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***  TRANSFERASE 26-JAN-16 5HTB  ***

elNémo ID: 19111415351141852

Job options:

ID        	=	 19111415351141852
JOBID     	=	 TRANSFERASE 26-JAN-16 5HTB
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


HEADER    TRANSFERASE                             26-JAN-16   5HTB              
TITLE     CRYSTAL STRUCTURE OF HASPIN (GSG2) IN COMPLEX WITH BISUBSTRATE        
TITLE    2 INHIBITOR ARC-3353                                                   
CAVEAT     5HTB    66N C 7 HAS WRONG CHIRALITY AT ATOM C33                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SERINE/THREONINE-PROTEIN KINASE HASPIN;                    
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: GERM CELL-SPECIFIC GENE 2 PROTEIN,H-HASPIN,HAPLOID GERM     
COMPND   5 CELL-SPECIFIC NUCLEAR PROTEIN KINASE;                                
COMPND   6 EC: 2.7.11.1;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 OTHER_DETAILS: KINASE DOMAIN (465-798);                              
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: (2R,3S,4R,5R,6R)-6-((1R,2R,3S,4R,6S)-4,6-DIAMINO-2,3-      
COMPND  11 DIHYDROXYCYCLOHEXYLOXY)-5-AMINO-2-(AMINOMETHYL)-TETRAHYDRO-2H-PYRAN- 
COMPND  12 3,4-DIOL;                                                            
COMPND  13 CHAIN: C;                                                            
COMPND  14 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: GSG2;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_VARIANT: R3-PRARE2;                                
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PNIC28-BSA4;                              
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 SYNTHETIC: YES;                                                      
SOURCE  13 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;                            
SOURCE  14 ORGANISM_TAXID: 32630                                                
KEYWDS    TRANSFERASE, KINASE, INHIBITOR, ALLOSTERIC, STRUCTURAL GENOMICS       
KEYWDS   2 CONSORTIUM (SGC), TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX,         
KEYWDS   3 BISUBSTRATE INHIBITOR                                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.CHAIKUAD,C.HEROVEN,D.LAVOGINA,K.KESTAV,A.URI,F.VON DELFT,           
AUTHOR   2 C.H.ARROWSMITH,A.M.EDWARDS,C.BOUNTRA,S.KNAPP,STRUCTURAL GENOMICS     
AUTHOR   3 CONSORTIUM (SGC)                                                     
REVDAT   1   11-MAY-16 5HTB    0                                                
JRNL        AUTH   D.LAVOGINA,K.KESTAV,A.CHAIKUAD,C.HEROVEN,S.KNAPP,A.URI       
JRNL        TITL   CO-CRYSTAL STRUCTURES OF THE PROTEIN KINASE HASPIN WITH      
JRNL        TITL 2 BISUBSTRATE INHIBITORS.                                      
JRNL        REF    ACTA CRYSTALLOGR.,SECT.F      V.  72   339 2016              
JRNL        REFN                   ESSN 2053-230X                               
JRNL        PMID   27139824                                                     
JRNL        DOI    10.1107/S2053230X16004611                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0103                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 24.91                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 52755                          
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) : 0.163                           
REMARK   3   R VALUE            (WORKING SET) : 0.162                           
REMARK   3   FREE R VALUE                     : 0.181                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2676                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.74                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3863                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.51                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2480                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 212                          
REMARK   3   BIN FREE R VALUE                    : 0.2500                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2683                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 56                                      
REMARK   3   SOLVENT ATOMS            : 370                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 17.70                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 24.57                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.70000                                             
REMARK   3    B22 (A**2) : 0.06000                                              
REMARK   3    B33 (A**2) : 0.64000                                              
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): 0.079         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.077         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.059         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.501         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.968                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.961                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2896 ; 0.016 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  2789 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3938 ; 1.626 ; 1.957       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  6458 ; 0.933 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   361 ; 6.078 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   130 ;35.707 ;24.769       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   518 ;12.199 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    12 ;14.935 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   441 ; 0.110 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3333 ; 0.009 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   669 ; 0.002 ; 0.020       
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):  1348 ; 0.778 ; 1.212       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1347 ; 0.775 ; 1.211       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1693 ; 1.232 ; 1.813       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  1694 ; 1.232 ; 1.814       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1548 ; 1.442 ; 1.492       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  1549 ; 1.442 ; 1.496       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  2230 ; 2.339 ; 2.165       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  3573 ; 7.204 ;12.092       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  3574 ; 7.204 ;12.110       
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  : 1                                          
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   471        A   798                          
REMARK   3    ORIGIN FOR THE GROUP (A):  25.8543  25.4397   8.4664              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0091 T22:   0.0174                                     
REMARK   3      T33:   0.0097 T12:   0.0105                                     
REMARK   3      T13:   0.0066 T23:   0.0059                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3981 L22:   1.8470                                     
REMARK   3      L33:   1.2000 L12:   0.5696                                     
REMARK   3      L13:   0.3793 L23:   0.6646                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0278 S12:   0.0179 S13:   0.0786                       
REMARK   3      S21:  -0.0369 S22:   0.0240 S23:   0.0139                       
REMARK   3      S31:  -0.0553 S32:  -0.0359 S33:  -0.0518                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
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 5HTB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 04-FEB-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000217726.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-FEB-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 6.5-7.0                            
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I04-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.91741                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 2M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : IMOSFLM                            
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 55487                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 24.910                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY                : 4.100                              
REMARK 200  R MERGE                    (I) : 0.08700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 8.9000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.79                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.55200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 2.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60.07                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.08                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 52-60% MPD AND 0.1 M SPG PH 6.5-7.0,     
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277.15K                  
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       38.89500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       40.87500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       39.44500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       40.87500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       38.89500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       39.44500            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2940 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 15180 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C                                  
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   442                                                      
REMARK 465     HIS A   443                                                      
REMARK 465     HIS A   444                                                      
REMARK 465     HIS A   445                                                      
REMARK 465     HIS A   446                                                      
REMARK 465     HIS A   447                                                      
REMARK 465     HIS A   448                                                      
REMARK 465     SER A   449                                                      
REMARK 465     SER A   450                                                      
REMARK 465     GLY A   451                                                      
REMARK 465     VAL A   452                                                      
REMARK 465     ASP A   453                                                      
REMARK 465     LEU A   454                                                      
REMARK 465     GLY A   455                                                      
REMARK 465     THR A   456                                                      
REMARK 465     GLU A   457                                                      
REMARK 465     ASN A   458                                                      
REMARK 465     LEU A   459                                                      
REMARK 465     TYR A   460                                                      
REMARK 465     PHE A   461                                                      
REMARK 465     GLN A   462                                                      
REMARK 465     SER A   463                                                      
REMARK 465     MET A   464                                                      
REMARK 465     GLY A   465                                                      
REMARK 465     GLU A   466                                                      
REMARK 465     CYS A   467                                                      
REMARK 465     SER A   468                                                      
REMARK 465     GLN A   469                                                      
REMARK 465     LYS A   470                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    ARG C   2   CZ    ARG C   2   NH2     0.100                       
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 C   2   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.9 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    GLU A 516      -11.47     83.59                                   
REMARK 500    ARG A 648       -0.27     70.77                                   
REMARK 500    ASP A 649       43.49   -153.59                                   
REMARK 500    LEU A 650       58.56    -92.64                                   
REMARK 500    ASP A 687       95.98     75.80                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 802  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 554   O                                                      
REMARK 620 2 PHE A 556   O    90.7                                              
REMARK 620 3 HOH A 907   O    78.9  91.8                                        
REMARK 620 4 HOH A1116   O    93.8  76.1 165.8                                  
REMARK 620 5 HOH A1138   O   113.0 153.4 104.1  89.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MRD A 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 802                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 803                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 6L5 C 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD C 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Ligand 66N C 7 bound to THR C 6   
DBREF  5HTB A  465   798  UNP    Q8TF76   HASP_HUMAN     465    798             
DBREF  5HTB C    1     7  PDB    5HTB     5HTB             1      7             
SEQADV 5HTB MET A  442  UNP  Q8TF76              INITIATING METHIONINE          
SEQADV 5HTB HIS A  443  UNP  Q8TF76              EXPRESSION TAG                 
SEQADV 5HTB HIS A  444  UNP  Q8TF76              EXPRESSION TAG                 
SEQADV 5HTB HIS A  445  UNP  Q8TF76              EXPRESSION TAG                 
SEQADV 5HTB HIS A  446  UNP  Q8TF76              EXPRESSION TAG                 
SEQADV 5HTB HIS A  447  UNP  Q8TF76              EXPRESSION TAG                 
SEQADV 5HTB HIS A  448  UNP  Q8TF76              EXPRESSION TAG                 
SEQADV 5HTB SER A  449  UNP  Q8TF76              EXPRESSION TAG                 
SEQADV 5HTB SER A  450  UNP  Q8TF76              EXPRESSION TAG                 
SEQADV 5HTB GLY A  451  UNP  Q8TF76              EXPRESSION TAG                 
SEQADV 5HTB VAL A  452  UNP  Q8TF76              EXPRESSION TAG                 
SEQADV 5HTB ASP A  453  UNP  Q8TF76              EXPRESSION TAG                 
SEQADV 5HTB LEU A  454  UNP  Q8TF76              EXPRESSION TAG                 
SEQADV 5HTB GLY A  455  UNP  Q8TF76              EXPRESSION TAG                 
SEQADV 5HTB THR A  456  UNP  Q8TF76              EXPRESSION TAG                 
SEQADV 5HTB GLU A  457  UNP  Q8TF76              EXPRESSION TAG                 
SEQADV 5HTB ASN A  458  UNP  Q8TF76              EXPRESSION TAG                 
SEQADV 5HTB LEU A  459  UNP  Q8TF76              EXPRESSION TAG                 
SEQADV 5HTB TYR A  460  UNP  Q8TF76              EXPRESSION TAG                 
SEQADV 5HTB PHE A  461  UNP  Q8TF76              EXPRESSION TAG                 
SEQADV 5HTB GLN A  462  UNP  Q8TF76              EXPRESSION TAG                 
SEQADV 5HTB SER A  463  UNP  Q8TF76              EXPRESSION TAG                 
SEQADV 5HTB MET A  464  UNP  Q8TF76              EXPRESSION TAG                 
SEQRES   1 A  357  MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU          
SEQRES   2 A  357  GLY THR GLU ASN LEU TYR PHE GLN SER MET GLY GLU CYS          
SEQRES   3 A  357  SER GLN LYS GLY PRO VAL PRO PHE SER HIS CYS LEU PRO          
SEQRES   4 A  357  THR GLU LYS LEU GLN ARG CYS GLU LYS ILE GLY GLU GLY          
SEQRES   5 A  357  VAL PHE GLY GLU VAL PHE GLN THR ILE ALA ASP HIS THR          
SEQRES   6 A  357  PRO VAL ALA ILE LYS ILE ILE ALA ILE GLU GLY PRO ASP          
SEQRES   7 A  357  LEU VAL ASN GLY SER HIS GLN LYS THR PHE GLU GLU ILE          
SEQRES   8 A  357  LEU PRO GLU ILE ILE ILE SER LYS GLU LEU SER LEU LEU          
SEQRES   9 A  357  SER GLY GLU VAL CYS ASN ARG THR GLU GLY PHE ILE GLY          
SEQRES  10 A  357  LEU ASN SER VAL HIS CYS VAL GLN GLY SER TYR PRO PRO          
SEQRES  11 A  357  LEU LEU LEU LYS ALA TRP ASP HIS TYR ASN SER THR LYS          
SEQRES  12 A  357  GLY SER ALA ASN ASP ARG PRO ASP PHE PHE LYS ASP ASP          
SEQRES  13 A  357  GLN LEU PHE ILE VAL LEU GLU PHE GLU PHE GLY GLY ILE          
SEQRES  14 A  357  ASP LEU GLU GLN MET ARG THR LYS LEU SER SER LEU ALA          
SEQRES  15 A  357  THR ALA LYS SER ILE LEU HIS GLN LEU THR ALA SER LEU          
SEQRES  16 A  357  ALA VAL ALA GLU ALA SER LEU ARG PHE GLU HIS ARG ASP          
SEQRES  17 A  357  LEU HIS TRP GLY ASN VAL LEU LEU LYS LYS THR SER LEU          
SEQRES  18 A  357  LYS LYS LEU HIS TYR THR LEU ASN GLY LYS SER SER THR          
SEQRES  19 A  357  ILE PRO SER CYS GLY LEU GLN VAL SER ILE ILE ASP TYR          
SEQRES  20 A  357  THR LEU SER ARG LEU GLU ARG ASP GLY ILE VAL VAL PHE          
SEQRES  21 A  357  CYS ASP VAL SER MET ASP GLU ASP LEU PHE THR GLY ASP          
SEQRES  22 A  357  GLY ASP TYR GLN PHE ASP ILE TYR ARG LEU MET LYS LYS          
SEQRES  23 A  357  GLU ASN ASN ASN ARG TRP GLY GLU TYR HIS PRO TYR SER          
SEQRES  24 A  357  ASN VAL LEU TRP LEU HIS TYR LEU THR ASP LYS MET LEU          
SEQRES  25 A  357  LYS GLN MET THR PHE LYS THR LYS CYS ASN THR PRO ALA          
SEQRES  26 A  357  MET LYS GLN ILE LYS ARG LYS ILE GLN GLU PHE HIS ARG          
SEQRES  27 A  357  THR MET LEU ASN PHE SER SER ALA THR ASP LEU LEU CYS          
SEQRES  28 A  357  GLN HIS SER LEU PHE LYS                                      
SEQRES   1 C    7  ALA ARG LYS LYS GLN THR 66N                                  
HET    66N  C   7       6                                                       
HET    MRD  A 801       8                                                       
HET     NA  A 802       1                                                       
HET    DMS  A 803       4                                                       
HET    6L5  C 101      35                                                       
HET    MPD  C 102       8                                                       
HETNAM     66N L-ALANINAMIDE                                                    
HETNAM     MRD (4R)-2-METHYLPENTANE-2,4-DIOL                                    
HETNAM      NA SODIUM ION                                                       
HETNAM     DMS DIMETHYL SULFOXIDE                                               
HETNAM     6L5 (3R)-4-AMINO-3-{[6-({[(2S,3S,4R,5R)-5-(6-AMINO-9H-               
HETNAM   2 6L5  PURIN-9-YL)-3,4-DIHYDROXYTETRAHYDROFURAN-2-                     
HETNAM   3 6L5  YL]CARBONYL}AMINO)HEXANOYL]AMINO}-4-OXOBUTANOIC ACID            
HETNAM   4 6L5  (NON-PREFERRED NAME)                                            
HETNAM     MPD (4S)-2-METHYL-2,4-PENTANEDIOL                                    
FORMUL   2  66N    C3 H8 N2 O                                                   
FORMUL   3  MRD    C6 H14 O2                                                    
FORMUL   4   NA    NA 1+                                                        
FORMUL   5  DMS    C2 H6 O S                                                    
FORMUL   6  6L5    C20 H28 N8 O8                                                
FORMUL   7  MPD    C6 H14 O2                                                    
FORMUL   8  HOH   *370(H2 O)                                                    
HELIX    1 AA1 PRO A  474  LEU A  479  1                                   6    
HELIX    2 AA2 PRO A  480  ARG A  486  1                                   7    
HELIX    3 AA3 THR A  528  LEU A  544  1                                  17    
HELIX    4 AA4 LEU A  545  GLU A  548  5                                   4    
HELIX    5 AA5 PRO A  570  LYS A  584  1                                  15    
HELIX    6 AA6 GLU A  613  ARG A  616  5                                   4    
HELIX    7 AA7 SER A  621  ARG A  644  1                                  24    
HELIX    8 AA8 ASP A  716  ASN A  730  1                                  15    
HELIX    9 AA9 PRO A  738  GLN A  755  1                                  18    
HELIX   10 AB1 THR A  764  MET A  781  1                                  18    
HELIX   11 AB2 LEU A  782  PHE A  784  5                                   3    
HELIX   12 AB3 SER A  786  HIS A  794  1                                   9    
HELIX   13 AB4 SER A  795  LYS A  798  5                                   4    
SHEET    1 AA1 5 GLU A 488  GLY A 493  0                                        
SHEET    2 AA1 5 GLY A 496  ALA A 503 -1  O  GLN A 500   N  GLU A 488           
SHEET    3 AA1 5 THR A 506  ILE A 515 -1  O  ILE A 510   N  PHE A 499           
SHEET    4 AA1 5 LEU A 599  GLU A 606 -1  O  PHE A 605   N  ALA A 509           
SHEET    5 AA1 5 LEU A 559  GLN A 566 -1  N  SER A 561   O  GLU A 604           
SHEET    1 AA2 2 LEU A 520  VAL A 521  0                                        
SHEET    2 AA2 2 SER A 524  HIS A 525 -1  O  SER A 524   N  VAL A 521           
SHEET    1 AA3 3 ILE A 610  ASP A 611  0                                        
SHEET    2 AA3 3 VAL A 655  LYS A 659 -1  O  LEU A 657   N  ILE A 610           
SHEET    3 AA3 3 LEU A 681  ILE A 685 -1  O  SER A 684   N  LEU A 656           
SHEET    1 AA4 2 LYS A 664  LEU A 669  0                                        
SHEET    2 AA4 2 LYS A 672  PRO A 677 -1  O  SER A 674   N  TYR A 667           
SHEET    1 AA5 2 LEU A 693  ARG A 695  0                                        
SHEET    2 AA5 2 ILE A 698  VAL A 700 -1  O  VAL A 700   N  LEU A 693           
LINK         O   GLU A 554                NA    NA A 802     1555   1555  2.50  
LINK         O   PHE A 556                NA    NA A 802     1555   1555  2.35  
LINK         NZ  LYS C   3                 C18 6L5 C 101     1555   1555  1.33  
LINK         C   THR C   6                 N11 66N C   7     1555   1555  1.34  
LINK        NA    NA A 802                 O   HOH A 907     1555   1555  2.18  
LINK        NA    NA A 802                 O   HOH A1116     1555   1555  2.35  
LINK        NA    NA A 802                 O   HOH A1138     1555   1555  2.14  
SITE     1 AC1  3 PRO A 571  ILE A 698  HOH A1023                               
SITE     1 AC2  6 GLU A 554  PHE A 556  GLU A 606  HOH A 907                    
SITE     2 AC2  6 HOH A1116  HOH A1138                                          
SITE     1 AC3  4 TYR A 667  LYS A 672  SER A 674  HOH A 945                    
SITE     1 AC4 31 ILE A 490  GLY A 491  GLU A 492  GLY A 493                    
SITE     2 AC4 31 VAL A 494  PHE A 495  GLY A 496  ALA A 509                    
SITE     3 AC4 31 ILE A 557  GLU A 606  PHE A 607  GLY A 608                    
SITE     4 AC4 31 GLY A 609  ASP A 611  GLY A 653  LEU A 656                    
SITE     5 AC4 31 ILE A 686  THR A 689  HOH A 929  HOH A 944                    
SITE     6 AC4 31 HOH A 985  HOH A1022  ARG C   2  LYS C   3                    
SITE     7 AC4 31 LYS C   4  MPD C 102  HOH C 203  HOH C 204                    
SITE     8 AC4 31 HOH C 207  HOH C 208  HOH C 212                               
SITE     1 AC5  4 THR A 689  LYS C   3  LYS C   4  6L5 C 101                    
SITE     1 AC6  2 GLN C   5  THR C   6                                          
CRYST1   77.790   78.890   81.750  90.00  90.00  90.00 P 21 21 21    4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.012855  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012676  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012232        0.00000                         
ATOM      1  N   GLY A 471      45.890  28.929  29.989  1.00 53.38           N  
ANISOU    1  N   GLY A 471     6781   6785   6717   -180  -1873   -794       N  
ATOM      2  CA  GLY A 471      45.331  30.301  30.250  1.00 50.78           C  
ANISOU    2  CA  GLY A 471     6499   6488   6309   -255  -1727   -856       C  
ATOM      3  C   GLY A 471      44.912  30.948  28.931  1.00 47.49           C  
ANISOU    3  C   GLY A 471     5984   6056   6003   -249  -1506   -874       C  
ATOM      4  O   GLY A 471      45.399  30.557  27.873  1.00 46.62           O  
ANISOU    4  O   GLY A 471     5743   5922   6047   -201  -1480   -872       O  
ATOM      5  N   PRO A 472      44.004  31.931  28.975  1.00 43.24           N  
ANISOU    5  N   PRO A 472     5510   5530   5388   -296  -1351   -894       N  
ATOM      6  CA  PRO A 472      43.600  32.537  27.700  1.00 39.83           C  
ANISOU    6  CA  PRO A 472     4999   5075   5061   -288  -1161   -899       C  
ATOM      7  C   PRO A 472      44.721  33.366  27.047  1.00 38.16           C  
ANISOU    7  C   PRO A 472     4634   4837   5028   -306  -1144   -988       C  
ATOM      8  O   PRO A 472      45.676  33.733  27.708  1.00 39.82           O  
ANISOU    8  O   PRO A 472     4805   5050   5275   -334  -1260  -1065       O  
ATOM      9  CB  PRO A 472      42.403  33.410  28.066  1.00 39.94           C  
ANISOU    9  CB  PRO A 472     5120   5098   4955   -329  -1029   -908       C  
ATOM     10  CG  PRO A 472      42.265  33.359  29.549  1.00 42.29           C  
ANISOU   10  CG  PRO A 472     5547   5436   5087   -371  -1133   -928       C  
ATOM     11  CD  PRO A 472      43.356  32.540  30.140  1.00 43.55           C  
ANISOU   11  CD  PRO A 472     5692   5602   5252   -357  -1344   -921       C  
ATOM     12  N   VAL A 473      44.605  33.604  25.746  1.00 35.46           N  
ANISOU   12  N   VAL A 473     4210   4471   4793   -295  -1003   -974       N  
ATOM     13  CA  VAL A 473      45.601  34.352  24.962  1.00 35.13           C  
ANISOU   13  CA  VAL A 473     4026   4405   4917   -327   -956  -1048       C  
ATOM     14  C   VAL A 473      45.044  35.736  24.591  1.00 33.60           C  
ANISOU   14  C   VAL A 473     3864   4175   4728   -382   -804  -1071       C  
ATOM     15  O   VAL A 473      43.819  35.952  24.675  1.00 29.93           O  
ANISOU   15  O   VAL A 473     3508   3704   4160   -373   -721  -1024       O  
ATOM     16  CB  VAL A 473      46.025  33.550  23.701  1.00 35.52           C  
ANISOU   16  CB  VAL A 473     3958   4453   5084   -285   -914  -1019       C  
ATOM     17  CG1 VAL A 473      46.619  32.211  24.148  1.00 37.51           C  
ANISOU   17  CG1 VAL A 473     4177   4723   5351   -222  -1084  -1007       C  
ATOM     18  CG2 VAL A 473      44.881  33.310  22.697  1.00 34.47           C  
ANISOU   18  CG2 VAL A 473     3877   4312   4907   -260   -765   -930       C  
ATOM     19  N   PRO A 474      45.916  36.682  24.173  1.00 32.82           N  
ANISOU   19  N   PRO A 474     3669   4046   4756   -439   -766  -1146       N  
ATOM     20  CA  PRO A 474      45.414  37.971  23.716  1.00 32.31           C  
ANISOU   20  CA  PRO A 474     3639   3927   4710   -490   -629  -1157       C  
ATOM     21  C   PRO A 474      44.868  37.861  22.356  1.00 30.33           C  
ANISOU   21  C   PRO A 474     3377   3657   4492   -474   -492  -1080       C  
ATOM     22  O   PRO A 474      45.169  36.894  21.635  1.00 30.23           O  
ANISOU   22  O   PRO A 474     3296   3673   4516   -439   -492  -1042       O  
ATOM     23  CB  PRO A 474      46.664  38.887  23.753  1.00 34.33           C  
ANISOU   23  CB  PRO A 474     3792   4156   5096   -569   -652  -1261       C  
ATOM     24  CG  PRO A 474      47.781  37.954  23.539  1.00 35.39           C  
ANISOU   24  CG  PRO A 474     3793   4334   5321   -548   -740  -1285       C  
ATOM     25  CD  PRO A 474      47.397  36.679  24.249  1.00 35.40           C  
ANISOU   25  CD  PRO A 474     3855   4382   5215   -467   -862  -1233       C  
ATOM     26  N   PHE A 475      44.026  38.806  21.970  1.00 29.01           N  
ANISOU   26  N   PHE A 475     3280   3435   4308   -495   -381  -1056       N  
ATOM     27  CA  PHE A 475      43.513  38.756  20.620  1.00 28.45           C  
ANISOU   27  CA  PHE A 475     3207   3341   4261   -484   -261   -976       C  
ATOM     28  C   PHE A 475      44.644  38.638  19.565  1.00 31.63           C  
ANISOU   28  C   PHE A 475     3486   3749   4783   -530   -221   -991       C  
ATOM     29  O   PHE A 475      44.454  37.969  18.531  1.00 30.59           O  
ANISOU   29  O   PHE A 475     3333   3638   4653   -506   -160   -929       O  
ATOM     30  CB  PHE A 475      42.648  39.960  20.305  1.00 27.79           C  
ANISOU   30  CB  PHE A 475     3205   3181   4175   -507   -166   -957       C  
ATOM     31  CG  PHE A 475      41.200  39.768  20.623  1.00 25.81           C  
ANISOU   31  CG  PHE A 475     3055   2932   3819   -443   -146   -907       C  
ATOM     32  CD1 PHE A 475      40.361  39.204  19.698  1.00 24.92           C  
ANISOU   32  CD1 PHE A 475     2964   2828   3678   -397    -85   -815       C  
ATOM     33  CD2 PHE A 475      40.685  40.201  21.835  1.00 26.41           C  
ANISOU   33  CD2 PHE A 475     3200   3005   3829   -435   -183   -963       C  
ATOM     34  CE1 PHE A 475      39.022  39.031  19.949  1.00 24.12           C  
ANISOU   34  CE1 PHE A 475     2939   2731   3495   -341    -64   -777       C  
ATOM     35  CE2 PHE A 475      39.328  40.054  22.103  1.00 25.10           C  
ANISOU   35  CE2 PHE A 475     3113   2847   3576   -383   -147   -931       C  
ATOM     36  CZ  PHE A 475      38.490  39.502  21.142  1.00 24.38           C  
ANISOU   36  CZ  PHE A 475     3031   2761   3472   -335    -87   -837       C  
ATOM     37  N   SER A 476      45.786  39.298  19.845  1.00 34.28           N  
ANISOU   37  N   SER A 476     3742   4071   5213   -601   -251  -1081       N  
ATOM     38  CA ASER A 476      46.984  39.280  18.982  0.50 36.67           C  
ANISOU   38  CA ASER A 476     3908   4385   5639   -662   -207  -1122       C  
ATOM     39  CA BSER A 476      46.941  39.296  18.941  0.50 36.40           C  
ANISOU   39  CA BSER A 476     3878   4350   5603   -662   -202  -1118       C  
ATOM     40  C   SER A 476      47.459  37.884  18.560  1.00 38.35           C  
ANISOU   40  C   SER A 476     4024   4668   5878   -605   -241  -1117       C  
ATOM     41  O   SER A 476      48.125  37.721  17.522  1.00 39.75           O  
ANISOU   41  O   SER A 476     4102   4863   6138   -644   -160  -1133       O  
ATOM     42  CB ASER A 476      48.148  39.967  19.706  0.50 37.88           C  
ANISOU   42  CB ASER A 476     3976   4528   5887   -734   -276  -1237       C  
ATOM     43  CB BSER A 476      48.079  40.121  19.557  0.50 37.40           C  
ANISOU   43  CB BSER A 476     3923   4457   5828   -744   -253  -1230       C  
ATOM     44  OG ASER A 476      47.795  41.264  20.104  0.50 38.56           O  
ANISOU   44  OG ASER A 476     4147   4542   5964   -790   -248  -1256       O  
ATOM     45  OG BSER A 476      48.533  39.518  20.746  0.50 37.67           O  
ANISOU   45  OG BSER A 476     3925   4539   5850   -699   -412  -1291       O  
ATOM     46  N   HIS A 477      47.171  36.884  19.383  1.00 40.46           N  
ANISOU   46  N   HIS A 477     4319   4974   6080   -519   -361  -1103       N  
ATOM     47  CA  HIS A 477      47.552  35.508  19.117  1.00 43.26           C  
ANISOU   47  CA  HIS A 477     4596   5379   6463   -452   -418  -1099       C  
ATOM     48  C   HIS A 477      46.793  34.905  17.921  1.00 42.34           C  
ANISOU   48  C   HIS A 477     4511   5269   6306   -419   -306  -1014       C  
ATOM     49  O   HIS A 477      47.352  34.192  17.112  1.00 42.13           O  
ANISOU   49  O   HIS A 477     4385   5271   6349   -407   -275  -1035       O  
ATOM     50  CB  HIS A 477      47.301  34.659  20.361  1.00 45.73           C  
ANISOU   50  CB  HIS A 477     4966   5712   6697   -377   -582  -1086       C  
ATOM     51  CG  HIS A 477      47.978  33.327  20.330  1.00 49.43           C  
ANISOU   51  CG  HIS A 477     5340   6214   7228   -310   -686  -1104       C  
ATOM     52  ND1 HIS A 477      49.316  33.176  20.624  1.00 52.54           N  
ANISOU   52  ND1 HIS A 477     5589   6622   7753   -315   -789  -1204       N  
ATOM     53  CD2 HIS A 477      47.514  32.085  20.027  1.00 50.40           C  
ANISOU   53  CD2 HIS A 477     5485   6349   7315   -232   -709  -1042       C  
ATOM     54  CE1 HIS A 477      49.646  31.897  20.515  1.00 53.23           C  
ANISOU   54  CE1 HIS A 477     5614   6724   7887   -235   -877  -1203       C  
ATOM     55  NE2 HIS A 477      48.570  31.214  20.164  1.00 51.37           N  
ANISOU   55  NE2 HIS A 477     5484   6485   7549   -187   -830  -1104       N  
ATOM     56  N   CYS A 478      45.514  35.203  17.828  1.00 40.36           N  
ANISOU   56  N   CYS A 478     4394   4994   5948   -405   -248   -930       N  
ATOM     57  CA  CYS A 478      44.652  34.722  16.736  1.00 39.37           C  
ANISOU   57  CA  CYS A 478     4314   4872   5772   -377   -152   -845       C  
ATOM     58  C   CYS A 478      44.699  35.633  15.573  1.00 39.87           C  
ANISOU   58  C   CYS A 478     4375   4906   5868   -453    -13   -829       C  
ATOM     59  O   CYS A 478      44.484  35.198  14.426  1.00 38.23           O  
ANISOU   59  O   CYS A 478     4163   4714   5649   -452     70   -786       O  
ATOM     60  CB  CYS A 478      43.193  34.767  17.176  1.00 38.67           C  
ANISOU   60  CB  CYS A 478     4365   4766   5560   -333   -153   -766       C  
ATOM     61  SG  CYS A 478      42.985  33.768  18.618  1.00 39.22           S  
ANISOU   61  SG  CYS A 478     4475   4869   5557   -265   -306   -768       S  
ATOM     62  N   LEU A 479      44.808  36.922  15.886  1.00 36.59           N  
ANISOU   62  N   LEU A 479     3990   4439   5473   -519     10   -852       N  
ATOM     63  CA  LEU A 479      44.746  37.952  14.898  1.00 37.81           C  
ANISOU   63  CA  LEU A 479     4175   4543   5649   -600    131   -821       C  
ATOM     64  C   LEU A 479      45.977  38.797  15.051  1.00 39.73           C  
ANISOU   64  C   LEU A 479     4331   4767   5998   -698    142   -910       C  
ATOM     65  O   LEU A 479      45.903  39.860  15.659  1.00 39.34           O  
ANISOU   65  O   LEU A 479     4330   4656   5961   -738    127   -931       O  
ATOM     66  CB  LEU A 479      43.475  38.785  15.138  1.00 37.87           C  
ANISOU   66  CB  LEU A 479     4322   4483   5585   -582    144   -756       C  
ATOM     67  CG  LEU A 479      42.200  38.071  14.739  1.00 37.60           C  
ANISOU   67  CG  LEU A 479     4365   4465   5458   -502    156   -666       C  
ATOM     68  CD1 LEU A 479      40.968  38.880  15.056  1.00 38.69           C  
ANISOU   68  CD1 LEU A 479     4616   4538   5547   -475    162   -622       C  
ATOM     69  CD2 LEU A 479      42.237  37.788  13.249  1.00 37.97           C  
ANISOU   69  CD2 LEU A 479     4402   4523   5501   -531    250   -610       C  
ATOM     70  N   PRO A 480      47.128  38.312  14.528  1.00 39.66           N  
ANISOU   70  N   PRO A 480     4185   4810   6076   -737    169   -974       N  
ATOM     71  CA  PRO A 480      48.263  39.231  14.408  1.00 41.30           C  
ANISOU   71  CA  PRO A 480     4304   4996   6391   -856    215  -1053       C  
ATOM     72  C   PRO A 480      47.883  40.421  13.498  1.00 42.44           C  
ANISOU   72  C   PRO A 480     4546   5065   6515   -956    344   -985       C  
ATOM     73  O   PRO A 480      46.829  40.395  12.831  1.00 41.86           O  
ANISOU   73  O   PRO A 480     4588   4966   6349   -926    394   -879       O  
ATOM     74  CB  PRO A 480      49.389  38.362  13.815  1.00 41.16           C  
ANISOU   74  CB  PRO A 480     4118   5056   6464   -871    244  -1131       C  
ATOM     75  CG  PRO A 480      48.791  37.050  13.484  1.00 41.09           C  
ANISOU   75  CG  PRO A 480     4126   5096   6391   -764    224  -1083       C  
ATOM     76  CD  PRO A 480      47.498  36.921  14.238  1.00 39.67           C  
ANISOU   76  CD  PRO A 480     4093   4886   6096   -672    142   -997       C  
ATOM     77  N   THR A 481      48.693  41.463  13.510  1.00 43.34           N  
ANISOU   77  N   THR A 481     4619   5135   6714  -1074    384  -1040       N  
ATOM     78  CA  THR A 481      48.300  42.759  12.918  1.00 44.96           C  
ANISOU   78  CA  THR A 481     4942   5238   6904  -1170    474   -971       C  
ATOM     79  C   THR A 481      47.779  42.666  11.492  1.00 42.81           C  
ANISOU   79  C   THR A 481     4747   4961   6558  -1203    593   -862       C  
ATOM     80  O   THR A 481      46.758  43.265  11.165  1.00 39.61           O  
ANISOU   80  O   THR A 481     4489   4475   6085  -1192    608   -760       O  
ATOM     81  CB  THR A 481      49.488  43.724  12.885  1.00 48.92           C  
ANISOU   81  CB  THR A 481     5362   5704   7521  -1320    524  -1052       C  
ATOM     82  OG1 THR A 481      50.061  43.778  14.192  1.00 51.99           O  
ANISOU   82  OG1 THR A 481     5668   6105   7980  -1295    403  -1163       O  
ATOM     83  CG2 THR A 481      49.057  45.135  12.437  1.00 50.32           C  
ANISOU   83  CG2 THR A 481     5679   5750   7689  -1419    593   -976       C  
ATOM     84  N   GLU A 482      48.530  41.934  10.659  1.00 41.67           N  
ANISOU   84  N   GLU A 482     4497   4902   6434  -1245    672   -896       N  
ATOM     85  CA AGLU A 482      48.183  41.878   9.240  0.50 41.65           C  
ANISOU   85  CA AGLU A 482     4569   4905   6353  -1301    796   -805       C  
ATOM     86  CA BGLU A 482      48.266  41.736   9.244  0.50 41.45           C  
ANISOU   86  CA BGLU A 482     4525   4893   6332  -1296    795   -816       C  
ATOM     87  C   GLU A 482      46.849  41.182   9.071  1.00 39.02           C  
ANISOU   87  C   GLU A 482     4344   4578   5903  -1171    749   -707       C  
ATOM     88  O   GLU A 482      46.035  41.664   8.295  1.00 39.24           O  
ANISOU   88  O   GLU A 482     4510   4549   5850  -1195    794   -595       O  
ATOM     89  CB AGLU A 482      49.254  41.233   8.354  0.50 43.47           C  
ANISOU   89  CB AGLU A 482     4661   5234   6622  -1380    907   -878       C  
ATOM     90  CB BGLU A 482      49.298  40.712   8.696  0.50 42.48           C  
ANISOU   90  CB BGLU A 482     4488   5142   6512  -1320    861   -911       C  
ATOM     91  CG AGLU A 482      48.969  41.407   6.855  0.50 44.40           C  
ANISOU   91  CG AGLU A 482     4878   5352   6641  -1476   1050   -785       C  
ATOM     92  CG BGLU A 482      50.766  41.174   8.739  0.50 44.64           C  
ANISOU   92  CG BGLU A 482     4604   5438   6918  -1451    922  -1035       C  
ATOM     93  CD AGLU A 482      49.014  42.857   6.400  0.50 46.06           C  
ANISOU   93  CD AGLU A 482     5203   5456   6843  -1628   1125   -714       C  
ATOM     94  CD BGLU A 482      51.458  41.008  10.099  0.50 45.22           C  
ANISOU   94  CD BGLU A 482     4542   5528   7111  -1393    787  -1156       C  
ATOM     95  OE1AGLU A 482      50.110  43.451   6.441  0.50 47.07           O  
ANISOU   95  OE1AGLU A 482     5238   5581   7066  -1761   1190   -794       O  
ATOM     96  OE1BGLU A 482      50.886  40.363  11.010  0.50 44.17           O  
ANISOU   96  OE1BGLU A 482     4430   5402   6949  -1249    647  -1149       O  
ATOM     97  OE2AGLU A 482      47.965  43.395   5.975  0.50 45.62           O  
ANISOU   97  OE2AGLU A 482     5327   5316   6691  -1619   1115   -579       O  
ATOM     98  OE2BGLU A 482      52.591  41.537  10.258  0.50 48.19           O  
ANISOU   98  OE2BGLU A 482     4794   5910   7607  -1502    819  -1259       O  
ATOM     99  N   LYS A 483      46.600  40.135   9.835  1.00 36.24           N  
ANISOU   99  N   LYS A 483     3939   4285   5546  -1041    650   -744       N  
ATOM    100  CA  LYS A 483      45.344  39.400   9.804  1.00 34.30           C  
ANISOU  100  CA  LYS A 483     3783   4050   5201   -920    600   -663       C  
ATOM    101  C   LYS A 483      44.181  40.242  10.358  1.00 33.16           C  
ANISOU  101  C   LYS A 483     3777   3812   5012   -876    544   -589       C  
ATOM    102  O   LYS A 483      43.060  40.274   9.830  1.00 31.06           O  
ANISOU  102  O   LYS A 483     3621   3514   4666   -834    552   -491       O  
ATOM    103  CB  LYS A 483      45.559  38.170  10.652  1.00 35.38           C  
ANISOU  103  CB  LYS A 483     3822   4260   5362   -813    502   -732       C  
ATOM    104  CG  LYS A 483      44.521  37.115  10.521  1.00 35.33           C  
ANISOU  104  CG  LYS A 483     3871   4286   5268   -702    463   -669       C  
ATOM    105  CD  LYS A 483      45.013  35.842  11.178  1.00 35.79           C  
ANISOU  105  CD  LYS A 483     3822   4412   5366   -620    376   -742       C  
ATOM    106  CE  LYS A 483      43.951  34.761  11.144  1.00 34.81           C  
ANISOU  106  CE  LYS A 483     3758   4311   5157   -515    330   -678       C  
ATOM    107  NZ  LYS A 483      44.548  33.550  11.768  1.00 35.61           N  
ANISOU  107  NZ  LYS A 483     3760   4462   5310   -444    237   -748       N  
ATOM    108  N   LEU A 484      44.463  40.925  11.450  1.00 33.00           N  
ANISOU  108  N   LEU A 484     3741   3747   5051   -883    482   -648       N  
ATOM    109  CA  LEU A 484      43.507  41.846  12.046  1.00 33.20           C  
ANISOU  109  CA  LEU A 484     3880   3678   5056   -850    438   -609       C  
ATOM    110  C   LEU A 484      43.143  42.990  11.078  1.00 33.28           C  
ANISOU  110  C   LEU A 484     4000   3584   5061   -930    511   -522       C  
ATOM    111  O   LEU A 484      41.974  43.319  10.911  1.00 32.09           O  
ANISOU  111  O   LEU A 484     3959   3370   4862   -874    492   -443       O  
ATOM    112  CB  LEU A 484      44.165  42.440  13.298  1.00 36.34           C  
ANISOU  112  CB  LEU A 484     4229   4052   5528   -873    373   -712       C  
ATOM    113  CG  LEU A 484      43.266  43.190  14.237  1.00 37.08           C  
ANISOU  113  CG  LEU A 484     4414   4068   5605   -821    313   -714       C  
ATOM    114  CD1 LEU A 484      42.107  42.336  14.747  1.00 37.28           C  
ANISOU  114  CD1 LEU A 484     4483   4139   5541   -693    257   -682       C  
ATOM    115  CD2 LEU A 484      44.141  43.737  15.377  1.00 39.15           C  
ANISOU  115  CD2 LEU A 484     4618   4318   5939   -865    254   -830       C  
ATOM    116  N   GLN A 485      44.162  43.572  10.433  1.00 34.10           N  
ANISOU  116  N   GLN A 485     4072   3668   5217  -1065    592   -538       N  
ATOM    117  CA  GLN A 485      43.989  44.673   9.451  1.00 36.35           C  
ANISOU  117  CA  GLN A 485     4471   3846   5493  -1169    663   -447       C  
ATOM    118  C   GLN A 485      43.176  44.281   8.254  1.00 35.85           C  
ANISOU  118  C   GLN A 485     4501   3793   5327  -1149    703   -328       C  
ATOM    119  O   GLN A 485      42.632  45.155   7.565  1.00 36.52           O  
ANISOU  119  O   GLN A 485     4717   3774   5385  -1194    721   -227       O  
ATOM    120  CB  GLN A 485      45.337  45.220   8.938  1.00 38.56           C  
ANISOU  120  CB  GLN A 485     4690   4124   5839  -1339    760   -490       C  
ATOM    121  CG  GLN A 485      46.047  46.082   9.962  1.00 41.11           C  
ANISOU  121  CG  GLN A 485     4960   4387   6272  -1392    722   -587       C  
ATOM    122  CD  GLN A 485      47.469  46.419   9.555  1.00 43.96           C  
ANISOU  122  CD  GLN A 485     5221   4771   6713  -1558    816   -655       C  
ATOM    123  OE1 GLN A 485      48.137  45.627   8.903  1.00 46.32           O  
ANISOU  123  OE1 GLN A 485     5421   5176   7001  -1599    891   -685       O  
ATOM    124  NE2 GLN A 485      47.936  47.600   9.941  1.00 46.52           N  
ANISOU  124  NE2 GLN A 485     5561   4991   7121  -1659    816   -689       N  
ATOM    125  N   ARG A 486      43.143  42.990   7.962  1.00 32.54           N  
ANISOU  125  N   ARG A 486     4017   3492   4853  -1089    712   -340       N  
ATOM    126  CA  ARG A 486      42.378  42.522   6.819  1.00 33.69           C  
ANISOU  126  CA  ARG A 486     4247   3659   4894  -1070    744   -238       C  
ATOM    127  C   ARG A 486      40.985  42.030   7.148  1.00 29.81           C  
ANISOU  127  C   ARG A 486     3814   3164   4349   -922    655   -186       C  
ATOM    128  O   ARG A 486      40.314  41.568   6.272  1.00 29.87           O  
ANISOU  128  O   ARG A 486     3881   3194   4273   -898    667   -110       O  
ATOM    129  CB  ARG A 486      43.199  41.507   6.040  1.00 35.78           C  
ANISOU  129  CB  ARG A 486     4419   4046   5131  -1119    830   -281       C  
ATOM    130  CG  ARG A 486      44.464  42.167   5.567  1.00 41.13           C  
ANISOU  130  CG  ARG A 486     5051   4719   5859  -1286    938   -324       C  
ATOM    131  CD  ARG A 486      45.300  41.234   4.738  1.00 45.00           C  
ANISOU  131  CD  ARG A 486     5440   5330   6328  -1343   1041   -383       C  
ATOM    132  NE  ARG A 486      44.746  41.194   3.386  1.00 49.40           N  
ANISOU  132  NE  ARG A 486     6123   5891   6756  -1395   1111   -276       N  
ATOM    133  CZ  ARG A 486      45.439  40.903   2.286  1.00 53.87           C  
ANISOU  133  CZ  ARG A 486     6665   6532   7272  -1512   1244   -297       C  
ATOM    134  NH1 ARG A 486      44.825  40.910   1.096  1.00 55.51           N  
ANISOU  134  NH1 ARG A 486     7013   6739   7341  -1558   1292   -189       N  
ATOM    135  NH2 ARG A 486      46.735  40.596   2.359  1.00 55.02           N  
ANISOU  135  NH2 ARG A 486     6645   6756   7503  -1584   1328   -430       N  
ATOM    136  N   CYS A 487      40.498  42.216   8.390  1.00 28.68           N  
ANISOU  136  N   CYS A 487     3660   2988   4249   -833    569   -228       N  
ATOM    137  CA  CYS A 487      39.173  41.701   8.764  1.00 26.56           C  
ANISOU  137  CA  CYS A 487     3431   2727   3933   -700    497   -193       C  
ATOM    138  C   CYS A 487      38.032  42.506   8.131  1.00 27.55           C  
ANISOU  138  C   CYS A 487     3686   2749   4033   -680    478    -87       C  
ATOM    139  O   CYS A 487      38.074  43.754   8.175  1.00 26.41           O  
ANISOU  139  O   CYS A 487     3606   2487   3942   -730    475    -69       O  
ATOM    140  CB  CYS A 487      38.977  41.627  10.291  1.00 26.71           C  
ANISOU  140  CB  CYS A 487     3404   2754   3992   -621    424   -277       C  
ATOM    141  SG  CYS A 487      39.874  40.159  11.066  1.00 29.20           S  
ANISOU  141  SG  CYS A 487     3579   3207   4307   -588    396   -375       S  
ATOM    142  N   GLU A 488      37.063  41.775   7.543  1.00 24.77           N  
ANISOU  142  N   GLU A 488     3368   2435   3607   -609    457    -22       N  
ATOM    143  CA  GLU A 488      35.750  42.273   7.049  1.00 25.41           C  
ANISOU  143  CA  GLU A 488     3554   2434   3666   -552    408     72       C  
ATOM    144  C   GLU A 488      34.622  41.467   7.645  1.00 21.91           C  
ANISOU  144  C   GLU A 488     3079   2042   3205   -423    349     55       C  
ATOM    145  O   GLU A 488      34.679  40.227   7.659  1.00 19.88           O  
ANISOU  145  O   GLU A 488     2760   1895   2899   -393    357     31       O  
ATOM    146  CB  GLU A 488      35.651  42.115   5.556  1.00 28.94           C  
ANISOU  146  CB  GLU A 488     4077   2888   4030   -609    439    173       C  
ATOM    147  CG  GLU A 488      36.582  43.121   4.906  1.00 34.86           C  
ANISOU  147  CG  GLU A 488     4888   3566   4792   -751    501    209       C  
ATOM    148  CD  GLU A 488      36.734  42.948   3.420  1.00 39.65           C  
ANISOU  148  CD  GLU A 488     5574   4196   5294   -841    554    300       C  
ATOM    149  OE1 GLU A 488      36.862  41.772   2.968  1.00 45.02           O  
ANISOU  149  OE1 GLU A 488     6203   4999   5903   -831    591    280       O  
ATOM    150  OE2 GLU A 488      36.809  44.002   2.733  1.00 44.17           O  
ANISOU  150  OE2 GLU A 488     6264   4662   5855   -931    563    387       O  
ATOM    151  N   LYS A 489      33.557  42.140   8.102  1.00 19.76           N  
ANISOU  151  N   LYS A 489     2846   1687   2976   -348    290     64       N  
ATOM    152  CA  LYS A 489      32.510  41.403   8.825  1.00 18.14           C  
ANISOU  152  CA  LYS A 489     2595   1537   2760   -237    249     29       C  
ATOM    153  C   LYS A 489      31.592  40.768   7.794  1.00 18.11           C  
ANISOU  153  C   LYS A 489     2623   1562   2695   -196    225    112       C  
ATOM    154  O   LYS A 489      31.212  41.450   6.808  1.00 20.29           O  
ANISOU  154  O   LYS A 489     2983   1756   2968   -212    200    200       O  
ATOM    155  CB  LYS A 489      31.687  42.313   9.753  1.00 17.92           C  
ANISOU  155  CB  LYS A 489     2577   1422   2809   -169    207    -18       C  
ATOM    156  CG  LYS A 489      30.570  41.558  10.453  1.00 17.07           C  
ANISOU  156  CG  LYS A 489     2421   1381   2686    -70    182    -58       C  
ATOM    157  CD  LYS A 489      29.813  42.418  11.423  1.00 17.88           C  
ANISOU  157  CD  LYS A 489     2518   1411   2864     -8    159   -128       C  
ATOM    158  CE  LYS A 489      28.422  41.857  11.690  1.00 17.46           C  
ANISOU  158  CE  LYS A 489     2427   1402   2805     87    138   -144       C  
ATOM    159  NZ  LYS A 489      27.723  42.688  12.720  1.00 18.44           N  
ANISOU  159  NZ  LYS A 489     2533   1467   3008    144    132   -239       N  
ATOM    160  N   ILE A 490      31.251  39.521   7.993  1.00 17.21           N  
ANISOU  160  N   ILE A 490     2453   1554   2533   -150    223     91       N  
ATOM    161  CA  ILE A 490      30.392  38.761   7.094  1.00 17.45           C  
ANISOU  161  CA  ILE A 490     2501   1625   2504   -112    198    155       C  
ATOM    162  C   ILE A 490      29.117  38.193   7.678  1.00 18.23           C  
ANISOU  162  C   ILE A 490     2558   1757   2611    -16    156    131       C  
ATOM    163  O   ILE A 490      28.318  37.571   6.951  1.00 19.96           O  
ANISOU  163  O   ILE A 490     2785   2008   2790     16    126    179       O  
ATOM    164  CB  ILE A 490      31.206  37.657   6.382  1.00 17.72           C  
ANISOU  164  CB  ILE A 490     2514   1756   2463   -167    244    162       C  
ATOM    165  CG1 ILE A 490      31.761  36.597   7.339  1.00 17.31           C  
ANISOU  165  CG1 ILE A 490     2373   1794   2411   -152    262     79       C  
ATOM    166  CG2 ILE A 490      32.298  38.307   5.546  1.00 18.65           C  
ANISOU  166  CG2 ILE A 490     2679   1840   2567   -274    296    193       C  
ATOM    167  CD1 ILE A 490      32.467  35.427   6.662  1.00 17.14           C  
ANISOU  167  CD1 ILE A 490     2318   1859   2336   -187    297     71       C  
ATOM    168  N   GLY A 491      28.944  38.243   8.985  1.00 16.64           N  
ANISOU  168  N   GLY A 491     2307   1566   2450     21    158     52       N  
ATOM    169  CA  GLY A 491      27.782  37.614   9.559  1.00 16.91           C  
ANISOU  169  CA  GLY A 491     2296   1646   2482     94    138     23       C  
ATOM    170  C   GLY A 491      27.634  37.975  11.032  1.00 16.22           C  
ANISOU  170  C   GLY A 491     2173   1557   2434    118    152    -70       C  
ATOM    171  O   GLY A 491      28.608  38.438  11.662  1.00 15.74           O  
ANISOU  171  O   GLY A 491     2116   1479   2387     75    172   -116       O  
ATOM    172  N   GLU A 492      26.444  37.728  11.582  1.00 16.14           N  
ANISOU  172  N   GLU A 492     2125   1571   2437    179    144   -105       N  
ATOM    173  CA  GLU A 492      26.186  37.979  12.990  1.00 16.13           C  
ANISOU  173  CA  GLU A 492     2093   1583   2453    195    170   -203       C  
ATOM    174  C   GLU A 492      25.009  37.167  13.471  1.00 15.70           C  
ANISOU  174  C   GLU A 492     1987   1601   2376    235    182   -232       C  
ATOM    175  O   GLU A 492      24.177  36.701  12.668  1.00 14.75           O  
ANISOU  175  O   GLU A 492     1850   1495   2260    268    159   -183       O  
ATOM    176  CB  GLU A 492      25.899  39.470  13.255  1.00 18.18           C  
ANISOU  176  CB  GLU A 492     2367   1731   2809    225    162   -249       C  
ATOM    177  CG  GLU A 492      24.631  39.982  12.512  1.00 19.59           C  
ANISOU  177  CG  GLU A 492     2537   1841   3063    300    120   -218       C  
ATOM    178  CD  GLU A 492      24.258  41.402  12.814  1.00 21.48           C  
ANISOU  178  CD  GLU A 492     2786   1958   3416    344    102   -272       C  
ATOM    179  OE1 GLU A 492      25.129  42.313  12.766  1.00 22.31           O  
ANISOU  179  OE1 GLU A 492     2945   1977   3554    305     96   -267       O  
ATOM    180  OE2 GLU A 492      23.036  41.619  13.107  1.00 22.54           O  
ANISOU  180  OE2 GLU A 492     2865   2079   3620    420     93   -328       O  
ATOM    181  N   GLY A 493      24.930  37.006  14.786  1.00 15.28           N  
ANISOU  181  N   GLY A 493     1915   1597   2294    225    220   -315       N  
ATOM    182  CA  GLY A 493      23.769  36.433  15.448  1.00 15.40           C  
ANISOU  182  CA  GLY A 493     1882   1678   2291    248    251   -362       C  
ATOM    183  C   GLY A 493      23.706  37.002  16.848  1.00 15.99           C  
ANISOU  183  C   GLY A 493     1953   1761   2361    237    298   -473       C  
ATOM    184  O   GLY A 493      24.593  37.769  17.249  1.00 16.14           O  
ANISOU  184  O   GLY A 493     2007   1735   2392    214    294   -508       O  
ATOM    185  N  AVAL A 494      22.683  36.589  17.598  0.50 16.21           N  
ANISOU  185  N  AVAL A 494     1939   1854   2366    243    347   -535       N  
ATOM    186  N  BVAL A 494      22.688  36.636  17.614  0.50 16.28           N  
ANISOU  186  N  BVAL A 494     1947   1860   2377    244    347   -537       N  
ATOM    187  CA AVAL A 494      22.487  37.023  19.008  0.50 17.02           C  
ANISOU  187  CA AVAL A 494     2040   1987   2442    222    408   -655       C  
ATOM    188  CA BVAL A 494      22.551  37.249  18.950  0.50 17.12           C  
ANISOU  188  CA BVAL A 494     2053   1980   2470    229    404   -659       C  
ATOM    189  C  AVAL A 494      23.756  36.957  19.835  0.50 16.79           C  
ANISOU  189  C  AVAL A 494     2076   1978   2324    157    399   -669       C  
ATOM    190  C  BVAL A 494      23.776  36.990  19.848  0.50 16.84           C  
ANISOU  190  C  BVAL A 494     2084   1983   2332    157    399   -671       C  
ATOM    191  O  AVAL A 494      24.042  37.877  20.632  0.50 17.39           O  
ANISOU  191  O  AVAL A 494     2171   2025   2413    148    419   -760       O  
ATOM    192  O  BVAL A 494      24.065  37.840  20.712  0.50 17.42           O  
ANISOU  192  O  BVAL A 494     2177   2034   2409    144    421   -763       O  
ATOM    193  CB AVAL A 494      21.413  36.153  19.667  0.50 17.43           C  
ANISOU  193  CB AVAL A 494     2051   2139   2435    202    473   -695       C  
ATOM    194  CB BVAL A 494      21.253  36.826  19.645  0.50 17.91           C  
ANISOU  194  CB BVAL A 494     2096   2158   2553    231    476   -733       C  
ATOM    195  CG1AVAL A 494      21.335  36.380  21.196  0.50 18.34           C  
ANISOU  195  CG1AVAL A 494     2184   2309   2475    153    547   -813       C  
ATOM    196  CG1BVAL A 494      21.214  35.324  19.763  0.50 17.34           C  
ANISOU  196  CG1BVAL A 494     2039   2184   2366    173    484   -667       C  
ATOM    197  CG2AVAL A 494      20.094  36.435  18.991  0.50 18.06           C  
ANISOU  197  CG2AVAL A 494     2043   2193   2627    273    481   -713       C  
ATOM    198  CG2BVAL A 494      21.104  37.516  21.016  0.50 19.01           C  
ANISOU  198  CG2BVAL A 494     2238   2316   2669    209    547   -873       C  
ATOM    199  N   PHE A 495      24.536  35.911  19.629  1.00 15.89           N  
ANISOU  199  N   PHE A 495     1995   1909   2132    115    361   -587       N  
ATOM    200  CA  PHE A 495      25.700  35.693  20.477  1.00 16.37           C  
ANISOU  200  CA  PHE A 495     2111   1999   2112     57    336   -601       C  
ATOM    201  C   PHE A 495      27.036  35.656  19.795  1.00 16.08           C  
ANISOU  201  C   PHE A 495     2091   1923   2095     44    272   -539       C  
ATOM    202  O   PHE A 495      28.012  35.253  20.418  1.00 16.56           O  
ANISOU  202  O   PHE A 495     2183   2014   2094      0    235   -543       O  
ATOM    203  CB  PHE A 495      25.536  34.610  21.562  1.00 17.61           C  
ANISOU  203  CB  PHE A 495     2303   2254   2136      0    352   -610       C  
ATOM    204  CG  PHE A 495      25.403  33.178  21.057  1.00 17.36           C  
ANISOU  204  CG  PHE A 495     2271   2267   2057    -12    326   -513       C  
ATOM    205  CD1 PHE A 495      26.527  32.430  20.647  1.00 17.73           C  
ANISOU  205  CD1 PHE A 495     2342   2309   2085    -25    252   -439       C  
ATOM    206  CD2 PHE A 495      24.172  32.546  21.094  1.00 18.98           C  
ANISOU  206  CD2 PHE A 495     2451   2521   2239    -15    377   -508       C  
ATOM    207  CE1 PHE A 495      26.403  31.096  20.233  1.00 17.93           C  
ANISOU  207  CE1 PHE A 495     2372   2367   2074    -34    225   -361       C  
ATOM    208  CE2 PHE A 495      24.046  31.204  20.695  1.00 19.10           C  
ANISOU  208  CE2 PHE A 495     2474   2572   2212    -34    351   -424       C  
ATOM    209  CZ  PHE A 495      25.150  30.489  20.261  1.00 18.34           C  
ANISOU  209  CZ  PHE A 495     2409   2460   2100    -41    274   -351       C  
ATOM    210  N   GLY A 496      27.118  36.208  18.613  1.00 15.77           N  
ANISOU  210  N   GLY A 496     2033   1814   2146     77    259   -494       N  
ATOM    211  CA  GLY A 496      28.412  36.167  17.905  1.00 16.10           C  
ANISOU  211  CA  GLY A 496     2084   1826   2206     52    217   -442       C  
ATOM    212  C   GLY A 496      28.520  37.044  16.692  1.00 15.66           C  
ANISOU  212  C   GLY A 496     2027   1684   2240     71    214   -400       C  
ATOM    213  O   GLY A 496      27.512  37.541  16.161  1.00 15.48           O  
ANISOU  213  O   GLY A 496     1996   1617   2270    117    225   -388       O  
ATOM    214  N   GLU A 497      29.770  37.200  16.268  1.00 15.05           N  
ANISOU  214  N   GLU A 497     1957   1584   2179     30    194   -379       N  
ATOM    215  CA  GLU A 497      30.135  38.016  15.118  1.00 15.38           C  
ANISOU  215  CA  GLU A 497     2012   1544   2286     19    196   -331       C  
ATOM    216  C   GLU A 497      31.046  37.130  14.267  1.00 14.81           C  
ANISOU  216  C   GLU A 497     1927   1515   2186    -17    189   -274       C  
ATOM    217  O   GLU A 497      31.854  36.375  14.826  1.00 14.19           O  
ANISOU  217  O   GLU A 497     1824   1496   2073    -41    173   -301       O  
ATOM    218  CB  GLU A 497      30.890  39.289  15.559  1.00 16.82           C  
ANISOU  218  CB  GLU A 497     2212   1650   2529    -18    197   -389       C  
ATOM    219  CG  GLU A 497      30.038  40.186  16.510  1.00 18.56           C  
ANISOU  219  CG  GLU A 497     2443   1825   2784     19    207   -472       C  
ATOM    220  CD  GLU A 497      29.008  41.077  15.791  1.00 20.43           C  
ANISOU  220  CD  GLU A 497     2696   1966   3102     73    207   -445       C  
ATOM    221  OE1 GLU A 497      29.105  41.140  14.546  1.00 21.62           O  
ANISOU  221  OE1 GLU A 497     2867   2075   3273     68    193   -353       O  
ATOM    222  OE2 GLU A 497      28.120  41.752  16.470  1.00 20.25           O  
ANISOU  222  OE2 GLU A 497     2665   1903   3125    121    219   -522       O  
ATOM    223  N   VAL A 498      30.894  37.190  12.964  1.00 13.78           N  
ANISOU  223  N   VAL A 498     1812   1357   2068    -18    197   -201       N  
ATOM    224  CA  VAL A 498      31.757  36.434  12.050  1.00 13.16           C  
ANISOU  224  CA  VAL A 498     1719   1318   1963    -57    207   -161       C  
ATOM    225  C   VAL A 498      32.473  37.383  11.078  1.00 13.73           C  
ANISOU  225  C   VAL A 498     1821   1323   2072   -116    233   -127       C  
ATOM    226  O   VAL A 498      31.810  38.267  10.442  1.00 13.86           O  
ANISOU  226  O   VAL A 498     1891   1264   2113   -106    230    -78       O  
ATOM    227  CB  VAL A 498      30.967  35.405  11.225  1.00 13.11           C  
ANISOU  227  CB  VAL A 498     1713   1358   1909    -23    201   -102       C  
ATOM    228  CG1 VAL A 498      31.889  34.514  10.397  1.00 13.60           C  
ANISOU  228  CG1 VAL A 498     1754   1470   1944    -60    216    -84       C  
ATOM    229  CG2 VAL A 498      30.051  34.522  12.114  1.00 13.30           C  
ANISOU  229  CG2 VAL A 498     1717   1439   1899     26    181   -124       C  
ATOM    230  N   PHE A 499      33.802  37.199  10.938  1.00 13.13           N  
ANISOU  230  N   PHE A 499     1711   1274   2004   -179    256   -153       N  
ATOM    231  CA  PHE A 499      34.627  38.040  10.083  1.00 14.19           C  
ANISOU  231  CA  PHE A 499     1868   1356   2168   -258    297   -130       C  
ATOM    232  C   PHE A 499      35.366  37.150   9.091  1.00 15.00           C  
ANISOU  232  C   PHE A 499     1939   1526   2235   -301    338   -114       C  
ATOM    233  O   PHE A 499      35.575  35.949   9.393  1.00 15.08           O  
ANISOU  233  O   PHE A 499     1891   1615   2226   -269    322   -149       O  
ATOM    234  CB  PHE A 499      35.672  38.793  10.882  1.00 14.83           C  
ANISOU  234  CB  PHE A 499     1919   1406   2310   -312    303   -202       C  
ATOM    235  CG  PHE A 499      35.091  39.737  11.945  1.00 15.30           C  
ANISOU  235  CG  PHE A 499     2008   1397   2408   -278    269   -242       C  
ATOM    236  CD1 PHE A 499      34.745  39.260  13.182  1.00 15.26           C  
ANISOU  236  CD1 PHE A 499     1976   1440   2384   -225    232   -303       C  
ATOM    237  CD2 PHE A 499      34.838  41.035  11.627  1.00 16.18           C  
ANISOU  237  CD2 PHE A 499     2181   1398   2569   -301    277   -217       C  
ATOM    238  CE1 PHE A 499      34.190  40.098  14.137  1.00 15.64           C  
ANISOU  238  CE1 PHE A 499     2049   1434   2459   -198    214   -355       C  
ATOM    239  CE2 PHE A 499      34.268  41.902  12.587  1.00 17.16           C  
ANISOU  239  CE2 PHE A 499     2327   1454   2740   -263    249   -269       C  
ATOM    240  CZ  PHE A 499      33.964  41.396  13.828  1.00 16.62           C  
ANISOU  240  CZ  PHE A 499     2222   1447   2647   -213    225   -345       C  
ATOM    241  N   GLN A 500      35.647  37.697   7.929  1.00 15.33           N  
ANISOU  241  N   GLN A 500     2028   1534   2264   -370    386    -61       N  
ATOM    242  CA AGLN A 500      36.564  37.104   6.958  0.50 16.31           C  
ANISOU  242  CA AGLN A 500     2120   1719   2360   -438    449    -67       C  
ATOM    243  CA BGLN A 500      36.584  37.073   7.013  0.50 16.01           C  
ANISOU  243  CA BGLN A 500     2077   1682   2323   -436    448    -71       C  
ATOM    244  C   GLN A 500      37.901  37.820   7.076  1.00 16.70           C  
