 GLU A 435     -12.885  39.866  31.252  1.00 33.36           O  
ANISOU 3270  OE2 GLU A 435     4134   4252   4286     14    176    108       O  
ATOM   3271  N   VAL A 436     -10.004  43.412  32.602  1.00 12.29           N  
ANISOU 3271  N   VAL A 436     1457   1631   1580     24    168     74       N  
ATOM   3272  CA  VAL A 436     -10.231  44.853  32.442  1.00 12.00           C  
ANISOU 3272  CA  VAL A 436     1426   1595   1536     17    169     62       C  
ATOM   3273  C   VAL A 436     -11.556  44.979  31.690  1.00 13.20           C  
ANISOU 3273  C   VAL A 436     1588   1733   1693     14    167     66       C  
ATOM   3274  O   VAL A 436     -11.928  44.043  30.973  1.00 13.26           O  
ANISOU 3274  O   VAL A 436     1598   1729   1710     12    166     72       O  
ATOM   3275  CB  VAL A 436      -9.093  45.508  31.605  1.00 13.52           C  
ANISOU 3275  CB  VAL A 436     1624   1782   1727      8    173     43       C  
ATOM   3276  CG1 VAL A 436      -7.774  45.528  32.378  1.00  9.70           C  
ANISOU 3276  CG1 VAL A 436     1128   1320   1238     10    175     33       C  
ATOM   3277  CG2 VAL A 436      -8.886  44.787  30.276  1.00 13.58           C  
ANISOU 3277  CG2 VAL A 436     1641   1772   1745      3    173     44       C  
ATOM   3278  N   ALA A 437     -12.278  46.089  31.827  1.00 11.00           N  
ANISOU 3278  N   ALA A 437     1315   1457   1406     14    167     62       N  
ATOM   3279  CA  ALA A 437     -13.591  46.169  31.176  1.00 11.39           C  
ANISOU 3279  CA  ALA A 437     1371   1499   1457     15    164     66       C  
ATOM   3280  C   ALA A 437     -14.118  47.589  31.171  1.00 11.21           C  
ANISOU 3280  C   ALA A 437     1359   1478   1422     18    166     60       C  
ATOM   3281  O   ALA A 437     -13.772  48.373  32.052  1.00 10.77           O  
ANISOU 3281  O   ALA A 437     1301   1430   1358     19    169     56       O  
ATOM   3282  CB  ALA A 437     -14.619  45.267  31.884  1.00 12.36           C  
ANISOU 3282  CB  ALA A 437     1483   1629   1584     18    161     80       C  
ATOM   3283  N   CYS A 438     -14.973  47.912  30.205  1.00 10.68           N  
ANISOU 3283  N   CYS A 438     1302   1403   1352     21    165     58       N  
ATOM   3284  CA  CYS A 438     -15.598  49.226  30.186  1.00 10.34           C  
ANISOU 3284  CA  CYS A 438     1272   1361   1296     29    167     54       C  
ATOM   3285  C   CYS A 438     -16.229  49.585  31.528  1.00 11.41           C  
ANISOU 3285  C   CYS A 438     1398   1512   1425     34    165     59       C  
ATOM   3286  O   CYS A 438     -16.113  50.730  31.967  1.00 10.49           O  
ANISOU 3286  O   CYS A 438     1290   1396   1298     37    171     54       O  
ATOM   3287  CB  CYS A 438     -16.699  49.297  29.128  1.00 10.14           C  
ANISOU 3287  CB  CYS A 438     1254   1333   1265     38    164     54       C  
ATOM   3288  SG  CYS A 438     -16.111  49.211  27.413  1.00 14.32           S  
ANISOU 3288  SG  CYS A 438     1798   1844   1796     37    167     46       S  
ATOM   3289  N   ASP A 439     -16.930  48.640  32.157  1.00 11.94           N  
ANISOU 3289  N   ASP A 439     1448   1589   1497     35    159     70       N  
ATOM   3290  CA  ASP A 439     -17.674  48.958  33.387  1.00 12.72           C  
ANISOU 3290  CA  ASP A 439     1538   1704   1589     42    157     76       C  
ATOM   3291  C   ASP A 439     -16.765  49.071  34.608  1.00 12.22           C  
ANISOU 3291  C   ASP A 439     1467   1650   1525     40    160     76       C  
ATOM   3292  O   ASP A 439     -17.110  49.773  35.556  1.00 12.78           O  
ANISOU 3292  O   ASP A 439     1535   1731   1586     46    160     77       O  
ATOM   3293  CB  ASP A 439     -18.816  47.981  33.665  1.00 13.40           C  
ANISOU 3293  CB  ASP A 439     1610   1800   1681     43    152     86       C  
ATOM   3294  CG  ASP A 439     -18.330  46.672  34.263  1.00 16.24           C  
ANISOU 3294  CG  ASP A 439     1957   2159   2052     36    154     95       C  
ATOM   3295  OD1 ASP A 439     -17.738  45.862  33.510  1.00 15.30           O  
ANISOU 3295  OD1 ASP A 439     1839   2027   1943     30    156     94       O  
ATOM   3296  OD2 ASP A 439     -18.557  46.456  35.477  1.00 15.17           O  
ANISOU 3296  OD2 ASP A 439     1811   2035   1915     40    155    104       O  
ATOM   3297  N   TYR A 440     -15.592  48.450  34.557  1.00 11.90           N  
ANISOU 3297  N   TYR A 440     1423   1605   1491     34    162     75       N  
ATOM   3298  CA  TYR A 440     -14.576  48.635  35.589  1.00 13.24           C  
ANISOU 3298  CA  TYR A 440     1584   1787   1656     34    164     70       C  
ATOM   3299  C   TYR A 440     -14.120  50.095  35.659  1.00 12.65           C  
ANISOU 3299  C   TYR A 440     1520   1713   1573     31    171     54       C  
ATOM   3300  O   TYR A 440     -13.910  50.656  36.742  1.00 13.52           O  
ANISOU 3300  O   TYR A 440     1623   1838   1675     34    172     49       O  
ATOM   3301  CB  TYR A 440     -13.330  47.803  35.277  1.00 14.67           C  
ANISOU 3301  CB  TYR A 440     1762   1966   1846     30    166     68       C  
ATOM   3302  CG  TYR A 440     -13.454  46.304  35.451  1.00 12.81           C  
ANISOU 3302  CG  TYR A 440     1516   1730   1618     34    163     83       C  
ATOM   3303  CD1 TYR A 440     -14.698  45.682  35.483  1.00  9.60           C  
ANISOU 3303  CD1 TYR A 440     1108   1320   1216     36    162     96       C  
ATOM   3304  CD2 TYR A 440     -12.308  45.520  35.579  1.00 12.24           C  
ANISOU 3304  CD2 TYR A 440     1439   1662   1550     37    165     83       C  
ATOM   3305  CE1 TYR A 440     -14.792  44.308  35.658  1.00 14.46           C  
ANISOU 3305  CE1 TYR A 440     1719   1933   1842     38    164    110       C  
ATOM   3306  CE2 TYR A 440     -12.378  44.143  35.752  1.00 12.46           C  
ANISOU 3306  CE2 TYR A 440     1463   1687   1584     42    166     99       C  
ATOM   3307  CZ  TYR A 440     -13.632  43.549  35.775  1.00 14.89           C  
ANISOU 3307  CZ  TYR A 440     1771   1987   1899     42    167    112       C  
ATOM   3308  OH  TYR A 440     -13.749  42.192  35.937  1.00 15.25           O  
ANISOU 3308  OH  TYR A 440     1815   2025   1952     45    172    126       O  
ATOM   3309  N   ASN A 441     -13.971  50.699  34.485  1.00 12.09           N  
ANISOU 3309  N   ASN A 441     1466   1624   1502     26    176     45       N  
ATOM   3310  CA  ASN A 441     -13.475  52.068  34.409  1.00 12.29           C  
ANISOU 3310  CA  ASN A 441     1506   1643   1520     21    187     29       C  
ATOM   3311  C   ASN A 441     -14.514  53.153  34.633  1.00 12.66           C  
ANISOU 3311  C   ASN A 441     1566   1688   1556     29    190     30       C  
ATOM   3312  O   ASN A 441     -14.141  54.295  34.859  1.00 13.30           O  
ANISOU 3312  O   ASN A 441     1658   1765   1630     25    201     16       O  
ATOM   3313  CB  ASN A 441     -12.759  52.313  33.079  1.00 10.90           C  
ANISOU 3313  CB  ASN A 441     1347   1447   1348     12    196     19       C  
ATOM   3314  CG  ASN A 441     -11.270  52.034  33.190  1.00 15.21           C  
ANISOU 3314  CG  ASN A 441     1882   1997   1898      0    200      6       C  
ATOM   3315  OD1 ASN A 441     -10.879  50.973  33.669  1.00 12.45           O  
ANISOU 3315  OD1 ASN A 441     1515   1662   1554      2    192     12       O  
ATOM   3316  ND2 ASN A 441     -10.439  52.997  32.796  1.00 12.14           N  
ANISOU 3316  ND2 ASN A 441     1506   1598   1506    -11    215    -12       N  
ATOM   3317  N   ALA A 442     -15.794  52.806  34.544  1.00 13.40           N  
ANISOU 3317  N   ALA A 442     1657   1784   1647     40    182     43       N  
ATOM   3318  CA  ALA A 442     -16.855  53.809  34.415  1.00 13.88           C  
ANISOU 3318  CA  ALA A 442     1733   1843   1697     52    184     44       C  
ATOM   3319  C   ALA A 442     -17.119  54.644  35.666  1.00 14.40           C  
ANISOU 3319  C   ALA A 442     1796   1921   1753     56    187     41       C  
ATOM   3320  O   ALA A 442     -16.941  55.863  35.604  1.00 17.13           O  
ANISOU 3320  O   ALA A 442     2161   2256   2090     57    199     31       O  
ATOM   3321  CB  ALA A 442     -18.136  53.169  33.885  1.00 12.02           C  
ANISOU 3321  CB  ALA A 442     1493   1612   1461     63    174     56       C  
ATOM   3322  N   GLY A 443     -17.529  54.029  36.777  1.00 14.12           N  
ANISOU 3322  N   GLY A 443     1739   1905   1718     60    178     51       N  
ATOM   3323  CA  GLY A 443     -17.596  54.718  38.076  1.00 12.63           C  
ANISOU 3323  CA  GLY A 443     1545   1731   1521     63    179     47       C  
ATOM   3324  C   GLY A 443     -16.260  55.328  38.485  1.00 15.91           C  
ANISOU 3324  C   GLY A 443     1961   2146   1936     51    189     29       C  
ATOM   3325  O   GLY A 443     -16.191  56.413  39.078  1.00 15.31           O  
ANISOU 3325  O   GLY A 443     1893   2072   1852     51    198     17       O  
ATOM   3326  N   PHE A 444     -15.183  54.633  38.141  1.00 13.34           N  
ANISOU 3326  N   PHE A 444     1628   1819   1619     41    190     24       N  
ATOM   3327  CA  PHE A 444     -13.815  55.054  38.469  1.00 14.64           C  
ANISOU 3327  CA  PHE A 444     1789   1988   1784     28    198      4       C  
ATOM   3328  C   PHE A 444     -13.501  56.427  37.883  1.00 14.76           C  
ANISOU 3328  C   PHE A 444     1828   1982   1794     18    216    -13       C  
ATOM   3329  O   PHE A 444     -12.937  57.296  38.562  1.00 14.91           O  
ANISOU 3329  O   PHE A 444     1847   2007   1808     10    226    -32       O  
ATOM   3330  CB  PHE A 444     -12.863  53.969  37.946  1.00 12.02           C  
ANISOU 3330  CB  PHE A 444     1447   1656   1462     21    195      4       C  
ATOM   3331  CG  PHE A 444     -11.404  54.169  38.280  1.00 14.06           C  
ANISOU 3331  CG  PHE A 444     1695   1926   1720      9    201    -17       C  
ATOM   3332  CD1 PHE A 444     -10.979  54.429  39.581  1.00  9.35           C  
ANISOU 3332  CD1 PHE A 444     1080   1355   1115     10    200    -28       C  
ATOM   3333  CD2 PHE A 444     -10.449  54.047  37.273  1.00 11.05           C  
ANISOU 3333  CD2 PHE A 444     1319   1531   1345     -2    208    -28       C  
ATOM   3334  CE1 PHE A 444      -9.628  54.604  39.869  1.00 16.91           C  
ANISOU 3334  CE1 PHE A 444     2024   2328   2070      0    206    -52       C  
ATOM   3335  CE2 PHE A 444      -9.086  54.188  37.549  1.00 16.60           C  
ANISOU 3335  CE2 PHE A 444     2010   2248   2048    -14    215    -50       C  
ATOM   3336  CZ  PHE A 444      -8.681  54.460  38.860  1.00 13.37           C  
ANISOU 3336  CZ  PHE A 444     1581   1868   1630    -13    213    -63       C  
ATOM   3337  N   VAL A 445     -13.883  56.632  36.625  1.00 14.03           N  
ANISOU 3337  N   VAL A 445     1759   1865   1703     20    221     -9       N  
ATOM   3338  CA  VAL A 445     -13.664  57.927  35.983  1.00 12.96           C  
ANISOU 3338  CA  VAL A 445     1653   1706   1563     14    242    -23       C  
ATOM   3339  C   VAL A 445     -14.395  59.033  36.751  1.00 13.92           C  
ANISOU 3339  C   VAL A 445     1786   1830   1674     23    248    -25       C  
ATOM   3340  O   VAL A 445     -13.844  60.115  36.990  1.00 14.82           O  
ANISOU 3340  O   VAL A 445     1913   1934   1784     12    267    -44       O  
ATOM   3341  CB  VAL A 445     -14.106  57.916  34.498  1.00 13.09           C  
ANISOU 3341  CB  VAL A 445     1693   1699   1579     22    245    -13       C  
ATOM   3342  CG1 VAL A 445     -14.325  59.333  34.003  1.00 12.04           C  
ANISOU 3342  CG1 VAL A 445     1596   1542   1437     26    267    -21       C  
ATOM   3343  CG2 VAL A 445     -13.071  57.199  33.619  1.00 11.65           C  
ANISOU 3343  CG2 VAL A 445     1507   1509   1408      9    246    -18       C  
ATOM   3344  N   GLY A 446     -15.639  58.771  37.137  1.00 13.79           N  
ANISOU 3344  N   GLY A 446     1763   1824   1651     41    235     -8       N  
ATOM   3345  CA  GLY A 446     -16.420  59.748  37.910  1.00 13.53           C  
ANISOU 3345  CA  GLY A 446     1738   1795   1605     52    239     -9       C  
ATOM   3346  C   GLY A 446     -15.784  60.100  39.243  1.00 14.37           C  
ANISOU 3346  C   GLY A 446     1829   1919   1711     41    242    -24       C  
ATOM   3347  O   GLY A 446     -15.685  61.274  39.610  1.00 14.38           O  
ANISOU 3347  O   GLY A 446     1846   1913   1706     37    258    -39       O  
ATOM   3348  N   ALA A 447     -15.316  59.095  39.971  1.00 13.39           N  
ANISOU 3348  N   ALA A 447     1674   1819   1593     37    229    -22       N  
ATOM   3349  CA  ALA A 447     -14.609  59.360  41.224  1.00 14.27           C  
ANISOU 3349  CA  ALA A 447     1766   1952   1700     29    230    -39       C  
ATOM   3350  C   ALA A 447     -13.298  60.120  41.013  1.00 13.47           C  
ANISOU 3350  C   ALA A 447     1672   1842   1602      7    249    -69       C  
ATOM   3351  O   ALA A 447     -12.942  60.991  41.813  1.00 14.50           O  
ANISOU 3351  O   ALA A 447     1801   1980   1727      0    260    -89       O  
ATOM   3352  CB  ALA A 447     -14.393  58.058  41.981  1.00 14.48           C  
ANISOU 3352  CB  ALA A 447     1761   2008   1731     34    212    -28       C  
ATOM   3353  N   LEU A 448     -12.590  59.827  39.926  1.00 11.07           N  
ANISOU 3353  N   LEU A 448     1376   1521   1306     -3    255    -72       N  
ATOM   3354  CA  LEU A 448     -11.379  60.571  39.600  1.00 12.70           C  
ANISOU 3354  CA  LEU A 448     1591   1716   1516    -26    277   -102       C  
ATOM   3355  C   LEU A 448     -11.657  62.025  39.218  1.00 13.52           C  
ANISOU 3355  C   LEU A 448     1731   1790   1615    -32    302   -113       C  
ATOM   3356  O   LEU A 448     -10.805  62.889  39.461  1.00 15.33           O  
ANISOU 3356  O   LEU A 448     1964   2015   1844    -52    323   -142       O  
ATOM   3357  CB  LEU A 448     -10.584  59.879  38.484  1.00 11.95           C  
ANISOU 3357  CB  LEU A 448     1497   1610   1431    -36    278   -102       C  
ATOM   3358  CG  LEU A 448      -9.938  58.539  38.883  1.00 10.87           C  
ANISOU 3358  CG  LEU A 448     1327   1503   1299    -34    259    -98       C  
ATOM   3359  CD1 LEU A 448      -9.339  57.859  37.656  1.00 11.26           C  
ANISOU 3359  CD1 LEU A 448     1381   1538   1358    -40    259    -94       C  
ATOM   3360  CD2 LEU A 448      -8.862  58.775  39.935  1.00 11.00           C  
ANISOU 3360  CD2 LEU A 448     1318   1549   1312    -46    262   -126       C  
ATOM   3361  N   CYS A 449     -12.823  62.281  38.617  1.00 14.81           N  
ANISOU 3361  N   CYS A 449     1919   1933   1772    -13    302    -92       N  
ATOM   3362  CA  CYS A 449     -13.234  63.645  38.287  1.00 15.71           C  
ANISOU 3362  CA  CYS A 449     2070   2018   1878    -10    326    -98       C  
ATOM   3363  C   CYS A 449     -13.405  64.420  39.594  1.00 17.82           C  
ANISOU 3363  C   CYS A 449     2332   2299   2138    -12    331   -112       C  
ATOM   3364  O   CYS A 449     -12.957  65.563  39.701  1.00 17.30           O  
ANISOU 3364  O   CYS A 449     2285   2215   2070    -27    357   -135       O  
ATOM   3365  CB  CYS A 449     -14.550  63.678  37.516  1.00 16.32           C  
ANISOU 3365  CB  CYS A 449     2171   2080   1947     16    320    -71       C  
ATOM   3366  SG  CYS A 449     -14.434  63.088  35.810  1.00 16.94           S  
ANISOU 3366  SG  CYS A 449     2267   2138   2032     20    321    -58       S  
ATOM   3367  N   ARG A 450     -14.039  63.791  40.582  1.00 18.57           N  
ANISOU 3367  N   ARG A 450     2399   2426   2230      1    307    -99       N  
ATOM   3368  CA  ARG A 450     -14.262  64.439  41.874  1.00 19.34           C  
ANISOU 3368  CA  ARG A 450     2487   2539   2319      2    308   -111       C  
ATOM   3369  C   ARG A 450     -12.949  64.771  42.593  1.00 20.06           C  
ANISOU 3369  C   ARG A 450     2560   2645   2413    -23    320   -145       C  
ATOM   3370  O   ARG A 450     -12.813  65.860  43.156  1.00 20.73           O  
ANISOU 3370  O   ARG A 450     2656   2725   2494    -33    338   -167       O  
ATOM   3371  CB  ARG A 450     -15.162  63.573  42.759  1.00 20.11           C  
ANISOU 3371  CB  ARG A 450     2557   2668   2412     23    281    -88       C  
ATOM   3372  CG  ARG A 450     -15.418  64.142  44.155  1.00 19.10           C  
ANISOU 3372  CG  ARG A 450     2417   2562   2275     26    280    -99       C  
ATOM   3373  CD  ARG A 450     -16.007  65.548  44.081  1.00 24.62           C  
ANISOU 3373  CD  ARG A 450     3151   3236   2965     31    300   -106       C  
ATOM   3374  NE  ARG A 450     -16.347  66.051  45.412  1.00 25.07           N  
ANISOU 3374  NE  ARG A 450     3196   3315   3013     36    298   -114       N  
ATOM   3375  CZ  ARG A 450     -15.465  66.580  46.255  1.00 27.44           C  
ANISOU 3375  CZ  ARG A 450     3484   3628   3312     17    309   -145       C  
ATOM   3376  NH1 ARG A 450     -14.181  66.684  45.930  1.00 27.03           N  
ANISOU 3376  NH1 ARG A 450     3429   3572   3269     -8    323   -171       N  
ATOM   3377  NH2 ARG A 450     -15.875  67.006  47.438  1.00 28.45           N  
ANISOU 3377  NH2 ARG A 450     3601   3777   3431     25    305   -151       N  
ATOM   3378  N   LEU A 451     -11.998  63.841  42.574  1.00 18.67           N  
ANISOU 3378  N   LEU A 451     2358   2489   2246    -34    309   -151       N  
ATOM   3379  CA  LEU A 451     -10.722  64.020  43.257  1.00 19.78           C  
ANISOU 3379  CA  LEU A 451     2474   2652   2387    -56    317   -186       C  
ATOM   3380  C   LEU A 451      -9.806  65.018  42.549  1.00 20.22           C  
ANISOU 3380  C   LEU A 451     2553   2679   2448    -85    350   -217       C  
ATOM   3381  O   LEU A 451      -9.102  65.789  43.211  1.00 20.57           O  
ANISOU 3381  O   LEU A 451     2590   2733   2491   -105    366   -252       O  
ATOM   3382  CB  LEU A 451     -10.007  62.685  43.486  1.00 17.27           C  
ANISOU 3382  CB  LEU A 451     2120   2367   2073    -54    296   -182       C  
ATOM   3383  CG  LEU A 451     -10.668  61.868  44.604  1.00 19.30           C  
ANISOU 3383  CG  LEU A 451     2350   2659   2323    -30    270   -162       C  
ATOM   3384  CD1 LEU A 451     -10.413  60.374  44.431  1.00 17.28           C  
ANISOU 3384  CD1 LEU A 451     2073   2420   2071    -19    249   -142       C  
ATOM   3385  CD2 LEU A 451     -10.176  62.327  45.987  1.00 16.92           C  
ANISOU 3385  CD2 LEU A 451     2024   2392   2011    -34    270   -189       C  
ATOM   3386  N   THR A 452      -9.814  65.013  41.219  1.00 20.06           N  
ANISOU 3386  N   THR A 452     2560   2625   2434    -87    360   -206       N  
ATOM   3387  CA  THR A 452      -9.057  66.035  40.495  1.00 21.37           C  
ANISOU 3387  CA  THR A 452     2755   2758   2605   -113    396   -232       C  
ATOM   3388  C   THR A 452      -9.714  67.409  40.653  1.00 22.80           C  
ANISOU 3388  C   THR A 452     2973   2911   2779   -111    421   -238       C  
ATOM   3389  O   THR A 452      -9.012  68.407  40.808  1.00 22.70           O  
ANISOU 3389  O   THR A 452     2972   2885   2768   -137    452   -272       O  
ATOM   3390  CB  THR A 452      -8.716  65.690  39.018  1.00 21.86           C  
ANISOU 3390  CB  THR A 452     2838   2793   2676   -117    404   -222       C  
ATOM   3391  OG1 THR A 452      -7.772  66.651  38.534  1.00 25.92           O  
ANISOU 3391  OG1 THR A 452     3373   3281   3195   -147    441   -254       O  
ATOM   3392  CG2 THR A 452      -9.913  65.748  38.099  1.00 20.67           C  
ANISOU 3392  CG2 THR A 452     2720   2611   2519    -91    402   -188       C  
ATOM   3393  N   ALA A 453     -11.043  67.466  40.653  1.00 22.70           N  
ANISOU 3393  N   ALA A 453     2976   2890   2758    -82    410   -208       N  
ATOM   3394  CA  ALA A 453     -11.725  68.726  40.941  1.00 25.00           C  
ANISOU 3394  CA  ALA A 453     3299   3157   3039    -75    431   -212       C  
ATOM   3395  C   ALA A 453     -11.222  69.342  42.247  1.00 26.11           C  
ANISOU 3395  C   ALA A 453     3422   3320   3179    -94    440   -246       C  
ATOM   3396  O   ALA A 453     -11.000  70.556  42.324  1.00 26.30           O  
ANISOU 3396  O   ALA A 453     3472   3318   3201   -110    473   -270       O  
ATOM   3397  CB  ALA A 453     -13.229  68.541  40.998  1.00 23.58           C  
ANISOU 3397  CB  ALA A 453     3129   2979   2849    -39    412   -177       C  
ATOM   3398  N   GLU A 454     -11.037  68.495  43.257  1.00 26.30           N  
ANISOU 3398  N   GLU A 454     3399   3390   3202    -92    411   -248       N  
ATOM   3399  CA  GLU A 454     -10.589  68.942  44.568  1.00 27.39           C  
ANISOU 3399  CA  GLU A 454     3513   3558   3336   -105    414   -279       C  
ATOM   3400  C   GLU A 454      -9.087  69.174  44.687  1.00 28.62           C  
ANISOU 3400  C   GLU A 454     3649   3724   3499   -142    432   -324       C  
ATOM   3401  O   GLU A 454      -8.695  70.189  45.253  1.00 27.71           O  
ANISOU 3401  O   GLU A 454     3538   3606   3382   -163    456   -359       O  
ATOM   3402  CB  GLU A 454     -11.017  67.955  45.650  1.00 28.01           C  
ANISOU 3402  CB  GLU A 454     3549   3683   3408    -84    377   -262       C  
ATOM   3403  CG  GLU A 454     -10.455  68.308  47.015  1.00 31.23           C  
ANISOU 3403  CG  GLU A 454     3927   4128   3809    -96    377   -296       C  
ATOM   3404  CD  GLU A 454     -11.408  67.944  48.119  1.00 40.29           C  
ANISOU 3404  CD  GLU A 454     5055   5306   4946    -68    352   -275       C  
ATOM   3405  OE1 GLU A 454     -11.906  66.795  48.102  1.00 42.04           O  
ANISOU 3405  OE1 GLU A 454     5261   5543   5166    -45    324   -242       O  
ATOM   3406  OE2 GLU A 454     -11.678  68.821  48.967  1.00 44.14           O  
ANISOU 3406  OE2 GLU A 454     5546   5798   5426    -69    361   -292       O  
ATOM   3407  N   TYR A 455      -8.260  68.263  44.172  1.00 28.23           N  
ANISOU 3407  N   TYR A 455     3579   3689   3457   -150    422   -325       N  
ATOM   3408  CA  TYR A 455      -6.809  68.325  44.387  1.00 29.42           C  
ANISOU 3408  CA  TYR A 455     3703   3861   3613   -182    434   -368       C  
ATOM   3409  C   TYR A 455      -6.025  68.794  43.165  1.00 31.23           C  
ANISOU 3409  C   TYR A 455     3960   4053   3853   -210    466   -386       C  
ATOM   3410  O   TYR A 455      -4.826  69.050  43.259  1.00 31.74           O  
ANISOU 3410  O   TYR A 455     4006   4129   3921   -242    484   -427       O  
ATOM   3411  CB  TYR A 455      -6.253  67.005  44.935  1.00 28.58           C  
ANISOU 3411  CB  TYR A 455     3547   3807   3504   -172    401   -365       C  
ATOM   3412  CG  TYR A 455      -6.894  66.579  46.244  1.00 30.05           C  
ANISOU 3412  CG  TYR A 455     3705   4033   3678   -146    373   -353       C  
ATOM   3413  CD1 TYR A 455      -6.520  67.163  47.455  1.00 33.43           C  
ANISOU 3413  CD1 TYR A 455     4110   4494   4098   -156    377   -388       C  
ATOM   3414  CD2 TYR A 455      -7.874  65.592  46.274  1.00 29.12           C  
ANISOU 3414  CD2 TYR A 455     3585   3922   3558   -113    344   -307       C  
ATOM   3415  CE1 TYR A 455      -7.114  66.777  48.661  1.00 35.19           C  
ANISOU 3415  CE1 TYR A 455     4308   4753   4308   -130    352   -375       C  
ATOM   3416  CE2 TYR A 455      -8.479  65.200  47.472  1.00 31.58           C  
ANISOU 3416  CE2 TYR A 455     3873   4268   3858    -90    321   -294       C  
ATOM   3417  CZ  TYR A 455      -8.091  65.793  48.662  1.00 35.20           C  
ANISOU 3417  CZ  TYR A 455     4309   4758   4306    -97    325   -327       C  
ATOM   3418  OH  TYR A 455      -8.692  65.413  49.844  1.00 36.32           O  
ANISOU 3418  OH  TYR A 455     4429   4935   4437    -72    303   -314       O  
ATOM   3419  N   GLY A 456      -6.704  68.957  42.034  1.00 31.14           N  
ANISOU 3419  N   GLY A 456     3991   3996   3845   -198    476   -356       N  
ATOM   3420  CA  GLY A 456      -6.042  69.363  40.793  1.00 32.72           C  
ANISOU 3420  CA  GLY A 456     4221   4157   4054   -220    507   -367       C  
ATOM   3421  C   GLY A 456      -5.074  68.329  40.253  1.00 32.70           C  
ANISOU 3421  C   GLY A 456     4190   4174   4059   -230    494   -370       C  
ATOM   3422  O   GLY A 456      -5.408  67.143  40.156  1.00 33.32           O  
ANISOU 3422  O   GLY A 456     4249   4273   4136   -206    460   -340       O  
ATOM   3423  N   GLY A 457      -3.865  68.782  39.923  1.00 32.63           N  
ANISOU 3423  N   GLY A 457     4180   4160   4058   -266    523   -409       N  
ATOM   3424  CA  GLY A 457      -2.841  67.950  39.296  1.00 32.66           C  
ANISOU 3424  CA  GLY A 457     4161   4178   4068   -278    516   -418       C  
ATOM   3425  C   GLY A 457      -2.688  68.339  37.837  1.00 32.16           C  
ANISOU 3425  C   GLY A 457     4141   4063   4013   -289    546   -411       C  
ATOM   3426  O   GLY A 457      -3.587  68.944  37.250  1.00 32.87           O  
ANISOU 3426  O   GLY A 457     4277   4110   4099   -275    561   -387       O  
ATOM   3427  N   THR A 458      -1.564  67.999  37.220  1.00 32.12           N  
ANISOU 3427  N   THR A 458     4123   4064   4015   -312    555   -431       N  
ATOM   3428  CA  THR A 458      -1.403  68.360  35.810  1.00 32.24           C  
ANISOU 3428  CA  THR A 458     4181   4030   4037   -322    584   -423       C  
ATOM   3429  C   THR A 458      -1.319  67.089  34.972  1.00 28.77           C  
ANISOU 3429  C   THR A 458     3729   3600   3601   -303    556   -394       C  
ATOM   3430  O   THR A 458      -0.608  66.152  35.330  1.00 29.02           O  
ANISOU 3430  O   THR A 458     3717   3675   3635   -305    532   -404       O  
ATOM   3431  CB  THR A 458      -0.200  69.304  35.546  1.00 33.37           C  
ANISOU 3431  CB  THR A 458     4333   4157   4188   -369    632   -473       C  
ATOM   3432  OG1 THR A 458       1.013  68.585  35.776  1.00 40.27           O  
ANISOU 3432  OG1 THR A 458     5157   5076   5066   -388    619   -502       O  
ATOM   3433  CG2 THR A 458      -0.224  70.522  36.465  1.00 33.96           C  
ANISOU 3433  CG2 THR A 458     4415   4225   4260   -390    660   -506       C  
ATOM   3434  N   PRO A 459      -2.055  67.044  33.854  1.00 27.23           N  
ANISOU 3434  N   PRO A 459     3574   3366   3405   -283    559   -359       N  
ATOM   3435  CA  PRO A 459      -2.016  65.847  33.016  1.00 26.05           C  
ANISOU 3435  CA  PRO A 459     3414   3223   3259   -266    534   -332       C  
ATOM   3436  C   PRO A 459      -0.649  65.737  32.341  1.00 26.09           C  
ANISOU 3436  C   PRO A 459     3410   3229   3273   -296    553   -361       C  
ATOM   3437  O   PRO A 459       0.084  66.723  32.298  1.00 24.70           O  
ANISOU 3437  O   PRO A 459     3247   3036   3100   -329    592   -396       O  
ATOM   3438  CB  PRO A 459      -3.109  66.128  31.985  1.00 25.05           C  
ANISOU 3438  CB  PRO A 459     3337   3053   3127   -240    541   -295       C  
ATOM   3439  CG  PRO A 459      -3.131  67.634  31.883  1.00 28.56           C  
ANISOU 3439  CG  PRO A 459     3824   3456   3569   -256    587   -314       C  
ATOM   3440  CD  PRO A 459      -2.969  68.068  33.315  1.00 26.78           C  
ANISOU 3440  CD  PRO A 459     3573   3259   3343   -271    586   -341       C  
ATOM   3441  N   LEU A 460      -0.295  64.559  31.836  1.00 25.22           N  
ANISOU 3441  N   LEU A 460     3278   3137   3166   -287    528   -347       N  
ATOM   3442  CA  LEU A 460       0.969  64.382  31.138  1.00 25.06           C  
ANISOU 3442  CA  LEU A 460     3248   3118   3153   -313    544   -372       C  
ATOM   3443  C   LEU A 460       0.998  65.023  29.751  1.00 25.65           C  
ANISOU 3443  C   LEU A 460     3372   3140   3231   -321    579   -366       C  
ATOM   3444  O   LEU A 460       0.123  64.774  28.921  1.00 22.91           O  
ANISOU 3444  O   LEU A 460     3054   2768   2881   -294    571   -328       O  
ATOM   3445  CB  LEU A 460       1.266  62.898  30.968  1.00 24.77           C  
ANISOU 3445  CB  LEU A 460     3177   3116   3119   -296    507   -356       C  
ATOM   3446  CG  LEU A 460       1.855  62.084  32.114  1.00 30.15           C  
ANISOU 3446  CG  LEU A 460     3803   3854   3797   -294    479   -372       C  
ATOM   3447  CD1 LEU A 460       1.968  60.631  31.631  1.00 28.07           C  
ANISOU 3447  CD1 LEU A 460     3521   3609   3535   -272    447   -347       C  
ATOM   3448  CD2 LEU A 460       3.225  62.676  32.512  1.00 30.86           C  
ANISOU 3448  CD2 LEU A 460     3869   3966   3888   -332    503   -426       C  
ATOM   3449  N   ALA A 461       2.013  65.842  29.493  1.00 25.51           N  
ANISOU 3449  N   ALA A 461     3363   3108   3218   -359    620   -403       N  
ATOM   3450  CA  ALA A 461       2.197  66.423  28.167  1.00 26.32           C  
ANISOU 3450  CA  ALA A 461     3513   3163   3325   -369    657   -400       C  
ATOM   3451  C   ALA A 461       2.663  65.326  27.223  1.00 26.80           C  
ANISOU 3451  C   ALA A 461     3560   3233   3389   -361    638   -386       C  
ATOM   3452  O   ALA A 461       3.356  64.394  27.634  1.00 26.64           O  
ANISOU 3452  O   ALA A 461     3492   3256   3372   -365    612   -398       O  
ATOM   3453  CB  ALA A 461       3.236  67.559  28.220  1.00 28.88           C  
ANISOU 3453  CB  ALA A 461     3847   3470   3654   -416    708   -448       C  
ATOM   3454  N   ASN A 462       2.287  65.408  25.953  1.00 28.33           N  
ANISOU 3454  N   ASN A 462     3795   3387   3582   -347    651   -360       N  
ATOM   3455  CA  ASN A 462       2.799  64.427  24.989  1.00 29.66           C  
ANISOU 3455  CA  ASN A 462     3952   3562   3754   -342    637   -350       C  
ATOM   3456  C   ASN A 462       2.433  62.968  25.323  1.00 27.64           C  
ANISOU 3456  C   ASN A 462     3657   3347   3497   -313    583   -325       C  
ATOM   3457  O   ASN A 462       3.158  62.026  25.013  1.00 27.28           O  
ANISOU 3457  O   ASN A 462     3583   3324   3456   -316    566   -330       O  
ATOM   3458  CB  ASN A 462       4.314  64.620  24.805  1.00 32.23           C  
ANISOU 3458  CB  ASN A 462     4261   3897   4088   -384    664   -393       C  
ATOM   3459  CG  ASN A 462       4.690  66.074  24.466  1.00 36.70           C  
ANISOU 3459  CG  ASN A 462     4868   4419   4655   -416    723   -419       C  
ATOM   3460  OD1 ASN A 462       4.174  66.646  23.501  1.00 38.33           O  
ANISOU 3460  OD1 ASN A 462     5127   4578   4858   -405    749   -397       O  
ATOM   3461  ND2 ASN A 462       5.585  66.672  25.256  1.00 36.24           N  
ANISOU 3461  ND2 ASN A 462     4788   4378   4603   -456    747   -466       N  
ATOM   3462  N   PHE A 463       1.293  62.793  25.981  1.00 25.95           N  
ANISOU 3462  N   PHE A 463     3441   3141   3277   -286    557   -301       N  
ATOM   3463  CA  PHE A 463       0.726  61.470  26.216  1.00 23.53           C  
ANISOU 3463  CA  PHE A 463     3106   2862   2969   -256    511   -273       C  
ATOM   3464  C   PHE A 463      -0.219  61.097  25.072  1.00 23.05           C  
ANISOU 3464  C   PHE A 463     3076   2776   2906   -227    501   -235       C  
ATOM   3465  O   PHE A 463      -1.023  61.934  24.658  1.00 24.29           O  
ANISOU 3465  O   PHE A 463     3273   2900   3055   -215    519   -222       O  
ATOM   3466  CB  PHE A 463      -0.021  61.465  27.555  1.00 22.44           C  
ANISOU 3466  CB  PHE A 463     2949   2748   2826   -243    489   -268       C  
ATOM   3467  CG  PHE A 463      -0.856  60.242  27.761  1.00 17.70           C  
ANISOU 3467  CG  PHE A 463     2329   2169   2224   -211    447   -235       C  
ATOM   3468  CD1 PHE A 463      -0.282  59.070  28.223  1.00 17.77           C  
ANISOU 3468  CD1 PHE A 463     2297   2216   2238   -209    420   -237       C  
ATOM   3469  CD2 PHE A 463      -2.197  60.255  27.438  1.00 16.26           C  
ANISOU 3469  CD2 PHE A 463     2172   1967   2036   -183    437   -202       C  
ATOM   3470  CE1 PHE A 463      -1.047  57.941  28.369  1.00 16.07           C  
ANISOU 3470  CE1 PHE A 463     2068   2015   2021   -181    386   -207       C  
ATOM   3471  CE2 PHE A 463      -2.983  59.120  27.590  1.00 16.25           C  
ANISOU 3471  CE2 PHE A 463     2153   1984   2035   -157    401   -174       C  
ATOM   3472  CZ  PHE A 463      -2.396  57.964  28.050  1.00 17.97           C  
ANISOU 3472  CZ  PHE A 463     2332   2235   2258   -157    378   -177       C  
ATOM   3473  N   PRO A 464      -0.160  59.850  24.566  1.00 21.55           N  
ANISOU 3473  N   PRO A 464     2867   2601   2719   -212    473   -219       N  
ATOM   3474  CA  PRO A 464       0.748  58.758  24.927  1.00 21.22           C  
ANISOU 3474  CA  PRO A 464     2782   2596   2684   -220    452   -230       C  
ATOM   3475  C   PRO A 464       2.080  58.862  24.190  1.00 20.84           C  
ANISOU 3475  C   PRO A 464     2732   2544   2641   -246    475   -256       C  
ATOM   3476  O   PRO A 464       2.130  59.388  23.084  1.00 21.05           O  
ANISOU 3476  O   PRO A 464     2793   2536   2667   -251    500   -253       O  
ATOM   3477  CB  PRO A 464       0.005  57.499  24.465  1.00 20.12           C  
ANISOU 3477  CB  PRO A 464     2636   2462   2545   -190    418   -197       C  
ATOM   3478  CG  PRO A 464      -0.841  57.971  23.313  1.00 20.22           C  
ANISOU 3478  CG  PRO A 464     2691   2437   2552   -175    430   -176       C  
ATOM   3479  CD  PRO A 464      -1.091  59.450  23.493  1.00 20.77           C  
ANISOU 3479  CD  PRO A 464     2793   2481   2616   -184    463   -186       C  
ATOM   3480  N   PRO A 465       3.166  58.390  24.813  1.00 21.85           N  
ANISOU 3480  N   PRO A 465     2820   2709   2773   -262    468   -282       N  
ATOM   3481  CA  PRO A 465       4.415  58.358  24.073  1.00 21.32           C  
ANISOU 3481  CA  PRO A 465     2747   2641   2709   -285    487   -306       C  
ATOM   3482  C   PRO A 465       4.433  57.178  23.093  1.00 22.46           C  
ANISOU 3482  C   PRO A 465     2889   2785   2856   -266    466   -282       C  
ATOM   3483  O   PRO A 465       3.745  56.175  23.326  1.00 20.87           O  
ANISOU 3483  O   PRO A 465     2676   2598   2655   -239    432   -256       O  
ATOM   3484  CB  PRO A 465       5.457  58.164  25.171  1.00 23.20           C  
ANISOU 3484  CB  PRO A 465     2939   2926   2948   -303    481   -341       C  
ATOM   3485  CG  PRO A 465       4.726  57.442  26.253  1.00 22.30           C  
ANISOU 3485  CG  PRO A 465     2801   2841   2829   -276    445   -321       C  
ATOM   3486  CD  PRO A 465       3.331  57.995  26.224  1.00 20.63           C  
ANISOU 3486  CD  PRO A 465     2625   2597   2615   -260    446   -293       C  
ATOM   3487  N   PRO A 466       5.230  57.291  22.012  1.00 22.05           N  
ANISOU 3487  N   PRO A 466     2850   2717   2808   -282    487   -294       N  
ATOM   3488  CA  PRO A 466       5.337  56.230  21.013  1.00 20.74           C  
ANISOU 3488  CA  PRO A 466     2683   2551   2646   -266    470   -275       C  
ATOM   3489  C   PRO A 466       5.903  54.940  21.613  1.00 21.36           C  
ANISOU 3489  C   PRO A 466     2716   2673   2725   -257    438   -278       C  
ATOM   3490  O   PRO A 466       6.741  54.996  22.513  1.00 20.49           O  
ANISOU 3490  O   PRO A 466     2574   2596   2614   -272    439   -306       O  
ATOM   3491  CB  PRO A 466       6.293  56.801  19.965  1.00 21.24           C  
ANISOU 3491  CB  PRO A 466     2764   2593   2711   -291    505   -296       C  
ATOM   3492  CG  PRO A 466       6.946  58.012  20.591  1.00 22.73           C  
ANISOU 3492  CG  PRO A 466     2953   2782   2901   -325    539   -333       C  
ATOM   3493  CD  PRO A 466       6.046  58.482  21.691  1.00 23.27           C  
ANISOU 3493  CD  PRO A 466     3022   2853   2965   -317    531   -326       C  
ATOM   3494  N   GLU A 467       5.415  53.795  21.144  1.00 19.65           N  
ANISOU 3494  N   GLU A 467     2497   2457   2509   -231    411   -250       N  
ATOM   3495  CA  GLU A 467       5.899  52.490  21.598  1.00 20.81           C  
ANISOU 3495  CA  GLU A 467     2608   2641   2658   -218    383   -248       C  
ATOM   3496  C   GLU A 467       7.080  52.027  20.756  1.00 21.57           C  
ANISOU 3496  C   GLU A 467     2694   2743   2756   -228    389   -263       C  
ATOM   3497  O   GLU A 467       7.220  52.406  19.595  1.00 21.32           O  
ANISOU 3497  O   GLU A 467     2688   2684   2728   -237    408   -263       O  
ATOM   3498  CB  GLU A 467       4.787  51.439  21.493  1.00 20.65           C  
ANISOU 3498  CB  GLU A 467     2591   2614   2638   -187    353   -211       C  
ATOM   3499  CG  GLU A 467       3.711  51.618  22.562  1.00 18.80           C  
ANISOU 3499  CG  GLU A 467     2356   2384   2401   -174    340   -196       C  
ATOM   3500  CD  GLU A 467       2.525  50.686  22.406  1.00 20.37           C  
ANISOU 3500  CD  GLU A 467     2561   2575   2602   -147    316   -162       C  
ATOM   3501  OE1 GLU A 467       2.495  49.861  21.456  1.00 17.98           O  
ANISOU 3501  OE1 GLU A 467     2264   2263   2303   -138    308   -149       O  
ATOM   3502  OE2 GLU A 467       1.609  50.804  23.259  1.00 14.67           O  
ANISOU 3502  OE2 GLU A 467     1838   1857   1877   -137    306   -150       O  
ATOM   3503  N   GLN A 468       7.927  51.201  21.354  1.00 23.23           N  
ANISOU 3503  N   GLN A 468     2867   2993   2964   -224    374   -276       N  
ATOM   3504  CA  GLN A 468       8.943  50.466  20.615  1.00 25.31           C  
ANISOU 3504  CA  GLN A 468     3118   3269   3230   -225    372   -286       C  
ATOM   3505  C   GLN A 468       8.245  49.346  19.833  1.00 24.70           C  
ANISOU 3505  C   GLN A 468     3054   3174   3156   -199    351   -250       C  
ATOM   3506  O   GLN A 468       7.379  48.662  20.368  1.00 24.04           O  
ANISOU 3506  O   GLN A 468     2967   3094   3073   -176    328   -226       O  
ATOM   3507  CB  GLN A 468       9.969  49.942  21.632  1.00 27.03           C  
ANISOU 3507  CB  GLN A 468     3290   3538   3440   -223    361   -309       C  
ATOM   3508  CG  GLN A 468      10.650  48.620  21.301  1.00 36.81           C  
ANISOU 3508  CG  GLN A 468     4509   4799   4677   -204    342   -304       C  
ATOM   3509  CD  GLN A 468      11.544  48.686  20.073  1.00 48.37           C  
ANISOU 3509  CD  GLN A 468     5979   6252   6144   -221    359   -320       C  
ATOM   3510  OE1 GLN A 468      11.532  49.670  19.327  1.00 51.38           O  
ANISOU 3510  OE1 GLN A 468     6386   6605   6531   -245    386   -329       O  
ATOM   3511  NE2 GLN A 468      12.318  47.620  19.848  1.00 50.75           N  
ANISOU 3511  NE2 GLN A 468     6259   6578   6443   -207    346   -322       N  
ATOM   3512  N   ARG A 469       8.564  49.195  18.554  1.00 24.71           N  
ANISOU 3512  N   ARG A 469     3070   3155   3160   -203    360   -249       N  
ATOM   3513  CA  ARG A 469       7.896  48.217  17.693  1.00 26.18           C  
ANISOU 3513  CA  ARG A 469     3271   3323   3351   -180    343   -219       C  
ATOM   3514  C   ARG A 469       8.849  47.076  17.322  1.00 27.07           C  
ANISOU 3514  C   ARG A 469     3363   3457   3465   -172    331   -224       C  
ATOM   3515  O   ARG A 469      10.063  47.281  17.284  1.00 28.47           O  
ANISOU 3515  O   ARG A 469     3523   3654   3639   -188    344   -251       O  
ATOM   3516  CB  ARG A 469       7.396  48.881  16.401  1.00 25.48           C  
ANISOU 3516  CB  ARG A 469     3221   3195   3265   -186    361   -210       C  
ATOM   3517  CG  ARG A 469       6.375  50.004  16.581  1.00 25.82           C  
ANISOU 3517  CG  ARG A 469     3290   3213   3304   -188    373   -202       C  
ATOM   3518  CD  ARG A 469       5.812  50.534  15.263  1.00 27.39           C  
ANISOU 3518  CD  ARG A 469     3529   3375   3502   -185    389   -189       C  
ATOM   3519  NE  ARG A 469       4.957  51.686  15.540  1.00 30.80           N  
ANISOU 3519  NE  ARG A 469     3986   3786   3928   -186    404   -184       N  
ATOM   3520  CZ  ARG A 469       4.136  52.270  14.672  1.00 33.31           C  
ANISOU 3520  CZ  ARG A 469     4340   4073   4240   -175    416   -168       C  
ATOM   3521  NH1 ARG A 469       4.030  51.818  13.428  1.00 30.43           N  
ANISOU 3521  NH1 ARG A 469     3990   3695   3874   -163    414   -156       N  
ATOM   3522  NH2 ARG A 469       3.397  53.303  15.059  1.00 28.94           N  
ANISOU 3522  NH2 ARG A 469     3809   3505   3681   -174    429   -164       N  
ATOM   3523  N   ASP A 470       8.302  45.894  17.040  1.00 26.60           N  
ANISOU 3523  N   ASP A 470     3305   3393   3409   -149    309   -199       N  
ATOM   3524  CA  ASP A 470       9.020  44.802  16.379  1.00 27.08           C  
ANISOU 3524  CA  ASP A 470     3356   3462   3471   -139    300   -198       C  
ATOM   3525  C   ASP A 470       8.732  44.786  14.882  1.00 27.20           C  
ANISOU 3525  C   ASP A 470     3398   3445   3491   -140    307   -188       C  
ATOM   3526  O   ASP A 470       7.790  45.432  14.402  1.00 24.89           O  
ANISOU 3526  O   ASP A 470     3132   3124   3199   -142    314   -176       O  
ATOM   3527  CB  ASP A 470       8.536  43.440  16.878  1.00 28.99           C  
ANISOU 3527  CB  ASP A 470     3587   3713   3714   -111    275   -176       C  
ATOM   3528  CG  ASP A 470       8.552  43.333  18.378  1.00 33.97           C  
ANISOU 3528  CG  ASP A 470     4194   4372   4338   -103    265   -178       C  
ATOM   3529  OD1 ASP A 470       9.569  43.784  18.950  1.00 40.50           O  
ANISOU 3529  OD1 ASP A 470     5000   5229   5159   -113    273   -204       O  
ATOM   3530  OD2 ASP A 470       7.561  42.810  18.943  1.00 34.70           O  
ANISOU 3530  OD2 ASP A 470     4291   4459   4433    -86    251   -155       O  
ATOM   3531  N   ASP A 471       9.511  43.993  14.148  1.00 25.71           N  
ANISOU 3531  N   ASP A 471     3202   3262   3303   -136    304   -192       N  
ATOM   3532  CA  ASP A 471       9.244  43.820  12.724  1.00 24.84           C  
ANISOU 3532  CA  ASP A 471     3116   3125   3196   -133    308   -182       C  
ATOM   3533  C   ASP A 471       7.907  43.110  12.570  1.00 21.55           C  
ANISOU 3533  C   ASP A 471     2712   2691   2784   -113    289   -154       C  
ATOM   3534  O   ASP A 471       7.597  42.188  13.312  1.00 20.78           O  
ANISOU 3534  O   ASP A 471     2600   2605   2689    -98    271   -143       O  
ATOM   3535  CB  ASP A 471      10.330  42.972  12.059  1.00 26.52           C  
ANISOU 3535  CB  ASP A 471     3316   3350   3410   -130    306   -192       C  
ATOM   3536  CG  ASP A 471      11.702  43.611  12.142  1.00 28.42           C  
ANISOU 3536  CG  ASP A 471     3540   3612   3646   -151    325   -223       C  
ATOM   3537  OD1 ASP A 471      11.787  44.824  11.871  1.00 28.89           O  
ANISOU 3537  OD1 ASP A 471     3614   3657   3704   -173    349   -236       O  
ATOM   3538  OD2 ASP A 471      12.674  42.883  12.443  1.00 34.12           O  
ANISOU 3538  OD2 ASP A 471     4235   4363   4364   -145    318   -235       O  
ATOM   3539  N   GLU A 472       7.121  43.519  11.582  1.00 20.35           N  
ANISOU 3539  N   GLU A 472     2587   2512   2633   -112    295   -144       N  
ATOM   3540  CA  GLU A 472       5.737  43.049  11.471  1.00 18.40           C  
ANISOU 3540  CA  GLU A 472     2352   2251   2388    -95    279   -122       C  
ATOM   3541  C   GLU A 472       5.540  42.120  10.269  1.00 18.80           C  
ANISOU 3541  C   GLU A 472     2410   2290   2443    -83    271   -113       C  
ATOM   3542  O   GLU A 472       4.897  41.080  10.392  1.00 18.51           O  
ANISOU 3542  O   GLU A 472     2368   2254   2411    -70    253   -101       O  
ATOM   3543  CB  GLU A 472       4.817  44.263  11.369  1.00 18.97           C  
ANISOU 3543  CB  GLU A 472     2446   2304   2454    -98    291   -117       C  
ATOM   3544  CG  GLU A 472       4.790  45.113  12.643  1.00 19.79           C  
ANISOU 3544  CG  GLU A 472     2543   2418   2555   -108    297   -123       C  
ATOM   3545  CD  GLU A 472       3.872  46.315  12.493  1.00 19.94           C  
ANISOU 3545  CD  GLU A 472     2588   2418   2568   -109    310   -117       C  
ATOM   3546  OE1 GLU A 472       4.233  47.255  11.749  1.00 18.12           O  
ANISOU 3546  OE1 GLU A 472     2379   2172   2333   -119    334   -126       O  
ATOM   3547  OE2 GLU A 472       2.772  46.292  13.080  1.00 16.61           O  
ANISOU 3547  OE2 GLU A 472     2168   1996   2146    -98    298   -104       O  
ATOM   3548  N   PHE A 473       6.126  42.488   9.129  1.00 16.53           N  
ANISOU 3548  N   PHE A 473     2135   1992   2151    -89    285   -122       N  
ATOM   3549  CA  PHE A 473       6.028  41.708   7.904  1.00 15.99           C  
ANISOU 3549  CA  PHE A 473     2075   1914   2084    -79    278   -117       C  
ATOM   3550  C   PHE A 473       7.452  41.349   7.512  1.00 16.48           C  
ANISOU 3550  C   PHE A 473     2126   1987   2148    -86    285   -132       C  
ATOM   3551  O   PHE A 473       8.294  42.236   7.400  1.00 18.85           O  
ANISOU 3551  O   PHE A 473     2429   2289   2443   -102    305   -147       O  
ATOM   3552  CB  PHE A 473       5.348  42.518   6.790  1.00 15.04           C  
ANISOU 3552  CB  PHE A 473     1984   1773   1957    -75    290   -112       C  
ATOM   3553  CG  PHE A 473       3.874  42.754   7.025  1.00 16.38           C  
ANISOU 3553  CG  PHE A 473     2163   1935   2123    -64    280    -98       C  
ATOM   3554  CD1 PHE A 473       3.436  43.856   7.756  1.00 15.79           C  
ANISOU 3554  CD1 PHE A 473     2097   1858   2043    -69    290    -96       C  
ATOM   3555  CD2 PHE A 473       2.929  41.852   6.543  1.00 17.09           C  
ANISOU 3555  CD2 PHE A 473     2252   2023   2215    -48    262    -88       C  
ATOM   3556  CE1 PHE A 473       2.076  44.084   7.968  1.00 14.99           C  
ANISOU 3556  CE1 PHE A 473     2004   1752   1938    -56    281    -84       C  
ATOM   3557  CE2 PHE A 473       1.571  42.063   6.744  1.00 14.51           C  
ANISOU 3557  CE2 PHE A 473     1932   1694   1885    -38    254    -77       C  
ATOM   3558  CZ  PHE A 473       1.142  43.178   7.475  1.00 16.55           C  
ANISOU 3558  CZ  PHE A 473     2199   1950   2137    -41    263    -75       C  
ATOM   3559  N   PHE A 474       7.731  40.063   7.308  1.00 15.58           N  
ANISOU 3559  N   PHE A 474     2000   1879   2039    -75    271   -129       N  
ATOM   3560  CA  PHE A 474       9.100  39.603   7.060  1.00 17.25           C  
ANISOU 3560  CA  PHE A 474     2197   2105   2250    -79    275   -143       C  
ATOM   3561  C   PHE A 474       9.134  38.143   6.620  1.00 15.34           C  
ANISOU 3561  C   PHE A 474     1949   1864   2014    -63    259   -136       C  
ATOM   3562  O   PHE A 474       8.229  37.373   6.929  1.00 14.84           O  
ANISOU 3562  O   PHE A 474     1886   1794   1956    -51    244   -121       O  
ATOM   3563  CB  PHE A 474      10.014  39.779   8.283  1.00 16.78           C  
ANISOU 3563  CB  PHE A 474     2113   2072   2188    -86    278   -156       C  
ATOM   3564  CG  PHE A 474       9.508  39.131   9.547  1.00 18.77           C  
ANISOU 3564  CG  PHE A 474     2351   2336   2443    -74    261   -145       C  
ATOM   3565  CD1 PHE A 474       9.843  37.818   9.858  1.00 17.30           C  
ANISOU 3565  CD1 PHE A 474     2151   2162   2260    -57    247   -140       C  
ATOM   3566  CD2 PHE A 474       8.751  39.857  10.457  1.00 20.59           C  
ANISOU 3566  CD2 PHE A 474     2583   2565   2672    -79    261   -140       C  
ATOM   3567  CE1 PHE A 474       9.408  37.214  11.038  1.00 17.19           C  
ANISOU 3567  CE1 PHE A 474     2127   2158   2247    -44    234   -128       C  
ATOM   3568  CE2 PHE A 474       8.303  39.266  11.638  1.00 22.47           C  
ANISOU 3568  CE2 PHE A 474     2809   2815   2913    -67    247   -129       C  
ATOM   3569  CZ  PHE A 474       8.641  37.947  11.937  1.00 23.69           C  
ANISOU 3569  CZ  PHE A 474     2950   2980   3069    -49    235   -123       C  
ATOM   3570  N   VAL A 475      10.169  37.785   5.866  1.00 15.87           N  
ANISOU 3570  N   VAL A 475     2013   1937   2080    -63    264   -147       N  
ATOM   3571  CA  VAL A 475      10.393  36.378   5.563  1.00 15.74           C  
ANISOU 3571  CA  VAL A 475     1989   1922   2069    -48    250   -142       C  
ATOM   3572  C   VAL A 475      11.251  35.731   6.652  1.00 16.35           C  
ANISOU 3572  C   VAL A 475     2042   2024   2144    -40    244   -146       C  
ATOM   3573  O   VAL A 475      12.232  36.319   7.101  1.00 15.91           O  
ANISOU 3573  O   VAL A 475     1971   1990   2081    -49    254   -162       O  
ATOM   3574  CB  VAL A 475      11.024  36.194   4.161  1.00 16.76           C  
ANISOU 3574  CB  VAL A 475     2126   2045   2196    -48    257   -150       C  
ATOM   3575  CG1 VAL A 475      11.387  34.729   3.920  1.00 14.97           C  
ANISOU 3575  CG1 VAL A 475     1892   1822   1974    -32    244   -147       C  
ATOM   3576  CG2 VAL A 475      10.036  36.650   3.088  1.00 12.96           C  
ANISOU 3576  CG2 VAL A 475     1669   1540   1713    -48    260   -143       C  
ATOM   3577  N   GLU A 476      10.846  34.544   7.096  1.00 16.42           N  
ANISOU 3577  N   GLU A 476     2047   2031   2158    -23    230   -133       N  
ATOM   3578  CA  GLU A 476      11.745  33.605   7.751  1.00 17.60           C  
ANISOU 3578  CA  GLU A 476     2180   2202   2305     -7    225   -135       C  
ATOM   3579  C   GLU A 476      12.052  32.511   6.732  1.00 18.28           C  
ANISOU 3579  C   GLU A 476     2271   2278   2394      4    221   -134       C  
ATOM   3580  O   GLU A 476      11.127  31.944   6.128  1.00 16.62           O  
ANISOU 3580  O   GLU A 476     2077   2044   2193      7    216   -123       O  
ATOM   3581  CB  GLU A 476      11.078  32.916   8.941  1.00 17.91           C  
ANISOU 3581  CB  GLU A 476     2216   2242   2347      7    215   -119       C  
ATOM   3582  CG  GLU A 476      10.757  33.815  10.135  1.00 20.87           C  
ANISOU 3582  CG  GLU A 476     2582   2629   2717      0    216   -119       C  
ATOM   3583  CD  GLU A 476       9.925  33.040  11.139  1.00 24.30           C  
ANISOU 3583  CD  GLU A 476     3017   3058   3155     15    208   -100       C  
ATOM   3584  OE1 GLU A 476       8.819  32.561  10.788  1.00 28.72           O  
ANISOU 3584  OE1 GLU A 476     3592   3593   3725     16    204    -86       O  
ATOM   3585  OE2 GLU A 476      10.416  32.860  12.265  1.00 26.45           O  
ANISOU 3585  OE2 GLU A 476     3274   3354   3419     27    206   -100       O  
ATOM   3586  N   ALA A 477      13.341  32.217   6.558  1.00 16.30           N  
ANISOU 3586  N   ALA A 477     2008   2048   2137     10    224   -147       N  
ATOM   3587  CA  ALA A 477      13.764  31.234   5.566  1.00 16.53           C  
ANISOU 3587  CA  ALA A 477     2043   2070   2168     21    222   -147       C  
ATOM   3588  C   ALA A 477      14.791  30.248   6.130  1.00 17.85           C  
ANISOU 3588  C   ALA A 477     2194   2260   2328     44    218   -150       C  
ATOM   3589  O   ALA A 477      15.524  30.547   7.086  1.00 18.11           O  
ANISOU 3589  O   ALA A 477     2207   2323   2350     49    219   -158       O  
ATOM   3590  CB  ALA A 477      14.314  31.943   4.315  1.00 14.55           C  
ANISOU 3590  CB  ALA A 477     1796   1816   1914      6    232   -162       C  
ATOM   3591  N   ALA A 478      14.815  29.065   5.523  1.00 18.19           N  
ANISOU 3591  N   ALA A 478     2246   2289   2375     60    214   -143       N  
ATOM   3592  CA  ALA A 478      15.798  28.038   5.835  1.00 17.50           C  
ANISOU 3592  CA  ALA A 478     2149   2220   2280     86    212   -144       C  
ATOM   3593  C   ALA A 478      16.219  27.334   4.545  1.00 18.81           C  
ANISOU 3593  C   ALA A 478     2323   2374   2448     92    212   -149       C  
ATOM   3594  O   ALA A 478      15.461  27.287   3.568  1.00 16.27           O  
ANISOU 3594  O   ALA A 478     2018   2025   2137     80    213   -145       O  
ATOM   3595  CB  ALA A 478      15.224  27.049   6.830  1.00 18.91           C  
ANISOU 3595  CB  ALA A 478     2334   2390   2461    109    207   -124       C  
ATOM   3596  N   ILE A 479      17.460  26.856   4.538  1.00 18.58           N  
ANISOU 3596  N   ILE A 479     2280   2370   2407    109    213   -159       N  
ATOM   3597  CA  ILE A 479      17.936  25.983   3.485  1.00 19.57           C  
ANISOU 3597  CA  ILE A 479     2413   2487   2534    121    213   -162       C  
ATOM   3598  C   ILE A 479      17.307  24.622   3.733  1.00 20.96           C  
ANISOU 3598  C   ILE A 479     2607   2639   2718    143    210   -142       C  
ATOM   3599  O   ILE A 479      17.694  23.896   4.662  1.00 21.25           O  
ANISOU 3599  O   ILE A 479     2639   2688   2746    170    209   -134       O  
ATOM   3600  CB  ILE A 479      19.471  25.855   3.443  1.00 19.52           C  
ANISOU 3600  CB  ILE A 479     2386   2519   2512    135    215   -179       C  
ATOM   3601  CG1 ILE A 479      20.120  27.226   3.235  1.00 20.73           C  
ANISOU 3601  CG1 ILE A 479     2520   2695   2658    109    223   -201       C  
ATOM   3602  CG2 ILE A 479      19.866  24.886   2.316  1.00 16.73           C  
ANISOU 3602  CG2 ILE A 479     2043   2152   2160    148    215   -180       C  
ATOM   3603  CD1 ILE A 479      21.581  27.344   3.711  1.00 21.03           C  
ANISOU 3603  CD1 ILE A 479     2529   2782   2678    119    225   -222       C  
ATOM   3604  N   ASN A 480      16.327  24.292   2.898  1.00 20.36           N  
ANISOU 3604  N   ASN A 480     2550   2527   2656    132    210   -136       N  
ATOM   3605  CA  ASN A 480      15.684  22.991   2.976  1.00 22.14           C  
ANISOU 3605  CA  ASN A 480     2795   2725   2892    148    210   -121       C  
ATOM   3606  C   ASN A 480      16.604  21.890   2.463  1.00 24.18           C  
ANISOU 3606  C   ASN A 480     3057   2985   3145    172    212   -124       C  
ATOM   3607  O   ASN A 480      16.669  20.812   3.046  1.00 25.59           O  
ANISOU 3607  O   ASN A 480     3244   3155   3322    198    215   -112       O  
ATOM   3608  CB  ASN A 480      14.367  22.993   2.206  1.00 23.06           C  
ANISOU 3608  CB  ASN A 480     2928   2807   3024    127    209   -118       C  
ATOM   3609  CG  ASN A 480      13.395  21.951   2.719  1.00 27.51           C  
ANISOU 3609  CG  ASN A 480     3508   3342   3600    135    212   -103       C  
ATOM   3610  OD1 ASN A 480      13.127  21.872   3.917  1.00 32.25           O  
ANISOU 3610  OD1 ASN A 480     4108   3946   4199    143    214    -91       O  
ATOM   3611  ND2 ASN A 480      12.875  21.137   1.814  1.00 34.72           N  
ANISOU 3611  ND2 ASN A 480     4436   4228   4525    132    215   -106       N  
ATOM   3612  N   GLN A 481      17.323  22.154   1.377  1.00 24.27           N  
ANISOU 3612  N   GLN A 481     3062   3005   3152    166    212   -139       N  
ATOM   3613  CA  GLN A 481      18.323  21.213   0.878  1.00 26.09           C  
ANISOU 3613  CA  GLN A 481     3293   3243   3375    190    214   -144       C  
ATOM   3614  C   GLN A 481      19.281  21.997   0.002  1.00 26.04           C  
ANISOU 3614  C   GLN A 481     3272   3261   3361    178    214   -164       C  
ATOM   3615  O   GLN A 481      18.850  22.886  -0.739  1.00 25.82           O  
ANISOU 3615  O   GLN A 481     3245   3225   3338    152    214   -171       O  
ATOM   3616  CB  GLN A 481      17.671  20.074   0.084  1.00 26.42           C  
ANISOU 3616  CB  GLN A 481     3359   3247   3431    194    216   -139       C  
ATOM   3617  CG  GLN A 481      18.678  19.043  -0.431  1.00 31.48           C  
ANISOU 3617  CG  GLN A 481     4003   3891   4064    221    219   -143       C  
ATOM   3618  CD  GLN A 481      18.050  17.832  -1.099  1.00 36.17           C  
ANISOU 3618  CD  GLN A 481     4622   4446   4672    226    224   -138       C  
ATOM   3619  OE1 GLN A 481      16.830  17.740  -1.264  1.00 35.83           O  
ANISOU 3619  OE1 GLN A 481     4592   4374   4646    207    225   -134       O  