ANISOU  244  C   GLN A 500     2127   1748   2469   -535    501   -120       C  
ATOM    245  O   GLN A 500      37.967  39.045   7.230  1.00 16.92           O  
ANISOU  245  O   GLN A 500     2204   1689   2535   -581    505   -103       O  
ATOM    246  CB AGLN A 500      35.983  37.221   5.519  0.50 17.54           C  
ANISOU  246  CB AGLN A 500     2367   1860   2439   -469    477     28       C  
ATOM    247  CB BGLN A 500      36.013  36.988   5.579  0.50 16.70           C  
ANISOU  247  CB BGLN A 500     2245   1770   2331   -460    475     18       C  
ATOM    248  CG AGLN A 500      36.809  36.536   4.432  0.50 18.98           C  
ANISOU  248  CG AGLN A 500     2525   2117   2571   -542    556     16       C  
ATOM    249  CG BGLN A 500      35.868  38.316   4.868  0.50 18.15           C  
ANISOU  249  CG BGLN A 500     2534   1858   2506   -529    492     97       C  
ATOM    250  CD AGLN A 500      36.242  36.751   3.004  0.50 20.78           C  
ANISOU  250  CD AGLN A 500     2865   2330   2701   -588    579    114       C  
ATOM    251  CD BGLN A 500      35.115  38.194   3.557  0.50 19.24           C  
ANISOU  251  CD BGLN A 500     2767   1993   2550   -539    489    194       C  
ATOM    252  OE1AGLN A 500      35.231  37.439   2.817  0.50 22.63           O  
ANISOU  252  OE1AGLN A 500     3193   2489   2916   -559    521    199       O  
ATOM    253  OE1BGLN A 500      34.470  37.138   3.270  0.50 19.03           O  
ANISOU  253  OE1BGLN A 500     2727   2033   2472   -478    464    200       O  
ATOM    254  NE2AGLN A 500      36.863  36.118   2.001  0.50 21.69           N  
ANISOU  254  NE2AGLN A 500     2968   2519   2753   -656    656     96       N  
ATOM    255  NE2BGLN A 500      35.207  39.243   2.729  0.50 20.63           N  
ANISOU  255  NE2BGLN A 500     3048   2091   2701   -624    510    273       N  
ATOM    256  N   THR A 501      39.000  37.082   7.024  1.00 16.67           N  
ANISOU  256  N   THR A 501     2026   1820   2488   -569    540   -193       N  
ATOM    257  CA  THR A 501      40.298  37.680   6.916  1.00 17.96           C  
ANISOU  257  CA  THR A 501     2135   1977   2711   -674    603   -249       C  
ATOM    258  C   THR A 501      41.200  36.767   6.069  1.00 18.22           C  
ANISOU  258  C   THR A 501     2085   2101   2735   -722    680   -300       C  
ATOM    259  O   THR A 501      40.654  35.886   5.388  1.00 16.83           O  
ANISOU  259  O   THR A 501     1933   1972   2491   -681    686   -269       O  
ATOM    260  CB  THR A 501      40.919  37.972   8.257  1.00 18.40           C  
ANISOU  260  CB  THR A 501     2117   2020   2855   -661    551   -334       C  
ATOM    261  OG1 THR A 501      42.054  38.772   8.026  1.00 19.88           O  
ANISOU  261  OG1 THR A 501     2263   2185   3103   -779    616   -377       O  
ATOM    262  CG2 THR A 501      41.117  36.694   9.101  1.00 17.69           C  
ANISOU  262  CG2 THR A 501     1933   2007   2783   -573    481   -403       C  
ATOM    263  N   ILE A 502      42.464  37.078   6.022  1.00 20.18           N  
ANISOU  263  N   ILE A 502     2249   2367   3052   -813    743   -375       N  
ATOM    264  CA  ILE A 502      43.395  36.380   5.119  1.00 22.33           C  
ANISOU  264  CA  ILE A 502     2434   2723   3327   -876    840   -440       C  
ATOM    265  C   ILE A 502      44.583  36.013   5.934  1.00 22.97           C  
ANISOU  265  C   ILE A 502     2352   2846   3530   -870    819   -571       C  
ATOM    266  O   ILE A 502      45.125  36.878   6.614  1.00 23.49           O  
ANISOU  266  O   ILE A 502     2388   2868   3668   -917    804   -604       O  
ATOM    267  CB  ILE A 502      43.905  37.298   4.011  1.00 25.87           C  
ANISOU  267  CB  ILE A 502     2934   3154   3741  -1033    968   -409       C  
ATOM    268  CG1 ILE A 502      42.778  37.854   3.136  1.00 27.74           C  
ANISOU  268  CG1 ILE A 502     3352   3333   3856  -1053    975   -265       C  
ATOM    269  CG2 ILE A 502      44.918  36.569   3.115  1.00 27.31           C  
ANISOU  269  CG2 ILE A 502     3012   3437   3928  -1106   1087   -499       C  
ATOM    270  CD1 ILE A 502      42.221  36.894   2.147  1.00 29.10           C  
ANISOU  270  CD1 ILE A 502     3565   3571   3922  -1025    999   -232       C  
ATOM    271  N   ALA A 503      45.078  34.783   5.773  1.00 22.79           N  
ANISOU  271  N   ALA A 503     2218   2902   3538   -823    823   -653       N  
ATOM    272  CA  ALA A 503      46.393  34.397   6.361  1.00 23.72           C  
ANISOU  272  CA  ALA A 503     2157   3062   3792   -825    808   -792       C  
ATOM    273  C   ALA A 503      47.052  33.510   5.315  1.00 23.25           C  
ANISOU  273  C   ALA A 503     2003   3086   3746   -854    910   -873       C  
ATOM    274  O   ALA A 503      46.370  32.685   4.763  1.00 22.41           O  
ANISOU  274  O   ALA A 503     1948   3004   3564   -797    911   -837       O  
ATOM    275  CB  ALA A 503      46.133  33.560   7.616  1.00 24.12           C  
ANISOU  275  CB  ALA A 503     2171   3110   3883   -685    650   -815       C  
ATOM    276  N   ASP A 504      48.347  33.697   5.090  1.00 23.95           N  
ANISOU  276  N   ASP A 504     1949   3215   3935   -943    993   -989       N  
ATOM    277  CA  ASP A 504      49.081  32.924   4.055  1.00 24.68           C  
ANISOU  277  CA  ASP A 504     1932   3394   4052   -984   1115  -1093       C  
ATOM    278  C   ASP A 504      48.258  32.869   2.738  1.00 24.01           C  
ANISOU  278  C   ASP A 504     1994   3327   3801  -1035   1221  -1001       C  
ATOM    279  O   ASP A 504      48.030  31.828   2.163  1.00 22.99           O  
ANISOU  279  O   ASP A 504     1853   3247   3636   -981   1238  -1031       O  
ATOM    280  CB  ASP A 504      49.385  31.523   4.606  1.00 24.80           C  
ANISOU  280  CB  ASP A 504     1813   3442   4167   -842   1010  -1194       C  
ATOM    281  CG  ASP A 504      50.591  31.544   5.617  1.00 25.83           C  
ANISOU  281  CG  ASP A 504     1757   3575   4481   -822    932  -1323       C  
ATOM    282  OD1 ASP A 504      51.609  32.151   5.331  1.00 27.19           O  
ANISOU  282  OD1 ASP A 504     1820   3778   4734   -936   1033  -1411       O  
ATOM    283  OD2 ASP A 504      50.438  30.911   6.700  1.00 25.77           O  
ANISOU  283  OD2 ASP A 504     1724   3539   4528   -693    761  -1327       O  
ATOM    284  N   HIS A 505      47.848  34.056   2.280  1.00 24.00           N  
ANISOU  284  N   HIS A 505     2136   3279   3704  -1145   1283   -890       N  
ATOM    285  CA  HIS A 505      47.181  34.218   0.989  1.00 24.30           C  
ANISOU  285  CA  HIS A 505     2326   3330   3579  -1221   1380   -795       C  
ATOM    286  C   HIS A 505      45.828  33.539   0.877  1.00 22.95           C  
ANISOU  286  C   HIS A 505     2275   3142   3302  -1101   1287   -698       C  
ATOM    287  O   HIS A 505      45.307  33.410  -0.212  1.00 23.85           O  
ANISOU  287  O   HIS A 505     2496   3282   3286  -1146   1351   -640       O  
ATOM    288  CB  HIS A 505      48.120  33.735  -0.149  1.00 25.80           C  
ANISOU  288  CB  HIS A 505     2422   3622   3760  -1327   1553   -910       C  
ATOM    289  CG  HIS A 505      49.382  34.507  -0.293  1.00 27.58           C  
ANISOU  289  CG  HIS A 505     2542   3870   4065  -1481   1681   -997       C  
ATOM    290  ND1 HIS A 505      50.206  34.353  -1.380  1.00 29.54           N  
ANISOU  290  ND1 HIS A 505     2725   4209   4289  -1616   1867  -1092       N  
ATOM    291  CD2 HIS A 505      49.957  35.464   0.468  1.00 28.20           C  
ANISOU  291  CD2 HIS A 505     2573   3897   4247  -1537   1660  -1009       C  
ATOM    292  CE1 HIS A 505      51.228  35.178  -1.284  1.00 30.90           C  
ANISOU  292  CE1 HIS A 505     2808   4384   4547  -1751   1959  -1155       C  
ATOM    293  NE2 HIS A 505      51.099  35.859  -0.160  1.00 30.36           N  
ANISOU  293  NE2 HIS A 505     2748   4226   4561  -1703   1829  -1105       N  
ATOM    294  N   THR A 506      45.246  33.052   1.983  1.00 21.00           N  
ANISOU  294  N   THR A 506     2013   2859   3106   -954   1135   -684       N  
ATOM    295  CA  THR A 506      44.087  32.248   1.981  1.00 19.66           C  
ANISOU  295  CA  THR A 506     1922   2685   2863   -841   1049   -619       C  
ATOM    296  C   THR A 506      43.010  32.848   2.908  1.00 18.42           C  
ANISOU  296  C   THR A 506     1869   2444   2688   -769    925   -508       C  
ATOM    297  O   THR A 506      43.276  33.170   4.059  1.00 17.43           O  
ANISOU  297  O   THR A 506     1692   2282   2649   -733    851   -534       O  
ATOM    298  CB  THR A 506      44.456  30.803   2.435  1.00 19.29           C  
ANISOU  298  CB  THR A 506     1740   2685   2904   -729    989   -730       C  
ATOM    299  OG1 THR A 506      45.599  30.377   1.671  1.00 20.74           O  
ANISOU  299  OG1 THR A 506     1801   2943   3138   -797   1111   -860       O  
ATOM    300  CG2 THR A 506      43.308  29.842   2.299  1.00 18.24           C  
ANISOU  300  CG2 THR A 506     1684   2552   2696   -628    916   -673       C  
ATOM    301  N   PRO A 507      41.779  32.968   2.408  1.00 18.31           N  
ANISOU  301  N   PRO A 507     1996   2401   2561   -747    899   -393       N  
ATOM    302  CA  PRO A 507      40.754  33.500   3.286  1.00 17.06           C  
ANISOU  302  CA  PRO A 507     1914   2167   2398   -675    791   -309       C  
ATOM    303  C   PRO A 507      40.363  32.520   4.355  1.00 16.18           C  
ANISOU  303  C   PRO A 507     1747   2067   2332   -547    683   -341       C  
ATOM    304  O   PRO A 507      40.362  31.301   4.104  1.00 15.77           O  
ANISOU  304  O   PRO A 507     1649   2069   2275   -497    674   -384       O  
ATOM    305  CB  PRO A 507      39.567  33.703   2.349  1.00 17.12           C  
ANISOU  305  CB  PRO A 507     2067   2154   2285   -679    789   -193       C  
ATOM    306  CG  PRO A 507      39.802  32.721   1.274  1.00 18.12           C  
ANISOU  306  CG  PRO A 507     2174   2360   2350   -704    857   -232       C  
ATOM    307  CD  PRO A 507      41.260  32.704   1.057  1.00 19.07           C  
ANISOU  307  CD  PRO A 507     2184   2530   2531   -791    963   -341       C  
ATOM    308  N   VAL A 508      39.987  33.038   5.519  1.00 15.23           N  
ANISOU  308  N   VAL A 508     1642   1894   2250   -500    602   -321       N  
ATOM    309  CA  VAL A 508      39.424  32.256   6.556  1.00 15.03           C  
ANISOU  309  CA  VAL A 508     1598   1873   2239   -394    500   -328       C  
ATOM    310  C   VAL A 508      38.267  33.006   7.192  1.00 14.40           C  
ANISOU  310  C   VAL A 508     1610   1732   2128   -356    444   -254       C  
ATOM    311  O   VAL A 508      38.161  34.199   6.980  1.00 14.67           O  
ANISOU  311  O   VAL A 508     1703   1712   2160   -408    473   -214       O  
ATOM    312  CB  VAL A 508      40.453  31.924   7.668  1.00 16.13           C  
ANISOU  312  CB  VAL A 508     1627   2027   2476   -371    448   -423       C  
ATOM    313  CG1 VAL A 508      41.570  31.033   7.080  1.00 17.24           C  
ANISOU  313  CG1 VAL A 508     1653   2226   2671   -388    492   -516       C  
ATOM    314  CG2 VAL A 508      41.026  33.156   8.264  1.00 17.19           C  
ANISOU  314  CG2 VAL A 508     1751   2118   2662   -429    453   -444       C  
ATOM    315  N   ALA A 509      37.432  32.290   7.931  1.00 13.50           N  
ANISOU  315  N   ALA A 509     1507   1627   1997   -271    369   -240       N  
ATOM    316  CA  ALA A 509      36.295  32.906   8.664  1.00 13.59           C  
ANISOU  316  CA  ALA A 509     1586   1591   1986   -228    322   -192       C  
ATOM    317  C   ALA A 509      36.526  32.744  10.149  1.00 14.23           C  
ANISOU  317  C   ALA A 509     1630   1676   2102   -193    257   -244       C  
ATOM    318  O   ALA A 509      37.012  31.681  10.610  1.00 15.60           O  
ANISOU  318  O   ALA A 509     1748   1890   2289   -164    214   -286       O  
ATOM    319  CB  ALA A 509      35.009  32.333   8.238  1.00 13.14           C  
ANISOU  319  CB  ALA A 509     1580   1545   1869   -177    302   -131       C  
ATOM    320  N   ILE A 510      36.323  33.807  10.914  1.00 14.09           N  
ANISOU  320  N   ILE A 510     1642   1609   2101   -200    243   -250       N  
ATOM    321  CA AILE A 510      36.592  33.858  12.336  0.50 14.31           C  
ANISOU  321  CA AILE A 510     1650   1639   2148   -183    185   -305       C  
ATOM    322  CA BILE A 510      36.511  33.709  12.330  0.50 14.15           C  
ANISOU  322  CA BILE A 510     1630   1625   2121   -176    182   -302       C  
ATOM    323  C   ILE A 510      35.238  34.130  13.011  1.00 13.97           C  
ANISOU  323  C   ILE A 510     1670   1577   2061   -136    165   -279       C  
ATOM    324  O   ILE A 510      34.632  35.148  12.686  1.00 13.50           O  
ANISOU  324  O   ILE A 510     1655   1462   2012   -142    194   -252       O  
ATOM    325  CB AILE A 510      37.545  35.055  12.671  0.50 15.49           C  
ANISOU  325  CB AILE A 510     1779   1746   2360   -246    199   -357       C  
ATOM    326  CB BILE A 510      37.741  34.474  12.839  0.50 15.28           C  
ANISOU  326  CB BILE A 510     1728   1748   2330   -231    178   -370       C  
ATOM    327  CG1AILE A 510      38.852  35.045  11.818  0.50 16.61           C  
ANISOU  327  CG1AILE A 510     1852   1904   2557   -313    248   -388       C  
ATOM    328  CG1BILE A 510      37.559  35.982  12.803  0.50 15.76           C  
ANISOU  328  CG1BILE A 510     1837   1735   2417   -273    213   -364       C  
ATOM    329  CG2AILE A 510      37.868  35.068  14.155  0.50 15.52           C  
ANISOU  329  CG2AILE A 510     1767   1759   2372   -232    128   -421       C  
ATOM    330  CG2BILE A 510      38.935  34.161  11.979  0.50 16.01           C  
ANISOU  330  CG2BILE A 510     1745   1867   2471   -279    218   -400       C  
ATOM    331  CD1AILE A 510      39.798  33.923  12.176  0.50 17.18           C  
ANISOU  331  CD1AILE A 510     1830   2036   2662   -294    203   -451       C  
ATOM    332  CD1BILE A 510      38.683  36.703  13.473  0.50 17.03           C  
ANISOU  332  CD1BILE A 510     1954   1876   2642   -328    200   -439       C  
ATOM    333  N   LYS A 511      34.818  33.285  13.933  1.00 13.10           N  
ANISOU  333  N   LYS A 511     1562   1506   1909    -96    116   -289       N  
ATOM    334  CA  LYS A 511      33.598  33.445  14.679  1.00 14.12           C  
ANISOU  334  CA  LYS A 511     1737   1632   1995    -62    109   -282       C  
ATOM    335  C   LYS A 511      33.978  33.770  16.121  1.00 13.77           C  
ANISOU  335  C   LYS A 511     1699   1592   1939    -76     70   -347       C  
ATOM    336  O   LYS A 511      34.790  33.072  16.745  1.00 13.92           O  
ANISOU  336  O   LYS A 511     1697   1645   1946    -84     14   -373       O  
ATOM    337  CB  LYS A 511      32.800  32.158  14.640  1.00 14.68           C  
ANISOU  337  CB  LYS A 511     1815   1751   2012    -26     92   -243       C  
ATOM    338  CG  LYS A 511      31.467  32.239  15.359  1.00 16.48           C  
ANISOU  338  CG  LYS A 511     2078   1987   2196     -1    101   -241       C  
ATOM    339  CD  LYS A 511      30.741  30.934  15.072  1.00 18.21           C  
ANISOU  339  CD  LYS A 511     2299   2248   2372     21     91   -195       C  
ATOM    340  CE  LYS A 511      29.380  30.922  15.692  1.00 19.71           C  
ANISOU  340  CE  LYS A 511     2509   2456   2523     37    112   -197       C  
ATOM    341  NZ  LYS A 511      28.728  29.610  15.372  1.00 19.22           N  
ANISOU  341  NZ  LYS A 511     2447   2432   2426     46    102   -152       N  
ATOM    342  N   ILE A 512      33.426  34.854  16.665  1.00 13.08           N  
ANISOU  342  N   ILE A 512     1643   1467   1858    -77     92   -379       N  
ATOM    343  CA  ILE A 512      33.886  35.376  17.954  1.00 13.60           C  
ANISOU  343  CA  ILE A 512     1722   1532   1912   -101     61   -454       C  
ATOM    344  C   ILE A 512      32.683  35.457  18.877  1.00 13.54           C  
ANISOU  344  C   ILE A 512     1757   1544   1844    -79     78   -479       C  
ATOM    345  O   ILE A 512      31.691  36.111  18.539  1.00 13.22           O  
ANISOU  345  O   ILE A 512     1727   1467   1830    -52    127   -476       O  
ATOM    346  CB  ILE A 512      34.506  36.771  17.787  1.00 14.52           C  
ANISOU  346  CB  ILE A 512     1833   1578   2107   -138     81   -496       C  
ATOM    347  CG1 ILE A 512      35.699  36.691  16.807  1.00 14.75           C  
ANISOU  347  CG1 ILE A 512     1812   1597   2195   -176     85   -476       C  
ATOM    348  CG2 ILE A 512      34.917  37.331  19.134  1.00 15.12           C  
ANISOU  348  CG2 ILE A 512     1925   1653   2168   -164     46   -584       C  
ATOM    349  CD1 ILE A 512      36.402  37.980  16.563  1.00 16.03           C  
ANISOU  349  CD1 ILE A 512     1970   1688   2435   -231    110   -509       C  
ATOM    350  N   ILE A 513      32.768  34.742  19.997  1.00 13.28           N  
ANISOU  350  N   ILE A 513     1749   1569   1730    -92     36   -503       N  
ATOM    351  CA  ILE A 513      31.663  34.657  20.977  1.00 14.33           C  
ANISOU  351  CA  ILE A 513     1925   1738   1781    -89     63   -532       C  
ATOM    352  C   ILE A 513      32.158  35.095  22.349  1.00 14.51           C  
ANISOU  352  C   ILE A 513     1988   1779   1748   -129     30   -614       C  
ATOM    353  O   ILE A 513      33.087  34.512  22.865  1.00 14.06           O  
ANISOU  353  O   ILE A 513     1942   1750   1651   -155    -48   -612       O  
ATOM    354  CB  ILE A 513      31.174  33.193  21.065  1.00 14.52           C  
ANISOU  354  CB  ILE A 513     1966   1823   1726    -84     45   -469       C  
ATOM    355  CG1 ILE A 513      30.648  32.736  19.682  1.00 14.72           C  
ANISOU  355  CG1 ILE A 513     1954   1835   1804    -46     74   -397       C  
ATOM    356  CG2 ILE A 513      30.100  33.054  22.145  1.00 14.92           C  
ANISOU  356  CG2 ILE A 513     2065   1924   1682   -102     85   -503       C  
ATOM    357  CD1 ILE A 513      30.423  31.238  19.594  1.00 14.93           C  
ANISOU  357  CD1 ILE A 513     1991   1906   1776    -44     44   -334       C  
ATOM    358  N   ALA A 514      31.487  36.060  22.980  1.00 15.06           N  
ANISOU  358  N   ALA A 514     2079   1834   1809   -133     83   -691       N  
ATOM    359  CA  ALA A 514      31.821  36.478  24.337  1.00 15.99           C  
ANISOU  359  CA  ALA A 514     2245   1976   1853   -178     60   -781       C  
ATOM    360  C   ALA A 514      31.263  35.450  25.315  1.00 16.65           C  
ANISOU  360  C   ALA A 514     2389   2147   1790   -207     55   -769       C  
ATOM    361  O   ALA A 514      30.095  35.011  25.166  1.00 16.51           O  
ANISOU  361  O   ALA A 514     2371   2160   1743   -191    122   -744       O  
ATOM    362  CB  ALA A 514      31.185  37.812  24.658  1.00 16.79           C  
ANISOU  362  CB  ALA A 514     2349   2031   1998   -169    130   -880       C  
ATOM    363  N   ILE A 515      32.058  35.056  26.279  1.00 16.94           N  
ANISOU  363  N   ILE A 515     2479   2223   1736   -253    -28   -784       N  
ATOM    364  CA  ILE A 515      31.621  34.086  27.257  1.00 18.06           C  
ANISOU  364  CA  ILE A 515     2700   2441   1720   -297    -44   -762       C  
ATOM    365  C   ILE A 515      31.902  34.511  28.699  1.00 19.71           C  
ANISOU  365  C   ILE A 515     2991   2691   1807   -361    -74   -850       C  
ATOM    366  O   ILE A 515      32.826  35.262  28.963  1.00 19.59           O  
ANISOU  366  O   ILE A 515     2968   2645   1829   -372   -130   -912       O  
ATOM    367  CB  ILE A 515      32.236  32.696  27.018  1.00 17.56           C  
ANISOU  367  CB  ILE A 515     2649   2392   1631   -295   -147   -654       C  
ATOM    368  CG1 ILE A 515      33.770  32.762  27.003  1.00 18.24           C  
ANISOU  368  CG1 ILE A 515     2708   2447   1774   -292   -271   -660       C  
ATOM    369  CG2 ILE A 515      31.728  32.094  25.719  1.00 16.49           C  
ANISOU  369  CG2 ILE A 515     2451   2234   1580   -243   -105   -572       C  
ATOM    370  CD1 ILE A 515      34.491  31.447  27.312  1.00 18.45           C  
ANISOU  370  CD1 ILE A 515     2771   2492   1748   -299   -405   -586       C  
ATOM    371  N   GLU A 516      31.064  34.023  29.622  1.00 21.00           N  
ANISOU  371  N   GLU A 516     3236   2927   1818   -413    -30   -859       N  
ATOM    372  CA  GLU A 516      31.319  33.936  31.048  1.00 23.17           C  
ANISOU  372  CA  GLU A 516     3622   3262   1920   -493    -77   -906       C  
ATOM    373  C   GLU A 516      31.029  35.214  31.812  1.00 24.21           C  
ANISOU  373  C   GLU A 516     3771   3404   2023   -522      0  -1057       C  
ATOM    374  O   GLU A 516      30.982  35.166  33.044  1.00 25.51           O  
ANISOU  374  O   GLU A 516     4039   3634   2017   -599     -9  -1111       O  
ATOM    375  CB  GLU A 516      32.764  33.453  31.415  1.00 24.35           C  
ANISOU  375  CB  GLU A 516     3810   3402   2040   -509   -258   -863       C  
ATOM    376  CG  GLU A 516      33.078  32.019  30.972  1.00 24.86           C  
ANISOU  376  CG  GLU A 516     3883   3462   2102   -491   -353   -724       C  
ATOM    377  CD  GLU A 516      32.353  30.932  31.784  1.00 26.61           C  
ANISOU  377  CD  GLU A 516     4227   3746   2138   -558   -352   -656       C  
ATOM    378  OE1 GLU A 516      31.902  31.199  32.907  1.00 29.71           O  
ANISOU  378  OE1 GLU A 516     4718   4200   2371   -635   -311   -715       O  
ATOM    379  OE2 GLU A 516      32.214  29.802  31.309  1.00 26.76           O  
ANISOU  379  OE2 GLU A 516     4250   3753   2165   -542   -387   -547       O  
ATOM    380  N   GLY A 517      30.807  36.331  31.106  1.00 23.73           N  
ANISOU  380  N   GLY A 517     3621   3276   2120   -464     73  -1126       N  
ATOM    381  CA  GLY A 517      30.531  37.622  31.753  1.00 25.29           C  
ANISOU  381  CA  GLY A 517     3826   3463   2321   -480    145  -1282       C  
ATOM    382  C   GLY A 517      29.100  37.713  32.257  1.00 26.49           C  
ANISOU  382  C   GLY A 517     3993   3674   2399   -499    294  -1357       C  
ATOM    383  O   GLY A 517      28.214  36.995  31.763  1.00 25.66           O  
ANISOU  383  O   GLY A 517     3856   3594   2299   -480    357  -1287       O  
ATOM    384  N   PRO A 518      28.861  38.573  33.255  1.00 28.46           N  
ANISOU  384  N   PRO A 518     4284   3949   2581   -542    354  -1510       N  
ATOM    385  CA  PRO A 518      27.514  38.674  33.895  1.00 30.59           C  
ANISOU  385  CA  PRO A 518     4565   4291   2767   -573    511  -1611       C  
ATOM    386  C   PRO A 518      26.535  39.602  33.161  1.00 31.50           C  
ANISOU  386  C   PRO A 518     4560   4337   3071   -484    627  -1695       C  
ATOM    387  O   PRO A 518      25.317  39.619  33.519  1.00 34.28           O  
ANISOU  387  O   PRO A 518     4888   4747   3390   -496    765  -1779       O  
ATOM    388  CB  PRO A 518      27.829  39.279  35.264  1.00 32.01           C  
ANISOU  388  CB  PRO A 518     4841   4522   2799   -655    516  -1755       C  
ATOM    389  CG  PRO A 518      29.023  40.123  34.998  1.00 31.47           C  
ANISOU  389  CG  PRO A 518     4753   4358   2847   -622    403  -1781       C  
ATOM    390  CD  PRO A 518      29.871  39.289  34.050  1.00 29.73           C  
ANISOU  390  CD  PRO A 518     4503   4098   2697   -586    274  -1601       C  
ATOM    391  N   ASP A 519      27.050  40.405  32.236  1.00 30.49           N  
ANISOU  391  N   ASP A 519     4364   4089   3134   -406    574  -1684       N  
ATOM    392  CA  ASP A 519      26.287  41.433  31.617  1.00 31.42           C  
ANISOU  392  CA  ASP A 519     4387   4118   3434   -322    652  -1766       C  
ATOM    393  C   ASP A 519      25.725  41.108  30.228  1.00 27.90           C  
ANISOU  393  C   ASP A 519     3848   3617   3134   -236    655  -1648       C  
ATOM    394  O   ASP A 519      26.112  40.087  29.596  1.00 26.89           O  
ANISOU  394  O   ASP A 519     3727   3510   2980   -240    589  -1493       O  
ATOM    395  CB  ASP A 519      27.124  42.678  31.590  1.00 34.55           C  
ANISOU  395  CB  ASP A 519     4782   4405   3938   -302    597  -1846       C  
ATOM    396  CG  ASP A 519      27.330  43.293  33.017  1.00 38.07           C  
ANISOU  396  CG  ASP A 519     5305   4897   4262   -376    625  -2019       C  
ATOM    397  OD1 ASP A 519      26.653  42.894  34.019  1.00 40.17           O  
ANISOU  397  OD1 ASP A 519     5620   5280   4364   -438    711  -2097       O  
ATOM    398  OD2 ASP A 519      28.167  44.223  33.154  1.00 41.91           O  
ANISOU  398  OD2 ASP A 519     5806   5304   4812   -381    565  -2088       O  
ATOM    399  N   LEU A 520      24.795  41.938  29.761  1.00 25.68           N  
ANISOU  399  N   LEU A 520     3484   3266   3006   -158    727  -1725       N  
ATOM    400  CA  LEU A 520      24.054  41.642  28.498  1.00 23.61           C  
ANISOU  400  CA  LEU A 520     3136   2962   2874    -77    732  -1626       C  
ATOM    401  C   LEU A 520      24.849  42.000  27.255  1.00 22.08           C  
ANISOU  401  C   LEU A 520     2926   2648   2816    -24    631  -1513       C  
ATOM    402  O   LEU A 520      25.563  43.017  27.236  1.00 21.84           O  
ANISOU  402  O   LEU A 520     2913   2522   2863    -17    590  -1560       O  
ATOM    403  CB  LEU A 520      22.723  42.393  28.441  1.00 24.41           C  
ANISOU  403  CB  LEU A 520     3145   3028   3101     -5    830  -1753       C  
ATOM    404  CG  LEU A 520      21.701  42.072  29.505  1.00 25.62           C  
ANISOU  404  CG  LEU A 520     3285   3303   3147    -53    961  -1879       C  
ATOM    405  CD1 LEU A 520      20.506  43.006  29.316  1.00 26.95           C  
ANISOU  405  CD1 LEU A 520     3338   3410   3491     39   1042  -2021       C  
ATOM    406  CD2 LEU A 520      21.256  40.640  29.472  1.00 24.99           C  
ANISOU  406  CD2 LEU A 520     3210   3341   2943   -106    988  -1772       C  
ATOM    407  N   VAL A 521      24.723  41.142  26.227  1.00 20.14           N  
ANISOU  407  N   VAL A 521     2651   2410   2591      2    596  -1366       N  
ATOM    408  CA  VAL A 521      25.289  41.394  24.916  1.00 19.42           C  
ANISOU  408  CA  VAL A 521     2542   2218   2620     47    519  -1254       C  
ATOM    409  C   VAL A 521      24.152  41.195  23.929  1.00 18.92           C  
ANISOU  409  C   VAL A 521     2407   2133   2649    121    541  -1201       C  
ATOM    410  O   VAL A 521      23.526  40.138  23.934  1.00 18.16           O  
ANISOU  410  O   VAL A 521     2291   2129   2481    109    571  -1158       O  
ATOM    411  CB  VAL A 521      26.420  40.402  24.610  1.00 18.64           C  
ANISOU  411  CB  VAL A 521     2484   2162   2436     -3    443  -1127       C  
ATOM    412  CG1 VAL A 521      26.920  40.529  23.176  1.00 18.36           C  
ANISOU  412  CG1 VAL A 521     2427   2041   2509     33    385  -1012       C  
ATOM    413  CG2 VAL A 521      27.542  40.672  25.581  1.00 19.12           C  
ANISOU  413  CG2 VAL A 521     2606   2238   2422    -70    404  -1187       C  
ATOM    414  N   ASN A 522      23.847  42.236  23.149  1.00 19.27           N  
ANISOU  414  N   ASN A 522     2417   2053   2853    194    522  -1212       N  
ATOM    415  CA  ASN A 522      22.734  42.169  22.176  1.00 19.63           C  
ANISOU  415  CA  ASN A 522     2392   2065   3002    274    521  -1167       C  
ATOM    416  C   ASN A 522      21.418  41.773  22.858  1.00 20.37           C  
ANISOU  416  C   ASN A 522     2418   2249   3073    288    611  -1264       C  
ATOM    417  O   ASN A 522      20.620  41.004  22.310  1.00 20.46           O  
ANISOU  417  O   ASN A 522     2376   2308   3089    311    619  -1206       O  
ATOM    418  CB  ASN A 522      23.084  41.221  21.059  1.00 18.39           C  
ANISOU  418  CB  ASN A 522     2246   1929   2813    266    463  -1001       C  
ATOM    419  CG  ASN A 522      24.453  41.521  20.466  1.00 17.94           C  
ANISOU  419  CG  ASN A 522     2249   1804   2764    233    395   -918       C  
ATOM    420  OD1 ASN A 522      24.873  42.684  20.441  1.00 18.96           O  
ANISOU  420  OD1 ASN A 522     2400   1826   2978    242    375   -960       O  
ATOM    421  ND2 ASN A 522      25.143  40.503  20.036  1.00 17.28           N  
ANISOU  421  ND2 ASN A 522     2187   1779   2598    190    364   -813       N  
ATOM    422  N   GLY A 523      21.255  42.274  24.071  1.00 21.41           N  
ANISOU  422  N   GLY A 523     2553   2410   3171    263    684  -1417       N  
ATOM    423  CA  GLY A 523      20.040  42.046  24.871  1.00 22.69           C  
ANISOU  423  CA  GLY A 523     2648   2663   3309    262    794  -1543       C  
ATOM    424  C   GLY A 523      19.899  40.701  25.561  1.00 22.69           C  
ANISOU  424  C   GLY A 523     2676   2823   3123    167    853  -1514       C  
ATOM    425  O   GLY A 523      18.881  40.485  26.255  1.00 23.21           O  
ANISOU  425  O   GLY A 523     2688   2974   3157    147    962  -1620       O  
ATOM    426  N   SER A 524      20.914  39.847  25.472  1.00 21.89           N  
ANISOU  426  N   SER A 524     2658   2759   2899    103    789  -1385       N  
ATOM    427  CA  SER A 524      20.874  38.496  26.093  1.00 22.64           C  
ANISOU  427  CA  SER A 524     2800   2988   2815     10    823  -1334       C  
ATOM    428  C   SER A 524      22.089  38.266  26.973  1.00 22.49           C  
ANISOU  428  C   SER A 524     2896   3006   2644    -75    781  -1321       C  
ATOM    429  O   SER A 524      23.149  38.853  26.717  1.00 21.87           O  
ANISOU  429  O   SER A 524     2852   2850   2608    -59    700  -1299       O  
ATOM    430  CB  SER A 524      20.776  37.406  25.019  1.00 22.54           C  
ANISOU  430  CB  SER A 524     2767   2985   2811     23    768  -1175       C  
ATOM    431  OG  SER A 524      19.472  37.472  24.411  1.00 25.40           O  
ANISOU  431  OG  SER A 524     3021   3341   3290     87    813  -1203       O  
ATOM    432  N   HIS A 525      21.970  37.377  27.963  1.00 22.52           N  
ANISOU  432  N   HIS A 525     2962   3124   2470   -170    826  -1326       N  
ATOM    433  CA  HIS A 525      23.141  36.983  28.748  1.00 22.45           C  
ANISOU  433  CA  HIS A 525     3070   3151   2308   -250    757  -1291       C  
ATOM    434  C   HIS A 525      24.170  36.228  27.924  1.00 21.02           C  
ANISOU  434  C   HIS A 525     2916   2933   2137   -238    630  -1130       C  
ATOM    435  O   HIS A 525      23.836  35.493  26.988  1.00 19.97           O  
ANISOU  435  O   HIS A 525     2740   2793   2054   -206    613  -1027       O  
ATOM    436  CB  HIS A 525      22.757  36.163  29.978  1.00 23.61           C  
ANISOU  436  CB  HIS A 525     3296   3424   2251   -362    822  -1317       C  
ATOM    437  CG  HIS A 525      22.236  37.003  31.078  1.00 25.96           C  
ANISOU  437  CG  HIS A 525     3604   3767   2494   -400    933  -1498       C  
ATOM    438  ND1 HIS A 525      23.046  37.842  31.817  1.00 26.79           N  
ANISOU  438  ND1 HIS A 525     3773   3851   2557   -423    900  -1589       N  
ATOM    439  CD2 HIS A 525      20.974  37.206  31.517  1.00 27.20           C  
ANISOU  439  CD2 HIS A 525     3702   3984   2649   -416   1081  -1621       C  
ATOM    440  CE1 HIS A 525      22.305  38.483  32.707  1.00 28.50           C  
ANISOU  440  CE1 HIS A 525     3980   4116   2730   -454   1026  -1761       C  
ATOM    441  NE2 HIS A 525      21.043  38.122  32.530  1.00 28.61           N  
ANISOU  441  NE2 HIS A 525     3915   4181   2774   -449   1141  -1786       N  
ATOM    442  N   GLN A 526      25.442  36.432  28.297  1.00 20.90           N  
ANISOU  442  N   GLN A 526     2966   2896   2078   -266    540  -1121       N  
ATOM    443  CA  GLN A 526      26.507  35.746  27.637  1.00 20.19           C  
ANISOU  443  CA  GLN A 526     2892   2777   2001   -258    423   -993       C  
ATOM    444  C   GLN A 526      26.420  34.245  27.906  1.00 20.25           C  
ANISOU  444  C   GLN A 526     2956   2859   1879   -312    395   -892       C  
ATOM    445  O   GLN A 526      26.075  33.814  28.997  1.00 21.04           O  
ANISOU  445  O   GLN A 526     3130   3037   1828   -389    429   -922       O  
ATOM    446  CB  GLN A 526      27.862  36.267  28.164  1.00 20.54           C  
ANISOU  446  CB  GLN A 526     2987   2795   2024   -286    333  -1027       C  
ATOM    447  CG  GLN A 526      28.175  37.681  27.722  1.00 20.73           C  
ANISOU  447  CG  GLN A 526     2961   2722   2193   -238    340  -1102       C  
ATOM    448  CD  GLN A 526      29.514  38.155  28.217  1.00 21.10           C  
ANISOU  448  CD  GLN A 526     3047   2744   2226   -274    251  -1138       C  
ATOM    449  OE1 GLN A 526      30.371  37.370  28.514  1.00 20.28           O  
ANISOU  449  OE1 GLN A 526     2984   2677   2045   -312    160  -1079       O  
ATOM    450  NE2 GLN A 526      29.669  39.475  28.372  1.00 22.15           N  
ANISOU  450  NE2 GLN A 526     3166   2810   2441   -264    272  -1246       N  
ATOM    451  N   LYS A 527      26.779  33.463  26.910  1.00 20.03           N  
ANISOU  451  N   LYS A 527     2901   2802   1908   -278    330   -775       N  
ATOM    452  CA  LYS A 527      26.905  31.999  27.098  1.00 20.80           C  
ANISOU  452  CA  LYS A 527     3057   2946   1901   -323    275   -671       C  
ATOM    453  C   LYS A 527      28.132  31.659  27.976  1.00 20.94           C  
ANISOU  453  C   LYS A 527     3166   2976   1816   -373    159   -653       C  
ATOM    454  O   LYS A 527      29.054  32.445  28.078  1.00 20.76           O  
ANISOU  454  O   LYS A 527     3135   2916   1837   -359    105   -702       O  
ATOM    455  CB  LYS A 527      27.001  31.305  25.760  1.00 20.63           C  
ANISOU  455  CB  LYS A 527     2976   2881   1980   -267    235   -568       C  
ATOM    456  CG  LYS A 527      25.849  31.579  24.794  1.00 21.68           C  
ANISOU  456  CG  LYS A 527     3022   2999   2217   -214    322   -573       C  
ATOM    457  CD  LYS A 527      24.527  31.430  25.463  1.00 24.57           C  
ANISOU  457  CD  LYS A 527     3389   3430   2515   -256    428   -623       C  
ATOM    458  CE  LYS A 527      23.401  31.577  24.467  1.00 26.02           C  
ANISOU  458  CE  LYS A 527     3474   3598   2814   -199    492   -625       C  
ATOM    459  NZ  LYS A 527      22.116  31.487  25.184  1.00 28.85           N  
ANISOU  459  NZ  LYS A 527     3815   4028   3119   -244    605   -695       N  
ATOM    460  N   THR A 528      28.100  30.502  28.623  1.00 21.13           N  
ANISOU  460  N   THR A 528     3277   3046   1705   -435    115   -584       N  
ATOM    461  CA  THR A 528      29.239  30.019  29.378  1.00 21.46           C  
ANISOU  461  CA  THR A 528     3408   3091   1655   -474    -23   -549       C  
ATOM    462  C   THR A 528      30.092  29.145  28.431  1.00 20.34           C  
ANISOU  462  C   THR A 528     3226   2891   1610   -418   -139   -446       C  
ATOM    463  O   THR A 528      29.640  28.710  27.336  1.00 18.79           O  
ANISOU  463  O   THR A 528     2961   2670   1509   -371   -101   -393       O  
ATOM    464  CB  THR A 528      28.799  29.145  30.540  1.00 22.65           C  
ANISOU  464  CB  THR A 528     3691   3308   1606   -574    -28   -512       C  
ATOM    465  OG1 THR A 528      28.031  28.069  29.996  1.00 22.40           O  
ANISOU  465  OG1 THR A 528     3653   3280   1579   -579      7   -420       O  
ATOM    466  CG2 THR A 528      27.941  29.929  31.510  1.00 23.96           C  
ANISOU  466  CG2 THR A 528     3898   3544   1662   -641    102   -626       C  
ATOM    467  N   PHE A 529      31.294  28.824  28.882  1.00 21.43           N  
ANISOU  467  N   PHE A 529     3408   3012   1722   -426   -283   -423       N  
ATOM    468  CA  PHE A 529      32.150  27.941  28.103  1.00 22.05           C  
ANISOU  468  CA  PHE A 529     3444   3038   1894   -373   -397   -343       C  
ATOM    469  C   PHE A 529      31.481  26.570  27.902  1.00 21.58           C  
ANISOU  469  C   PHE A 529     3430   2980   1788   -387   -401   -239       C  
ATOM    470  O   PHE A 529      31.484  25.995  26.774  1.00 19.67           O  
ANISOU  470  O   PHE A 529     3116   2699   1658   -331   -402   -190       O  
ATOM    471  CB  PHE A 529      33.492  27.756  28.801  1.00 24.64           C  
ANISOU  471  CB  PHE A 529     3814   3351   2198   -381   -566   -343       C  
ATOM    472  CG  PHE A 529      34.377  26.797  28.084  1.00 26.55           C  
ANISOU  472  CG  PHE A 529     4005   3539   2545   -323   -686   -276       C  
ATOM    473  CD1 PHE A 529      34.798  27.086  26.804  1.00 27.30           C  
ANISOU  473  CD1 PHE A 529     3968   3594   2811   -254   -653   -295       C  
ATOM    474  CD2 PHE A 529      34.701  25.570  28.630  1.00 28.60           C  
ANISOU  474  CD2 PHE A 529     4350   3782   2733   -338   -823   -193       C  
ATOM    475  CE1 PHE A 529      35.592  26.202  26.077  1.00 28.03           C  
ANISOU  475  CE1 PHE A 529     4000   3641   3009   -198   -745   -252       C  
ATOM    476  CE2 PHE A 529      35.500  24.687  27.917  1.00 29.43           C  
ANISOU  476  CE2 PHE A 529     4394   3828   2959   -273   -932   -147       C  
ATOM    477  CZ  PHE A 529      35.945  25.003  26.646  1.00 28.99           C  
ANISOU  477  CZ  PHE A 529     4194   3743   3078   -202   -886   -184       C  
ATOM    478  N   GLU A 530      30.801  26.112  28.950  1.00 22.49           N  
ANISOU  478  N   GLU A 530     3664   3144   1737   -471   -383   -214       N  
ATOM    479  CA AGLU A 530      30.046  24.824  28.915  0.50 23.56           C  
ANISOU  479  CA AGLU A 530     3861   3281   1809   -510   -376   -115       C  
ATOM    480  CA BGLU A 530      30.094  24.828  28.901  0.50 23.16           C  
ANISOU  480  CA BGLU A 530     3808   3228   1762   -507   -380   -115       C  
ATOM    481  C   GLU A 530      28.994  24.816  27.825  1.00 21.94           C  
ANISOU  481  C   GLU A 530     3560   3077   1700   -476   -243   -115       C  
ATOM    482  O   GLU A 530      28.737  23.774  27.175  1.00 22.38           O  
ANISOU  482  O   GLU A 530     3607   3101   1796   -462   -264    -37       O  
ATOM    483  CB AGLU A 530      29.367  24.538  30.275  0.50 25.68           C  
ANISOU  483  CB AGLU A 530     4278   3614   1865   -630   -344   -101       C  
ATOM    484  CB BGLU A 530      29.523  24.480  30.289  0.50 24.68           C  
ANISOU  484  CB BGLU A 530     4156   3481   1742   -626   -366    -95       C  
ATOM    485  CG AGLU A 530      28.382  23.360  30.318  0.50 27.10           C  
ANISOU  485  CG AGLU A 530     4524   3803   1968   -697   -299    -10       C  
ATOM    486  CG BGLU A 530      30.521  24.639  31.459  0.50 26.46           C  
ANISOU  486  CG BGLU A 530     4490   3714   1850   -668   -503   -104       C  
ATOM    487  CD AGLU A 530      27.273  23.541  31.351  0.50 29.36           C  
ANISOU  487  CD AGLU A 530     4899   4180   2078   -819   -163    -45       C  
ATOM    488  CD BGLU A 530      30.552  26.060  32.092  0.50 26.94           C  
ANISOU  488  CD BGLU A 530     4540   3828   1866   -690   -431   -236       C  
ATOM    489  OE1AGLU A 530      26.078  23.729  30.969  0.50 30.16           O  
ANISOU  489  OE1AGLU A 530     4929   4321   2209   -834     -1    -86       O  
ATOM    490  OE1BGLU A 530      31.346  26.940  31.631  0.50 25.36           O  
ANISOU  490  OE1BGLU A 530     4242   3596   1796   -617   -463   -306       O  
ATOM    491  OE2AGLU A 530      27.591  23.495  32.553  0.50 31.83           O  
ANISOU  491  OE2AGLU A 530     5350   4526   2219   -904   -219    -38       O  
ATOM    492  OE2BGLU A 530      29.822  26.293  33.116  0.50 29.04           O  
ANISOU  492  OE2BGLU A 530     4906   4169   1961   -789   -345   -277       O  
ATOM    493  N   GLU A 531      28.351  25.960  27.602  1.00 21.05           N  
ANISOU  493  N   GLU A 531     3374   2993   1629   -460   -114   -206       N  
ATOM    494  CA  GLU A 531      27.318  26.084  26.597  1.00 20.39           C  
ANISOU  494  CA  GLU A 531     3196   2911   1640   -424      1   -214       C  
ATOM    495  C   GLU A 531      27.852  26.107  25.157  1.00 18.73           C  
ANISOU  495  C   GLU A 531     2883   2639   1596   -329    -38   -190       C  
ATOM    496  O   GLU A 531      27.124  25.771  24.217  1.00 17.79           O  
ANISOU  496  O   GLU A 531     2705   2511   1543   -301     14   -163       O  
ATOM    497  CB  GLU A 531      26.489  27.326  26.839  1.00 21.86           C  
ANISOU  497  CB  GLU A 531     3336   3136   1832   -428    134   -322       C  
ATOM    498  CG  GLU A 531      25.456  27.086  27.932  1.00 23.94           C  
ANISOU  498  CG  GLU A 531     3672   3478   1947   -527    228   -349       C  
ATOM    499  CD  GLU A 531      24.799  28.348  28.470  1.00 26.81           C  
ANISOU  499  CD  GLU A 531     4002   3885   2301   -538    352   -483       C  
ATOM    500  OE1 GLU A 531      25.393  29.459  28.412  1.00 25.59           O  
ANISOU  500  OE1 GLU A 531     3812   3699   2214   -488    336   -556       O  
ATOM    501  OE2 GLU A 531      23.684  28.179  29.077  1.00 29.68           O  
ANISOU  501  OE2 GLU A 531     4383   4317   2577   -611    469   -521       O  
ATOM    502  N   ILE A 532      29.087  26.572  24.999  1.00 17.97           N  
ANISOU  502  N   ILE A 532     2762   2505   1560   -288   -120   -211       N  
ATOM    503  CA  ILE A 532      29.713  26.649  23.686  1.00 17.91           C  
ANISOU  503  CA  ILE A 532     2663   2447   1696   -214   -146   -198       C  
ATOM    504  C   ILE A 532      30.494  25.374  23.350  1.00 17.29           C  
ANISOU  504  C   ILE A 532     2595   2332   1641   -195   -260   -127       C  
ATOM    505  O   ILE A 532      30.739  25.101  22.175  1.00 16.87           O  
ANISOU  505  O   ILE A 532     2471   2247   1691   -143   -262   -109       O  
ATOM    506  CB  ILE A 532      30.604  27.912  23.604  1.00 18.50           C  
ANISOU  506  CB  ILE A 532     2691   2499   1841   -187   -155   -271       C  
ATOM    507  CG1 ILE A 532      29.750  29.167  23.822  1.00 19.26           C  
ANISOU  507  CG1 ILE A 532     2771   2611   1935   -194    -44   -345       C  
ATOM    508  CG2 ILE A 532      31.320  27.993  22.264  1.00 18.68           C  
ANISOU  508  CG2 ILE A 532     2625   2475   1998   -129   -172   -258       C  
ATOM    509  CD1 ILE A 532      28.508  29.296  22.980  1.00 18.79           C  
ANISOU  509  CD1 ILE A 532     2661   2553   1927   -166     56   -337       C  
ATOM    510  N   LEU A 533      30.899  24.626  24.368  1.00 18.61           N  
ANISOU  510  N   LEU A 533     2854   2502   1716   -236   -357    -90       N  
ATOM    511  CA  LEU A 533      31.678  23.422  24.165  1.00 19.24           C  
ANISOU  511  CA  LEU A 533     2948   2533   1830   -210   -484    -28       C  
ATOM    512  C   LEU A 533      31.044  22.435  23.134  1.00 18.01           C  
ANISOU  512  C   LEU A 533     2762   2352   1729   -187   -454     27       C  
ATOM    513  O   LEU A 533      31.750  21.897  22.293  1.00 17.45           O  
ANISOU  513  O   LEU A 533     2634   2236   1762   -130   -512     36       O  
ATOM    514  CB  LEU A 533      31.965  22.759  25.509  1.00 21.47           C  
ANISOU  514  CB  LEU A 533     3357   2816   1983   -268   -597     17       C  
ATOM    515  CG  LEU A 533      32.871  21.556  25.469  1.00 23.06           C  
ANISOU  515  CG  LEU A 533     3583   2952   2229   -235   -760     78       C  
ATOM    516  CD1 LEU A 533      34.194  21.867  24.754  1.00 23.04           C  
ANISOU  516  CD1 LEU A 533     3460   2911   2381   -152   -831     22       C  
ATOM    517  CD2 LEU A 533      33.117  21.096  26.894  1.00 25.39           C  
ANISOU  517  CD2 LEU A 533     4023   3247   2378   -300   -880    126       C  
ATOM    518  N   PRO A 534      29.736  22.205  23.193  1.00 18.36           N  
ANISOU  518  N   PRO A 534     2838   2428   1710   -232   -360     53       N  
ATOM    519  CA  PRO A 534      29.188  21.285  22.215  1.00 17.71           C  
ANISOU  519  CA  PRO A 534     2725   2320   1685   -213   -342     98       C  
ATOM    520  C   PRO A 534      29.457  21.694  20.771  1.00 16.95           C  
ANISOU  520  C   PRO A 534     2514   2206   1721   -138   -306     62       C  
ATOM    521  O   PRO A 534      29.847  20.829  19.951  1.00 15.83           O  
ANISOU  521  O   PRO A 534     2344   2021   1650   -100   -356     86       O  
ATOM    522  CB  PRO A 534      27.696  21.292  22.531  1.00 18.43           C  
ANISOU  522  CB  PRO A 534     2845   2461   1697   -278   -228    106       C  
ATOM    523  CG  PRO A 534      27.635  21.606  23.980  1.00 19.39           C  
ANISOU  523  CG  PRO A 534     3062   2623   1683   -352   -228     98       C  
ATOM    524  CD  PRO A 534      28.726  22.580  24.200  1.00 19.11           C  
ANISOU  524  CD  PRO A 534     3001   2583   1677   -311   -275     40       C  
ATOM    525  N   GLU A 535      29.271  22.966  20.425  1.00 16.81           N  
ANISOU  525  N   GLU A 535     2437   2215   1735   -120   -223      6       N  
ATOM    526  CA  GLU A 535      29.607  23.426  19.069  1.00 17.91           C  
ANISOU  526  CA  GLU A 535     2486   2335   1983    -62   -193    -20       C  
ATOM    527  C   GLU A 535      31.073  23.202  18.698  1.00 16.97           C  
ANISOU  527  C   GLU A 535     2330   2180   1939    -23   -276    -36       C  
ATOM    528  O   GLU A 535      31.392  22.846  17.556  1.00 16.92           O  
ANISOU  528  O   GLU A 535     2267   2153   2008     13   -273    -38       O  
ATOM    529  CB  GLU A 535      29.275  24.914  18.861  1.00 21.09           C  
ANISOU  529  CB  GLU A 535     2848   2757   2409    -53   -108    -71       C  
ATOM    530  CG  GLU A 535      29.727  25.447  17.504  1.00 23.02           C  
ANISOU  530  CG  GLU A 535     3020   2977   2749     -9    -84    -86       C  
ATOM    531  CD  GLU A 535      29.561  26.952  17.293  1.00 26.98           C  
ANISOU  531  CD  GLU A 535     3495   3474   3283     -1    -20   -128       C  
ATOM    532  OE1 GLU A 535      29.003  27.715  18.127  1.00 27.57           O  
ANISOU  532  OE1 GLU A 535     3590   3562   3322    -19     17   -161       O  
ATOM    533  OE2 GLU A 535      30.083  27.417  16.246  1.00 31.58           O  
ANISOU  533  OE2 GLU A 535     4035   4033   3932     20     -6   -132       O  
ATOM    534  N   ILE A 536      31.970  23.429  19.658  1.00 16.25           N  
ANISOU  534  N   ILE A 536     2264   2085   1828    -34   -349    -57       N  
ATOM    535  CA  ILE A 536      33.406  23.210  19.430  1.00 16.38           C  
ANISOU  535  CA  ILE A 536     2228   2067   1927      3   -438    -85       C  
ATOM    536  C   ILE A 536      33.655  21.750  19.130  1.00 15.84           C  
ANISOU  536  C   ILE A 536     2166   1959   1893     30   -519    -47       C  
ATOM    537  O   ILE A 536      34.344  21.402  18.153  1.00 16.01           O  
ANISOU  537  O   ILE A 536     2111   1957   2016     75   -531    -75       O  
ATOM    538  CB  ILE A 536      34.245  23.653  20.640  1.00 17.40           C  
ANISOU  538  CB  ILE A 536     2387   2199   2023    -16   -522   -115       C  
ATOM    539  CG1 ILE A 536      34.061  25.184  20.911  1.00 17.86           C  
ANISOU  539  CG1 ILE A 536     2435   2288   2062    -42   -439   -169       C  
ATOM    540  CG2 ILE A 536      35.701  23.195  20.503  1.00 18.87           C  
ANISOU  540  CG2 ILE A 536     2513   2350   2308     26   -637   -145       C  
ATOM    541  CD1 ILE A 536      34.638  25.639  22.232  1.00 18.80           C  
ANISOU  541  CD1 ILE A 536     2604   2419   2119    -75   -513   -201       C  
ATOM    542  N   ILE A 537      33.091  20.873  19.946  1.00 15.15           N  
ANISOU  542  N   ILE A 537     2173   1860   1723     -1   -572     15       N  
ATOM    543  CA  ILE A 537      33.281  19.446  19.775  1.00 15.62           C  
ANISOU  543  CA  ILE A 537     2256   1863   1815     21   -664     58       C  
ATOM    544  C   ILE A 537      32.739  18.964  18.425  1.00 14.54           C  
ANISOU  544  C   ILE A 537     2065   1718   1741     47   -592     57       C  
ATOM    545  O   ILE A 537      33.421  18.233  17.677  1.00 14.26           O  
ANISOU  545  O   ILE A 537     1976   1638   1802     97   -641     35       O  
ATOM    546  CB  ILE A 537      32.618  18.657  20.955  1.00 16.94           C  
ANISOU  546  CB  ILE A 537     2558   2018   1861    -41   -723    139       C  
ATOM    547  CG1 ILE A 537      33.390  18.890  22.268  1.00 18.69           C  
ANISOU  547  CG1 ILE A 537     2846   2236   2018    -62   -835    143       C  
ATOM    548  CG2 ILE A 537      32.514  17.164  20.634  1.00 17.50           C  
ANISOU  548  CG2 ILE A 537     2664   2018   1968    -27   -798    194       C  
ATOM    549  CD1 ILE A 537      32.591  18.497  23.517  1.00 20.14           C  
ANISOU  549  CD1 ILE A 537     3180   2435   2039   -151   -853    217       C  
ATOM    550  N   ILE A 538      31.523  19.385  18.116  1.00 13.10           N  
ANISOU  550  N   ILE A 538     1892   1578   1507     13   -479     72       N  
ATOM    551  CA  ILE A 538      30.849  18.926  16.892  1.00 13.34           C  
ANISOU  551  CA  ILE A 538     1884   1605   1578     28   -419     76       C  
ATOM    552  C   ILE A 538      31.573  19.466  15.640  1.00 12.77           C  
ANISOU  552  C   ILE A 538     1714   1539   1597     77   -378     14       C  
ATOM    553  O   ILE A 538      31.784  18.734  14.666  1.00 12.98           O  
ANISOU  553  O   ILE A 538     1705   1542   1686    107   -385     -2       O  
ATOM    554  CB  ILE A 538      29.383  19.274  16.952  1.00 12.94           C  
ANISOU  554  CB  ILE A 538     1859   1600   1458    -19   -324    101       C  
ATOM    555  CG1 ILE A 538      28.749  18.449  18.088  1.00 14.30           C  
ANISOU  555  CG1 ILE A 538     2129   1763   1541    -81   -360    161       C  
ATOM    556  CG2 ILE A 538      28.750  18.975  15.600  1.00 12.68           C  
ANISOU  556  CG2 ILE A 538     1777   1569   1472      0   -270     96       C  
ATOM    557  CD1 ILE A 538      27.244  18.688  18.243  1.00 14.59           C  
ANISOU  557  CD1 ILE A 538     2178   1850   1514   -138   -258    175       C  
ATOM    558  N   SER A 539      32.007  20.719  15.724  1.00 12.86           N  
ANISOU  558  N   SER A 539     1692   1580   1615     77   -338    -24       N  
ATOM    559  CA  SER A 539      32.789  21.333  14.652  1.00 13.59           C  
ANISOU  559  CA  SER A 539     1702   1679   1783    103   -294    -78       C  
ATOM    560  C   SER A 539      34.015  20.502  14.328  1.00 14.07           C  
ANISOU  560  C   SER A 539     1710   1705   1931    142   -365   -120       C  
ATOM    561  O   SER A 539      34.305  20.233  13.161  1.00 14.95           O  
ANISOU  561  O   SER A 539     1767   1817   2098    162   -327   -156       O  
ATOM    562  CB  SER A 539      33.207  22.759  15.022  1.00 13.63           C  
ANISOU  562  CB  SER A 539     1689   1705   1785     88   -258   -110       C  
ATOM    563  OG  SER A 539      32.111  23.624  15.144  1.00 14.27           O  
ANISOU  563  OG  SER A 539     1802   1810   1810     64   -186    -89       O  
ATOM    564  N   LYS A 540      34.695  20.042  15.370  1.00 15.26           N  
ANISOU  564  N   LYS A 540     1881   1825   2093    154   -474   -118       N  
ATOM    565  CA  LYS A 540      35.906  19.282  15.191  1.00 16.64           C  
ANISOU  565  CA  LYS A 540     1993   1958   2370    202   -560   -168       C  
ATOM    566  C   LYS A 540      35.569  17.907  14.608  1.00 15.47           C  
ANISOU  566  C   LYS A 540     1858   1766   2254    229   -591   -152       C  
ATOM    567  O   LYS A 540      36.209  17.443  13.648  1.00 14.87           O  
ANISOU  567  O   LYS A 540     1703   1675   2271    268   -581   -217       O  
ATOM    568  CB  LYS A 540      36.682  19.162  16.505  1.00 18.83           C  
ANISOU  568  CB  LYS A 540     2294   2207   2652    210   -692   -164       C  
ATOM    569  CG  LYS A 540      37.963  18.359  16.327  1.00 22.92           C  
ANISOU  569  CG  LYS A 540     2732   2675   3303    273   -799   -225       C  
ATOM    570  CD  LYS A 540      38.883  19.003  15.260  1.00 26.11           C  
ANISOU  570  CD  LYS A 540     2998   3111   3810    290   -715   -327       C  
ATOM    571  CE  LYS A 540      40.306  18.448  15.262  1.00 31.33           C  
ANISOU  571  CE  LYS A 540     3550   3735   4620    350   -818   -414       C  
ATOM    572  NZ  LYS A 540      41.169  19.240  14.297  1.00 34.06           N  
ANISOU  572  NZ  LYS A 540     3761   4128   5052    342   -709   -519       N  
ATOM    573  N   GLU A 541      34.551  17.240  15.151  1.00 15.39           N  
ANISOU  573  N   GLU A 541     1945   1735   2168    203   -620    -75       N  
ATOM    574  CA  GLU A 541      34.270  15.888  14.685  1.00 16.23           C  
ANISOU  574  CA  GLU A 541     2070   1784   2312    224   -663    -60       C  
ATOM    575  C   GLU A 541      33.882  15.889  13.203  1.00 14.93           C  
ANISOU  575  C   GLU A 541     1850   1649   2175    231   -557   -102       C  
ATOM    576  O   GLU A 541      34.247  14.958  12.447  1.00 14.53           O  
ANISOU  576  O   GLU A 541     1761   1556   2202    269   -581   -148       O  
ATOM    577  CB  GLU A 541      33.102  15.256  15.491  1.00 18.52           C  
ANISOU  577  CB  GLU A 541     2479   2053   2505    171   -692     36       C  
ATOM    578  CG  GLU A 541      33.498  14.897  16.943  1.00 21.62           C  
ANISOU  578  CG  GLU A 541     2956   2400   2857    157   -822     90       C  
ATOM    579  CD  GLU A 541      34.572  13.870  17.046  1.00 26.17           C  
ANISOU  579  CD  GLU A 541     3518   2885   3541    220   -970     72       C  
ATOM    580  OE1 GLU A 541      34.627  12.909  16.215  1.00 28.29           O  
ANISOU  580  OE1 GLU A 541     3756   3097   3895    260   -988     46       O  
ATOM    581  OE2 GLU A 541      35.431  14.032  17.974  1.00 31.25           O  
ANISOU  581  OE2 GLU A 541     4175   3507   4190    236  -1080     74       O  
ATOM    582  N   LEU A 542      33.091  16.881  12.805  1.00 13.23           N  
ANISOU  582  N   LEU A 542     1636   1498   1891    193   -447    -88       N  
ATOM    583  CA  LEU A 542      32.613  16.942  11.394  1.00 12.47           C  
ANISOU  583  CA  LEU A 542     1507   1433   1799    191   -356   -116       C  
ATOM    584  C   LEU A 542      33.726  17.345  10.420  1.00 12.74           C  
ANISOU  584  C   LEU A 542     1452   1487   1903    216   -310   -202       C  
ATOM    585  O   LEU A 542      33.848  16.802   9.319  1.00 13.38           O  
ANISOU  585  O   LEU A 542     1499   1569   2017    230   -278   -251       O  
ATOM    586  CB  LEU A 542      31.457  17.858  11.273  1.00 11.73           C  
ANISOU  586  CB  LEU A 542     1442   1391   1624    150   -274    -72       C  
ATOM    587  CG  LEU A 542      30.213  17.398  12.008  1.00 12.01           C  
ANISOU  587  CG  LEU A 542     1549   1421   1595    115   -291     -3       C  
ATOM    588  CD1 LEU A 542      29.255  18.587  12.067  1.00 11.75           C  
ANISOU  588  CD1 LEU A 542     1521   1442   1502     86   -212     19       C  
ATOM    589  CD2 LEU A 542      29.606  16.171  11.368  1.00 12.65           C  
ANISOU  589  CD2 LEU A 542     1644   1470   1690    112   -309      5       C  
ATOM    590  N   SER A 543      34.593  18.217  10.877  1.00 12.52           N  
ANISOU  590  N   SER A 543     1385   1475   1898    217   -309   -229       N  
ATOM    591  CA  SER A 543      35.789  18.577  10.112  1.00 13.57           C  
ANISOU  591  CA  SER A 543     1423   1626   2106    230   -265   -319       C  
ATOM    592  C   SER A 543      36.672  17.370   9.892  1.00 14.25           C  
ANISOU  592  C   SER A 543     1449   1666   2298    283   -332   -391       C  
ATOM    593  O   SER A 543      37.218  17.192   8.782  1.00 14.65           O  
ANISOU  593  O   SER A 543     1430   1736   2400    290   -268   -474       O  
ATOM    594  CB  SER A 543      36.563  19.680  10.814  1.00 13.74           C  
ANISOU  594  CB  SER A 543     1412   1665   2143    215   -268   -335       C  
ATOM    595  OG  SER A 543      37.682  20.140  10.038  1.00 15.32           O  
ANISOU  595  OG  SER A 543     1514   1891   2414    209   -206   -424       O  
ATOM    596  N   LEU A 544      36.822  16.496  10.912  1.00 14.12           N  
ANISOU  596  N   LEU A 544     1463   1586   2318    319   -462   -365       N  
ATOM    597  CA  LEU A 544      37.668  15.348  10.779  1.00 15.39           C  
ANISOU  597  CA  LEU A 544     1565   1683   2597    381   -546   -434       C  
ATOM    598  C   LEU A 544      37.195  14.288   9.783  1.00 14.72           C  
ANISOU  598  C   LEU A 544     1488   1572   2534    397   -522   -462       C  
ATOM    599  O   LEU A 544      37.996  13.413   9.376  1.00 14.87           O  
ANISOU  599  O   LEU A 544     1436   1544   2671    454   -565   -553       O  
ATOM    600  CB  LEU A 544      37.874  14.680  12.178  1.00 16.89           C  
ANISOU  600  CB  LEU A 544     1810   1796   2810    412   -713   -379       C  
ATOM    601  CG  LEU A 544      38.741  15.457  13.119  1.00 18.36           C  
ANISOU  601  CG  LEU A 544     1964   1996   3017    415   -772   -390       C  
ATOM    602  CD1 LEU A 544      38.612  14.858  14.544  1.00 19.63           C  
ANISOU  602  CD1 LEU A 544     2225   2088   3145    424   -935   -303       C  
ATOM    603  CD2 LEU A 544      40.174  15.391  12.647  1.00 19.90           C  
ANISOU  603  CD2 LEU A 544     2011   2184   3365    469   -789   -518       C  
ATOM    604  N   LEU A 545      35.910  14.362   9.392  1.00 13.91           N  
ANISOU  604  N   LEU A 545     1463   1497   2326    351   -458   -395       N  
ATOM    605  CA  LEU A 545      35.364  13.461   8.403  1.00 14.27           C  
ANISOU  605  CA  LEU A 545     1521   1526   2376    354   -431   -422       C  
ATOM    606  C   LEU A 545      36.094  13.575   7.050  1.00 14.94           C  
ANISOU  606  C   LEU A 545     1513   1655   2508    363   -334   -543       C  
ATOM    607  O   LEU A 545      36.098  12.621   6.307  1.00 15.68           O  
ANISOU  607  O   LEU A 545     1592   1719   2647    386   -335   -607       O  
ATOM    608  CB  LEU A 545      33.875  13.643   8.196  1.00 13.87           C  
ANISOU  608  CB  LEU A 545     1555   1507   2209    299   -382   -337       C  
ATOM    609  CG  LEU A 545      33.020  13.288   9.420  1.00 13.74           C  
ANISOU  609  CG  LEU A 545     1630   1448   2143    276   -460   -230       C  
ATOM    610  CD1 LEU A 545      31.565  13.647   9.056  1.00 13.80           C  
ANISOU  610  CD1 LEU A 545     1689   1506   2050    220   -388   -170       C  
ATOM    611  CD2 LEU A 545      33.225  11.826   9.819  1.00 15.05           C  
ANISOU  611  CD2 LEU A 545     1826   1509   2384    310   -578   -230       C  
ATOM    612  N   SER A 546      36.748  14.708   6.769  1.00 14.94           N  
ANISOU  612  N   SER A 546     1455   1722   2499    340   -251   -580       N  
ATOM    613  CA  SER A 546      37.555  14.801   5.521  1.00 16.36           C  
ANISOU  613  CA  SER A 546     1546   1950   2719    334   -148   -703       C  
ATOM    614  C   SER A 546      38.729  13.846   5.444  1.00 17.81           C  
ANISOU  614  C   SER A 546     1625   2085   3058    402   -197   -831       C  
ATOM    615  O   SER A 546      39.263  13.566   4.327  1.00 18.86           O  
ANISOU  615  O   SER A 546     1687   2249   3230    401   -110   -952       O  
ATOM    616  CB  SER A 546      38.015  16.263   5.288  1.00 16.75           C  
ANISOU  616  CB  SER A 546     1563   2076   2726    278    -46   -707       C  
ATOM    617  OG  SER A 546      38.967  16.612   6.284  1.00 17.19           O  
ANISOU  617  OG  SER A 546     1555   2111   2865    304   -107   -726       O  
ATOM    618  N   GLY A 547      39.247  13.392   6.611  1.00 17.86           N  
ANISOU  618  N   GLY A 547     1612   2016   3159    461   -335   -818       N  
ATOM    619  CA  GLY A 547      40.373  12.541   6.664  1.00 19.08           C  
ANISOU  619  CA  GLY A 547     1660   2111   3480    538   -408   -936       C  
ATOM    620  C   GLY A 547      40.082  11.117   7.082  1.00 19.31           C  
ANISOU  620  C   GLY A 547     1736   2021   3578    603   -549   -919       C  
ATOM    621  O   GLY A 547      41.017  10.323   7.226  1.00 20.78           O  
ANISOU  621  O   GLY A 547     1836   2135   3924    684   -639  -1015       O  
ATOM    622  N   GLU A 548      38.794  10.772   7.214  1.00 18.49           N  
ANISOU  622  N   GLU A 548     1763   1894   3367    569   -567   -805       N  
ATOM    623  CA  GLU A 548      38.407   9.368   7.537  1.00 19.63           C  
ANISOU  623  CA  GLU A 548     1971   1918   3571    613   -694   -780       C  
ATOM    624  C   GLU A 548      38.398   8.421   6.332  1.00 20.04           C  
ANISOU  624  C   GLU A 548     1985   1944   3687    639   -648   -897       C  
ATOM    625  O   GLU A 548      38.645   8.815   5.175  1.00 19.28           O  
ANISOU  625  O   GLU A 548     1820   1933   3572    616   -509  -1000       O  
ATOM    626  CB  GLU A 548      37.085   9.333   8.321  1.00 19.53           C  
ANISOU  626  CB  GLU A 548     2107   1885   3428    556   -739   -615       C  
ATOM    627  CG  GLU A 548      37.244   9.864   9.749  1.00 20.66           C  
ANISOU  627  CG  GLU A 548     2296   2016   3538    549   -830   -515       C  
ATOM    628  CD  GLU A 548      38.070   8.937  10.628  1.00 24.01           C  
ANISOU  628  CD  GLU A 548     2716   2317   4089    623  -1013   -521       C  
ATOM    629  OE1 GLU A 548      38.524   7.867  10.211  1.00 25.67           O  
ANISOU  629  OE1 GLU A 548     2885   2439   4430    689  -1077   -601       O  
ATOM    630  OE2 GLU A 548      38.311   9.310  11.774  1.00 28.60           O  
ANISOU  630  OE2 GLU A 548     3337   2887   4643    619  -1102   -449       O  
ATOM    631  N   VAL A 549      38.143   7.137   6.581  1.00 20.57           N  
ANISOU  631  N   VAL A 549     2102   1887   3827    682   -766   -888       N  
ATOM    632  CA  VAL A 549      38.243   6.136   5.551  1.00 21.40           C  
ANISOU  632  CA  VAL A 549     2168   1947   4018    718   -743  -1015       C  
ATOM    633  C   VAL A 549      36.902   5.535   5.208  1.00 21.25           C  
ANISOU  633  C   VAL A 549     2266   1902   3906    663   -735   -944       C  
ATOM    634  O   VAL A 549      36.449   5.618   4.051  1.00 22.45           O  
ANISOU  634  O   VAL A 549     2412   2125   3991    622   -616  -1006       O  
ATOM    635  CB  VAL A 549      39.241   5.023   5.985  1.00 23.22           C  
ANISOU  635  CB  VAL A 549     2335   2032   4457    829   -898  -1100       C  
ATOM    636  CG1 VAL A 549      39.331   3.946   4.925  1.00 24.36           C  
ANISOU  636  CG1 VAL A 549     2437   2119   4701    871   -874  -1247       C  
ATOM    637  CG2 VAL A 549      40.605   5.626   6.215  1.00 24.06           C  
ANISOU  637  CG2 VAL A 549     2298   2175   4670    884   -901  -1193       C  
ATOM    638  N   CYS A 550      36.226   4.902   6.168  1.00 21.12           N  
ANISOU  638  N   CYS A 550     2360   1784   3879    654   -861   -817       N  
ATOM    639  CA  CYS A 550      34.956   4.234   5.868  1.00 21.35           C  
ANISOU  639  CA  CYS A 550     2492   1781   3841    596   -858   -758       C  
ATOM    640  C   CYS A 550      33.841   5.232   5.614  1.00 19.07           C  
ANISOU  640  C   CYS A 550     2252   1622   3371    500   -741   -671       C  
ATOM    641  O   CYS A 550      32.968   4.953   4.851  1.00 18.81           O  
ANISOU  641  O   CYS A 550     2253   1611   3282    454   -688   -680       O  
ATOM    642  CB  CYS A 550      34.510   3.333   7.013  1.00 23.38           C  
ANISOU  642  CB  CYS A 550     2861   1896   4125    591  -1014   -636       C  
ATOM    643  SG  CYS A 550      35.664   1.996   7.301  1.00 28.82           S  
ANISOU  643  SG  CYS A 550     3514   2397   5041    711  -1188   -725       S  
ATOM    644  N   ASN A 551      33.824   6.324   6.391  1.00 17.57           N  
ANISOU  644  N   ASN A 551     2073   1501   3101    471   -722   -580       N  
ATOM    645  CA  ASN A 551      32.842   7.362   6.271  1.00 16.39           C  
ANISOU  645  CA  ASN A 551     1961   1464   2802    394   -624   -500       C  
ATOM    646  C   ASN A 551      33.560   8.697   6.126  1.00 16.00           C  
ANISOU  646  C   ASN A 551     1840   1519   2721    398   -538   -531       C  
ATOM    647  O   ASN A 551      34.038   9.280   7.117  1.00 15.65           O  
ANISOU  647  O   ASN A 551     1791   1476   2680    409   -579   -482       O  
ATOM    648  CB  ASN A 551      31.889   7.323   7.471  1.00 16.17           C  
ANISOU  648  CB  ASN A 551     2036   1406   2703    341   -685   -351       C  
ATOM    649  CG  ASN A 551      30.836   6.247   7.306  1.00 16.76           C  
ANISOU  649  CG  ASN A 551     2184   1413   2771    299   -719   -317       C  
ATOM    650  OD1 ASN A 551      30.112   6.219   6.293  1.00 16.62           O  
ANISOU  650  OD1 ASN A 551     2159   1445   2712    265   -647   -353       O  
ATOM    651  ND2 ASN A 551      30.814   5.284   8.234  1.00 17.46           N  
ANISOU  651  ND2 ASN A 551     2345   1380   2910    299   -840   -254       N  
ATOM    652  N   ARG A 552      33.646   9.162   4.874  1.00 15.95           N  
ANISOU  652  N   ARG A 552     1784   1597   2679    382   -423   -613       N  
ATOM    653  CA  ARG A 552      34.505  10.288   4.505  1.00 16.28           C  
ANISOU  653  CA  ARG A 552     1750   1726   2709    381   -332   -666       C  
ATOM    654  C   ARG A 552      33.715  11.282   3.705  1.00 15.13           C  
ANISOU  654  C   ARG A 552     1637   1684   2428    313   -221   -630       C  
ATOM    655  O   ARG A 552      33.031  10.940   2.746  1.00 14.82           O  
ANISOU  655  O   ARG A 552     1628   1668   2337    285   -182   -652       O  
ATOM    656  CB  ARG A 552      35.704   9.826   3.667  1.00 18.46           C  
ANISOU  656  CB  ARG A 552     1924   1998   3094    428   -296   -830       C  
ATOM    657  CG  ARG A 552      36.769  10.849   3.398  1.00 20.77           C  
ANISOU  657  CG  ARG A 552     2124   2368   3400    423   -208   -898       C  
ATOM    658  CD  ARG A 552      37.776  10.285   2.401  1.00 24.05           C  
ANISOU  658  CD  ARG A 552     2436   2790   3913    455   -147  -1076       C  
ATOM    659  NE  ARG A 552      38.835  11.204   2.044  1.00 28.47           N  
ANISOU  659  NE  ARG A 552     2897   3431   4491    436    -44  -1158       N  
ATOM    660  CZ  ARG A 552      40.078  11.228   2.565  1.00 31.66           C  
ANISOU  660  CZ  ARG A 552     3184   3811   5035    488    -79  -1239       C  
ATOM    661  NH1 ARG A 552      40.461  10.420   3.562  1.00 33.10           N  
ANISOU  661  NH1 ARG A 552     3340   3884   5351    574   -234  -1237       N  
ATOM    662  NH2 ARG A 552      40.963  12.123   2.110  1.00 34.32           N  
ANISOU  662  NH2 ARG A 552     3430   4234   5378    449     38  -1317       N  
ATOM    663  N   THR A 553      33.788  12.536   4.139  1.00 14.79           N  
ANISOU  663  N   THR A 553     1593   1698   2330    287   -182   -570       N  
ATOM    664  CA  THR A 553      33.160  13.649   3.363  1.00 14.75           C  
ANISOU  664  CA  THR A 553     1617   1783   2206    228    -84   -533       C  
ATOM    665  C   THR A 553      33.918  14.946   3.681  1.00 15.14           C  
ANISOU  665  C   THR A 553     1628   1877   2249    214    -34   -525       C  
ATOM    666  O   THR A 553      34.351  15.155   4.814  1.00 14.18           O  
ANISOU  666  O   THR A 553     1490   1724   2175    238    -90   -496       O  
ATOM    667  CB  THR A 553      31.670  13.836   3.701  1.00 14.11           C  
ANISOU  667  CB  THR A 553     1615   1706   2039    194   -110   -419       C  
ATOM    668  OG1 THR A 553      31.119  14.951   2.958  1.00 14.63           O  
ANISOU  668  OG1 THR A 553     1706   1847   2007    149    -35   -384       O  
ATOM    669  CG2 THR A 553      31.404  14.103   5.210  1.00 14.14           C  
ANISOU  669  CG2 THR A 553     1647   1677   2051    200   -174   -329       C  
ATOM    670  N   GLU A 554      34.002  15.825   2.676  1.00 15.24           N  
ANISOU  670  N   GLU A 554     1639   1960   2190    167     67   -543       N  
ATOM    671  CA  GLU A 554      34.520  17.190   2.887  1.00 16.34           C  
ANISOU  671  CA  GLU A 554     1761   2139   2309    136    122   -519       C  
ATOM    672  C   GLU A 554      33.365  18.204   2.918  1.00 15.45           C  
ANISOU  672  C   GLU A 554     1727   2050   2093     98    134   -407       C  
ATOM    673  O   GLU A 554      33.632  19.372   2.885  1.00 15.81           O  
ANISOU  673  O   GLU A 554     1775   2122   2110     65    183   -383       O  
ATOM    674  CB  GLU A 554      35.463  17.549   1.753  1.00 19.28           C  
ANISOU  674  CB  GLU A 554     2084   2566   2674     97    231   -613       C  
ATOM    675  CG  GLU A 554      36.696  16.689   1.731  1.00 23.92           C  
ANISOU  675  CG  GLU A 554     2569   3135   3384    138    230   -745       C  
ATOM    676  CD  GLU A 554      37.673  17.082   0.659  1.00 28.04           C  
ANISOU  676  CD  GLU A 554     3029   3723   3901     88    359   -851       C  
ATOM    677  OE1 GLU A 554      37.574  18.227   0.153  1.00 33.43           O  
ANISOU  677  OE1 GLU A 554     3754   4459   4489     13    442   -805       O  
ATOM    678  OE2 GLU A 554      38.561  16.263   0.360  1.00 31.81           O  
ANISOU  678  OE2 GLU A 554     3415   4194   4476    120    376   -984       O  
ATOM    679  N   GLY A 555      32.124  17.754   3.067  1.00 13.87           N  
ANISOU  679  N   GLY A 555     1582   1833   1853    105     83   -345       N  
ATOM    680  CA  GLY A 555      30.958  18.599   2.963  1.00 13.44           C  
ANISOU  680  CA  GLY A 555     1587   1801   1719     78     89   -257       C  
ATOM    681  C   GLY A 555      30.684  19.485   4.191  1.00 12.84           C  
ANISOU  681  C   GLY A 555     1518   1709   1650     85     65   -190       C  
ATOM    682  O   GLY A 555      29.716  20.264   4.151  1.00 13.64           O  
ANISOU  682  O   GLY A 555     1657   1823   1702     71     70   -126       O  
ATOM    683  N   PHE A 556      31.400  19.264   5.314  1.00 11.69           N  
ANISOU  683  N   PHE A 556     1342   1533   1568    110     27   -206       N  
ATOM    684  CA  PHE A 556      31.269  20.102   6.490  1.00 11.80           C  
ANISOU  684  CA  PHE A 556     1366   1536   1580    110      9   -158       C  
ATOM    685  C   PHE A 556      32.451  21.089   6.496  1.00 12.84           C  
ANISOU  685  C   PHE A 556     1459   1680   1741     97     51   -195       C  
ATOM    686  O   PHE A 556      33.562  20.794   6.030  1.00 16.22           O  
ANISOU  686  O   PHE A 556     1833   2112   2216     99     73   -267       O  
ATOM    687  CB  PHE A 556      31.237  19.272   7.762  1.00 11.68           C  
ANISOU  687  CB  PHE A 556     1359   1482   1596    133    -69   -144       C  
ATOM    688  CG  PHE A 556      30.038  18.374   7.816  1.00 11.12           C  
ANISOU  688  CG  PHE A 556     1330   1398   1497    128   -101   -103       C  
ATOM    689  CD1 PHE A 556      28.817  18.838   8.287  1.00 11.22           C  
ANISOU  689  CD1 PHE A 556     1376   1427   1460    107    -92    -45       C  
ATOM    690  CD2 PHE A 556      30.126  17.096   7.359  1.00 11.32           C  
ANISOU  690  CD2 PHE A 556     1352   1394   1554    141   -135   -134       C  
ATOM    691  CE1 PHE A 556      27.696  18.026   8.277  1.00 11.37           C  
ANISOU  691  CE1 PHE A 556     1420   1440   1459     92   -112    -15       C  
ATOM    692  CE2 PHE A 556      29.008  16.265   7.346  1.00 11.45           C  
ANISOU  692  CE2 PHE A 556     1406   1396   1549    126   -162    -99       C  
ATOM    693  CZ  PHE A 556      27.806  16.716   7.787  1.00 11.33           C  
ANISOU  693  CZ  PHE A 556     1418   1403   1483     98   -149    -40       C  
ATOM    694  N   ILE A 557      32.279  22.195   7.109  1.00 12.82           N  
ANISOU  694  N   ILE A 557     1473   1677   1722     84     61   -159       N  
ATOM    695  CA  ILE A 557      33.324  23.234   7.066  1.00 12.68           C  
ANISOU  695  CA  ILE A 557     1421   1664   1731     59    105   -191       C  
ATOM    696  C   ILE A 557      34.592  22.829   7.820  1.00 12.84           C  
ANISOU  696  C   ILE A 557     1378   1671   1829     78     65   -254       C  
ATOM    697  O   ILE A 557      34.527  22.204   8.895  1.00 13.18           O  
ANISOU  697  O   ILE A 557     1427   1689   1890    109    -14   -244       O  
ATOM    698  CB  ILE A 557      32.717  24.560   7.615  1.00 12.39           C  
ANISOU  698  CB  ILE A 557     1425   1618   1665     44    117   -139       C  
ATOM    699  CG1 ILE A 557      33.554  25.782   7.262  1.00 12.76           C  
ANISOU  699  CG1 ILE A 557     1457   1663   1728      2    174   -157       C  
ATOM    700  CG2 ILE A 557      32.454  24.497   9.086  1.00 12.45           C  
ANISOU  700  CG2 ILE A 557     1443   1609   1680     65     59   -126       C  
ATOM    701  CD1 ILE A 557      33.592  26.100   5.794  1.00 13.89           C  
ANISOU  701  CD1 ILE A 557     1621   1824   1832    -39    242   -148       C  
ATOM    702  N   GLY A 558      35.760  23.117   7.247  1.00 13.00           N  
ANISOU  702  N   GLY A 558     1335   1707   1897     56    115   -321       N  
ATOM    703  CA  GLY A 558      36.971  22.819   7.913  1.00 13.66           C  
ANISOU  703  CA  GLY A 558     1341   1778   2070     77     70   -389       C  
ATOM    704  C   GLY A 558      37.144  23.667   9.162  1.00 14.01           C  
ANISOU  704  C   GLY A 558     1396   1807   2122     71     25   -368       C  
ATOM    705  O   GLY A 558      36.871  24.851   9.117  1.00 14.15           O  
ANISOU  705  O   GLY A 558     1444   1829   2102     32     76   -337       O  
ATOM    706  N   LEU A 559      37.623  23.080  10.248  1.00 14.44           N  
ANISOU  706  N   LEU A 559     1427   1836   2223    109    -75   -387       N  
ATOM    707  CA  LEU A 559      37.936  23.826  11.440  1.00 14.69           C  
ANISOU  707  CA  LEU A 559     1466   1858   2259     99   -124   -382       C  
ATOM    708  C   LEU A 559      39.427  23.918  11.591  1.00 15.71           C  
ANISOU  708  C   LEU A 559     1490   1987   2493    101   -152   -471       C  
ATOM    709  O   LEU A 559      40.118  22.883  11.671  1.00 16.59           O  
ANISOU  709  O   LEU A 559     1540   2082   2682    148   -223   -521       O  
ATOM    710  CB  LEU A 559      37.384  23.128  12.679  1.00 15.43           C  
ANISOU  710  CB  LEU A 559     1624   1925   2314    130   -232   -333       C  
ATOM    711  CG  LEU A 559      37.664  23.776  14.017  1.00 15.57           C  
ANISOU  711  CG  LEU A 559     1665   1937   2315    117   -295   -331       C  
ATOM    712  CD1 LEU A 559      36.911  25.077  14.194  1.00 15.52           C  
ANISOU  712  CD1 LEU A 559     1710   1946   2242     76   -222   -300       C  
ATOM    713  CD2 LEU A 559      37.263  22.806  15.111  1.00 16.40           C  
ANISOU  713  CD2 LEU A 559     1838   2017   2374    140   -407   -283       C  
ATOM    714  N   ASN A 560      39.955  25.142  11.572  1.00 14.82           N  
ANISOU  714  N   ASN A 560     1346   1887   2397     51    -96   -499       N  
ATOM    715  CA  ASN A 560      41.386  25.369  11.669  1.00 15.91           C  
ANISOU  715  CA  ASN A 560     1370   2033   2644     39   -110   -593       C  
ATOM    716  C   ASN A 560      41.891  25.445  13.103  1.00 16.27           C  
ANISOU  716  C   ASN A 560     1406   2058   2720     60   -238   -608       C  
ATOM    717  O   ASN A 560      42.961  24.912  13.419  1.00 16.48           O  
ANISOU  717  O   ASN A 560     1337   2077   2849     92   -319   -682       O  
ATOM    718  CB  ASN A 560      41.760  26.630  10.915  1.00 16.87           C  
ANISOU  718  CB  ASN A 560     1465   2175   2771    -40     13   -616       C  
ATOM    719  CG  ASN A 560      41.512  26.537   9.419  1.00 17.82           C  
ANISOU  719  CG  ASN A 560     1590   2322   2860    -73    136   -613       C  
ATOM    720  OD1 ASN A 560      41.311  25.463   8.855  1.00 18.29           O  
ANISOU  720  OD1 ASN A 560     1640   2391   2918    -34    134   -624       O  
ATOM    721  ND2 ASN A 560      41.546  27.682   8.759  1.00 19.45           N  
ANISOU  721  ND2 ASN A 560     1817   2536   3038   -151    240   -598       N  
ATOM    722  N   SER A 561      41.223  26.203  13.965  1.00 15.80           N  
ANISOU  722  N   SER A 561     1435   1989   2579     38   -256   -553       N  
ATOM    723  CA  SER A 561      41.674  26.378  15.347  1.00 16.71           C  
ANISOU  723  CA  SER A 561     1557   2091   2699     45   -375   -570       C  
ATOM    724  C   SER A 561      40.541  26.923  16.220  1.00 16.02           C  
ANISOU  724  C   SER A 561     1596   2000   2490     27   -379   -500       C  
ATOM    725  O   SER A 561      39.536  27.437  15.711  1.00 14.95           O  
ANISOU  725  O   SER A 561     1520   1868   2293      7   -282   -452       O  
ATOM    726  CB  SER A 561      42.836  27.282  15.449  1.00 18.32           C  
ANISOU  726  CB  SER A 561     1668   2302   2991      4   -368   -652       C  
ATOM    727  OG  SER A 561      42.487  28.579  15.066  1.00 19.12           O  
ANISOU  727  OG  SER A 561     1801   2405   3057    -60   -255   -639       O  
ATOM    728  N   VAL A 562      40.704  26.745  17.521  1.00 16.53           N  
ANISOU  728  N   VAL A 562     1701   2058   2523     37   -497   -499       N  
ATOM    729  CA  VAL A 562      39.797  27.295  18.505  1.00 16.51           C  
ANISOU  729  CA  VAL A 562     1809   2060   2406     11   -501   -458       C  
ATOM    730  C   VAL A 562      40.677  27.851  19.611  1.00 17.54           C  
ANISOU  730  C   VAL A 562     1926   2190   2549    -11   -595   -514       C  
ATOM    731  O   VAL A 562      41.642  27.189  20.055  1.00 18.61           O  
ANISOU  731  O   VAL A 562     2013   2317   2741     16   -722   -545       O  
ATOM    732  CB  VAL A 562      38.845  26.245  19.108  1.00 17.18           C  
ANISOU  732  CB  VAL A 562     1993   2143   2391     33   -556   -383       C  
ATOM    733  CG1 VAL A 562      37.819  26.920  20.065  1.00 17.46           C  
ANISOU  733  CG1 VAL A 562     2135   2196   2302     -6   -526   -355       C  
ATOM    734  CG2 VAL A 562      38.037  25.554  18.046  1.00 17.34           C  
ANISOU  734  CG2 VAL A 562     2018   2161   2408     55   -483   -334       C  
ATOM    735  N   HIS A 563      40.424  29.095  20.027  1.00 17.55           N  
ANISOU  735  N   HIS A 563     1962   2195   2513    -57   -543   -537       N  
ATOM    736  CA  HIS A 563      41.178  29.720  21.090  1.00 19.71           C  
ANISOU  736  CA  HIS A 563     2231   2469   2787    -87   -628   -598       C  
ATOM    737  C   HIS A 563      40.218  30.368  22.068  1.00 19.23           C  
ANISOU  737  C   HIS A 563     2288   2418   2600   -119   -608   -585       C  
ATOM    738  O   HIS A 563      39.122  30.732  21.696  1.00 17.82           O  
ANISOU  738  O   HIS A 563     2158   2239   2375   -123   -499   -550       O  
ATOM    739  CB  HIS A 563      42.118  30.801  20.552  1.00 22.03           C  
ANISOU  739  CB  HIS A 563     2425   2751   3194   -126   -576   -675       C  
ATOM    740  CG  HIS A 563      43.248  30.272  19.730  1.00 24.36           C  
ANISOU  740  CG  HIS A 563     2586   3047   3623   -108   -592   -718       C  
ATOM    741  ND1 HIS A 563      43.172  30.158  18.360  1.00 26.29           N  
ANISOU  741  ND1 HIS A 563     2777   3292   3921   -107   -476   -705       N  
ATOM    742  CD2 HIS A 563      44.469  29.812  20.077  1.00 28.09           C  
ANISOU  742  CD2 HIS A 563     2961   3522   4188    -90   -711   -782       C  
ATOM    743  CE1 HIS A 563      44.302  29.673  17.889  1.00 27.25           C  
ANISOU  743  CE1 HIS A 563     2771   3421   4160    -94   -505   -768       C  
ATOM    744  NE2 HIS A 563      45.104  29.437  18.912  1.00 29.19           N  
ANISOU  744  NE2 HIS A 563     2981   3666   4444    -78   -651   -817       N  
ATOM    745  N   CYS A 564      40.638  30.405  23.318  1.00 20.55           N  
ANISOU  745  N   CYS A 564     2499   2597   2712   -138   -721   -616       N  
ATOM    746  CA  CYS A 564      40.026  31.252  24.321  1.00 21.33           C  
ANISOU  746  CA  CYS A 564     2691   2710   2703   -182   -700   -642       C  
ATOM    747  C   CYS A 564      40.916  32.476  24.482  1.00 21.56           C  
ANISOU  747  C   CYS A 564     2661   2722   2809   -221   -705   -736       C  
ATOM    748  O   CYS A 564      42.118  32.395  24.867  1.00 21.45           O  
ANISOU  748  O   CYS A 564     2586   2708   2854   -228   -823   -787       O  
ATOM    749  CB  CYS A 564      39.879  30.501  25.640  1.00 23.54           C  
ANISOU  749  CB  CYS A 564     3078   3019   2847   -193   -822   -615       C  
ATOM    750  SG  CYS A 564      39.096  31.564  26.910  1.00 27.24           S  
ANISOU  750  SG  CYS A 564     3665   3518   3166   -258   -776   -669       S  
ATOM    751  N   VAL A 565      40.311  33.635  24.238  1.00 20.99           N  
ANISOU  751  N   VAL A 565     2605   2628   2740   -247   -585   -764       N  
ATOM    752  CA  VAL A 565      40.994  34.895  24.152  1.00 22.34           C  
ANISOU  752  CA  VAL A 565     2725   2766   2999   -290   -559   -845       C  
ATOM    753  C   VAL A 565      40.476  35.795  25.276  1.00 22.04           C  
ANISOU  753  C   VAL A 565     2776   2728   2869   -327   -553   -905       C  
ATOM    754  O   VAL A 565      39.321  35.659  25.684  1.00 21.02           O  
ANISOU  754  O   VAL A 565     2736   2620   2632   -317   -505   -879       O  
ATOM    755  CB  VAL A 565      40.671  35.434  22.734  1.00 23.60           C  
ANISOU  755  CB  VAL A 565     2836   2882   3248   -287   -423   -815       C  
ATOM    756  CG1 VAL A 565      40.697  36.912  22.611  1.00 25.44           C  
ANISOU  756  CG1 VAL A 565     3068   3060   3537   -333   -352   -872       C  
ATOM    757  CG2 VAL A 565      41.563  34.715  21.725  1.00 24.69           C  
ANISOU  757  CG2 VAL A 565     2868   3027   3488   -271   -435   -795       C  
ATOM    758  N   GLN A 566      41.337  36.642  25.820  1.00 22.41           N  
ANISOU  758  N   GLN A 566     2799   2758   2959   -374   -605   -996       N  
ATOM    759  CA AGLN A 566      40.940  37.608  26.862  0.50 22.99           C  
ANISOU  759  CA AGLN A 566     2953   2827   2956   -414   -596  -1075       C  
ATOM    760  CA BGLN A 566      40.939  37.608  26.853  0.50 23.25           C  
ANISOU  760  CA BGLN A 566     2985   2860   2991   -414   -595  -1075       C  
ATOM    761  C   GLN A 566      41.328  39.015  26.411  1.00 23.72           C  
ANISOU  761  C   GLN A 566     2995   2847   3172   -454   -530  -1147       C  
ATOM    762  O   GLN A 566      42.452  39.233  25.928  1.00 24.31           O  
ANISOU  762  O   GLN A 566     2973   2897   3365   -481   -562  -1173       O  
ATOM    763  CB AGLN A 566      41.578  37.266  28.208  0.50 23.87           C  
ANISOU  763  CB AGLN A 566     3111   2987   2973   -444   -747  -1124       C  
ATOM    764  CB BGLN A 566      41.598  37.258  28.167  0.50 24.49           C  
ANISOU  764  CB BGLN A 566     3185   3064   3056   -443   -746  -1123       C  
ATOM    765  CG AGLN A 566      41.115  38.179  29.346  0.50 24.64           C  
ANISOU  765  CG AGLN A 566     3305   3092   2967   -491   -733  -1216       C  
ATOM    766  CG BGLN A 566      41.240  38.183  29.320  0.50 25.73           C  
ANISOU  766  CG BGLN A 566     3434   3228   3116   -492   -742  -1219       C  
ATOM    767  CD AGLN A 566      41.597  37.743  30.713  0.50 25.72           C  
ANISOU  767  CD AGLN A 566     3517   3287   2970   -526   -886  -1252       C  
ATOM    768  CD BGLN A 566      41.910  37.743  30.582  0.50 27.21           C  
ANISOU  768  CD BGLN A 566     3676   3468   3195   -525   -907  -1255       C  
ATOM    769  OE1AGLN A 566      42.768  37.378  30.899  0.50 26.14           O  
ANISOU  769  OE1AGLN A 566     3514   3347   3072   -532  -1031  -1263       O  
ATOM    770  OE1BGLN A 566      41.960  36.556  30.868  0.50 27.34           O  
ANISOU  770  OE1BGLN A 566     3728   3528   3132   -503  -1000  -1179       O  
ATOM    771  NE2AGLN A 566      40.702  37.798  31.687  0.50 25.88           N  
ANISOU  771  NE2AGLN A 566     3662   3350   2820   -553   -857  -1276       N  
ATOM    772  NE2BGLN A 566      42.465  38.682  31.325  0.50 28.46           N  
ANISOU  772  NE2BGLN A 566     3845   3617   3353   -580   -956  -1368       N  
ATOM    773  N   GLY A 567      40.406  39.974  26.579  1.00 23.73           N  
ANISOU  773  N   GLY A 567     3058   2809   3150   -461   -437  -1185       N  
ATOM    774  CA  GLY A 567      40.671  41.361  26.274  1.00 24.53           C  
ANISOU  774  CA  GLY A 567     3135   2824   3361   -501   -382  -1253       C  
ATOM    775  C   GLY A 567      39.499  42.108  25.733  1.00 24.39           C  
ANISOU  775  C   GLY A 567     3158   2741   3370   -473   -259  -1237       C  
ATOM    776  O   GLY A 567      38.458  41.550  25.504  1.00 23.69           O  
ANISOU  776  O   GLY A 567     3102   2679   3221   -421   -208  -1175       O  
ATOM    777  N   SER A 568      39.653  43.425  25.599  1.00 25.92           N  
ANISOU  777  N   SER A 568     3350   2840   3658   -509   -221  -1303       N  
ATOM    778  CA  SER A 568      38.586  44.228  24.959  1.00 26.67           C  
ANISOU  778  CA  SER A 568     3478   2848   3807   -474   -118  -1284       C  
ATOM    779  C   SER A 568      38.615  43.938  23.487  1.00 24.86           C  
ANISOU  779  C   SER A 568     3205   2589   3652   -457    -72  -1166       C  
ATOM    780  O   SER A 568      39.591  43.395  22.958  1.00 25.17           O  
ANISOU  780  O   SER A 568     3180   2658   3724   -487   -103  -1125       O  
ATOM    781  CB  SER A 568      38.762  45.724  25.220  1.00 28.47           C  
ANISOU  781  CB  SER A 568     3727   2965   4125   -517   -101  -1385       C  
ATOM    782  OG  SER A 568      40.108  46.092  25.073  1.00 31.51           O  
ANISOU  782  OG  SER A 568     4058   3322   4593   -593   -149  -1414       O  
ATOM    783  N   TYR A 569      37.537  44.286  22.817  1.00 24.29           N  
ANISOU  783  N   TYR A 569     3164   2459   3606   -409     -1  -1116       N  
ATOM    784  CA  TYR A 569      37.429  44.074  21.409  1.00 23.11           C  
ANISOU  784  CA  TYR A 569     2992   2278   3509   -396     42  -1003       C  
ATOM    785  C   TYR A 569      38.460  44.923  20.640  1.00 23.94           C  
ANISOU  785  C   TYR A 569     3071   2297   3728   -473     54   -996       C  
ATOM    786  O   TYR A 569      38.611  46.108  20.905  1.00 23.98           O  
ANISOU  786  O   TYR A 569     3103   2205   3804   -511     59  -1060       O  
ATOM    787  CB  TYR A 569      36.011  44.417  20.925  1.00 23.22           C  
ANISOU  787  CB  TYR A 569     3050   2236   3535   -327     98   -961       C  
ATOM    788  CG  TYR A 569      35.390  43.416  20.005  1.00 21.35           C  
ANISOU  788  CG  TYR A 569     2802   2050   3259   -277    120   -848       C  
ATOM    789  CD1 TYR A 569      34.904  42.257  20.514  1.00 20.57           C  
ANISOU  789  CD1 TYR A 569     2698   2058   3059   -238    107   -837       C  
ATOM    790  CD2 TYR A 569      35.181  43.660  18.645  1.00 20.75           C  
ANISOU  790  CD2 TYR A 569     2734   1910   3242   -272    152   -752       C  
ATOM    791  CE1 TYR A 569      34.233  41.337  19.721  1.00 19.43           C  
ANISOU  791  CE1 TYR A 569     2544   1956   2881   -193    126   -743       C  
ATOM    792  CE2 TYR A 569      34.541  42.730  17.826  1.00 20.36           C  
ANISOU  792  CE2 TYR A 569     2677   1910   3148   -226    167   -658       C  
ATOM    793  CZ  TYR A 569      34.058  41.554  18.369  1.00 19.08           C  
ANISOU  793  CZ  TYR A 569     2500   1856   2895   -184    154   -657       C  
ATOM    794  OH  TYR A 569      33.392  40.575  17.678  1.00 19.07           O  
ANISOU  794  OH  TYR A 569     2490   1906   2851   -142    165   -576       O  
ATOM    795  N   PRO A 570      39.171  44.305  19.686  1.00 23.69           N  
ANISOU  795  N   PRO A 570     2986   2300   3715   -502     65   -923       N  
ATOM    796  CA  PRO A 570      40.153  45.095  18.968  1.00 25.25           C  
ANISOU  796  CA  PRO A 570     3157   2424   4012   -593     93   -921       C  
ATOM    797  C   PRO A 570      39.531  46.256  18.178  1.00 26.11           C  
ANISOU  797  C   PRO A 570     3338   2395   4186   -605    146   -870       C  
ATOM    798  O   PRO A 570      38.536  46.063  17.516  1.00 25.03           O  
ANISOU  798  O   PRO A 570     3245   2242   4022   -544    172   -788       O  
ATOM    799  CB  PRO A 570      40.785  44.097  18.010  1.00 24.17           C  
ANISOU  799  CB  PRO A 570     2954   2362   3868   -611    113   -852       C  
ATOM    800  CG  PRO A 570      40.627  42.785  18.688  1.00 23.47           C  
ANISOU  800  CG  PRO A 570     2836   2391   3693   -543     56   -861       C  
ATOM    801  CD  PRO A 570      39.328  42.864  19.430  1.00 22.97           C  
ANISOU  801  CD  PRO A 570     2848   2320   3558   -470     46   -869       C  
ATOM    802  N   PRO A 571      40.116  47.432  18.272  1.00 29.08           N  
ANISOU  802  N   PRO A 571     3730   2669   4652   -682    151   -921       N  
ATOM    803  CA  PRO A 571      39.724  48.587  17.447  1.00 30.32           C  
ANISOU  803  CA  PRO A 571     3962   2672   4884   -711    189   -863       C  
ATOM    804  C   PRO A 571      39.614  48.258  15.962  1.00 29.47           C  
ANISOU  804  C   PRO A 571     3874   2560   4762   -729    240   -725       C  
ATOM    805  O   PRO A 571      38.661  48.676  15.294  1.00 28.84           O  
ANISOU  805  O   PRO A 571     3873   2394   4690   -686    250   -644       O  
ATOM    806  CB  PRO A 571      40.818  49.587  17.737  1.00 32.61           C  
ANISOU  806  CB  PRO A 571     4239   2885   5268   -825    186   -939       C  
ATOM    807  CG  PRO A 571      41.117  49.344  19.183  1.00 32.50           C  
ANISOU  807  CG  PRO A 571     4179   2945   5224   -805    125  -1073       C  
ATOM    808  CD  PRO A 571      41.027  47.857  19.364  1.00 30.80           C  
ANISOU  808  CD  PRO A 571     3909   2891   4904   -741    103  -1048       C  
ATOM    809  N   LEU A 572      40.498  47.437  15.455  1.00 29.36           N  
ANISOU  809  N   LEU A 572     3790   2645   4722   -781    267   -701       N  
ATOM    810  CA  LEU A 572      40.360  47.004  14.037  1.00 29.53           C  
ANISOU  810  CA  LEU A 572     3832   2681   4706   -798    322   -578       C  
ATOM    811  C   LEU A 572      39.099  46.163  13.696  1.00 27.53           C  
ANISOU  811  C   LEU A 572     3613   2478   4370   -682    310   -503       C  
ATOM    812  O   LEU A 572      38.508  46.261  12.586  1.00 26.76           O  
ANISOU  812  O   LEU A 572     3583   2337   4250   -677    335   -395       O  
ATOM    813  CB  LEU A 572      41.642  46.298  13.626  1.00 31.32           C  
ANISOU  813  CB  LEU A 572     3959   3008   4933   -881    362   -597       C  
ATOM    814  CG  LEU A 572      42.833  47.289  13.508  1.00 34.32           C  
ANISOU  814  CG  LEU A 572     4315   3319   5407  -1025    400   -642       C  
ATOM    815  CD1 LEU A 572      44.153  46.529  13.447  1.00 35.56           C  
ANISOU  815  CD1 LEU A 572     4334   3592   5585  -1091    426   -707       C  
ATOM    816  CD2 LEU A 572      42.660  48.186  12.293  1.00 36.16           C  
ANISOU  816  CD2 LEU A 572     4650   3434   5654  -1109    465   -534       C  
ATOM    817  N   LEU A 573      38.657  45.339  14.635  1.00 25.33           N  
ANISOU  817  N   LEU A 573     3295   2289   4040   -594    267   -556       N  
ATOM    818  CA  LEU A 573      37.385  44.627  14.440  1.00 23.61           C  
ANISOU  818  CA  LEU A 573     3106   2110   3755   -489    255   -498       C  
ATOM    819  C   LEU A 573      36.176  45.559  14.545  1.00 23.44           C  
ANISOU  819  C   LEU A 573     3161   1976   3770   -427    239   -486       C  
ATOM    820  O   LEU A 573      35.179  45.372  13.842  1.00 22.52           O  
ANISOU  820  O   LEU A 573     3083   1844   3631   -368    237   -407       O  
ATOM    821  CB  LEU A 573      37.243  43.474  15.437  1.00 22.52           C  
ANISOU  821  CB  LEU A 573     2912   2095   3548   -426    218   -554       C  
ATOM    822  CG  LEU A 573      38.238  42.351  15.247  1.00 22.85           C  
ANISOU  822  CG  LEU A 573     2876   2245   3561   -456    217   -556       C  
ATOM    823  CD1 LEU A 573      37.920  41.235  16.236  1.00 22.30           C  
ANISOU  823  CD1 LEU A 573     2778   2274   3420   -387    165   -592       C  
ATOM    824  CD2 LEU A 573      38.201  41.777  13.815  1.00 22.72           C  
ANISOU  824  CD2 LEU A 573     2860   2253   3520   -468    265   -460       C  
ATOM    825  N   LEU A 574      36.259  46.525  15.441  1.00 24.63           N  
ANISOU  825  N   LEU A 574     3326   2050   3981   -437    220   -575       N  
ATOM    826  CA  LEU A 574      35.219  47.568  15.546  1.00 25.77           C  
ANISOU  826  CA  LEU A 574     3536   2065   4190   -381    203   -583       C  
ATOM    827  C   LEU A 574      35.050  48.314  14.234  1.00 26.59           C  
ANISOU  827  C   LEU A 574     3715   2042   4345   -411    209   -468       C  
ATOM    828  O   LEU A 574      33.949  48.643  13.831  1.00 25.69           O  
ANISOU  828  O   LEU A 574     3650   1855   4258   -336    183   -420       O  
ATOM    829  CB  LEU A 574      35.512  48.572  16.668  1.00 26.84           C  
ANISOU  829  CB  LEU A 574     3679   2127   4394   -403    187   -710       C  
ATOM    830  CG  LEU A 574      35.435  48.011  18.066  1.00 26.44           C  
ANISOU  830  CG  LEU A 574     3581   2184   4280   -366    172   -828       C  
ATOM    831  CD1 LEU A 574      35.842  49.075  19.078  1.00 28.08           C  
ANISOU  831  CD1 LEU A 574     3803   2314   4551   -404    156   -958       C  
ATOM    832  CD2 LEU A 574      34.029  47.504  18.335  1.00 26.06           C  
ANISOU  832  CD2 LEU A 574     3535   2182   4186   -256    176   -830       C  
ATOM    833  N   LYS A 575      36.165  48.617  13.584  1.00 28.64           N  
ANISOU  833  N   LYS A 575     3986   2274   4623   -528    239   -428       N  
ATOM    834  CA  LYS A 575      36.125  49.248  12.277  1.00 30.12           C  
ANISOU  834  CA  LYS A 575     4261   2352   4833   -582    249   -304       C  
ATOM    835  C   LYS A 575      35.373  48.421  11.236  1.00 28.07           C  
ANISOU  835  C   LYS A 575     4025   2150   4491   -531    248   -189       C  
ATOM    836  O   LYS A 575      34.536  48.935  10.471  1.00 27.98           O  
ANISOU  836  O   LYS A 575     4098   2035   4497   -496    212    -97       O  
ATOM    837  CB  LYS A 575      37.555  49.491  11.793  1.00 33.22           C  
ANISOU  837  CB  LYS A 575     4644   2743   5236   -736    305   -292       C  
ATOM    838  CG  LYS A 575      37.646  50.432  10.631  1.00 37.22           C  
ANISOU  838  CG  LYS A 575     5263   3109   5772   -825    320   -176       C  
ATOM    839  CD  LYS A 575      39.094  50.546  10.137  1.00 39.90           C  
ANISOU  839  CD  LYS A 575     5576   3472   6111   -993    397   -172       C  
ATOM    840  CE  LYS A 575      39.175  51.403   8.874  1.00 43.13           C  
ANISOU  840  CE  LYS A 575     6117   3749   6522  -1102    423    -37       C  
ATOM    841  NZ  LYS A 575      38.568  50.693   7.710  1.00 43.64           N  
ANISOU  841  NZ  LYS A 575     6236   3871   6475  -1075    431     88       N  
ATOM    842  N   ALA A 576      35.669  47.124  11.182  1.00 25.64           N  
ANISOU  842  N   ALA A 576     3643   2002   4097   -524    277   -194       N  
ATOM    843  CA  ALA A 576      34.957  46.224  10.329  1.00 23.58           C  
ANISOU  843  CA  ALA A 576     3393   1810   3756   -472    274   -107       C  
ATOM    844  C   ALA A 576      33.457  46.178  10.687  1.00 22.50           C  
ANISOU  844  C   ALA A 576     3268   1650   3631   -337    216   -109       C  
ATOM    845  O   ALA A 576      32.593  46.064   9.820  1.00 22.39           O  
ANISOU  845  O   ALA A 576     3302   1612   3593   -292    186    -19       O  
ATOM    846  CB  ALA A 576      35.555  44.824  10.425  1.00 23.32           C  
ANISOU  846  CB  ALA A 576     3269   1945   3647   -480    308   -138       C  
ATOM    847  N   TRP A 577      33.192  46.158  11.990  1.00 22.01           N  
ANISOU  847  N   TRP A 577     3153   1614   3597   -279    203   -221       N  
ATOM    848  CA  TRP A 577      31.827  46.067  12.513  1.00 21.33           C  
ANISOU  848  CA  TRP A 577     3054   1525   3526   -159    168   -255       C  
ATOM    849  C   TRP A 577      31.056  47.294  12.019  1.00 22.61           C  
ANISOU  849  C   TRP A 577     3291   1518   3784   -121    121   -212       C  
ATOM    850  O   TRP A 577      29.943  47.145  11.481  1.00 22.80           O  
ANISOU  850  O   TRP A 577     3327   1523   3813    -40     81   -157       O  
ATOM    851  CB  TRP A 577      31.840  46.020  14.019  1.00 20.87           C  
ANISOU  851  CB  TRP A 577     2940   1514   3474   -132    175   -391       C  
ATOM    852  CG  TRP A 577      30.516  45.618  14.582  1.00 20.05           C  
ANISOU  852  CG  TRP A 577     2804   1453   3361    -26    165   -435       C  
ATOM    853  CD1 TRP A 577      30.132  44.370  14.988  1.00 19.30           C  
ANISOU  853  CD1 TRP A 577     2657   1498   3179      7    180   -449       C  
ATOM    854  CD2 TRP A 577      29.424  46.481  14.841  1.00 21.08           C  
ANISOU  854  CD2 TRP A 577     2946   1484   3581     54    142   -481       C  
ATOM    855  NE1 TRP A 577      28.831  44.412  15.449  1.00 19.28           N  
ANISOU  855  NE1 TRP A 577     2630   1495   3199     95    177   -498       N  
ATOM    856  CE2 TRP A 577      28.374  45.688  15.366  1.00 20.67           C  
ANISOU  856  CE2 TRP A 577     2838   1529   3489    130    154   -524       C  
ATOM    857  CE3 TRP A 577      29.197  47.842  14.628  1.00 22.42           C  
ANISOU  857  CE3 TRP A 577     3167   1482   3869     71    109   -488       C  
ATOM    858  CZ2 TRP A 577      27.118  46.225  15.706  1.00 21.23           C  
ANISOU  858  CZ2 TRP A 577     2885   1542   3640    224    144   -590       C  
ATOM    859  CZ3 TRP A 577      27.933  48.381  14.966  1.00 23.38           C  
ANISOU  859  CZ3 TRP A 577     3271   1535   4079    176     85   -551       C  
ATOM    860  CH2 TRP A 577      26.918  47.542  15.494  1.00 22.61           C  
ANISOU  860  CH2 TRP A 577     3099   1551   3941    252    108   -606       C  
ATOM    861  N   ASP A 578      31.672  48.463  12.144  1.00 24.27           N  
ANISOU  861  N   ASP A 578     3548   1599   4073   -181    118   -234       N  
ATOM    862  CA  ASP A 578      31.049  49.740  11.709  1.00 27.01           C  
ANISOU  862  CA  ASP A 578     3978   1755   4529   -150     60   -193       C  
ATOM    863  C   ASP A 578      30.740  49.754  10.212  1.00 28.12           C  
ANISOU  863  C   ASP A 578     4203   1842   4639   -164     23    -31       C  
ATOM    864  O   ASP A 578      29.691  50.229   9.789  1.00 28.35           O  
ANISOU  864  O   ASP A 578     4275   1767   4728    -80    -51     17       O  
ATOM    865  CB  ASP A 578      31.918  50.939  12.075  1.00 28.14           C  
ANISOU  865  CB  ASP A 578     4167   1768   4759   -233     66   -241       C  
ATOM    866  CG  ASP A 578      31.993  51.192  13.586  1.00 28.92           C  
ANISOU  866  CG  ASP A 578     4201   1883   4903   -204     81   -413       C  
ATOM    867  OD1 ASP A 578      31.092  50.760  14.380  1.00 28.89           O  
ANISOU  867  OD1 ASP A 578     4137   1949   4890   -101     79   -499       O  
ATOM    868  OD2 ASP A 578      32.965  51.844  14.009  1.00 29.61           O  
ANISOU  868  OD2 ASP A 578     4301   1918   5032   -293     99   -469       O  
ATOM    869  N   HIS A 579      31.646  49.205   9.404  1.00 28.64           N  
ANISOU  869  N   HIS A 579     4290   1982   4610   -271     70     49       N  
ATOM    870  CA  HIS A 579      31.419  49.190   7.963  1.00 29.97           C  
ANISOU  870  CA  HIS A 579     4552   2113   4724   -303     41    203       C  
ATOM    871  C   HIS A 579      30.214  48.335   7.572  1.00 28.15           C  
ANISOU  871  C   HIS A 579     4296   1955   4445   -191     -7    242       C  
ATOM    872  O   HIS A 579      29.409  48.715   6.720  1.00 29.22           O  
ANISOU  872  O   HIS A 579     4509   1998   4594   -150    -86    341       O  
ATOM    873  CB  HIS A 579      32.703  48.777   7.214  1.00 31.72           C  
ANISOU  873  CB  HIS A 579     4792   2410   4849   -452    123    258       C  
ATOM    874  CG  HIS A 579      32.531  48.731   5.720  1.00 34.36           C  
ANISOU  874  CG  HIS A 579     5235   2720   5100   -504    106    411       C  
ATOM    875  ND1 HIS A 579      32.652  49.851   4.921  1.00 37.83           N  
ANISOU  875  ND1 HIS A 579     5815   2997   5564   -582     73    519       N  
ATOM    876  CD2 HIS A 579      32.175  47.715   4.896  1.00 35.14           C  
ANISOU  876  CD2 HIS A 579     5335   2930   5088   -488    108    475       C  
ATOM    877  CE1 HIS A 579      32.413  49.514   3.663  1.00 38.09           C  
ANISOU  877  CE1 HIS A 579     5934   3050   5488   -619     58    646       C  
ATOM    878  NE2 HIS A 579      32.113  48.227   3.627  1.00 37.75           N  
ANISOU  878  NE2 HIS A 579     5805   3174   5364   -560     79    616       N  
ATOM    879  N   TYR A 580      30.055  47.187   8.213  1.00 25.73           N  
ANISOU  879  N   TYR A 580     3883   1808   4087   -142     30    166       N  
ATOM    880  CA  TYR A 580      28.918  46.323   7.992  1.00 24.14           C  
ANISOU  880  CA  TYR A 580     3642   1683   3849    -42     -9    185       C  
ATOM    881  C   TYR A 580      27.607  47.031   8.446  1.00 24.74           C  
ANISOU  881  C   TYR A 580     3705   1654   4043     84    -85    143       C  
ATOM    882  O   TYR A 580      26.553  46.880   7.781  1.00 25.09           O  
ANISOU  882  O   TYR A 580     3761   1679   4095    160   -157    204       O  
ATOM    883  CB  TYR A 580      29.098  45.007   8.776  1.00 22.52           C  
ANISOU  883  CB  TYR A 580     3327   1655   3575    -27     50    101       C  
ATOM    884  CG  TYR A 580      28.020  43.987   8.629  1.00 22.23           C  
ANISOU  884  CG  TYR A 580     3240   1710   3495     58     25    111       C  
ATOM    885  CD1 TYR A 580      26.833  44.078   9.366  1.00 22.41           C  
ANISOU  885  CD1 TYR A 580     3207   1723   3587    165     -7     41       C  
ATOM    886  CD2 TYR A 580      28.180  42.888   7.789  1.00 21.76           C  
ANISOU  886  CD2 TYR A 580     3180   1755   3331     26     41    176       C  
ATOM    887  CE1 TYR A 580      25.847  43.119   9.253  1.00 22.59           C  
ANISOU  887  CE1 TYR A 580     3173   1833   3575    231    -24     44       C  
ATOM    888  CE2 TYR A 580      27.207  41.906   7.686  1.00 21.77           C  
ANISOU  888  CE2 TYR A 580     3133   1842   3298     96     17    178       C  
ATOM    889  CZ  TYR A 580      26.039  42.036   8.410  1.00 22.41           C  
ANISOU  889  CZ  TYR A 580     3158   1907   3449    195    -16    117       C  
ATOM    890  OH  TYR A 580      25.094  41.088   8.298  1.00 23.44           O  
ANISOU  890  OH  TYR A 580     3235   2120   3551    251    -34    117       O  
ATOM    891  N   ASN A 581      27.671  47.739   9.566  1.00 24.44           N  
ANISOU  891  N   ASN A 581     3633   1558   4096    109    -71     29       N  
ATOM    892  CA  ASN A 581      26.462  48.383  10.099  1.00 26.01           C  
ANISOU  892  CA  ASN A 581     3799   1665   4417    231   -128    -42       C  
ATOM    893  C   ASN A 581      25.996  49.504   9.157  1.00 29.03           C  
ANISOU  893  C   ASN A 581     4282   1853   4894    260   -231     56       C  
ATOM    894  O   ASN A 581      24.819  49.754   9.023  1.00 29.66           O  
ANISOU  894  O   ASN A 581     4340   1869   5060    373   -309     51       O  
ATOM    895  CB  ASN A 581      26.732  48.943  11.468  1.00 25.98           C  
ANISOU  895  CB  ASN A 581     3749   1638   4482    238    -83   -194       C  
ATOM    896  CG  ASN A 581      25.458  49.373  12.199  1.00 26.52           C  
ANISOU  896  CG  ASN A 581     3753   1656   4666    367   -113   -307       C  
ATOM    897  OD1 ASN A 581      24.396  48.746  12.088  1.00 25.95           O  
ANISOU  897  OD1 ASN A 581     3618   1651   4593    451   -131   -311       O  
ATOM    898  ND2 ASN A 581      25.603  50.367  13.007  1.00 28.01           N  
ANISOU  898  ND2 ASN A 581     3946   1743   4954    376   -106   -414       N  
ATOM    899  N   SER A 582      26.950  50.185   8.547  1.00 31.53           N  
ANISOU  899  N   SER A 582     4706   2073   5200    153   -233    141       N  
ATOM    900  CA  SER A 582      26.655  51.234   7.551  1.00 35.22           C  
ANISOU  900  CA  SER A 582     5301   2346   5735    154   -336    263       C  
ATOM    901  C   SER A 582      26.051  50.725   6.245  1.00 37.34           C  
ANISOU  901  C   SER A 582     5628   2635   5923    170   -410    410       C  
ATOM    902  O   SER A 582      25.285  51.439   5.600  1.00 39.67           O  
ANISOU  902  O   SER A 582     5998   2781   6295    232   -533    489       O  
ATOM    903  CB  SER A 582      27.927  51.955   7.233  1.00 36.25           C  
ANISOU  903  CB  SER A 582     5536   2390   5848      5   -299    321       C  
ATOM    904  OG  SER A 582      28.315  52.649   8.384  1.00 38.03           O  
ANISOU  904  OG  SER A 582     5721   2555   6175      4   -263    187       O  
ATOM    905  N   THR A 583      26.465  49.550   5.812  1.00 36.28           N  
ANISOU  905  N   THR A 583     5471   2675   5639    109   -345    449       N  
ATOM    906  CA  THR A 583      26.109  49.029   4.499  1.00 37.80           C  
ANISOU  906  CA  THR A 583     5735   2901   5728     94   -402    587       C  
ATOM    907  C   THR A 583      24.974  48.051   4.570  1.00 37.62           C  
ANISOU  907  C   THR A 583     5610   2991   5694    209   -438    551       C  
ATOM    908  O   THR A 583      24.087  48.093   3.754  1.00 40.27           O  
ANISOU  908  O   THR A 583     5988   3278   6035    268   -548    634       O  
ATOM    909  CB  THR A 583      27.344  48.382   3.837  1.00 37.81           C  
ANISOU  909  CB  THR A 583     5782   3014   5569    -61   -301    650       C  
ATOM    910  OG1 THR A 583      27.891  47.388   4.721  1.00 38.20           O  
ANISOU  910  OG1 THR A 583     5704   3233   5578    -73   -191    532       O  
ATOM    911  CG2 THR A 583      28.397  49.461   3.566  1.00 39.62           C  
ANISOU  911  CG2 THR A 583     6126   3115   5813   -192   -273    705       C  
ATOM    912  N   LYS A 584      24.991  47.154   5.534  1.00 35.53           N  
ANISOU  912  N   LYS A 584     5214   2874   5411    236   -352    431       N  
ATOM    913  CA  LYS A 584      23.971  46.114   5.651  1.00 35.65           C  
ANISOU  913  CA  LYS A 584     5129   3009   5408    327   -369    392       C  
ATOM    914  C   LYS A 584      23.004  46.347   6.827  1.00 34.42           C  
ANISOU  914  C   LYS A 584     4855   2838   5386    448   -377    253       C  
ATOM    915  O   LYS A 584      21.858  45.921   6.778  1.00 36.55           O  
ANISOU  915  O   LYS A 584     5051   3143   5692    541   -428    231       O  
ATOM    916  CB  LYS A 584      24.627  44.750   5.784  1.00 35.51           C  
ANISOU  916  CB  LYS A 584     5056   3179   5256    261   -267    368       C  
ATOM    917  CG  LYS A 584      25.302  44.252   4.515  1.00 37.64           C  
ANISOU  917  CG  LYS A 584     5416   3497   5389    160   -257    487       C  
ATOM    918  CD  LYS A 584      25.811  42.850   4.718  1.00 38.04           C  
ANISOU  918  CD  LYS A 584     5393   3724   5335    120   -167    443       C  
ATOM    919  CE  LYS A 584      25.911  41.996   3.460  1.00 39.52           C  
ANISOU  919  CE  LYS A 584     5632   3990   5393     68   -173    532       C  
ATOM    920  NZ  LYS A 584      26.588  40.689   3.830  1.00 38.99           N  
ANISOU  920  NZ  LYS A 584     5485   4078   5249     30    -78    468       N  
ATOM    921  N   GLY A 585      23.463  47.013   7.875  1.00 32.81           N  
ANISOU  921  N   GLY A 585     4628   2585   5252    440   -323    152       N  
ATOM    922  CA  GLY A 585      22.674  47.182   9.093  1.00 31.32           C  
ANISOU  922  CA  GLY A 585     4328   2404   5170    535   -302     -1       C  
ATOM    923  C   GLY A 585      22.909  46.011  10.008  1.00 28.21           C  
ANISOU  923  C   GLY A 585     3843   2196   4680    506   -194    -89       C  
ATOM    924  O   GLY A 585      22.933  44.855   9.572  1.00 27.12           O  
ANISOU  924  O   GLY A 585     3687   2185   4432    478   -175    -37       O  
ATOM    925  N   SER A 586      23.102  46.318  11.285  1.00 26.80           N  
ANISOU  925  N   SER A 586     3615   2028   4539    509   -129   -224       N  
ATOM    926  CA  SER A 586      23.267  45.281  12.309  1.00 24.45           C  
ANISOU  926  CA  SER A 586     3243   1897   4151    482    -36   -312       C  
ATOM    927  C   SER A 586      22.087  45.316  13.255  1.00 24.65           C  
ANISOU  927  C   SER A 586     3167   1949   4249    570    -12   -447       C  
ATOM    928  O   SER A 586      21.563  46.366  13.530  1.00 25.53           O  
ANISOU  928  O   SER A 586     3265   1943   4492    636    -40   -518       O  
ATOM    929  CB  SER A 586      24.527  45.523  13.123  1.00 23.43           C  
ANISOU  929  CB  SER A 586     3142   1780   3980    396     25   -368       C  
ATOM    930  OG  SER A 586      24.678  44.469  14.062  1.00 21.86           O  
ANISOU  930  OG  SER A 586     2885   1737   3682    369     94   -436       O  
ATOM    931  N   ALA A 587      21.712  44.148  13.728  1.00 24.06           N  
ANISOU  931  N   ALA A 587     3024   2027   4090    564     44   -481       N  
ATOM    932  CA  ALA A 587      20.777  44.007  14.841  1.00 25.04           C  
ANISOU  932  CA  ALA A 587     3052   2215   4247    611    105   -625       C  
ATOM    933  C   ALA A 587      21.493  44.001  16.221  1.00 24.80           C  
ANISOU  933  C   ALA A 587     3028   2248   4147    548    193   -735       C  
ATOM    934  O   ALA A 587      20.822  43.975  17.256  1.00 26.10           O  
ANISOU  934  O   ALA A 587     3128   2468   4321    569    258   -867       O  
ATOM    935  CB  ALA A 587      20.003  42.718  14.669  1.00 24.96           C  
ANISOU  935  CB  ALA A 587     2975   2338   4171    619    124   -600       C  
ATOM    936  N   ASN A 588      22.824  44.052  16.235  1.00 22.46           N  
ANISOU  936  N   ASN A 588     2807   1945   3781    467    193   -690       N  
ATOM    937  CA  ASN A 588      23.593  43.871  17.456  1.00 21.08           C  
ANISOU  937  CA  ASN A 588     2645   1844   3522    399    254   -776       C  
ATOM    938  C   ASN A 588      24.112  45.220  18.015  1.00 21.55           C  
ANISOU  938  C   ASN A 588     2740   1786   3663    392    252   -866       C  
ATOM    939  O   ASN A 588      24.149  46.235  17.339  1.00 21.36           O  
ANISOU  939  O   ASN A 588     2749   1615   3751    421    199   -834       O  
ATOM    940  CB  ASN A 588      24.782  42.924  17.162  1.00 19.60           C  
ANISOU  940  CB  ASN A 588     2499   1736   3210    313    248   -679       C  
ATOM    941  CG  ASN A 588      24.388  41.469  17.035  1.00 18.87           C  
ANISOU  941  CG  ASN A 588     2374   1776   3020    306    265   -627       C  
ATOM    942  OD1 ASN A 588      23.247  41.083  17.278  1.00 19.07           O  
ANISOU  942  OD1 ASN A 588     2343   1851   3051    349    291   -666       O  
ATOM    943  ND2 ASN A 588      25.383  40.632  16.719  1.00 17.53           N  
ANISOU  943  ND2 ASN A 588     2233   1664   2761    244    252   -550       N  
ATOM    944  N   ASP A 589      24.514  45.203  19.269  1.00 21.24           N  
ANISOU  944  N   ASP A 589     2702   1809   3560    346    305   -978       N  
ATOM    945  CA  ASP A 589      25.199  46.339  19.864  1.00 22.34           C  
ANISOU  945  CA  ASP A 589     2881   1853   3754    319    303  -1068       C  
ATOM    946  C   ASP A 589      26.612  46.435  19.262  1.00 21.83           C  
ANISOU  946  C   ASP A 589     2879   1749   3667    240    259   -967       C  
ATOM    947  O   ASP A 589      27.270  45.406  18.995  1.00 20.61           O  
ANISOU  947  O   ASP A 589     2729   1694   3408    187    256   -883       O  
ATOM    948  CB  ASP A 589      25.373  46.134  21.339  1.00 22.73           C  
ANISOU  948  CB  ASP A 589     2925   2002   3708    275    364  -1204       C  
ATOM    949  CG  ASP A 589      24.055  46.039  22.065  1.00 23.50           C  
ANISOU  949  CG  ASP A 589     2959   2156   3813    331    432  -1324       C  
ATOM    950  OD1 ASP A 589      23.163  46.888  21.860  1.00 24.60           O  
ANISOU  950  OD1 ASP A 589     3057   2195   4096    415    432  -1389       O  
ATOM    951  OD2 ASP A 589      23.975  45.120  22.888  1.00 23.93           O  
ANISOU  951  OD2 ASP A 589     3007   2354   3729    284    485  -1358       O  
ATOM    952  N   ARG A 590      27.060  47.659  19.075  1.00 22.52           N  
ANISOU  952  N   ARG A 590     3008   1689   3860    231    229   -987       N  
ATOM    953  CA  ARG A 590      28.469  47.874  18.746  1.00 22.92           C  
ANISOU  953  CA  ARG A 590     3108   1706   3894    137    206   -928       C  
ATOM    954  C   ARG A 590      29.359  47.316  19.890  1.00 22.30           C  
ANISOU  954  C   ARG A 590     3021   1750   3704     64    231  -1007       C  
ATOM    955  O   ARG A 590      29.208  47.731  21.041  1.00 22.27           O  
ANISOU  955  O   ARG A 590     3013   1753   3695     66    254  -1145       O  
ATOM    956  CB  ARG A 590      28.741  49.339  18.597  1.00 24.64           C  
ANISOU  956  CB  ARG A 590     3375   1742   4246    129    176   -961       C  
ATOM    957  CG  ARG A 590      30.108  49.650  18.062  1.00 25.07           C  
ANISOU  957  CG  ARG A 590     3476   1746   4302     24    158   -890       C  
ATOM    958  CD  ARG A 590      30.219  51.129  17.719  1.00 27.38           C  
ANISOU  958  CD  ARG A 590     3830   1834   4740     16    123   -897       C  
ATOM    959  NE  ARG A 590      31.497  51.355  17.028  1.00 28.30           N  
ANISOU  959  NE  ARG A 590     3991   1908   4854   -100    116   -809       N  
ATOM    960  CZ  ARG A 590      32.618  51.794  17.591  1.00 29.72           C  
ANISOU  960  CZ  ARG A 590     4176   2072   5044   -194    126   -877       C  
ATOM    961  NH1 ARG A 590      32.670  52.157  18.862  1.00 30.81           N  
ANISOU  961  NH1 ARG A 590     4294   2219   5195   -189    133  -1034       N  
ATOM    962  NH2 ARG A 590      33.706  51.957  16.830  1.00 30.60           N  
ANISOU  962  NH2 ARG A 590     4316   2150   5161   -303    130   -792       N  
ATOM    963  N   PRO A 591      30.268  46.383  19.572  1.00 21.66           N  
ANISOU  963  N   PRO A 591     2935   1760   3534      2    220   -924       N  
ATOM    964  CA  PRO A 591      30.976  45.638  20.617  1.00 21.63           C  
ANISOU  964  CA  PRO A 591     2919   1881   3419    -51    223   -983       C  
ATOM    965  C   PRO A 591      32.152  46.403  21.193  1.00 23.13           C  
ANISOU  965  C   PRO A 591     3128   2024   3637   -126    200  -1058       C  
ATOM    966  O   PRO A 591      33.245  45.879  21.279  1.00 23.78           O  
ANISOU  966  O   PRO A 591     3198   2168   3671   -190    173  -1038       O  
ATOM    967  CB  PRO A 591      31.398  44.330  19.901  1.00 20.66           C  
ANISOU  967  CB  PRO A 591     2775   1857   3218    -70    210   -863       C  
ATOM    968  CG  PRO A 591      31.565  44.755  18.482  1.00 20.43           C  
ANISOU  968  CG  PRO A 591     2760   1735   3269    -74    202   -757       C  
ATOM    969  CD  PRO A 591      30.504  45.809  18.237  1.00 20.93           C  
ANISOU  969  CD  PRO A 591     2845   1674   3432     -9    205   -776       C  
ATOM    970  N   ASP A 592      31.900  47.600  21.682  1.00 24.17           N  
ANISOU  970  N   ASP A 592     3283   2051   3850   -116    207  -1161       N  
ATOM    971  CA  ASP A 592      32.961  48.485  22.137  1.00 25.04           C  
ANISOU  971  CA  ASP A 592     3413   2092   4009   -191    183  -1237       C  
ATOM    972  C   ASP A 592      32.966  48.623  23.662  1.00 24.94           C  
ANISOU  972  C   ASP A 592     3409   2137   3928   -206    187  -1396       C  
ATOM    973  O   ASP A 592      33.673  49.415  24.176  1.00 26.21           O  
ANISOU  973  O   ASP A 592     3588   2240   4130   -260    165  -1483       O  
ATOM    974  CB  ASP A 592      32.828  49.853  21.431  1.00 26.99           C  
ANISOU  974  CB  ASP A 592     3696   2148   4412   -183    178  -1228       C  
ATOM    975  CG  ASP A 592      31.485  50.539  21.724  1.00 28.59           C  
ANISOU  975  CG  ASP A 592     3907   2270   4687    -87    199  -1308       C  
ATOM    976  OD1 ASP A 592      30.873  50.199  22.762  1.00 29.73           O  
ANISOU  976  OD1 ASP A 592     4029   2505   4760    -52    231  -1417       O  
ATOM    977  OD2 ASP A 592      31.067  51.457  20.963  1.00 30.72           O  
ANISOU  977  OD2 ASP A 592     4205   2381   5087    -50    181  -1270       O  
ATOM    978  N   PHE A 593      32.162  47.842  24.363  1.00 23.71           N  
ANISOU  978  N   PHE A 593     3246   2099   3665   -167    216  -1433       N  
ATOM    979  CA  PHE A 593      31.926  48.022  25.796  1.00 24.36           C  
ANISOU  979  CA  PHE A 593     3351   2238   3668   -181    236  -1589       C  
ATOM    980  C   PHE A 593      32.586  46.913  26.635  1.00 23.51           C  
ANISOU  980  C   PHE A 593     3255   2286   3391   -240    200  -1586       C  
ATOM    981  O   PHE A 593      32.441  46.922  27.863  1.00 24.52           O  
ANISOU  981  O   PHE A 593     3417   2481   3418   -267    211  -1704       O  
ATOM    982  CB  PHE A 593      30.405  47.982  26.085  1.00 24.83           C  
ANISOU  982  CB  PHE A 593     3396   2320   3719   -102    310  -1648       C  
ATOM    983  CG  PHE A 593      29.737  46.795  25.503  1.00 23.53           C  
ANISOU  983  CG  PHE A 593     3200   2247   3493    -62    329  -1529       C  
ATOM    984  CD1 PHE A 593      29.654  45.587  26.194  1.00 23.23           C  
ANISOU  984  CD1 PHE A 593     3172   2366   3290    -93    340  -1517       C  
ATOM    985  CD2 PHE A 593      29.193  46.854  24.228  1.00 23.01           C  
ANISOU  985  CD2 PHE A 593     3104   2106   3531      1    328  -1421       C  
ATOM    986  CE1 PHE A 593      29.105  44.446  25.585  1.00 22.34           C  
ANISOU  986  CE1 PHE A 593     3032   2327   3129    -64    352  -1399       C  
ATOM    987  CE2 PHE A 593      28.599  45.755  23.650  1.00 22.12           C  
ANISOU  987  CE2 PHE A 593     2963   2076   3366     33    340  -1314       C  
ATOM    988  CZ  PHE A 593      28.582  44.521  24.299  1.00 21.57           C  
ANISOU  988  CZ  PHE A 593     2896   2158   3141     -1    353  -1301       C  
ATOM    989  N   PHE A 594      33.289  45.972  25.998  1.00 21.93           N  
ANISOU  989  N   PHE A 594     3033   2140   3160   -261    155  -1458       N  
ATOM    990  CA  PHE A 594      33.942  44.870  26.718  1.00 21.20           C  
ANISOU  990  CA  PHE A 594     2952   2178   2924   -307     99  -1443       C  
ATOM    991  C   PHE A 594      35.205  45.373  27.417  1.00 22.05           C  
ANISOU  991  C   PHE A 594     3072   2275   3033   -382     26  -1525       C  
ATOM    992  O   PHE A 594      35.926  46.216  26.879  1.00 22.63           O  
ANISOU  992  O   PHE A 594     3121   2249   3231   -410      9  -1533       O  
ATOM    993  CB  PHE A 594      34.314  43.762  25.769  1.00 19.73           C  
ANISOU  993  CB  PHE A 594     2729   2037   2732   -297     69  -1295       C  
ATOM    994  CG  PHE A 594      33.132  43.085  25.157  1.00 18.82           C  
ANISOU  994  CG  PHE A 594     2602   1951   2597   -232    126  -1214       C  
ATOM    995  CD1 PHE A 594      32.331  42.275  25.921  1.00 18.95           C  
ANISOU  995  CD1 PHE A 594     2646   2068   2486   -222    151  -1228       C  
ATOM    996  CD2 PHE A 594      32.894  43.185  23.830  1.00 18.33           C  
ANISOU  996  CD2 PHE A 594     2508   1823   2633   -194    149  -1119       C  
ATOM    997  CE1 PHE A 594      31.276  41.576  25.363  1.00 18.14           C  
ANISOU  997  CE1 PHE A 594     2524   1997   2369   -172    200  -1155       C  
ATOM    998  CE2 PHE A 594      31.822  42.539  23.244  1.00 17.60           C  
ANISOU  998  CE2 PHE A 594     2402   1760   2525   -137    189  -1047       C  
ATOM    999  CZ  PHE A 594      31.037  41.686  23.993  1.00 17.72           C  
ANISOU  999  CZ  PHE A 594     2430   1877   2426   -125    213  -1064       C  
ATOM   1000  N   LYS A 595      35.433  44.885  28.627  1.00 22.28           N  
ANISOU 1000  N   LYS A 595     3143   2403   2919   -421    -19  -1589       N  
ATOM   1001  CA  LYS A 595      36.593  45.285  29.437  1.00 23.10           C  
ANISOU 1001  CA  LYS A 595     3261   2511   3004   -494   -107  -1678       C  
ATOM   1002  C   LYS A 595      37.788  44.357  29.155  1.00 22.02           C  
ANISOU 1002  C   LYS A 595     3080   2427   2859   -521   -211  -1589       C  
ATOM   1003  O   LYS A 595      37.647  43.319  28.528  1.00 20.21           O  
ANISOU 1003  O   LYS A 595     2826   2244   2610   -486   -212  -1471       O  
ATOM   1004  CB  LYS A 595      36.258  45.233  30.936  1.00 24.74           C  
ANISOU 1004  CB  LYS A 595     3550   2803   3047   -528   -117  -1795       C  
ATOM   1005  CG  LYS A 595      35.154  46.165  31.405  1.00 26.19           C  
ANISOU 1005  CG  LYS A 595     3769   2946   3235   -506    -12  -1921       C  
ATOM   1006  CD  LYS A 595      35.414  47.597  31.045  1.00 27.48           C  
ANISOU 1006  CD  LYS A 595     3907   2962   3571   -507      5  -2004       C  
ATOM   1007  CE  LYS A 595      34.398  48.515  31.656  1.00 29.12           C  
ANISOU 1007  CE  LYS A 595     4149   3127   3789   -483     95  -2155       C  
ATOM   1008  NZ  LYS A 595      34.804  49.914  31.415  1.00 30.45           N  
ANISOU 1008  NZ  LYS A 595     4305   3138   4125   -493     90  -2242       N  
ATOM   1009  N   ASP A 596      38.940  44.723  29.733  1.00 22.55           N  
ANISOU 1009  N   ASP A 596     3138   2492   2939   -585   -303  -1664       N  
ATOM   1010  CA  ASP A 596      40.163  43.950  29.501  1.00 22.32           C  
ANISOU 1010  CA  ASP A 596     3046   2503   2930   -608   -411  -1605       C  
ATOM   1011  C   ASP A 596      40.172  42.532  30.153  1.00 22.34           C  
ANISOU 1011  C   ASP A 596     3087   2626   2777   -594   -498  -1547       C  
ATOM   1012  O   ASP A 596      41.026  41.709  29.813  1.00 22.41           O  
ANISOU 1012  O   ASP A 596     3035   2664   2816   -590   -584  -1482       O  
ATOM   1013  CB  ASP A 596      41.413  44.770  29.870  1.00 23.35           C  
ANISOU 1013  CB  ASP A 596     3137   2592   3142   -680   -492  -1707       C  
ATOM   1014  CG  ASP A 596      41.540  45.049  31.368  1.00 24.62           C  
ANISOU 1014  CG  ASP A 596     3376   2801   3177   -727   -569  -1833       C  
ATOM   1015  OD1 ASP A 596      40.556  44.759  32.109  1.00 24.56           O  
ANISOU 1015  OD1 ASP A 596     3461   2852   3018   -708   -533  -1851       O  
ATOM   1016  OD2 ASP A 596      42.588  45.610  31.827  1.00 25.60           O  
ANISOU 1016  OD2 ASP A 596     3473   2906   3349   -790   -658  -1925       O  
ATOM   1017  N   ASP A 597      39.174  42.217  30.987  1.00 22.65           N  
ANISOU 1017  N   ASP A 597     3222   2726   2659   -586   -465  -1563       N  
ATOM   1018  CA  ASP A 597      39.014  40.853  31.515  1.00 22.61           C  
ANISOU 1018  CA  ASP A 597     3272   2821   2499   -579   -533  -1486       C  
ATOM   1019  C   ASP A 597      38.061  39.978  30.723  1.00 21.19           C  
ANISOU 1019  C   ASP A 597     3084   2658   2309   -521   -452  -1366       C  
ATOM   1020  O   ASP A 597      37.900  38.817  31.058  1.00 21.04           O  
ANISOU 1020  O   ASP A 597     3111   2708   2176   -517   -503  -1291       O  
ATOM   1021  CB  ASP A 597      38.593  40.880  33.000  1.00 24.38           C  
ANISOU 1021  CB  ASP A 597     3619   3117   2527   -630   -556  -1570       C  
ATOM   1022  CG  ASP A 597      37.188  41.401  33.198  1.00 25.07           C  
ANISOU 1022  CG  ASP A 597     3757   3206   2562   -620   -400  -1626       C  
ATOM   1023  OD1 ASP A 597      36.688  42.167  32.346  1.00 24.81           O  
ANISOU 1023  OD1 ASP A 597     3664   3092   2670   -577   -293  -1640       O  
ATOM   1024  OD2 ASP A 597      36.579  41.111  34.261  1.00 26.88           O  
ANISOU 1024  OD2 ASP A 597     4089   3517   2608   -659   -383  -1668       O  
ATOM   1025  N   GLN A 598      37.423  40.511  29.694  1.00 20.14           N  
ANISOU 1025  N   GLN A 598     2901   2459   2292   -479   -335  -1344       N  
ATOM   1026  CA  GLN A 598      36.423  39.738  28.997  1.00 19.19           C  
ANISOU 1026  CA  GLN A 598     2776   2359   2156   -426   -259  -1243       C  
ATOM   1027  C   GLN A 598      37.024  38.529  28.268  1.00 18.50           C  
ANISOU 1027  C   GLN A 598     2640   2294   2095   -401   -329  -1123       C  
ATOM   1028  O   GLN A 598      37.984  38.672  27.574  1.00 18.18           O  
ANISOU 1028  O   GLN A 598     2524   2213   2171   -401   -368  -1109       O  