ATOM   3620  NE2 GLN A 481      18.900  16.892  -1.500  1.00 40.29           N  
ANISOU 3620  NE2 GLN A 481     5149   4969   5187    251    227   -140       N  
ATOM   3621  N   ALA A 482      20.571  21.705   0.127  1.00 25.69           N  
ANISOU 3621  N   ALA A 482     3211   3246   3300    199    214   -173       N  
ATOM   3622  CA  ALA A 482      21.569  22.243  -0.779  1.00 26.10           C  
ANISOU 3622  CA  ALA A 482     3250   3322   3345    190    217   -193       C  
ATOM   3623  C   ALA A 482      22.236  21.101  -1.545  1.00 27.87           C  
ANISOU 3623  C   ALA A 482     3480   3542   3565    214    217   -196       C  
ATOM   3624  O   ALA A 482      22.721  20.126  -0.964  1.00 28.31           O  
ANISOU 3624  O   ALA A 482     3536   3606   3612    247    216   -189       O  
ATOM   3625  CB  ALA A 482      22.602  23.062  -0.028  1.00 27.60           C  
ANISOU 3625  CB  ALA A 482     3410   3557   3518    190    218   -208       C  
ATOM   3626  N   SER A 483      22.256  21.232  -2.866  1.00 26.72           N  
ANISOU 3626  N   SER A 483     3341   3384   3424    200    219   -205       N  
ATOM   3627  CA  SER A 483      22.823  20.201  -3.719  1.00 24.90           C  
ANISOU 3627  CA  SER A 483     3119   3149   3193    220    219   -209       C  
ATOM   3628  C   SER A 483      23.881  20.832  -4.617  1.00 23.89           C  
ANISOU 3628  C   SER A 483     2975   3048   3055    210    223   -229       C  
ATOM   3629  O   SER A 483      23.971  22.061  -4.733  1.00 20.98           O  
ANISOU 3629  O   SER A 483     2594   2692   2684    184    227   -240       O  
ATOM   3630  CB  SER A 483      21.676  19.522  -4.476  1.00 25.09           C  
ANISOU 3630  CB  SER A 483     3170   3128   3234    214    219   -200       C  
ATOM   3631  OG  SER A 483      21.976  19.268  -5.826  1.00 26.00           O  
ANISOU 3631  OG  SER A 483     3291   3237   3350    211    220   -210       O  
ATOM   3632  N   ASP A 484      24.689  20.005  -5.269  1.00 23.20           N  
ANISOU 3632  N   ASP A 484     2888   2967   2960    231    223   -236       N  
ATOM   3633  CA  ASP A 484      25.667  20.575  -6.191  1.00 23.85           C  
ANISOU 3633  CA  ASP A 484     2955   3073   3033    221    228   -256       C  
ATOM   3634  C   ASP A 484      25.017  21.118  -7.467  1.00 21.39           C  
ANISOU 3634  C   ASP A 484     2658   2735   2732    194    231   -259       C  
ATOM   3635  O   ASP A 484      25.690  21.742  -8.287  1.00 20.24           O  
ANISOU 3635  O   ASP A 484     2503   2605   2580    181    238   -274       O  
ATOM   3636  CB  ASP A 484      26.799  19.591  -6.481  1.00 27.67           C  
ANISOU 3636  CB  ASP A 484     3431   3576   3504    252    227   -263       C  
ATOM   3637  CG  ASP A 484      26.298  18.214  -6.869  1.00 31.37           C  
ANISOU 3637  CG  ASP A 484     3927   4011   3982    275    224   -250       C  
ATOM   3638  OD1 ASP A 484      25.121  18.090  -7.273  1.00 32.13           O  
ANISOU 3638  OD1 ASP A 484     4044   4067   4094    260    223   -240       O  
ATOM   3639  OD2 ASP A 484      27.101  17.255  -6.766  1.00 38.47           O  
ANISOU 3639  OD2 ASP A 484     4823   4922   4869    308    224   -251       O  
ATOM   3640  N   HIS A 485      23.703  20.946  -7.604  1.00 18.38           N  
ANISOU 3640  N   HIS A 485     2298   2317   2366    185    228   -245       N  
ATOM   3641  CA  HIS A 485      23.006  21.555  -8.738  1.00 18.53           C  
ANISOU 3641  CA  HIS A 485     2330   2317   2393    163    230   -248       C  
ATOM   3642  C   HIS A 485      21.734  22.336  -8.409  1.00 18.25           C  
ANISOU 3642  C   HIS A 485     2304   2263   2367    141    229   -239       C  
ATOM   3643  O   HIS A 485      21.022  22.732  -9.333  1.00 14.85           O  
ANISOU 3643  O   HIS A 485     1886   1815   1941    128    230   -240       O  
ATOM   3644  CB  HIS A 485      22.749  20.552  -9.873  1.00 17.55           C  
ANISOU 3644  CB  HIS A 485     2222   2170   2274    173    227   -249       C  
ATOM   3645  CG  HIS A 485      21.588  19.633  -9.644  1.00 19.57           C  
ANISOU 3645  CG  HIS A 485     2496   2392   2544    179    221   -237       C  
ATOM   3646  ND1 HIS A 485      21.688  18.459  -8.926  1.00 22.16           N  
ANISOU 3646  ND1 HIS A 485     2830   2713   2875    203    220   -229       N  
ATOM   3647  CD2 HIS A 485      20.300  19.712 -10.061  1.00 18.40           C  
ANISOU 3647  CD2 HIS A 485     2363   2219   2409    165    218   -234       C  
ATOM   3648  CE1 HIS A 485      20.512  17.855  -8.909  1.00 21.92           C  
ANISOU 3648  CE1 HIS A 485     2817   2650   2859    199    218   -221       C  
ATOM   3649  NE2 HIS A 485      19.651  18.596  -9.587  1.00 25.35           N  
ANISOU 3649  NE2 HIS A 485     3255   3075   3299    176    216   -225       N  
ATOM   3650  N   PHE A 486      21.464  22.568  -7.123  1.00 18.76           N  
ANISOU 3650  N   PHE A 486     2362   2332   2432    141    227   -230       N  
ATOM   3651  CA  PHE A 486      20.293  23.364  -6.733  1.00 18.34           C  
ANISOU 3651  CA  PHE A 486     2316   2264   2387    121    226   -222       C  
ATOM   3652  C   PHE A 486      20.324  23.912  -5.314  1.00 18.84           C  
ANISOU 3652  C   PHE A 486     2367   2343   2448    118    227   -216       C  
ATOM   3653  O   PHE A 486      21.085  23.441  -4.462  1.00 18.32           O  
ANISOU 3653  O   PHE A 486     2288   2298   2375    136    225   -217       O  
ATOM   3654  CB  PHE A 486      18.968  22.635  -6.984  1.00 17.20           C  
ANISOU 3654  CB  PHE A 486     2191   2085   2256    123    220   -211       C  
ATOM   3655  CG  PHE A 486      18.692  21.438  -6.103  1.00 17.46           C  
ANISOU 3655  CG  PHE A 486     2229   2107   2296    141    216   -200       C  
ATOM   3656  CD1 PHE A 486      18.210  21.591  -4.800  1.00 17.20           C  
ANISOU 3656  CD1 PHE A 486     2193   2074   2266    141    215   -188       C  
ATOM   3657  CD2 PHE A 486      18.796  20.152  -6.628  1.00 14.52           C  
ANISOU 3657  CD2 PHE A 486     1868   1720   1929    158    215   -200       C  
ATOM   3658  CE1 PHE A 486      17.904  20.479  -4.021  1.00 17.28           C  
ANISOU 3658  CE1 PHE A 486     2212   2070   2282    159    214   -176       C  
ATOM   3659  CE2 PHE A 486      18.479  19.027  -5.861  1.00 17.88           C  
ANISOU 3659  CE2 PHE A 486     2303   2128   2361    175    216   -189       C  
ATOM   3660  CZ  PHE A 486      18.037  19.186  -4.557  1.00 21.95           C  
ANISOU 3660  CZ  PHE A 486     2817   2644   2879    176    216   -176       C  
ATOM   3661  N   THR A 487      19.512  24.948  -5.119  1.00 17.41           N  
ANISOU 3661  N   THR A 487     2189   2153   2270     97    229   -213       N  
ATOM   3662  CA  THR A 487      19.146  25.451  -3.805  1.00 16.58           C  
ANISOU 3662  CA  THR A 487     2077   2055   2165     92    228   -205       C  
ATOM   3663  C   THR A 487      17.653  25.230  -3.634  1.00 16.84           C  
ANISOU 3663  C   THR A 487     2127   2059   2211     88    222   -191       C  
ATOM   3664  O   THR A 487      16.856  25.596  -4.501  1.00 17.10           O  
ANISOU 3664  O   THR A 487     2172   2074   2248     77    222   -191       O  
ATOM   3665  CB  THR A 487      19.385  26.967  -3.711  1.00 15.81           C  
ANISOU 3665  CB  THR A 487     1972   1973   2062     69    238   -215       C  
ATOM   3666  OG1 THR A 487      20.785  27.218  -3.834  1.00 18.75           O  
ANISOU 3666  OG1 THR A 487     2326   2375   2423     68    246   -232       O  
ATOM   3667  CG2 THR A 487      18.897  27.502  -2.364  1.00 13.17           C  
ANISOU 3667  CG2 THR A 487     1630   1644   1729     63    236   -208       C  
ATOM   3668  N   GLU A 488      17.277  24.661  -2.497  1.00 15.33           N  
ANISOU 3668  N   GLU A 488     1934   1865   2024     99    217   -179       N  
ATOM   3669  CA  GLU A 488      15.876  24.531  -2.169  1.00 15.42           C  
ANISOU 3669  CA  GLU A 488     1958   1851   2046     93    213   -167       C  
ATOM   3670  C   GLU A 488      15.631  25.267  -0.864  1.00 15.95           C  
ANISOU 3670  C   GLU A 488     2017   1931   2112     87    213   -160       C  
ATOM   3671  O   GLU A 488      16.291  24.980   0.132  1.00 15.26           O  
ANISOU 3671  O   GLU A 488     1917   1861   2017    101    213   -157       O  
ATOM   3672  CB  GLU A 488      15.509  23.059  -2.004  1.00 16.24           C  
ANISOU 3672  CB  GLU A 488     2074   1936   2161    111    210   -158       C  
ATOM   3673  CG  GLU A 488      14.007  22.849  -1.818  1.00 20.25           C  
ANISOU 3673  CG  GLU A 488     2594   2418   2682    101    208   -148       C  
ATOM   3674  CD  GLU A 488      13.699  21.377  -1.930  1.00 29.73           C  
ANISOU 3674  CD  GLU A 488     3807   3594   3892    114    209   -144       C  
ATOM   3675  OE1 GLU A 488      13.914  20.681  -0.919  1.00 34.02           O  
ANISOU 3675  OE1 GLU A 488     4353   4136   4435    131    213   -133       O  
ATOM   3676  OE2 GLU A 488      13.310  20.923  -3.029  1.00 32.86           O  
ANISOU 3676  OE2 GLU A 488     4214   3975   4296    110    209   -152       O  
ATOM   3677  N   ILE A 489      14.681  26.194  -0.897  1.00 15.71           N  
ANISOU 3677  N   ILE A 489     1992   1891   2085     69    213   -157       N  
ATOM   3678  CA  ILE A 489      14.371  27.073   0.222  1.00 15.87           C  
ANISOU 3678  CA  ILE A 489     2004   1920   2103     60    214   -152       C  
ATOM   3679  C   ILE A 489      12.991  26.780   0.796  1.00 16.64           C  
ANISOU 3679  C   ILE A 489     2112   1998   2211     58    208   -138       C  
ATOM   3680  O   ILE A 489      12.028  26.599   0.049  1.00 14.59           O  
ANISOU 3680  O   ILE A 489     1865   1718   1959     52    206   -137       O  
ATOM   3681  CB  ILE A 489      14.382  28.549  -0.231  1.00 16.26           C  
ANISOU 3681  CB  ILE A 489     2054   1976   2147     39    221   -161       C  
ATOM   3682  CG1 ILE A 489      15.727  28.934  -0.862  1.00 17.33           C  
ANISOU 3682  CG1 ILE A 489     2180   2130   2272     36    230   -177       C  
ATOM   3683  CG2 ILE A 489      13.979  29.473   0.924  1.00 13.92           C  
ANISOU 3683  CG2 ILE A 489     1752   1688   1849     29    223   -157       C  
ATOM   3684  CD1 ILE A 489      16.934  28.891   0.086  1.00 16.28           C  
ANISOU 3684  CD1 ILE A 489     2025   2029   2131     43    232   -186       C  
ATOM   3685  N   LYS A 490      12.911  26.745   2.127  1.00 15.53           N  
ANISOU 3685  N   LYS A 490     1964   1866   2070     64    207   -129       N  
ATOM   3686  CA  LYS A 490      11.635  26.824   2.824  1.00 16.16           C  
ANISOU 3686  CA  LYS A 490     2050   1932   2158     58    204   -117       C  
ATOM   3687  C   LYS A 490      11.497  28.276   3.263  1.00 16.15           C  
ANISOU 3687  C   LYS A 490     2041   1942   2149     42    206   -120       C  
ATOM   3688  O   LYS A 490      12.355  28.771   4.003  1.00 15.28           O  
ANISOU 3688  O   LYS A 490     1918   1856   2031     44    209   -125       O  
ATOM   3689  CB  LYS A 490      11.625  25.909   4.056  1.00 17.98           C  
ANISOU 3689  CB  LYS A 490     2278   2162   2389     76    204   -104       C  
ATOM   3690  CG  LYS A 490      10.310  25.945   4.855  1.00 19.31           C  
ANISOU 3690  CG  LYS A 490     2453   2316   2566     69    202    -91       C  
ATOM   3691  CD  LYS A 490      10.373  25.085   6.121  1.00 24.78           C  
ANISOU 3691  CD  LYS A 490     3145   3009   3258     88    205    -77       C  
ATOM   3692  CE  LYS A 490      10.481  23.606   5.786  1.00 32.27           C  
ANISOU 3692  CE  LYS A 490     4108   3939   4214    105    210    -72       C  
ATOM   3693  NZ  LYS A 490      10.777  22.741   6.971  1.00 36.84           N  
ANISOU 3693  NZ  LYS A 490     4689   4518   4788    130    215    -57       N  
ATOM   3694  N   ALA A 491      10.444  28.951   2.808  1.00 15.33           N  
ANISOU 3694  N   ALA A 491     1948   1826   2050     28    206   -119       N  
ATOM   3695  CA  ALA A 491      10.219  30.352   3.171  1.00 15.28           C  
ANISOU 3695  CA  ALA A 491     1939   1827   2038     14    210   -121       C  
ATOM   3696  C   ALA A 491       8.818  30.569   3.724  1.00 16.39           C  
ANISOU 3696  C   ALA A 491     2085   1955   2184      9    205   -110       C  
ATOM   3697  O   ALA A 491       7.836  30.075   3.172  1.00 14.89           O  
ANISOU 3697  O   ALA A 491     1906   1750   2002     10    201   -107       O  
ATOM   3698  CB  ALA A 491      10.436  31.264   1.998  1.00 15.20           C  
ANISOU 3698  CB  ALA A 491     1937   1816   2022      3    217   -131       C  
ATOM   3699  N   LEU A 492       8.748  31.297   4.835  1.00 16.79           N  
ANISOU 3699  N   LEU A 492     2129   2018   2231      5    207   -106       N  
ATOM   3700  CA  LEU A 492       7.477  31.590   5.479  1.00 16.96           C  
ANISOU 3700  CA  LEU A 492     2154   2030   2256      1    203    -96       C  
ATOM   3701  C   LEU A 492       7.343  33.105   5.471  1.00 16.40           C  
ANISOU 3701  C   LEU A 492     2087   1965   2178    -11    209   -101       C  
ATOM   3702  O   LEU A 492       8.104  33.792   6.147  1.00 15.92           O  
ANISOU 3702  O   LEU A 492     2017   1920   2111    -16    216   -106       O  
ATOM   3703  CB  LEU A 492       7.489  31.089   6.926  1.00 18.19           C  
ANISOU 3703  CB  LEU A 492     2301   2195   2415      9    200    -86       C  
ATOM   3704  CG  LEU A 492       7.037  29.658   7.235  1.00 21.02           C  
ANISOU 3704  CG  LEU A 492     2662   2539   2782     21    197    -75       C  
ATOM   3705  CD1 LEU A 492       7.941  28.671   6.531  1.00 18.88           C  
ANISOU 3705  CD1 LEU A 492     2393   2267   2513     33    198    -80       C  
ATOM   3706  CD2 LEU A 492       7.094  29.443   8.744  1.00 21.99           C  
ANISOU 3706  CD2 LEU A 492     2777   2673   2903     31    197    -64       C  
ATOM   3707  N   LEU A 493       6.379  33.620   4.712  1.00 15.32           N  
ANISOU 3707  N   LEU A 493     1963   1816   2040    -16    209   -100       N  
ATOM   3708  CA  LEU A 493       6.123  35.056   4.713  1.00 15.82           C  
ANISOU 3708  CA  LEU A 493     2034   1880   2095    -25    218   -102       C  
ATOM   3709  C   LEU A 493       5.185  35.365   5.880  1.00 15.51           C  
ANISOU 3709  C   LEU A 493     1992   1842   2058    -26    213    -92       C  
ATOM   3710  O   LEU A 493       4.047  34.898   5.870  1.00 15.98           O  
ANISOU 3710  O   LEU A 493     2054   1894   2123    -22    204    -85       O  
ATOM   3711  CB  LEU A 493       5.464  35.481   3.408  1.00 14.38           C  
ANISOU 3711  CB  LEU A 493     1869   1686   1908    -23    219   -103       C  
ATOM   3712  CG  LEU A 493       5.024  36.945   3.366  1.00 16.62           C  
ANISOU 3712  CG  LEU A 493     2165   1966   2181    -28    230   -103       C  
ATOM   3713  CD1 LEU A 493       6.186  37.832   3.753  1.00 14.78           C  
ANISOU 3713  CD1 LEU A 493     1931   1741   1944    -40    246   -111       C  
ATOM   3714  CD2 LEU A 493       4.492  37.248   1.958  1.00 16.65           C  
ANISOU 3714  CD2 LEU A 493     2186   1961   2176    -20    232   -104       C  
ATOM   3715  N   ASN A 494       5.665  36.131   6.859  1.00 14.56           N  
ANISOU 3715  N   ASN A 494     1864   1734   1933    -33    219    -94       N  
ATOM   3716  CA  ASN A 494       4.970  36.342   8.129  1.00 14.38           C  
ANISOU 3716  CA  ASN A 494     1835   1716   1912    -33    215    -85       C  
ATOM   3717  C   ASN A 494       4.150  37.629   8.149  1.00 14.47           C  
ANISOU 3717  C   ASN A 494     1858   1721   1917    -39    221    -84       C  
ATOM   3718  O   ASN A 494       4.576  38.647   7.604  1.00 13.49           O  
ANISOU 3718  O   ASN A 494     1744   1595   1785    -47    233    -92       O  
ATOM   3719  CB  ASN A 494       5.987  36.464   9.279  1.00 15.16           C  
ANISOU 3719  CB  ASN A 494     1917   1835   2008    -35    218    -90       C  
ATOM   3720  CG  ASN A 494       6.550  35.120   9.741  1.00 18.11           C  
ANISOU 3720  CG  ASN A 494     2278   2216   2385    -22    211    -86       C  
ATOM   3721  OD1 ASN A 494       6.363  34.754  10.897  1.00 19.71           O  
ANISOU 3721  OD1 ASN A 494     2472   2427   2589    -14    206    -78       O  
ATOM   3722  ND2 ASN A 494       7.274  34.412   8.867  1.00 16.05           N  
ANISOU 3722  ND2 ASN A 494     2018   1954   2126    -17    211    -92       N  
ATOM   3723  N   ASN A 495       2.993  37.589   8.813  1.00 14.17           N  
ANISOU 3723  N   ASN A 495     1820   1682   1882    -36    213    -73       N  
ATOM   3724  CA  ASN A 495       2.305  38.813   9.188  1.00 14.38           C  
ANISOU 3724  CA  ASN A 495     1854   1706   1901    -40    218    -71       C  
ATOM   3725  C   ASN A 495       2.099  38.721  10.689  1.00 14.05           C  
ANISOU 3725  C   ASN A 495     1799   1675   1862    -41    213    -65       C  
ATOM   3726  O   ASN A 495       1.173  38.052  11.149  1.00 15.42           O  
ANISOU 3726  O   ASN A 495     1969   1847   2042    -35    203    -55       O  
ATOM   3727  CB  ASN A 495       0.968  38.969   8.444  1.00 14.22           C  
ANISOU 3727  CB  ASN A 495     1848   1677   1878    -33    213    -66       C  
ATOM   3728  CG  ASN A 495       0.139  40.155   8.940  1.00 15.76           C  
ANISOU 3728  CG  ASN A 495     2052   1871   2065    -33    217    -62       C  
ATOM   3729  OD1 ASN A 495       0.538  40.863   9.871  1.00 14.02           O  
ANISOU 3729  OD1 ASN A 495     1828   1656   1842    -41    225    -63       O  
ATOM   3730  ND2 ASN A 495      -1.027  40.367   8.319  1.00 12.66           N  
ANISOU 3730  ND2 ASN A 495     1669   1474   1666    -24    213    -58       N  
ATOM   3731  N   ARG A 496       2.996  39.361  11.432  1.00 15.14           N  
ANISOU 3731  N   ARG A 496     1930   1826   1996    -48    221    -72       N  
ATOM   3732  CA  ARG A 496       2.870  39.505  12.883  1.00 15.23           C  
ANISOU 3732  CA  ARG A 496     1928   1851   2007    -48    218    -69       C  
ATOM   3733  C   ARG A 496       2.621  40.980  13.223  1.00 16.43           C  
ANISOU 3733  C   ARG A 496     2088   2002   2151    -58    229    -73       C  
ATOM   3734  O   ARG A 496       3.155  41.502  14.217  1.00 15.28           O  
ANISOU 3734  O   ARG A 496     1931   1870   2002    -64    234    -81       O  
ATOM   3735  CB  ARG A 496       4.152  39.040  13.583  1.00 14.05           C  
ANISOU 3735  CB  ARG A 496     1760   1722   1857    -47    219    -76       C  
ATOM   3736  CG  ARG A 496       4.558  37.628  13.196  1.00 16.17           C  
ANISOU 3736  CG  ARG A 496     2023   1989   2131    -35    211    -72       C  
ATOM   3737  CD  ARG A 496       5.645  37.094  14.120  1.00 17.89           C  
ANISOU 3737  CD  ARG A 496     2221   2230   2344    -27    210    -77       C  
ATOM   3738  NE  ARG A 496       6.206  35.863  13.563  1.00 19.02           N  
ANISOU 3738  NE  ARG A 496     2363   2372   2491    -15    206    -75       N  
ATOM   3739  CZ  ARG A 496       7.237  35.211  14.095  1.00 19.79           C  
ANISOU 3739  CZ  ARG A 496     2445   2489   2583     -2    204    -79       C  
ATOM   3740  NH1 ARG A 496       7.784  35.652  15.221  1.00 14.03           N  
ANISOU 3740  NH1 ARG A 496     1699   1786   1845      0    205    -85       N  
ATOM   3741  NH2 ARG A 496       7.723  34.133  13.493  1.00 19.39           N  
ANISOU 3741  NH2 ARG A 496     2396   2434   2535      8    202    -77       N  
ATOM   3742  N   SER A 497       1.790  41.639  12.415  1.00 14.99           N  
ANISOU 3742  N   SER A 497     1925   1803   1965    -57    233    -70       N  
ATOM   3743  CA  SER A 497       1.498  43.060  12.618  1.00 14.74           C  
ANISOU 3743  CA  SER A 497     1907   1767   1925    -64    246    -73       C  
ATOM   3744  C   SER A 497       0.793  43.294  13.948  1.00 14.56           C  
ANISOU 3744  C   SER A 497     1876   1753   1902    -62    240    -67       C  
ATOM   3745  O   SER A 497       0.066  42.426  14.440  1.00 12.94           O  
ANISOU 3745  O   SER A 497     1661   1553   1703    -54    225    -55       O  
ATOM   3746  CB  SER A 497       0.677  43.649  11.462  1.00 13.50           C  
ANISOU 3746  CB  SER A 497     1774   1592   1761    -57    252    -69       C  
ATOM   3747  OG  SER A 497      -0.546  42.948  11.287  1.00 14.28           O  
ANISOU 3747  OG  SER A 497     1873   1690   1862    -44    236    -57       O  
ATOM   3748  N   SER A 498       1.002  44.484  14.509  1.00 13.80           N  
ANISOU 3748  N   SER A 498     1784   1659   1800    -72    254    -74       N  
ATOM   3749  CA  SER A 498       0.414  44.845  15.798  1.00 13.61           C  
ANISOU 3749  CA  SER A 498     1752   1644   1774    -71    249    -70       C  
ATOM   3750  C   SER A 498       0.327  46.365  16.000  1.00 13.72           C  
ANISOU 3750  C   SER A 498     1781   1650   1779    -81    268    -77       C  
ATOM   3751  O   SER A 498      -0.308  46.803  16.953  1.00 13.23           O  
ANISOU 3751  O   SER A 498     1717   1594   1715    -79    265    -73       O  
ATOM   3752  CB  SER A 498       1.217  44.211  16.942  1.00 14.50           C  
ANISOU 3752  CB  SER A 498     1838   1780   1890    -73    243    -75       C  
ATOM   3753  OG  SER A 498       0.378  43.854  18.032  1.00 13.63           O  
ANISOU 3753  OG  SER A 498     1718   1678   1781    -64    230    -62       O  
ATOM   3754  N   TRP A 499       0.942  47.171  15.130  1.00 13.13           N  
ANISOU 3754  N   TRP A 499     1725   1563   1701    -90    288    -89       N  
ATOM   3755  CA  TRP A 499       0.878  48.631  15.259  1.00 14.67           C  
ANISOU 3755  CA  TRP A 499     1939   1745   1887    -99    310    -96       C  
ATOM   3756  C   TRP A 499       0.179  49.371  14.110  1.00 14.52           C  
ANISOU 3756  C   TRP A 499     1955   1701   1859    -89    323    -88       C  
ATOM   3757  O   TRP A 499       0.811  50.164  13.428  1.00 15.95           O  
ANISOU 3757  O   TRP A 499     2155   1866   2036    -99    347    -98       O  
ATOM   3758  CB  TRP A 499       2.279  49.223  15.470  1.00 15.45           C  
ANISOU 3758  CB  TRP A 499     2033   1850   1988   -123    331   -120       C  
ATOM   3759  CG  TRP A 499       2.880  48.836  16.782  1.00 13.99           C  
ANISOU 3759  CG  TRP A 499     1815   1693   1806   -130    321   -131       C  
ATOM   3760  CD1 TRP A 499       2.822  49.545  17.964  1.00 16.90           C  
ANISOU 3760  CD1 TRP A 499     2176   2073   2172   -138    326   -139       C  
ATOM   3761  CD2 TRP A 499       3.627  47.649  17.060  1.00 16.09           C  
ANISOU 3761  CD2 TRP A 499     2053   1983   2078   -127    305   -134       C  
ATOM   3762  NE1 TRP A 499       3.489  48.857  18.951  1.00 14.21           N  
ANISOU 3762  NE1 TRP A 499     1802   1762   1833   -139    313   -148       N  
ATOM   3763  CE2 TRP A 499       3.988  47.693  18.428  1.00 15.21           C  
ANISOU 3763  CE2 TRP A 499     1917   1897   1964   -131    301   -144       C  
ATOM   3764  CE3 TRP A 499       4.027  46.550  16.284  1.00 15.33           C  
ANISOU 3764  CE3 TRP A 499     1951   1887   1986   -119    295   -129       C  
ATOM   3765  CZ2 TRP A 499       4.742  46.689  19.035  1.00 14.04           C  
ANISOU 3765  CZ2 TRP A 499     1740   1777   1817   -124    287   -149       C  
ATOM   3766  CZ3 TRP A 499       4.773  45.549  16.894  1.00 20.99           C  
ANISOU 3766  CZ3 TRP A 499     2640   2630   2705   -114    282   -134       C  
ATOM   3767  CH2 TRP A 499       5.120  45.625  18.257  1.00 21.16           C  
ANISOU 3767  CH2 TRP A 499     2638   2678   2722   -115    278   -143       C  
ATOM   3768  N   PRO A 500      -1.124  49.153  13.878  1.00 15.36           N  
ANISOU 3768  N   PRO A 500     2069   1804   1961    -69    309    -71       N  
ATOM   3769  CA  PRO A 500      -2.011  48.169  14.466  1.00 15.40           C  
ANISOU 3769  CA  PRO A 500     2054   1824   1972    -58    282    -59       C  
ATOM   3770  C   PRO A 500      -1.902  46.852  13.695  1.00 15.55           C  
ANISOU 3770  C   PRO A 500     2062   1846   1997    -51    267    -55       C  
ATOM   3771  O   PRO A 500      -1.372  46.834  12.573  1.00 13.68           O  
ANISOU 3771  O   PRO A 500     1838   1600   1760    -52    275    -59       O  
ATOM   3772  CB  PRO A 500      -3.398  48.777  14.236  1.00 15.90           C  
ANISOU 3772  CB  PRO A 500     2136   1880   2024    -40    281    -47       C  
ATOM   3773  CG  PRO A 500      -3.249  49.691  13.046  1.00 19.67           C  
ANISOU 3773  CG  PRO A 500     2646   2337   2489    -34    302    -49       C  
ATOM   3774  CD  PRO A 500      -1.784  49.903  12.788  1.00 17.21           C  
ANISOU 3774  CD  PRO A 500     2336   2018   2183    -55    321    -64       C  
ATOM   3775  N   ALA A 501      -2.431  45.776  14.276  1.00 15.06           N  
ANISOU 3775  N   ALA A 501     1981   1797   1944    -46    247    -47       N  
ATOM   3776  CA  ALA A 501      -2.678  44.552  13.513  1.00 13.66           C  
ANISOU 3776  CA  ALA A 501     1797   1620   1774    -38    233    -42       C  
ATOM   3777  C   ALA A 501      -3.459  44.952  12.257  1.00 15.00           C  
ANISOU 3777  C   ALA A 501     1987   1779   1933    -25    235    -40       C  
ATOM   3778  O   ALA A 501      -4.354  45.791  12.315  1.00 13.70           O  
ANISOU 3778  O   ALA A 501     1835   1612   1758    -16    238    -35       O  
ATOM   3779  CB  ALA A 501      -3.455  43.538  14.349  1.00 11.61           C  
ANISOU 3779  CB  ALA A 501     1517   1370   1521    -34    215    -33       C  
ATOM   3780  N   ARG A 502      -3.091  44.389  11.110  1.00 15.07           N  
ANISOU 3780  N   ARG A 502     1999   1782   1942    -22    234    -43       N  
ATOM   3781  CA  ARG A 502      -3.671  44.816   9.840  1.00 14.19           C  
ANISOU 3781  CA  ARG A 502     1909   1663   1819     -7    238    -42       C  
ATOM   3782  C   ARG A 502      -3.451  43.767   8.759  1.00 15.54           C  
ANISOU 3782  C   ARG A 502     2074   1834   1994     -4    230    -46       C  
ATOM   3783  O   ARG A 502      -2.625  42.873   8.933  1.00 14.61           O  
ANISOU 3783  O   ARG A 502     1942   1719   1889    -14    226    -49       O  
ATOM   3784  CB  ARG A 502      -3.063  46.156   9.382  1.00 15.96           C  
ANISOU 3784  CB  ARG A 502     2159   1873   2031     -9    263    -46       C  
ATOM   3785  CG  ARG A 502      -1.552  46.172   9.103  1.00 12.08           C  
ANISOU 3785  CG  ARG A 502     1668   1375   1545    -26    277    -56       C  
ATOM   3786  CD  ARG A 502      -1.026  47.623   9.009  1.00 16.47           C  
ANISOU 3786  CD  ARG A 502     2249   1916   2091    -33    306    -61       C  
ATOM   3787  NE  ARG A 502       0.421  47.663   8.786  1.00 17.05           N  
ANISOU 3787  NE  ARG A 502     2320   1986   2170    -52    322    -75       N  
ATOM   3788  CZ  ARG A 502       1.329  47.543   9.752  1.00 21.30           C  
ANISOU 3788  CZ  ARG A 502     2838   2535   2718    -71    323    -86       C  
ATOM   3789  NH1 ARG A 502       0.955  47.408  11.021  1.00 13.97           N  
ANISOU 3789  NH1 ARG A 502     1892   1621   1795    -74    311    -83       N  
ATOM   3790  NH2 ARG A 502       2.627  47.570   9.460  1.00 19.35           N  
ANISOU 3790  NH2 ARG A 502     2588   2289   2475    -88    338   -100       N  
ATOM   3791  N   LEU A 503      -4.145  43.913   7.631  1.00 16.95           N  
ANISOU 3791  N   LEU A 503     2267   2012   2161     12    228    -45       N  
ATOM   3792  CA  LEU A 503      -4.067  42.932   6.554  1.00 17.28           C  
ANISOU 3792  CA  LEU A 503     2303   2055   2206     17    220    -51       C  
ATOM   3793  C   LEU A 503      -3.521  43.655   5.346  1.00 18.54           C  
ANISOU 3793  C   LEU A 503     2487   2204   2352     25    235    -53       C  
ATOM   3794  O   LEU A 503      -3.893  44.804   5.096  1.00 18.23           O  
ANISOU 3794  O   LEU A 503     2470   2159   2296     37    248    -49       O  
ATOM   3795  CB  LEU A 503      -5.458  42.371   6.247  1.00 17.63           C  
ANISOU 3795  CB  LEU A 503     2338   2111   2246     31    203    -51       C  
ATOM   3796  CG  LEU A 503      -6.193  41.833   7.481  1.00 18.01           C  
ANISOU 3796  CG  LEU A 503     2367   2169   2307     23    191    -47       C  
ATOM   3797  CD1 LEU A 503      -7.685  41.686   7.202  1.00 20.50           C  
ANISOU 3797  CD1 LEU A 503     2675   2499   2613     37    179    -50       C  
ATOM   3798  CD2 LEU A 503      -5.572  40.518   7.984  1.00 16.23           C  
ANISOU 3798  CD2 LEU A 503     2121   1941   2101      7    184    -49       C  
ATOM   3799  N   ILE A 504      -2.634  42.986   4.615  1.00 15.92           N  
ANISOU 3799  N   ILE A 504     2153   1869   2027     20    236    -59       N  
ATOM   3800  CA  ILE A 504      -2.070  43.546   3.388  1.00 16.58           C  
ANISOU 3800  CA  ILE A 504     2258   1942   2097     28    252    -62       C  
ATOM   3801  C   ILE A 504      -2.351  42.583   2.244  1.00 15.60           C  
ANISOU 3801  C   ILE A 504     2128   1825   1972     40    239    -67       C  
ATOM   3802  O   ILE A 504      -1.957  41.417   2.311  1.00 15.09           O  
ANISOU 3802  O   ILE A 504     2045   1764   1923     30    227    -72       O  
ATOM   3803  CB  ILE A 504      -0.547  43.803   3.485  1.00 15.05           C  
ANISOU 3803  CB  ILE A 504     2068   1739   1910      9    270    -68       C  
ATOM   3804  CG1 ILE A 504      -0.253  44.870   4.549  1.00 22.22           C  
ANISOU 3804  CG1 ILE A 504     2981   2641   2817     -3    285    -67       C  
ATOM   3805  CG2 ILE A 504       0.004  44.239   2.135  1.00 15.44           C  
ANISOU 3805  CG2 ILE A 504     2140   1778   1948     17    286    -70       C  
ATOM   3806  CD1 ILE A 504       1.225  45.250   4.660  1.00 23.65           C  
ANISOU 3806  CD1 ILE A 504     3164   2816   3003    -24    306    -77       C  
ATOM   3807  N   LYS A 505      -3.031  43.067   1.209  1.00 15.63           N  
ANISOU 3807  N   LYS A 505     2150   1832   1957     63    241    -66       N  
ATOM   3808  CA  LYS A 505      -3.432  42.206   0.100  1.00 17.85           C  
ANISOU 3808  CA  LYS A 505     2424   2123   2234     76    228    -74       C  
ATOM   3809  C   LYS A 505      -2.263  41.897  -0.832  1.00 17.80           C  
ANISOU 3809  C   LYS A 505     2424   2107   2229     72    237    -79       C  
ATOM   3810  O   LYS A 505      -2.036  40.733  -1.171  1.00 17.47           O  
ANISOU 3810  O   LYS A 505     2366   2071   2200     66    224    -87       O  
ATOM   3811  CB  LYS A 505      -4.571  42.824  -0.719  1.00 19.19           C  
ANISOU 3811  CB  LYS A 505     2608   2303   2378    106    226    -72       C  
ATOM   3812  CG  LYS A 505      -5.205  41.852  -1.715  1.00 20.70           C  
ANISOU 3812  CG  LYS A 505     2786   2513   2566    120    208    -84       C  
ATOM   3813  CD  LYS A 505      -6.166  42.553  -2.666  1.00 32.92           C  
ANISOU 3813  CD  LYS A 505     4349   4074   4083    155    208    -84       C  
ATOM   3814  CE  LYS A 505      -7.041  41.549  -3.413  1.00 38.85           C  
ANISOU 3814  CE  LYS A 505     5078   4851   4831    166    187   -101       C  
ATOM   3815  NZ  LYS A 505      -6.308  40.723  -4.426  1.00 38.36           N  
ANISOU 3815  NZ  LYS A 505     5012   4787   4774    163    185   -111       N  
ATOM   3816  N   ASP A 506      -1.529  42.929  -1.238  1.00 16.89           N  
ANISOU 3816  N   ASP A 506     2335   1979   2103     74    260    -75       N  
ATOM   3817  CA  ASP A 506      -0.577  42.774  -2.342  1.00 19.05           C  
ANISOU 3817  CA  ASP A 506     2619   2246   2374     75    270    -80       C  
ATOM   3818  C   ASP A 506       0.829  42.459  -1.865  1.00 18.90           C  
ANISOU 3818  C   ASP A 506     2589   2218   2371     48    279    -84       C  
ATOM   3819  O   ASP A 506       1.764  43.207  -2.156  1.00 19.83           O  
ANISOU 3819  O   ASP A 506     2725   2324   2485     41    302    -85       O  
ATOM   3820  CB  ASP A 506      -0.569  44.019  -3.224  1.00 19.99           C  
ANISOU 3820  CB  ASP A 506     2773   2354   2468     94    294    -73       C  
ATOM   3821  CG  ASP A 506      -1.945  44.314  -3.791  1.00 26.30           C  
ANISOU 3821  CG  ASP A 506     3581   3166   3245    127    285    -69       C  
ATOM   3822  OD1 ASP A 506      -2.603  43.352  -4.239  1.00 26.32           O  
ANISOU 3822  OD1 ASP A 506     3564   3186   3248    137    262    -77       O  
ATOM   3823  OD2 ASP A 506      -2.374  45.485  -3.753  1.00 33.49           O  
ANISOU 3823  OD2 ASP A 506     4517   4069   4137    143    301    -60       O  
ATOM   3824  N   LEU A 507       0.968  41.341  -1.154  1.00 17.58           N  
ANISOU 3824  N   LEU A 507     2395   2059   2224     34    261    -89       N  
ATOM   3825  CA  LEU A 507       2.253  40.954  -0.582  1.00 15.74           C  
ANISOU 3825  CA  LEU A 507     2149   1824   2007     13    266    -94       C  
ATOM   3826  C   LEU A 507       3.092  40.140  -1.557  1.00 15.97           C  
ANISOU 3826  C   LEU A 507     2174   1853   2039     13    265   -102       C  
ATOM   3827  O   LEU A 507       2.579  39.275  -2.281  1.00 15.62           O  
ANISOU 3827  O   LEU A 507     2124   1814   1994     25    250   -104       O  
ATOM   3828  CB  LEU A 507       2.056  40.168   0.716  1.00 14.79           C  
ANISOU 3828  CB  LEU A 507     2004   1711   1902      2    250    -92       C  
ATOM   3829  CG  LEU A 507       1.704  40.927   1.999  1.00 16.80           C  
ANISOU 3829  CG  LEU A 507     2257   1967   2158     -4    254    -87       C  
ATOM   3830  CD1 LEU A 507       1.275  39.943   3.084  1.00 16.70           C  
ANISOU 3830  CD1 LEU A 507     2221   1963   2161     -9    235    -84       C  
ATOM   3831  CD2 LEU A 507       2.878  41.783   2.494  1.00 15.11           C  
ANISOU 3831  CD2 LEU A 507     2047   1748   1944    -21    274    -91       C  
ATOM   3832  N   SER A 508       4.389  40.433  -1.563  1.00 14.82           N  
ANISOU 3832  N   SER A 508     2031   1704   1896      0    281   -107       N  
ATOM   3833  CA  SER A 508       5.364  39.633  -2.308  1.00 14.45           C  
ANISOU 3833  CA  SER A 508     1977   1659   1853     -2    281   -116       C  
ATOM   3834  C   SER A 508       6.715  39.696  -1.612  1.00 15.23           C  
ANISOU 3834  C   SER A 508     2063   1761   1960    -22    292   -123       C  
ATOM   3835  O   SER A 508       6.971  40.614  -0.823  1.00 13.48           O  
ANISOU 3835  O   SER A 508     1844   1538   1738    -35    306   -124       O  
ATOM   3836  CB  SER A 508       5.507  40.112  -3.765  1.00 14.57           C  
ANISOU 3836  CB  SER A 508     2015   1667   1853      9    295   -117       C  
ATOM   3837  OG  SER A 508       6.164  41.373  -3.880  1.00 14.84           O  
ANISOU 3837  OG  SER A 508     2069   1690   1878      1    323   -117       O  
ATOM   3838  N   TYR A 509       7.580  38.730  -1.913  1.00 14.26           N  
ANISOU 3838  N   TYR A 509     1927   1645   1845    -24    286   -131       N  
ATOM   3839  CA  TYR A 509       8.988  38.872  -1.577  1.00 13.53           C  
ANISOU 3839  CA  TYR A 509     1823   1559   1755    -40    299   -142       C  
ATOM   3840  C   TYR A 509       9.864  38.420  -2.735  1.00 15.20           C  
ANISOU 3840  C   TYR A 509     2038   1772   1965    -37    304   -150       C  
ATOM   3841  O   TYR A 509       9.402  37.716  -3.637  1.00 14.67           O  
ANISOU 3841  O   TYR A 509     1975   1701   1896    -23    293   -147       O  
ATOM   3842  CB  TYR A 509       9.363  38.126  -0.294  1.00 14.06           C  
ANISOU 3842  CB  TYR A 509     1864   1641   1834    -46    286   -144       C  
ATOM   3843  CG  TYR A 509       9.124  36.634  -0.342  1.00 13.36           C  
ANISOU 3843  CG  TYR A 509     1764   1557   1755    -33    265   -140       C  
ATOM   3844  CD1 TYR A 509      10.075  35.758  -0.868  1.00 13.44           C  
ANISOU 3844  CD1 TYR A 509     1764   1572   1767    -30    262   -148       C  
ATOM   3845  CD2 TYR A 509       7.940  36.101   0.152  1.00 13.83           C  
ANISOU 3845  CD2 TYR A 509     1821   1613   1821    -25    248   -130       C  
ATOM   3846  CE1 TYR A 509       9.842  34.368  -0.879  1.00 11.19           C  
ANISOU 3846  CE1 TYR A 509     1471   1288   1492    -18    245   -144       C  
ATOM   3847  CE2 TYR A 509       7.691  34.724   0.119  1.00 13.93           C  
ANISOU 3847  CE2 TYR A 509     1825   1625   1843    -16    233   -127       C  
ATOM   3848  CZ  TYR A 509       8.655  33.867  -0.395  1.00 13.36           C  
ANISOU 3848  CZ  TYR A 509     1745   1556   1773    -13    232   -134       C  
ATOM   3849  OH  TYR A 509       8.424  32.502  -0.379  1.00 13.64           O  
ANISOU 3849  OH  TYR A 509     1775   1589   1819     -4    219   -132       O  
ATOM   3850  N   ASN A 510      11.133  38.808  -2.684  1.00 16.25           N  
ANISOU 3850  N   ASN A 510     2165   1911   2096    -52    322   -162       N  
ATOM   3851  CA  ASN A 510      12.063  38.484  -3.765  1.00 17.46           C  
ANISOU 3851  CA  ASN A 510     2319   2066   2246    -52    330   -171       C  
ATOM   3852  C   ASN A 510      13.196  37.580  -3.274  1.00 17.00           C  
ANISOU 3852  C   ASN A 510     2235   2028   2197    -56    322   -183       C  
ATOM   3853  O   ASN A 510      13.661  37.730  -2.148  1.00 16.90           O  
ANISOU 3853  O   ASN A 510     2204   2029   2188    -67    323   -189       O  
ATOM   3854  CB  ASN A 510      12.673  39.771  -4.342  1.00 18.74           C  
ANISOU 3854  CB  ASN A 510     2501   2219   2399    -65    362   -179       C  
ATOM   3855  CG  ASN A 510      11.676  40.620  -5.122  1.00 21.33           C  
ANISOU 3855  CG  ASN A 510     2861   2527   2714    -53    372   -166       C  
ATOM   3856  OD1 ASN A 510      10.583  40.167  -5.467  1.00 18.50           O  
ANISOU 3856  OD1 ASN A 510     2509   2165   2353    -33    354   -155       O  
ATOM   3857  ND2 ASN A 510      12.069  41.863  -5.425  1.00 16.98           N  
ANISOU 3857  ND2 ASN A 510     2332   1963   2154    -65    404   -170       N  
ATOM   3858  N   TYR A 511      13.650  36.662  -4.126  1.00 15.87           N  
ANISOU 3858  N   TYR A 511     2087   1887   2053    -47    315   -186       N  
ATOM   3859  CA  TYR A 511      14.854  35.887  -3.853  1.00 15.13           C  
ANISOU 3859  CA  TYR A 511     1971   1813   1963    -48    312   -198       C  
ATOM   3860  C   TYR A 511      15.881  36.221  -4.936  1.00 16.68           C  
ANISOU 3860  C   TYR A 511     2173   2011   2153    -55    331   -211       C  
ATOM   3861  O   TYR A 511      15.646  35.931  -6.118  1.00 15.84           O  
ANISOU 3861  O   TYR A 511     2081   1894   2043    -44    330   -207       O  
ATOM   3862  CB  TYR A 511      14.543  34.376  -3.812  1.00 16.53           C  
ANISOU 3862  CB  TYR A 511     2139   1992   2149    -30    287   -191       C  
ATOM   3863  CG  TYR A 511      15.736  33.545  -3.366  1.00 16.15           C  
ANISOU 3863  CG  TYR A 511     2067   1965   2102    -26    283   -201       C  
ATOM   3864  CD1 TYR A 511      16.686  33.108  -4.292  1.00 19.56           C  
ANISOU 3864  CD1 TYR A 511     2496   2403   2531    -22    288   -212       C  
ATOM   3865  CD2 TYR A 511      15.922  33.215  -2.024  1.00 15.74           C  
ANISOU 3865  CD2 TYR A 511     1997   1929   2054    -24    275   -201       C  
ATOM   3866  CE1 TYR A 511      17.802  32.380  -3.899  1.00 15.68           C  
ANISOU 3866  CE1 TYR A 511     1983   1934   2038    -16    284   -222       C  
ATOM   3867  CE2 TYR A 511      17.040  32.497  -1.614  1.00 16.83           C  
ANISOU 3867  CE2 TYR A 511     2114   2090   2191    -16    272   -210       C  
ATOM   3868  CZ  TYR A 511      17.968  32.072  -2.558  1.00 17.42           C  
ANISOU 3868  CZ  TYR A 511     2185   2171   2260    -12    276   -221       C  
ATOM   3869  OH  TYR A 511      19.078  31.357  -2.160  1.00 19.22           O  
ANISOU 3869  OH  TYR A 511     2392   2425   2484     -1    272   -231       O  
ATOM   3870  N   TYR A 512      16.984  36.845  -4.518  1.00 15.88           N  
ANISOU 3870  N   TYR A 512     2059   1925   2049    -73    349   -227       N  
ATOM   3871  CA  TYR A 512      18.036  37.360  -5.405  1.00 17.39           C  
ANISOU 3871  CA  TYR A 512     2254   2119   2234    -86    373   -242       C  
ATOM   3872  C   TYR A 512      19.204  36.386  -5.530  1.00 18.54           C  
ANISOU 3872  C   TYR A 512     2375   2289   2380    -81    366   -256       C  
ATOM   3873  O   TYR A 512      19.656  35.839  -4.511  1.00 17.28           O  
ANISOU 3873  O   TYR A 512     2190   2152   2223    -78    353   -262       O  
ATOM   3874  CB  TYR A 512      18.584  38.687  -4.869  1.00 18.66           C  
ANISOU 3874  CB  TYR A 512     2414   2283   2391   -113    401   -257       C  
ATOM   3875  CG  TYR A 512      17.568  39.813  -4.847  1.00 18.41           C  
ANISOU 3875  CG  TYR A 512     2410   2226   2356   -118    415   -245       C  
ATOM   3876  CD1 TYR A 512      17.295  40.549  -5.988  1.00 17.33           C  
ANISOU 3876  CD1 TYR A 512     2306   2066   2211   -117    436   -239       C  
ATOM   3877  CD2 TYR A 512      16.884  40.136  -3.679  1.00 19.43           C  
ANISOU 3877  CD2 TYR A 512     2535   2356   2490   -121    407   -239       C  
ATOM   3878  CE1 TYR A 512      16.358  41.585  -5.975  1.00 20.00           C  
ANISOU 3878  CE1 TYR A 512     2672   2381   2544   -118    449   -226       C  
ATOM   3879  CE2 TYR A 512      15.957  41.173  -3.647  1.00 14.88           C  
ANISOU 3879  CE2 TYR A 512     1985   1756   1909   -124    420   -228       C  
ATOM   3880  CZ  TYR A 512      15.696  41.879  -4.804  1.00 17.23           C  
ANISOU 3880  CZ  TYR A 512     2315   2031   2198   -121    441   -221       C  
ATOM   3881  OH  TYR A 512      14.772  42.896  -4.790  1.00 18.89           O  
ANISOU 3881  OH  TYR A 512     2554   2220   2402   -119    454   -209       O  
ATOM   3882  N   MET A 513      19.661  36.158  -6.763  1.00 18.80           N  
ANISOU 3882  N   MET A 513     2417   2317   2408    -76    373   -260       N  
ATOM   3883  CA  MET A 513      20.807  35.289  -7.018  1.00 21.14           C  
ANISOU 3883  CA  MET A 513     2692   2635   2702    -71    368   -273       C  
ATOM   3884  C   MET A 513      21.842  36.017  -7.873  1.00 21.93           C  
ANISOU 3884  C   MET A 513     2796   2741   2796    -88    397   -291       C  
ATOM   3885  O   MET A 513      21.510  36.978  -8.568  1.00 22.30           O  
ANISOU 3885  O   MET A 513     2868   2766   2838    -98    418   -287       O  
ATOM   3886  CB  MET A 513      20.418  34.046  -7.832  1.00 20.04           C  
ANISOU 3886  CB  MET A 513     2560   2489   2566    -46    347   -262       C  
ATOM   3887  CG  MET A 513      19.240  33.218  -7.367  1.00 27.13           C  
ANISOU 3887  CG  MET A 513     3461   3375   3472    -28    322   -244       C  
ATOM   3888  SD  MET A 513      18.386  32.591  -8.845  1.00 36.06           S  
ANISOU 3888  SD  MET A 513     4615   4483   4601    -10    312   -234       S  
ATOM   3889  CE  MET A 513      16.868  33.550  -8.736  1.00 30.71           C  
ANISOU 3889  CE  MET A 513     3960   3784   3924    -13    314   -219       C  
ATOM   3890  N   ASP A 514      23.080  35.531  -7.814  1.00 22.43           N  
ANISOU 3890  N   ASP A 514     2833   2832   2856    -90    398   -310       N  
ATOM   3891  CA  ASP A 514      24.150  35.928  -8.724  1.00 21.97           C  
ANISOU 3891  CA  ASP A 514     2774   2781   2791   -104    422   -328       C  
ATOM   3892  C   ASP A 514      24.422  34.728  -9.631  1.00 20.62           C  
ANISOU 3892  C   ASP A 514     2601   2614   2618    -80    406   -324       C  
ATOM   3893  O   ASP A 514      24.784  33.651  -9.153  1.00 20.54           O  
ANISOU 3893  O   ASP A 514     2569   2624   2610    -63    385   -326       O  
ATOM   3894  CB  ASP A 514      25.398  36.290  -7.922  1.00 22.59           C  
ANISOU 3894  CB  ASP A 514     2821   2895   2868   -125    436   -356       C  
ATOM   3895  CG  ASP A 514      26.518  36.866  -8.784  1.00 27.74           C  
ANISOU 3895  CG  ASP A 514     3471   3555   3513   -145    467   -378       C  
ATOM   3896  OD1 ASP A 514      26.570  36.642 -10.016  1.00 27.53           O  
ANISOU 3896  OD1 ASP A 514     3461   3514   3482   -137    472   -372       O  
ATOM   3897  OD2 ASP A 514      27.363  37.572  -8.196  1.00 31.36           O  
ANISOU 3897  OD2 ASP A 514     3909   4036   3970   -171    487   -404       O  
ATOM   3898  N   LEU A 515      24.207  34.906 -10.929  1.00 20.27           N  
ANISOU 3898  N   LEU A 515     2582   2549   2570    -77    417   -318       N  
ATOM   3899  CA  LEU A 515      24.359  33.809 -11.888  1.00 21.52           C  
ANISOU 3899  CA  LEU A 515     2741   2707   2726    -54    402   -314       C  
ATOM   3900  C   LEU A 515      25.724  33.833 -12.593  1.00 22.21           C  
ANISOU 3900  C   LEU A 515     2817   2815   2806    -63    420   -335       C  
ATOM   3901  O   LEU A 515      25.896  33.196 -13.630  1.00 21.81           O  
ANISOU 3901  O   LEU A 515     2773   2761   2752    -48    415   -333       O  
ATOM   3902  CB  LEU A 515      23.208  33.830 -12.901  1.00 19.68           C  
ANISOU 3902  CB  LEU A 515     2540   2443   2491    -40    398   -295       C  
ATOM   3903  CG  LEU A 515      21.798  33.634 -12.316  1.00 22.20           C  
ANISOU 3903  CG  LEU A 515     2869   2746   2817    -29    377   -276       C  
ATOM   3904  CD1 LEU A 515      20.740  33.520 -13.408  1.00 20.84           C  
ANISOU 3904  CD1 LEU A 515     2724   2552   2641    -12    371   -262       C  
ATOM   3905  CD2 LEU A 515      21.720  32.414 -11.412  1.00 18.85           C  
ANISOU 3905  CD2 LEU A 515     2424   2335   2403    -15    349   -274       C  
ATOM   3906  N   THR A 516      26.688  34.559 -12.027  1.00 23.38           N  
ANISOU 3906  N   THR A 516     2946   2984   2952    -87    441   -356       N  
ATOM   3907  CA  THR A 516      28.036  34.638 -12.597  1.00 23.16           C  
ANISOU 3907  CA  THR A 516     2903   2979   2918    -99    460   -380       C  
ATOM   3908  C   THR A 516      28.589  33.250 -12.894  1.00 23.79           C  
ANISOU 3908  C   THR A 516     2963   3078   2994    -73    437   -383       C  
ATOM   3909  O   THR A 516      29.029  33.009 -14.012  1.00 24.41           O  
ANISOU 3909  O   THR A 516     3049   3156   3068    -67    444   -386       O  
ATOM   3910  CB  THR A 516      29.019  35.448 -11.722  1.00 24.76           C  
ANISOU 3910  CB  THR A 516     3079   3210   3118   -129    482   -408       C  
ATOM   3911  OG1 THR A 516      28.575  36.813 -11.684  1.00 26.01           O  
ANISOU 3911  OG1 THR A 516     3260   3343   3278   -156    511   -406       O  
ATOM   3912  CG2 THR A 516      30.452  35.399 -12.301  1.00 22.83           C  
ANISOU 3912  CG2 THR A 516     2812   2994   2866   -140    500   -435       C  
ATOM   3913  N   GLU A 517      28.501  32.327 -11.941  1.00 22.70           N  
ANISOU 3913  N   GLU A 517     2806   2957   2860    -54    409   -379       N  
ATOM   3914  CA  GLU A 517      29.047  30.996 -12.154  1.00 23.75           C  
ANISOU 3914  CA  GLU A 517     2924   3109   2990    -27    389   -382       C  
ATOM   3915  C   GLU A 517      28.348  30.212 -13.274  1.00 24.37           C  
ANISOU 3915  C   GLU A 517     3028   3160   3072     -5    376   -363       C  
ATOM   3916  O   GLU A 517      28.993  29.405 -13.953  1.00 25.03           O  
ANISOU 3916  O   GLU A 517     3105   3254   3150     10    371   -370       O  
ATOM   3917  CB  GLU A 517      29.134  30.206 -10.845  1.00 23.62           C  
ANISOU 3917  CB  GLU A 517     2883   3115   2975     -9    367   -381       C  
ATOM   3918  CG  GLU A 517      27.819  29.591 -10.389  1.00 21.89           C  
ANISOU 3918  CG  GLU A 517     2682   2868   2765      8    344   -355       C  
ATOM   3919  CD  GLU A 517      26.951  30.576  -9.626  1.00 22.08           C  
ANISOU 3919  CD  GLU A 517     2715   2878   2796    -10    349   -346       C  
ATOM   3920  OE1 GLU A 517      27.322  31.761  -9.478  1.00 22.29           O  
ANISOU 3920  OE1 GLU A 517     2738   2911   2819    -37    372   -360       O  
ATOM   3921  OE2 GLU A 517      25.903  30.133  -9.127  1.00 22.09           O  
ANISOU 3921  OE2 GLU A 517     2727   2860   2804      2    332   -327       O  
ATOM   3922  N   VAL A 518      27.055  30.469 -13.474  1.00 24.26           N  
ANISOU 3922  N   VAL A 518     3041   3112   3063     -4    371   -343       N  
ATOM   3923  CA  VAL A 518      26.275  29.851 -14.544  1.00 23.54           C  
ANISOU 3923  CA  VAL A 518     2974   2997   2974     14    360   -329       C  
ATOM   3924  C   VAL A 518      26.829  30.251 -15.914  1.00 25.67           C  
ANISOU 3924  C   VAL A 518     3255   3264   3234      9    380   -336       C  
ATOM   3925  O   VAL A 518      27.078  29.399 -16.776  1.00 24.79           O  
ANISOU 3925  O   VAL A 518     3144   3153   3119     26    371   -338       O  
ATOM   3926  CB  VAL A 518      24.781  30.251 -14.454  1.00 23.43           C  
ANISOU 3926  CB  VAL A 518     2984   2953   2966     14    354   -309       C  
ATOM   3927  CG1 VAL A 518      23.953  29.628 -15.583  1.00 22.94           C  
ANISOU 3927  CG1 VAL A 518     2943   2870   2903     33    342   -298       C  
ATOM   3928  CG2 VAL A 518      24.193  29.913 -13.070  1.00 22.71           C  
ANISOU 3928  CG2 VAL A 518     2881   2862   2883     17    336   -300       C  
ATOM   3929  N   PHE A 519      27.010  31.554 -16.117  1.00 26.24           N  
ANISOU 3929  N   PHE A 519     3337   3331   3301    -14    408   -342       N  
ATOM   3930  CA  PHE A 519      27.507  32.047 -17.398  1.00 28.42           C  
ANISOU 3930  CA  PHE A 519     3627   3602   3567    -20    432   -348       C  
ATOM   3931  C   PHE A 519      28.940  31.590 -17.644  1.00 29.57           C  
ANISOU 3931  C   PHE A 519     3748   3778   3708    -22    438   -369       C  
ATOM   3932  O   PHE A 519      29.289  31.207 -18.756  1.00 30.53           O  
ANISOU 3932  O   PHE A 519     3876   3899   3823    -11    441   -371       O  
ATOM   3933  CB  PHE A 519      27.407  33.566 -17.465  1.00 27.76           C  
ANISOU 3933  CB  PHE A 519     3563   3504   3480    -46    466   -348       C  
ATOM   3934  CG  PHE A 519      26.025  34.088 -17.187  1.00 28.78           C  
ANISOU 3934  CG  PHE A 519     3716   3605   3611    -42    461   -327       C  
ATOM   3935  CD1 PHE A 519      24.907  33.433 -17.683  1.00 28.02           C  
ANISOU 3935  CD1 PHE A 519     3636   3493   3516    -16    437   -309       C  
ATOM   3936  CD2 PHE A 519      25.847  35.232 -16.429  1.00 28.82           C  
ANISOU 3936  CD2 PHE A 519     3727   3603   3619    -65    480   -328       C  
ATOM   3937  CE1 PHE A 519      23.637  33.911 -17.420  1.00 29.99           C  
ANISOU 3937  CE1 PHE A 519     3905   3721   3766    -12    432   -293       C  
ATOM   3938  CE2 PHE A 519      24.580  35.736 -16.184  1.00 25.86           C  
ANISOU 3938  CE2 PHE A 519     3374   3204   3245    -60    476   -309       C  
ATOM   3939  CZ  PHE A 519      23.478  35.071 -16.681  1.00 27.68           C  
ANISOU 3939  CZ  PHE A 519     3619   3421   3474    -33    452   -291       C  
ATOM   3940  N   GLU A 520      29.752  31.600 -16.594  1.00 30.41           N  
ANISOU 3940  N   GLU A 520     3824   3913   3816    -33    439   -386       N  
ATOM   3941  CA  GLU A 520      31.133  31.146 -16.718  1.00 32.10           C  
ANISOU 3941  CA  GLU A 520     4009   4162   4023    -33    443   -409       C  
ATOM   3942  C   GLU A 520      31.248  29.665 -17.074  1.00 30.41           C  
ANISOU 3942  C   GLU A 520     3788   3955   3808      0    416   -404       C  
ATOM   3943  O   GLU A 520      32.184  29.281 -17.773  1.00 29.54           O  
ANISOU 3943  O   GLU A 520     3668   3864   3691      5    421   -418       O  
ATOM   3944  CB  GLU A 520      31.925  31.477 -15.457  1.00 33.00           C  
ANISOU 3944  CB  GLU A 520     4090   4310   4137    -50    449   -430       C  
ATOM   3945  CG  GLU A 520      32.410  32.919 -15.450  1.00 39.40           C  
ANISOU 3945  CG  GLU A 520     4901   5123   4946    -89    487   -447       C  
ATOM   3946  CD  GLU A 520      32.967  33.356 -14.110  1.00 45.53           C  
ANISOU 3946  CD  GLU A 520     5645   5931   5723   -108    491   -469       C  
ATOM   3947  OE1 GLU A 520      33.089  32.513 -13.190  1.00 50.29           O  
ANISOU 3947  OE1 GLU A 520     6223   6558   6325    -88    464   -470       O  
ATOM   3948  OE2 GLU A 520      33.275  34.561 -13.983  1.00 45.33           O  
ANISOU 3948  OE2 GLU A 520     5620   5904   5697   -142    523   -485       O  
ATOM   3949  N   ALA A 521      30.294  28.843 -16.639  1.00 28.43           N  
ANISOU 3949  N   ALA A 521     3545   3689   3566     22    388   -385       N  
ATOM   3950  CA  ALA A 521      30.278  27.428 -17.030  1.00 28.17           C  
ANISOU 3950  CA  ALA A 521     3512   3657   3534     53    365   -380       C  
ATOM   3951  C   ALA A 521      29.768  27.239 -18.457  1.00 27.20           C  
ANISOU 3951  C   ALA A 521     3415   3509   3409     62    365   -371       C  
ATOM   3952  O   ALA A 521      29.778  26.122 -18.979  1.00 26.84           O  
ANISOU 3952  O   ALA A 521     3371   3461   3363     86    349   -369       O  
ATOM   3953  CB  ALA A 521      29.443  26.581 -16.059  1.00 27.56           C  
ANISOU 3953  CB  ALA A 521     3435   3570   3466     71    339   -364       C  
ATOM   3954  N   GLY A 522      29.314  28.324 -19.077  1.00 25.93           N  
ANISOU 3954  N   GLY A 522     3276   3330   3245     45    385   -366       N  
ATOM   3955  CA  GLY A 522      28.742  28.269 -20.421  1.00 26.72           C  
ANISOU 3955  CA  GLY A 522     3402   3408   3341     56    386   -358       C  
ATOM   3956  C   GLY A 522      27.240  28.063 -20.511  1.00 25.97           C  
ANISOU 3956  C   GLY A 522     3330   3286   3253     68    369   -338       C  
ATOM   3957  O   GLY A 522      26.735  27.737 -21.581  1.00 26.03           O  
ANISOU 3957  O   GLY A 522     3354   3280   3255     82    364   -333       O  
ATOM   3958  N   TYR A 523      26.518  28.243 -19.406  1.00 24.94           N  
ANISOU 3958  N   TYR A 523     3197   3148   3131     62    360   -330       N  
ATOM   3959  CA  TYR A 523      25.073  28.018 -19.388  1.00 24.29           C  
ANISOU 3959  CA  TYR A 523     3132   3042   3055     72    343   -314       C  
ATOM   3960  C   TYR A 523      24.349  29.358 -19.405  1.00 25.35           C  
ANISOU 3960  C   TYR A 523     3285   3161   3184     58    360   -304       C  
ATOM   3961  O   TYR A 523      24.995  30.401 -19.359  1.00 24.48           O  
ANISOU 3961  O   TYR A 523     3176   3056   3068     39    385   -310       O  
ATOM   3962  CB  TYR A 523      24.676  27.210 -18.151  1.00 24.52           C  
ANISOU 3962  CB  TYR A 523     3147   3071   3096     78    321   -309       C  
ATOM   3963  CG  TYR A 523      25.074  25.755 -18.252  1.00 23.67           C  
ANISOU 3963  CG  TYR A 523     3029   2970   2992     99    304   -313       C  
ATOM   3964  CD1 TYR A 523      26.404  25.376 -18.125  1.00 22.51           C  
ANISOU 3964  CD1 TYR A 523     2863   2849   2841    102    308   -326       C  
ATOM   3965  CD2 TYR A 523      24.124  24.766 -18.489  1.00 21.97           C  
ANISOU 3965  CD2 TYR A 523     2823   2737   2785    115    285   -306       C  
ATOM   3966  CE1 TYR A 523      26.788  24.051 -18.238  1.00 25.64           C  
ANISOU 3966  CE1 TYR A 523     3251   3250   3239    124    294   -330       C  
ATOM   3967  CE2 TYR A 523      24.502  23.425 -18.596  1.00 23.82           C  
ANISOU 3967  CE2 TYR A 523     3052   2975   3023    134    273   -311       C  
ATOM   3968  CZ  TYR A 523      25.833  23.080 -18.472  1.00 24.02           C  
ANISOU 3968  CZ  TYR A 523     3060   3023   3043    140    277   -321       C  
ATOM   3969  OH  TYR A 523      26.240  21.764 -18.558  1.00 25.33           O  
ANISOU 3969  OH  TYR A 523     3222   3191   3211    162    267   -325       O  
ATOM   3970  N   SER A 524      23.022  29.338 -19.491  1.00 26.55           N  
ANISOU 3970  N   SER A 524     3453   3294   3338     67    347   -291       N  
ATOM   3971  CA  SER A 524      22.252  30.578 -19.507  1.00 28.48           C  
ANISOU 3971  CA  SER A 524     3718   3525   3577     59    362   -281       C  
ATOM   3972  C   SER A 524      21.094  30.492 -18.522  1.00 27.50           C  
ANISOU 3972  C   SER A 524     3594   3391   3462     59    344   -270       C  
ATOM   3973  O   SER A 524      20.887  29.451 -17.890  1.00 25.48           O  
ANISOU 3973  O   SER A 524     3323   3138   3218     66    322   -271       O  
ATOM   3974  CB  SER A 524      21.726  30.864 -20.913  1.00 28.41           C  
ANISOU 3974  CB  SER A 524     3734   3505   3553     74    368   -276       C  
ATOM   3975  OG  SER A 524      20.718  29.929 -21.237  1.00 33.75           O  
ANISOU 3975  OG  SER A 524     4413   4177   4234     94    342   -273       O  
ATOM   3976  N   VAL A 525      20.331  31.580 -18.429  1.00 27.09           N  
ANISOU 3976  N   VAL A 525     3560   3327   3405     54    355   -261       N  
ATOM   3977  CA  VAL A 525      19.164  31.646 -17.555  1.00 26.85           C  
ANISOU 3977  CA  VAL A 525     3530   3287   3381     54    341   -250       C  
ATOM   3978  C   VAL A 525      18.131  30.588 -17.940  1.00 27.14           C  
ANISOU 3978  C   VAL A 525     3567   3320   3422     74    315   -247       C  
ATOM   3979  O   VAL A 525      17.497  30.000 -17.063  1.00 27.13           O  
ANISOU 3979  O   VAL A 525     3556   3316   3433     74    297   -244       O  
ATOM   3980  CB  VAL A 525      18.545  33.066 -17.541  1.00 27.86           C  
ANISOU 3980  CB  VAL A 525     3681   3404   3500     48    360   -240       C  
ATOM   3981  CG1 VAL A 525      17.543  33.210 -16.419  1.00 25.39           C  
ANISOU 3981  CG1 VAL A 525     3364   3084   3195     45    348   -231       C  
ATOM   3982  CG2 VAL A 525      19.635  34.106 -17.352  1.00 29.94           C  
ANISOU 3982  CG2 VAL A 525     3946   3668   3759     26    392   -246       C  
ATOM   3983  N   ASP A 526      17.981  30.339 -19.241  1.00 27.30           N  
ANISOU 3983  N   ASP A 526     3599   3340   3432     90    314   -250       N  
ATOM   3984  CA  ASP A 526      17.179  29.244 -19.792  1.00 28.01           C  
ANISOU 3984  CA  ASP A 526     3687   3429   3525    107    291   -254       C  
ATOM   3985  C   ASP A 526      17.432  27.889 -19.139  1.00 26.38           C  
ANISOU 3985  C   ASP A 526     3460   3224   3336    107    273   -260       C  
ATOM   3986  O   ASP A 526      16.552  27.036 -19.162  1.00 27.81           O  
ANISOU 3986  O   ASP A 526     3639   3401   3525    115    255   -262       O  
ATOM   3987  CB  ASP A 526      17.507  29.027 -21.279  1.00 30.07           C  
ANISOU 3987  CB  ASP A 526     3957   3694   3773    123    295   -261       C  
ATOM   3988  CG  ASP A 526      17.136  30.204 -22.150  1.00 36.89           C  
ANISOU 3988  CG  ASP A 526     4844   4555   4615    132    312   -255       C  
ATOM   3989  OD1 ASP A 526      16.365  31.070 -21.686  1.00 45.20           O  
ANISOU 3989  OD1 ASP A 526     5908   5602   5664    130    317   -244       O  
ATOM   3990  OD2 ASP A 526      17.618  30.252 -23.304  1.00 45.68           O  
ANISOU 3990  OD2 ASP A 526     5967   5672   5714    143    322   -259       O  
ATOM   3991  N   ASP A 527      18.632  27.677 -18.608  1.00 25.26           N  
ANISOU 3991  N   ASP A 527     3305   3091   3200     98    279   -264       N  
ATOM   3992  CA  ASP A 527      19.045  26.386 -18.058  1.00 24.43           C  
ANISOU 3992  CA  ASP A 527     3185   2989   3108    102    265   -269       C  
ATOM   3993  C   ASP A 527      18.752  26.217 -16.564  1.00 24.50           C  
ANISOU 3993  C   ASP A 527     3183   2995   3130     95    258   -262       C  
ATOM   3994  O   ASP A 527      18.996  25.152 -15.983  1.00 23.46           O  
ANISOU 3994  O   ASP A 527     3041   2864   3008    101    248   -263       O  
ATOM   3995  CB  ASP A 527      20.548  26.218 -18.289  1.00 24.68           C  
ANISOU 3995  CB  ASP A 527     3206   3036   3136    102    275   -278       C  
ATOM   3996  CG  ASP A 527      20.911  26.128 -19.762  1.00 25.46           C  
ANISOU 3996  CG  ASP A 527     3314   3137   3223    112    281   -286       C  
ATOM   3997  OD1 ASP A 527      20.227  25.413 -20.525  1.00 25.69           O  
ANISOU 3997  OD1 ASP A 527     3350   3159   3253    126    269   -289       O  
ATOM   3998  OD2 ASP A 527      21.895  26.781 -20.154  1.00 28.88           O  
ANISOU 3998  OD2 ASP A 527     3746   3580   3646    106    299   -291       O  
ATOM   3999  N   ILE A 528      18.266  27.290 -15.948  1.00 23.29           N  
ANISOU 3999  N   ILE A 528     3033   2839   2974     83    265   -254       N  
ATOM   4000  CA  ILE A 528      17.943  27.303 -14.528  1.00 22.41           C  
ANISOU 4000  CA  ILE A 528     2913   2727   2873     75    259   -246       C  
ATOM   4001  C   ILE A 528      16.424  27.209 -14.402  1.00 23.16           C  
ANISOU 4001  C   ILE A 528     3017   2808   2974     77    247   -239       C  
ATOM   4002  O   ILE A 528      15.703  27.972 -15.042  1.00 23.48           O  
ANISOU 4002  O   ILE A 528     3070   2844   3005     78    251   -236       O  
ATOM   4003  CB  ILE A 528      18.487  28.574 -13.838  1.00 23.44           C  
ANISOU 4003  CB  ILE A 528     3040   2866   2998     58    276   -245       C  
ATOM   4004  CG1 ILE A 528      19.964  28.818 -14.191  1.00 21.35           C  
ANISOU 4004  CG1 ILE A 528     2767   2618   2726     53    292   -256       C  
ATOM   4005  CG2 ILE A 528      18.251  28.516 -12.328  1.00 19.31           C  
ANISOU 4005  CG2 ILE A 528     2505   2345   2485     52    269   -238       C  
ATOM   4006  CD1 ILE A 528      20.947  27.712 -13.795  1.00 20.70           C  
ANISOU 4006  CD1 ILE A 528     2664   2550   2648     62    283   -264       C  
ATOM   4007  N   LYS A 529      15.944  26.250 -13.616  1.00 21.17           N  
ANISOU 4007  N   LYS A 529     2757   2549   2735     80    234   -236       N  
ATOM   4008  CA  LYS A 529      14.526  25.888 -13.581  1.00 22.62           C  
ANISOU 4008  CA  LYS A 529     2946   2721   2925     82    222   -233       C  
ATOM   4009  C   LYS A 529      13.975  26.078 -12.165  1.00 20.93           C  
ANISOU 4009  C   LYS A 529     2726   2503   2720     74    219   -223       C  
ATOM   4010  O   LYS A 529      14.636  25.695 -11.200  1.00 20.27           O  
ANISOU 4010  O   LYS A 529     2634   2424   2643     73    219   -219       O  
ATOM   4011  CB  LYS A 529      14.446  24.416 -13.987  1.00 23.56           C  
ANISOU 4011  CB  LYS A 529     3063   2832   3054     92    212   -241       C  
ATOM   4012  CG  LYS A 529      13.112  23.705 -13.885  1.00 31.63           C  
ANISOU 4012  CG  LYS A 529     4087   3842   4087     92    201   -244       C  
ATOM   4013  CD  LYS A 529      13.405  22.206 -13.814  1.00 39.42           C  
ANISOU 4013  CD  LYS A 529     5072   4818   5086     98    197   -250       C  
ATOM   4014  CE  LYS A 529      12.579  21.383 -14.778  1.00 41.70           C  
ANISOU 4014  CE  LYS A 529     5365   5098   5379    101    190   -264       C  
ATOM   4015  NZ  LYS A 529      12.960  21.643 -16.194  1.00 46.48           N  
ANISOU 4015  NZ  LYS A 529     5974   5714   5971    110    191   -275       N  
ATOM   4016  N   VAL A 530      12.781  26.649 -12.038  1.00 17.52           N  
ANISOU 4016  N   VAL A 530     2301   2067   2288     70    215   -218       N  
ATOM   4017  CA  VAL A 530      12.141  26.859 -10.741  1.00 17.46           C  
ANISOU 4017  CA  VAL A 530     2289   2056   2288     62    212   -208       C  
ATOM   4018  C   VAL A 530      11.022  25.835 -10.546  1.00 17.40           C  
ANISOU 4018  C   VAL A 530     2280   2037   2293     63    200   -210       C  
ATOM   4019  O   VAL A 530      10.185  25.660 -11.428  1.00 16.65           O  
ANISOU 4019  O   VAL A 530     2190   1940   2196     67    194   -218       O  
ATOM   4020  CB  VAL A 530      11.615  28.306 -10.587  1.00 18.25           C  
ANISOU 4020  CB  VAL A 530     2397   2159   2379     55    219   -201       C  
ATOM   4021  CG1 VAL A 530      10.860  28.483  -9.278  1.00 19.29           C  
ANISOU 4021  CG1 VAL A 530     2523   2287   2518     48    214   -192       C  
ATOM   4022  CG2 VAL A 530      12.779  29.294 -10.618  1.00 19.55           C  
ANISOU 4022  CG2 VAL A 530     2563   2332   2533     49    235   -201       C  
ATOM   4023  N   THR A 531      11.019  25.129  -9.416  1.00 15.63           N  
ANISOU 4023  N   THR A 531     2049   1806   2082     61    198   -204       N  
ATOM   4024  CA  THR A 531       9.951  24.174  -9.138  1.00 16.56           C  
ANISOU 4024  CA  THR A 531     2167   1911   2213     60    190   -206       C  
ATOM   4025  C   THR A 531       9.470  24.365  -7.704  1.00 17.32           C  
ANISOU 4025  C   THR A 531     2260   2004   2317     53    190   -193       C  
ATOM   4026  O   THR A 531      10.163  24.977  -6.894  1.00 14.94           O  
ANISOU 4026  O   THR A 531     1954   1711   2011     52    195   -184       O  
ATOM   4027  CB  THR A 531      10.397  22.706  -9.298  1.00 18.50           C  
ANISOU 4027  CB  THR A 531     2414   2145   2470     67    191   -211       C  
ATOM   4028  OG1 THR A 531      11.553  22.478  -8.483  1.00 17.47           O  
ANISOU 4028  OG1 THR A 531     2280   2019   2339     73    196   -203       O  
ATOM   4029  CG2 THR A 531      10.754  22.386 -10.748  1.00 15.58           C  
ANISOU 4029  CG2 THR A 531     2047   1777   2093     74    190   -226       C  
ATOM   4030  N   ILE A 532       8.295  23.822  -7.402  1.00 17.37           N  
ANISOU 4030  N   ILE A 532     2265   1999   2333     47    186   -194       N  
ATOM   4031  CA  ILE A 532       7.671  23.983  -6.099  1.00 17.39           C  
ANISOU 4031  CA  ILE A 532     2266   1999   2343     41    186   -183       C  
ATOM   4032  C   ILE A 532       7.551  22.620  -5.432  1.00 18.21           C  
ANISOU 4032  C   ILE A 532     2370   2084   2461     42    189   -180       C  
ATOM   4033  O   ILE A 532       7.070  21.682  -6.052  1.00 18.87           O  
ANISOU 4033  O   ILE A 532     2457   2156   2554     40    190   -192       O  
ATOM   4034  CB  ILE A 532       6.258  24.587  -6.264  1.00 18.39           C  
ANISOU 4034  CB  ILE A 532     2391   2128   2468     33    181   -186       C  
ATOM   4035  CG1 ILE A 532       6.351  25.973  -6.899  1.00 20.62           C  
ANISOU 4035  CG1 ILE A 532     2677   2425   2732     35    180   -186       C  
ATOM   4036  CG2 ILE A 532       5.532  24.643  -4.921  1.00 15.50           C  
ANISOU 4036  CG2 ILE A 532     2022   1757   2110     25    181   -175       C  
ATOM   4037  CD1 ILE A 532       7.397  26.867  -6.281  1.00 23.20           C  
ANISOU 4037  CD1 ILE A 532     3004   2759   3052     35    188   -175       C  
ATOM   4038  N   GLY A 533       7.975  22.521  -4.173  1.00 18.82           N  
ANISOU 4038  N   GLY A 533     2447   2162   2542     45    194   -166       N  
ATOM   4039  CA  GLY A 533       7.902  21.270  -3.437  1.00 17.21           C  
ANISOU 4039  CA  GLY A 533     2247   1939   2350     50    200   -160       C  
ATOM   4040  C   GLY A 533       6.788  21.193  -2.401  1.00 19.29           C  
ANISOU 4040  C   GLY A 533     2511   2193   2623     41    202   -152       C  
ATOM   4041  O   GLY A 533       6.495  20.115  -1.876  1.00 16.92           O  
ANISOU 4041  O   GLY A 533     2218   1873   2335     42    211   -148       O  
ATOM   4042  N   TYR A 534       6.175  22.335  -2.105  1.00 16.77           N  
ANISOU 4042  N   TYR A 534     2185   1886   2299     32    196   -149       N  
ATOM   4043  CA  TYR A 534       5.092  22.440  -1.134  1.00 16.75           C  
ANISOU 4043  CA  TYR A 534     2181   1879   2303     22    197   -142       C  
ATOM   4044  C   TYR A 534       4.574  23.870  -1.215  1.00 18.37           C  
ANISOU 4044  C   TYR A 534     2380   2101   2497     15    190   -142       C  
ATOM   4045  O   TYR A 534       5.359  24.819  -1.194  1.00 17.17           O  
ANISOU 4045  O   TYR A 534     2225   1964   2333     20    188   -137       O  
ATOM   4046  CB  TYR A 534       5.556  22.211   0.318  1.00 14.75           C  
ANISOU 4046  CB  TYR A 534     1929   1623   2051     31    204   -123       C  
ATOM   4047  CG  TYR A 534       4.469  22.497   1.343  1.00 15.29           C  
ANISOU 4047  CG  TYR A 534     1994   1689   2125     21    204   -115       C  
ATOM   4048  CD1 TYR A 534       3.249  21.823   1.309  1.00 15.28           C  
ANISOU 4048  CD1 TYR A 534     1997   1672   2137      9    209   -121       C  
ATOM   4049  CD2 TYR A 534       4.662  23.438   2.362  1.00 17.24           C  
ANISOU 4049  CD2 TYR A 534     2234   1951   2363     23    202   -102       C  
ATOM   4050  CE1 TYR A 534       2.226  22.097   2.248  1.00 16.01           C  
ANISOU 4050  CE1 TYR A 534     2085   1762   2234      0    210   -114       C  
ATOM   4051  CE2 TYR A 534       3.659  23.709   3.304  1.00 18.93           C  
ANISOU 4051  CE2 TYR A 534     2447   2164   2582     15    203    -94       C  
ATOM   4052  CZ  TYR A 534       2.448  23.040   3.243  1.00 21.43           C  
ANISOU 4052  CZ  TYR A 534     2766   2463   2911      4    206   -100       C  
ATOM   4053  OH  TYR A 534       1.466  23.299   4.183  1.00 20.46           O  
ANISOU 4053  OH  TYR A 534     2640   2340   2792     -4    208    -92       O  
ATOM   4054  N   CYS A 535       3.257  24.014  -1.295  1.00 18.65           N  
ANISOU 4054  N   CYS A 535     2413   2135   2537      5    186   -148       N  
ATOM   4055  CA  CYS A 535       2.676  25.335  -1.152  1.00 20.73           C  
ANISOU 4055  CA  CYS A 535     2672   2413   2790      1    180   -145       C  
ATOM   4056  C   CYS A 535       1.433  25.203  -0.275  1.00 18.48           C  
ANISOU 4056  C   CYS A 535     2383   2124   2513     -8    181   -142       C  
ATOM   4057  O   CYS A 535       0.565  24.354  -0.494  1.00 18.69           O  
ANISOU 4057  O   CYS A 535     2407   2141   2551    -16    182   -153       O  
ATOM   4058  CB  CYS A 535       2.480  26.009  -2.515  1.00 23.01           C  
ANISOU 4058  CB  CYS A 535     2962   2714   3067      4    174   -158       C  
ATOM   4059  SG  CYS A 535       1.090  25.454  -3.463  1.00 36.80           S  
ANISOU 4059  SG  CYS A 535     4704   4461   4817     -1    169   -179       S  
ATOM   4060  N   GLU A 536       1.441  25.966   0.808  1.00 17.53           N  
ANISOU 4060  N   GLU A 536     2260   2011   2389     -8    181   -127       N  
ATOM   4061  CA  GLU A 536       0.425  25.863   1.857  1.00 17.17           C  
ANISOU 4061  CA  GLU A 536     2210   1961   2351    -15    182   -121       C  
ATOM   4062  C   GLU A 536      -0.999  26.100   1.360  1.00 18.36           C  
ANISOU 4062  C   GLU A 536     2356   2118   2501    -24    177   -134       C  
ATOM   4063  O   GLU A 536      -1.275  27.062   0.624  1.00 17.58           O  
ANISOU 4063  O   GLU A 536     2255   2034   2389    -20    169   -141       O  
ATOM   4064  CB  GLU A 536       0.770  26.850   2.979  1.00 18.23           C  
ANISOU 4064  CB  GLU A 536     2342   2105   2477    -12    182   -105       C  
ATOM   4065  CG  GLU A 536      -0.200  26.812   4.142  1.00 19.56           C  
ANISOU 4065  CG  GLU A 536     2507   2272   2652    -19    184    -96       C  
ATOM   4066  CD  GLU A 536       0.222  27.687   5.318  1.00 21.41           C  
ANISOU 4066  CD  GLU A 536     2738   2516   2878    -15    184    -81       C  
ATOM   4067  OE1 GLU A 536       1.367  28.195   5.351  1.00 21.38           O  
ANISOU 4067  OE1 GLU A 536     2735   2522   2867     -8    185    -78       O  
ATOM   4068  OE2 GLU A 536      -0.607  27.827   6.244  1.00 23.49           O  
ANISOU 4068  OE2 GLU A 536     2998   2780   3144    -19    185    -74       O  
ATOM   4069  N   SER A 537      -1.903  25.226   1.795  1.00 17.56           N  
ANISOU 4069  N   SER A 537     2250   2006   2413    -35    181   -139       N  
ATOM   4070  CA  SER A 537      -3.302  25.318   1.423  1.00 19.54           C  
ANISOU 4070  CA  SER A 537     2492   2265   2665    -45    177   -154       C  
ATOM   4071  C   SER A 537      -3.894  26.696   1.723  1.00 19.42           C  
ANISOU 4071  C   SER A 537     2472   2271   2635    -41    168   -149       C  
ATOM   4072  O   SER A 537      -3.665  27.254   2.797  1.00 18.73           O  
ANISOU 4072  O   SER A 537     2387   2184   2546    -39    170   -131       O  
ATOM   4073  CB  SER A 537      -4.093  24.236   2.156  1.00 20.92           C  
ANISOU 4073  CB  SER A 537     2665   2425   2858    -59    188   -157       C  
ATOM   4074  OG  SER A 537      -5.426  24.272   1.699  1.00 23.12           O  
ANISOU 4074  OG  SER A 537     2931   2716   3137    -70    183   -178       O  
ATOM   4075  N   GLY A 538      -4.660  27.244   0.785  1.00 20.34           N  
ANISOU 4075  N   GLY A 538     2582   2404   2739    -38    160   -164       N  
ATOM   4076  CA  GLY A 538      -5.396  28.484   1.043  1.00 20.82           C  
ANISOU 4076  CA  GLY A 538     2640   2484   2786    -32    153   -160       C  
ATOM   4077  C   GLY A 538      -4.611  29.756   0.761  1.00 22.20           C  
ANISOU 4077  C   GLY A 538     2826   2666   2943    -17    151   -148       C  
ATOM   4078  O   GLY A 538      -5.130  30.861   0.928  1.00 22.29           O  
ANISOU 4078  O   GLY A 538     2839   2690   2940    -10    148   -144       O  
ATOM   4079  N   MET A 539      -3.358  29.614   0.332  1.00 21.98           N  
ANISOU 4079  N   MET A 539     2807   2629   2915    -13    155   -145       N  
ATOM   4080  CA  MET A 539      -2.475  30.756   0.081  1.00 21.33           C  
ANISOU 4080  CA  MET A 539     2736   2551   2818     -3    158   -135       C  
ATOM   4081  C   MET A 539      -2.147  30.894  -1.414  1.00 22.88           C  
ANISOU 4081  C   MET A 539     2938   2752   3002      7    156   -147       C  
ATOM   4082  O   MET A 539      -1.078  30.471  -1.863  1.00 23.77           O  
ANISOU 4082  O   MET A 539     3056   2857   3118      7    160   -148       O  
ATOM   4083  CB  MET A 539      -1.178  30.621   0.885  1.00 19.39           C  
ANISOU 4083  CB  MET A 539     2493   2295   2579     -6    165   -122       C  
ATOM   4084  CG  MET A 539      -1.318  30.430   2.392  1.00 19.16           C  
ANISOU 4084  CG  MET A 539     2459   2261   2560    -13    167   -110       C  
ATOM   4085  SD  MET A 539      -2.192  31.801   3.191  1.00 24.92           S  
ANISOU 4085  SD  MET A 539     3187   3002   3278    -13    165   -101       S  
ATOM   4086  CE  MET A 539      -1.623  31.507   4.876  1.00 24.77           C  
ANISOU 4086  CE  MET A 539     3163   2977   3269    -18    171    -85       C  
ATOM   4087  N   ASP A 540      -3.056  31.504  -2.170  1.00 22.13           N  
ANISOU 4087  N   ASP A 540     2844   2672   2891     17    150   -155       N  
ATOM   4088  CA  ASP A 540      -2.941  31.620  -3.626  1.00 20.70           C  
ANISOU 4088  CA  ASP A 540     2669   2499   2696     31    148   -167       C  
ATOM   4089  C   ASP A 540      -1.637  32.331  -3.968  1.00 20.15           C  
ANISOU 4089  C   ASP A 540     2614   2422   2618     37    158   -157       C  
ATOM   4090  O   ASP A 540      -1.439  33.479  -3.570  1.00 18.87           O  
ANISOU 4090  O   ASP A 540     2463   2259   2445     40    165   -145       O  
ATOM   4091  CB  ASP A 540      -4.133  32.435  -4.129  1.00 20.88           C  
ANISOU 4091  CB  ASP A 540     2691   2542   2698     46    142   -174       C  
ATOM   4092  CG  ASP A 540      -4.292  32.430  -5.643  1.00 28.69           C  
ANISOU 4092  CG  ASP A 540     3683   3545   3670     64    138   -189       C  
ATOM   4093  OD1 ASP A 540      -3.934  31.428  -6.312  1.00 31.49           O  
ANISOU 4093  OD1 ASP A 540     4033   3897   4035     59    135   -202       O  
ATOM   4094  OD2 ASP A 540      -4.821  33.445  -6.166  1.00 32.48           O  
ANISOU 4094  OD2 ASP A 540     4172   4041   4127     85    137   -188       O  
ATOM   4095  N   VAL A 541      -0.747  31.650  -4.682  1.00 17.69           N  
ANISOU 4095  N   VAL A 541     2305   2104   2311     36    160   -163       N  
ATOM   4096  CA  VAL A 541       0.597  32.176  -4.884  1.00 18.36           C  
ANISOU 4096  CA  VAL A 541     2401   2182   2391     38    171   -155       C  
ATOM   4097  C   VAL A 541       1.024  32.105  -6.353  1.00 19.41           C  
ANISOU 4097  C   VAL A 541     2543   2319   2513     50    172   -165       C  
ATOM   4098  O   VAL A 541       0.615  31.206  -7.100  1.00 18.31           O  
ANISOU 4098  O   VAL A 541     2396   2183   2376     53    164   -179       O  
ATOM   4099  CB  VAL A 541       1.617  31.497  -3.939  1.00 17.89           C  
ANISOU 4099  CB  VAL A 541     2336   2111   2349     25    175   -149       C  
ATOM   4100  CG1 VAL A 541       1.765  30.007  -4.231  1.00 18.64           C  
ANISOU 4100  CG1 VAL A 541     2422   2199   2458     21    170   -158       C  
ATOM   4101  CG2 VAL A 541       2.979  32.185  -3.983  1.00 18.24           C  
ANISOU 4101  CG2 VAL A 541     2388   2152   2387     24    187   -143       C  
ATOM   4102  N   GLU A 542       1.840  33.070  -6.760  1.00 18.98           N  
ANISOU 4102  N   GLU A 542     2503   2262   2445     56    185   -158       N  
ATOM   4103  CA  GLU A 542       2.487  32.994  -8.061  1.00 21.22           C  
ANISOU 4103  CA  GLU A 542     2795   2547   2718     66    189   -165       C  
ATOM   4104  C   GLU A 542       3.987  33.224  -7.951  1.00 19.62           C  
ANISOU 4104  C   GLU A 542     2598   2335   2519     57    203   -160       C  
ATOM   4105  O   GLU A 542       4.443  33.983  -7.095  1.00 19.01           O  
ANISOU 4105  O   GLU A 542     2524   2253   2442     48    213   -151       O  
ATOM   4106  CB  GLU A 542       1.820  33.946  -9.055  1.00 22.38           C  
ANISOU 4106  CB  GLU A 542     2957   2704   2841     87    192   -166       C  
ATOM   4107  CG  GLU A 542       2.216  35.387  -8.966  1.00 29.57           C  
ANISOU 4107  CG  GLU A 542     3889   3609   3736     91    210   -153       C  
ATOM   4108  CD  GLU A 542       1.843  36.125 -10.242  1.00 41.71           C  
ANISOU 4108  CD  GLU A 542     5446   5155   5248    117    216   -154       C  
ATOM   4109  OE1 GLU A 542       1.890  35.486 -11.315  1.00 43.91           O  
ANISOU 4109  OE1 GLU A 542     5721   5440   5520    128    210   -165       O  
ATOM   4110  OE2 GLU A 542       1.501  37.328 -10.168  1.00 44.20           O  
ANISOU 4110  OE2 GLU A 542     5779   5467   5545    128    228   -143       O  
ATOM   4111  N   ILE A 543       4.754  32.518  -8.775  1.00 19.52           N  
ANISOU 4111  N   ILE A 543     2585   2322   2508     60    203   -168       N  
ATOM   4112  CA  ILE A 543       6.203  32.683  -8.768  1.00 18.80           C  
ANISOU 4112  CA  ILE A 543     2497   2226   2419     52    216   -166       C  
ATOM   4113  C   ILE A 543       6.568  33.155 -10.166  1.00 19.19           C  
ANISOU 4113  C   ILE A 543     2562   2278   2452     65    225   -171       C  
ATOM   4114  O   ILE A 543       6.120  32.563 -11.144  1.00 19.01           O  
ANISOU 4114  O   ILE A 543     2538   2260   2424     77    216   -180       O  
ATOM   4115  CB  ILE A 543       6.957  31.383  -8.405  1.00 19.73           C  
ANISOU 4115  CB  ILE A 543     2599   2341   2554     45    210   -171       C  
ATOM   4116  CG1 ILE A 543       6.561  30.895  -7.007  1.00 22.66           C  
ANISOU 4116  CG1 ILE A 543     2958   2710   2941     35    202   -165       C  
ATOM   4117  CG2 ILE A 543       8.461  31.660  -8.356  1.00 19.32           C  
ANISOU 4117  CG2 ILE A 543     2548   2290   2501     39    223   -171       C  
ATOM   4118  CD1 ILE A 543       5.306  30.051  -6.936  1.00 25.95           C  
ANISOU 4118  CD1 ILE A 543     3369   3125   3367     37    189   -170       C  
ATOM   4119  N   SER A 544       7.324  34.245 -10.253  1.00 19.27           N  
ANISOU 4119  N   SER A 544     2586   2284   2451     62    245   -165       N  
ATOM   4120  CA  SER A 544       7.703  34.836 -11.536  1.00 20.28           C  
ANISOU 4120  CA  SER A 544     2732   2412   2561     74    259   -167       C  
ATOM   4121  C   SER A 544       8.805  34.012 -12.188  1.00 21.75           C  
ANISOU 4121  C   SER A 544     2911   2599   2752     72    259   -176       C  
ATOM   4122  O   SER A 544       9.513  33.270 -11.496  1.00 21.25           O  
ANISOU 4122  O   SER A 544     2831   2536   2704     59    255   -179       O  
ATOM   4123  CB  SER A 544       8.261  36.251 -11.331  1.00 19.33           C  
ANISOU 4123  CB  SER A 544     2630   2283   2430     67    285   -159       C  
ATOM   4124  OG  SER A 544       9.556  36.246 -10.732  1.00 17.34           O  
ANISOU 4124  OG  SER A 544     2369   2029   2189     47    296   -162       O  
ATOM   4125  N   PRO A 545       8.985  34.176 -13.510  1.00 23.06           N  
ANISOU 4125  N   PRO A 545     3091   2767   2903     87    266   -180       N  
ATOM   4126  CA  PRO A 545      10.218  33.675 -14.118  1.00 22.98           C  
ANISOU 4126  CA  PRO A 545     3077   2758   2895     83    273   -187       C  
ATOM   4127  C   PRO A 545      11.433  34.335 -13.458  1.00 22.28           C  
ANISOU 4127  C   PRO A 545     2989   2665   2811     63    293   -186       C  
ATOM   4128  O   PRO A 545      11.297  35.376 -12.812  1.00 20.83           O  
ANISOU 4128  O   PRO A 545     2813   2476   2623     55    307   -178       O  
ATOM   4129  CB  PRO A 545      10.117  34.154 -15.570  1.00 24.33           C  
ANISOU 4129  CB  PRO A 545     3268   2930   3044    103    283   -188       C  
ATOM   4130  CG  PRO A 545       8.646  34.399 -15.801  1.00 24.85           C  
ANISOU 4130  CG  PRO A 545     3341   3001   3098    122    271   -185       C  
ATOM   4131  CD  PRO A 545       8.086  34.834 -14.480  1.00 22.84           C  
ANISOU 4131  CD  PRO A 545     3081   2742   2852    109    269   -177       C  
ATOM   4132  N   ILE A 546      12.614  33.748 -13.639  1.00 21.88           N  
ANISOU 4132  N   ILE A 546     2928   2619   2766     56    296   -194       N  
ATOM   4133  CA  ILE A 546      13.878  34.380 -13.256  1.00 22.74           C  
ANISOU 4133  CA  ILE A 546     3034   2729   2875     39    318   -198       C  
ATOM   4134  C   ILE A 546      14.036  35.668 -14.062  1.00 23.85           C  
ANISOU 4134  C   ILE A 546     3201   2861   2998     40    345   -194       C  
ATOM   4135  O   ILE A 546      13.932  35.647 -15.285  1.00 23.39           O  
ANISOU 4135  O   ILE A 546     3157   2801   2927     56    349   -194       O  
ATOM   4136  CB  ILE A 546      15.087  33.433 -13.475  1.00 21.59           C  
ANISOU 4136  CB  ILE A 546     2871   2593   2736     35    315   -209       C  
ATOM   4137  CG1 ILE A 546      14.919  32.189 -12.593  1.00 20.81           C  
ANISOU 4137  CG1 ILE A 546     2750   2499   2654     37    291   -210       C  
ATOM   4138  CG2 ILE A 546      16.392  34.142 -13.103  1.00 22.34           C  
ANISOU 4138  CG2 ILE A 546     2961   2695   2831     16    338   -217       C  
ATOM   4139  CD1 ILE A 546      15.849  31.040 -12.936  1.00 17.76           C  
ANISOU 4139  CD1 ILE A 546     2351   2122   2274     42    284   -220       C  
ATOM   4140  N   THR A 547      14.278  36.773 -13.365  1.00 22.86           N  
ANISOU 4140  N   THR A 547     3082   2729   2872     23    366   -192       N  
ATOM   4141  CA  THR A 547      14.104  38.110 -13.915  1.00 23.50           C  
ANISOU 4141  CA  THR A 547     3195   2797   2937     26    394   -185       C  
ATOM   4142  C   THR A 547      15.409  38.860 -13.715  1.00 23.75           C  
ANISOU 4142  C   THR A 547     3227   2826   2969      0    425   -194       C  
ATOM   4143  O   THR A 547      15.992  38.817 -12.631  1.00 21.37           O  
ANISOU 4143  O   THR A 547     2905   2533   2681    -20    425   -203       O  
ATOM   4144  CB  THR A 547      12.922  38.810 -13.202  1.00 22.59           C  
ANISOU 4144  CB  THR A 547     3090   2673   2818     30    391   -173       C  
ATOM   4145  OG1 THR A 547      11.747  38.024 -13.433  1.00 23.71           O  
ANISOU 4145  OG1 THR A 547     3227   2822   2960     51    362   -168       O  
ATOM   4146  CG2 THR A 547      12.672  40.221 -13.728  1.00 24.48           C  
ANISOU 4146  CG2 THR A 547     3365   2896   3039     36    422   -163       C  
ATOM   4147  N   HIS A 548      15.883  39.507 -14.776  1.00 25.44           N  
ANISOU 4147  N   HIS A 548     3465   3031   3169      3    453   -195       N  
ATOM   4148  CA  HIS A 548      17.147  40.226 -14.701  1.00 27.22           C  
ANISOU 4148  CA  HIS A 548     3692   3255   3396    -22    486   -207       C  
ATOM   4149  C   HIS A 548      16.995  41.494 -13.873  1.00 27.61           C  
ANISOU 4149  C   HIS A 548     3755   3290   3445    -41    511   -205       C  
ATOM   4150  O   HIS A 548      16.042  42.238 -14.088  1.00 28.91           O  
ANISOU 4150  O   HIS A 548     3948   3437   3597    -26    520   -190       O  
ATOM   4151  CB  HIS A 548      17.632  40.562 -16.114  1.00 29.33           C  
ANISOU 4151  CB  HIS A 548     3983   3512   3647    -14    511   -207       C  
ATOM   4152  CG  HIS A 548      19.001  41.165 -16.150  1.00 33.21           C  
ANISOU 4152  CG  HIS A 548     4473   4003   4139    -43    547   -222       C  
ATOM   4153  ND1 HIS A 548      19.363  42.134 -17.061  1.00 38.29           N  
ANISOU 4153  ND1 HIS A 548     5149   4628   4768    -45    587   -220       N  
ATOM   4154  CD2 HIS A 548      20.091  40.950 -15.374  1.00 33.57           C  
ANISOU 4154  CD2 HIS A 548     4488   4066   4198    -70    550   -242       C  
ATOM   4155  CE1 HIS A 548      20.622  42.478 -16.855  1.00 38.59           C  
ANISOU 4155  CE1 HIS A 548     5177   4671   4813    -76    614   -239       C  
ATOM   4156  NE2 HIS A 548      21.086  41.774 -15.839  1.00 36.65           N  
ANISOU 4156  NE2 HIS A 548     4891   4449   4583    -92    591   -254       N  
ATOM   4157  N   LEU A 549      17.908  41.730 -12.934  1.00 27.55           N  
ANISOU 4157  N   LEU A 549     3727   3291   3449    -71    523   -220       N  
ATOM   4158  CA  LEU A 549      17.968  42.998 -12.211  1.00 28.92           C  
ANISOU 4158  CA  LEU A 549     3913   3451   3622    -94    553   -224       C  
ATOM   4159  C   LEU A 549      19.050  43.906 -12.809  1.00 30.81           C  
ANISOU 4159  C   LEU A 549     4170   3679   3855   -117    599   -237       C  
ATOM   4160  O   LEU A 549      18.734  44.945 -13.391  1.00 31.97           O  
ANISOU 4160  O   LEU A 549     4355   3800   3990   -113    631   -227       O  
ATOM   4161  CB  LEU A 549      18.195  42.779 -10.710  1.00 28.26           C  
ANISOU 4161  CB  LEU A 549     3796   3385   3554   -114    538   -235       C  
ATOM   4162  CG  LEU A 549      18.098  43.992  -9.780  1.00 29.45           C  
ANISOU 4162  CG  LEU A 549     3956   3525   3707   -137    563   -239       C  
ATOM   4163  CD1 LEU A 549      16.655  44.392  -9.525  1.00 28.65           C  
ANISOU 4163  CD1 LEU A 549     3877   3406   3600   -118    553   -217       C  
ATOM   4164  CD2 LEU A 549      18.811  43.747  -8.464  1.00 27.22           C  
ANISOU 4164  CD2 LEU A 549     3635   3267   3438   -161    554   -259       C  
ATOM   4165  N   TYR A 550      20.318  43.537 -12.650  1.00 30.82           N  
ANISOU 4165  N   TYR A 550     4142   3701   3865   -139    605   -259       N  
ATOM   4166  CA  TYR A 550      21.419  44.229 -13.319  1.00 32.68           C  
ANISOU 4166  CA  TYR A 550     4389   3930   4095   -162    648   -275       C  
ATOM   4167  C   TYR A 550      22.668  43.357 -13.219  1.00 32.28           C  
ANISOU 4167  C   TYR A 550     4298   3912   4053   -176    637   -299       C  
ATOM   4168  O   TYR A 550      22.774  42.533 -12.305  1.00 31.29           O  
ANISOU 4168  O   TYR A 550     4137   3812   3937   -175    605   -306       O  
ATOM   4169  CB  TYR A 550      21.682  45.622 -12.722  1.00 32.60           C  
ANISOU 4169  CB  TYR A 550     4395   3902   4086   -194    690   -286       C  
ATOM   4170  CG  TYR A 550      22.173  45.606 -11.293  1.00 35.18           C  
ANISOU 4170  CG  TYR A 550     4685   4253   4428   -222    683   -307       C  
ATOM   4171  CD1 TYR A 550      23.514  45.382 -10.996  1.00 37.91           C  
ANISOU 4171  CD1 TYR A 550     4995   4627   4781   -250    691   -338       C  
ATOM   4172  CD2 TYR A 550      21.293  45.826 -10.238  1.00 38.11           C  
ANISOU 4172  CD2 TYR A 550     5053   4621   4804   -219    666   -298       C  
ATOM   4173  CE1 TYR A 550      23.963  45.352  -9.687  1.00 40.34           C  
ANISOU 4173  CE1 TYR A 550     5266   4962   5099   -272    683   -360       C  
ATOM   4174  CE2 TYR A 550      21.732  45.814  -8.925  1.00 39.17           C  
ANISOU 4174  CE2 TYR A 550     5153   4779   4950   -243    659   -318       C  
ATOM   4175  CZ  TYR A 550      23.066  45.572  -8.657  1.00 42.43           C  
ANISOU 4175  CZ  TYR A 550     5531   5222   5368   -268    667   -349       C  
ATOM   4176  OH  TYR A 550      23.504  45.560  -7.352  1.00 44.79           O  
ANISOU 4176  OH  TYR A 550     5794   5549   5675   -288    659   -370       O  
ATOM   4177  N   ASP A 551      23.604  43.555 -14.146  1.00 30.93           N  
ANISOU 4177  N   ASP A 551     4135   3740   3876   -186    666   -310       N  
ATOM   4178  CA  ASP A 551      24.827  42.760 -14.208  1.00 30.63           C  
ANISOU 4178  CA  ASP A 551     4059   3734   3842   -197    658   -333       C  
ATOM   4179  C   ASP A 551      24.448  41.280 -14.269  1.00 28.43           C  
ANISOU 4179  C   ASP A 551     3760   3474   3567   -164    608   -323       C  
ATOM   4180  O   ASP A 551      23.648  40.881 -15.122  1.00 28.40           O  
ANISOU 4180  O   ASP A 551     3778   3456   3556   -135    594   -302       O  
ATOM   4181  CB  ASP A 551      25.754  43.067 -13.024  1.00 31.01           C  
ANISOU 4181  CB  ASP A 551     4073   3807   3900   -232    669   -363       C  
ATOM   4182  CG  ASP A 551      26.296  44.495 -13.048  1.00 38.37           C  
ANISOU 4182  CG  ASP A 551     5024   4721   4831   -269    724   -380       C  
ATOM   4183  OD1 ASP A 551      26.324  45.117 -14.134  1.00 39.08           O  
ANISOU 4183  OD1 ASP A 551     5151   4784   4911   -270    758   -372       O  
ATOM   4184  OD2 ASP A 551      26.696  44.991 -11.972  1.00 39.05           O  
ANISOU 4184  OD2 ASP A 551     5089   4821   4925   -298    735   -402       O  
ATOM   4185  N   ASN A 552      25.002  40.474 -13.370  1.00 26.58           N  
ANISOU 4185  N   ASN A 552     3485   3272   3342   -169    584   -338       N  
ATOM   4186  CA  ASN A 552      24.648  39.049 -13.311  1.00 26.66           C  
ANISOU 4186  CA  ASN A 552     3476   3296   3355   -139    539   -328       C  
ATOM   4187  C   ASN A 552      23.682  38.744 -12.166  1.00 25.36           C  
ANISOU 4187  C   ASN A 552     3303   3132   3200   -130    510   -315       C  
ATOM   4188  O   ASN A 552      23.601  37.611 -11.695  1.00 25.81           O  
ANISOU 4188  O   ASN A 552     3337   3206   3262   -113    477   -313       O  
ATOM   4189  CB  ASN A 552      25.900  38.166 -13.219  1.00 25.98           C  
ANISOU 4189  CB  ASN A 552     3352   3245   3271   -142    530   -350       C  
ATOM   4190  CG  ASN A 552      26.791  38.291 -14.446  1.00 26.58           C  
ANISOU 4190  CG  ASN A 552     3436   3322   3339   -147    554   -361       C  
ATOM   4191  OD1 ASN A 552      26.334  38.639 -15.531  1.00 25.33           O  
ANISOU 4191  OD1 ASN A 552     3312   3139   3174   -138    568   -346       O  
ATOM   4192  ND2 ASN A 552      28.072  38.017 -14.271  1.00 28.15           N  
ANISOU 4192  ND2 ASN A 552     3604   3553   3538   -161    561   -386       N  
ATOM   4193  N   ILE A 553      22.956  39.762 -11.718  1.00 24.69           N  
ANISOU 4193  N   ILE A 553     3238   3027   3114   -140    524   -307       N  
ATOM   4194  CA  ILE A 553      22.037  39.580 -10.597  1.00 24.33           C  
ANISOU 4194  CA  ILE A 553     3186   2982   3077   -133    500   -296       C  
ATOM   4195  C   ILE A 553      20.638  39.389 -11.146  1.00 22.44           C  
ANISOU 4195  C   ILE A 553     2973   2719   2834   -106    483   -269       C  
ATOM   4196  O   ILE A 553      20.169  40.195 -11.945  1.00 23.03           O  
ANISOU 4196  O   ILE A 553     3081   2770   2899   -102    504   -259       O  
ATOM   4197  CB  ILE A 553      22.016  40.760  -9.595  1.00 24.34           C  
ANISOU 4197  CB  ILE A 553     3188   2979   3081   -159    522   -304       C  
ATOM   4198  CG1 ILE A 553      23.417  41.078  -9.059  1.00 28.02           C  
ANISOU 4198  CG1 ILE A 553     3625   3471   3549   -189    542   -335       C  
ATOM   4199  CG2 ILE A 553      21.036  40.472  -8.441  1.00 24.45           C  
ANISOU 4199  CG2 ILE A 553     3193   2995   3102   -149    494   -291       C  
ATOM   4200  CD1 ILE A 553      24.184  39.905  -8.469  1.00 34.38           C  
ANISOU 4200  CD1 ILE A 553     4388   4315   4358   -182    515   -349       C  
ATOM   4201  N   TYR A 554      19.994  38.313 -10.709  1.00 21.78           N  
ANISOU 4201  N   TYR A 554     2875   2643   2757    -86    447   -260       N  
ATOM   4202  CA  TYR A 554      18.650  37.972 -11.149  1.00 21.56           C  
ANISOU 4202  CA  TYR A 554     2866   2598   2727    -62    427   -239       C  
ATOM   4203  C   TYR A 554      17.828  37.639  -9.918  1.00 20.75           C  
ANISOU 4203  C   TYR A 554     2750   2499   2633    -59    403   -231       C  
ATOM   4204  O   TYR A 554      18.395  37.373  -8.857  1.00 23.16           O  
ANISOU 4204  O   TYR A 554     3030   2822   2947    -70    397   -240       O  
ATOM   4205  CB  TYR A 554      18.693  36.735 -12.049  1.00 20.43           C  
ANISOU 4205  CB  TYR A 554     2717   2461   2583    -40    406   -238       C  
ATOM   4206  CG  TYR A 554      19.303  36.983 -13.404  1.00 21.73           C  
ANISOU 4206  CG  TYR A 554     2897   2620   2736    -38    427   -243       C  
ATOM   4207  CD1 TYR A 554      20.674  37.177 -13.544  1.00 21.27           C  
ANISOU 4207  CD1 TYR A 554     2827   2575   2677    -56    448   -260       C  
ATOM   4208  CD2 TYR A 554      18.511  37.019 -14.544  1.00 23.10           C  
ANISOU 4208  CD2 TYR A 554     3096   2779   2899    -17    425   -231       C  
ATOM   4209  CE1 TYR A 554      21.243  37.397 -14.794  1.00 25.00           C  
ANISOU 4209  CE1 TYR A 554     3315   3043   3139    -54    468   -265       C  
ATOM   4210  CE2 TYR A 554      19.074  37.243 -15.795  1.00 26.11           C  
ANISOU 4210  CE2 TYR A 554     3494   3158   3269    -12    445   -234       C  
ATOM   4211  CZ  TYR A 554      20.441  37.430 -15.909  1.00 27.61           C  
ANISOU 4211  CZ  TYR A 554     3673   3357   3459    -32    467   -250       C  
ATOM   4212  OH  TYR A 554      21.010  37.656 -17.147  1.00 27.32           O  
ANISOU 4212  OH  TYR A 554     3652   3316   3410    -28    488   -254       O  
ATOM   4213  N   TYR A 555      16.506  37.610 -10.065  1.00 21.21           N  
ANISOU 4213  N   TYR A 555     2824   2543   2690    -42    390   -215       N  
ATOM   4214  CA  TYR A 555      15.640  37.250  -8.938  1.00 19.42           C  
ANISOU 4214  CA  TYR A 555     2586   2318   2472    -39    368   -206       C  
ATOM   4215  C   TYR A 555      14.354  36.576  -9.384  1.00 18.22           C  
ANISOU 4215  C   TYR A 555     2443   2159   2320    -16    344   -193       C  
ATOM   4216  O   TYR A 555      13.973  36.645 -10.561  1.00 18.05           O  
ANISOU 4216  O   TYR A 555     2439   2129   2288     -2    347   -190       O  
ATOM   4217  CB  TYR A 555      15.301  38.494  -8.113  1.00 20.61           C  
ANISOU 4217  CB  TYR A 555     2746   2462   2622    -53    384   -203       C  
ATOM   4218  CG  TYR A 555      14.435  39.499  -8.834  1.00 23.02           C  
ANISOU 4218  CG  TYR A 555     3085   2745   2914    -45    400   -192       C  
ATOM   4219  CD1 TYR A 555      14.987  40.393  -9.750  1.00 26.75           C  
ANISOU 4219  CD1 TYR A 555     3580   3206   3374    -50    431   -195       C  
ATOM   4220  CD2 TYR A 555      13.067  39.568  -8.584  1.00 23.28           C  
ANISOU 4220  CD2 TYR A 555     3128   2771   2945    -30    385   -177       C  
ATOM   4221  CE1 TYR A 555      14.197  41.328 -10.414  1.00 25.96           C  
ANISOU 4221  CE1 TYR A 555     3515   3087   3260    -38    448   -182       C  
ATOM   4222  CE2 TYR A 555      12.268  40.495  -9.240  1.00 26.89           C  
ANISOU 4222  CE2 TYR A 555     3616   3212   3387    -18    399   -166       C  
ATOM   4223  CZ  TYR A 555      12.840  41.360 -10.156  1.00 27.04           C  
ANISOU 4223  CZ  TYR A 555     3660   3219   3393    -20    430   -168       C  
ATOM   4224  OH  TYR A 555      12.045  42.276 -10.790  1.00 28.03           O  
ANISOU 4224  OH  TYR A 555     3820   3329   3502     -3    446   -155       O  
ATOM   4225  N   ILE A 556      13.686  35.926  -8.436  1.00 15.62           N  
ANISOU 4225  N   ILE A 556     2098   1833   2001    -12    323   -188       N  
ATOM   4226  CA  ILE A 556      12.293  35.543  -8.643  1.00 13.71           C  
ANISOU 4226  CA  ILE A 556     1865   1584   1760      3    304   -177       C  
ATOM   4227  C   ILE A 556      11.496  36.305  -7.592  1.00 13.99           C  
ANISOU 4227  C   ILE A 556     1903   1616   1797     -2    305   -169       C  
ATOM   4228  O   ILE A 556      11.986  36.546  -6.489  1.00 13.85           O  
ANISOU 4228  O   ILE A 556     1872   1603   1785    -17    309   -171       O  
ATOM   4229  CB  ILE A 556      12.000  34.026  -8.494  1.00 13.46           C  
ANISOU 4229  CB  ILE A 556     1816   1557   1740     12    279   -178       C  
ATOM   4230  CG1 ILE A 556      12.534  33.498  -7.151  1.00 14.62           C  
ANISOU 4230  CG1 ILE A 556     1942   1713   1900      3    272   -179       C  
ATOM   4231  CG2 ILE A 556      12.613  33.240  -9.662  1.00 13.56           C  
ANISOU 4231  CG2 ILE A 556     1828   1572   1750     22    277   -187       C  
ATOM   4232  CD1 ILE A 556      12.145  32.027  -6.895  1.00 20.71           C  
ANISOU 4232  CD1 ILE A 556     2700   2484   2682     14    251   -178       C  
ATOM   4233  N   LYS A 557      10.284  36.693  -7.971  1.00 14.27           N  
ANISOU 4233  N   LYS A 557     1954   1643   1824      9    301   -160       N  
ATOM   4234  CA  LYS A 557       9.328  37.300  -7.050  1.00 15.39           C  
ANISOU 4234  CA  LYS A 557     2099   1781   1965      7    298   -151       C  
ATOM   4235  C   LYS A 557       8.261  36.272  -6.694  1.00 14.07           C  
ANISOU 4235  C   LYS A 557     1919   1619   1808     17    272   -148       C  
ATOM   4236  O   LYS A 557       7.648  35.676  -7.581  1.00 15.07           O  
ANISOU 4236  O   LYS A 557     2048   1746   1931     31    261   -150       O  
ATOM   4237  CB  LYS A 557       8.644  38.520  -7.670  1.00 13.69           C  
ANISOU 4237  CB  LYS A 557     1911   1556   1732     18    314   -144       C  
ATOM   4238  CG  LYS A 557       7.592  39.127  -6.716  1.00 14.52           C  
ANISOU 4238  CG  LYS A 557     2020   1659   1838     18    310   -135       C  
ATOM   4239  CD  LYS A 557       6.999  40.429  -7.261  1.00 17.72           C  
ANISOU 4239  CD  LYS A 557     2455   2053   2222     31    329   -127       C  
ATOM   4240  CE  LYS A 557       8.002  41.585  -7.134  1.00 14.97           C  
ANISOU 4240  CE  LYS A 557     2122   1692   1870     14    362   -129       C  
ATOM   4241  NZ  LYS A 557       8.300  41.921  -5.699  1.00 17.15           N  
ANISOU 4241  NZ  LYS A 557     2385   1971   2159     -8    365   -131       N  
ATOM   4242  N   ILE A 558       8.057  36.054  -5.399  1.00 13.52           N  
ANISOU 4242  N   ILE A 558     1834   1551   1749      8    264   -144       N  
ATOM   4243  CA  ILE A 558       6.943  35.237  -4.930  1.00 14.05           C  
ANISOU 4243  CA  ILE A 558     1892   1621   1826     14    243   -140       C  
ATOM   4244  C   ILE A 558       5.818  36.194  -4.539  1.00 15.11           C  
ANISOU 4244  C   ILE A 558     2036   1752   1952     17    244   -132       C  
ATOM   4245  O   ILE A 558       6.017  37.006  -3.631  1.00 15.77           O  
ANISOU 4245  O   ILE A 558     2120   1835   2035      7    254   -128       O  
ATOM   4246  CB  ILE A 558       7.362  34.405  -3.694  1.00 14.31           C  
ANISOU 4246  CB  ILE A 558     1903   1657   1874      4    235   -140       C  
ATOM   4247  CG1 ILE A 558       8.373  33.310  -4.079  1.00 14.21           C  
ANISOU 4247  CG1 ILE A 558     1882   1648   1869      6    232   -147       C  
ATOM   4248  CG2 ILE A 558       6.150  33.688  -3.094  1.00 14.20           C  
ANISOU 4248  CG2 ILE A 558     1882   1641   1869      8    219   -135       C  
ATOM   4249  CD1 ILE A 558       9.767  33.782  -4.465  1.00 17.18           C  
ANISOU 4249  CD1 ILE A 558     2259   2029   2238      0    247   -155       C  
ATOM   4250  N   SER A 559       4.657  36.110  -5.192  1.00 15.19           N  
ANISOU 4250  N   SER A 559     2052   1765   1955     32    235   -132       N  
ATOM   4251  CA  SER A 559       3.554  37.023  -4.887  1.00 15.36           C  
ANISOU 4251  CA  SER A 559     2084   1787   1966     39    236   -124       C  
ATOM   4252  C   SER A 559       2.329  36.265  -4.382  1.00 16.21           C  
ANISOU 4252  C   SER A 559     2175   1900   2081     41    216   -125       C  
ATOM   4253  O   SER A 559       1.903  35.285  -5.003  1.00 16.96           O  
ANISOU 4253  O   SER A 559     2262   2000   2180     47    203   -134       O  
ATOM   4254  CB  SER A 559       3.126  37.845  -6.111  1.00 15.41           C  
ANISOU 4254  CB  SER A 559     2112   1793   1950     58    244   -124       C  
ATOM   4255  OG  SER A 559       4.215  38.473  -6.770  1.00 16.68           O  
ANISOU 4255  OG  SER A 559     2289   1945   2102     57    265   -124       O  
ATOM   4256  N   TYR A 560       1.780  36.710  -3.256  1.00 15.04           N  
ANISOU 4256  N   TYR A 560     2024   1753   1936     35    215   -118       N  
ATOM   4257  CA  TYR A 560       0.486  36.217  -2.769  1.00 14.87           C  
ANISOU 4257  CA  TYR A 560     1991   1739   1921     38    199   -118       C  
ATOM   4258  C   TYR A 560      -0.634  37.121  -3.294  1.00 16.00           C  
ANISOU 4258  C   TYR A 560     2145   1889   2043     56    199   -117       C  
ATOM   4259  O   TYR A 560      -0.680  38.311  -2.985  1.00 15.48           O  
ANISOU 4259  O   TYR A 560     2095   1821   1966     60    210   -108       O  
ATOM   4260  CB  TYR A 560       0.511  36.115  -1.235  1.00 13.19           C  
ANISOU 4260  CB  TYR A 560     1766   1524   1721     23    198   -110       C  
ATOM   4261  CG  TYR A 560       1.415  34.982  -0.814  1.00 15.34           C  
ANISOU 4261  CG  TYR A 560     2024   1791   2010     12    195   -113       C  
ATOM   4262  CD1 TYR A 560       0.932  33.679  -0.774  1.00 16.12           C  
ANISOU 4262  CD1 TYR A 560     2111   1889   2122     11    183   -117       C  
ATOM   4263  CD2 TYR A 560       2.774  35.193  -0.559  1.00 15.37           C  
ANISOU 4263  CD2 TYR A 560     2030   1793   2017      5    206   -112       C  
ATOM   4264  CE1 TYR A 560       1.762  32.611  -0.458  1.00 17.01           C  
ANISOU 4264  CE1 TYR A 560     2216   1997   2250      5    183   -118       C  
ATOM   4265  CE2 TYR A 560       3.623  34.125  -0.239  1.00 16.66           C  
ANISOU 4265  CE2 TYR A 560     2180   1955   2192      0    203   -114       C  
ATOM   4266  CZ  TYR A 560       3.099  32.839  -0.187  1.00 17.28           C  
ANISOU 4266  CZ  TYR A 560     2250   2030   2283      1    192   -116       C  
ATOM   4267  OH  TYR A 560       3.894  31.756   0.127  1.00 15.84           O  
ANISOU 4267  OH  TYR A 560     2060   1846   2112      0    191   -116       O  
ATOM   4268  N   ILE A 561      -1.519  36.566  -4.117  1.00 18.91           N  
ANISOU 4268  N   ILE A 561     2509   2270   2406     69    186   -127       N  
ATOM   4269  CA  ILE A 561      -2.570  37.348  -4.762  1.00 21.84           C  
ANISOU 4269  CA  ILE A 561     2890   2654   2754     92    185   -128       C  
ATOM   4270  C   ILE A 561      -3.614  37.879  -3.773  1.00 21.96           C  
ANISOU 4270  C   ILE A 561     2901   2676   2767     93    180   -122       C  
ATOM   4271  O   ILE A 561      -4.051  39.026  -3.880  1.00 22.54           O  
ANISOU 4271  O   ILE A 561     2990   2752   2820    110    188   -114       O  
ATOM   4272  CB  ILE A 561      -3.258  36.530  -5.871  1.00 23.29           C  
ANISOU 4272  CB  ILE A 561     3063   2854   2931    105    171   -145       C  
ATOM   4273  CG1 ILE A 561      -2.213  36.034  -6.886  1.00 25.37           C  
ANISOU 4273  CG1 ILE A 561     3332   3112   3196    105    176   -150       C  
ATOM   4274  CG2 ILE A 561      -4.418  37.312  -6.513  1.00 26.01           C  
ANISOU 4274  CG2 ILE A 561     3414   3218   3248    133    167   -147       C  
ATOM   4275  CD1 ILE A 561      -1.190  37.060  -7.343  1.00 26.10           C  
ANISOU 4275  CD1 ILE A 561     3449   3192   3276    112    195   -139       C  
ATOM   4276  N   ASP A 562      -4.034  37.065  -2.814  1.00 20.31           N  
ANISOU 4276  N   ASP A 562     2671   2469   2577     76    170   -124       N  
ATOM   4277  CA  ASP A 562      -4.790  37.637  -1.696  1.00 18.93           C  
ANISOU 4277  CA  ASP A 562     2493   2297   2402     74    169   -116       C  
ATOM   4278  C   ASP A 562      -3.996  37.492  -0.408  1.00 17.90           C  
ANISOU 4278  C   ASP A 562     2357   2151   2290     52    174   -106       C  
ATOM   4279  O   ASP A 562      -4.230  36.571   0.375  1.00 17.48           O  
ANISOU 4279  O   ASP A 562     2287   2099   2256     38    167   -108       O  
ATOM   4280  CB  ASP A 562      -6.198  37.055  -1.570  1.00 18.52           C  
ANISOU 4280  CB  ASP A 562     2421   2263   2351     77    153   -127       C  
ATOM   4281  CG  ASP A 562      -7.060  37.796  -0.541  1.00 24.23           C  
ANISOU 4281  CG  ASP A 562     3143   2993   3070     78    152   -118       C  
ATOM   4282  OD1 ASP A 562      -6.635  38.804   0.077  1.00 21.77           O  
ANISOU 4282  OD1 ASP A 562     2846   2671   2753     79    163   -104       O  
ATOM   4283  OD2 ASP A 562      -8.191  37.330  -0.314  1.00 26.31           O  
ANISOU 4283  OD2 ASP A 562     3388   3271   3334     78    141   -128       O  
ATOM   4284  N   GLY A 563      -3.069  38.423  -0.185  1.00 16.66           N  
ANISOU 4284  N   GLY A 563     2216   1984   2128     49    189    -97       N  
ATOM   4285  CA  GLY A 563      -2.220  38.373   0.998  1.00 15.96           C  
ANISOU 4285  CA  GLY A 563     2122   1887   2055     31    195    -90       C  
ATOM   4286  C   GLY A 563      -2.954  38.567   2.320  1.00 16.68           C  
ANISOU 4286  C   GLY A 563     2203   1981   2151     25    190    -83       C  
ATOM   4287  O   GLY A 563      -2.368  38.314   3.376  1.00 15.72           O  
ANISOU 4287  O   GLY A 563     2073   1856   2043     11    192    -78       O  
ATOM   4288  N   THR A 564      -4.218  38.997   2.296  1.00 15.92           N  
ANISOU 4288  N   THR A 564     2108   1895   2044     37    184    -82       N  
ATOM   4289  CA  THR A 564      -4.992  39.133   3.540  1.00 15.48           C  
ANISOU 4289  CA  THR A 564     2042   1844   1993     31    179    -76       C  
ATOM   4290  C   THR A 564      -5.188  37.820   4.296  1.00 17.17           C  
ANISOU 4290  C   THR A 564     2236   2060   2229     17    169    -78       C  
ATOM   4291  O   THR A 564      -5.442  37.817   5.509  1.00 16.05           O  
ANISOU 4291  O   THR A 564     2085   1917   2094      9    168    -71       O  
ATOM   4292  CB  THR A 564      -6.365  39.829   3.325  1.00 17.52           C  
ANISOU 4292  CB  THR A 564     2305   2116   2235     49    174    -77       C  
ATOM   4293  OG1 THR A 564      -7.263  38.942   2.638  1.00 16.52           O  
ANISOU 4293  OG1 THR A 564     2164   2003   2107     55    161    -89       O  
ATOM   4294  CG2 THR A 564      -6.195  41.132   2.515  1.00 16.84           C  
ANISOU 4294  CG2 THR A 564     2246   2027   2125     68    187    -73       C  
ATOM   4295  N   ASN A 565      -5.039  36.702   3.590  1.00 15.78           N  
ANISOU 4295  N   ASN A 565     2052   1882   2062     15    164    -88       N  
ATOM   4296  CA  ASN A 565      -5.050  35.383   4.230  1.00 16.42           C  
ANISOU 4296  CA  ASN A 565     2116   1957   2162      1    160    -89       C  
ATOM   4297  C   ASN A 565      -3.812  35.085   5.063  1.00 15.72           C  
ANISOU 4297  C   ASN A 565     2028   1859   2085     -7    166    -80       C  
ATOM   4298  O   ASN A 565      -3.810  34.121   5.823  1.00 16.61           O  
ANISOU 4298  O   ASN A 565     2131   1967   2213    -15    165    -77       O  
ATOM   4299  CB  ASN A 565      -5.304  34.270   3.201  1.00 16.53           C  
ANISOU 4299  CB  ASN A 565     2124   1972   2182      1    154   -104       C  
ATOM   4300  CG  ASN A 565      -6.632  34.460   2.486  1.00 22.55           C  
ANISOU 4300  CG  ASN A 565     2882   2751   2933     11    146   -116       C  
ATOM   4301  OD1 ASN A 565      -6.710  34.526   1.255  1.00 24.53           O  
ANISOU 4301  OD1 ASN A 565     3137   3010   3173     22    143   -127       O  
ATOM   4302  ND2 ASN A 565      -7.674  34.659   3.274  1.00 15.77           N  
ANISOU 4302  ND2 ASN A 565     2015   1902   2075      8    142   -115       N  
ATOM   4303  N   ILE A 566      -2.752  35.873   4.900  1.00 14.60           N  
ANISOU 4303  N   ILE A 566     1896   1714   1935     -5    175    -77       N  
ATOM   4304  CA  ILE A 566      -1.627  35.821   5.845  1.00 15.11           C  
ANISOU 4304  CA  ILE A 566     1957   1776   2007    -13    181    -71       C  
ATOM   4305  C   ILE A 566      -1.922  36.858   6.920  1.00 15.59           C  
ANISOU 4305  C   ILE A 566     2019   1842   2062    -15    184    -63       C  
ATOM   4306  O   ILE A 566      -1.871  38.067   6.662  1.00 15.52           O  
ANISOU 4306  O   ILE A 566     2022   1833   2041    -12    192    -63       O  
ATOM   4307  CB  ILE A 566      -0.263  36.115   5.174  1.00 14.79           C  
ANISOU 4307  CB  ILE A 566     1924   1732   1961    -13    190    -75       C  
ATOM   4308  CG1 ILE A 566      -0.173  35.322   3.867  1.00 15.23           C  
ANISOU 4308  CG1 ILE A 566     1983   1785   2019     -9    186    -84       C  
ATOM   4309  CG2 ILE A 566       0.914  35.857   6.149  1.00 13.18           C  
ANISOU 4309  CG2 ILE A 566     1711   1532   1765    -20    194    -73       C  
ATOM   4310  CD1 ILE A 566       1.091  35.618   3.043  1.00 19.32           C  
ANISOU 4310  CD1 ILE A 566     2509   2300   2531     -8    195    -90       C  
ATOM   4311  N   CYS A 567      -2.225  36.365   8.120  1.00 15.70           N  
ANISOU 4311  N   CYS A 567     2021   1858   2085    -19    180    -56       N  
ATOM   4312  CA  CYS A 567      -2.738  37.216   9.185  1.00 16.02           C  
ANISOU 4312  CA  CYS A 567     2060   1904   2121    -21    181    -49       C  
ATOM   4313  C   CYS A 567      -2.541  36.578  10.560  1.00 16.16           C  
ANISOU 4313  C   CYS A 567     2066   1925   2148    -24    180    -41       C  
ATOM   4314  O   CYS A 567      -2.595  35.347  10.695  1.00 15.77           O  
ANISOU 4314  O   CYS A 567     2009   1871   2109    -25    177    -39       O  
ATOM   4315  CB  CYS A 567      -4.224  37.500   8.956  1.00 15.27           C  
ANISOU 4315  CB  CYS A 567     1966   1812   2020    -15    175    -49       C  
ATOM   4316  SG  CYS A 567      -5.240  36.011   8.715  1.00 19.79           S  
ANISOU 4316  SG  CYS A 567     2527   2385   2606    -17    166    -54       S  
ATOM   4317  N   PRO A 568      -2.338  37.416  11.591  1.00 16.54           N  
ANISOU 4317  N   PRO A 568     2112   1981   2191    -26    184    -36       N  
ATOM   4318  CA  PRO A 568      -1.979  36.891  12.914  1.00 16.48           C  
ANISOU 4318  CA  PRO A 568     2092   1979   2189    -27    183    -29       C  
ATOM   4319  C   PRO A 568      -3.163  36.329  13.706  1.00 17.07           C  
ANISOU 4319  C   PRO A 568     2161   2054   2271    -26    178    -19       C  