ATOM   1029  CB  GLN A 598      35.707  40.631  27.978  1.00 18.59           C  
ANISOU 1029  CB  GLN A 598     2654   2196   2211   -384   -143  -1244       C  
ATOM   1030  CG  GLN A 598      34.680  39.877  27.151  1.00 17.54           C  
ANISOU 1030  CG  GLN A 598     2506   2081   2077   -328    -74  -1142       C  
ATOM   1031  CD  GLN A 598      33.450  39.505  27.974  1.00 17.74           C  
ANISOU 1031  CD  GLN A 598     2594   2176   1972   -327    -12  -1170       C  
ATOM   1032  OE1 GLN A 598      32.887  40.345  28.727  1.00 18.73           O  
ANISOU 1032  OE1 GLN A 598     2753   2295   2068   -341     45  -1283       O  
ATOM   1033  NE2 GLN A 598      33.077  38.261  27.895  1.00 17.23           N  
ANISOU 1033  NE2 GLN A 598     2544   2176   1826   -319    -22  -1079       N  
ATOM   1034  N   LEU A 599      36.404  37.362  28.417  1.00 18.38           N  
ANISOU 1034  N   LEU A 599     2668   2341   1976   -385   -333  -1045       N  
ATOM   1035  CA  LEU A 599      36.745  36.147  27.651  1.00 18.06           C  
ANISOU 1035  CA  LEU A 599     2585   2312   1965   -350   -384   -933       C  
ATOM   1036  C   LEU A 599      35.923  36.005  26.410  1.00 17.03           C  
ANISOU 1036  C   LEU A 599     2409   2153   1908   -301   -280   -864       C  
ATOM   1037  O   LEU A 599      34.705  36.305  26.387  1.00 16.73           O  
ANISOU 1037  O   LEU A 599     2399   2118   1841   -287   -179   -872       O  
ATOM   1038  CB  LEU A 599      36.550  34.884  28.531  1.00 18.81           C  
ANISOU 1038  CB  LEU A 599     2766   2479   1904   -367   -462   -878       C  
ATOM   1039  CG  LEU A 599      37.423  34.879  29.778  1.00 20.85           C  
ANISOU 1039  CG  LEU A 599     3084   2768   2072   -417   -597   -931       C  
ATOM   1040  CD1 LEU A 599      37.028  33.698  30.681  1.00 21.98           C  
ANISOU 1040  CD1 LEU A 599     3342   2974   2036   -445   -664   -865       C  
ATOM   1041  CD2 LEU A 599      38.919  34.837  29.434  1.00 21.34           C  
ANISOU 1041  CD2 LEU A 599     3055   2796   2256   -405   -721   -940       C  
ATOM   1042  N   PHE A 600      36.562  35.452  25.384  1.00 16.53           N  
ANISOU 1042  N   PHE A 600     2274   2071   1937   -273   -309   -799       N  
ATOM   1043  CA  PHE A 600      35.876  35.107  24.150  1.00 15.96           C  
ANISOU 1043  CA  PHE A 600     2165   1980   1918   -229   -230   -723       C  
ATOM   1044  C   PHE A 600      36.344  33.727  23.719  1.00 16.10           C  
ANISOU 1044  C   PHE A 600     2156   2024   1937   -206   -299   -646       C  
ATOM   1045  O   PHE A 600      37.469  33.348  24.017  1.00 17.27           O  
ANISOU 1045  O   PHE A 600     2277   2179   2107   -215   -401   -661       O  
ATOM   1046  CB  PHE A 600      36.215  36.072  23.003  1.00 15.73           C  
ANISOU 1046  CB  PHE A 600     2069   1882   2026   -224   -171   -731       C  
ATOM   1047  CG  PHE A 600      35.827  37.506  23.247  1.00 16.43           C  
ANISOU 1047  CG  PHE A 600     2178   1916   2147   -240   -111   -804       C  
ATOM   1048  CD1 PHE A 600      36.631  38.347  23.989  1.00 17.57           C  
ANISOU 1048  CD1 PHE A 600     2326   2038   2311   -285   -152   -894       C  
ATOM   1049  CD2 PHE A 600      34.630  38.023  22.723  1.00 16.32           C  
ANISOU 1049  CD2 PHE A 600     2178   1865   2156   -206    -20   -789       C  
ATOM   1050  CE1 PHE A 600      36.263  39.672  24.206  1.00 18.32           C  
ANISOU 1050  CE1 PHE A 600     2443   2070   2448   -298    -98   -968       C  
ATOM   1051  CE2 PHE A 600      34.267  39.353  22.945  1.00 16.84           C  
ANISOU 1051  CE2 PHE A 600     2262   1865   2271   -211     26   -862       C  
ATOM   1052  CZ  PHE A 600      35.068  40.163  23.682  1.00 17.85           C  
ANISOU 1052  CZ  PHE A 600     2398   1967   2417   -257     -9   -952       C  
ATOM   1053  N   ILE A 601      35.485  33.033  23.017  1.00 15.25           N  
ANISOU 1053  N   ILE A 601     2051   1925   1818   -173   -247   -575       N  
ATOM   1054  CA  ILE A 601      35.912  31.882  22.165  1.00 15.60           C  
ANISOU 1054  CA  ILE A 601     2049   1973   1906   -142   -285   -509       C  
ATOM   1055  C   ILE A 601      36.022  32.378  20.752  1.00 14.84           C  
ANISOU 1055  C   ILE A 601     1883   1838   1916   -126   -210   -496       C  
ATOM   1056  O   ILE A 601      35.109  33.028  20.219  1.00 13.91           O  
ANISOU 1056  O   ILE A 601     1778   1700   1809   -118   -122   -484       O  
ATOM   1057  CB  ILE A 601      34.880  30.739  22.239  1.00 16.03           C  
ANISOU 1057  CB  ILE A 601     2156   2058   1876   -126   -277   -438       C  
ATOM   1058  CG1 ILE A 601      34.787  30.193  23.663  1.00 17.64           C  
ANISOU 1058  CG1 ILE A 601     2448   2300   1954   -159   -352   -437       C  
ATOM   1059  CG2 ILE A 601      35.214  29.603  21.233  1.00 16.18           C  
ANISOU 1059  CG2 ILE A 601     2126   2069   1951    -90   -306   -378       C  
ATOM   1060  CD1 ILE A 601      36.084  29.597  24.141  1.00 19.13           C  
ANISOU 1060  CD1 ILE A 601     2629   2484   2154   -160   -495   -440       C  
ATOM   1061  N   VAL A 602      37.145  32.078  20.119  1.00 15.12           N  
ANISOU 1061  N   VAL A 602     1846   1865   2034   -124   -246   -502       N  
ATOM   1062  CA  VAL A 602      37.392  32.479  18.758  1.00 15.11           C  
ANISOU 1062  CA  VAL A 602     1785   1835   2119   -126   -172   -491       C  
ATOM   1063  C   VAL A 602      37.593  31.185  17.948  1.00 15.04           C  
ANISOU 1063  C   VAL A 602     1737   1848   2131    -93   -189   -448       C  
ATOM   1064  O   VAL A 602      38.554  30.463  18.197  1.00 16.22           O  
ANISOU 1064  O   VAL A 602     1839   2010   2316    -83   -269   -473       O  
ATOM   1065  CB  VAL A 602      38.651  33.344  18.659  1.00 16.42           C  
ANISOU 1065  CB  VAL A 602     1886   1976   2375   -169   -179   -557       C  
ATOM   1066  CG1 VAL A 602      38.953  33.727  17.206  1.00 16.81           C  
ANISOU 1066  CG1 VAL A 602     1885   2002   2501   -189    -91   -540       C  
ATOM   1067  CG2 VAL A 602      38.527  34.612  19.462  1.00 17.30           C  
ANISOU 1067  CG2 VAL A 602     2037   2058   2477   -203   -169   -609       C  
ATOM   1068  N   LEU A 603      36.703  30.904  17.043  1.00 14.69           N  
ANISOU 1068  N   LEU A 603     1710   1804   2069    -73   -124   -393       N  
ATOM   1069  CA  LEU A 603      36.765  29.687  16.179  1.00 15.18           C  
ANISOU 1069  CA  LEU A 603     1740   1881   2145    -43   -130   -359       C  
ATOM   1070  C   LEU A 603      37.228  30.168  14.821  1.00 15.19           C  
ANISOU 1070  C   LEU A 603     1690   1872   2210    -65    -51   -366       C  
ATOM   1071  O   LEU A 603      36.623  31.101  14.264  1.00 15.30           O  
ANISOU 1071  O   LEU A 603     1736   1863   2215    -84     20   -341       O  
ATOM   1072  CB  LEU A 603      35.448  28.960  16.064  1.00 16.27           C  
ANISOU 1072  CB  LEU A 603     1935   2032   2213    -16   -115   -296       C  
ATOM   1073  CG  LEU A 603      34.802  28.419  17.347  1.00 17.98           C  
ANISOU 1073  CG  LEU A 603     2218   2266   2346    -11   -171   -278       C  
ATOM   1074  CD1 LEU A 603      33.758  29.414  17.795  1.00 20.07           C  
ANISOU 1074  CD1 LEU A 603     2531   2531   2563    -26   -110   -281       C  
ATOM   1075  CD2 LEU A 603      34.075  27.110  17.163  1.00 19.44           C  
ANISOU 1075  CD2 LEU A 603     2431   2463   2490     10   -189   -223       C  
ATOM   1076  N   GLU A 604      38.277  29.561  14.260  1.00 14.62           N  
ANISOU 1076  N   GLU A 604     1540   1812   2202    -65    -62   -402       N  
ATOM   1077  CA  GLU A 604      38.720  29.895  12.914  1.00 15.13           C  
ANISOU 1077  CA  GLU A 604     1560   1878   2310    -99     27   -412       C  
ATOM   1078  C   GLU A 604      38.390  28.745  12.018  1.00 14.43           C  
ANISOU 1078  C   GLU A 604     1464   1812   2206    -67     42   -388       C  
ATOM   1079  O   GLU A 604      38.771  27.619  12.305  1.00 13.64           O  
ANISOU 1079  O   GLU A 604     1327   1723   2132    -27    -24   -413       O  
ATOM   1080  CB  GLU A 604      40.249  30.125  12.850  1.00 17.24           C  
ANISOU 1080  CB  GLU A 604     1723   2153   2674   -136     26   -497       C  
ATOM   1081  CG  GLU A 604      40.694  30.506  11.449  1.00 19.81           C  
ANISOU 1081  CG  GLU A 604     2010   2487   3028   -192    139   -509       C  
ATOM   1082  CD  GLU A 604      42.135  30.754  11.285  1.00 24.51           C  
ANISOU 1082  CD  GLU A 604     2493   3097   3723   -241    162   -599       C  
ATOM   1083  OE1 GLU A 604      42.611  31.734  11.978  1.00 31.00           O  
ANISOU 1083  OE1 GLU A 604     3302   3896   4581   -282    145   -630       O  
ATOM   1084  OE2 GLU A 604      42.805  30.036  10.469  1.00 25.47           O  
ANISOU 1084  OE2 GLU A 604     2532   3253   3892   -244    202   -650       O  
ATOM   1085  N   PHE A 605      37.681  29.042  10.932  1.00 13.44           N  
ANISOU 1085  N   PHE A 605     1381   1687   2040    -85    121   -341       N  
ATOM   1086  CA  PHE A 605      37.240  28.041   9.958  1.00 13.61           C  
ANISOU 1086  CA  PHE A 605     1408   1730   2033    -63    142   -319       C  
ATOM   1087  C   PHE A 605      37.781  28.328   8.583  1.00 14.05           C  
ANISOU 1087  C   PHE A 605     1437   1803   2097   -115    236   -339       C  
ATOM   1088  O   PHE A 605      38.136  29.464   8.225  1.00 13.74           O  
ANISOU 1088  O   PHE A 605     1405   1750   2064   -176    297   -337       O  
ATOM   1089  CB  PHE A 605      35.736  28.102   9.798  1.00 13.49           C  
ANISOU 1089  CB  PHE A 605     1478   1707   1942    -43    147   -241       C  
ATOM   1090  CG  PHE A 605      34.953  27.777  11.024  1.00 13.68           C  
ANISOU 1090  CG  PHE A 605     1539   1724   1936     -5     79   -217       C  
ATOM   1091  CD1 PHE A 605      34.568  26.466  11.284  1.00 13.80           C  
ANISOU 1091  CD1 PHE A 605     1560   1751   1932     32     27   -205       C  
ATOM   1092  CD2 PHE A 605      34.565  28.766  11.904  1.00 14.67           C  
ANISOU 1092  CD2 PHE A 605     1699   1829   2047    -13     74   -210       C  
ATOM   1093  CE1 PHE A 605      33.818  26.121  12.407  1.00 14.05           C  
ANISOU 1093  CE1 PHE A 605     1636   1780   1922     50    -25   -177       C  
ATOM   1094  CE2 PHE A 605      33.744  28.427  12.989  1.00 14.41           C  
ANISOU 1094  CE2 PHE A 605     1706   1801   1969     11     29   -193       C  
ATOM   1095  CZ  PHE A 605      33.421  27.119  13.262  1.00 14.65           C  
ANISOU 1095  CZ  PHE A 605     1746   1849   1973     36    -18   -174       C  
ATOM   1096  N   GLU A 606      37.843  27.271   7.767  1.00 14.66           N  
ANISOU 1096  N   GLU A 606     1490   1910   2171    -98    252   -359       N  
ATOM   1097  CA  GLU A 606      37.915  27.419   6.339  1.00 16.14           C  
ANISOU 1097  CA  GLU A 606     1689   2122   2321   -149    347   -359       C  
ATOM   1098  C   GLU A 606      36.860  28.454   5.882  1.00 14.33           C  
ANISOU 1098  C   GLU A 606     1564   1868   2011   -180    376   -265       C  
ATOM   1099  O   GLU A 606      35.765  28.482   6.408  1.00 13.70           O  
ANISOU 1099  O   GLU A 606     1538   1766   1899   -136    321   -207       O  
ATOM   1100  CB  GLU A 606      37.545  26.051   5.728  1.00 18.33           C  
ANISOU 1100  CB  GLU A 606     1963   2425   2577   -108    334   -373       C  
ATOM   1101  CG  GLU A 606      37.403  26.004   4.222  1.00 22.51           C  
ANISOU 1101  CG  GLU A 606     2524   2989   3041   -157    422   -371       C  
ATOM   1102  CD  GLU A 606      36.886  24.647   3.738  1.00 26.32           C  
ANISOU 1102  CD  GLU A 606     3012   3488   3502   -111    396   -388       C  
ATOM   1103  OE1 GLU A 606      36.754  24.533   2.488  1.00 31.48           O  
ANISOU 1103  OE1 GLU A 606     3696   4176   4089   -153    464   -394       O  
ATOM   1104  OE2 GLU A 606      36.540  23.725   4.550  1.00 27.14           O  
ANISOU 1104  OE2 GLU A 606     3103   3568   3641    -43    308   -388       O  
ATOM   1105  N   PHE A 607      37.214  29.268   4.913  1.00 15.15           N  
ANISOU 1105  N   PHE A 607     1694   1976   2088   -257    458   -254       N  
ATOM   1106  CA  PHE A 607      36.204  30.165   4.269  1.00 14.91           C  
ANISOU 1106  CA  PHE A 607     1773   1913   1980   -283    471   -157       C  
ATOM   1107  C   PHE A 607      35.443  29.304   3.286  1.00 14.82           C  
ANISOU 1107  C   PHE A 607     1803   1936   1893   -266    471   -129       C  
ATOM   1108  O   PHE A 607      36.043  28.720   2.366  1.00 15.85           O  
ANISOU 1108  O   PHE A 607     1910   2114   1999   -304    533   -176       O  
ATOM   1109  CB  PHE A 607      36.860  31.330   3.563  1.00 16.63           C  
ANISOU 1109  CB  PHE A 607     2022   2112   2185   -382    551   -142       C  
ATOM   1110  CG  PHE A 607      35.882  32.256   2.920  1.00 17.18           C  
ANISOU 1110  CG  PHE A 607     2212   2132   2184   -405    544    -36       C  
ATOM   1111  CD1 PHE A 607      35.180  33.155   3.691  1.00 17.54           C  
ANISOU 1111  CD1 PHE A 607     2299   2107   2259   -369    485     12       C  
ATOM   1112  CD2 PHE A 607      35.697  32.240   1.555  1.00 18.39           C  
ANISOU 1112  CD2 PHE A 607     2438   2307   2244   -462    590      8       C  
ATOM   1113  CE1 PHE A 607      34.233  34.024   3.096  1.00 17.95           C  
ANISOU 1113  CE1 PHE A 607     2458   2099   2265   -376    460    108       C  
ATOM   1114  CE2 PHE A 607      34.778  33.091   0.961  1.00 18.82           C  
ANISOU 1114  CE2 PHE A 607     2610   2306   2235   -477    559    114       C  
ATOM   1115  CZ  PHE A 607      34.028  33.954   1.743  1.00 18.50           C  
ANISOU 1115  CZ  PHE A 607     2601   2186   2242   -426    488    163       C  
ATOM   1116  N   GLY A 608      34.152  29.184   3.537  1.00 14.22           N  
ANISOU 1116  N   GLY A 608     1777   1839   1787   -208    404    -67       N  
ATOM   1117  CA  GLY A 608      33.276  28.261   2.847  1.00 14.39           C  
ANISOU 1117  CA  GLY A 608     1829   1888   1750   -179    380    -45       C  
ATOM   1118  C   GLY A 608      32.529  28.825   1.666  1.00 15.23           C  
ANISOU 1118  C   GLY A 608     2030   1988   1769   -215    387     30       C  
ATOM   1119  O   GLY A 608      31.889  28.050   0.976  1.00 16.02           O  
ANISOU 1119  O   GLY A 608     2153   2117   1814   -201    367     39       O  
ATOM   1120  N   GLY A 609      32.719  30.107   1.370  1.00 16.66           N  
ANISOU 1120  N   GLY A 609     2267   2129   1935   -269    414     78       N  
ATOM   1121  CA  GLY A 609      32.015  30.808   0.271  1.00 17.49           C  
ANISOU 1121  CA  GLY A 609     2481   2209   1956   -306    402    168       C  
ATOM   1122  C   GLY A 609      30.864  31.614   0.826  1.00 17.71           C  
ANISOU 1122  C   GLY A 609     2545   2166   2016   -246    318    236       C  
ATOM   1123  O   GLY A 609      30.953  32.187   1.908  1.00 18.14           O  
ANISOU 1123  O   GLY A 609     2565   2178   2150   -217    305    220       O  
ATOM   1124  N   ILE A 610      29.802  31.694   0.050  1.00 17.48           N  
ANISOU 1124  N   ILE A 610     2587   2125   1930   -230    258    305       N  
ATOM   1125  CA  ILE A 610      28.659  32.587   0.323  1.00 18.32           C  
ANISOU 1125  CA  ILE A 610     2731   2156   2074   -174    173    371       C  
ATOM   1126  C   ILE A 610      27.448  31.732   0.650  1.00 16.45           C  
ANISOU 1126  C   ILE A 610     2447   1947   1856    -90    104    359       C  
ATOM   1127  O   ILE A 610      27.214  30.717  -0.009  1.00 15.39           O  
ANISOU 1127  O   ILE A 610     2313   1873   1663    -95     97    349       O  
ATOM   1128  CB  ILE A 610      28.317  33.391  -0.965  1.00 20.36           C  
ANISOU 1128  CB  ILE A 610     3115   2370   2252   -222    137    470       C  
ATOM   1129  CG1 ILE A 610      29.534  34.064  -1.563  1.00 22.98           C  
ANISOU 1129  CG1 ILE A 610     3510   2689   2534   -335    221    488       C  
ATOM   1130  CG2 ILE A 610      27.166  34.347  -0.723  1.00 20.98           C  
ANISOU 1130  CG2 ILE A 610     3226   2357   2390   -154     34    533       C  
ATOM   1131  CD1 ILE A 610      30.260  34.902  -0.581  1.00 24.01           C  
ANISOU 1131  CD1 ILE A 610     3602   2764   2758   -346    261    459       C  
ATOM   1132  N   ASP A 611      26.657  32.130   1.635  1.00 16.27           N  
ANISOU 1132  N   ASP A 611     2382   1883   1915    -21     58    353       N  
ATOM   1133  CA  ASP A 611      25.489  31.347   1.992  1.00 16.17           C  
ANISOU 1133  CA  ASP A 611     2315   1901   1926     46      6    335       C  
ATOM   1134  C   ASP A 611      24.418  31.298   0.890  1.00 16.17           C  
ANISOU 1134  C   ASP A 611     2362   1899   1884     62    -75    394       C  
ATOM   1135  O   ASP A 611      24.314  32.171   0.063  1.00 15.30           O  
ANISOU 1135  O   ASP A 611     2333   1737   1743     44   -115    462       O  
ATOM   1136  CB  ASP A 611      24.906  31.747   3.368  1.00 17.55           C  
ANISOU 1136  CB  ASP A 611     2426   2047   2196    106     -6    298       C  
ATOM   1137  CG  ASP A 611      24.414  33.113   3.406  1.00 20.95           C  
ANISOU 1137  CG  ASP A 611     2888   2390   2682    136    -48    332       C  
ATOM   1138  OD1 ASP A 611      23.246  33.298   2.988  1.00 24.60           O  
ANISOU 1138  OD1 ASP A 611     3351   2829   3166    185   -123    364       O  
ATOM   1139  OD2 ASP A 611      25.143  34.076   3.836  1.00 23.69           O  
ANISOU 1139  OD2 ASP A 611     3256   2681   3063    115    -16    327       O  
ATOM   1140  N   LEU A 612      23.648  30.218   0.912  1.00 15.37           N  
ANISOU 1140  N   LEU A 612     2210   1850   1779     93   -104    367       N  
ATOM   1141  CA  LEU A 612      22.665  29.953  -0.094  1.00 16.09           C  
ANISOU 1141  CA  LEU A 612     2331   1953   1830    106   -186    407       C  
ATOM   1142  C   LEU A 612      21.602  31.048  -0.152  1.00 16.59           C  
ANISOU 1142  C   LEU A 612     2404   1944   1955    164   -279    456       C  
ATOM   1143  O   LEU A 612      21.191  31.473  -1.236  1.00 16.17           O  
ANISOU 1143  O   LEU A 612     2426   1863   1854    158   -359    524       O  
ATOM   1144  CB  LEU A 612      22.043  28.572   0.220  1.00 16.38           C  
ANISOU 1144  CB  LEU A 612     2292   2054   1877    126   -192    354       C  
ATOM   1145  CG  LEU A 612      20.978  28.024  -0.752  1.00 17.86           C  
ANISOU 1145  CG  LEU A 612     2490   2269   2029    136   -279    375       C  
ATOM   1146  CD1 LEU A 612      21.519  27.925  -2.175  1.00 18.58           C  
ANISOU 1146  CD1 LEU A 612     2683   2379   1996     75   -288    412       C  
ATOM   1147  CD2 LEU A 612      20.415  26.703  -0.231  1.00 17.95           C  
ANISOU 1147  CD2 LEU A 612     2418   2332   2070    148   -274    315       C  
ATOM   1148  N   GLU A 613      21.239  31.559   1.024  1.00 16.53           N  
ANISOU 1148  N   GLU A 613     2326   1901   2053    217   -269    419       N  
ATOM   1149  CA  GLU A 613      20.287  32.672   1.127  1.00 18.64           C  
ANISOU 1149  CA  GLU A 613     2584   2088   2409    284   -351    444       C  
ATOM   1150  C   GLU A 613      20.786  33.899   0.345  1.00 18.80           C  
ANISOU 1150  C   GLU A 613     2721   2019   2403    259   -389    526       C  
ATOM   1151  O   GLU A 613      20.032  34.529  -0.427  1.00 18.83           O  
ANISOU 1151  O   GLU A 613     2774   1962   2419    292   -501    591       O  
ATOM   1152  CB  GLU A 613      20.027  33.034   2.580  1.00 19.82           C  
ANISOU 1152  CB  GLU A 613     2644   2220   2668    332   -307    371       C  
ATOM   1153  CG  GLU A 613      19.097  34.216   2.712  1.00 22.89           C  
ANISOU 1153  CG  GLU A 613     3012   2518   3166    409   -385    376       C  
ATOM   1154  CD  GLU A 613      18.718  34.507   4.167  1.00 25.35           C  
ANISOU 1154  CD  GLU A 613     3224   2825   3582    455   -331    282       C  
ATOM   1155  OE1 GLU A 613      19.408  34.024   5.106  1.00 27.90           O  
ANISOU 1155  OE1 GLU A 613     3523   3199   3877    416   -233    230       O  
ATOM   1156  OE2 GLU A 613      17.665  35.160   4.321  1.00 28.14           O  
ANISOU 1156  OE2 GLU A 613     3522   3127   4044    531   -393    257       O  
ATOM   1157  N   GLN A 614      22.076  34.234   0.512  1.00 17.88           N  
ANISOU 1157  N   GLN A 614     2653   1891   2249    194   -303    528       N  
ATOM   1158  CA  GLN A 614      22.665  35.349  -0.227  1.00 19.65           C  
ANISOU 1158  CA  GLN A 614     2996   2032   2439    145   -321    609       C  
ATOM   1159  C   GLN A 614      22.909  35.068  -1.685  1.00 19.98           C  
ANISOU 1159  C   GLN A 614     3147   2101   2342     73   -346    685       C  
ATOM   1160  O   GLN A 614      23.109  35.994  -2.481  1.00 21.56           O  
ANISOU 1160  O   GLN A 614     3467   2227   2499     30   -388    774       O  
ATOM   1161  CB  GLN A 614      23.961  35.861   0.418  1.00 20.08           C  
ANISOU 1161  CB  GLN A 614     3060   2065   2506     88   -218    581       C  
ATOM   1162  CG  GLN A 614      23.697  36.531   1.723  1.00 21.32           C  
ANISOU 1162  CG  GLN A 614     3145   2165   2790    151   -212    521       C  
ATOM   1163  CD  GLN A 614      24.899  37.255   2.275  1.00 22.70           C  
ANISOU 1163  CD  GLN A 614     3341   2298   2985     95   -135    500       C  
ATOM   1164  OE1 GLN A 614      25.259  38.330   1.788  1.00 25.93           O  
ANISOU 1164  OE1 GLN A 614     3841   2614   3399     55   -154    563       O  
ATOM   1165  NE2 GLN A 614      25.491  36.714   3.296  1.00 22.92           N  
ANISOU 1165  NE2 GLN A 614     3292   2387   3030     88    -59    416       N  
ATOM   1166  N   MET A 615      22.841  33.803  -2.071  1.00 19.14           N  
ANISOU 1166  N   MET A 615     3012   2097   2164     55   -326    652       N  
ATOM   1167  CA  MET A 615      22.966  33.384  -3.460  1.00 20.58           C  
ANISOU 1167  CA  MET A 615     3293   2322   2205    -12   -349    705       C  
ATOM   1168  C   MET A 615      21.582  33.156  -4.117  1.00 20.43           C  
ANISOU 1168  C   MET A 615     3283   2302   2179     45   -491    744       C  
ATOM   1169  O   MET A 615      21.500  32.583  -5.192  1.00 20.32           O  
ANISOU 1169  O   MET A 615     3335   2340   2045     -1   -522    771       O  
ATOM   1170  CB  MET A 615      23.775  32.089  -3.566  1.00 21.33           C  
ANISOU 1170  CB  MET A 615     3351   2527   2227    -68   -243    632       C  
ATOM   1171  CG  MET A 615      25.210  32.256  -3.097  1.00 21.89           C  
ANISOU 1171  CG  MET A 615     3411   2606   2301   -130   -113    590       C  
ATOM   1172  SD  MET A 615      26.178  33.297  -4.175  1.00 26.46           S  
ANISOU 1172  SD  MET A 615     4137   3144   2771   -250    -69    671       S  
ATOM   1173  CE  MET A 615      26.456  32.106  -5.465  1.00 26.98           C  
ANISOU 1173  CE  MET A 615     4252   3323   2677   -325    -28    648       C  
ATOM   1174  N   ARG A 616      20.521  33.683  -3.501  1.00 20.13           N  
ANISOU 1174  N   ARG A 616     3177   2202   2271    143   -581    742       N  
ATOM   1175  CA  ARG A 616      19.129  33.510  -4.028  1.00 20.80           C  
ANISOU 1175  CA  ARG A 616     3242   2282   2381    210   -728    766       C  
ATOM   1176  C   ARG A 616      18.956  33.833  -5.481  1.00 21.86           C  
ANISOU 1176  C   ARG A 616     3523   2392   2393    167   -839    870       C  
ATOM   1177  O   ARG A 616      18.216  33.123  -6.178  1.00 22.37           O  
ANISOU 1177  O   ARG A 616     3585   2508   2407    175   -924    872       O  
ATOM   1178  CB  ARG A 616      18.123  34.372  -3.226  1.00 21.42           C  
ANISOU 1178  CB  ARG A 616     3234   2272   2631    321   -810    750       C  
ATOM   1179  CG  ARG A 616      16.666  33.908  -3.355  1.00 22.36           C  
ANISOU 1179  CG  ARG A 616     3259   2414   2822    401   -929    723       C  
ATOM   1180  CD  ARG A 616      15.683  34.933  -2.759  1.00 23.12           C  
ANISOU 1180  CD  ARG A 616     3277   2411   3096    512  -1022    708       C  
ATOM   1181  NE  ARG A 616      15.569  36.166  -3.518  1.00 24.37           N  
ANISOU 1181  NE  ARG A 616     3554   2444   3262    534  -1153    813       N  
ATOM   1182  CZ  ARG A 616      14.811  36.334  -4.622  1.00 26.29           C  
ANISOU 1182  CZ  ARG A 616     3862   2653   3476    559  -1327    891       C  
ATOM   1183  NH1 ARG A 616      14.739  37.519  -5.197  1.00 27.09           N  
ANISOU 1183  NH1 ARG A 616     4079   2622   3592    581  -1452    992       N  
ATOM   1184  NH2 ARG A 616      14.105  35.322  -5.164  1.00 26.27           N  
ANISOU 1184  NH2 ARG A 616     3813   2740   3429    560  -1388    870       N  
ATOM   1185  N   THR A 617      19.649  34.864  -5.956  1.00 22.22           N  
ANISOU 1185  N   THR A 617     3702   2360   2382    110   -838    957       N  
ATOM   1186  CA  THR A 617      19.534  35.356  -7.313  1.00 24.30           C  
ANISOU 1186  CA  THR A 617     4135   2583   2516     57   -948   1076       C  
ATOM   1187  C   THR A 617      20.769  35.098  -8.158  1.00 24.59           C  
ANISOU 1187  C   THR A 617     4300   2680   2363    -89   -834   1106       C  
ATOM   1188  O   THR A 617      20.908  35.666  -9.221  1.00 25.58           O  
ANISOU 1188  O   THR A 617     4592   2767   2361   -161   -896   1213       O  
ATOM   1189  CB  THR A 617      19.259  36.889  -7.320  1.00 26.05           C  
ANISOU 1189  CB  THR A 617     4437   2643   2816     96  -1059   1174       C  
ATOM   1190  OG1 THR A 617      20.379  37.597  -6.745  1.00 25.51           O  
ANISOU 1190  OG1 THR A 617     4397   2524   2770     41   -932   1173       O  
ATOM   1191  CG2 THR A 617      17.998  37.241  -6.487  1.00 26.04           C  
ANISOU 1191  CG2 THR A 617     4296   2576   3024    250  -1173   1128       C  
ATOM   1192  N   LYS A 618      21.674  34.241  -7.681  1.00 23.68           N  
ANISOU 1192  N   LYS A 618     4109   2660   2229   -134   -668   1008       N  
ATOM   1193  CA  LYS A 618      23.013  34.182  -8.280  1.00 25.10           C  
ANISOU 1193  CA  LYS A 618     4384   2887   2267   -270   -532   1015       C  
ATOM   1194  C   LYS A 618      23.368  32.860  -8.949  1.00 25.15           C  
ANISOU 1194  C   LYS A 618     4386   3025   2143   -333   -458    946       C  
ATOM   1195  O   LYS A 618      24.385  32.794  -9.607  1.00 26.99           O  
ANISOU 1195  O   LYS A 618     4701   3305   2248   -450   -349    945       O  
ATOM   1196  CB  LYS A 618      24.087  34.466  -7.217  1.00 24.61           C  
ANISOU 1196  CB  LYS A 618     4244   2811   2295   -287   -386    952       C  
ATOM   1197  CG  LYS A 618      23.903  35.731  -6.394  1.00 25.82           C  
ANISOU 1197  CG  LYS A 618     4386   2835   2588   -230   -431    991       C  
ATOM   1198  CD  LYS A 618      24.144  36.921  -7.233  1.00 28.69           C  
ANISOU 1198  CD  LYS A 618     4923   3102   2876   -306   -479   1118       C  
ATOM   1199  CE  LYS A 618      23.927  38.163  -6.422  1.00 30.12           C  
ANISOU 1199  CE  LYS A 618     5093   3142   3210   -243   -533   1149       C  
ATOM   1200  NZ  LYS A 618      24.142  39.248  -7.324  1.00 33.47           N  
ANISOU 1200  NZ  LYS A 618     5702   3462   3553   -325   -590   1284       N  
ATOM   1201  N   LEU A 619      22.569  31.823  -8.801  1.00 24.59           N  
ANISOU 1201  N   LEU A 619     4222   3013   2107   -265   -508    881       N  
ATOM   1202  CA  LEU A 619      22.884  30.511  -9.376  1.00 25.04           C  
ANISOU 1202  CA  LEU A 619     4268   3187   2060   -317   -441    801       C  
ATOM   1203  C   LEU A 619      22.455  30.397 -10.808  1.00 26.20           C  
ANISOU 1203  C   LEU A 619     4557   3365   2033   -379   -531    862       C  
ATOM   1204  O   LEU A 619      21.476  31.049 -11.248  1.00 26.67           O  
ANISOU 1204  O   LEU A 619     4687   3362   2084   -342   -696    958       O  
ATOM   1205  CB  LEU A 619      22.244  29.406  -8.560  1.00 24.48           C  
ANISOU 1205  CB  LEU A 619     4040   3157   2104   -228   -454    704       C  
ATOM   1206  CG  LEU A 619      22.633  29.294  -7.069  1.00 24.47           C  
ANISOU 1206  CG  LEU A 619     3898   3140   2261   -171   -367    633       C  
ATOM   1207  CD1 LEU A 619      22.026  28.079  -6.421  1.00 23.95           C  
ANISOU 1207  CD1 LEU A 619     3704   3120   2274   -109   -375    547       C  
ATOM   1208  CD2 LEU A 619      24.138  29.264  -6.911  1.00 24.95           C  
ANISOU 1208  CD2 LEU A 619     3963   3227   2290   -245   -210    587       C  
ATOM   1209  N   SER A 620      23.182  29.575 -11.567  1.00 25.97           N  
ANISOU 1209  N   SER A 620     4573   3432   1863   -473   -429    801       N  
ATOM   1210  CA ASER A 620      22.994  29.465 -12.992  0.50 27.67           C  
ANISOU 1210  CA ASER A 620     4944   3693   1876   -560   -486    848       C  
ATOM   1211  CA BSER A 620      22.975  29.506 -13.000  0.50 27.93           C  
ANISOU 1211  CA BSER A 620     4981   3723   1909   -560   -490    853       C  
ATOM   1212  C   SER A 620      21.634  28.878 -13.414  1.00 27.92           C  
ANISOU 1212  C   SER A 620     4967   3741   1900   -496   -660    853       C  
ATOM   1213  O   SER A 620      20.929  29.437 -14.289  1.00 29.27           O  
ANISOU 1213  O   SER A 620     5269   3881   1971   -512   -812    959       O  
ATOM   1214  CB ASER A 620      24.145  28.642 -13.595  0.50 27.94           C  
ANISOU 1214  CB ASER A 620     5003   3834   1777   -674   -312    748       C  
ATOM   1215  CB BSER A 620      24.148  28.798 -13.693  0.50 28.62           C  
ANISOU 1215  CB BSER A 620     5112   3914   1847   -683   -319    766       C  
ATOM   1216  OG ASER A 620      23.788  28.143 -14.852  0.50 28.89           O  
ANISOU 1216  OG ASER A 620     5241   4022   1712   -741   -366    752       O  
ATOM   1217  OG BSER A 620      24.330  27.513 -13.145  0.50 27.54           O  
ANISOU 1217  OG BSER A 620     4826   3842   1796   -637   -242    622       O  
ATOM   1218  N   SER A 621      21.305  27.739 -12.842  1.00 26.91           N  
ANISOU 1218  N   SER A 621     4694   3662   1870   -432   -641    742       N  
ATOM   1219  CA  SER A 621      20.082  27.004 -13.185  1.00 27.43           C  
ANISOU 1219  CA  SER A 621     4727   3755   1941   -382   -785    720       C  
ATOM   1220  C   SER A 621      19.746  25.951 -12.148  1.00 26.17           C  
ANISOU 1220  C   SER A 621     4383   3616   1944   -302   -750    608       C  
ATOM   1221  O   SER A 621      20.556  25.648 -11.245  1.00 23.54           O  
ANISOU 1221  O   SER A 621     3959   3287   1697   -293   -610    541       O  
ATOM   1222  CB  SER A 621      20.228  26.328 -14.563  1.00 29.29           C  
ANISOU 1222  CB  SER A 621     5089   4078   1962   -483   -789    694       C  
ATOM   1223  OG  SER A 621      20.912  25.106 -14.431  1.00 29.21           O  
ANISOU 1223  OG  SER A 621     5005   4146   1950   -512   -646    554       O  
ATOM   1224  N   LEU A 622      18.564  25.351 -12.310  1.00 26.78           N  
ANISOU 1224  N   LEU A 622     4409   3709   2058   -254   -880    588       N  
ATOM   1225  CA  LEU A 622      18.143  24.224 -11.463  1.00 26.33           C  
ANISOU 1225  CA  LEU A 622     4192   3675   2136   -199   -854    484       C  
ATOM   1226  C   LEU A 622      19.059  22.980 -11.506  1.00 25.15           C  
ANISOU 1226  C   LEU A 622     4021   3591   1943   -253   -712    367       C  
ATOM   1227  O   LEU A 622      19.015  22.210 -10.621  1.00 24.96           O  
ANISOU 1227  O   LEU A 622     3880   3567   2039   -214   -664    296       O  
ATOM   1228  CB  LEU A 622      16.700  23.791 -11.761  1.00 28.33           C  
ANISOU 1228  CB  LEU A 622     4398   3937   2428   -155  -1021    479       C  
ATOM   1229  CG  LEU A 622      15.607  24.522 -10.992  1.00 28.84           C  
ANISOU 1229  CG  LEU A 622     4362   3937   2660    -56  -1133    527       C  
ATOM   1230  CD1 LEU A 622      14.244  24.077 -11.521  1.00 30.81           C  
ANISOU 1230  CD1 LEU A 622     4570   4206   2931    -28  -1305    515       C  
ATOM   1231  CD2 LEU A 622      15.678  24.327  -9.483  1.00 26.98           C  
ANISOU 1231  CD2 LEU A 622     3973   3679   2601      1  -1030    472       C  
ATOM   1232  N   ALA A 623      19.891  22.821 -12.523  1.00 26.72           N  
ANISOU 1232  N   ALA A 623     4337   3842   1974   -345   -645    347       N  
ATOM   1233  CA  ALA A 623      20.904  21.743 -12.489  1.00 26.34           C  
ANISOU 1233  CA  ALA A 623     4254   3845   1910   -386   -496    222       C  
ATOM   1234  C   ALA A 623      21.874  21.938 -11.318  1.00 24.85           C  
ANISOU 1234  C   ALA A 623     3976   3622   1845   -356   -365    198       C  
ATOM   1235  O   ALA A 623      22.296  20.972 -10.634  1.00 24.31           O  
ANISOU 1235  O   ALA A 623     3808   3558   1870   -331   -290    101       O  
ATOM   1236  CB  ALA A 623      21.660  21.715 -13.807  1.00 27.89           C  
ANISOU 1236  CB  ALA A 623     4591   4106   1898   -496   -433    200       C  
ATOM   1237  N   THR A 624      22.175  23.202 -11.026  1.00 24.36           N  
ANISOU 1237  N   THR A 624     3949   3514   1793   -354   -353    289       N  
ATOM   1238  CA  THR A 624      23.022  23.548  -9.858  1.00 23.66           C  
ANISOU 1238  CA  THR A 624     3777   3388   1826   -324   -248    274       C  
ATOM   1239  C   THR A 624      22.316  23.137  -8.566  1.00 22.71           C  
ANISOU 1239  C   THR A 624     3522   3230   1879   -230   -291    254       C  
ATOM   1240  O   THR A 624      22.914  22.589  -7.646  1.00 20.61           O  
ANISOU 1240  O   THR A 624     3166   2958   1706   -206   -211    189       O  
ATOM   1241  CB  THR A 624      23.339  25.063  -9.860  1.00 24.74           C  
ANISOU 1241  CB  THR A 624     3988   3473   1938   -346   -245    381       C  
ATOM   1242  OG1 THR A 624      23.786  25.427 -11.164  1.00 27.65           O  
ANISOU 1242  OG1 THR A 624     4504   3879   2124   -448   -223    416       O  
ATOM   1243  CG2 THR A 624      24.385  25.459  -8.871  1.00 24.76           C  
ANISOU 1243  CG2 THR A 624     3925   3447   2034   -339   -129    358       C  
ATOM   1244  N   ALA A 625      21.016  23.406  -8.489  1.00 22.57           N  
ANISOU 1244  N   ALA A 625     3487   3185   1904   -179   -421    309       N  
ATOM   1245  CA  ALA A 625      20.265  23.054  -7.314  1.00 22.24           C  
ANISOU 1245  CA  ALA A 625     3320   3116   2015   -104   -452    287       C  
ATOM   1246  C   ALA A 625      20.344  21.549  -7.034  1.00 21.65           C  
ANISOU 1246  C   ALA A 625     3176   3074   1975   -109   -411    187       C  
ATOM   1247  O   ALA A 625      20.437  21.098  -5.867  1.00 22.37           O  
ANISOU 1247  O   ALA A 625     3176   3145   2179    -74   -367    151       O  
ATOM   1248  CB  ALA A 625      18.813  23.481  -7.503  1.00 22.82           C  
ANISOU 1248  CB  ALA A 625     3379   3168   2123    -58   -600    343       C  
ATOM   1249  N   LYS A 626      20.284  20.742  -8.078  1.00 22.54           N  
ANISOU 1249  N   LYS A 626     3339   3233   1993   -154   -431    141       N  
ATOM   1250  CA ALYS A 626      20.413  19.296  -7.912  0.50 22.32           C  
ANISOU 1250  CA ALYS A 626     3257   3223   2000   -161   -397     41       C  
ATOM   1251  CA BLYS A 626      20.419  19.306  -7.946  0.50 22.60           C  
ANISOU 1251  CA BLYS A 626     3295   3259   2031   -162   -397     42       C  
ATOM   1252  C   LYS A 626      21.780  18.888  -7.308  1.00 21.72           C  
ANISOU 1252  C   LYS A 626     3150   3140   1965   -166   -267    -23       C  
ATOM   1253  O   LYS A 626      21.836  18.042  -6.388  1.00 20.56           O  
ANISOU 1253  O   LYS A 626     2924   2966   1923   -136   -247    -70       O  
ATOM   1254  CB ALYS A 626      20.179  18.559  -9.196  0.50 23.96           C  
ANISOU 1254  CB ALYS A 626     3532   3480   2093   -212   -438     -9       C  
ATOM   1255  CB BLYS A 626      20.266  18.667  -9.286  0.50 24.74           C  
ANISOU 1255  CB BLYS A 626     3641   3581   2177   -217   -433     -4       C  
ATOM   1256  CG ALYS A 626      20.579  17.092  -9.185  0.50 24.21           C  
ANISOU 1256  CG ALYS A 626     3526   3522   2152   -227   -386   -127       C  
ATOM   1257  CG BLYS A 626      19.888  17.217  -9.256  0.50 25.36           C  
ANISOU 1257  CG BLYS A 626     3668   3666   2302   -219   -450    -97       C  
ATOM   1258  CD ALYS A 626      19.963  16.335 -10.346  0.50 25.44           C  
ANISOU 1258  CD ALYS A 626     3734   3719   2214   -271   -458   -179       C  
ATOM   1259  CD BLYS A 626      21.100  16.321  -9.276  0.50 25.83           C  
ANISOU 1259  CD BLYS A 626     3723   3732   2360   -241   -336   -202       C  
ATOM   1260  CE ALYS A 626      20.939  15.329 -10.936  0.50 26.35           C  
ANISOU 1260  CE ALYS A 626     3876   3861   2275   -313   -367   -303       C  
ATOM   1261  CE BLYS A 626      20.634  14.904  -9.386  0.50 26.34           C  
ANISOU 1261  CE BLYS A 626     3752   3790   2466   -247   -372   -291       C  
ATOM   1262  NZ ALYS A 626      21.177  14.097 -10.130  0.50 26.27           N  
ANISOU 1262  NZ ALYS A 626     3777   3804   2399   -283   -331   -390       N  
ATOM   1263  NZ BLYS A 626      19.790  14.840 -10.602  0.50 27.27           N  
ANISOU 1263  NZ BLYS A 626     3940   3954   2467   -288   -466   -293       N  
ATOM   1264  N   SER A 627      22.867  19.431  -7.840  1.00 20.26           N  
ANISOU 1264  N   SER A 627     3026   2975   1698   -208   -186    -27       N  
ATOM   1265  CA  SER A 627      24.185  19.154  -7.244  1.00 19.25           C  
ANISOU 1265  CA  SER A 627     2850   2839   1625   -207    -71    -92       C  
ATOM   1266  C   SER A 627      24.228  19.553  -5.786  1.00 17.16           C  
ANISOU 1266  C   SER A 627     2508   2522   1490   -150    -66    -54       C  
ATOM   1267  O   SER A 627      24.760  18.800  -4.922  1.00 16.37           O  
ANISOU 1267  O   SER A 627     2338   2398   1483   -122    -30   -111       O  
ATOM   1268  CB  SER A 627      25.282  19.858  -8.017  1.00 20.40           C  
ANISOU 1268  CB  SER A 627     3064   3019   1668   -271     22    -97       C  
ATOM   1269  OG  SER A 627      26.522  19.720  -7.347  1.00 20.16           O  
ANISOU 1269  OG  SER A 627     2967   2978   1714   -264    123   -160       O  
ATOM   1270  N   ILE A 628      23.658  20.709  -5.458  1.00 16.29           N  
ANISOU 1270  N   ILE A 628     2411   2387   1390   -131   -110     39       N  
ATOM   1271  CA  ILE A 628      23.654  21.196  -4.092  1.00 14.90           C  
ANISOU 1271  CA  ILE A 628     2170   2167   1324    -82   -102     69       C  
ATOM   1272  C   ILE A 628      22.920  20.198  -3.183  1.00 14.26           C  
ANISOU 1272  C   ILE A 628     2013   2070   1336    -44   -141     41       C  
ATOM   1273  O   ILE A 628      23.407  19.831  -2.126  1.00 12.64           O  
ANISOU 1273  O   ILE A 628     1756   1842   1206    -23   -105     15       O  
ATOM   1274  CB  ILE A 628      23.046  22.609  -3.998  1.00 15.02           C  
ANISOU 1274  CB  ILE A 628     2214   2153   1340    -64   -151    162       C  
ATOM   1275  CG1 ILE A 628      23.997  23.630  -4.641  1.00 15.60           C  
ANISOU 1275  CG1 ILE A 628     2365   2225   1336   -113    -96    196       C  
ATOM   1276  CG2 ILE A 628      22.809  23.007  -2.566  1.00 14.31           C  
ANISOU 1276  CG2 ILE A 628     2050   2022   1363    -13   -148    177       C  
ATOM   1277  CD1 ILE A 628      23.347  24.934  -5.046  1.00 16.54           C  
ANISOU 1277  CD1 ILE A 628     2553   2309   1424   -110   -166    294       C  
ATOM   1278  N   LEU A 629      21.743  19.738  -3.649  1.00 14.40           N  
ANISOU 1278  N   LEU A 629     2030   2102   1341    -43   -220     47       N  
ATOM   1279  CA  LEU A 629      20.952  18.819  -2.830  1.00 14.45           C  
ANISOU 1279  CA  LEU A 629     1967   2092   1431    -23   -252     25       C  
ATOM   1280  C   LEU A 629      21.643  17.458  -2.660  1.00 13.59           C  
ANISOU 1280  C   LEU A 629     1843   1973   1346    -37   -214    -52       C  
ATOM   1281  O   LEU A 629      21.583  16.874  -1.587  1.00 14.36           O  
ANISOU 1281  O   LEU A 629     1895   2040   1522    -23   -208    -60       O  
ATOM   1282  CB  LEU A 629      19.541  18.651  -3.407  1.00 15.19           C  
ANISOU 1282  CB  LEU A 629     2051   2203   1516    -25   -346     40       C  
ATOM   1283  CG  LEU A 629      18.631  19.909  -3.296  1.00 15.86           C  
ANISOU 1283  CG  LEU A 629     2121   2281   1624      9   -405    110       C  
ATOM   1284  CD1 LEU A 629      17.370  19.716  -4.158  1.00 17.04           C  
ANISOU 1284  CD1 LEU A 629     2266   2453   1757      6   -516    115       C  
ATOM   1285  CD2 LEU A 629      18.295  20.334  -1.884  1.00 15.75           C  
ANISOU 1285  CD2 LEU A 629     2031   2239   1713     45   -379    125       C  
ATOM   1286  N   HIS A 630      22.311  16.982  -3.704  1.00 14.32           N  
ANISOU 1286  N   HIS A 630     1981   2090   1372    -66   -190   -108       N  
ATOM   1287  CA  HIS A 630      23.008  15.725  -3.670  1.00 14.22           C  
ANISOU 1287  CA  HIS A 630     1952   2058   1391    -71   -160   -194       C  
ATOM   1288  C   HIS A 630      24.190  15.833  -2.687  1.00 13.93           C  
ANISOU 1288  C   HIS A 630     1881   1990   1423    -45    -98   -207       C  
ATOM   1289  O   HIS A 630      24.425  14.948  -1.844  1.00 13.08           O  
ANISOU 1289  O   HIS A 630     1736   1835   1397    -25   -106   -235       O  
ATOM   1290  CB  HIS A 630      23.502  15.382  -5.069  1.00 15.72           C  
ANISOU 1290  CB  HIS A 630     2196   2290   1488   -109   -134   -264       C  
ATOM   1291  CG  HIS A 630      23.953  13.969  -5.250  1.00 16.63           C  
ANISOU 1291  CG  HIS A 630     2294   2383   1642   -111   -120   -370       C  
ATOM   1292  ND1 HIS A 630      24.068  13.402  -6.499  1.00 18.37           N  
ANISOU 1292  ND1 HIS A 630     2558   2640   1782   -148   -111   -452       N  
ATOM   1293  CD2 HIS A 630      24.215  12.977  -4.367  1.00 16.76           C  
ANISOU 1293  CD2 HIS A 630     2262   2337   1768    -82   -128   -409       C  
ATOM   1294  CE1 HIS A 630      24.444  12.140  -6.380  1.00 18.54           C  
ANISOU 1294  CE1 HIS A 630     2550   2619   1876   -135   -105   -547       C  
ATOM   1295  NE2 HIS A 630      24.541  11.853  -5.103  1.00 18.39           N  
ANISOU 1295  NE2 HIS A 630     2477   2534   1974    -94   -122   -517       N  
ATOM   1296  N   GLN A 631      24.930  16.926  -2.806  1.00 13.22           N  
ANISOU 1296  N   GLN A 631     1807   1920   1298    -49    -45   -184       N  
ATOM   1297  CA  GLN A 631      26.056  17.173  -1.858  1.00 13.06           C  
ANISOU 1297  CA  GLN A 631     1746   1873   1344    -26      5   -197       C  
ATOM   1298  C   GLN A 631      25.606  17.217  -0.430  1.00 12.41           C  
ANISOU 1298  C   GLN A 631     1627   1749   1338      6    -31   -147       C  
ATOM   1299  O   GLN A 631      26.262  16.631   0.475  1.00 12.58           O  
ANISOU 1299  O   GLN A 631     1615   1732   1431     28    -30   -174       O  
ATOM   1300  CB  GLN A 631      26.831  18.463  -2.204  1.00 13.02           C  
ANISOU 1300  CB  GLN A 631     1763   1893   1290    -49     67   -174       C  
ATOM   1301  CG  GLN A 631      27.536  18.391  -3.519  1.00 14.07           C  
ANISOU 1301  CG  GLN A 631     1934   2073   1341    -97    128   -235       C  
ATOM   1302  CD  GLN A 631      28.338  19.629  -3.804  1.00 14.56           C  
ANISOU 1302  CD  GLN A 631     2021   2156   1356   -135    198   -209       C  
ATOM   1303  OE1 GLN A 631      29.171  20.026  -2.992  1.00 14.19           O  
ANISOU 1303  OE1 GLN A 631     1926   2088   1378   -121    236   -218       O  
ATOM   1304  NE2 GLN A 631      28.136  20.228  -4.988  1.00 15.86           N  
ANISOU 1304  NE2 GLN A 631     2268   2361   1400   -192    215   -179       N  
ATOM   1305  N   LEU A 632      24.543  17.968  -0.153  1.00 12.55           N  
ANISOU 1305  N   LEU A 632     1651   1773   1344      9    -64    -76       N  
ATOM   1306  CA  LEU A 632      24.026  18.032   1.178  1.00 11.89           C  
ANISOU 1306  CA  LEU A 632     1535   1662   1320     29    -84    -38       C  
ATOM   1307  C   LEU A 632      23.562  16.660   1.712  1.00 11.85           C  
ANISOU 1307  C   LEU A 632     1513   1628   1361     24   -120    -59       C  
ATOM   1308  O   LEU A 632      23.860  16.292   2.877  1.00 10.98           O  
ANISOU 1308  O   LEU A 632     1390   1484   1300     31   -121    -52       O  
ATOM   1309  CB  LEU A 632      22.872  19.052   1.282  1.00 12.79           C  
ANISOU 1309  CB  LEU A 632     1645   1790   1425     36   -109     23       C  
ATOM   1310  CG  LEU A 632      23.290  20.521   1.137  1.00 13.00           C  
ANISOU 1310  CG  LEU A 632     1693   1819   1428     44    -82     58       C  
ATOM   1311  CD1 LEU A 632      22.054  21.380   0.863  1.00 14.45           C  
ANISOU 1311  CD1 LEU A 632     1877   2007   1608     59   -130    108       C  
ATOM   1312  CD2 LEU A 632      24.070  21.017   2.349  1.00 13.46           C  
ANISOU 1312  CD2 LEU A 632     1730   1853   1531     58    -43     59       C  
ATOM   1313  N   THR A 633      22.815  15.931   0.884  1.00 11.81           N  
ANISOU 1313  N   THR A 633     1516   1634   1336      4   -155    -79       N  
ATOM   1314  CA  THR A 633      22.307  14.621   1.326  1.00 11.61           C  
ANISOU 1314  CA  THR A 633     1480   1572   1358    -12   -190    -96       C  
ATOM   1315  C   THR A 633      23.489  13.689   1.619  1.00 11.78           C  
ANISOU 1315  C   THR A 633     1510   1544   1424      2   -184   -146       C  
ATOM   1316  O   THR A 633      23.472  12.986   2.623  1.00 11.78           O  
ANISOU 1316  O   THR A 633     1509   1493   1475     -2   -208   -131       O  
ATOM   1317  CB  THR A 633      21.382  14.016   0.266  1.00 12.52           C  
ANISOU 1317  CB  THR A 633     1603   1707   1448    -39   -233   -122       C  
ATOM   1318  OG1 THR A 633      20.305  14.966  -0.031  1.00 12.60           O  
ANISOU 1318  OG1 THR A 633     1598   1760   1428    -41   -256    -76       O  
ATOM   1319  CG2 THR A 633      20.755  12.722   0.764  1.00 12.92           C  
ANISOU 1319  CG2 THR A 633     1643   1713   1553    -68   -269   -134       C  
ATOM   1320  N   ALA A 634      24.487  13.681   0.735  1.00 12.18           N  
ANISOU 1320  N   ALA A 634     1567   1606   1454     14   -154   -208       N  
ATOM   1321  CA  ALA A 634      25.640  12.817   0.960  1.00 12.79           C  
ANISOU 1321  CA  ALA A 634     1633   1633   1594     38   -152   -272       C  
ATOM   1322  C   ALA A 634      26.386  13.160   2.277  1.00 13.28           C  
ANISOU 1322  C   ALA A 634     1677   1662   1708     66   -153   -239       C  
ATOM   1323  O   ALA A 634      26.750  12.281   3.041  1.00 13.34           O  
ANISOU 1323  O   ALA A 634     1684   1604   1782     82   -197   -247       O  
ATOM   1324  CB  ALA A 634      26.581  12.867  -0.211  1.00 13.31           C  
ANISOU 1324  CB  ALA A 634     1695   1732   1632     41   -101   -358       C  
ATOM   1325  N   SER A 635      26.625  14.440   2.523  1.00 13.17           N  
ANISOU 1325  N   SER A 635     1654   1687   1662     69   -114   -201       N  
ATOM   1326  CA  SER A 635      27.360  14.847   3.730  1.00 13.42           C  
ANISOU 1326  CA  SER A 635     1670   1694   1734     90   -118   -178       C  
ATOM   1327  C   SER A 635      26.618  14.421   4.962  1.00 12.29           C  
ANISOU 1327  C   SER A 635     1548   1515   1608     80   -166   -117       C  
ATOM   1328  O   SER A 635      27.176  13.876   5.916  1.00 11.91           O  
ANISOU 1328  O   SER A 635     1506   1415   1605     93   -208   -112       O  
ATOM   1329  CB  SER A 635      27.512  16.372   3.711  1.00 14.51           C  
ANISOU 1329  CB  SER A 635     1803   1881   1831     85    -67   -146       C  
ATOM   1330  OG  SER A 635      28.380  16.737   2.661  1.00 17.24           O  
ANISOU 1330  OG  SER A 635     2137   2256   2158     81    -15   -201       O  
ATOM   1331  N   LEU A 636      25.334  14.696   4.967  1.00 11.49           N  
ANISOU 1331  N   LEU A 636     1457   1441   1468     50   -162    -71       N  
ATOM   1332  CA  LEU A 636      24.503  14.267   6.087  1.00 11.43           C  
ANISOU 1332  CA  LEU A 636     1467   1410   1467     22   -189    -19       C  
ATOM   1333  C   LEU A 636      24.441  12.749   6.279  1.00 11.80           C  
ANISOU 1333  C   LEU A 636     1540   1389   1553      5   -244    -28       C  
ATOM   1334  O   LEU A 636      24.507  12.251   7.422  1.00 11.93           O  
ANISOU 1334  O   LEU A 636     1590   1359   1585    -12   -277     11       O  
ATOM   1335  CB  LEU A 636      23.109  14.882   5.955  1.00 11.81           C  
ANISOU 1335  CB  LEU A 636     1499   1506   1481     -5   -167     14       C  
ATOM   1336  CG  LEU A 636      22.991  16.357   6.084  1.00 11.64           C  
ANISOU 1336  CG  LEU A 636     1459   1530   1435     11   -128     34       C  
ATOM   1337  CD1 LEU A 636      21.601  16.821   5.741  1.00 12.93           C  
ANISOU 1337  CD1 LEU A 636     1594   1731   1588     -2   -124     52       C  
ATOM   1338  CD2 LEU A 636      23.377  16.831   7.476  1.00 11.65           C  
ANISOU 1338  CD2 LEU A 636     1468   1520   1437     11   -113     59       C  
ATOM   1339  N   ALA A 637      24.400  12.001   5.174  1.00 11.73           N  
ANISOU 1339  N   ALA A 637     1528   1368   1561      8   -257    -80       N  
ATOM   1340  CA  ALA A 637      24.403  10.544   5.237  1.00 12.29           C  
ANISOU 1340  CA  ALA A 637     1626   1359   1683     -4   -314   -100       C  
ATOM   1341  C   ALA A 637      25.708  10.044   5.866  1.00 12.59           C  
ANISOU 1341  C   ALA A 637     1675   1326   1783     39   -357   -119       C  
ATOM   1342  O   ALA A 637      25.708   9.185   6.709  1.00 13.20           O  
ANISOU 1342  O   ALA A 637     1793   1325   1895     25   -417    -84       O  
ATOM   1343  CB  ALA A 637      24.200   9.953   3.856  1.00 12.59           C  
ANISOU 1343  CB  ALA A 637     1655   1403   1725     -6   -315   -171       C  
ATOM   1344  N   VAL A 638      26.825  10.594   5.428  1.00 12.29           N  
ANISOU 1344  N   VAL A 638     1599   1311   1759     87   -330   -174       N  
ATOM   1345  CA  VAL A 638      28.109  10.164   5.967  1.00 13.13           C  
ANISOU 1345  CA  VAL A 638     1694   1352   1941    137   -379   -207       C  
ATOM   1346  C   VAL A 638      28.211  10.466   7.446  1.00 13.00           C  
ANISOU 1346  C   VAL A 638     1711   1313   1916    129   -420   -126       C  
ATOM   1347  O   VAL A 638      28.740   9.641   8.213  1.00 13.86           O  
ANISOU 1347  O   VAL A 638     1850   1336   2082    148   -505   -113       O  
ATOM   1348  CB  VAL A 638      29.280  10.813   5.162  1.00 13.58           C  
ANISOU 1348  CB  VAL A 638     1687   1455   2018    180   -324   -294       C  
ATOM   1349  CG1 VAL A 638      30.647  10.599   5.836  1.00 14.76           C  
ANISOU 1349  CG1 VAL A 638     1801   1550   2257    235   -376   -331       C  
ATOM   1350  CG2 VAL A 638      29.262  10.329   3.716  1.00 14.15           C  
ANISOU 1350  CG2 VAL A 638     1740   1545   2091    180   -286   -385       C  
ATOM   1351  N   ALA A 639      27.728  11.644   7.861  1.00 11.82           N  
ANISOU 1351  N   ALA A 639     1562   1236   1695    102   -366    -75       N  
ATOM   1352  CA  ALA A 639      27.730  11.988   9.255  1.00 12.31           C  
ANISOU 1352  CA  ALA A 639     1660   1289   1728     84   -394     -7       C  
ATOM   1353  C   ALA A 639      26.763  11.138  10.072  1.00 12.56           C  
ANISOU 1353  C   ALA A 639     1763   1276   1734     25   -434     64       C  
ATOM   1354  O   ALA A 639      27.055  10.826  11.197  1.00 12.56           O  
ANISOU 1354  O   ALA A 639     1816   1229   1726     12   -493    112       O  
ATOM   1355  CB  ALA A 639      27.465  13.455   9.441  1.00 11.44           C  
ANISOU 1355  CB  ALA A 639     1528   1261   1557     72   -322     12       C  
ATOM   1356  N   GLU A 640      25.587  10.807   9.511  1.00 12.30           N  
ANISOU 1356  N   GLU A 640     1731   1262   1681    -19   -401     71       N  
ATOM   1357  CA  GLU A 640      24.699   9.857  10.182  1.00 13.18           C  
ANISOU 1357  CA  GLU A 640     1905   1324   1779    -88   -433    131       C  
ATOM   1358  C   GLU A 640      25.415   8.517  10.481  1.00 14.05           C  
ANISOU 1358  C   GLU A 640     2071   1312   1954    -74   -537    136       C  
ATOM   1359  O   GLU A 640      25.380   7.971  11.575  1.00 14.88           O  
ANISOU 1359  O   GLU A 640     2255   1357   2043   -115   -594    206       O  
ATOM   1360  CB  GLU A 640      23.456   9.602   9.290  1.00 13.81           C  
ANISOU 1360  CB  GLU A 640     1958   1437   1852   -131   -392    114       C  
ATOM   1361  CG  GLU A 640      22.431  10.675   9.360  1.00 13.89           C  
ANISOU 1361  CG  GLU A 640     1928   1544   1807   -163   -314    131       C  
ATOM   1362  CD  GLU A 640      21.277  10.428   8.356  1.00 15.36           C  
ANISOU 1362  CD  GLU A 640     2074   1761   2000   -193   -294    105       C  
ATOM   1363  OE1 GLU A 640      21.326   9.414   7.622  1.00 16.00           O  
ANISOU 1363  OE1 GLU A 640     2166   1791   2122   -194   -336     72       O  
ATOM   1364  OE2 GLU A 640      20.345  11.285   8.275  1.00 16.56           O  
ANISOU 1364  OE2 GLU A 640     2178   1989   2125   -210   -241    109       O  
ATOM   1365  N   ALA A 641      26.079   8.005   9.468  1.00 14.36           N  
ANISOU 1365  N   ALA A 641     2073   1313   2070    -14   -563     58       N  
ATOM   1366  CA  ALA A 641      26.722   6.727   9.535  1.00 15.61           C  
ANISOU 1366  CA  ALA A 641     2268   1346   2316     15   -663     41       C  
ATOM   1367  C   ALA A 641      27.864   6.729  10.513  1.00 16.36           C  
ANISOU 1367  C   ALA A 641     2388   1385   2444     61   -746     64       C  
ATOM   1368  O   ALA A 641      28.075   5.719  11.199  1.00 17.76           O  
ANISOU 1368  O   ALA A 641     2639   1447   2663     55   -853    110       O  
ATOM   1369  CB  ALA A 641      27.189   6.287   8.135  1.00 15.94           C  
ANISOU 1369  CB  ALA A 641     2248   1374   2433     72   -654    -75       C  
ATOM   1370  N   SER A 642      28.640   7.784  10.548  1.00 15.59           N  
ANISOU 1370  N   SER A 642     2232   1355   2337    108   -712     32       N  
ATOM   1371  CA ASER A 642      29.865   7.839  11.348  0.50 15.88           C  
ANISOU 1371  CA ASER A 642     2269   1343   2420    163   -800     33       C  
ATOM   1372  CA BSER A 642      29.851   7.758  11.374  0.50 16.58           C  
ANISOU 1372  CA BSER A 642     2363   1426   2512    161   -806     36       C  
ATOM   1373  C   SER A 642      29.569   8.219  12.787  1.00 16.12           C  
ANISOU 1373  C   SER A 642     2383   1383   2358    106   -830    140       C  
ATOM   1374  O   SER A 642      30.198   7.677  13.724  1.00 17.28           O  
ANISOU 1374  O   SER A 642     2591   1444   2530    121   -951    184       O  
ATOM   1375  CB ASER A 642      30.833   8.890  10.774  0.50 15.04           C  
ANISOU 1375  CB ASER A 642     2059   1315   2342    223   -740    -53       C  
ATOM   1376  CB BSER A 642      30.955   8.628  10.787  0.50 16.67           C  
ANISOU 1376  CB BSER A 642     2269   1497   2570    232   -764    -58       C  
ATOM   1377  OG ASER A 642      32.051   8.915  11.492  0.50 14.92           O  
ANISOU 1377  OG ASER A 642     2026   1255   2389    278   -831    -67       O  
ATOM   1378  OG BSER A 642      30.445   9.893  10.515  0.50 16.61           O  
ANISOU 1378  OG BSER A 642     2231   1607   2474    198   -647    -52       O  
ATOM   1379  N   LEU A 643      28.610   9.140  12.939  1.00 14.89           N  
ANISOU 1379  N   LEU A 643     2230   1328   2099     44   -726    175       N  
ATOM   1380  CA  LEU A 643      28.422   9.894  14.205  1.00 15.33           C  
ANISOU 1380  CA  LEU A 643     2340   1429   2056     -5   -717    244       C  
ATOM   1381  C   LEU A 643      27.004   9.970  14.738  1.00 15.01           C  
ANISOU 1381  C   LEU A 643     2358   1434   1913   -108   -648    312       C  
ATOM   1382  O   LEU A 643      26.776  10.652  15.748  1.00 14.33           O  
ANISOU 1382  O   LEU A 643     2312   1397   1737   -154   -621    354       O  
ATOM   1383  CB  LEU A 643      28.975  11.316  14.025  1.00 15.27           C  
ANISOU 1383  CB  LEU A 643     2253   1513   2037     35   -650    191       C  
ATOM   1384  CG  LEU A 643      30.496  11.398  13.808  1.00 15.94           C  
ANISOU 1384  CG  LEU A 643     2276   1565   2216    121   -716    124       C  
ATOM   1385  CD1 LEU A 643      30.850  12.739  13.092  1.00 15.72           C  
ANISOU 1385  CD1 LEU A 643     2153   1630   2190    148   -614     56       C  
ATOM   1386  CD2 LEU A 643      31.184  11.313  15.141  1.00 17.15           C  
ANISOU 1386  CD2 LEU A 643     2491   1674   2352    122   -827    172       C  
ATOM   1387  N   ARG A 644      26.050   9.304  14.065  1.00 15.02           N  
ANISOU 1387  N   ARG A 644     2356   1423   1928   -147   -614    312       N  
ATOM   1388  CA  ARG A 644      24.650   9.473  14.434  1.00 15.60           C  
ANISOU 1388  CA  ARG A 644     2453   1554   1920   -244   -530    356       C  
ATOM   1389  C   ARG A 644      24.287  10.982  14.583  1.00 14.37           C  
ANISOU 1389  C   ARG A 644     2237   1517   1705   -244   -425    332       C  
ATOM   1390  O   ARG A 644      23.715  11.448  15.581  1.00 14.06           O  
ANISOU 1390  O   ARG A 644     2235   1526   1581   -310   -378    369       O  
ATOM   1391  CB  ARG A 644      24.331   8.619  15.676  1.00 18.05           C  
ANISOU 1391  CB  ARG A 644     2888   1800   2169   -337   -584    450       C  
ATOM   1392  CG  ARG A 644      24.457   7.149  15.343  1.00 20.18           C  
ANISOU 1392  CG  ARG A 644     3212   1943   2513   -341   -679    471       C  
ATOM   1393  CD  ARG A 644      24.502   6.244  16.549  1.00 23.83           C  
ANISOU 1393  CD  ARG A 644     3818   2310   2926   -417   -771    574       C  
ATOM   1394  NE  ARG A 644      23.288   6.280  17.373  1.00 26.00           N  
ANISOU 1394  NE  ARG A 644     4158   2637   3086   -557   -687    642       N  
ATOM   1395  CZ  ARG A 644      22.211   5.488  17.263  1.00 28.51           C  
ANISOU 1395  CZ  ARG A 644     4506   2929   3398   -658   -650    673       C  
ATOM   1396  NH1 ARG A 644      21.238   5.614  18.167  1.00 30.04           N  
ANISOU 1396  NH1 ARG A 644     4755   3180   3478   -792   -566    729       N  
ATOM   1397  NH2 ARG A 644      22.073   4.577  16.293  1.00 29.51           N  
ANISOU 1397  NH2 ARG A 644     4608   2978   3627   -638   -689    643       N  
ATOM   1398  N   PHE A 645      24.698  11.720  13.548  1.00 13.28           N  
ANISOU 1398  N   PHE A 645     2011   1420   1615   -168   -393    264       N  
ATOM   1399  CA  PHE A 645      24.575  13.161  13.503  1.00 12.59           C  
ANISOU 1399  CA  PHE A 645     1867   1421   1497   -149   -314    236       C  
ATOM   1400  C   PHE A 645      23.228  13.639  13.032  1.00 12.22           C  
ANISOU 1400  C   PHE A 645     1770   1441   1431   -183   -228    225       C  
ATOM   1401  O   PHE A 645      22.692  13.113  12.053  1.00 12.69           O  
ANISOU 1401  O   PHE A 645     1799   1494   1528   -183   -226    207       O  
ATOM   1402  CB  PHE A 645      25.618  13.684  12.537  1.00 12.51           C  
ANISOU 1402  CB  PHE A 645     1794   1415   1545    -65   -321    175       C  
ATOM   1403  CG  PHE A 645      25.579  15.168  12.325  1.00 11.40           C  
ANISOU 1403  CG  PHE A 645     1600   1347   1384    -43   -248    148       C  
ATOM   1404  CD1 PHE A 645      25.984  16.061  13.346  1.00 11.55           C  
ANISOU 1404  CD1 PHE A 645     1635   1389   1365    -47   -239    156       C  
ATOM   1405  CD2 PHE A 645      25.167  15.680  11.111  1.00 11.35           C  
ANISOU 1405  CD2 PHE A 645     1538   1380   1395    -21   -199    115       C  
ATOM   1406  CE1 PHE A 645      26.004  17.411  13.125  1.00 10.87           C  
ANISOU 1406  CE1 PHE A 645     1504   1352   1273    -25   -179    127       C  
ATOM   1407  CE2 PHE A 645      25.175  17.040  10.869  1.00 10.81           C  
ANISOU 1407  CE2 PHE A 645     1433   1360   1316      0   -145     98       C  
ATOM   1408  CZ  PHE A 645      25.579  17.929  11.874  1.00 10.52           C  
ANISOU 1408  CZ  PHE A 645     1406   1337   1254     -1   -132    102       C  
ATOM   1409  N   GLU A 646      22.723  14.660  13.713  1.00 12.23           N  
ANISOU 1409  N   GLU A 646     1758   1505   1383   -206   -163    226       N  
ATOM   1410  CA  GLU A 646      21.615  15.469  13.224  1.00 12.02           C  
ANISOU 1410  CA  GLU A 646     1660   1546   1362   -209    -86    198       C  
ATOM   1411  C   GLU A 646      22.067  16.927  13.252  1.00 11.65           C  
ANISOU 1411  C   GLU A 646     1578   1537   1313   -156    -52    167       C  
ATOM   1412  O   GLU A 646      22.492  17.431  14.297  1.00 12.08           O  
ANISOU 1412  O   GLU A 646     1664   1599   1325   -168    -43    172       O  
ATOM   1413  CB  GLU A 646      20.426  15.343  14.123  1.00 12.72           C  
ANISOU 1413  CB  GLU A 646     1757   1672   1406   -294    -29    215       C  
ATOM   1414  CG  GLU A 646      19.694  14.010  14.110  1.00 13.50           C  
ANISOU 1414  CG  GLU A 646     1883   1738   1507   -368    -44    246       C  
ATOM   1415  CD  GLU A 646      18.647  13.997  15.184  1.00 14.36           C  
ANISOU 1415  CD  GLU A 646     2004   1893   1558   -468     32    260       C  
ATOM   1416  OE1 GLU A 646      17.767  14.885  15.163  1.00 14.43           O  
ANISOU 1416  OE1 GLU A 646     1931   1973   1577   -469    110    214       O  
ATOM   1417  OE2 GLU A 646      18.784  13.194  16.143  1.00 15.00           O  
ANISOU 1417  OE2 GLU A 646     2181   1939   1580   -546     13    314       O  
ATOM   1418  N   HIS A 647      21.887  17.631  12.166  1.00 11.41           N  
ANISOU 1418  N   HIS A 647     1487   1528   1321   -108    -34    138       N  
ATOM   1419  CA  HIS A 647      22.286  19.061  12.130  1.00 11.16           C  
ANISOU 1419  CA  HIS A 647     1428   1518   1293    -63     -5    113       C  
ATOM   1420  C   HIS A 647      21.330  19.953  12.967  1.00 11.52           C  
ANISOU 1420  C   HIS A 647     1448   1608   1322    -84     59     97       C  