ATOM   4320  O   PRO A 568      -3.510  36.838  14.783  1.00 16.13           O  
ANISOU 4320  O   PRO A 568     2037   1942   2148    -26    178    -13       O  
ATOM   4321  CB  PRO A 568      -1.358  38.103  13.613  1.00 16.66           C  
ANISOU 4321  CB  PRO A 568     2115   2012   2203    -30    190    -31       C  
ATOM   4322  CG  PRO A 568      -1.989  39.299  12.949  1.00 17.78           C  
ANISOU 4322  CG  PRO A 568     2270   2149   2336    -31    193    -35       C  
ATOM   4323  CD  PRO A 568      -2.164  38.880  11.506  1.00 16.37           C  
ANISOU 4323  CD  PRO A 568     2101   1962   2158    -28    191    -39       C  
ATOM   4324  N   ILE A 569      -3.759  35.259  13.190  1.00 16.31           N  
ANISOU 4324  N   ILE A 569     2064   1948   2184    -26    175    -20       N  
ATOM   4325  CA  ILE A 569      -4.981  34.734  13.797  1.00 16.91           C  
ANISOU 4325  CA  ILE A 569     2135   2023   2267    -28    173    -14       C  
ATOM   4326  C   ILE A 569      -4.797  33.337  14.388  1.00 19.17           C  
ANISOU 4326  C   ILE A 569     2417   2299   2565    -28    177     -7       C  
ATOM   4327  O   ILE A 569      -5.725  32.772  14.958  1.00 19.54           O  
ANISOU 4327  O   ILE A 569     2461   2343   2620    -31    179     -2       O  
ATOM   4328  CB  ILE A 569      -6.176  34.747  12.829  1.00 16.63           C  
ANISOU 4328  CB  ILE A 569     2100   1986   2231    -31    168    -24       C  
ATOM   4329  CG1 ILE A 569      -5.986  33.719  11.703  1.00 14.90           C  
ANISOU 4329  CG1 ILE A 569     1883   1757   2020    -33    168    -33       C  
ATOM   4330  CG2 ILE A 569      -6.420  36.152  12.275  1.00 14.89           C  
ANISOU 4330  CG2 ILE A 569     1886   1774   1994    -26    165    -28       C  
ATOM   4331  CD1 ILE A 569      -7.230  33.563  10.827  1.00 18.52           C  
ANISOU 4331  CD1 ILE A 569     2338   2219   2478    -36    163    -46       C  
ATOM   4332  N   GLY A 570      -3.594  32.792  14.279  1.00 20.29           N  
ANISOU 4332  N   GLY A 570     2561   2439   2709    -22    180     -6       N  
ATOM   4333  CA  GLY A 570      -3.375  31.406  14.682  1.00 23.13           C  
ANISOU 4333  CA  GLY A 570     2922   2787   3079    -18    187      0       C  
ATOM   4334  C   GLY A 570      -2.077  30.833  14.145  1.00 25.67           C  
ANISOU 4334  C   GLY A 570     3247   3105   3400    -10    189     -2       C  
ATOM   4335  O   GLY A 570      -1.381  31.454  13.321  1.00 23.39           O  
ANISOU 4335  O   GLY A 570     2958   2822   3104    -11    186    -11       O  
ATOM   4336  N   GLN A 571      -1.749  29.639  14.632  1.00 27.30           N  
ANISOU 4336  N   GLN A 571     3457   3302   3613     -2    196      6       N  
ATOM   4337  CA  GLN A 571      -0.455  29.029  14.352  1.00 28.86           C  
ANISOU 4337  CA  GLN A 571     3657   3499   3808     10    199      6       C  
ATOM   4338  C   GLN A 571      -0.280  28.751  12.858  1.00 28.92           C  
ANISOU 4338  C   GLN A 571     3669   3496   3820      3    197     -7       C  
ATOM   4339  O   GLN A 571       0.836  28.790  12.340  1.00 29.50           O  
ANISOU 4339  O   GLN A 571     3742   3576   3888     10    196    -13       O  
ATOM   4340  CB  GLN A 571      -0.318  27.713  15.115  1.00 31.70           C  
ANISOU 4340  CB  GLN A 571     4023   3846   4173     23    210     19       C  
ATOM   4341  CG  GLN A 571       1.007  27.579  15.844  1.00 39.55           C  
ANISOU 4341  CG  GLN A 571     5014   4856   5155     45    211     26       C  
ATOM   4342  CD  GLN A 571       0.839  27.713  17.347  1.00 47.00           C  
ANISOU 4342  CD  GLN A 571     5953   5811   6091     56    214     41       C  
ATOM   4343  OE1 GLN A 571       1.647  27.188  18.115  1.00 50.74           O  
ANISOU 4343  OE1 GLN A 571     6427   6294   6556     79    219     51       O  
ATOM   4344  NE2 GLN A 571      -0.217  28.406  17.776  1.00 47.91           N  
ANISOU 4344  NE2 GLN A 571     6065   5928   6208     43    212     43       N  
ATOM   4345  N   GLU A 572      -1.374  28.473  12.160  1.00 28.25           N  
ANISOU 4345  N   GLU A 572     3588   3399   3745     -8    197    -14       N  
ATOM   4346  CA  GLU A 572      -1.253  28.188  10.738  1.00 30.17           C  
ANISOU 4346  CA  GLU A 572     3835   3635   3992    -13    195    -28       C  
ATOM   4347  C   GLU A 572      -1.201  29.443   9.865  1.00 27.60           C  
ANISOU 4347  C   GLU A 572     3507   3323   3656    -17    186    -39       C  
ATOM   4348  O   GLU A 572      -0.502  29.484   8.850  1.00 26.73           O  
ANISOU 4348  O   GLU A 572     3400   3213   3543    -15    185    -48       O  
ATOM   4349  CB  GLU A 572      -2.426  27.312  10.296  1.00 32.20           C  
ANISOU 4349  CB  GLU A 572     4094   3876   4262    -24    199    -36       C  
ATOM   4350  CG  GLU A 572      -2.011  26.146   9.415  1.00 41.76           C  
ANISOU 4350  CG  GLU A 572     5312   5070   5482    -24    205    -44       C  
ATOM   4351  CD  GLU A 572      -1.526  24.943  10.212  1.00 51.12           C  
ANISOU 4351  CD  GLU A 572     6507   6239   6675    -14    218    -31       C  
ATOM   4352  OE1 GLU A 572      -0.951  25.121  11.310  1.00 55.27           O  
ANISOU 4352  OE1 GLU A 572     7033   6772   7194     -1    221    -15       O  
ATOM   4353  OE2 GLU A 572      -1.724  23.808   9.727  1.00 56.00           O  
ANISOU 4353  OE2 GLU A 572     7133   6836   7305    -18    228    -37       O  
ATOM   4354  N   GLN A 573      -1.947  30.473  10.250  1.00 22.92           N  
ANISOU 4354  N   GLN A 573     2911   2740   3057    -22    182    -38       N  
ATOM   4355  CA  GLN A 573      -2.216  31.542   9.298  1.00 21.14           C  
ANISOU 4355  CA  GLN A 573     2687   2521   2821    -24    177    -47       C  
ATOM   4356  C   GLN A 573      -1.264  32.740   9.344  1.00 18.47           C  
ANISOU 4356  C   GLN A 573     2351   2194   2470    -21    178    -47       C  
ATOM   4357  O   GLN A 573      -1.269  33.561   8.427  1.00 18.00           O  
ANISOU 4357  O   GLN A 573     2298   2138   2403    -21    177    -55       O  
ATOM   4358  CB  GLN A 573      -3.690  31.952   9.393  1.00 22.41           C  
ANISOU 4358  CB  GLN A 573     2845   2686   2981    -29    173    -49       C  
ATOM   4359  CG  GLN A 573      -4.670  30.773   9.373  1.00 28.12           C  
ANISOU 4359  CG  GLN A 573     3565   3401   3719    -37    174    -54       C  
ATOM   4360  CD  GLN A 573      -5.101  30.246  10.755  1.00 36.92           C  
ANISOU 4360  CD  GLN A 573     4675   4510   4841    -40    180    -41       C  
ATOM   4361  OE1 GLN A 573      -4.341  30.235  11.735  1.00 35.20           O  
ANISOU 4361  OE1 GLN A 573     4459   4293   4623    -33    184    -28       O  
ATOM   4362  NE2 GLN A 573      -6.349  29.785  10.825  1.00 40.01           N  
ANISOU 4362  NE2 GLN A 573     5060   4899   5240    -50    181    -47       N  
ATOM   4363  N   TYR A 574      -0.449  32.866  10.389  1.00 15.87           N  
ANISOU 4363  N   TYR A 574     2017   1872   2139    -18    181    -40       N  
ATOM   4364  CA  TYR A 574       0.402  34.041  10.515  1.00 16.00           C  
ANISOU 4364  CA  TYR A 574     2033   1900   2144    -19    185    -43       C  
ATOM   4365  C   TYR A 574       1.560  34.061   9.518  1.00 16.29           C  
ANISOU 4365  C   TYR A 574     2073   1937   2178    -18    188    -53       C  
ATOM   4366  O   TYR A 574       2.200  35.100   9.316  1.00 14.85           O  
ANISOU 4366  O   TYR A 574     1893   1761   1986    -23    194    -60       O  
ATOM   4367  CB  TYR A 574       0.919  34.203  11.952  1.00 15.81           C  
ANISOU 4367  CB  TYR A 574     1999   1888   2118    -16    187    -36       C  
ATOM   4368  CG  TYR A 574       2.030  33.248  12.335  1.00 18.38           C  
ANISOU 4368  CG  TYR A 574     2319   2220   2446     -7    188    -34       C  
ATOM   4369  CD1 TYR A 574       3.359  33.498  11.970  1.00 20.31           C  
ANISOU 4369  CD1 TYR A 574     2558   2474   2682     -5    192    -45       C  
ATOM   4370  CD2 TYR A 574       1.756  32.107  13.074  1.00 20.48           C  
ANISOU 4370  CD2 TYR A 574     2583   2480   2718      1    188    -23       C  
ATOM   4371  CE1 TYR A 574       4.384  32.625  12.327  1.00 20.26           C  
ANISOU 4371  CE1 TYR A 574     2545   2477   2676      6    193    -44       C  
ATOM   4372  CE2 TYR A 574       2.778  31.229  13.444  1.00 17.54           C  
ANISOU 4372  CE2 TYR A 574     2206   2113   2344     15    191    -20       C  
ATOM   4373  CZ  TYR A 574       4.076  31.497  13.069  1.00 24.06           C  
ANISOU 4373  CZ  TYR A 574     3026   2951   3161     19    192    -31       C  
ATOM   4374  OH  TYR A 574       5.059  30.611  13.445  1.00 25.83           O  
ANISOU 4374  OH  TYR A 574     3246   3184   3382     36    194    -28       O  
ATOM   4375  N   ALA A 575       1.841  32.911   8.911  1.00 16.14           N  
ANISOU 4375  N   ALA A 575     2054   1909   2165    -14    187    -55       N  
ATOM   4376  CA  ALA A 575       2.845  32.863   7.844  1.00 16.99           C  
ANISOU 4376  CA  ALA A 575     2167   2018   2271    -13    190    -65       C  
ATOM   4377  C   ALA A 575       2.382  31.926   6.734  1.00 17.50           C  
ANISOU 4377  C   ALA A 575     2237   2069   2343    -11    186    -69       C  
ATOM   4378  O   ALA A 575       1.757  30.900   7.011  1.00 17.01           O  
ANISOU 4378  O   ALA A 575     2174   1998   2291    -10    184    -65       O  
ATOM   4379  CB  ALA A 575       4.176  32.390   8.387  1.00 15.92           C  
ANISOU 4379  CB  ALA A 575     2022   1892   2134     -6    193    -65       C  
ATOM   4380  N   ALA A 576       2.694  32.267   5.487  1.00 17.47           N  
ANISOU 4380  N   ALA A 576     2240   2064   2333    -11    188    -79       N  
ATOM   4381  CA  ALA A 576       2.485  31.317   4.390  1.00 17.26           C  
ANISOU 4381  CA  ALA A 576     2216   2027   2312     -9    185    -86       C  
ATOM   4382  C   ALA A 576       3.788  30.605   4.060  1.00 16.34           C  
ANISOU 4382  C   ALA A 576     2099   1911   2198     -3    188    -90       C  
ATOM   4383  O   ALA A 576       4.796  31.246   3.766  1.00 17.02           O  
ANISOU 4383  O   ALA A 576     2185   2005   2275     -3    193    -94       O  
ATOM   4384  CB  ALA A 576       1.969  32.012   3.135  1.00 14.68           C  
ANISOU 4384  CB  ALA A 576     1899   1701   1977     -8    183    -94       C  
ATOM   4385  N   GLU A 577       3.727  29.279   4.014  1.00 15.68           N  
ANISOU 4385  N   GLU A 577     2015   1817   2125      0    187    -89       N  
ATOM   4386  CA  GLU A 577       4.900  28.481   3.747  1.00 15.51           C  
ANISOU 4386  CA  GLU A 577     1993   1794   2104      8    190    -92       C  
ATOM   4387  C   GLU A 577       4.929  28.065   2.281  1.00 16.19           C  
ANISOU 4387  C   GLU A 577     2085   1873   2191      9    188   -103       C  
ATOM   4388  O   GLU A 577       3.936  27.557   1.758  1.00 14.98           O  
ANISOU 4388  O   GLU A 577     1935   1709   2045      5    185   -108       O  
ATOM   4389  CB  GLU A 577       4.937  27.239   4.646  1.00 16.21           C  
ANISOU 4389  CB  GLU A 577     2082   1875   2203     16    192    -82       C  
ATOM   4390  CG  GLU A 577       6.104  26.334   4.261  1.00 17.24           C  
ANISOU 4390  CG  GLU A 577     2213   2003   2332     29    196    -85       C  
ATOM   4391  CD  GLU A 577       6.381  25.230   5.271  1.00 25.08           C  
ANISOU 4391  CD  GLU A 577     3208   2990   3330     43    201    -73       C  
ATOM   4392  OE1 GLU A 577       5.767  25.235   6.352  1.00 27.02           O  
ANISOU 4392  OE1 GLU A 577     3452   3233   3578     43    203    -62       O  
ATOM   4393  OE2 GLU A 577       7.242  24.369   5.001  1.00 26.41           O  
ANISOU 4393  OE2 GLU A 577     3380   3156   3498     56    205    -74       O  
ATOM   4394  N   LEU A 578       6.097  28.240   1.663  1.00 15.72           N  
ANISOU 4394  N   LEU A 578     2026   1821   2125     13    191   -109       N  
ATOM   4395  CA  LEU A 578       6.350  27.786   0.301  1.00 14.99           C  
ANISOU 4395  CA  LEU A 578     1939   1723   2032     16    191   -120       C  
ATOM   4396  C   LEU A 578       7.720  27.134   0.295  1.00 15.52           C  
ANISOU 4396  C   LEU A 578     2003   1794   2098     25    194   -122       C  
ATOM   4397  O   LEU A 578       8.655  27.665   0.895  1.00 17.15           O  
ANISOU 4397  O   LEU A 578     2202   2016   2298     27    198   -120       O  
ATOM   4398  CB  LEU A 578       6.327  28.979  -0.667  1.00 14.63           C  
ANISOU 4398  CB  LEU A 578     1899   1685   1975     12    192   -127       C  
ATOM   4399  CG  LEU A 578       6.663  28.757  -2.144  1.00 15.95           C  
ANISOU 4399  CG  LEU A 578     2071   1849   2137     16    192   -139       C  
ATOM   4400  CD1 LEU A 578       5.547  27.940  -2.777  1.00 19.28           C  
ANISOU 4400  CD1 LEU A 578     2496   2262   2567     17    185   -145       C  
ATOM   4401  CD2 LEU A 578       6.885  30.083  -2.927  1.00 13.83           C  
ANISOU 4401  CD2 LEU A 578     1811   1589   1854     15    198   -142       C  
ATOM   4402  N   GLN A 579       7.838  25.969  -0.334  1.00 14.89           N  
ANISOU 4402  N   GLN A 579     1928   1704   2026     32    194   -127       N  
ATOM   4403  CA  GLN A 579       9.149  25.382  -0.577  1.00 16.10           C  
ANISOU 4403  CA  GLN A 579     2079   1862   2176     44    197   -130       C  
ATOM   4404  C   GLN A 579       9.453  25.496  -2.059  1.00 15.80           C  
ANISOU 4404  C   GLN A 579     2045   1824   2133     43    197   -143       C  
ATOM   4405  O   GLN A 579       8.710  24.953  -2.875  1.00 15.01           O  
ANISOU 4405  O   GLN A 579     1952   1711   2039     41    194   -149       O  
ATOM   4406  CB  GLN A 579       9.171  23.924  -0.120  1.00 16.22           C  
ANISOU 4406  CB  GLN A 579     2098   1862   2200     55    200   -124       C  
ATOM   4407  CG  GLN A 579       9.150  23.890   1.408  1.00 24.01           C  
ANISOU 4407  CG  GLN A 579     3080   2853   3187     61    202   -110       C  
ATOM   4408  CD  GLN A 579       8.997  22.495   1.985  1.00 30.73           C  
ANISOU 4408  CD  GLN A 579     3940   3686   4047     73    208   -101       C  
ATOM   4409  OE1 GLN A 579       9.390  21.502   1.367  1.00 30.13           O  
ANISOU 4409  OE1 GLN A 579     3872   3598   3975     83    212   -105       O  
ATOM   4410  NE2 GLN A 579       8.435  22.425   3.189  1.00 31.73           N  
ANISOU 4410  NE2 GLN A 579     4068   3809   4178     74    211    -88       N  
ATOM   4411  N   PHE A 580      10.508  26.224  -2.414  1.00 14.09           N  
ANISOU 4411  N   PHE A 580     1824   1623   1905     43    201   -148       N  
ATOM   4412  CA  PHE A 580      10.819  26.371  -3.835  1.00 14.66           C  
ANISOU 4412  CA  PHE A 580     1901   1695   1971     43    202   -159       C  
ATOM   4413  C   PHE A 580      12.263  25.935  -4.086  1.00 15.51           C  
ANISOU 4413  C   PHE A 580     2004   1814   2075     53    206   -165       C  
ATOM   4414  O   PHE A 580      13.140  26.055  -3.216  1.00 15.47           O  
ANISOU 4414  O   PHE A 580     1988   1823   2065     56    209   -163       O  
ATOM   4415  CB  PHE A 580      10.541  27.795  -4.353  1.00 14.52           C  
ANISOU 4415  CB  PHE A 580     1888   1683   1943     33    206   -162       C  
ATOM   4416  CG  PHE A 580      11.319  28.890  -3.669  1.00 14.68           C  
ANISOU 4416  CG  PHE A 580     1902   1718   1955     26    215   -160       C  
ATOM   4417  CD1 PHE A 580      12.596  29.237  -4.106  1.00 14.61           C  
ANISOU 4417  CD1 PHE A 580     1889   1721   1938     25    224   -169       C  
ATOM   4418  CD2 PHE A 580      10.758  29.609  -2.619  1.00 15.69           C  
ANISOU 4418  CD2 PHE A 580     2028   1848   2084     19    215   -152       C  
ATOM   4419  CE1 PHE A 580      13.314  30.263  -3.503  1.00 12.89           C  
ANISOU 4419  CE1 PHE A 580     1665   1519   1714     15    234   -172       C  
ATOM   4420  CE2 PHE A 580      11.473  30.643  -1.988  1.00 15.73           C  
ANISOU 4420  CE2 PHE A 580     2027   1867   2082     10    224   -154       C  
ATOM   4421  CZ  PHE A 580      12.738  30.988  -2.447  1.00 13.97           C  
ANISOU 4421  CZ  PHE A 580     1798   1656   1851      7    235   -165       C  
ATOM   4422  N   ARG A 581      12.498  25.434  -5.290  1.00 14.87           N  
ANISOU 4422  N   ARG A 581     1928   1727   1993     57    206   -174       N  
ATOM   4423  CA  ARG A 581      13.801  24.936  -5.681  1.00 15.09           C  
ANISOU 4423  CA  ARG A 581     1951   1764   2015     68    209   -181       C  
ATOM   4424  C   ARG A 581      14.230  25.658  -6.947  1.00 16.01           C  
ANISOU 4424  C   ARG A 581     2071   1887   2122     63    214   -191       C  
ATOM   4425  O   ARG A 581      13.432  25.794  -7.873  1.00 17.14           O  
ANISOU 4425  O   ARG A 581     2225   2021   2266     61    212   -194       O  
ATOM   4426  CB  ARG A 581      13.729  23.431  -5.955  1.00 17.23           C  
ANISOU 4426  CB  ARG A 581     2229   2022   2297     81    205   -182       C  
ATOM   4427  CG  ARG A 581      15.093  22.855  -6.391  1.00 16.35           C  
ANISOU 4427  CG  ARG A 581     2112   1920   2178     95    209   -189       C  
ATOM   4428  CD  ARG A 581      14.943  21.412  -6.832  1.00 23.82           C  
ANISOU 4428  CD  ARG A 581     3067   2848   3133    107    207   -191       C  
ATOM   4429  NE  ARG A 581      14.617  20.563  -5.694  1.00 27.13           N  
ANISOU 4429  NE  ARG A 581     3491   3256   3562    116    208   -179       N  
ATOM   4430  CZ  ARG A 581      14.709  19.238  -5.695  1.00 33.65           C  
ANISOU 4430  CZ  ARG A 581     4325   4064   4393    130    211   -178       C  
ATOM   4431  NH1 ARG A 581      15.094  18.592  -6.789  1.00 32.12           N  
ANISOU 4431  NH1 ARG A 581     4138   3865   4201    137    212   -189       N  
ATOM   4432  NH2 ARG A 581      14.410  18.566  -4.592  1.00 33.94           N  
ANISOU 4432  NH2 ARG A 581     4368   4089   4436    139    216   -165       N  
ATOM   4433  N   ILE A 582      15.471  26.142  -6.964  1.00 15.16           N  
ANISOU 4433  N   ILE A 582     1955   1798   2005     62    222   -197       N  
ATOM   4434  CA  ILE A 582      16.047  26.808  -8.134  1.00 15.08           C  
ANISOU 4434  CA  ILE A 582     1949   1795   1986     58    231   -207       C  
ATOM   4435  C   ILE A 582      17.206  25.900  -8.534  1.00 16.06           C  
ANISOU 4435  C   ILE A 582     2066   1928   2107     71    231   -215       C  
ATOM   4436  O   ILE A 582      18.122  25.702  -7.739  1.00 16.44           O  
ANISOU 4436  O   ILE A 582     2099   1993   2153     76    232   -217       O  
ATOM   4437  CB  ILE A 582      16.552  28.229  -7.759  1.00 16.06           C  
ANISOU 4437  CB  ILE A 582     2069   1932   2101     43    244   -209       C  
ATOM   4438  CG1 ILE A 582      15.384  29.076  -7.220  1.00 17.36           C  
ANISOU 4438  CG1 ILE A 582     2241   2087   2268     33    244   -200       C  
ATOM   4439  CG2 ILE A 582      17.188  28.944  -8.955  1.00 15.43           C  
ANISOU 4439  CG2 ILE A 582     1995   1856   2010     37    258   -219       C  
ATOM   4440  CD1 ILE A 582      15.825  30.310  -6.436  1.00 21.19           C  
ANISOU 4440  CD1 ILE A 582     2720   2584   2747     17    256   -202       C  
ATOM   4441  N   ALA A 583      17.135  25.315  -9.725  1.00 16.46           N  
ANISOU 4441  N   ALA A 583     2125   1970   2158     78    228   -221       N  
ATOM   4442  CA  ALA A 583      18.028  24.216 -10.097  1.00 17.35           C  
ANISOU 4442  CA  ALA A 583     2233   2087   2270     93    226   -227       C  
ATOM   4443  C   ALA A 583      18.697  24.429 -11.442  1.00 17.43           C  
ANISOU 4443  C   ALA A 583     2246   2103   2271     94    233   -239       C  
ATOM   4444  O   ALA A 583      18.048  24.805 -12.423  1.00 18.01           O  
ANISOU 4444  O   ALA A 583     2332   2167   2342     90    233   -241       O  
ATOM   4445  CB  ALA A 583      17.255  22.901 -10.145  1.00 17.31           C  
ANISOU 4445  CB  ALA A 583     2237   2061   2277    104    217   -224       C  
ATOM   4446  N   ALA A 584      19.993  24.134 -11.465  1.00 17.24           N  
ANISOU 4446  N   ALA A 584     2210   2097   2241    102    237   -247       N  
ATOM   4447  CA  ALA A 584      20.758  23.941 -12.693  1.00 16.75           C  
ANISOU 4447  CA  ALA A 584     2150   2041   2171    107    242   -258       C  
ATOM   4448  C   ALA A 584      20.475  22.504 -13.137  1.00 18.37           C  
ANISOU 4448  C   ALA A 584     2363   2232   2385    125    231   -258       C  
ATOM   4449  O   ALA A 584      19.802  21.776 -12.408  1.00 16.86           O  
ANISOU 4449  O   ALA A 584     2175   2026   2203    130    224   -250       O  
ATOM   4450  CB  ALA A 584      22.240  24.150 -12.391  1.00 15.72           C  
ANISOU 4450  CB  ALA A 584     2001   1938   2031    108    251   -268       C  
ATOM   4451  N   PRO A 585      20.922  22.092 -14.341  1.00 18.64           N  
ANISOU 4451  N   PRO A 585     2401   2266   2414    133    233   -268       N  
ATOM   4452  CA  PRO A 585      20.594  20.721 -14.747  1.00 19.56           C  
ANISOU 4452  CA  PRO A 585     2525   2366   2538    148    224   -270       C  
ATOM   4453  C   PRO A 585      21.184  19.654 -13.815  1.00 20.12           C  
ANISOU 4453  C   PRO A 585     2590   2439   2613    165    222   -266       C  
ATOM   4454  O   PRO A 585      22.287  19.808 -13.277  1.00 19.23           O  
ANISOU 4454  O   PRO A 585     2464   2350   2492    172    226   -267       O  
ATOM   4455  CB  PRO A 585      21.195  20.622 -16.157  1.00 19.23           C  
ANISOU 4455  CB  PRO A 585     2486   2330   2487    154    227   -282       C  
ATOM   4456  CG  PRO A 585      21.106  22.045 -16.655  1.00 19.05           C  
ANISOU 4456  CG  PRO A 585     2465   2316   2455    138    236   -283       C  
ATOM   4457  CD  PRO A 585      21.506  22.862 -15.454  1.00 18.93           C  
ANISOU 4457  CD  PRO A 585     2439   2314   2438    127    242   -277       C  
ATOM   4458  N   GLN A 586      20.426  18.583 -13.608  1.00 20.24           N  
ANISOU 4458  N   GLN A 586     2617   2431   2641    173    217   -262       N  
ATOM   4459  CA  GLN A 586      20.900  17.441 -12.841  1.00 21.97           C  
ANISOU 4459  CA  GLN A 586     2838   2646   2864    193    217   -256       C  
ATOM   4460  C   GLN A 586      22.221  16.995 -13.468  1.00 21.26           C  
ANISOU 4460  C   GLN A 586     2742   2574   2762    211    220   -266       C  
ATOM   4461  O   GLN A 586      22.344  16.906 -14.690  1.00 20.28           O  
ANISOU 4461  O   GLN A 586     2621   2447   2635    210    220   -277       O  
ATOM   4462  CB  GLN A 586      19.881  16.297 -12.862  1.00 22.25           C  
ANISOU 4462  CB  GLN A 586     2890   2648   2914    196    216   -254       C  
ATOM   4463  CG  GLN A 586      20.282  15.147 -11.934  1.00 30.21           C  
ANISOU 4463  CG  GLN A 586     3904   3647   3925    219    220   -245       C  
ATOM   4464  CD  GLN A 586      19.558  13.839 -12.216  1.00 36.50           C  
ANISOU 4464  CD  GLN A 586     4721   4409   4736    224    224   -247       C  
ATOM   4465  OE1 GLN A 586      18.413  13.824 -12.663  1.00 40.17           O  
ANISOU 4465  OE1 GLN A 586     5194   4855   5214    206    223   -253       O  
ATOM   4466  NE2 GLN A 586      20.223  12.727 -11.924  1.00 41.74           N  
ANISOU 4466  NE2 GLN A 586     5394   5064   5398    250    231   -243       N  
ATOM   4467  N   GLY A 587      23.219  16.753 -12.626  1.00 21.22           N  
ANISOU 4467  N   GLY A 587     2725   2588   2748    229    222   -263       N  
ATOM   4468  CA  GLY A 587      24.531  16.307 -13.089  1.00 18.54           C  
ANISOU 4468  CA  GLY A 587     2378   2270   2396    249    224   -272       C  
ATOM   4469  C   GLY A 587      25.564  17.410 -13.168  1.00 19.87           C  
ANISOU 4469  C   GLY A 587     2524   2475   2549    240    228   -282       C  
ATOM   4470  O   GLY A 587      26.763  17.129 -13.169  1.00 18.34           O  
ANISOU 4470  O   GLY A 587     2317   2308   2343    257    230   -290       O  
ATOM   4471  N   THR A 588      25.120  18.664 -13.239  1.00 18.74           N  
ANISOU 4471  N   THR A 588     2376   2334   2407    213    231   -283       N  
ATOM   4472  CA  THR A 588      26.059  19.778 -13.343  1.00 18.73           C  
ANISOU 4472  CA  THR A 588     2356   2365   2393    200    239   -294       C  
ATOM   4473  C   THR A 588      26.682  20.076 -11.983  1.00 19.74           C  
ANISOU 4473  C   THR A 588     2464   2521   2514    204    240   -294       C  
ATOM   4474  O   THR A 588      26.184  19.625 -10.943  1.00 20.20           O  
ANISOU 4474  O   THR A 588     2525   2570   2577    214    234   -282       O  
ATOM   4475  CB  THR A 588      25.436  21.054 -13.939  1.00 20.45           C  
ANISOU 4475  CB  THR A 588     2580   2575   2613    171    246   -296       C  
ATOM   4476  OG1 THR A 588      24.355  21.497 -13.101  1.00 17.41           O  
ANISOU 4476  OG1 THR A 588     2201   2175   2237    159    242   -283       O  
ATOM   4477  CG2 THR A 588      24.947  20.795 -15.367  1.00 18.63           C  
ANISOU 4477  CG2 THR A 588     2368   2325   2386    171    245   -299       C  
ATOM   4478  N   LYS A 589      27.778  20.825 -12.007  1.00 19.11           N  
ANISOU 4478  N   LYS A 589     2363   2476   2422    196    249   -309       N  
ATOM   4479  CA  LYS A 589      28.622  20.986 -10.834  1.00 21.97           C  
ANISOU 4479  CA  LYS A 589     2700   2873   2772    204    249   -315       C  
ATOM   4480  C   LYS A 589      29.074  22.422 -10.583  1.00 22.14           C  
ANISOU 4480  C   LYS A 589     2703   2921   2789    175    261   -330       C  
ATOM   4481  O   LYS A 589      29.997  22.641  -9.800  1.00 26.02           O  
ANISOU 4481  O   LYS A 589     3168   3450   3268    179    264   -343       O  
ATOM   4482  CB  LYS A 589      29.864  20.094 -10.941  1.00 21.07           C  
ANISOU 4482  CB  LYS A 589     2571   2788   2644    234    248   -326       C  
ATOM   4483  CG  LYS A 589      29.590  18.630 -11.195  1.00 23.19           C  
ANISOU 4483  CG  LYS A 589     2860   3033   2917    265    239   -314       C  
ATOM   4484  CD  LYS A 589      28.989  17.921 -10.010  1.00 22.18           C  
ANISOU 4484  CD  LYS A 589     2741   2891   2793    285    232   -296       C  
ATOM   4485  CE  LYS A 589      29.093  16.428 -10.239  1.00 25.31           C  
ANISOU 4485  CE  LYS A 589     3154   3271   3189    320    229   -289       C  
ATOM   4486  NZ  LYS A 589      28.177  15.694  -9.350  1.00 30.68           N  
ANISOU 4486  NZ  LYS A 589     3855   3922   3880    334    227   -268       N  
ATOM   4487  N   PHE A 590      28.442  23.394 -11.228  1.00 21.24           N  
ANISOU 4487  N   PHE A 590     2601   2786   2681    146    270   -329       N  
ATOM   4488  CA  PHE A 590      28.869  24.786 -11.132  1.00 19.28           C  
ANISOU 4488  CA  PHE A 590     2340   2556   2428    116    287   -343       C  
ATOM   4489  C   PHE A 590      28.041  25.621 -10.150  1.00 20.95           C  
ANISOU 4489  C   PHE A 590     2554   2758   2647     98    288   -334       C  
ATOM   4490  O   PHE A 590      28.485  26.690  -9.726  1.00 19.96           O  
ANISOU 4490  O   PHE A 590     2413   2651   2516     76    301   -347       O  
ATOM   4491  CB  PHE A 590      28.830  25.432 -12.519  1.00 19.75           C  
ANISOU 4491  CB  PHE A 590     2414   2600   2487     98    301   -348       C  
ATOM   4492  CG  PHE A 590      27.479  25.371 -13.191  1.00 19.00           C  
ANISOU 4492  CG  PHE A 590     2350   2464   2403     97    295   -330       C  
ATOM   4493  CD1 PHE A 590      26.462  26.239 -12.812  1.00 20.83           C  
ANISOU 4493  CD1 PHE A 590     2595   2677   2642     79    298   -319       C  
ATOM   4494  CD2 PHE A 590      27.224  24.460 -14.213  1.00 20.33           C  
ANISOU 4494  CD2 PHE A 590     2534   2615   2574    114    287   -325       C  
ATOM   4495  CE1 PHE A 590      25.211  26.198 -13.409  1.00 19.58           C  
ANISOU 4495  CE1 PHE A 590     2462   2486   2491     80    292   -304       C  
ATOM   4496  CE2 PHE A 590      25.966  24.420 -14.836  1.00 15.31           C  
ANISOU 4496  CE2 PHE A 590     1922   1946   1946    113    281   -312       C  
ATOM   4497  CZ  PHE A 590      24.966  25.294 -14.440  1.00 19.94           C  
ANISOU 4497  CZ  PHE A 590     2519   2517   2538     96    284   -302       C  
ATOM   4498  N   TRP A 591      26.843  25.152  -9.806  1.00 18.87           N  
ANISOU 4498  N   TRP A 591     2309   2465   2394    107    275   -313       N  
ATOM   4499  CA  TRP A 591      25.888  25.949  -9.032  1.00 20.51           C  
ANISOU 4499  CA  TRP A 591     2524   2660   2609     90    276   -303       C  
ATOM   4500  C   TRP A 591      26.528  26.460  -7.746  1.00 20.57           C  
ANISOU 4500  C   TRP A 591     2505   2699   2609     85    279   -313       C  
ATOM   4501  O   TRP A 591      27.042  25.682  -6.954  1.00 21.00           O  
ANISOU 4501  O   TRP A 591     2544   2776   2658    107    270   -314       O  
ATOM   4502  CB  TRP A 591      24.622  25.139  -8.719  1.00 18.98           C  
ANISOU 4502  CB  TRP A 591     2348   2434   2426    104    260   -282       C  
ATOM   4503  CG  TRP A 591      23.562  25.914  -7.998  1.00 19.32           C  
ANISOU 4503  CG  TRP A 591     2399   2463   2478     88    260   -271       C  
ATOM   4504  CD1 TRP A 591      23.203  25.780  -6.696  1.00 16.75           C  
ANISOU 4504  CD1 TRP A 591     2067   2141   2154     93    253   -262       C  
ATOM   4505  CD2 TRP A 591      22.754  26.969  -8.534  1.00 18.72           C  
ANISOU 4505  CD2 TRP A 591     2339   2367   2405     66    268   -267       C  
ATOM   4506  NE1 TRP A 591      22.201  26.664  -6.387  1.00 19.52           N  
ANISOU 4506  NE1 TRP A 591     2428   2476   2512     74    255   -254       N  
ATOM   4507  CE2 TRP A 591      21.916  27.418  -7.494  1.00 17.28           C  
ANISOU 4507  CE2 TRP A 591     2159   2178   2229     58    265   -257       C  
ATOM   4508  CE3 TRP A 591      22.654  27.570  -9.792  1.00 15.50           C  
ANISOU 4508  CE3 TRP A 591     1945   1947   1994     54    279   -271       C  
ATOM   4509  CZ2 TRP A 591      20.964  28.425  -7.677  1.00 18.01           C  
ANISOU 4509  CZ2 TRP A 591     2266   2252   2324     40    271   -250       C  
ATOM   4510  CZ3 TRP A 591      21.723  28.583  -9.970  1.00 18.65           C  
ANISOU 4510  CZ3 TRP A 591     2362   2329   2396     39    286   -264       C  
ATOM   4511  CH2 TRP A 591      20.890  28.994  -8.921  1.00 18.56           C  
ANISOU 4511  CH2 TRP A 591     2350   2310   2389     32    282   -254       C  
ATOM   4512  N   ASP A 592      26.508  27.771  -7.549  1.00 20.95           N  
ANISOU 4512  N   ASP A 592     2550   2752   2657     56    294   -322       N  
ATOM   4513  CA  ASP A 592      27.147  28.343  -6.375  1.00 22.31           C  
ANISOU 4513  CA  ASP A 592     2695   2958   2822     47    299   -336       C  
ATOM   4514  C   ASP A 592      26.202  29.325  -5.677  1.00 21.10           C  
ANISOU 4514  C   ASP A 592     2551   2788   2676     26    303   -328       C  
ATOM   4515  O   ASP A 592      26.078  30.478  -6.076  1.00 21.20           O  
ANISOU 4515  O   ASP A 592     2572   2791   2690      0    321   -334       O  
ATOM   4516  CB  ASP A 592      28.471  29.018  -6.759  1.00 22.37           C  
ANISOU 4516  CB  ASP A 592     2681   2999   2820     29    317   -365       C  
ATOM   4517  CG  ASP A 592      29.219  29.564  -5.549  1.00 26.16           C  
ANISOU 4517  CG  ASP A 592     3128   3520   3291     20    323   -386       C  
ATOM   4518  OD1 ASP A 592      28.777  29.354  -4.397  1.00 22.08           O  
ANISOU 4518  OD1 ASP A 592     2605   3008   2774     32    310   -376       O  
ATOM   4519  OD2 ASP A 592      30.266  30.208  -5.757  1.00 29.79           O  
ANISOU 4519  OD2 ASP A 592     3567   4009   3742      1    340   -413       O  
ATOM   4520  N   PRO A 593      25.527  28.868  -4.620  1.00 21.80           N  
ANISOU 4520  N   PRO A 593     2640   2873   2769     41    288   -312       N  
ATOM   4521  CA  PRO A 593      24.588  29.757  -3.939  1.00 21.83           C  
ANISOU 4521  CA  PRO A 593     2651   2861   2779     23    291   -304       C  
ATOM   4522  C   PRO A 593      25.322  30.755  -3.035  1.00 23.29           C  
ANISOU 4522  C   PRO A 593     2812   3080   2957      3    303   -325       C  
ATOM   4523  O   PRO A 593      24.696  31.709  -2.562  1.00 23.25           O  
ANISOU 4523  O   PRO A 593     2812   3063   2956    -16    310   -322       O  
ATOM   4524  CB  PRO A 593      23.769  28.782  -3.092  1.00 21.18           C  
ANISOU 4524  CB  PRO A 593     2575   2768   2702     47    271   -282       C  
ATOM   4525  CG  PRO A 593      24.756  27.698  -2.744  1.00 20.38           C  
ANISOU 4525  CG  PRO A 593     2454   2696   2591     76    262   -288       C  
ATOM   4526  CD  PRO A 593      25.611  27.544  -3.977  1.00 20.87           C  
ANISOU 4526  CD  PRO A 593     2516   2765   2649     75    270   -302       C  
ATOM   4527  N   THR A 594      26.624  30.547  -2.812  1.00 23.32           N  
ANISOU 4527  N   THR A 594     2786   3125   2948      9    306   -348       N  
ATOM   4528  CA  THR A 594      27.374  31.336  -1.825  1.00 25.26           C  
ANISOU 4528  CA  THR A 594     3002   3410   3185     -6    315   -372       C  
ATOM   4529  C   THR A 594      27.570  32.782  -2.268  1.00 25.02           C  
ANISOU 4529  C   THR A 594     2974   3373   3157    -47    343   -391       C  
ATOM   4530  O   THR A 594      27.863  33.643  -1.436  1.00 27.16           O  
ANISOU 4530  O   THR A 594     3227   3666   3425    -67    353   -409       O  
ATOM   4531  CB  THR A 594      28.757  30.747  -1.400  1.00 23.95           C  
ANISOU 4531  CB  THR A 594     2799   3298   3003     12    311   -396       C  
ATOM   4532  OG1 THR A 594      29.686  30.896  -2.475  1.00 26.51           O  
ANISOU 4532  OG1 THR A 594     3116   3633   3323      1    325   -416       O  
ATOM   4533  CG2 THR A 594      28.667  29.288  -0.981  1.00 24.71           C  
ANISOU 4533  CG2 THR A 594     2895   3399   3094     57    288   -377       C  
ATOM   4534  N   ASN A 595      27.388  33.061  -3.555  1.00 24.39           N  
ANISOU 4534  N   ASN A 595     2918   3264   3083    -59    355   -386       N  
ATOM   4535  CA  ASN A 595      27.405  34.449  -4.005  1.00 24.05           C  
ANISOU 4535  CA  ASN A 595     2887   3206   3042    -96    385   -398       C  
ATOM   4536  C   ASN A 595      26.015  35.063  -4.203  1.00 22.63           C  
ANISOU 4536  C   ASN A 595     2744   2981   2873   -104    387   -373       C  
ATOM   4537  O   ASN A 595      25.916  36.193  -4.669  1.00 21.08           O  
ANISOU 4537  O   ASN A 595     2564   2766   2677   -130    413   -379       O  
ATOM   4538  CB  ASN A 595      28.280  34.628  -5.255  1.00 24.38           C  
ANISOU 4538  CB  ASN A 595     2931   3252   3080   -108    404   -414       C  
ATOM   4539  CG  ASN A 595      27.808  33.802  -6.435  1.00 26.64           C  
ANISOU 4539  CG  ASN A 595     3242   3509   3368    -86    393   -393       C  
ATOM   4540  OD1 ASN A 595      26.732  33.204  -6.400  1.00 24.07           O  
ANISOU 4540  OD1 ASN A 595     2936   3158   3050    -66    373   -366       O  
ATOM   4541  ND2 ASN A 595      28.618  33.751  -7.487  1.00 25.21           N  
ANISOU 4541  ND2 ASN A 595     3060   3334   3182    -91    407   -405       N  
ATOM   4542  N   ASP A 596      24.957  34.337  -3.839  1.00 21.39           N  
ANISOU 4542  N   ASP A 596     2599   2807   2722    -81    363   -347       N  
ATOM   4543  CA  ASP A 596      23.584  34.823  -3.975  1.00 19.89           C  
ANISOU 4543  CA  ASP A 596     2440   2577   2539    -84    363   -324       C  
ATOM   4544  C   ASP A 596      23.194  35.720  -2.807  1.00 20.06           C  
ANISOU 4544  C   ASP A 596     2456   2602   2563   -101    368   -327       C  
ATOM   4545  O   ASP A 596      23.295  35.328  -1.638  1.00 20.00           O  
ANISOU 4545  O   ASP A 596     2427   2617   2554    -91    354   -329       O  
ATOM   4546  CB  ASP A 596      22.609  33.639  -4.054  1.00 19.16           C  
ANISOU 4546  CB  ASP A 596     2360   2467   2453    -55    336   -298       C  
ATOM   4547  CG  ASP A 596      22.858  32.771  -5.284  1.00 19.85           C  
ANISOU 4547  CG  ASP A 596     2455   2546   2539    -39    330   -296       C  
ATOM   4548  OD1 ASP A 596      23.677  33.172  -6.139  1.00 18.94           O  
ANISOU 4548  OD1 ASP A 596     2340   2438   2419    -51    348   -311       O  
ATOM   4549  OD2 ASP A 596      22.240  31.692  -5.392  1.00 20.92           O  
ANISOU 4549  OD2 ASP A 596     2598   2669   2679    -17    310   -280       O  
ATOM   4550  N   PHE A 597      22.750  36.925  -3.140  1.00 20.16           N  
ANISOU 4550  N   PHE A 597     2491   2591   2577   -123    390   -326       N  
ATOM   4551  CA  PHE A 597      22.329  37.920  -2.147  1.00 20.28           C  
ANISOU 4551  CA  PHE A 597     2506   2605   2594   -141    400   -329       C  
ATOM   4552  C   PHE A 597      21.362  37.338  -1.105  1.00 18.69           C  
ANISOU 4552  C   PHE A 597     2301   2401   2397   -122    373   -309       C  
ATOM   4553  O   PHE A 597      21.546  37.525   0.095  1.00 19.15           O  
ANISOU 4553  O   PHE A 597     2339   2482   2454   -126    369   -318       O  
ATOM   4554  CB  PHE A 597      21.701  39.101  -2.896  1.00 19.33           C  
ANISOU 4554  CB  PHE A 597     2421   2448   2474   -158    425   -322       C  
ATOM   4555  CG  PHE A 597      21.182  40.208  -2.006  1.00 23.60           C  
ANISOU 4555  CG  PHE A 597     2968   2981   3017   -177    438   -323       C  
ATOM   4556  CD1 PHE A 597      22.022  41.251  -1.618  1.00 23.74           C  
ANISOU 4556  CD1 PHE A 597     2975   3012   3032   -208    467   -351       C  
ATOM   4557  CD2 PHE A 597      19.858  40.225  -1.589  1.00 21.68           C  
ANISOU 4557  CD2 PHE A 597     2741   2716   2777   -164    422   -299       C  
ATOM   4558  CE1 PHE A 597      21.553  42.294  -0.825  1.00 25.18           C  
ANISOU 4558  CE1 PHE A 597     3165   3185   3217   -226    481   -353       C  
ATOM   4559  CE2 PHE A 597      19.376  41.264  -0.778  1.00 20.32           C  
ANISOU 4559  CE2 PHE A 597     2576   2536   2606   -180    435   -300       C  
ATOM   4560  CZ  PHE A 597      20.223  42.300  -0.410  1.00 22.05           C  
ANISOU 4560  CZ  PHE A 597     2787   2767   2824   -211    464   -327       C  
ATOM   4561  N   SER A 598      20.322  36.641  -1.557  1.00 18.46           N  
ANISOU 4561  N   SER A 598     2292   2347   2372   -101    355   -284       N  
ATOM   4562  CA  SER A 598      19.298  36.124  -0.652  1.00 17.85           C  
ANISOU 4562  CA  SER A 598     2215   2265   2301    -85    333   -264       C  
ATOM   4563  C   SER A 598      19.704  34.864   0.111  1.00 18.79           C  
ANISOU 4563  C   SER A 598     2311   2408   2420    -63    311   -263       C  
ATOM   4564  O   SER A 598      18.996  34.439   1.018  1.00 17.03           O  
ANISOU 4564  O   SER A 598     2086   2184   2200    -50    296   -249       O  
ATOM   4565  CB  SER A 598      17.983  35.894  -1.402  1.00 18.98           C  
ANISOU 4565  CB  SER A 598     2388   2374   2449    -74    324   -241       C  
ATOM   4566  OG  SER A 598      17.439  37.112  -1.882  1.00 16.52           O  
ANISOU 4566  OG  SER A 598     2100   2041   2136    -89    342   -238       O  
ATOM   4567  N   TYR A 599      20.849  34.273  -0.219  1.00 19.97           N  
ANISOU 4567  N   TYR A 599     2443   2580   2563    -56    312   -278       N  
ATOM   4568  CA  TYR A 599      21.285  33.064   0.485  1.00 21.24           C  
ANISOU 4568  CA  TYR A 599     2583   2765   2721    -29    293   -276       C  
ATOM   4569  C   TYR A 599      22.086  33.463   1.720  1.00 21.41           C  
ANISOU 4569  C   TYR A 599     2574   2826   2734    -34    296   -295       C  
ATOM   4570  O   TYR A 599      22.298  32.623   2.596  1.00 21.14           O  
ANISOU 4570  O   TYR A 599     2524   2814   2694    -10    281   -291       O  
ATOM   4571  CB  TYR A 599      22.193  32.223  -0.427  1.00 20.55           C  
ANISOU 4571  CB  TYR A 599     2490   2687   2629    -16    292   -284       C  
ATOM   4572  CG  TYR A 599      22.425  30.761  -0.071  1.00 23.39           C  
ANISOU 4572  CG  TYR A 599     2841   3058   2985     17    273   -275       C  
ATOM   4573  CD1 TYR A 599      21.404  29.814  -0.197  1.00 23.02           C  
ANISOU 4573  CD1 TYR A 599     2815   2983   2949     35    259   -251       C  
ATOM   4574  CD2 TYR A 599      23.690  30.309   0.316  1.00 23.06           C  
ANISOU 4574  CD2 TYR A 599     2772   3058   2932     31    272   -292       C  
ATOM   4575  CE1 TYR A 599      21.620  28.458   0.058  1.00 20.12           C  
ANISOU 4575  CE1 TYR A 599     2444   2620   2579     66    246   -242       C  
ATOM   4576  CE2 TYR A 599      23.922  28.958   0.567  1.00 20.72           C  
ANISOU 4576  CE2 TYR A 599     2472   2769   2631     66    257   -283       C  
ATOM   4577  CZ  TYR A 599      22.886  28.045   0.439  1.00 22.79           C  
ANISOU 4577  CZ  TYR A 599     2758   2997   2904     82    245   -257       C  
ATOM   4578  OH  TYR A 599      23.106  26.709   0.687  1.00 19.57           O  
ANISOU 4578  OH  TYR A 599     2350   2592   2492    117    235   -247       O  
ATOM   4579  N   GLN A 600      22.541  34.714   1.781  1.00 21.25           N  
ANISOU 4579  N   GLN A 600     2546   2816   2710    -64    317   -316       N  
ATOM   4580  CA  GLN A 600      23.467  35.128   2.846  1.00 24.22           C  
ANISOU 4580  CA  GLN A 600     2888   3235   3076    -71    322   -342       C  
ATOM   4581  C   GLN A 600      22.891  34.870   4.230  1.00 24.27           C  
ANISOU 4581  C   GLN A 600     2887   3253   3082    -56    305   -330       C  
ATOM   4582  O   GLN A 600      21.772  35.304   4.513  1.00 25.20           O  
ANISOU 4582  O   GLN A 600     3023   3342   3207    -62    304   -312       O  
ATOM   4583  CB  GLN A 600      23.794  36.622   2.791  1.00 24.80           C  
ANISOU 4583  CB  GLN A 600     2960   3311   3150   -111    349   -366       C  
ATOM   4584  CG  GLN A 600      24.563  37.184   1.597  1.00 29.78           C  
ANISOU 4584  CG  GLN A 600     3597   3937   3781   -134    374   -385       C  
ATOM   4585  CD  GLN A 600      24.557  38.716   1.654  1.00 40.15           C  
ANISOU 4585  CD  GLN A 600     4917   5239   5096   -173    404   -402       C  
ATOM   4586  OE1 GLN A 600      23.640  39.366   1.134  1.00 40.53           O  
ANISOU 4586  OE1 GLN A 600     5000   5247   5152   -183    415   -385       O  
ATOM   4587  NE2 GLN A 600      25.532  39.294   2.354  1.00 36.75           N  
ANISOU 4587  NE2 GLN A 600     4455   4847   4659   -193    418   -436       N  
ATOM   4588  N   GLY A 601      23.658  34.211   5.096  1.00 23.73           N  
ANISOU 4588  N   GLY A 601     2788   3226   3001    -34    294   -340       N  
ATOM   4589  CA  GLY A 601      23.243  34.006   6.486  1.00 23.85           C  
ANISOU 4589  CA  GLY A 601     2792   3256   3012    -17    280   -331       C  
ATOM   4590  C   GLY A 601      22.258  32.872   6.717  1.00 23.41           C  
ANISOU 4590  C   GLY A 601     2757   3175   2962     13    261   -296       C  
ATOM   4591  O   GLY A 601      21.968  32.503   7.858  1.00 22.84           O  
ANISOU 4591  O   GLY A 601     2677   3116   2885     33    250   -286       O  
ATOM   4592  N   LEU A 602      21.722  32.303   5.640  1.00 22.12           N  
ANISOU 4592  N   LEU A 602     2620   2975   2809     18    259   -278       N  
ATOM   4593  CA  LEU A 602      20.774  31.209   5.806  1.00 22.56           C  
ANISOU 4593  CA  LEU A 602     2695   3004   2872     43    244   -248       C  
ATOM   4594  C   LEU A 602      21.406  29.956   6.400  1.00 22.84           C  
ANISOU 4594  C   LEU A 602     2717   3065   2896     82    232   -244       C  
ATOM   4595  O   LEU A 602      22.553  29.639   6.103  1.00 25.03           O  
ANISOU 4595  O   LEU A 602     2976   3370   3161     92    234   -261       O  
ATOM   4596  CB  LEU A 602      20.101  30.847   4.478  1.00 21.72           C  
ANISOU 4596  CB  LEU A 602     2618   2856   2778     39    244   -234       C  
ATOM   4597  CG  LEU A 602      19.218  31.935   3.852  1.00 22.77           C  
ANISOU 4597  CG  LEU A 602     2770   2958   2921     10    254   -231       C  
ATOM   4598  CD1 LEU A 602      18.431  31.358   2.683  1.00 19.04           C  
ANISOU 4598  CD1 LEU A 602     2325   2450   2459     14    250   -215       C  
ATOM   4599  CD2 LEU A 602      18.287  32.554   4.894  1.00 18.91           C  
ANISOU 4599  CD2 LEU A 602     2284   2463   2435      2    251   -221       C  
ATOM   4600  N   THR A 603      20.636  29.249   7.215  1.00 22.32           N  
ANISOU 4600  N   THR A 603     2660   2986   2831    103    222   -221       N  
ATOM   4601  CA  THR A 603      21.024  27.945   7.732  1.00 25.25           C  
ANISOU 4601  CA  THR A 603     3028   3371   3192    144    214   -210       C  
ATOM   4602  C   THR A 603      19.869  26.980   7.499  1.00 24.91           C  
ANISOU 4602  C   THR A 603     3017   3282   3164    156    209   -180       C  
ATOM   4603  O   THR A 603      18.849  27.326   6.892  1.00 22.40           O  
ANISOU 4603  O   THR A 603     2719   2927   2862    132    211   -172       O  
ATOM   4604  CB  THR A 603      21.269  27.984   9.261  1.00 24.79           C  
ANISOU 4604  CB  THR A 603     2949   3348   3118    164    209   -210       C  
ATOM   4605  OG1 THR A 603      20.036  28.310   9.910  1.00 28.53           O  
ANISOU 4605  OG1 THR A 603     3438   3797   3603    154    207   -192       O  
ATOM   4606  CG2 THR A 603      22.323  29.034   9.640  1.00 27.29           C  
ANISOU 4606  CG2 THR A 603     3231   3714   3420    149    214   -244       C  
ATOM   4607  N   ARG A 604      20.037  25.777   8.041  1.00 24.68           N  
ANISOU 4607  N   ARG A 604     2992   3256   3128    193    205   -166       N  
ATOM   4608  CA  ARG A 604      19.030  24.734   7.997  1.00 25.95           C  
ANISOU 4608  CA  ARG A 604     3182   3375   3300    206    204   -140       C  
ATOM   4609  C   ARG A 604      17.879  25.028   8.954  1.00 25.91           C  
ANISOU 4609  C   ARG A 604     3185   3354   3303    199    203   -123       C  
ATOM   4610  O   ARG A 604      16.864  24.346   8.918  1.00 24.38           O  
ANISOU 4610  O   ARG A 604     3015   3124   3123    201    205   -103       O  
ATOM   4611  CB  ARG A 604      19.681  23.388   8.334  1.00 28.28           C  
ANISOU 4611  CB  ARG A 604     3481   3680   3584    250    204   -130       C  
ATOM   4612  CG  ARG A 604      20.699  22.903   7.293  1.00 32.03           C  
ANISOU 4612  CG  ARG A 604     3952   4164   4052    260    205   -143       C  
ATOM   4613  CD  ARG A 604      20.050  22.063   6.191  1.00 45.81           C  
ANISOU 4613  CD  ARG A 604     5727   5862   5816    256    208   -132       C  
ATOM   4614  NE  ARG A 604      20.947  21.634   5.113  1.00 50.06           N  
ANISOU 4614  NE  ARG A 604     6262   6406   6349    263    209   -145       N  
ATOM   4615  CZ  ARG A 604      20.614  20.732   4.190  1.00 52.31           C  
ANISOU 4615  CZ  ARG A 604     6572   6657   6647    267    212   -138       C  
ATOM   4616  NH1 ARG A 604      19.414  20.167   4.238  1.00 52.97           N  
ANISOU 4616  NH1 ARG A 604     6681   6698   6747    263    215   -119       N  
ATOM   4617  NH2 ARG A 604      21.460  20.389   3.223  1.00 48.03           N  
ANISOU 4617  NH2 ARG A 604     6027   6122   6100    274    213   -150       N  
ATOM   4618  N   GLU A 605      18.036  26.046   9.797  1.00 25.95           N  
ANISOU 4618  N   GLU A 605     3170   3388   3300    188    202   -133       N  
ATOM   4619  CA  GLU A 605      17.022  26.423  10.766  1.00 27.39           C  
ANISOU 4619  CA  GLU A 605     3357   3560   3487    182    201   -119       C  
ATOM   4620  C   GLU A 605      16.323  27.691  10.290  1.00 25.19           C  
ANISOU 4620  C   GLU A 605     3081   3267   3221    142    203   -127       C  
ATOM   4621  O   GLU A 605      16.981  28.649   9.878  1.00 24.59           O  
ANISOU 4621  O   GLU A 605     2990   3210   3141    122    206   -149       O  
ATOM   4622  CB  GLU A 605      17.697  26.690  12.115  1.00 28.73           C  
ANISOU 4622  CB  GLU A 605     3502   3775   3636    202    198   -126       C  
ATOM   4623  CG  GLU A 605      17.209  25.815  13.253  1.00 38.63           C  
ANISOU 4623  CG  GLU A 605     4767   5025   4885    234    197   -101       C  
ATOM   4624  CD  GLU A 605      17.788  24.406  13.244  1.00 48.20           C  
ANISOU 4624  CD  GLU A 605     5988   6237   6086    275    199    -90       C  
ATOM   4625  OE1 GLU A 605      17.980  23.831  12.151  1.00 53.50           O  
ANISOU 4625  OE1 GLU A 605     6672   6888   6766    274    201    -91       O  
ATOM   4626  OE2 GLU A 605      18.039  23.850  14.339  1.00 53.59           O  
ANISOU 4626  OE2 GLU A 605     6668   6941   6753    312    199    -79       O  
ATOM   4627  N   LEU A 606      14.994  27.694  10.369  1.00 25.15           N  
ANISOU 4627  N   LEU A 606     3095   3228   3230    131    202   -110       N  
ATOM   4628  CA  LEU A 606      14.195  28.862  10.018  1.00 24.79           C  
ANISOU 4628  CA  LEU A 606     3054   3168   3194     98    204   -114       C  
ATOM   4629  C   LEU A 606      14.615  30.091  10.813  1.00 25.12           C  
ANISOU 4629  C   LEU A 606     3076   3241   3227     85    206   -129       C  
ATOM   4630  O   LEU A 606      14.671  30.052  12.047  1.00 24.35           O  
ANISOU 4630  O   LEU A 606     2966   3164   3120     99    203   -125       O  
ATOM   4631  CB  LEU A 606      12.735  28.562  10.349  1.00 25.73           C  
ANISOU 4631  CB  LEU A 606     3192   3256   3327     95    202    -93       C  
ATOM   4632  CG  LEU A 606      11.586  28.711   9.349  1.00 26.53           C  
ANISOU 4632  CG  LEU A 606     3313   3323   3444     75    202    -89       C  
ATOM   4633  CD1 LEU A 606      11.926  28.520   7.881  1.00 23.26           C  
ANISOU 4633  CD1 LEU A 606     2906   2896   3034     69    204    -99       C  
ATOM   4634  CD2 LEU A 606      10.525  27.702   9.758  1.00 28.88           C  
ANISOU 4634  CD2 LEU A 606     3625   3594   3752     85    201    -69       C  
ATOM   4635  N   ALA A 607      14.904  31.181  10.110  1.00 24.39           N  
ANISOU 4635  N   ALA A 607     2980   3152   3135     59    213   -147       N  
ATOM   4636  CA  ALA A 607      15.236  32.446  10.767  1.00 24.46           C  
ANISOU 4636  CA  ALA A 607     2971   3184   3136     41    218   -164       C  
ATOM   4637  C   ALA A 607      14.809  33.621   9.902  1.00 23.13           C  
ANISOU 4637  C   ALA A 607     2816   2995   2975      9    228   -172       C  
ATOM   4638  O   ALA A 607      14.819  33.513   8.678  1.00 21.82           O  
ANISOU 4638  O   ALA A 607     2663   2810   2815      3    232   -173       O  
ATOM   4639  CB  ALA A 607      16.739  32.552  11.053  1.00 24.89           C  
ANISOU 4639  CB  ALA A 607     2998   3284   3175     47    221   -189       C  
ATOM   4640  N   LYS A 608      14.493  34.746  10.538  1.00 21.82           N  
ANISOU 4640  N   LYS A 608     2646   2834   2808     -7    234   -178       N  
ATOM   4641  CA  LYS A 608      14.172  35.977   9.821  1.00 21.80           C  
ANISOU 4641  CA  LYS A 608     2657   2813   2810    -35    248   -186       C  
ATOM   4642  C   LYS A 608      15.363  36.376   8.964  1.00 21.56           C  
ANISOU 4642  C   LYS A 608     2619   2795   2775    -49    261   -210       C  
ATOM   4643  O   LYS A 608      16.515  36.295   9.385  1.00 20.73           O  
ANISOU 4643  O   LYS A 608     2490   2725   2661    -46    263   -229       O  
ATOM   4644  CB  LYS A 608      13.854  37.092  10.819  1.00 22.58           C  
ANISOU 4644  CB  LYS A 608     2751   2921   2906    -50    254   -193       C  
ATOM   4645  CG  LYS A 608      13.627  38.450  10.194  1.00 23.37           C  
ANISOU 4645  CG  LYS A 608     2866   3003   3008    -78    272   -202       C  
ATOM   4646  CD  LYS A 608      12.987  39.392  11.212  1.00 26.96           C  
ANISOU 4646  CD  LYS A 608     3320   3458   3462    -88    275   -202       C  
ATOM   4647  CE  LYS A 608      13.794  39.499  12.494  1.00 30.57           C  
ANISOU 4647  CE  LYS A 608     3747   3956   3910    -87    274   -219       C  
ATOM   4648  NZ  LYS A 608      12.989  40.287  13.487  1.00 31.69           N  
ANISOU 4648  NZ  LYS A 608     3891   4095   4052    -94    274   -215       N  
ATOM   4649  N   THR A 609      15.090  36.807   7.743  1.00 20.66           N  
ANISOU 4649  N   THR A 609     2527   2655   2667    -62    271   -209       N  
ATOM   4650  CA  THR A 609      16.167  37.292   6.901  1.00 20.95           C  
ANISOU 4650  CA  THR A 609     2560   2700   2699    -78    287   -231       C  
ATOM   4651  C   THR A 609      15.821  38.614   6.236  1.00 21.31           C  
ANISOU 4651  C   THR A 609     2627   2722   2747   -103    308   -236       C  
ATOM   4652  O   THR A 609      14.760  38.787   5.639  1.00 22.30           O  
ANISOU 4652  O   THR A 609     2778   2817   2877   -101    307   -218       O  
ATOM   4653  CB  THR A 609      16.596  36.266   5.831  1.00 20.43           C  
ANISOU 4653  CB  THR A 609     2498   2630   2635    -64    282   -228       C  
ATOM   4654  OG1 THR A 609      17.430  36.926   4.871  1.00 22.75           O  
ANISOU 4654  OG1 THR A 609     2794   2925   2926    -82    301   -247       O  
ATOM   4655  CG2 THR A 609      15.394  35.672   5.101  1.00 18.79           C  
ANISOU 4655  CG2 THR A 609     2315   2386   2435    -52    271   -203       C  
ATOM   4656  N   LYS A 610      16.756  39.547   6.305  1.00 21.48           N  
ANISOU 4656  N   LYS A 610     2637   2760   2763   -126    329   -262       N  
ATOM   4657  CA  LYS A 610      16.541  40.834   5.668  1.00 23.36           C  
ANISOU 4657  CA  LYS A 610     2898   2973   3002   -150    354   -268       C  
ATOM   4658  C   LYS A 610      16.846  40.794   4.169  1.00 21.96           C  
ANISOU 4658  C   LYS A 610     2740   2778   2824   -153    366   -268       C  
ATOM   4659  O   LYS A 610      16.518  41.735   3.448  1.00 21.26           O  
ANISOU 4659  O   LYS A 610     2678   2664   2736   -166    387   -266       O  
ATOM   4660  CB  LYS A 610      17.286  41.951   6.419  1.00 26.01           C  
ANISOU 4660  CB  LYS A 610     3219   3329   3334   -178    376   -296       C  
ATOM   4661  CG  LYS A 610      18.806  41.963   6.309  1.00 30.62           C  
ANISOU 4661  CG  LYS A 610     3775   3945   3912   -192    389   -328       C  
ATOM   4662  CD  LYS A 610      19.323  43.236   6.989  1.00 39.47           C  
ANISOU 4662  CD  LYS A 610     4885   5079   5030   -224    414   -358       C  
ATOM   4663  CE  LYS A 610      20.807  43.189   7.302  1.00 41.60           C  
ANISOU 4663  CE  LYS A 610     5117   5395   5294   -237    423   -395       C  
ATOM   4664  NZ  LYS A 610      21.038  42.138   8.332  1.00 45.80           N  
ANISOU 4664  NZ  LYS A 610     5615   5966   5818   -209    393   -394       N  
ATOM   4665  N   TYR A 611      17.379  39.671   3.687  1.00 20.58           N  
ANISOU 4665  N   TYR A 611     2554   2615   2650   -136    353   -267       N  
ATOM   4666  CA  TYR A 611      17.812  39.577   2.288  1.00 20.64           C  
ANISOU 4666  CA  TYR A 611     2575   2610   2656   -138    364   -270       C  
ATOM   4667  C   TYR A 611      16.781  38.979   1.332  1.00 19.57           C  
ANISOU 4667  C   TYR A 611     2465   2444   2524   -119    351   -245       C  
ATOM   4668  O   TYR A 611      17.065  38.809   0.148  1.00 19.42           O  
ANISOU 4668  O   TYR A 611     2458   2416   2503   -117    357   -246       O  
ATOM   4669  CB  TYR A 611      19.166  38.872   2.180  1.00 20.36           C  
ANISOU 4669  CB  TYR A 611     2512   2606   2616   -135    362   -290       C  
ATOM   4670  CG  TYR A 611      20.211  39.523   3.054  1.00 23.08           C  
ANISOU 4670  CG  TYR A 611     2829   2984   2955   -156    376   -320       C  
ATOM   4671  CD1 TYR A 611      20.702  40.788   2.749  1.00 27.67           C  
ANISOU 4671  CD1 TYR A 611     3417   3561   3536   -188    408   -341       C  
ATOM   4672  CD2 TYR A 611      20.668  38.895   4.205  1.00 26.52           C  
ANISOU 4672  CD2 TYR A 611     3232   3457   3387   -143    359   -327       C  
ATOM   4673  CE1 TYR A 611      21.636  41.408   3.557  1.00 31.00           C  
ANISOU 4673  CE1 TYR A 611     3810   4015   3953   -210    423   -373       C  
ATOM   4674  CE2 TYR A 611      21.611  39.498   5.022  1.00 29.67           C  
ANISOU 4674  CE2 TYR A 611     3601   3891   3778   -161    371   -358       C  
ATOM   4675  CZ  TYR A 611      22.091  40.750   4.685  1.00 34.64           C  
ANISOU 4675  CZ  TYR A 611     4234   4516   4408   -196    403   -382       C  
ATOM   4676  OH  TYR A 611      23.026  41.357   5.487  1.00 35.00           O  
ANISOU 4676  OH  TYR A 611     4250   4600   4448   -217    416   -417       O  
ATOM   4677  N   MET A 612      15.607  38.638   1.858  1.00 19.07           N  
ANISOU 4677  N   MET A 612     2409   2371   2465   -105    333   -225       N  
ATOM   4678  CA  MET A 612      14.445  38.300   1.030  1.00 18.58           C  
ANISOU 4678  CA  MET A 612     2371   2282   2406    -90    323   -204       C  
ATOM   4679  C   MET A 612      13.388  39.354   1.340  1.00 17.26           C  
ANISOU 4679  C   MET A 612     2223   2096   2237    -97    330   -195       C  
ATOM   4680  O   MET A 612      12.489  39.109   2.160  1.00 16.23           O  
ANISOU 4680  O   MET A 612     2090   1966   2111    -89    315   -182       O  
ATOM   4681  CB  MET A 612      13.931  36.887   1.340  1.00 18.37           C  
ANISOU 4681  CB  MET A 612     2336   2258   2386    -68    296   -190       C  
ATOM   4682  CG  MET A 612      14.920  35.810   0.903  1.00 16.76           C  
ANISOU 4682  CG  MET A 612     2118   2068   2182    -58    290   -198       C  
ATOM   4683  SD  MET A 612      14.496  34.127   1.409  1.00 17.95           S  
ANISOU 4683  SD  MET A 612     2259   2220   2340    -33    264   -184       S  
ATOM   4684  CE  MET A 612      12.999  33.963   0.452  1.00 18.17           C  
ANISOU 4684  CE  MET A 612     2312   2216   2373    -27    257   -168       C  
ATOM   4685  N   PRO A 613      13.537  40.545   0.724  1.00 16.54           N  
ANISOU 4685  N   PRO A 613     2151   1991   2139   -111    356   -201       N  
ATOM   4686  CA  PRO A 613      12.745  41.689   1.155  1.00 16.25           C  
ANISOU 4686  CA  PRO A 613     2133   1941   2101   -119    368   -195       C  
ATOM   4687  C   PRO A 613      11.272  41.537   0.806  1.00 16.63           C  
ANISOU 4687  C   PRO A 613     2200   1970   2147    -99    354   -173       C  
ATOM   4688  O   PRO A 613      10.937  40.883  -0.180  1.00 16.15           O  
ANISOU 4688  O   PRO A 613     2147   1901   2084    -84    344   -165       O  
ATOM   4689  CB  PRO A 613      13.374  42.866   0.397  1.00 15.24           C  
ANISOU 4689  CB  PRO A 613     2025   1800   1966   -137    403   -207       C  
ATOM   4690  CG  PRO A 613      13.957  42.249  -0.828  1.00 13.68           C  
ANISOU 4690  CG  PRO A 613     1830   1600   1765   -129    404   -210       C  
ATOM   4691  CD  PRO A 613      14.402  40.882  -0.426  1.00 15.54           C  
ANISOU 4691  CD  PRO A 613     2036   1860   2008   -120    377   -212       C  
ATOM   4692  N   VAL A 614      10.415  42.116   1.640  1.00 16.71           N  
ANISOU 4692  N   VAL A 614     2215   1975   2157   -100    352   -165       N  
ATOM   4693  CA  VAL A 614       8.965  42.028   1.490  1.00 15.93           C  
ANISOU 4693  CA  VAL A 614     2131   1864   2056    -82    338   -147       C  
ATOM   4694  C   VAL A 614       8.394  43.341   0.951  1.00 17.25           C  
ANISOU 4694  C   VAL A 614     2330   2011   2211    -81    359   -141       C  
ATOM   4695  O   VAL A 614       8.836  44.425   1.348  1.00 17.25           O  
ANISOU 4695  O   VAL A 614     2338   2005   2208    -97    383   -150       O  
ATOM   4696  CB  VAL A 614       8.292  41.696   2.846  1.00 16.09           C  
ANISOU 4696  CB  VAL A 614     2134   1895   2083    -80    319   -140       C  
ATOM   4697  CG1 VAL A 614       6.759  41.662   2.711  1.00 12.72           C  
ANISOU 4697  CG1 VAL A 614     1720   1457   1654    -63    306   -123       C  
ATOM   4698  CG2 VAL A 614       8.815  40.360   3.355  1.00 13.62           C  
ANISOU 4698  CG2 VAL A 614     1794   1600   1780    -76    300   -142       C  
ATOM   4699  N   PHE A 615       7.443  43.231   0.027  1.00 15.97           N  
ANISOU 4699  N   PHE A 615     2187   1839   2042    -60    353   -129       N  
ATOM   4700  CA  PHE A 615       6.854  44.382  -0.651  1.00 16.83           C  
ANISOU 4700  CA  PHE A 615     2330   1929   2136    -51    373   -122       C  
ATOM   4701  C   PHE A 615       5.343  44.353  -0.464  1.00 18.27           C  
ANISOU 4701  C   PHE A 615     2517   2111   2312    -30    355   -107       C  
ATOM   4702  O   PHE A 615       4.737  43.281  -0.452  1.00 17.36           O  
ANISOU 4702  O   PHE A 615     2385   2007   2203    -19    328   -104       O  
ATOM   4703  CB  PHE A 615       7.152  44.339  -2.154  1.00 16.06           C  
ANISOU 4703  CB  PHE A 615     2251   1823   2028    -39    383   -122       C  
ATOM   4704  CG  PHE A 615       8.611  44.374  -2.470  1.00 19.49           C  
ANISOU 4704  CG  PHE A 615     2680   2257   2465    -59    403   -137       C  
ATOM   4705  CD1 PHE A 615       9.393  43.231  -2.331  1.00 19.42           C  
ANISOU 4705  CD1 PHE A 615     2642   2266   2468    -65    386   -146       C  
ATOM   4706  CD2 PHE A 615       9.205  45.556  -2.891  1.00 18.28           C  
ANISOU 4706  CD2 PHE A 615     2553   2088   2304    -70    439   -142       C  
ATOM   4707  CE1 PHE A 615      10.763  43.272  -2.584  1.00 21.37           C  
ANISOU 4707  CE1 PHE A 615     2882   2517   2718    -83    403   -162       C  
ATOM   4708  CE2 PHE A 615      10.572  45.606  -3.154  1.00 20.31           C  
ANISOU 4708  CE2 PHE A 615     2803   2347   2564    -91    459   -158       C  
ATOM   4709  CZ  PHE A 615      11.349  44.459  -3.001  1.00 20.71           C  
ANISOU 4709  CZ  PHE A 615     2822   2420   2627    -97    439   -169       C  
ATOM   4710  N   ASP A 616       4.758  45.541  -0.338  1.00 17.67           N  
ANISOU 4710  N   ASP A 616     2466   2023   2225    -25    372   -101       N  
ATOM   4711  CA  ASP A 616       3.317  45.743  -0.410  1.00 18.31           C  
ANISOU 4711  CA  ASP A 616     2558   2104   2295     -1    360    -88       C  
ATOM   4712  C   ASP A 616       3.105  46.523  -1.709  1.00 20.07           C  
ANISOU 4712  C   ASP A 616     2816   2312   2496     19    380    -82       C  
ATOM   4713  O   ASP A 616       3.466  47.706  -1.789  1.00 17.20           O  
ANISOU 4713  O   ASP A 616     2480   1930   2123     14    412    -81       O  
ATOM   4714  CB  ASP A 616       2.885  46.596   0.786  1.00 19.24           C  
ANISOU 4714  CB  ASP A 616     2679   2218   2413     -9    366    -84       C  
ATOM   4715  CG  ASP A 616       1.424  47.028   0.718  1.00 21.40           C  
ANISOU 4715  CG  ASP A 616     2966   2491   2671     16    359    -71       C  
ATOM   4716  OD1 ASP A 616       0.702  46.765  -0.276  1.00 23.13           O  
ANISOU 4716  OD1 ASP A 616     3195   2714   2878     42    350    -66       O  
ATOM   4717  OD2 ASP A 616       0.985  47.609   1.726  1.00 26.23           O  
ANISOU 4717  OD2 ASP A 616     3579   3102   3285     11    361    -68       O  
ATOM   4718  N   GLY A 617       2.567  45.865  -2.738  1.00 18.50           N  
ANISOU 4718  N   GLY A 617     2618   2121   2289     42    365    -78       N  
ATOM   4719  CA  GLY A 617       2.515  46.491  -4.058  1.00 20.11           C  
ANISOU 4719  CA  GLY A 617     2855   2314   2471     64    384    -73       C  
ATOM   4720  C   GLY A 617       3.962  46.667  -4.480  1.00 20.89           C  
ANISOU 4720  C   GLY A 617     2960   2400   2575     43    409    -82       C  
ATOM   4721  O   GLY A 617       4.755  45.738  -4.317  1.00 19.54           O  
ANISOU 4721  O   GLY A 617     2763   2239   2421     26    397    -92       O  
ATOM   4722  N   ALA A 618       4.310  47.855  -4.972  1.00 20.98           N  
ANISOU 4722  N   ALA A 618     3008   2390   2572     46    445    -78       N  
ATOM   4723  CA  ALA A 618       5.683  48.162  -5.364  1.00 23.44           C  
ANISOU 4723  CA  ALA A 618     3328   2688   2887     23    474    -88       C  
ATOM   4724  C   ALA A 618       6.523  48.764  -4.237  1.00 24.00           C  
ANISOU 4724  C   ALA A 618     3392   2752   2973    -12    494   -100       C  
ATOM   4725  O   ALA A 618       7.691  49.070  -4.460  1.00 27.23           O  
ANISOU 4725  O   ALA A 618     3805   3153   3387    -35    520   -112       O  
ATOM   4726  CB  ALA A 618       5.730  49.068  -6.618  1.00 21.31           C  
ANISOU 4726  CB  ALA A 618     3103   2398   2594     44    507    -80       C  
ATOM   4727  N   THR A 619       5.968  48.904  -3.034  1.00 23.56           N  
ANISOU 4727  N   THR A 619     3323   2702   2925    -19    482    -98       N  
ATOM   4728  CA  THR A 619       6.671  49.533  -1.921  1.00 22.85           C  
ANISOU 4728  CA  THR A 619     3225   2608   2847    -51    500   -111       C  
ATOM   4729  C   THR A 619       7.370  48.481  -1.062  1.00 22.84           C  
ANISOU 4729  C   THR A 619     3179   2631   2866    -73    476   -125       C  
ATOM   4730  O   THR A 619       6.715  47.583  -0.525  1.00 21.11           O  
ANISOU 4730  O   THR A 619     2936   2430   2655    -63    442   -119       O  
ATOM   4731  CB  THR A 619       5.686  50.325  -1.015  1.00 23.39           C  
ANISOU 4731  CB  THR A 619     3305   2670   2910    -45    502   -102       C  
ATOM   4732  OG1 THR A 619       4.969  51.286  -1.801  1.00 22.84           O  
ANISOU 4732  OG1 THR A 619     3279   2578   2819    -19    524    -87       O  
ATOM   4733  CG2 THR A 619       6.422  51.057   0.106  1.00 23.58           C  
ANISOU 4733  CG2 THR A 619     3323   2690   2946    -79    523   -117       C  
ATOM   4734  N   LYS A 620       8.682  48.607  -0.894  1.00 21.32           N  
ANISOU 4734  N   LYS A 620     2976   2442   2683   -102    495   -144       N  
ATOM   4735  CA  LYS A 620       9.401  47.712   0.012  1.00 21.06           C  
ANISOU 4735  CA  LYS A 620     2900   2434   2665   -119    474   -158       C  
ATOM   4736  C   LYS A 620       9.043  48.021   1.455  1.00 19.84           C  
ANISOU 4736  C   LYS A 620     2730   2288   2517   -130    467   -160       C  
ATOM   4737  O   LYS A 620       9.200  49.165   1.884  1.00 19.61           O  
ANISOU 4737  O   LYS A 620     2717   2247   2486   -146    495   -168       O  
ATOM   4738  CB  LYS A 620      10.920  47.827  -0.167  1.00 20.60           C  
ANISOU 4738  CB  LYS A 620     2831   2381   2612   -147    497   -181       C  
ATOM   4739  CG  LYS A 620      11.710  46.869   0.728  1.00 21.15           C  
ANISOU 4739  CG  LYS A 620     2856   2482   2695   -159    475   -196       C  
ATOM   4740  CD  LYS A 620      13.153  46.698   0.267  1.00 23.88           C  
ANISOU 4740  CD  LYS A 620     3190   2840   3044   -179    491   -218       C  
ATOM   4741  CE  LYS A 620      13.929  48.011   0.336  1.00 27.44           C  
ANISOU 4741  CE  LYS A 620     3654   3278   3492   -209    535   -238       C  
ATOM   4742  NZ  LYS A 620      14.108  48.387   1.759  1.00 25.08           N  
ANISOU 4742  NZ  LYS A 620     3332   2995   3199   -229    535   -253       N  
ATOM   4743  N   ILE A 621       8.580  47.025   2.208  1.00 18.11           N  
ANISOU 4743  N   ILE A 621     2484   2089   2307   -121    432   -155       N  
ATOM   4744  CA  ILE A 621       8.206  47.268   3.599  1.00 18.15           C  
ANISOU 4744  CA  ILE A 621     2474   2104   2317   -128    424   -155       C  
ATOM   4745  C   ILE A 621       9.163  46.631   4.598  1.00 18.83           C  
ANISOU 4745  C   ILE A 621     2521   2217   2414   -145    413   -172       C  
ATOM   4746  O   ILE A 621       9.057  46.861   5.790  1.00 20.94           O  
ANISOU 4746  O   ILE A 621     2774   2495   2684   -153    409   -176       O  
ATOM   4747  CB  ILE A 621       6.728  46.866   3.903  1.00 18.88           C  
ANISOU 4747  CB  ILE A 621     2567   2196   2407   -104    397   -135       C  
ATOM   4748  CG1 ILE A 621       6.455  45.394   3.560  1.00 16.73           C  
ANISOU 4748  CG1 ILE A 621     2276   1937   2141    -88    366   -127       C  
ATOM   4749  CG2 ILE A 621       5.770  47.769   3.117  1.00 17.10           C  
ANISOU 4749  CG2 ILE A 621     2380   1948   2168    -86    411   -121       C  
ATOM   4750  CD1 ILE A 621       5.076  44.900   3.966  1.00 22.49           C  
ANISOU 4750  CD1 ILE A 621     3002   2670   2872    -69    340   -112       C  
ATOM   4751  N   PHE A 622      10.053  45.762   4.140  1.00 18.26           N  
ANISOU 4751  N   PHE A 622     2432   2158   2346   -146    406   -181       N  
ATOM   4752  CA  PHE A 622      11.020  45.151   5.041  1.00 19.16           C  
ANISOU 4752  CA  PHE A 622     2510   2302   2467   -157    397   -197       C  
ATOM   4753  C   PHE A 622      12.197  44.602   4.249  1.00 20.18           C  
ANISOU 4753  C   PHE A 622     2629   2441   2597   -162    402   -211       C  
ATOM   4754  O   PHE A 622      11.997  44.045   3.166  1.00 20.86           O  
ANISOU 4754  O   PHE A 622     2727   2516   2681   -148    396   -200       O  
ATOM   4755  CB  PHE A 622      10.414  44.011   5.861  1.00 18.56           C  
ANISOU 4755  CB  PHE A 622     2413   2242   2397   -139    363   -184       C  
ATOM   4756  CG  PHE A 622      11.399  43.378   6.801  1.00 21.24           C  
ANISOU 4756  CG  PHE A 622     2717   2613   2740   -144    353   -199       C  
ATOM   4757  CD1 PHE A 622      11.736  44.000   8.004  1.00 24.70           C  
ANISOU 4757  CD1 PHE A 622     3138   3068   3176   -159    360   -213       C  
ATOM   4758  CD2 PHE A 622      12.030  42.190   6.462  1.00 17.69           C  
ANISOU 4758  CD2 PHE A 622     2250   2177   2292   -134    339   -200       C  
ATOM   4759  CE1 PHE A 622      12.687  43.430   8.841  1.00 26.12           C  
ANISOU 4759  CE1 PHE A 622     3285   3282   3357   -160    351   -229       C  
ATOM   4760  CE2 PHE A 622      12.945  41.602   7.301  1.00 20.61           C  
ANISOU 4760  CE2 PHE A 622     2589   2578   2662   -133    331   -213       C  
ATOM   4761  CZ  PHE A 622      13.291  42.234   8.490  1.00 22.89           C  
ANISOU 4761  CZ  PHE A 622     2860   2888   2948   -146    337   -228       C  
ATOM   4762  N   GLY A 623      13.401  44.759   4.797  1.00 20.87           N  
ANISOU 4762  N   GLY A 623     2693   2551   2685   -182    413   -235       N  
ATOM   4763  CA  GLY A 623      14.594  44.116   4.268  1.00 22.58           C  
ANISOU 4763  CA  GLY A 623     2891   2785   2902   -186    414   -251       C  
ATOM   4764  C   GLY A 623      15.388  44.972   3.301  1.00 24.52           C  
ANISOU 4764  C   GLY A 623     3153   3018   3144   -207    449   -267       C  
ATOM   4765  O   GLY A 623      15.126  46.170   3.164  1.00 25.38           O  
ANISOU 4765  O   GLY A 623     3287   3104   3249   -221    476   -269       O  
ATOM   4766  N   GLU A 624      16.365  44.361   2.638  1.00 24.48           N  
ANISOU 4766  N   GLU A 624     3135   3026   3138   -208    449   -279       N  
ATOM   4767  CA  GLU A 624      17.278  45.093   1.763  1.00 25.93           C  
ANISOU 4767  CA  GLU A 624     3331   3202   3319   -230    484   -298       C  
ATOM   4768  C   GLU A 624      17.315  44.526   0.350  1.00 26.74           C  
ANISOU 4768  C   GLU A 624     3450   3291   3419   -214    482   -286       C  
ATOM   4769  O   GLU A 624      16.944  43.374   0.111  1.00 26.04           O  
ANISOU 4769  O   GLU A 624     3354   3207   3331   -189    452   -270       O  
ATOM   4770  CB  GLU A 624      18.681  45.107   2.368  1.00 25.60           C  
ANISOU 4770  CB  GLU A 624     3251   3196   3277   -252    493   -332       C  
ATOM   4771  CG  GLU A 624      18.762  45.940   3.656  1.00 31.06           C  
ANISOU 4771  CG  GLU A 624     3929   3901   3970   -274    504   -350       C  
ATOM   4772  CD  GLU A 624      19.987  45.638   4.506  1.00 37.70           C  
ANISOU 4772  CD  GLU A 624     4724   4791   4810   -286    500   -383       C  
ATOM   4773  OE1 GLU A 624      20.923  44.959   4.031  1.00 39.79           O  
ANISOU 4773  OE1 GLU A 624     4969   5077   5072   -284    497   -396       O  
ATOM   4774  OE2 GLU A 624      20.022  46.084   5.673  1.00 41.36           O  
ANISOU 4774  OE2 GLU A 624     5168   5272   5272   -298    501   -398       O  
ATOM   4775  N   VAL A 625      17.738  45.353  -0.597  1.00 26.67           N  
ANISOU 4775  N   VAL A 625     3464   3262   3405   -230    516   -294       N  
ATOM   4776  CA  VAL A 625      17.835  44.923  -1.985  1.00 26.10           C  
ANISOU 4776  CA  VAL A 625     3410   3177   3328   -216    518   -284       C  
ATOM   4777  C   VAL A 625      19.295  45.037  -2.417  1.00 27.94           C  
ANISOU 4777  C   VAL A 625     3629   3426   3561   -239    542   -312       C  
ATOM   4778  O   VAL A 625      20.042  45.808  -1.814  1.00 26.31           O  
ANISOU 4778  O   VAL A 625     3409   3229   3355   -269    567   -338       O  
ATOM   4779  CB  VAL A 625      16.907  45.729  -2.923  1.00 26.71           C  
ANISOU 4779  CB  VAL A 625     3534   3215   3397   -205    537   -264       C  
ATOM   4780  CG1 VAL A 625      15.440  45.491  -2.554  1.00 27.12           C  
ANISOU 4780  CG1 VAL A 625     3597   3258   3449   -180    510   -238       C  
ATOM   4781  CG2 VAL A 625      17.259  47.228  -2.926  1.00 26.60           C  
ANISOU 4781  CG2 VAL A 625     3544   3181   3380   -234    584   -277       C  
ATOM   4782  N   PRO A 626      19.712  44.269  -3.441  1.00 28.31           N  
ANISOU 4782  N   PRO A 626     3675   3476   3605   -226    535   -310       N  
ATOM   4783  CA  PRO A 626      21.083  44.416  -3.930  1.00 30.37           C  
ANISOU 4783  CA  PRO A 626     3922   3751   3864   -248    560   -337       C  
ATOM   4784  C   PRO A 626      21.301  45.817  -4.511  1.00 32.33           C  
ANISOU 4784  C   PRO A 626     4204   3971   4108   -273    609   -345       C  
ATOM   4785  O   PRO A 626      20.440  46.337  -5.226  1.00 33.17           O  
ANISOU 4785  O   PRO A 626     4351   4043   4209   -261    621   -323       O  
ATOM   4786  CB  PRO A 626      21.182  43.366  -5.042  1.00 29.24           C  
ANISOU 4786  CB  PRO A 626     3782   3609   3718   -223    542   -325       C  
ATOM   4787  CG  PRO A 626      20.046  42.410  -4.824  1.00 28.49           C  
ANISOU 4787  CG  PRO A 626     3686   3511   3625   -191    502   -299       C  
ATOM   4788  CD  PRO A 626      18.962  43.264  -4.216  1.00 29.63           C  
ANISOU 4788  CD  PRO A 626     3852   3634   3770   -192    507   -285       C  
ATOM   4789  N   GLY A 627      22.440  46.429  -4.207  1.00 35.40           N  
ANISOU 4789  N   GLY A 627     4575   4375   4499   -308    639   -378       N  
ATOM   4790  CA  GLY A 627      22.700  47.781  -4.697  1.00 38.52           C  
ANISOU 4790  CA  GLY A 627     5003   4741   4892   -337    691   -389       C  
ATOM   4791  C   GLY A 627      22.367  48.913  -3.739  1.00 41.63           C  
ANISOU 4791  C   GLY A 627     5407   5122   5289   -360    713   -397       C  
ATOM   4792  O   GLY A 627      22.303  50.071  -4.156  1.00 41.96           O  
ANISOU 4792  O   GLY A 627     5486   5129   5328   -378    757   -399       O  
ATOM   4793  N   GLY A 628      22.146  48.603  -2.463  1.00 43.59           N  
ANISOU 4793  N   GLY A 628     5624   5395   5542   -358    685   -402       N  
ATOM   4794  CA  GLY A 628      22.182  49.643  -1.429  1.00 45.40           C  
ANISOU 4794  CA  GLY A 628     5849   5623   5775   -388    709   -422       C  
ATOM   4795  C   GLY A 628      20.882  49.970  -0.722  1.00 46.31           C  
ANISOU 4795  C   GLY A 628     5984   5720   5891   -372    694   -398       C  
ATOM   4796  O   GLY A 628      20.891  50.545   0.374  1.00 48.08           O  
ANISOU 4796  O   GLY A 628     6195   5953   6119   -391    701   -414       O  
TER    4797      GLY A 628                                                      
ATOM   4798  N   SER B  30     -11.508 -38.062 -12.202  1.00 33.45           N  
ANISOU 4798  N   SER B  30     4271   3835   4601   -111   -520    142       N  
ATOM   4799  CA  SER B  30     -12.586 -37.292 -11.518  1.00 33.88           C  
ANISOU 4799  CA  SER B  30     4272   3896   4705   -114   -519    164       C  
ATOM   4800  C   SER B  30     -12.597 -35.805 -11.886  1.00 32.10           C  
ANISOU 4800  C   SER B  30     4050   3680   4466   -108   -512    162       C  
ATOM   4801  O   SER B  30     -13.606 -35.280 -12.351  1.00 33.47           O  
ANISOU 4801  O   SER B  30     4211   3838   4667   -115   -546    175       O  
ATOM   4802  CB  SER B  30     -12.485 -37.460  -9.999  1.00 35.01           C  
ANISOU 4802  CB  SER B  30     4368   4062   4870   -110   -472    174       C  
ATOM   4803  OG  SER B  30     -12.759 -38.800  -9.619  1.00 38.82           O  
ANISOU 4803  OG  SER B  30     4839   4533   5376   -118   -483    181       O  
ATOM   4804  N   TYR B  31     -11.477 -35.126 -11.664  1.00 28.86           N  
ANISOU 4804  N   TYR B  31     3654   3294   4015    -94   -469    148       N  
ATOM   4805  CA  TYR B  31     -11.304 -33.726 -12.043  1.00 25.98           C  
ANISOU 4805  CA  TYR B  31     3297   2939   3632    -87   -460    143       C  
ATOM   4806  C   TYR B  31     -10.480 -33.665 -13.324  1.00 24.97           C  
ANISOU 4806  C   TYR B  31     3230   2801   3453    -83   -473    123       C  
ATOM   4807  O   TYR B  31      -9.927 -34.678 -13.737  1.00 23.32           O  
ANISOU 4807  O   TYR B  31     3054   2581   3222    -83   -480    112       O  
ATOM   4808  CB  TYR B  31     -10.614 -32.962 -10.904  1.00 24.11           C  
ANISOU 4808  CB  TYR B  31     3035   2735   3387    -75   -403    142       C  
ATOM   4809  CG  TYR B  31     -11.528 -32.848  -9.712  1.00 22.46           C  
ANISOU 4809  CG  TYR B  31     2771   2534   3227    -77   -388    164       C  
ATOM   4810  CD1 TYR B  31     -12.499 -31.848  -9.662  1.00 23.42           C  
ANISOU 4810  CD1 TYR B  31     2866   2653   3379    -78   -396    179       C  
ATOM   4811  CD2 TYR B  31     -11.472 -33.770  -8.669  1.00 19.53           C  
ANISOU 4811  CD2 TYR B  31     2377   2168   2873    -78   -368    170       C  
ATOM   4812  CE1 TYR B  31     -13.366 -31.748  -8.592  1.00 23.41           C  
ANISOU 4812  CE1 TYR B  31     2815   2655   3423    -79   -379    200       C  
ATOM   4813  CE2 TYR B  31     -12.332 -33.676  -7.585  1.00 18.78           C  
ANISOU 4813  CE2 TYR B  31     2234   2077   2821    -79   -351    190       C  
ATOM   4814  CZ  TYR B  31     -13.275 -32.659  -7.563  1.00 21.53           C  
ANISOU 4814  CZ  TYR B  31     2557   2423   3199    -79   -356    206       C  
ATOM   4815  OH  TYR B  31     -14.155 -32.551  -6.515  1.00 23.68           O  
ANISOU 4815  OH  TYR B  31     2783   2696   3517    -78   -336    228       O  
ATOM   4816  N   ASN B  32     -10.384 -32.494 -13.947  1.00 22.09           N  
ANISOU 4816  N   ASN B  32     2883   2440   3070    -77   -474    119       N  
ATOM   4817  CA  ASN B  32      -9.373 -32.309 -14.978  1.00 21.72           C  
ANISOU 4817  CA  ASN B  32     2892   2388   2970    -69   -471    100       C  
ATOM   4818  C   ASN B  32      -8.044 -32.008 -14.276  1.00 21.69           C  
ANISOU 4818  C   ASN B  32     2886   2413   2941    -55   -413     90       C  
ATOM   4819  O   ASN B  32      -7.717 -30.852 -13.983  1.00 21.59           O  
ANISOU 4819  O   ASN B  32     2861   2420   2921    -48   -386     90       O  
ATOM   4820  CB  ASN B  32      -9.755 -31.194 -15.958  1.00 21.77           C  
ANISOU 4820  CB  ASN B  32     2920   2384   2966    -68   -494     99       C  
ATOM   4821  CG  ASN B  32      -8.787 -31.084 -17.122  1.00 23.33           C  
ANISOU 4821  CG  ASN B  32     3182   2573   3109    -59   -493     81       C  
ATOM   4822  OD1 ASN B  32      -7.681 -31.633 -17.102  1.00 21.97           O  
ANISOU 4822  OD1 ASN B  32     3034   2406   2907    -50   -463     69       O  
ATOM   4823  ND2 ASN B  32      -9.194 -30.349 -18.143  1.00 27.20           N  
ANISOU 4823  ND2 ASN B  32     3700   3046   3587    -59   -523     80       N  
ATOM   4824  N   TYR B  33      -7.301 -33.067 -13.962  1.00 19.96           N  
ANISOU 4824  N   TYR B  33     2677   2196   2710    -54   -396     83       N  
ATOM   4825  CA  TYR B  33      -6.041 -32.921 -13.246  1.00 19.13           C  
ANISOU 4825  CA  TYR B  33     2566   2115   2585    -42   -345     76       C  
ATOM   4826  C   TYR B  33      -4.985 -32.207 -14.077  1.00 19.50           C  
ANISOU 4826  C   TYR B  33     2653   2163   2589    -31   -327     62       C  
ATOM   4827  O   TYR B  33      -4.078 -31.588 -13.516  1.00 19.08           O  
ANISOU 4827  O   TYR B  33     2590   2132   2526    -21   -287     60       O  
ATOM   4828  CB  TYR B  33      -5.514 -34.289 -12.810  1.00 17.29           C  
ANISOU 4828  CB  TYR B  33     2337   1881   2352    -43   -335     72       C  
ATOM   4829  CG  TYR B  33      -6.450 -34.979 -11.851  1.00 17.97           C  
ANISOU 4829  CG  TYR B  33     2379   1966   2480    -54   -346     87       C  
ATOM   4830  CD1 TYR B  33      -6.678 -34.460 -10.578  1.00 14.83           C  
ANISOU 4830  CD1 TYR B  33     1934   1592   2108    -53   -319     98       C  
ATOM   4831  CD2 TYR B  33      -7.114 -36.138 -12.218  1.00 14.55           C  
ANISOU 4831  CD2 TYR B  33     1954   1510   2062    -64   -382     90       C  
ATOM   4832  CE1 TYR B  33      -7.532 -35.084  -9.687  1.00 18.33           C  
ANISOU 4832  CE1 TYR B  33     2339   2033   2590    -61   -325    112       C  
ATOM   4833  CE2 TYR B  33      -7.968 -36.774 -11.334  1.00 19.07           C  
ANISOU 4833  CE2 TYR B  33     2486   2083   2677    -73   -390    104       C  
ATOM   4834  CZ  TYR B  33      -8.188 -36.242 -10.085  1.00 22.70           C  
ANISOU 4834  CZ  TYR B  33     2898   2564   3161    -71   -360    116       C  
ATOM   4835  OH  TYR B  33      -9.050 -36.890  -9.229  1.00 20.26           O  
ANISOU 4835  OH  TYR B  33     2550   2253   2894    -79   -365    132       O  
ATOM   4836  N   ALA B  34      -5.090 -32.330 -15.400  1.00 18.52           N  
ANISOU 4836  N   ALA B  34     2578   2015   2442    -30   -356     55       N  
ATOM   4837  CA  ALA B  34      -4.182 -31.631 -16.301  1.00 18.49           C  
ANISOU 4837  CA  ALA B  34     2617   2009   2399    -18   -339     44       C  
ATOM   4838  C   ALA B  34      -4.383 -30.120 -16.175  1.00 18.32           C  
ANISOU 4838  C   ALA B  34     2575   2003   2382    -15   -329     49       C  
ATOM   4839  O   ALA B  34      -3.407 -29.363 -16.133  1.00 18.00           O  
ANISOU 4839  O   ALA B  34     2539   1977   2321     -4   -294     44       O  
ATOM   4840  CB  ALA B  34      -4.331 -32.105 -17.746  1.00 19.40           C  
ANISOU 4840  CB  ALA B  34     2793   2091   2485    -18   -373     36       C  
ATOM   4841  N   GLU B  35      -5.642 -29.692 -16.112  1.00 18.59           N  
ANISOU 4841  N   GLU B  35     2584   2033   2444    -25   -361     59       N  
ATOM   4842  CA  GLU B  35      -5.944 -28.283 -15.907  1.00 18.74           C  
ANISOU 4842  CA  GLU B  35     2581   2066   2472    -22   -353     65       C  
ATOM   4843  C   GLU B  35      -5.471 -27.832 -14.528  1.00 17.31           C  
ANISOU 4843  C   GLU B  35     2355   1916   2305    -18   -309     69       C  
ATOM   4844  O   GLU B  35      -4.876 -26.753 -14.404  1.00 17.31           O  
ANISOU 4844  O   GLU B  35     2353   1931   2292    -10   -283     67       O  
ATOM   4845  CB  GLU B  35      -7.442 -27.990 -16.061  1.00 19.89           C  
ANISOU 4845  CB  GLU B  35     2705   2199   2651    -34   -396     78       C  
ATOM   4846  CG  GLU B  35      -7.780 -26.498 -15.918  1.00 22.18           C  
ANISOU 4846  CG  GLU B  35     2974   2503   2950    -30   -387     84       C  
ATOM   4847  CD  GLU B  35      -9.281 -26.238 -15.783  1.00 30.81           C  
ANISOU 4847  CD  GLU B  35     4032   3585   4087    -41   -422    102       C  
ATOM   4848  OE1 GLU B  35     -10.093 -27.101 -16.180  1.00 33.04           O  
ANISOU 4848  OE1 GLU B  35     4319   3845   4388    -52   -464    108       O  
ATOM   4849  OE2 GLU B  35      -9.670 -25.173 -15.265  1.00 28.67           O  
ANISOU 4849  OE2 GLU B  35     3729   3328   3834    -39   -409    110       O  
ATOM   4850  N   ALA B  36      -5.743 -28.632 -13.497  1.00 15.50           N  
ANISOU 4850  N   ALA B  36     2093   1694   2103    -24   -304     76       N  
ATOM   4851  CA  ALA B  36      -5.293 -28.255 -12.158  1.00 15.77           C  
ANISOU 4851  CA  ALA B  36     2090   1754   2147    -19   -264     80       C  
ATOM   4852  C   ALA B  36      -3.770 -28.094 -12.110  1.00 14.56           C  
ANISOU 4852  C   ALA B  36     1955   1612   1962     -9   -228     69       C  
ATOM   4853  O   ALA B  36      -3.261 -27.127 -11.545  1.00 12.90           O  
ANISOU 4853  O   ALA B  36     1731   1420   1748     -2   -200     69       O  
ATOM   4854  CB  ALA B  36      -5.772 -29.262 -11.119  1.00 16.35           C  
ANISOU 4854  CB  ALA B  36     2131   1829   2251    -26   -264     89       C  
ATOM   4855  N   LEU B  37      -3.047 -29.021 -12.741  1.00 14.85           N  
ANISOU 4855  N   LEU B  37     2026   1637   1977     -6   -228     60       N  
ATOM   4856  CA  LEU B  37      -1.581 -28.972 -12.807  1.00 14.31           C  
ANISOU 4856  CA  LEU B  37     1977   1577   1884      4   -194     51       C  
ATOM   4857  C   LEU B  37      -1.061 -27.722 -13.526  1.00 15.01           C  
ANISOU 4857  C   LEU B  37     2085   1666   1949     13   -182     47       C  
ATOM   4858  O   LEU B  37      -0.162 -27.021 -13.031  1.00 13.33           O  
ANISOU 4858  O   LEU B  37     1862   1471   1732     19   -150     47       O  
ATOM   4859  CB  LEU B  37      -1.040 -30.224 -13.511  1.00 15.25           C  
ANISOU 4859  CB  LEU B  37     2132   1676   1983      6   -198     44       C  
ATOM   4860  CG  LEU B  37       0.474 -30.284 -13.711  1.00 15.11           C  
ANISOU 4860  CG  LEU B  37     2135   1661   1942     18   -162     37       C  
ATOM   4861  CD1 LEU B  37       1.177 -30.217 -12.340  1.00 12.76           C  
ANISOU 4861  CD1 LEU B  37     1799   1387   1660     19   -130     42       C  
ATOM   4862  CD2 LEU B  37       0.798 -31.608 -14.432  1.00 17.29           C  
ANISOU 4862  CD2 LEU B  37     2450   1917   2203     20   -169     31       C  
ATOM   4863  N   GLN B  38      -1.629 -27.459 -14.702  1.00 15.55           N  
ANISOU 4863  N   GLN B  38     2185   1717   2005     12   -209     44       N  
ATOM   4864  CA  GLN B  38      -1.314 -26.256 -15.489  1.00 15.02           C  
ANISOU 4864  CA  GLN B  38     2139   1649   1917     20   -202     41       C  
ATOM   4865  C   GLN B  38      -1.400 -24.978 -14.657  1.00 14.64           C  
ANISOU 4865  C   GLN B  38     2053   1623   1883     21   -185     47       C  
ATOM   4866  O   GLN B  38      -0.502 -24.139 -14.696  1.00 13.80           O  
ANISOU 4866  O   GLN B  38     1952   1527   1763     29   -158     44       O  
ATOM   4867  CB  GLN B  38      -2.291 -26.163 -16.661  1.00 15.85           C  
ANISOU 4867  CB  GLN B  38     2276   1732   2015     15   -244     40       C  
ATOM   4868  CG  GLN B  38      -2.333 -24.861 -17.448  1.00 14.53           C  
ANISOU 4868  CG  GLN B  38     2126   1562   1831     21   -246     39       C  
ATOM   4869  CD  GLN B  38      -3.370 -24.924 -18.570  1.00 20.66           C  
ANISOU 4869  CD  GLN B  38     2935   2313   2602     15   -294     39       C  
ATOM   4870  OE1 GLN B  38      -4.507 -25.339 -18.343  1.00 19.22           O  
ANISOU 4870  OE1 GLN B  38     2732   2123   2447      3   -329     46       O  
ATOM   4871  NE2 GLN B  38      -2.979 -24.520 -19.780  1.00 16.76           N  
ANISOU 4871  NE2 GLN B  38     2491   1802   2073     23   -297     32       N  
ATOM   4872  N   LYS B  39      -2.491 -24.831 -13.915  1.00 14.28           N  
ANISOU 4872  N   LYS B  39     1973   1585   1868     12   -201     56       N  
ATOM   4873  CA  LYS B  39      -2.701 -23.666 -13.064  1.00 14.82           C  
ANISOU 4873  CA  LYS B  39     2006   1672   1951     13   -185     62       C  
ATOM   4874  C   LYS B  39      -1.792 -23.676 -11.831  1.00 13.79           C  
ANISOU 4874  C   LYS B  39     1852   1561   1824     16   -150     63       C  
ATOM   4875  O   LYS B  39      -1.298 -22.618 -11.433  1.00 15.20           O  
ANISOU 4875  O   LYS B  39     2022   1754   1999     22   -128     63       O  
ATOM   4876  CB  LYS B  39      -4.185 -23.535 -12.684  1.00 12.94           C  
ANISOU 4876  CB  LYS B  39     1738   1431   1745      4   -211     74       C  
ATOM   4877  CG  LYS B  39      -5.054 -23.202 -13.900  1.00 16.08           C  
ANISOU 4877  CG  LYS B  39     2158   1810   2141      1   -248     75       C  
ATOM   4878  CD  LYS B  39      -6.554 -23.194 -13.629  1.00 16.28           C  
ANISOU 4878  CD  LYS B  39     2152   1827   2204     -8   -277     89       C  
ATOM   4879  CE  LYS B  39      -7.290 -22.661 -14.866  1.00 15.68           C  
ANISOU 4879  CE  LYS B  39     2099   1732   2124    -11   -315     90       C  
ATOM   4880  NZ  LYS B  39      -8.764 -22.669 -14.673  1.00 18.30           N  
ANISOU 4880  NZ  LYS B  39     2399   2053   2498    -20   -346    106       N  
ATOM   4881  N   ALA B  40      -1.591 -24.844 -11.220  1.00 13.51           N  
ANISOU 4881  N   ALA B  40     1809   1527   1797     13   -146     63       N  
ATOM   4882  CA  ALA B  40      -0.770 -24.948 -10.013  1.00 12.83           C  
ANISOU 4882  CA  ALA B  40     1701   1456   1715     15   -116     65       C  
ATOM   4883  C   ALA B  40       0.684 -24.550 -10.287  1.00 13.65           C  
ANISOU 4883  C   ALA B  40     1822   1564   1797     24    -90     58       C  
ATOM   4884  O   ALA B  40       1.337 -23.983  -9.412  1.00 14.95           O  
ANISOU 4884  O   ALA B  40     1970   1744   1964     27    -68     61       O  
ATOM   4885  CB  ALA B  40      -0.839 -26.349  -9.387  1.00 12.88           C  
ANISOU 4885  CB  ALA B  40     1697   1460   1734     10   -118     67       C  
ATOM   4886  N   ILE B  41       1.167 -24.842 -11.494  1.00 14.52           N  
ANISOU 4886  N   ILE B  41     1968   1661   1887     29    -93     52       N  
ATOM   4887  CA  ILE B  41       2.490 -24.428 -11.987  1.00 14.12           C  
ANISOU 4887  CA  ILE B  41     1937   1609   1817     39    -68     48       C  
ATOM   4888  C   ILE B  41       2.526 -22.925 -12.281  1.00 14.61           C  
ANISOU 4888  C   ILE B  41     2000   1678   1873     43    -62     48       C  
ATOM   4889  O   ILE B  41       3.510 -22.256 -11.978  1.00 14.69           O  
ANISOU 4889  O   ILE B  41     2003   1696   1880     49    -38     50       O  
ATOM   4890  CB  ILE B  41       2.887 -25.203 -13.265  1.00 14.43           C  
ANISOU 4890  CB  ILE B  41     2018   1627   1834     45    -71     41       C  
ATOM   4891  CG1 ILE B  41       3.131 -26.683 -12.947  1.00 15.26           C  
ANISOU 4891  CG1 ILE B  41     2125   1727   1945     42    -71     40       C  
ATOM   4892  CG2 ILE B  41       4.154 -24.613 -13.904  1.00 12.37           C  
ANISOU 4892  CG2 ILE B  41     1779   1363   1555     57    -42     39       C  
ATOM   4893  CD1 ILE B  41       3.181 -27.566 -14.188  1.00 13.09           C  
ANISOU 4893  CD1 ILE B  41     1895   1428   1649     46    -81     34       C  
ATOM   4894  N   TYR B  42       1.471 -22.402 -12.901  1.00 13.74           N  
ANISOU 4894  N   TYR B  42     1897   1562   1762     41    -86     48       N  
ATOM   4895  CA  TYR B  42       1.397 -20.987 -13.264  1.00 13.72           C  
ANISOU 4895  CA  TYR B  42     1896   1562   1752     45    -83     49       C  
ATOM   4896  C   TYR B  42       1.496 -20.106 -12.026  1.00 13.42           C  
ANISOU 4896  C   TYR B  42     1823   1545   1730     43    -67     54       C  
ATOM   4897  O   TYR B  42       2.049 -19.000 -12.087  1.00 14.12           O  
ANISOU 4897  O   TYR B  42     1912   1640   1812     49    -52     54       O  
ATOM   4898  CB  TYR B  42       0.064 -20.722 -13.973  1.00 13.59           C  
ANISOU 4898  CB  TYR B  42     1889   1536   1738     40   -116     50       C  
ATOM   4899  CG  TYR B  42      -0.296 -19.275 -14.242  1.00 16.90           C  
ANISOU 4899  CG  TYR B  42     2304   1959   2155     42   -118     52       C  
ATOM   4900  CD1 TYR B  42      -0.992 -18.522 -13.301  1.00 15.50           C  
ANISOU 4900  CD1 TYR B  42     2092   1796   2000     38   -119     59       C  
ATOM   4901  CD2 TYR B  42       0.024 -18.678 -15.464  1.00 15.12           C  
ANISOU 4901  CD2 TYR B  42     2114   1722   1906     49   -119     48       C  
ATOM   4902  CE1 TYR B  42      -1.366 -17.207 -13.563  1.00 16.34           C  
ANISOU 4902  CE1 TYR B  42     2196   1905   2105     41   -121     61       C  
ATOM   4903  CE2 TYR B  42      -0.352 -17.365 -15.748  1.00 17.01           C  
ANISOU 4903  CE2 TYR B  42     2351   1965   2145     51   -123     50       C  
ATOM   4904  CZ  TYR B  42      -1.041 -16.643 -14.789  1.00 17.55           C  
ANISOU 4904  CZ  TYR B  42     2383   2049   2237     46   -124     57       C  
ATOM   4905  OH  TYR B  42      -1.440 -15.366 -15.080  1.00 13.79           O  
ANISOU 4905  OH  TYR B  42     1904   1574   1759     49   -128     59       O  
ATOM   4906  N   PHE B  43       0.948 -20.587 -10.910  1.00 11.36           N  
ANISOU 4906  N   PHE B  43     1534   1292   1489     37    -71     59       N  
ATOM   4907  CA  PHE B  43       1.114 -19.913  -9.620  1.00 12.34           C  
ANISOU 4907  CA  PHE B  43     1630   1432   1624     36    -54     64       C  
ATOM   4908  C   PHE B  43       2.539 -19.434  -9.363  1.00 10.92           C  
ANISOU 4908  C   PHE B  43     1453   1259   1436     42    -29     62       C  
ATOM   4909  O   PHE B  43       2.731 -18.310  -8.895  1.00 12.77           O  
ANISOU 4909  O   PHE B  43     1677   1502   1671     44    -19     64       O  
ATOM   4910  CB  PHE B  43       0.664 -20.813  -8.463  1.00 12.46           C  
ANISOU 4910  CB  PHE B  43     1623   1452   1658     30    -55     68       C  
ATOM   4911  CG  PHE B  43       0.997 -20.256  -7.099  1.00 13.84           C  
ANISOU 4911  CG  PHE B  43     1776   1640   1840     31    -37     73       C  
ATOM   4912  CD1 PHE B  43       0.342 -19.129  -6.610  1.00 14.89           C  
ANISOU 4912  CD1 PHE B  43     1896   1780   1980     32    -35     77       C  
ATOM   4913  CD2 PHE B  43       1.977 -20.844  -6.322  1.00 15.54           C  
ANISOU 4913  CD2 PHE B  43     1988   1861   2055     31    -23     72       C  
ATOM   4914  CE1 PHE B  43       0.659 -18.606  -5.357  1.00 16.13           C  
ANISOU 4914  CE1 PHE B  43     2040   1946   2139     33    -18     80       C  
ATOM   4915  CE2 PHE B  43       2.294 -20.335  -5.051  1.00 18.49           C  
ANISOU 4915  CE2 PHE B  43     2347   2245   2434     31     -9     76       C  
ATOM   4916  CZ  PHE B  43       1.632 -19.217  -4.577  1.00 18.61           C  
ANISOU 4916  CZ  PHE B  43     2352   2264   2451     32     -7     80       C  
ATOM   4917  N   TYR B  44       3.535 -20.283  -9.617  1.00 11.74           N  
ANISOU 4917  N   TYR B  44     1569   1358   1533     45    -19     59       N  
ATOM   4918  CA  TYR B  44       4.922 -19.891  -9.370  1.00 10.40           C  
ANISOU 4918  CA  TYR B  44     1398   1192   1361     50      3     61       C  
ATOM   4919  C   TYR B  44       5.378 -18.711 -10.221  1.00 12.90           C  
ANISOU 4919  C   TYR B  44     1728   1505   1666     56     12     60       C  
ATOM   4920  O   TYR B  44       6.204 -17.919  -9.763  1.00 12.89           O  
ANISOU 4920  O   TYR B  44     1717   1510   1668     59     27     63       O  
ATOM   4921  CB  TYR B  44       5.885 -21.073  -9.526  1.00  9.85           C  
ANISOU 4921  CB  TYR B  44     1337   1114   1290     52     14     60       C  
ATOM   4922  CG  TYR B  44       5.676 -22.068  -8.417  1.00 11.23           C  
ANISOU 4922  CG  TYR B  44     1492   1294   1478     45     10     62       C  
ATOM   4923  CD1 TYR B  44       6.236 -21.862  -7.165  1.00 10.84           C  
ANISOU 4923  CD1 TYR B  44     1422   1255   1439     43     19     67       C  
ATOM   4924  CD2 TYR B  44       4.870 -23.192  -8.604  1.00 12.33           C  
ANISOU 4924  CD2 TYR B  44     1637   1427   1619     41     -5     60       C  
ATOM   4925  CE1 TYR B  44       6.014 -22.773  -6.131  1.00 11.91           C  
ANISOU 4925  CE1 TYR B  44     1543   1395   1586     37     15     70       C  
ATOM   4926  CE2 TYR B  44       4.642 -24.105  -7.572  1.00 11.93           C  
ANISOU 4926  CE2 TYR B  44     1569   1381   1581     35     -8     63       C  
ATOM   4927  CZ  TYR B  44       5.229 -23.887  -6.343  1.00 14.66           C  
ANISOU 4927  CZ  TYR B  44     1895   1738   1937     34      3     68       C  
ATOM   4928  OH  TYR B  44       5.024 -24.784  -5.309  1.00 11.51           O  
ANISOU 4928  OH  TYR B  44     1481   1342   1548     29      1     71       O  
ATOM   4929  N   GLU B  45       4.838 -18.570 -11.432  1.00 13.05           N  
ANISOU 4929  N   GLU B  45     1771   1514   1671     59      1     56       N  
ATOM   4930  CA  GLU B  45       5.149 -17.373 -12.224  1.00 13.32           C  
ANISOU 4930  CA  GLU B  45     1819   1545   1694     66      9     56       C  
ATOM   4931  C   GLU B  45       4.609 -16.106 -11.575  1.00 13.45           C  
ANISOU 4931  C   GLU B  45     1815   1574   1718     63      5     58       C  
ATOM   4932  O   GLU B  45       5.197 -15.035 -11.741  1.00 13.04           O  
ANISOU 4932  O   GLU B  45     1766   1525   1664     68     17     60       O  
ATOM   4933  CB  GLU B  45       4.667 -17.508 -13.674  1.00 13.32           C  
ANISOU 4933  CB  GLU B  45     1854   1529   1675     70     -3     51       C  
ATOM   4934  CG  GLU B  45       5.516 -18.528 -14.409  1.00 16.33           C  
ANISOU 4934  CG  GLU B  45     2262   1895   2044     77      9     49       C  
ATOM   4935  CD  GLU B  45       4.965 -18.998 -15.746  1.00 17.60           C  
ANISOU 4935  CD  GLU B  45     2465   2038   2185     80     -6     43       C  
ATOM   4936  OE1 GLU B  45       4.400 -18.172 -16.502  1.00 14.98           O  
ANISOU 4936  OE1 GLU B  45     2149   1700   1841     82    -18     42       O  
ATOM   4937  OE2 GLU B  45       5.113 -20.212 -16.028  1.00 16.48           O  
ANISOU 4937  OE2 GLU B  45     2339   1883   2036     81     -8     41       O  
ATOM   4938  N   CYS B  46       3.483 -16.219 -10.870  1.00 11.41           N  
ANISOU 4938  N   CYS B  46     1540   1322   1472     56    -10     60       N  
ATOM   4939  CA  CYS B  46       2.930 -15.094 -10.114  1.00 12.12           C  
ANISOU 4939  CA  CYS B  46     1611   1423   1571     54    -11     63       C  
ATOM   4940  C   CYS B  46       3.851 -14.697  -8.958  1.00 12.78           C  
ANISOU 4940  C   CYS B  46     1677   1516   1660     54      6     66       C  
ATOM   4941  O   CYS B  46       3.812 -13.542  -8.514  1.00 11.86           O  
ANISOU 4941  O   CYS B  46     1553   1405   1545     55     10     68       O  
ATOM   4942  CB  CYS B  46       1.539 -15.418  -9.552  1.00 12.37           C  
ANISOU 4942  CB  CYS B  46     1625   1456   1616     48    -27     66       C  
ATOM   4943  SG  CYS B  46       0.316 -15.801 -10.827  1.00 13.40           S  
ANISOU 4943  SG  CYS B  46     1772   1572   1746     46    -56     66       S  
ATOM   4944  N   GLN B  47       4.664 -15.641  -8.475  1.00 12.35           N  
ANISOU 4944  N   GLN B  47     1620   1461   1609     53     14     66       N  
ATOM   4945  CA  GLN B  47       5.570 -15.395  -7.337  1.00 12.12           C  
ANISOU 4945  CA  GLN B  47     1576   1439   1588     51     26     70       C  
ATOM   4946  C   GLN B  47       6.955 -14.885  -7.752  1.00 12.88           C  
ANISOU 4946  C   GLN B  47     1679   1532   1683     56     41     72       C  
ATOM   4947  O   GLN B  47       7.781 -14.592  -6.886  1.00 13.70           O  
ANISOU 4947  O   GLN B  47     1772   1638   1795     54     47     76       O  
ATOM   4948  CB  GLN B  47       5.747 -16.675  -6.513  1.00 11.69           C  
ANISOU 4948  CB  GLN B  47     1513   1385   1542     47     25     71       C  
ATOM   4949  CG  GLN B  47       4.430 -17.202  -5.900  1.00 12.50           C  
ANISOU 4949  CG  GLN B  47     1606   1491   1650     42     14     72       C  
ATOM   4950  CD  GLN B  47       3.728 -16.202  -4.998  1.00 15.58           C  
ANISOU 4950  CD  GLN B  47     1985   1888   2044     42     14     75       C  
ATOM   4951  OE1 GLN B  47       2.861 -15.447  -5.455  1.00 17.22           O  
ANISOU 4951  OE1 GLN B  47     2194   2096   2252     43      8     75       O  
ATOM   4952  NE2 GLN B  47       4.087 -16.198  -3.708  1.00 16.84           N  
ANISOU 4952  NE2 GLN B  47     2136   2052   2207     39     20     78       N  
ATOM   4953  N   GLN B  48       7.235 -14.781  -9.054  1.00 12.21           N  
ANISOU 4953  N   GLN B  48     1612   1438   1588     62     46     70       N  
ATOM   4954  CA  GLN B  48       8.613 -14.476  -9.461  1.00 10.95           C  
ANISOU 4954  CA  GLN B  48     1457   1272   1431     68     64     75       C  
ATOM   4955  C   GLN B  48       9.036 -13.045  -9.133  1.00 12.31           C  
ANISOU 4955  C   GLN B  48     1620   1449   1608     68     69     78       C  
ATOM   4956  O   GLN B  48       8.336 -12.091  -9.485  1.00 12.57           O  
ANISOU 4956  O   GLN B  48     1658   1484   1633     69     64     76       O  
ATOM   4957  CB  GLN B  48       8.846 -14.787 -10.945  1.00  9.58           C  
ANISOU 4957  CB  GLN B  48     1309   1085   1244     76     73     73       C  
ATOM   4958  CG  GLN B  48       8.825 -16.283 -11.286  1.00 10.66           C  
ANISOU 4958  CG  GLN B  48     1458   1214   1377     77     73     70       C  
ATOM   4959  CD  GLN B  48       8.851 -16.520 -12.800  1.00 14.19           C  
ANISOU 4959  CD  GLN B  48     1939   1645   1805     86     79     67       C  
ATOM   4960  OE1 GLN B  48       8.540 -15.614 -13.583  1.00 15.85           O  
ANISOU 4960  OE1 GLN B  48     2165   1853   2004     90     77     65       O  
ATOM   4961  NE2 GLN B  48       9.241 -17.723 -13.212  1.00 13.21           N  
ANISOU 4961  NE2 GLN B  48     1831   1511   1678     90     86     66       N  
ATOM   4962  N   ALA B  49      10.186 -12.905  -8.472  1.00 11.12           N  
ANISOU 4962  N   ALA B  49     1456   1296   1471     67     78     85       N  
ATOM   4963  CA  ALA B  49      10.826 -11.602  -8.327  1.00 12.77           C  
ANISOU 4963  CA  ALA B  49     1659   1505   1687     68     83     90       C  
ATOM   4964  C   ALA B  49      11.566 -11.213  -9.606  1.00 13.21           C  
ANISOU 4964  C   ALA B  49     1727   1550   1741     77    101     94       C  
ATOM   4965  O   ALA B  49      11.872 -12.084 -10.431  1.00 15.52           O  
ANISOU 4965  O   ALA B  49     2032   1833   2029     83    113     95       O  
ATOM   4966  CB  ALA B  49      11.794 -11.618  -7.154  1.00  9.50           C  
ANISOU 4966  CB  ALA B  49     1226   1090   1290     62     82     98       C  
ATOM   4967  N   GLY B  50      11.876  -9.929  -9.771  1.00 13.33           N  
ANISOU 4967  N   GLY B  50     1741   1565   1759     78    105     98       N  
ATOM   4968  CA  GLY B  50      12.597  -9.485 -10.971  1.00 14.35           C  
ANISOU 4968  CA  GLY B  50     1881   1682   1887     88    125    103       C  
ATOM   4969  C   GLY B  50      14.058  -9.916 -11.001  1.00 14.14           C  
ANISOU 4969  C   GLY B  50     1844   1643   1882     92    145    116       C  
ATOM   4970  O   GLY B  50      14.657 -10.138  -9.942  1.00 15.60           O  
ANISOU 4970  O   GLY B  50     2009   1830   2086     84    138    121       O  
ATOM   4971  N   PRO B  51      14.652 -10.017 -12.209  1.00 14.57           N  
ANISOU 4971  N   PRO B  51     1915   1684   1934    103    169    121       N  
ATOM   4972  CA  PRO B  51      13.981  -9.743 -13.486  1.00 14.32           C  
ANISOU 4972  CA  PRO B  51     1914   1649   1878    112    174    114       C  
ATOM   4973  C   PRO B  51      13.186 -10.959 -13.947  1.00 14.33           C  
ANISOU 4973  C   PRO B  51     1936   1649   1858    113    168    105       C  
ATOM   4974  O   PRO B  51      13.637 -12.096 -13.778  1.00 14.27           O  
ANISOU 4974  O   PRO B  51     1926   1636   1857    114    174    107       O  
ATOM   4975  CB  PRO B  51      15.150  -9.497 -14.454  1.00 14.58           C  
ANISOU 4975  CB  PRO B  51     1955   1664   1919    124    207    127       C  
ATOM   4976  CG  PRO B  51      16.220 -10.414 -13.901  1.00 15.94           C  
ANISOU 4976  CG  PRO B  51     2108   1830   2117    124    219    137       C  
ATOM   4977  CD  PRO B  51      16.107 -10.170 -12.404  1.00 14.09           C  
ANISOU 4977  CD  PRO B  51     1843   1609   1899    109    193    136       C  
ATOM   4978  N   LEU B  52      12.013 -10.723 -14.523  1.00 14.93           N  
ANISOU 4978  N   LEU B  52     2032   1727   1911    114    152     95       N  
ATOM   4979  CA  LEU B  52      11.158 -11.816 -14.985  1.00 15.71           C  
ANISOU 4979  CA  LEU B  52     2153   1823   1992    114    140     86       C  
ATOM   4980  C   LEU B  52      11.703 -12.414 -16.276  1.00 17.38           C  
ANISOU 4980  C   LEU B  52     2398   2015   2188    127    162     87       C  
ATOM   4981  O   LEU B  52      12.222 -11.682 -17.117  1.00 18.67           O  
ANISOU 4981  O   LEU B  52     2577   2168   2346    136    181     92       O  
ATOM   4982  CB  LEU B  52       9.735 -11.311 -15.229  1.00 15.74           C  
ANISOU 4982  CB  LEU B  52     2166   1833   1979    109    114     77       C  
ATOM   4983  CG  LEU B  52       8.968 -10.699 -14.054  1.00 17.82           C  
ANISOU 4983  CG  LEU B  52     2402   2114   2254     98     94     75       C  
ATOM   4984  CD1 LEU B  52       7.544 -10.421 -14.543  1.00 14.07           C  
ANISOU 4984  CD1 LEU B  52     1940   1641   1765     96     71     68       C  
ATOM   4985  CD2 LEU B  52       8.958 -11.686 -12.861  1.00 13.70           C  
ANISOU 4985  CD2 LEU B  52     1858   1600   1746     90     87     75       C  
ATOM   4986  N   PRO B  53      11.582 -13.737 -16.446  1.00 17.44           N  
ANISOU 4986  N   PRO B  53     2420   2016   2190    127    160     84       N  
ATOM   4987  CA  PRO B  53      12.016 -14.356 -17.700  1.00 18.13           C  
ANISOU 4987  CA  PRO B  53     2546   2081   2259    141    181     84       C  
ATOM   4988  C   PRO B  53      11.044 -13.966 -18.808  1.00 20.16           C  
ANISOU 4988  C   PRO B  53     2842   2330   2486    144    166     76       C  
ATOM   4989  O   PRO B  53       9.915 -13.549 -18.515  1.00 17.95           O  
ANISOU 4989  O   PRO B  53     2554   2062   2202    135    135     69       O  
ATOM   4990  CB  PRO B  53      11.906 -15.857 -17.413  1.00 19.87           C  
ANISOU 4990  CB  PRO B  53     2770   2299   2480    138    175     80       C  
ATOM   4991  CG  PRO B  53      10.830 -15.964 -16.321  1.00 17.04           C  
ANISOU 4991  CG  PRO B  53     2384   1960   2129    122    140     73       C  
ATOM   4992  CD  PRO B  53      10.915 -14.681 -15.529  1.00 15.41           C  
ANISOU 4992  CD  PRO B  53     2146   1769   1939    116    137     78       C  
ATOM   4993  N   GLU B  54      11.477 -14.099 -20.060  1.00 21.51           N  
ANISOU 4993  N   GLU B  54     3055   2480   2636    159    187     77       N  
ATOM   4994  CA  GLU B  54      10.637 -13.731 -21.203  1.00 24.57           C  
ANISOU 4994  CA  GLU B  54     3485   2856   2993    163    172     70       C  
ATOM   4995  C   GLU B  54       9.399 -14.613 -21.301  1.00 22.69           C  
ANISOU 4995  C   GLU B  54     3264   2616   2740    154    134     59       C  
ATOM   4996  O   GLU B  54       8.363 -14.183 -21.805  1.00 22.20           O  
ANISOU 4996  O   GLU B  54     3220   2552   2661    151    106     53       O  
ATOM   4997  CB  GLU B  54      11.439 -13.778 -22.507  1.00 26.99           C  
ANISOU 4997  CB  GLU B  54     3839   3137   3278    182    207     75       C  
ATOM   4998  CG  GLU B  54      12.571 -12.753 -22.528  1.00 37.08           C  
ANISOU 4998  CG  GLU B  54     5100   4413   4572    191    243     88       C  
ATOM   4999  CD  GLU B  54      12.091 -11.302 -22.506  1.00 48.94           C  
ANISOU 4999  CD  GLU B  54     6590   5927   6075    187    230     88       C  
ATOM   5000  OE1 GLU B  54      11.442 -10.871 -23.486  1.00 53.55           O  
ANISOU 5000  OE1 GLU B  54     7212   6501   6630    191    219     83       O  
ATOM   5001  OE2 GLU B  54      12.379 -10.572 -21.528  1.00 51.32           O  
ANISOU 5001  OE2 GLU B  54     6846   6246   6404    179    229     93       O  
ATOM   5002  N   TRP B  55       9.498 -15.825 -20.762  1.00 20.91           N  
ANISOU 5002  N   TRP B  55     3029   2392   2523    150    132     57       N  
ATOM   5003  CA  TRP B  55       8.382 -16.766 -20.771  1.00 19.91           C  
ANISOU 5003  CA  TRP B  55     2915   2263   2387    141     96     48       C  
ATOM   5004  C   TRP B  55       7.317 -16.572 -19.686  1.00 19.77           C  
ANISOU 5004  C   TRP B  55     2856   2267   2389    124     62     46       C  
ATOM   5005  O   TRP B  55       6.324 -17.309 -19.666  1.00 19.36           O  
ANISOU 5005  O   TRP B  55     2809   2212   2335    116     31     40       O  
ATOM   5006  CB  TRP B  55       8.901 -18.211 -20.791  1.00 19.69           C  
ANISOU 5006  CB  TRP B  55     2900   2222   2357    145    108     47       C  
ATOM   5007  CG  TRP B  55       9.979 -18.549 -19.775  1.00 22.10           C  
ANISOU 5007  CG  TRP B  55     3165   2538   2690    145    135     55       C  
ATOM   5008  CD1 TRP B  55      11.329 -18.602 -20.001  1.00 23.91           C  
ANISOU 5008  CD1 TRP B  55     3398   2757   2926    158    177     65       C  
ATOM   5009  CD2 TRP B  55       9.789 -18.913 -18.396  1.00 16.96           C  
ANISOU 5009  CD2 TRP B  55     2468   1907   2066    131    122     56       C  
ATOM   5010  NE1 TRP B  55      11.984 -18.961 -18.847  1.00 20.54           N  
ANISOU 5010  NE1 TRP B  55     2928   2344   2530    152    186     71       N  
ATOM   5011  CE2 TRP B  55      11.066 -19.169 -17.853  1.00 17.44           C  
ANISOU 5011  CE2 TRP B  55     2507   1971   2148    136    153     66       C  
ATOM   5012  CE3 TRP B  55       8.658 -19.055 -17.574  1.00 14.07           C  
ANISOU 5012  CE3 TRP B  55     2077   1557   1709    117     87     51       C  
ATOM   5013  CZ2 TRP B  55      11.257 -19.546 -16.517  1.00 16.25           C  
ANISOU 5013  CZ2 TRP B  55     2314   1836   2023    126    148     69       C  
ATOM   5014  CZ3 TRP B  55       8.846 -19.437 -16.235  1.00 16.56           C  
ANISOU 5014  CZ3 TRP B  55     2351   1889   2050    108     86     55       C  
ATOM   5015  CH2 TRP B  55      10.137 -19.674 -15.727  1.00 16.81           C  
ANISOU 5015  CH2 TRP B  55     2366   1922   2099    112    115     63       C  
ATOM   5016  N   ASN B  56       7.509 -15.616 -18.775  1.00 18.01           N  
ANISOU 5016  N   ASN B  56     2592   2063   2187    120     69     51       N  
ATOM   5017  CA  ASN B  56       6.515 -15.364 -17.731  1.00 18.16           C  
ANISOU 5017  CA  ASN B  56     2575   2100   2223    106     42     50       C  
ATOM   5018  C   ASN B  56       5.165 -14.988 -18.352  1.00 19.10           C  
ANISOU 5018  C   ASN B  56     2710   2214   2331    102      9     45       C  
ATOM   5019  O   ASN B  56       5.107 -14.104 -19.195  1.00 18.29           O  
ANISOU 5019  O   ASN B  56     2629   2105   2213    108      9     45       O  
ATOM   5020  CB  ASN B  56       6.997 -14.275 -16.759  1.00 16.77           C  