ATOM   1421  O   HIS A 647      21.757  20.748  13.794  1.00 11.86           O  
ANISOU 1421  O   HIS A 647     1506   1657   1342    -81     80     82       O  
ATOM   1422  CB  HIS A 647      22.340  19.600  10.716  1.00 11.24           C  
ANISOU 1422  CB  HIS A 647     1398   1531   1340    -14     -8     97       C  
ATOM   1423  CG  HIS A 647      22.893  20.973  10.666  1.00 11.32           C  
ANISOU 1423  CG  HIS A 647     1397   1546   1358     23     14     82       C  
ATOM   1424  ND1 HIS A 647      22.145  22.091  11.018  1.00 11.93           N  
ANISOU 1424  ND1 HIS A 647     1444   1643   1444     32     52     69       N  
ATOM   1425  CD2 HIS A 647      24.131  21.434  10.357  1.00 11.91           C  
ANISOU 1425  CD2 HIS A 647     1483   1602   1441     48      4     72       C  
ATOM   1426  CE1 HIS A 647      22.917  23.163  10.968  1.00 11.82           C  
ANISOU 1426  CE1 HIS A 647     1436   1614   1440     61     61     58       C  
ATOM   1427  NE2 HIS A 647      24.114  22.797  10.545  1.00 11.47           N  
ANISOU 1427  NE2 HIS A 647     1415   1550   1394     66     35     62       N  
ATOM   1428  N   ARG A 648      20.031  19.716  12.761  1.00 11.32           N  
ANISOU 1428  N   ARG A 648     1378   1610   1313   -110     87     90       N  
ATOM   1429  CA  ARG A 648      18.916  20.338  13.519  1.00 12.13           C  
ANISOU 1429  CA  ARG A 648     1435   1759   1413   -138    157     58       C  
ATOM   1430  C   ARG A 648      18.643  21.872  13.259  1.00 12.21           C  
ANISOU 1430  C   ARG A 648     1386   1783   1472    -75    184     15       C  
ATOM   1431  O   ARG A 648      17.676  22.405  13.742  1.00 12.65           O  
ANISOU 1431  O   ARG A 648     1386   1873   1549    -83    239    -28       O  
ATOM   1432  CB  ARG A 648      18.972  20.045  14.981  1.00 12.92           C  
ANISOU 1432  CB  ARG A 648     1590   1876   1443   -207    195     63       C  
ATOM   1433  CG  ARG A 648      18.899  18.588  15.281  1.00 13.24           C  
ANISOU 1433  CG  ARG A 648     1689   1898   1445   -280    170    110       C  
ATOM   1434  CD  ARG A 648      18.846  18.300  16.755  1.00 14.12           C  
ANISOU 1434  CD  ARG A 648     1871   2028   1467   -366    208    125       C  
ATOM   1435  NE  ARG A 648      18.716  16.874  17.022  1.00 14.64           N  
ANISOU 1435  NE  ARG A 648     2004   2061   1496   -444    177    183       N  
ATOM   1436  CZ  ARG A 648      18.804  16.302  18.212  1.00 15.42           C  
ANISOU 1436  CZ  ARG A 648     2200   2157   1503   -533    183    224       C  
ATOM   1437  NH1 ARG A 648      18.999  17.035  19.290  1.00 16.12           N  
ANISOU 1437  NH1 ARG A 648     2325   2285   1515   -558    226    205       N  
ATOM   1438  NH2 ARG A 648      18.659  14.971  18.323  1.00 15.95           N  
ANISOU 1438  NH2 ARG A 648     2334   2176   1548   -604    144    285       N  
ATOM   1439  N   ASP A 649      19.420  22.497  12.397  1.00 12.07           N  
ANISOU 1439  N   ASP A 649     1375   1732   1478    -15    144     24       N  
ATOM   1440  CA  ASP A 649      19.243  23.903  12.059  1.00 12.97           C  
ANISOU 1440  CA  ASP A 649     1451   1836   1640     43    153     -2       C  
ATOM   1441  C   ASP A 649      19.750  24.291  10.672  1.00 12.51           C  
ANISOU 1441  C   ASP A 649     1403   1744   1606     91    100     26       C  
ATOM   1442  O   ASP A 649      20.444  25.289  10.488  1.00 12.74           O  
ANISOU 1442  O   ASP A 649     1452   1744   1646    122     97     26       O  
ATOM   1443  CB  ASP A 649      19.847  24.808  13.140  1.00 13.72           C  
ANISOU 1443  CB  ASP A 649     1571   1926   1716     44    190    -32       C  
ATOM   1444  CG  ASP A 649      19.386  26.255  13.017  1.00 15.63           C  
ANISOU 1444  CG  ASP A 649     1767   2151   2022     98    207    -73       C  
ATOM   1445  OD1 ASP A 649      18.280  26.523  12.523  1.00 16.14           O  
ANISOU 1445  OD1 ASP A 649     1765   2221   2146    126    205    -91       O  
ATOM   1446  OD2 ASP A 649      20.157  27.154  13.374  1.00 16.60           O  
ANISOU 1446  OD2 ASP A 649     1917   2245   2145    114    214    -89       O  
ATOM   1447  N   LEU A 650      19.466  23.466   9.659  1.00 13.09           N  
ANISOU 1447  N   LEU A 650     1473   1823   1680     87     60     50       N  
ATOM   1448  CA  LEU A 650      20.110  23.622   8.396  1.00 12.56           C  
ANISOU 1448  CA  LEU A 650     1435   1733   1605    112     19     76       C  
ATOM   1449  C   LEU A 650      19.272  24.519   7.453  1.00 12.93           C  
ANISOU 1449  C   LEU A 650     1452   1770   1690    154    -16     84       C  
ATOM   1450  O   LEU A 650      18.880  24.099   6.340  1.00 12.36           O  
ANISOU 1450  O   LEU A 650     1381   1705   1611    157    -64    102       O  
ATOM   1451  CB  LEU A 650      20.392  22.244   7.783  1.00 13.54           C  
ANISOU 1451  CB  LEU A 650     1583   1863   1700     84     -9     88       C  
ATOM   1452  CG  LEU A 650      21.418  22.249   6.644  1.00 14.96           C  
ANISOU 1452  CG  LEU A 650     1804   2027   1855     95    -30     98       C  
ATOM   1453  CD1 LEU A 650      22.733  22.900   7.016  1.00 15.05           C  
ANISOU 1453  CD1 LEU A 650     1843   2018   1859    101     -3     94       C  
ATOM   1454  CD2 LEU A 650      21.537  20.794   6.171  1.00 15.53           C  
ANISOU 1454  CD2 LEU A 650     1888   2102   1910     69    -53     90       C  
ATOM   1455  N   HIS A 651      19.030  25.740   7.922  1.00 12.66           N  
ANISOU 1455  N   HIS A 651     1397   1716   1698    187     -1     68       N  
ATOM   1456  CA  HIS A 651      18.377  26.739   7.113  1.00 13.18           C  
ANISOU 1456  CA  HIS A 651     1444   1752   1811    237    -49     81       C  
ATOM   1457  C   HIS A 651      19.362  27.265   6.098  1.00 12.96           C  
ANISOU 1457  C   HIS A 651     1492   1687   1745    240    -78    129       C  
ATOM   1458  O   HIS A 651      20.576  26.974   6.172  1.00 13.19           O  
ANISOU 1458  O   HIS A 651     1569   1717   1726    208    -46    135       O  
ATOM   1459  CB  HIS A 651      17.737  27.807   7.966  1.00 14.18           C  
ANISOU 1459  CB  HIS A 651     1517   1859   2010    275    -25     37       C  
ATOM   1460  CG  HIS A 651      18.691  28.594   8.775  1.00 14.78           C  
ANISOU 1460  CG  HIS A 651     1631   1905   2078    273     21     21       C  
ATOM   1461  ND1 HIS A 651      19.491  29.573   8.230  1.00 15.92           N  
ANISOU 1461  ND1 HIS A 651     1833   1992   2225    290     -1     54       N  
ATOM   1462  CD2 HIS A 651      18.961  28.582  10.096  1.00 14.93           C  
ANISOU 1462  CD2 HIS A 651     1644   1944   2084    248     86    -25       C  
ATOM   1463  CE1 HIS A 651      20.259  30.093   9.175  1.00 15.47           C  
ANISOU 1463  CE1 HIS A 651     1794   1919   2164    278     47     23       C  
ATOM   1464  NE2 HIS A 651      19.950  29.521  10.322  1.00 15.09           N  
ANISOU 1464  NE2 HIS A 651     1710   1919   2103    255     96    -25       N  
ATOM   1465  N   TRP A 652      18.869  28.035   5.141  1.00 12.76           N  
ANISOU 1465  N   TRP A 652     1480   1628   1742    275   -141    162       N  
ATOM   1466  CA  TRP A 652      19.698  28.392   4.003  1.00 13.31           C  
ANISOU 1466  CA  TRP A 652     1634   1670   1752    258   -168    217       C  
ATOM   1467  C   TRP A 652      20.818  29.373   4.298  1.00 13.84           C  
ANISOU 1467  C   TRP A 652     1751   1691   1816    247   -126    227       C  
ATOM   1468  O   TRP A 652      21.635  29.638   3.437  1.00 14.09           O  
ANISOU 1468  O   TRP A 652     1854   1707   1794    215   -127    267       O  
ATOM   1469  CB  TRP A 652      18.886  28.791   2.792  1.00 14.23           C  
ANISOU 1469  CB  TRP A 652     1773   1765   1870    285   -262    264       C  
ATOM   1470  CG  TRP A 652      17.971  29.968   2.907  1.00 15.06           C  
ANISOU 1470  CG  TRP A 652     1846   1810   2065    350   -322    270       C  
ATOM   1471  CD1 TRP A 652      17.606  30.671   4.053  1.00 15.46           C  
ANISOU 1471  CD1 TRP A 652     1832   1833   2210    391   -289    219       C  
ATOM   1472  CD2 TRP A 652      17.337  30.620   1.821  1.00 16.14           C  
ANISOU 1472  CD2 TRP A 652     2019   1901   2212    384   -431    326       C  
ATOM   1473  NE1 TRP A 652      16.736  31.717   3.702  1.00 16.60           N  
ANISOU 1473  NE1 TRP A 652     1958   1910   2439    459   -375    233       N  
ATOM   1474  CE2 TRP A 652      16.575  31.701   2.348  1.00 17.04           C  
ANISOU 1474  CE2 TRP A 652     2079   1951   2446    456   -470    305       C  
ATOM   1475  CE3 TRP A 652      17.335  30.408   0.440  1.00 16.41           C  
ANISOU 1475  CE3 TRP A 652     2132   1940   2162    359   -507    390       C  
ATOM   1476  CZ2 TRP A 652      15.824  32.536   1.523  1.00 18.26           C  
ANISOU 1476  CZ2 TRP A 652     2253   2036   2648    511   -596    354       C  
ATOM   1477  CZ3 TRP A 652      16.598  31.243  -0.357  1.00 18.03           C  
ANISOU 1477  CZ3 TRP A 652     2369   2085   2397    404   -630    445       C  
ATOM   1478  CH2 TRP A 652      15.858  32.274   0.173  1.00 18.53           C  
ANISOU 1478  CH2 TRP A 652     2376   2077   2590    483   -681    430       C  
ATOM   1479  N   GLY A 653      20.831  29.967   5.489  1.00 13.37           N  
ANISOU 1479  N   GLY A 653     1656   1611   1814    266    -88    186       N  
ATOM   1480  CA  GLY A 653      22.013  30.738   5.876  1.00 13.81           C  
ANISOU 1480  CA  GLY A 653     1754   1629   1865    244    -45    184       C  
ATOM   1481  C   GLY A 653      23.168  29.876   6.368  1.00 13.45           C  
ANISOU 1481  C   GLY A 653     1712   1627   1772    197     11    158       C  
ATOM   1482  O   GLY A 653      24.270  30.394   6.553  1.00 14.19           O  
ANISOU 1482  O   GLY A 653     1834   1698   1861    170     42    153       O  
ATOM   1483  N   ASN A 654      22.904  28.581   6.631  1.00 12.19           N  
ANISOU 1483  N   ASN A 654     1520   1523   1587    187     16    139       N  
ATOM   1484  CA  ASN A 654      23.906  27.640   7.152  1.00 11.59           C  
ANISOU 1484  CA  ASN A 654     1446   1478   1480    153     47    114       C  
ATOM   1485  C   ASN A 654      24.418  26.653   6.068  1.00 11.88           C  
ANISOU 1485  C   ASN A 654     1504   1541   1471    128     38    127       C  
ATOM   1486  O   ASN A 654      25.063  25.660   6.410  1.00 11.36           O  
ANISOU 1486  O   ASN A 654     1429   1495   1393    111     49    102       O  
ATOM   1487  CB  ASN A 654      23.343  26.902   8.358  1.00 11.80           C  
ANISOU 1487  CB  ASN A 654     1435   1534   1512    152     58     82       C  
ATOM   1488  CG  ASN A 654      23.244  27.787   9.596  1.00 12.43           C  
ANISOU 1488  CG  ASN A 654     1502   1601   1621    161     87     48       C  
ATOM   1489  OD1 ASN A 654      23.892  28.824   9.668  1.00 12.99           O  
ANISOU 1489  OD1 ASN A 654     1592   1634   1710    166     97     42       O  
ATOM   1490  ND2 ASN A 654      22.446  27.376  10.575  1.00 13.00           N  
ANISOU 1490  ND2 ASN A 654     1544   1703   1692    155    106     20       N  
ATOM   1491  N   VAL A 655      24.153  26.966   4.803  1.00 11.90           N  
ANISOU 1491  N   VAL A 655     1538   1536   1446    126     15    162       N  
ATOM   1492  CA  VAL A 655      24.660  26.231   3.679  1.00 11.80           C  
ANISOU 1492  CA  VAL A 655     1556   1550   1380     96     16    165       C  
ATOM   1493  C   VAL A 655      25.500  27.199   2.887  1.00 12.77           C  
ANISOU 1493  C   VAL A 655     1731   1650   1471     64     42    190       C  
ATOM   1494  O   VAL A 655      24.989  28.235   2.441  1.00 14.44           O  
ANISOU 1494  O   VAL A 655     1981   1826   1682     72     12    238       O  
ATOM   1495  CB  VAL A 655      23.514  25.680   2.842  1.00 12.56           C  
ANISOU 1495  CB  VAL A 655     1655   1666   1451    105    -37    185       C  
ATOM   1496  CG1 VAL A 655      24.019  25.027   1.588  1.00 12.92           C  
ANISOU 1496  CG1 VAL A 655     1743   1740   1428     69    -33    180       C  
ATOM   1497  CG2 VAL A 655      22.693  24.709   3.691  1.00 12.40           C  
ANISOU 1497  CG2 VAL A 655     1578   1666   1466    121    -51    158       C  
ATOM   1498  N   LEU A 656      26.790  26.912   2.720  1.00 12.09           N  
ANISOU 1498  N   LEU A 656     1646   1579   1367     26     94    157       N  
ATOM   1499  CA  LEU A 656      27.671  27.778   1.951  1.00 12.82           C  
ANISOU 1499  CA  LEU A 656     1787   1658   1426    -24    137    174       C  
ATOM   1500  C   LEU A 656      28.090  27.191   0.604  1.00 13.37           C  
ANISOU 1500  C   LEU A 656     1895   1771   1416    -73    165    165       C  
ATOM   1501  O   LEU A 656      28.298  25.960   0.466  1.00 13.27           O  
ANISOU 1501  O   LEU A 656     1847   1798   1395    -70    175    111       O  
ATOM   1502  CB  LEU A 656      28.945  28.056   2.746  1.00 13.41           C  
ANISOU 1502  CB  LEU A 656     1824   1725   1547    -44    190    128       C  
ATOM   1503  CG  LEU A 656      28.782  28.555   4.177  1.00 14.20           C  
ANISOU 1503  CG  LEU A 656     1889   1792   1716     -7    172    117       C  
ATOM   1504  CD1 LEU A 656      30.150  28.917   4.759  1.00 14.65           C  
ANISOU 1504  CD1 LEU A 656     1915   1841   1810    -38    216     71       C  
ATOM   1505  CD2 LEU A 656      27.868  29.757   4.230  1.00 15.16           C  
ANISOU 1505  CD2 LEU A 656     2046   1860   1852     14    141    169       C  
ATOM   1506  N   LEU A 657      28.232  28.060  -0.389  1.00 13.80           N  
ANISOU 1506  N   LEU A 657     2025   1812   1406   -124    179    215       N  
ATOM   1507  CA  LEU A 657      28.653  27.691  -1.730  1.00 15.27           C  
ANISOU 1507  CA  LEU A 657     2265   2043   1492   -189    218    209       C  
ATOM   1508  C   LEU A 657      29.920  28.395  -2.142  1.00 16.25           C  
ANISOU 1508  C   LEU A 657     2418   2170   1588   -271    310    199       C  
ATOM   1509  O   LEU A 657      30.053  29.615  -1.983  1.00 15.96           O  
ANISOU 1509  O   LEU A 657     2421   2078   1564   -295    312    254       O  
ATOM   1510  CB  LEU A 657      27.566  28.071  -2.790  1.00 16.34           C  
ANISOU 1510  CB  LEU A 657     2496   2169   1543   -197    144    291       C  
ATOM   1511  CG  LEU A 657      26.151  27.629  -2.451  1.00 16.64           C  
ANISOU 1511  CG  LEU A 657     2504   2199   1619   -120     44    308       C  
ATOM   1512  CD1 LEU A 657      25.216  28.207  -3.473  1.00 18.30           C  
ANISOU 1512  CD1 LEU A 657     2805   2390   1760   -127    -41    391       C  
ATOM   1513  CD2 LEU A 657      25.980  26.150  -2.271  1.00 16.74           C  
ANISOU 1513  CD2 LEU A 657     2453   2262   1646    -97     45    237       C  
ATOM   1514  N   LYS A 658      30.871  27.634  -2.698  1.00 17.28           N  
ANISOU 1514  N   LYS A 658     2523   2360   1684   -320    391    122       N  
ATOM   1515  CA  LYS A 658      32.127  28.164  -3.235  1.00 19.94           C  
ANISOU 1515  CA  LYS A 658     2872   2717   1987   -416    500     94       C  
ATOM   1516  C   LYS A 658      32.387  27.570  -4.608  1.00 20.54           C  
ANISOU 1516  C   LYS A 658     2999   2862   1942   -489    561     59       C  
ATOM   1517  O   LYS A 658      32.110  26.411  -4.825  1.00 18.82           O  
ANISOU 1517  O   LYS A 658     2750   2686   1716   -452    544      0       O  
ATOM   1518  CB  LYS A 658      33.259  27.687  -2.301  1.00 22.40           C  
ANISOU 1518  CB  LYS A 658     3058   3043   2411   -397    553    -11       C  
ATOM   1519  CG  LYS A 658      34.450  28.557  -2.202  1.00 27.17           C  
ANISOU 1519  CG  LYS A 658     3638   3639   3044   -471    640    -35       C  
ATOM   1520  CD  LYS A 658      35.576  27.925  -1.328  1.00 28.55           C  
ANISOU 1520  CD  LYS A 658     3673   3834   3339   -442    675   -152       C  
ATOM   1521  CE  LYS A 658      35.187  26.803  -0.359  1.00 29.22           C  
ANISOU 1521  CE  LYS A 658     3686   3914   3504   -333    590   -192       C  
ATOM   1522  NZ  LYS A 658      36.363  26.463   0.553  1.00 30.73           N  
ANISOU 1522  NZ  LYS A 658     3754   4107   3815   -310    603   -289       N  
ATOM   1523  N   LYS A 659      32.985  28.352  -5.524  1.00 21.79           N  
ANISOU 1523  N   LYS A 659     3238   3036   2006   -601    641     87       N  
ATOM   1524  CA  LYS A 659      33.359  27.827  -6.790  1.00 24.15           C  
ANISOU 1524  CA  LYS A 659     3586   3411   2179   -686    721     40       C  
ATOM   1525  C   LYS A 659      34.427  26.736  -6.614  1.00 23.41           C  
ANISOU 1525  C   LYS A 659     3358   3380   2156   -679    817   -121       C  
ATOM   1526  O   LYS A 659      35.292  26.825  -5.718  1.00 22.53           O  
ANISOU 1526  O   LYS A 659     3136   3253   2171   -659    855   -181       O  
ATOM   1527  CB  LYS A 659      33.968  28.903  -7.684  1.00 28.82           C  
ANISOU 1527  CB  LYS A 659     4285   4008   2658   -826    810     94       C  
ATOM   1528  CG  LYS A 659      33.002  29.815  -8.400  1.00 32.62           C  
ANISOU 1528  CG  LYS A 659     4937   4441   3018   -863    723    247       C  
ATOM   1529  CD  LYS A 659      33.793  30.868  -9.194  1.00 38.08           C  
ANISOU 1529  CD  LYS A 659     5737   5131   3602  -1019    825    300       C  
ATOM   1530  CE  LYS A 659      34.857  30.210 -10.110  1.00 41.55           C  
ANISOU 1530  CE  LYS A 659     6161   5685   3943  -1136    993    182       C  
ATOM   1531  NZ  LYS A 659      35.524  31.103 -11.105  1.00 46.70           N  
ANISOU 1531  NZ  LYS A 659     6943   6355   4447  -1316   1106    235       N  
ATOM   1532  N   THR A 660      34.340  25.718  -7.444  1.00 23.41           N  
ANISOU 1532  N   THR A 660     3367   3444   2084   -691    843   -193       N  
ATOM   1533  CA  THR A 660      35.398  24.680  -7.535  1.00 24.00           C  
ANISOU 1533  CA  THR A 660     3324   3578   2218   -694    943   -360       C  
ATOM   1534  C   THR A 660      35.689  24.377  -8.972  1.00 25.78           C  
ANISOU 1534  C   THR A 660     3618   3888   2289   -800   1047   -420       C  
ATOM   1535  O   THR A 660      34.774  24.377  -9.811  1.00 25.24           O  
ANISOU 1535  O   THR A 660     3679   3835   2078   -828    995   -349       O  
ATOM   1536  CB  THR A 660      35.025  23.362  -6.801  1.00 23.01           C  
ANISOU 1536  CB  THR A 660     3102   3433   2209   -568    858   -430       C  
ATOM   1537  OG1 THR A 660      36.107  22.422  -6.932  1.00 24.10           O  
ANISOU 1537  OG1 THR A 660     3125   3615   2417   -567    948   -595       O  
ATOM   1538  CG2 THR A 660      33.820  22.704  -7.401  1.00 22.98           C  
ANISOU 1538  CG2 THR A 660     3179   3438   2116   -541    774   -395       C  
ATOM   1539  N   SER A 661      36.960  24.075  -9.272  1.00 26.99           N  
ANISOU 1539  N   SER A 661     3682   4102   2470   -860   1193   -561       N  
ATOM   1540  CA ASER A 661      37.363  23.596 -10.595  0.50 28.95           C  
ANISOU 1540  CA ASER A 661     3973   4445   2582   -961   1317   -661       C  
ATOM   1541  CA BSER A 661      37.335  23.607 -10.599  0.50 28.76           C  
ANISOU 1541  CA BSER A 661     3952   4420   2555   -961   1314   -657       C  
ATOM   1542  C   SER A 661      37.182  22.106 -10.748  1.00 28.54           C  
ANISOU 1542  C   SER A 661     3854   4418   2572   -882   1292   -792       C  
ATOM   1543  O   SER A 661      37.297  21.600 -11.818  1.00 29.24           O  
ANISOU 1543  O   SER A 661     3987   4580   2543   -949   1372   -876       O  
ATOM   1544  CB ASER A 661      38.845  23.928 -10.894  0.50 30.59           C  
ANISOU 1544  CB ASER A 661     4098   4715   2808  -1071   1505   -777       C  
ATOM   1545  CB BSER A 661      38.784  24.014 -10.934  0.50 30.23           C  
ANISOU 1545  CB BSER A 661     4068   4668   2750  -1077   1502   -763       C  
ATOM   1546  OG ASER A 661      39.040  25.312 -11.096  0.50 31.38           O  
ANISOU 1546  OG ASER A 661     4295   4803   2825  -1187   1554   -660       O  
ATOM   1547  OG BSER A 661      39.661  23.672  -9.874  0.50 29.47           O  
ANISOU 1547  OG BSER A 661     3782   4546   2868   -997   1514   -869       O  
ATOM   1548  N   LEU A 662      36.906  21.398  -9.664  1.00 27.70           N  
ANISOU 1548  N   LEU A 662     3647   4246   2633   -743   1182   -810       N  
ATOM   1549  CA  LEU A 662      36.716  19.954  -9.767  1.00 28.07           C  
ANISOU 1549  CA  LEU A 662     3636   4297   2733   -666   1148   -929       C  
ATOM   1550  C   LEU A 662      35.365  19.643 -10.405  1.00 28.61           C  
ANISOU 1550  C   LEU A 662     3837   4366   2667   -664   1050   -850       C  
ATOM   1551  O   LEU A 662      34.355  20.222 -10.015  1.00 27.36           O  
ANISOU 1551  O   LEU A 662     3754   4159   2484   -635    933   -697       O  
ATOM   1552  CB  LEU A 662      36.797  19.309  -8.401  1.00 28.28           C  
ANISOU 1552  CB  LEU A 662     3534   4243   2967   -530   1049   -954       C  
ATOM   1553  CG  LEU A 662      38.148  19.405  -7.660  1.00 29.64           C  
ANISOU 1553  CG  LEU A 662     3553   4407   3303   -510   1114  -1051       C  
ATOM   1554  CD1 LEU A 662      37.902  18.830  -6.276  1.00 29.51           C  
ANISOU 1554  CD1 LEU A 662     3459   4299   3454   -376    973  -1028       C  
ATOM   1555  CD2 LEU A 662      39.219  18.661  -8.419  1.00 32.36           C  
ANISOU 1555  CD2 LEU A 662     3801   4816   3676   -543   1249  -1253       C  
ATOM   1556  N   LYS A 663      35.365  18.704 -11.335  1.00 29.53           N  
ANISOU 1556  N   LYS A 663     3970   4537   2713   -689   1095   -968       N  
ATOM   1557  CA  LYS A 663      34.168  18.266 -12.037  1.00 31.40           C  
ANISOU 1557  CA  LYS A 663     4324   4784   2824   -693   1004   -923       C  
ATOM   1558  C   LYS A 663      33.307  17.385 -11.155  1.00 29.67           C  
ANISOU 1558  C   LYS A 663     4051   4484   2737   -566    855   -904       C  
ATOM   1559  O   LYS A 663      32.106  17.379 -11.279  1.00 28.34           O  
ANISOU 1559  O   LYS A 663     3965   4296   2505   -551    740   -807       O  
ATOM   1560  CB  LYS A 663      34.563  17.465 -13.299  1.00 35.13           C  
ANISOU 1560  CB  LYS A 663     4821   5343   3183   -766   1112  -1084       C  
ATOM   1561  CG  LYS A 663      35.330  18.247 -14.353  1.00 40.74           C  
ANISOU 1561  CG  LYS A 663     5607   6150   3722   -919   1275  -1111       C  
ATOM   1562  CD  LYS A 663      34.529  19.453 -14.846  1.00 44.02           C  
ANISOU 1562  CD  LYS A 663     6204   6572   3951  -1002   1216   -912       C  
ATOM   1563  CE  LYS A 663      35.168  20.126 -16.066  1.00 48.90           C  
ANISOU 1563  CE  LYS A 663     6935   7288   4355  -1177   1372   -929       C  
ATOM   1564  NZ  LYS A 663      35.363  21.597 -15.774  1.00 50.58           N  
ANISOU 1564  NZ  LYS A 663     7209   7469   4541  -1240   1382   -768       N  
ATOM   1565  N   LYS A 664      33.929  16.637 -10.253  1.00 29.03           N  
ANISOU 1565  N   LYS A 664     3833   4353   2843   -479    853   -997       N  
ATOM   1566  CA  LYS A 664      33.179  15.827  -9.341  1.00 29.06           C  
ANISOU 1566  CA  LYS A 664     3796   4274   2970   -373    718   -969       C  
ATOM   1567  C   LYS A 664      33.805  15.791  -7.968  1.00 26.82           C  
ANISOU 1567  C   LYS A 664     3395   3921   2873   -291    691   -970       C  
ATOM   1568  O   LYS A 664      35.035  15.948  -7.807  1.00 26.63           O  
ANISOU 1568  O   LYS A 664     3282   3912   2923   -297    782  -1057       O  
ATOM   1569  CB  LYS A 664      32.957  14.441  -9.891  1.00 33.14           C  
ANISOU 1569  CB  LYS A 664     4304   4789   3500   -350    700  -1096       C  
ATOM   1570  CG  LYS A 664      34.191  13.627 -10.083  1.00 35.74           C  
ANISOU 1570  CG  LYS A 664     4527   5128   3926   -334    800  -1290       C  
ATOM   1571  CD  LYS A 664      33.932  12.485 -11.063  1.00 40.22           C  
ANISOU 1571  CD  LYS A 664     5123   5718   4443   -347    811  -1425       C  
ATOM   1572  CE  LYS A 664      35.253  11.816 -11.466  1.00 43.12           C  
ANISOU 1572  CE  LYS A 664     5381   6110   4891   -345    940  -1643       C  
ATOM   1573  NZ  LYS A 664      35.065  10.408 -11.914  1.00 45.51           N  
ANISOU 1573  NZ  LYS A 664     5669   6382   5243   -305    913  -1792       N  
ATOM   1574  N   LEU A 665      32.932  15.592  -7.005  1.00 24.11           N  
ANISOU 1574  N   LEU A 665     3054   3507   2599   -221    565   -874       N  
ATOM   1575  CA  LEU A 665      33.292  15.560  -5.614  1.00 23.12           C  
ANISOU 1575  CA  LEU A 665     2846   3313   2627   -146    512   -848       C  
ATOM   1576  C   LEU A 665      33.172  14.127  -5.138  1.00 22.41           C  
ANISOU 1576  C   LEU A 665     2706   3153   2657    -70    435   -919       C  
ATOM   1577  O   LEU A 665      32.354  13.381  -5.642  1.00 22.19           O  
ANISOU 1577  O   LEU A 665     2726   3118   2587    -72    391   -931       O  
ATOM   1578  CB  LEU A 665      32.395  16.468  -4.817  1.00 22.17           C  
ANISOU 1578  CB  LEU A 665     2773   3163   2486   -135    435   -686       C  
ATOM   1579  CG  LEU A 665      32.456  17.889  -5.428  1.00 23.38           C  
ANISOU 1579  CG  LEU A 665     2994   3371   2519   -214    501   -613       C  
ATOM   1580  CD1 LEU A 665      31.348  18.674  -4.844  1.00 23.19           C  
ANISOU 1580  CD1 LEU A 665     3025   3316   2472   -197    415   -467       C  
ATOM   1581  CD2 LEU A 665      33.783  18.573  -5.269  1.00 23.60           C  
ANISOU 1581  CD2 LEU A 665     2960   3419   2587   -245    600   -660       C  
ATOM   1582  N   HIS A 666      33.999  13.762  -4.151  1.00 21.57           N  
ANISOU 1582  N   HIS A 666     2505   2988   2701     -5    409   -962       N  
ATOM   1583  CA  HIS A 666      34.104  12.377  -3.698  1.00 21.38           C  
ANISOU 1583  CA  HIS A 666     2433   2882   2807     69    333  -1037       C  
ATOM   1584  C   HIS A 666      33.652  12.230  -2.270  1.00 19.17           C  
ANISOU 1584  C   HIS A 666     2156   2519   2609    125    214   -930       C  
ATOM   1585  O   HIS A 666      33.910  13.115  -1.412  1.00 18.97           O  
ANISOU 1585  O   HIS A 666     2114   2494   2599    130    205   -853       O  
ATOM   1586  CB  HIS A 666      35.564  11.936  -3.772  1.00 23.62           C  
ANISOU 1586  CB  HIS A 666     2601   3159   3215    105    390  -1196       C  
ATOM   1587  CG  HIS A 666      36.112  11.939  -5.150  1.00 26.18           C  
ANISOU 1587  CG  HIS A 666     2912   3569   3467     45    525  -1330       C  
ATOM   1588  ND1 HIS A 666      36.150  10.812  -5.915  1.00 28.36           N  
ANISOU 1588  ND1 HIS A 666     3176   3834   3765     59    540  -1467       N  
ATOM   1589  CD2 HIS A 666      36.593  12.943  -5.925  1.00 27.12           C  
ANISOU 1589  CD2 HIS A 666     3039   3786   3478    -41    656  -1347       C  
ATOM   1590  CE1 HIS A 666      36.662  11.104  -7.101  1.00 29.12           C  
ANISOU 1590  CE1 HIS A 666     3270   4028   3766    -16    681  -1573       C  
ATOM   1591  NE2 HIS A 666      36.930  12.395  -7.128  1.00 28.54           N  
ANISOU 1591  NE2 HIS A 666     3213   4022   3608    -82    754  -1496       N  
ATOM   1592  N   TYR A 667      32.957  11.135  -1.988  1.00 18.25           N  
ANISOU 1592  N   TYR A 667     2066   2331   2537    158    123   -922       N  
ATOM   1593  CA  TYR A 667      32.613  10.750  -0.592  1.00 17.31           C  
ANISOU 1593  CA  TYR A 667     1954   2122   2500    204      8   -832       C  
ATOM   1594  C   TYR A 667      32.674   9.252  -0.474  1.00 16.82           C  
ANISOU 1594  C   TYR A 667     1882   1962   2547    252    -69   -903       C  
ATOM   1595  O   TYR A 667      32.640   8.538  -1.503  1.00 17.65           O  
ANISOU 1595  O   TYR A 667     1987   2072   2647    245    -39  -1008       O  
ATOM   1596  CB  TYR A 667      31.235  11.284  -0.169  1.00 16.25           C  
ANISOU 1596  CB  TYR A 667     1897   2002   2274    166    -29   -686       C  
ATOM   1597  CG  TYR A 667      30.080  10.601  -0.809  1.00 16.44           C  
ANISOU 1597  CG  TYR A 667     1977   2022   2246    137    -57   -679       C  
ATOM   1598  CD1 TYR A 667      29.627  10.983  -2.076  1.00 17.16           C  
ANISOU 1598  CD1 TYR A 667     2103   2193   2225     87      0   -701       C  
ATOM   1599  CD2 TYR A 667      29.474   9.516  -0.193  1.00 16.63           C  
ANISOU 1599  CD2 TYR A 667     2024   1961   2335    153   -147   -655       C  
ATOM   1600  CE1 TYR A 667      28.606  10.302  -2.694  1.00 17.57           C  
ANISOU 1600  CE1 TYR A 667     2200   2242   2235     60    -37   -708       C  
ATOM   1601  CE2 TYR A 667      28.470   8.838  -0.778  1.00 17.28           C  
ANISOU 1601  CE2 TYR A 667     2147   2034   2383    121   -174   -660       C  
ATOM   1602  CZ  TYR A 667      27.991   9.247  -2.026  1.00 18.05           C  
ANISOU 1602  CZ  TYR A 667     2270   2217   2371     76   -123   -688       C  
ATOM   1603  OH  TYR A 667      26.975   8.507  -2.570  1.00 19.37           O  
ANISOU 1603  OH  TYR A 667     2475   2373   2513     44   -165   -699       O  
ATOM   1604  N   THR A 668      32.748   8.787   0.782  1.00 16.11           N  
ANISOU 1604  N   THR A 668     1792   1779   2549    297   -172   -845       N  
ATOM   1605  CA  THR A 668      32.724   7.346   1.077  1.00 16.95           C  
ANISOU 1605  CA  THR A 668     1908   1765   2767    342   -271   -884       C  
ATOM   1606  C   THR A 668      31.674   7.144   2.165  1.00 16.08           C  
ANISOU 1606  C   THR A 668     1880   1598   2633    318   -362   -735       C  
ATOM   1607  O   THR A 668      31.706   7.823   3.167  1.00 14.90           O  
ANISOU 1607  O   THR A 668     1741   1457   2464    315   -385   -641       O  
ATOM   1608  CB  THR A 668      34.108   6.825   1.527  1.00 17.93           C  
ANISOU 1608  CB  THR A 668     1949   1814   3052    425   -321   -978       C  
ATOM   1609  OG1 THR A 668      35.075   7.108   0.494  1.00 19.09           O  
ANISOU 1609  OG1 THR A 668     2006   2031   3217    434   -212  -1128       O  
ATOM   1610  CG2 THR A 668      34.056   5.339   1.743  1.00 19.14           C  
ANISOU 1610  CG2 THR A 668     2121   1827   3325    473   -433  -1018       C  
ATOM   1611  N   LEU A 669      30.718   6.267   1.908  1.00 16.57           N  
ANISOU 1611  N   LEU A 669     1998   1613   2685    289   -401   -722       N  
ATOM   1612  CA  LEU A 669      29.687   5.922   2.856  1.00 17.25           C  
ANISOU 1612  CA  LEU A 669     2158   1643   2753    251   -475   -596       C  
ATOM   1613  C   LEU A 669      29.745   4.430   3.196  1.00 18.44           C  
ANISOU 1613  C   LEU A 669     2343   1647   3018    276   -582   -618       C  
ATOM   1614  O   LEU A 669      29.567   3.553   2.310  1.00 19.74           O  
ANISOU 1614  O   LEU A 669     2508   1772   3219    277   -585   -709       O  
ATOM   1615  CB  LEU A 669      28.302   6.256   2.298  1.00 17.35           C  
ANISOU 1615  CB  LEU A 669     2210   1731   2653    177   -430   -545       C  
ATOM   1616  CG  LEU A 669      27.101   5.831   3.169  1.00 17.94           C  
ANISOU 1616  CG  LEU A 669     2350   1758   2710    121   -488   -431       C  
ATOM   1617  CD1 LEU A 669      27.055   6.714   4.410  1.00 17.26           C  
ANISOU 1617  CD1 LEU A 669     2276   1698   2584    110   -488   -321       C  
ATOM   1618  CD2 LEU A 669      25.769   5.891   2.434  1.00 18.21           C  
ANISOU 1618  CD2 LEU A 669     2400   1851   2667     55   -457   -418       C  
ATOM   1619  N   ASN A 670      29.960   4.130   4.472  1.00 19.35           N  
ANISOU 1619  N   ASN A 670     2495   1674   3184    292   -675   -533       N  
ATOM   1620  CA  ASN A 670      30.188   2.746   4.944  1.00 21.14           C  
ANISOU 1620  CA  ASN A 670     2765   1736   3531    323   -800   -539       C  
ATOM   1621  C   ASN A 670      31.080   1.914   4.012  1.00 23.00           C  
ANISOU 1621  C   ASN A 670     2937   1907   3896    399   -814   -707       C  
ATOM   1622  O   ASN A 670      30.787   0.767   3.661  1.00 23.98           O  
ANISOU 1622  O   ASN A 670     3094   1927   4091    400   -867   -753       O  
ATOM   1623  CB  ASN A 670      28.855   2.073   5.217  1.00 21.78           C  
ANISOU 1623  CB  ASN A 670     2939   1767   3570    238   -833   -449       C  
ATOM   1624  CG  ASN A 670      28.116   2.719   6.351  1.00 21.45           C  
ANISOU 1624  CG  ASN A 670     2956   1767   3427    168   -830   -296       C  
ATOM   1625  OD1 ASN A 670      28.726   3.081   7.366  1.00 22.51           O  
ANISOU 1625  OD1 ASN A 670     3104   1883   3564    193   -876   -235       O  
ATOM   1626  ND2 ASN A 670      26.815   2.942   6.171  1.00 21.99           N  
ANISOU 1626  ND2 ASN A 670     3050   1901   3404     81   -773   -243       N  
ATOM   1627  N   GLY A 671      32.212   2.502   3.656  1.00 23.40           N  
ANISOU 1627  N   GLY A 671     2891   2016   3985    462   -763   -804       N  
ATOM   1628  CA  GLY A 671      33.195   1.880   2.826  1.00 25.39           C  
ANISOU 1628  CA  GLY A 671     3059   2226   4363    537   -756   -981       C  
ATOM   1629  C   GLY A 671      32.975   1.872   1.345  1.00 25.82           C  
ANISOU 1629  C   GLY A 671     3080   2364   4365    510   -638  -1110       C  
ATOM   1630  O   GLY A 671      33.823   1.341   0.645  1.00 26.84           O  
ANISOU 1630  O   GLY A 671     3135   2464   4599    570   -619  -1276       O  
ATOM   1631  N   LYS A 672      31.871   2.428   0.857  1.00 25.58           N  
ANISOU 1631  N   LYS A 672     3102   2436   4181    423   -564  -1047       N  
ATOM   1632  CA  LYS A 672      31.573   2.470  -0.575  1.00 27.06           C  
ANISOU 1632  CA  LYS A 672     3277   2712   4292    386   -463  -1157       C  
ATOM   1633  C   LYS A 672      31.804   3.870  -1.067  1.00 24.98           C  
ANISOU 1633  C   LYS A 672     2979   2609   3905    353   -340  -1150       C  
ATOM   1634  O   LYS A 672      31.152   4.814  -0.583  1.00 23.04           O  
ANISOU 1634  O   LYS A 672     2770   2427   3555    307   -328  -1013       O  
ATOM   1635  CB  LYS A 672      30.120   2.069  -0.860  1.00 29.30           C  
ANISOU 1635  CB  LYS A 672     3647   2991   4493    308   -485  -1092       C  
ATOM   1636  CG  LYS A 672      29.828   0.665  -0.379  1.00 34.41           C  
ANISOU 1636  CG  LYS A 672     4343   3471   5262    323   -605  -1090       C  
ATOM   1637  CD  LYS A 672      28.551   0.045  -0.932  1.00 37.77           C  
ANISOU 1637  CD  LYS A 672     4833   3884   5636    248   -619  -1081       C  
ATOM   1638  CE  LYS A 672      28.248  -1.317  -0.273  1.00 41.40           C  
ANISOU 1638  CE  LYS A 672     5352   4158   6220    249   -745  -1054       C  
ATOM   1639  NZ  LYS A 672      29.460  -2.167  -0.041  1.00 44.34           N  
ANISOU 1639  NZ  LYS A 672     5690   4389   6767    350   -817  -1153       N  
ATOM   1640  N   SER A 673      32.727   4.025  -2.001  1.00 25.50           N  
ANISOU 1640  N   SER A 673     2973   2734   3981    373   -247  -1300       N  
ATOM   1641  CA  SER A 673      33.058   5.367  -2.500  1.00 25.77           C  
ANISOU 1641  CA  SER A 673     2980   2914   3898    331   -125  -1295       C  
ATOM   1642  C   SER A 673      32.193   5.746  -3.715  1.00 24.67           C  
ANISOU 1642  C   SER A 673     2902   2881   3590    248    -47  -1301       C  
ATOM   1643  O   SER A 673      31.891   4.900  -4.571  1.00 24.95           O  
ANISOU 1643  O   SER A 673     2960   2902   3619    235    -43  -1400       O  
ATOM   1644  CB  SER A 673      34.502   5.454  -2.862  1.00 28.01           C  
ANISOU 1644  CB  SER A 673     3154   3221   4266    376    -51  -1448       C  
ATOM   1645  OG  SER A 673      35.273   5.431  -1.688  1.00 29.22           O  
ANISOU 1645  OG  SER A 673     3250   3297   4554    447   -129  -1417       O  
ATOM   1646  N   SER A 674      31.806   7.002  -3.796  1.00 23.18           N  
ANISOU 1646  N   SER A 674     2746   2794   3270    194      6  -1197       N  
ATOM   1647  CA ASER A 674      30.995   7.511  -4.897  0.50 23.18           C  
ANISOU 1647  CA ASER A 674     2811   2893   3102    117     62  -1181       C  
ATOM   1648  CA BSER A 674      31.104   7.473  -4.992  0.50 22.71           C  
ANISOU 1648  CA BSER A 674     2747   2837   3046    118     71  -1199       C  
ATOM   1649  C   SER A 674      31.412   8.921  -5.256  1.00 22.51           C  
ANISOU 1649  C   SER A 674     2726   2919   2909     73    160  -1144       C  
ATOM   1650  O   SER A 674      32.225   9.536  -4.534  1.00 21.42           O  
ANISOU 1650  O   SER A 674     2532   2778   2830    101    182  -1120       O  
ATOM   1651  CB ASER A 674      29.548   7.498  -4.497  0.50 22.74           C  
ANISOU 1651  CB ASER A 674     2825   2817   2997     88    -24  -1046       C  
ATOM   1652  CB BSER A 674      29.604   7.218  -4.928  0.50 21.83           C  
ANISOU 1652  CB BSER A 674     2712   2708   2875     82    -11  -1098       C  
ATOM   1653  OG ASER A 674      29.037   6.214  -4.577  0.50 24.28           O  
ANISOU 1653  OG ASER A 674     3039   2931   3256     97    -95  -1095       O  
ATOM   1654  OG BSER A 674      29.039   7.348  -6.236  0.50 21.57           O  
ANISOU 1654  OG BSER A 674     2733   2758   2703     19     30  -1139       O  
ATOM   1655  N   THR A 675      30.854   9.426  -6.365  1.00 22.42           N  
ANISOU 1655  N   THR A 675     2781   2998   2739      2    211  -1137       N  
ATOM   1656  CA  THR A 675      31.107  10.789  -6.764  1.00 23.08           C  
ANISOU 1656  CA  THR A 675     2889   3175   2704    -53    293  -1081       C  
ATOM   1657  C   THR A 675      29.818  11.530  -7.041  1.00 21.79           C  
ANISOU 1657  C   THR A 675     2818   3053   2408   -101    246   -945       C  
ATOM   1658  O   THR A 675      28.764  10.938  -7.250  1.00 22.45           O  
ANISOU 1658  O   THR A 675     2942   3118   2468   -107    169   -925       O  
ATOM   1659  CB  THR A 675      32.029  10.895  -7.993  1.00 25.03           C  
ANISOU 1659  CB  THR A 675     3130   3507   2875   -106    425  -1219       C  
ATOM   1660  OG1 THR A 675      31.417  10.254  -9.103  1.00 27.20           O  
ANISOU 1660  OG1 THR A 675     3470   3814   3049   -149    424  -1287       O  
ATOM   1661  CG2 THR A 675      33.348  10.263  -7.723  1.00 26.24           C  
ANISOU 1661  CG2 THR A 675     3170   3625   3177    -52    477  -1367       C  
ATOM   1662  N   ILE A 676      29.941  12.843  -7.057  1.00 21.02           N  
ANISOU 1662  N   ILE A 676     2746   3008   2234   -135    288   -858       N  
ATOM   1663  CA  ILE A 676      28.823  13.752  -7.320  1.00 20.62           C  
ANISOU 1663  CA  ILE A 676     2777   2991   2068   -174    240   -725       C  
ATOM   1664  C   ILE A 676      29.335  14.809  -8.301  1.00 21.49           C  
ANISOU 1664  C   ILE A 676     2945   3182   2037   -249    332   -718       C  
ATOM   1665  O   ILE A 676      30.314  15.511  -7.999  1.00 21.48           O  
ANISOU 1665  O   ILE A 676     2908   3191   2061   -258    410   -720       O  
ATOM   1666  CB  ILE A 676      28.350  14.475  -6.028  1.00 19.05           C  
ANISOU 1666  CB  ILE A 676     2555   2745   1937   -132    180   -593       C  
ATOM   1667  CG1 ILE A 676      27.950  13.459  -4.937  1.00 18.36           C  
ANISOU 1667  CG1 ILE A 676     2417   2577   1981    -73    101   -593       C  
ATOM   1668  CG2 ILE A 676      27.191  15.474  -6.331  1.00 18.45           C  
ANISOU 1668  CG2 ILE A 676     2551   2699   1760   -161    126   -468       C  
ATOM   1669  CD1 ILE A 676      27.723  14.082  -3.579  1.00 17.65           C  
ANISOU 1669  CD1 ILE A 676     2300   2447   1958    -38     63   -489       C  
ATOM   1670  N   PRO A 677      28.621  15.013  -9.418  1.00 22.36           N  
ANISOU 1670  N   PRO A 677     3154   3348   1996   -309    314   -694       N  
ATOM   1671  CA  PRO A 677      28.973  16.152 -10.273  1.00 23.08           C  
ANISOU 1671  CA  PRO A 677     3326   3505   1937   -391    384   -650       C  
ATOM   1672  C   PRO A 677      28.787  17.465  -9.595  1.00 21.91           C  
ANISOU 1672  C   PRO A 677     3192   3331   1802   -383    357   -507       C  
ATOM   1673  O   PRO A 677      27.788  17.693  -8.969  1.00 22.16           O  
ANISOU 1673  O   PRO A 677     3223   3319   1878   -336    253   -410       O  
ATOM   1674  CB  PRO A 677      28.002  15.983 -11.487  1.00 24.48           C  
ANISOU 1674  CB  PRO A 677     3617   3732   1953   -447    324   -636       C  
ATOM   1675  CG  PRO A 677      27.589  14.534 -11.438  1.00 24.64           C  
ANISOU 1675  CG  PRO A 677     3591   3724   2048   -404    273   -737       C  
ATOM   1676  CD  PRO A 677      27.510  14.211  -9.991  1.00 22.98           C  
ANISOU 1676  CD  PRO A 677     3278   3428   2025   -315    224   -708       C  
ATOM   1677  N   SER A 678      29.815  18.317  -9.628  1.00 22.46           N  
ANISOU 1677  N   SER A 678     3260   3423   1853   -427    460   -505       N  
ATOM   1678  CA  SER A 678      29.831  19.516  -8.842  1.00 21.54           C  
ANISOU 1678  CA  SER A 678     3140   3266   1777   -414    444   -390       C  
ATOM   1679  C   SER A 678      28.988  20.652  -9.426  1.00 22.31           C  
ANISOU 1679  C   SER A 678     3360   3369   1749   -459    384   -251       C  
ATOM   1680  O   SER A 678      28.594  21.519  -8.693  1.00 21.11           O  
ANISOU 1680  O   SER A 678     3205   3166   1650   -424    329   -150       O  
ATOM   1681  CB  SER A 678      31.256  20.033  -8.702  1.00 21.43           C  
ANISOU 1681  CB  SER A 678     3078   3270   1793   -455    574   -443       C  
ATOM   1682  OG  SER A 678      31.745  20.447  -9.933  1.00 22.41           O  
ANISOU 1682  OG  SER A 678     3285   3464   1765   -564    671   -466       O  
ATOM   1683  N   CYS A 679      28.827  20.686 -10.744  1.00 24.72           N  
ANISOU 1683  N   CYS A 679     3775   3732   1886   -539    398   -254       N  
ATOM   1684  CA  CYS A 679      28.306  21.893 -11.444  1.00 27.12           C  
ANISOU 1684  CA  CYS A 679     4216   4037   2052   -601    349   -119       C  
ATOM   1685  C   CYS A 679      29.054  23.118 -11.057  1.00 26.75           C  
ANISOU 1685  C   CYS A 679     4178   3961   2024   -636    416    -54       C  
ATOM   1686  O   CYS A 679      28.469  24.200 -10.944  1.00 27.74           O  
ANISOU 1686  O   CYS A 679     4371   4036   2133   -632    338     79       O  
ATOM   1687  CB  CYS A 679      26.808  22.109 -11.144  1.00 28.50           C  
ANISOU 1687  CB  CYS A 679     4411   4161   2257   -530    178    -11       C  
ATOM   1688  SG  CYS A 679      25.816  20.764 -11.790  1.00 32.74           S  
ANISOU 1688  SG  CYS A 679     4955   4736   2750   -512     87    -79       S  
ATOM   1689  N   GLY A 680      30.360  22.961 -10.803  1.00 25.44           N  
ANISOU 1689  N   GLY A 680     3934   3819   1911   -665    556   -152       N  
ATOM   1690  CA  GLY A 680      31.223  24.083 -10.465  1.00 24.84           C  
ANISOU 1690  CA  GLY A 680     3858   3722   1859   -714    635   -109       C  
ATOM   1691  C   GLY A 680      31.133  24.648  -9.074  1.00 22.76           C  
ANISOU 1691  C   GLY A 680     3512   3377   1757   -629    582    -54       C  
ATOM   1692  O   GLY A 680      31.720  25.684  -8.814  1.00 22.20           O  
ANISOU 1692  O   GLY A 680     3454   3279   1703   -672    631     -7       O  
ATOM   1693  N   LEU A 681      30.416  23.974  -8.176  1.00 21.69           N  
ANISOU 1693  N   LEU A 681     3298   3206   1738   -519    488    -63       N  
ATOM   1694  CA  LEU A 681      30.248  24.421  -6.812  1.00 20.88           C  
ANISOU 1694  CA  LEU A 681     3123   3035   1777   -440    438    -20       C  
ATOM   1695  C   LEU A 681      30.539  23.317  -5.775  1.00 19.07           C  
ANISOU 1695  C   LEU A 681     2762   2796   1686   -360    435   -115       C  
ATOM   1696  O   LEU A 681      30.196  22.142  -5.975  1.00 18.23           O  
ANISOU 1696  O   LEU A 681     2632   2710   1586   -329    407   -177       O  
ATOM   1697  CB  LEU A 681      28.818  24.930  -6.551  1.00 22.43           C  
ANISOU 1697  CB  LEU A 681     3366   3179   1977   -384    302     95       C  
ATOM   1698  CG  LEU A 681      28.378  26.235  -7.213  1.00 25.51           C  
ANISOU 1698  CG  LEU A 681     3881   3539   2275   -432    260    217       C  
ATOM   1699  CD1 LEU A 681      26.930  26.438  -6.786  1.00 26.32           C  
ANISOU 1699  CD1 LEU A 681     3982   3590   2427   -347    117    292       C  
ATOM   1700  CD2 LEU A 681      29.230  27.440  -6.813  1.00 26.18           C  
ANISOU 1700  CD2 LEU A 681     3976   3580   2391   -474    325    256       C  
ATOM   1701  N   GLN A 682      31.160  23.745  -4.675  1.00 18.33           N  
ANISOU 1701  N   GLN A 682     2596   2666   1703   -330    454   -119       N  
ATOM   1702  CA AGLN A 682      31.384  22.895  -3.516  0.50 17.88           C  
ANISOU 1702  CA AGLN A 682     2433   2585   1778   -253    427   -181       C  
ATOM   1703  CA BGLN A 682      31.356  22.901  -3.520  0.50 18.18           C  
ANISOU 1703  CA BGLN A 682     2472   2622   1814   -253    425   -179       C  
ATOM   1704  C   GLN A 682      30.530  23.466  -2.398  1.00 16.50           C  
ANISOU 1704  C   GLN A 682     2255   2354   1662   -194    342    -94       C  
ATOM   1705  O   GLN A 682      30.698  24.628  -2.045  1.00 16.18           O  
ANISOU 1705  O   GLN A 682     2231   2284   1631   -210    353    -40       O  
ATOM   1706  CB AGLN A 682      32.865  22.927  -3.130  0.50 19.22           C  
ANISOU 1706  CB AGLN A 682     2518   2763   2023   -271    513   -268       C  
ATOM   1707  CB BGLN A 682      32.803  22.931  -3.118  0.50 20.03           C  
ANISOU 1707  CB BGLN A 682     2623   2864   2124   -269    509   -263       C  
ATOM   1708  CG AGLN A 682      33.205  21.979  -2.009  0.50 20.03           C  
ANISOU 1708  CG AGLN A 682     2519   2835   2255   -192    471   -332       C  
ATOM   1709  CG BGLN A 682      33.062  22.120  -1.892  0.50 21.28           C  
ANISOU 1709  CG BGLN A 682     2685   2988   2413   -189    460   -313       C  
ATOM   1710  CD AGLN A 682      34.663  22.045  -1.639  0.50 21.65           C  
ANISOU 1710  CD AGLN A 682     2631   3048   2548   -203    538   -422       C  
ATOM   1711  CD BGLN A 682      34.483  21.737  -1.871  0.50 23.71           C  
ANISOU 1711  CD BGLN A 682     2901   3316   2794   -200    533   -430       C  
ATOM   1712  OE1AGLN A 682      35.547  22.299  -2.507  0.50 23.35           O  
ANISOU 1712  OE1AGLN A 682     2833   3310   2727   -274    643   -485       O  
ATOM   1713  OE1BGLN A 682      34.843  20.654  -2.341  0.50 25.91           O  
ANISOU 1713  OE1BGLN A 682     3138   3615   3092   -187    554   -529       O  
ATOM   1714  NE2AGLN A 682      34.953  21.773  -0.365  0.50 21.19           N  
ANISOU 1714  NE2AGLN A 682     2502   2947   2602   -139    477   -435       N  
ATOM   1715  NE2BGLN A 682      35.346  22.694  -1.463  0.50 24.28           N  
ANISOU 1715  NE2BGLN A 682     2938   3384   2905   -232    581   -431       N  
ATOM   1716  N   VAL A 683      29.669  22.638  -1.827  1.00 15.15           N  
ANISOU 1716  N   VAL A 683     2057   2165   1533   -133    267    -92       N  
ATOM   1717  CA  VAL A 683      28.831  22.991  -0.732  1.00 14.59           C  
ANISOU 1717  CA  VAL A 683     1972   2053   1519    -83    200    -32       C  
ATOM   1718  C   VAL A 683      29.509  22.649   0.599  1.00 14.46           C  
ANISOU 1718  C   VAL A 683     1881   2011   1602    -45    202    -72       C  
ATOM   1719  O   VAL A 683      30.098  21.575   0.716  1.00 15.10           O  
ANISOU 1719  O   VAL A 683     1917   2097   1722    -31    207   -143       O  
ATOM   1720  CB  VAL A 683      27.488  22.202  -0.824  1.00 15.10           C  
ANISOU 1720  CB  VAL A 683     2045   2118   1573    -51    124    -11       C  
ATOM   1721  CG1 VAL A 683      26.618  22.486   0.420  1.00 15.11           C  
ANISOU 1721  CG1 VAL A 683     2017   2086   1640     -5     72     34       C  
ATOM   1722  CG2 VAL A 683      26.836  22.537  -2.153  1.00 16.25           C  
ANISOU 1722  CG2 VAL A 683     2266   2290   1618    -86    103     28       C  
ATOM   1723  N   SER A 684      29.453  23.574   1.563  1.00 13.37           N  
ANISOU 1723  N   SER A 684     1735   1842   1502    -30    191    -32       N  
ATOM   1724  CA  SER A 684      29.862  23.348   2.958  1.00 13.70           C  
ANISOU 1724  CA  SER A 684     1724   1860   1621      3    172    -55       C  
ATOM   1725  C   SER A 684      28.722  23.618   3.913  1.00 13.54           C  
ANISOU 1725  C   SER A 684     1713   1818   1615     35    122     -3       C  
ATOM   1726  O   SER A 684      28.066  24.669   3.859  1.00 15.16           O  
ANISOU 1726  O   SER A 684     1946   2010   1805     35    118     46       O  
ATOM   1727  CB  SER A 684      31.011  24.217   3.353  1.00 13.91           C  
ANISOU 1727  CB  SER A 684     1726   1876   1682    -18    215    -76       C  
ATOM   1728  OG  SER A 684      32.124  23.984   2.515  1.00 15.24           O  
ANISOU 1728  OG  SER A 684     1871   2072   1848    -54    276   -139       O  
ATOM   1729  N   ILE A 685      28.506  22.714   4.842  1.00 11.95           N  
ANISOU 1729  N   ILE A 685     1486   1607   1446     60     84    -16       N  
ATOM   1730  CA  ILE A 685      27.576  22.914   5.911  1.00 11.95           C  
ANISOU 1730  CA  ILE A 685     1488   1596   1458     77     56     17       C  
ATOM   1731  C   ILE A 685      28.276  23.598   7.103  1.00 11.89           C  
ANISOU 1731  C   ILE A 685     1467   1571   1479     80     63      6       C  
ATOM   1732  O   ILE A 685      29.377  23.200   7.497  1.00 11.91           O  
ANISOU 1732  O   ILE A 685     1448   1566   1510     80     56    -31       O  
ATOM   1733  CB  ILE A 685      26.967  21.559   6.327  1.00 12.35           C  
ANISOU 1733  CB  ILE A 685     1533   1645   1514     84     16     15       C  
ATOM   1734  CG1 ILE A 685      26.085  21.000   5.207  1.00 13.27           C  
ANISOU 1734  CG1 ILE A 685     1661   1779   1602     78      2     23       C  
ATOM   1735  CG2 ILE A 685      26.211  21.671   7.635  1.00 12.57           C  
ANISOU 1735  CG2 ILE A 685     1562   1668   1547     85      2     38       C  
ATOM   1736  CD1 ILE A 685      25.776  19.518   5.361  1.00 14.26           C  
ANISOU 1736  CD1 ILE A 685     1784   1894   1742     74    -33      7       C  
ATOM   1737  N   ILE A 686      27.602  24.555   7.721  1.00 11.54           N  
ANISOU 1737  N   ILE A 686     1432   1518   1435     86     68     30       N  
ATOM   1738  CA  ILE A 686      28.092  25.187   8.928  1.00 11.96           C  
ANISOU 1738  CA  ILE A 686     1479   1557   1507     85     71     14       C  
ATOM   1739  C   ILE A 686      27.072  25.188  10.072  1.00 12.77           C  
ANISOU 1739  C   ILE A 686     1586   1665   1598     91     62     22       C  
ATOM   1740  O   ILE A 686      25.885  24.862   9.870  1.00 11.85           O  
ANISOU 1740  O   ILE A 686     1467   1563   1472     96     60     41       O  
ATOM   1741  CB  ILE A 686      28.513  26.674   8.630  1.00 12.26           C  
ANISOU 1741  CB  ILE A 686     1526   1573   1561     76    103     15       C  
ATOM   1742  CG1 ILE A 686      27.309  27.497   8.152  1.00 12.62           C  
ANISOU 1742  CG1 ILE A 686     1590   1603   1602     91    106     52       C  
ATOM   1743  CG2 ILE A 686      29.652  26.742   7.618  1.00 11.97           C  
ANISOU 1743  CG2 ILE A 686     1484   1537   1528     50    131      0       C  
ATOM   1744  CD1 ILE A 686      27.545  28.993   8.186  1.00 13.47           C  
ANISOU 1744  CD1 ILE A 686     1715   1667   1736     87    124     56       C  
ATOM   1745  N   ASP A 687      27.551  25.625  11.265  1.00 12.64           N  
ANISOU 1745  N   ASP A 687     1576   1644   1585     83     61     -1       N  
ATOM   1746  CA  ASP A 687      26.723  26.078  12.417  1.00 14.17           C  
ANISOU 1746  CA  ASP A 687     1778   1846   1761     79     76    -10       C  
ATOM   1747  C   ASP A 687      26.070  24.959  13.185  1.00 13.87           C  
ANISOU 1747  C   ASP A 687     1755   1833   1683     58     62      1       C  
ATOM   1748  O   ASP A 687      24.996  24.460  12.799  1.00 14.44           O  
ANISOU 1748  O   ASP A 687     1814   1921   1751     56     72     19       O  
ATOM   1749  CB  ASP A 687      25.695  27.106  12.049  1.00 15.51           C  
ANISOU 1749  CB  ASP A 687     1932   2007   1954     99    107    -10       C  
ATOM   1750  CG  ASP A 687      25.183  27.825  13.265  1.00 18.78           C  
ANISOU 1750  CG  ASP A 687     2345   2425   2364     96    135    -48       C  
ATOM   1751  OD1 ASP A 687      24.923  27.154  14.287  1.00 19.08           O  
ANISOU 1751  OD1 ASP A 687     2396   2495   2357     68    139    -59       O  
ATOM   1752  OD2 ASP A 687      25.120  29.068  13.242  1.00 23.13           O  
ANISOU 1752  OD2 ASP A 687     2891   2946   2953    115    152    -70       O  
ATOM   1753  N   TYR A 688      26.734  24.558  14.265  1.00 13.86           N  
ANISOU 1753  N   TYR A 688     1784   1833   1651     36     33     -7       N  
ATOM   1754  CA  TYR A 688      26.320  23.350  14.980  1.00 14.14           C  
ANISOU 1754  CA  TYR A 688     1855   1880   1639      3      8     19       C  
ATOM   1755  C   TYR A 688      25.761  23.619  16.338  1.00 14.65           C  
ANISOU 1755  C   TYR A 688     1954   1972   1642    -37     35      7       C  
ATOM   1756  O   TYR A 688      25.709  22.709  17.174  1.00 14.99           O  
ANISOU 1756  O   TYR A 688     2049   2020   1626    -80      6     32       O  
ATOM   1757  CB  TYR A 688      27.482  22.397  15.034  1.00 14.07           C  
ANISOU 1757  CB  TYR A 688     1865   1842   1637      8    -65     30       C  
ATOM   1758  CG  TYR A 688      28.175  22.237  13.697  1.00 13.69           C  
ANISOU 1758  CG  TYR A 688     1775   1774   1652     44    -75     19       C  
ATOM   1759  CD1 TYR A 688      27.490  21.749  12.597  1.00 13.17           C  
ANISOU 1759  CD1 TYR A 688     1691   1712   1599     52    -57     33       C  
ATOM   1760  CD2 TYR A 688      29.487  22.583  13.526  1.00 13.62           C  
ANISOU 1760  CD2 TYR A 688     1741   1749   1684     63    -97    -13       C  
ATOM   1761  CE1 TYR A 688      28.090  21.632  11.355  1.00 13.53           C  
ANISOU 1761  CE1 TYR A 688     1708   1750   1684     75    -55     16       C  
ATOM   1762  CE2 TYR A 688      30.131  22.446  12.289  1.00 13.47           C  
ANISOU 1762  CE2 TYR A 688     1680   1723   1715     84    -87    -34       C  
ATOM   1763  CZ  TYR A 688      29.401  21.963  11.189  1.00 13.90           C  
ANISOU 1763  CZ  TYR A 688     1730   1785   1767     88    -63    -19       C  
ATOM   1764  OH  TYR A 688      30.041  21.753   9.999  1.00 15.62           O  
ANISOU 1764  OH  TYR A 688     1916   2001   2016     99    -47    -47       O  
ATOM   1765  N   THR A 689      25.226  24.827  16.580  1.00 15.55           N  
ANISOU 1765  N   THR A 689     2043   2102   1763    -30     94    -34       N  
ATOM   1766  CA  THR A 689      24.608  25.141  17.877  1.00 16.16           C  
ANISOU 1766  CA  THR A 689     2148   2215   1777    -73    138    -66       C  
ATOM   1767  C   THR A 689      23.466  24.230  18.294  1.00 16.59           C  
ANISOU 1767  C   THR A 689     2216   2307   1782   -125    173    -46       C  
ATOM   1768  O   THR A 689      23.268  23.961  19.491  1.00 18.07           O  
ANISOU 1768  O   THR A 689     2458   2525   1882   -188    193    -52       O  
ATOM   1769  CB  THR A 689      24.158  26.622  17.928  1.00 17.51           C  
ANISOU 1769  CB  THR A 689     2278   2388   1989    -45    198   -128       C  
ATOM   1770  OG1 THR A 689      25.315  27.458  17.753  1.00 17.34           O  
ANISOU 1770  OG1 THR A 689     2260   2328   2003    -17    167   -145       O  
ATOM   1771  CG2 THR A 689      23.556  26.962  19.221  1.00 18.45           C  
ANISOU 1771  CG2 THR A 689     2418   2547   2044    -89    256   -181       C  
ATOM   1772  N   LEU A 690      22.664  23.791  17.333  1.00 14.93           N  
ANISOU 1772  N   LEU A 690     1957   2097   1619   -110    185    -27       N  
ATOM   1773  CA  LEU A 690      21.557  22.904  17.690  1.00 16.29           C  
ANISOU 1773  CA  LEU A 690     2132   2304   1754   -170    223    -13       C  
ATOM   1774  C   LEU A 690      21.840  21.420  17.420  1.00 15.03           C  
ANISOU 1774  C   LEU A 690     2019   2117   1575   -200    160     54       C  
ATOM   1775  O   LEU A 690      20.970  20.566  17.704  1.00 15.73           O  
ANISOU 1775  O   LEU A 690     2119   2224   1632   -263    186     74       O  
ATOM   1776  CB  LEU A 690      20.324  23.272  16.914  1.00 17.13           C  
ANISOU 1776  CB  LEU A 690     2148   2429   1930   -144    271    -42       C  
ATOM   1777  CG  LEU A 690      19.339  24.263  17.396  1.00 19.82           C  
ANISOU 1777  CG  LEU A 690     2429   2809   2294   -142    352   -114       C  
ATOM   1778  CD1 LEU A 690      18.012  24.035  16.639  1.00 19.64           C  
ANISOU 1778  CD1 LEU A 690     2316   2806   2340   -133    377   -128       C  
ATOM   1779  CD2 LEU A 690      19.107  24.246  18.923  1.00 21.27           C  
ANISOU 1779  CD2 LEU A 690     2657   3041   2384   -221    421   -151       C  
ATOM   1780  N   SER A 691      23.050  21.083  16.961  1.00 13.20           N  
ANISOU 1780  N   SER A 691     1813   1838   1364   -162     81     80       N  
ATOM   1781  CA  SER A 691      23.347  19.746  16.440  1.00 12.97           C  
ANISOU 1781  CA  SER A 691     1811   1768   1350   -167     15    127       C  
ATOM   1782  C   SER A 691      23.556  18.703  17.554  1.00 13.73           C  
ANISOU 1782  C   SER A 691     2002   1845   1372   -234    -30    175       C  
ATOM   1783  O   SER A 691      23.719  19.015  18.737  1.00 14.07           O  
ANISOU 1783  O   SER A 691     2100   1907   1339   -275    -23    176       O  
ATOM   1784  CB  SER A 691      24.548  19.767  15.505  1.00 12.20           C  
ANISOU 1784  CB  SER A 691     1693   1629   1312   -100    -44    121       C  
ATOM   1785  OG  SER A 691      24.436  20.734  14.475  1.00 12.74           O  
ANISOU 1785  OG  SER A 691     1697   1710   1433    -52     -7     90       O  
ATOM   1786  N   ARG A 692      23.528  17.453  17.132  1.00 13.83           N  
ANISOU 1786  N   ARG A 692     2038   1812   1403   -247    -82    216       N  
ATOM   1787  CA  ARG A 692      23.596  16.288  18.004  1.00 14.61           C  
ANISOU 1787  CA  ARG A 692     2236   1871   1443   -315   -138    277       C  
ATOM   1788  C   ARG A 692      24.413  15.230  17.306  1.00 14.46           C  
ANISOU 1788  C   ARG A 692     2230   1771   1492   -270   -239    300       C  
ATOM   1789  O   ARG A 692      24.262  15.022  16.095  1.00 13.81           O  
ANISOU 1789  O   ARG A 692     2084   1678   1484   -228   -232    274       O  
ATOM   1790  CB  ARG A 692      22.186  15.791  18.290  1.00 16.05           C  
ANISOU 1790  CB  ARG A 692     2430   2086   1584   -406    -65    297       C  
ATOM   1791  CG  ARG A 692      22.073  14.492  19.035  1.00 17.11           C  
ANISOU 1791  CG  ARG A 692     2673   2170   1657   -494   -115    372       C  
ATOM   1792  CD  ARG A 692      21.846  13.257  18.156  1.00 16.89           C  
ANISOU 1792  CD  ARG A 692     2644   2076   1699   -496   -165    400       C  
ATOM   1793  NE  ARG A 692      21.560  12.151  19.077  1.00 18.43           N  
ANISOU 1793  NE  ARG A 692     2957   2223   1821   -603   -197    479       N  
ATOM   1794  CZ  ARG A 692      22.182  10.990  19.184  1.00 18.21           C  
ANISOU 1794  CZ  ARG A 692     3019   2091   1808   -609   -314    541       C  
ATOM   1795  NH1 ARG A 692      23.094  10.602  18.287  1.00 17.85           N  
ANISOU 1795  NH1 ARG A 692     2942   1975   1868   -508   -406    520       N  
ATOM   1796  NH2 ARG A 692      21.833  10.177  20.177  1.00 19.26           N  
ANISOU 1796  NH2 ARG A 692     3277   2187   1852   -724   -334    622       N  
ATOM   1797  N   LEU A 693      25.309  14.585  18.064  1.00 14.77           N  
ANISOU 1797  N   LEU A 693     2352   1750   1508   -277   -341    342       N  
ATOM   1798  CA  LEU A 693      25.997  13.412  17.569  1.00 15.46           C  
ANISOU 1798  CA  LEU A 693     2460   1746   1669   -239   -446    361       C  
ATOM   1799  C   LEU A 693      26.434  12.576  18.751  1.00 17.48           C  
ANISOU 1799  C   LEU A 693     2840   1935   1868   -285   -553    435       C  
ATOM   1800  O   LEU A 693      26.165  12.943  19.904  1.00 17.98           O  
ANISOU 1800  O   LEU A 693     2976   2036   1820   -355   -534    469       O  
ATOM   1801  CB  LEU A 693      27.163  13.766  16.664  1.00 15.02           C  
ANISOU 1801  CB  LEU A 693     2322   1672   1712   -136   -483    298       C  
ATOM   1802  CG  LEU A 693      28.220  14.723  17.192  1.00 15.50           C  
ANISOU 1802  CG  LEU A 693     2366   1755   1768    -96   -509    268       C  
ATOM   1803  CD1 LEU A 693      29.020  14.210  18.341  1.00 17.15           C  
ANISOU 1803  CD1 LEU A 693     2662   1909   1947   -107   -632    312       C  
ATOM   1804  CD2 LEU A 693      29.137  15.059  15.999  1.00 15.71           C  
ANISOU 1804  CD2 LEU A 693     2291   1778   1902    -11   -507    195       C  
ATOM   1805  N   GLU A 694      27.078  11.457  18.472  1.00 18.77           N  
ANISOU 1805  N   GLU A 694     3032   1995   2104   -249   -668    456       N  
ATOM   1806  CA  GLU A 694      27.599  10.585  19.543  1.00 21.53           C  
ANISOU 1806  CA  GLU A 694     3511   2258   2414   -281   -804    536       C  
ATOM   1807  C   GLU A 694      28.828   9.809  19.113  1.00 22.25           C  
ANISOU 1807  C   GLU A 694     3583   2238   2632   -184   -950    517       C  
ATOM   1808  O   GLU A 694      28.993   9.495  17.942  1.00 21.81           O  
ANISOU 1808  O   GLU A 694     3440   2158   2689   -119   -937    455       O  
ATOM   1809  CB  GLU A 694      26.513   9.665  20.065  1.00 24.64           C  
ANISOU 1809  CB  GLU A 694     4014   2620   2729   -399   -790    622       C  
ATOM   1810  CG  GLU A 694      26.208   8.503  19.154  1.00 26.53           C  
ANISOU 1810  CG  GLU A 694     4242   2772   3065   -389   -820    625       C  
ATOM   1811  CD  GLU A 694      25.038   7.679  19.647  1.00 28.67           C  
ANISOU 1811  CD  GLU A 694     4614   3020   3260   -524   -787    706       C  
ATOM   1812  OE1 GLU A 694      25.286   6.690  20.360  1.00 30.40           O  
ANISOU 1812  OE1 GLU A 694     4965   3131   3453   -571   -903    794       O  
ATOM   1813  OE2 GLU A 694      23.874   8.005  19.295  1.00 28.97           O  