ANISOU 5020  CB  ASN B  56     2362   1943   2067    104     56     55       C  
ATOM   5021  CG  ASN B  56       5.973 -13.943 -15.688  1.00 19.78           C  
ANISOU 5021  CG  ASN B  56     2710   2341   2464     92     33     55       C  
ATOM   5022  OD1 ASN B  56       4.968 -13.282 -15.966  1.00 16.00           O  
ANISOU 5022  OD1 ASN B  56     2234   1863   1982     89     13     53       O  
ATOM   5023  ND2 ASN B  56       6.263 -14.328 -14.437  1.00 12.58           N  
ANISOU 5023  ND2 ASN B  56     1767   1440   1571     86     38     57       N  
ATOM   5024  N   ARG B  57       4.091 -15.666 -17.939  1.00 17.18           N  
ANISOU 5024  N   ARG B  57     2456   1974   2097     91    -20     43       N  
ATOM   5025  CA  ARG B  57       2.784 -15.519 -18.565  1.00 17.68           C  
ANISOU 5025  CA  ARG B  57     2534   2029   2154     86    -56     41       C  
ATOM   5026  C   ARG B  57       1.818 -14.612 -17.806  1.00 16.31           C  
ANISOU 5026  C   ARG B  57     2324   1870   2001     78    -72     45       C  
ATOM   5027  O   ARG B  57       0.642 -14.554 -18.153  1.00 16.86           O  
ANISOU 5027  O   ARG B  57     2397   1933   2074     72   -104     45       O  
ATOM   5028  CB  ARG B  57       2.113 -16.892 -18.717  1.00 16.51           C  
ANISOU 5028  CB  ARG B  57     2398   1869   2006     80    -82     37       C  
ATOM   5029  CG  ARG B  57       2.855 -17.834 -19.643  1.00 19.89           C  
ANISOU 5029  CG  ARG B  57     2870   2276   2409     88    -71     33       C  
ATOM   5030  CD  ARG B  57       2.287 -19.236 -19.557  1.00 17.88           C  
ANISOU 5030  CD  ARG B  57     2622   2011   2158     81    -95     30       C  
ATOM   5031  NE  ARG B  57       2.741 -19.872 -18.323  1.00 15.48           N  
ANISOU 5031  NE  ARG B  57     2281   1725   1877     77    -78     32       N  
ATOM   5032  CZ  ARG B  57       2.242 -21.011 -17.855  1.00 19.64           C  
ANISOU 5032  CZ  ARG B  57     2797   2249   2415     69    -95     32       C  
ATOM   5033  NH1 ARG B  57       1.258 -21.606 -18.510  1.00 14.55           N  
ANISOU 5033  NH1 ARG B  57     2175   1588   1766     63   -131     29       N  
ATOM   5034  NH2 ARG B  57       2.723 -21.549 -16.738  1.00 14.36           N  
ANISOU 5034  NH2 ARG B  57     2095   1595   1765     66    -78     34       N  
ATOM   5035  N   VAL B  58       2.301 -13.889 -16.805  1.00 15.41           N  
ANISOU 5035  N   VAL B  58     2178   1775   1902     78    -51     48       N  
ATOM   5036  CA  VAL B  58       1.422 -13.150 -15.909  1.00 13.62           C  
ANISOU 5036  CA  VAL B  58     1916   1562   1695     71    -61     53       C  
ATOM   5037  C   VAL B  58       1.397 -11.664 -16.268  1.00 15.99           C  
ANISOU 5037  C   VAL B  58     2219   1865   1991     76    -57     54       C  
ATOM   5038  O   VAL B  58       2.342 -10.934 -15.949  1.00 14.45           O  
ANISOU 5038  O   VAL B  58     2016   1677   1794     81    -32     56       O  
ATOM   5039  CB  VAL B  58       1.870 -13.305 -14.439  1.00 13.20           C  
ANISOU 5039  CB  VAL B  58     1827   1525   1660     68    -44     55       C  
ATOM   5040  CG1 VAL B  58       0.792 -12.741 -13.513  1.00 10.68           C  
ANISOU 5040  CG1 VAL B  58     1479   1217   1362     62    -55     60       C  
ATOM   5041  CG2 VAL B  58       2.140 -14.772 -14.084  1.00 14.17           C  
ANISOU 5041  CG2 VAL B  58     1950   1646   1787     65    -43     54       C  
ATOM   5042  N   GLU B  59       0.330 -11.202 -16.921  1.00 16.12           N  
ANISOU 5042  N   GLU B  59     2244   1874   2005     74    -82     56       N  
ATOM   5043  CA  GLU B  59       0.295  -9.824 -17.442  1.00 15.78           C  
ANISOU 5043  CA  GLU B  59     2208   1831   1955     79    -80     57       C  
ATOM   5044  C   GLU B  59       0.345  -8.783 -16.323  1.00 16.44           C  
ANISOU 5044  C   GLU B  59     2257   1933   2056     78    -64     61       C  
ATOM   5045  O   GLU B  59       0.698  -7.622 -16.563  1.00 16.06           O  
ANISOU 5045  O   GLU B  59     2212   1887   2001     83    -53     62       O  
ATOM   5046  CB  GLU B  59      -0.968  -9.574 -18.292  1.00 18.47           C  
ANISOU 5046  CB  GLU B  59     2563   2159   2295     76   -114     59       C  
ATOM   5047  CG  GLU B  59      -2.277  -9.691 -17.493  1.00 17.51           C  
ANISOU 5047  CG  GLU B  59     2406   2042   2202     66   -137     65       C  
ATOM   5048  CD  GLU B  59      -3.530  -9.363 -18.303  1.00 25.79           C  
ANISOU 5048  CD  GLU B  59     3465   3078   3256     62   -173     70       C  
ATOM   5049  OE1 GLU B  59      -3.569  -8.343 -19.014  1.00 26.71           O  
ANISOU 5049  OE1 GLU B  59     3597   3190   3361     67   -176     70       O  
ATOM   5050  OE2 GLU B  59      -4.517 -10.115 -18.214  1.00 20.31           O  
ANISOU 5050  OE2 GLU B  59     2761   2376   2580     54   -201     74       O  
ATOM   5051  N   TRP B  60      -0.023  -9.180 -15.106  1.00 12.74           N  
ANISOU 5051  N   TRP B  60     1757   1474   1607     72    -64     64       N  
ATOM   5052  CA  TRP B  60      -0.013  -8.230 -13.995  1.00 14.46           C  
ANISOU 5052  CA  TRP B  60     1948   1707   1839     71    -50     67       C  
ATOM   5053  C   TRP B  60       1.262  -8.295 -13.135  1.00 13.40           C  
ANISOU 5053  C   TRP B  60     1804   1582   1704     73    -24     66       C  
ATOM   5054  O   TRP B  60       1.300  -7.743 -12.037  1.00 16.47           O  
ANISOU 5054  O   TRP B  60     2171   1980   2103     71    -14     69       O  
ATOM   5055  CB  TRP B  60      -1.282  -8.387 -13.144  1.00 14.02           C  
ANISOU 5055  CB  TRP B  60     1865   1655   1806     65    -63     73       C  
ATOM   5056  CG  TRP B  60      -1.589  -9.824 -12.773  1.00 12.78           C  
ANISOU 5056  CG  TRP B  60     1702   1496   1659     60    -72     74       C  
ATOM   5057  CD1 TRP B  60      -2.304 -10.738 -13.514  1.00 15.35           C  
ANISOU 5057  CD1 TRP B  60     2038   1808   1986     56    -97     74       C  
ATOM   5058  CD2 TRP B  60      -1.221 -10.494 -11.556  1.00 12.62           C  
ANISOU 5058  CD2 TRP B  60     1663   1484   1647     57    -58     74       C  
ATOM   5059  NE1 TRP B  60      -2.378 -11.941 -12.834  1.00 11.76           N  
ANISOU 5059  NE1 TRP B  60     1571   1355   1542     51    -98     75       N  
ATOM   5060  CE2 TRP B  60      -1.731 -11.811 -11.631  1.00 13.74           C  
ANISOU 5060  CE2 TRP B  60     1804   1618   1796     52    -73     75       C  
ATOM   5061  CE3 TRP B  60      -0.496 -10.111 -10.413  1.00 13.75           C  
ANISOU 5061  CE3 TRP B  60     1792   1638   1792     59    -35     75       C  
ATOM   5062  CZ2 TRP B  60      -1.547 -12.742 -10.599  1.00 15.86           C  
ANISOU 5062  CZ2 TRP B  60     2057   1893   2075     49    -64     76       C  
ATOM   5063  CZ3 TRP B  60      -0.319 -11.036  -9.388  1.00 14.18           C  
ANISOU 5063  CZ3 TRP B  60     1834   1697   1855     55    -29     76       C  
ATOM   5064  CH2 TRP B  60      -0.826 -12.344  -9.498  1.00 15.68           C  
ANISOU 5064  CH2 TRP B  60     2022   1881   2052     51    -42     76       C  
ATOM   5065  N   ARG B  61       2.299  -8.966 -13.627  1.00 13.70           N  
ANISOU 5065  N   ARG B  61     1859   1614   1730     76    -13     63       N  
ATOM   5066  CA  ARG B  61       3.595  -8.929 -12.961  1.00 14.19           C  
ANISOU 5066  CA  ARG B  61     1913   1682   1796     77      9     64       C  
ATOM   5067  C   ARG B  61       4.628  -8.269 -13.864  1.00 14.85           C  
ANISOU 5067  C   ARG B  61     2015   1759   1867     85     26     65       C  
ATOM   5068  O   ARG B  61       4.699  -8.528 -15.074  1.00 15.32           O  
ANISOU 5068  O   ARG B  61     2102   1806   1911     91     25     63       O  
ATOM   5069  CB  ARG B  61       4.059 -10.324 -12.500  1.00 13.52           C  
ANISOU 5069  CB  ARG B  61     1824   1597   1715     75     13     63       C  
ATOM   5070  CG  ARG B  61       3.217 -10.951 -11.382  1.00 12.43           C  
ANISOU 5070  CG  ARG B  61     1664   1466   1591     67      2     64       C  
ATOM   5071  CD  ARG B  61       3.261 -10.122 -10.077  1.00 13.28           C  
ANISOU 5071  CD  ARG B  61     1750   1585   1710     65     10     68       C  
ATOM   5072  NE  ARG B  61       4.586  -9.516  -9.990  1.00 14.80           N  
ANISOU 5072  NE  ARG B  61     1944   1778   1900     68     27     69       N  
ATOM   5073  CZ  ARG B  61       5.699 -10.171  -9.684  1.00 16.64           C  
ANISOU 5073  CZ  ARG B  61     2175   2010   2136     68     37     70       C  
ATOM   5074  NH1 ARG B  61       5.638 -11.449  -9.312  1.00 15.45           N  
ANISOU 5074  NH1 ARG B  61     2021   1859   1989     64     34     69       N  
ATOM   5075  NH2 ARG B  61       6.869  -9.539  -9.745  1.00 14.50           N  
ANISOU 5075  NH2 ARG B  61     1904   1737   1867     71     51     73       N  
ATOM   5076  N   GLY B  62       5.430  -7.402 -13.260  1.00 15.12           N  
ANISOU 5076  N   GLY B  62     2036   1800   1909     86     41     68       N  
ATOM   5077  CA  GLY B  62       6.587  -6.824 -13.938  1.00 15.85           C  
ANISOU 5077  CA  GLY B  62     2140   1885   1996     93     61     71       C  
ATOM   5078  C   GLY B  62       7.855  -7.083 -13.152  1.00 16.78           C  
ANISOU 5078  C   GLY B  62     2241   2004   2128     92     77     76       C  
ATOM   5079  O   GLY B  62       7.849  -7.808 -12.153  1.00 14.36           O  
ANISOU 5079  O   GLY B  62     1920   1704   1832     86     72     76       O  
ATOM   5080  N   ASP B  63       8.962  -6.511 -13.616  1.00 18.07           N  
ANISOU 5080  N   ASP B  63     2409   2161   2295     98     96     82       N  
ATOM   5081  CA  ASP B  63      10.242  -6.654 -12.920  1.00 17.69           C  
ANISOU 5081  CA  ASP B  63     2343   2111   2265     97    110     90       C  
ATOM   5082  C   ASP B  63      10.126  -5.940 -11.581  1.00 18.61           C  
ANISOU 5082  C   ASP B  63     2437   2238   2394     88     99     90       C  
ATOM   5083  O   ASP B  63       9.801  -4.757 -11.516  1.00 23.89           O  
ANISOU 5083  O   ASP B  63     3104   2910   3061     88     95     90       O  
ATOM   5084  CB  ASP B  63      11.377  -6.040 -13.746  1.00 18.41           C  
ANISOU 5084  CB  ASP B  63     2441   2190   2360    106    134     98       C  
ATOM   5085  CG  ASP B  63      11.754  -6.879 -14.959  1.00 23.29           C  
ANISOU 5085  CG  ASP B  63     3085   2795   2968    116    152    100       C  
ATOM   5086  OD1 ASP B  63      11.270  -8.023 -15.124  1.00 20.09           O  
ANISOU 5086  OD1 ASP B  63     2692   2388   2552    115    144     94       O  
ATOM   5087  OD2 ASP B  63      12.560  -6.373 -15.770  1.00 24.50           O  
ANISOU 5087  OD2 ASP B  63     3249   2936   3122    125    174    107       O  
ATOM   5088  N   ALA B  64      10.322  -6.655 -10.486  1.00 17.27           N  
ANISOU 5088  N   ALA B  64     2252   2073   2235     82     93     91       N  
ATOM   5089  CA  ALA B  64      10.130  -6.048  -9.179  1.00 14.11           C  
ANISOU 5089  CA  ALA B  64     1837   1680   1842     74     82     91       C  
ATOM   5090  C   ALA B  64      11.378  -6.325  -8.363  1.00 13.90           C  
ANISOU 5090  C   ALA B  64     1797   1650   1835     70     85     99       C  
ATOM   5091  O   ALA B  64      12.137  -7.255  -8.659  1.00 13.59           O  
ANISOU 5091  O   ALA B  64     1755   1604   1803     72     94    103       O  
ATOM   5092  CB  ALA B  64       8.918  -6.645  -8.494  1.00 13.62           C  
ANISOU 5092  CB  ALA B  64     1773   1627   1774     70     68     84       C  
ATOM   5093  N   THR B  65      11.525  -5.543  -7.299  1.00 12.84           N  
ANISOU 5093  N   THR B  65     1652   1517   1706     64     75    101       N  
ATOM   5094  CA  THR B  65      12.639  -5.653  -6.372  1.00 13.50           C  
ANISOU 5094  CA  THR B  65     1723   1595   1809     58     71    109       C  
ATOM   5095  C   THR B  65      13.972  -5.789  -7.093  1.00 13.83           C  
ANISOU 5095  C   THR B  65     1759   1625   1870     62     86    120       C  
ATOM   5096  O   THR B  65      14.812  -6.607  -6.744  1.00 12.46           O  
ANISOU 5096  O   THR B  65     1575   1446   1713     59     87    127       O  
ATOM   5097  CB  THR B  65      12.382  -6.715  -5.276  1.00 13.38           C  
ANISOU 5097  CB  THR B  65     1704   1584   1793     52     60    106       C  
ATOM   5098  OG1 THR B  65      12.102  -7.999  -5.851  1.00 15.34           O  
ANISOU 5098  OG1 THR B  65     1956   1834   2038     55     67    103       O  
ATOM   5099  CG2 THR B  65      11.192  -6.308  -4.426  1.00 14.75           C  
ANISOU 5099  CG2 THR B  65     1884   1766   1953     49     49     98       C  
ATOM   5100  N   MET B  66      14.171  -4.930  -8.092  1.00 15.37           N  
ANISOU 5100  N   MET B  66     1958   1815   2064     68     98    123       N  
ATOM   5101  CA  MET B  66      15.385  -4.982  -8.890  1.00 14.72           C  
ANISOU 5101  CA  MET B  66     1871   1720   2000     74    118    135       C  
ATOM   5102  C   MET B  66      16.608  -4.481  -8.123  1.00 16.42           C  
ANISOU 5102  C   MET B  66     2066   1925   2246     67    112    148       C  
ATOM   5103  O   MET B  66      17.726  -4.665  -8.597  1.00 14.95           O  
ANISOU 5103  O   MET B  66     1869   1726   2083     71    129    162       O  
ATOM   5104  CB  MET B  66      15.186  -4.251 -10.228  1.00 16.20           C  
ANISOU 5104  CB  MET B  66     2073   1904   2176     84    135    135       C  
ATOM   5105  CG  MET B  66      14.156  -4.942 -11.132  1.00 13.05           C  
ANISOU 5105  CG  MET B  66     1697   1510   1750     91    139    124       C  
ATOM   5106  SD  MET B  66      14.685  -6.606 -11.605  1.00 16.31           S  
ANISOU 5106  SD  MET B  66     2115   1915   2167     96    155    127       S  
ATOM   5107  CE  MET B  66      16.189  -6.222 -12.534  1.00 19.64           C  
ANISOU 5107  CE  MET B  66     2534   2316   2609    107    187    144       C  
ATOM   5108  N   ASN B  67      16.418  -3.871  -6.951  1.00 13.28           N  
ANISOU 5108  N   ASN B  67     1663   1531   1849     58     89    146       N  
ATOM   5109  CA  ASN B  67      17.566  -3.492  -6.122  1.00 15.53           C  
ANISOU 5109  CA  ASN B  67     1931   1804   2163     50     77    159       C  
ATOM   5110  C   ASN B  67      17.998  -4.559  -5.138  1.00 15.22           C  
ANISOU 5110  C   ASN B  67     1883   1763   2137     42     63    162       C  
ATOM   5111  O   ASN B  67      18.895  -4.316  -4.341  1.00 17.64           O  
ANISOU 5111  O   ASN B  67     2176   2057   2466     34     47    173       O  
ATOM   5112  CB  ASN B  67      17.319  -2.202  -5.339  1.00 15.42           C  
ANISOU 5112  CB  ASN B  67     1922   1791   2145     43     56    156       C  
ATOM   5113  CG  ASN B  67      17.203  -1.002  -6.242  1.00 22.74           C  
ANISOU 5113  CG  ASN B  67     2854   2717   3069     49     68    157       C  
ATOM   5114  OD1 ASN B  67      16.412  -0.097  -5.994  1.00 32.27           O  
ANISOU 5114  OD1 ASN B  67     4071   3930   4257     48     59    148       O  
ATOM   5115  ND2 ASN B  67      18.016  -0.975  -7.284  1.00 21.91           N  
ANISOU 5115  ND2 ASN B  67     2740   2602   2981     56     90    168       N  
ATOM   5116  N   ASP B  68      17.356  -5.720  -5.173  1.00 15.24           N  
ANISOU 5116  N   ASP B  68     1892   1773   2122     45     68    154       N  
ATOM   5117  CA  ASP B  68      17.694  -6.801  -4.241  1.00 15.81           C  
ANISOU 5117  CA  ASP B  68     1956   1844   2204     38     56    156       C  
ATOM   5118  C   ASP B  68      19.138  -7.271  -4.369  1.00 16.03           C  
ANISOU 5118  C   ASP B  68     1964   1856   2268     38     63    174       C  
ATOM   5119  O   ASP B  68      19.715  -7.272  -5.462  1.00 16.23           O  
ANISOU 5119  O   ASP B  68     1984   1873   2307     46     87    183       O  
ATOM   5120  CB  ASP B  68      16.751  -7.981  -4.448  1.00 15.10           C  
ANISOU 5120  CB  ASP B  68     1877   1765   2093     42     63    145       C  
ATOM   5121  CG  ASP B  68      15.416  -7.800  -3.735  1.00 16.02           C  
ANISOU 5121  CG  ASP B  68     2008   1896   2183     39     49    131       C  
ATOM   5122  OD1 ASP B  68      15.147  -6.730  -3.125  1.00 16.27           O  
ANISOU 5122  OD1 ASP B  68     2044   1927   2208     35     36    129       O  
ATOM   5123  OD2 ASP B  68      14.635  -8.775  -3.787  1.00 15.06           O  
ANISOU 5123  OD2 ASP B  68     1892   1782   2048     41     51    123       O  
ATOM   5124  N   GLU B  69      19.723  -7.669  -3.246  1.00 16.54           N  
ANISOU 5124  N   GLU B  69     2019   1914   2351     28     42    181       N  
ATOM   5125  CA  GLU B  69      21.109  -8.143  -3.249  1.00 17.17           C  
ANISOU 5125  CA  GLU B  69     2075   1977   2470     26     45    200       C  
ATOM   5126  C   GLU B  69      21.277  -9.373  -4.140  1.00 17.22           C  
ANISOU 5126  C   GLU B  69     2079   1983   2480     36     73    203       C  
ATOM   5127  O   GLU B  69      22.320  -9.530  -4.783  1.00 16.04           O  
ANISOU 5127  O   GLU B  69     1912   1818   2361     42     92    220       O  
ATOM   5128  CB  GLU B  69      21.574  -8.485  -1.835  1.00 17.05           C  
ANISOU 5128  CB  GLU B  69     2053   1955   2469     13     13    206       C  
ATOM   5129  CG  GLU B  69      22.944  -9.157  -1.752  1.00 18.70           C  
ANISOU 5129  CG  GLU B  69     2236   2145   2722     11     13    227       C  
ATOM   5130  CD  GLU B  69      24.112  -8.248  -2.102  1.00 26.93           C  
ANISOU 5130  CD  GLU B  69     3257   3168   3804     10     15    247       C  
ATOM   5131  OE1 GLU B  69      23.952  -7.009  -2.124  1.00 24.90           O  
ANISOU 5131  OE1 GLU B  69     3005   2910   3542      7      6    245       O  
ATOM   5132  OE2 GLU B  69      25.203  -8.796  -2.365  1.00 30.63           O  
ANISOU 5132  OE2 GLU B  69     3702   3622   4313     12     25    267       O  
ATOM   5133  N   VAL B  70      20.276 -10.253  -4.140  1.00 15.10           N  
ANISOU 5133  N   VAL B  70     1826   1728   2183     39     75    188       N  
ATOM   5134  CA  VAL B  70      20.198 -11.355  -5.110  1.00 14.56           C  
ANISOU 5134  CA  VAL B  70     1762   1659   2108     49    102    186       C  
ATOM   5135  C   VAL B  70      18.884 -11.268  -5.892  1.00 15.35           C  
ANISOU 5135  C   VAL B  70     1886   1773   2170     56    111    169       C  
ATOM   5136  O   VAL B  70      17.795 -11.210  -5.308  1.00 14.50           O  
ANISOU 5136  O   VAL B  70     1789   1679   2039     51     94    155       O  
ATOM   5137  CB  VAL B  70      20.329 -12.744  -4.428  1.00 15.52           C  
ANISOU 5137  CB  VAL B  70     1878   1781   2236     45     94    187       C  
ATOM   5138  CG1 VAL B  70      20.448 -13.867  -5.472  1.00 11.47           C  
ANISOU 5138  CG1 VAL B  70     1370   1264   1722     56    123    188       C  
ATOM   5139  CG2 VAL B  70      21.560 -12.778  -3.500  1.00 12.49           C  
ANISOU 5139  CG2 VAL B  70     1470   1383   1890     36     78    205       C  
ATOM   5140  N   LEU B  71      18.998 -11.260  -7.216  1.00 14.30           N  
ANISOU 5140  N   LEU B  71     1763   1635   2035     68    137    170       N  
ATOM   5141  CA  LEU B  71      17.839 -11.142  -8.108  1.00 15.58           C  
ANISOU 5141  CA  LEU B  71     1950   1806   2163     75    144    156       C  
ATOM   5142  C   LEU B  71      17.136 -12.465  -8.395  1.00 13.88           C  
ANISOU 5142  C   LEU B  71     1749   1595   1928     77    147    146       C  
ATOM   5143  O   LEU B  71      17.712 -13.530  -8.177  1.00 16.64           O  
ANISOU 5143  O   LEU B  71     2091   1939   2292     78    152    152       O  
ATOM   5144  CB  LEU B  71      18.267 -10.484  -9.422  1.00 13.79           C  
ANISOU 5144  CB  LEU B  71     1732   1568   1936     86    170    162       C  
ATOM   5145  CG  LEU B  71      18.819  -9.064  -9.261  1.00 16.46           C  
ANISOU 5145  CG  LEU B  71     2058   1903   2292     84    167    171       C  
ATOM   5146  CD1 LEU B  71      19.339  -8.603 -10.610  1.00 18.33           C  
ANISOU 5146  CD1 LEU B  71     2304   2127   2532     97    199    180       C  
ATOM   5147  CD2 LEU B  71      17.727  -8.120  -8.738  1.00 18.06           C  
ANISOU 5147  CD2 LEU B  71     2268   2120   2473     77    144    158       C  
ATOM   5148  N   GLY B  72      15.889 -12.411  -8.866  1.00 15.14           N  
ANISOU 5148  N   GLY B  72     1929   1765   2059     79    141    132       N  
ATOM   5149  CA  GLY B  72      15.139 -13.633  -9.167  1.00 12.93           C  
ANISOU 5149  CA  GLY B  72     1663   1487   1761     81    140    122       C  
ATOM   5150  C   GLY B  72      14.664 -14.342  -7.903  1.00 14.47           C  
ANISOU 5150  C   GLY B  72     1846   1692   1957     71    120    118       C  
ATOM   5151  O   GLY B  72      14.576 -13.730  -6.844  1.00 14.31           O  
ANISOU 5151  O   GLY B  72     1814   1679   1943     63    104    118       O  
ATOM   5152  N   GLY B  73      14.351 -15.632  -8.004  1.00 14.22           N  
ANISOU 5152  N   GLY B  73     1822   1660   1921     71    120    114       N  
ATOM   5153  CA  GLY B  73      13.749 -16.355  -6.888  1.00 14.89           C  
ANISOU 5153  CA  GLY B  73     1898   1754   2005     63    102    109       C  
ATOM   5154  C   GLY B  73      12.255 -16.053  -6.765  1.00 13.95           C  
ANISOU 5154  C   GLY B  73     1787   1646   1866     59     86     98       C  
ATOM   5155  O   GLY B  73      11.693 -15.268  -7.526  1.00 13.56           O  
ANISOU 5155  O   GLY B  73     1750   1598   1804     63     87     94       O  
ATOM   5156  N   TRP B  74      11.618 -16.651  -5.767  1.00 11.76           N  
ANISOU 5156  N   TRP B  74     1503   1376   1588     52     73     95       N  
ATOM   5157  CA  TRP B  74      10.203 -16.433  -5.514  1.00 10.93           C  
ANISOU 5157  CA  TRP B  74     1401   1280   1470     49     60     87       C  
ATOM   5158  C   TRP B  74       9.969 -15.645  -4.228  1.00 11.84           C  
ANISOU 5158  C   TRP B  74     1508   1403   1588     44     51     89       C  
ATOM   5159  O   TRP B  74      10.631 -15.907  -3.222  1.00  9.93           O  
ANISOU 5159  O   TRP B  74     1256   1159   1355     39     47     93       O  
ATOM   5160  CB  TRP B  74       9.506 -17.781  -5.372  1.00  9.62           C  
ANISOU 5160  CB  TRP B  74     1237   1115   1301     47     54     84       C  
ATOM   5161  CG  TRP B  74       9.521 -18.682  -6.594  1.00 11.75           C  
ANISOU 5161  CG  TRP B  74     1522   1377   1566     52     59     81       C  
ATOM   5162  CD1 TRP B  74       9.299 -18.330  -7.907  1.00 10.87           C  
ANISOU 5162  CD1 TRP B  74     1428   1258   1441     59     63     77       C  
ATOM   5163  CD2 TRP B  74       9.679 -20.106  -6.591  1.00 12.07           C  
ANISOU 5163  CD2 TRP B  74     1563   1411   1608     51     60     80       C  
ATOM   5164  NE1 TRP B  74       9.343 -19.459  -8.723  1.00  8.87           N  
ANISOU 5164  NE1 TRP B  74     1191    995   1182     62     66     74       N  
ATOM   5165  CE2 TRP B  74       9.573 -20.555  -7.931  1.00  8.60           C  
ANISOU 5165  CE2 TRP B  74     1146    962   1158     58     65     76       C  
ATOM   5166  CE3 TRP B  74       9.893 -21.049  -5.583  1.00 11.59           C  
ANISOU 5166  CE3 TRP B  74     1491   1354   1559     46     57     83       C  
ATOM   5167  CZ2 TRP B  74       9.721 -21.896  -8.283  1.00  8.99           C  
ANISOU 5167  CZ2 TRP B  74     1206   1003   1207     59     67     75       C  
ATOM   5168  CZ3 TRP B  74      10.024 -22.385  -5.938  1.00 11.99           C  
ANISOU 5168  CZ3 TRP B  74     1548   1397   1610     47     60     82       C  
ATOM   5169  CH2 TRP B  74       9.914 -22.798  -7.274  1.00 11.27           C  
ANISOU 5169  CH2 TRP B  74     1478   1295   1507     54     65     78       C  
ATOM   5170  N   TYR B  75       8.976 -14.753  -4.260  1.00 11.33           N  
ANISOU 5170  N   TYR B  75     1446   1343   1514     44     46     85       N  
ATOM   5171  CA  TYR B  75       8.386 -14.192  -3.042  1.00 11.73           C  
ANISOU 5171  CA  TYR B  75     1492   1399   1562     40     39     85       C  
ATOM   5172  C   TYR B  75       7.676 -15.364  -2.376  1.00 11.54           C  
ANISOU 5172  C   TYR B  75     1465   1378   1539     37     34     84       C  
ATOM   5173  O   TYR B  75       7.128 -16.219  -3.072  1.00 10.54           O  
ANISOU 5173  O   TYR B  75     1340   1251   1412     38     34     81       O  
ATOM   5174  CB  TYR B  75       7.366 -13.100  -3.373  1.00 12.22           C  
ANISOU 5174  CB  TYR B  75     1559   1466   1617     43     37     82       C  
ATOM   5175  CG  TYR B  75       7.971 -11.978  -4.183  1.00 13.39           C  
ANISOU 5175  CG  TYR B  75     1712   1612   1763     47     42     82       C  
ATOM   5176  CD1 TYR B  75       9.111 -11.307  -3.734  1.00 11.01           C  
ANISOU 5176  CD1 TYR B  75     1408   1307   1469     45     44     87       C  
ATOM   5177  CD2 TYR B  75       7.402 -11.593  -5.393  1.00 14.59           C  
ANISOU 5177  CD2 TYR B  75     1871   1762   1907     52     43     79       C  
ATOM   5178  CE1 TYR B  75       9.683 -10.278  -4.487  1.00 10.16           C  
ANISOU 5178  CE1 TYR B  75     1302   1195   1361     49     49     89       C  
ATOM   5179  CE2 TYR B  75       7.961 -10.557  -6.156  1.00 11.28           C  
ANISOU 5179  CE2 TYR B  75     1459   1341   1487     56     49     80       C  
ATOM   5180  CZ  TYR B  75       9.094  -9.921  -5.692  1.00 12.06           C  
ANISOU 5180  CZ  TYR B  75     1552   1436   1594     54     54     85       C  
ATOM   5181  OH  TYR B  75       9.628  -8.911  -6.450  1.00 12.09           O  
ANISOU 5181  OH  TYR B  75     1560   1436   1598     58     61     87       O  
ATOM   5182  N   ASP B  76       7.707 -15.436  -1.046  1.00 10.78           N  
ANISOU 5182  N   ASP B  76     1367   1284   1445     34     31     87       N  
ATOM   5183  CA  ASP B  76       7.308 -16.684  -0.401  1.00 11.68           C  
ANISOU 5183  CA  ASP B  76     1477   1399   1562     31     29     87       C  
ATOM   5184  C   ASP B  76       5.807 -16.975  -0.466  1.00 11.51           C  
ANISOU 5184  C   ASP B  76     1454   1380   1539     32     29     86       C  
ATOM   5185  O   ASP B  76       5.362 -18.082  -0.792  1.00 12.27           O  
ANISOU 5185  O   ASP B  76     1546   1476   1640     31     27     85       O  
ATOM   5186  CB  ASP B  76       7.765 -16.677   1.065  1.00 11.35           C  
ANISOU 5186  CB  ASP B  76     1436   1354   1520     27     26     91       C  
ATOM   5187  CG  ASP B  76       7.355 -17.940   1.791  1.00 15.06           C  
ANISOU 5187  CG  ASP B  76     1904   1825   1993     25     25     93       C  
ATOM   5188  OD1 ASP B  76       7.813 -19.023   1.375  1.00 13.26           O  
ANISOU 5188  OD1 ASP B  76     1670   1595   1771     23     25     93       O  
ATOM   5189  OD2 ASP B  76       6.542 -17.860   2.735  1.00 13.58           O  
ANISOU 5189  OD2 ASP B  76     1720   1638   1799     25     27     94       O  
ATOM   5190  N   ALA B  77       5.008 -15.984  -0.097  1.00 10.97           N  
ANISOU 5190  N   ALA B  77     1387   1314   1467     34     31     86       N  
ATOM   5191  CA  ALA B  77       3.619 -16.257   0.234  1.00 11.10           C  
ANISOU 5191  CA  ALA B  77     1398   1332   1487     36     33     89       C  
ATOM   5192  C   ALA B  77       2.784 -15.102  -0.311  1.00 11.57           C  
ANISOU 5192  C   ALA B  77     1457   1392   1545     40     34     88       C  
ATOM   5193  O   ALA B  77       2.824 -14.833  -1.507  1.00 13.70           O  
ANISOU 5193  O   ALA B  77     1728   1661   1814     41     29     85       O  
ATOM   5194  CB  ALA B  77       3.465 -16.448   1.760  1.00  9.78           C  
ANISOU 5194  CB  ALA B  77     1233   1163   1318     35     39     93       C  
ATOM   5195  N   GLY B  78       2.054 -14.397   0.545  1.00 11.73           N  
ANISOU 5195  N   GLY B  78     1478   1412   1565     43     41     92       N  
ATOM   5196  CA  GLY B  78       1.203 -13.314   0.087  1.00 12.61           C  
ANISOU 5196  CA  GLY B  78     1589   1524   1679     47     43     93       C  
ATOM   5197  C   GLY B  78       1.878 -11.959   0.167  1.00 14.25           C  
ANISOU 5197  C   GLY B  78     1806   1732   1875     49     46     90       C  
ATOM   5198  O   GLY B  78       1.236 -10.941  -0.094  1.00 12.95           O  
ANISOU 5198  O   GLY B  78     1642   1567   1710     53     49     91       O  
ATOM   5199  N   ALA B  79       3.181 -11.964   0.458  1.00 13.89           N  
ANISOU 5199  N   ALA B  79     1768   1686   1822     46     43     88       N  
ATOM   5200  CA  ALA B  79       3.980 -10.739   0.557  1.00 13.06           C  
ANISOU 5200  CA  ALA B  79     1672   1579   1709     47     43     86       C  
ATOM   5201  C   ALA B  79       5.285 -10.889  -0.209  1.00 12.99           C  
ANISOU 5201  C   ALA B  79     1663   1570   1703     44     37     84       C  
ATOM   5202  O   ALA B  79       5.305 -11.628  -1.184  1.00 14.22           O  
ANISOU 5202  O   ALA B  79     1813   1726   1862     43     35     83       O  
ATOM   5203  CB  ALA B  79       4.242 -10.382   2.030  1.00 12.23           C  
ANISOU 5203  CB  ALA B  79     1580   1470   1597     46     45     88       C  
ATOM   5204  N   HIS B  80       6.351 -10.188   0.184  1.00 11.45           N  
ANISOU 5204  N   HIS B  80     1474   1371   1505     41     33     85       N  
ATOM   5205  CA  HIS B  80       7.467  -9.983  -0.745  1.00 11.77           C  
ANISOU 5205  CA  HIS B  80     1511   1409   1551     41     32     85       C  
ATOM   5206  C   HIS B  80       8.822 -10.352  -0.162  1.00 12.13           C  
ANISOU 5206  C   HIS B  80     1554   1448   1604     35     26     90       C  
ATOM   5207  O   HIS B  80       9.853  -9.935  -0.670  1.00 11.39           O  
ANISOU 5207  O   HIS B  80     1457   1349   1518     35     25     93       O  
ATOM   5208  CB  HIS B  80       7.438  -8.576  -1.345  1.00 11.67           C  
ANISOU 5208  CB  HIS B  80     1502   1396   1535     44     34     84       C  
ATOM   5209  CG  HIS B  80       6.125  -8.283  -1.999  1.00 13.24           C  
ANISOU 5209  CG  HIS B  80     1701   1599   1729     49     37     81       C  
ATOM   5210  ND1 HIS B  80       5.144  -7.540  -1.381  1.00 14.17           N  
ANISOU 5210  ND1 HIS B  80     1823   1719   1842     51     40     81       N  
ATOM   5211  CD2 HIS B  80       5.567  -8.774  -3.131  1.00 12.74           C  
ANISOU 5211  CD2 HIS B  80     1635   1538   1666     51     38     79       C  
ATOM   5212  CE1 HIS B  80       4.059  -7.533  -2.135  1.00 14.25           C  
ANISOU 5212  CE1 HIS B  80     1828   1732   1854     55     41     81       C  
ATOM   5213  NE2 HIS B  80       4.292  -8.267  -3.208  1.00 15.81           N  
ANISOU 5213  NE2 HIS B  80     2022   1929   2053     54     38     79       N  
ATOM   5214  N   VAL B  81       8.825 -11.135   0.911  1.00 11.65           N  
ANISOU 5214  N   VAL B  81     1496   1386   1543     32     21     91       N  
ATOM   5215  CA  VAL B  81      10.108 -11.585   1.451  1.00 11.70           C  
ANISOU 5215  CA  VAL B  81     1499   1385   1559     26     13     97       C  
ATOM   5216  C   VAL B  81      10.550 -12.798   0.645  1.00 12.31           C  
ANISOU 5216  C   VAL B  81     1564   1462   1647     26     18     98       C  
ATOM   5217  O   VAL B  81       9.711 -13.629   0.291  1.00 11.95           O  
ANISOU 5217  O   VAL B  81     1518   1423   1598     29     23     94       O  
ATOM   5218  CB  VAL B  81      10.016 -11.996   2.936  1.00 11.28           C  
ANISOU 5218  CB  VAL B  81     1456   1328   1501     22      4     98       C  
ATOM   5219  CG1 VAL B  81      11.381 -12.454   3.443  1.00 10.52           C  
ANISOU 5219  CG1 VAL B  81     1355   1222   1418     15     -8    105       C  
ATOM   5220  CG2 VAL B  81       9.565 -10.825   3.792  1.00 10.76           C  
ANISOU 5220  CG2 VAL B  81     1407   1259   1421     23      1     97       C  
ATOM   5221  N   LYS B  82      11.850 -12.893   0.362  1.00 10.32           N  
ANISOU 5221  N   LYS B  82     1305   1203   1411     24     16    105       N  
ATOM   5222  CA  LYS B  82      12.442 -14.129  -0.133  1.00 11.74           C  
ANISOU 5222  CA  LYS B  82     1476   1381   1603     25     22    108       C  
ATOM   5223  C   LYS B  82      13.008 -14.898   1.053  1.00 11.59           C  
ANISOU 5223  C   LYS B  82     1454   1357   1592     18     10    113       C  
ATOM   5224  O   LYS B  82      14.029 -14.487   1.609  1.00 12.13           O  
ANISOU 5224  O   LYS B  82     1518   1416   1672     13      0    121       O  
ATOM   5225  CB  LYS B  82      13.544 -13.847  -1.175  1.00 11.16           C  
ANISOU 5225  CB  LYS B  82     1394   1299   1544     28     31    115       C  
ATOM   5226  CG  LYS B  82      13.051 -13.033  -2.373  1.00 12.18           C  
ANISOU 5226  CG  LYS B  82     1530   1432   1664     35     42    110       C  
ATOM   5227  CD  LYS B  82      14.209 -12.717  -3.341  1.00 15.98           C  
ANISOU 5227  CD  LYS B  82     2005   1903   2161     39     55    118       C  
ATOM   5228  CE  LYS B  82      13.791 -11.696  -4.392  1.00 19.11           C  
ANISOU 5228  CE  LYS B  82     2410   2302   2548     46     64    115       C  
ATOM   5229  NZ  LYS B  82      14.931 -11.366  -5.306  1.00 15.55           N  
ANISOU 5229  NZ  LYS B  82     1954   1839   2113     51     80    124       N  
ATOM   5230  N   PHE B  83      12.348 -15.995   1.418  1.00 10.80           N  
ANISOU 5230  N   PHE B  83     1355   1261   1485     18     11    110       N  
ATOM   5231  CA  PHE B  83      12.745 -16.862   2.530  1.00  9.91           C  
ANISOU 5231  CA  PHE B  83     1242   1145   1378     12      1    114       C  
ATOM   5232  C   PHE B  83      13.346 -18.147   1.987  1.00 10.38           C  
ANISOU 5232  C   PHE B  83     1291   1202   1452     13      7    118       C  
ATOM   5233  O   PHE B  83      12.604 -18.992   1.491  1.00  9.73           O  
ANISOU 5233  O   PHE B  83     1209   1125   1363     16     16    113       O  
ATOM   5234  CB  PHE B  83      11.532 -17.274   3.366  1.00  7.76           C  
ANISOU 5234  CB  PHE B  83      979    878   1089     12      0    109       C  
ATOM   5235  CG  PHE B  83      10.976 -16.195   4.269  1.00 11.56           C  
ANISOU 5235  CG  PHE B  83     1476   1359   1556     12     -4    107       C  
ATOM   5236  CD1 PHE B  83      11.704 -15.721   5.363  1.00 10.36           C  
ANISOU 5236  CD1 PHE B  83     1335   1198   1404      7    -19    112       C  
ATOM   5237  CD2 PHE B  83       9.667 -15.764   4.107  1.00  8.33           C  
ANISOU 5237  CD2 PHE B  83     1073    958   1135     17      5    102       C  
ATOM   5238  CE1 PHE B  83      11.148 -14.799   6.252  1.00 12.69           C  
ANISOU 5238  CE1 PHE B  83     1650   1490   1682      8    -23    110       C  
ATOM   5239  CE2 PHE B  83       9.099 -14.812   4.984  1.00 14.21           C  
ANISOU 5239  CE2 PHE B  83     1833   1699   1865     19      4    101       C  
ATOM   5240  CZ  PHE B  83       9.850 -14.334   6.064  1.00 11.03           C  
ANISOU 5240  CZ  PHE B  83     1445   1287   1458     14     -9    104       C  
ATOM   5241  N   ASN B  84      14.665 -18.323   2.109  1.00 10.59           N  
ANISOU 5241  N   ASN B  84     1306   1217   1498     10      3    128       N  
ATOM   5242  CA  ASN B  84      15.314 -19.428   1.390  1.00 10.78           C  
ANISOU 5242  CA  ASN B  84     1319   1237   1537     13     14    133       C  
ATOM   5243  C   ASN B  84      14.913 -20.822   1.830  1.00 11.01           C  
ANISOU 5243  C   ASN B  84     1349   1269   1563     11     13    131       C  
ATOM   5244  O   ASN B  84      14.953 -21.733   1.000  1.00 10.89           O  
ANISOU 5244  O   ASN B  84     1331   1253   1553     16     26    130       O  
ATOM   5245  CB  ASN B  84      16.852 -19.332   1.409  1.00  9.99           C  
ANISOU 5245  CB  ASN B  84     1205   1124   1467     11     11    147       C  
ATOM   5246  CG  ASN B  84      17.379 -18.311   0.398  1.00 15.63           C  
ANISOU 5246  CG  ASN B  84     1914   1833   2190     16     22    151       C  
ATOM   5247  OD1 ASN B  84      16.699 -17.327   0.111  1.00 12.72           O  
ANISOU 5247  OD1 ASN B  84     1555   1471   1806     18     24    144       O  
ATOM   5248  ND2 ASN B  84      18.573 -18.555  -0.161  1.00 15.21           N  
ANISOU 5248  ND2 ASN B  84     1847   1768   2165     19     33    164       N  
ATOM   5249  N   LEU B  85      14.549 -21.014   3.101  1.00 10.24           N  
ANISOU 5249  N   LEU B  85     1258   1173   1459      6      0    130       N  
ATOM   5250  CA  LEU B  85      14.194 -22.366   3.533  1.00 10.24           C  
ANISOU 5250  CA  LEU B  85     1257   1175   1457      4      0    129       C  
ATOM   5251  C   LEU B  85      12.963 -22.922   2.801  1.00 10.57           C  
ANISOU 5251  C   LEU B  85     1303   1226   1486      9     11    120       C  
ATOM   5252  O   LEU B  85      13.068 -23.969   2.157  1.00 10.27           O  
ANISOU 5252  O   LEU B  85     1260   1186   1453     11     19    119       O  
ATOM   5253  CB  LEU B  85      14.082 -22.495   5.066  1.00  9.88           C  
ANISOU 5253  CB  LEU B  85     1220   1127   1405     -1    -16    131       C  
ATOM   5254  CG  LEU B  85      13.707 -23.861   5.658  1.00 11.03           C  
ANISOU 5254  CG  LEU B  85     1367   1274   1549     -3    -16    132       C  
ATOM   5255  CD1 LEU B  85      14.658 -24.954   5.163  1.00 11.38           C  
ANISOU 5255  CD1 LEU B  85     1397   1313   1614     -3    -13    138       C  
ATOM   5256  CD2 LEU B  85      13.721 -23.792   7.187  1.00 11.55           C  
ANISOU 5256  CD2 LEU B  85     1445   1334   1606     -8    -32    135       C  
ATOM   5257  N   PRO B  86      11.797 -22.257   2.922  1.00 11.14           N  
ANISOU 5257  N   PRO B  86     1384   1305   1541     10     11    113       N  
ATOM   5258  CA  PRO B  86      10.655 -22.788   2.180  1.00 10.40           C  
ANISOU 5258  CA  PRO B  86     1291   1217   1440     14     19    106       C  
ATOM   5259  C   PRO B  86      10.825 -22.604   0.669  1.00 11.42           C  
ANISOU 5259  C   PRO B  86     1421   1345   1571     19     28    103       C  
ATOM   5260  O   PRO B  86      10.260 -23.390  -0.093  1.00  9.92           O  
ANISOU 5260  O   PRO B  86     1234   1156   1379     21     32     99       O  
ATOM   5261  CB  PRO B  86       9.473 -21.950   2.693  1.00 11.50           C  
ANISOU 5261  CB  PRO B  86     1437   1362   1566     14     18    103       C  
ATOM   5262  CG  PRO B  86      10.074 -20.681   3.173  1.00 11.63           C  
ANISOU 5262  CG  PRO B  86     1459   1377   1581     13     13    105       C  
ATOM   5263  CD  PRO B  86      11.426 -21.081   3.746  1.00  8.86           C  
ANISOU 5263  CD  PRO B  86     1105   1018   1242      9      5    112       C  
ATOM   5264  N   MET B  87      11.610 -21.627   0.216  1.00 10.27           N  
ANISOU 5264  N   MET B  87     1275   1197   1430     21     31    105       N  
ATOM   5265  CA  MET B  87      11.764 -21.478  -1.241  1.00 11.85           C  
ANISOU 5265  CA  MET B  87     1480   1394   1629     28     42    103       C  
ATOM   5266  C   MET B  87      12.512 -22.677  -1.838  1.00 11.19           C  
ANISOU 5266  C   MET B  87     1395   1302   1555     31     51    106       C  
ATOM   5267  O   MET B  87      12.109 -23.217  -2.866  1.00 11.39           O  
ANISOU 5267  O   MET B  87     1430   1325   1573     35     58    101       O  
ATOM   5268  CB  MET B  87      12.535 -20.208  -1.608  1.00  9.79           C  
ANISOU 5268  CB  MET B  87     1217   1129   1372     30     46    107       C  
ATOM   5269  CG  MET B  87      12.330 -19.729  -3.052  1.00 12.15           C  
ANISOU 5269  CG  MET B  87     1526   1427   1663     37     57    103       C  
ATOM   5270  SD  MET B  87      13.684 -18.734  -3.738  1.00 15.18           S  
ANISOU 5270  SD  MET B  87     1906   1801   2060     42     70    112       S  
ATOM   5271  CE  MET B  87      13.656 -17.316  -2.645  1.00 14.55           C  
ANISOU 5271  CE  MET B  87     1820   1725   1981     36     55    113       C  
ATOM   5272  N   ALA B  88      13.629 -23.045  -1.219  1.00 10.47           N  
ANISOU 5272  N   ALA B  88     1293   1205   1481     28     51    115       N  
ATOM   5273  CA  ALA B  88      14.404 -24.217  -1.619  1.00 11.59           C  
ANISOU 5273  CA  ALA B  88     1431   1337   1635     31     61    120       C  
ATOM   5274  C   ALA B  88      13.605 -25.509  -1.414  1.00 10.08           C  
ANISOU 5274  C   ALA B  88     1244   1149   1436     29     57    114       C  
ATOM   5275  O   ALA B  88      13.699 -26.433  -2.224  1.00 12.00           O  
ANISOU 5275  O   ALA B  88     1493   1386   1680     34     67    113       O  
ATOM   5276  CB  ALA B  88      15.715 -24.276  -0.816  1.00 10.81           C  
ANISOU 5276  CB  ALA B  88     1316   1231   1559     27     58    133       C  
ATOM   5277  N   TYR B  89      12.839 -25.600  -0.330  1.00 10.59           N  
ANISOU 5277  N   TYR B  89     1306   1222   1495     23     44    112       N  
ATOM   5278  CA  TYR B  89      12.008 -26.791  -0.103  1.00 10.28           C  
ANISOU 5278  CA  TYR B  89     1268   1184   1450     20     40    108       C  
ATOM   5279  C   TYR B  89      11.057 -26.954  -1.286  1.00 11.51           C  
ANISOU 5279  C   TYR B  89     1436   1341   1595     25     43     99       C  
ATOM   5280  O   TYR B  89      10.888 -28.055  -1.817  1.00 10.74           O  
ANISOU 5280  O   TYR B  89     1344   1238   1497     26     45     97       O  
ATOM   5281  CB  TYR B  89      11.194 -26.693   1.191  1.00  9.63           C  
ANISOU 5281  CB  TYR B  89     1184   1110   1362     15     29    107       C  
ATOM   5282  CG  TYR B  89       9.990 -27.607   1.186  1.00 10.09           C  
ANISOU 5282  CG  TYR B  89     1245   1172   1416     13     27    103       C  
ATOM   5283  CD1 TYR B  89      10.107 -28.931   1.607  1.00 12.62           C  
ANISOU 5283  CD1 TYR B  89     1561   1489   1743     11     25    105       C  
ATOM   5284  CD2 TYR B  89       8.739 -27.135   0.802  1.00  7.60           C  
ANISOU 5284  CD2 TYR B  89      933    860   1091     14     24     98       C  
ATOM   5285  CE1 TYR B  89       9.010 -29.784   1.595  1.00 12.43           C  
ANISOU 5285  CE1 TYR B  89     1538   1466   1718      9     22    102       C  
ATOM   5286  CE2 TYR B  89       7.626 -27.974   0.784  1.00  7.19           C  
ANISOU 5286  CE2 TYR B  89      880    809   1040     12     20     96       C  
ATOM   5287  CZ  TYR B  89       7.783 -29.294   1.197  1.00 13.63           C  
ANISOU 5287  CZ  TYR B  89     1692   1622   1863     10     20     98       C  
ATOM   5288  OH  TYR B  89       6.723 -30.167   1.180  1.00 11.33           O  
ANISOU 5288  OH  TYR B  89     1399   1329   1574      8     15     97       O  
ATOM   5289  N   SER B  90      10.444 -25.839  -1.681  1.00 10.28           N  
ANISOU 5289  N   SER B  90     1286   1189   1429     26     41     95       N  
ATOM   5290  CA  SER B  90       9.446 -25.840  -2.735  1.00 11.32           C  
ANISOU 5290  CA  SER B  90     1429   1320   1550     29     39     88       C  
ATOM   5291  C   SER B  90      10.092 -26.261  -4.046  1.00 11.56           C  
ANISOU 5291  C   SER B  90     1474   1340   1578     36     50     86       C  
ATOM   5292  O   SER B  90       9.515 -27.076  -4.762  1.00 10.54           O  
ANISOU 5292  O   SER B  90     1357   1204   1441     37     46     81       O  
ATOM   5293  CB  SER B  90       8.754 -24.478  -2.860  1.00 11.74           C  
ANISOU 5293  CB  SER B  90     1484   1380   1595     29     35     85       C  
ATOM   5294  OG  SER B  90       8.108 -24.136  -1.639  1.00 12.94           O  
ANISOU 5294  OG  SER B  90     1627   1540   1748     25     29     87       O  
ATOM   5295  N   ALA B  91      11.289 -25.731  -4.321  1.00 10.47           N  
ANISOU 5295  N   ALA B  91     1334   1196   1445     41     63     92       N  
ATOM   5296  CA  ALA B  91      12.064 -26.104  -5.493  1.00 10.75           C  
ANISOU 5296  CA  ALA B  91     1384   1219   1480     49     80     93       C  
ATOM   5297  C   ALA B  91      12.451 -27.586  -5.436  1.00 10.46           C  
ANISOU 5297  C   ALA B  91     1348   1175   1450     50     85     94       C  
ATOM   5298  O   ALA B  91      12.364 -28.283  -6.443  1.00 11.32           O  
ANISOU 5298  O   ALA B  91     1477   1272   1550     56     91     90       O  
ATOM   5299  CB  ALA B  91      13.315 -25.228  -5.595  1.00 11.04           C  
ANISOU 5299  CB  ALA B  91     1413   1251   1528     54     95    102       C  
ATOM   5300  N   ALA B  92      12.867 -28.079  -4.272  1.00 10.34           N  
ANISOU 5300  N   ALA B  92     1314   1163   1449     44     80    101       N  
ATOM   5301  CA  ALA B  92      13.187 -29.498  -4.150  1.00 11.49           C  
ANISOU 5301  CA  ALA B  92     1459   1302   1603     44     84    103       C  
ATOM   5302  C   ALA B  92      11.976 -30.382  -4.474  1.00 11.05           C  
ANISOU 5302  C   ALA B  92     1417   1247   1534     42     73     93       C  
ATOM   5303  O   ALA B  92      12.105 -31.437  -5.101  1.00 13.51           O  
ANISOU 5303  O   ALA B  92     1742   1548   1844     46     79     91       O  
ATOM   5304  CB  ALA B  92      13.776 -29.826  -2.772  1.00 10.92           C  
ANISOU 5304  CB  ALA B  92     1366   1234   1548     38     78    111       C  
ATOM   5305  N   MET B  93      10.805 -29.967  -4.017  1.00 10.07           N  
ANISOU 5305  N   MET B  93     1289   1132   1402     36     56     89       N  
ATOM   5306  CA  MET B  93       9.576 -30.737  -4.262  1.00 11.38           C  
ANISOU 5306  CA  MET B  93     1464   1298   1562     32     42     82       C  
ATOM   5307  C   MET B  93       9.165 -30.699  -5.735  1.00 11.66           C  
ANISOU 5307  C   MET B  93     1524   1322   1582     37     41     75       C  
ATOM   5308  O   MET B  93       8.717 -31.708  -6.300  1.00 11.26           O  
ANISOU 5308  O   MET B  93     1489   1262   1526     37     34     70       O  
ATOM   5309  CB  MET B  93       8.455 -30.203  -3.365  1.00  9.04           C  
ANISOU 5309  CB  MET B  93     1154   1014   1267     25     28     82       C  
ATOM   5310  CG  MET B  93       8.687 -30.488  -1.865  1.00 12.20           C  
ANISOU 5310  CG  MET B  93     1535   1421   1677     19     28     88       C  
ATOM   5311  SD  MET B  93       8.987 -32.237  -1.474  1.00 12.90           S  
ANISOU 5311  SD  MET B  93     1621   1503   1776     17     28     91       S  
ATOM   5312  CE  MET B  93       7.342 -32.961  -1.608  1.00 11.54           C  
ANISOU 5312  CE  MET B  93     1450   1330   1602     12     12     87       C  
ATOM   5313  N   LEU B  94       9.356 -29.553  -6.384  1.00 11.07           N  
ANISOU 5313  N   LEU B  94     1458   1248   1499     42     47     74       N  
ATOM   5314  CA  LEU B  94       9.089 -29.484  -7.831  1.00 11.10           C  
ANISOU 5314  CA  LEU B  94     1492   1239   1486     49     47     67       C  
ATOM   5315  C   LEU B  94      10.037 -30.397  -8.613  1.00 12.05           C  
ANISOU 5315  C   LEU B  94     1632   1342   1602     58     65     68       C  
ATOM   5316  O   LEU B  94       9.636 -31.035  -9.591  1.00 12.51           O  
ANISOU 5316  O   LEU B  94     1719   1386   1646     61     60     62       O  
ATOM   5317  CB  LEU B  94       9.147 -28.038  -8.337  1.00 10.21           C  
ANISOU 5317  CB  LEU B  94     1384   1129   1365     53     52     67       C  
ATOM   5318  CG  LEU B  94       8.097 -27.054  -7.789  1.00 14.63           C  
ANISOU 5318  CG  LEU B  94     1929   1702   1925     46     35     66       C  
ATOM   5319  CD1 LEU B  94       8.158 -25.813  -8.677  1.00 12.97           C  
ANISOU 5319  CD1 LEU B  94     1732   1490   1704     52     40     64       C  
ATOM   5320  CD2 LEU B  94       6.647 -27.598  -7.804  1.00 11.81           C  
ANISOU 5320  CD2 LEU B  94     1573   1344   1568     39     11     62       C  
ATOM   5321  N   GLY B  95      11.296 -30.444  -8.185  1.00 13.29           N  
ANISOU 5321  N   GLY B  95     1776   1499   1773     62     86     76       N  
ATOM   5322  CA  GLY B  95      12.271 -31.372  -8.745  1.00 12.09           C  
ANISOU 5322  CA  GLY B  95     1638   1331   1623     71    107     79       C  
ATOM   5323  C   GLY B  95      11.859 -32.812  -8.519  1.00 14.35           C  
ANISOU 5323  C   GLY B  95     1929   1613   1911     67     97     76       C  
ATOM   5324  O   GLY B  95      11.942 -33.632  -9.433  1.00 10.78           O  
ANISOU 5324  O   GLY B  95     1505   1144   1447     74    103     72       O  
ATOM   5325  N   TRP B  96      11.422 -33.131  -7.299  1.00 12.22           N  
ANISOU 5325  N   TRP B  96     1632   1355   1653     56     81     78       N  
ATOM   5326  CA  TRP B  96      10.955 -34.481  -7.018  1.00 13.32           C  
ANISOU 5326  CA  TRP B  96     1773   1491   1794     51     70     75       C  
ATOM   5327  C   TRP B  96       9.770 -34.883  -7.915  1.00 13.87           C  
ANISOU 5327  C   TRP B  96     1870   1552   1847     49     51     65       C  
ATOM   5328  O   TRP B  96       9.740 -36.007  -8.419  1.00 14.34           O  
ANISOU 5328  O   TRP B  96     1948   1597   1901     52     50     62       O  
ATOM   5329  CB  TRP B  96      10.663 -34.644  -5.524  1.00 13.15           C  
ANISOU 5329  CB  TRP B  96     1721   1486   1789     41     59     80       C  
ATOM   5330  CG  TRP B  96      10.508 -36.072  -5.043  1.00 16.22           C  
ANISOU 5330  CG  TRP B  96     2105   1870   2185     37     53     81       C  
ATOM   5331  CD1 TRP B  96      10.757 -37.224  -5.744  1.00 13.17           C  
ANISOU 5331  CD1 TRP B  96     1738   1468   1795     41     59     78       C  
ATOM   5332  CD2 TRP B  96      10.127 -36.477  -3.725  1.00 12.24           C  
ANISOU 5332  CD2 TRP B  96     1578   1377   1694     27     42     85       C  
ATOM   5333  NE1 TRP B  96      10.508 -38.321  -4.947  1.00 15.51           N  
ANISOU 5333  NE1 TRP B  96     2023   1767   2103     35     50     80       N  
ATOM   5334  CE2 TRP B  96      10.121 -37.889  -3.704  1.00 17.49           C  
ANISOU 5334  CE2 TRP B  96     2247   2033   2363     26     41     84       C  
ATOM   5335  CE3 TRP B  96       9.751 -35.778  -2.568  1.00 13.43           C  
ANISOU 5335  CE3 TRP B  96     1708   1543   1851     21     35     89       C  
ATOM   5336  CZ2 TRP B  96       9.797 -38.623  -2.550  1.00 12.01           C  
ANISOU 5336  CZ2 TRP B  96     1536   1346   1681     19     33     89       C  
ATOM   5337  CZ3 TRP B  96       9.417 -36.501  -1.428  1.00 13.07           C  
ANISOU 5337  CZ3 TRP B  96     1647   1502   1814     14     28     93       C  
ATOM   5338  CH2 TRP B  96       9.445 -37.914  -1.430  1.00 15.27           C  
ANISOU 5338  CH2 TRP B  96     1928   1772   2098     13     27     93       C  
ATOM   5339  N   ALA B  97       8.807 -33.990  -8.143  1.00 12.09           N  
ANISOU 5339  N   ALA B  97     1646   1333   1614     46     35     61       N  
ATOM   5340  CA  ALA B  97       7.707 -34.266  -9.075  1.00 11.80           C  
ANISOU 5340  CA  ALA B  97     1635   1285   1563     43     13     53       C  
ATOM   5341  C   ALA B  97       8.227 -34.673 -10.467  1.00 14.90           C  
ANISOU 5341  C   ALA B  97     2070   1655   1936     54     23     48       C  
ATOM   5342  O   ALA B  97       7.770 -35.661 -11.063  1.00 16.88           O  
ANISOU 5342  O   ALA B  97     2346   1890   2177     54     10     43       O  
ATOM   5343  CB  ALA B  97       6.804 -33.029  -9.190  1.00 10.11           C  
ANISOU 5343  CB  ALA B  97     1416   1079   1345     39     -1     52       C  
ATOM   5344  N   LEU B  98       9.191 -33.918 -10.983  1.00 14.74           N  
ANISOU 5344  N   LEU B  98     2060   1632   1908     65     48     50       N  
ATOM   5345  CA  LEU B  98       9.818 -34.217 -12.274  1.00 16.32           C  
ANISOU 5345  CA  LEU B  98     2302   1808   2088     79     66     47       C  
ATOM   5346  C   LEU B  98      10.601 -35.534 -12.249  1.00 17.64           C  
ANISOU 5346  C   LEU B  98     2477   1962   2260     84     84     50       C  
ATOM   5347  O   LEU B  98      10.473 -36.330 -13.178  1.00 16.81           O  
ANISOU 5347  O   LEU B  98     2412   1837   2138     90     83     44       O  
ATOM   5348  CB  LEU B  98      10.738 -33.068 -12.700  1.00 14.73           C  
ANISOU 5348  CB  LEU B  98     2104   1607   1884     90     94     52       C  
ATOM   5349  CG  LEU B  98      10.059 -31.804 -13.235  1.00 16.20           C  
ANISOU 5349  CG  LEU B  98     2299   1797   2056     89     81     48       C  
ATOM   5350  CD1 LEU B  98      11.113 -30.712 -13.375  1.00 15.48           C  
ANISOU 5350  CD1 LEU B  98     2201   1709   1970     98    110     56       C  
ATOM   5351  CD2 LEU B  98       9.375 -32.008 -14.584  1.00 14.78           C  
ANISOU 5351  CD2 LEU B  98     2170   1597   1848     93     66     39       C  
ATOM   5352  N   TYR B  99      11.366 -35.766 -11.181  1.00 17.24           N  
ANISOU 5352  N   TYR B  99     2391   1923   2233     82     98     59       N  
ATOM   5353  CA  TYR B  99      12.110 -37.007 -10.983  1.00 17.49           C  
ANISOU 5353  CA  TYR B  99     2423   1945   2275     87    114     63       C  
ATOM   5354  C   TYR B  99      11.198 -38.226 -11.037  1.00 18.74           C  
ANISOU 5354  C   TYR B  99     2596   2096   2426     80     90     55       C  
ATOM   5355  O   TYR B  99      11.531 -39.219 -11.675  1.00 18.33           O  
ANISOU 5355  O   TYR B  99     2573   2024   2365     87    100     53       O  
ATOM   5356  CB  TYR B  99      12.809 -37.001  -9.627  1.00 16.88           C  
ANISOU 5356  CB  TYR B  99     2302   1885   2227     81    122     74       C  
ATOM   5357  CG  TYR B  99      13.739 -38.166  -9.354  1.00 17.95           C  
ANISOU 5357  CG  TYR B  99     2431   2009   2376     86    140     80       C  
ATOM   5358  CD1 TYR B  99      14.984 -38.255  -9.979  1.00 20.11           C  
ANISOU 5358  CD1 TYR B  99     2717   2267   2655    102    175     88       C  
ATOM   5359  CD2 TYR B  99      13.413 -39.132  -8.404  1.00 17.17           C  
ANISOU 5359  CD2 TYR B  99     2314   1918   2291     77    125     81       C  
ATOM   5360  CE1 TYR B  99      15.852 -39.321  -9.702  1.00 20.98           C  
ANISOU 5360  CE1 TYR B  99     2820   2367   2782    107    194     97       C  
ATOM   5361  CE2 TYR B  99      14.272 -40.194  -8.115  1.00 15.97           C  
ANISOU 5361  CE2 TYR B  99     2156   1757   2153     81    142     88       C  
ATOM   5362  CZ  TYR B  99      15.485 -40.280  -8.767  1.00 18.96           C  
ANISOU 5362  CZ  TYR B  99     2547   2120   2537     96    175     96       C  
ATOM   5363  OH  TYR B  99      16.335 -41.310  -8.455  1.00 18.77           O  
ANISOU 5363  OH  TYR B  99     2514   2086   2531    100    192    104       O  
ATOM   5364  N   GLU B 100      10.068 -38.173 -10.344  1.00 16.78           N  
ANISOU 5364  N   GLU B 100     2327   1861   2184     65     59     52       N  
ATOM   5365  CA  GLU B 100       9.173 -39.327 -10.335  1.00 17.79           C  
ANISOU 5365  CA  GLU B 100     2466   1982   2312     57     34     47       C  
ATOM   5366  C   GLU B 100       8.316 -39.407 -11.596  1.00 18.94           C  
ANISOU 5366  C   GLU B 100     2653   2108   2432     58     13     37       C  
ATOM   5367  O   GLU B 100       8.176 -40.480 -12.188  1.00 17.96           O  
ANISOU 5367  O   GLU B 100     2560   1964   2298     60      5     32       O  
ATOM   5368  CB  GLU B 100       8.243 -39.293  -9.119  1.00 16.62           C  
ANISOU 5368  CB  GLU B 100     2278   1853   2181     42     11     50       C  
ATOM   5369  CG  GLU B 100       8.957 -39.306  -7.764  1.00 14.11           C  
ANISOU 5369  CG  GLU B 100     1922   1552   1885     40     26     59       C  
ATOM   5370  CD  GLU B 100       9.728 -40.582  -7.460  1.00 18.48           C  