ANISOU 1813  OE2 GLU A 694     4596   3140   3271   -584   -651    681       O  
ATOM   1814  N   ARG A 695      29.701   9.489  20.067  1.00 24.02           N  
ANISOU 1814  N   ARG A 695     3890   2397   2840   -172  -1093    564       N  
ATOM   1815  CA  ARG A 695      30.825   8.578  19.810  1.00 26.29           C  
ANISOU 1815  CA  ARG A 695     4168   2560   3262    -80  -1256    551       C  
ATOM   1816  C   ARG A 695      30.919   7.657  21.010  1.00 27.20           C  
ANISOU 1816  C   ARG A 695     4453   2572   3311   -137  -1410    669       C  
ATOM   1817  O   ARG A 695      30.890   8.135  22.139  1.00 26.05           O  
ANISOU 1817  O   ARG A 695     4399   2469   3032   -201  -1429    726       O  
ATOM   1818  CB  ARG A 695      32.160   9.290  19.688  1.00 29.43           C  
ANISOU 1818  CB  ARG A 695     4463   2976   3744     23  -1311    468       C  
ATOM   1819  CG  ARG A 695      32.299  10.016  18.376  1.00 32.18           C  
ANISOU 1819  CG  ARG A 695     4651   3398   4179     85  -1183    352       C  
ATOM   1820  CD  ARG A 695      33.671  10.629  18.260  1.00 36.03           C  
ANISOU 1820  CD  ARG A 695     5034   3896   4758    174  -1236    268       C  
ATOM   1821  NE  ARG A 695      34.679   9.677  17.845  1.00 42.05           N  
ANISOU 1821  NE  ARG A 695     5746   4551   5679    267  -1364    219       N  
ATOM   1822  CZ  ARG A 695      35.988   9.884  17.928  1.00 48.43           C  
ANISOU 1822  CZ  ARG A 695     6470   5340   6593    348  -1456    150       C  
ATOM   1823  NH1 ARG A 695      36.819   8.938  17.507  1.00 54.09           N  
ANISOU 1823  NH1 ARG A 695     7130   5953   7470    438  -1568     93       N  
ATOM   1824  NH2 ARG A 695      36.495  10.999  18.486  1.00 52.15           N  
ANISOU 1824  NH2 ARG A 695     6909   5886   7021    341  -1445    130       N  
ATOM   1825  N   ASP A 696      30.967   6.369  20.744  1.00 28.26           N  
ANISOU 1825  N   ASP A 696     4636   2571   3529   -121  -1513    704       N  
ATOM   1826  CA  ASP A 696      31.016   5.341  21.807  1.00 31.78           C  
ANISOU 1826  CA  ASP A 696     5264   2892   3920   -180  -1677    833       C  
ATOM   1827  C   ASP A 696      29.945   5.556  22.912  1.00 32.18           C  
ANISOU 1827  C   ASP A 696     5465   3008   3754   -346  -1601    943       C  
ATOM   1828  O   ASP A 696      30.191   5.451  24.091  1.00 32.87           O  
ANISOU 1828  O   ASP A 696     5695   3066   3728   -403  -1706   1034       O  
ATOM   1829  CB  ASP A 696      32.421   5.301  22.374  1.00 33.86           C  
ANISOU 1829  CB  ASP A 696     5534   3082   4248    -85  -1874    830       C  
ATOM   1830  CG  ASP A 696      33.507   5.191  21.271  1.00 34.62           C  
ANISOU 1830  CG  ASP A 696     5455   3132   4566     77  -1924    696       C  
ATOM   1831  OD1 ASP A 696      33.492   4.247  20.432  1.00 38.80           O  
ANISOU 1831  OD1 ASP A 696     5950   3564   5230    126  -1951    661       O  
ATOM   1832  OD2 ASP A 696      34.399   6.026  21.260  1.00 34.98           O  
ANISOU 1832  OD2 ASP A 696     5396   3239   4655    149  -1935    618       O  
ATOM   1833  N   GLY A 697      28.740   5.926  22.476  1.00 31.68           N  
ANISOU 1833  N   GLY A 697     5359   3045   3633   -423  -1408    920       N  
ATOM   1834  CA  GLY A 697      27.622   6.115  23.386  1.00 31.08           C  
ANISOU 1834  CA  GLY A 697     5397   3043   3371   -584  -1304    998       C  
ATOM   1835  C   GLY A 697      27.559   7.387  24.172  1.00 30.45           C  
ANISOU 1835  C   GLY A 697     5315   3102   3153   -624  -1217    977       C  
ATOM   1836  O   GLY A 697      26.650   7.533  24.968  1.00 31.65           O  
ANISOU 1836  O   GLY A 697     5560   3319   3147   -761  -1124   1030       O  
ATOM   1837  N   ILE A 698      28.504   8.333  23.977  1.00 27.78           N  
ANISOU 1837  N   ILE A 698     4872   2813   2872   -513  -1239    893       N  
ATOM   1838  CA  ILE A 698      28.468   9.603  24.678  1.00 27.16           C  
ANISOU 1838  CA  ILE A 698     4786   2861   2674   -546  -1155    858       C  
ATOM   1839  C   ILE A 698      27.846  10.574  23.692  1.00 24.84           C  
ANISOU 1839  C   ILE A 698     4326   2675   2435   -512   -969    752       C  
ATOM   1840  O   ILE A 698      28.385  10.756  22.590  1.00 22.06           O  
ANISOU 1840  O   ILE A 698     3841   2310   2231   -398   -973    675       O  
ATOM   1841  CB  ILE A 698      29.884  10.101  25.075  1.00 27.88           C  
ANISOU 1841  CB  ILE A 698     4860   2934   2800   -453  -1296    827       C  
ATOM   1842  CG1 ILE A 698      30.637   9.050  25.894  1.00 30.99           C  
ANISOU 1842  CG1 ILE A 698     5404   3196   3175   -457  -1522    930       C  
ATOM   1843  CG2 ILE A 698      29.805  11.407  25.822  1.00 27.88           C  
ANISOU 1843  CG2 ILE A 698     4859   3059   2673   -495  -1210    785       C  
ATOM   1844  CD1 ILE A 698      29.923   8.567  27.134  1.00 32.10           C  
ANISOU 1844  CD1 ILE A 698     5756   3330   3112   -616  -1539   1057       C  
ATOM   1845  N   VAL A 699      26.713  11.151  24.077  1.00 24.04           N  
ANISOU 1845  N   VAL A 699     4237   2677   2219   -612   -812    746       N  
ATOM   1846  CA  VAL A 699      25.962  12.024  23.196  1.00 22.90           C  
ANISOU 1846  CA  VAL A 699     3947   2627   2126   -586   -647    656       C  
ATOM   1847  C   VAL A 699      26.200  13.494  23.519  1.00 22.01           C  
ANISOU 1847  C   VAL A 699     3776   2613   1975   -558   -576    580       C  
ATOM   1848  O   VAL A 699      26.152  13.908  24.693  1.00 23.82           O  
ANISOU 1848  O   VAL A 699     4094   2889   2068   -632   -565    598       O  
ATOM   1849  CB  VAL A 699      24.451  11.757  23.306  1.00 23.35           C  
ANISOU 1849  CB  VAL A 699     4024   2735   2113   -706   -510    678       C  
ATOM   1850  CG1 VAL A 699      23.703  12.557  22.271  1.00 22.11           C  
ANISOU 1850  CG1 VAL A 699     3709   2657   2036   -662   -371    586       C  
ATOM   1851  CG2 VAL A 699      24.193  10.269  23.149  1.00 24.53           C  
ANISOU 1851  CG2 VAL A 699     4255   2777   2287   -757   -584    762       C  
ATOM   1852  N   VAL A 700      26.448  14.281  22.482  1.00 19.79           N  
ANISOU 1852  N   VAL A 700     3352   2361   1806   -460   -527    496       N  
ATOM   1853  CA  VAL A 700      26.671  15.696  22.597  1.00 19.76           C  
ANISOU 1853  CA  VAL A 700     3281   2434   1794   -426   -460    420       C  
ATOM   1854  C   VAL A 700      25.537  16.358  21.846  1.00 18.58           C  
ANISOU 1854  C   VAL A 700     3030   2353   1677   -428   -306    365       C  
ATOM   1855  O   VAL A 700      25.269  16.023  20.718  1.00 17.60           O  
ANISOU 1855  O   VAL A 700     2832   2207   1647   -385   -290    354       O  
ATOM   1856  CB  VAL A 700      27.999  16.115  21.906  1.00 19.52           C  
ANISOU 1856  CB  VAL A 700     3165   2368   1882   -310   -538    368       C  
ATOM   1857  CG1 VAL A 700      28.180  17.626  21.917  1.00 19.40           C  
ANISOU 1857  CG1 VAL A 700     3079   2424   1870   -281   -461    289       C  
ATOM   1858  CG2 VAL A 700      29.135  15.424  22.571  1.00 20.49           C  
ANISOU 1858  CG2 VAL A 700     3367   2418   2001   -293   -706    413       C  
ATOM   1859  N   PHE A 701      24.820  17.236  22.518  1.00 19.78           N  
ANISOU 1859  N   PHE A 701     3183   2585   1747   -482   -199    328       N  
ATOM   1860  CA  PHE A 701      23.598  17.853  21.919  1.00 19.19           C  
ANISOU 1860  CA  PHE A 701     3009   2574   1710   -486    -59    272       C  
ATOM   1861  C   PHE A 701      23.200  19.090  22.710  1.00 20.25           C  
ANISOU 1861  C   PHE A 701     3130   2785   1778   -513     39    204       C  
ATOM   1862  O   PHE A 701      23.760  19.345  23.770  1.00 20.65           O  
ANISOU 1862  O   PHE A 701     3264   2849   1735   -549      6    205       O  
ATOM   1863  CB  PHE A 701      22.428  16.843  21.882  1.00 19.84           C  
ANISOU 1863  CB  PHE A 701     3112   2659   1766   -571    -10    315       C  
ATOM   1864  CG  PHE A 701      21.792  16.525  23.238  1.00 21.04           C  
ANISOU 1864  CG  PHE A 701     3372   2853   1770   -706     42    347       C  
ATOM   1865  CD1 PHE A 701      22.437  15.714  24.169  1.00 22.54           C  
ANISOU 1865  CD1 PHE A 701     3712   2995   1859   -768    -58    431       C  
ATOM   1866  CD2 PHE A 701      20.538  17.021  23.569  1.00 21.44           C  
ANISOU 1866  CD2 PHE A 701     3374   2990   1781   -775    191    293       C  
ATOM   1867  CE1 PHE A 701      21.836  15.399  25.384  1.00 24.58           C  
ANISOU 1867  CE1 PHE A 701     4085   3293   1960   -908     -5    468       C  
ATOM   1868  CE2 PHE A 701      19.935  16.706  24.781  1.00 23.03           C  
ANISOU 1868  CE2 PHE A 701     3674   3240   1837   -914    259    314       C  
ATOM   1869  CZ  PHE A 701      20.585  15.922  25.702  1.00 24.63           C  
ANISOU 1869  CZ  PHE A 701     4042   3398   1919   -987    165    405       C  
ATOM   1870  N   CYS A 702      22.231  19.824  22.189  1.00 20.06           N  
ANISOU 1870  N   CYS A 702     3004   2810   1809   -495    149    140       N  
ATOM   1871  CA  CYS A 702      21.710  21.011  22.807  1.00 20.88           C  
ANISOU 1871  CA  CYS A 702     3075   2980   1880   -510    251     57       C  
ATOM   1872  C   CYS A 702      20.264  20.705  23.259  1.00 21.70           C  
ANISOU 1872  C   CYS A 702     3165   3148   1933   -605    372     37       C  
ATOM   1873  O   CYS A 702      19.365  20.459  22.408  1.00 20.26           O  
ANISOU 1873  O   CYS A 702     2893   2971   1835   -592    414     29       O  
ATOM   1874  CB  CYS A 702      21.707  22.166  21.794  1.00 20.67           C  
ANISOU 1874  CB  CYS A 702     2928   2947   1979   -404    277     -8       C  
ATOM   1875  SG  CYS A 702      21.214  23.674  22.611  1.00 24.84           S  
ANISOU 1875  SG  CYS A 702     3421   3534   2485   -410    385   -121       S  
ATOM   1876  N   ASP A 703      20.067  20.610  24.569  1.00 22.67           N  
ANISOU 1876  N   ASP A 703     3381   3319   1915   -711    420     34       N  
ATOM   1877  CA  ASP A 703      18.748  20.359  25.143  1.00 23.93           C  
ANISOU 1877  CA  ASP A 703     3531   3552   2011   -822    553      3       C  
ATOM   1878  C   ASP A 703      17.824  21.587  25.055  1.00 24.73           C  
ANISOU 1878  C   ASP A 703     3497   3719   2182   -787    685   -128       C  
ATOM   1879  O   ASP A 703      17.883  22.485  25.890  1.00 26.43           O  
ANISOU 1879  O   ASP A 703     3726   3979   2336   -802    746   -207       O  
ATOM   1880  CB  ASP A 703      18.870  19.866  26.596  1.00 26.13           C  
ANISOU 1880  CB  ASP A 703     3967   3864   2095   -960    568     42       C  
ATOM   1881  CG  ASP A 703      17.541  19.406  27.170  1.00 28.47           C  
ANISOU 1881  CG  ASP A 703     4265   4236   2315  -1101    712     22       C  
ATOM   1882  OD1 ASP A 703      16.509  19.448  26.463  1.00 28.12           O  
ANISOU 1882  OD1 ASP A 703     4085   4218   2380  -1086    797    -28       O  
ATOM   1883  OD2 ASP A 703      17.530  18.942  28.339  1.00 30.85           O  
ANISOU 1883  OD2 ASP A 703     4709   4572   2441  -1236    738     61       O  
ATOM   1884  N   VAL A 704      16.931  21.606  24.063  1.00 24.33           N  
ANISOU 1884  N   VAL A 704     3313   3670   2260   -741    725   -157       N  
ATOM   1885  CA  VAL A 704      16.008  22.750  23.866  1.00 24.58           C  
ANISOU 1885  CA  VAL A 704     3202   3749   2388   -690    829   -283       C  
ATOM   1886  C   VAL A 704      14.576  22.401  24.284  1.00 26.23           C  
ANISOU 1886  C   VAL A 704     3344   4039   2584   -792    969   -341       C  
ATOM   1887  O   VAL A 704      13.620  23.094  23.900  1.00 26.14           O  
ANISOU 1887  O   VAL A 704     3184   4059   2688   -744   1043   -441       O  
ATOM   1888  CB  VAL A 704      16.038  23.272  22.419  1.00 23.13           C  
ANISOU 1888  CB  VAL A 704     2905   3509   2374   -551    762   -289       C  
ATOM   1889  CG1 VAL A 704      17.365  23.963  22.149  1.00 23.04           C  
ANISOU 1889  CG1 VAL A 704     2941   3435   2380   -461    665   -268       C  
ATOM   1890  CG2 VAL A 704      15.785  22.137  21.408  1.00 22.16           C  
ANISOU 1890  CG2 VAL A 704     2764   3352   2304   -552    700   -207       C  
ATOM   1891  N   SER A 705      14.439  21.348  25.097  1.00 27.36           N  
ANISOU 1891  N   SER A 705     3596   4211   2587   -935   1001   -280       N  
ATOM   1892  CA  SER A 705      13.109  20.876  25.563  1.00 29.35           C  
ANISOU 1892  CA  SER A 705     3795   4545   2810  -1063   1146   -329       C  
ATOM   1893  C   SER A 705      12.311  21.968  26.269  1.00 31.07           C  
ANISOU 1893  C   SER A 705     3918   4855   3033  -1079   1304   -489       C  
ATOM   1894  O   SER A 705      11.072  22.004  26.139  1.00 32.16           O  
ANISOU 1894  O   SER A 705     3915   5053   3250  -1112   1420   -577       O  
ATOM   1895  CB  SER A 705      13.243  19.655  26.445  1.00 30.21           C  
ANISOU 1895  CB  SER A 705     4070   4662   2744  -1228   1152   -227       C  
ATOM   1896  OG  SER A 705      14.045  19.935  27.567  1.00 31.27           O  
ANISOU 1896  OG  SER A 705     4353   4813   2716  -1277   1143   -215       O  
ATOM   1897  N   MET A 706      12.986  22.874  26.971  1.00 31.34           N  
ANISOU 1897  N   MET A 706     4010   4898   2999  -1051   1309   -541       N  
ATOM   1898  CA  MET A 706      12.280  23.947  27.688  1.00 34.58           C  
ANISOU 1898  CA  MET A 706     4334   5391   3414  -1063   1461   -710       C  
ATOM   1899  C   MET A 706      12.401  25.312  26.998  1.00 33.49           C  
ANISOU 1899  C   MET A 706     4070   5206   3450   -888   1425   -805       C  
ATOM   1900  O   MET A 706      12.012  26.324  27.573  1.00 33.40           O  
ANISOU 1900  O   MET A 706     3995   5239   3456   -873   1527   -950       O  
ATOM   1901  CB  MET A 706      12.804  24.038  29.123  1.00 37.40           C  
ANISOU 1901  CB  MET A 706     4854   5802   3555  -1178   1514   -724       C  
ATOM   1902  CG  MET A 706      12.751  22.739  29.917  1.00 40.48           C  
ANISOU 1902  CG  MET A 706     5402   6230   3750  -1363   1540   -618       C  
ATOM   1903  SD  MET A 706      11.114  21.999  29.973  1.00 47.51           S  
ANISOU 1903  SD  MET A 706     6182   7210   4660  -1504   1720   -668       S  
ATOM   1904  CE  MET A 706      10.177  23.300  30.776  1.00 47.88           C  
ANISOU 1904  CE  MET A 706     6094   7378   4721  -1521   1937   -909       C  
ATOM   1905  N   ASP A 707      12.883  25.352  25.753  1.00 30.87           N  
ANISOU 1905  N   ASP A 707     3701   4781   3247   -760   1284   -729       N  
ATOM   1906  CA  ASP A 707      13.077  26.630  25.063  1.00 31.94           C  
ANISOU 1906  CA  ASP A 707     3742   4857   3536   -604   1235   -796       C  
ATOM   1907  C   ASP A 707      11.739  27.296  24.742  1.00 34.09           C  
ANISOU 1907  C   ASP A 707     3823   5162   3968   -552   1328   -933       C  
ATOM   1908  O   ASP A 707      10.866  26.693  24.119  1.00 33.42           O  
ANISOU 1908  O   ASP A 707     3641   5094   3963   -562   1339   -921       O  
ATOM   1909  CB  ASP A 707      13.906  26.449  23.776  1.00 31.08           C  
ANISOU 1909  CB  ASP A 707     3651   4648   3509   -499   1071   -676       C  
ATOM   1910  CG  ASP A 707      14.389  27.791  23.179  1.00 30.95           C  
ANISOU 1910  CG  ASP A 707     3586   4559   3614   -358   1009   -721       C  
ATOM   1911  OD1 ASP A 707      13.558  28.657  22.790  1.00 32.19           O  
ANISOU 1911  OD1 ASP A 707     3610   4708   3913   -280   1045   -818       O  
ATOM   1912  OD2 ASP A 707      15.612  27.978  23.090  1.00 32.77           O  
ANISOU 1912  OD2 ASP A 707     3911   4734   3807   -326    918   -659       O  
ATOM   1913  N   GLU A 708      11.621  28.554  25.167  1.00 37.50           N  
ANISOU 1913  N   GLU A 708     4199   5594   4455   -492   1385  -1067       N  
ATOM   1914  CA  GLU A 708      10.374  29.307  25.121  1.00 41.37           C  
ANISOU 1914  CA  GLU A 708     4505   6116   5097   -442   1484  -1229       C  
ATOM   1915  C   GLU A 708      10.045  29.971  23.803  1.00 39.27           C  
ANISOU 1915  C   GLU A 708     4109   5762   5051   -281   1380  -1233       C  
ATOM   1916  O   GLU A 708       8.924  30.438  23.640  1.00 40.26           O  
ANISOU 1916  O   GLU A 708     4066   5907   5323   -233   1440  -1356       O  
ATOM   1917  CB  GLU A 708      10.377  30.403  26.207  1.00 46.19           C  
ANISOU 1917  CB  GLU A 708     5114   6759   5679   -446   1592  -1389       C  
ATOM   1918  CG  GLU A 708      10.271  29.860  27.610  1.00 50.94           C  
ANISOU 1918  CG  GLU A 708     5809   7476   6071   -620   1737  -1433       C  
ATOM   1919  CD  GLU A 708       9.977  30.946  28.647  1.00 57.08           C  
ANISOU 1919  CD  GLU A 708     6549   8303   6835   -628   1873  -1631       C  
ATOM   1920  OE1 GLU A 708      10.103  32.170  28.349  1.00 60.23           O  
ANISOU 1920  OE1 GLU A 708     6878   8626   7379   -492   1834  -1722       O  
ATOM   1921  OE2 GLU A 708       9.619  30.565  29.776  1.00 61.72           O  
ANISOU 1921  OE2 GLU A 708     7186   9004   7262   -778   2022  -1698       O  
ATOM   1922  N   ASP A 709      10.992  30.081  22.884  1.00 35.71           N  
ANISOU 1922  N   ASP A 709     3728   5214   4626   -197   1227  -1111       N  
ATOM   1923  CA  ASP A 709      10.672  30.723  21.614  1.00 35.75           C  
ANISOU 1923  CA  ASP A 709     3629   5134   4821    -55   1122  -1105       C  
ATOM   1924  C   ASP A 709      11.134  30.029  20.364  1.00 30.66           C  
ANISOU 1924  C   ASP A 709     3028   4433   4187    -22    983   -948       C  
ATOM   1925  O   ASP A 709      10.692  30.401  19.286  1.00 30.32           O  
ANISOU 1925  O   ASP A 709     2899   4335   4286     77    899   -939       O  
ATOM   1926  CB  ASP A 709      11.149  32.164  21.594  1.00 39.40           C  
ANISOU 1926  CB  ASP A 709     4092   5509   5368     54   1083  -1168       C  
ATOM   1927  CG  ASP A 709      12.583  32.299  21.857  1.00 40.67           C  
ANISOU 1927  CG  ASP A 709     4414   5629   5411     35   1029  -1089       C  
ATOM   1928  OD1 ASP A 709      13.385  31.707  21.116  1.00 44.39           O  
ANISOU 1928  OD1 ASP A 709     4968   6062   5839     36    925   -946       O  
ATOM   1929  OD2 ASP A 709      12.939  33.059  22.795  1.00 48.77           O  
ANISOU 1929  OD2 ASP A 709     5478   6657   6395     23   1088  -1180       O  
ATOM   1930  N   LEU A 710      11.998  29.035  20.478  1.00 27.40           N  
ANISOU 1930  N   LEU A 710     2749   4033   3630   -102    951   -830       N  
ATOM   1931  CA  LEU A 710      12.441  28.279  19.276  1.00 23.89           C  
ANISOU 1931  CA  LEU A 710     2344   3539   3193    -77    828   -693       C  
ATOM   1932  C   LEU A 710      11.264  27.704  18.469  1.00 23.86           C  
ANISOU 1932  C   LEU A 710     2220   3560   3288    -69    815   -697       C  
ATOM   1933  O   LEU A 710      11.360  27.577  17.254  1.00 23.86           O  
ANISOU 1933  O   LEU A 710     2209   3507   3350     -4    705   -625       O  
ATOM   1934  CB  LEU A 710      13.384  27.140  19.675  1.00 22.56           C  
ANISOU 1934  CB  LEU A 710     2319   3386   2865   -173    810   -587       C  
ATOM   1935  CG  LEU A 710      14.043  26.373  18.537  1.00 21.44           C  
ANISOU 1935  CG  LEU A 710     2231   3192   2723   -147    690   -462       C  
ATOM   1936  CD1 LEU A 710      14.884  27.285  17.683  1.00 20.52           C  
ANISOU 1936  CD1 LEU A 710     2134   2994   2667    -42    597   -431       C  
ATOM   1937  CD2 LEU A 710      14.890  25.289  19.150  1.00 21.08           C  
ANISOU 1937  CD2 LEU A 710     2317   3158   2534   -240    679   -381       C  
ATOM   1938  N   PHE A 711      10.197  27.326  19.165  1.00 24.00           N  
ANISOU 1938  N   PHE A 711     2151   3660   3307   -146    931   -782       N  
ATOM   1939  CA  PHE A 711       9.046  26.636  18.558  1.00 24.81           C  
ANISOU 1939  CA  PHE A 711     2132   3799   3495   -165    932   -794       C  
ATOM   1940  C   PHE A 711       7.868  27.524  18.201  1.00 26.01           C  
ANISOU 1940  C   PHE A 711     2096   3953   3834    -73    942   -919       C  
ATOM   1941  O   PHE A 711       6.840  27.010  17.802  1.00 26.33           O  
ANISOU 1941  O   PHE A 711     2017   4032   3956    -92    949   -949       O  
ATOM   1942  CB  PHE A 711       8.629  25.467  19.458  1.00 25.43           C  
ANISOU 1942  CB  PHE A 711     2237   3966   3461   -327   1047   -795       C  
ATOM   1943  CG  PHE A 711       9.771  24.577  19.779  1.00 24.72           C  
ANISOU 1943  CG  PHE A 711     2332   3857   3203   -405   1012   -668       C  
ATOM   1944  CD1 PHE A 711      10.343  23.802  18.786  1.00 23.18           C  
ANISOU 1944  CD1 PHE A 711     2201   3604   3001   -384    888   -546       C  
ATOM   1945  CD2 PHE A 711      10.363  24.603  21.048  1.00 25.56           C  
ANISOU 1945  CD2 PHE A 711     2553   3996   3162   -488   1089   -675       C  
ATOM   1946  CE1 PHE A 711      11.447  23.021  19.051  1.00 22.80           C  
ANISOU 1946  CE1 PHE A 711     2314   3527   2823   -438    843   -439       C  
ATOM   1947  CE2 PHE A 711      11.460  23.805  21.313  1.00 25.14           C  
ANISOU 1947  CE2 PHE A 711     2669   3913   2969   -546   1030   -556       C  
ATOM   1948  CZ  PHE A 711      11.984  23.002  20.322  1.00 23.52           C  
ANISOU 1948  CZ  PHE A 711     2512   3646   2779   -518    908   -440       C  
ATOM   1949  N   THR A 712       8.019  28.842  18.341  1.00 26.95           N  
ANISOU 1949  N   THR A 712     2187   4023   4029     27    935   -993       N  
ATOM   1950  CA  THR A 712       6.911  29.762  18.095  1.00 29.10           C  
ANISOU 1950  CA  THR A 712     2277   4284   4495    126    939  -1124       C  
ATOM   1951  C   THR A 712       7.163  30.733  16.913  1.00 28.51           C  
ANISOU 1951  C   THR A 712     2194   4088   4548    283    773  -1079       C  
ATOM   1952  O   THR A 712       6.469  31.735  16.769  1.00 30.15           O  
ANISOU 1952  O   THR A 712     2278   4256   4922    387    752  -1182       O  
ATOM   1953  CB  THR A 712       6.616  30.560  19.377  1.00 31.05           C  
ANISOU 1953  CB  THR A 712     2472   4575   4750    109   1088  -1285       C  
ATOM   1954  OG1 THR A 712       7.711  31.399  19.636  1.00 30.92           O  
ANISOU 1954  OG1 THR A 712     2579   4489   4681    155   1055  -1262       O  
ATOM   1955  CG2 THR A 712       6.429  29.630  20.601  1.00 32.49           C  
ANISOU 1955  CG2 THR A 712     2690   4880   4774    -66   1258  -1321       C  
ATOM   1956  N   GLY A 713       8.122  30.437  16.052  1.00 27.41           N  
ANISOU 1956  N   GLY A 713     2186   3889   4338    298    654   -929       N  
ATOM   1957  CA  GLY A 713       8.313  31.258  14.850  1.00 27.26           C  
ANISOU 1957  CA  GLY A 713     2174   3761   4422    425    498   -872       C  
ATOM   1958  C   GLY A 713       7.254  31.129  13.777  1.00 28.33           C  
ANISOU 1958  C   GLY A 713     2186   3885   4693    489    395   -873       C  
ATOM   1959  O   GLY A 713       6.466  30.154  13.765  1.00 27.45           O  
ANISOU 1959  O   GLY A 713     1991   3854   4586    424    430   -894       O  
ATOM   1960  N   ASP A 714       7.220  32.120  12.875  1.00 29.58           N  
ANISOU 1960  N   ASP A 714     2334   3939   4964    613    259   -849       N  
ATOM   1961  CA AASP A 714       6.216  32.191  11.789  0.50 31.22           C  
ANISOU 1961  CA AASP A 714     2429   4119   5314    694    126   -848       C  
ATOM   1962  CA BASP A 714       6.289  32.072  11.733  0.50 31.20           C  
ANISOU 1962  CA BASP A 714     2439   4120   5294    685    124   -834       C  
ATOM   1963  C   ASP A 714       6.819  32.861  10.548  1.00 30.86           C  
ANISOU 1963  C   ASP A 714     2492   3955   5278    780    -48   -726       C  
ATOM   1964  O   ASP A 714       7.866  33.483  10.649  1.00 31.47           O  
ANISOU 1964  O   ASP A 714     2699   3968   5292    789    -49   -673       O  
ATOM   1965  CB AASP A 714       4.979  32.981  12.244  0.50 33.72           C  
ANISOU 1965  CB AASP A 714     2547   4434   5831    775    154  -1015       C  
ATOM   1966  CB BASP A 714       4.863  32.492  12.110  0.50 33.94           C  
ANISOU 1966  CB BASP A 714     2568   4494   5832    742    155   -996       C  
ATOM   1967  CG AASP A 714       3.711  32.547  11.525  0.50 35.42           C  
ANISOU 1967  CG AASP A 714     2598   4681   6179    808     71  -1052       C  
ATOM   1968  CG BASP A 714       4.772  33.902  12.613  0.50 35.32           C  
ANISOU 1968  CG BASP A 714     2696   4591   6135    845    167  -1100       C  
ATOM   1969  OD1AASP A 714       3.770  31.577  10.729  0.50 34.91           O  
ANISOU 1969  OD1AASP A 714     2580   4647   6037    756      2   -951       O  
ATOM   1970  OD1BASP A 714       5.812  34.585  12.722  0.50 35.16           O  
ANISOU 1970  OD1BASP A 714     2816   4494   6051    864    154  -1044       O  
ATOM   1971  OD2AASP A 714       2.655  33.173  11.765  0.50 37.62           O  
ANISOU 1971  OD2AASP A 714     2693   4954   6646    887     75  -1193       O  
ATOM   1972  OD2BASP A 714       3.637  34.325  12.926  0.50 38.66           O  
ANISOU 1972  OD2BASP A 714     2930   5027   6732    904    193  -1249       O  
ATOM   1973  N   GLY A 715       6.154  32.700   9.397  1.00 31.27           N  
ANISOU 1973  N   GLY A 715     2494   3985   5401    832   -193   -682       N  
ATOM   1974  CA  GLY A 715       6.512  33.417   8.180  1.00 31.12           C  
ANISOU 1974  CA  GLY A 715     2571   3853   5401    914   -369   -573       C  
ATOM   1975  C   GLY A 715       7.508  32.745   7.235  1.00 29.50           C  
ANISOU 1975  C   GLY A 715     2538   3647   5023    851   -429   -417       C  
ATOM   1976  O   GLY A 715       7.891  33.350   6.200  1.00 30.87           O  
ANISOU 1976  O   GLY A 715     2813   3731   5186    902   -565   -318       O  
ATOM   1977  N   ASP A 716       7.960  31.533   7.576  1.00 26.50           N  
ANISOU 1977  N   ASP A 716     2201   3360   4508    740   -329   -397       N  
ATOM   1978  CA  ASP A 716       8.875  30.776   6.727  1.00 24.19           C  
ANISOU 1978  CA  ASP A 716     2054   3075   4063    678   -372   -273       C  
ATOM   1979  C   ASP A 716       8.717  29.306   7.179  1.00 22.79           C  
ANISOU 1979  C   ASP A 716     1844   3004   3810    574   -278   -296       C  
ATOM   1980  O   ASP A 716       8.571  29.015   8.366  1.00 21.98           O  
ANISOU 1980  O   ASP A 716     1688   2957   3706    523   -146   -371       O  
ATOM   1981  CB  ASP A 716      10.296  31.298   6.933  1.00 23.51           C  
ANISOU 1981  CB  ASP A 716     2119   2938   3877    660   -330   -212       C  
ATOM   1982  CG  ASP A 716      11.340  30.703   5.948  1.00 23.11           C  
ANISOU 1982  CG  ASP A 716     2215   2884   3680    607   -376    -93       C  
ATOM   1983  OD1 ASP A 716      11.395  29.473   5.734  1.00 22.29           O  
ANISOU 1983  OD1 ASP A 716     2122   2849   3498    539   -356    -75       O  
ATOM   1984  OD2 ASP A 716      12.253  31.469   5.516  1.00 23.79           O  
ANISOU 1984  OD2 ASP A 716     2415   2900   3725    621   -410    -26       O  
ATOM   1985  N   TYR A 717       8.707  28.384   6.229  1.00 22.09           N  
ANISOU 1985  N   TYR A 717     1794   2942   3659    536   -348   -233       N  
ATOM   1986  CA  TYR A 717       8.655  26.979   6.551  1.00 20.69           C  
ANISOU 1986  CA  TYR A 717     1608   2843   3410    436   -275   -242       C  
ATOM   1987  C   TYR A 717       9.756  26.589   7.539  1.00 19.42           C  
ANISOU 1987  C   TYR A 717     1541   2700   3137    363   -149   -227       C  
ATOM   1988  O   TYR A 717       9.596  25.653   8.365  1.00 18.90           O  
ANISOU 1988  O   TYR A 717     1451   2695   3035    279    -52   -260       O  
ATOM   1989  CB  TYR A 717       8.774  26.183   5.244  1.00 20.91           C  
ANISOU 1989  CB  TYR A 717     1700   2875   3371    414   -382   -168       C  
ATOM   1990  CG  TYR A 717       8.704  24.690   5.323  1.00 20.07           C  
ANISOU 1990  CG  TYR A 717     1594   2830   3201    316   -336   -170       C  
ATOM   1991  CD1 TYR A 717       7.760  24.045   6.114  1.00 21.08           C  
ANISOU 1991  CD1 TYR A 717     1600   3018   3390    261   -261   -247       C  
ATOM   1992  CD2 TYR A 717       9.518  23.903   4.476  1.00 19.45           C  
ANISOU 1992  CD2 TYR A 717     1636   2746   3009    275   -378    -99       C  
ATOM   1993  CE1 TYR A 717       7.689  22.650   6.132  1.00 20.77           C  
ANISOU 1993  CE1 TYR A 717     1574   3022   3297    163   -229   -241       C  
ATOM   1994  CE2 TYR A 717       9.438  22.521   4.459  1.00 19.05           C  
ANISOU 1994  CE2 TYR A 717     1590   2736   2913    191   -353   -104       C  
ATOM   1995  CZ  TYR A 717       8.509  21.894   5.293  1.00 19.67           C  
ANISOU 1995  CZ  TYR A 717     1557   2863   3053    134   -283   -170       C  
ATOM   1996  OH  TYR A 717       8.467  20.503   5.297  1.00 19.14           O  
ANISOU 1996  OH  TYR A 717     1508   2822   2942     42   -259   -167       O  
ATOM   1997  N   GLN A 718      10.895  27.280   7.478  1.00 18.30           N  
ANISOU 1997  N   GLN A 718     1512   2503   2937    388   -153   -175       N  
ATOM   1998  CA  GLN A 718      11.938  27.074   8.462  1.00 17.97           C  
ANISOU 1998  CA  GLN A 718     1550   2473   2806    333    -50   -170       C  
ATOM   1999  C   GLN A 718      11.389  26.891   9.871  1.00 18.36           C  
ANISOU 1999  C   GLN A 718     1522   2578   2877    287     69   -256       C  
ATOM   2000  O   GLN A 718      11.808  25.969  10.620  1.00 17.31           O  
ANISOU 2000  O   GLN A 718     1435   2486   2655    202    145   -248       O  
ATOM   2001  CB  GLN A 718      12.896  28.258   8.448  1.00 18.47           C  
ANISOU 2001  CB  GLN A 718     1692   2467   2860    382    -63   -142       C  
ATOM   2002  CG  GLN A 718      14.048  28.120   9.419  1.00 18.48           C  
ANISOU 2002  CG  GLN A 718     1773   2476   2774    329     25   -139       C  
ATOM   2003  CD  GLN A 718      14.886  29.358   9.542  1.00 18.62           C  
ANISOU 2003  CD  GLN A 718     1849   2427   2799    371     21   -130       C  
ATOM   2004  OE1 GLN A 718      14.961  30.176   8.630  1.00 19.32           O  
ANISOU 2004  OE1 GLN A 718     1963   2451   2925    426    -57    -91       O  
ATOM   2005  NE2 GLN A 718      15.614  29.452  10.659  1.00 18.35           N  
ANISOU 2005  NE2 GLN A 718     1851   2405   2718    334    101   -159       N  
ATOM   2006  N   PHE A 719      10.450  27.764  10.270  1.00 19.20           N  
ANISOU 2006  N   PHE A 719     1514   2682   3098    341     88   -343       N  
ATOM   2007  CA  PHE A 719       9.989  27.761  11.660  1.00 20.39           C  
ANISOU 2007  CA  PHE A 719     1597   2889   3260    293    221   -439       C  
ATOM   2008  C   PHE A 719       9.070  26.578  11.973  1.00 20.83           C  
ANISOU 2008  C   PHE A 719     1573   3028   3314    206    280   -475       C  
ATOM   2009  O   PHE A 719       8.989  26.162  13.132  1.00 20.76           O  
ANISOU 2009  O   PHE A 719     1561   3076   3249    121    402   -520       O  
ATOM   2010  CB  PHE A 719       9.374  29.143  12.061  1.00 22.50           C  
ANISOU 2010  CB  PHE A 719     1767   3125   3659    381    237   -541       C  
ATOM   2011  CG  PHE A 719      10.392  30.223  11.979  1.00 22.79           C  
ANISOU 2011  CG  PHE A 719     1901   3076   3681    440    200   -505       C  
ATOM   2012  CD1 PHE A 719      11.433  30.256  12.882  1.00 22.67           C  
ANISOU 2012  CD1 PHE A 719     1986   3068   3559    387    279   -498       C  
ATOM   2013  CD2 PHE A 719      10.452  31.055  10.868  1.00 24.58           C  
ANISOU 2013  CD2 PHE A 719     2146   3214   3979    534     71   -454       C  
ATOM   2014  CE1 PHE A 719      12.493  31.161  12.738  1.00 23.62           C  
ANISOU 2014  CE1 PHE A 719     2204   3111   3662    427    241   -458       C  
ATOM   2015  CE2 PHE A 719      11.477  31.981  10.749  1.00 24.32           C  
ANISOU 2015  CE2 PHE A 719     2218   3098   3923    569     41   -409       C  
ATOM   2016  CZ  PHE A 719      12.508  32.012  11.657  1.00 23.89           C  
ANISOU 2016  CZ  PHE A 719     2249   3056   3774    514    128   -413       C  
ATOM   2017  N   ASP A 720       8.452  25.983  10.931  1.00 21.05           N  
ANISOU 2017  N   ASP A 720     1551   3060   3386    213    192   -447       N  
ATOM   2018  CA  ASP A 720       7.724  24.737  11.107  1.00 22.11           C  
ANISOU 2018  CA  ASP A 720     1628   3263   3509    116    237   -465       C  
ATOM   2019  C   ASP A 720       8.659  23.577  11.386  1.00 20.13           C  
ANISOU 2019  C   ASP A 720     1516   3020   3112     18    270   -385       C  
ATOM   2020  O   ASP A 720       8.280  22.627  12.055  1.00 19.46           O  
ANISOU 2020  O   ASP A 720     1418   2987   2990    -88    351   -401       O  
ATOM   2021  CB  ASP A 720       6.908  24.390   9.867  1.00 23.94           C  
ANISOU 2021  CB  ASP A 720     1781   3492   3823    149    119   -456       C  
ATOM   2022  CG  ASP A 720       5.802  25.395   9.580  1.00 27.06           C  
ANISOU 2022  CG  ASP A 720     2017   3879   4386    247     66   -543       C  
ATOM   2023  OD1 ASP A 720       5.164  25.932  10.499  1.00 28.19           O  
ANISOU 2023  OD1 ASP A 720     2047   4053   4609    252    162   -649       O  
ATOM   2024  OD2 ASP A 720       5.487  25.550   8.383  1.00 30.95           O  
ANISOU 2024  OD2 ASP A 720     2488   4336   4934    314    -78   -509       O  
ATOM   2025  N   ILE A 721       9.847  23.606  10.800  1.00 18.98           N  
ANISOU 2025  N   ILE A 721     1499   2820   2892     49    201   -298       N  
ATOM   2026  CA  ILE A 721      10.781  22.478  10.934  1.00 17.77           C  
ANISOU 2026  CA  ILE A 721     1470   2661   2621    -27    211   -226       C  
ATOM   2027  C   ILE A 721      11.124  22.306  12.422  1.00 17.49           C  
ANISOU 2027  C   ILE A 721     1480   2654   2511   -103    326   -244       C  
ATOM   2028  O   ILE A 721      11.168  21.166  12.903  1.00 17.39           O  
ANISOU 2028  O   ILE A 721     1514   2661   2433   -200    362   -217       O  
ATOM   2029  CB  ILE A 721      12.087  22.633  10.103  1.00 16.80           C  
ANISOU 2029  CB  ILE A 721     1465   2479   2439     22    130   -149       C  
ATOM   2030  CG1 ILE A 721      11.789  22.920   8.633  1.00 16.75           C  
ANISOU 2030  CG1 ILE A 721     1434   2447   2482     90     18   -127       C  
ATOM   2031  CG2 ILE A 721      12.955  21.406  10.257  1.00 16.33           C  
ANISOU 2031  CG2 ILE A 721     1508   2411   2285    -48    135    -94       C  
ATOM   2032  CD1 ILE A 721      11.116  21.778   7.897  1.00 17.37           C  
ANISOU 2032  CD1 ILE A 721     1481   2549   2571     46    -31   -121       C  
ATOM   2033  N   TYR A 722      11.314  23.403  13.183  1.00 17.26           N  
ANISOU 2033  N   TYR A 722     1443   2626   2489    -67    380   -292       N  
ATOM   2034  CA  TYR A 722      11.605  23.213  14.596  1.00 17.38           C  
ANISOU 2034  CA  TYR A 722     1512   2676   2416   -149    484   -311       C  
ATOM   2035  C   TYR A 722      10.464  22.454  15.293  1.00 18.60           C  
ANISOU 2035  C   TYR A 722     1593   2902   2571   -255    580   -362       C  
ATOM   2036  O   TYR A 722      10.711  21.550  16.131  1.00 18.49           O  
ANISOU 2036  O   TYR A 722     1662   2911   2453   -365    636   -329       O  
ATOM   2037  CB  TYR A 722      11.915  24.523  15.335  1.00 17.70           C  
ANISOU 2037  CB  TYR A 722     1550   2710   2463   -100    533   -372       C  
ATOM   2038  CG  TYR A 722      12.993  25.303  14.694  1.00 16.80           C  
ANISOU 2038  CG  TYR A 722     1504   2525   2354    -13    449   -325       C  
ATOM   2039  CD1 TYR A 722      14.340  24.819  14.649  1.00 16.19           C  
ANISOU 2039  CD1 TYR A 722     1555   2415   2182    -33    406   -243       C  
ATOM   2040  CD2 TYR A 722      12.702  26.509  14.047  1.00 17.46           C  
ANISOU 2040  CD2 TYR A 722     1522   2566   2544     91    403   -359       C  
ATOM   2041  CE1 TYR A 722      15.332  25.553  13.979  1.00 15.04           C  
ANISOU 2041  CE1 TYR A 722     1460   2209   2047     39    338   -206       C  
ATOM   2042  CE2 TYR A 722      13.680  27.237  13.410  1.00 16.73           C  
ANISOU 2042  CE2 TYR A 722     1499   2404   2452    156    331   -310       C  
ATOM   2043  CZ  TYR A 722      14.996  26.738  13.363  1.00 15.75           C  
ANISOU 2043  CZ  TYR A 722     1493   2260   2229    124    306   -235       C  
ATOM   2044  OH  TYR A 722      15.971  27.469  12.673  1.00 15.43           O  
ANISOU 2044  OH  TYR A 722     1512   2156   2194    179    244   -191       O  
ATOM   2045  N   ARG A 723       9.216  22.831  14.975  1.00 19.69           N  
ANISOU 2045  N   ARG A 723     1578   3074   2831   -226    598   -444       N  
ATOM   2046  CA  ARG A 723       8.076  22.143  15.511  1.00 21.32           C  
ANISOU 2046  CA  ARG A 723     1692   3351   3056   -330    693   -503       C  
ATOM   2047  C   ARG A 723       7.950  20.686  15.072  1.00 21.00           C  
ANISOU 2047  C   ARG A 723     1690   3309   2979   -419    658   -432       C  
ATOM   2048  O   ARG A 723       7.594  19.816  15.916  1.00 22.04           O  
ANISOU 2048  O   ARG A 723     1843   3485   3045   -554    752   -433       O  
ATOM   2049  CB  ARG A 723       6.768  22.915  15.194  1.00 22.71           C  
ANISOU 2049  CB  ARG A 723     1670   3560   3398   -265    708   -621       C  
ATOM   2050  CG  ARG A 723       6.698  24.279  15.841  1.00 24.01           C  
ANISOU 2050  CG  ARG A 723     1781   3729   3613   -194    768   -718       C  
ATOM   2051  CD  ARG A 723       5.373  24.974  15.569  1.00 26.00           C  
ANISOU 2051  CD  ARG A 723     1825   4007   4048   -126    777   -845       C  
ATOM   2052  NE  ARG A 723       5.367  25.624  14.253  1.00 26.07           N  
ANISOU 2052  NE  ARG A 723     1798   3939   4169     17    612   -813       N  
ATOM   2053  CZ  ARG A 723       5.802  26.860  13.991  1.00 26.15           C  
ANISOU 2053  CZ  ARG A 723     1825   3877   4233    140    547   -820       C  
ATOM   2054  NH1 ARG A 723       5.708  27.331  12.760  1.00 26.05           N  
ANISOU 2054  NH1 ARG A 723     1790   3795   4311    250    392   -778       N  
ATOM   2055  NH2 ARG A 723       6.304  27.642  14.951  1.00 26.54           N  
ANISOU 2055  NH2 ARG A 723     1918   3919   4244    147    632   -869       N  
ATOM   2056  N   LEU A 724       8.215  20.422  13.797  1.00 19.64           N  
ANISOU 2056  N   LEU A 724     1533   3085   2843   -354    528   -373       N  
ATOM   2057  CA  LEU A 724       8.153  19.080  13.256  1.00 19.79           C  
ANISOU 2057  CA  LEU A 724     1592   3090   2838   -425    481   -314       C  
ATOM   2058  C   LEU A 724       9.272  18.184  13.853  1.00 19.31           C  
ANISOU 2058  C   LEU A 724     1704   2992   2640   -500    489   -224       C  
ATOM   2059  O   LEU A 724       9.034  16.995  14.048  1.00 19.90           O  
ANISOU 2059  O   LEU A 724     1814   3065   2681   -607    506   -192       O  
ATOM   2060  CB  LEU A 724       8.272  19.083  11.745  1.00 19.29           C  
ANISOU 2060  CB  LEU A 724     1518   2982   2831   -335    340   -281       C  
ATOM   2061  CG  LEU A 724       7.089  19.712  11.004  1.00 20.29           C  
ANISOU 2061  CG  LEU A 724     1480   3135   3096   -269    294   -355       C  
ATOM   2062  CD1 LEU A 724       7.346  20.004   9.525  1.00 19.82           C  
ANISOU 2062  CD1 LEU A 724     1436   3028   3068   -167    144   -314       C  
ATOM   2063  CD2 LEU A 724       5.897  18.794  11.144  1.00 21.89           C  
ANISOU 2063  CD2 LEU A 724     1575   3390   3353   -372    339   -404       C  
ATOM   2064  N   MET A 725      10.425  18.760  14.160  1.00 18.27           N  
ANISOU 2064  N   MET A 725     1671   2826   2443   -447    473   -189       N  
ATOM   2065  CA  MET A 725      11.471  18.011  14.896  1.00 18.24           C  
ANISOU 2065  CA  MET A 725     1821   2789   2320   -512    476   -115       C  
ATOM   2066  C   MET A 725      10.993  17.609  16.260  1.00 19.62           C  
ANISOU 2066  C   MET A 725     2020   3013   2422   -642    591   -129       C  
ATOM   2067  O   MET A 725      11.203  16.468  16.683  1.00 19.72           O  
ANISOU 2067  O   MET A 725     2130   3002   2361   -742    589    -66       O  
ATOM   2068  CB  MET A 725      12.749  18.796  15.021  1.00 17.08           C  
ANISOU 2068  CB  MET A 725     1756   2605   2129   -432    438    -89       C  
ATOM   2069  CG  MET A 725      13.574  18.813  13.777  1.00 16.40           C  
ANISOU 2069  CG  MET A 725     1700   2461   2072   -341    328    -47       C  
ATOM   2070  SD  MET A 725      15.214  19.524  14.025  1.00 15.67           S  
ANISOU 2070  SD  MET A 725     1708   2323   1922   -275    291    -14       S  
ATOM   2071  CE  MET A 725      14.847  21.130  14.649  1.00 16.13           C  
ANISOU 2071  CE  MET A 725     1701   2418   2010   -228    361    -89       C  
ATOM   2072  N   LYS A 726      10.384  18.561  16.972  1.00 21.01           N  
ANISOU 2072  N   LYS A 726     2117   3253   2613   -643    691   -215       N  
ATOM   2073  CA  LYS A 726       9.880  18.319  18.315  1.00 23.33           C  
ANISOU 2073  CA  LYS A 726     2430   3610   2824   -776    823   -246       C  
ATOM   2074  C   LYS A 726       8.787  17.222  18.312  1.00 24.69           C  
ANISOU 2074  C   LYS A 726     2549   3816   3018   -903    877   -251       C  
ATOM   2075  O   LYS A 726       8.701  16.403  19.241  1.00 24.55           O  
ANISOU 2075  O   LYS A 726     2620   3814   2893  -1048    946   -213       O  
ATOM   2076  CB  LYS A 726       9.349  19.608  18.942  1.00 24.94           C  
ANISOU 2076  CB  LYS A 726     2535   3880   3063   -742    926   -365       C  
ATOM   2077  CG  LYS A 726       8.903  19.465  20.386  1.00 27.90           C  
ANISOU 2077  CG  LYS A 726     2938   4332   3330   -885   1080   -411       C  
ATOM   2078  CD  LYS A 726       8.612  20.849  20.961  1.00 30.36           C  
ANISOU 2078  CD  LYS A 726     3163   4696   3676   -828   1170   -539       C  
ATOM   2079  CE  LYS A 726       7.837  20.830  22.227  1.00 34.76           C  
ANISOU 2079  CE  LYS A 726     3697   5352   4159   -967   1348   -627       C  
ATOM   2080  NZ  LYS A 726       8.069  22.163  22.863  1.00 37.10           N  
ANISOU 2080  NZ  LYS A 726     3973   5672   4451   -899   1405   -730       N  
ATOM   2081  N   LYS A 727       7.957  17.223  17.275  1.00 25.08           N  
ANISOU 2081  N   LYS A 727     2458   3872   3201   -855    839   -295       N  
ATOM   2082  CA  LYS A 727       6.965  16.168  17.075  1.00 27.44           C  
ANISOU 2082  CA  LYS A 727     2695   4192   3539   -967    868   -300       C  
ATOM   2083  C   LYS A 727       7.621  14.774  16.880  1.00 25.97           C  
ANISOU 2083  C   LYS A 727     2660   3927   3279  -1039    790   -181       C  
ATOM   2084  O   LYS A 727       7.250  13.804  17.579  1.00 26.97           O  
ANISOU 2084  O   LYS A 727     2843   4063   3343  -1196    858   -149       O  
ATOM   2085  CB  LYS A 727       6.040  16.499  15.881  1.00 28.98           C  
ANISOU 2085  CB  LYS A 727     2710   4402   3900   -882    810   -371       C  
ATOM   2086  CG  LYS A 727       4.807  15.606  15.756  1.00 33.11           C  
ANISOU 2086  CG  LYS A 727     3125   4967   4490  -1001    858   -412       C  
ATOM   2087  CD  LYS A 727       3.852  15.752  16.965  1.00 37.44           C  
ANISOU 2087  CD  LYS A 727     3584   5612   5028  -1127   1043   -504       C  
ATOM   2088  CE  LYS A 727       2.362  15.570  16.638  1.00 41.40           C  
ANISOU 2088  CE  LYS A 727     3873   6182   5675  -1181   1094   -612       C  
ATOM   2089  NZ  LYS A 727       1.465  16.323  17.576  1.00 44.17           N  
ANISOU 2089  NZ  LYS A 727     4077   6637   6067  -1225   1264   -751       N  
ATOM   2090  N   GLU A 728       8.593  14.699  15.990  1.00 24.17           N  
ANISOU 2090  N   GLU A 728     2503   3623   3059   -933    656   -120       N  
ATOM   2091  CA  GLU A 728       9.313  13.460  15.680  1.00 23.76           C  
ANISOU 2091  CA  GLU A 728     2583   3483   2961   -971    567    -22       C  
ATOM   2092  C   GLU A 728      10.028  12.887  16.904  1.00 23.69           C  
ANISOU 2092  C   GLU A 728     2741   3443   2816  -1069    598     55       C  
ATOM   2093  O   GLU A 728      10.013  11.702  17.101  1.00 23.68           O  
ANISOU 2093  O   GLU A 728     2827   3392   2780  -1173    580    118       O  
ATOM   2094  CB  GLU A 728      10.330  13.746  14.574  1.00 23.63           C  
ANISOU 2094  CB  GLU A 728     2600   3404   2975   -825    437      6       C  
ATOM   2095  CG  GLU A 728      11.449  12.708  14.341  1.00 23.87           C  
ANISOU 2095  CG  GLU A 728     2777   3336   2956   -828    341     93       C  
ATOM   2096  CD  GLU A 728      10.952  11.339  13.956  1.00 25.38           C  
ANISOU 2096  CD  GLU A 728     2984   3482   3176   -919    309    118       C  
ATOM   2097  OE1 GLU A 728       9.792  11.227  13.432  1.00 27.74           O  
ANISOU 2097  OE1 GLU A 728     3164   3825   3553   -953    332     63       O  
ATOM   2098  OE2 GLU A 728      11.703  10.345  14.212  1.00 25.45           O  
ANISOU 2098  OE2 GLU A 728     3126   3406   3138   -960    255    190       O  
ATOM   2099  N   ASN A 729      10.660  13.756  17.712  1.00 22.56           N  
ANISOU 2099  N   ASN A 729     2648   3324   2599  -1034    633     51       N  
ATOM   2100  CA  ASN A 729      11.457  13.273  18.848  1.00 23.10           C  
ANISOU 2100  CA  ASN A 729     2889   3359   2529  -1115    635    130       C  
ATOM   2101  C   ASN A 729      10.732  13.301  20.198  1.00 24.98           C  
ANISOU 2101  C   ASN A 729     3148   3675   2667  -1266    781    108       C  
ATOM   2102  O   ASN A 729      11.348  13.018  21.242  1.00 25.65           O  
ANISOU 2102  O   ASN A 729     3386   3743   2617  -1342    785    173       O  
ATOM   2103  CB  ASN A 729      12.827  13.963  18.899  1.00 21.52           C  
ANISOU 2103  CB  ASN A 729     2764   3120   2292   -997    555    156       C  
ATOM   2104  CG  ASN A 729      12.764  15.422  19.289  1.00 20.82           C  
ANISOU 2104  CG  ASN A 729     2604   3104   2203   -933    627     73       C  
ATOM   2105  OD1 ASN A 729      11.817  15.900  19.901  1.00 21.97           O  
ANISOU 2105  OD1 ASN A 729     2675   3332   2341   -994    751      0       O  
ATOM   2106  ND2 ASN A 729      13.770  16.145  18.875  1.00 19.37           N  
ANISOU 2106  ND2 ASN A 729     2435   2886   2040   -809    552     75       N  
ATOM   2107  N   ASN A 730       9.441  13.671  20.203  1.00 25.95           N  
ANISOU 2107  N   ASN A 730     3119   3888   2854  -1313    900     10       N  
ATOM   2108  CA  ASN A 730       8.683  13.754  21.453  1.00 28.72           C  
ANISOU 2108  CA  ASN A 730     3471   4329   3114  -1464   1064    -34       C  
ATOM   2109  C   ASN A 730       9.344  14.647  22.503  1.00 28.30           C  
ANISOU 2109  C   ASN A 730     3499   4313   2941  -1450   1111    -52       C  
ATOM   2110  O   ASN A 730       9.223  14.394  23.701  1.00 29.03           O  
ANISOU 2110  O   ASN A 730     3692   4449   2890  -1595   1207    -35       O  
ATOM   2111  CB  ASN A 730       8.469  12.366  22.027  1.00 30.85           C  
ANISOU 2111  CB  ASN A 730     3868   4566   3289  -1650   1087     59       C  
ATOM   2112  CG  ASN A 730       7.595  11.546  21.170  1.00 32.57           C  
ANISOU 2112  CG  ASN A 730     3987   4765   3622  -1695   1076     50       C  
ATOM   2113  OD1 ASN A 730       6.410  11.804  21.104  1.00 36.43           O  
ANISOU 2113  OD1 ASN A 730     4313   5341   4188  -1744   1187    -51       O  
ATOM   2114  ND2 ASN A 730       8.153  10.562  20.497  1.00 32.76           N  
ANISOU 2114  ND2 ASN A 730     4101   4678   3670  -1677    939    144       N  
ATOM   2115  N   ASN A 731      10.016  15.685  22.018  1.00 26.57           N  
ANISOU 2115  N   ASN A 731     3238   4076   2780  -1283   1042    -87       N  
ATOM   2116  CA  ASN A 731      10.743  16.638  22.823  1.00 26.82           C  
ANISOU 2116  CA  ASN A 731     3335   4131   2726  -1243   1062   -112       C  
ATOM   2117  C   ASN A 731      11.888  16.061  23.633  1.00 26.97           C  
ANISOU 2117  C   ASN A 731     3567   4097   2585  -1300    991      1       C  
ATOM   2118  O   ASN A 731      12.249  16.643  24.678  1.00 26.99           O  
ANISOU 2118  O   ASN A 731     3643   4141   2469  -1334   1042    -23       O  
ATOM   2119  CB  ASN A 731       9.787  17.406  23.736  1.00 28.32           C  
ANISOU 2119  CB  ASN A 731     3437   4436   2887  -1315   1242   -240       C  
ATOM   2120  CG  ASN A 731      10.300  18.774  24.116  1.00 27.78           C  
ANISOU 2120  CG  ASN A 731     3354   4391   2810  -1214   1258   -319       C  
ATOM   2121  OD1 ASN A 731      11.081  19.413  23.385  1.00 26.37           O  
ANISOU 2121  OD1 ASN A 731     3162   4151   2707  -1062   1146   -307       O  
ATOM   2122  ND2 ASN A 731       9.833  19.251  25.236  1.00 29.11           N  
ANISOU 2122  ND2 ASN A 731     3520   4649   2890  -1305   1406   -408       N  
ATOM   2123  N   ARG A 732      12.495  14.974  23.117  1.00 26.38           N  
ANISOU 2123  N   ARG A 732     3585   3924   2515  -1298    862    116       N  
ATOM   2124  CA  ARG A 732      13.646  14.324  23.753  1.00 26.62           C  
ANISOU 2124  CA  ARG A 732     3811   3880   2422  -1333    757    231       C  
ATOM   2125  C   ARG A 732      14.845  14.449  22.824  1.00 23.71           C  
ANISOU 2125  C   ARG A 732     3448   3422   2139  -1169    598    266       C  
ATOM   2126  O   ARG A 732      15.043  13.636  21.898  1.00 22.38           O  
ANISOU 2126  O   ARG A 732     3275   3175   2052  -1130    504    315       O  
ATOM   2127  CB  ARG A 732      13.342  12.861  24.068  1.00 29.43           C  
ANISOU 2127  CB  ARG A 732     4282   4186   2713  -1483    742    333       C  
ATOM   2128  CG  ARG A 732      12.262  12.701  25.144  1.00 32.91           C  
ANISOU 2128  CG  ARG A 732     4745   4720   3039  -1675    912    308       C  
ATOM   2129  CD  ARG A 732      12.181  11.288  25.679  1.00 36.13           C  
ANISOU 2129  CD  ARG A 732     5318   5064   3345  -1842    885    434       C  
ATOM   2130  NE  ARG A 732      11.453  10.407  24.763  1.00 38.41           N  
ANISOU 2130  NE  ARG A 732     5527   5308   3757  -1871    876    445       N  
ATOM   2131  CZ  ARG A 732      10.125  10.182  24.751  1.00 40.59           C  
ANISOU 2131  CZ  ARG A 732     5698   5657   4068  -1993   1019    386       C  
ATOM   2132  NH1 ARG A 732       9.606   9.337  23.848  1.00 40.88           N  
ANISOU 2132  NH1 ARG A 732     5671   5638   4222  -2008    981    402       N  
ATOM   2133  NH2 ARG A 732       9.295  10.803  25.594  1.00 42.51           N  
ANISOU 2133  NH2 ARG A 732     5885   6030   4238  -2097   1201    298       N  
ATOM   2134  N   TRP A 733      15.627  15.489  23.082  1.00 21.68           N  
ANISOU 2134  N   TRP A 733     3195   3179   1862  -1082    578    229       N  
ATOM   2135  CA  TRP A 733      16.671  15.942  22.139  1.00 20.33           C  
ANISOU 2135  CA  TRP A 733     2989   2948   1787   -922    462    229       C  
ATOM   2136  C   TRP A 733      17.955  15.105  22.221  1.00 19.59           C  
ANISOU 2136  C   TRP A 733     3029   2756   1659   -904    311    327       C  
ATOM   2137  O   TRP A 733      18.801  15.206  21.341  1.00 17.54           O  
ANISOU 2137  O   TRP A 733     2738   2441   1487   -787    217    330       O  
ATOM   2138  CB  TRP A 733      16.907  17.472  22.302  1.00 20.27           C  
ANISOU 2138  CB  TRP A 733     2914   2993   1795   -838    507    138       C  
ATOM   2139  CG  TRP A 733      15.649  18.199  21.991  1.00 20.60           C  
ANISOU 2139  CG  TRP A 733     2807   3108   1913   -831    628     38       C  
ATOM   2140  CD1 TRP A 733      14.610  18.403  22.838  1.00 22.15           C  
ANISOU 2140  CD1 TRP A 733     2972   3389   2055   -932    767    -26       C  
ATOM   2141  CD2 TRP A 733      15.229  18.681  20.710  1.00 20.01           C  
ANISOU 2141  CD2 TRP A 733     2591   3025   1986   -725    614     -8       C  
ATOM   2142  NE1 TRP A 733      13.549  18.970  22.156  1.00 22.16           N  
ANISOU 2142  NE1 TRP A 733     2805   3432   2182   -885    837   -116       N  
ATOM   2143  CE2 TRP A 733      13.897  19.159  20.856  1.00 21.33           C  
ANISOU 2143  CE2 TRP A 733     2637   3269   2198   -758    737   -101       C  
ATOM   2144  CE3 TRP A 733      15.824  18.719  19.447  1.00 19.02           C  
ANISOU 2144  CE3 TRP A 733     2433   2837   1956   -611    511     17       C  
ATOM   2145  CZ2 TRP A 733      13.167  19.725  19.783  1.00 20.67           C  
ANISOU 2145  CZ2 TRP A 733     2401   3192   2259   -669    737   -162       C  
ATOM   2146  CZ3 TRP A 733      15.095  19.286  18.374  1.00 19.17           C  
ANISOU 2146  CZ3 TRP A 733     2317   2869   2098   -535    520    -37       C  
ATOM   2147  CH2 TRP A 733      13.772  19.765  18.569  1.00 19.80           C  
ANISOU 2147  CH2 TRP A 733     2280   3017   2225   -562    623   -121       C  
ATOM   2148  N   GLY A 734      18.122  14.293  23.269  1.00 21.09           N  
ANISOU 2148  N   GLY A 734     3368   2922   1722  -1018    286    406       N  
ATOM   2149  CA  GLY A 734      19.297  13.417  23.330  1.00 21.60           C  
ANISOU 2149  CA  GLY A 734     3554   2879   1775   -992    124    500       C  
ATOM   2150  C   GLY A 734      19.160  12.205  22.420  1.00 22.20           C  
ANISOU 2150  C   GLY A 734     3626   2866   1944   -987     55    551       C  
ATOM   2151  O   GLY A 734      20.163  11.583  22.025  1.00 22.47           O  
ANISOU 2151  O   GLY A 734     3706   2801   2031   -916    -84    597       O  
ATOM   2152  N   GLU A 735      17.928  11.831  22.075  1.00 22.30           N  
ANISOU 2152  N   GLU A 735     3577   2911   1985  -1061    149    534       N  
ATOM   2153  CA  GLU A 735      17.715  10.661  21.206  1.00 22.23           C  
ANISOU 2153  CA  GLU A 735     3564   2818   2065  -1066     87    573       C  
ATOM   2154  C   GLU A 735      18.206  10.891  19.783  1.00 20.04           C  
ANISOU 2154  C   GLU A 735     3175   2509   1929   -914     24    521       C  
ATOM   2155  O   GLU A 735      18.324  12.042  19.341  1.00 19.66           O  
ANISOU 2155  O   GLU A 735     3026   2523   1922   -822     63    448       O  
ATOM   2156  CB  GLU A 735      16.235  10.332  21.155  1.00 23.75           C  
ANISOU 2156  CB  GLU A 735     3696   3065   2261  -1184    210    550       C  
ATOM   2157  CG  GLU A 735      15.650   9.880  22.475  1.00 26.56           C  
ANISOU 2157  CG  GLU A 735     4170   3449   2474  -1365    286    606       C  
ATOM   2158  CD  GLU A 735      14.189   9.496  22.368  1.00 28.43           C  
ANISOU 2158  CD  GLU A 735     4331   3741   2731  -1491    414    575       C  
ATOM   2159  OE1 GLU A 735      13.544   9.744  21.302  1.00 28.52           O  
ANISOU 2159  OE1 GLU A 735     4181   3784   2872  -1428    446    497       O  
ATOM   2160  OE2 GLU A 735      13.677   8.969  23.377  1.00 30.52           O  
ANISOU 2160  OE2 GLU A 735     4698   4021   2877  -1661    483    627       O  
ATOM   2161  N   TYR A 736      18.414   9.812  19.026  1.00 19.67           N  
ANISOU 2161  N   TYR A 736     3149   2367   1959   -896    -65    553       N  
ATOM   2162  CA  TYR A 736      18.787   9.917  17.648  1.00 18.00           C  
ANISOU 2162  CA  TYR A 736     2840   2132   1867   -773   -111    498       C  
ATOM   2163  C   TYR A 736      17.535   9.747  16.746  1.00 17.70           C  
ANISOU 2163  C   TYR A 736     2697   2134   1895   -804    -44    451       C  
ATOM   2164  O   TYR A 736      16.879   8.696  16.785  1.00 18.02           O  
ANISOU 2164  O   TYR A 736     2774   2131   1942   -900    -46    486       O  
ATOM   2165  CB  TYR A 736      19.786   8.826  17.317  1.00 18.49           C  
ANISOU 2165  CB  TYR A 736     2979   2065   1981   -729   -250    541       C  
ATOM   2166  CG  TYR A 736      20.282   8.819  15.893  1.00 17.15           C  
ANISOU 2166  CG  TYR A 736     2722   1869   1925   -611   -296    477       C  
ATOM   2167  CD1 TYR A 736      20.729   9.975  15.272  1.00 16.07           C  
ANISOU 2167  CD1 TYR A 736     2493   1797   1816   -509   -268    411       C  
ATOM   2168  CD2 TYR A 736      20.377   7.616  15.185  1.00 17.65           C  
ANISOU 2168  CD2 TYR A 736     2807   1834   2064   -606   -371    482       C  
ATOM   2169  CE1 TYR A 736      21.193   9.945  13.967  1.00 15.44           C  
ANISOU 2169  CE1 TYR A 736     2346   1698   1821   -418   -301    355       C  
ATOM   2170  CE2 TYR A 736      20.917   7.560  13.920  1.00 16.70           C  
ANISOU 2170  CE2 TYR A 736     2618   1692   2035   -504   -409    415       C  
ATOM   2171  CZ  TYR A 736      21.325   8.727  13.310  1.00 15.86           C  
ANISOU 2171  CZ  TYR A 736     2424   1663   1940   -415   -370    353       C  
ATOM   2172  OH  TYR A 736      21.821   8.660  12.041  1.00 16.18           O  
ANISOU 2172  OH  TYR A 736     2405   1689   2052   -332   -396    287       O  
ATOM   2173  N   HIS A 737      17.232  10.785  15.976  1.00 16.73           N  
ANISOU 2173  N   HIS A 737     2449   2086   1820   -727      6    376       N  
ATOM   2174  CA  HIS A 737      16.102  10.794  15.024  1.00 17.07           C  
ANISOU 2174  CA  HIS A 737     2377   2172   1934   -734     50    323       C  
ATOM   2175  C   HIS A 737      16.623  11.394  13.718  1.00 15.90           C  
ANISOU 2175  C   HIS A 737     2157   2028   1856   -603      3    273       C  
ATOM   2176  O   HIS A 737      16.476  12.562  13.449  1.00 15.58           O  
ANISOU 2176  O   HIS A 737     2040   2052   1828   -542     43    228       O  
ATOM   2177  CB  HIS A 737      14.939  11.632  15.575  1.00 17.99           C  
ANISOU 2177  CB  HIS A 737     2411   2396   2030   -790    172    279       C  
ATOM   2178  CG  HIS A 737      14.267  11.003  16.732  1.00 19.86           C  
ANISOU 2178  CG  HIS A 737     2708   2644   2193   -941    241    317       C  
ATOM   2179  ND1 HIS A 737      13.227  10.115  16.588  1.00 21.19           N  
ANISOU 2179  ND1 HIS A 737     2852   2810   2391  -1048    273    320       N  
ATOM   2180  CD2 HIS A 737      14.535  11.058  18.061  1.00 21.28           C  
ANISOU 2180  CD2 HIS A 737     2989   2834   2261  -1016    279    360       C  
ATOM   2181  CE1 HIS A 737      12.848   9.687  17.783  1.00 22.65           C  
ANISOU 2181  CE1 HIS A 737     3116   3006   2485  -1189    341    363       C  
ATOM   2182  NE2 HIS A 737      13.635  10.243  18.691  1.00 22.72           N  
ANISOU 2182  NE2 HIS A 737     3208   3024   2399  -1172    343    390       N  
ATOM   2183  N   PRO A 738      17.274  10.574  12.889  1.00 15.73           N  
ANISOU 2183  N   PRO A 738     2167   1930   1880   -561    -83    278       N  
ATOM   2184  CA  PRO A 738      17.859  11.139  11.690  1.00 15.08           C  
ANISOU 2184  CA  PRO A 738     2031   1857   1843   -451   -116    230       C  
ATOM   2185  C   PRO A 738      16.803  11.629  10.684  1.00 14.88           C  
ANISOU 2185  C   PRO A 738     1900   1895   1857   -437    -86    179       C  
ATOM   2186  O   PRO A 738      17.171  12.266   9.693  1.00 14.73           O  
ANISOU 2186  O   PRO A 738     1843   1895   1857   -356   -107    146       O  
ATOM   2187  CB  PRO A 738      18.646   9.960  11.089  1.00 15.27           C  
ANISOU 2187  CB  PRO A 738     2112   1785   1907   -429   -204    234       C  
ATOM   2188  CG  PRO A 738      18.004   8.747  11.634  1.00 16.18           C  
ANISOU 2188  CG  PRO A 738     2282   1843   2021   -534   -217    276       C  
ATOM   2189  CD  PRO A 738      17.575   9.144  13.041  1.00 16.93           C  
ANISOU 2189  CD  PRO A 738     2411   1980   2042   -613   -153    324       C  
ATOM   2190  N   TYR A 739      15.518  11.370  10.954  1.00 15.40           N  
ANISOU 2190  N   TYR A 739     1920   1997   1933   -520    -40    174       N  
ATOM   2191  CA  TYR A 739      14.481  11.998  10.169  1.00 15.56           C  
ANISOU 2191  CA  TYR A 739     1828   2085   1999   -500    -20    123       C  
ATOM   2192  C   TYR A 739      14.572  13.509  10.207  1.00 14.68           C  
ANISOU 2192  C   TYR A 739     1663   2031   1883   -423     14     99       C  
ATOM   2193  O   TYR A 739      14.124  14.175   9.262  1.00 14.06           O  
ANISOU 2193  O   TYR A 739     1511   1987   1845   -366     -6     64       O  
ATOM   2194  CB  TYR A 739      13.102  11.577  10.634  1.00 16.33           C  
ANISOU 2194  CB  TYR A 739     1867   2219   2119   -605     36    110       C  
ATOM   2195  CG  TYR A 739      11.980  11.976   9.703  1.00 16.55           C  
ANISOU 2195  CG  TYR A 739     1768   2305   2216   -586     29     51       C  
ATOM   2196  CD1 TYR A 739      11.907  11.434   8.420  1.00 17.02           C  
ANISOU 2196  CD1 TYR A 739     1816   2339   2313   -560    -52     31       C  
ATOM   2197  CD2 TYR A 739      10.943  12.800  10.129  1.00 17.15           C  
ANISOU 2197  CD2 TYR A 739     1735   2457   2325   -600     98      8       C  
ATOM   2198  CE1 TYR A 739      10.867  11.780   7.559  1.00 17.24           C  
ANISOU 2198  CE1 TYR A 739     1733   2418   2401   -543    -79    -20       C  
ATOM   2199  CE2 TYR A 739       9.870  13.112   9.289  1.00 17.71           C  
ANISOU 2199  CE2 TYR A 739     1680   2574   2475   -578     74    -49       C  
ATOM   2200  CZ  TYR A 739       9.877  12.615   7.986  1.00 17.97           C  
ANISOU 2200  CZ  TYR A 739     1714   2580   2535   -548    -24    -56       C  
ATOM   2201  OH  TYR A 739       8.822  12.884   7.105  1.00 18.70           O  
ANISOU 2201  OH  TYR A 739     1688   2715   2701   -527    -71   -109       O  
ATOM   2202  N   SER A 740      15.163  14.098  11.261  1.00 14.47           N  
ANISOU 2202  N   SER A 740     1679   2011   1808   -419     56    119       N  
ATOM   2203  CA  SER A 740      15.304  15.568  11.240  1.00 13.80           C  
ANISOU 2203  CA  SER A 740     1547   1968   1729   -342     83     91       C  
ATOM   2204  C   SER A 740      16.133  16.031  10.064  1.00 13.13           C  
ANISOU 2204  C   SER A 740     1469   1860   1659   -249     21     88       C  
ATOM   2205  O   SER A 740      15.906  17.136   9.536  1.00 13.38           O  
ANISOU 2205  O   SER A 740     1448   1919   1717   -187     21     64       O  