ANISOU 5370  CD  GLU B 100     2475   2098   2449     43     39     63       C  
ATOM   5371  OE1 GLU B 100       9.388 -41.656  -8.010  1.00 17.45           O  
ANISOU 5371  OE1 GLU B 100     2367   1952   2311     43     31     58       O  
ATOM   5372  OE2 GLU B 100      10.686 -40.529  -6.652  1.00 16.06           O  
ANISOU 5372  OE2 GLU B 100     2144   1800   2157     45     57     71       O  
ATOM   5373  N   TYR B 101       7.757 -38.277 -12.024  1.00 18.43           N  
ANISOU 5373  N   TYR B 101     2595   2048   2359     57      1     35       N  
ATOM   5374  CA  TYR B 101       6.648 -38.326 -12.986  1.00 20.23           C  
ANISOU 5374  CA  TYR B 101     2855   2259   2569     53    -30     27       C  
ATOM   5375  C   TYR B 101       6.810 -37.502 -14.264  1.00 21.10           C  
ANISOU 5375  C   TYR B 101     3007   2356   2653     63    -25     22       C  
ATOM   5376  O   TYR B 101       5.890 -37.429 -15.077  1.00 21.07           O  
ANISOU 5376  O   TYR B 101     3033   2338   2634     59    -55     16       O  
ATOM   5377  CB  TYR B 101       5.293 -38.054 -12.311  1.00 17.53           C  
ANISOU 5377  CB  TYR B 101     2483   1932   2245     37    -65     29       C  
ATOM   5378  CG  TYR B 101       5.006 -38.957 -11.123  1.00 18.99           C  
ANISOU 5378  CG  TYR B 101     2633   2127   2455     27    -71     34       C  
ATOM   5379  CD1 TYR B 101       4.985 -40.342 -11.262  1.00 17.57           C  
ANISOU 5379  CD1 TYR B 101     2468   1931   2275     25    -78     32       C  
ATOM   5380  CD2 TYR B 101       4.759 -38.428  -9.853  1.00 19.22           C  
ANISOU 5380  CD2 TYR B 101     2615   2179   2506     20    -68     42       C  
ATOM   5381  CE1 TYR B 101       4.771 -41.177 -10.173  1.00 19.21           C  
ANISOU 5381  CE1 TYR B 101     2644   2147   2505     17    -82     37       C  
ATOM   5382  CE2 TYR B 101       4.511 -39.267  -8.752  1.00 13.12           C  
ANISOU 5382  CE2 TYR B 101     1814   1414   1754     12    -72     47       C  
ATOM   5383  CZ  TYR B 101       4.507 -40.634  -8.923  1.00 20.55           C  
ANISOU 5383  CZ  TYR B 101     2768   2341   2696     11    -79     45       C  
ATOM   5384  OH  TYR B 101       4.285 -41.468  -7.844  1.00 21.88           O  
ANISOU 5384  OH  TYR B 101     2909   2517   2886      3    -81     51       O  
ATOM   5385  N   GLY B 102       7.973 -36.886 -14.437  1.00 22.56           N  
ANISOU 5385  N   GLY B 102     3194   2543   2833     76     11     25       N  
ATOM   5386  CA  GLY B 102       8.235 -35.998 -15.567  1.00 24.69           C  
ANISOU 5386  CA  GLY B 102     3501   2801   3079     87     22     22       C  
ATOM   5387  C   GLY B 102       8.011 -36.638 -16.925  1.00 27.36           C  
ANISOU 5387  C   GLY B 102     3902   3107   3385     95     13     14       C  
ATOM   5388  O   GLY B 102       7.469 -35.995 -17.818  1.00 27.48           O  
ANISOU 5388  O   GLY B 102     3948   3111   3379     96     -2      9       O  
ATOM   5389  N   ASP B 103       8.403 -37.900 -17.089  1.00 28.81           N  
ANISOU 5389  N   ASP B 103     4107   3274   3565     99     22     12       N  
ATOM   5390  CA  ASP B 103       8.141 -38.606 -18.346  1.00 32.50           C  
ANISOU 5390  CA  ASP B 103     4640   3707   3999    106     10      3       C  
ATOM   5391  C   ASP B 103       6.664 -38.923 -18.533  1.00 32.93           C  
ANISOU 5391  C   ASP B 103     4706   3755   4051     90    -45     -3       C  
ATOM   5392  O   ASP B 103       6.213 -39.148 -19.654  1.00 34.54           O  
ANISOU 5392  O   ASP B 103     4965   3930   4225     93    -66    -11       O  
ATOM   5393  CB  ASP B 103       8.915 -39.918 -18.421  1.00 32.78           C  
ANISOU 5393  CB  ASP B 103     4695   3725   4032    115     34      3       C  
ATOM   5394  CG  ASP B 103      10.350 -39.713 -18.846  1.00 39.19           C  
ANISOU 5394  CG  ASP B 103     5524   4528   4837    136     89      9       C  
ATOM   5395  OD1 ASP B 103      10.762 -38.551 -19.034  1.00 40.16           O  
ANISOU 5395  OD1 ASP B 103     5639   4658   4958    143    109     14       O  
ATOM   5396  OD2 ASP B 103      11.070 -40.721 -18.991  1.00 47.08           O  
ANISOU 5396  OD2 ASP B 103     6542   5511   5835    147    114     11       O  
ATOM   5397  N   ASP B 104       5.915 -38.928 -17.436  1.00 31.03           N  
ANISOU 5397  N   ASP B 104     4412   3537   3840     73    -69      0       N  
ATOM   5398  CA  ASP B 104       4.573 -39.487 -17.460  1.00 30.72           C  
ANISOU 5398  CA  ASP B 104     4375   3489   3807     57   -119     -2       C  
ATOM   5399  C   ASP B 104       3.502 -38.456 -17.761  1.00 29.99           C  
ANISOU 5399  C   ASP B 104     4279   3400   3714     49   -153     -2       C  
ATOM   5400  O   ASP B 104       2.329 -38.807 -17.843  1.00 31.24           O  
ANISOU 5400  O   ASP B 104     4437   3549   3882     35   -198     -3       O  
ATOM   5401  CB  ASP B 104       4.259 -40.138 -16.118  1.00 29.59           C  
ANISOU 5401  CB  ASP B 104     4177   3366   3699     45   -126      3       C  
ATOM   5402  CG  ASP B 104       5.143 -41.327 -15.833  1.00 31.12           C  
ANISOU 5402  CG  ASP B 104     4376   3554   3895     51   -101      3       C  
ATOM   5403  OD1 ASP B 104       5.466 -42.058 -16.784  1.00 32.89           O  
ANISOU 5403  OD1 ASP B 104     4652   3750   4094     60    -98     -2       O  
ATOM   5404  OD2 ASP B 104       5.517 -41.526 -14.660  1.00 32.96           O  
ANISOU 5404  OD2 ASP B 104     4561   3808   4153     48    -84     10       O  
ATOM   5405  N   ILE B 105       3.893 -37.197 -17.893  1.00 29.44           N  
ANISOU 5405  N   ILE B 105     4203   3342   3638     56   -133      0       N  
ATOM   5406  CA  ILE B 105       2.909 -36.128 -17.991  1.00 30.97           C  
ANISOU 5406  CA  ILE B 105     4384   3545   3839     47   -162      0       C  
ATOM   5407  C   ILE B 105       2.886 -35.481 -19.377  1.00 33.48           C  
ANISOU 5407  C   ILE B 105     4758   3839   4121     56   -169     -5       C  
ATOM   5408  O   ILE B 105       2.559 -34.297 -19.491  1.00 32.00           O  
ANISOU 5408  O   ILE B 105     4561   3663   3935     55   -175     -3       O  
ATOM   5409  CB  ILE B 105       3.123 -35.050 -16.893  1.00 30.12           C  
ANISOU 5409  CB  ILE B 105     4217   3470   3754     45   -140      8       C  
ATOM   5410  CG1 ILE B 105       4.535 -34.451 -16.973  1.00 26.80           C  
ANISOU 5410  CG1 ILE B 105     3802   3057   3323     61    -91      9       C  
ATOM   5411  CG2 ILE B 105       2.830 -35.625 -15.496  1.00 27.55           C  
ANISOU 5411  CG2 ILE B 105     3838   3164   3463     34   -143     15       C  
ATOM   5412  CD1 ILE B 105       4.706 -33.193 -16.146  1.00 29.56           C  
ANISOU 5412  CD1 ILE B 105     4106   3435   3690     60    -76     16       C  
ATOM   5413  N   GLU B 106       3.215 -36.244 -20.421  1.00 35.97           N  
ANISOU 5413  N   GLU B 106     5136   4124   4406     65   -169    -12       N  
ATOM   5414  CA  GLU B 106       3.213 -35.699 -21.790  1.00 38.62           C  
ANISOU 5414  CA  GLU B 106     5534   4434   4703     75   -175    -18       C  
ATOM   5415  C   GLU B 106       1.853 -35.223 -22.288  1.00 37.97           C  
ANISOU 5415  C   GLU B 106     5463   4342   4620     62   -231    -19       C  
ATOM   5416  O   GLU B 106       1.766 -34.163 -22.905  1.00 39.92           O  
ANISOU 5416  O   GLU B 106     5727   4587   4851     67   -233    -20       O  
ATOM   5417  CB  GLU B 106       3.875 -36.628 -22.819  1.00 40.78           C  
ANISOU 5417  CB  GLU B 106     5878   4673   4940     90   -161    -26       C  
ATOM   5418  CG  GLU B 106       5.415 -36.660 -22.791  1.00 46.84           C  
ANISOU 5418  CG  GLU B 106     6651   5444   5699    110    -96    -23       C  
ATOM   5419  CD  GLU B 106       6.067 -35.443 -22.138  1.00 53.24           C  
ANISOU 5419  CD  GLU B 106     7412   6285   6529    114    -60    -15       C  
ATOM   5420  OE1 GLU B 106       6.049 -35.358 -20.888  1.00 57.31           O  
ANISOU 5420  OE1 GLU B 106     7862   6831   7080    104    -57     -8       O  
ATOM   5421  OE2 GLU B 106       6.624 -34.588 -22.862  1.00 53.56           O  
ANISOU 5421  OE2 GLU B 106     7480   6319   6549    128    -34    -14       O  
ATOM   5422  N   ALA B 107       0.796 -35.978 -22.004  1.00 38.64           N  
ANISOU 5422  N   ALA B 107     5535   4421   4725     45   -277    -18       N  
ATOM   5423  CA  ALA B 107      -0.562 -35.569 -22.370  1.00 38.19           C  
ANISOU 5423  CA  ALA B 107     5478   4353   4676     31   -334    -16       C  
ATOM   5424  C   ALA B 107      -0.940 -34.180 -21.855  1.00 37.02           C  
ANISOU 5424  C   ALA B 107     5282   4233   4550     27   -331     -9       C  
ATOM   5425  O   ALA B 107      -1.614 -33.423 -22.556  1.00 38.08           O  
ANISOU 5425  O   ALA B 107     5435   4355   4675     24   -361     -8       O  
ATOM   5426  CB  ALA B 107      -1.595 -36.601 -21.913  1.00 39.49           C  
ANISOU 5426  CB  ALA B 107     5622   4511   4871     13   -379    -13       C  
ATOM   5427  N   SER B 108      -0.501 -33.845 -20.642  1.00 34.20           N  
ANISOU 5427  N   SER B 108     4864   3910   4220     27   -296     -2       N  
ATOM   5428  CA  SER B 108      -0.839 -32.575 -20.015  1.00 29.63           C  
ANISOU 5428  CA  SER B 108     4237   3356   3662     24   -291      4       C  
ATOM   5429  C   SER B 108      -0.198 -31.369 -20.701  1.00 28.48           C  
ANISOU 5429  C   SER B 108     4116   3213   3490     37   -267      1       C  
ATOM   5430  O   SER B 108      -0.692 -30.248 -20.546  1.00 28.26           O  
ANISOU 5430  O   SER B 108     4065   3199   3474     33   -274      6       O  
ATOM   5431  CB  SER B 108      -0.451 -32.593 -18.534  1.00 29.87           C  
ANISOU 5431  CB  SER B 108     4205   3420   3724     21   -259     11       C  
ATOM   5432  OG  SER B 108       0.942 -32.394 -18.361  1.00 25.47           O  
ANISOU 5432  OG  SER B 108     3650   2874   3153     36   -209      8       O  
ATOM   5433  N   GLY B 109       0.907 -31.583 -21.412  1.00 25.78           N  
ANISOU 5433  N   GLY B 109     3821   2857   3115     53   -235     -5       N  
ATOM   5434  CA  GLY B 109       1.683 -30.482 -21.990  1.00 24.95           C  
ANISOU 5434  CA  GLY B 109     3737   2755   2988     67   -203     -6       C  
ATOM   5435  C   GLY B 109       2.425 -29.564 -21.018  1.00 24.61           C  
ANISOU 5435  C   GLY B 109     3641   2744   2964     71   -161      0       C  
ATOM   5436  O   GLY B 109       2.920 -28.507 -21.418  1.00 25.43           O  
ANISOU 5436  O   GLY B 109     3755   2852   3055     81   -139      1       O  
ATOM   5437  N   GLN B 110       2.544 -29.967 -19.754  1.00 22.57           N  
ANISOU 5437  N   GLN B 110     3330   2508   2736     64   -150      5       N  
ATOM   5438  CA  GLN B 110       3.039 -29.093 -18.680  1.00 21.49           C  
ANISOU 5438  CA  GLN B 110     3139   2402   2621     65   -121     12       C  
ATOM   5439  C   GLN B 110       4.500 -29.318 -18.280  1.00 20.98           C  
ANISOU 5439  C   GLN B 110     3067   2345   2557     76    -73     14       C  
ATOM   5440  O   GLN B 110       5.051 -28.567 -17.469  1.00 20.00           O  
ANISOU 5440  O   GLN B 110     2905   2243   2450     78    -49     19       O  
ATOM   5441  CB  GLN B 110       2.162 -29.254 -17.426  1.00 20.74           C  
ANISOU 5441  CB  GLN B 110     2990   2327   2562     50   -141     17       C  
ATOM   5442  CG  GLN B 110       0.702 -28.824 -17.621  1.00 19.25           C  
ANISOU 5442  CG  GLN B 110     2794   2134   2384     38   -185     20       C  
ATOM   5443  CD  GLN B 110       0.575 -27.504 -18.369  1.00 23.38           C  
ANISOU 5443  CD  GLN B 110     3335   2656   2892     43   -188     19       C  
ATOM   5444  OE1 GLN B 110       1.031 -26.462 -17.903  1.00 25.21           O  
ANISOU 5444  OE1 GLN B 110     3541   2907   3129     47   -163     22       O  
ATOM   5445  NE2 GLN B 110      -0.050 -27.543 -19.543  1.00 22.92           N  
ANISOU 5445  NE2 GLN B 110     3321   2573   2814     42   -221     15       N  
ATOM   5446  N   ARG B 111       5.130 -30.355 -18.823  1.00 19.67           N  
ANISOU 5446  N   ARG B 111     2938   2160   2376     85    -59     10       N  
ATOM   5447  CA  ARG B 111       6.480 -30.691 -18.406  1.00 19.35           C  
ANISOU 5447  CA  ARG B 111     2886   2124   2342     95    -15     14       C  
ATOM   5448  C   ARG B 111       7.435 -29.508 -18.572  1.00 19.28           C  
ANISOU 5448  C   ARG B 111     2873   2123   2330    107     21     20       C  
ATOM   5449  O   ARG B 111       8.220 -29.221 -17.666  1.00 16.71           O  
ANISOU 5449  O   ARG B 111     2506   1814   2026    108     46     27       O  
ATOM   5450  CB  ARG B 111       7.011 -31.950 -19.107  1.00 20.74           C  
ANISOU 5450  CB  ARG B 111     3107   2274   2498    105     -3     10       C  
ATOM   5451  CG  ARG B 111       8.420 -32.325 -18.668  1.00 21.52           C  
ANISOU 5451  CG  ARG B 111     3191   2376   2609    116     43     17       C  
ATOM   5452  CD  ARG B 111       9.029 -33.448 -19.502  1.00 27.20           C  
ANISOU 5452  CD  ARG B 111     3960   3065   3306    129     62     14       C  
ATOM   5453  NE  ARG B 111      10.275 -33.888 -18.883  1.00 34.32           N  
ANISOU 5453  NE  ARG B 111     4837   3974   4229    137    103     23       N  
ATOM   5454  CZ  ARG B 111      10.839 -35.078 -19.066  1.00 40.21           C  
ANISOU 5454  CZ  ARG B 111     5604   4702   4971    145    121     23       C  
ATOM   5455  NH1 ARG B 111      10.284 -35.974 -19.874  1.00 38.58           N  
ANISOU 5455  NH1 ARG B 111     5448   4470   4738    146    101     13       N  
ATOM   5456  NH2 ARG B 111      11.963 -35.373 -18.424  1.00 41.05           N  
ANISOU 5456  NH2 ARG B 111     5680   4814   5100    151    157     33       N  
ATOM   5457  N   LEU B 112       7.392 -28.826 -19.716  1.00 18.30           N  
ANISOU 5457  N   LEU B 112     2791   1983   2179    116     22     17       N  
ATOM   5458  CA  LEU B 112       8.330 -27.724 -19.927  1.00 18.64           C  
ANISOU 5458  CA  LEU B 112     2830   2030   2220    128     58     23       C  
ATOM   5459  C   LEU B 112       8.003 -26.550 -19.005  1.00 17.77           C  
ANISOU 5459  C   LEU B 112     2669   1949   2134    118     50     27       C  
ATOM   5460  O   LEU B 112       8.913 -25.881 -18.522  1.00 16.75           O  
ANISOU 5460  O   LEU B 112     2513   1832   2019    123     80     35       O  
ATOM   5461  CB  LEU B 112       8.375 -27.248 -21.384  1.00 20.63           C  
ANISOU 5461  CB  LEU B 112     3143   2258   2438    141     64     19       C  
ATOM   5462  CG  LEU B 112       9.232 -26.026 -21.749  1.00 24.11           C  
ANISOU 5462  CG  LEU B 112     3585   2700   2875    154    100     26       C  
ATOM   5463  CD1 LEU B 112      10.721 -26.201 -21.424  1.00 29.01           C  
ANISOU 5463  CD1 LEU B 112     4188   3321   3512    166    151     36       C  
ATOM   5464  CD2 LEU B 112       9.052 -25.707 -23.231  1.00 28.01           C  
ANISOU 5464  CD2 LEU B 112     4145   3167   3330    166     99     21       C  
ATOM   5465  N   HIS B 113       6.724 -26.281 -18.769  1.00 15.06           N  
ANISOU 5465  N   HIS B 113     2312   1613   1794    104     10     24       N  
ATOM   5466  CA  HIS B 113       6.386 -25.203 -17.845  1.00 16.78           C  
ANISOU 5466  CA  HIS B 113     2483   1856   2033     96      4     28       C  
ATOM   5467  C   HIS B 113       6.937 -25.531 -16.452  1.00 16.28           C  
ANISOU 5467  C   HIS B 113     2372   1813   1999     91     20     34       C  
ATOM   5468  O   HIS B 113       7.445 -24.650 -15.768  1.00 15.30           O  
ANISOU 5468  O   HIS B 113     2218   1706   1890     91     36     40       O  
ATOM   5469  CB  HIS B 113       4.873 -24.979 -17.763  1.00 18.18           C  
ANISOU 5469  CB  HIS B 113     2652   2037   2216     83    -39     25       C  
ATOM   5470  CG  HIS B 113       4.270 -24.436 -19.022  1.00 21.16           C  
ANISOU 5470  CG  HIS B 113     3072   2397   2569     86    -59     21       C  
ATOM   5471  ND1 HIS B 113       4.507 -23.154 -19.477  1.00 20.70           N  
ANISOU 5471  ND1 HIS B 113     3021   2341   2501     93    -47     23       N  
ATOM   5472  CD2 HIS B 113       3.411 -24.998 -19.908  1.00 23.84           C  
ANISOU 5472  CD2 HIS B 113     3451   2715   2892     83    -93     16       C  
ATOM   5473  CE1 HIS B 113       3.822 -22.951 -20.590  1.00 21.03           C  
ANISOU 5473  CE1 HIS B 113     3105   2365   2521     94    -72     18       C  
ATOM   5474  NE2 HIS B 113       3.160 -24.059 -20.880  1.00 20.18           N  
ANISOU 5474  NE2 HIS B 113     3018   2241   2408     88   -102     14       N  
ATOM   5475  N   LEU B 114       6.862 -26.798 -16.053  1.00 14.59           N  
ANISOU 5475  N   LEU B 114     2155   1596   1792     86     13     33       N  
ATOM   5476  CA  LEU B 114       7.374 -27.190 -14.747  1.00 15.63           C  
ANISOU 5476  CA  LEU B 114     2244   1744   1948     81     26     38       C  
ATOM   5477  C   LEU B 114       8.900 -27.045 -14.673  1.00 14.90           C  
ANISOU 5477  C   LEU B 114     2147   1651   1861     92     66     45       C  
ATOM   5478  O   LEU B 114       9.429 -26.490 -13.702  1.00 16.04           O  
ANISOU 5478  O   LEU B 114     2256   1812   2026     90     77     52       O  
ATOM   5479  CB  LEU B 114       6.888 -28.592 -14.362  1.00 14.85           C  
ANISOU 5479  CB  LEU B 114     2143   1641   1857     74      9     36       C  
ATOM   5480  CG  LEU B 114       7.310 -29.172 -13.002  1.00 15.43           C  
ANISOU 5480  CG  LEU B 114     2177   1730   1955     68     18     42       C  
ATOM   5481  CD1 LEU B 114       7.050 -28.173 -11.867  1.00 15.54           C  
ANISOU 5481  CD1 LEU B 114     2149   1766   1986     61     15     47       C  
ATOM   5482  CD2 LEU B 114       6.568 -30.481 -12.755  1.00 13.78           C  
ANISOU 5482  CD2 LEU B 114     1969   1515   1751     60     -3     39       C  
ATOM   5483  N   GLU B 115       9.606 -27.490 -15.709  1.00 14.65           N  
ANISOU 5483  N   GLU B 115     2154   1598   1813    106     87     44       N  
ATOM   5484  CA  GLU B 115      11.064 -27.379 -15.775  1.00 15.60           C  
ANISOU 5484  CA  GLU B 115     2271   1712   1941    118    128     53       C  
ATOM   5485  C   GLU B 115      11.593 -25.938 -15.706  1.00 16.70           C  
ANISOU 5485  C   GLU B 115     2393   1861   2088    122    144     60       C  
ATOM   5486  O   GLU B 115      12.542 -25.644 -14.955  1.00 15.53           O  
ANISOU 5486  O   GLU B 115     2212   1722   1964    122    163     70       O  
ATOM   5487  CB  GLU B 115      11.591 -28.073 -17.042  1.00 15.10           C  
ANISOU 5487  CB  GLU B 115     2259   1621   1856    133    149     52       C  
ATOM   5488  CG  GLU B 115      11.467 -29.596 -16.966  1.00 15.63           C  
ANISOU 5488  CG  GLU B 115     2338   1677   1920    132    143     48       C  
ATOM   5489  CD  GLU B 115      11.751 -30.302 -18.287  1.00 23.37           C  
ANISOU 5489  CD  GLU B 115     3379   2628   2873    147    159     44       C  
ATOM   5490  OE1 GLU B 115      11.697 -29.618 -19.329  1.00 21.51           O  
ANISOU 5490  OE1 GLU B 115     3180   2377   2613    156    165     41       O  
ATOM   5491  OE2 GLU B 115      12.010 -31.531 -18.280  1.00 23.29           O  
ANISOU 5491  OE2 GLU B 115     3381   2605   2863    149    165     43       O  
ATOM   5492  N   ARG B 116      11.010 -25.050 -16.509  1.00 15.93           N  
ANISOU 5492  N   ARG B 116     2319   1761   1972    124    134     56       N  
ATOM   5493  CA  ARG B 116      11.444 -23.651 -16.523  1.00 16.66           C  
ANISOU 5493  CA  ARG B 116     2399   1861   2070    127    148     62       C  
ATOM   5494  C   ARG B 116      11.178 -22.979 -15.177  1.00 16.01           C  
ANISOU 5494  C   ARG B 116     2267   1803   2011    114    133     64       C  
ATOM   5495  O   ARG B 116      12.043 -22.265 -14.668  1.00 14.14           O  
ANISOU 5495  O   ARG B 116     2004   1574   1792    116    151     73       O  
ATOM   5496  CB  ARG B 116      10.683 -22.883 -17.593  1.00 17.90           C  
ANISOU 5496  CB  ARG B 116     2590   2010   2200    131    135     55       C  
ATOM   5497  CG  ARG B 116      11.202 -23.187 -18.987  1.00 21.31           C  
ANISOU 5497  CG  ARG B 116     3074   2414   2606    147    158     55       C  
ATOM   5498  CD  ARG B 116      10.374 -22.503 -20.063  1.00 25.41           C  
ANISOU 5498  CD  ARG B 116     3633   2923   3096    150    140     47       C  
ATOM   5499  NE  ARG B 116      11.105 -22.612 -21.329  1.00 31.79           N  
ANISOU 5499  NE  ARG B 116     4493   3704   3879    169    172     49       N  
ATOM   5500  CZ  ARG B 116      10.719 -22.081 -22.484  1.00 36.79           C  
ANISOU 5500  CZ  ARG B 116     5173   4321   4483    176    167     45       C  
ATOM   5501  NH1 ARG B 116       9.588 -21.388 -22.572  1.00 35.51           N  
ANISOU 5501  NH1 ARG B 116     5011   4167   4313    166    129     39       N  
ATOM   5502  NH2 ARG B 116      11.467 -22.263 -23.564  1.00 38.95           N  
ANISOU 5502  NH2 ARG B 116     5495   4568   4734    195    200     48       N  
ATOM   5503  N   ASN B 117       9.993 -23.210 -14.612  1.00 14.54           N  
ANISOU 5503  N   ASN B 117     2069   1629   1825    102    100     58       N  
ATOM   5504  CA  ASN B 117       9.683 -22.643 -13.295  1.00 15.16           C  
ANISOU 5504  CA  ASN B 117     2106   1729   1924     90     88     61       C  
ATOM   5505  C   ASN B 117      10.656 -23.114 -12.220  1.00 14.31           C  
ANISOU 5505  C   ASN B 117     1969   1628   1840     88    103     68       C  
ATOM   5506  O   ASN B 117      11.056 -22.335 -11.370  1.00 16.15           O  
ANISOU 5506  O   ASN B 117     2174   1872   2087     85    106     74       O  
ATOM   5507  CB  ASN B 117       8.232 -22.909 -12.887  1.00 13.77           C  
ANISOU 5507  CB  ASN B 117     1923   1561   1747     79     55     55       C  
ATOM   5508  CG  ASN B 117       7.295 -21.878 -13.463  1.00 17.26           C  
ANISOU 5508  CG  ASN B 117     2374   2003   2177     78     38     51       C  
ATOM   5509  OD1 ASN B 117       6.581 -22.115 -14.447  1.00 19.72           O  
ANISOU 5509  OD1 ASN B 117     2716   2302   2472     79     22     46       O  
ATOM   5510  ND2 ASN B 117       7.353 -20.687 -12.892  1.00 13.66           N  
ANISOU 5510  ND2 ASN B 117     1897   1562   1731     76     42     55       N  
ATOM   5511  N   LEU B 118      11.015 -24.394 -12.246  1.00 16.66           N  
ANISOU 5511  N   LEU B 118     2274   1917   2140     90    109     69       N  
ATOM   5512  CA  LEU B 118      12.049 -24.926 -11.366  1.00 15.39           C  
ANISOU 5512  CA  LEU B 118     2087   1758   2000     89    124     77       C  
ATOM   5513  C   LEU B 118      13.391 -24.225 -11.567  1.00 15.72           C  
ANISOU 5513  C   LEU B 118     2123   1794   2055     98    153     88       C  
ATOM   5514  O   LEU B 118      13.995 -23.751 -10.602  1.00 13.40           O  
ANISOU 5514  O   LEU B 118     1798   1509   1783     94    154     97       O  
ATOM   5515  CB  LEU B 118      12.235 -26.431 -11.593  1.00 15.31           C  
ANISOU 5515  CB  LEU B 118     2092   1736   1989     92    129     76       C  
ATOM   5516  CG  LEU B 118      13.286 -27.117 -10.705  1.00 14.85           C  
ANISOU 5516  CG  LEU B 118     2008   1679   1956     92    143     86       C  
ATOM   5517  CD1 LEU B 118      13.108 -26.827  -9.205  1.00 13.00           C  
ANISOU 5517  CD1 LEU B 118     1736   1463   1739     79    126     89       C  
ATOM   5518  CD2 LEU B 118      13.285 -28.632 -10.944  1.00 11.48           C  
ANISOU 5518  CD2 LEU B 118     1596   1240   1525     94    145     83       C  
ATOM   5519  N   ALA B 119      13.855 -24.182 -12.813  1.00 13.32           N  
ANISOU 5519  N   ALA B 119     1848   1472   1738    112    175     90       N  
ATOM   5520  CA  ALA B 119      15.150 -23.581 -13.156  1.00 15.11           C  
ANISOU 5520  CA  ALA B 119     2070   1689   1980    122    207    102       C  
ATOM   5521  C   ALA B 119      15.263 -22.155 -12.607  1.00 15.37           C  
ANISOU 5521  C   ALA B 119     2078   1735   2024    117    201    107       C  
ATOM   5522  O   ALA B 119      16.320 -21.737 -12.114  1.00 15.13           O  
ANISOU 5522  O   ALA B 119     2023   1705   2021    118    215    120       O  
ATOM   5523  CB  ALA B 119      15.353 -23.597 -14.691  1.00 15.65           C  
ANISOU 5523  CB  ALA B 119     2183   1736   2026    139    231    101       C  
ATOM   5524  N   PHE B 120      14.164 -21.410 -12.664  1.00 15.31           N  
ANISOU 5524  N   PHE B 120     2077   1739   2000    111    178     97       N  
ATOM   5525  CA  PHE B 120      14.177 -20.025 -12.202  1.00 15.74           C  
ANISOU 5525  CA  PHE B 120     2112   1805   2063    106    172    100       C  
ATOM   5526  C   PHE B 120      14.545 -19.931 -10.716  1.00 15.55           C  
ANISOU 5526  C   PHE B 120     2050   1793   2064     95    162    107       C  
ATOM   5527  O   PHE B 120      15.340 -19.060 -10.336  1.00 14.79           O  
ANISOU 5527  O   PHE B 120     1936   1698   1986     95    169    116       O  
ATOM   5528  CB  PHE B 120      12.835 -19.348 -12.481  1.00 15.70           C  
ANISOU 5528  CB  PHE B 120     2119   1808   2036    102    149     89       C  
ATOM   5529  CG  PHE B 120      12.812 -17.865 -12.183  1.00 15.02           C  
ANISOU 5529  CG  PHE B 120     2019   1732   1955     99    146     92       C  
ATOM   5530  CD1 PHE B 120      13.222 -16.949 -13.137  1.00 17.80           C  
ANISOU 5530  CD1 PHE B 120     2386   2075   2300    109    163     95       C  
ATOM   5531  CD2 PHE B 120      12.324 -17.397 -10.971  1.00 14.70           C  
ANISOU 5531  CD2 PHE B 120     1952   1707   1923     88    126     91       C  
ATOM   5532  CE1 PHE B 120      13.186 -15.583 -12.867  1.00 19.10           C  
ANISOU 5532  CE1 PHE B 120     2538   2248   2470    106    159     98       C  
ATOM   5533  CE2 PHE B 120      12.272 -16.045 -10.694  1.00 14.43           C  
ANISOU 5533  CE2 PHE B 120     1909   1681   1892     86    122     92       C  
ATOM   5534  CZ  PHE B 120      12.684 -15.140 -11.646  1.00 11.92           C  
ANISOU 5534  CZ  PHE B 120     1604   1355   1570     94    137     96       C  
ATOM   5535  N   ALA B 121      13.969 -20.799  -9.880  1.00 15.00           N  
ANISOU 5535  N   ALA B 121     1971   1732   1994     87    143    102       N  
ATOM   5536  CA  ALA B 121      14.300 -20.780  -8.446  1.00 12.95           C  
ANISOU 5536  CA  ALA B 121     1682   1482   1756     77    132    107       C  
ATOM   5537  C   ALA B 121      15.716 -21.306  -8.193  1.00 13.64           C  
ANISOU 5537  C   ALA B 121     1754   1558   1868     80    149    121       C  
ATOM   5538  O   ALA B 121      16.450 -20.776  -7.355  1.00 13.46           O  
ANISOU 5538  O   ALA B 121     1709   1538   1867     75    146    130       O  
ATOM   5539  CB  ALA B 121      13.304 -21.614  -7.641  1.00 11.97           C  
ANISOU 5539  CB  ALA B 121     1554   1368   1625     68    111    100       C  
ATOM   5540  N   LEU B 122      16.092 -22.381  -8.877  1.00 11.59           N  
ANISOU 5540  N   LEU B 122     1508   1287   1609     88    166    122       N  
ATOM   5541  CA  LEU B 122      17.459 -22.904  -8.736  1.00 12.73           C  
ANISOU 5541  CA  LEU B 122     1637   1419   1781     92    186    137       C  
ATOM   5542  C   LEU B 122      18.529 -21.880  -9.102  1.00 13.09           C  
ANISOU 5542  C   LEU B 122     1673   1455   1846     99    206    151       C  
ATOM   5543  O   LEU B 122      19.550 -21.795  -8.421  1.00 12.67           O  
ANISOU 5543  O   LEU B 122     1592   1396   1823     96    208    165       O  
ATOM   5544  CB  LEU B 122      17.658 -24.218  -9.508  1.00 12.04           C  
ANISOU 5544  CB  LEU B 122     1570   1317   1688    102    205    136       C  
ATOM   5545  CG  LEU B 122      16.695 -25.342  -9.086  1.00 13.76           C  
ANISOU 5545  CG  LEU B 122     1793   1542   1891     95    185    125       C  
ATOM   5546  CD1 LEU B 122      16.896 -26.602  -9.922  1.00 14.62           C  
ANISOU 5546  CD1 LEU B 122     1926   1635   1992    104    203    124       C  
ATOM   5547  CD2 LEU B 122      16.766 -25.704  -7.603  1.00 10.92           C  
ANISOU 5547  CD2 LEU B 122     1405   1194   1549     82    165    128       C  
ATOM   5548  N   ASP B 123      18.306 -21.099 -10.159  1.00 12.88           N  
ANISOU 5548  N   ASP B 123     1667   1423   1803    107    218    148       N  
ATOM   5549  CA  ASP B 123      19.264 -20.043 -10.498  1.00 13.34           C  
ANISOU 5549  CA  ASP B 123     1715   1473   1881    113    237    162       C  
ATOM   5550  C   ASP B 123      19.455 -19.067  -9.336  1.00 14.27           C  
ANISOU 5550  C   ASP B 123     1802   1601   2017    100    214    167       C  
ATOM   5551  O   ASP B 123      20.580 -18.659  -9.034  1.00 13.69           O  
ANISOU 5551  O   ASP B 123     1705   1518   1976    100    222    183       O  
ATOM   5552  CB  ASP B 123      18.849 -19.291 -11.767  1.00 15.03           C  
ANISOU 5552  CB  ASP B 123     1958   1681   2070    124    251    156       C  
ATOM   5553  CG  ASP B 123      18.957 -20.164 -13.013  1.00 16.39           C  
ANISOU 5553  CG  ASP B 123     2164   1836   2225    139    279    154       C  
ATOM   5554  OD1 ASP B 123      19.594 -21.242 -12.972  1.00 16.04           O  
ANISOU 5554  OD1 ASP B 123     2117   1781   2194    144    294    161       O  
ATOM   5555  OD2 ASP B 123      18.357 -19.774 -14.030  1.00 21.44           O  
ANISOU 5555  OD2 ASP B 123     2836   2472   2836    146    284    146       O  
ATOM   5556  N   TYR B 124      18.351 -18.693  -8.695  1.00 12.99           N  
ANISOU 5556  N   TYR B 124     1642   1456   1835     90    186    153       N  
ATOM   5557  CA  TYR B 124      18.435 -17.848  -7.498  1.00 13.38           C  
ANISOU 5557  CA  TYR B 124     1670   1515   1898     78    163    156       C  
ATOM   5558  C   TYR B 124      19.264 -18.500  -6.381  1.00 12.48           C  
ANISOU 5558  C   TYR B 124     1532   1398   1813     70    153    167       C  
ATOM   5559  O   TYR B 124      20.111 -17.830  -5.774  1.00 13.76           O  
ANISOU 5559  O   TYR B 124     1673   1554   2000     65    146    180       O  
ATOM   5560  CB  TYR B 124      17.040 -17.416  -7.017  1.00 11.53           C  
ANISOU 5560  CB  TYR B 124     1444   1298   1637     70    138    140       C  
ATOM   5561  CG  TYR B 124      17.014 -16.813  -5.617  1.00 14.45           C  
ANISOU 5561  CG  TYR B 124     1798   1676   2015     58    114    142       C  
ATOM   5562  CD1 TYR B 124      17.185 -15.440  -5.404  1.00 13.49           C  
ANISOU 5562  CD1 TYR B 124     1672   1556   1898     55    107    145       C  
ATOM   5563  CD2 TYR B 124      16.871 -17.637  -4.510  1.00 12.65           C  
ANISOU 5563  CD2 TYR B 124     1562   1452   1790     50     98    141       C  
ATOM   5564  CE1 TYR B 124      17.167 -14.900  -4.117  1.00 15.72           C  
ANISOU 5564  CE1 TYR B 124     1944   1842   2185     45     84    146       C  
ATOM   5565  CE2 TYR B 124      16.859 -17.120  -3.238  1.00 12.71           C  
ANISOU 5565  CE2 TYR B 124     1560   1464   1802     40     76    142       C  
ATOM   5566  CZ  TYR B 124      17.006 -15.765  -3.045  1.00 12.26           C  
ANISOU 5566  CZ  TYR B 124     1502   1408   1748     38     68    144       C  
ATOM   5567  OH  TYR B 124      16.984 -15.315  -1.750  1.00 19.69           O  
ANISOU 5567  OH  TYR B 124     2440   2351   2690     28     46    145       O  
ATOM   5568  N   LEU B 125      19.022 -19.783  -6.104  1.00 11.53           N  
ANISOU 5568  N   LEU B 125     1413   1278   1688     69    150    163       N  
ATOM   5569  CA  LEU B 125      19.772 -20.474  -5.056  1.00 12.37           C  
ANISOU 5569  CA  LEU B 125     1499   1380   1820     62    140    174       C  
ATOM   5570  C   LEU B 125      21.272 -20.479  -5.359  1.00 13.24           C  
ANISOU 5570  C   LEU B 125     1590   1471   1968     68    159    194       C  
ATOM   5571  O   LEU B 125      22.077 -20.306  -4.452  1.00 12.92           O  
ANISOU 5571  O   LEU B 125     1526   1425   1956     60    145    207       O  
ATOM   5572  CB  LEU B 125      19.272 -21.907  -4.827  1.00 11.92           C  
ANISOU 5572  CB  LEU B 125     1448   1326   1752     61    137    166       C  
ATOM   5573  CG  LEU B 125      17.783 -22.080  -4.475  1.00 13.86           C  
ANISOU 5573  CG  LEU B 125     1709   1589   1966     55    118    148       C  
ATOM   5574  CD1 LEU B 125      17.486 -23.559  -4.205  1.00 11.90           C  
ANISOU 5574  CD1 LEU B 125     1464   1342   1715     54    116    145       C  
ATOM   5575  CD2 LEU B 125      17.444 -21.237  -3.260  1.00 10.34           C  
ANISOU 5575  CD2 LEU B 125     1255   1154   1519     44     93    147       C  
ATOM   5576  N   VAL B 126      21.642 -20.672  -6.624  1.00 12.74           N  
ANISOU 5576  N   VAL B 126     1538   1397   1906     82    192    199       N  
ATOM   5577  CA  VAL B 126      23.051 -20.591  -7.045  1.00 13.57           C  
ANISOU 5577  CA  VAL B 126     1624   1480   2049     90    217    221       C  
ATOM   5578  C   VAL B 126      23.598 -19.182  -6.834  1.00 14.99           C  
ANISOU 5578  C   VAL B 126     1787   1658   2251     86    210    232       C  
ATOM   5579  O   VAL B 126      24.709 -19.014  -6.309  1.00 14.69           O  
ANISOU 5579  O   VAL B 126     1719   1606   2253     82    207    252       O  
ATOM   5580  CB  VAL B 126      23.242 -21.033  -8.520  1.00 14.28           C  
ANISOU 5580  CB  VAL B 126     1736   1557   2131    108    259    223       C  
ATOM   5581  CG1 VAL B 126      24.641 -20.667  -9.047  1.00 13.57           C  
ANISOU 5581  CG1 VAL B 126     1627   1444   2082    119    290    248       C  
ATOM   5582  CG2 VAL B 126      22.987 -22.528  -8.658  1.00 12.88           C  
ANISOU 5582  CG2 VAL B 126     1573   1378   1943    112    266    216       C  
ATOM   5583  N   ALA B 127      22.798 -18.180  -7.199  1.00 13.53           N  
ANISOU 5583  N   ALA B 127     1618   1483   2038     86    205    220       N  
ATOM   5584  CA  ALA B 127      23.209 -16.775  -7.062  1.00 14.48           C  
ANISOU 5584  CA  ALA B 127     1726   1601   2175     82    198    228       C  
ATOM   5585  C   ALA B 127      23.398 -16.315  -5.606  1.00 14.21           C  
ANISOU 5585  C   ALA B 127     1671   1570   2156     65    160    232       C  
ATOM   5586  O   ALA B 127      24.016 -15.280  -5.359  1.00 13.00           O  
ANISOU 5586  O   ALA B 127     1502   1410   2025     61    152    243       O  
ATOM   5587  CB  ALA B 127      22.250 -15.837  -7.812  1.00 12.92           C  
ANISOU 5587  CB  ALA B 127     1552   1413   1941     86    202    213       C  
ATOM   5588  N   CYS B 128      22.909 -17.099  -4.650  1.00 13.17           N  
ANISOU 5588  N   CYS B 128     1541   1449   2013     56    137    223       N  
ATOM   5589  CA  CYS B 128      23.015 -16.747  -3.235  1.00 13.18           C  
ANISOU 5589  CA  CYS B 128     1531   1453   2024     41    100    225       C  
ATOM   5590  C   CYS B 128      24.358 -17.132  -2.631  1.00 13.56           C  
ANISOU 5590  C   CYS B 128     1551   1482   2118     36     92    247       C  
ATOM   5591  O   CYS B 128      24.633 -16.779  -1.489  1.00 13.09           O  
ANISOU 5591  O   CYS B 128     1482   1419   2070     23     60    252       O  
ATOM   5592  CB  CYS B 128      21.926 -17.443  -2.418  1.00 13.11           C  
ANISOU 5592  CB  CYS B 128     1537   1460   1984     34     81    208       C  
ATOM   5593  SG  CYS B 128      20.297 -16.675  -2.579  1.00 15.62           S  
ANISOU 5593  SG  CYS B 128     1882   1798   2254     35     75    185       S  
ATOM   5594  N   ASP B 129      25.166 -17.866  -3.390  1.00 12.80           N  
ANISOU 5594  N   ASP B 129     1442   1372   2047     46    122    261       N  
ATOM   5595  CA  ASP B 129      26.466 -18.338  -2.916  1.00 15.81           C  
ANISOU 5595  CA  ASP B 129     1793   1734   2478     42    118    285       C  
ATOM   5596  C   ASP B 129      27.352 -17.185  -2.463  1.00 14.94           C  
ANISOU 5596  C   ASP B 129     1661   1610   2405     34     98    303       C  
ATOM   5597  O   ASP B 129      27.523 -16.226  -3.199  1.00 14.66           O  
ANISOU 5597  O   ASP B 129     1625   1570   2375     40    114    308       O  
ATOM   5598  CB  ASP B 129      27.187 -19.114  -4.021  1.00 14.54           C  
ANISOU 5598  CB  ASP B 129     1625   1558   2340     58    161    299       C  
ATOM   5599  CG  ASP B 129      28.517 -19.682  -3.562  1.00 20.91           C  
ANISOU 5599  CG  ASP B 129     2398   2343   3202     56    159    326       C  
ATOM   5600  OD1 ASP B 129      28.673 -20.006  -2.364  1.00 17.71           O  
ANISOU 5600  OD1 ASP B 129     1981   1938   2808     42    124    328       O  
ATOM   5601  OD2 ASP B 129      29.411 -19.816  -4.420  1.00 21.92           O  
ANISOU 5601  OD2 ASP B 129     2511   2452   3363     68    195    345       O  
ATOM   5602  N   ARG B 130      27.900 -17.275  -1.256  1.00 15.70           N  
ANISOU 5602  N   ARG B 130     1741   1698   2526     20     62    313       N  
ATOM   5603  CA  ARG B 130      28.933 -16.336  -0.824  1.00 17.82           C  
ANISOU 5603  CA  ARG B 130     1985   1947   2838     11     40    335       C  
ATOM   5604  C   ARG B 130      30.180 -17.080  -0.321  1.00 18.46           C  
ANISOU 5604  C   ARG B 130     2034   2006   2974      6     30    361       C  
ATOM   5605  O   ARG B 130      31.027 -16.490   0.347  1.00 21.18           O  
ANISOU 5605  O   ARG B 130     2357   2332   3357     -5      0    380       O  
ATOM   5606  CB  ARG B 130      28.376 -15.367   0.232  1.00 17.75           C  
ANISOU 5606  CB  ARG B 130     1992   1946   2806     -3     -3    323       C  
ATOM   5607  CG  ARG B 130      27.270 -14.422  -0.265  1.00 18.04           C  
ANISOU 5607  CG  ARG B 130     2055   2000   2796      1      5    301       C  
ATOM   5608  CD  ARG B 130      27.783 -13.446  -1.322  1.00 23.18           C  
ANISOU 5608  CD  ARG B 130     2694   2642   3469      9     31    313       C  
ATOM   5609  NE  ARG B 130      26.821 -12.471  -1.845  1.00 19.44           N  
ANISOU 5609  NE  ARG B 130     2244   2184   2957     13     39    295       N  
ATOM   5610  CZ  ARG B 130      25.963 -12.695  -2.840  1.00 26.26           C  
ANISOU 5610  CZ  ARG B 130     3128   3062   3786     26     70    279       C  
ATOM   5611  NH1 ARG B 130      25.851 -13.900  -3.403  1.00 18.97           N  
ANISOU 5611  NH1 ARG B 130     2208   2141   2856     36     96    277       N  
ATOM   5612  NH2 ARG B 130      25.181 -11.702  -3.257  1.00 26.38           N  
ANISOU 5612  NH2 ARG B 130     3162   3090   3772     29     73    266       N  
ATOM   5613  N   GLY B 131      30.285 -18.377  -0.604  1.00 18.41           N  
ANISOU 5613  N   GLY B 131     2024   1999   2971     14     53    363       N  
ATOM   5614  CA  GLY B 131      31.501 -19.145  -0.294  1.00 18.98           C  
ANISOU 5614  CA  GLY B 131     2062   2047   3099     12     50    391       C  
ATOM   5615  C   GLY B 131      31.491 -19.826   1.064  1.00 18.10           C  
ANISOU 5615  C   GLY B 131     1951   1937   2988     -2      7    389       C  
ATOM   5616  O   GLY B 131      31.228 -21.024   1.160  1.00 19.68           O  
ANISOU 5616  O   GLY B 131     2158   2144   3176      1     15    383       O  
ATOM   5617  N   ASP B 132      31.771 -19.057   2.113  1.00 19.63           N  
ANISOU 5617  N   ASP B 132     2141   2123   3194    -19    -40    395       N  
ATOM   5618  CA  ASP B 132      31.743 -19.547   3.495  1.00 21.01           C  
ANISOU 5618  CA  ASP B 132     2322   2295   3364    -34    -87    393       C  
ATOM   5619  C   ASP B 132      30.357 -19.354   4.116  1.00 19.77           C  
ANISOU 5619  C   ASP B 132     2207   2163   3140    -38   -105    362       C  
ATOM   5620  O   ASP B 132      30.169 -19.575   5.314  1.00 19.26           O  
ANISOU 5620  O   ASP B 132     2156   2098   3062    -51   -144    357       O  
ATOM   5621  CB  ASP B 132      32.783 -18.806   4.351  1.00 21.66           C  
ANISOU 5621  CB  ASP B 132     2383   2352   3494    -50   -134    417       C  
ATOM   5622  CG  ASP B 132      32.550 -17.300   4.420  1.00 26.95           C  
ANISOU 5622  CG  ASP B 132     3065   3022   4151    -56   -152    411       C  
ATOM   5623  OD1 ASP B 132      31.533 -16.765   3.925  1.00 30.69           O  
ANISOU 5623  OD1 ASP B 132     3565   3518   4577    -49   -132    388       O  
ATOM   5624  OD2 ASP B 132      33.420 -16.613   4.991  1.00 33.46           O  
ANISOU 5624  OD2 ASP B 132     3872   3823   5015    -69   -190    431       O  
ATOM   5625  N   SER B 133      29.412 -18.923   3.282  1.00 18.96           N  
ANISOU 5625  N   SER B 133     2124   2080   2998    -28    -75    342       N  
ATOM   5626  CA  SER B 133      28.072 -18.539   3.695  1.00 18.65           C  
ANISOU 5626  CA  SER B 133     2121   2063   2900    -31    -86    315       C  
ATOM   5627  C   SER B 133      27.207 -18.319   2.454  1.00 17.67           C  
ANISOU 5627  C   SER B 133     2011   1957   2745    -16    -45    298       C  
ATOM   5628  O   SER B 133      27.707 -18.417   1.330  1.00 17.62           O  
ANISOU 5628  O   SER B 133     1988   1943   2760     -5    -10    308       O  
ATOM   5629  CB  SER B 133      28.133 -17.275   4.556  1.00 19.01           C  
ANISOU 5629  CB  SER B 133     2176   2101   2943    -44   -126    315       C  
ATOM   5630  OG  SER B 133      28.837 -16.263   3.867  1.00 20.87           O  
ANISOU 5630  OG  SER B 133     2394   2325   3211    -42   -118    329       O  
ATOM   5631  N   VAL B 134      25.910 -18.094   2.649  1.00 15.22           N  
ANISOU 5631  N   VAL B 134     1730   1667   2385    -16    -48    274       N  
ATOM   5632  CA  VAL B 134      24.987 -17.776   1.555  1.00 15.48           C  
ANISOU 5632  CA  VAL B 134     1779   1716   2386     -5    -16    258       C  
ATOM   5633  C   VAL B 134      24.090 -16.620   1.988  1.00 15.95           C  
ANISOU 5633  C   VAL B 134     1860   1786   2411     -9    -34    243       C  
ATOM   5634  O   VAL B 134      23.883 -16.413   3.191  1.00 16.02           O  
ANISOU 5634  O   VAL B 134     1881   1795   2409    -20    -67    239       O  
ATOM   5635  CB  VAL B 134      24.054 -18.966   1.178  1.00 15.36           C  
ANISOU 5635  CB  VAL B 134     1778   1717   2341      2      3    242       C  
ATOM   5636  CG1 VAL B 134      24.853 -20.210   0.786  1.00 15.22           C  
ANISOU 5636  CG1 VAL B 134     1742   1688   2351      8     22    255       C  
ATOM   5637  CG2 VAL B 134      23.120 -19.318   2.350  1.00 11.49           C  
ANISOU 5637  CG2 VAL B 134     1308   1239   1819     -5    -21    227       C  
ATOM   5638  N   VAL B 135      23.552 -15.887   1.018  1.00 13.68           N  
ANISOU 5638  N   VAL B 135     1581   1508   2107     -1    -12    234       N  
ATOM   5639  CA  VAL B 135      22.442 -14.970   1.295  1.00 15.03           C  
ANISOU 5639  CA  VAL B 135     1775   1693   2241     -3    -22    216       C  
ATOM   5640  C   VAL B 135      21.239 -15.878   1.522  1.00 15.54           C  
ANISOU 5640  C   VAL B 135     1859   1775   2270     -1    -18    199       C  
ATOM   5641  O   VAL B 135      20.912 -16.677   0.632  1.00 14.59           O  
ANISOU 5641  O   VAL B 135     1738   1660   2143      7      6    194       O  
ATOM   5642  CB  VAL B 135      22.153 -14.042   0.103  1.00 14.32           C  
ANISOU 5642  CB  VAL B 135     1689   1607   2143      5      0    212       C  
ATOM   5643  CG1 VAL B 135      20.861 -13.241   0.344  1.00 13.93           C  
ANISOU 5643  CG1 VAL B 135     1664   1574   2054      4     -6    194       C  
ATOM   5644  CG2 VAL B 135      23.357 -13.121  -0.113  1.00 12.07           C  
ANISOU 5644  CG2 VAL B 135     1384   1305   1896      3     -2    231       C  
ATOM   5645  N   TYR B 136      20.631 -15.807   2.710  1.00 12.58           N  
ANISOU 5645  N   TYR B 136     1500   1404   1874     -8    -42    191       N  
ATOM   5646  CA  TYR B 136      19.522 -16.731   2.999  1.00 13.54           C  
ANISOU 5646  CA  TYR B 136     1636   1539   1967     -6    -37    177       C  
ATOM   5647  C   TYR B 136      18.160 -16.056   3.119  1.00 13.38           C  
ANISOU 5647  C   TYR B 136     1637   1533   1911     -4    -36    161       C  
ATOM   5648  O   TYR B 136      17.138 -16.723   3.316  1.00 13.75           O  
ANISOU 5648  O   TYR B 136     1695   1591   1936     -2    -30    151       O  
ATOM   5649  CB  TYR B 136      19.818 -17.600   4.229  1.00 13.26           C  
ANISOU 5649  CB  TYR B 136     1602   1498   1936    -14    -59    182       C  
ATOM   5650  CG  TYR B 136      19.769 -16.857   5.549  1.00 14.07           C  
ANISOU 5650  CG  TYR B 136     1722   1595   2029    -24    -89    182       C  
ATOM   5651  CD1 TYR B 136      20.897 -16.195   6.043  1.00 13.21           C  
ANISOU 5651  CD1 TYR B 136     1606   1467   1945    -32   -114    196       C  
ATOM   5652  CD2 TYR B 136      18.604 -16.858   6.320  1.00 14.15           C  
ANISOU 5652  CD2 TYR B 136     1757   1614   2004    -23    -93    169       C  
ATOM   5653  CE1 TYR B 136      20.851 -15.516   7.259  1.00 14.35           C  
ANISOU 5653  CE1 TYR B 136     1772   1603   2076    -40   -145    195       C  
ATOM   5654  CE2 TYR B 136      18.546 -16.179   7.537  1.00 13.16           C  
ANISOU 5654  CE2 TYR B 136     1654   1481   1865    -30   -119    168       C  
ATOM   5655  CZ  TYR B 136      19.678 -15.518   7.994  1.00 16.19           C  
ANISOU 5655  CZ  TYR B 136     2034   1845   2270    -39   -146    180       C  
ATOM   5656  OH  TYR B 136      19.626 -14.860   9.196  1.00 16.75           O  
ANISOU 5656  OH  TYR B 136     2132   1905   2325    -46   -174    179       O  
ATOM   5657  N   GLN B 137      18.149 -14.731   3.011  1.00 11.79           N  
ANISOU 5657  N   GLN B 137     1442   1331   1707     -4    -40    160       N  
ATOM   5658  CA  GLN B 137      16.901 -13.976   3.108  1.00 12.00           C  
ANISOU 5658  CA  GLN B 137     1486   1368   1702     -2    -38    147       C  
ATOM   5659  C   GLN B 137      17.075 -12.625   2.433  1.00 11.59           C  
ANISOU 5659  C   GLN B 137     1434   1315   1654      0    -34    148       C  
ATOM   5660  O   GLN B 137      18.129 -12.013   2.582  1.00 11.30           O  
ANISOU 5660  O   GLN B 137     1388   1265   1639     -4    -46    159       O  
ATOM   5661  CB  GLN B 137      16.472 -13.765   4.568  1.00 11.52           C  
ANISOU 5661  CB  GLN B 137     1446   1305   1624     -8    -59    144       C  
ATOM   5662  CG  GLN B 137      15.033 -13.222   4.694  1.00 10.91           C  
ANISOU 5662  CG  GLN B 137     1388   1240   1516     -3    -50    131       C  
ATOM   5663  CD  GLN B 137      14.478 -13.351   6.101  1.00 13.06           C  
ANISOU 5663  CD  GLN B 137     1683   1510   1770     -6    -62    127       C  
ATOM   5664  OE1 GLN B 137      14.530 -14.431   6.665  1.00 10.88           O  
ANISOU 5664  OE1 GLN B 137     1406   1232   1493     -8    -66    129       O  
ATOM   5665  NE2 GLN B 137      13.936 -12.265   6.669  1.00  8.62           N  
ANISOU 5665  NE2 GLN B 137     1141    944   1188     -5    -67    123       N  
ATOM   5666  N   ILE B 138      16.070 -12.177   1.687  1.00 12.87           N  
ANISOU 5666  N   ILE B 138     1604   1488   1797      7    -18    138       N  
ATOM   5667  CA  ILE B 138      15.984 -10.766   1.292  1.00 13.30           C  
ANISOU 5667  CA  ILE B 138     1662   1542   1847      9    -17    136       C  
ATOM   5668  C   ILE B 138      14.652 -10.211   1.787  1.00 13.75           C  
ANISOU 5668  C   ILE B 138     1738   1609   1875     10    -19    125       C  
ATOM   5669  O   ILE B 138      13.593 -10.753   1.451  1.00 13.73           O  
ANISOU 5669  O   ILE B 138     1740   1618   1858     16     -7    116       O  
ATOM   5670  CB  ILE B 138      15.957 -10.560  -0.239  1.00 14.10           C  
ANISOU 5670  CB  ILE B 138     1757   1648   1952     17      5    136       C  
ATOM   5671  CG1 ILE B 138      16.969 -11.431  -0.990  1.00 18.64           C  
ANISOU 5671  CG1 ILE B 138     2315   2215   2551     20     18    146       C  
ATOM   5672  CG2 ILE B 138      16.105  -9.060  -0.580  1.00 16.10           C  
ANISOU 5672  CG2 ILE B 138     2012   1898   2207     18      4    137       C  
ATOM   5673  CD1 ILE B 138      18.379 -11.011  -0.833  1.00 15.10           C  
ANISOU 5673  CD1 ILE B 138     1851   1751   2135     16     11    162       C  
ATOM   5674  N   GLY B 139      14.697  -9.119   2.546  1.00 13.41           N  
ANISOU 5674  N   GLY B 139     1708   1560   1827      7    -33    125       N  
ATOM   5675  CA  GLY B 139      13.495  -8.522   3.105  1.00 12.73           C  
ANISOU 5675  CA  GLY B 139     1642   1480   1715      9    -32    115       C  
ATOM   5676  C   GLY B 139      13.486  -8.702   4.613  1.00 14.29           C  
ANISOU 5676  C   GLY B 139     1858   1669   1903      4    -50    116       C  
ATOM   5677  O   GLY B 139      13.956  -9.716   5.120  1.00 15.45           O  
ANISOU 5677  O   GLY B 139     2000   1812   2056      0    -58    120       O  
ATOM   5678  N   ASP B 140      13.016  -7.677   5.322  1.00 15.15           N  
ANISOU 5678  N   ASP B 140     1988   1774   1994      5    -56    112       N  
ATOM   5679  CA  ASP B 140      12.692  -7.746   6.742  1.00 15.49           C  
ANISOU 5679  CA  ASP B 140     2057   1808   2018      3    -67    110       C  
ATOM   5680  C   ASP B 140      11.226  -8.161   6.860  1.00 15.22           C  
ANISOU 5680  C   ASP B 140     2030   1785   1964     11    -46    103       C  
ATOM   5681  O   ASP B 140      10.345  -7.458   6.384  1.00 14.39           O  
ANISOU 5681  O   ASP B 140     1927   1687   1852     18    -31     98       O  
ATOM   5682  CB  ASP B 140      12.905  -6.364   7.372  1.00 17.27           C  
ANISOU 5682  CB  ASP B 140     2306   2020   2234      0    -82    110       C  
ATOM   5683  CG  ASP B 140      12.395  -6.287   8.811  1.00 19.98           C  
ANISOU 5683  CG  ASP B 140     2686   2353   2551      1    -90    107       C  
ATOM   5684  OD1 ASP B 140      12.554  -7.246   9.602  1.00 22.01           O  
ANISOU 5684  OD1 ASP B 140     2951   2606   2805     -1    -98    109       O  
ATOM   5685  OD2 ASP B 140      11.832  -5.236   9.165  1.00 27.90           O  
ANISOU 5685  OD2 ASP B 140     3711   3352   3536      6    -87    102       O  
ATOM   5686  N   GLY B 141      10.952  -9.292   7.500  1.00 16.27           N  
ANISOU 5686  N   GLY B 141     2167   1919   2093     11    -44    104       N  
ATOM   5687  CA  GLY B 141       9.590  -9.781   7.611  1.00 16.33           C  
ANISOU 5687  CA  GLY B 141     2178   1936   2089     19    -23     99       C  
ATOM   5688  C   GLY B 141       8.608  -8.798   8.230  1.00 17.30           C  
ANISOU 5688  C   GLY B 141     2325   2055   2191     26    -13     96       C  
ATOM   5689  O   GLY B 141       7.517  -8.615   7.694  1.00 15.44           O  
ANISOU 5689  O   GLY B 141     2082   1828   1954     34      6     94       O  
ATOM   5690  N   ALA B 142       8.976  -8.173   9.347  1.00 16.49           N  
ANISOU 5690  N   ALA B 142     2253   1937   2074     24    -26     97       N  
ATOM   5691  CA  ALA B 142       8.085  -7.208   9.999  1.00 16.59           C  
ANISOU 5691  CA  ALA B 142     2294   1944   2066     33    -14     94       C  
ATOM   5692  C   ALA B 142       7.732  -6.041   9.066  1.00 17.17           C  
ANISOU 5692  C   ALA B 142     2357   2023   2143     37     -5     91       C  
ATOM   5693  O   ALA B 142       6.548  -5.761   8.870  1.00 15.97           O  
ANISOU 5693  O   ALA B 142     2205   1877   1986     46     16     90       O  
ATOM   5694  CB  ALA B 142       8.683  -6.690  11.308  1.00 16.60           C  
ANISOU 5694  CB  ALA B 142     2334   1924   2048     29    -33     95       C  
ATOM   5695  N   ALA B 143       8.734  -5.373   8.494  1.00 15.27           N  
ANISOU 5695  N   ALA B 143     2108   1780   1912     30    -23     92       N  
ATOM   5696  CA  ALA B 143       8.468  -4.223   7.613  1.00 16.37           C  
ANISOU 5696  CA  ALA B 143     2239   1924   2055     34    -16     89       C  
ATOM   5697  C   ALA B 143       7.683  -4.616   6.364  1.00 15.96           C  
ANISOU 5697  C   ALA B 143     2159   1890   2015     39      3     88       C  
ATOM   5698  O   ALA B 143       6.780  -3.900   5.909  1.00 17.80           O  
ANISOU 5698  O   ALA B 143     2390   2127   2244     46     17     86       O  
ATOM   5699  CB  ALA B 143       9.794  -3.548   7.197  1.00 16.59           C  
ANISOU 5699  CB  ALA B 143     2261   1945   2097     25    -38     92       C  
ATOM   5700  N   ASP B 144       8.043  -5.762   5.796  1.00 15.32           N  
ANISOU 5700  N   ASP B 144     2056   1816   1947     35      1     89       N  
ATOM   5701  CA  ASP B 144       7.467  -6.191   4.529  1.00 14.63           C  
ANISOU 5701  CA  ASP B 144     1945   1742   1871     39     14     88       C  
ATOM   5702  C   ASP B 144       5.993  -6.517   4.752  1.00 16.22           C  
ANISOU 5702  C   ASP B 144     2148   1949   2066     46     32     87       C  
ATOM   5703  O   ASP B 144       5.133  -6.042   4.006  1.00 16.59           O  
ANISOU 5703  O   ASP B 144     2186   2001   2114     52     42     86       O  
ATOM   5704  CB  ASP B 144       8.245  -7.382   3.966  1.00 12.33           C  
ANISOU 5704  CB  ASP B 144     1634   1454   1593     33      8     90       C  
ATOM   5705  CG  ASP B 144       7.756  -7.801   2.582  1.00 15.73           C  
ANISOU 5705  CG  ASP B 144     2046   1896   2033     37     19     88       C  
ATOM   5706  OD1 ASP B 144       6.688  -8.430   2.482  1.00 17.27           O  
ANISOU 5706  OD1 ASP B 144     2238   2097   2227     40     28     87       O  
ATOM   5707  OD2 ASP B 144       8.429  -7.518   1.571  1.00 15.47           O  
ANISOU 5707  OD2 ASP B 144     2004   1863   2008     36     18     89       O  
ATOM   5708  N   HIS B 145       5.694  -7.283   5.797  1.00 15.86           N  
ANISOU 5708  N   HIS B 145     2112   1899   2014     47     35     89       N  
ATOM   5709  CA  HIS B 145       4.307  -7.681   6.037  1.00 15.80           C  
ANISOU 5709  CA  HIS B 145     2103   1894   2005     54     54     91       C  
ATOM   5710  C   HIS B 145       3.389  -6.568   6.539  1.00 16.74           C  
ANISOU 5710  C   HIS B 145     2239   2008   2114     63     68     92       C  
ATOM   5711  O   HIS B 145       2.180  -6.633   6.321  1.00 16.25           O  
ANISOU 5711  O   HIS B 145     2167   1948   2058     71     85     96       O  
ATOM   5712  CB  HIS B 145       4.264  -8.901   6.962  1.00 16.52           C  
ANISOU 5712  CB  HIS B 145     2199   1982   2093     53     55     94       C  
ATOM   5713  CG  HIS B 145       4.832 -10.127   6.311  1.00 19.88           C  
ANISOU 5713  CG  HIS B 145     2604   2415   2533     46     46     94       C  
ATOM   5714  ND1 HIS B 145       4.523 -11.408   6.716  1.00 21.21           N  
ANISOU 5714  ND1 HIS B 145     2768   2584   2705     46     50     97       N  
ATOM   5715  CD2 HIS B 145       5.660 -10.259   5.246  1.00 18.42           C  
ANISOU 5715  CD2 HIS B 145     2403   2235   2359     41     36     92       C  
ATOM   5716  CE1 HIS B 145       5.151 -12.275   5.942  1.00 23.31           C  
ANISOU 5716  CE1 HIS B 145     3016   2855   2982     40     41     96       C  
ATOM   5717  NE2 HIS B 145       5.854 -11.606   5.044  1.00 21.11           N  
ANISOU 5717  NE2 HIS B 145     2732   2580   2709     37     33     93       N  
ATOM   5718  N   LYS B 146       3.968  -5.571   7.204  1.00 16.98           N  
ANISOU 5718  N   LYS B 146     2294   2028   2130     63     61     90       N  
ATOM   5719  CA  LYS B 146       3.242  -4.379   7.631  1.00 19.75           C  
ANISOU 5719  CA  LYS B 146     2664   2371   2469     72     75     91       C  
ATOM   5720  C   LYS B 146       2.607  -3.591   6.486  1.00 18.38           C  