ATOM   2206  CB  SER A 740      15.867  16.099  12.530  1.00 14.50           C  
ANISOU 2206  CB  SER A 740     1685   2064   1760   -356    132    103       C  
ATOM   2207  OG  SER A 740      17.208  15.613  12.676  1.00 13.86           O  
ANISOU 2207  OG  SER A 740     1702   1924   1641   -339     77    145       O  
ATOM   2208  N   ASN A 741      17.132  15.242   9.654  1.00 12.32           N  
ANISOU 2208  N   ASN A 741     1436   1704   1541   -238    -32    109       N  
ATOM   2209  CA  ASN A 741      17.916  15.594   8.481  1.00 11.91           C  
ANISOU 2209  CA  ASN A 741     1391   1639   1496   -166    -75     96       C  
ATOM   2210  C   ASN A 741      17.082  15.615   7.204  1.00 11.96           C  
ANISOU 2210  C   ASN A 741     1345   1670   1531   -152   -108     72       C  
ATOM   2211  O   ASN A 741      17.275  16.482   6.323  1.00 12.81           O  
ANISOU 2211  O   ASN A 741     1440   1794   1635    -96   -126     64       O  
ATOM   2212  CB  ASN A 741      19.134  14.669   8.304  1.00 11.90           C  
ANISOU 2212  CB  ASN A 741     1457   1577   1486   -158   -118    103       C  
ATOM   2213  CG  ASN A 741      20.164  14.806   9.423  1.00 12.14           C  
ANISOU 2213  CG  ASN A 741     1539   1580   1492   -153   -111    126       C  
ATOM   2214  OD1 ASN A 741      20.419  15.907   9.952  1.00 12.00           O  
ANISOU 2214  OD1 ASN A 741     1512   1591   1457   -129    -77    127       O  
ATOM   2215  ND2 ASN A 741      20.742  13.678   9.810  1.00 12.72           N  
ANISOU 2215  ND2 ASN A 741     1670   1592   1570   -175   -154    143       N  
ATOM   2216  N   VAL A 742      16.170  14.677   7.103  1.00 12.28           N  
ANISOU 2216  N   VAL A 742     1362   1711   1595   -209   -121     63       N  
ATOM   2217  CA  VAL A 742      15.194  14.655   5.981  1.00 12.74           C  
ANISOU 2217  CA  VAL A 742     1361   1798   1683   -204   -163     35       C  
ATOM   2218  C   VAL A 742      14.320  15.910   6.010  1.00 13.08           C  
ANISOU 2218  C   VAL A 742     1322   1892   1757   -170   -148     23       C  
ATOM   2219  O   VAL A 742      14.100  16.541   4.958  1.00 13.32           O  
ANISOU 2219  O   VAL A 742     1329   1938   1794   -119   -199     15       O  
ATOM   2220  CB  VAL A 742      14.351  13.359   6.009  1.00 13.69           C  
ANISOU 2220  CB  VAL A 742     1464   1905   1832   -285   -177     22       C  
ATOM   2221  CG1 VAL A 742      13.308  13.354   4.952  1.00 14.42           C  
ANISOU 2221  CG1 VAL A 742     1487   2032   1960   -285   -227    -12       C  
ATOM   2222  CG2 VAL A 742      15.266  12.122   5.858  1.00 13.52           C  
ANISOU 2222  CG2 VAL A 742     1529   1814   1796   -306   -208     29       C  
ATOM   2223  N   LEU A 743      13.836  16.283   7.181  1.00 13.50           N  
ANISOU 2223  N   LEU A 743     1335   1968   1828   -196    -82     18       N  
ATOM   2224  CA  LEU A 743      12.996  17.490   7.309  1.00 14.26           C  
ANISOU 2224  CA  LEU A 743     1340   2105   1973   -155    -64    -10       C  
ATOM   2225  C   LEU A 743      13.761  18.711   6.777  1.00 13.31           C  
ANISOU 2225  C   LEU A 743     1252   1969   1838    -67    -92      6       C  
ATOM   2226  O   LEU A 743      13.224  19.514   5.990  1.00 12.94           O  
ANISOU 2226  O   LEU A 743     1158   1931   1829    -13   -143     -3       O  
ATOM   2227  CB  LEU A 743      12.537  17.712   8.736  1.00 14.73           C  
ANISOU 2227  CB  LEU A 743     1362   2193   2041   -201     29    -30       C  
ATOM   2228  CG  LEU A 743      11.517  16.741   9.247  1.00 15.94           C  
ANISOU 2228  CG  LEU A 743     1466   2374   2219   -299     71    -52       C  
ATOM   2229  CD1 LEU A 743      11.296  16.810  10.760  1.00 16.45           C  
ANISOU 2229  CD1 LEU A 743     1528   2468   2256   -369    180    -64       C  
ATOM   2230  CD2 LEU A 743      10.205  16.974   8.541  1.00 16.99           C  
ANISOU 2230  CD2 LEU A 743     1469   2545   2442   -284     39   -103       C  
ATOM   2231  N   TRP A 744      15.020  18.859   7.186  1.00 12.44           N  
ANISOU 2231  N   TRP A 744     1222   1830   1675    -56    -67     32       N  
ATOM   2232  CA  TRP A 744      15.804  19.982   6.688  1.00 12.08           C  
ANISOU 2232  CA  TRP A 744     1209   1766   1614     10    -86     48       C  
ATOM   2233  C   TRP A 744      16.070  19.937   5.245  1.00 12.42           C  
ANISOU 2233  C   TRP A 744     1285   1799   1636     37   -154     63       C  
ATOM   2234  O   TRP A 744      16.014  20.978   4.592  1.00 12.18           O  
ANISOU 2234  O   TRP A 744     1254   1763   1612     85   -187     76       O  
ATOM   2235  CB  TRP A 744      17.117  20.184   7.476  1.00 12.07           C  
ANISOU 2235  CB  TRP A 744     1276   1741   1571     11    -44     63       C  
ATOM   2236  CG  TRP A 744      16.807  20.789   8.806  1.00 12.43           C  
ANISOU 2236  CG  TRP A 744     1292   1802   1629      1     19     44       C  
ATOM   2237  CD1 TRP A 744      16.857  20.173  10.028  1.00 12.29           C  
ANISOU 2237  CD1 TRP A 744     1294   1792   1582    -58     67     42       C  
ATOM   2238  CD2 TRP A 744      16.379  22.141   9.046  1.00 12.59           C  
ANISOU 2238  CD2 TRP A 744     1265   1827   1691     47     39     19       C  
ATOM   2239  NE1 TRP A 744      16.476  21.042  11.008  1.00 13.01           N  
ANISOU 2239  NE1 TRP A 744     1353   1907   1683    -57    127     10       N  
ATOM   2240  CE2 TRP A 744      16.184  22.269  10.421  1.00 13.43           C  
ANISOU 2240  CE2 TRP A 744     1358   1955   1790     13    110    -10       C  
ATOM   2241  CE3 TRP A 744      16.148  23.250   8.214  1.00 12.96           C  
ANISOU 2241  CE3 TRP A 744     1287   1856   1780    113     -3     20       C  
ATOM   2242  CZ2 TRP A 744      15.750  23.476  11.007  1.00 13.81           C  
ANISOU 2242  CZ2 TRP A 744     1356   2010   1879     47    151    -55       C  
ATOM   2243  CZ3 TRP A 744      15.722  24.444   8.798  1.00 13.63           C  
ANISOU 2243  CZ3 TRP A 744     1326   1935   1918    152     25    -15       C  
ATOM   2244  CH2 TRP A 744      15.490  24.531  10.165  1.00 14.02           C  
ANISOU 2244  CH2 TRP A 744     1349   2010   1969    121    105    -61       C  
ATOM   2245  N   LEU A 745      16.364  18.765   4.700  1.00 12.21           N  
ANISOU 2245  N   LEU A 745     1294   1766   1579      3   -178     61       N  
ATOM   2246  CA  LEU A 745      16.552  18.637   3.266  1.00 12.45           C  
ANISOU 2246  CA  LEU A 745     1359   1797   1574     16   -237     63       C  
ATOM   2247  C   LEU A 745      15.277  18.963   2.468  1.00 13.14           C  
ANISOU 2247  C   LEU A 745     1392   1910   1691     31   -306     58       C  
ATOM   2248  O   LEU A 745      15.371  19.527   1.390  1.00 13.45           O  
ANISOU 2248  O   LEU A 745     1466   1951   1695     59   -360     76       O  
ATOM   2249  CB  LEU A 745      17.045  17.242   2.880  1.00 12.55           C  
ANISOU 2249  CB  LEU A 745     1413   1795   1560    -23   -247     43       C  
ATOM   2250  CG  LEU A 745      18.480  16.935   3.347  1.00 12.68           C  
ANISOU 2250  CG  LEU A 745     1486   1779   1553    -22   -206     43       C  
ATOM   2251  CD1 LEU A 745      18.756  15.473   3.309  1.00 13.20           C  
ANISOU 2251  CD1 LEU A 745     1575   1814   1625    -57   -219     17       C  
ATOM   2252  CD2 LEU A 745      19.529  17.703   2.486  1.00 12.84           C  
ANISOU 2252  CD2 LEU A 745     1551   1801   1525     11   -199     45       C  
ATOM   2253  N   HIS A 746      14.122  18.675   3.052  1.00 13.29           N  
ANISOU 2253  N   HIS A 746     1326   1948   1774      9   -303     35       N  
ATOM   2254  CA  HIS A 746      12.839  19.023   2.415  1.00 13.94           C  
ANISOU 2254  CA  HIS A 746     1331   2055   1909     30   -376     19       C  
ATOM   2255  C   HIS A 746      12.652  20.539   2.418  1.00 14.45           C  
ANISOU 2255  C   HIS A 746     1371   2109   2008    102   -396     36       C  
ATOM   2256  O   HIS A 746      12.259  21.128   1.406  1.00 15.16           O  
ANISOU 2256  O   HIS A 746     1464   2194   2100    143   -489     53       O  
ATOM   2257  CB  HIS A 746      11.690  18.320   3.145  1.00 14.46           C  
ANISOU 2257  CB  HIS A 746     1297   2149   2049    -21   -350    -23       C  
ATOM   2258  CG  HIS A 746      10.362  18.522   2.490  1.00 15.74           C  
ANISOU 2258  CG  HIS A 746     1360   2338   2282     -3   -432    -53       C  
ATOM   2259  ND1 HIS A 746       9.391  19.325   3.034  1.00 16.69           N  
ANISOU 2259  ND1 HIS A 746     1365   2478   2498     29   -423    -86       N  
ATOM   2260  CD2 HIS A 746       9.874  18.090   1.307  1.00 16.46           C  
ANISOU 2260  CD2 HIS A 746     1448   2440   2366     -8   -533    -61       C  
ATOM   2261  CE1 HIS A 746       8.345  19.373   2.219  1.00 18.14           C  
ANISOU 2261  CE1 HIS A 746     1470   2681   2743     49   -523   -112       C  
ATOM   2262  NE2 HIS A 746       8.599  18.593   1.177  1.00 17.99           N  
ANISOU 2262  NE2 HIS A 746     1520   2659   2657     22   -594    -95       N  
ATOM   2263  N   TYR A 747      12.967  21.172   3.540  1.00 14.17           N  
ANISOU 2263  N   TYR A 747     1324   2064   1997    116   -319     32       N  
ATOM   2264  CA  TYR A 747      12.968  22.636   3.598  1.00 14.26           C  
ANISOU 2264  CA  TYR A 747     1326   2048   2045    185   -333     44       C  
ATOM   2265  C   TYR A 747      13.908  23.288   2.537  1.00 14.12           C  
ANISOU 2265  C   TYR A 747     1415   1994   1955    214   -385    101       C  
ATOM   2266  O   TYR A 747      13.519  24.241   1.886  1.00 14.73           O  
ANISOU 2266  O   TYR A 747     1493   2046   2058    265   -461    125       O  
ATOM   2267  CB  TYR A 747      13.283  23.120   5.047  1.00 14.03           C  
ANISOU 2267  CB  TYR A 747     1277   2015   2039    183   -231     20       C  
ATOM   2268  CG  TYR A 747      13.936  24.499   5.083  1.00 13.72           C  
ANISOU 2268  CG  TYR A 747     1281   1929   2002    241   -232     42       C  
ATOM   2269  CD1 TYR A 747      15.304  24.621   4.887  1.00 13.22           C  
ANISOU 2269  CD1 TYR A 747     1321   1840   1862    230   -213     83       C  
ATOM   2270  CD2 TYR A 747      13.181  25.689   5.256  1.00 14.69           C  
ANISOU 2270  CD2 TYR A 747     1336   2027   2217    306   -257     17       C  
ATOM   2271  CE1 TYR A 747      15.925  25.818   4.832  1.00 13.11           C  
ANISOU 2271  CE1 TYR A 747     1351   1780   1850    268   -215    106       C  
ATOM   2272  CE2 TYR A 747      13.839  26.942   5.267  1.00 14.53           C  
ANISOU 2272  CE2 TYR A 747     1369   1949   2203    353   -262     41       C  
ATOM   2273  CZ  TYR A 747      15.192  26.991   5.004  1.00 14.06           C  
ANISOU 2273  CZ  TYR A 747     1420   1867   2055    328   -243     90       C  
ATOM   2274  OH  TYR A 747      15.896  28.173   4.954  1.00 14.66           O  
ANISOU 2274  OH  TYR A 747     1553   1883   2133    358   -246    117       O  
ATOM   2275  N   LEU A 748      15.106  22.726   2.352  1.00 13.66           N  
ANISOU 2275  N   LEU A 748     1445   1934   1812    177   -346    120       N  
ATOM   2276  CA  LEU A 748      16.061  23.197   1.339  1.00 13.32           C  
ANISOU 2276  CA  LEU A 748     1501   1869   1690    182   -372    164       C  
ATOM   2277  C   LEU A 748      15.571  22.997  -0.059  1.00 14.12           C  
ANISOU 2277  C   LEU A 748     1634   1983   1747    178   -468    183       C  
ATOM   2278  O   LEU A 748      15.672  23.883  -0.888  1.00 14.23           O  
ANISOU 2278  O   LEU A 748     1706   1974   1725    200   -525    229       O  
ATOM   2279  CB  LEU A 748      17.405  22.572   1.572  1.00 12.71           C  
ANISOU 2279  CB  LEU A 748     1483   1793   1553    143   -299    157       C  
ATOM   2280  CG  LEU A 748      18.108  23.102   2.834  1.00 12.85           C  
ANISOU 2280  CG  LEU A 748     1493   1790   1598    151   -222    151       C  
ATOM   2281  CD1 LEU A 748      19.184  22.179   3.352  1.00 12.30           C  
ANISOU 2281  CD1 LEU A 748     1451   1723   1499    116   -166    130       C  
ATOM   2282  CD2 LEU A 748      18.653  24.486   2.594  1.00 13.49           C  
ANISOU 2282  CD2 LEU A 748     1619   1835   1673    180   -223    184       C  
ATOM   2283  N   THR A 749      14.944  21.862  -0.315  1.00 14.07           N  
ANISOU 2283  N   THR A 749     1592   2011   1744    147   -496    149       N  
ATOM   2284  CA  THR A 749      14.374  21.591  -1.632  1.00 14.87           C  
ANISOU 2284  CA  THR A 749     1719   2131   1800    140   -598    157       C  
ATOM   2285  C   THR A 749      13.252  22.561  -1.942  1.00 15.71           C  
ANISOU 2285  C   THR A 749     1776   2224   1970    195   -702    180       C  
ATOM   2286  O   THR A 749      13.120  23.092  -3.065  1.00 16.06           O  
ANISOU 2286  O   THR A 749     1885   2258   1959    209   -802    224       O  
ATOM   2287  CB  THR A 749      13.900  20.091  -1.708  1.00 14.81           C  
ANISOU 2287  CB  THR A 749     1672   2156   1799     89   -603    104       C  
ATOM   2288  OG1 THR A 749      14.984  19.220  -1.380  1.00 13.69           O  
ANISOU 2288  OG1 THR A 749     1578   2010   1615     50   -518     82       O  
ATOM   2289  CG2 THR A 749      13.325  19.736  -3.078  1.00 15.70           C  
ANISOU 2289  CG2 THR A 749     1815   2293   1858     74   -714    101       C  
ATOM   2290  N   ASP A 750      12.427  22.806  -0.930  1.00 15.97           N  
ANISOU 2290  N   ASP A 750     1693   2254   2120    226   -683    147       N  
ATOM   2291  CA  ASP A 750      11.358  23.784  -1.025  1.00 17.74           C  
ANISOU 2291  CA  ASP A 750     1843   2457   2441    293   -775    150       C  
ATOM   2292  C   ASP A 750      11.897  25.210  -1.365  1.00 17.62           C  
ANISOU 2292  C   ASP A 750     1911   2380   2406    346   -813    216       C  
ATOM   2293  O   ASP A 750      11.353  25.895  -2.234  1.00 18.66           O  
ANISOU 2293  O   ASP A 750     2062   2480   2547    389   -942    256       O  
ATOM   2294  CB  ASP A 750      10.611  23.760   0.312  1.00 18.29           C  
ANISOU 2294  CB  ASP A 750     1773   2542   2636    305   -702     84       C  
ATOM   2295  CG  ASP A 750       9.395  24.540   0.318  1.00 19.67           C  
ANISOU 2295  CG  ASP A 750     1834   2703   2937    374   -785     56       C  
ATOM   2296  OD1 ASP A 750       8.342  24.015  -0.111  1.00 21.93           O  
ANISOU 2296  OD1 ASP A 750     2033   3021   3277    370   -863     20       O  
ATOM   2297  OD2 ASP A 750       9.428  25.713   0.766  1.00 21.03           O  
ANISOU 2297  OD2 ASP A 750     1992   2828   3172    438   -779     60       O  
ATOM   2298  N   LYS A 751      13.005  25.611  -0.724  1.00 17.07           N  
ANISOU 2298  N   LYS A 751     1898   2286   2304    335   -708    230       N  
ATOM   2299  CA  LYS A 751      13.659  26.866  -1.073  1.00 17.55           C  
ANISOU 2299  CA  LYS A 751     2049   2282   2335    363   -732    294       C  
ATOM   2300  C   LYS A 751      14.118  26.868  -2.538  1.00 17.95           C  
ANISOU 2300  C   LYS A 751     2234   2331   2256    329   -807    362       C  
ATOM   2301  O   LYS A 751      13.892  27.868  -3.262  1.00 18.28           O  
ANISOU 2301  O   LYS A 751     2337   2319   2290    362   -910    427       O  
ATOM   2302  CB  LYS A 751      14.860  27.163  -0.162  1.00 16.73           C  
ANISOU 2302  CB  LYS A 751     1982   2162   2212    343   -603    290       C  
ATOM   2303  CG  LYS A 751      14.522  27.626   1.254  1.00 16.77           C  
ANISOU 2303  CG  LYS A 751     1889   2152   2330    380   -537    235       C  
ATOM   2304  CD  LYS A 751      13.933  29.043   1.266  1.00 18.29           C  
ANISOU 2304  CD  LYS A 751     2059   2272   2619    458   -608    249       C  
ATOM   2305  CE  LYS A 751      13.500  29.471   2.678  1.00 18.79           C  
ANISOU 2305  CE  LYS A 751     2014   2329   2797    495   -534    171       C  
ATOM   2306  NZ  LYS A 751      12.085  29.056   3.052  1.00 20.02           N  
ANISOU 2306  NZ  LYS A 751     2022   2526   3058    524   -555     98       N  
ATOM   2307  N   MET A 752      14.711  25.759  -2.981  1.00 17.60           N  
ANISOU 2307  N   MET A 752     2236   2341   2110    262   -760    346       N  
ATOM   2308  CA  MET A 752      15.182  25.693  -4.379  1.00 19.18           C  
ANISOU 2308  CA  MET A 752     2566   2553   2169    215   -813    395       C  
ATOM   2309  C   MET A 752      14.036  25.875  -5.358  1.00 20.08           C  
ANISOU 2309  C   MET A 752     2686   2664   2279    242   -978    427       C  
ATOM   2310  O   MET A 752      14.168  26.546  -6.381  1.00 20.91           O  
ANISOU 2310  O   MET A 752     2907   2742   2294    232  -1062    500       O  
ATOM   2311  CB  MET A 752      15.923  24.376  -4.688  1.00 19.50           C  
ANISOU 2311  CB  MET A 752     2639   2654   2117    145   -735    347       C  
ATOM   2312  CG  MET A 752      17.132  24.081  -3.848  1.00 20.29           C  
ANISOU 2312  CG  MET A 752     2735   2756   2217    119   -592    314       C  
ATOM   2313  SD  MET A 752      18.398  25.313  -4.173  1.00 22.66           S  
ANISOU 2313  SD  MET A 752     3149   3017   2444     97   -540    376       S  
ATOM   2314  CE  MET A 752      19.714  24.503  -3.277  1.00 22.61           C  
ANISOU 2314  CE  MET A 752     3109   3033   2448     65   -391    307       C  
ATOM   2315  N   LEU A 753      12.885  25.314  -5.053  1.00 19.52           N  
ANISOU 2315  N   LEU A 753     2492   2617   2305    272  -1032    374       N  
ATOM   2316  CA  LEU A 753      11.766  25.362  -5.976  1.00 21.07           C  
ANISOU 2316  CA  LEU A 753     2678   2818   2510    297  -1201    391       C  
ATOM   2317  C   LEU A 753      10.938  26.629  -5.907  1.00 22.07           C  
ANISOU 2317  C   LEU A 753     2763   2876   2749    387  -1322    431       C  
ATOM   2318  O   LEU A 753      10.265  26.985  -6.882  1.00 22.88           O  
ANISOU 2318  O   LEU A 753     2904   2959   2831    412  -1489    477       O  
ATOM   2319  CB  LEU A 753      10.874  24.133  -5.747  1.00 20.92           C  
ANISOU 2319  CB  LEU A 753     2536   2859   2555    281  -1211    307       C  
ATOM   2320  CG  LEU A 753      11.507  22.836  -6.235  1.00 20.48           C  
ANISOU 2320  CG  LEU A 753     2543   2858   2380    197  -1151    272       C  
ATOM   2321  CD1 LEU A 753      10.629  21.698  -5.706  1.00 20.47           C  
ANISOU 2321  CD1 LEU A 753     2408   2897   2474    179  -1141    188       C  
ATOM   2322  CD2 LEU A 753      11.649  22.792  -7.762  1.00 21.80           C  
ANISOU 2322  CD2 LEU A 753     2846   3044   2392    158  -1256    313       C  
ATOM   2323  N   LYS A 754      10.982  27.328  -4.782  1.00 21.91           N  
ANISOU 2323  N   LYS A 754     2668   2812   2846    437  -1249    412       N  
ATOM   2324  CA  LYS A 754      10.087  28.410  -4.499  1.00 23.61           C  
ANISOU 2324  CA  LYS A 754     2803   2959   3208    533  -1348    416       C  
ATOM   2325  C   LYS A 754      10.691  29.786  -4.292  1.00 24.43           C  
ANISOU 2325  C   LYS A 754     2986   2968   3330    573  -1342    478       C  
ATOM   2326  O   LYS A 754      10.043  30.795  -4.655  1.00 25.31           O  
ANISOU 2326  O   LYS A 754     3098   2998   3520    649  -1487    520       O  
ATOM   2327  CB  LYS A 754       9.241  28.084  -3.262  1.00 24.09           C  
ANISOU 2327  CB  LYS A 754     2668   3050   3435    570  -1280    309       C  
ATOM   2328  CG  LYS A 754       8.344  26.859  -3.470  1.00 24.71           C  
ANISOU 2328  CG  LYS A 754     2645   3208   3536    538  -1314    244       C  
ATOM   2329  CD  LYS A 754       7.517  26.648  -2.235  1.00 25.67           C  
ANISOU 2329  CD  LYS A 754     2578   3358   3818    561  -1234    141       C  
ATOM   2330  CE  LYS A 754       6.658  25.408  -2.398  1.00 26.67           C  
ANISOU 2330  CE  LYS A 754     2603   3560   3970    513  -1256     77       C  
ATOM   2331  NZ  LYS A 754       5.946  25.166  -1.117  1.00 27.11           N  
ANISOU 2331  NZ  LYS A 754     2484   3650   4165    512  -1147    -23       N  
ATOM   2332  N   GLN A 755      11.881  29.866  -3.736  1.00 23.52           N  
ANISOU 2332  N   GLN A 755     2932   2850   3153    526  -1193    484       N  
ATOM   2333  CA AGLN A 755      12.512  31.149  -3.408  0.50 24.65           C  
ANISOU 2333  CA AGLN A 755     3142   2901   3324    554  -1170    531       C  
ATOM   2334  CA BGLN A 755      12.479  31.157  -3.435  0.50 24.25           C  
ANISOU 2334  CA BGLN A 755     3090   2849   3274    555  -1176    533       C  
ATOM   2335  C   GLN A 755      13.752  31.440  -4.234  1.00 24.31           C  
ANISOU 2335  C   GLN A 755     3283   2838   3115    477  -1145    623       C  
ATOM   2336  O   GLN A 755      14.039  32.596  -4.528  1.00 25.95           O  
ANISOU 2336  O   GLN A 755     3584   2952   3322    492  -1198    698       O  
ATOM   2337  CB AGLN A 755      12.855  31.217  -1.927  0.50 24.32           C  
ANISOU 2337  CB AGLN A 755     3006   2864   3369    565  -1018    453       C  
ATOM   2338  CB BGLN A 755      12.657  31.330  -1.922  0.50 23.49           C  
ANISOU 2338  CB BGLN A 755     2887   2750   3287    580  -1037    451       C  
ATOM   2339  CG AGLN A 755      11.656  31.012  -1.027  0.50 25.77           C  
ANISOU 2339  CG AGLN A 755     3007   3072   3711    628  -1017    354       C  
ATOM   2340  CG BGLN A 755      11.312  31.364  -1.184  0.50 24.61           C  
ANISOU 2340  CG BGLN A 755     2850   2898   3605    660  -1072    362       C  
ATOM   2341  CD AGLN A 755      11.128  32.291  -0.446  0.50 27.85           C  
ANISOU 2341  CD AGLN A 755     3207   3246   4130    722  -1058    330       C  
ATOM   2342  CD BGLN A 755      11.471  31.407   0.339  0.50 24.10           C  
ANISOU 2342  CD BGLN A 755     2686   2849   3621    666   -920    271       C  
ATOM   2343  OE1AGLN A 755      11.435  32.631   0.705  0.50 28.41           O  
ANISOU 2343  OE1AGLN A 755     3229   3307   4260    731   -942    270       O  
ATOM   2344  OE1BGLN A 755      10.772  30.709   1.084  0.50 24.31           O  
ANISOU 2344  OE1BGLN A 755     2580   2942   3715    665   -863    183       O  
ATOM   2345  NE2AGLN A 755      10.348  33.011  -1.218  0.50 29.61           N  
ANISOU 2345  NE2AGLN A 755     3432   3397   4421    794  -1228    371       N  
ATOM   2346  NE2BGLN A 755      12.376  32.244   0.798  0.50 24.06           N  
ANISOU 2346  NE2BGLN A 755     2751   2785   3605    665   -856    292       N  
ATOM   2347  N   MET A 756      14.459  30.418  -4.673  1.00 23.28           N  
ANISOU 2347  N   MET A 756     3209   2789   2848    390  -1069    615       N  
ATOM   2348  CA  MET A 756      15.610  30.674  -5.565  1.00 23.74           C  
ANISOU 2348  CA  MET A 756     3437   2839   2743    307  -1038    691       C  
ATOM   2349  C   MET A 756      15.115  31.118  -6.918  1.00 24.24           C  
ANISOU 2349  C   MET A 756     3619   2870   2720    300  -1203    785       C  
ATOM   2350  O   MET A 756      14.062  30.666  -7.416  1.00 24.03           O  
ANISOU 2350  O   MET A 756     3551   2870   2710    333  -1330    775       O  
ATOM   2351  CB  MET A 756      16.508  29.453  -5.753  1.00 24.14           C  
ANISOU 2351  CB  MET A 756     3512   2986   2675    219   -914    644       C  
ATOM   2352  CG  MET A 756      17.064  28.821  -4.475  1.00 24.29           C  
ANISOU 2352  CG  MET A 756     3427   3041   2762    217   -764    556       C  
ATOM   2353  SD  MET A 756      18.131  29.831  -3.478  1.00 25.47           S  
ANISOU 2353  SD  MET A 756     3586   3129   2961    218   -653    562       S  
ATOM   2354  CE  MET A 756      19.566  29.842  -4.532  1.00 25.65           C  
ANISOU 2354  CE  MET A 756     3760   3172   2813    109   -582    608       C  
ATOM   2355  N   THR A 757      15.876  32.018  -7.545  1.00 23.74           N  
ANISOU 2355  N   THR A 757     3713   2747   2560    250  -1210    880       N  
ATOM   2356  CA  THR A 757      15.533  32.453  -8.860  1.00 25.18           C  
ANISOU 2356  CA  THR A 757     4041   2897   2631    225  -1365    984       C  
ATOM   2357  C   THR A 757      16.807  32.404  -9.691  1.00 25.55           C  
ANISOU 2357  C   THR A 757     4257   2978   2471     93  -1267   1035       C  
ATOM   2358  O   THR A 757      17.867  32.916  -9.243  1.00 24.86           O  
ANISOU 2358  O   THR A 757     4203   2862   2380     48  -1136   1042       O  
ATOM   2359  CB  THR A 757      14.890  33.879  -8.864  1.00 26.25           C  
ANISOU 2359  CB  THR A 757     4210   2890   2873    308  -1522   1070       C  
ATOM   2360  OG1 THR A 757      14.570  34.228 -10.190  1.00 27.58           O  
ANISOU 2360  OG1 THR A 757     4538   3025   2915    277  -1689   1183       O  
ATOM   2361  CG2 THR A 757      15.790  34.897  -8.234  1.00 25.94           C  
ANISOU 2361  CG2 THR A 757     4215   2765   2877    294  -1424   1100       C  
ATOM   2362  N   PHE A 758      16.727  31.692 -10.795  1.00 25.93           N  
ANISOU 2362  N   PHE A 758     4391   3100   2359     27  -1311   1047       N  
ATOM   2363  CA  PHE A 758      17.891  31.293 -11.545  1.00 26.59           C  
ANISOU 2363  CA  PHE A 758     4601   3255   2247   -105  -1186   1050       C  
ATOM   2364  C   PHE A 758      18.149  32.173 -12.752  1.00 28.65           C  
ANISOU 2364  C   PHE A 758     5081   3469   2336   -190  -1267   1185       C  
ATOM   2365  O   PHE A 758      17.215  32.727 -13.395  1.00 28.75           O  
ANISOU 2365  O   PHE A 758     5171   3420   2333   -152  -1469   1278       O  
ATOM   2366  CB  PHE A 758      17.754  29.812 -11.950  1.00 26.40           C  
ANISOU 2366  CB  PHE A 758     4532   3353   2147   -138  -1154    953       C  
ATOM   2367  CG  PHE A 758      17.689  28.905 -10.789  1.00 25.02           C  
ANISOU 2367  CG  PHE A 758     4169   3219   2119    -80  -1057    831       C  
ATOM   2368  CD1 PHE A 758      18.864  28.517 -10.130  1.00 23.87           C  
ANISOU 2368  CD1 PHE A 758     3980   3107   1983   -120   -866    762       C  
ATOM   2369  CD2 PHE A 758      16.469  28.518 -10.237  1.00 24.92           C  
ANISOU 2369  CD2 PHE A 758     4015   3203   2251     15  -1154    787       C  
ATOM   2370  CE1 PHE A 758      18.809  27.723  -9.030  1.00 23.12           C  
ANISOU 2370  CE1 PHE A 758     3730   3039   2018    -70   -791    664       C  
ATOM   2371  CE2 PHE A 758      16.435  27.721  -9.090  1.00 23.96           C  
ANISOU 2371  CE2 PHE A 758     3733   3113   2258     54  -1055    685       C  
ATOM   2372  CZ  PHE A 758      17.600  27.317  -8.499  1.00 22.89           C  
ANISOU 2372  CZ  PHE A 758     3579   3006   2112     12   -881    630       C  
ATOM   2373  N   LYS A 759      19.437  32.288 -13.088  1.00 29.88           N  
ANISOU 2373  N   LYS A 759     5340   3655   2356   -312  -1110   1195       N  
ATOM   2374  CA  LYS A 759      19.868  33.165 -14.202  1.00 32.98           C  
ANISOU 2374  CA  LYS A 759     5960   4006   2564   -424  -1150   1329       C  
ATOM   2375  C   LYS A 759      19.361  32.659 -15.534  1.00 33.66           C  
ANISOU 2375  C   LYS A 759     6178   4158   2454   -484  -1266   1365       C  
ATOM   2376  O   LYS A 759      18.967  33.454 -16.417  1.00 35.42           O  
ANISOU 2376  O   LYS A 759     6576   4314   2567   -518  -1423   1503       O  
ATOM   2377  CB  LYS A 759      21.392  33.300 -14.247  1.00 35.11           C  
ANISOU 2377  CB  LYS A 759     6291   4312   2736   -556   -931   1309       C  
ATOM   2378  CG  LYS A 759      21.952  34.007 -13.032  1.00 36.56           C  
ANISOU 2378  CG  LYS A 759     6378   4418   3096   -512   -836   1293       C  
ATOM   2379  CD  LYS A 759      23.466  34.243 -13.159  1.00 39.78           C  
ANISOU 2379  CD  LYS A 759     6849   4856   3409   -652   -632   1279       C  
ATOM   2380  CE  LYS A 759      24.262  32.928 -13.025  1.00 40.47           C  
ANISOU 2380  CE  LYS A 759     6827   5085   3464   -693   -453   1124       C  
ATOM   2381  NZ  LYS A 759      25.736  33.201 -12.959  1.00 42.47           N  
ANISOU 2381  NZ  LYS A 759     7098   5364   3676   -811   -253   1090       N  
ATOM   2382  N   THR A 760      19.368  31.329 -15.666  1.00 32.55           N  
ANISOU 2382  N   THR A 760     5957   4141   2270   -498  -1197   1242       N  
ATOM   2383  CA  THR A 760      18.763  30.601 -16.792  1.00 34.01           C  
ANISOU 2383  CA  THR A 760     6226   4403   2292   -539  -1308   1237       C  
ATOM   2384  C   THR A 760      17.615  29.680 -16.306  1.00 33.14           C  
ANISOU 2384  C   THR A 760     5936   4323   2334   -418  -1410   1145       C  
ATOM   2385  O   THR A 760      17.809  28.836 -15.416  1.00 30.56           O  
ANISOU 2385  O   THR A 760     5438   4040   2132   -375  -1287   1020       O  
ATOM   2386  CB  THR A 760      19.825  29.748 -17.493  1.00 34.73           C  
ANISOU 2386  CB  THR A 760     6388   4621   2186   -679  -1125   1153       C  
ATOM   2387  OG1 THR A 760      20.817  30.627 -18.022  1.00 36.41           O  
ANISOU 2387  OG1 THR A 760     6772   4813   2249   -807  -1032   1240       O  
ATOM   2388  CG2 THR A 760      19.228  28.975 -18.673  1.00 36.43           C  
ANISOU 2388  CG2 THR A 760     6700   4922   2221   -730  -1233   1135       C  
ATOM   2389  N   LYS A 761      16.427  29.840 -16.893  1.00 34.76           N  
ANISOU 2389  N   LYS A 761     6181   4499   2527   -369  -1640   1207       N  
ATOM   2390  CA  LYS A 761      15.271  29.070 -16.452  1.00 34.87           C  
ANISOU 2390  CA  LYS A 761     6019   4535   2696   -261  -1746   1124       C  
ATOM   2391  C   LYS A 761      15.349  27.751 -17.203  1.00 36.13           C  
ANISOU 2391  C   LYS A 761     6201   4821   2707   -339  -1707   1026       C  
ATOM   2392  O   LYS A 761      16.264  27.527 -17.972  1.00 36.07           O  
ANISOU 2392  O   LYS A 761     6333   4876   2496   -462  -1599   1021       O  
ATOM   2393  CB  LYS A 761      13.941  29.809 -16.788  1.00 36.56           C  
ANISOU 2393  CB  LYS A 761     6248   4663   2978   -171  -2023   1221       C  
ATOM   2394  CG  LYS A 761      13.860  31.240 -16.270  1.00 36.87           C  
ANISOU 2394  CG  LYS A 761     6304   4561   3145    -99  -2089   1329       C  
ATOM   2395  CD  LYS A 761      13.449  31.394 -14.845  1.00 35.28           C  
ANISOU 2395  CD  LYS A 761     5879   4307   3217     30  -2046   1257       C  
ATOM   2396  CE  LYS A 761      13.185  32.858 -14.468  1.00 35.82           C  
ANISOU 2396  CE  LYS A 761     5971   4223   3418    112  -2152   1360       C  
ATOM   2397  NZ  LYS A 761      14.218  33.268 -13.485  1.00 33.95           N  
ANISOU 2397  NZ  LYS A 761     5697   3955   3248     96  -1944   1334       N  
ATOM   2398  N   CYS A 762      14.336  26.904 -17.015  1.00 38.29           N  
ANISOU 2398  N   CYS A 762     6336   5127   3084   -272  -1802    946       N  
ATOM   2399  CA  CYS A 762      14.256  25.615 -17.691  1.00 40.57           C  
ANISOU 2399  CA  CYS A 762     6635   5523   3258   -335  -1789    843       C  
ATOM   2400  C   CYS A 762      13.600  25.811 -19.035  1.00 42.89           C  
ANISOU 2400  C   CYS A 762     7092   5834   3371   -381  -1998    918       C  
ATOM   2401  O   CYS A 762      12.379  25.636 -19.213  1.00 44.53           O  
ANISOU 2401  O   CYS A 762     7236   6032   3651   -316  -2198    917       O  
ATOM   2402  CB  CYS A 762      13.519  24.594 -16.812  1.00 41.03           C  
ANISOU 2402  CB  CYS A 762     6471   5603   3516   -255  -1783    720       C  
ATOM   2403  SG  CYS A 762      14.306  24.463 -15.213  1.00 42.24           S  
ANISOU 2403  SG  CYS A 762     6460   5728   3860   -208  -1556    653       S  
ATOM   2404  N   ASN A 763      14.409  26.251 -19.989  1.00 43.09           N  
ANISOU 2404  N   ASN A 763     7335   5880   3157   -499  -1957    991       N  
ATOM   2405  CA  ASN A 763      13.896  26.531 -21.317  1.00 45.46           C  
ANISOU 2405  CA  ASN A 763     7830   6195   3247   -561  -2156   1081       C  
ATOM   2406  C   ASN A 763      13.900  25.308 -22.243  1.00 46.96           C  
ANISOU 2406  C   ASN A 763     8077   6510   3254   -654  -2142    970       C  
ATOM   2407  O   ASN A 763      13.108  25.262 -23.192  1.00 49.53           O  
ANISOU 2407  O   ASN A 763     8506   6856   3455   -676  -2351   1011       O  
ATOM   2408  CB  ASN A 763      14.646  27.719 -21.968  1.00 46.47           C  
ANISOU 2408  CB  ASN A 763     8194   6276   3187   -656  -2146   1235       C  
ATOM   2409  CG  ASN A 763      14.572  28.995 -21.121  1.00 45.21           C  
ANISOU 2409  CG  ASN A 763     7991   5975   3211   -562  -2185   1348       C  
ATOM   2410  OD1 ASN A 763      13.464  29.459 -20.772  1.00 45.17           O  
ANISOU 2410  OD1 ASN A 763     7897   5884   3380   -434  -2390   1397       O  
ATOM   2411  ND2 ASN A 763      15.744  29.555 -20.747  1.00 43.70           N  
ANISOU 2411  ND2 ASN A 763     7846   5758   3000   -622  -1987   1376       N  
ATOM   2412  N   THR A 764      14.795  24.357 -22.009  1.00 45.87           N  
ANISOU 2412  N   THR A 764     7883   6451   3097   -710  -1910    830       N  
ATOM   2413  CA  THR A 764      14.903  23.184 -22.893  1.00 47.37           C  
ANISOU 2413  CA  THR A 764     8130   6754   3113   -802  -1877    707       C  
ATOM   2414  C   THR A 764      14.147  21.998 -22.268  1.00 45.95           C  
ANISOU 2414  C   THR A 764     7737   6592   3128   -719  -1905    568       C  
ATOM   2415  O   THR A 764      13.928  21.982 -21.060  1.00 43.25           O  
ANISOU 2415  O   THR A 764     7206   6193   3034   -615  -1865    547       O  
ATOM   2416  CB  THR A 764      16.368  22.784 -23.112  1.00 47.35           C  
ANISOU 2416  CB  THR A 764     8195   6826   2971   -918  -1606    619       C  
ATOM   2417  OG1 THR A 764      16.926  22.361 -21.899  1.00 45.31           O  
ANISOU 2417  OG1 THR A 764     7744   6545   2927   -851  -1426    527       O  
ATOM   2418  CG2 THR A 764      17.193  23.962 -23.658  1.00 48.83           C  
ANISOU 2418  CG2 THR A 764     8584   6996   2972  -1019  -1548    753       C  
ATOM   2419  N   PRO A 765      13.721  21.001 -23.100  1.00 47.48           N  
ANISOU 2419  N   PRO A 765     7968   6866   3205   -773  -1976    471       N  
ATOM   2420  CA  PRO A 765      13.096  19.793 -22.498  1.00 46.40           C  
ANISOU 2420  CA  PRO A 765     7633   6742   3255   -712  -1980    329       C  
ATOM   2421  C   PRO A 765      13.974  19.099 -21.460  1.00 44.55           C  
ANISOU 2421  C   PRO A 765     7255   6502   3168   -690  -1736    217       C  
ATOM   2422  O   PRO A 765      13.470  18.694 -20.410  1.00 43.58           O  
ANISOU 2422  O   PRO A 765     6942   6336   3279   -602  -1735    175       O  
ATOM   2423  CB  PRO A 765      12.789  18.896 -23.725  1.00 48.26           C  
ANISOU 2423  CB  PRO A 765     7978   7069   3292   -804  -2064    239       C  
ATOM   2424  CG  PRO A 765      12.707  19.849 -24.874  1.00 50.29           C  
ANISOU 2424  CG  PRO A 765     8468   7342   3300   -876  -2207    375       C  
ATOM   2425  CD  PRO A 765      13.712  20.942 -24.569  1.00 49.64           C  
ANISOU 2425  CD  PRO A 765     8465   7215   3181   -894  -2067    487       C  
ATOM   2426  N   ALA A 766      15.280  19.048 -21.684  1.00 44.74           N  
ANISOU 2426  N   ALA A 766     7366   6565   3068   -769  -1534    177       N  
ATOM   2427  CA  ALA A 766      16.188  18.447 -20.714  1.00 43.13           C  
ANISOU 2427  CA  ALA A 766     7031   6349   3007   -744  -1317     75       C  
ATOM   2428  C   ALA A 766      16.176  19.183 -19.339  1.00 41.30           C  
ANISOU 2428  C   ALA A 766     6663   6028   3002   -639  -1286    155       C  
ATOM   2429  O   ALA A 766      16.232  18.572 -18.291  1.00 39.68           O  
ANISOU 2429  O   ALA A 766     6298   5792   2986   -578  -1207     85       O  
ATOM   2430  CB  ALA A 766      17.595  18.444 -21.274  1.00 44.15           C  
ANISOU 2430  CB  ALA A 766     7276   6536   2961   -848  -1117     23       C  
ATOM   2431  N   MET A 767      16.121  20.509 -19.375  1.00 42.50           N  
ANISOU 2431  N   MET A 767     6892   6134   3122   -627  -1350    303       N  
ATOM   2432  CA  MET A 767      16.042  21.297 -18.152  1.00 41.18           C  
ANISOU 2432  CA  MET A 767     6609   5881   3157   -530  -1335    377       C  
ATOM   2433  C   MET A 767      14.648  21.158 -17.504  1.00 38.86           C  
ANISOU 2433  C   MET A 767     6162   5543   3060   -424  -1497    383       C  
ATOM   2434  O   MET A 767      14.546  21.072 -16.272  1.00 35.57           O  
ANISOU 2434  O   MET A 767     5585   5082   2846   -348  -1436    358       O  
ATOM   2435  CB  MET A 767      16.393  22.770 -18.403  1.00 44.24           C  
ANISOU 2435  CB  MET A 767     7128   6220   3461   -550  -1360    528       C  
ATOM   2436  CG  MET A 767      17.888  23.062 -18.573  1.00 46.28           C  
ANISOU 2436  CG  MET A 767     7480   6504   3599   -643  -1152    521       C  
ATOM   2437  SD  MET A 767      18.989  22.758 -17.170  1.00 51.00           S  
ANISOU 2437  SD  MET A 767     7911   7081   4385   -600   -920    432       S  
ATOM   2438  CE  MET A 767      18.015  23.095 -15.686  1.00 47.01           C  
ANISOU 2438  CE  MET A 767     7216   6481   4163   -449  -1012    471       C  
ATOM   2439  N   LYS A 768      13.581  21.110 -18.292  1.00 39.99           N  
ANISOU 2439  N   LYS A 768     6346   5702   3147   -424  -1699    408       N  
ATOM   2440  CA  LYS A 768      12.249  20.848 -17.716  1.00 39.86           C  
ANISOU 2440  CA  LYS A 768     6161   5656   3326   -333  -1842    387       C  
ATOM   2441  C   LYS A 768      12.224  19.476 -16.988  1.00 38.77           C  
ANISOU 2441  C   LYS A 768     5868   5544   3318   -327  -1731    243       C  
ATOM   2442  O   LYS A 768      11.539  19.331 -15.979  1.00 36.88           O  
ANISOU 2442  O   LYS A 768     5459   5269   3284   -254  -1746    222       O  
ATOM   2443  CB  LYS A 768      11.124  21.017 -18.742  1.00 42.78           C  
ANISOU 2443  CB  LYS A 768     6598   6041   3618   -335  -2093    432       C  
ATOM   2444  CG  LYS A 768      10.903  22.503 -19.102  1.00 44.09           C  
ANISOU 2444  CG  LYS A 768     6874   6140   3736   -302  -2238    594       C  
ATOM   2445  CD  LYS A 768       9.578  22.780 -19.807  1.00 46.94           C  
ANISOU 2445  CD  LYS A 768     7248   6489   4099   -263  -2523    646       C  
ATOM   2446  CE  LYS A 768       9.514  24.214 -20.376  1.00 48.42           C  
ANISOU 2446  CE  LYS A 768     7597   6604   4197   -247  -2678    817       C  
ATOM   2447  NZ  LYS A 768       9.708  25.313 -19.371  1.00 47.22           N  
ANISOU 2447  NZ  LYS A 768     7376   6348   4215   -160  -2626    893       N  
ATOM   2448  N   GLN A 769      13.020  18.515 -17.466  1.00 39.44           N  
ANISOU 2448  N   GLN A 769     6016   5686   3284   -408  -1612    145       N  
ATOM   2449  CA  GLN A 769      13.133  17.198 -16.825  1.00 39.35           C  
ANISOU 2449  CA  GLN A 769     5880   5683   3388   -408  -1506     13       C  
ATOM   2450  C   GLN A 769      13.801  17.246 -15.460  1.00 36.35           C  
ANISOU 2450  C   GLN A 769     5389   5253   3167   -358  -1343      7       C  
ATOM   2451  O   GLN A 769      13.364  16.577 -14.540  1.00 34.68           O  
ANISOU 2451  O   GLN A 769     5037   5016   3124   -320  -1323    -46       O  
ATOM   2452  CB  GLN A 769      13.919  16.233 -17.734  1.00 42.09           C  
ANISOU 2452  CB  GLN A 769     6331   6094   3569   -501  -1419    -99       C  
ATOM   2453  CG  GLN A 769      14.110  14.825 -17.177  1.00 42.70           C  
ANISOU 2453  CG  GLN A 769     6300   6164   3760   -504  -1319   -239       C  
ATOM   2454  CD  GLN A 769      12.781  14.131 -16.849  1.00 45.44           C  
ANISOU 2454  CD  GLN A 769     6521   6493   4252   -474  -1450   -276       C  
ATOM   2455  OE1 GLN A 769      11.782  14.277 -17.583  1.00 48.15           O  
ANISOU 2455  OE1 GLN A 769     6890   6863   4542   -485  -1627   -254       O  
ATOM   2456  NE2 GLN A 769      12.762  13.372 -15.739  1.00 46.11           N  
ANISOU 2456  NE2 GLN A 769     6468   6531   4518   -443  -1369   -332       N  
ATOM   2457  N   ILE A 770      14.913  17.993 -15.343  1.00 34.34           N  
ANISOU 2457  N   ILE A 770     5207   4988   2851   -369  -1223     56       N  
ATOM   2458  CA  ILE A 770      15.575  18.177 -14.063  1.00 32.06           C  
ANISOU 2458  CA  ILE A 770     4824   4654   2705   -322  -1085     59       C  
ATOM   2459  C   ILE A 770      14.595  18.791 -13.088  1.00 29.12           C  
ANISOU 2459  C   ILE A 770     4331   4227   2507   -237  -1167    123       C  
ATOM   2460  O   ILE A 770      14.506  18.331 -11.960  1.00 27.32           O  
ANISOU 2460  O   ILE A 770     3976   3971   2432   -198  -1103     83       O  
ATOM   2461  CB  ILE A 770      16.867  19.026 -14.185  1.00 33.20           C  
ANISOU 2461  CB  ILE A 770     5066   4796   2752   -354   -960    106       C  
ATOM   2462  CG1 ILE A 770      17.928  18.235 -14.961  1.00 34.49           C  
ANISOU 2462  CG1 ILE A 770     5310   5020   2776   -438   -838      5       C  
ATOM   2463  CG2 ILE A 770      17.448  19.363 -12.811  1.00 31.74           C  
ANISOU 2463  CG2 ILE A 770     4780   4559   2722   -299   -845    119       C  
ATOM   2464  CD1 ILE A 770      18.819  19.100 -15.844  1.00 36.57           C  
ANISOU 2464  CD1 ILE A 770     5729   5316   2851   -515   -777     57       C  
ATOM   2465  N   LYS A 771      13.829  19.784 -13.554  1.00 29.41           N  
ANISOU 2465  N   LYS A 771     4410   4248   2517   -210  -1316    217       N  
ATOM   2466  CA  LYS A 771      12.819  20.461 -12.721  1.00 29.13           C  
ANISOU 2466  CA  LYS A 771     4253   4160   2656   -121  -1407    267       C  
ATOM   2467  C   LYS A 771      11.807  19.450 -12.216  1.00 27.83           C  
ANISOU 2467  C   LYS A 771     3936   4009   2630   -102  -1449    184       C  
ATOM   2468  O   LYS A 771      11.523  19.413 -11.021  1.00 25.95           O  
ANISOU 2468  O   LYS A 771     3563   3742   2556    -55  -1392    165       O  
ATOM   2469  CB  LYS A 771      12.107  21.574 -13.475  1.00 32.25           C  
ANISOU 2469  CB  LYS A 771     4721   4530   3002    -93  -1589    371       C  
ATOM   2470  CG  LYS A 771      11.153  22.352 -12.606  1.00 34.03           C  
ANISOU 2470  CG  LYS A 771     4813   4696   3423      7  -1672    408       C  
ATOM   2471  CD  LYS A 771      10.419  23.414 -13.400  1.00 37.41           C  
ANISOU 2471  CD  LYS A 771     5312   5084   3819     46  -1878    508       C  
ATOM   2472  CE  LYS A 771      10.177  24.648 -12.557  1.00 38.65           C  
ANISOU 2472  CE  LYS A 771     5402   5155   4128    140  -1898    570       C  
ATOM   2473  NZ  LYS A 771       9.257  25.531 -13.334  1.00 41.98           N  
ANISOU 2473  NZ  LYS A 771     5871   5528   4551    191  -2135    655       N  
ATOM   2474  N   ARG A 772      11.339  18.584 -13.115  1.00 28.60           N  
ANISOU 2474  N   ARG A 772     4062   4153   2652   -150  -1534    127       N  
ATOM   2475  CA  ARG A 772      10.378  17.543 -12.729  1.00 29.12           C  
ANISOU 2475  CA  ARG A 772     3989   4231   2844   -150  -1575     42       C  
ATOM   2476  C   ARG A 772      10.987  16.548 -11.725  1.00 27.05           C  
ANISOU 2476  C   ARG A 772     3655   3957   2667   -169  -1403    -34       C  
ATOM   2477  O   ARG A 772      10.315  16.100 -10.793  1.00 25.97           O  
ANISOU 2477  O   ARG A 772     3379   3802   2685   -151  -1389    -68       O  
ATOM   2478  CB  ARG A 772       9.804  16.786 -13.972  1.00 31.74           C  
ANISOU 2478  CB  ARG A 772     4377   4613   3068   -207  -1707    -11       C  
ATOM   2479  CG  ARG A 772       8.845  17.614 -14.833  1.00 35.29           C  
ANISOU 2479  CG  ARG A 772     4863   5070   3475   -180  -1923     58       C  
ATOM   2480  CD  ARG A 772       8.080  16.743 -15.841  1.00 39.31           C  
ANISOU 2480  CD  ARG A 772     5390   5630   3917   -233  -2067    -11       C  
ATOM   2481  NE  ARG A 772       9.018  16.151 -16.806  1.00 41.71           N  
ANISOU 2481  NE  ARG A 772     5860   5981   4008   -321  -2002    -55       N  
ATOM   2482  CZ  ARG A 772       9.308  16.630 -18.027  1.00 44.98           C  
ANISOU 2482  CZ  ARG A 772     6455   6429   4206   -366  -2083     -5       C  
ATOM   2483  NH1 ARG A 772       8.695  17.713 -18.546  1.00 47.84           N  
ANISOU 2483  NH1 ARG A 772     6875   6777   4526   -331  -2264    105       N  
ATOM   2484  NH2 ARG A 772      10.215  15.985 -18.763  1.00 46.09           N  
ANISOU 2484  NH2 ARG A 772     6726   6618   4168   -453  -1985    -72       N  
ATOM   2485  N   LYS A 773      12.252  16.199 -11.899  1.00 26.32           N  
ANISOU 2485  N   LYS A 773     3656   3871   2475   -209  -1276    -61       N  
ATOM   2486  CA  LYS A 773      12.887  15.309 -10.926  1.00 25.67           C  
ANISOU 2486  CA  LYS A 773     3511   3763   2480   -217  -1132   -124       C  
ATOM   2487  C   LYS A 773      13.044  15.951  -9.552  1.00 22.92           C  
ANISOU 2487  C   LYS A 773     3079   3372   2259   -162  -1052    -73       C  
ATOM   2488  O   LYS A 773      12.905  15.268  -8.522  1.00 21.41           O  
ANISOU 2488  O   LYS A 773     2794   3154   2186   -160   -991   -110       O  
ATOM   2489  CB  LYS A 773      14.223  14.798 -11.423  1.00 28.36           C  
ANISOU 2489  CB  LYS A 773     3953   4118   2704   -262  -1020   -178       C  
ATOM   2490  CG  LYS A 773      14.096  13.664 -12.449  1.00 32.28           C  
ANISOU 2490  CG  LYS A 773     4500   4648   3115   -324  -1060   -277       C  
ATOM   2491  CD  LYS A 773      15.478  13.114 -12.881  1.00 36.97           C  
ANISOU 2491  CD  LYS A 773     5177   5255   3613   -364   -930   -356       C  
ATOM   2492  CE  LYS A 773      16.436  12.680 -11.725  1.00 39.50           C  
ANISOU 2492  CE  LYS A 773     5433   5522   4051   -335   -789   -387       C  
ATOM   2493  NZ  LYS A 773      16.818  11.225 -11.664  1.00 42.12           N  
ANISOU 2493  NZ  LYS A 773     5744   5825   4433   -357   -739   -510       N  
ATOM   2494  N   ILE A 774      13.345  17.249  -9.501  1.00 21.29           N  
ANISOU 2494  N   ILE A 774     2912   3152   2025   -123  -1051     10       N  
ATOM   2495  CA  ILE A 774      13.463  17.915  -8.219  1.00 20.29           C  
ANISOU 2495  CA  ILE A 774     2709   2986   2015    -72   -981     49       C  
ATOM   2496  C   ILE A 774      12.058  18.074  -7.599  1.00 19.84           C  
ANISOU 2496  C   ILE A 774     2518   2921   2102    -31  -1063     52       C  
ATOM   2497  O   ILE A 774      11.906  17.973  -6.388  1.00 18.83           O  
ANISOU 2497  O   ILE A 774     2293   2773   2089    -13   -990     38       O  
ATOM   2498  CB  ILE A 774      14.163  19.283  -8.296  1.00 21.06           C  
ANISOU 2498  CB  ILE A 774     2883   3062   2059    -44   -957    131       C  
ATOM   2499  CG1 ILE A 774      15.600  19.111  -8.774  1.00 21.31           C  
ANISOU 2499  CG1 ILE A 774     3023   3107   1965    -93   -850    116       C  
ATOM   2500  CG2 ILE A 774      14.181  19.948  -6.938  1.00 20.00           C  
ANISOU 2500  CG2 ILE A 774     2662   2885   2051      9   -893    158       C  
ATOM   2501  CD1 ILE A 774      16.257  20.442  -9.055  1.00 22.69           C  
ANISOU 2501  CD1 ILE A 774     3289   3264   2069    -88   -834    198       C  
ATOM   2502  N   GLN A 775      11.056  18.335  -8.421  1.00 20.89           N  
ANISOU 2502  N   GLN A 775     2642   3070   2224    -20  -1212     65       N  
ATOM   2503  CA  GLN A 775       9.660  18.399  -7.927  1.00 21.48           C  
ANISOU 2503  CA  GLN A 775     2567   3144   2449     16  -1296     46       C  
ATOM   2504  C   GLN A 775       9.230  17.047  -7.350  1.00 21.16           C  
ANISOU 2504  C   GLN A 775     2430   3119   2488    -35  -1244    -38       C  
ATOM   2505  O   GLN A 775       8.608  16.995  -6.293  1.00 20.40           O  
ANISOU 2505  O   GLN A 775     2207   3016   2528    -23  -1202    -60       O  
ATOM   2506  CB  GLN A 775       8.712  18.851  -9.013  1.00 23.70           C  
ANISOU 2506  CB  GLN A 775     2859   3440   2705     37  -1486     70       C  
ATOM   2507  CG  GLN A 775       8.838  20.325  -9.376  1.00 24.73           C  
ANISOU 2507  CG  GLN A 775     3061   3534   2800     99  -1562    165       C  
ATOM   2508  CD  GLN A 775       8.013  20.696 -10.567  1.00 27.10           C  
ANISOU 2508  CD  GLN A 775     3404   3843   3051    114  -1769    199       C  
ATOM   2509  OE1 GLN A 775       7.821  19.899 -11.486  1.00 28.35           O  
ANISOU 2509  OE1 GLN A 775     3613   4045   3114     58  -1841    165       O  
ATOM   2510  NE2 GLN A 775       7.480  21.943 -10.565  1.00 28.54           N  
ANISOU 2510  NE2 GLN A 775     3566   3976   3303    195  -1883    266       N  
ATOM   2511  N   GLU A 776       9.606  15.971  -8.032  1.00 21.48           N  
ANISOU 2511  N   GLU A 776     2540   3179   2442    -98  -1239    -86       N  
ATOM   2512  CA  GLU A 776       9.328  14.618  -7.554  1.00 22.06           C  
ANISOU 2512  CA  GLU A 776     2548   3250   2584   -155  -1192   -162       C  
ATOM   2513  C   GLU A 776      10.042  14.314  -6.235  1.00 20.38           C  
ANISOU 2513  C   GLU A 776     2312   3001   2432   -161  -1037   -161       C  
ATOM   2514  O   GLU A 776       9.468  13.707  -5.342  1.00 20.25           O  
ANISOU 2514  O   GLU A 776     2200   2974   2522   -190   -998   -190       O  
ATOM   2515  CB  GLU A 776       9.667  13.590  -8.652  1.00 23.85           C  
ANISOU 2515  CB  GLU A 776     2867   3493   2701   -216  -1225   -221       C  
ATOM   2516  CG  GLU A 776       9.144  12.185  -8.383  1.00 25.98           C  
ANISOU 2516  CG  GLU A 776     3071   3751   3048   -280  -1218   -302       C  
ATOM   2517  CD  GLU A 776      10.093  11.257  -7.672  1.00 26.66           C  
ANISOU 2517  CD  GLU A 776     3187   3790   3151   -311  -1085   -333       C  
ATOM   2518  OE1 GLU A 776      11.267  11.653  -7.417  1.00 29.00           O  
ANISOU 2518  OE1 GLU A 776     3554   4070   3396   -281   -994   -302       O  
ATOM   2519  OE2 GLU A 776       9.657  10.107  -7.340  1.00 29.33           O  
ANISOU 2519  OE2 GLU A 776     3477   4102   3565   -367  -1078   -390       O  
ATOM   2520  N   PHE A 777      11.307  14.737  -6.108  1.00 18.83           N  
ANISOU 2520  N   PHE A 777     2206   2787   2163   -140   -951   -127       N  
ATOM   2521  CA  PHE A 777      12.029  14.655  -4.850  1.00 18.03           C  
ANISOU 2521  CA  PHE A 777     2087   2651   2113   -134   -824   -116       C  
ATOM   2522  C   PHE A 777      11.289  15.348  -3.705  1.00 17.32           C  
ANISOU 2522  C   PHE A 777     1889   2556   2135   -103   -802    -88       C  
ATOM   2523  O   PHE A 777      11.046  14.771  -2.656  1.00 16.69           O  
ANISOU 2523  O   PHE A 777     1747   2464   2133   -133   -737   -107       O  
ATOM   2524  CB  PHE A 777      13.445  15.244  -5.070  1.00 17.82           C  
ANISOU 2524  CB  PHE A 777     2166   2614   1992   -111   -758    -85       C  
ATOM   2525  CG  PHE A 777      14.418  15.089  -3.924  1.00 17.29           C  
ANISOU 2525  CG  PHE A 777     2098   2510   1961   -105   -640    -80       C  
ATOM   2526  CD1 PHE A 777      14.835  13.829  -3.486  1.00 17.06           C  
ANISOU 2526  CD1 PHE A 777     2071   2451   1961   -142   -592   -128       C  
ATOM   2527  CD2 PHE A 777      15.018  16.205  -3.348  1.00 16.98           C  
ANISOU 2527  CD2 PHE A 777     2069   2460   1922    -63   -588    -29       C  
ATOM   2528  CE1 PHE A 777      15.798  13.696  -2.511  1.00 16.52           C  
ANISOU 2528  CE1 PHE A 777     2013   2344   1918   -133   -506   -120       C  
ATOM   2529  CE2 PHE A 777      15.978  16.075  -2.364  1.00 16.62           C  
ANISOU 2529  CE2 PHE A 777     2030   2385   1900    -59   -494    -28       C  
ATOM   2530  CZ  PHE A 777      16.361  14.817  -1.915  1.00 15.91           C  
ANISOU 2530  CZ  PHE A 777     1941   2267   1838    -92   -457    -71       C  
ATOM   2531  N   HIS A 778      10.854  16.563  -3.962  1.00 17.92           N  
ANISOU 2531  N   HIS A 778     1945   2644   2221    -47   -863    -48       N  
ATOM   2532  CA  HIS A 778      10.130  17.348  -2.984  1.00 18.52           C  
ANISOU 2532  CA  HIS A 778     1913   2717   2408     -7   -846    -37       C  
ATOM   2533  C   HIS A 778       8.885  16.642  -2.471  1.00 19.03           C  
ANISOU 2533  C   HIS A 778     1843   2803   2584    -45   -856    -92       C  
ATOM   2534  O   HIS A 778       8.599  16.698  -1.295  1.00 19.20           O  
ANISOU 2534  O   HIS A 778     1786   2824   2686    -54   -773   -106       O  
ATOM   2535  CB  HIS A 778       9.727  18.681  -3.632  1.00 19.83           C  
ANISOU 2535  CB  HIS A 778     2080   2879   2574     63   -949      7       C  
ATOM   2536  CG  HIS A 778       9.051  19.640  -2.712  1.00 21.33           C  
ANISOU 2536  CG  HIS A 778     2159   3058   2886    120   -936      7       C  
ATOM   2537  ND1 HIS A 778       7.688  19.708  -2.604  1.00 23.89           N  
ANISOU 2537  ND1 HIS A 778     2344   3402   3331    139  -1006    -36       N  
ATOM   2538  CD2 HIS A 778       9.537  20.634  -1.938  1.00 21.40           C  
ANISOU 2538  CD2 HIS A 778     2175   3037   2920    166   -867     36       C  
ATOM   2539  CE1 HIS A 778       7.361  20.675  -1.770  1.00 24.31           C  
ANISOU 2539  CE1 HIS A 778     2316   3438   3481    196   -972    -41       C  
ATOM   2540  NE2 HIS A 778       8.468  21.278  -1.385  1.00 23.22           N  
ANISOU 2540  NE2 HIS A 778     2273   3268   3283    214   -894      5       N  
ATOM   2541  N   ARG A 779       8.155  15.986  -3.347  1.00 19.84           N  
ANISOU 2541  N   ARG A 779     1922   2928   2688    -77   -955   -128       N  
ATOM   2542  CA  ARG A 779       6.861  15.413  -2.943  1.00 21.04           C  
ANISOU 2542  CA  ARG A 779     1930   3104   2960   -118   -975   -186       C  
ATOM   2543  C   ARG A 779       6.996  14.002  -2.397  1.00 20.32           C  
ANISOU 2543  C   ARG A 779     1842   3000   2877   -212   -892   -223       C  
ATOM   2544  O   ARG A 779       6.000  13.445  -1.927  1.00 21.61           O  
ANISOU 2544  O   ARG A 779     1891   3181   3137   -268   -882   -269       O  
ATOM   2545  CB  ARG A 779       5.826  15.509  -4.070  1.00 23.81           C  
ANISOU 2545  CB  ARG A 779     2227   3485   3334   -103  -1139   -212       C  
ATOM   2546  CG  ARG A 779       6.073  14.654  -5.246  1.00 25.13           C  
ANISOU 2546  CG  ARG A 779     2490   3658   3400   -149  -1216   -230       C  
ATOM   2547  CD  ARG A 779       4.978  14.792  -6.279  1.00 27.89           C  
ANISOU 2547  CD  ARG A 779     2782   4040   3774   -136  -1393   -256       C  
ATOM   2548  NE  ARG A 779       5.347  13.924  -7.377  1.00 29.30           N  
ANISOU 2548  NE  ARG A 779     3073   4227   3833   -189  -1451   -280       N  
ATOM   2549  CZ  ARG A 779       5.781  14.334  -8.559  1.00 29.96           C  
ANISOU 2549  CZ  ARG A 779     3283   4320   3779   -167  -1545   -247       C  
ATOM   2550  NH1 ARG A 779       6.107  13.439  -9.469  1.00 31.45           N  
ANISOU 2550  NH1 ARG A 779     3566   4522   3860   -226  -1577   -289       N  
ATOM   2551  NH2 ARG A 779       5.805  15.618  -8.860  1.00 31.31           N  
ANISOU 2551  NH2 ARG A 779     3486   4487   3923    -92  -1614   -177       N  
ATOM   2552  N   THR A 780       8.187  13.400  -2.514  1.00 18.38           N  
ANISOU 2552  N   THR A 780     1724   2721   2539   -234   -841   -207       N  
ATOM   2553  CA  THR A 780       8.416  12.019  -2.016  1.00 18.11           C  
ANISOU 2553  CA  THR A 780     1711   2652   2516   -317   -777   -236       C  
ATOM   2554  C   THR A 780       9.387  11.881  -0.861  1.00 17.03           C  
ANISOU 2554  C   THR A 780     1629   2475   2368   -325   -656   -201       C  
ATOM   2555  O   THR A 780       9.311  10.921  -0.099  1.00 16.80           O  
ANISOU 2555  O   THR A 780     1594   2413   2376   -395   -602   -210       O  
ATOM   2556  CB  THR A 780       8.917  11.125  -3.161  1.00 18.35           C  
ANISOU 2556  CB  THR A 780     1837   2665   2469   -343   -835   -270       C  
ATOM   2557  OG1 THR A 780      10.125  11.694  -3.733  1.00 17.82           O  
ANISOU 2557  OG1 THR A 780     1883   2593   2294   -288   -825   -241       O  
ATOM   2558  CG2 THR A 780       7.849  10.938  -4.196  1.00 19.70           C  
ANISOU 2558  CG2 THR A 780     1956   2875   2655   -363   -961   -315       C  
ATOM   2559  N   MET A 781      10.287  12.845  -0.695  1.00 16.33           N  
ANISOU 2559  N   MET A 781     1593   2382   2228   -258   -620   -157       N  
ATOM   2560  CA  MET A 781      11.418  12.648   0.208  1.00 15.85           C  
ANISOU 2560  CA  MET A 781     1601   2280   2141   -260   -527   -128       C  
ATOM   2561  C   MET A 781      11.001  12.470   1.676  1.00 16.10           C  
ANISOU 2561  C   MET A 781     1578   2305   2235   -307   -445   -116       C  
ATOM   2562  O   MET A 781      11.721  11.804   2.436  1.00 15.37           O  
ANISOU 2562  O   MET A 781     1546   2166   2128   -340   -391    -98       O  
ATOM   2563  CB  MET A 781      12.431  13.799   0.073  1.00 15.46           C  
ANISOU 2563  CB  MET A 781     1610   2233   2031   -185   -507    -90       C  
ATOM   2564  CG  MET A 781      11.910  15.165   0.483  1.00 16.05           C  
ANISOU 2564  CG  MET A 781     1620   2336   2141   -134   -502    -63       C  
ATOM   2565  SD  MET A 781      12.946  16.466  -0.246  1.00 16.07           S  
ANISOU 2565  SD  MET A 781     1706   2334   2063    -58   -519    -20       S  
ATOM   2566  CE  MET A 781      14.404  16.174   0.748  1.00 15.90           C  
ANISOU 2566  CE  MET A 781     1751   2275   2014    -67   -413     -7       C  
ATOM   2567  N   LEU A 782       9.870  13.062   2.087  1.00 16.92           N  
ANISOU 2567  N   LEU A 782     1570   2452   2405   -310   -438   -129       N  
ATOM   2568  CA  LEU A 782       9.464  12.935   3.495  1.00 17.23           C  
ANISOU 2568  CA  LEU A 782     1561   2497   2488   -367   -342   -125       C  
ATOM   2569  C   LEU A 782       9.055  11.500   3.901  1.00 17.73           C  
ANISOU 2569  C   LEU A 782     1627   2533   2575   -481   -318   -138       C  
ATOM   2570  O   LEU A 782       8.823  11.236   5.079  1.00 18.06           O  
ANISOU 2570  O   LEU A 782     1657   2574   2631   -549   -234   -126       O  
ATOM   2571  CB  LEU A 782       8.317  13.893   3.810  1.00 18.26           C  
ANISOU 2571  CB  LEU A 782     1556   2687   2697   -345   -329   -157       C  
ATOM   2572  CG  LEU A 782       8.701  15.355   3.890  1.00 18.23           C  
ANISOU 2572  CG  LEU A 782     1550   2693   2684   -246   -325   -139       C  
ATOM   2573  CD1 LEU A 782       7.466  16.204   4.168  1.00 19.81           C  
ANISOU 2573  CD1 LEU A 782     1600   2940   2986   -220   -322   -188       C  
ATOM   2574  CD2 LEU A 782       9.778  15.608   4.928  1.00 17.65           C  
ANISOU 2574  CD2 LEU A 782     1560   2594   2552   -243   -234   -101       C  
ATOM   2575  N   ASN A 783       8.917  10.602   2.905  1.00 17.91           N  
ANISOU 2575  N   ASN A 783     1671   2534   2602   -507   -395   -165       N  
ATOM   2576  CA  ASN A 783       8.686   9.184   3.161  1.00 18.39           C  
ANISOU 2576  CA  ASN A 783     1757   2545   2686   -613   -386   -175       C  
ATOM   2577  C   ASN A 783       9.943   8.363   3.266  1.00 18.14           C  
ANISOU 2577  C   ASN A 783     1861   2429   2603   -615   -385   -146       C  
ATOM   2578  O   ASN A 783       9.890   7.147   3.204  1.00 18.82           O  
ANISOU 2578  O   ASN A 783     1987   2454   2710   -686   -405   -157       O  
ATOM   2579  CB  ASN A 783       7.739   8.605   2.086  1.00 19.47           C  
ANISOU 2579  CB  ASN A 783     1830   2698   2869   -649   -474   -235       C  
ATOM   2580  CG  ASN A 783       6.362   9.218   2.171  1.00 20.87           C  
ANISOU 2580  CG  ASN A 783     1850   2951   3127   -663   -477   -273       C  
ATOM   2581  OD1 ASN A 783       5.800   9.356   3.260  1.00 21.48           O  
ANISOU 2581  OD1 ASN A 783     1858   3053   3249   -717   -387   -271       O  
ATOM   2582  ND2 ASN A 783       5.818   9.642   1.036  1.00 21.28           N  
ANISOU 2582  ND2 ASN A 783     1844   3045   3198   -612   -582   -312       N  
ATOM   2583  N   PHE A 784      11.082   9.018   3.440  1.00 17.10           N  
ANISOU 2583  N   PHE A 784     1795   2287   2415   -537   -364   -112       N  
ATOM   2584  CA  PHE A 784      12.358   8.348   3.722  1.00 16.93           C  
ANISOU 2584  CA  PHE A 784     1886   2185   2360   -528   -360    -87       C  
ATOM   2585  C   PHE A 784      12.781   8.613   5.157  1.00 17.17           C  
ANISOU 2585  C   PHE A 784     1950   2200   2373   -543   -289    -29       C  
ATOM   2586  O   PHE A 784      12.462   9.680   5.727  1.00 17.22           O  
ANISOU 2586  O   PHE A 784     1904   2269   2371   -523   -237    -15       O  
ATOM   2587  CB  PHE A 784      13.417   8.805   2.729  1.00 16.20           C  
ANISOU 2587  CB  PHE A 784     1842   2094   2220   -434   -396   -106       C  
ATOM   2588  CG  PHE A 784      13.154   8.312   1.305  1.00 16.77           C  
ANISOU 2588  CG  PHE A 784     1912   2171   2286   -433   -469   -168       C  
ATOM   2589  CD1 PHE A 784      12.083   8.826   0.554  1.00 16.92           C  
ANISOU 2589  CD1 PHE A 784     1856   2259   2312   -433   -513   -193       C  
ATOM   2590  CD2 PHE A 784      13.975   7.381   0.718  1.00 16.94           C  
ANISOU 2590  CD2 PHE A 784     2006   2131   2298   -429   -498   -208       C  
ATOM   2591  CE1 PHE A 784      11.811   8.322  -0.716  1.00 17.53           C  
ANISOU 2591  CE1 PHE A 784     1943   2344   2374   -443   -589   -250       C  
ATOM   2592  CE2 PHE A 784      13.738   6.906  -0.543  1.00 17.81           C  
ANISOU 2592  CE2 PHE A 784     2123   2250   2394   -436   -558   -274       C  
ATOM   2593  CZ  PHE A 784      12.645   7.375  -1.282  1.00 17.92           C  
ANISOU 2593  CZ  PHE A 784     2073   2336   2399   -447   -607   -293       C  
ATOM   2594  N   SER A 785      13.531   7.681   5.729  1.00 17.41           N  
ANISOU 2594  N   SER A 785     2072   2145   2398   -574   -294      1       N  
ATOM   2595  CA ASER A 785      13.763   7.704   7.189  0.50 17.51           C  
ANISOU 2595  CA ASER A 785     2131   2137   2385   -618   -238     63       C  
ATOM   2596  CA BSER A 785      13.803   7.665   7.189  0.50 17.77           C  
ANISOU 2596  CA BSER A 785     2168   2166   2418   -618   -240     64       C  
ATOM   2597  C   SER A 785      15.012   8.458   7.634  1.00 16.70           C  
ANISOU 2597  C   SER A 785     2078   2030   2238   -536   -228     91       C  
ATOM   2598  O   SER A 785      15.142   8.759   8.839  1.00 16.75           O  
ANISOU 2598  O   SER A 785     2114   2042   2209   -565   -182    137       O  
ATOM   2599  CB ASER A 785      13.818   6.282   7.722  0.50 18.45           C  
ANISOU 2599  CB ASER A 785     2332   2155   2522   -708   -262     97       C  
ATOM   2600  CB BSER A 785      14.011   6.233   7.667  0.50 18.96           C  
ANISOU 2600  CB BSER A 785     2409   2209   2586   -696   -271     97       C  
ATOM   2601  OG ASER A 785      14.848   5.548   7.077  0.50 18.59           O  
ANISOU 2601  OG ASER A 785     2419   2085   2560   -653   -337     78       O  
ATOM   2602  OG BSER A 785      12.793   5.553   7.733  0.50 20.86           O  
ANISOU 2602  OG BSER A 785     2612   2452   2863   -807   -256     89       O  
ATOM   2603  N   SER A 786      15.917   8.770   6.710  1.00 15.47           N  
ANISOU 2603  N   SER A 786     1932   1869   2078   -444   -267     60       N  
ATOM   2604  CA  SER A 786      17.186   9.413   7.048  1.00 14.60           C  
ANISOU 2604  CA  SER A 786     1861   1749   1937   -371   -261     76       C  
ATOM   2605  C   SER A 786      17.820   9.949   5.780  1.00 14.11           C  
ANISOU 2605  C   SER A 786     1780   1713   1869   -288   -282     27       C  
ATOM   2606  O   SER A 786      17.385   9.583   4.694  1.00 14.15           O  
ANISOU 2606  O   SER A 786     1765   1727   1885   -292   -313    -16       O  
ATOM   2607  CB  SER A 786      18.122   8.382   7.708  1.00 15.11           C  
ANISOU 2607  CB  SER A 786     2016   1713   2014   -383   -302    105       C  
ATOM   2608  OG  SER A 786      18.367   7.299   6.825  1.00 15.36           O  
ANISOU 2608  OG  SER A 786     2069   1676   2091   -377   -361     62       O  
ATOM   2609  N   ALA A 787      18.856  10.778   5.896  1.00 13.46           N  
ANISOU 2609  N   ALA A 787     1710   1641   1762   -224   -265     31       N  
ATOM   2610  CA  ALA A 787      19.666  11.156   4.729  1.00 13.10           C  
ANISOU 2610  CA  ALA A 787     1662   1611   1703   -161   -276    -15       C  
ATOM   2611  C   ALA A 787      20.316   9.923   4.084  1.00 13.62           C  
ANISOU 2611  C   ALA A 787     1764   1612   1801   -156   -319    -66       C  
ATOM   2612  O   ALA A 787      20.447   9.841   2.874  1.00 13.68           O  
ANISOU 2612  O   ALA A 787     1765   1637   1794   -137   -328   -122       O  
ATOM   2613  CB  ALA A 787      20.722  12.191   5.096  1.00 12.95           C  
ANISOU 2613  CB  ALA A 787     1648   1609   1663   -108   -244     -3       C  
ATOM   2614  N   THR A 788      20.722   8.955   4.914  1.00 13.98           N  
ANISOU 2614  N   THR A 788     1852   1574   1887   -173   -348    -49       N  
ATOM   2615  CA  THR A 788      21.308   7.726   4.362  1.00 15.37           C  
ANISOU 2615  CA  THR A 788     2058   1669   2115   -161   -398   -106       C  
ATOM   2616  C   THR A 788      20.282   6.966   3.437  1.00 16.55           C  
ANISOU 2616  C   THR A 788     2198   1817   2274   -210   -421   -147       C  
ATOM   2617  O   THR A 788      20.638   6.479   2.350  1.00 16.56           O  
ANISOU 2617  O   THR A 788     2201   1805   2286   -187   -439   -227       O  
ATOM   2618  CB  THR A 788      21.779   6.821   5.488  1.00 16.17           C  
ANISOU 2618  CB  THR A 788     2214   1665   2264   -174   -445    -65       C  
ATOM   2619  OG1 THR A 788      22.736   7.516   6.318  1.00 15.60           O  
ANISOU 2619  OG1 THR A 788     2148   1597   2180   -130   -437    -34       O  
ATOM   2620  CG2 THR A 788      22.466   5.569   4.912  1.00 17.85           C  
ANISOU 2620  CG2 THR A 788     2452   1777   2551   -146   -506   -135       C  
ATOM   2621  N   ASP A 789      19.030   6.828   3.923  1.00 17.14           N  
ANISOU 2621  N   ASP A 789     2261   1906   2347   -282   -418   -100       N  
ATOM   2622  CA  ASP A 789      17.940   6.226   3.133  1.00 19.32           C  
ANISOU 2622  CA  ASP A 789     2515   2190   2636   -337   -443   -137       C  
ATOM   2623  C   ASP A 789      17.735   7.003   1.812  1.00 17.74           C  
ANISOU 2623  C   ASP A 789     2274   2080   2387   -301   -439   -189       C  
ATOM   2624  O   ASP A 789      17.615   6.418   0.713  1.00 17.32           O  
ANISOU 2624  O   ASP A 789     2226   2021   2333   -307   -474   -259       O  
ATOM   2625  CB  ASP A 789      16.661   6.213   4.007  1.00 21.67           C  
ANISOU 2625  CB  ASP A 789     2784   2507   2942   -422   -422    -79       C  
ATOM   2626  CG  ASP A 789      15.516   5.376   3.438  1.00 26.18           C  
ANISOU 2626  CG  ASP A 789     3329   3069   3548   -498   -454   -114       C  
ATOM   2627  OD1 ASP A 789      15.797   4.393   2.696  1.00 29.89           O  
ANISOU 2627  OD1 ASP A 789     3834   3473   4049   -500   -504   -171       O  
ATOM   2628  OD2 ASP A 789      14.302   5.632   3.835  1.00 28.35           O  
ANISOU 2628  OD2 ASP A 789     3544   3396   3830   -564   -427    -90       O  
ATOM   2629  N   LEU A 790      17.686   8.311   1.916  1.00 16.32           N  
ANISOU 2629  N   LEU A 790     2061   1977   2163   -267   -403   -155       N  
ATOM   2630  CA  LEU A 790      17.534   9.152   0.739  1.00 16.54           C  
ANISOU 2630  CA  LEU A 790     2068   2081   2135   -235   -408   -184       C  
ATOM   2631  C   LEU A 790      18.654   8.942  -0.235  1.00 16.72           C  
ANISOU 2631  C   LEU A 790     2133   2094   2126   -196   -408   -248       C  
ATOM   2632  O   LEU A 790      18.410   8.698  -1.409  1.00 17.40           O  
ANISOU 2632  O   LEU A 790     2229   2207   2177   -206   -437   -304       O  
ATOM   2633  CB  LEU A 790      17.488  10.640   1.077  1.00 16.59           C  
ANISOU 2633  CB  LEU A 790     2045   2150   2108   -198   -372   -132       C  
ATOM   2634  CG  LEU A 790      16.201  11.180   1.588  1.00 17.40           C  
ANISOU 2634  CG  LEU A 790     2085   2295   2233   -224   -371    -96       C  
ATOM   2635  CD1 LEU A 790      16.433  12.612   2.066  1.00 17.28           C  
ANISOU 2635  CD1 LEU A 790     2052   2318   2198   -176   -331    -54       C  
ATOM   2636  CD2 LEU A 790      15.119  11.099   0.509  1.00 17.17           C  
ANISOU 2636  CD2 LEU A 790     2018   2307   2201   -244   -430   -128       C  
ATOM   2637  N   LEU A 791      19.886   9.017   0.232  1.00 15.95           N  
ANISOU 2637  N   LEU A 791     2056   1962   2041   -155   -376   -250       N  
ATOM   2638  CA  LEU A 791      21.034   8.916  -0.688  1.00 16.22           C  
ANISOU 2638  CA  LEU A 791     2114   1998   2051   -118   -357   -326       C  
ATOM   2639  C   LEU A 791      21.050   7.544  -1.381  1.00 17.37           C  
ANISOU 2639  C   LEU A 791     2281   2090   2231   -137   -394   -414       C  
ATOM   2640  O   LEU A 791      21.277   7.436  -2.580  1.00 18.49           O  
ANISOU 2640  O   LEU A 791     2437   2265   2323   -137   -387   -492       O  
ATOM   2641  CB  LEU A 791      22.374   9.081   0.083  1.00 16.21           C  
ANISOU 2641  CB  LEU A 791     2114   1958   2088    -71   -324   -323       C  
ATOM   2642  CG  LEU A 791      23.612   9.109  -0.737  1.00 16.54           C  
ANISOU 2642  CG  LEU A 791     2157   2011   2117    -35   -287   -408       C  
ATOM   2643  CD1 LEU A 791      23.611  10.379  -1.584  1.00 16.98           C  
ANISOU 2643  CD1 LEU A 791     2215   2162   2073    -39   -240   -397       C  
ATOM   2644  CD2 LEU A 791      24.805   9.019   0.176  1.00 16.63           C  
ANISOU 2644  CD2 LEU A 791     2153   1967   2198     10   -278   -412       C  
ATOM   2645  N   CYS A 792      20.800   6.491  -0.606  1.00 17.28           N  
ANISOU 2645  N   CYS A 792     2278   1988   2299   -160   -432   -403       N  
ATOM   2646  CA  CYS A 792      20.939   5.114  -1.114  1.00 19.44           C  
ANISOU 2646  CA  CYS A 792     2576   2182   2628   -173   -473   -489       C  
ATOM   2647  C   CYS A 792      19.764   4.640  -1.912  1.00 19.73           C  
ANISOU 2647  C   CYS A 792     2613   2240   2644   -232   -512   -521       C  
ATOM   2648  O   CYS A 792      19.943   3.738  -2.759  1.00 20.91           O  
ANISOU 2648  O   CYS A 792     2783   2352   2810   -238   -536   -621       O  
ATOM   2649  CB  CYS A 792      21.205   4.142   0.023  1.00 19.86           C  
ANISOU 2649  CB  CYS A 792     2655   2112   2780   -176   -513   -457       C  
ATOM   2650  SG  CYS A 792      22.793   4.492   0.882  1.00 22.58           S  
ANISOU 2650  SG  CYS A 792     2999   2415   3166    -95   -495   -443       S  
ATOM   2651  N   GLN A 793      18.562   5.167  -1.638  1.00 19.69           N  
ANISOU 2651  N   GLN A 793     2578   2288   2614   -277   -522   -451       N  
ATOM   2652  CA AGLN A 793      17.327   4.604  -2.234  0.50 20.80           C  
ANISOU 2652  CA AGLN A 793     2705   2440   2758   -342   -573   -480       C  
ATOM   2653  CA BGLN A 793      17.331   4.618  -2.237  0.50 20.74           C  
ANISOU 2653  CA BGLN A 793     2697   2433   2749   -341   -572   -479       C  
ATOM   2654  C   GLN A 793      16.566   5.563  -3.148  1.00 20.48           C  
ANISOU 2654  C   GLN A 793     2635   2513   2634   -346   -587   -478       C  
ATOM   2655  O   GLN A 793      15.781   5.107  -3.973  1.00 21.62           O  
ANISOU 2655  O   GLN A 793     2773   2675   2765   -388   -641   -529       O  
ATOM   2656  CB AGLN A 793      16.380   4.044  -1.155  0.50 21.75           C  
ANISOU 2656  CB AGLN A 793     2805   2507   2950   -410   -590   -417       C  
ATOM   2657  CB BGLN A 793      16.396   4.131  -1.150  0.50 21.44           C  
ANISOU 2657  CB BGLN A 793     2765   2474   2907   -407   -587   -414       C  
ATOM   2658  CG AGLN A 793      16.967   2.908  -0.320  0.50 23.54           C  
ANISOU 2658  CG AGLN A 793     3083   2602   3259   -424   -603   -409       C  
ATOM   2659  CG BGLN A 793      17.043   3.167  -0.189  0.50 22.81           C  
ANISOU 2659  CG BGLN A 793     2986   2524   3156   -414   -592   -394       C  
ATOM   2660  CD AGLN A 793      16.120   2.500   0.898  0.50 25.10           C  
ANISOU 2660  CD AGLN A 793     3278   2753   3504   -506   -603   -325       C  
ATOM   2661  CD BGLN A 793      17.259   1.828  -0.836  0.50 24.80           C  
ANISOU 2661  CD BGLN A 793     3278   2681   3464   -430   -642   -485       C  
ATOM   2662  OE1AGLN A 793      14.936   2.784   0.995  0.50 27.03           O  
ANISOU 2662  OE1AGLN A 793     3470   3058   3742   -567   -595   -300       O  
ATOM   2663  OE1BGLN A 793      16.438   1.381  -1.631  0.50 26.29           O  
ANISOU 2663  OE1BGLN A 793     3453   2885   3651   -480   -677   -540       O  
ATOM   2664  NE2AGLN A 793      16.758   1.867   1.849  0.50 25.95           N  
ANISOU 2664  NE2AGLN A 793     3444   2756   3659   -508   -612   -283       N  
ATOM   2665  NE2BGLN A 793      18.372   1.179  -0.501  0.50 26.38           N  
ANISOU 2665  NE2BGLN A 793     3523   2778   3721   -385   -654   -508       N  
ATOM   2666  N   HIS A 794      16.762   6.866  -3.008  1.00 19.01           N  
ANISOU 2666  N   HIS A 794     2434   2396   2395   -304   -552   -420       N  
ATOM   2667  CA  HIS A 794      15.970   7.811  -3.830  1.00 19.18           C  
ANISOU 2667  CA  HIS A 794     2433   2510   2345   -305   -586   -405       C  
ATOM   2668  C   HIS A 794      16.402   7.873  -5.291  1.00 20.05           C  
ANISOU 2668  C   HIS A 794     2597   2664   2356   -298   -605   -475       C  
ATOM   2669  O   HIS A 794      17.590   7.983  -5.583  1.00 20.16           O  
ANISOU 2669  O   HIS A 794     2656   2677   2329   -267   -552   -508       O  
ATOM   2670  CB  HIS A 794      15.913   9.216  -3.258  1.00 17.84           C  
ANISOU 2670  CB  HIS A 794     2233   2388   2156   -265   -555   -321       C  
ATOM   2671  CG  HIS A 794      14.717   9.984  -3.758  1.00 17.80           C  
ANISOU 2671  CG  HIS A 794     2183   2449   2129   -271   -616   -295       C  
ATOM   2672  ND1 HIS A 794      14.635  10.483  -5.029  1.00 18.25           N  
ANISOU 2672  ND1 HIS A 794     2278   2561   2096   -261   -667   -312       N  
ATOM   2673  CD2 HIS A 794      13.537  10.284  -3.165  1.00 17.56           C  
ANISOU 2673  CD2 HIS A 794     2073   2438   2162   -287   -640   -259       C  
ATOM   2674  CE1 HIS A 794      13.464  11.052  -5.210  1.00 18.72           C  
ANISOU 2674  CE1 HIS A 794     2282   2661   2170   -262   -737   -283       C  
ATOM   2675  NE2 HIS A 794      12.765  10.913  -4.099  1.00 18.34           N  
ANISOU 2675  NE2 HIS A 794     2152   2594   2224   -276   -718   -260       N  
ATOM   2676  N   SER A 795      15.417   7.797  -6.205  1.00 21.02           N  
ANISOU 2676  N   SER A 795     2716   2833   2439   -333   -681   -501       N  
ATOM   2677  CA  SER A 795      15.673   7.855  -7.632  1.00 22.24           C  
ANISOU 2677  CA  SER A 795     2935   3040   2477   -341   -709   -565       C  
ATOM   2678  C   SER A 795      16.463   9.078  -8.095  1.00 22.50           C  
ANISOU 2678  C   SER A 795     3018   3131   2401   -306   -665   -526       C  
ATOM   2679  O   SER A 795      17.130   8.997  -9.102  1.00 23.51           O  
ANISOU 2679  O   SER A 795     3214   3291   2429   -318   -644   -589       O  
ATOM   2680  CB  SER A 795      14.354   7.761  -8.456  1.00 23.52           C  
ANISOU 2680  CB  SER A 795     3080   3248   2608   -384   -820   -581       C  
ATOM   2681  OG  SER A 795      13.558   8.922  -8.290  1.00 22.89           O  
ANISOU 2681  OG  SER A 795     2957   3217   2524   -361   -866   -493       O  
ATOM   2682  N   LEU A 796      16.367  10.195  -7.400  1.00 21.47           N  
ANISOU 2682  N   LEU A 796     2856   3013   2287   -270   -648   -430       N  
ATOM   2683  CA  LEU A 796      17.098  11.425  -7.801  1.00 22.27           C  
ANISOU 2683  CA  LEU A 796     3010   3159   2293   -243   -609   -383       C  
ATOM   2684  C   LEU A 796      18.606  11.186  -7.907  1.00 23.23           C  
ANISOU 2684  C   LEU A 796     3174   3268   2385   -236   -507   -440       C  
ATOM   2685  O   LEU A 796      19.256  11.788  -8.742  1.00 24.15           O  
ANISOU 2685  O   LEU A 796     3355   3432   2390   -247   -472   -448       O  
ATOM   2686  CB  LEU A 796      16.856  12.577  -6.822  1.00 21.06           C  
ANISOU 2686  CB  LEU A 796     2808   3001   2191   -202   -597   -281       C  
ATOM   2687  CG  LEU A 796      17.419  13.967  -7.182  1.00 20.79           C  
ANISOU 2687  CG  LEU A 796     2827   2999   2072   -179   -573   -218       C  
ATOM   2688  CD1 LEU A 796      16.812  14.430  -8.499  1.00 22.33           C  
ANISOU 2688  CD1 LEU A 796     3086   3247   2153   -202   -664   -203       C  
ATOM   2689  CD2 LEU A 796      17.220  15.010  -6.081  1.00 20.22           C  
ANISOU 2689  CD2 LEU A 796     2701   2907   2073   -134   -557   -135       C  
ATOM   2690  N   PHE A 797      19.125  10.309  -7.062  1.00 23.95           N  
ANISOU 2690  N   PHE A 797     3228   3293   2578   -222   -464   -480       N  
ATOM   2691  CA  PHE A 797      20.555  10.076  -6.973  1.00 25.46           C  
ANISOU 2691  CA  PHE A 797     3433   3462   2778   -201   -376   -538       C  
ATOM   2692  C   PHE A 797      21.039   8.829  -7.678  1.00 30.46           C  
ANISOU 2692  C   PHE A 797     4088   4071   3413   -219   -364   -669       C  
ATOM   2693  O   PHE A 797      22.125   8.309  -7.326  1.00 34.34           O  
ANISOU 2693  O   PHE A 797     4562   4514   3970   -190   -306   -733       O  
ATOM   2694  CB  PHE A 797      20.951  10.016  -5.522  1.00 23.84           C  
ANISOU 2694  CB  PHE A 797     3177   3192   2690   -163   -347   -494       C  
ATOM   2695  CG  PHE A 797      20.488  11.177  -4.732  1.00 22.40           C  
ANISOU 2695  CG  PHE A 797     2968   3029   2516   -145   -351   -382       C  
ATOM   2696  CD1 PHE A 797      20.752  12.461  -5.134  1.00 21.77           C  
ANISOU 2696  CD1 PHE A 797     2914   3002   2357   -137   -325   -335       C  
ATOM   2697  CD2 PHE A 797      19.708  10.988  -3.596  1.00 20.96           C  
ANISOU 2697  CD2 PHE A 797     2738   2807   2419   -144   -380   -327       C  
ATOM   2698  CE1 PHE A 797      20.272  13.547  -4.421  1.00 20.64           C  
ANISOU 2698  CE1 PHE A 797     2745   2867   2232   -115   -334   -242       C  
ATOM   2699  CE2 PHE A 797      19.279  12.046  -2.868  1.00 20.46           C  
ANISOU 2699  CE2 PHE A 797     2645   2762   2365   -126   -375   -243       C  
ATOM   2700  CZ  PHE A 797      19.535  13.332  -3.265  1.00 20.10           C  
ANISOU 2700  CZ  PHE A 797     2619   2763   2255   -106   -356   -203       C  
ATOM   2701  N   LYS A 798      20.261   8.315  -8.630  1.00 32.75           N  
ANISOU 2701  N   LYS A 798     4411   4388   3646   -262   -424   -720       N  
ATOM   2702  CA  LYS A 798      20.699   7.195  -9.454  1.00 37.09           C  
ANISOU 2702  CA  LYS A 798     4989   4921   4182   -284   -411   -861       C  
ATOM   2703  C   LYS A 798      21.281   7.708 -10.752  1.00 40.21           C  
ANISOU 2703  C   LYS A 798     5453   5407   4418   -315   -359   -920       C  
ATOM   2704  O   LYS A 798      20.963   8.816 -11.200  1.00 41.38           O  
ANISOU 2704  O   LYS A 798     5644   5628   4452   -335   -373   -838       O  
ATOM   2705  CB  LYS A 798      19.550   6.291  -9.812  1.00 37.18           C  
ANISOU 2705  CB  LYS A 798     5003   4913   4212   -325   -505   -898       C  
ATOM   2706  CG  LYS A 798      18.729   5.848  -8.633  1.00 37.56           C  
ANISOU 2706  CG  LYS A 798     4990   4884   4395   -322   -559   -830       C  
ATOM   2707  CD  LYS A 798      19.447   4.866  -7.769  1.00 37.29           C  
ANISOU 2707  CD  LYS A 798     4935   4742   4494   -294   -528   -871       C  
ATOM   2708  CE  LYS A 798      18.460   4.235  -6.791  1.00 38.11           C  
ANISOU 2708  CE  LYS A 798     5001   4772   4709   -321   -589   -812       C  
ATOM   2709  NZ  LYS A 798      19.210   3.681  -5.639  1.00 36.83           N  
ANISOU 2709  NZ  LYS A 798     4826   4504   4662   -287   -562   -794       N  
ATOM   2710  OXT LYS A 798      22.044   6.981 -11.411  1.00 45.03           O  
ANISOU 2710  OXT LYS A 798     6083   6016   5008   -326   -304  -1055       O  
TER    2711      LYS A 798                                                      
ATOM   2712  N   ALA C   1      16.332  32.606   8.030  1.00 26.92           N  
ATOM   2713  CA  ALA C   1      16.604  33.570   9.125  1.00 24.07           C  
ATOM   2714  C   ALA C   1      17.370  32.853  10.235  1.00 20.84           C  
ATOM   2715  O   ALA C   1      17.413  31.633  10.257  1.00 18.74           O  
ATOM   2716  CB  ALA C   1      15.276  34.166   9.680  1.00 25.30           C  
ATOM   2717  N   ARG C   2      17.932  33.604  11.181  1.00 19.17           N  
ATOM   2718  CA  ARG C   2      18.504  32.969  12.359  1.00 19.43           C  
ATOM   2719  C   ARG C   2      17.370  32.361  13.181  1.00 19.32           C  
ATOM   2720  O   ARG C   2      16.260  32.900  13.202  1.00 21.27           O  
ATOM   2721  CB  ARG C   2      19.357  33.940  13.188  1.00 18.70           C  
ATOM   2722  CG  ARG C   2      20.458  34.667  12.366  1.00 19.30           C  
ATOM   2723  CD  ARG C   2      21.406  33.698  11.658  1.00 19.85           C  
ATOM   2724  NE  ARG C   2      21.998  32.822  12.652  1.00 19.55           N  
ATOM   2725  CZ  ARG C   2      22.644  31.622  12.395  1.00 23.12           C  
ATOM   2726  NH1 ARG C   2      23.012  30.793  13.366  1.00 20.69           N  
ATOM   2727  NH2 ARG C   2      22.914  31.354  11.021  1.00 20.82           N  
ATOM   2728  N   LYS C   3      17.646  31.237  13.841  1.00 18.96           N  
ATOM   2729  CA  LYS C   3      16.626  30.530  14.605  1.00 20.03           C  
ATOM   2730  C   LYS C   3      16.106  31.357  15.782  1.00 23.68           C  
ATOM   2731  O   LYS C   3      14.994  31.132  16.250  1.00 23.54           O  
ATOM   2732  CB  LYS C   3      17.136  29.196  15.132  1.00 19.85           C  
ATOM   2733  CG  LYS C   3      18.222  29.270  16.204  1.00 18.40           C  
ATOM   2734  CD  LYS C   3      18.651  27.917  16.691  1.00 18.80           C  
ATOM   2735  CE  LYS C   3      19.658  27.962  17.798  1.00 19.11           C  
ATOM   2736  NZ  LYS C   3      20.897  28.574  17.339  1.00 17.80           N  
ATOM   2737  N   LYS C   4      16.968  32.228  16.313  1.00 24.56           N  
ATOM   2738  CA  LYS C   4      16.616  33.210  17.324  1.00 30.23           C  
ATOM   2739  C   LYS C   4      17.245  34.540  16.942  1.00 31.22           C  
ATOM   2740  O   LYS C   4      18.333  34.555  16.378  1.00 28.26           O  
ATOM   2741  CB  LYS C   4      17.132  32.808  18.699  1.00 32.46           C  
ATOM   2742  CG  LYS C   4      16.543  31.550  19.307  1.00 35.07           C  
ATOM   2743  CD  LYS C   4      17.399  30.992  20.432  1.00 38.32           C  
ATOM   2744  CE  LYS C   4      16.624  30.110  21.388  1.00 40.11           C  
ATOM   2745  NZ  LYS C   4      15.782  30.866  22.314  1.00 40.79           N  
ATOM   2746  N   GLN C   5      16.556  35.647  17.248  1.00 33.06           N  
ATOM   2747  CA  GLN C   5      16.940  36.960  16.751  1.00 36.79           C  
ATOM   2748  C   GLN C   5      17.119  37.969  17.885  1.00 39.74           C  
ATOM   2749  O   GLN C   5      16.579  37.773  18.969  1.00 36.56           O  
ATOM   2750  CB  GLN C   5      15.944  37.451  15.707  1.00 40.03           C  
ATOM   2751  CG  GLN C   5      16.101  36.712  14.381  1.00 43.44           C  
ATOM   2752  CD  GLN C   5      15.190  37.240  13.300  1.00 49.31           C  
ATOM   2753  OE1 GLN C   5      15.413  38.327  12.757  1.00 56.05           O  
ATOM   2754  NE2 GLN C   5      14.152  36.479  12.986  1.00 51.11           N  
ATOM   2755  N   THR C   6      17.917  39.021  17.637  1.00 44.62           N  
ATOM   2756  CA  THR C   6      17.816  40.254  18.400  1.00 49.18           C  
ATOM   2757  C   THR C   6      16.732  41.164  17.827  1.00 57.73           C  
ATOM   2758  O   THR C   6      16.779  41.536  16.655  1.00 56.06           O  
ATOM   2759  CB  THR C   6      19.113  41.070  18.522  1.00 45.70           C  
ATOM   2760  OG1 THR C   6      20.278  40.266  18.295  1.00 41.06           O  
ATOM   2761  CG2 THR C   6      19.210  41.745  19.870  1.00 43.25           C  
HETATM 2762  O3  66N C   7      12.884  41.991  19.940  1.00 78.14           O  
HETATM 2763  N11 66N C   7      15.756  41.515  18.669  1.00 67.80           N  
HETATM 2764  C33 66N C   7      14.585  40.677  18.871  1.00 73.70           C  
HETATM 2765  C35 66N C   7      13.710  40.662  17.620  1.00 73.38           C  
HETATM 2766  C34 66N C   7      13.767  41.138  20.070  1.00 77.84           C  
HETATM 2767  N12 66N C   7      14.076  40.590  21.239  1.00 77.33           N  
TER    2768      66N C   7                                                      
HETATM 2769  C1  MRD A 801      31.524  12.452  22.587  1.00 37.23           C  
HETATM 2770  C2  MRD A 801      32.875  12.908  22.095  1.00 39.41           C  
HETATM 2771  O2  MRD A 801      33.747  11.767  22.080  1.00 38.56           O  
HETATM 2772  CM  MRD A 801      32.697  13.436  20.676  1.00 39.58           C  
HETATM 2773  C3  MRD A 801      33.448  13.955  23.063  1.00 41.37           C  
HETATM 2774  C4  MRD A 801      34.836  14.478  22.657  1.00 45.85           C  
HETATM 2775  O4  MRD A 801      35.753  13.394  22.393  1.00 49.45           O  
HETATM 2776  C5  MRD A 801      35.438  15.380  23.741  1.00 46.61           C  
HETATM 2777 NA    NA A 802      35.107  20.848   4.261  1.00 22.65          NA  
HETATM 2778  S   DMS A 803      26.504   5.074  -1.257  0.80 36.16           S  
HETATM 2779  O   DMS A 803      26.308   3.654  -0.853  0.80 29.62           O  
HETATM 2780  C1  DMS A 803      27.998   5.173  -2.084  0.80 30.78           C  
HETATM 2781  C2  DMS A 803      25.300   5.569  -2.392  0.80 34.22           C  
HETATM 2782  N1  6L5 C 101      31.055  32.438   5.523  1.00 14.17           N  
HETATM 2783  C2  6L5 C 101      32.452  30.380   6.874  1.00 12.30           C  
HETATM 2784  N3  6L5 C 101      29.736  32.510   7.558  1.00 15.21           N  
HETATM 2785  C4  6L5 C 101      29.818  31.786   8.717  1.00 14.04           C  
HETATM 2786  C5  6L5 C 101      28.811  33.608   7.230  1.00 17.78           C  
HETATM 2787  C6  6L5 C 101      27.593  33.200   6.394  1.00 17.59           C  
HETATM 2788  C8  6L5 C 101      26.893  33.887   8.550  1.00 17.46           C  
HETATM 2789  C11 6L5 C 101      26.410  33.907  13.105  1.00 16.72           C  
HETATM 2790  C12 6L5 C 101      25.988  33.305  14.429  1.00 16.62           C  
HETATM 2791  C14 6L5 C 101      26.510  33.016  16.892  1.00 15.88           C  
HETATM 2792  C15 6L5 C 101      25.040  32.987  17.243  1.00 16.35           C  
HETATM 2793  C16 6L5 C 101      23.033  31.606  17.412  1.00 18.59           C  
HETATM 2794  C17 6L5 C 101      22.713  30.119  17.291  1.00 18.92           C  
HETATM 2795  C18 6L5 C 101      21.425  29.653  17.900  1.00 20.09           C  
HETATM 2796  C7  6L5 C 101      26.616  32.800   7.494  1.00 17.12           C  
HETATM 2797  N2  6L5 C 101      33.111  29.365   7.430  1.00 12.10           N  
HETATM 2798  C9  6L5 C 101      26.597  33.380   9.945  1.00 17.11           C  
HETATM 2799  C10 6L5 C 101      25.373  33.678  12.019  1.00 16.71           C  
HETATM 2800  C13 6L5 C 101      26.768  33.839  15.631  1.00 16.43           C  
HETATM 2801  N4  6L5 C 101      30.770  30.890   8.724  1.00 14.09           N  
HETATM 2802  O13 6L5 C 101      24.457  33.993  17.635  1.00 15.75           O  
HETATM 2803  N5  6L5 C 101      25.811  34.134  10.709  1.00 15.90           N  
HETATM 2804  O1  6L5 C 101      27.111  32.341  10.347  1.00 16.74           O  
HETATM 2805  O   6L5 C 101      28.297  34.183   8.426  1.00 17.87           O  
HETATM 2806  O14 6L5 C 101      25.251  32.784   7.056  1.00 17.63           O  
HETATM 2807  O15 6L5 C 101      27.120  34.311   5.639  1.00 20.12           O  
HETATM 2808  C1  6L5 C 101      31.365  31.033   7.483  1.00 13.46           C  
HETATM 2809  C   6L5 C 101      30.739  32.031   6.753  1.00 13.68           C  
HETATM 2810  C3  6L5 C 101      32.099  31.747   5.048  1.00 13.28           C  
HETATM 2811  N   6L5 C 101      32.806  30.776   5.644  1.00 12.25           N  
HETATM 2812  N6  6L5 C 101      24.417  31.827  17.040  1.00 15.93           N  
HETATM 2813  C52 6L5 C 101      22.092  32.458  16.563  1.00 22.58           C  
HETATM 2814  N21 6L5 C 101      21.072  33.041  17.191  1.00 22.58           N  
HETATM 2815  O12 6L5 C 101      22.316  32.609  15.363  1.00 24.24           O  
HETATM 2816  O11 6L5 C 101      20.917  30.239  18.861  1.00 21.36           O  
HETATM 2817  C1  MPD C 102      20.132  29.475  21.959  1.00 39.61           C  
HETATM 2818  C2  MPD C 102      20.445  28.027  22.300  1.00 39.35           C  
HETATM 2819  O2  MPD C 102      19.858  27.751  23.564  1.00 37.06           O  
HETATM 2820  CM  MPD C 102      19.810  27.062  21.299  1.00 37.98           C  
HETATM 2821  C3  MPD C 102      21.964  27.783  22.287  1.00 38.14           C  
HETATM 2822  C4  MPD C 102      22.742  27.986  23.576  1.00 39.47           C  
HETATM 2823  O4  MPD C 102      22.577  26.923  24.521  1.00 40.41           O  
HETATM 2824  C5  MPD C 102      24.237  28.031  23.243  1.00 35.76           C  
HETATM 2825  O   HOH A 901      36.813  21.942  -4.448  1.00 43.97           O  
HETATM 2826  O   HOH A 902      12.403   4.453   4.559  1.00 40.50           O  
HETATM 2827  O   HOH A 903      48.574  42.144  22.176  1.00 46.94           O  
HETATM 2828  O   HOH A 904      28.308  45.171  35.433  1.00 52.13           O  
HETATM 2829  O   HOH A 905      40.594  25.087   6.505  1.00 39.09           O  
HETATM 2830  O   HOH A 906      32.499  37.378   1.702  1.00 32.08           O  
HETATM 2831  O   HOH A 907      33.925  22.322   3.184  1.00 33.59           O  
HETATM 2832  O   HOH A 908      32.129   2.384  19.366  1.00 30.74           O  
HETATM 2833  O   HOH A 909      41.276  21.777  14.148  1.00 44.93           O  
HETATM 2834  O   HOH A 910      23.431  25.430 -14.604  1.00 41.93           O  
HETATM 2835  O   HOH A 911      37.163  20.690   0.675  1.00 42.62           O  
HETATM 2836  O   HOH A 912      34.139  42.148  32.177  1.00 28.59           O  
HETATM 2837  O   HOH A 913      27.123  27.425  19.842  1.00 23.62           O  
HETATM 2838  O   HOH A 914      13.421  12.634  -8.402  1.00 29.52           O  
HETATM 2839  O   HOH A 915      27.713  34.458  24.381  1.00 20.36           O  
HETATM 2840  O   HOH A 916      10.382  28.359   0.111  1.00 34.59           O  
HETATM 2841  O   HOH A 917      14.672  30.218   5.951  1.00 18.69           O  
HETATM 2842  O   HOH A 918      34.798  42.174  35.812  1.00 33.67           O  
HETATM 2843  O   HOH A 919       4.908  27.644   6.973  1.00 45.74           O  
HETATM 2844  O   HOH A 920      24.053  39.708  -0.045  1.00 38.61           O  
HETATM 2845  O   HOH A 921      29.939  11.674 -10.693  1.00 35.22           O  
HETATM 2846  O   HOH A 922      20.336  40.158  -7.209  1.00 39.20           O  
HETATM 2847  O   HOH A 923       3.408  13.617  -2.146  1.00 30.93           O  
HETATM 2848  O   HOH A 924      31.971  25.411   0.335  1.00 16.09           O  
HETATM 2849  O   HOH A 925      25.085  23.500  21.310  1.00 22.63           O  
HETATM 2850  O   HOH A 926      44.790  31.255   9.287  1.00 40.89           O  
HETATM 2851  O   HOH A 927      39.772  28.809   3.589  1.00 17.14           O  
HETATM 2852  O   HOH A 928      17.403  16.248 -17.988  1.00 43.43           O  
HETATM 2853  O   HOH A 929      30.286  34.146   3.515  1.00 25.03           O  
HETATM 2854  O   HOH A 930      30.497   7.698  16.327  1.00 40.85           O  
HETATM 2855  O   HOH A 931      32.790  21.115   0.963  1.00 37.31           O  
HETATM 2856  O   HOH A 932      13.229   4.794  -4.493  1.00 39.48           O  
HETATM 2857  O   HOH A 933       3.015  27.189   9.667  1.00 43.19           O  
HETATM 2858  O   HOH A 934      30.667  14.586   0.397  1.00 26.14           O  
HETATM 2859  O   HOH A 935       6.518  29.876  24.531  1.00 47.02           O  
HETATM 2860  O   HOH A 936       4.803  26.115  19.200  1.00 41.81           O  
HETATM 2861  O   HOH A 937      33.328  44.911   7.569  1.00 21.38           O  
HETATM 2862  O   HOH A 938      33.201  15.300  -0.113  1.00 23.11           O  
HETATM 2863  O   HOH A 939      20.165  29.785  13.163  1.00 17.24           O  
HETATM 2864  O   HOH A 940      36.294  36.344  -0.569  1.00 51.75           O  
HETATM 2865  O   HOH A 941      22.095   6.263  10.951  1.00 30.20           O  
HETATM 2866  O   HOH A 942      47.724  29.040  18.908  1.00 37.56           O  
HETATM 2867  O   HOH A 943      11.679  32.982   3.413  1.00 38.68           O  
HETATM 2868  O   HOH A 944      27.171  30.467  12.301  1.00 29.84           O  
HETATM 2869  O   HOH A 945      27.155   2.531   1.401  1.00 26.68           O  
HETATM 2870  O   HOH A 946      25.443   9.333  -4.578  1.00 21.76           O  
HETATM 2871  O   HOH A 947      38.056  13.692   1.529  1.00 35.39           O  
HETATM 2872  O   HOH A 948      37.471   6.581   1.794  1.00 21.93           O  
HETATM 2873  O   HOH A 949      26.286  26.000 -11.869  1.00 34.67           O  
HETATM 2874  O   HOH A 950      14.206   7.644  11.067  1.00 22.91           O  
HETATM 2875  O   HOH A 951      22.192  27.321  15.086  1.00 18.64           O  
HETATM 2876  O   HOH A 952      18.158  36.391  -0.072  1.00 33.94           O  
HETATM 2877  O   HOH A 953      10.873   9.702  21.330  1.00 39.36           O  
HETATM 2878  O   HOH A 954      20.129  19.520  20.025  1.00 18.83           O  
HETATM 2879  O   HOH A 955      30.782  32.915  34.627  1.00 44.82           O  
HETATM 2880  O   HOH A 956      35.991   3.020  -0.777  1.00 39.88           O  
HETATM 2881  O   HOH A 957      16.155  13.609  19.411  1.00 22.53           O  
HETATM 2882  O   HOH A 958      37.510  11.303  13.372  1.00 29.17           O  
HETATM 2883  O   HOH A 959      23.848  14.522  -8.921  1.00 27.50           O  
HETATM 2884  O   HOH A 960      16.796  26.747 -14.075  1.00 24.86           O  
HETATM 2885  O   HOH A 961      43.655  41.931  29.335  1.00 38.07           O  
HETATM 2886  O   HOH A 962      12.081  15.916  27.255  1.00 41.83           O  
HETATM 2887  O   HOH A 963      18.545  39.337  22.661  1.00 25.91           O  
HETATM 2888  O   HOH A 964      33.989  22.573  11.880  1.00 37.26           O  
HETATM 2889  O   HOH A 965      18.378   2.507   3.896  1.00 50.11           O  
HETATM 2890  O   HOH A 966      13.017  28.254  -8.109  1.00 30.07           O  
HETATM 2891  O   HOH A 967      31.891  38.945  19.203  1.00 19.11           O  
HETATM 2892  O   HOH A 968       7.586  12.621  12.774  1.00 35.35           O  
HETATM 2893  O   HOH A 969      24.314  37.598  23.381  1.00 18.20           O  
HETATM 2894  O   HOH A 970      41.093  21.625 -10.878  1.00 44.84           O  
HETATM 2895  O   HOH A 971      27.433  49.476  22.074  1.00 28.16           O  
HETATM 2896  O   HOH A 972      23.403  18.623 -11.357  1.00 35.00           O  
HETATM 2897  O   HOH A 973      34.141   8.529   9.834  1.00 16.06           O  
HETATM 2898  O   HOH A 974      25.803  37.662  30.756  1.00 24.52           O  
HETATM 2899  O   HOH A 975      30.207  19.062  -0.694  1.00 20.11           O  
HETATM 2900  O   HOH A 976      26.595  26.581  31.734  1.00 34.47           O  
HETATM 2901  O   HOH A 977      28.980  44.942   4.362  1.00 55.01           O  
HETATM 2902  O   HOH A 978      41.100  30.405  16.644  1.00 21.81           O  
HETATM 2903  O   HOH A 979      27.636  43.348  20.709  1.00 19.53           O  
HETATM 2904  O   HOH A 980       5.768  20.387  17.827  1.00 29.14           O  
HETATM 2905  O   HOH A 981      21.165  40.700  11.384  1.00 42.81           O  
HETATM 2906  O   HOH A 982      34.944  12.504  13.347  1.00 19.69           O  
HETATM 2907  O   HOH A 983      30.103  25.597  14.241  1.00 28.23           O  
HETATM 2908  O   HOH A 984      26.865   9.041  -6.889  1.00 30.91           O  
HETATM 2909  O   HOH A 985      27.596  34.539   2.784  1.00 33.78           O  
HETATM 2910  O   HOH A 986      14.142  10.845 -10.109  1.00 33.62           O  
HETATM 2911  O   HOH A 987      17.831  36.187   6.825  1.00 47.57           O  
HETATM 2912  O   HOH A 988      13.045  18.777  29.807  1.00 44.17           O  
HETATM 2913  O   HOH A 989      12.313  32.915 -10.929  1.00 31.28           O  
HETATM 2914  O   HOH A 990      24.509  31.671  29.712  1.00 29.46           O  
HETATM 2915  O   HOH A 991      32.642  21.323  10.643  1.00 22.09           O  
HETATM 2916  O   HOH A 992      42.295  43.297  23.178  1.00 27.52           O  
HETATM 2917  O   HOH A 993      22.596  42.039   8.775  1.00 34.64           O  
HETATM 2918  O   HOH A 994       7.317  21.139 -13.849  1.00 34.88           O  
HETATM 2919  O   HOH A 995      37.353  22.937 -14.494  1.00 51.17           O  
HETATM 2920  O   HOH A 996      21.524  11.401 -10.287  1.00 42.87           O  
HETATM 2921  O   HOH A 997      35.830   9.470  -0.633  1.00 21.17           O  
HETATM 2922  O   HOH A 998      15.634  33.800   5.524  1.00 27.36           O  
HETATM 2923  O   HOH A 999      40.490  12.502  10.000  1.00 21.53           O  
HETATM 2924  O   HOH A1000      18.807  17.558  11.407  1.00 12.85           O  
HETATM 2925  O   HOH A1001      22.988  48.250  15.905  1.00 37.54           O  
HETATM 2926  O   HOH A1002      28.066  37.859   4.244  1.00 30.01           O  
HETATM 2927  O   HOH A1003      27.218  25.050  21.581  1.00 19.34           O  
HETATM 2928  O   HOH A1004      23.958   4.232  14.342  1.00 39.74           O  
HETATM 2929  O   HOH A1005      20.732  45.636  21.747  1.00 30.37           O  
HETATM 2930  O   HOH A1006       7.384  27.240   1.759  1.00 29.32           O  
HETATM 2931  O   HOH A1007       6.269  29.081   9.847  1.00 30.65           O  
HETATM 2932  O   HOH A1008      23.414  35.201  24.298  1.00 28.17           O  
HETATM 2933  O   HOH A1009       9.431  27.963  15.345  1.00 19.83           O  
HETATM 2934  O   HOH A1010      35.310  17.973  -1.966  1.00 40.92           O  
HETATM 2935  O   HOH A1011      19.885  31.571  -7.949  1.00 22.62           O  
HETATM 2936  O   HOH A1012      15.662  14.877  16.934  1.00 19.97           O  
HETATM 2937  O   HOH A1013      23.542   5.983   8.459  1.00 24.20           O  
HETATM 2938  O   HOH A1014       6.067  19.282   5.879  1.00 27.19           O  
HETATM 2939  O   HOH A1015      34.345  36.889  30.589  1.00 18.45           O  
HETATM 2940  O   HOH A1016      29.449  35.877  35.224  1.00 45.48           O  
HETATM 2941  O   HOH A1017      36.058   6.720  18.970  1.00 40.24           O  
HETATM 2942  O   HOH A1018      35.899  12.732   0.472  1.00 41.92           O  
HETATM 2943  O   HOH A1019      34.995   8.703  -4.542  1.00 34.87           O  
HETATM 2944  O   HOH A1020      34.185   9.853  12.987  1.00 29.85           O  
HETATM 2945  O   HOH A1021      37.063  47.880  22.370  1.00 31.41           O  
HETATM 2946  O   HOH A1022      25.806  29.567  16.022  1.00 17.06           O  
HETATM 2947  O   HOH A1023      33.210   9.374  23.375  1.00 30.94           O  
HETATM 2948  O   HOH A1024      19.795   6.517  -4.738  1.00 21.32           O  
HETATM 2949  O   HOH A1025      36.377   8.152  13.399  1.00 35.37           O  
HETATM 2950  O   HOH A1026      21.762  33.654  27.198  1.00 23.17           O  
HETATM 2951  O   HOH A1027      17.872   1.519  -4.515  1.00 45.57           O  
HETATM 2952  O   HOH A1028      39.883  18.637  10.837  1.00 23.37           O  
HETATM 2953  O   HOH A1029      44.908  44.738  30.557  1.00 18.88           O  
HETATM 2954  O   HOH A1030      20.835  43.867  20.041  1.00 31.75           O  
HETATM 2955  O   HOH A1031      18.025  15.191 -12.731  1.00 45.62           O  
HETATM 2956  O   HOH A1032      31.749  49.077  29.492  1.00 42.48           O  
HETATM 2957  O   HOH A1033      29.015  29.215  12.625  1.00 33.41           O  
HETATM 2958  O   HOH A1034      27.987   2.994  10.055  1.00 34.90           O  
HETATM 2959  O   HOH A1035      33.830  17.328   6.485  1.00 13.21           O  
HETATM 2960  O   HOH A1036      33.470  42.920  29.632  1.00 18.90           O  
HETATM 2961  O   HOH A1037       8.392  30.387  -0.346  1.00 39.03           O  
HETATM 2962  O   HOH A1038      11.476  26.273   2.585  1.00 17.31           O  
HETATM 2963  O   HOH A1039      28.019  41.137  19.198  1.00 21.40           O  
HETATM 2964  O   HOH A1040      52.425  37.841   1.309  1.00 45.71           O  
HETATM 2965  O   HOH A1041      44.844  39.252  27.385  1.00 44.61           O  
HETATM 2966  O   HOH A1042      29.236  21.061  27.665  1.00 46.20           O  
HETATM 2967  O   HOH A1043      34.938  52.839  12.285  1.00 43.39           O  
HETATM 2968  O   HOH A1044      15.545  17.473  29.668  1.00 46.19           O  
HETATM 2969  O   HOH A1045       5.974  17.802 -11.231  1.00 43.47           O  
HETATM 2970  O   HOH A1046      52.702  43.190  14.939  1.00 48.39           O  
HETATM 2971  O   HOH A1047      17.689  39.441  28.572  1.00 36.79           O  
HETATM 2972  O   HOH A1048      22.827  23.650  14.387  1.00 13.85           O  
HETATM 2973  O   HOH A1049      20.846  36.887  -4.068  1.00 26.53           O  
HETATM 2974  O   HOH A1050      43.643  40.897  23.806  1.00 27.78           O  
HETATM 2975  O   HOH A1051      16.553   7.710 -11.533  1.00 44.56           O  
HETATM 2976  O   HOH A1052      29.655  41.668   4.478  1.00 47.63           O  
HETATM 2977  O   HOH A1053      39.257  40.113   4.111  1.00 47.75           O  
HETATM 2978  O   HOH A1054       7.957  14.768   0.648  1.00 18.71           O  
HETATM 2979  O   HOH A1055      29.038  37.364  21.969  1.00 15.33           O  
HETATM 2980  O   HOH A1056      39.012  24.665  -7.323  1.00 33.05           O  
HETATM 2981  O   HOH A1057      22.211  39.557  15.153  1.00 21.44           O  
HETATM 2982  O   HOH A1058      49.753  35.684   6.502  1.00 33.75           O  
HETATM 2983  O   HOH A1059      23.335   7.489  -4.504  1.00 27.99           O  
HETATM 2984  O   HOH A1060      22.703  44.469  25.318  1.00 22.46           O  
HETATM 2985  O   HOH A1061      30.333  18.897 -12.863  1.00 37.38           O  
HETATM 2986  O   HOH A1062      38.137  19.267   7.105  1.00 19.04           O  
HETATM 2987  O   HOH A1063      21.962  35.153   4.694  1.00 32.70           O  
HETATM 2988  O   HOH A1064      27.807   5.431  19.856  1.00 32.49           O  
HETATM 2989  O   HOH A1065      15.703  23.488  27.449  1.00 29.52           O  
HETATM 2990  O   HOH A1066      25.180  39.405   6.029  1.00 32.79           O  
HETATM 2991  O   HOH A1067       9.805  24.108  24.559  1.00 39.30           O  
HETATM 2992  O   HOH A1068      28.448  51.614  13.846  1.00 27.60           O  
HETATM 2993  O   HOH A1069      33.390  25.208  32.541  1.00 46.64           O  
HETATM 2994  O   HOH A1070      31.557  44.961  29.703  1.00 35.02           O  
HETATM 2995  O   HOH A1071      25.909  35.024 -10.463  1.00 43.27           O  
HETATM 2996  O   HOH A1072      36.286  52.853  17.595  1.00 46.03           O  
HETATM 2997  O   HOH A1073       4.970  11.310  -6.340  1.00 28.23           O  
HETATM 2998  O   HOH A1074       8.106  30.282  -6.664  1.00 49.16           O  
HETATM 2999  O   HOH A1075      30.139  26.684  11.759  1.00 19.84           O  
HETATM 3000  O   HOH A1076       8.782   9.147  16.958  1.00 46.52           O  
HETATM 3001  O   HOH A1077       8.808  29.204   3.512  1.00 25.70           O  
HETATM 3002  O   HOH A1078      36.324  24.984  -3.815  1.00 42.11           O  
HETATM 3003  O   HOH A1079      28.435  50.998  23.991  1.00 38.61           O  
HETATM 3004  O   HOH A1080      25.318  21.179  19.662  1.00 17.95           O  
HETATM 3005  O   HOH A1081      15.919  16.802  25.599  1.00 27.03           O  
HETATM 3006  O   HOH A1082      27.759  45.515  12.398  1.00 19.64           O  
HETATM 3007  O   HOH A1083      22.087  21.288  26.455  1.00 28.71           O  
HETATM 3008  O   HOH A1084       7.498  15.367  12.289  1.00 32.06           O  
HETATM 3009  O   HOH A1085      35.795  16.672  18.989  1.00 34.46           O  
HETATM 3010  O   HOH A1086      31.074   5.526  18.020  1.00 42.33           O  
HETATM 3011  O   HOH A1087      34.131   1.797  -3.100  1.00 32.58           O  
HETATM 3012  O   HOH A1088       8.483  21.935  27.338  1.00 43.86           O  
HETATM 3013  O   HOH A1089      44.291  29.039  12.902  1.00 41.65           O  
HETATM 3014  O   HOH A1090       6.490  16.521  21.045  1.00 41.31           O  
HETATM 3015  O   HOH A1091      15.094   8.941  25.857  1.00 35.12           O  
HETATM 3016  O   HOH A1092      27.739  19.456   2.061  1.00 20.56           O  
HETATM 3017  O   HOH A1093      22.603   3.007  -3.511  1.00 39.58           O  
HETATM 3018  O   HOH A1094      29.858   5.004  -7.656  1.00 44.89           O  
HETATM 3019  O   HOH A1095       7.528  32.559  22.246  1.00 46.07           O  
HETATM 3020  O   HOH A1096       7.566  15.570 -11.391  1.00 40.86           O  
HETATM 3021  O   HOH A1097       9.249  27.681  21.972  1.00 25.54           O  
HETATM 3022  O   HOH A1098      24.299  50.779  15.525  1.00 46.42           O  
HETATM 3023  O   HOH A1099      23.045  30.685 -16.220  1.00 32.55           O  
HETATM 3024  O   HOH A1100      13.361  15.256  15.234  1.00 20.20           O  
HETATM 3025  O   HOH A1101      24.576   5.271  12.123  1.00 29.58           O  
HETATM 3026  O   HOH A1102      29.004  16.479  -0.365  1.00 21.49           O  
HETATM 3027  O   HOH A1103      37.684  14.975  -8.345  1.00 40.23           O  
HETATM 3028  O   HOH A1104      37.614  36.886  33.167  1.00 38.16           O  
HETATM 3029  O   HOH A1105      36.733  29.173  -4.897  1.00 37.19           O  
HETATM 3030  O   HOH A1106      12.954  34.583  -0.770  1.00 44.69           O  
HETATM 3031  O   HOH A1107      17.345   5.057   8.419  1.00 41.70           O  
HETATM 3032  O   HOH A1108      45.714  45.055   5.299  1.00 48.07           O  
HETATM 3033  O   HOH A1109       6.021  17.841   0.142  1.00 45.97           O  
HETATM 3034  O   HOH A1110      40.356  16.584   8.805  1.00 31.92           O  
HETATM 3035  O   HOH A1111       9.618   8.357  14.236  1.00 50.46           O  
HETATM 3036  O   HOH A1112      42.534   8.600   5.478  1.00 34.06           O  
HETATM 3037  O   HOH A1113      42.347  44.188  26.300  1.00 33.56           O  
HETATM 3038  O   HOH A1114      38.251  13.431  17.837  1.00 47.46           O  
HETATM 3039  O   HOH A1115      24.698  24.208  24.102  1.00 28.43           O  
HETATM 3040  O   HOH A1116      35.864  19.089   5.617  1.00 21.97           O  
HETATM 3041  O   HOH A1117      14.200   9.588  12.945  1.00 17.86           O  
HETATM 3042  O   HOH A1118      48.085  29.647  27.262  1.00 49.91           O  
HETATM 3043  O   HOH A1119      21.677  38.333 -10.067  1.00 35.47           O  
HETATM 3044  O   HOH A1120      25.497  36.889   6.855  1.00 22.41           O  
HETATM 3045  O   HOH A1121      17.392  36.655  26.268  1.00 52.34           O  
HETATM 3046  O   HOH A1122      40.909  22.588   8.695  1.00 47.68           O  
HETATM 3047  O   HOH A1123      18.218   7.296  20.472  1.00 28.28           O  
HETATM 3048  O   HOH A1124      34.488  51.682   9.516  1.00 40.38           O  
HETATM 3049  O   HOH A1125      25.032  16.905  -9.471  1.00 27.64           O  
HETATM 3050  O   HOH A1126      17.302  25.771 -20.048  1.00 35.25           O  
HETATM 3051  O   HOH A1127      35.956  15.709  -3.223  1.00 31.19           O  
HETATM 3052  O   HOH A1128       4.331  22.925  -2.040  1.00 44.23           O  
HETATM 3053  O   HOH A1129      34.884   7.258  23.858  1.00 31.86           O  
HETATM 3054  O   HOH A1130      40.453  45.747  10.360  1.00 51.37           O  
HETATM 3055  O   HOH A1131      17.578  37.977  -2.422  1.00 39.73           O  
HETATM 3056  O   HOH A1132      20.139  18.254  29.457  1.00 42.73           O  
HETATM 3057  O   HOH A1133      31.082  51.710  25.254  1.00 51.04           O  
HETATM 3058  O   HOH A1134      21.053  34.168   7.517  1.00 55.60           O  
HETATM 3059  O   HOH A1135      25.714  10.724  26.793  1.00 36.91           O  
HETATM 3060  O   HOH A1136      37.859  51.428  15.889  1.00 44.64           O  
HETATM 3061  O   HOH A1137      28.403  42.103  28.646  1.00 37.73           O  
HETATM 3062  O   HOH A1138      37.069  21.060   3.446  1.00 35.05           O  
HETATM 3063  O   HOH A1139      28.558  14.673  26.195  1.00 43.31           O  
HETATM 3064  O   HOH A1140      19.327  36.119  28.269  1.00 29.94           O  
HETATM 3065  O   HOH A1141      33.526  31.159  -4.817  1.00 29.26           O  
HETATM 3066  O   HOH A1142      16.651  13.006  25.472  1.00 26.81           O  
HETATM 3067  O   HOH A1143      44.460  30.826   6.045  1.00 37.76           O  
HETATM 3068  O   HOH A1144       3.788  23.193   7.804  1.00 44.11           O  
HETATM 3069  O   HOH A1145      39.239  37.380   3.244  1.00 36.63           O  
HETATM 3070  O   HOH A1146      25.749  17.813  25.354  1.00 32.01           O  
HETATM 3071  O   HOH A1147      28.995  44.480  30.313  1.00 41.26           O  
HETATM 3072  O   HOH A1148      13.737  30.057  26.616  1.00 46.39           O  
HETATM 3073  O   HOH A1149      14.055  30.819 -11.765  1.00 22.01           O  
HETATM 3074  O   HOH A1150      30.027  29.257  34.165  1.00 47.55           O  
HETATM 3075  O   HOH A1151      25.485   2.141   3.628  1.00 31.11           O  
HETATM 3076  O   HOH A1152      22.944  25.579  30.347  1.00 48.41           O  
HETATM 3077  O   HOH A1153      16.298  36.226   1.887  1.00 40.36           O  
HETATM 3078  O   HOH A1154      26.306  22.109  27.677  1.00 43.69           O  
HETATM 3079  O   HOH A1155       5.162  14.190  19.688  1.00 48.96           O  
HETATM 3080  O   HOH A1156      24.660   3.544   8.159  1.00 23.91           O  
HETATM 3081  O   HOH A1157      39.351   9.765  16.136  1.00 44.49           O  
HETATM 3082  O   HOH A1158      28.055  52.229  11.342  1.00 37.72           O  
HETATM 3083  O   HOH A1159      48.508  36.751   3.422  1.00 21.18           O  
HETATM 3084  O   HOH A1160      28.049  33.999  31.260  1.00 29.80           O  
HETATM 3085  O   HOH A1161      32.556   6.040  12.809  1.00 30.92           O  
HETATM 3086  O   HOH A1162      18.722  34.741  23.365  1.00 48.96           O  
HETATM 3087  O   HOH A1163      16.818  19.558 -24.253  1.00 45.48           O  
HETATM 3088  O   HOH A1164      42.267  32.439  14.916  1.00 34.01           O  
HETATM 3089  O   HOH A1165      33.320  39.309  31.555  1.00 28.07           O  
HETATM 3090  O   HOH A1166      29.947  40.803  31.099  1.00 36.02           O  
HETATM 3091  O   HOH A1167      42.119  14.564   3.967  1.00 52.47           O  
HETATM 3092  O   HOH A1168      11.257  27.561 -14.431  1.00 43.35           O  
HETATM 3093  O   HOH A1169       6.644  19.255  -5.645  1.00 37.57           O  
HETATM 3094  O   HOH A1170      43.445  29.233  23.697  1.00 28.29           O  
HETATM 3095  O   HOH A1171      38.355  39.653  36.291  1.00 45.24           O  
HETATM 3096  O   HOH A1172      43.028  24.815  18.054  1.00 30.39           O  
HETATM 3097  O   HOH A1173      12.337  30.478  -9.949  1.00 46.83           O  
HETATM 3098  O   HOH A1174       4.741  12.235   3.492  1.00 45.67           O  
HETATM 3099  O   HOH A1175      39.086  37.603   0.476  1.00 51.22           O  
HETATM 3100  O   HOH A1176       3.947  23.683  12.214  1.00 32.49           O  
HETATM 3101  O   HOH A1177      22.028  37.357  10.559  1.00 34.23           O  
HETATM 3102  O   HOH A1178      35.297  46.231  23.673  1.00 28.27           O  
HETATM 3103  O   HOH A1179      25.876  28.567 -10.454  1.00 22.20           O  
HETATM 3104  O   HOH A1180      35.374  52.617  20.276  1.00 43.07           O  
HETATM 3105  O   HOH A1181      28.202   6.716  16.808  1.00 44.52           O  
HETATM 3106  O   HOH A1182      47.122  38.180   0.443  1.00 46.78           O  
HETATM 3107  O   HOH A1183      25.798  37.226  -3.435  1.00 44.16           O  
HETATM 3108  O   HOH A1184      31.053  31.915  -3.833  1.00 50.97           O  
HETATM 3109  O   HOH A1185       7.014  31.133  -4.004  1.00 48.01           O  
HETATM 3110  O   HOH A1186      38.209  17.945 -12.380  1.00 38.87           O  
HETATM 3111  O   HOH A1187      15.372   7.143  19.038  1.00 54.80           O  
HETATM 3112  O   HOH A1188       2.710  10.091   0.962  1.00 28.34           O  
HETATM 3113  O   HOH A1189      24.103  28.205  32.190  1.00 54.44           O  
HETATM 3114  O   HOH A1190       9.206  21.447 -15.839  1.00 36.39           O  
HETATM 3115  O   HOH A1191       9.018  32.222   3.231  1.00 47.04           O  
HETATM 3116  O   HOH A1192      33.062   8.279  14.927  1.00 43.80           O  
HETATM 3117  O   HOH A1193      51.830  34.771  19.510  1.00 50.24           O  
HETATM 3118  O   HOH A1194      37.201  16.104 -11.075  1.00 29.83           O  
HETATM 3119  O   HOH A1195       9.751  34.022  13.307  1.00 40.83           O  
HETATM 3120  O   HOH A1196      22.908   6.442  22.486  1.00 50.47           O  
HETATM 3121  O   HOH A1197      37.841  14.253  -2.032  1.00 45.34           O  
HETATM 3122  O   HOH A1198      27.793   5.295  14.370  1.00 50.27           O  
HETATM 3123  O   HOH A1199      43.381  11.669   4.178  1.00 30.68           O  
HETATM 3124  O   HOH A1200       4.891  18.182  -2.153  1.00 45.31           O  
HETATM 3125  O   HOH A1201      21.215  33.742  23.063  1.00 45.06           O  
HETATM 3126  O   HOH A1202      20.090   6.483   9.435  1.00 47.61           O  
HETATM 3127  O   HOH A1203      31.120  44.534   5.804  1.00 42.02           O  
HETATM 3128  O   HOH A1204       3.375  29.950  14.826  1.00 41.20           O  
HETATM 3129  O   HOH A1205       6.241  22.796   2.140  1.00 51.00           O  
HETATM 3130  O   HOH A1206      30.319  28.341 -10.255  1.00 46.40           O  
HETATM 3131  O   HOH A1207      33.858  22.383 -12.526  1.00 46.90           O  
HETATM 3132  O   HOH A1208       8.515  24.207 -16.397  1.00 47.47           O  
HETATM 3133  O   HOH A1209       7.235  23.312  -7.410  1.00 35.81           O  
HETATM 3134  O   HOH A1210       5.175  15.114   0.990  1.00 39.64           O  
HETATM 3135  O   HOH A1211      48.667  27.725  20.746  1.00 49.54           O  
HETATM 3136  O   HOH A1212      25.641   3.183  10.680  1.00 37.97           O  
HETATM 3137  O   HOH A1213      32.877  18.071  -0.858  1.00 29.69           O  
HETATM 3138  O   HOH A1214      39.998  11.209  19.358  1.00 50.13           O  
HETATM 3139  O   HOH A1215      42.011  21.271  -8.345  1.00 41.28           O  
HETATM 3140  O   HOH A1216      41.486  27.207   5.066  1.00 31.43           O  
HETATM 3141  O   HOH A1217      27.222  37.087  24.023  1.00 19.21           O  
HETATM 3142  O   HOH A1218      22.920  39.793   4.304  1.00 37.53           O  
HETATM 3143  O   HOH A1219      39.300  12.234  22.083  1.00 48.64           O  
HETATM 3144  O   HOH A1220      34.428   6.781  -6.587  1.00 46.59           O  
HETATM 3145  O   HOH A1221      31.718  21.171 -13.878  1.00 46.71           O  
HETATM 3146  O   HOH A1222      40.794  23.083  16.398  1.00 47.07           O  
HETATM 3147  O   HOH A1223      32.296   6.536  -8.565  1.00 53.23           O  
HETATM 3148  O   HOH A1224      35.575  46.159   6.388  1.00 34.13           O  
HETATM 3149  O   HOH A1225       5.098  18.428  19.677  1.00 42.41           O  
HETATM 3150  O   HOH A1226      16.176   5.592  10.953  1.00 49.12           O  
HETATM 3151  O   HOH A1227       5.847  11.647  14.569  1.00 45.15           O  
HETATM 3152  O   HOH A1228      10.220   7.595  18.855  1.00 53.64           O  
HETATM 3153  O   HOH A1229      14.056  27.972 -13.189  1.00 16.54           O  
HETATM 3154  O   HOH A1230      27.748  32.837  33.639  1.00 46.85           O  
HETATM 3155  O   HOH A1231      17.200  14.651 -15.551  1.00 44.24           O  
HETATM 3156  O   HOH A1232      21.157  37.578   4.078  1.00 44.28           O  
HETATM 3157  O   HOH A1233      20.006  38.082   1.606  1.00 41.33           O  
HETATM 3158  O   HOH A1234      33.381  36.914  -0.811  1.00 43.03           O  
HETATM 3159  O   HOH A1235      35.434  53.964  31.673  1.00 39.16           O  
HETATM 3160  O   HOH A1236      35.175  35.763  33.009  1.00 33.80           O  
HETATM 3161  O   HOH A1237      30.290  36.700   2.718  1.00 38.61           O  
HETATM 3162  O   HOH A1238      12.488  27.550 -10.554  1.00 41.84           O  
HETATM 3163  O   HOH A1239      30.320  31.608  -6.554  1.00 60.70           O  
HETATM 3164  O   HOH A1240      21.933  32.218  29.476  1.00 37.56           O  
HETATM 3165  O   HOH A1241      40.547  27.645   1.187  1.00 38.10           O  
HETATM 3166  O   HOH A1242       5.722  22.742  19.183  1.00 38.59           O  
HETATM 3167  O   HOH A1243       6.088  12.029  10.508  1.00 43.92           O  
HETATM 3168  O   HOH A1244       4.761  18.668   3.429  1.00 37.26           O  
HETATM 3169  O   HOH A1245       5.128  24.967   3.268  1.00 50.03           O  
HETATM 3170  O   HOH A1246       6.639  26.725  22.600  1.00 36.05           O  
HETATM 3171  O   HOH A1247      33.674  32.215  -2.472  1.00 41.68           O  
HETATM 3172  O   HOH A1248      29.744  39.619  20.610  1.00 27.03           O  
HETATM 3173  O   HOH A1249      43.619  14.530   6.515  1.00 42.59           O  
HETATM 3174  O   HOH A1250       2.567  16.443  -2.346  1.00 46.21           O  
HETATM 3175  O   HOH A1251       3.947  20.601   6.960  1.00 36.53           O  
HETATM 3176  O   HOH A1252       5.709  17.190   7.700  1.00 31.53           O  
HETATM 3177  O   HOH A1253      33.685  34.787  -2.185  1.00 44.58           O  
HETATM 3178  O   HOH C 201      20.414  35.905  15.799  1.00 24.66           O  
HETATM 3179  O   HOH C 202      18.629  32.269   6.946  1.00 37.46           O  
HETATM 3180  O   HOH C 203      20.661  32.468  20.203  1.00 34.49           O  
HETATM 3181  O   HOH C 204      22.770  32.787   8.709  1.00 29.07           O  
HETATM 3182  O   HOH C 205      12.544  29.946  15.944  1.00 31.16           O  
HETATM 3183  O   HOH C 206      13.974  33.991  14.475  1.00 37.94           O  
HETATM 3184  O   HOH C 207      23.581  35.030   6.187  1.00 40.89           O  
HETATM 3185  O   HOH C 208      24.647  36.533   9.453  1.00 18.88           O  
HETATM 3186  O   HOH C 209      13.928  34.880  18.409  1.00 44.87           O  
HETATM 3187  O   HOH C 210      17.751  36.602  11.065  1.00 25.01           O  
HETATM 3188  O   HOH C 211      17.312  35.859  21.179  1.00 50.02           O  
HETATM 3189  O   HOH C 212      31.815  28.336  10.072  1.00 16.28           O  
HETATM 3190  O   HOH C 213      19.839  38.559  14.961  1.00 33.94           O  
HETATM 3191  O   HOH C 214      19.028  38.131  12.659  1.00 44.95           O  
HETATM 3192  O   HOH C 215      19.889  36.135   9.024  1.00 44.63           O  
HETATM 3193  O   HOH C 216      11.438  32.762  15.989  1.00 44.26           O  
HETATM 3194  O   HOH C 217      18.370  40.903  11.658  1.00 45.69           O  
CONECT  673 2777                                                                
CONECT  686 2777                                                                
CONECT 2736 2795                                                                
CONECT 2757 2763                                                                
CONECT 2762 2766                                                                
CONECT 2763 2757 2764                                                           
CONECT 2764 2763 2765 2766                                                      
CONECT 2765 2764                                                                
CONECT 2766 2762 2764 2767                                                      
CONECT 2767 2766                                                                
CONECT 2769 2770                                                                
CONECT 2770 2769 2771 2772 2773                                                 
CONECT 2771 2770                                                                
CONECT 2772 2770                                                                
CONECT 2773 2770 2774                                                           
CONECT 2774 2773 2775 2776                                                      
CONECT 2775 2774                                                                
CONECT 2776 2774                                                                
CONECT 2777  673  686 2831 3040                                                 
CONECT 2777 3062                                                                
CONECT 2778 2779 2780 2781                                                      
CONECT 2779 2778                                                                
CONECT 2780 2778                                                                
CONECT 2781 2778                                                                
CONECT 2782 2809 2810                                                           
CONECT 2783 2797 2808 2811                                                      
CONECT 2784 2785 2786 2809                                                      
CONECT 2785 2784 2801                                                           
CONECT 2786 2784 2787 2805                                                      
CONECT 2787 2786 2796 2807                                                      
CONECT 2788 2796 2798 2805                                                      
CONECT 2789 2790 2799                                                           
CONECT 2790 2789 2800                                                           
CONECT 2791 2792 2800                                                           
CONECT 2792 2791 2802 2812                                                      
CONECT 2793 2794 2812 2813                                                      
CONECT 2794 2793 2795                                                           
CONECT 2795 2736 2794 2816                                                      
CONECT 2796 2787 2788 2806                                                      
CONECT 2797 2783                                                                
CONECT 2798 2788 2803 2804                                                      
CONECT 2799 2789 2803                                                           
CONECT 2800 2790 2791                                                           
CONECT 2801 2785 2808                                                           
CONECT 2802 2792                                                                
CONECT 2803 2798 2799                                                           
CONECT 2804 2798                                                                
CONECT 2805 2786 2788                                                           
CONECT 2806 2796                                                                
CONECT 2807 2787                                                                
CONECT 2808 2783 2801 2809                                                      
CONECT 2809 2782 2784 2808                                                      
CONECT 2810 2782 2811                                                           
CONECT 2811 2783 2810                                                           
CONECT 2812 2792 2793                                                           
CONECT 2813 2793 2814 2815                                                      
CONECT 2814 2813                                                                
CONECT 2815 2813                                                                
CONECT 2816 2795                                                                
CONECT 2817 2818                                                                
CONECT 2818 2817 2819 2820 2821                                                 
CONECT 2819 2818                                                                
CONECT 2820 2818                                                                
CONECT 2821 2818 2822                                                           
CONECT 2822 2821 2823 2824                                                      
CONECT 2823 2822                                                                
CONECT 2824 2822                                                                
CONECT 2831 2777                                                                
CONECT 3040 2777                                                                
CONECT 3062 2777                                                                
MASTER      390    0    6   13   14    0   14    6 3109    2   70   29          
END                                                                             



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elNémo is maintained by Yves-Henri Sanejouand.
It was developed by Karsten Suhre.
Between 2003 and 2014, it was hosted by IGS (Marseille).
Last modification: October 18th, 2018.