ANISOU 5720  C   LYS B 146     2472   2206   2306     76     83     90       C  
ATOM   5721  O   LYS B 146       1.635  -2.864   6.692  1.00 15.19           O  
ANISOU 5721  O   LYS B 146     2075   1797   1899     86    100     93       O  
ATOM   5722  CB  LYS B 146       4.221  -3.426   8.307  1.00 20.47           C  
ANISOU 5722  CB  LYS B 146     2784   2449   2544     68     59     88       C  
ATOM   5723  CG  LYS B 146       3.577  -2.590   9.390  1.00 30.50           C  
ANISOU 5723  CG  LYS B 146     4089   3704   3794     78     73     88       C  
ATOM   5724  CD  LYS B 146       4.463  -1.425   9.807  1.00 36.63           C  
ANISOU 5724  CD  LYS B 146     4893   4467   4555     74     54     85       C  
ATOM   5725  CE  LYS B 146       3.700  -0.576  10.816  1.00 41.67           C  
ANISOU 5725  CE  LYS B 146     5571   5090   5171     86     72     85       C  
ATOM   5726  NZ  LYS B 146       4.301   0.773  10.981  1.00 45.24           N  
ANISOU 5726  NZ  LYS B 146     6046   5529   5611     84     57     81       N  
ATOM   5727  N   TRP B 147       3.183  -3.709   5.295  1.00 16.30           N  
ANISOU 5727  N   TRP B 147     2186   1952   2055     70     70     88       N  
ATOM   5728  CA  TRP B 147       2.714  -2.963   4.137  1.00 17.36           C  
ANISOU 5728  CA  TRP B 147     2305   2092   2197     73     74     87       C  
ATOM   5729  C   TRP B 147       1.918  -3.819   3.160  1.00 17.55           C  
ANISOU 5729  C   TRP B 147     2303   2126   2237     74     78     89       C  
ATOM   5730  O   TRP B 147       2.286  -4.967   2.876  1.00 17.84           O  
ANISOU 5730  O   TRP B 147     2329   2168   2280     68     71     89       O  
ATOM   5731  CB  TRP B 147       3.910  -2.363   3.408  1.00 16.51           C  
ANISOU 5731  CB  TRP B 147     2194   1985   2091     66     57     83       C  
ATOM   5732  CG  TRP B 147       3.561  -1.585   2.191  1.00 13.77           C  
ANISOU 5732  CG  TRP B 147     1835   1645   1751     69     60     83       C  
ATOM   5733  CD1 TRP B 147       3.054  -0.318   2.143  1.00 14.31           C  
ANISOU 5733  CD1 TRP B 147     1912   1710   1815     75     67     82       C  
ATOM   5734  CD2 TRP B 147       3.761  -1.993   0.838  1.00 13.37           C  
ANISOU 5734  CD2 TRP B 147     1765   1602   1711     67     55     82       C  
ATOM   5735  NE1 TRP B 147       2.923   0.090   0.836  1.00 17.55           N  
ANISOU 5735  NE1 TRP B 147     2307   2127   2234     76     65     82       N  
ATOM   5736  CE2 TRP B 147       3.357  -0.918   0.014  1.00 14.34           C  
ANISOU 5736  CE2 TRP B 147     1886   1727   1835     71     58     81       C  
ATOM   5737  CE3 TRP B 147       4.272  -3.154   0.245  1.00 13.99           C  
ANISOU 5737  CE3 TRP B 147     1832   1686   1798     62     49     82       C  
ATOM   5738  CZ2 TRP B 147       3.411  -0.978  -1.378  1.00 14.63           C  
ANISOU 5738  CZ2 TRP B 147     1910   1769   1878     71     55     80       C  
ATOM   5739  CZ3 TRP B 147       4.331  -3.213  -1.144  1.00 18.25           C  
ANISOU 5739  CZ3 TRP B 147     2360   2230   2343     62     48     81       C  
ATOM   5740  CH2 TRP B 147       3.916  -2.126  -1.937  1.00 16.37           C  
ANISOU 5740  CH2 TRP B 147     2122   1993   2104     66     50     80       C  
ATOM   5741  N   TRP B 148       0.833  -3.239   2.653  1.00 14.86           N  
ANISOU 5741  N   TRP B 148     1955   1788   1904     80     88     92       N  
ATOM   5742  CA  TRP B 148      -0.089  -3.944   1.774  1.00 14.12           C  
ANISOU 5742  CA  TRP B 148     1838   1699   1826     81     90     96       C  
ATOM   5743  C   TRP B 148      -0.080  -3.235   0.420  1.00 13.87           C  
ANISOU 5743  C   TRP B 148     1797   1672   1799     81     81     93       C  
ATOM   5744  O   TRP B 148      -0.650  -2.153   0.263  1.00 15.73           O  
ANISOU 5744  O   TRP B 148     2034   1905   2035     86     87     95       O  
ATOM   5745  CB  TRP B 148      -1.510  -4.016   2.363  1.00 14.71           C  
ANISOU 5745  CB  TRP B 148     1908   1769   1911     90    108    104       C  
ATOM   5746  CG  TRP B 148      -2.323  -5.077   1.666  1.00 14.82           C  
ANISOU 5746  CG  TRP B 148     1898   1787   1944     88    104    109       C  
ATOM   5747  CD1 TRP B 148      -3.029  -4.941   0.499  1.00 17.08           C  
ANISOU 5747  CD1 TRP B 148     2167   2075   2245     88     96    112       C  
ATOM   5748  CD2 TRP B 148      -2.436  -6.455   2.044  1.00 14.18           C  
ANISOU 5748  CD2 TRP B 148     1810   1707   1871     84    104    112       C  
ATOM   5749  NE1 TRP B 148      -3.592  -6.147   0.143  1.00 18.37           N  
ANISOU 5749  NE1 TRP B 148     2314   2240   2426     84     90    116       N  
ATOM   5750  CE2 TRP B 148      -3.253  -7.089   1.080  1.00 17.38           C  
ANISOU 5750  CE2 TRP B 148     2193   2113   2295     82     96    117       C  
ATOM   5751  CE3 TRP B 148      -1.947  -7.207   3.116  1.00 15.81           C  
ANISOU 5751  CE3 TRP B 148     2027   1910   2067     83    109    112       C  
ATOM   5752  CZ2 TRP B 148      -3.566  -8.451   1.134  1.00 20.14           C  
ANISOU 5752  CZ2 TRP B 148     2530   2462   2657     79     92    120       C  
ATOM   5753  CZ3 TRP B 148      -2.278  -8.569   3.184  1.00 20.79           C  
ANISOU 5753  CZ3 TRP B 148     2645   2542   2710     80    108    116       C  
ATOM   5754  CH2 TRP B 148      -3.070  -9.172   2.191  1.00 21.93           C  
ANISOU 5754  CH2 TRP B 148     2767   2688   2875     78    100    120       C  
ATOM   5755  N   GLY B 149       0.603  -3.822  -0.554  1.00 14.24           N  
ANISOU 5755  N   GLY B 149     1838   1725   1848     75     68     89       N  
ATOM   5756  CA  GLY B 149       0.653  -3.257  -1.908  1.00 13.22           C  
ANISOU 5756  CA  GLY B 149     1703   1597   1720     75     61     87       C  
ATOM   5757  C   GLY B 149       1.452  -4.149  -2.839  1.00 15.24           C  
ANISOU 5757  C   GLY B 149     1956   1856   1976     70     51     84       C  
ATOM   5758  O   GLY B 149       1.952  -5.199  -2.402  1.00 14.84           O  
ANISOU 5758  O   GLY B 149     1904   1806   1926     66     49     83       O  
ATOM   5759  N   SER B 150       1.591  -3.728  -4.099  1.00 14.03           N  
ANISOU 5759  N   SER B 150     1803   1703   1822     70     45     82       N  
ATOM   5760  CA  SER B 150       2.126  -4.589  -5.151  1.00 13.13           C  
ANISOU 5760  CA  SER B 150     1689   1590   1708     68     38     79       C  
ATOM   5761  C   SER B 150       3.648  -4.639  -5.215  1.00 12.51           C  
ANISOU 5761  C   SER B 150     1617   1510   1625     65     40     77       C  
ATOM   5762  O   SER B 150       4.317  -3.632  -4.960  1.00 12.36           O  
ANISOU 5762  O   SER B 150     1601   1489   1603     66     43     78       O  
ATOM   5763  CB  SER B 150       1.540  -4.178  -6.504  1.00 12.77           C  
ANISOU 5763  CB  SER B 150     1646   1542   1661     71     31     79       C  
ATOM   5764  OG  SER B 150       0.129  -4.299  -6.451  1.00 13.54           O  
ANISOU 5764  OG  SER B 150     1735   1639   1769     72     26     83       O  
ATOM   5765  N   ALA B 151       4.169  -5.806  -5.586  1.00 10.23           N  
ANISOU 5765  N   ALA B 151     1328   1221   1338     63     38     77       N  
ATOM   5766  CA  ALA B 151       5.615  -6.056  -5.653  1.00 11.27           C  
ANISOU 5766  CA  ALA B 151     1461   1349   1471     61     42     77       C  
ATOM   5767  C   ALA B 151       6.406  -4.968  -6.386  1.00 13.07           C  
ANISOU 5767  C   ALA B 151     1694   1573   1697     64     47     79       C  
ATOM   5768  O   ALA B 151       7.475  -4.538  -5.917  1.00 14.27           O  
ANISOU 5768  O   ALA B 151     1844   1722   1854     62     50     82       O  
ATOM   5769  CB  ALA B 151       5.876  -7.435  -6.299  1.00  8.77           C  
ANISOU 5769  CB  ALA B 151     1145   1030   1155     61     42     76       C  
ATOM   5770  N   GLU B 152       5.874  -4.517  -7.523  1.00 12.85           N  
ANISOU 5770  N   GLU B 152     1674   1545   1664     69     47     77       N  
ATOM   5771  CA  GLU B 152       6.613  -3.644  -8.434  1.00 13.24           C  
ANISOU 5771  CA  GLU B 152     1729   1589   1710     73     54     79       C  
ATOM   5772  C   GLU B 152       6.856  -2.239  -7.878  1.00 13.20           C  
ANISOU 5772  C   GLU B 152     1722   1585   1707     72     55     81       C  
ATOM   5773  O   GLU B 152       7.670  -1.501  -8.419  1.00 11.77           O  
ANISOU 5773  O   GLU B 152     1544   1399   1528     74     61     84       O  
ATOM   5774  CB  GLU B 152       5.911  -3.535  -9.786  1.00 13.71           C  
ANISOU 5774  CB  GLU B 152     1801   1646   1759     78     52     77       C  
ATOM   5775  CG  GLU B 152       5.869  -4.821 -10.607  1.00 13.57           C  
ANISOU 5775  CG  GLU B 152     1793   1623   1737     79     50     75       C  
ATOM   5776  CD  GLU B 152       4.795  -5.812 -10.145  1.00 16.40           C  
ANISOU 5776  CD  GLU B 152     2146   1986   2099     75     38     72       C  
ATOM   5777  OE1 GLU B 152       3.972  -5.517  -9.249  1.00 16.15           O  
ANISOU 5777  OE1 GLU B 152     2103   1960   2073     72     32     73       O  
ATOM   5778  OE2 GLU B 152       4.765  -6.935 -10.682  1.00 15.68           O  
ANISOU 5778  OE2 GLU B 152     2062   1890   2003     75     34     70       O  
ATOM   5779  N   VAL B 153       6.168  -1.872  -6.803  1.00 13.61           N  
ANISOU 5779  N   VAL B 153     1771   1641   1759     70     50     80       N  
ATOM   5780  CA  VAL B 153       6.315  -0.537  -6.221  1.00 14.74           C  
ANISOU 5780  CA  VAL B 153     1915   1782   1902     70     50     81       C  
ATOM   5781  C   VAL B 153       6.865  -0.526  -4.795  1.00 15.17           C  
ANISOU 5781  C   VAL B 153     1968   1834   1959     65     46     82       C  
ATOM   5782  O   VAL B 153       6.975   0.537  -4.176  1.00 15.11           O  
ANISOU 5782  O   VAL B 153     1966   1823   1950     64     44     82       O  
ATOM   5783  CB  VAL B 153       5.000   0.287  -6.306  1.00 14.69           C  
ANISOU 5783  CB  VAL B 153     1911   1778   1890     74     49     79       C  
ATOM   5784  CG1 VAL B 153       4.620   0.534  -7.773  1.00 14.62           C  
ANISOU 5784  CG1 VAL B 153     1906   1769   1878     79     49     79       C  
ATOM   5785  CG2 VAL B 153       3.856  -0.403  -5.571  1.00 13.75           C  
ANISOU 5785  CG2 VAL B 153     1787   1663   1772     74     48     78       C  
ATOM   5786  N   ILE B 154       7.265  -1.693  -4.287  1.00 14.85           N  
ANISOU 5786  N   ILE B 154     1925   1794   1923     61     44     83       N  
ATOM   5787  CA  ILE B 154       7.629  -1.794  -2.874  1.00 14.30           C  
ANISOU 5787  CA  ILE B 154     1857   1720   1854     56     38     84       C  
ATOM   5788  C   ILE B 154       8.888  -0.999  -2.531  1.00 15.00           C  
ANISOU 5788  C   ILE B 154     1948   1800   1950     51     31     88       C  
ATOM   5789  O   ILE B 154       9.034  -0.524  -1.402  1.00 15.02           O  
ANISOU 5789  O   ILE B 154     1959   1797   1949     48     23     88       O  
ATOM   5790  CB  ILE B 154       7.741  -3.258  -2.394  1.00 14.52           C  
ANISOU 5790  CB  ILE B 154     1881   1750   1885     52     36     84       C  
ATOM   5791  CG1 ILE B 154       7.688  -3.317  -0.861  1.00 15.06           C  
ANISOU 5791  CG1 ILE B 154     1957   1814   1949     49     30     84       C  
ATOM   5792  CG2 ILE B 154       9.012  -3.902  -2.954  1.00 10.80           C  
ANISOU 5792  CG2 ILE B 154     1402   1275   1426     50     36     88       C  
ATOM   5793  CD1 ILE B 154       7.517  -4.757  -0.311  1.00 14.19           C  
ANISOU 5793  CD1 ILE B 154     1843   1706   1840     47     29     84       C  
ATOM   5794  N   GLU B 155       9.760  -0.782  -3.512  1.00 14.51           N  
ANISOU 5794  N   GLU B 155     1880   1735   1898     52     35     92       N  
ATOM   5795  CA  GLU B 155      10.981  -0.015  -3.253  1.00 14.71           C  
ANISOU 5795  CA  GLU B 155     1902   1749   1935     47     28     99       C  
ATOM   5796  C   GLU B 155      10.738   1.474  -2.990  1.00 16.10           C  
ANISOU 5796  C   GLU B 155     2088   1922   2106     48     24     97       C  
ATOM   5797  O   GLU B 155      11.613   2.155  -2.456  1.00 16.04           O  
ANISOU 5797  O   GLU B 155     2081   1904   2108     43     13    102       O  
ATOM   5798  CB  GLU B 155      11.995  -0.239  -4.382  1.00 13.69           C  
ANISOU 5798  CB  GLU B 155     1761   1616   1822     49     38    106       C  
ATOM   5799  CG  GLU B 155      12.551  -1.675  -4.385  1.00 15.34           C  
ANISOU 5799  CG  GLU B 155     1962   1824   2041     47     40    109       C  
ATOM   5800  CD  GLU B 155      13.377  -1.986  -5.627  1.00 19.07           C  
ANISOU 5800  CD  GLU B 155     2427   2291   2526     52     56    117       C  
ATOM   5801  OE1 GLU B 155      13.252  -1.229  -6.610  1.00 19.91           O  
ANISOU 5801  OE1 GLU B 155     2538   2397   2629     58     66    117       O  
ATOM   5802  OE2 GLU B 155      14.143  -2.975  -5.635  1.00 20.63           O  
ANISOU 5802  OE2 GLU B 155     2615   2483   2737     51     60    123       O  
ATOM   5803  N   LYS B 156       9.548   1.969  -3.335  1.00 14.13           N  
ANISOU 5803  N   LYS B 156     1845   1681   1843     54     31     92       N  
ATOM   5804  CA  LYS B 156       9.168   3.341  -3.045  1.00 13.90           C  
ANISOU 5804  CA  LYS B 156     1826   1648   1807     56     29     90       C  
ATOM   5805  C   LYS B 156       8.765   3.446  -1.576  1.00 16.48           C  
ANISOU 5805  C   LYS B 156     2167   1971   2124     54     21     87       C  
ATOM   5806  O   LYS B 156       8.853   4.514  -0.976  1.00 14.55           O  
ANISOU 5806  O   LYS B 156     1935   1718   1874     53     15     87       O  
ATOM   5807  CB  LYS B 156       8.028   3.806  -3.970  1.00 16.17           C  
ANISOU 5807  CB  LYS B 156     2113   1943   2085     64     39     86       C  
ATOM   5808  CG  LYS B 156       8.413   3.956  -5.442  1.00 16.36           C  
ANISOU 5808  CG  LYS B 156     2131   1968   2115     67     47     89       C  
ATOM   5809  CD  LYS B 156       9.544   4.977  -5.694  1.00 20.97           C  
ANISOU 5809  CD  LYS B 156     2714   2543   2710     65     46     95       C  
ATOM   5810  CE  LYS B 156       9.140   6.390  -5.247  1.00 22.48           C  
ANISOU 5810  CE  LYS B 156     2914   2731   2894     66     41     93       C  
ATOM   5811  NZ  LYS B 156      10.141   7.406  -5.699  1.00 23.96           N  
ANISOU 5811  NZ  LYS B 156     3099   2909   3094     65     41     99       N  
ATOM   5812  N   GLU B 157       8.359   2.317  -0.993  1.00 15.92           N  
ANISOU 5812  N   GLU B 157     2096   1903   2048     53     22     85       N  
ATOM   5813  CA  GLU B 157       7.876   2.276   0.374  1.00 16.07           C  
ANISOU 5813  CA  GLU B 157     2132   1918   2056     53     19     83       C  
ATOM   5814  C   GLU B 157       8.988   2.004   1.384  1.00 16.90           C  
ANISOU 5814  C   GLU B 157     2245   2012   2164     44      2     86       C  
ATOM   5815  O   GLU B 157       8.967   2.563   2.484  1.00 17.41           O  
ANISOU 5815  O   GLU B 157     2331   2066   2217     43     -6     85       O  
ATOM   5816  CB  GLU B 157       6.781   1.207   0.487  1.00 16.66           C  
ANISOU 5816  CB  GLU B 157     2202   2000   2125     57     29     81       C  
ATOM   5817  CG  GLU B 157       6.262   0.967   1.902  1.00 14.72           C  
ANISOU 5817  CG  GLU B 157     1974   1750   1868     59     31     80       C  
ATOM   5818  CD  GLU B 157       5.459   2.131   2.453  1.00 20.94           C  
ANISOU 5818  CD  GLU B 157     2780   2531   2643     66     39     79       C  
ATOM   5819  OE1 GLU B 157       4.952   2.971   1.678  1.00 21.08           O  
ANISOU 5819  OE1 GLU B 157     2792   2553   2663     70     46     78       O  
ATOM   5820  OE2 GLU B 157       5.309   2.197   3.685  1.00 22.43           O  
ANISOU 5820  OE2 GLU B 157     2991   2711   2819     67     39     78       O  
ATOM   5821  N   MET B 158       9.941   1.141   1.037  1.00 15.68           N  
ANISOU 5821  N   MET B 158     2075   1857   2024     39     -3     90       N  
ATOM   5822  CA  MET B 158      10.958   0.736   1.994  1.00 16.62           C  
ANISOU 5822  CA  MET B 158     2199   1964   2150     30    -22     95       C  
ATOM   5823  C   MET B 158      12.222   0.271   1.274  1.00 16.84           C  
ANISOU 5823  C   MET B 158     2205   1989   2202     25    -27    103       C  
ATOM   5824  O   MET B 158      12.195  -0.086   0.092  1.00 15.37           O  
ANISOU 5824  O   MET B 158     2003   1812   2024     29    -12    104       O  
ATOM   5825  CB  MET B 158      10.402  -0.369   2.902  1.00 15.88           C  
ANISOU 5825  CB  MET B 158     2114   1873   2045     31    -21     92       C  
ATOM   5826  CG  MET B 158      10.166  -1.701   2.174  1.00 15.46           C  
ANISOU 5826  CG  MET B 158     2042   1832   2000     32     -9     92       C  
ATOM   5827  SD  MET B 158       9.233  -2.928   3.110  1.00 17.20           S  
ANISOU 5827  SD  MET B 158     2269   2056   2207     35     -3     89       S  
ATOM   5828  CE  MET B 158       7.570  -2.287   2.925  1.00 11.80           C  
ANISOU 5828  CE  MET B 158     1592   1380   1509     45     15     84       C  
ATOM   5829  N   THR B 159      13.334   0.264   2.003  1.00 16.89           N  
ANISOU 5829  N   THR B 159     2213   1982   2221     16    -47    110       N  
ATOM   5830  CA  THR B 159      14.571  -0.331   1.521  1.00 17.01           C  
ANISOU 5830  CA  THR B 159     2206   1991   2264     11    -52    121       C  
ATOM   5831  C   THR B 159      14.671  -1.754   2.059  1.00 15.90           C  
ANISOU 5831  C   THR B 159     2062   1852   2125      8    -55    121       C  
ATOM   5832  O   THR B 159      14.396  -1.985   3.239  1.00 17.54           O  
ANISOU 5832  O   THR B 159     2289   2056   2319      5    -68    118       O  
ATOM   5833  CB  THR B 159      15.755   0.559   1.956  1.00 20.32           C  
ANISOU 5833  CB  THR B 159     2625   2392   2703      2    -75    130       C  
ATOM   5834  OG1 THR B 159      15.618   1.812   1.277  1.00 24.28           O  
ANISOU 5834  OG1 THR B 159     3126   2893   3204      5    -68    130       O  
ATOM   5835  CG2 THR B 159      17.089  -0.057   1.562  1.00 21.68           C  
ANISOU 5835  CG2 THR B 159     2771   2555   2910     -3    -80    145       C  
ATOM   5836  N   ARG B 160      15.056  -2.716   1.221  1.00 14.65           N  
ANISOU 5836  N   ARG B 160     1884   1700   1982     10    -42    126       N  
ATOM   5837  CA  ARG B 160      15.030  -4.127   1.630  1.00 13.70           C  
ANISOU 5837  CA  ARG B 160     1759   1582   1861      9    -42    126       C  
ATOM   5838  C   ARG B 160      16.398  -4.686   1.998  1.00 13.81           C  
ANISOU 5838  C   ARG B 160     1760   1582   1903      0    -58    138       C  
ATOM   5839  O   ARG B 160      17.251  -4.803   1.129  1.00 12.80           O  
ANISOU 5839  O   ARG B 160     1611   1450   1800      1    -49    148       O  
ATOM   5840  CB  ARG B 160      14.449  -4.968   0.497  1.00 12.93           C  
ANISOU 5840  CB  ARG B 160     1652   1498   1761     17    -18    121       C  
ATOM   5841  CG  ARG B 160      12.987  -4.669   0.241  1.00 14.29           C  
ANISOU 5841  CG  ARG B 160     1836   1684   1909     24     -6    110       C  
ATOM   5842  CD  ARG B 160      12.535  -5.048  -1.174  1.00 11.60           C  
ANISOU 5842  CD  ARG B 160     1487   1352   1567     31     12    107       C  
ATOM   5843  NE  ARG B 160      12.841  -6.426  -1.544  1.00 11.08           N  
ANISOU 5843  NE  ARG B 160     1412   1287   1509     32     18    110       N  
ATOM   5844  CZ  ARG B 160      12.114  -7.498  -1.232  1.00 16.66           C  
ANISOU 5844  CZ  ARG B 160     2121   2001   2208     32     20    105       C  
ATOM   5845  NH1 ARG B 160      10.981  -7.412  -0.521  1.00 13.36           N  
ANISOU 5845  NH1 ARG B 160     1713   1589   1773     33     17     98       N  
ATOM   5846  NH2 ARG B 160      12.515  -8.676  -1.699  1.00 13.88           N  
ANISOU 5846  NH2 ARG B 160     1761   1649   1864     33     26    107       N  
ATOM   5847  N   PRO B 161      16.602  -5.081   3.268  1.00 13.70           N  
ANISOU 5847  N   PRO B 161     1757   1560   1886     -6    -79    140       N  
ATOM   5848  CA  PRO B 161      17.904  -5.611   3.670  1.00 13.71           C  
ANISOU 5848  CA  PRO B 161     1745   1547   1917    -15    -98    153       C  
ATOM   5849  C   PRO B 161      18.078  -7.061   3.215  1.00 14.69           C  
ANISOU 5849  C   PRO B 161     1852   1678   2052    -12    -83    156       C  
ATOM   5850  O   PRO B 161      17.077  -7.716   2.904  1.00 13.76           O  
ANISOU 5850  O   PRO B 161     1739   1575   1914     -5    -65    146       O  
ATOM   5851  CB  PRO B 161      17.845  -5.529   5.208  1.00 14.76           C  
ANISOU 5851  CB  PRO B 161     1904   1669   2035    -23   -127    151       C  
ATOM   5852  CG  PRO B 161      16.372  -5.777   5.499  1.00 13.90           C  
ANISOU 5852  CG  PRO B 161     1816   1575   1889    -15   -111    136       C  
ATOM   5853  CD  PRO B 161      15.642  -5.025   4.392  1.00 11.64           C  
ANISOU 5853  CD  PRO B 161     1525   1302   1596     -6    -87    130       C  
ATOM   5854  N   TYR B 162      19.316  -7.555   3.135  1.00 13.25           N  
ANISOU 5854  N   TYR B 162     1648   1482   1903    -17    -91    171       N  
ATOM   5855  CA  TYR B 162      19.542  -8.982   2.873  1.00 13.77           C  
ANISOU 5855  CA  TYR B 162     1699   1551   1980    -14    -79    175       C  
ATOM   5856  C   TYR B 162      20.262  -9.557   4.086  1.00 13.99           C  
ANISOU 5856  C   TYR B 162     1727   1565   2021    -25   -108    183       C  
ATOM   5857  O   TYR B 162      20.829  -8.800   4.875  1.00 13.97           O  
ANISOU 5857  O   TYR B 162     1732   1548   2028    -34   -136    190       O  
ATOM   5858  CB  TYR B 162      20.404  -9.210   1.626  1.00 14.41           C  
ANISOU 5858  CB  TYR B 162     1754   1628   2092     -9    -57    187       C  
ATOM   5859  CG  TYR B 162      21.809  -8.693   1.769  1.00 17.61           C  
ANISOU 5859  CG  TYR B 162     2140   2012   2538    -16    -73    206       C  
ATOM   5860  CD1 TYR B 162      22.107  -7.343   1.563  1.00 24.13           C  
ANISOU 5860  CD1 TYR B 162     2965   2830   3372    -18    -79    211       C  
ATOM   5861  CD2 TYR B 162      22.837  -9.549   2.163  1.00 24.13           C  
ANISOU 5861  CD2 TYR B 162     2947   2825   3396    -22    -84    221       C  
ATOM   5862  CE1 TYR B 162      23.407  -6.866   1.727  1.00 28.24           C  
ANISOU 5862  CE1 TYR B 162     3464   3329   3934    -25    -96    231       C  
ATOM   5863  CE2 TYR B 162      24.129  -9.084   2.341  1.00 28.04           C  
ANISOU 5863  CE2 TYR B 162     3421   3297   3934    -29   -101    242       C  
ATOM   5864  CZ  TYR B 162      24.407  -7.747   2.108  1.00 29.93           C  
ANISOU 5864  CZ  TYR B 162     3659   3529   4184    -31   -108    247       C  
ATOM   5865  OH  TYR B 162      25.694  -7.312   2.307  1.00 31.43           O  
ANISOU 5865  OH  TYR B 162     3826   3695   4420    -39   -127    269       O  
ATOM   5866  N   PHE B 163      20.272 -10.879   4.223  1.00 12.81           N  
ANISOU 5866  N   PHE B 163     1572   1419   1874    -24   -102    184       N  
ATOM   5867  CA  PHE B 163      20.847 -11.530   5.399  1.00 11.99           C  
ANISOU 5867  CA  PHE B 163     1472   1304   1781    -34   -130    192       C  
ATOM   5868  C   PHE B 163      21.712 -12.691   4.935  1.00 14.67           C  
ANISOU 5868  C   PHE B 163     1783   1637   2151    -33   -120    204       C  
ATOM   5869  O   PHE B 163      21.329 -13.410   4.009  1.00 14.56           O  
ANISOU 5869  O   PHE B 163     1761   1636   2134    -24    -91    200       O  
ATOM   5870  CB  PHE B 163      19.738 -11.966   6.372  1.00 11.82           C  
ANISOU 5870  CB  PHE B 163     1479   1291   1721    -34   -135    178       C  
ATOM   5871  CG  PHE B 163      18.931 -10.796   6.857  1.00 13.03           C  
ANISOU 5871  CG  PHE B 163     1658   1445   1844    -33   -142    167       C  
ATOM   5872  CD1 PHE B 163      19.454  -9.933   7.813  1.00 16.31           C  
ANISOU 5872  CD1 PHE B 163     2092   1844   2261    -42   -174    172       C  
ATOM   5873  CD2 PHE B 163      17.730 -10.463   6.249  1.00 10.75           C  
ANISOU 5873  CD2 PHE B 163     1378   1174   1530    -24   -117    154       C  
ATOM   5874  CE1 PHE B 163      18.752  -8.807   8.219  1.00 16.59           C  
ANISOU 5874  CE1 PHE B 163     2155   1879   2269    -41   -179    162       C  
ATOM   5875  CE2 PHE B 163      17.018  -9.349   6.656  1.00 14.44           C  
ANISOU 5875  CE2 PHE B 163     1870   1643   1974    -22   -121    145       C  
ATOM   5876  CZ  PHE B 163      17.528  -8.511   7.649  1.00 12.82           C  
ANISOU 5876  CZ  PHE B 163     1684   1420   1767    -30   -150    149       C  
ATOM   5877  N   VAL B 164      22.879 -12.819   5.561  1.00 13.56           N  
ANISOU 5877  N   VAL B 164     1630   1477   2044    -42   -147    221       N  
ATOM   5878  CA  VAL B 164      23.885 -13.796   5.179  1.00 14.93           C  
ANISOU 5878  CA  VAL B 164     1774   1642   2256    -42   -139    237       C  
ATOM   5879  C   VAL B 164      24.158 -14.701   6.373  1.00 14.37           C  
ANISOU 5879  C   VAL B 164     1709   1562   2188    -51   -167    242       C  
ATOM   5880  O   VAL B 164      24.194 -14.242   7.513  1.00 15.35           O  
ANISOU 5880  O   VAL B 164     1852   1676   2302    -61   -202    242       O  
ATOM   5881  CB  VAL B 164      25.191 -13.077   4.764  1.00 15.80           C  
ANISOU 5881  CB  VAL B 164     1857   1731   2414    -46   -146    259       C  
ATOM   5882  CG1 VAL B 164      26.315 -14.078   4.567  1.00 21.90           C  
ANISOU 5882  CG1 VAL B 164     2598   2490   3232    -46   -142    279       C  
ATOM   5883  CG2 VAL B 164      24.960 -12.293   3.468  1.00 17.66           C  
ANISOU 5883  CG2 VAL B 164     2087   1975   2648    -35   -114    256       C  
ATOM   5884  N   GLY B 165      24.298 -15.993   6.116  1.00 14.38           N  
ANISOU 5884  N   GLY B 165     1696   1567   2199    -47   -151    245       N  
ATOM   5885  CA  GLY B 165      24.667 -16.920   7.190  1.00 15.88           C  
ANISOU 5885  CA  GLY B 165     1888   1747   2396    -55   -177    251       C  
ATOM   5886  C   GLY B 165      24.909 -18.293   6.606  1.00 16.06           C  
ANISOU 5886  C   GLY B 165     1891   1774   2436    -48   -152    257       C  
ATOM   5887  O   GLY B 165      25.088 -18.440   5.392  1.00 14.85           O  
ANISOU 5887  O   GLY B 165     1720   1625   2297    -38   -119    260       O  
ATOM   5888  N   LYS B 166      24.933 -19.293   7.480  1.00 13.75           N  
ANISOU 5888  N   LYS B 166     1604   1479   2141    -53   -168    258       N  
ATOM   5889  CA  LYS B 166      25.295 -20.645   7.073  1.00 14.72           C  
ANISOU 5889  CA  LYS B 166     1707   1601   2282    -49   -149    265       C  
ATOM   5890  C   LYS B 166      24.480 -21.676   7.847  1.00 15.25           C  
ANISOU 5890  C   LYS B 166     1795   1679   2320    -50   -154    253       C  
ATOM   5891  O   LYS B 166      24.945 -22.797   8.082  1.00 16.82           O  
ANISOU 5891  O   LYS B 166     1982   1872   2536    -51   -156    261       O  
ATOM   5892  CB  LYS B 166      26.801 -20.890   7.227  1.00 14.23           C  
ANISOU 5892  CB  LYS B 166     1615   1515   2276    -55   -166    291       C  
ATOM   5893  CG  LYS B 166      27.343 -20.628   8.630  1.00 16.20           C  
ANISOU 5893  CG  LYS B 166     1872   1745   2535    -70   -217    301       C  
ATOM   5894  CD  LYS B 166      28.854 -20.840   8.719  1.00 20.11           C  
ANISOU 5894  CD  LYS B 166     2332   2214   3092    -77   -235    330       C  
ATOM   5895  CE  LYS B 166      29.357 -20.329  10.063  1.00 25.19           C  
ANISOU 5895  CE  LYS B 166     2989   2837   3744    -93   -292    339       C  
ATOM   5896  NZ  LYS B 166      30.775 -20.721  10.299  1.00 29.07           N  
ANISOU 5896  NZ  LYS B 166     3446   3301   4296   -102   -316    369       N  
ATOM   5897  N   GLY B 167      23.250 -21.326   8.215  1.00 13.88           N  
ANISOU 5897  N   GLY B 167     1650   1520   2101    -48   -153    234       N  
ATOM   5898  CA  GLY B 167      22.429 -22.280   8.971  1.00 14.31           C  
ANISOU 5898  CA  GLY B 167     1724   1583   2127    -49   -155    224       C  
ATOM   5899  C   GLY B 167      22.334 -23.618   8.265  1.00 13.02           C  
ANISOU 5899  C   GLY B 167     1546   1428   1972    -41   -128    223       C  
ATOM   5900  O   GLY B 167      22.084 -23.655   7.050  1.00 14.27           O  
ANISOU 5900  O   GLY B 167     1694   1596   2132    -32    -98    218       O  
ATOM   5901  N   SER B 168      22.527 -24.716   9.000  1.00 13.40           N  
ANISOU 5901  N   SER B 168     1594   1471   2025    -45   -140    228       N  
ATOM   5902  CA  SER B 168      22.550 -26.051   8.384  1.00 13.45           C  
ANISOU 5902  CA  SER B 168     1585   1482   2041    -39   -116    229       C  
ATOM   5903  C   SER B 168      21.219 -26.437   7.724  1.00 13.57           C  
ANISOU 5903  C   SER B 168     1613   1518   2025    -30    -88    210       C  
ATOM   5904  O   SER B 168      21.197 -27.063   6.660  1.00 15.31           O  
ANISOU 5904  O   SER B 168     1822   1742   2253    -22    -62    209       O  
ATOM   5905  CB  SER B 168      22.956 -27.105   9.424  1.00 12.00           C  
ANISOU 5905  CB  SER B 168     1402   1290   1867    -46   -137    237       C  
ATOM   5906  OG  SER B 168      24.328 -26.931   9.753  1.00 16.20           O  
ANISOU 5906  OG  SER B 168     1915   1800   2439    -53   -160    257       O  
ATOM   5907  N   ALA B 169      20.108 -26.082   8.367  1.00 12.34           N  
ANISOU 5907  N   ALA B 169     1481   1372   1834    -31    -94    197       N  
ATOM   5908  CA  ALA B 169      18.791 -26.352   7.796  1.00 12.23           C  
ANISOU 5908  CA  ALA B 169     1477   1375   1794    -24    -71    182       C  
ATOM   5909  C   ALA B 169      18.608 -25.635   6.453  1.00 11.77           C  
ANISOU 5909  C   ALA B 169     1412   1323   1735    -17    -50    177       C  
ATOM   5910  O   ALA B 169      18.321 -26.274   5.438  1.00 13.26           O  
ANISOU 5910  O   ALA B 169     1595   1517   1924    -10    -28    172       O  
ATOM   5911  CB  ALA B 169      17.690 -25.974   8.770  1.00 11.63           C  
ANISOU 5911  CB  ALA B 169     1426   1306   1685    -26    -79    172       C  
ATOM   5912  N   VAL B 170      18.806 -24.321   6.423  1.00 11.08           N  
ANISOU 5912  N   VAL B 170     1328   1234   1648    -18    -57    178       N  
ATOM   5913  CA  VAL B 170      18.534 -23.595   5.186  1.00 12.94           C  
ANISOU 5913  CA  VAL B 170     1561   1475   1880    -11    -38    172       C  
ATOM   5914  C   VAL B 170      19.546 -23.963   4.083  1.00 13.74           C  
ANISOU 5914  C   VAL B 170     1642   1568   2010     -5    -20    182       C  
ATOM   5915  O   VAL B 170      19.153 -24.271   2.952  1.00 12.82           O  
ANISOU 5915  O   VAL B 170     1527   1457   1887      2      3    176       O  
ATOM   5916  CB  VAL B 170      18.337 -22.072   5.384  1.00 12.73           C  
ANISOU 5916  CB  VAL B 170     1544   1448   1842    -13    -47    169       C  
ATOM   5917  CG1 VAL B 170      19.637 -21.384   5.850  1.00 12.88           C  
ANISOU 5917  CG1 VAL B 170     1554   1452   1888    -20    -68    184       C  
ATOM   5918  CG2 VAL B 170      17.893 -21.442   4.061  1.00 11.40           C  
ANISOU 5918  CG2 VAL B 170     1374   1288   1667     -5    -25    162       C  
ATOM   5919  N   VAL B 171      20.832 -23.996   4.422  1.00 11.85           N  
ANISOU 5919  N   VAL B 171     1385   1312   1802    -10    -31    198       N  
ATOM   5920  CA  VAL B 171      21.843 -24.406   3.451  1.00 12.25           C  
ANISOU 5920  CA  VAL B 171     1416   1352   1884     -3    -11    211       C  
ATOM   5921  C   VAL B 171      21.666 -25.852   2.970  1.00 13.25           C  
ANISOU 5921  C   VAL B 171     1542   1481   2010      2      7    208       C  
ATOM   5922  O   VAL B 171      21.810 -26.151   1.779  1.00 13.41           O  
ANISOU 5922  O   VAL B 171     1559   1499   2035     12     35    209       O  
ATOM   5923  CB  VAL B 171      23.258 -24.143   3.987  1.00 13.11           C  
ANISOU 5923  CB  VAL B 171     1504   1442   2035    -10    -29    232       C  
ATOM   5924  CG1 VAL B 171      24.303 -24.617   2.979  1.00 14.07           C  
ANISOU 5924  CG1 VAL B 171     1602   1549   2191     -1     -3    248       C  
ATOM   5925  CG2 VAL B 171      23.416 -22.615   4.230  1.00 11.61           C  
ANISOU 5925  CG2 VAL B 171     1317   1249   1845    -15    -46    234       C  
ATOM   5926  N   GLY B 172      21.353 -26.745   3.899  1.00 12.02           N  
ANISOU 5926  N   GLY B 172     1390   1328   1847     -3     -6    206       N  
ATOM   5927  CA  GLY B 172      21.081 -28.131   3.554  1.00 13.20           C  
ANISOU 5927  CA  GLY B 172     1541   1480   1994      1      8    202       C  
ATOM   5928  C   GLY B 172      19.882 -28.262   2.627  1.00 13.39           C  
ANISOU 5928  C   GLY B 172     1582   1517   1988      9     27    185       C  
ATOM   5929  O   GLY B 172      19.944 -29.043   1.672  1.00 14.47           O  
ANISOU 5929  O   GLY B 172     1719   1651   2128     17     49    184       O  
ATOM   5930  N   GLN B 173      18.804 -27.512   2.873  1.00 12.12           N  
ANISOU 5930  N   GLN B 173     1436   1369   1800      6     19    173       N  
ATOM   5931  CA  GLN B 173      17.637 -27.588   1.966  1.00 10.91           C  
ANISOU 5931  CA  GLN B 173     1297   1227   1622     12     34    158       C  
ATOM   5932  C   GLN B 173      17.984 -27.021   0.583  1.00 12.55           C  
ANISOU 5932  C   GLN B 173     1506   1430   1834     21     54    159       C  
ATOM   5933  O   GLN B 173      17.521 -27.545  -0.436  1.00 11.57           O  
ANISOU 5933  O   GLN B 173     1392   1305   1698     29     70    151       O  
ATOM   5934  CB  GLN B 173      16.412 -26.868   2.543  1.00 10.56           C  
ANISOU 5934  CB  GLN B 173     1265   1194   1551      8     22    147       C  
ATOM   5935  CG  GLN B 173      15.132 -27.039   1.728  1.00 11.10           C  
ANISOU 5935  CG  GLN B 173     1345   1271   1598     13     32    134       C  
ATOM   5936  CD  GLN B 173      14.670 -28.484   1.635  1.00 13.46           C  
ANISOU 5936  CD  GLN B 173     1646   1571   1895     14     35    131       C  
ATOM   5937  OE1 GLN B 173      14.635 -29.058   0.551  1.00 15.19           O  
ANISOU 5937  OE1 GLN B 173     1870   1787   2114     20     48    128       O  
ATOM   5938  NE2 GLN B 173      14.317 -29.081   2.768  1.00 13.28           N  
ANISOU 5938  NE2 GLN B 173     1623   1551   1871      8     24    132       N  
ATOM   5939  N   MET B 174      18.766 -25.940   0.541  1.00 11.60           N  
ANISOU 5939  N   MET B 174     1376   1303   1727     21     53    167       N  
ATOM   5940  CA  MET B 174      19.294 -25.420  -0.732  1.00 12.57           C  
ANISOU 5940  CA  MET B 174     1498   1418   1858     31     75    171       C  
ATOM   5941  C   MET B 174      20.104 -26.468  -1.509  1.00 13.18           C  
ANISOU 5941  C   MET B 174     1571   1482   1954     40     99    180       C  
ATOM   5942  O   MET B 174      19.986 -26.590  -2.735  1.00 12.72           O  
ANISOU 5942  O   MET B 174     1525   1419   1887     50    122    176       O  
ATOM   5943  CB  MET B 174      20.140 -24.163  -0.507  1.00 12.22           C  
ANISOU 5943  CB  MET B 174     1441   1366   1832     28     69    182       C  
ATOM   5944  CG  MET B 174      19.323 -22.954  -0.025  1.00  9.72           C  
ANISOU 5944  CG  MET B 174     1136   1062   1495     22     51    173       C  
ATOM   5945  SD  MET B 174      20.320 -21.578   0.612  1.00 14.65           S  
ANISOU 5945  SD  MET B 174     1746   1676   2143     15     34    186       S  
ATOM   5946  CE  MET B 174      21.177 -21.042  -0.870  1.00 14.51           C  
ANISOU 5946  CE  MET B 174     1719   1648   2146     27     64    197       C  
ATOM   5947  N   ALA B 175      20.928 -27.215  -0.782  1.00 12.45           N  
ANISOU 5947  N   ALA B 175     1462   1381   1886     36     92    192       N  
ATOM   5948  CA  ALA B 175      21.680 -28.326  -1.355  1.00 13.81           C  
ANISOU 5948  CA  ALA B 175     1628   1540   2078     44    114    201       C  
ATOM   5949  C   ALA B 175      20.772 -29.386  -1.974  1.00 14.02           C  
ANISOU 5949  C   ALA B 175     1675   1571   2078     49    126    187       C  
ATOM   5950  O   ALA B 175      20.991 -29.788  -3.123  1.00 13.28           O  
ANISOU 5950  O   ALA B 175     1594   1468   1984     61    153    187       O  
ATOM   5951  CB  ALA B 175      22.597 -28.953  -0.314  1.00 10.43           C  
ANISOU 5951  CB  ALA B 175     1177   1102   1681     37    100    217       C  
ATOM   5952  N   ALA B 176      19.756 -29.814  -1.221  1.00 14.33           N  
ANISOU 5952  N   ALA B 176     1722   1623   2097     41    105    175       N  
ATOM   5953  CA  ALA B 176      18.832 -30.845  -1.693  1.00 14.26           C  
ANISOU 5953  CA  ALA B 176     1731   1619   2067     44    111    163       C  
ATOM   5954  C   ALA B 176      18.136 -30.395  -2.981  1.00 14.32           C  
ANISOU 5954  C   ALA B 176     1762   1628   2051     52    124    151       C  
ATOM   5955  O   ALA B 176      18.046 -31.170  -3.923  1.00 14.32           O  
ANISOU 5955  O   ALA B 176     1778   1619   2043     61    140    147       O  
ATOM   5956  CB  ALA B 176      17.785 -31.158  -0.621  1.00 14.47           C  
ANISOU 5956  CB  ALA B 176     1759   1659   2078     34     87    154       C  
ATOM   5957  N   ALA B 177      17.651 -29.153  -3.004  1.00 12.88           N  
ANISOU 5957  N   ALA B 177     1582   1454   1857     50    116    146       N  
ATOM   5958  CA  ALA B 177      16.950 -28.601  -4.162  1.00 13.95           C  
ANISOU 5958  CA  ALA B 177     1739   1590   1969     56    124    136       C  
ATOM   5959  C   ALA B 177      17.837 -28.652  -5.408  1.00 13.92           C  
ANISOU 5959  C   ALA B 177     1744   1569   1972     70    154    143       C  
ATOM   5960  O   ALA B 177      17.387 -29.026  -6.481  1.00 13.66           O  
ANISOU 5960  O   ALA B 177     1737   1530   1921     78    165    135       O  
ATOM   5961  CB  ALA B 177      16.458 -27.152  -3.894  1.00 10.40           C  
ANISOU 5961  CB  ALA B 177     1288   1152   1511     52    112    132       C  
ATOM   5962  N   LEU B 178      19.097 -28.263  -5.246  1.00 13.41           N  
ANISOU 5962  N   LEU B 178     1662   1496   1937     73    166    159       N  
ATOM   5963  CA  LEU B 178      20.046 -28.222  -6.343  1.00 13.17           C  
ANISOU 5963  CA  LEU B 178     1637   1447   1918     87    198    169       C  
ATOM   5964  C   LEU B 178      20.414 -29.642  -6.762  1.00 13.91           C  
ANISOU 5964  C   LEU B 178     1740   1528   2017     95    217    171       C  
ATOM   5965  O   LEU B 178      20.687 -29.876  -7.936  1.00 15.48           O  
ANISOU 5965  O   LEU B 178     1960   1711   2209    109    245    172       O  
ATOM   5966  CB  LEU B 178      21.287 -27.411  -5.933  1.00 11.14           C  
ANISOU 5966  CB  LEU B 178     1352   1183   1697     86    204    188       C  
ATOM   5967  CG  LEU B 178      20.942 -25.915  -5.996  1.00 13.14           C  
ANISOU 5967  CG  LEU B 178     1606   1445   1941     83    194    184       C  
ATOM   5968  CD1 LEU B 178      21.991 -25.066  -5.291  1.00 11.92           C  
ANISOU 5968  CD1 LEU B 178     1422   1286   1821     77    187    201       C  
ATOM   5969  CD2 LEU B 178      20.768 -25.433  -7.453  1.00  9.07           C  
ANISOU 5969  CD2 LEU B 178     1116    922   1407     96    220    180       C  
ATOM   5970  N   ALA B 179      20.405 -30.584  -5.823  1.00 12.90           N  
ANISOU 5970  N   ALA B 179     1599   1404   1899     87    202    173       N  
ATOM   5971  CA  ALA B 179      20.791 -31.957  -6.124  1.00 15.06           C  
ANISOU 5971  CA  ALA B 179     1878   1664   2178     94    219    176       C  
ATOM   5972  C   ALA B 179      19.741 -32.599  -7.044  1.00 15.56           C  
ANISOU 5972  C   ALA B 179     1978   1726   2206     99    222    159       C  
ATOM   5973  O   ALA B 179      20.063 -33.083  -8.128  1.00 14.45           O  
ANISOU 5973  O   ALA B 179     1862   1569   2060    113    249    159       O  
ATOM   5974  CB  ALA B 179      20.967 -32.757  -4.821  1.00 14.31           C  
ANISOU 5974  CB  ALA B 179     1760   1574   2102     83    199    181       C  
ATOM   5975  N   VAL B 180      18.473 -32.574  -6.641  1.00 15.47           N  
ANISOU 5975  N   VAL B 180     1974   1731   2172     88    193    144       N  
ATOM   5976  CA  VAL B 180      17.425 -33.144  -7.500  1.00 13.63           C  
ANISOU 5976  CA  VAL B 180     1775   1495   1908     91    190    128       C  
ATOM   5977  C   VAL B 180      17.307 -32.331  -8.798  1.00 14.79           C  
ANISOU 5977  C   VAL B 180     1949   1634   2035    102    205    124       C  
ATOM   5978  O   VAL B 180      17.193 -32.896  -9.893  1.00 13.67           O  
ANISOU 5978  O   VAL B 180     1841   1476   1875    112    219    119       O  
ATOM   5979  CB  VAL B 180      16.068 -33.340  -6.762  1.00 13.31           C  
ANISOU 5979  CB  VAL B 180     1731   1471   1853     78    157    116       C  
ATOM   5980  CG1 VAL B 180      15.516 -31.992  -6.277  1.00 11.18           C  
ANISOU 5980  CG1 VAL B 180     1450   1219   1579     70    140    113       C  
ATOM   5981  CG2 VAL B 180      15.034 -33.999  -7.675  1.00 11.58           C  
ANISOU 5981  CG2 VAL B 180     1544   1246   1607     80    150    103       C  
ATOM   5982  N   GLY B 181      17.419 -31.008  -8.700  1.00 13.94           N  
ANISOU 5982  N   GLY B 181     1830   1534   1931    100    203    127       N  
ATOM   5983  CA  GLY B 181      17.418 -30.162  -9.894  1.00 15.57           C  
ANISOU 5983  CA  GLY B 181     2062   1732   2122    111    219    125       C  
ATOM   5984  C   GLY B 181      18.494 -30.542 -10.907  1.00 16.50           C  
ANISOU 5984  C   GLY B 181     2196   1825   2245    128    258    135       C  
ATOM   5985  O   GLY B 181      18.230 -30.585 -12.110  1.00 16.66           O  
ANISOU 5985  O   GLY B 181     2256   1832   2240    140    272    128       O  
ATOM   5986  N   SER B 182      19.696 -30.853 -10.425  1.00 15.14           N  
ANISOU 5986  N   SER B 182     1999   1646   2107    132    277    151       N  
ATOM   5987  CA  SER B 182      20.779 -31.306 -11.282  1.00 16.99           C  
ANISOU 5987  CA  SER B 182     2246   1856   2353    149    318    164       C  
ATOM   5988  C   SER B 182      20.358 -32.555 -12.062  1.00 17.63           C  
ANISOU 5988  C   SER B 182     2366   1922   2409    158    327    154       C  
ATOM   5989  O   SER B 182      20.701 -32.675 -13.231  1.00 18.20           O  
ANISOU 5989  O   SER B 182     2473   1974   2468    175    358    156       O  
ATOM   5990  CB  SER B 182      22.053 -31.578 -10.473  1.00 17.22           C  
ANISOU 5990  CB  SER B 182     2234   1879   2428    149    331    185       C  
ATOM   5991  OG  SER B 182      22.026 -32.844  -9.825  1.00 13.59           O  
ANISOU 5991  OG  SER B 182     1767   1420   1976    144    321    184       O  
ATOM   5992  N   ILE B 183      19.609 -33.463 -11.434  1.00 18.45           N  
ANISOU 5992  N   ILE B 183     2467   2036   2504    146    300    143       N  
ATOM   5993  CA  ILE B 183      19.166 -34.678 -12.130  1.00 18.16           C  
ANISOU 5993  CA  ILE B 183     2469   1985   2444    153    304    133       C  
ATOM   5994  C   ILE B 183      18.139 -34.351 -13.204  1.00 18.83           C  
ANISOU 5994  C   ILE B 183     2600   2065   2489    156    293    117       C  
ATOM   5995  O   ILE B 183      18.345 -34.647 -14.394  1.00 17.51           O  
ANISOU 5995  O   ILE B 183     2475   1875   2301    172    318    115       O  
ATOM   5996  CB  ILE B 183      18.555 -35.737 -11.204  1.00 17.33           C  
ANISOU 5996  CB  ILE B 183     2350   1891   2342    139    275    127       C  
ATOM   5997  CG1 ILE B 183      19.538 -36.059 -10.073  1.00 13.74           C  
ANISOU 5997  CG1 ILE B 183     1851   1440   1927    135    281    143       C  
ATOM   5998  CG2 ILE B 183      18.159 -36.976 -12.036  1.00 15.86           C  
ANISOU 5998  CG2 ILE B 183     2207   1687   2133    147    280    117       C  
ATOM   5999  CD1 ILE B 183      18.926 -36.865  -8.912  1.00 17.99           C  
ANISOU 5999  CD1 ILE B 183     2370   1994   2471    119    249    137       C  
ATOM   6000  N   VAL B 184      17.073 -33.675 -12.785  1.00 17.09           N  
ANISOU 6000  N   VAL B 184     2370   1865   2257    142    258    107       N  
ATOM   6001  CA  VAL B 184      15.924 -33.494 -13.674  1.00 16.99           C  
ANISOU 6001  CA  VAL B 184     2397   1849   2209    141    239     91       C  
ATOM   6002  C   VAL B 184      16.127 -32.467 -14.775  1.00 17.93           C  
ANISOU 6002  C   VAL B 184     2544   1956   2310    153    258     92       C  
ATOM   6003  O   VAL B 184      15.433 -32.500 -15.794  1.00 16.83           O  
ANISOU 6003  O   VAL B 184     2449   1804   2139    158    250     81       O  
ATOM   6004  CB  VAL B 184      14.595 -33.297 -12.913  1.00 16.19           C  
ANISOU 6004  CB  VAL B 184     2278   1769   2103    122    195     81       C  
ATOM   6005  CG1 VAL B 184      14.419 -34.467 -11.981  1.00 15.42           C  
ANISOU 6005  CG1 VAL B 184     2161   1677   2019    113    181     81       C  
ATOM   6006  CG2 VAL B 184      14.577 -31.978 -12.132  1.00 12.61           C  
ANISOU 6006  CG2 VAL B 184     1789   1338   1664    114    186     86       C  
ATOM   6007  N   LEU B 185      17.081 -31.564 -14.573  1.00 17.86           N  
ANISOU 6007  N   LEU B 185     2510   1951   2324    158    281    105       N  
ATOM   6008  CA  LEU B 185      17.406 -30.579 -15.597  1.00 19.37           C  
ANISOU 6008  CA  LEU B 185     2726   2130   2502    171    304    108       C  
ATOM   6009  C   LEU B 185      18.754 -30.867 -16.274  1.00 20.91           C  
ANISOU 6009  C   LEU B 185     2934   2301   2710    192    355    124       C  
ATOM   6010  O   LEU B 185      19.210 -30.071 -17.090  1.00 21.89           O  
ANISOU 6010  O   LEU B 185     3076   2413   2828    205    381    130       O  
ATOM   6011  CB  LEU B 185      17.348 -29.160 -15.019  1.00 19.51           C  
ANISOU 6011  CB  LEU B 185     2710   2169   2534    163    292    112       C  
ATOM   6012  CG  LEU B 185      15.990 -28.793 -14.387  1.00 19.05           C  
ANISOU 6012  CG  LEU B 185     2641   2133   2464    145    247     99       C  
ATOM   6013  CD1 LEU B 185      16.008 -27.410 -13.762  1.00 17.37           C  
ANISOU 6013  CD1 LEU B 185     2395   1938   2264    137    238    103       C  
ATOM   6014  CD2 LEU B 185      14.839 -28.887 -15.394  1.00 21.47           C  
ANISOU 6014  CD2 LEU B 185     2993   2432   2733    146    228     84       C  
ATOM   6015  N   LYS B 186      19.394 -31.983 -15.929  1.00 22.70           N  
ANISOU 6015  N   LYS B 186     3151   2519   2955    195    370    131       N  
ATOM   6016  CA  LYS B 186      20.661 -32.412 -16.546  1.00 24.65           C  
ANISOU 6016  CA  LYS B 186     3409   2738   3216    216    421    147       C  
ATOM   6017  C   LYS B 186      21.696 -31.298 -16.516  1.00 23.74           C  
ANISOU 6017  C   LYS B 186     3265   2622   3132    223    449    166       C  
ATOM   6018  O   LYS B 186      22.220 -30.883 -17.546  1.00 23.40           O  
ANISOU 6018  O   LYS B 186     3250   2558   3081    241    487    174       O  
ATOM   6019  CB  LYS B 186      20.448 -32.916 -17.977  1.00 26.11           C  
ANISOU 6019  CB  LYS B 186     3662   2895   3361    234    443    139       C  
ATOM   6020  CG  LYS B 186      19.587 -34.161 -18.010  1.00 32.90           C  
ANISOU 6020  CG  LYS B 186     4550   3752   4196    227    416    123       C  
ATOM   6021  CD  LYS B 186      19.059 -34.478 -19.407  1.00 42.85           C  
ANISOU 6021  CD  LYS B 186     5883   4986   5409    241    422    110       C  
ATOM   6022  CE  LYS B 186      18.248 -35.768 -19.352  1.00 46.63           C  
ANISOU 6022  CE  LYS B 186     6386   5460   5868    233    393     95       C  
ATOM   6023  NZ  LYS B 186      17.257 -35.897 -20.457  1.00 51.38           N  
ANISOU 6023  NZ  LYS B 186     7054   6045   6422    235    372     78       N  
ATOM   6024  N   ASN B 187      21.977 -30.808 -15.312  1.00 23.11           N  
ANISOU 6024  N   ASN B 187     3130   2562   3087    208    431    175       N  
ATOM   6025  CA  ASN B 187      22.699 -29.552 -15.166  1.00 21.70           C  
ANISOU 6025  CA  ASN B 187     2922   2386   2935    209    443    190       C  
ATOM   6026  C   ASN B 187      23.831 -29.706 -14.159  1.00 22.26           C  
ANISOU 6026  C   ASN B 187     2940   2458   3059    205    451    211       C  
ATOM   6027  O   ASN B 187      23.602 -29.837 -12.949  1.00 19.08           O  
ANISOU 6027  O   ASN B 187     2503   2074   2670    187    416    209       O  
ATOM   6028  CB  ASN B 187      21.754 -28.415 -14.766  1.00 20.63           C  
ANISOU 6028  CB  ASN B 187     2777   2275   2783    194    405    177       C  
ATOM   6029  CG  ASN B 187      22.472 -27.081 -14.641  1.00 24.11           C  
ANISOU 6029  CG  ASN B 187     3190   2718   3251    195    416    192       C  
ATOM   6030  OD1 ASN B 187      23.516 -26.983 -13.999  1.00 23.78           O  
ANISOU 6030  OD1 ASN B 187     3109   2673   3253    193    427    212       O  
ATOM   6031  ND2 ASN B 187      21.936 -26.056 -15.290  1.00 24.06           N  
ANISOU 6031  ND2 ASN B 187     3205   2715   3221    197    413    185       N  
ATOM   6032  N   ASP B 188      25.054 -29.695 -14.682  1.00 22.39           N  
ANISOU 6032  N   ASP B 188     2952   2451   3105    222    497    233       N  
ATOM   6033  CA  ASP B 188      26.222 -29.946 -13.857  1.00 23.41           C  
ANISOU 6033  CA  ASP B 188     3032   2574   3289    220    506    257       C  
ATOM   6034  C   ASP B 188      26.538 -28.815 -12.874  1.00 21.35           C  
ANISOU 6034  C   ASP B 188     2722   2328   3060    205    480    267       C  
ATOM   6035  O   ASP B 188      27.158 -29.032 -11.836  1.00 22.09           O  
ANISOU 6035  O   ASP B 188     2773   2424   3193    194    466    280       O  
ATOM   6036  CB  ASP B 188      27.449 -30.216 -14.729  1.00 26.72           C  
ANISOU 6036  CB  ASP B 188     3456   2959   3734    244    566    280       C  
ATOM   6037  CG  ASP B 188      28.592 -30.769 -13.913  1.00 32.62           C  
ANISOU 6037  CG  ASP B 188     4155   3697   4540    243    575    305       C  
ATOM   6038  OD1 ASP B 188      28.475 -31.922 -13.442  1.00 42.44           O  
ANISOU 6038  OD1 ASP B 188     5397   4943   5784    238    564    300       O  
ATOM   6039  OD2 ASP B 188      29.563 -30.017 -13.683  1.00 45.37           O  
ANISOU 6039  OD2 ASP B 188     5732   5305   6201    244    588    329       O  
ATOM   6040  N   THR B 189      26.150 -27.595 -13.220  1.00 20.69           N  
ANISOU 6040  N   THR B 189     2647   2253   2961    203    474    261       N  
ATOM   6041  CA  THR B 189      26.344 -26.452 -12.332  1.00 20.08           C  
ANISOU 6041  CA  THR B 189     2530   2189   2908    188    447    268       C  
ATOM   6042  C   THR B 189      25.494 -26.619 -11.076  1.00 18.16           C  
ANISOU 6042  C   THR B 189     2272   1972   2654    166    394    253       C  
ATOM   6043  O   THR B 189      26.007 -26.457  -9.981  1.00 16.02           O  
ANISOU 6043  O   THR B 189     1962   1706   2417    153    373    264       O  
ATOM   6044  CB  THR B 189      25.978 -25.149 -13.040  1.00 21.17           C  
ANISOU 6044  CB  THR B 189     2685   2330   3026    192    451    263       C  
ATOM   6045  OG1 THR B 189      26.835 -25.012 -14.177  1.00 25.19           O  
ANISOU 6045  OG1 THR B 189     3209   2813   3548    214    503    280       O  
ATOM   6046  CG2 THR B 189      26.158 -23.938 -12.133  1.00 20.70           C  
ANISOU 6046  CG2 THR B 189     2588   2284   2990    176    422    270       C  
ATOM   6047  N   TYR B 190      24.213 -26.960 -11.224  1.00 15.89           N  
ANISOU 6047  N   TYR B 190     2015   1699   2321    161    374    228       N  
ATOM   6048  CA  TYR B 190      23.406 -27.237 -10.040  1.00 16.31           C  
ANISOU 6048  CA  TYR B 190     2055   1775   2365    142    330    215       C  
ATOM   6049  C   TYR B 190      24.046 -28.308  -9.151  1.00 15.91           C  
ANISOU 6049  C   TYR B 190     1979   1721   2345    137    325    226       C  
ATOM   6050  O   TYR B 190      24.061 -28.182  -7.928  1.00 15.28           O  
ANISOU 6050  O   TYR B 190     1871   1653   2281    122    294    228       O  
ATOM   6051  CB  TYR B 190      22.002 -27.681 -10.446  1.00 15.19           C  
ANISOU 6051  CB  TYR B 190     1950   1644   2176    140    314    190       C  
ATOM   6052  CG  TYR B 190      21.199 -26.637 -11.193  1.00 17.66           C  
ANISOU 6052  CG  TYR B 190     2288   1963   2458    142    310    178       C  
ATOM   6053  CD1 TYR B 190      21.495 -25.278 -11.088  1.00 17.62           C  
ANISOU 6053  CD1 TYR B 190     2267   1963   2465    140    308    185       C  
ATOM   6054  CD2 TYR B 190      20.090 -27.009 -11.953  1.00 16.12           C  
ANISOU 6054  CD2 TYR B 190     2132   1769   2222    145    303    160       C  
ATOM   6055  CE1 TYR B 190      20.740 -24.323 -11.764  1.00 16.78           C  
ANISOU 6055  CE1 TYR B 190     2182   1861   2329    142    304    174       C  
ATOM   6056  CE2 TYR B 190      19.326 -26.058 -12.620  1.00 15.70           C  
ANISOU 6056  CE2 TYR B 190     2101   1721   2141    146    296    149       C  
ATOM   6057  CZ  TYR B 190      19.657 -24.719 -12.523  1.00 16.25           C  
ANISOU 6057  CZ  TYR B 190     2155   1796   2224    145    297    157       C  
ATOM   6058  OH  TYR B 190      18.904 -23.770 -13.195  1.00 23.19           O  
ANISOU 6058  OH  TYR B 190     3056   2679   3076    146    291    147       O  
ATOM   6059  N   LEU B 191      24.580 -29.366  -9.764  1.00 16.85           N  
ANISOU 6059  N   LEU B 191     2109   1821   2471    151    356    233       N  
ATOM   6060  CA  LEU B 191      25.206 -30.432  -8.984  1.00 17.34           C  
ANISOU 6060  CA  LEU B 191     2148   1878   2563    147    354    244       C  
ATOM   6061  C   LEU B 191      26.408 -29.912  -8.195  1.00 17.57           C  
ANISOU 6061  C   LEU B 191     2131   1900   2645    142    351    269       C  
ATOM   6062  O   LEU B 191      26.575 -30.261  -7.028  1.00 17.32           O  
ANISOU 6062  O   LEU B 191     2072   1875   2632    128    323    273       O  
ATOM   6063  CB  LEU B 191      25.632 -31.614  -9.867  1.00 17.55           C  
ANISOU 6063  CB  LEU B 191     2196   1882   2589    165    392    249       C  
ATOM   6064  CG  LEU B 191      26.235 -32.808  -9.108  1.00 19.48           C  
ANISOU 6064  CG  LEU B 191     2416   2120   2863    162    390    260       C  
ATOM   6065  CD1 LEU B 191      25.295 -33.346  -8.038  1.00 20.32           C  
ANISOU 6065  CD1 LEU B 191     2519   2249   2952    143    346    243       C  
ATOM   6066  CD2 LEU B 191      26.628 -33.932 -10.058  1.00 21.78           C  
ANISOU 6066  CD2 LEU B 191     2734   2388   3152    181    432    264       C  
ATOM   6067  N   ARG B 192      27.252 -29.109  -8.841  1.00 16.86           N  
ANISOU 6067  N   ARG B 192     2032   1794   2579    153    379    286       N  
ATOM   6068  CA  ARG B 192      28.429 -28.567  -8.172  1.00 18.78           C  
ANISOU 6068  CA  ARG B 192     2230   2027   2876    147    376    312       C  
ATOM   6069  C   ARG B 192      27.993 -27.722  -6.978  1.00 18.70           C  
ANISOU 6069  C   ARG B 192     2201   2037   2864    126    326    305       C  
ATOM   6070  O   ARG B 192      28.571 -27.847  -5.893  1.00 15.50           O  
ANISOU 6070  O   A